data_8QLA
# 
_entry.id   8QLA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8QLA         pdb_00008qla 10.2210/pdb8qla/pdb 
WWPDB D_1292133185 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-13 
# 
_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_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2024-11-13 
_pdbx_database_PDB_obs_spr.pdb_id           8QLA 
_pdbx_database_PDB_obs_spr.replace_pdb_id   7YYW 
_pdbx_database_PDB_obs_spr.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                        8QLA 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 Joerg.standfuss@psi.ch Joerg  Standfuss ? 'principal investigator/group leader' 0000-0001-8825-386X 
3 tobias.weinert@psi.ch  Tobias Weinert   ? 'principal investigator/group leader' 0000-0002-0339-3722 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Weinert, T.'     1 0000-0002-0339-3722 
'Wranik, M.'      2 ?                   
'Seidel, H.-P.'   3 ?                   
'Church, J.'      4 ?                   
'Steinmetz, M.O.' 5 ?                   
'Schapiro, I.'    6 ?                   
'Standfuss, J.'   7 ?                   
# 
_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                     'Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution' 
_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 'Weinert, T.'     1 0000-0002-0339-3722 
primary 'Wranik, M.'      2 ?                   
primary 'Seidel, H.-P.'   3 ?                   
primary 'Church, J.'      4 ?                   
primary 'Steinmetz, M.O.' 5 ?                   
primary 'Schapiro, I.'    6 ?                   
primary 'Standfuss, J.'   7 ?                   
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Tubulin alpha-1B chain'                      50204.445 1   ? ? ? ? 
2 polymer     nat 'Tubulin beta-2B chain'                       49999.887 1   ? ? ? ? 
3 polymer     man 'Designed Ankyrin Repeat Protein (DARPIN) D1' 18068.439 1   ? ? ? ? 
4 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                   523.180   1   ? ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                               24.305    1   ? ? ? ? 
6 non-polymer syn 'CALCIUM ION'                                 40.078    1   ? ? ? ? 
7 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                    443.201   1   ? ? ? ? 
8 non-polymer syn 'Azo-Combretastatin A4 (cis)'                 318.325   1   ? ? ? ? 
9 water       nat water                                         18.015    253 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Alpha-tubulin ubiquitous,Tubulin K-alpha-1,Tubulin alpha-ubiquitous chain' 
# 
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
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
A ? 
2 'polypeptide(L)' no no 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
B ? 
3 'polypeptide(L)' no no 
;MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDASGLTPLHLAATYGHLEIVEVLLKHGADVNAIDIMG
STPLHLAALIGHLEIVEVLLKHGADVNAVDTWGDTPLHLAAIMGHLEIVEVLLKHGADVNAQDKFGKTAFDISIDNGNED
LAEILQKLN
;
;MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDASGLTPLHLAATYGHLEIVEVLLKHGADVNAIDIMG
STPLHLAALIGHLEIVEVLLKHGADVNAVDTWGDTPLHLAAIMGHLEIVEVLLKHGADVNAQDKFGKTAFDISIDNGNED
LAEILQKLN
;
F ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "GUANOSINE-5'-TRIPHOSPHATE"   GTP 
5 'MAGNESIUM ION'               MG  
6 'CALCIUM ION'                 CA  
7 "GUANOSINE-5'-DIPHOSPHATE"    GDP 
8 'Azo-Combretastatin A4 (cis)' IBL 
9 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 
1 451 TYR 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   ARG n 
3 3   GLY n 
3 4   SER n 
3 5   HIS n 
3 6   HIS n 
3 7   HIS n 
3 8   HIS n 
3 9   HIS n 
3 10  HIS n 
3 11  GLY n 
3 12  SER n 
3 13  ASP n 
3 14  LEU n 
3 15  GLY n 
3 16  LYS n 
3 17  LYS n 
3 18  LEU n 
3 19  LEU n 
3 20  GLU n 
3 21  ALA n 
3 22  ALA n 
3 23  ARG n 
3 24  ALA n 
3 25  GLY n 
3 26  GLN n 
3 27  ASP n 
3 28  ASP n 
3 29  GLU n 
3 30  VAL n 
3 31  ARG n 
3 32  ILE n 
3 33  LEU n 
3 34  MET n 
3 35  ALA n 
3 36  ASN n 
3 37  GLY n 
3 38  ALA n 
3 39  ASP n 
3 40  VAL n 
3 41  ASN n 
3 42  ALA n 
3 43  THR n 
3 44  ASP n 
3 45  ALA n 
3 46  SER n 
3 47  GLY n 
3 48  LEU n 
3 49  THR n 
3 50  PRO n 
3 51  LEU n 
3 52  HIS n 
3 53  LEU n 
3 54  ALA n 
3 55  ALA n 
3 56  THR n 
3 57  TYR n 
3 58  GLY n 
3 59  HIS n 
3 60  LEU n 
3 61  GLU n 
3 62  ILE n 
3 63  VAL n 
3 64  GLU n 
3 65  VAL n 
3 66  LEU n 
3 67  LEU n 
3 68  LYS n 
3 69  HIS n 
3 70  GLY n 
3 71  ALA n 
3 72  ASP n 
3 73  VAL n 
3 74  ASN n 
3 75  ALA n 
3 76  ILE n 
3 77  ASP n 
3 78  ILE n 
3 79  MET n 
3 80  GLY n 
3 81  SER n 
3 82  THR n 
3 83  PRO n 
3 84  LEU n 
3 85  HIS n 
3 86  LEU n 
3 87  ALA n 
3 88  ALA n 
3 89  LEU n 
3 90  ILE n 
3 91  GLY n 
3 92  HIS n 
3 93  LEU n 
3 94  GLU n 
3 95  ILE n 
3 96  VAL n 
3 97  GLU n 
3 98  VAL n 
3 99  LEU n 
3 100 LEU n 
3 101 LYS n 
3 102 HIS n 
3 103 GLY n 
3 104 ALA n 
3 105 ASP n 
3 106 VAL n 
3 107 ASN n 
3 108 ALA n 
3 109 VAL n 
3 110 ASP n 
3 111 THR n 
3 112 TRP n 
3 113 GLY n 
3 114 ASP n 
3 115 THR n 
3 116 PRO n 
3 117 LEU n 
3 118 HIS n 
3 119 LEU n 
3 120 ALA n 
3 121 ALA n 
3 122 ILE n 
3 123 MET n 
3 124 GLY n 
3 125 HIS n 
3 126 LEU n 
3 127 GLU n 
3 128 ILE n 
3 129 VAL n 
3 130 GLU n 
3 131 VAL n 
3 132 LEU n 
3 133 LEU n 
3 134 LYS n 
3 135 HIS n 
3 136 GLY n 
3 137 ALA n 
3 138 ASP n 
3 139 VAL n 
3 140 ASN n 
3 141 ALA n 
3 142 GLN n 
3 143 ASP n 
3 144 LYS n 
3 145 PHE n 
3 146 GLY n 
3 147 LYS n 
3 148 THR n 
3 149 ALA n 
3 150 PHE n 
3 151 ASP n 
3 152 ILE n 
3 153 SER n 
3 154 ILE n 
3 155 ASP n 
3 156 ASN n 
3 157 GLY n 
3 158 ASN n 
3 159 GLU n 
3 160 ASP n 
3 161 LEU n 
3 162 ALA n 
3 163 GLU n 
3 164 ILE n 
3 165 LEU n 
3 166 GLN n 
3 167 LYS n 
3 168 LEU n 
3 169 ASN n 
# 
_entity_src_gen.entity_id                          3 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_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      'synthetic construct' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     32630 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1 451 'domestic cattle' 'Bos taurus' 9913 ? ? ? brain ? ? ? ? ? ? ? brain ? ? ? ? ? 
2 1 sample 1 445 'domestic cattle' 'Bos taurus' 9913 ? ? ? brain ? ? ? ? ? ? ? brain ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                       ?                                                          'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                      ?                                                          
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                    ?                                                          'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'               ?                                                          'C4 H7 N O4' 
133.103 
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  
IBL non-polymer         . 'Azo-Combretastatin A4 (cis)' '2-methoxy-5-[(Z)-(3,4,5-trimethoxyphenyl)diazenyl]phenol' 'C16 H18 N2 O5' 
318.325 
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 ?   ?   ?   A . n 
A 1 439 SER 439 439 ?   ?   ?   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 
A 1 451 TYR 451 451 ?   ?   ?   A . n 
B 2 1   MET 1   1   1   MET MET B . n 
B 2 2   ARG 2   2   2   ARG ARG B . n 
B 2 3   GLU 3   3   3   GLU GLU B . n 
B 2 4   ILE 4   4   4   ILE ILE B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   HIS 6   6   6   HIS HIS B . n 
B 2 7   ILE 7   7   7   ILE ILE B . n 
B 2 8   GLN 8   8   8   GLN GLN B . n 
B 2 9   ALA 9   9   9   ALA ALA B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  GLN 11  11  11  GLN GLN B . n 
B 2 12  CYS 12  12  12  CYS CYS B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  ASN 14  14  14  ASN ASN B . n 
B 2 15  GLN 15  15  15  GLN GLN B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  GLY 17  17  17  GLY GLY B . n 
B 2 18  ALA 18  18  18  ALA ALA B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  PHE 20  20  20  PHE PHE B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  VAL 23  23  23  VAL VAL B . n 
B 2 24  ILE 24  24  24  ILE ILE B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  ASP 26  26  26  ASP ASP B . n 
B 2 27  GLU 27  27  27  GLU GLU B . n 
B 2 28  HIS 28  28  28  HIS HIS B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ILE 30  30  30  ILE ILE B . n 
B 2 31  ASP 31  31  31  ASP ASP B . n 
B 2 32  PRO 32  32  32  PRO PRO B . n 
B 2 33  THR 33  33  33  THR THR B . n 
B 2 34  GLY 34  34  34  GLY GLY B . n 
B 2 35  SER 35  35  35  SER SER B . n 
B 2 36  TYR 36  36  36  TYR TYR B . n 
B 2 37  HIS 37  37  37  HIS HIS B . n 
B 2 38  GLY 38  38  38  GLY GLY B . n 
B 2 39  ASP 39  39  39  ASP ASP B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  LEU 42  42  42  LEU LEU B . n 
B 2 43  GLN 43  43  43  GLN GLN B . n 
B 2 44  LEU 44  44  44  LEU LEU B . n 
B 2 45  GLU 45  45  45  GLU GLU B . n 
B 2 46  ARG 46  46  46  ARG ARG B . n 
B 2 47  ILE 47  47  47  ILE ILE B . n 
B 2 48  ASN 48  48  48  ASN ASN B . n 
B 2 49  VAL 49  49  49  VAL VAL B . n 
B 2 50  TYR 50  50  50  TYR TYR B . n 
B 2 51  TYR 51  51  51  TYR TYR B . n 
B 2 52  ASN 52  52  52  ASN ASN B . n 
B 2 53  GLU 53  53  53  GLU GLU B . n 
B 2 54  ALA 54  54  54  ALA ALA B . n 
B 2 55  THR 55  55  55  THR THR B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  PRO 61  61  61  PRO PRO B . n 
B 2 62  ARG 62  62  62  ARG ARG B . n 
B 2 63  ALA 63  63  63  ALA ALA B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  LEU 65  65  65  LEU LEU B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PRO 70  70  70  PRO PRO B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  THR 72  72  72  THR THR B . n 
B 2 73  MET 73  73  73  MET MET B . n 
B 2 74  ASP 74  74  74  ASP ASP B . n 
B 2 75  SER 75  75  75  SER SER B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  ARG 77  77  77  ARG ARG B . n 
B 2 78  SER 78  78  78  SER SER B . n 
B 2 79  GLY 79  79  79  GLY GLY B . n 
B 2 80  PRO 80  80  80  PRO PRO B . n 
B 2 81  PHE 81  81  81  PHE PHE B . n 
B 2 82  GLY 82  82  82  GLY GLY B . n 
B 2 83  GLN 83  83  83  GLN GLN B . n 
B 2 84  ILE 84  84  84  ILE ILE B . n 
B 2 85  PHE 85  85  85  PHE PHE B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  PRO 87  87  87  PRO PRO B . n 
B 2 88  ASP 88  88  88  ASP ASP B . n 
B 2 89  ASN 89  89  89  ASN ASN B . n 
B 2 90  PHE 90  90  90  PHE PHE B . n 
B 2 91  VAL 91  91  91  VAL VAL B . n 
B 2 92  PHE 92  92  92  PHE PHE B . n 
B 2 93  GLY 93  93  93  GLY GLY B . n 
B 2 94  GLN 94  94  94  GLN GLN B . n 
B 2 95  SER 95  95  95  SER SER B . n 
B 2 96  GLY 96  96  96  GLY GLY B . n 
B 2 97  ALA 97  97  97  ALA ALA B . n 
B 2 98  GLY 98  98  98  GLY GLY B . n 
B 2 99  ASN 99  99  99  ASN ASN B . n 
B 2 100 ASN 100 100 100 ASN ASN B . n 
B 2 101 TRP 101 101 101 TRP TRP B . n 
B 2 102 ALA 102 102 102 ALA ALA B . n 
B 2 103 LYS 103 103 103 LYS LYS B . n 
B 2 104 GLY 104 104 104 GLY GLY B . n 
B 2 105 HIS 105 105 105 HIS HIS B . n 
B 2 106 TYR 106 106 106 TYR TYR B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 GLU 108 108 108 GLU GLU B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 ALA 110 110 110 ALA ALA B . n 
B 2 111 GLU 111 111 111 GLU GLU B . n 
B 2 112 LEU 112 112 112 LEU LEU B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 ASP 114 114 114 ASP ASP B . n 
B 2 115 SER 115 115 115 SER SER B . n 
B 2 116 VAL 116 116 116 VAL VAL B . n 
B 2 117 LEU 117 117 117 LEU LEU B . n 
B 2 118 ASP 118 118 118 ASP ASP B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 VAL 120 120 120 VAL VAL B . n 
B 2 121 ARG 121 121 121 ARG ARG B . n 
B 2 122 LYS 122 122 122 LYS LYS B . n 
B 2 123 GLU 123 123 123 GLU GLU B . n 
B 2 124 SER 124 124 124 SER SER B . n 
B 2 125 GLU 125 125 125 GLU GLU B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 CYS 127 127 127 CYS CYS B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 CYS 129 129 129 CYS CYS B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 GLY 132 132 132 GLY GLY B . n 
B 2 133 PHE 133 133 133 PHE PHE B . n 
B 2 134 GLN 134 134 134 GLN GLN B . n 
B 2 135 LEU 135 135 135 LEU LEU B . n 
B 2 136 THR 136 136 136 THR THR B . n 
B 2 137 HIS 137 137 137 HIS HIS B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 LEU 139 139 139 LEU LEU B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 GLY 141 141 141 GLY GLY B . n 
B 2 142 GLY 142 142 142 GLY GLY B . n 
B 2 143 THR 143 143 143 THR THR B . n 
B 2 144 GLY 144 144 144 GLY GLY B . n 
B 2 145 SER 145 145 145 SER SER B . n 
B 2 146 GLY 146 146 146 GLY GLY B . n 
B 2 147 MET 147 147 147 MET MET B . n 
B 2 148 GLY 148 148 148 GLY GLY B . n 
B 2 149 THR 149 149 149 THR THR B . n 
B 2 150 LEU 150 150 150 LEU LEU B . n 
B 2 151 LEU 151 151 151 LEU LEU B . n 
B 2 152 ILE 152 152 152 ILE ILE B . n 
B 2 153 SER 153 153 153 SER SER B . n 
B 2 154 LYS 154 154 154 LYS LYS B . n 
B 2 155 ILE 155 155 155 ILE ILE B . n 
B 2 156 ARG 156 156 156 ARG ARG B . n 
B 2 157 GLU 157 157 157 GLU GLU B . n 
B 2 158 GLU 158 158 158 GLU GLU B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 ASP 161 161 161 ASP ASP B . n 
B 2 162 ARG 162 162 162 ARG ARG B . n 
B 2 163 ILE 163 163 163 ILE ILE B . n 
B 2 164 MET 164 164 164 MET MET B . n 
B 2 165 ASN 165 165 165 ASN ASN B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 PHE 167 167 167 PHE PHE B . n 
B 2 168 SER 168 168 168 SER SER B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 MET 170 170 170 MET MET B . n 
B 2 171 PRO 171 171 171 PRO PRO B . n 
B 2 172 SER 172 172 172 SER SER B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 LYS 174 174 174 LYS LYS B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 SER 176 176 176 SER SER B . n 
B 2 177 ASP 177 177 177 ASP ASP B . n 
B 2 178 THR 178 178 178 THR THR B . n 
B 2 179 VAL 179 179 179 VAL VAL B . n 
B 2 180 VAL 180 180 180 VAL VAL B . n 
B 2 181 GLU 181 181 181 GLU GLU B . n 
B 2 182 PRO 182 182 182 PRO PRO B . n 
B 2 183 TYR 183 183 183 TYR TYR B . n 
B 2 184 ASN 184 184 184 ASN ASN B . n 
B 2 185 ALA 185 185 185 ALA ALA B . n 
B 2 186 THR 186 186 186 THR THR B . n 
B 2 187 LEU 187 187 187 LEU LEU B . n 
B 2 188 SER 188 188 188 SER SER B . n 
B 2 189 VAL 189 189 189 VAL VAL B . n 
B 2 190 HIS 190 190 190 HIS HIS B . n 
B 2 191 GLN 191 191 191 GLN GLN B . n 
B 2 192 LEU 192 192 192 LEU LEU B . n 
B 2 193 VAL 193 193 193 VAL VAL B . n 
B 2 194 GLU 194 194 194 GLU GLU B . n 
B 2 195 ASN 195 195 195 ASN ASN B . n 
B 2 196 THR 196 196 196 THR THR B . n 
B 2 197 ASP 197 197 197 ASP ASP B . n 
B 2 198 GLU 198 198 198 GLU GLU B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 TYR 200 200 200 TYR TYR B . n 
B 2 201 CYS 201 201 201 CYS CYS B . n 
B 2 202 ILE 202 202 202 ILE ILE B . n 
B 2 203 ASP 203 203 203 ASP ASP B . n 
B 2 204 ASN 204 204 204 ASN ASN B . n 
B 2 205 GLU 205 205 205 GLU GLU B . n 
B 2 206 ALA 206 206 206 ALA ALA B . n 
B 2 207 LEU 207 207 207 LEU LEU B . n 
B 2 208 TYR 208 208 208 TYR TYR B . n 
B 2 209 ASP 209 209 209 ASP ASP B . n 
B 2 210 ILE 210 210 210 ILE ILE B . n 
B 2 211 CYS 211 211 211 CYS CYS B . n 
B 2 212 PHE 212 212 212 PHE PHE B . n 
B 2 213 ARG 213 213 213 ARG ARG B . n 
B 2 214 THR 214 214 214 THR THR B . n 
B 2 215 LEU 215 215 215 LEU LEU B . n 
B 2 216 LYS 216 216 216 LYS LYS B . n 
B 2 217 LEU 217 217 217 LEU LEU B . n 
B 2 218 THR 218 218 218 THR THR B . n 
B 2 219 THR 219 219 219 THR THR B . n 
B 2 220 PRO 220 220 220 PRO PRO B . n 
B 2 221 THR 221 221 221 THR THR B . n 
B 2 222 TYR 222 222 222 TYR TYR B . n 
B 2 223 GLY 223 223 223 GLY GLY B . n 
B 2 224 ASP 224 224 224 ASP ASP B . n 
B 2 225 LEU 225 225 225 LEU LEU B . n 
B 2 226 ASN 226 226 226 ASN ASN B . n 
B 2 227 HIS 227 227 227 HIS HIS B . n 
B 2 228 LEU 228 228 228 LEU LEU B . n 
B 2 229 VAL 229 229 229 VAL VAL B . n 
B 2 230 SER 230 230 230 SER SER B . n 
B 2 231 ALA 231 231 231 ALA ALA B . n 
B 2 232 THR 232 232 232 THR THR B . n 
B 2 233 MET 233 233 233 MET MET B . n 
B 2 234 SER 234 234 234 SER SER B . n 
B 2 235 GLY 235 235 235 GLY GLY B . n 
B 2 236 VAL 236 236 236 VAL VAL B . n 
B 2 237 THR 237 237 237 THR THR B . n 
B 2 238 THR 238 238 238 THR THR B . n 
B 2 239 CYS 239 239 239 CYS CYS B . n 
B 2 240 LEU 240 240 240 LEU LEU B . n 
B 2 241 ARG 241 241 241 ARG ARG B . n 
B 2 242 PHE 242 242 242 PHE PHE B . n 
B 2 243 PRO 243 243 243 PRO PRO B . n 
B 2 244 GLY 244 244 244 GLY GLY B . n 
B 2 245 GLN 245 245 245 GLN GLN B . n 
B 2 246 LEU 246 246 246 LEU LEU B . n 
B 2 247 ASN 247 247 247 ASN ASN B . n 
B 2 248 ALA 248 248 248 ALA ALA B . n 
B 2 249 ASP 249 249 249 ASP ASP B . n 
B 2 250 LEU 250 250 250 LEU LEU B . n 
B 2 251 ARG 251 251 251 ARG ARG B . n 
B 2 252 LYS 252 252 252 LYS LYS B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 ALA 254 254 254 ALA ALA B . n 
B 2 255 VAL 255 255 255 VAL VAL B . n 
B 2 256 ASN 256 256 256 ASN ASN B . n 
B 2 257 MET 257 257 257 MET MET B . n 
B 2 258 VAL 258 258 258 VAL VAL B . n 
B 2 259 PRO 259 259 259 PRO PRO B . n 
B 2 260 PHE 260 260 260 PHE PHE B . n 
B 2 261 PRO 261 261 261 PRO PRO B . n 
B 2 262 ARG 262 262 262 ARG ARG B . n 
B 2 263 LEU 263 263 263 LEU LEU B . n 
B 2 264 HIS 264 264 264 HIS HIS B . n 
B 2 265 PHE 265 265 265 PHE PHE B . n 
B 2 266 PHE 266 266 266 PHE PHE B . n 
B 2 267 MET 267 267 267 MET MET B . n 
B 2 268 PRO 268 268 268 PRO PRO B . n 
B 2 269 GLY 269 269 269 GLY GLY B . n 
B 2 270 PHE 270 270 270 PHE PHE B . n 
B 2 271 ALA 271 271 271 ALA ALA B . n 
B 2 272 PRO 272 272 272 PRO PRO B . n 
B 2 273 LEU 273 273 273 LEU LEU B . n 
B 2 274 THR 274 274 274 THR THR B . n 
B 2 275 SER 275 275 275 SER SER B . n 
B 2 276 ARG 276 276 276 ARG ARG B . n 
B 2 277 GLY 277 277 277 GLY GLY B . n 
B 2 278 SER 278 278 278 SER SER B . n 
B 2 279 GLN 279 279 ?   ?   ?   B . n 
B 2 280 GLN 280 280 ?   ?   ?   B . n 
B 2 281 TYR 281 281 ?   ?   ?   B . n 
B 2 282 ARG 282 282 ?   ?   ?   B . n 
B 2 283 ALA 283 283 ?   ?   ?   B . n 
B 2 284 LEU 284 284 284 LEU LEU B . n 
B 2 285 THR 285 285 285 THR THR B . n 
B 2 286 VAL 286 286 286 VAL VAL B . n 
B 2 287 PRO 287 287 287 PRO PRO B . n 
B 2 288 GLU 288 288 288 GLU GLU B . n 
B 2 289 LEU 289 289 289 LEU LEU B . n 
B 2 290 THR 290 290 290 THR THR B . n 
B 2 291 GLN 291 291 291 GLN GLN B . n 
B 2 292 GLN 292 292 292 GLN GLN B . n 
B 2 293 MET 293 293 293 MET MET B . n 
B 2 294 PHE 294 294 294 PHE PHE B . n 
B 2 295 ASP 295 295 295 ASP ASP B . n 
B 2 296 SER 296 296 296 SER SER B . n 
B 2 297 LYS 297 297 297 LYS LYS B . n 
B 2 298 ASN 298 298 298 ASN ASN B . n 
B 2 299 MET 299 299 299 MET MET B . n 
B 2 300 MET 300 300 300 MET MET B . n 
B 2 301 ALA 301 301 301 ALA ALA B . n 
B 2 302 ALA 302 302 302 ALA ALA B . n 
B 2 303 CYS 303 303 303 CYS CYS B . n 
B 2 304 ASP 304 304 304 ASP ASP B . n 
B 2 305 PRO 305 305 305 PRO PRO B . n 
B 2 306 ARG 306 306 306 ARG ARG B . n 
B 2 307 HIS 307 307 307 HIS HIS B . n 
B 2 308 GLY 308 308 308 GLY GLY B . n 
B 2 309 ARG 309 309 309 ARG ARG B . n 
B 2 310 TYR 310 310 310 TYR TYR B . n 
B 2 311 LEU 311 311 311 LEU LEU B . n 
B 2 312 THR 312 312 312 THR THR B . n 
B 2 313 VAL 313 313 313 VAL VAL B . n 
B 2 314 ALA 314 314 314 ALA ALA B . n 
B 2 315 ALA 315 315 315 ALA ALA B . n 
B 2 316 ILE 316 316 316 ILE ILE B . n 
B 2 317 PHE 317 317 317 PHE PHE B . n 
B 2 318 ARG 318 318 318 ARG ARG B . n 
B 2 319 GLY 319 319 319 GLY GLY B . n 
B 2 320 ARG 320 320 320 ARG ARG B . n 
B 2 321 MET 321 321 321 MET MET B . n 
B 2 322 SER 322 322 322 SER SER B . n 
B 2 323 MET 323 323 323 MET MET B . n 
B 2 324 LYS 324 324 324 LYS LYS B . n 
B 2 325 GLU 325 325 325 GLU GLU B . n 
B 2 326 VAL 326 326 326 VAL VAL B . n 
B 2 327 ASP 327 327 327 ASP ASP B . n 
B 2 328 GLU 328 328 328 GLU GLU B . n 
B 2 329 GLN 329 329 329 GLN GLN B . n 
B 2 330 MET 330 330 330 MET MET B . n 
B 2 331 LEU 331 331 331 LEU LEU B . n 
B 2 332 ASN 332 332 332 ASN ASN B . n 
B 2 333 VAL 333 333 333 VAL VAL B . n 
B 2 334 GLN 334 334 334 GLN GLN B . n 
B 2 335 ASN 335 335 335 ASN ASN B . n 
B 2 336 LYS 336 336 336 LYS LYS B . n 
B 2 337 ASN 337 337 337 ASN ASN B . n 
B 2 338 SER 338 338 338 SER SER B . n 
B 2 339 SER 339 339 339 SER SER B . n 
B 2 340 TYR 340 340 340 TYR TYR B . n 
B 2 341 PHE 341 341 341 PHE PHE B . n 
B 2 342 VAL 342 342 342 VAL VAL B . n 
B 2 343 GLU 343 343 343 GLU GLU B . n 
B 2 344 TRP 344 344 344 TRP TRP B . n 
B 2 345 ILE 345 345 345 ILE ILE B . n 
B 2 346 PRO 346 346 346 PRO PRO B . n 
B 2 347 ASN 347 347 347 ASN ASN B . n 
B 2 348 ASN 348 348 348 ASN ASN B . n 
B 2 349 VAL 349 349 349 VAL VAL B . n 
B 2 350 LYS 350 350 350 LYS LYS B . n 
B 2 351 THR 351 351 351 THR THR B . n 
B 2 352 ALA 352 352 352 ALA ALA B . n 
B 2 353 VAL 353 353 353 VAL VAL B . n 
B 2 354 CYS 354 354 354 CYS CYS B . n 
B 2 355 ASP 355 355 355 ASP ASP B . n 
B 2 356 ILE 356 356 356 ILE ILE B . n 
B 2 357 PRO 357 357 357 PRO PRO B . n 
B 2 358 PRO 358 358 358 PRO PRO B . n 
B 2 359 ARG 359 359 359 ARG ARG B . n 
B 2 360 GLY 360 360 360 GLY GLY B . n 
B 2 361 LEU 361 361 361 LEU LEU B . n 
B 2 362 LYS 362 362 362 LYS LYS B . n 
B 2 363 MET 363 363 363 MET MET B . n 
B 2 364 SER 364 364 364 SER SER B . n 
B 2 365 ALA 365 365 365 ALA ALA B . n 
B 2 366 THR 366 366 366 THR THR B . n 
B 2 367 PHE 367 367 367 PHE PHE B . n 
B 2 368 ILE 368 368 368 ILE ILE B . n 
B 2 369 GLY 369 369 369 GLY GLY B . n 
B 2 370 ASN 370 370 370 ASN ASN B . n 
B 2 371 SER 371 371 371 SER SER B . n 
B 2 372 THR 372 372 372 THR THR B . n 
B 2 373 ALA 373 373 373 ALA ALA B . n 
B 2 374 ILE 374 374 374 ILE ILE B . n 
B 2 375 GLN 375 375 375 GLN GLN B . n 
B 2 376 GLU 376 376 376 GLU GLU B . n 
B 2 377 LEU 377 377 377 LEU LEU B . n 
B 2 378 PHE 378 378 378 PHE PHE B . n 
B 2 379 LYS 379 379 379 LYS LYS B . n 
B 2 380 ARG 380 380 380 ARG ARG B . n 
B 2 381 ILE 381 381 381 ILE ILE B . n 
B 2 382 SER 382 382 382 SER SER B . n 
B 2 383 GLU 383 383 383 GLU GLU B . n 
B 2 384 GLN 384 384 384 GLN GLN B . n 
B 2 385 PHE 385 385 385 PHE PHE B . n 
B 2 386 THR 386 386 386 THR THR B . n 
B 2 387 ALA 387 387 387 ALA ALA B . n 
B 2 388 MET 388 388 388 MET MET B . n 
B 2 389 PHE 389 389 389 PHE PHE B . n 
B 2 390 ARG 390 390 390 ARG ARG B . n 
B 2 391 ARG 391 391 391 ARG ARG B . n 
B 2 392 LYS 392 392 392 LYS LYS B . n 
B 2 393 ALA 393 393 393 ALA ALA B . n 
B 2 394 PHE 394 394 394 PHE PHE B . n 
B 2 395 LEU 395 395 395 LEU LEU B . n 
B 2 396 HIS 396 396 396 HIS HIS B . n 
B 2 397 TRP 397 397 397 TRP TRP B . n 
B 2 398 TYR 398 398 398 TYR TYR B . n 
B 2 399 THR 399 399 399 THR THR B . n 
B 2 400 GLY 400 400 400 GLY GLY B . n 
B 2 401 GLU 401 401 401 GLU GLU B . n 
B 2 402 GLY 402 402 402 GLY GLY B . n 
B 2 403 MET 403 403 403 MET MET B . n 
B 2 404 ASP 404 404 404 ASP ASP B . n 
B 2 405 GLU 405 405 405 GLU GLU B . n 
B 2 406 MET 406 406 406 MET MET B . n 
B 2 407 GLU 407 407 407 GLU GLU B . n 
B 2 408 PHE 408 408 408 PHE PHE B . n 
B 2 409 THR 409 409 409 THR THR B . n 
B 2 410 GLU 410 410 410 GLU GLU B . n 
B 2 411 ALA 411 411 411 ALA ALA B . n 
B 2 412 GLU 412 412 412 GLU GLU B . n 
B 2 413 SER 413 413 413 SER SER B . n 
B 2 414 ASN 414 414 414 ASN ASN B . n 
B 2 415 MET 415 415 415 MET MET B . n 
B 2 416 ASN 416 416 416 ASN ASN B . n 
B 2 417 ASP 417 417 417 ASP ASP B . n 
B 2 418 LEU 418 418 418 LEU LEU B . n 
B 2 419 VAL 419 419 419 VAL VAL B . n 
B 2 420 SER 420 420 420 SER SER B . n 
B 2 421 GLU 421 421 421 GLU GLU B . n 
B 2 422 TYR 422 422 422 TYR TYR B . n 
B 2 423 GLN 423 423 423 GLN GLN B . n 
B 2 424 GLN 424 424 424 GLN GLN B . n 
B 2 425 TYR 425 425 425 TYR TYR B . n 
B 2 426 GLN 426 426 426 GLN GLN B . n 
B 2 427 ASP 427 427 427 ASP ASP B . n 
B 2 428 ALA 428 428 428 ALA ALA B . n 
B 2 429 THR 429 429 429 THR THR B . n 
B 2 430 ALA 430 430 ?   ?   ?   B . n 
B 2 431 ASP 431 431 ?   ?   ?   B . n 
B 2 432 GLU 432 432 ?   ?   ?   B . n 
B 2 433 GLN 433 433 ?   ?   ?   B . n 
B 2 434 GLY 434 434 ?   ?   ?   B . n 
B 2 435 GLU 435 435 ?   ?   ?   B . n 
B 2 436 PHE 436 436 ?   ?   ?   B . n 
B 2 437 GLU 437 437 ?   ?   ?   B . n 
B 2 438 GLU 438 438 ?   ?   ?   B . n 
B 2 439 GLU 439 439 ?   ?   ?   B . n 
B 2 440 GLU 440 440 ?   ?   ?   B . n 
B 2 441 GLY 441 441 ?   ?   ?   B . n 
B 2 442 GLU 442 442 ?   ?   ?   B . n 
B 2 443 ASP 443 443 ?   ?   ?   B . n 
B 2 444 GLU 444 444 ?   ?   ?   B . n 
B 2 445 ALA 445 445 ?   ?   ?   B . n 
C 3 1   MET 1   1   ?   ?   ?   F . n 
C 3 2   ARG 2   2   ?   ?   ?   F . n 
C 3 3   GLY 3   3   ?   ?   ?   F . n 
C 3 4   SER 4   4   ?   ?   ?   F . n 
C 3 5   HIS 5   5   ?   ?   ?   F . n 
C 3 6   HIS 6   6   ?   ?   ?   F . n 
C 3 7   HIS 7   7   ?   ?   ?   F . n 
C 3 8   HIS 8   8   ?   ?   ?   F . n 
C 3 9   HIS 9   9   ?   ?   ?   F . n 
C 3 10  HIS 10  10  ?   ?   ?   F . n 
C 3 11  GLY 11  11  ?   ?   ?   F . n 
C 3 12  SER 12  12  ?   ?   ?   F . n 
C 3 13  ASP 13  13  13  ASP ASP F . n 
C 3 14  LEU 14  14  14  LEU LEU F . n 
C 3 15  GLY 15  15  15  GLY GLY F . n 
C 3 16  LYS 16  16  16  LYS LYS F . n 
C 3 17  LYS 17  17  17  LYS LYS F . n 
C 3 18  LEU 18  18  18  LEU LEU F . n 
C 3 19  LEU 19  19  19  LEU LEU F . n 
C 3 20  GLU 20  20  20  GLU GLU F . n 
C 3 21  ALA 21  21  21  ALA ALA F . n 
C 3 22  ALA 22  22  22  ALA ALA F . n 
C 3 23  ARG 23  23  23  ARG ARG F . n 
C 3 24  ALA 24  24  24  ALA ALA F . n 
C 3 25  GLY 25  25  25  GLY GLY F . n 
C 3 26  GLN 26  26  26  GLN GLN F . n 
C 3 27  ASP 27  27  27  ASP ASP F . n 
C 3 28  ASP 28  28  28  ASP ASP F . n 
C 3 29  GLU 29  29  29  GLU GLU F . n 
C 3 30  VAL 30  30  30  VAL VAL F . n 
C 3 31  ARG 31  31  31  ARG ARG F . n 
C 3 32  ILE 32  32  32  ILE ILE F . n 
C 3 33  LEU 33  33  33  LEU LEU F . n 
C 3 34  MET 34  34  34  MET MET F . n 
C 3 35  ALA 35  35  35  ALA ALA F . n 
C 3 36  ASN 36  36  36  ASN ASN F . n 
C 3 37  GLY 37  37  37  GLY GLY F . n 
C 3 38  ALA 38  38  38  ALA ALA F . n 
C 3 39  ASP 39  39  39  ASP ASP F . n 
C 3 40  VAL 40  40  40  VAL VAL F . n 
C 3 41  ASN 41  41  41  ASN ASN F . n 
C 3 42  ALA 42  42  42  ALA ALA F . n 
C 3 43  THR 43  43  43  THR THR F . n 
C 3 44  ASP 44  44  44  ASP ASP F . n 
C 3 45  ALA 45  45  45  ALA ALA F . n 
C 3 46  SER 46  46  46  SER SER F . n 
C 3 47  GLY 47  47  47  GLY GLY F . n 
C 3 48  LEU 48  48  48  LEU LEU F . n 
C 3 49  THR 49  49  49  THR THR F . n 
C 3 50  PRO 50  50  50  PRO PRO F . n 
C 3 51  LEU 51  51  51  LEU LEU F . n 
C 3 52  HIS 52  52  52  HIS HIS F . n 
C 3 53  LEU 53  53  53  LEU LEU F . n 
C 3 54  ALA 54  54  54  ALA ALA F . n 
C 3 55  ALA 55  55  55  ALA ALA F . n 
C 3 56  THR 56  56  56  THR THR F . n 
C 3 57  TYR 57  57  57  TYR TYR F . n 
C 3 58  GLY 58  58  58  GLY GLY F . n 
C 3 59  HIS 59  59  59  HIS HIS F . n 
C 3 60  LEU 60  60  60  LEU LEU F . n 
C 3 61  GLU 61  61  61  GLU GLU F . n 
C 3 62  ILE 62  62  62  ILE ILE F . n 
C 3 63  VAL 63  63  63  VAL VAL F . n 
C 3 64  GLU 64  64  64  GLU GLU F . n 
C 3 65  VAL 65  65  65  VAL VAL F . n 
C 3 66  LEU 66  66  66  LEU LEU F . n 
C 3 67  LEU 67  67  67  LEU LEU F . n 
C 3 68  LYS 68  68  68  LYS LYS F . n 
C 3 69  HIS 69  69  69  HIS HIS F . n 
C 3 70  GLY 70  70  70  GLY GLY F . n 
C 3 71  ALA 71  71  71  ALA ALA F . n 
C 3 72  ASP 72  72  72  ASP ASP F . n 
C 3 73  VAL 73  73  73  VAL VAL F . n 
C 3 74  ASN 74  74  74  ASN ASN F . n 
C 3 75  ALA 75  75  75  ALA ALA F . n 
C 3 76  ILE 76  76  76  ILE ILE F . n 
C 3 77  ASP 77  77  77  ASP ASP F . n 
C 3 78  ILE 78  78  78  ILE ILE F . n 
C 3 79  MET 79  79  79  MET MET F . n 
C 3 80  GLY 80  80  80  GLY GLY F . n 
C 3 81  SER 81  81  81  SER SER F . n 
C 3 82  THR 82  82  82  THR THR F . n 
C 3 83  PRO 83  83  83  PRO PRO F . n 
C 3 84  LEU 84  84  84  LEU LEU F . n 
C 3 85  HIS 85  85  85  HIS HIS F . n 
C 3 86  LEU 86  86  86  LEU LEU F . n 
C 3 87  ALA 87  87  87  ALA ALA F . n 
C 3 88  ALA 88  88  88  ALA ALA F . n 
C 3 89  LEU 89  89  89  LEU LEU F . n 
C 3 90  ILE 90  90  90  ILE ILE F . n 
C 3 91  GLY 91  91  91  GLY GLY F . n 
C 3 92  HIS 92  92  92  HIS HIS F . n 
C 3 93  LEU 93  93  93  LEU LEU F . n 
C 3 94  GLU 94  94  94  GLU GLU F . n 
C 3 95  ILE 95  95  95  ILE ILE F . n 
C 3 96  VAL 96  96  96  VAL VAL F . n 
C 3 97  GLU 97  97  97  GLU GLU F . n 
C 3 98  VAL 98  98  98  VAL VAL F . n 
C 3 99  LEU 99  99  99  LEU LEU F . n 
C 3 100 LEU 100 100 100 LEU LEU F . n 
C 3 101 LYS 101 101 101 LYS LYS F . n 
C 3 102 HIS 102 102 102 HIS HIS F . n 
C 3 103 GLY 103 103 103 GLY GLY F . n 
C 3 104 ALA 104 104 104 ALA ALA F . n 
C 3 105 ASP 105 105 105 ASP ASP F . n 
C 3 106 VAL 106 106 106 VAL VAL F . n 
C 3 107 ASN 107 107 107 ASN ASN F . n 
C 3 108 ALA 108 108 108 ALA ALA F . n 
C 3 109 VAL 109 109 109 VAL VAL F . n 
C 3 110 ASP 110 110 110 ASP ASP F . n 
C 3 111 THR 111 111 111 THR THR F . n 
C 3 112 TRP 112 112 112 TRP TRP F . n 
C 3 113 GLY 113 113 113 GLY GLY F . n 
C 3 114 ASP 114 114 114 ASP ASP F . n 
C 3 115 THR 115 115 115 THR THR F . n 
C 3 116 PRO 116 116 116 PRO PRO F . n 
C 3 117 LEU 117 117 117 LEU LEU F . n 
C 3 118 HIS 118 118 118 HIS HIS F . n 
C 3 119 LEU 119 119 119 LEU LEU F . n 
C 3 120 ALA 120 120 120 ALA ALA F . n 
C 3 121 ALA 121 121 121 ALA ALA F . n 
C 3 122 ILE 122 122 122 ILE ILE F . n 
C 3 123 MET 123 123 123 MET MET F . n 
C 3 124 GLY 124 124 124 GLY GLY F . n 
C 3 125 HIS 125 125 125 HIS HIS F . n 
C 3 126 LEU 126 126 126 LEU LEU F . n 
C 3 127 GLU 127 127 127 GLU GLU F . n 
C 3 128 ILE 128 128 128 ILE ILE F . n 
C 3 129 VAL 129 129 129 VAL VAL F . n 
C 3 130 GLU 130 130 130 GLU GLU F . n 
C 3 131 VAL 131 131 131 VAL VAL F . n 
C 3 132 LEU 132 132 132 LEU LEU F . n 
C 3 133 LEU 133 133 133 LEU LEU F . n 
C 3 134 LYS 134 134 134 LYS LYS F . n 
C 3 135 HIS 135 135 135 HIS HIS F . n 
C 3 136 GLY 136 136 136 GLY GLY F . n 
C 3 137 ALA 137 137 137 ALA ALA F . n 
C 3 138 ASP 138 138 138 ASP ASP F . n 
C 3 139 VAL 139 139 139 VAL VAL F . n 
C 3 140 ASN 140 140 140 ASN ASN F . n 
C 3 141 ALA 141 141 141 ALA ALA F . n 
C 3 142 GLN 142 142 142 GLN GLN F . n 
C 3 143 ASP 143 143 143 ASP ASP F . n 
C 3 144 LYS 144 144 144 LYS LYS F . n 
C 3 145 PHE 145 145 145 PHE PHE F . n 
C 3 146 GLY 146 146 146 GLY GLY F . n 
C 3 147 LYS 147 147 147 LYS LYS F . n 
C 3 148 THR 148 148 148 THR THR F . n 
C 3 149 ALA 149 149 149 ALA ALA F . n 
C 3 150 PHE 150 150 150 PHE PHE F . n 
C 3 151 ASP 151 151 151 ASP ASP F . n 
C 3 152 ILE 152 152 152 ILE ILE F . n 
C 3 153 SER 153 153 153 SER SER F . n 
C 3 154 ILE 154 154 154 ILE ILE F . n 
C 3 155 ASP 155 155 155 ASP ASP F . n 
C 3 156 ASN 156 156 156 ASN ASN F . n 
C 3 157 GLY 157 157 157 GLY GLY F . n 
C 3 158 ASN 158 158 158 ASN ASN F . n 
C 3 159 GLU 159 159 159 GLU GLU F . n 
C 3 160 ASP 160 160 160 ASP ASP F . n 
C 3 161 LEU 161 161 161 LEU LEU F . n 
C 3 162 ALA 162 162 162 ALA ALA F . n 
C 3 163 GLU 163 163 163 GLU GLU F . n 
C 3 164 ILE 164 164 164 ILE ILE F . n 
C 3 165 LEU 165 165 165 LEU LEU F . n 
C 3 166 GLN 166 166 166 GLN GLN F . n 
C 3 167 LYS 167 167 167 LYS LYS F . n 
C 3 168 LEU 168 168 ?   ?   ?   F . n 
C 3 169 ASN 169 169 ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 GTP 1   501 501 GTP GTP A . 
E 5 MG  1   502 502 MG  MG  A . 
F 6 CA  1   503 1   CA  CA  A . 
G 7 GDP 1   501 501 GDP GDP B . 
H 8 IBL 1   502 601 IBL XXX B . 
I 9 HOH 1   601 112 HOH HOH A . 
I 9 HOH 2   602 12  HOH HOH A . 
I 9 HOH 3   603 53  HOH HOH A . 
I 9 HOH 4   604 206 HOH HOH A . 
I 9 HOH 5   605 117 HOH HOH A . 
I 9 HOH 6   606 122 HOH HOH A . 
I 9 HOH 7   607 8   HOH HOH A . 
I 9 HOH 8   608 123 HOH HOH A . 
I 9 HOH 9   609 185 HOH HOH A . 
I 9 HOH 10  610 150 HOH HOH A . 
I 9 HOH 11  611 6   HOH HOH A . 
I 9 HOH 12  612 79  HOH HOH A . 
I 9 HOH 13  613 160 HOH HOH A . 
I 9 HOH 14  614 199 HOH HOH A . 
I 9 HOH 15  615 11  HOH HOH A . 
I 9 HOH 16  616 288 HOH HOH A . 
I 9 HOH 17  617 302 HOH HOH A . 
I 9 HOH 18  618 270 HOH HOH A . 
I 9 HOH 19  619 68  HOH HOH A . 
I 9 HOH 20  620 1   HOH HOH A . 
I 9 HOH 21  621 7   HOH HOH A . 
I 9 HOH 22  622 158 HOH HOH A . 
I 9 HOH 23  623 192 HOH HOH A . 
I 9 HOH 24  624 35  HOH HOH A . 
I 9 HOH 25  625 304 HOH HOH A . 
I 9 HOH 26  626 306 HOH HOH A . 
I 9 HOH 27  627 216 HOH HOH A . 
I 9 HOH 28  628 58  HOH HOH A . 
I 9 HOH 29  629 91  HOH HOH A . 
I 9 HOH 30  630 140 HOH HOH A . 
I 9 HOH 31  631 40  HOH HOH A . 
I 9 HOH 32  632 108 HOH HOH A . 
I 9 HOH 33  633 148 HOH HOH A . 
I 9 HOH 34  634 152 HOH HOH A . 
I 9 HOH 35  635 118 HOH HOH A . 
I 9 HOH 36  636 180 HOH HOH A . 
I 9 HOH 37  637 257 HOH HOH A . 
I 9 HOH 38  638 292 HOH HOH A . 
I 9 HOH 39  639 214 HOH HOH A . 
I 9 HOH 40  640 4   HOH HOH A . 
I 9 HOH 41  641 19  HOH HOH A . 
I 9 HOH 42  642 49  HOH HOH A . 
I 9 HOH 43  643 27  HOH HOH A . 
I 9 HOH 44  644 48  HOH HOH A . 
I 9 HOH 45  645 97  HOH HOH A . 
I 9 HOH 46  646 237 HOH HOH A . 
I 9 HOH 47  647 276 HOH HOH A . 
I 9 HOH 48  648 28  HOH HOH A . 
I 9 HOH 49  649 41  HOH HOH A . 
I 9 HOH 50  650 111 HOH HOH A . 
I 9 HOH 51  651 277 HOH HOH A . 
I 9 HOH 52  652 65  HOH HOH A . 
I 9 HOH 53  653 5   HOH HOH A . 
I 9 HOH 54  654 78  HOH HOH A . 
I 9 HOH 55  655 256 HOH HOH A . 
I 9 HOH 56  656 188 HOH HOH A . 
I 9 HOH 57  657 171 HOH HOH A . 
I 9 HOH 58  658 127 HOH HOH A . 
I 9 HOH 59  659 17  HOH HOH A . 
I 9 HOH 60  660 26  HOH HOH A . 
I 9 HOH 61  661 80  HOH HOH A . 
I 9 HOH 62  662 121 HOH HOH A . 
I 9 HOH 63  663 174 HOH HOH A . 
I 9 HOH 64  664 233 HOH HOH A . 
I 9 HOH 65  665 89  HOH HOH A . 
I 9 HOH 66  666 263 HOH HOH A . 
I 9 HOH 67  667 13  HOH HOH A . 
I 9 HOH 68  668 301 HOH HOH A . 
I 9 HOH 69  669 102 HOH HOH A . 
I 9 HOH 70  670 59  HOH HOH A . 
I 9 HOH 71  671 52  HOH HOH A . 
I 9 HOH 72  672 146 HOH HOH A . 
I 9 HOH 73  673 39  HOH HOH A . 
I 9 HOH 74  674 139 HOH HOH A . 
I 9 HOH 75  675 129 HOH HOH A . 
I 9 HOH 76  676 207 HOH HOH A . 
I 9 HOH 77  677 149 HOH HOH A . 
I 9 HOH 78  678 61  HOH HOH A . 
I 9 HOH 79  679 98  HOH HOH A . 
I 9 HOH 80  680 137 HOH HOH A . 
I 9 HOH 81  681 285 HOH HOH A . 
I 9 HOH 82  682 57  HOH HOH A . 
I 9 HOH 83  683 305 HOH HOH A . 
I 9 HOH 84  684 268 HOH HOH A . 
I 9 HOH 85  685 162 HOH HOH A . 
I 9 HOH 86  686 54  HOH HOH A . 
I 9 HOH 87  687 24  HOH HOH A . 
I 9 HOH 88  688 194 HOH HOH A . 
I 9 HOH 89  689 176 HOH HOH A . 
I 9 HOH 90  690 190 HOH HOH A . 
I 9 HOH 91  691 172 HOH HOH A . 
I 9 HOH 92  692 295 HOH HOH A . 
I 9 HOH 93  693 76  HOH HOH A . 
I 9 HOH 94  694 156 HOH HOH A . 
I 9 HOH 95  695 168 HOH HOH A . 
I 9 HOH 96  696 46  HOH HOH A . 
I 9 HOH 97  697 138 HOH HOH A . 
I 9 HOH 98  698 83  HOH HOH A . 
I 9 HOH 99  699 265 HOH HOH A . 
I 9 HOH 100 700 136 HOH HOH A . 
I 9 HOH 101 701 132 HOH HOH A . 
I 9 HOH 102 702 95  HOH HOH A . 
I 9 HOH 103 703 81  HOH HOH A . 
I 9 HOH 104 704 260 HOH HOH A . 
I 9 HOH 105 705 193 HOH HOH A . 
I 9 HOH 106 706 131 HOH HOH A . 
I 9 HOH 107 707 100 HOH HOH A . 
I 9 HOH 108 708 94  HOH HOH A . 
I 9 HOH 109 709 16  HOH HOH A . 
I 9 HOH 110 710 298 HOH HOH A . 
I 9 HOH 111 711 215 HOH HOH A . 
I 9 HOH 112 712 184 HOH HOH A . 
I 9 HOH 113 713 204 HOH HOH A . 
I 9 HOH 114 714 88  HOH HOH A . 
I 9 HOH 115 715 223 HOH HOH A . 
I 9 HOH 116 716 177 HOH HOH A . 
I 9 HOH 117 717 246 HOH HOH A . 
I 9 HOH 118 718 220 HOH HOH A . 
I 9 HOH 119 719 226 HOH HOH A . 
I 9 HOH 120 720 271 HOH HOH A . 
I 9 HOH 121 721 243 HOH HOH A . 
I 9 HOH 122 722 242 HOH HOH A . 
I 9 HOH 123 723 238 HOH HOH A . 
J 9 HOH 1   601 164 HOH HOH B . 
J 9 HOH 2   602 125 HOH HOH B . 
J 9 HOH 3   603 275 HOH HOH B . 
J 9 HOH 4   604 3   HOH HOH B . 
J 9 HOH 5   605 14  HOH HOH B . 
J 9 HOH 6   606 96  HOH HOH B . 
J 9 HOH 7   607 217 HOH HOH B . 
J 9 HOH 8   608 142 HOH HOH B . 
J 9 HOH 9   609 62  HOH HOH B . 
J 9 HOH 10  610 36  HOH HOH B . 
J 9 HOH 11  611 107 HOH HOH B . 
J 9 HOH 12  612 289 HOH HOH B . 
J 9 HOH 13  613 248 HOH HOH B . 
J 9 HOH 14  614 21  HOH HOH B . 
J 9 HOH 15  615 159 HOH HOH B . 
J 9 HOH 16  616 10  HOH HOH B . 
J 9 HOH 17  617 179 HOH HOH B . 
J 9 HOH 18  618 169 HOH HOH B . 
J 9 HOH 19  619 110 HOH HOH B . 
J 9 HOH 20  620 71  HOH HOH B . 
J 9 HOH 21  621 99  HOH HOH B . 
J 9 HOH 22  622 225 HOH HOH B . 
J 9 HOH 23  623 56  HOH HOH B . 
J 9 HOH 24  624 18  HOH HOH B . 
J 9 HOH 25  625 198 HOH HOH B . 
J 9 HOH 26  626 181 HOH HOH B . 
J 9 HOH 27  627 218 HOH HOH B . 
J 9 HOH 28  628 247 HOH HOH B . 
J 9 HOH 29  629 69  HOH HOH B . 
J 9 HOH 30  630 43  HOH HOH B . 
J 9 HOH 31  631 203 HOH HOH B . 
J 9 HOH 32  632 51  HOH HOH B . 
J 9 HOH 33  633 144 HOH HOH B . 
J 9 HOH 34  634 182 HOH HOH B . 
J 9 HOH 35  635 130 HOH HOH B . 
J 9 HOH 36  636 32  HOH HOH B . 
J 9 HOH 37  637 105 HOH HOH B . 
J 9 HOH 38  638 33  HOH HOH B . 
J 9 HOH 39  639 303 HOH HOH B . 
J 9 HOH 40  640 34  HOH HOH B . 
J 9 HOH 41  641 253 HOH HOH B . 
J 9 HOH 42  642 244 HOH HOH B . 
J 9 HOH 43  643 37  HOH HOH B . 
J 9 HOH 44  644 273 HOH HOH B . 
J 9 HOH 45  645 126 HOH HOH B . 
J 9 HOH 46  646 230 HOH HOH B . 
J 9 HOH 47  647 234 HOH HOH B . 
J 9 HOH 48  648 154 HOH HOH B . 
J 9 HOH 49  649 205 HOH HOH B . 
J 9 HOH 50  650 209 HOH HOH B . 
J 9 HOH 51  651 77  HOH HOH B . 
J 9 HOH 52  652 294 HOH HOH B . 
J 9 HOH 53  653 63  HOH HOH B . 
J 9 HOH 54  654 72  HOH HOH B . 
J 9 HOH 55  655 250 HOH HOH B . 
J 9 HOH 56  656 196 HOH HOH B . 
J 9 HOH 57  657 261 HOH HOH B . 
J 9 HOH 58  658 211 HOH HOH B . 
J 9 HOH 59  659 93  HOH HOH B . 
J 9 HOH 60  660 269 HOH HOH B . 
J 9 HOH 61  661 201 HOH HOH B . 
J 9 HOH 62  662 109 HOH HOH B . 
J 9 HOH 63  663 166 HOH HOH B . 
J 9 HOH 64  664 165 HOH HOH B . 
J 9 HOH 65  665 221 HOH HOH B . 
J 9 HOH 66  666 278 HOH HOH B . 
J 9 HOH 67  667 103 HOH HOH B . 
J 9 HOH 68  668 274 HOH HOH B . 
J 9 HOH 69  669 254 HOH HOH B . 
J 9 HOH 70  670 229 HOH HOH B . 
J 9 HOH 71  671 70  HOH HOH B . 
J 9 HOH 72  672 210 HOH HOH B . 
J 9 HOH 73  673 280 HOH HOH B . 
K 9 HOH 1   201 116 HOH HOH F . 
K 9 HOH 2   202 287 HOH HOH F . 
K 9 HOH 3   203 86  HOH HOH F . 
K 9 HOH 4   204 236 HOH HOH F . 
K 9 HOH 5   205 281 HOH HOH F . 
K 9 HOH 6   206 143 HOH HOH F . 
K 9 HOH 7   207 92  HOH HOH F . 
K 9 HOH 8   208 291 HOH HOH F . 
K 9 HOH 9   209 82  HOH HOH F . 
K 9 HOH 10  210 124 HOH HOH F . 
K 9 HOH 11  211 255 HOH HOH F . 
K 9 HOH 12  212 115 HOH HOH F . 
K 9 HOH 13  213 23  HOH HOH F . 
K 9 HOH 14  214 31  HOH HOH F . 
K 9 HOH 15  215 264 HOH HOH F . 
K 9 HOH 16  216 44  HOH HOH F . 
K 9 HOH 17  217 64  HOH HOH F . 
K 9 HOH 18  218 195 HOH HOH F . 
K 9 HOH 19  219 29  HOH HOH F . 
K 9 HOH 20  220 104 HOH HOH F . 
K 9 HOH 21  221 151 HOH HOH F . 
K 9 HOH 22  222 20  HOH HOH F . 
K 9 HOH 23  223 191 HOH HOH F . 
K 9 HOH 24  224 157 HOH HOH F . 
K 9 HOH 25  225 22  HOH HOH F . 
K 9 HOH 26  226 73  HOH HOH F . 
K 9 HOH 27  227 15  HOH HOH F . 
K 9 HOH 28  228 114 HOH HOH F . 
K 9 HOH 29  229 38  HOH HOH F . 
K 9 HOH 30  230 50  HOH HOH F . 
K 9 HOH 31  231 75  HOH HOH F . 
K 9 HOH 32  232 9   HOH HOH F . 
K 9 HOH 33  233 85  HOH HOH F . 
K 9 HOH 34  234 30  HOH HOH F . 
K 9 HOH 35  235 187 HOH HOH F . 
K 9 HOH 36  236 133 HOH HOH F . 
K 9 HOH 37  237 84  HOH HOH F . 
K 9 HOH 38  238 47  HOH HOH F . 
K 9 HOH 39  239 183 HOH HOH F . 
K 9 HOH 40  240 120 HOH HOH F . 
K 9 HOH 41  241 251 HOH HOH F . 
K 9 HOH 42  242 66  HOH HOH F . 
K 9 HOH 43  243 25  HOH HOH F . 
K 9 HOH 44  244 45  HOH HOH F . 
K 9 HOH 45  245 231 HOH HOH F . 
K 9 HOH 46  246 186 HOH HOH F . 
K 9 HOH 47  247 67  HOH HOH F . 
K 9 HOH 48  248 170 HOH HOH F . 
K 9 HOH 49  249 219 HOH HOH F . 
K 9 HOH 50  250 224 HOH HOH F . 
K 9 HOH 51  251 227 HOH HOH F . 
K 9 HOH 52  252 241 HOH HOH F . 
K 9 HOH 53  253 245 HOH HOH F . 
K 9 HOH 54  254 240 HOH HOH F . 
K 9 HOH 55  255 212 HOH HOH F . 
K 9 HOH 56  256 101 HOH HOH F . 
K 9 HOH 57  257 60  HOH HOH F . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 40  ? CG  ? A LYS 40  CG  
2  1 Y 1 A LYS 40  ? CD  ? A LYS 40  CD  
3  1 Y 1 A LYS 40  ? CE  ? A LYS 40  CE  
4  1 Y 1 A LYS 40  ? NZ  ? A LYS 40  NZ  
5  1 Y 1 A LYS 163 ? CG  ? A LYS 163 CG  
6  1 Y 1 A LYS 163 ? CD  ? A LYS 163 CD  
7  1 Y 1 A LYS 163 ? CE  ? A LYS 163 CE  
8  1 Y 1 A LYS 163 ? NZ  ? A LYS 163 NZ  
9  1 Y 1 A GLU 220 ? CG  ? A GLU 220 CG  
10 1 Y 1 A GLU 220 ? CD  ? A GLU 220 CD  
11 1 Y 1 A GLU 220 ? OE1 ? A GLU 220 OE1 
12 1 Y 1 A GLU 220 ? OE2 ? A GLU 220 OE2 
13 1 Y 1 B ASN 48  ? CG  ? B ASN 48  CG  
14 1 Y 1 B ASN 48  ? OD1 ? B ASN 48  OD1 
15 1 Y 1 B ASN 48  ? ND2 ? B ASN 48  ND2 
16 1 Y 1 B THR 55  ? OG1 ? B THR 55  OG1 
17 1 Y 1 B THR 55  ? CG2 ? B THR 55  CG2 
18 1 Y 1 B ASN 57  ? CG  ? B ASN 57  CG  
19 1 Y 1 B ASN 57  ? OD1 ? B ASN 57  OD1 
20 1 Y 1 B ASN 57  ? ND2 ? B ASN 57  ND2 
21 1 Y 1 B GLN 94  ? CG  ? B GLN 94  CG  
22 1 Y 1 B GLN 94  ? CD  ? B GLN 94  CD  
23 1 Y 1 B GLN 94  ? OE1 ? B GLN 94  OE1 
24 1 Y 1 B GLN 94  ? NE2 ? B GLN 94  NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20_4459: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.9.0              2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? 0.9.0              3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20_4459          4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.71 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QLA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.530 
_cell.length_a_esd                 ? 
_cell.length_b                     92.580 
_cell.length_b_esd                 ? 
_cell.length_c                     83.990 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8QLA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QLA 
_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             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.45 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M Ammonium sulfate, 0.1M Bis/Tris-methane pH=5.5, 21% PEG 3000 (m/v)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI JUNGFRAU 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SwissFEL ARAMIS BEAMLINE ESA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ESA 
_diffrn_source.pdbx_synchrotron_site       'SwissFEL ARAMIS' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QLA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               11.09 
_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                                     122150 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                347.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.16 
_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                                   0.968 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   0.172 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.76 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.56 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12154 
_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                                  0.274 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  2.043 
_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                                 8QLA 
_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                            1.80 
_refine.ls_d_res_low                             9.49 
_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                     102263 
_refine.ls_number_reflns_R_free                  1972 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.85 
_refine.ls_percent_reflns_R_free                 1.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2667 
_refine.ls_R_factor_R_free                       0.3024 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2659 
_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                          0.00 
_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                 36.44 
_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                            0.28 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        9.49 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               8214 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7876 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         85 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 16262 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.645  ? 22090 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.706 ? 5934  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.044  ? 2454  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 2904  ? 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' 1.80 1.85 . . 140 7104 98.00 . . . . 0.3648 . . . . . . . . . . . 0.3662 
'X-RAY DIFFRACTION' 1.85 1.90 . . 142 7157 99.00 . . . . 0.3635 . . . . . . . . . . . 0.4239 
'X-RAY DIFFRACTION' 1.90 1.95 . . 143 7238 99.00 . . . . 0.3484 . . . . . . . . . . . 0.3479 
'X-RAY DIFFRACTION' 1.95 2.02 . . 142 7171 99.00 . . . . 0.3255 . . . . . . . . . . . 0.3584 
'X-RAY DIFFRACTION' 2.02 2.09 . . 140 7149 99.00 . . . . 0.3093 . . . . . . . . . . . 0.3763 
'X-RAY DIFFRACTION' 2.09 2.17 . . 141 7146 99.00 . . . . 0.3058 . . . . . . . . . . . 0.3938 
'X-RAY DIFFRACTION' 2.17 2.27 . . 143 7209 99.00 . . . . 0.2999 . . . . . . . . . . . 0.4169 
'X-RAY DIFFRACTION' 2.27 2.39 . . 139 7157 99.00 . . . . 0.2980 . . . . . . . . . . . 0.3404 
'X-RAY DIFFRACTION' 2.39 2.53 . . 140 7175 99.00 . . . . 0.2962 . . . . . . . . . . . 0.3870 
'X-RAY DIFFRACTION' 2.53 2.72 . . 139 7149 99.00 . . . . 0.2864 . . . . . . . . . . . 0.3397 
'X-RAY DIFFRACTION' 2.72 2.99 . . 142 7203 99.00 . . . . 0.2736 . . . . . . . . . . . 0.3041 
'X-RAY DIFFRACTION' 2.99 3.40 . . 142 7141 98.00 . . . . 0.2441 . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 3.40 4.23 . . 139 7143 98.00 . . . . 0.2245 . . . . . . . . . . . 0.2443 
'X-RAY DIFFRACTION' 4.23 9.49 . . 140 7149 97.00 . . . . 0.2407 . . . . . . . . . . . 0.2653 
# 
_struct.entry_id                     8QLA 
_struct.title                        
'Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution: 10 ns structure' 
_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        8QLA 
_struct_keywords.text            'Complex, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 8 ? 
I N N 9 ? 
J N N 9 ? 
K N N 9 ? 
# 
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_BOVIN P81947 ? 1 
;MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT
GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD
YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR
GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA
KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
;
1 
2 UNP TBB2B_BOVIN Q6B856 ? 2 
;MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP
FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP
DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR
MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG
EGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
;
1 
3 PDB 8QLA        8QLA   ? 3 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8QLA A 1 ? 451 ? P81947 1 ? 451 ? 1 451 
2 2 8QLA B 1 ? 445 ? Q6B856 1 ? 445 ? 1 445 
3 3 8QLA F 1 ? 169 ? 8QLA   1 ? 169 ? 1 169 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6270  ? 
1 MORE         -53   ? 
1 'SSA (A^2)'  37140 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 10  ? GLY A 29  ? GLY A 10  GLY A 29  1 ? 20 
HELX_P HELX_P2  AA2 SER A 48  ? THR A 51  ? SER A 48  THR A 51  5 ? 4  
HELX_P HELX_P3  AA3 PRO A 72  ? GLY A 81  ? PRO A 72  GLY A 81  1 ? 10 
HELX_P HELX_P4  AA4 THR A 82  ? LEU A 86  ? THR A 82  LEU A 86  5 ? 5  
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 ILE A 110 ? GLU A 113 ? ILE A 110 GLU A 113 5 ? 4  
HELX_P HELX_P8  AA8 ILE A 114 ? ASP A 127 ? ILE A 114 ASP A 127 1 ? 14 
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 ? THR A 193 ? VAL A 182 THR A 193 1 ? 12 
HELX_P HELX_P11 AB2 ASN A 206 ? ASN A 216 ? ASN A 206 ASN A 216 1 ? 11 
HELX_P HELX_P12 AB3 THR A 223 ? PHE A 244 ? THR A 223 PHE A 244 1 ? 22 
HELX_P HELX_P13 AB4 ASP A 251 ? VAL A 260 ? ASP A 251 VAL A 260 1 ? 10 
HELX_P HELX_P14 AB5 SER A 287 ? ALA A 294 ? SER A 287 ALA A 294 1 ? 8  
HELX_P HELX_P15 AB6 CYS A 295 ? GLN A 301 ? CYS A 295 GLN A 301 5 ? 7  
HELX_P HELX_P16 AB7 ASP A 306 ? GLY A 310 ? ASP A 306 GLY A 310 5 ? 5  
HELX_P HELX_P17 AB8 VAL A 324 ? LYS A 338 ? VAL A 324 LYS A 338 1 ? 15 
HELX_P HELX_P18 AB9 ILE A 384 ? ALA A 400 ? ILE A 384 ALA A 400 1 ? 17 
HELX_P HELX_P19 AC1 VAL A 405 ? GLY A 410 ? VAL A 405 GLY A 410 1 ? 6  
HELX_P HELX_P20 AC2 GLU A 415 ? GLY A 436 ? GLU A 415 GLY A 436 1 ? 22 
HELX_P HELX_P21 AC3 ALA B 9   ? GLY B 29  ? ALA B 9   GLY B 29  1 ? 21 
HELX_P HELX_P22 AC4 SER B 40  ? LEU B 44  ? SER B 40  LEU B 44  5 ? 5  
HELX_P HELX_P23 AC5 ARG B 46  ? VAL B 49  ? ARG B 46  VAL B 49  5 ? 4  
HELX_P HELX_P24 AC6 PRO B 70  ? SER B 78  ? PRO B 70  SER B 78  1 ? 9  
HELX_P HELX_P25 AC7 ARG B 86  ? PHE B 90  ? ARG B 86  PHE B 90  5 ? 5  
HELX_P HELX_P26 AC8 ASN B 100 ? TYR B 106 ? ASN B 100 TYR B 106 1 ? 7  
HELX_P HELX_P27 AC9 LEU B 112 ? SER B 126 ? LEU B 112 SER B 126 1 ? 15 
HELX_P HELX_P28 AD1 SER B 145 ? TYR B 159 ? SER B 145 TYR B 159 1 ? 15 
HELX_P HELX_P29 AD2 VAL B 180 ? THR B 196 ? VAL B 180 THR B 196 1 ? 17 
HELX_P HELX_P30 AD3 ASN B 204 ? THR B 214 ? ASN B 204 THR B 214 1 ? 11 
HELX_P HELX_P31 AD4 THR B 221 ? VAL B 236 ? THR B 221 VAL B 236 1 ? 16 
HELX_P HELX_P32 AD5 THR B 237 ? PHE B 242 ? THR B 237 PHE B 242 1 ? 6  
HELX_P HELX_P33 AD6 ASP B 249 ? VAL B 258 ? ASP B 249 VAL B 258 1 ? 10 
HELX_P HELX_P34 AD7 THR B 285 ? PHE B 294 ? THR B 285 PHE B 294 1 ? 10 
HELX_P HELX_P35 AD8 ASP B 304 ? GLY B 308 ? ASP B 304 GLY B 308 5 ? 5  
HELX_P HELX_P36 AD9 SER B 322 ? ASN B 337 ? SER B 322 ASN B 337 1 ? 16 
HELX_P HELX_P37 AE1 SER B 338 ? PHE B 341 ? SER B 338 PHE B 341 5 ? 4  
HELX_P HELX_P38 AE2 ILE B 374 ? ARG B 390 ? ILE B 374 ARG B 390 1 ? 17 
HELX_P HELX_P39 AE3 LEU B 395 ? GLY B 400 ? LEU B 395 GLY B 400 1 ? 6  
HELX_P HELX_P40 AE4 ASP B 404 ? ASP B 427 ? ASP B 404 ASP B 427 1 ? 24 
HELX_P HELX_P41 AE5 LEU C 14  ? GLY C 25  ? LEU F 14  GLY F 25  1 ? 12 
HELX_P HELX_P42 AE6 GLN C 26  ? ASN C 36  ? GLN F 26  ASN F 36  1 ? 11 
HELX_P HELX_P43 AE7 THR C 49  ? TYR C 57  ? THR F 49  TYR F 57  1 ? 9  
HELX_P HELX_P44 AE8 HIS C 59  ? LYS C 68  ? HIS F 59  LYS F 68  1 ? 10 
HELX_P HELX_P45 AE9 THR C 82  ? GLY C 91  ? THR F 82  GLY F 91  1 ? 10 
HELX_P HELX_P46 AF1 HIS C 92  ? HIS C 102 ? HIS F 92  HIS F 102 1 ? 11 
HELX_P HELX_P47 AF2 THR C 115 ? MET C 123 ? THR F 115 MET F 123 1 ? 9  
HELX_P HELX_P48 AF3 HIS C 125 ? HIS C 135 ? HIS F 125 HIS F 135 1 ? 11 
HELX_P HELX_P49 AF4 THR C 148 ? ASN C 156 ? THR F 148 ASN F 156 1 ? 9  
HELX_P HELX_P50 AF5 ASN C 158 ? LYS C 167 ? ASN F 158 LYS F 167 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 39 OD1 A ? ? 1_555 F CA  . CA A ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.552 ? ? 
metalc2  metalc ? ? A ASP 39 OD1 B ? ? 1_555 F CA  . CA B ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.730 ? ? 
metalc3  metalc ? ? A ASP 39 OD2 A ? ? 1_555 F CA  . CA A ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.491 ? ? 
metalc4  metalc ? ? A ASP 39 OD2 B ? ? 1_555 F CA  . CA B ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc5  metalc ? ? A THR 41 O   A ? ? 1_555 F CA  . CA A ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc6  metalc ? ? A THR 41 O   B ? ? 1_555 F CA  . CA B ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc7  metalc ? ? A THR 41 OG1 A ? ? 1_555 F CA  . CA A ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc8  metalc ? ? A THR 41 OG1 B ? ? 1_555 F CA  . CA B ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.536 ? ? 
metalc9  metalc ? ? A GLY 44 O   A ? ? 1_555 F CA  . CA A ? A GLY 44  A CA  503 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc10 metalc ? ? A GLY 44 O   B ? ? 1_555 F CA  . CA B ? A GLY 44  A CA  503 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc11 metalc ? ? A GLU 55 OE1 A ? ? 1_555 F CA  . CA A ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.781 ? ? 
metalc12 metalc ? ? A GLU 55 OE1 B ? ? 1_555 F CA  . CA B ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.670 ? ? 
metalc13 metalc ? ? A GLU 55 OE2 A ? ? 1_555 F CA  . CA A ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.746 ? ? 
metalc14 metalc ? ? A GLU 55 OE2 B ? ? 1_555 F CA  . CA B ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc15 metalc ? ? D GTP .  O1G A ? ? 1_555 E MG  . MG A ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 1.898 ? ? 
metalc16 metalc ? ? D GTP .  O1G B ? ? 1_555 E MG  . MG B ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc17 metalc ? ? D GTP .  O2G A ? ? 1_555 E MG  . MG A ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.976 ? ? 
metalc18 metalc ? ? D GTP .  O2B A ? ? 1_555 E MG  . MG A ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.689 ? ? 
metalc19 metalc ? ? D GTP .  O2B B ? ? 1_555 E MG  . MG B ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc20 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 615 1_555 ? ? ? ? ? ? ? 2.642 ? ? 
metalc21 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 615 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc22 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 620 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc23 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 620 1_555 ? ? ? ? ? ? ? 2.178 ? ? 
metalc24 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 621 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
metalc25 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 621 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc26 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 626 1_555 ? ? ? ? ? ? ? 1.919 ? ? 
metalc27 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 626 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OD2 A A ASP 39 ? A ASP 39  ? 1_555 51.6  ? 
2  OD1 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 O   A A THR 41 ? A THR 41  ? 1_555 89.3  ? 
3  OD2 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 O   A A THR 41 ? A THR 41  ? 1_555 91.1  ? 
4  OD1 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OG1 A A THR 41 ? A THR 41  ? 1_555 81.8  ? 
5  OD2 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OG1 A A THR 41 ? A THR 41  ? 1_555 131.2 ? 
6  O   A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OG1 A A THR 41 ? A THR 41  ? 1_555 72.6  ? 
7  OD1 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 O   A A GLY 44 ? A GLY 44  ? 1_555 161.5 ? 
8  OD2 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 O   A A GLY 44 ? A GLY 44  ? 1_555 140.2 ? 
9  O   A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 O   A A GLY 44 ? A GLY 44  ? 1_555 77.6  ? 
10 OG1 A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 O   A A GLY 44 ? A GLY 44  ? 1_555 81.9  ? 
11 OD1 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE1 A A GLU 55 ? A GLU 55  ? 1_555 114.7 ? 
12 OD2 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE1 A A GLU 55 ? A GLU 55  ? 1_555 64.6  ? 
13 O   A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE1 A A GLU 55 ? A GLU 55  ? 1_555 78.4  ? 
14 OG1 A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE1 A A GLU 55 ? A GLU 55  ? 1_555 146.4 ? 
15 O   A A GLY 44 ? A GLY 44  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE1 A A GLU 55 ? A GLU 55  ? 1_555 75.7  ? 
16 OD1 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE2 A A GLU 55 ? A GLU 55  ? 1_555 111.9 ? 
17 OD2 A A ASP 39 ? A ASP 39  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE2 A A GLU 55 ? A GLU 55  ? 1_555 69.2  ? 
18 O   A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE2 A A GLU 55 ? A GLU 55  ? 1_555 125.2 ? 
19 OG1 A A THR 41 ? A THR 41  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE2 A A GLU 55 ? A GLU 55  ? 1_555 155.9 ? 
20 O   A A GLY 44 ? A GLY 44  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE2 A A GLU 55 ? A GLU 55  ? 1_555 86.4  ? 
21 OE1 A A GLU 55 ? A GLU 55  ? 1_555 CA A F CA . ? A CA 503 ? 1_555 OE2 A A GLU 55 ? A GLU 55  ? 1_555 46.9  ? 
22 OD1 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OD2 B A ASP 39 ? A ASP 39  ? 1_555 50.9  ? 
23 OD1 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 O   B A THR 41 ? A THR 41  ? 1_555 74.3  ? 
24 OD2 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 O   B A THR 41 ? A THR 41  ? 1_555 81.2  ? 
25 OD1 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OG1 B A THR 41 ? A THR 41  ? 1_555 65.9  ? 
26 OD2 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OG1 B A THR 41 ? A THR 41  ? 1_555 115.4 ? 
27 O   B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OG1 B A THR 41 ? A THR 41  ? 1_555 69.4  ? 
28 OD1 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 O   B A GLY 44 ? A GLY 44  ? 1_555 149.2 ? 
29 OD2 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 O   B A GLY 44 ? A GLY 44  ? 1_555 149.1 ? 
30 O   B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 O   B A GLY 44 ? A GLY 44  ? 1_555 85.7  ? 
31 OG1 B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 O   B A GLY 44 ? A GLY 44  ? 1_555 85.4  ? 
32 OD1 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE1 B A GLU 55 ? A GLU 55  ? 1_555 126.3 ? 
33 OD2 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE1 B A GLU 55 ? A GLU 55  ? 1_555 78.9  ? 
34 O   B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE1 B A GLU 55 ? A GLU 55  ? 1_555 81.2  ? 
35 OG1 B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE1 B A GLU 55 ? A GLU 55  ? 1_555 143.9 ? 
36 O   B A GLY 44 ? A GLY 44  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE1 B A GLU 55 ? A GLU 55  ? 1_555 71.5  ? 
37 OD1 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE2 B A GLU 55 ? A GLU 55  ? 1_555 121.2 ? 
38 OD2 B A ASP 39 ? A ASP 39  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE2 B A GLU 55 ? A GLU 55  ? 1_555 78.0  ? 
39 O   B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE2 B A GLU 55 ? A GLU 55  ? 1_555 130.1 ? 
40 OG1 B A THR 41 ? A THR 41  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE2 B A GLU 55 ? A GLU 55  ? 1_555 159.4 ? 
41 O   B A GLY 44 ? A GLY 44  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE2 B A GLU 55 ? A GLU 55  ? 1_555 89.6  ? 
42 OE1 B A GLU 55 ? A GLU 55  ? 1_555 CA B F CA . ? A CA 503 ? 1_555 OE2 B A GLU 55 ? A GLU 55  ? 1_555 50.6  ? 
43 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O2G A D GTP .  ? A GTP 501 ? 1_555 56.1  ? 
44 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O2B A D GTP .  ? A GTP 501 ? 1_555 86.1  ? 
45 O2G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O2B A D GTP .  ? A GTP 501 ? 1_555 74.5  ? 
46 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 615 ? 1_555 59.6  ? 
47 O2G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 615 ? 1_555 113.9 ? 
48 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 615 ? 1_555 87.8  ? 
49 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 84.8  ? 
50 O2G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 100.1 ? 
51 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 170.9 ? 
52 O   ? I HOH .  ? A HOH 615 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 87.7  ? 
53 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 109.5 ? 
54 O2G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 53.5  ? 
55 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 75.6  ? 
56 O   ? I HOH .  ? A HOH 615 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 161.2 ? 
57 O   ? I HOH .  ? A HOH 620 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 107.4 ? 
58 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 146.0 ? 
59 O2G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 158.0 ? 
60 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 101.8 ? 
61 O   ? I HOH .  ? A HOH 615 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 87.3  ? 
62 O   ? I HOH .  ? A HOH 620 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 86.0  ? 
63 O   ? I HOH .  ? A HOH 621 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 104.5 ? 
64 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O2B B D GTP .  ? A GTP 501 ? 1_555 93.8  ? 
65 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 615 ? 1_555 96.1  ? 
66 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 615 ? 1_555 85.2  ? 
67 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 92.8  ? 
68 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 172.0 ? 
69 O   ? I HOH .  ? A HOH 615 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 620 ? 1_555 98.6  ? 
70 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 88.7  ? 
71 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 88.0  ? 
72 O   ? I HOH .  ? A HOH 615 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 171.9 ? 
73 O   ? I HOH .  ? A HOH 620 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 621 ? 1_555 87.7  ? 
74 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 165.2 ? 
75 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 97.3  ? 
76 O   ? I HOH .  ? A HOH 615 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 94.6  ? 
77 O   ? I HOH .  ? A HOH 620 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 75.4  ? 
78 O   ? I HOH .  ? A HOH 621 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 626 ? 1_555 81.9  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 273 A . ? ALA 273 A PRO 274 A ? PRO 274 A 1 -1.01 
2 ALA 273 A . ? ALA 273 A PRO 274 A ? PRO 274 A 1 -4.60 
3 ALA 271 B . ? ALA 271 B PRO 272 B ? PRO 272 B 1 -1.29 
4 ALA 271 B . ? ALA 271 B PRO 272 B ? PRO 272 B 1 -1.09 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 2  ? 
AA3 ? 4  ? 
AA4 ? 6  ? 
AA5 ? 10 ? 
AA6 ? 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      
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA4 5 6  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? parallel      
AA6 1 2  ? anti-parallel 
# 
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 ? PHE A 138 ? GLY A 134 PHE A 138 
AA1 5  SER A 165 ? TYR A 172 ? SER A 165 TYR A 172 
AA1 6  CYS A 200 ? ASP A 205 ? CYS A 200 ASP A 205 
AA2 1  PHE A 53  ? GLU A 55  ? PHE A 53  GLU A 55  
AA2 2  HIS A 61  ? PRO A 63  ? HIS A 61  PRO A 63  
AA3 1  LEU A 269 ? ALA A 273 ? LEU A 269 ALA A 273 
AA3 2  ARG A 373 ? THR A 381 ? ARG A 373 THR A 381 
AA3 3  TYR A 312 ? GLY A 321 ? TYR A 312 GLY A 321 
AA3 4  LYS A 352 ? ASN A 356 ? LYS A 352 ASN A 356 
AA4 1  VAL B 91  ? PHE B 92  ? VAL B 91  PHE B 92  
AA4 2  ALA B 63  ? ASP B 67  ? ALA B 63  ASP B 67  
AA4 3  GLU B 3   ? GLN B 8   ? GLU B 3   GLN B 8   
AA4 4  LEU B 130 ? SER B 138 ? LEU B 130 SER B 138 
AA4 5  ILE B 163 ? MET B 170 ? ILE B 163 MET B 170 
AA4 6  ILE B 202 ? ASP B 203 ? ILE B 202 ASP B 203 
AA5 1  VAL B 91  ? PHE B 92  ? VAL B 91  PHE B 92  
AA5 2  ALA B 63  ? ASP B 67  ? ALA B 63  ASP B 67  
AA5 3  GLU B 3   ? GLN B 8   ? GLU B 3   GLN B 8   
AA5 4  LEU B 130 ? SER B 138 ? LEU B 130 SER B 138 
AA5 5  ILE B 163 ? MET B 170 ? ILE B 163 MET B 170 
AA5 6  GLU B 198 ? TYR B 200 ? GLU B 198 TYR B 200 
AA5 7  PHE B 265 ? ALA B 271 ? PHE B 265 ALA B 271 
AA5 8  SER B 364 ? SER B 371 ? SER B 364 SER B 371 
AA5 9  TYR B 310 ? ARG B 318 ? TYR B 310 ARG B 318 
AA5 10 VAL B 349 ? ALA B 352 ? VAL B 349 ALA B 352 
AA6 1  TYR B 51  ? ALA B 54  ? TYR B 51  ALA B 54  
AA6 2  LYS B 58  ? PRO B 61  ? LYS B 58  PRO B 61  
# 
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 PHE A 135 ? N PHE A 135 O SER A 165 ? O SER A 165 
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 LEU A 269 ? N LEU A 269 O SER A 379 ? O SER A 379 
AA3 2 3  O ASN A 380 ? O ASN A 380 N ALA A 314 ? N ALA A 314 
AA3 3 4  N LEU A 317 ? N LEU A 317 O LYS A 352 ? O LYS A 352 
AA4 1 2  O VAL B 91  ? O VAL B 91  N LEU B 65  ? N LEU B 65  
AA4 2 3  O VAL B 66  ? O VAL B 66  N GLN B 8   ? N GLN B 8   
AA4 3 4  N GLU B 3   ? N GLU B 3   O GLN B 131 ? O GLN B 131 
AA4 4 5  N PHE B 133 ? N PHE B 133 O ASN B 165 ? O ASN B 165 
AA4 5 6  N SER B 168 ? N SER B 168 O ILE B 202 ? O ILE B 202 
AA5 1 2  O VAL B 91  ? O VAL B 91  N LEU B 65  ? N LEU B 65  
AA5 2 3  O VAL B 66  ? O VAL B 66  N GLN B 8   ? N GLN B 8   
AA5 3 4  N GLU B 3   ? N GLU B 3   O GLN B 131 ? O GLN B 131 
AA5 4 5  N PHE B 133 ? N PHE B 133 O ASN B 165 ? O ASN B 165 
AA5 5 6  N THR B 166 ? N THR B 166 O TYR B 200 ? O TYR B 200 
AA5 6 7  N THR B 199 ? N THR B 199 O PHE B 266 ? O PHE B 266 
AA5 7 8  N GLY B 269 ? N GLY B 269 O PHE B 367 ? O PHE B 367 
AA5 8 9  O ILE B 368 ? O ILE B 368 N ALA B 314 ? N ALA B 314 
AA5 9 10 N ALA B 315 ? N ALA B 315 O LYS B 350 ? O LYS B 350 
AA6 1 2  N ASN B 52  ? N ASN B 52  O VAL B 60  ? O VAL B 60  
# 
_pdbx_entry_details.entry_id                   8QLA 
_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 OE1 F GLU 94  ? B O F HOH 201 ? ? 2.13 
2  1 O   A LYS 164 ? A O A HOH 601 ? ? 2.14 
3  1 O   A HOH 609 ? ? O A HOH 703 ? ? 2.15 
4  1 O   A THR 82  ? A O A HOH 602 ? ? 2.16 
5  1 O   A HOH 618 ? ? O A HOH 720 ? ? 2.16 
6  1 O   A LEU 269 ? A O A HOH 603 ? ? 2.16 
7  1 O   F HOH 218 ? ? O F HOH 251 ? ? 2.17 
8  1 NH1 F ARG 31  ? B O F HOH 202 ? ? 2.17 
9  1 O   F LEU 67  ? A O F HOH 203 ? ? 2.19 
10 1 O   A GLY 95  ? A O A HOH 604 ? ? 2.19 
11 1 O   B PHE 294 ? B O B HOH 601 ? ? 2.19 
12 1 NE2 B GLN 11  ? A O B HOH 602 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 83  ? A -91.15  33.24   
2  1 TYR A 108 ? A -113.04 -76.16  
3  1 THR A 109 ? B -103.79 -81.11  
4  1 THR A 179 ? A -121.26 -58.12  
5  1 HIS A 266 ? B -108.17 41.26   
6  1 LYS A 280 ? B -103.29 70.28   
7  1 CYS A 315 ? B -163.96 109.83  
8  1 ASP A 322 ? A -69.85  83.88   
9  1 ILE A 335 ? B -82.87  42.82   
10 1 THR A 337 ? B -136.40 -36.86  
11 1 THR A 349 ? A -61.92  94.72   
12 1 TYR A 357 ? A -87.92  33.79   
13 1 PHE A 404 ? B 68.47   -3.14   
14 1 ARG B 2   ? A -139.19 -39.81  
15 1 ARG B 2   ? B -142.60 -94.21  
16 1 ASP B 39  ? A -157.65 45.13   
17 1 ARG B 46  ? A -109.10 41.39   
18 1 ASP B 67  ? A -171.77 147.23  
19 1 PHE B 81  ? A -95.61  37.88   
20 1 GLN B 94  ? B -90.81  -72.37  
21 1 THR B 107 ? A -116.58 -84.47  
22 1 THR B 107 ? B -116.84 -91.63  
23 1 CYS B 129 ? B -153.40 86.41   
24 1 PHE B 167 ? A -110.18 76.32   
25 1 PRO B 243 ? A -60.72  -86.30  
26 1 ASN B 247 ? A -97.42  59.30   
27 1 ASN B 247 ? B -62.42  82.21   
28 1 LEU B 263 ? A -105.21 71.56   
29 1 ALA B 302 ? A -68.93  70.78   
30 1 ALA B 365 ? A -162.79 111.74  
31 1 ASP F 39  ? A -56.77  107.34  
32 1 ASP F 44  ? A -94.11  -158.23 
33 1 ASP F 143 ? A -88.84  -157.93 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 723 ? 5.84 . 
2 1 O ? B HOH 671 ? 5.98 . 
3 1 O ? B HOH 672 ? 6.28 . 
4 1 O ? B HOH 673 ? 6.43 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 438 ? A ASP 438 
2  1 Y 1 A SER 439 ? A SER 439 
3  1 Y 1 A VAL 440 ? A VAL 440 
4  1 Y 1 A GLU 441 ? A GLU 441 
5  1 Y 1 A GLY 442 ? A GLY 442 
6  1 Y 1 A GLU 443 ? A GLU 443 
7  1 Y 1 A GLY 444 ? A GLY 444 
8  1 Y 1 A GLU 445 ? A GLU 445 
9  1 Y 1 A GLU 446 ? A GLU 446 
10 1 Y 1 A GLU 447 ? A GLU 447 
11 1 Y 1 A GLY 448 ? A GLY 448 
12 1 Y 1 A GLU 449 ? A GLU 449 
13 1 Y 1 A GLU 450 ? A GLU 450 
14 1 Y 1 A TYR 451 ? A TYR 451 
15 1 Y 1 B GLN 279 ? B GLN 279 
16 1 Y 1 B GLN 280 ? B GLN 280 
17 1 Y 1 B TYR 281 ? B TYR 281 
18 1 Y 1 B ARG 282 ? B ARG 282 
19 1 Y 1 B ALA 283 ? B ALA 283 
20 1 Y 1 B ALA 430 ? B ALA 430 
21 1 Y 1 B ASP 431 ? B ASP 431 
22 1 Y 1 B GLU 432 ? B GLU 432 
23 1 Y 1 B GLN 433 ? B GLN 433 
24 1 Y 1 B GLY 434 ? B GLY 434 
25 1 Y 1 B GLU 435 ? B GLU 435 
26 1 Y 1 B PHE 436 ? B PHE 436 
27 1 Y 1 B GLU 437 ? B GLU 437 
28 1 Y 1 B GLU 438 ? B GLU 438 
29 1 Y 1 B GLU 439 ? B GLU 439 
30 1 Y 1 B GLU 440 ? B GLU 440 
31 1 Y 1 B GLY 441 ? B GLY 441 
32 1 Y 1 B GLU 442 ? B GLU 442 
33 1 Y 1 B ASP 443 ? B ASP 443 
34 1 Y 1 B GLU 444 ? B GLU 444 
35 1 Y 1 B ALA 445 ? B ALA 445 
36 1 Y 1 F MET 1   ? C MET 1   
37 1 Y 1 F ARG 2   ? C ARG 2   
38 1 Y 1 F GLY 3   ? C GLY 3   
39 1 Y 1 F SER 4   ? C SER 4   
40 1 Y 1 F HIS 5   ? C HIS 5   
41 1 Y 1 F HIS 6   ? C HIS 6   
42 1 Y 1 F HIS 7   ? C HIS 7   
43 1 Y 1 F HIS 8   ? C HIS 8   
44 1 Y 1 F HIS 9   ? C HIS 9   
45 1 Y 1 F HIS 10  ? C HIS 10  
46 1 Y 1 F GLY 11  ? C GLY 11  
47 1 Y 1 F SER 12  ? C SER 12  
48 1 Y 1 F LEU 168 ? C LEU 168 
49 1 Y 1 F ASN 169 ? C ASN 169 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CA  CA     CA N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
GDP PB     P  N N 89  
GDP O1B    O  N N 90  
GDP O2B    O  N N 91  
GDP O3B    O  N N 92  
GDP O3A    O  N N 93  
GDP PA     P  N N 94  
GDP O1A    O  N N 95  
GDP O2A    O  N N 96  
GDP "O5'"  O  N N 97  
GDP "C5'"  C  N N 98  
GDP "C4'"  C  N R 99  
GDP "O4'"  O  N N 100 
GDP "C3'"  C  N S 101 
GDP "O3'"  O  N N 102 
GDP "C2'"  C  N R 103 
GDP "O2'"  O  N N 104 
GDP "C1'"  C  N R 105 
GDP N9     N  Y N 106 
GDP C8     C  Y N 107 
GDP N7     N  Y N 108 
GDP C5     C  Y N 109 
GDP C6     C  N N 110 
GDP O6     O  N N 111 
GDP N1     N  N N 112 
GDP C2     C  N N 113 
GDP N2     N  N N 114 
GDP N3     N  N N 115 
GDP C4     C  Y N 116 
GDP HOB2   H  N N 117 
GDP HOB3   H  N N 118 
GDP HOA2   H  N N 119 
GDP "H5'"  H  N N 120 
GDP "H5''" H  N N 121 
GDP "H4'"  H  N N 122 
GDP "H3'"  H  N N 123 
GDP "HO3'" H  N N 124 
GDP "H2'"  H  N N 125 
GDP "HO2'" H  N N 126 
GDP "H1'"  H  N N 127 
GDP H8     H  N N 128 
GDP HN1    H  N N 129 
GDP HN21   H  N N 130 
GDP HN22   H  N N 131 
GLN N      N  N N 132 
GLN CA     C  N S 133 
GLN C      C  N N 134 
GLN O      O  N N 135 
GLN CB     C  N N 136 
GLN CG     C  N N 137 
GLN CD     C  N N 138 
GLN OE1    O  N N 139 
GLN NE2    N  N N 140 
GLN OXT    O  N N 141 
GLN H      H  N N 142 
GLN H2     H  N N 143 
GLN HA     H  N N 144 
GLN HB2    H  N N 145 
GLN HB3    H  N N 146 
GLN HG2    H  N N 147 
GLN HG3    H  N N 148 
GLN HE21   H  N N 149 
GLN HE22   H  N N 150 
GLN HXT    H  N N 151 
GLU N      N  N N 152 
GLU CA     C  N S 153 
GLU C      C  N N 154 
GLU O      O  N N 155 
GLU CB     C  N N 156 
GLU CG     C  N N 157 
GLU CD     C  N N 158 
GLU OE1    O  N N 159 
GLU OE2    O  N N 160 
GLU OXT    O  N N 161 
GLU H      H  N N 162 
GLU H2     H  N N 163 
GLU HA     H  N N 164 
GLU HB2    H  N N 165 
GLU HB3    H  N N 166 
GLU HG2    H  N N 167 
GLU HG3    H  N N 168 
GLU HE2    H  N N 169 
GLU HXT    H  N N 170 
GLY N      N  N N 171 
GLY CA     C  N N 172 
GLY C      C  N N 173 
GLY O      O  N N 174 
GLY OXT    O  N N 175 
GLY H      H  N N 176 
GLY H2     H  N N 177 
GLY HA2    H  N N 178 
GLY HA3    H  N N 179 
GLY HXT    H  N N 180 
GTP PG     P  N N 181 
GTP O1G    O  N N 182 
GTP O2G    O  N N 183 
GTP O3G    O  N N 184 
GTP O3B    O  N N 185 
GTP PB     P  N N 186 
GTP O1B    O  N N 187 
GTP O2B    O  N N 188 
GTP O3A    O  N N 189 
GTP PA     P  N N 190 
GTP O1A    O  N N 191 
GTP O2A    O  N N 192 
GTP "O5'"  O  N N 193 
GTP "C5'"  C  N N 194 
GTP "C4'"  C  N R 195 
GTP "O4'"  O  N N 196 
GTP "C3'"  C  N S 197 
GTP "O3'"  O  N N 198 
GTP "C2'"  C  N R 199 
GTP "O2'"  O  N N 200 
GTP "C1'"  C  N R 201 
GTP N9     N  Y N 202 
GTP C8     C  Y N 203 
GTP N7     N  Y N 204 
GTP C5     C  Y N 205 
GTP C6     C  N N 206 
GTP O6     O  N N 207 
GTP N1     N  N N 208 
GTP C2     C  N N 209 
GTP N2     N  N N 210 
GTP N3     N  N N 211 
GTP C4     C  Y N 212 
GTP HOG2   H  N N 213 
GTP HOG3   H  N N 214 
GTP HOB2   H  N N 215 
GTP HOA2   H  N N 216 
GTP "H5'"  H  N N 217 
GTP "H5''" H  N N 218 
GTP "H4'"  H  N N 219 
GTP "H3'"  H  N N 220 
GTP "HO3'" H  N N 221 
GTP "H2'"  H  N N 222 
GTP "HO2'" H  N N 223 
GTP "H1'"  H  N N 224 
GTP H8     H  N N 225 
GTP HN1    H  N N 226 
GTP HN21   H  N N 227 
GTP HN22   H  N N 228 
HIS N      N  N N 229 
HIS CA     C  N S 230 
HIS C      C  N N 231 
HIS O      O  N N 232 
HIS CB     C  N N 233 
HIS CG     C  Y N 234 
HIS ND1    N  Y N 235 
HIS CD2    C  Y N 236 
HIS CE1    C  Y N 237 
HIS NE2    N  Y N 238 
HIS OXT    O  N N 239 
HIS H      H  N N 240 
HIS H2     H  N N 241 
HIS HA     H  N N 242 
HIS HB2    H  N N 243 
HIS HB3    H  N N 244 
HIS HD1    H  N N 245 
HIS HD2    H  N N 246 
HIS HE1    H  N N 247 
HIS HE2    H  N N 248 
HIS HXT    H  N N 249 
HOH O      O  N N 250 
HOH H1     H  N N 251 
HOH H2     H  N N 252 
IBL N1     N  N N 253 
IBL C7     C  Y N 254 
IBL C8     C  N N 255 
IBL C9     C  Y N 256 
IBL O1     O  N N 257 
IBL C1     C  Y N 258 
IBL C5     C  Y N 259 
IBL C6     C  Y N 260 
IBL C4     C  Y N 261 
IBL O4     O  N N 262 
IBL C3     C  Y N 263 
IBL O3     O  N N 264 
IBL C2     C  Y N 265 
IBL N      N  N N 266 
IBL C      C  N N 267 
IBL O      O  N N 268 
IBL C10    C  N N 269 
IBL C11    C  Y N 270 
IBL C12    C  N N 271 
IBL C13    C  Y N 272 
IBL C14    C  Y N 273 
IBL C15    C  Y N 274 
IBL O2     O  N N 275 
IBL H6     H  N N 276 
IBL H8     H  N N 277 
IBL H7     H  N N 278 
IBL H5     H  N N 279 
IBL H17    H  N N 280 
IBL H4     H  N N 281 
IBL H3     H  N N 282 
IBL H      H  N N 283 
IBL H2     H  N N 284 
IBL H1     H  N N 285 
IBL H10    H  N N 286 
IBL H11    H  N N 287 
IBL H9     H  N N 288 
IBL H14    H  N N 289 
IBL H13    H  N N 290 
IBL H12    H  N N 291 
IBL H15    H  N N 292 
IBL H16    H  N N 293 
ILE N      N  N N 294 
ILE CA     C  N S 295 
ILE C      C  N N 296 
ILE O      O  N N 297 
ILE CB     C  N S 298 
ILE CG1    C  N N 299 
ILE CG2    C  N N 300 
ILE CD1    C  N N 301 
ILE OXT    O  N N 302 
ILE H      H  N N 303 
ILE H2     H  N N 304 
ILE HA     H  N N 305 
ILE HB     H  N N 306 
ILE HG12   H  N N 307 
ILE HG13   H  N N 308 
ILE HG21   H  N N 309 
ILE HG22   H  N N 310 
ILE HG23   H  N N 311 
ILE HD11   H  N N 312 
ILE HD12   H  N N 313 
ILE HD13   H  N N 314 
ILE HXT    H  N N 315 
LEU N      N  N N 316 
LEU CA     C  N S 317 
LEU C      C  N N 318 
LEU O      O  N N 319 
LEU CB     C  N N 320 
LEU CG     C  N N 321 
LEU CD1    C  N N 322 
LEU CD2    C  N N 323 
LEU OXT    O  N N 324 
LEU H      H  N N 325 
LEU H2     H  N N 326 
LEU HA     H  N N 327 
LEU HB2    H  N N 328 
LEU HB3    H  N N 329 
LEU HG     H  N N 330 
LEU HD11   H  N N 331 
LEU HD12   H  N N 332 
LEU HD13   H  N N 333 
LEU HD21   H  N N 334 
LEU HD22   H  N N 335 
LEU HD23   H  N N 336 
LEU HXT    H  N N 337 
LYS N      N  N N 338 
LYS CA     C  N S 339 
LYS C      C  N N 340 
LYS O      O  N N 341 
LYS CB     C  N N 342 
LYS CG     C  N N 343 
LYS CD     C  N N 344 
LYS CE     C  N N 345 
LYS NZ     N  N N 346 
LYS OXT    O  N N 347 
LYS H      H  N N 348 
LYS H2     H  N N 349 
LYS HA     H  N N 350 
LYS HB2    H  N N 351 
LYS HB3    H  N N 352 
LYS HG2    H  N N 353 
LYS HG3    H  N N 354 
LYS HD2    H  N N 355 
LYS HD3    H  N N 356 
LYS HE2    H  N N 357 
LYS HE3    H  N N 358 
LYS HZ1    H  N N 359 
LYS HZ2    H  N N 360 
LYS HZ3    H  N N 361 
LYS HXT    H  N N 362 
MET N      N  N N 363 
MET CA     C  N S 364 
MET C      C  N N 365 
MET O      O  N N 366 
MET CB     C  N N 367 
MET CG     C  N N 368 
MET SD     S  N N 369 
MET CE     C  N N 370 
MET OXT    O  N N 371 
MET H      H  N N 372 
MET H2     H  N N 373 
MET HA     H  N N 374 
MET HB2    H  N N 375 
MET HB3    H  N N 376 
MET HG2    H  N N 377 
MET HG3    H  N N 378 
MET HE1    H  N N 379 
MET HE2    H  N N 380 
MET HE3    H  N N 381 
MET HXT    H  N N 382 
MG  MG     MG N N 383 
PHE N      N  N N 384 
PHE CA     C  N S 385 
PHE C      C  N N 386 
PHE O      O  N N 387 
PHE CB     C  N N 388 
PHE CG     C  Y N 389 
PHE CD1    C  Y N 390 
PHE CD2    C  Y N 391 
PHE CE1    C  Y N 392 
PHE CE2    C  Y N 393 
PHE CZ     C  Y N 394 
PHE OXT    O  N N 395 
PHE H      H  N N 396 
PHE H2     H  N N 397 
PHE HA     H  N N 398 
PHE HB2    H  N N 399 
PHE HB3    H  N N 400 
PHE HD1    H  N N 401 
PHE HD2    H  N N 402 
PHE HE1    H  N N 403 
PHE HE2    H  N N 404 
PHE HZ     H  N N 405 
PHE HXT    H  N N 406 
PRO N      N  N N 407 
PRO CA     C  N S 408 
PRO C      C  N N 409 
PRO O      O  N N 410 
PRO CB     C  N N 411 
PRO CG     C  N N 412 
PRO CD     C  N N 413 
PRO OXT    O  N N 414 
PRO H      H  N N 415 
PRO HA     H  N N 416 
PRO HB2    H  N N 417 
PRO HB3    H  N N 418 
PRO HG2    H  N N 419 
PRO HG3    H  N N 420 
PRO HD2    H  N N 421 
PRO HD3    H  N N 422 
PRO HXT    H  N N 423 
SER N      N  N N 424 
SER CA     C  N S 425 
SER C      C  N N 426 
SER O      O  N N 427 
SER CB     C  N N 428 
SER OG     O  N N 429 
SER OXT    O  N N 430 
SER H      H  N N 431 
SER H2     H  N N 432 
SER HA     H  N N 433 
SER HB2    H  N N 434 
SER HB3    H  N N 435 
SER HG     H  N N 436 
SER HXT    H  N N 437 
THR N      N  N N 438 
THR CA     C  N S 439 
THR C      C  N N 440 
THR O      O  N N 441 
THR CB     C  N R 442 
THR OG1    O  N N 443 
THR CG2    C  N N 444 
THR OXT    O  N N 445 
THR H      H  N N 446 
THR H2     H  N N 447 
THR HA     H  N N 448 
THR HB     H  N N 449 
THR HG1    H  N N 450 
THR HG21   H  N N 451 
THR HG22   H  N N 452 
THR HG23   H  N N 453 
THR HXT    H  N N 454 
TRP N      N  N N 455 
TRP CA     C  N S 456 
TRP C      C  N N 457 
TRP O      O  N N 458 
TRP CB     C  N N 459 
TRP CG     C  Y N 460 
TRP CD1    C  Y N 461 
TRP CD2    C  Y N 462 
TRP NE1    N  Y N 463 
TRP CE2    C  Y N 464 
TRP CE3    C  Y N 465 
TRP CZ2    C  Y N 466 
TRP CZ3    C  Y N 467 
TRP CH2    C  Y N 468 
TRP OXT    O  N N 469 
TRP H      H  N N 470 
TRP H2     H  N N 471 
TRP HA     H  N N 472 
TRP HB2    H  N N 473 
TRP HB3    H  N N 474 
TRP HD1    H  N N 475 
TRP HE1    H  N N 476 
TRP HE3    H  N N 477 
TRP HZ2    H  N N 478 
TRP HZ3    H  N N 479 
TRP HH2    H  N N 480 
TRP HXT    H  N N 481 
TYR N      N  N N 482 
TYR CA     C  N S 483 
TYR C      C  N N 484 
TYR O      O  N N 485 
TYR CB     C  N N 486 
TYR CG     C  Y N 487 
TYR CD1    C  Y N 488 
TYR CD2    C  Y N 489 
TYR CE1    C  Y N 490 
TYR CE2    C  Y N 491 
TYR CZ     C  Y N 492 
TYR OH     O  N N 493 
TYR OXT    O  N N 494 
TYR H      H  N N 495 
TYR H2     H  N N 496 
TYR HA     H  N N 497 
TYR HB2    H  N N 498 
TYR HB3    H  N N 499 
TYR HD1    H  N N 500 
TYR HD2    H  N N 501 
TYR HE1    H  N N 502 
TYR HE2    H  N N 503 
TYR HH     H  N N 504 
TYR HXT    H  N N 505 
VAL N      N  N N 506 
VAL CA     C  N S 507 
VAL C      C  N N 508 
VAL O      O  N N 509 
VAL CB     C  N N 510 
VAL CG1    C  N N 511 
VAL CG2    C  N N 512 
VAL OXT    O  N N 513 
VAL H      H  N N 514 
VAL H2     H  N N 515 
VAL HA     H  N N 516 
VAL HB     H  N N 517 
VAL HG11   H  N N 518 
VAL HG12   H  N N 519 
VAL HG13   H  N N 520 
VAL HG21   H  N N 521 
VAL HG22   H  N N 522 
VAL HG23   H  N N 523 
VAL HXT    H  N N 524 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GDP PB    O1B    doub N N 83  
GDP PB    O2B    sing N N 84  
GDP PB    O3B    sing N N 85  
GDP PB    O3A    sing N N 86  
GDP O2B   HOB2   sing N N 87  
GDP O3B   HOB3   sing N N 88  
GDP O3A   PA     sing N N 89  
GDP PA    O1A    doub N N 90  
GDP PA    O2A    sing N N 91  
GDP PA    "O5'"  sing N N 92  
GDP O2A   HOA2   sing N N 93  
GDP "O5'" "C5'"  sing N N 94  
GDP "C5'" "C4'"  sing N N 95  
GDP "C5'" "H5'"  sing N N 96  
GDP "C5'" "H5''" sing N N 97  
GDP "C4'" "O4'"  sing N N 98  
GDP "C4'" "C3'"  sing N N 99  
GDP "C4'" "H4'"  sing N N 100 
GDP "O4'" "C1'"  sing N N 101 
GDP "C3'" "O3'"  sing N N 102 
GDP "C3'" "C2'"  sing N N 103 
GDP "C3'" "H3'"  sing N N 104 
GDP "O3'" "HO3'" sing N N 105 
GDP "C2'" "O2'"  sing N N 106 
GDP "C2'" "C1'"  sing N N 107 
GDP "C2'" "H2'"  sing N N 108 
GDP "O2'" "HO2'" sing N N 109 
GDP "C1'" N9     sing N N 110 
GDP "C1'" "H1'"  sing N N 111 
GDP N9    C8     sing Y N 112 
GDP N9    C4     sing Y N 113 
GDP C8    N7     doub Y N 114 
GDP C8    H8     sing N N 115 
GDP N7    C5     sing Y N 116 
GDP C5    C6     sing N N 117 
GDP C5    C4     doub Y N 118 
GDP C6    O6     doub N N 119 
GDP C6    N1     sing N N 120 
GDP N1    C2     sing N N 121 
GDP N1    HN1    sing N N 122 
GDP C2    N2     sing N N 123 
GDP C2    N3     doub N N 124 
GDP N2    HN21   sing N N 125 
GDP N2    HN22   sing N N 126 
GDP N3    C4     sing N N 127 
GLN N     CA     sing N N 128 
GLN N     H      sing N N 129 
GLN N     H2     sing N N 130 
GLN CA    C      sing N N 131 
GLN CA    CB     sing N N 132 
GLN CA    HA     sing N N 133 
GLN C     O      doub N N 134 
GLN C     OXT    sing N N 135 
GLN CB    CG     sing N N 136 
GLN CB    HB2    sing N N 137 
GLN CB    HB3    sing N N 138 
GLN CG    CD     sing N N 139 
GLN CG    HG2    sing N N 140 
GLN CG    HG3    sing N N 141 
GLN CD    OE1    doub N N 142 
GLN CD    NE2    sing N N 143 
GLN NE2   HE21   sing N N 144 
GLN NE2   HE22   sing N N 145 
GLN OXT   HXT    sing N N 146 
GLU N     CA     sing N N 147 
GLU N     H      sing N N 148 
GLU N     H2     sing N N 149 
GLU CA    C      sing N N 150 
GLU CA    CB     sing N N 151 
GLU CA    HA     sing N N 152 
GLU C     O      doub N N 153 
GLU C     OXT    sing N N 154 
GLU CB    CG     sing N N 155 
GLU CB    HB2    sing N N 156 
GLU CB    HB3    sing N N 157 
GLU CG    CD     sing N N 158 
GLU CG    HG2    sing N N 159 
GLU CG    HG3    sing N N 160 
GLU CD    OE1    doub N N 161 
GLU CD    OE2    sing N N 162 
GLU OE2   HE2    sing N N 163 
GLU OXT   HXT    sing N N 164 
GLY N     CA     sing N N 165 
GLY N     H      sing N N 166 
GLY N     H2     sing N N 167 
GLY CA    C      sing N N 168 
GLY CA    HA2    sing N N 169 
GLY CA    HA3    sing N N 170 
GLY C     O      doub N N 171 
GLY C     OXT    sing N N 172 
GLY OXT   HXT    sing N N 173 
GTP PG    O1G    doub N N 174 
GTP PG    O2G    sing N N 175 
GTP PG    O3G    sing N N 176 
GTP PG    O3B    sing N N 177 
GTP O2G   HOG2   sing N N 178 
GTP O3G   HOG3   sing N N 179 
GTP O3B   PB     sing N N 180 
GTP PB    O1B    doub N N 181 
GTP PB    O2B    sing N N 182 
GTP PB    O3A    sing N N 183 
GTP O2B   HOB2   sing N N 184 
GTP O3A   PA     sing N N 185 
GTP PA    O1A    doub N N 186 
GTP PA    O2A    sing N N 187 
GTP PA    "O5'"  sing N N 188 
GTP O2A   HOA2   sing N N 189 
GTP "O5'" "C5'"  sing N N 190 
GTP "C5'" "C4'"  sing N N 191 
GTP "C5'" "H5'"  sing N N 192 
GTP "C5'" "H5''" sing N N 193 
GTP "C4'" "O4'"  sing N N 194 
GTP "C4'" "C3'"  sing N N 195 
GTP "C4'" "H4'"  sing N N 196 
GTP "O4'" "C1'"  sing N N 197 
GTP "C3'" "O3'"  sing N N 198 
GTP "C3'" "C2'"  sing N N 199 
GTP "C3'" "H3'"  sing N N 200 
GTP "O3'" "HO3'" sing N N 201 
GTP "C2'" "O2'"  sing N N 202 
GTP "C2'" "C1'"  sing N N 203 
GTP "C2'" "H2'"  sing N N 204 
GTP "O2'" "HO2'" sing N N 205 
GTP "C1'" N9     sing N N 206 
GTP "C1'" "H1'"  sing N N 207 
GTP N9    C8     sing Y N 208 
GTP N9    C4     sing Y N 209 
GTP C8    N7     doub Y N 210 
GTP C8    H8     sing N N 211 
GTP N7    C5     sing Y N 212 
GTP C5    C6     sing N N 213 
GTP C5    C4     doub Y N 214 
GTP C6    O6     doub N N 215 
GTP C6    N1     sing N N 216 
GTP N1    C2     sing N N 217 
GTP N1    HN1    sing N N 218 
GTP C2    N2     sing N N 219 
GTP C2    N3     doub N N 220 
GTP N2    HN21   sing N N 221 
GTP N2    HN22   sing N N 222 
GTP N3    C4     sing N N 223 
HIS N     CA     sing N N 224 
HIS N     H      sing N N 225 
HIS N     H2     sing N N 226 
HIS CA    C      sing N N 227 
HIS CA    CB     sing N N 228 
HIS CA    HA     sing N N 229 
HIS C     O      doub N N 230 
HIS C     OXT    sing N N 231 
HIS CB    CG     sing N N 232 
HIS CB    HB2    sing N N 233 
HIS CB    HB3    sing N N 234 
HIS CG    ND1    sing Y N 235 
HIS CG    CD2    doub Y N 236 
HIS ND1   CE1    doub Y N 237 
HIS ND1   HD1    sing N N 238 
HIS CD2   NE2    sing Y N 239 
HIS CD2   HD2    sing N N 240 
HIS CE1   NE2    sing Y N 241 
HIS CE1   HE1    sing N N 242 
HIS NE2   HE2    sing N N 243 
HIS OXT   HXT    sing N N 244 
HOH O     H1     sing N N 245 
HOH O     H2     sing N N 246 
IBL C12   O3     sing N N 247 
IBL O3    C11    sing N N 248 
IBL C11   C13    doub Y N 249 
IBL C11   C9     sing Y N 250 
IBL C10   O2     sing N N 251 
IBL C13   C5     sing Y N 252 
IBL O2    C9     sing N N 253 
IBL C9    C7     doub Y N 254 
IBL N1    C5     sing N N 255 
IBL N1    N      doub N N 256 
IBL C5    C6     doub Y N 257 
IBL C7    C6     sing Y N 258 
IBL C7    O1     sing N N 259 
IBL N     C4     sing N N 260 
IBL C3    C4     doub Y N 261 
IBL C3    C2     sing Y N 262 
IBL C4    C14    sing Y N 263 
IBL O1    C8     sing N N 264 
IBL C2    C1     doub Y N 265 
IBL C14   C15    doub Y N 266 
IBL C1    C15    sing Y N 267 
IBL C1    O      sing N N 268 
IBL C     O      sing N N 269 
IBL C15   O4     sing N N 270 
IBL C8    H6     sing N N 271 
IBL C8    H8     sing N N 272 
IBL C8    H7     sing N N 273 
IBL C6    H5     sing N N 274 
IBL O4    H17    sing N N 275 
IBL C3    H4     sing N N 276 
IBL C2    H3     sing N N 277 
IBL C     H      sing N N 278 
IBL C     H2     sing N N 279 
IBL C     H1     sing N N 280 
IBL C10   H10    sing N N 281 
IBL C10   H11    sing N N 282 
IBL C10   H9     sing N N 283 
IBL C12   H14    sing N N 284 
IBL C12   H13    sing N N 285 
IBL C12   H12    sing N N 286 
IBL C13   H15    sing N N 287 
IBL C14   H16    sing N N 288 
ILE N     CA     sing N N 289 
ILE N     H      sing N N 290 
ILE N     H2     sing N N 291 
ILE CA    C      sing N N 292 
ILE CA    CB     sing N N 293 
ILE CA    HA     sing N N 294 
ILE C     O      doub N N 295 
ILE C     OXT    sing N N 296 
ILE CB    CG1    sing N N 297 
ILE CB    CG2    sing N N 298 
ILE CB    HB     sing N N 299 
ILE CG1   CD1    sing N N 300 
ILE CG1   HG12   sing N N 301 
ILE CG1   HG13   sing N N 302 
ILE CG2   HG21   sing N N 303 
ILE CG2   HG22   sing N N 304 
ILE CG2   HG23   sing N N 305 
ILE CD1   HD11   sing N N 306 
ILE CD1   HD12   sing N N 307 
ILE CD1   HD13   sing N N 308 
ILE OXT   HXT    sing N N 309 
LEU N     CA     sing N N 310 
LEU N     H      sing N N 311 
LEU N     H2     sing N N 312 
LEU CA    C      sing N N 313 
LEU CA    CB     sing N N 314 
LEU CA    HA     sing N N 315 
LEU C     O      doub N N 316 
LEU C     OXT    sing N N 317 
LEU CB    CG     sing N N 318 
LEU CB    HB2    sing N N 319 
LEU CB    HB3    sing N N 320 
LEU CG    CD1    sing N N 321 
LEU CG    CD2    sing N N 322 
LEU CG    HG     sing N N 323 
LEU CD1   HD11   sing N N 324 
LEU CD1   HD12   sing N N 325 
LEU CD1   HD13   sing N N 326 
LEU CD2   HD21   sing N N 327 
LEU CD2   HD22   sing N N 328 
LEU CD2   HD23   sing N N 329 
LEU OXT   HXT    sing N N 330 
LYS N     CA     sing N N 331 
LYS N     H      sing N N 332 
LYS N     H2     sing N N 333 
LYS CA    C      sing N N 334 
LYS CA    CB     sing N N 335 
LYS CA    HA     sing N N 336 
LYS C     O      doub N N 337 
LYS C     OXT    sing N N 338 
LYS CB    CG     sing N N 339 
LYS CB    HB2    sing N N 340 
LYS CB    HB3    sing N N 341 
LYS CG    CD     sing N N 342 
LYS CG    HG2    sing N N 343 
LYS CG    HG3    sing N N 344 
LYS CD    CE     sing N N 345 
LYS CD    HD2    sing N N 346 
LYS CD    HD3    sing N N 347 
LYS CE    NZ     sing N N 348 
LYS CE    HE2    sing N N 349 
LYS CE    HE3    sing N N 350 
LYS NZ    HZ1    sing N N 351 
LYS NZ    HZ2    sing N N 352 
LYS NZ    HZ3    sing N N 353 
LYS OXT   HXT    sing N N 354 
MET N     CA     sing N N 355 
MET N     H      sing N N 356 
MET N     H2     sing N N 357 
MET CA    C      sing N N 358 
MET CA    CB     sing N N 359 
MET CA    HA     sing N N 360 
MET C     O      doub N N 361 
MET C     OXT    sing N N 362 
MET CB    CG     sing N N 363 
MET CB    HB2    sing N N 364 
MET CB    HB3    sing N N 365 
MET CG    SD     sing N N 366 
MET CG    HG2    sing N N 367 
MET CG    HG3    sing N N 368 
MET SD    CE     sing N N 369 
MET CE    HE1    sing N N 370 
MET CE    HE2    sing N N 371 
MET CE    HE3    sing N N 372 
MET OXT   HXT    sing N N 373 
PHE N     CA     sing N N 374 
PHE N     H      sing N N 375 
PHE N     H2     sing N N 376 
PHE CA    C      sing N N 377 
PHE CA    CB     sing N N 378 
PHE CA    HA     sing N N 379 
PHE C     O      doub N N 380 
PHE C     OXT    sing N N 381 
PHE CB    CG     sing N N 382 
PHE CB    HB2    sing N N 383 
PHE CB    HB3    sing N N 384 
PHE CG    CD1    doub Y N 385 
PHE CG    CD2    sing Y N 386 
PHE CD1   CE1    sing Y N 387 
PHE CD1   HD1    sing N N 388 
PHE CD2   CE2    doub Y N 389 
PHE CD2   HD2    sing N N 390 
PHE CE1   CZ     doub Y N 391 
PHE CE1   HE1    sing N N 392 
PHE CE2   CZ     sing Y N 393 
PHE CE2   HE2    sing N N 394 
PHE CZ    HZ     sing N N 395 
PHE OXT   HXT    sing N N 396 
PRO N     CA     sing N N 397 
PRO N     CD     sing N N 398 
PRO N     H      sing N N 399 
PRO CA    C      sing N N 400 
PRO CA    CB     sing N N 401 
PRO CA    HA     sing N N 402 
PRO C     O      doub N N 403 
PRO C     OXT    sing N N 404 
PRO CB    CG     sing N N 405 
PRO CB    HB2    sing N N 406 
PRO CB    HB3    sing N N 407 
PRO CG    CD     sing N N 408 
PRO CG    HG2    sing N N 409 
PRO CG    HG3    sing N N 410 
PRO CD    HD2    sing N N 411 
PRO CD    HD3    sing N N 412 
PRO OXT   HXT    sing N N 413 
SER N     CA     sing N N 414 
SER N     H      sing N N 415 
SER N     H2     sing N N 416 
SER CA    C      sing N N 417 
SER CA    CB     sing N N 418 
SER CA    HA     sing N N 419 
SER C     O      doub N N 420 
SER C     OXT    sing N N 421 
SER CB    OG     sing N N 422 
SER CB    HB2    sing N N 423 
SER CB    HB3    sing N N 424 
SER OG    HG     sing N N 425 
SER OXT   HXT    sing N N 426 
THR N     CA     sing N N 427 
THR N     H      sing N N 428 
THR N     H2     sing N N 429 
THR CA    C      sing N N 430 
THR CA    CB     sing N N 431 
THR CA    HA     sing N N 432 
THR C     O      doub N N 433 
THR C     OXT    sing N N 434 
THR CB    OG1    sing N N 435 
THR CB    CG2    sing N N 436 
THR CB    HB     sing N N 437 
THR OG1   HG1    sing N N 438 
THR CG2   HG21   sing N N 439 
THR CG2   HG22   sing N N 440 
THR CG2   HG23   sing N N 441 
THR OXT   HXT    sing N N 442 
TRP N     CA     sing N N 443 
TRP N     H      sing N N 444 
TRP N     H2     sing N N 445 
TRP CA    C      sing N N 446 
TRP CA    CB     sing N N 447 
TRP CA    HA     sing N N 448 
TRP C     O      doub N N 449 
TRP C     OXT    sing N N 450 
TRP CB    CG     sing N N 451 
TRP CB    HB2    sing N N 452 
TRP CB    HB3    sing N N 453 
TRP CG    CD1    doub Y N 454 
TRP CG    CD2    sing Y N 455 
TRP CD1   NE1    sing Y N 456 
TRP CD1   HD1    sing N N 457 
TRP CD2   CE2    doub Y N 458 
TRP CD2   CE3    sing Y N 459 
TRP NE1   CE2    sing Y N 460 
TRP NE1   HE1    sing N N 461 
TRP CE2   CZ2    sing Y N 462 
TRP CE3   CZ3    doub Y N 463 
TRP CE3   HE3    sing N N 464 
TRP CZ2   CH2    doub Y N 465 
TRP CZ2   HZ2    sing N N 466 
TRP CZ3   CH2    sing Y N 467 
TRP CZ3   HZ3    sing N N 468 
TRP CH2   HH2    sing N N 469 
TRP OXT   HXT    sing N N 470 
TYR N     CA     sing N N 471 
TYR N     H      sing N N 472 
TYR N     H2     sing N N 473 
TYR CA    C      sing N N 474 
TYR CA    CB     sing N N 475 
TYR CA    HA     sing N N 476 
TYR C     O      doub N N 477 
TYR C     OXT    sing N N 478 
TYR CB    CG     sing N N 479 
TYR CB    HB2    sing N N 480 
TYR CB    HB3    sing N N 481 
TYR CG    CD1    doub Y N 482 
TYR CG    CD2    sing Y N 483 
TYR CD1   CE1    sing Y N 484 
TYR CD1   HD1    sing N N 485 
TYR CD2   CE2    doub Y N 486 
TYR CD2   HD2    sing N N 487 
TYR CE1   CZ     doub Y N 488 
TYR CE1   HE1    sing N N 489 
TYR CE2   CZ     sing Y N 490 
TYR CE2   HE2    sing N N 491 
TYR CZ    OH     sing N N 492 
TYR OH    HH     sing N N 493 
TYR OXT   HXT    sing N N 494 
VAL N     CA     sing N N 495 
VAL N     H      sing N N 496 
VAL N     H2     sing N N 497 
VAL CA    C      sing N N 498 
VAL CA    CB     sing N N 499 
VAL CA    HA     sing N N 500 
VAL C     O      doub N N 501 
VAL C     OXT    sing N N 502 
VAL CB    CG1    sing N N 503 
VAL CB    CG2    sing N N 504 
VAL CB    HB     sing N N 505 
VAL CG1   HG11   sing N N 506 
VAL CG1   HG12   sing N N 507 
VAL CG1   HG13   sing N N 508 
VAL CG2   HG21   sing N N 509 
VAL CG2   HG22   sing N N 510 
VAL CG2   HG23   sing N N 511 
VAL OXT   HXT    sing N N 512 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland 310030_207462 1 
'Swiss National Science Foundation' Switzerland 310030_197674 2 
'Swiss National Science Foundation' Switzerland 310030_192566 3 
'Swiss National Science Foundation' Switzerland CRSII5_213507 4 
# 
_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   7YYQ 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_atom_sites.entry_id                    8QLA 
_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]   0.013417 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001579 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010801 
_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]   0.011988 
_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 
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     A MET A 1 1   ? -28.685 -3.421  36.337  0.20 45.86  ? 1   MET A N     1 
ATOM   2     N  N     B MET A 1 1   ? -28.316 -3.085  37.064  0.80 41.33  ? 1   MET A N     1 
ATOM   3     C  CA    A MET A 1 1   ? -27.232 -3.557  36.303  0.20 44.18  ? 1   MET A CA    1 
ATOM   4     C  CA    B MET A 1 1   ? -27.407 -3.923  36.286  0.80 45.44  ? 1   MET A CA    1 
ATOM   5     C  C     A MET A 1 1   ? -26.624 -2.765  35.145  0.20 41.15  ? 1   MET A C     1 
ATOM   6     C  C     B MET A 1 1   ? -26.922 -3.202  35.019  0.80 44.94  ? 1   MET A C     1 
ATOM   7     O  O     A MET A 1 1   ? -27.332 -2.078  34.408  0.20 39.64  ? 1   MET A O     1 
ATOM   8     O  O     B MET A 1 1   ? -27.714 -2.850  34.144  0.80 48.30  ? 1   MET A O     1 
ATOM   9     C  CB    A MET A 1 1   ? -26.839 -5.034  36.205  0.20 41.95  ? 1   MET A CB    1 
ATOM   10    C  CB    B MET A 1 1   ? -28.093 -5.245  35.927  0.80 46.91  ? 1   MET A CB    1 
ATOM   11    C  CG    A MET A 1 1   ? -27.531 -5.810  35.087  0.20 41.92  ? 1   MET A CG    1 
ATOM   12    C  CG    B MET A 1 1   ? -27.159 -6.359  35.481  0.80 42.11  ? 1   MET A CG    1 
ATOM   13    S  SD    A MET A 1 1   ? -26.879 -5.491  33.431  0.20 35.05  ? 1   MET A SD    1 
ATOM   14    S  SD    B MET A 1 1   ? -26.489 -6.075  33.830  0.80 44.39  ? 1   MET A SD    1 
ATOM   15    C  CE    A MET A 1 1   ? -27.787 -6.717  32.490  0.20 37.42  ? 1   MET A CE    1 
ATOM   16    C  CE    B MET A 1 1   ? -28.003 -6.133  32.876  0.80 37.01  ? 1   MET A CE    1 
ATOM   17    N  N     A ARG A 1 2   ? -25.305 -2.865  34.993  0.20 35.83  ? 2   ARG A N     1 
ATOM   18    N  N     B ARG A 1 2   ? -25.610 -2.999  34.932  0.80 34.51  ? 2   ARG A N     1 
ATOM   19    C  CA    A ARG A 1 2   ? -24.581 -2.155  33.939  0.20 34.24  ? 2   ARG A CA    1 
ATOM   20    C  CA    B ARG A 1 2   ? -24.969 -2.363  33.788  0.80 33.52  ? 2   ARG A CA    1 
ATOM   21    C  C     A ARG A 1 2   ? -23.558 -3.109  33.337  0.20 32.21  ? 2   ARG A C     1 
ATOM   22    C  C     B ARG A 1 2   ? -23.911 -3.302  33.213  0.80 32.90  ? 2   ARG A C     1 
ATOM   23    O  O     A ARG A 1 2   ? -22.604 -3.502  34.013  0.20 32.39  ? 2   ARG A O     1 
ATOM   24    O  O     B ARG A 1 2   ? -23.169 -3.943  33.959  0.80 34.29  ? 2   ARG A O     1 
ATOM   25    C  CB    A ARG A 1 2   ? -23.912 -0.892  34.487  0.20 33.98  ? 2   ARG A CB    1 
ATOM   26    C  CB    B ARG A 1 2   ? -24.341 -1.015  34.196  0.80 34.02  ? 2   ARG A CB    1 
ATOM   27    C  CG    A ARG A 1 2   ? -24.894 0.101   35.106  0.20 37.02  ? 2   ARG A CG    1 
ATOM   28    C  CG    B ARG A 1 2   ? -25.321 -0.046  34.875  0.80 38.01  ? 2   ARG A CG    1 
ATOM   29    C  CD    A ARG A 1 2   ? -24.188 1.232   35.833  0.20 34.00  ? 2   ARG A CD    1 
ATOM   30    C  CD    B ARG A 1 2   ? -24.726 1.350   35.005  0.80 35.73  ? 2   ARG A CD    1 
ATOM   31    N  NE    A ARG A 1 2   ? -23.322 1.997   34.945  0.20 38.92  ? 2   ARG A NE    1 
ATOM   32    N  NE    B ARG A 1 2   ? -24.418 1.904   33.693  0.80 36.55  ? 2   ARG A NE    1 
ATOM   33    C  CZ    A ARG A 1 2   ? -22.687 3.107   35.296  0.20 42.47  ? 2   ARG A CZ    1 
ATOM   34    C  CZ    B ARG A 1 2   ? -23.576 2.904   33.475  0.80 47.04  ? 2   ARG A CZ    1 
ATOM   35    N  NH1   A ARG A 1 2   ? -22.810 3.618   36.510  0.20 31.54  ? 2   ARG A NH1   1 
ATOM   36    N  NH1   B ARG A 1 2   ? -22.937 3.502   34.468  0.80 51.00  ? 2   ARG A NH1   1 
ATOM   37    N  NH2   A ARG A 1 2   ? -21.912 3.720   34.405  0.20 37.20  ? 2   ARG A NH2   1 
ATOM   38    N  NH2   B ARG A 1 2   ? -23.362 3.308   32.225  0.80 42.91  ? 2   ARG A NH2   1 
ATOM   39    N  N     A GLU A 1 3   ? -23.753 -3.466  32.069  0.20 29.86  ? 3   GLU A N     1 
ATOM   40    N  N     B GLU A 1 3   ? -23.845 -3.380  31.887  0.80 29.56  ? 3   GLU A N     1 
ATOM   41    C  CA    A GLU A 1 3   ? -22.957 -4.510  31.435  0.20 31.13  ? 3   GLU A CA    1 
ATOM   42    C  CA    B GLU A 1 3   ? -23.058 -4.412  31.213  0.80 32.05  ? 3   GLU A CA    1 
ATOM   43    C  C     A GLU A 1 3   ? -21.507 -4.075  31.244  0.20 26.11  ? 3   GLU A C     1 
ATOM   44    C  C     B GLU A 1 3   ? -21.593 -4.018  31.068  0.80 25.17  ? 3   GLU A C     1 
ATOM   45    O  O     A GLU A 1 3   ? -21.194 -2.885  31.158  0.20 25.56  ? 3   GLU A O     1 
ATOM   46    O  O     B GLU A 1 3   ? -21.262 -2.841  30.913  0.80 24.32  ? 3   GLU A O     1 
ATOM   47    C  CB    A GLU A 1 3   ? -23.548 -4.888  30.075  0.20 27.69  ? 3   GLU A CB    1 
ATOM   48    C  CB    B GLU A 1 3   ? -23.624 -4.700  29.822  0.80 26.16  ? 3   GLU A CB    1 
ATOM   49    C  CG    A GLU A 1 3   ? -24.983 -5.396  30.111  0.20 29.32  ? 3   GLU A CG    1 
ATOM   50    C  CG    B GLU A 1 3   ? -25.023 -5.323  29.817  0.80 28.20  ? 3   GLU A CG    1 
ATOM   51    C  CD    A GLU A 1 3   ? -26.010 -4.279  30.142  0.20 31.24  ? 3   GLU A CD    1 
ATOM   52    C  CD    B GLU A 1 3   ? -26.157 -4.304  29.762  0.80 31.38  ? 3   GLU A CD    1 
ATOM   53    O  OE1   A GLU A 1 3   ? -25.616 -3.095  30.183  0.20 32.37  ? 3   GLU A OE1   1 
ATOM   54    O  OE1   B GLU A 1 3   ? -25.927 -3.108  30.020  0.80 32.13  ? 3   GLU A OE1   1 
ATOM   55    O  OE2   A GLU A 1 3   ? -27.217 -4.589  30.121  0.20 30.90  ? 3   GLU A OE2   1 
ATOM   56    O  OE2   B GLU A 1 3   ? -27.291 -4.714  29.437  0.80 31.89  ? 3   GLU A OE2   1 
ATOM   57    N  N     A CYS A 1 4   ? -20.621 -5.067  31.171  0.20 28.39  ? 4   CYS A N     1 
ATOM   58    N  N     B CYS A 1 4   ? -20.721 -5.030  31.117  0.80 28.50  ? 4   CYS A N     1 
ATOM   59    C  CA    A CYS A 1 4   ? -19.216 -4.862  30.841  0.20 28.64  ? 4   CYS A CA    1 
ATOM   60    C  CA    B CYS A 1 4   ? -19.301 -4.918  30.786  0.80 28.78  ? 4   CYS A CA    1 
ATOM   61    C  C     A CYS A 1 4   ? -18.780 -5.952  29.874  0.20 26.82  ? 4   CYS A C     1 
ATOM   62    C  C     B CYS A 1 4   ? -18.959 -5.886  29.663  0.80 26.54  ? 4   CYS A C     1 
ATOM   63    O  O     A CYS A 1 4   ? -19.006 -7.138  30.131  0.20 28.44  ? 4   CYS A O     1 
ATOM   64    O  O     B CYS A 1 4   ? -19.375 -7.049  29.690  0.80 31.15  ? 4   CYS A O     1 
ATOM   65    C  CB    A CYS A 1 4   ? -18.328 -4.885  32.093  0.20 31.68  ? 4   CYS A CB    1 
ATOM   66    C  CB    B CYS A 1 4   ? -18.385 -5.248  31.978  0.80 31.70  ? 4   CYS A CB    1 
ATOM   67    S  SG    A CYS A 1 4   ? -18.466 -3.430  33.167  0.20 22.76  ? 4   CYS A SG    1 
ATOM   68    S  SG    B CYS A 1 4   ? -18.630 -4.286  33.481  0.80 32.28  ? 4   CYS A SG    1 
ATOM   69    N  N     A ILE A 1 5   ? -18.159 -5.547  28.767  0.20 28.60  ? 5   ILE A N     1 
ATOM   70    N  N     B ILE A 1 5   ? -18.162 -5.415  28.702  0.80 28.67  ? 5   ILE A N     1 
ATOM   71    C  CA    A ILE A 1 5   ? -17.676 -6.467  27.742  0.20 26.23  ? 5   ILE A CA    1 
ATOM   72    C  CA    B ILE A 1 5   ? -17.656 -6.219  27.592  0.80 26.96  ? 5   ILE A CA    1 
ATOM   73    C  C     A ILE A 1 5   ? -16.190 -6.712  27.966  0.20 26.23  ? 5   ILE A C     1 
ATOM   74    C  C     B ILE A 1 5   ? -16.160 -6.422  27.791  0.80 26.74  ? 5   ILE A C     1 
ATOM   75    O  O     A ILE A 1 5   ? -15.435 -5.783  28.284  0.20 25.70  ? 5   ILE A O     1 
ATOM   76    O  O     B ILE A 1 5   ? -15.414 -5.448  27.964  0.80 25.58  ? 5   ILE A O     1 
ATOM   77    C  CB    A ILE A 1 5   ? -17.948 -5.910  26.329  0.20 23.61  ? 5   ILE A CB    1 
ATOM   78    C  CB    B ILE A 1 5   ? -17.938 -5.537  26.239  0.80 22.01  ? 5   ILE A CB    1 
ATOM   79    C  CG1   A ILE A 1 5   ? -19.447 -5.671  26.130  0.20 23.66  ? 5   ILE A CG1   1 
ATOM   80    C  CG1   B ILE A 1 5   ? -19.442 -5.526  25.928  0.80 22.74  ? 5   ILE A CG1   1 
ATOM   81    C  CG2   A ILE A 1 5   ? -17.407 -6.851  25.251  0.20 23.53  ? 5   ILE A CG2   1 
ATOM   82    C  CG2   B ILE A 1 5   ? -17.100 -6.181  25.080  0.80 24.56  ? 5   ILE A CG2   1 
ATOM   83    C  CD1   A ILE A 1 5   ? -19.800 -5.002  24.814  0.20 27.13  ? 5   ILE A CD1   1 
ATOM   84    C  CD1   B ILE A 1 5   ? -19.860 -4.401  24.974  0.80 25.99  ? 5   ILE A CD1   1 
ATOM   85    N  N     A SER A 1 6   ? -15.768 -7.964  27.811  0.20 25.79  ? 6   SER A N     1 
ATOM   86    N  N     B SER A 1 6   ? -15.719 -7.677  27.762  0.80 26.17  ? 6   SER A N     1 
ATOM   87    C  CA    A SER A 1 6   ? -14.379 -8.363  28.003  0.20 25.29  ? 6   SER A CA    1 
ATOM   88    C  CA    B SER A 1 6   ? -14.297 -8.008  27.826  0.80 25.10  ? 6   SER A CA    1 
ATOM   89    C  C     A SER A 1 6   ? -13.729 -8.635  26.653  0.20 23.41  ? 6   SER A C     1 
ATOM   90    C  C     B SER A 1 6   ? -13.748 -8.234  26.420  0.80 21.96  ? 6   SER A C     1 
ATOM   91    O  O     A SER A 1 6   ? -14.255 -9.413  25.852  0.20 23.49  ? 6   SER A O     1 
ATOM   92    O  O     B SER A 1 6   ? -14.414 -8.847  25.579  0.80 22.28  ? 6   SER A O     1 
ATOM   93    C  CB    A SER A 1 6   ? -14.285 -9.602  28.895  0.20 25.49  ? 6   SER A CB    1 
ATOM   94    C  CB    B SER A 1 6   ? -14.061 -9.257  28.679  0.80 23.58  ? 6   SER A CB    1 
ATOM   95    O  OG    A SER A 1 6   ? -14.749 -9.318  30.204  0.20 29.16  ? 6   SER A OG    1 
ATOM   96    O  OG    B SER A 1 6   ? -14.578 -9.079  29.992  0.80 31.25  ? 6   SER A OG    1 
ATOM   97    N  N     A ILE A 1 7   ? -12.587 -7.997  26.408  0.20 23.62  ? 7   ILE A N     1 
ATOM   98    N  N     B ILE A 1 7   ? -12.531 -7.743  26.174  0.80 23.59  ? 7   ILE A N     1 
ATOM   99    C  CA    A ILE A 1 7   ? -11.846 -8.142  25.161  0.20 24.76  ? 7   ILE A CA    1 
ATOM   100   C  CA    B ILE A 1 7   ? -11.859 -7.877  24.878  0.80 24.41  ? 7   ILE A CA    1 
ATOM   101   C  C     A ILE A 1 7   ? -10.541 -8.866  25.459  0.20 24.41  ? 7   ILE A C     1 
ATOM   102   C  C     B ILE A 1 7   ? -10.481 -8.483  25.134  0.80 26.05  ? 7   ILE A C     1 
ATOM   103   O  O     A ILE A 1 7   ? -9.861  -8.562  26.447  0.20 22.08  ? 7   ILE A O     1 
ATOM   104   O  O     B ILE A 1 7   ? -9.691  -7.925  25.909  0.80 21.78  ? 7   ILE A O     1 
ATOM   105   C  CB    A ILE A 1 7   ? -11.590 -6.774  24.497  0.20 22.77  ? 7   ILE A CB    1 
ATOM   106   C  CB    B ILE A 1 7   ? -11.742 -6.523  24.146  0.80 22.01  ? 7   ILE A CB    1 
ATOM   107   C  CG1   A ILE A 1 7   ? -12.920 -6.064  24.217  0.20 24.60  ? 7   ILE A CG1   1 
ATOM   108   C  CG1   B ILE A 1 7   ? -13.108 -5.821  24.071  0.80 24.67  ? 7   ILE A CG1   1 
ATOM   109   C  CG2   A ILE A 1 7   ? -10.784 -6.935  23.211  0.20 25.42  ? 7   ILE A CG2   1 
ATOM   110   C  CG2   B ILE A 1 7   ? -11.177 -6.697  22.715  0.80 22.54  ? 7   ILE A CG2   1 
ATOM   111   C  CD1   A ILE A 1 7   ? -12.769 -4.663  23.645  0.20 25.86  ? 7   ILE A CD1   1 
ATOM   112   C  CD1   B ILE A 1 7   ? -13.021 -4.367  23.577  0.80 25.08  ? 7   ILE A CD1   1 
ATOM   113   N  N     A HIS A 1 8   ? -10.199 -9.835  24.611  0.20 22.49  ? 8   HIS A N     1 
ATOM   114   N  N     B HIS A 1 8   ? -10.196 -9.630  24.509  0.80 22.42  ? 8   HIS A N     1 
ATOM   115   C  CA    A HIS A 1 8   ? -8.990  -10.634 24.770  0.20 25.58  ? 8   HIS A CA    1 
ATOM   116   C  CA    B HIS A 1 8   ? -8.924  -10.327 24.686  0.80 26.80  ? 8   HIS A CA    1 
ATOM   117   C  C     A HIS A 1 8   ? -8.256  -10.669 23.436  0.20 22.63  ? 8   HIS A C     1 
ATOM   118   C  C     B HIS A 1 8   ? -8.110  -10.241 23.390  0.80 21.67  ? 8   HIS A C     1 
ATOM   119   O  O     A HIS A 1 8   ? -8.799  -11.163 22.443  0.20 24.36  ? 8   HIS A O     1 
ATOM   120   O  O     B HIS A 1 8   ? -8.576  -10.684 22.339  0.80 25.49  ? 8   HIS A O     1 
ATOM   121   C  CB    A HIS A 1 8   ? -9.335  -12.047 25.249  0.20 25.18  ? 8   HIS A CB    1 
ATOM   122   C  CB    B HIS A 1 8   ? -9.177  -11.782 25.090  0.80 25.83  ? 8   HIS A CB    1 
ATOM   123   C  CG    A HIS A 1 8   ? -10.282 -12.074 26.409  0.20 25.89  ? 8   HIS A CG    1 
ATOM   124   C  CG    B HIS A 1 8   ? -10.159 -11.932 26.213  0.80 26.15  ? 8   HIS A CG    1 
ATOM   125   N  ND1   A HIS A 1 8   ? -9.868  -11.901 27.713  0.20 25.63  ? 8   HIS A ND1   1 
ATOM   126   N  ND1   B HIS A 1 8   ? -9.788  -11.876 27.540  0.80 25.15  ? 8   HIS A ND1   1 
ATOM   127   C  CD2   A HIS A 1 8   ? -11.625 -12.241 26.461  0.20 25.22  ? 8   HIS A CD2   1 
ATOM   128   C  CD2   B HIS A 1 8   ? -11.502 -12.117 26.206  0.80 25.35  ? 8   HIS A CD2   1 
ATOM   129   C  CE1   A HIS A 1 8   ? -10.915 -11.964 28.518  0.20 30.08  ? 8   HIS A CE1   1 
ATOM   130   C  CE1   B HIS A 1 8   ? -10.861 -12.022 28.300  0.80 31.87  ? 8   HIS A CE1   1 
ATOM   131   N  NE2   A HIS A 1 8   ? -11.993 -12.173 27.783  0.20 28.00  ? 8   HIS A NE2   1 
ATOM   132   N  NE2   B HIS A 1 8   ? -11.913 -12.176 27.515  0.80 28.85  ? 8   HIS A NE2   1 
ATOM   133   N  N     A VAL A 1 9   ? -7.027  -10.151 23.417  0.20 22.36  ? 9   VAL A N     1 
ATOM   134   N  N     B VAL A 1 9   ? -6.898  -9.681  23.470  0.80 22.55  ? 9   VAL A N     1 
ATOM   135   C  CA    A VAL A 1 9   ? -6.280  -9.909  22.188  0.20 23.29  ? 9   VAL A CA    1 
ATOM   136   C  CA    B VAL A 1 9   ? -6.103  -9.325  22.294  0.80 22.78  ? 9   VAL A CA    1 
ATOM   137   C  C     A VAL A 1 9   ? -5.024  -10.771 22.180  0.20 22.55  ? 9   VAL A C     1 
ATOM   138   C  C     B VAL A 1 9   ? -4.767  -10.060 22.339  0.80 23.20  ? 9   VAL A C     1 
ATOM   139   O  O     A VAL A 1 9   ? -4.394  -10.982 23.222  0.20 21.09  ? 9   VAL A O     1 
ATOM   140   O  O     B VAL A 1 9   ? -3.947  -9.828  23.242  0.80 19.36  ? 9   VAL A O     1 
ATOM   141   C  CB    A VAL A 1 9   ? -5.909  -8.417  22.041  0.20 24.45  ? 9   VAL A CB    1 
ATOM   142   C  CB    B VAL A 1 9   ? -5.863  -7.811  22.195  0.80 24.77  ? 9   VAL A CB    1 
ATOM   143   C  CG1   A VAL A 1 9   ? -5.343  -8.134  20.649  0.20 21.27  ? 9   VAL A CG1   1 
ATOM   144   C  CG1   B VAL A 1 9   ? -5.037  -7.505  20.932  0.80 21.10  ? 9   VAL A CG1   1 
ATOM   145   C  CG2   A VAL A 1 9   ? -7.110  -7.533  22.329  0.20 23.68  ? 9   VAL A CG2   1 
ATOM   146   C  CG2   B VAL A 1 9   ? -7.170  -7.050  22.163  0.80 23.23  ? 9   VAL A CG2   1 
ATOM   147   N  N     A GLY A 1 10  ? -4.660  -11.263 20.997  0.20 22.64  ? 10  GLY A N     1 
ATOM   148   N  N     B GLY A 1 10  ? -4.529  -10.911 21.346  0.80 23.14  ? 10  GLY A N     1 
ATOM   149   C  CA    A GLY A 1 10  ? -3.417  -11.994 20.844  0.20 21.15  ? 10  GLY A CA    1 
ATOM   150   C  CA    B GLY A 1 10  ? -3.252  -11.587 21.228  0.80 20.36  ? 10  GLY A CA    1 
ATOM   151   C  C     A GLY A 1 10  ? -3.431  -13.335 21.563  0.20 21.83  ? 10  GLY A C     1 
ATOM   152   C  C     B GLY A 1 10  ? -3.173  -12.803 22.134  0.80 23.38  ? 10  GLY A C     1 
ATOM   153   O  O     A GLY A 1 10  ? -4.479  -13.898 21.893  0.20 22.21  ? 10  GLY A O     1 
ATOM   154   O  O     B GLY A 1 10  ? -4.067  -13.090 22.950  0.80 20.61  ? 10  GLY A O     1 
ATOM   155   N  N     A GLN A 1 11  ? -2.224  -13.844 21.810  0.20 23.06  ? 11  GLN A N     1 
ATOM   156   N  N     B GLN A 1 11  ? -2.054  -13.518 21.999  0.80 23.09  ? 11  GLN A N     1 
ATOM   157   C  CA    A GLN A 1 11  ? -2.084  -15.131 22.484  0.20 24.14  ? 11  GLN A CA    1 
ATOM   158   C  CA    B GLN A 1 11  ? -1.911  -14.819 22.651  0.80 25.70  ? 11  GLN A CA    1 
ATOM   159   C  C     A GLN A 1 11  ? -2.321  -15.008 23.985  0.20 22.78  ? 11  GLN A C     1 
ATOM   160   C  C     B GLN A 1 11  ? -2.084  -14.717 24.158  0.80 21.89  ? 11  GLN A C     1 
ATOM   161   O  O     A GLN A 1 11  ? -3.129  -15.751 24.553  0.20 25.21  ? 11  GLN A O     1 
ATOM   162   O  O     B GLN A 1 11  ? -2.839  -15.493 24.754  0.80 27.60  ? 11  GLN A O     1 
ATOM   163   C  CB    A GLN A 1 11  ? -0.700  -15.722 22.218  0.20 23.26  ? 11  GLN A CB    1 
ATOM   164   C  CB    B GLN A 1 11  ? -0.555  -15.444 22.340  0.80 22.38  ? 11  GLN A CB    1 
ATOM   165   C  CG    A GLN A 1 11  ? -0.387  -16.939 23.075  0.20 23.36  ? 11  GLN A CG    1 
ATOM   166   C  CG    B GLN A 1 11  ? -0.274  -16.655 23.223  0.80 22.16  ? 11  GLN A CG    1 
ATOM   167   C  CD    A GLN A 1 11  ? 0.974   -17.534 22.772  0.20 25.85  ? 11  GLN A CD    1 
ATOM   168   C  CD    B GLN A 1 11  ? 0.980   -17.413 22.828  0.80 26.04  ? 11  GLN A CD    1 
ATOM   169   O  OE1   A GLN A 1 11  ? 1.544   -17.298 21.705  0.20 25.18  ? 11  GLN A OE1   1 
ATOM   170   O  OE1   B GLN A 1 11  ? 1.169   -17.759 21.657  0.80 23.37  ? 11  GLN A OE1   1 
ATOM   171   N  NE2   A GLN A 1 11  ? 1.503   -18.307 23.712  0.20 25.03  ? 11  GLN A NE2   1 
ATOM   172   N  NE2   B GLN A 1 11  ? 1.842   -17.672 23.804  0.80 25.18  ? 11  GLN A NE2   1 
ATOM   173   N  N     A ALA A 1 12  ? -1.615  -14.085 24.643  0.20 22.38  ? 12  ALA A N     1 
ATOM   174   N  N     B ALA A 1 12  ? -1.351  -13.798 24.801  0.80 20.24  ? 12  ALA A N     1 
ATOM   175   C  CA    A ALA A 1 12  ? -1.726  -13.967 26.094  0.20 24.48  ? 12  ALA A CA    1 
ATOM   176   C  CA    B ALA A 1 12  ? -1.459  -13.671 26.249  0.80 25.48  ? 12  ALA A CA    1 
ATOM   177   C  C     A ALA A 1 12  ? -3.121  -13.536 26.522  0.20 22.68  ? 12  ALA A C     1 
ATOM   178   C  C     B ALA A 1 12  ? -2.884  -13.329 26.653  0.80 22.71  ? 12  ALA A C     1 
ATOM   179   O  O     A ALA A 1 12  ? -3.596  -13.954 27.584  0.20 23.56  ? 12  ALA A O     1 
ATOM   180   O  O     B ALA A 1 12  ? -3.440  -13.937 27.575  0.80 24.10  ? 12  ALA A O     1 
ATOM   181   C  CB    A ALA A 1 12  ? -0.683  -12.986 26.628  0.20 23.41  ? 12  ALA A CB    1 
ATOM   182   C  CB    B ALA A 1 12  ? -0.483  -12.619 26.773  0.80 22.90  ? 12  ALA A CB    1 
ATOM   183   N  N     A GLY A 1 13  ? -3.792  -12.709 25.719  0.20 20.62  ? 13  GLY A N     1 
ATOM   184   N  N     B GLY A 1 13  ? -3.504  -12.371 25.959  0.80 18.29  ? 13  GLY A N     1 
ATOM   185   C  CA    A GLY A 1 13  ? -5.125  -12.261 26.091  0.20 21.96  ? 13  GLY A CA    1 
ATOM   186   C  CA    B GLY A 1 13  ? -4.851  -11.959 26.341  0.80 21.77  ? 13  GLY A CA    1 
ATOM   187   C  C     A GLY A 1 13  ? -6.152  -13.376 26.061  0.20 23.04  ? 13  GLY A C     1 
ATOM   188   C  C     B GLY A 1 13  ? -5.887  -13.048 26.132  0.80 22.61  ? 13  GLY A C     1 
ATOM   189   O  O     A GLY A 1 13  ? -6.982  -13.491 26.968  0.20 23.19  ? 13  GLY A O     1 
ATOM   190   O  O     B GLY A 1 13  ? -6.817  -13.193 26.932  0.80 22.42  ? 13  GLY A O     1 
ATOM   191   N  N     A VAL A 1 14  ? -6.114  -14.212 25.021  0.20 22.09  ? 14  VAL A N     1 
ATOM   192   N  N     B VAL A 1 14  ? -5.750  -13.807 25.040  0.80 21.36  ? 14  VAL A N     1 
ATOM   193   C  CA    A VAL A 1 14  ? -7.094  -15.289 24.892  0.20 21.00  ? 14  VAL A CA    1 
ATOM   194   C  CA    B VAL A 1 14  ? -6.678  -14.889 24.713  0.80 22.89  ? 14  VAL A CA    1 
ATOM   195   C  C     A VAL A 1 14  ? -6.831  -16.379 25.924  0.20 24.20  ? 14  VAL A C     1 
ATOM   196   C  C     B VAL A 1 14  ? -6.547  -16.034 25.710  0.80 20.53  ? 14  VAL A C     1 
ATOM   197   O  O     A VAL A 1 14  ? -7.756  -16.859 26.591  0.20 23.27  ? 14  VAL A O     1 
ATOM   198   O  O     B VAL A 1 14  ? -7.554  -16.557 26.216  0.80 26.08  ? 14  VAL A O     1 
ATOM   199   C  CB    A VAL A 1 14  ? -7.088  -15.852 23.459  0.20 22.35  ? 14  VAL A CB    1 
ATOM   200   C  CB    B VAL A 1 14  ? -6.426  -15.369 23.272  0.80 20.05  ? 14  VAL A CB    1 
ATOM   201   C  CG1   A VAL A 1 14  ? -7.987  -17.074 23.363  0.20 21.31  ? 14  VAL A CG1   1 
ATOM   202   C  CG1   B VAL A 1 14  ? -7.002  -16.749 23.049  0.80 21.86  ? 14  VAL A CG1   1 
ATOM   203   C  CG2   A VAL A 1 14  ? -7.538  -14.787 22.475  0.20 23.08  ? 14  VAL A CG2   1 
ATOM   204   C  CG2   B VAL A 1 14  ? -6.984  -14.368 22.271  0.80 25.65  ? 14  VAL A CG2   1 
ATOM   205   N  N     A GLN A 1 15  ? -5.566  -16.784 26.079  0.20 22.19  ? 15  GLN A N     1 
ATOM   206   N  N     B GLN A 1 15  ? -5.307  -16.439 26.011  0.80 21.32  ? 15  GLN A N     1 
ATOM   207   C  CA    A GLN A 1 15  ? -5.240  -17.848 27.026  0.20 25.63  ? 15  GLN A CA    1 
ATOM   208   C  CA    B GLN A 1 15  ? -5.092  -17.572 26.910  0.80 26.11  ? 15  GLN A CA    1 
ATOM   209   C  C     A GLN A 1 15  ? -5.482  -17.439 28.475  0.20 22.66  ? 15  GLN A C     1 
ATOM   210   C  C     B GLN A 1 15  ? -5.503  -17.244 28.341  0.80 21.31  ? 15  GLN A C     1 
ATOM   211   O  O     A GLN A 1 15  ? -5.580  -18.314 29.342  0.20 24.51  ? 15  GLN A O     1 
ATOM   212   O  O     B GLN A 1 15  ? -6.122  -18.075 29.005  0.80 23.77  ? 15  GLN A O     1 
ATOM   213   C  CB    A GLN A 1 15  ? -3.791  -18.307 26.836  0.20 25.24  ? 15  GLN A CB    1 
ATOM   214   C  CB    B GLN A 1 15  ? -3.638  -18.053 26.835  0.80 24.79  ? 15  GLN A CB    1 
ATOM   215   C  CG    A GLN A 1 15  ? -3.590  -19.106 25.552  0.20 26.36  ? 15  GLN A CG    1 
ATOM   216   C  CG    B GLN A 1 15  ? -3.388  -18.798 25.510  0.80 26.82  ? 15  GLN A CG    1 
ATOM   217   C  CD    A GLN A 1 15  ? -2.217  -19.746 25.440  0.20 33.20  ? 15  GLN A CD    1 
ATOM   218   C  CD    B GLN A 1 15  ? -2.061  -19.534 25.420  0.80 34.39  ? 15  GLN A CD    1 
ATOM   219   O  OE1   A GLN A 1 15  ? -1.866  -20.296 24.394  0.20 33.69  ? 15  GLN A OE1   1 
ATOM   220   O  OE1   B GLN A 1 15  ? -1.998  -20.636 24.866  0.80 39.47  ? 15  GLN A OE1   1 
ATOM   221   N  NE2   A GLN A 1 15  ? -1.436  -19.685 26.515  0.20 25.70  ? 15  GLN A NE2   1 
ATOM   222   N  NE2   B GLN A 1 15  ? -0.989  -18.923 25.928  0.80 28.48  ? 15  GLN A NE2   1 
ATOM   223   N  N     A ILE A 1 16  ? -5.580  -16.145 28.761  0.20 22.81  ? 16  ILE A N     1 
ATOM   224   N  N     B ILE A 1 16  ? -5.178  -16.047 28.834  0.80 22.16  ? 16  ILE A N     1 
ATOM   225   C  CA    A ILE A 1 16  ? -5.986  -15.701 30.092  0.20 24.68  ? 16  ILE A CA    1 
ATOM   226   C  CA    B ILE A 1 16  ? -5.665  -15.648 30.156  0.80 25.52  ? 16  ILE A CA    1 
ATOM   227   C  C     A ILE A 1 16  ? -7.500  -15.599 30.194  0.20 25.35  ? 16  ILE A C     1 
ATOM   228   C  C     B ILE A 1 16  ? -7.179  -15.509 30.146  0.80 25.75  ? 16  ILE A C     1 
ATOM   229   O  O     A ILE A 1 16  ? -8.087  -16.010 31.197  0.20 26.79  ? 16  ILE A O     1 
ATOM   230   O  O     B ILE A 1 16  ? -7.857  -15.936 31.086  0.80 26.77  ? 16  ILE A O     1 
ATOM   231   C  CB    A ILE A 1 16  ? -5.304  -14.363 30.439  0.20 27.96  ? 16  ILE A CB    1 
ATOM   232   C  CB    B ILE A 1 16  ? -4.971  -14.352 30.611  0.80 28.99  ? 16  ILE A CB    1 
ATOM   233   C  CG1   A ILE A 1 16  ? -3.816  -14.583 30.695  0.20 24.83  ? 16  ILE A CG1   1 
ATOM   234   C  CG1   B ILE A 1 16  ? -3.500  -14.636 30.854  0.80 25.55  ? 16  ILE A CG1   1 
ATOM   235   C  CG2   A ILE A 1 16  ? -5.971  -13.713 31.647  0.20 24.29  ? 16  ILE A CG2   1 
ATOM   236   C  CG2   B ILE A 1 16  ? -5.637  -13.779 31.880  0.80 23.75  ? 16  ILE A CG2   1 
ATOM   237   C  CD1   A ILE A 1 16  ? -3.069  -13.314 30.990  0.20 26.53  ? 16  ILE A CD1   1 
ATOM   238   C  CD1   B ILE A 1 16  ? -2.666  -13.399 30.946  0.80 28.13  ? 16  ILE A CD1   1 
ATOM   239   N  N     A GLY A 1 17  ? -8.144  -15.060 29.158  0.20 24.30  ? 17  GLY A N     1 
ATOM   240   N  N     B GLY A 1 17  ? -7.730  -14.935 29.074  0.80 25.05  ? 17  GLY A N     1 
ATOM   241   C  CA    A GLY A 1 17  ? -9.594  -15.001 29.147  0.20 26.78  ? 17  GLY A CA    1 
ATOM   242   C  CA    B GLY A 1 17  ? -9.173  -14.830 28.953  0.80 26.70  ? 17  GLY A CA    1 
ATOM   243   C  C     A GLY A 1 17  ? -10.239 -16.371 29.134  0.20 29.87  ? 17  GLY A C     1 
ATOM   244   C  C     B GLY A 1 17  ? -9.860  -16.175 29.062  0.80 33.08  ? 17  GLY A C     1 
ATOM   245   O  O     A GLY A 1 17  ? -11.324 -16.555 29.687  0.20 28.36  ? 17  GLY A O     1 
ATOM   246   O  O     B GLY A 1 17  ? -10.836 -16.328 29.798  0.80 26.96  ? 17  GLY A O     1 
ATOM   247   N  N     A ASN A 1 18  ? -9.583  -17.354 28.515  0.20 26.56  ? 18  ASN A N     1 
ATOM   248   N  N     B ASN A 1 18  ? -9.333  -17.184 28.363  0.80 24.38  ? 18  ASN A N     1 
ATOM   249   C  CA    A ASN A 1 18  ? -10.141 -18.700 28.508  0.20 29.87  ? 18  ASN A CA    1 
ATOM   250   C  CA    B ASN A 1 18  ? -9.928  -18.511 28.462  0.80 29.42  ? 18  ASN A CA    1 
ATOM   251   C  C     A ASN A 1 18  ? -10.131 -19.305 29.907  0.20 32.13  ? 18  ASN A C     1 
ATOM   252   C  C     B ASN A 1 18  ? -9.914  -19.018 29.902  0.80 32.84  ? 18  ASN A C     1 
ATOM   253   O  O     A ASN A 1 18  ? -11.059 -20.032 30.283  0.20 29.53  ? 18  ASN A O     1 
ATOM   254   O  O     B ASN A 1 18  ? -10.919 -19.553 30.392  0.80 29.21  ? 18  ASN A O     1 
ATOM   255   C  CB    A ASN A 1 18  ? -9.371  -19.578 27.527  0.20 32.79  ? 18  ASN A CB    1 
ATOM   256   C  CB    B ASN A 1 18  ? -9.202  -19.474 27.529  0.80 32.78  ? 18  ASN A CB    1 
ATOM   257   C  CG    A ASN A 1 18  ? -10.163 -20.789 27.089  0.20 38.86  ? 18  ASN A CG    1 
ATOM   258   C  CG    B ASN A 1 18  ? -9.787  -20.866 27.568  0.80 41.45  ? 18  ASN A CG    1 
ATOM   259   O  OD1   A ASN A 1 18  ? -11.380 -20.851 27.280  0.20 41.99  ? 18  ASN A OD1   1 
ATOM   260   O  OD1   B ASN A 1 18  ? -9.112  -21.824 27.947  0.80 47.38  ? 18  ASN A OD1   1 
ATOM   261   N  ND2   A ASN A 1 18  ? -9.482  -21.757 26.492  0.20 35.62  ? 18  ASN A ND2   1 
ATOM   262   N  ND2   B ASN A 1 18  ? -11.058 -20.985 27.194  0.80 45.78  ? 18  ASN A ND2   1 
ATOM   263   N  N     A ALA A 1 19  ? -9.098  -19.007 30.696  0.20 28.17  ? 19  ALA A N     1 
ATOM   264   N  N     B ALA A 1 19  ? -8.802  -18.818 30.608  0.80 28.13  ? 19  ALA A N     1 
ATOM   265   C  CA    A ALA A 1 19  ? -9.052  -19.471 32.077  0.20 29.17  ? 19  ALA A CA    1 
ATOM   266   C  CA    B ALA A 1 19  ? -8.711  -19.245 32.002  0.80 29.44  ? 19  ALA A CA    1 
ATOM   267   C  C     A ALA A 1 19  ? -9.933  -18.629 32.992  0.20 26.66  ? 19  ALA A C     1 
ATOM   268   C  C     B ALA A 1 19  ? -9.721  -18.513 32.885  0.80 26.09  ? 19  ALA A C     1 
ATOM   269   O  O     A ALA A 1 19  ? -10.493 -19.155 33.961  0.20 28.34  ? 19  ALA A O     1 
ATOM   270   O  O     B ALA A 1 19  ? -10.359 -19.127 33.748  0.80 28.76  ? 19  ALA A O     1 
ATOM   271   C  CB    A ALA A 1 19  ? -7.609  -19.467 32.586  0.20 27.91  ? 19  ALA A CB    1 
ATOM   272   C  CB    B ALA A 1 19  ? -7.284  -19.032 32.513  0.80 26.70  ? 19  ALA A CB    1 
ATOM   273   N  N     A CYS A 1 20  ? -10.068 -17.331 32.707  0.20 25.71  ? 20  CYS A N     1 
ATOM   274   N  N     B CYS A 1 20  ? -9.873  -17.199 32.687  0.80 25.13  ? 20  CYS A N     1 
ATOM   275   C  CA    A CYS A 1 20  ? -10.915 -16.476 33.533  0.20 21.66  ? 20  CYS A CA    1 
ATOM   276   C  CA    B CYS A 1 20  ? -10.781 -16.401 33.516  0.80 20.75  ? 20  CYS A CA    1 
ATOM   277   C  C     A CYS A 1 20  ? -12.390 -16.797 33.335  0.20 28.58  ? 20  CYS A C     1 
ATOM   278   C  C     B CYS A 1 20  ? -12.230 -16.816 33.324  0.80 28.74  ? 20  CYS A C     1 
ATOM   279   O  O     A CYS A 1 20  ? -13.165 -16.811 34.301  0.20 24.24  ? 20  CYS A O     1 
ATOM   280   O  O     B CYS A 1 20  ? -12.995 -16.938 34.300  0.80 23.61  ? 20  CYS A O     1 
ATOM   281   C  CB    A CYS A 1 20  ? -10.643 -15.005 33.222  0.20 26.34  ? 20  CYS A CB    1 
ATOM   282   C  CB    B CYS A 1 20  ? -10.624 -14.921 33.182  0.80 26.28  ? 20  CYS A CB    1 
ATOM   283   S  SG    A CYS A 1 20  ? -9.064  -14.395 33.846  0.20 29.96  ? 20  CYS A SG    1 
ATOM   284   S  SG    B CYS A 1 20  ? -9.082  -14.185 33.735  0.80 31.57  ? 20  CYS A SG    1 
ATOM   285   N  N     A TRP A 1 21  ? -12.803 -17.047 32.090  0.20 27.56  ? 21  TRP A N     1 
ATOM   286   N  N     B TRP A 1 21  ? -12.645 -16.998 32.071  0.80 27.41  ? 21  TRP A N     1 
ATOM   287   C  CA    A TRP A 1 21  ? -14.191 -17.426 31.853  0.20 27.92  ? 21  TRP A CA    1 
ATOM   288   C  CA    B TRP A 1 21  ? -14.043 -17.324 31.824  0.80 28.34  ? 21  TRP A CA    1 
ATOM   289   C  C     A TRP A 1 21  ? -14.482 -18.826 32.375  0.20 28.69  ? 21  TRP A C     1 
ATOM   290   C  C     B TRP A 1 21  ? -14.394 -18.707 32.340  0.80 28.61  ? 21  TRP A C     1 
ATOM   291   O  O     A TRP A 1 21  ? -15.621 -19.114 32.760  0.20 28.39  ? 21  TRP A O     1 
ATOM   292   O  O     B TRP A 1 21  ? -15.523 -18.924 32.789  0.80 27.50  ? 21  TRP A O     1 
ATOM   293   C  CB    A TRP A 1 21  ? -14.525 -17.322 30.364  0.20 28.36  ? 21  TRP A CB    1 
ATOM   294   C  CB    B TRP A 1 21  ? -14.364 -17.187 30.334  0.80 28.35  ? 21  TRP A CB    1 
ATOM   295   C  CG    A TRP A 1 21  ? -14.650 -15.907 29.887  0.20 26.54  ? 21  TRP A CG    1 
ATOM   296   C  CG    B TRP A 1 21  ? -14.472 -15.761 29.942  0.80 26.33  ? 21  TRP A CG    1 
ATOM   297   C  CD1   A TRP A 1 21  ? -13.817 -15.253 29.026  0.20 25.65  ? 21  TRP A CD1   1 
ATOM   298   C  CD1   B TRP A 1 21  ? -13.539 -15.019 29.266  0.80 24.11  ? 21  TRP A CD1   1 
ATOM   299   C  CD2   A TRP A 1 21  ? -15.667 -14.965 30.253  0.20 26.02  ? 21  TRP A CD2   1 
ATOM   300   C  CD2   B TRP A 1 21  ? -15.564 -14.871 30.229  0.80 25.58  ? 21  TRP A CD2   1 
ATOM   301   N  NE1   A TRP A 1 21  ? -14.252 -13.965 28.832  0.20 28.40  ? 21  TRP A NE1   1 
ATOM   302   N  NE1   B TRP A 1 21  ? -13.988 -13.731 29.108  0.80 29.95  ? 21  TRP A NE1   1 
ATOM   303   C  CE2   A TRP A 1 21  ? -15.388 -13.763 29.573  0.20 27.85  ? 21  TRP A CE2   1 
ATOM   304   C  CE2   B TRP A 1 21  ? -15.229 -13.613 29.685  0.80 28.43  ? 21  TRP A CE2   1 
ATOM   305   C  CE3   A TRP A 1 21  ? -16.789 -15.023 31.087  0.20 27.49  ? 21  TRP A CE3   1 
ATOM   306   C  CE3   B TRP A 1 21  ? -16.794 -15.020 30.881  0.80 27.36  ? 21  TRP A CE3   1 
ATOM   307   C  CZ2   A TRP A 1 21  ? -16.185 -12.628 29.704  0.20 28.45  ? 21  TRP A CZ2   1 
ATOM   308   C  CZ2   B TRP A 1 21  ? -16.073 -12.506 29.782  0.80 28.51  ? 21  TRP A CZ2   1 
ATOM   309   C  CZ3   A TRP A 1 21  ? -17.579 -13.894 31.215  0.20 26.41  ? 21  TRP A CZ3   1 
ATOM   310   C  CZ3   B TRP A 1 21  ? -17.635 -13.921 30.974  0.80 25.72  ? 21  TRP A CZ3   1 
ATOM   311   C  CH2   A TRP A 1 21  ? -17.276 -12.714 30.525  0.20 28.07  ? 21  TRP A CH2   1 
ATOM   312   C  CH2   B TRP A 1 21  ? -17.274 -12.680 30.421  0.80 28.29  ? 21  TRP A CH2   1 
ATOM   313   N  N     A GLU A 1 22  ? -13.477 -19.706 32.397  0.20 28.99  ? 22  GLU A N     1 
ATOM   314   N  N     B GLU A 1 22  ? -13.455 -19.657 32.289  0.80 28.61  ? 22  GLU A N     1 
ATOM   315   C  CA    A GLU A 1 22  ? -13.665 -21.007 33.029  0.20 30.82  ? 22  GLU A CA    1 
ATOM   316   C  CA    B GLU A 1 22  ? -13.705 -20.944 32.929  0.80 30.98  ? 22  GLU A CA    1 
ATOM   317   C  C     A GLU A 1 22  ? -13.883 -20.859 34.530  0.20 31.01  ? 22  GLU A C     1 
ATOM   318   C  C     B GLU A 1 22  ? -14.012 -20.754 34.413  0.80 31.22  ? 22  GLU A C     1 
ATOM   319   O  O     A GLU A 1 22  ? -14.660 -21.611 35.130  0.20 29.04  ? 22  GLU A O     1 
ATOM   320   O  O     B GLU A 1 22  ? -15.076 -21.166 34.901  0.80 24.78  ? 22  GLU A O     1 
ATOM   321   C  CB    A GLU A 1 22  ? -12.466 -21.913 32.751  0.20 34.70  ? 22  GLU A CB    1 
ATOM   322   C  CB    B GLU A 1 22  ? -12.510 -21.878 32.728  0.80 34.83  ? 22  GLU A CB    1 
ATOM   323   C  CG    A GLU A 1 22  ? -12.531 -23.251 33.474  0.20 36.15  ? 22  GLU A CG    1 
ATOM   324   C  CG    B GLU A 1 22  ? -12.558 -23.129 33.597  0.80 35.39  ? 22  GLU A CG    1 
ATOM   325   C  CD    A GLU A 1 22  ? -11.269 -24.075 33.308  0.20 47.75  ? 22  GLU A CD    1 
ATOM   326   C  CD    B GLU A 1 22  ? -11.439 -24.113 33.290  0.80 48.14  ? 22  GLU A CD    1 
ATOM   327   O  OE1   A GLU A 1 22  ? -10.367 -23.641 32.564  0.20 50.82  ? 22  GLU A OE1   1 
ATOM   328   O  OE1   B GLU A 1 22  ? -10.501 -23.742 32.558  0.80 50.97  ? 22  GLU A OE1   1 
ATOM   329   O  OE2   A GLU A 1 22  ? -11.181 -25.158 33.924  0.20 54.31  ? 22  GLU A OE2   1 
ATOM   330   O  OE2   B GLU A 1 22  ? -11.502 -25.260 33.782  0.80 55.99  ? 22  GLU A OE2   1 
ATOM   331   N  N     A LEU A 1 23  ? -13.212 -19.888 35.152  0.20 28.61  ? 23  LEU A N     1 
ATOM   332   N  N     B LEU A 1 23  ? -13.114 -20.078 35.135  0.80 28.11  ? 23  LEU A N     1 
ATOM   333   C  CA    A LEU A 1 23  ? -13.396 -19.664 36.582  0.20 30.20  ? 23  LEU A CA    1 
ATOM   334   C  CA    B LEU A 1 23  ? -13.339 -19.837 36.562  0.80 30.71  ? 23  LEU A CA    1 
ATOM   335   C  C     A LEU A 1 23  ? -14.697 -18.924 36.870  0.20 30.57  ? 23  LEU A C     1 
ATOM   336   C  C     B LEU A 1 23  ? -14.653 -19.108 36.806  0.80 30.91  ? 23  LEU A C     1 
ATOM   337   O  O     A LEU A 1 23  ? -15.340 -19.174 37.895  0.20 28.06  ? 23  LEU A O     1 
ATOM   338   O  O     B LEU A 1 23  ? -15.437 -19.517 37.672  0.80 26.51  ? 23  LEU A O     1 
ATOM   339   C  CB    A LEU A 1 23  ? -12.201 -18.897 37.152  0.20 28.20  ? 23  LEU A CB    1 
ATOM   340   C  CB    B LEU A 1 23  ? -12.173 -19.054 37.166  0.80 28.06  ? 23  LEU A CB    1 
ATOM   341   C  CG    A LEU A 1 23  ? -12.212 -18.610 38.655  0.20 29.29  ? 23  LEU A CG    1 
ATOM   342   C  CG    B LEU A 1 23  ? -12.296 -18.763 38.664  0.80 29.28  ? 23  LEU A CG    1 
ATOM   343   C  CD1   A LEU A 1 23  ? -12.417 -19.889 39.452  0.20 30.69  ? 23  LEU A CD1   1 
ATOM   344   C  CD1   B LEU A 1 23  ? -12.509 -20.043 39.469  0.80 30.55  ? 23  LEU A CD1   1 
ATOM   345   C  CD2   A LEU A 1 23  ? -10.922 -17.930 39.063  0.20 29.29  ? 23  LEU A CD2   1 
ATOM   346   C  CD2   B LEU A 1 23  ? -11.075 -18.047 39.145  0.80 28.74  ? 23  LEU A CD2   1 
ATOM   347   N  N     A TYR A 1 24  ? -15.094 -18.001 35.988  0.20 27.48  ? 24  TYR A N     1 
ATOM   348   N  N     B TYR A 1 24  ? -14.915 -18.022 36.058  0.80 26.80  ? 24  TYR A N     1 
ATOM   349   C  CA    A TYR A 1 24  ? -16.378 -17.326 36.161  0.20 29.50  ? 24  TYR A CA    1 
ATOM   350   C  CA    B TYR A 1 24  ? -16.196 -17.322 36.196  0.80 29.74  ? 24  TYR A CA    1 
ATOM   351   C  C     A TYR A 1 24  ? -17.530 -18.323 36.124  0.20 32.07  ? 24  TYR A C     1 
ATOM   352   C  C     B TYR A 1 24  ? -17.363 -18.299 36.117  0.80 32.20  ? 24  TYR A C     1 
ATOM   353   O  O     A TYR A 1 24  ? -18.485 -18.212 36.905  0.20 30.46  ? 24  TYR A O     1 
ATOM   354   O  O     B TYR A 1 24  ? -18.314 -18.230 36.913  0.80 30.85  ? 24  TYR A O     1 
ATOM   355   C  CB    A TYR A 1 24  ? -16.561 -16.258 35.081  0.20 23.63  ? 24  TYR A CB    1 
ATOM   356   C  CB    B TYR A 1 24  ? -16.363 -16.251 35.108  0.80 22.47  ? 24  TYR A CB    1 
ATOM   357   C  CG    A TYR A 1 24  ? -15.593 -15.099 35.172  0.20 29.67  ? 24  TYR A CG    1 
ATOM   358   C  CG    B TYR A 1 24  ? -15.460 -15.029 35.163  0.80 29.91  ? 24  TYR A CG    1 
ATOM   359   C  CD1   A TYR A 1 24  ? -15.060 -14.702 36.392  0.20 29.52  ? 24  TYR A CD1   1 
ATOM   360   C  CD1   B TYR A 1 24  ? -14.563 -14.816 36.212  0.80 31.76  ? 24  TYR A CD1   1 
ATOM   361   C  CD2   A TYR A 1 24  ? -15.209 -14.403 34.033  0.20 26.87  ? 24  TYR A CD2   1 
ATOM   362   C  CD2   B TYR A 1 24  ? -15.516 -14.080 34.151  0.80 27.27  ? 24  TYR A CD2   1 
ATOM   363   C  CE1   A TYR A 1 24  ? -14.171 -13.640 36.473  0.20 30.93  ? 24  TYR A CE1   1 
ATOM   364   C  CE1   B TYR A 1 24  ? -13.734 -13.679 36.231  0.80 29.57  ? 24  TYR A CE1   1 
ATOM   365   C  CE2   A TYR A 1 24  ? -14.323 -13.342 34.105  0.20 27.72  ? 24  TYR A CE2   1 
ATOM   366   C  CE2   B TYR A 1 24  ? -14.703 -12.942 34.168  0.80 27.37  ? 24  TYR A CE2   1 
ATOM   367   C  CZ    A TYR A 1 24  ? -13.808 -12.965 35.326  0.20 28.02  ? 24  TYR A CZ    1 
ATOM   368   C  CZ    B TYR A 1 24  ? -13.823 -12.747 35.205  0.80 26.96  ? 24  TYR A CZ    1 
ATOM   369   O  OH    A TYR A 1 24  ? -12.929 -11.908 35.399  0.20 35.86  ? 24  TYR A OH    1 
ATOM   370   O  OH    B TYR A 1 24  ? -13.032 -11.616 35.213  0.80 37.74  ? 24  TYR A OH    1 
ATOM   371   N  N     A CYS A 1 25  ? -17.458 -19.308 35.225  0.20 31.80  ? 25  CYS A N     1 
ATOM   372   N  N     B CYS A 1 25  ? -17.319 -19.210 35.140  0.80 31.76  ? 25  CYS A N     1 
ATOM   373   C  CA    A CYS A 1 25  ? -18.517 -20.307 35.139  0.20 31.42  ? 25  CYS A CA    1 
ATOM   374   C  CA    B CYS A 1 25  ? -18.395 -20.182 35.000  0.80 30.44  ? 25  CYS A CA    1 
ATOM   375   C  C     A CYS A 1 25  ? -18.590 -21.146 36.407  0.20 31.93  ? 25  CYS A C     1 
ATOM   376   C  C     B CYS A 1 25  ? -18.557 -20.998 36.273  0.80 31.85  ? 25  CYS A C     1 
ATOM   377   O  O     A CYS A 1 25  ? -19.683 -21.508 36.857  0.20 31.85  ? 25  CYS A O     1 
ATOM   378   O  O     B CYS A 1 25  ? -19.677 -21.197 36.756  0.80 30.63  ? 25  CYS A O     1 
ATOM   379   C  CB    A CYS A 1 25  ? -18.304 -21.195 33.913  0.20 37.92  ? 25  CYS A CB    1 
ATOM   380   C  CB    B CYS A 1 25  ? -18.145 -21.092 33.796  0.80 38.17  ? 25  CYS A CB    1 
ATOM   381   S  SG    A CYS A 1 25  ? -18.559 -20.357 32.331  0.20 109.05 ? 25  CYS A SG    1 
ATOM   382   S  SG    B CYS A 1 25  ? -18.548 -20.328 32.210  0.80 95.60  ? 25  CYS A SG    1 
ATOM   383   N  N     A LEU A 1 26  ? -17.438 -21.464 37.000  0.20 30.40  ? 26  LEU A N     1 
ATOM   384   N  N     B LEU A 1 26  ? -17.445 -21.468 36.841  0.80 30.34  ? 26  LEU A N     1 
ATOM   385   C  CA    A LEU A 1 26  ? -17.433 -22.256 38.224  0.20 29.05  ? 26  LEU A CA    1 
ATOM   386   C  CA    B LEU A 1 26  ? -17.538 -22.273 38.055  0.80 28.82  ? 26  LEU A CA    1 
ATOM   387   C  C     A LEU A 1 26  ? -17.857 -21.442 39.440  0.20 30.91  ? 26  LEU A C     1 
ATOM   388   C  C     B LEU A 1 26  ? -18.077 -21.452 39.218  0.80 32.01  ? 26  LEU A C     1 
ATOM   389   O  O     A LEU A 1 26  ? -18.417 -22.005 40.388  0.20 30.04  ? 26  LEU A O     1 
ATOM   390   O  O     B LEU A 1 26  ? -18.826 -21.972 40.055  0.80 28.11  ? 26  LEU A O     1 
ATOM   391   C  CB    A LEU A 1 26  ? -16.050 -22.861 38.457  0.20 26.91  ? 26  LEU A CB    1 
ATOM   392   C  CB    B LEU A 1 26  ? -16.179 -22.873 38.406  0.80 26.46  ? 26  LEU A CB    1 
ATOM   393   C  CG    A LEU A 1 26  ? -15.581 -23.848 37.389  0.20 31.70  ? 26  LEU A CG    1 
ATOM   394   C  CG    B LEU A 1 26  ? -15.601 -23.837 37.364  0.80 31.66  ? 26  LEU A CG    1 
ATOM   395   C  CD1   A LEU A 1 26  ? -14.182 -24.347 37.698  0.20 33.10  ? 26  LEU A CD1   1 
ATOM   396   C  CD1   B LEU A 1 26  ? -14.226 -24.320 37.784  0.80 32.95  ? 26  LEU A CD1   1 
ATOM   397   C  CD2   A LEU A 1 26  ? -16.556 -25.010 37.269  0.20 34.70  ? 26  LEU A CD2   1 
ATOM   398   C  CD2   B LEU A 1 26  ? -16.535 -25.012 37.145  0.80 35.23  ? 26  LEU A CD2   1 
ATOM   399   N  N     A GLU A 1 27  ? -17.611 -20.131 39.435  0.20 27.02  ? 27  GLU A N     1 
ATOM   400   N  N     B GLU A 1 27  ? -17.722 -20.163 39.277  0.80 26.03  ? 27  GLU A N     1 
ATOM   401   C  CA    A GLU A 1 27  ? -18.036 -19.295 40.554  0.20 28.56  ? 27  GLU A CA    1 
ATOM   402   C  CA    B GLU A 1 27  ? -18.184 -19.311 40.376  0.80 27.96  ? 27  GLU A CA    1 
ATOM   403   C  C     A GLU A 1 27  ? -19.518 -18.952 40.485  0.20 32.69  ? 27  GLU A C     1 
ATOM   404   C  C     B GLU A 1 27  ? -19.692 -19.094 40.336  0.80 33.82  ? 27  GLU A C     1 
ATOM   405   O  O     A GLU A 1 27  ? -20.142 -18.719 41.527  0.20 27.61  ? 27  GLU A O     1 
ATOM   406   O  O     B GLU A 1 27  ? -20.341 -19.025 41.391  0.80 27.17  ? 27  GLU A O     1 
ATOM   407   C  CB    A GLU A 1 27  ? -17.212 -18.007 40.603  0.20 31.21  ? 27  GLU A CB    1 
ATOM   408   C  CB    B GLU A 1 27  ? -17.458 -17.965 40.335  0.80 31.09  ? 27  GLU A CB    1 
ATOM   409   C  CG    A GLU A 1 27  ? -15.752 -18.220 40.968  0.20 30.91  ? 27  GLU A CG    1 
ATOM   410   C  CG    B GLU A 1 27  ? -15.960 -18.075 40.578  0.80 30.63  ? 27  GLU A CG    1 
ATOM   411   C  CD    A GLU A 1 27  ? -14.968 -16.923 41.024  0.20 29.98  ? 27  GLU A CD    1 
ATOM   412   C  CD    B GLU A 1 27  ? -15.282 -16.730 40.699  0.80 28.58  ? 27  GLU A CD    1 
ATOM   413   O  OE1   A GLU A 1 27  ? -15.597 -15.844 41.057  0.20 31.87  ? 27  GLU A OE1   1 
ATOM   414   O  OE1   B GLU A 1 27  ? -15.965 -15.705 40.505  0.80 36.02  ? 27  GLU A OE1   1 
ATOM   415   O  OE2   A GLU A 1 27  ? -13.720 -16.983 41.032  0.20 29.67  ? 27  GLU A OE2   1 
ATOM   416   O  OE2   B GLU A 1 27  ? -14.061 -16.701 40.981  0.80 30.35  ? 27  GLU A OE2   1 
ATOM   417   N  N     A HIS A 1 28  ? -20.090 -18.906 39.282  0.20 28.65  ? 28  HIS A N     1 
ATOM   418   N  N     B HIS A 1 28  ? -20.265 -18.972 39.139  0.80 27.92  ? 28  HIS A N     1 
ATOM   419   C  CA    A HIS A 1 28  ? -21.507 -18.622 39.101  0.20 32.33  ? 28  HIS A CA    1 
ATOM   420   C  CA    B HIS A 1 28  ? -21.665 -18.607 38.964  0.80 32.37  ? 28  HIS A CA    1 
ATOM   421   C  C     A HIS A 1 28  ? -22.348 -19.873 38.890  0.20 33.30  ? 28  HIS A C     1 
ATOM   422   C  C     B HIS A 1 28  ? -22.583 -19.800 38.747  0.80 34.26  ? 28  HIS A C     1 
ATOM   423   O  O     A HIS A 1 28  ? -23.581 -19.782 38.915  0.20 33.37  ? 28  HIS A O     1 
ATOM   424   O  O     B HIS A 1 28  ? -23.810 -19.620 38.722  0.80 31.57  ? 28  HIS A O     1 
ATOM   425   C  CB    A HIS A 1 28  ? -21.712 -17.671 37.914  0.20 34.33  ? 28  HIS A CB    1 
ATOM   426   C  CB    B HIS A 1 28  ? -21.810 -17.642 37.782  0.80 34.75  ? 28  HIS A CB    1 
ATOM   427   C  CG    A HIS A 1 28  ? -21.173 -16.293 38.142  0.20 36.70  ? 28  HIS A CG    1 
ATOM   428   C  CG    B HIS A 1 28  ? -21.189 -16.301 38.018  0.80 37.29  ? 28  HIS A CG    1 
ATOM   429   N  ND1   A HIS A 1 28  ? -21.823 -15.360 38.922  0.20 31.89  ? 28  HIS A ND1   1 
ATOM   430   N  ND1   B HIS A 1 28  ? -21.754 -15.354 38.849  0.80 31.88  ? 28  HIS A ND1   1 
ATOM   431   C  CD2   A HIS A 1 28  ? -20.051 -15.687 37.687  0.20 28.35  ? 28  HIS A CD2   1 
ATOM   432   C  CD2   B HIS A 1 28  ? -20.053 -15.745 37.529  0.80 27.66  ? 28  HIS A CD2   1 
ATOM   433   C  CE1   A HIS A 1 28  ? -21.121 -14.240 38.942  0.20 30.53  ? 28  HIS A CE1   1 
ATOM   434   C  CE1   B HIS A 1 28  ? -20.989 -14.276 38.865  0.80 30.38  ? 28  HIS A CE1   1 
ATOM   435   N  NE2   A HIS A 1 28  ? -20.042 -14.412 38.199  0.20 31.28  ? 28  HIS A NE2   1 
ATOM   436   N  NE2   B HIS A 1 28  ? -19.953 -14.486 38.070  0.80 31.08  ? 28  HIS A NE2   1 
ATOM   437   N  N     A GLY A 1 29  ? -21.719 -21.027 38.678  0.20 32.95  ? 29  GLY A N     1 
ATOM   438   N  N     B GLY A 1 29  ? -22.028 -20.999 38.571  0.80 32.82  ? 29  GLY A N     1 
ATOM   439   C  CA    A GLY A 1 29  ? -22.444 -22.265 38.481  0.20 32.42  ? 29  GLY A CA    1 
ATOM   440   C  CA    B GLY A 1 29  ? -22.821 -22.187 38.334  0.80 32.16  ? 29  GLY A CA    1 
ATOM   441   C  C     A GLY A 1 29  ? -22.901 -22.530 37.066  0.20 36.26  ? 29  GLY A C     1 
ATOM   442   C  C     B GLY A 1 29  ? -23.355 -22.250 36.920  0.80 40.94  ? 29  GLY A C     1 
ATOM   443   O  O     A GLY A 1 29  ? -23.816 -23.339 36.871  0.20 35.68  ? 29  GLY A O     1 
ATOM   444   O  O     B GLY A 1 29  ? -24.554 -22.479 36.713  0.80 26.68  ? 29  GLY A O     1 
ATOM   445   N  N     A ILE A 1 30  ? -22.299 -21.881 36.074  0.20 33.18  ? 30  ILE A N     1 
ATOM   446   N  N     B ILE A 1 30  ? -22.473 -22.021 35.945  0.80 32.19  ? 30  ILE A N     1 
ATOM   447   C  CA    A ILE A 1 30  ? -22.701 -22.033 34.680  0.20 36.42  ? 30  ILE A CA    1 
ATOM   448   C  CA    B ILE A 1 30  ? -22.780 -22.125 34.522  0.80 36.45  ? 30  ILE A CA    1 
ATOM   449   C  C     A ILE A 1 30  ? -22.004 -23.252 34.092  0.20 40.13  ? 30  ILE A C     1 
ATOM   450   C  C     B ILE A 1 30  ? -22.016 -23.319 33.966  0.80 40.37  ? 30  ILE A C     1 
ATOM   451   O  O     A ILE A 1 30  ? -20.783 -23.405 34.215  0.20 37.75  ? 30  ILE A O     1 
ATOM   452   O  O     B ILE A 1 30  ? -20.812 -23.462 34.208  0.80 37.81  ? 30  ILE A O     1 
ATOM   453   C  CB    A ILE A 1 30  ? -22.375 -20.764 33.873  0.20 34.65  ? 30  ILE A CB    1 
ATOM   454   C  CB    B ILE A 1 30  ? -22.409 -20.835 33.762  0.80 34.35  ? 30  ILE A CB    1 
ATOM   455   C  CG1   A ILE A 1 30  ? -23.094 -19.555 34.476  0.20 33.15  ? 30  ILE A CG1   1 
ATOM   456   C  CG1   B ILE A 1 30  ? -23.132 -19.630 34.366  0.80 32.84  ? 30  ILE A CG1   1 
ATOM   457   C  CG2   A ILE A 1 30  ? -22.755 -20.946 32.409  0.20 35.41  ? 30  ILE A CG2   1 
ATOM   458   C  CG2   B ILE A 1 30  ? -22.720 -20.976 32.273  0.80 35.00  ? 30  ILE A CG2   1 
ATOM   459   C  CD1   A ILE A 1 30  ? -22.811 -18.251 33.768  0.20 37.24  ? 30  ILE A CD1   1 
ATOM   460   C  CD1   B ILE A 1 30  ? -22.471 -18.294 34.095  0.80 37.81  ? 30  ILE A CD1   1 
ATOM   461   N  N     A GLN A 1 31  ? -22.783 -24.119 33.449  0.20 42.11  ? 31  GLN A N     1 
ATOM   462   N  N     B GLN A 1 31  ? -22.714 -24.169 33.227  0.80 42.78  ? 31  GLN A N     1 
ATOM   463   C  CA    A GLN A 1 31  ? -22.242 -25.305 32.813  0.20 42.52  ? 31  GLN A CA    1 
ATOM   464   C  CA    B GLN A 1 31  ? -22.138 -25.370 32.648  0.80 42.40  ? 31  GLN A CA    1 
ATOM   465   C  C     A GLN A 1 31  ? -21.496 -24.926 31.534  0.20 40.84  ? 31  GLN A C     1 
ATOM   466   C  C     B GLN A 1 31  ? -21.393 -25.036 31.358  0.80 40.49  ? 31  GLN A C     1 
ATOM   467   O  O     A GLN A 1 31  ? -21.660 -23.819 31.016  0.20 43.15  ? 31  GLN A O     1 
ATOM   468   O  O     B GLN A 1 31  ? -21.559 -23.949 30.803  0.80 44.01  ? 31  GLN A O     1 
ATOM   469   C  CB    A GLN A 1 31  ? -23.369 -26.289 32.507  0.20 43.74  ? 31  GLN A CB    1 
ATOM   470   C  CB    B GLN A 1 31  ? -23.244 -26.393 32.402  0.80 43.49  ? 31  GLN A CB    1 
ATOM   471   C  CG    A GLN A 1 31  ? -24.110 -26.781 33.739  0.20 47.80  ? 31  GLN A CG    1 
ATOM   472   C  CG    B GLN A 1 31  ? -23.891 -26.877 33.694  0.80 47.57  ? 31  GLN A CG    1 
ATOM   473   C  CD    A GLN A 1 31  ? -25.286 -27.676 33.394  0.20 55.96  ? 31  GLN A CD    1 
ATOM   474   C  CD    B GLN A 1 31  ? -24.858 -28.031 33.479  0.80 59.31  ? 31  GLN A CD    1 
ATOM   475   O  OE1   A GLN A 1 31  ? -25.738 -27.714 32.249  0.20 56.12  ? 31  GLN A OE1   1 
ATOM   476   O  OE1   B GLN A 1 31  ? -25.328 -28.267 32.362  0.80 62.96  ? 31  GLN A OE1   1 
ATOM   477   N  NE2   A GLN A 1 31  ? -25.787 -28.403 34.386  0.20 57.05  ? 31  GLN A NE2   1 
ATOM   478   N  NE2   B GLN A 1 31  ? -25.156 -28.761 34.552  0.80 58.01  ? 31  GLN A NE2   1 
ATOM   479   N  N     A PRO A 1 32  ? -20.651 -25.824 31.014  0.20 41.12  ? 32  PRO A N     1 
ATOM   480   N  N     B PRO A 1 32  ? -20.538 -25.943 30.872  0.80 40.59  ? 32  PRO A N     1 
ATOM   481   C  CA    A PRO A 1 32  ? -19.929 -25.502 29.772  0.20 41.56  ? 32  PRO A CA    1 
ATOM   482   C  CA    B PRO A 1 32  ? -19.770 -25.634 29.655  0.80 41.01  ? 32  PRO A CA    1 
ATOM   483   C  C     A PRO A 1 32  ? -20.838 -25.186 28.597  0.20 44.07  ? 32  PRO A C     1 
ATOM   484   C  C     B PRO A 1 32  ? -20.635 -25.351 28.436  0.80 44.76  ? 32  PRO A C     1 
ATOM   485   O  O     A PRO A 1 32  ? -20.429 -24.445 27.694  0.20 43.84  ? 32  PRO A O     1 
ATOM   486   O  O     B PRO A 1 32  ? -20.135 -24.757 27.470  0.80 43.97  ? 32  PRO A O     1 
ATOM   487   C  CB    A PRO A 1 32  ? -19.095 -26.765 29.517  0.20 43.85  ? 32  PRO A CB    1 
ATOM   488   C  CB    B PRO A 1 32  ? -18.912 -26.890 29.450  0.80 43.87  ? 32  PRO A CB    1 
ATOM   489   C  CG    A PRO A 1 32  ? -18.899 -27.358 30.862  0.20 43.18  ? 32  PRO A CG    1 
ATOM   490   C  CG    B PRO A 1 32  ? -18.791 -27.494 30.793  0.80 43.04  ? 32  PRO A CG    1 
ATOM   491   C  CD    A PRO A 1 32  ? -20.169 -27.080 31.617  0.20 38.53  ? 32  PRO A CD    1 
ATOM   492   C  CD    B PRO A 1 32  ? -20.093 -27.205 31.494  0.80 37.83  ? 32  PRO A CD    1 
ATOM   493   N  N     A ASP A 1 33  ? -22.060 -25.718 28.575  0.20 44.17  ? 33  ASP A N     1 
ATOM   494   N  N     B ASP A 1 33  ? -21.909 -25.746 28.443  0.80 44.61  ? 33  ASP A N     1 
ATOM   495   C  CA    A ASP A 1 33  ? -22.987 -25.435 27.486  0.20 43.18  ? 33  ASP A CA    1 
ATOM   496   C  CA    B ASP A 1 33  ? -22.803 -25.461 27.327  0.80 42.85  ? 33  ASP A CA    1 
ATOM   497   C  C     A ASP A 1 33  ? -23.769 -24.143 27.691  0.20 42.44  ? 33  ASP A C     1 
ATOM   498   C  C     B ASP A 1 33  ? -23.608 -24.184 27.526  0.80 42.40  ? 33  ASP A C     1 
ATOM   499   O  O     A ASP A 1 33  ? -24.595 -23.799 26.838  0.20 43.81  ? 33  ASP A O     1 
ATOM   500   O  O     B ASP A 1 33  ? -24.465 -23.875 26.691  0.80 44.20  ? 33  ASP A O     1 
ATOM   501   C  CB    A ASP A 1 33  ? -23.958 -26.607 27.294  0.20 45.31  ? 33  ASP A CB    1 
ATOM   502   C  CB    B ASP A 1 33  ? -23.754 -26.640 27.082  0.80 44.68  ? 33  ASP A CB    1 
ATOM   503   C  CG    A ASP A 1 33  ? -24.746 -26.933 28.551  0.20 47.98  ? 33  ASP A CG    1 
ATOM   504   C  CG    B ASP A 1 33  ? -24.677 -26.915 28.260  0.80 48.37  ? 33  ASP A CG    1 
ATOM   505   O  OD1   A ASP A 1 33  ? -24.526 -26.274 29.587  0.20 45.77  ? 33  ASP A OD1   1 
ATOM   506   O  OD1   B ASP A 1 33  ? -24.434 -26.388 29.367  0.80 46.09  ? 33  ASP A OD1   1 
ATOM   507   O  OD2   A ASP A 1 33  ? -25.589 -27.855 28.503  0.20 54.12  ? 33  ASP A OD2   1 
ATOM   508   O  OD2   B ASP A 1 33  ? -25.654 -27.673 28.080  0.80 58.08  ? 33  ASP A OD2   1 
ATOM   509   N  N     A GLY A 1 34  ? -23.534 -23.426 28.789  0.20 41.04  ? 34  GLY A N     1 
ATOM   510   N  N     B GLY A 1 34  ? -23.352 -23.438 28.601  0.80 40.86  ? 34  GLY A N     1 
ATOM   511   C  CA    A GLY A 1 34  ? -24.190 -22.162 29.045  0.20 37.93  ? 34  GLY A CA    1 
ATOM   512   C  CA    B GLY A 1 34  ? -24.071 -22.214 28.884  0.80 37.51  ? 34  GLY A CA    1 
ATOM   513   C  C     A GLY A 1 34  ? -25.394 -22.221 29.961  0.20 34.88  ? 34  GLY A C     1 
ATOM   514   C  C     B GLY A 1 34  ? -25.285 -22.363 29.777  0.80 34.06  ? 34  GLY A C     1 
ATOM   515   O  O     A GLY A 1 34  ? -25.990 -21.173 30.234  0.20 35.11  ? 34  GLY A O     1 
ATOM   516   O  O     B GLY A 1 34  ? -25.896 -21.351 30.129  0.80 33.74  ? 34  GLY A O     1 
ATOM   517   N  N     A GLN A 1 35  ? -25.770 -23.401 30.445  0.20 39.10  ? 35  GLN A N     1 
ATOM   518   N  N     B GLN A 1 35  ? -25.661 -23.581 30.148  0.80 37.09  ? 35  GLN A N     1 
ATOM   519   C  CA    A GLN A 1 35  ? -26.942 -23.526 31.299  0.20 42.06  ? 35  GLN A CA    1 
ATOM   520   C  CA    B GLN A 1 35  ? -26.839 -23.776 30.985  0.80 43.67  ? 35  GLN A CA    1 
ATOM   521   C  C     A GLN A 1 35  ? -26.610 -23.146 32.738  0.20 42.59  ? 35  GLN A C     1 
ATOM   522   C  C     B GLN A 1 35  ? -26.529 -23.437 32.435  0.80 44.51  ? 35  GLN A C     1 
ATOM   523   O  O     A GLN A 1 35  ? -25.506 -23.393 33.231  0.20 40.79  ? 35  GLN A O     1 
ATOM   524   O  O     B GLN A 1 35  ? -25.437 -23.726 32.932  0.80 39.33  ? 35  GLN A O     1 
ATOM   525   C  CB    A GLN A 1 35  ? -27.493 -24.952 31.250  0.20 43.77  ? 35  GLN A CB    1 
ATOM   526   C  CB    B GLN A 1 35  ? -27.348 -25.213 30.874  0.80 42.75  ? 35  GLN A CB    1 
ATOM   527   C  CG    A GLN A 1 35  ? -28.132 -25.330 29.922  0.20 46.10  ? 35  GLN A CG    1 
ATOM   528   C  CG    B GLN A 1 35  ? -28.145 -25.469 29.606  0.80 47.14  ? 35  GLN A CG    1 
ATOM   529   C  CD    A GLN A 1 35  ? -29.441 -24.601 29.669  0.20 46.06  ? 35  GLN A CD    1 
ATOM   530   C  CD    B GLN A 1 35  ? -29.288 -24.481 29.435  0.80 46.65  ? 35  GLN A CD    1 
ATOM   531   O  OE1   A GLN A 1 35  ? -30.061 -24.068 30.593  0.20 44.48  ? 35  GLN A OE1   1 
ATOM   532   O  OE1   B GLN A 1 35  ? -30.115 -24.299 30.337  0.80 45.92  ? 35  GLN A OE1   1 
ATOM   533   N  NE2   A GLN A 1 35  ? -29.869 -24.576 28.412  0.20 43.71  ? 35  GLN A NE2   1 
ATOM   534   N  NE2   B GLN A 1 35  ? -29.328 -23.822 28.283  0.80 41.33  ? 35  GLN A NE2   1 
ATOM   535   N  N     A MET A 1 36  ? -27.588 -22.540 33.412  0.20 38.98  ? 36  MET A N     1 
ATOM   536   N  N     B MET A 1 36  ? -27.510 -22.836 33.113  0.80 39.46  ? 36  MET A N     1 
ATOM   537   C  CA    A MET A 1 36  ? -27.438 -22.113 34.802  0.20 39.00  ? 36  MET A CA    1 
ATOM   538   C  CA    B MET A 1 36  ? -27.352 -22.362 34.487  0.80 35.38  ? 36  MET A CA    1 
ATOM   539   C  C     A MET A 1 36  ? -28.701 -22.493 35.560  0.20 43.25  ? 36  MET A C     1 
ATOM   540   C  C     B MET A 1 36  ? -28.587 -22.739 35.292  0.80 42.80  ? 36  MET A C     1 
ATOM   541   O  O     A MET A 1 36  ? -29.682 -21.738 35.581  0.20 45.22  ? 36  MET A O     1 
ATOM   542   O  O     B MET A 1 36  ? -29.540 -21.954 35.395  0.80 45.47  ? 36  MET A O     1 
ATOM   543   C  CB    A MET A 1 36  ? -27.171 -20.610 34.899  0.20 38.69  ? 36  MET A CB    1 
ATOM   544   C  CB    B MET A 1 36  ? -27.121 -20.851 34.530  0.80 37.68  ? 36  MET A CB    1 
ATOM   545   C  CG    A MET A 1 36  ? -26.978 -20.094 36.316  0.20 37.34  ? 36  MET A CG    1 
ATOM   546   C  CG    B MET A 1 36  ? -26.972 -20.257 35.930  0.80 34.18  ? 36  MET A CG    1 
ATOM   547   S  SD    A MET A 1 36  ? -26.758 -18.303 36.380  0.20 42.41  ? 36  MET A SD    1 
ATOM   548   S  SD    B MET A 1 36  ? -26.528 -18.503 35.880  0.80 45.43  ? 36  MET A SD    1 
ATOM   549   C  CE    A MET A 1 36  ? -26.464 -18.061 38.130  0.20 42.06  ? 36  MET A CE    1 
ATOM   550   C  CE    B MET A 1 36  ? -26.567 -18.092 37.624  0.80 43.43  ? 36  MET A CE    1 
ATOM   551   N  N     A PRO A 1 37  ? -28.712 -23.667 36.201  0.20 47.17  ? 37  PRO A N     1 
ATOM   552   N  N     B PRO A 1 37  ? -28.596 -23.931 35.898  0.80 47.64  ? 37  PRO A N     1 
ATOM   553   C  CA    A PRO A 1 37  ? -29.951 -24.140 36.847  0.20 46.09  ? 37  PRO A CA    1 
ATOM   554   C  CA    B PRO A 1 37  ? -29.807 -24.400 36.603  0.80 46.60  ? 37  PRO A CA    1 
ATOM   555   C  C     A PRO A 1 37  ? -30.447 -23.242 37.967  0.20 49.29  ? 37  PRO A C     1 
ATOM   556   C  C     B PRO A 1 37  ? -30.301 -23.468 37.699  0.80 47.86  ? 37  PRO A C     1 
ATOM   557   O  O     A PRO A 1 37  ? -31.651 -23.238 38.256  0.20 52.10  ? 37  PRO A O     1 
ATOM   558   O  O     B PRO A 1 37  ? -31.483 -23.542 38.063  0.80 54.91  ? 37  PRO A O     1 
ATOM   559   C  CB    A PRO A 1 37  ? -29.560 -25.529 37.374  0.20 47.83  ? 37  PRO A CB    1 
ATOM   560   C  CB    B PRO A 1 37  ? -29.370 -25.752 37.188  0.80 47.85  ? 37  PRO A CB    1 
ATOM   561   C  CG    A PRO A 1 37  ? -28.379 -25.938 36.553  0.20 46.76  ? 37  PRO A CG    1 
ATOM   562   C  CG    B PRO A 1 37  ? -28.216 -26.186 36.352  0.80 46.93  ? 37  PRO A CG    1 
ATOM   563   C  CD    A PRO A 1 37  ? -27.636 -24.669 36.263  0.20 44.90  ? 37  PRO A CD    1 
ATOM   564   C  CD    B PRO A 1 37  ? -27.513 -24.931 35.923  0.80 44.41  ? 37  PRO A CD    1 
ATOM   565   N  N     A SER A 1 38  ? -29.560 -22.485 38.614  0.20 50.61  ? 38  SER A N     1 
ATOM   566   N  N     B SER A 1 38  ? -29.442 -22.602 38.242  0.80 53.44  ? 38  SER A N     1 
ATOM   567   C  CA    A SER A 1 38  ? -29.968 -21.593 39.691  0.20 49.94  ? 38  SER A CA    1 
ATOM   568   C  CA    B SER A 1 38  ? -29.805 -21.739 39.360  0.80 50.21  ? 38  SER A CA    1 
ATOM   569   C  C     A SER A 1 38  ? -30.643 -20.323 39.188  0.20 51.14  ? 38  SER A C     1 
ATOM   570   C  C     B SER A 1 38  ? -30.521 -20.466 38.929  0.80 52.32  ? 38  SER A C     1 
ATOM   571   O  O     A SER A 1 38  ? -31.256 -19.610 39.989  0.20 50.80  ? 38  SER A O     1 
ATOM   572   O  O     B SER A 1 38  ? -31.083 -19.775 39.786  0.80 50.13  ? 38  SER A O     1 
ATOM   573   C  CB    A SER A 1 38  ? -28.760 -21.222 40.554  0.20 51.56  ? 38  SER A CB    1 
ATOM   574   C  CB    B SER A 1 38  ? -28.556 -21.364 40.164  0.80 52.24  ? 38  SER A CB    1 
ATOM   575   O  OG    A SER A 1 38  ? -27.770 -20.557 39.788  0.20 49.21  ? 38  SER A OG    1 
ATOM   576   O  OG    B SER A 1 38  ? -27.719 -20.485 39.425  0.80 49.09  ? 38  SER A OG    1 
ATOM   577   N  N     A ASP A 1 39  ? -30.548 -20.024 37.894  0.20 45.95  ? 39  ASP A N     1 
ATOM   578   N  N     B ASP A 1 39  ? -30.504 -20.131 37.640  0.80 44.58  ? 39  ASP A N     1 
ATOM   579   C  CA    A ASP A 1 39  ? -31.171 -18.832 37.330  0.20 48.79  ? 39  ASP A CA    1 
ATOM   580   C  CA    B ASP A 1 39  ? -31.162 -18.927 37.145  0.80 48.64  ? 39  ASP A CA    1 
ATOM   581   C  C     A ASP A 1 39  ? -32.645 -19.122 37.072  0.20 50.83  ? 39  ASP A C     1 
ATOM   582   C  C     B ASP A 1 39  ? -32.651 -19.207 36.979  0.80 50.72  ? 39  ASP A C     1 
ATOM   583   O  O     A ASP A 1 39  ? -32.983 -19.952 36.221  0.20 53.19  ? 39  ASP A O     1 
ATOM   584   O  O     B ASP A 1 39  ? -33.061 -19.897 36.040  0.80 53.51  ? 39  ASP A O     1 
ATOM   585   C  CB    A ASP A 1 39  ? -30.457 -18.412 36.048  0.20 46.51  ? 39  ASP A CB    1 
ATOM   586   C  CB    B ASP A 1 39  ? -30.536 -18.477 35.828  0.80 45.25  ? 39  ASP A CB    1 
ATOM   587   C  CG    A ASP A 1 39  ? -30.872 -17.031 35.574  0.20 53.56  ? 39  ASP A CG    1 
ATOM   588   C  CG    B ASP A 1 39  ? -31.050 -17.120 35.368  0.80 55.16  ? 39  ASP A CG    1 
ATOM   589   O  OD1   A ASP A 1 39  ? -31.634 -16.353 36.297  0.20 49.72  ? 39  ASP A OD1   1 
ATOM   590   O  OD1   B ASP A 1 39  ? -31.818 -16.479 36.123  0.80 48.40  ? 39  ASP A OD1   1 
ATOM   591   O  OD2   A ASP A 1 39  ? -30.434 -16.624 34.478  0.20 47.87  ? 39  ASP A OD2   1 
ATOM   592   O  OD2   B ASP A 1 39  ? -30.680 -16.689 34.253  0.80 46.56  ? 39  ASP A OD2   1 
ATOM   593   N  N     A LYS A 1 40  ? -33.525 -18.436 37.805  0.20 54.19  ? 40  LYS A N     1 
ATOM   594   N  N     B LYS A 1 40  ? -33.463 -18.659 37.887  0.80 54.94  ? 40  LYS A N     1 
ATOM   595   C  CA    A LYS A 1 40  ? -34.957 -18.675 37.668  0.20 57.47  ? 40  LYS A CA    1 
ATOM   596   C  CA    B LYS A 1 40  ? -34.906 -18.868 37.840  0.80 59.29  ? 40  LYS A CA    1 
ATOM   597   C  C     A LYS A 1 40  ? -35.564 -17.900 36.506  0.20 55.65  ? 40  LYS A C     1 
ATOM   598   C  C     B LYS A 1 40  ? -35.587 -18.043 36.755  0.80 57.54  ? 40  LYS A C     1 
ATOM   599   O  O     A LYS A 1 40  ? -36.512 -18.382 35.874  0.20 51.91  ? 40  LYS A O     1 
ATOM   600   O  O     B LYS A 1 40  ? -36.724 -18.357 36.379  0.80 51.44  ? 40  LYS A O     1 
ATOM   601   C  CB    A LYS A 1 40  ? -35.676 -18.314 38.969  0.20 53.22  ? 40  LYS A CB    1 
ATOM   602   C  CB    B LYS A 1 40  ? -35.527 -18.545 39.202  0.80 52.75  ? 40  LYS A CB    1 
ATOM   603   N  N     A THR A 1 41  ? -35.046 -16.710 36.211  0.20 51.31  ? 41  THR A N     1 
ATOM   604   N  N     B THR A 1 41  ? -34.930 -17.000 36.250  0.80 49.42  ? 41  THR A N     1 
ATOM   605   C  CA    A THR A 1 41  ? -35.564 -15.890 35.118  0.20 54.25  ? 41  THR A CA    1 
ATOM   606   C  CA    B THR A 1 41  ? -35.476 -16.170 35.181  0.80 54.25  ? 41  THR A CA    1 
ATOM   607   C  C     A THR A 1 41  ? -34.924 -16.354 33.817  0.20 55.12  ? 41  THR A C     1 
ATOM   608   C  C     B THR A 1 41  ? -34.851 -16.617 33.865  0.80 55.45  ? 41  THR A C     1 
ATOM   609   O  O     A THR A 1 41  ? -33.753 -16.074 33.549  0.20 55.90  ? 41  THR A O     1 
ATOM   610   O  O     B THR A 1 41  ? -33.661 -16.388 33.623  0.80 56.10  ? 41  THR A O     1 
ATOM   611   C  CB    A THR A 1 41  ? -35.292 -14.412 35.374  0.20 52.15  ? 41  THR A CB    1 
ATOM   612   C  CB    B THR A 1 41  ? -35.216 -14.687 35.439  0.80 51.55  ? 41  THR A CB    1 
ATOM   613   O  OG1   A THR A 1 41  ? -33.894 -14.215 35.617  0.20 43.90  ? 41  THR A OG1   1 
ATOM   614   O  OG1   B THR A 1 41  ? -33.818 -14.472 35.672  0.80 39.16  ? 41  THR A OG1   1 
ATOM   615   C  CG2   A THR A 1 41  ? -36.084 -13.926 36.579  0.20 51.76  ? 41  THR A CG2   1 
ATOM   616   C  CG2   B THR A 1 41  ? -36.008 -14.211 36.644  0.80 51.28  ? 41  THR A CG2   1 
ATOM   617   N  N     A ILE A 1 42  ? -35.695 -17.068 33.003  0.20 49.21  ? 42  ILE A N     1 
ATOM   618   N  N     B ILE A 1 42  ? -35.648 -17.246 33.023  0.80 48.11  ? 42  ILE A N     1 
ATOM   619   C  CA    A ILE A 1 42  ? -35.216 -17.584 31.726  0.20 48.64  ? 42  ILE A CA    1 
ATOM   620   C  CA    B ILE A 1 42  ? -35.176 -17.767 31.747  0.80 47.68  ? 42  ILE A CA    1 
ATOM   621   C  C     A ILE A 1 42  ? -35.423 -16.521 30.657  0.20 52.37  ? 42  ILE A C     1 
ATOM   622   C  C     B ILE A 1 42  ? -35.251 -16.667 30.699  0.80 53.04  ? 42  ILE A C     1 
ATOM   623   O  O     A ILE A 1 42  ? -36.502 -15.924 30.561  0.20 52.79  ? 42  ILE A O     1 
ATOM   624   O  O     B ILE A 1 42  ? -36.182 -15.852 30.699  0.80 52.64  ? 42  ILE A O     1 
ATOM   625   C  CB    A ILE A 1 42  ? -35.938 -18.889 31.353  0.20 54.40  ? 42  ILE A CB    1 
ATOM   626   C  CB    B ILE A 1 42  ? -35.997 -19.004 31.330  0.80 54.87  ? 42  ILE A CB    1 
ATOM   627   C  CG1   A ILE A 1 42  ? -35.706 -19.951 32.431  0.20 53.81  ? 42  ILE A CG1   1 
ATOM   628   C  CG1   B ILE A 1 42  ? -35.781 -20.142 32.340  0.80 54.35  ? 42  ILE A CG1   1 
ATOM   629   C  CG2   A ILE A 1 42  ? -35.472 -19.385 29.988  0.20 47.36  ? 42  ILE A CG2   1 
ATOM   630   C  CG2   B ILE A 1 42  ? -35.642 -19.442 29.906  0.80 46.82  ? 42  ILE A CG2   1 
ATOM   631   C  CD1   A ILE A 1 42  ? -36.408 -21.266 32.158  0.20 50.58  ? 42  ILE A CD1   1 
ATOM   632   C  CD1   B ILE A 1 42  ? -36.514 -21.433 32.002  0.80 50.07  ? 42  ILE A CD1   1 
ATOM   633   N  N     A GLY A 1 43  ? -34.387 -16.276 29.854  0.20 47.01  ? 43  GLY A N     1 
ATOM   634   N  N     B GLY A 1 43  ? -34.250 -16.624 29.818  0.80 44.73  ? 43  GLY A N     1 
ATOM   635   C  CA    A GLY A 1 43  ? -34.454 -15.297 28.792  0.20 49.31  ? 43  GLY A CA    1 
ATOM   636   C  CA    B GLY A 1 43  ? -34.272 -15.745 28.666  0.80 49.25  ? 43  GLY A CA    1 
ATOM   637   C  C     A GLY A 1 43  ? -34.205 -13.865 29.213  0.20 49.72  ? 43  GLY A C     1 
ATOM   638   C  C     B GLY A 1 43  ? -34.027 -14.283 28.957  0.80 49.60  ? 43  GLY A C     1 
ATOM   639   O  O     A GLY A 1 43  ? -33.909 -13.024 28.353  0.20 51.73  ? 43  GLY A O     1 
ATOM   640   O  O     B GLY A 1 43  ? -34.132 -13.456 28.041  0.80 54.48  ? 43  GLY A O     1 
ATOM   641   N  N     A GLY A 1 44  ? -34.329 -13.552 30.501  0.20 53.03  ? 44  GLY A N     1 
ATOM   642   N  N     B GLY A 1 44  ? -33.690 -13.940 30.190  0.80 49.81  ? 44  GLY A N     1 
ATOM   643   C  CA    A GLY A 1 44  ? -34.080 -12.214 30.996  0.20 51.72  ? 44  GLY A CA    1 
ATOM   644   C  CA    B GLY A 1 44  ? -33.562 -12.550 30.567  0.80 45.81  ? 44  GLY A CA    1 
ATOM   645   C  C     A GLY A 1 44  ? -33.427 -12.225 32.362  0.20 53.57  ? 44  GLY A C     1 
ATOM   646   C  C     B GLY A 1 44  ? -33.162 -12.469 32.023  0.80 51.87  ? 44  GLY A C     1 
ATOM   647   O  O     A GLY A 1 44  ? -33.034 -13.285 32.860  0.20 52.94  ? 44  GLY A O     1 
ATOM   648   O  O     B GLY A 1 44  ? -33.093 -13.479 32.731  0.80 52.18  ? 44  GLY A O     1 
ATOM   649   N  N     A GLY A 1 45  ? -33.295 -11.063 32.970  0.20 55.12  ? 45  GLY A N     1 
ATOM   650   N  N     B GLY A 1 45  ? -32.871 -11.253 32.457  0.80 51.08  ? 45  GLY A N     1 
ATOM   651   C  CA    A GLY A 1 45  ? -32.720 -10.955 34.296  0.20 52.24  ? 45  GLY A CA    1 
ATOM   652   C  CA    B GLY A 1 45  ? -32.621 -11.033 33.867  0.80 53.86  ? 45  GLY A CA    1 
ATOM   653   C  C     A GLY A 1 45  ? -31.951 -9.660  34.462  0.20 48.83  ? 45  GLY A C     1 
ATOM   654   C  C     B GLY A 1 45  ? -31.835 -9.773  34.123  0.80 49.86  ? 45  GLY A C     1 
ATOM   655   O  O     A GLY A 1 45  ? -31.383 -9.101  33.528  0.20 50.46  ? 45  GLY A O     1 
ATOM   656   O  O     B GLY A 1 45  ? -31.165 -9.223  33.247  0.80 50.97  ? 45  GLY A O     1 
ATOM   657   N  N     A ASP A 1 46  ? -31.928 -9.170  35.697  0.20 47.16  ? 46  ASP A N     1 
ATOM   658   N  N     B ASP A 1 46  ? -31.918 -9.317  35.373  0.80 45.87  ? 46  ASP A N     1 
ATOM   659   C  CA    A ASP A 1 46  ? -31.207 -7.961  36.071  0.20 47.22  ? 46  ASP A CA    1 
ATOM   660   C  CA    B ASP A 1 46  ? -31.177 -8.158  35.856  0.80 46.46  ? 46  ASP A CA    1 
ATOM   661   C  C     A ASP A 1 46  ? -30.373 -8.215  37.318  0.20 46.00  ? 46  ASP A C     1 
ATOM   662   C  C     B ASP A 1 46  ? -30.252 -8.522  37.013  0.80 45.74  ? 46  ASP A C     1 
ATOM   663   O  O     A ASP A 1 46  ? -30.285 -7.375  38.218  0.20 47.78  ? 46  ASP A O     1 
ATOM   664   O  O     B ASP A 1 46  ? -29.889 -7.650  37.807  0.80 50.43  ? 46  ASP A O     1 
ATOM   665   C  CB    A ASP A 1 46  ? -32.173 -6.796  36.282  0.20 55.25  ? 46  ASP A CB    1 
ATOM   666   C  CB    B ASP A 1 46  ? -32.139 -7.048  36.286  0.80 56.31  ? 46  ASP A CB    1 
ATOM   667   C  CG    A ASP A 1 46  ? -31.467 -5.451  36.338  0.20 51.46  ? 46  ASP A CG    1 
ATOM   668   C  CG    B ASP A 1 46  ? -32.541 -6.143  35.140  0.80 60.16  ? 46  ASP A CG    1 
ATOM   669   O  OD1   A ASP A 1 46  ? -31.008 -4.969  35.280  0.20 53.87  ? 46  ASP A OD1   1 
ATOM   670   O  OD1   B ASP A 1 46  ? -31.656 -5.459  34.579  0.80 62.50  ? 46  ASP A OD1   1 
ATOM   671   O  OD2   A ASP A 1 46  ? -31.372 -4.874  37.441  0.20 49.37  ? 46  ASP A OD2   1 
ATOM   672   O  OD2   B ASP A 1 46  ? -33.743 -6.117  34.800  0.80 62.99  ? 46  ASP A OD2   1 
ATOM   673   N  N     A ASP A 1 47  ? -29.746 -9.386  37.388  0.20 40.38  ? 47  ASP A N     1 
ATOM   674   N  N     B ASP A 1 47  ? -29.874 -9.791  37.137  0.80 36.00  ? 47  ASP A N     1 
ATOM   675   C  CA    A ASP A 1 47  ? -28.963 -9.772  38.550  0.20 40.36  ? 47  ASP A CA    1 
ATOM   676   C  CA    B ASP A 1 47  ? -29.016 -10.198 38.240  0.80 42.18  ? 47  ASP A CA    1 
ATOM   677   C  C     A ASP A 1 47  ? -27.515 -9.314  38.376  0.20 40.09  ? 47  ASP A C     1 
ATOM   678   C  C     B ASP A 1 47  ? -27.587 -9.716  38.012  0.80 42.57  ? 47  ASP A C     1 
ATOM   679   O  O     A ASP A 1 47  ? -27.163 -8.627  37.413  0.20 40.58  ? 47  ASP A O     1 
ATOM   680   O  O     B ASP A 1 47  ? -27.168 -9.424  36.887  0.80 35.97  ? 47  ASP A O     1 
ATOM   681   C  CB    A ASP A 1 47  ? -29.052 -11.280 38.773  0.20 37.94  ? 47  ASP A CB    1 
ATOM   682   C  CB    B ASP A 1 47  ? -29.007 -11.713 38.399  0.80 36.41  ? 47  ASP A CB    1 
ATOM   683   C  CG    A ASP A 1 47  ? -30.479 -11.769 38.892  0.20 41.95  ? 47  ASP A CG    1 
ATOM   684   C  CG    B ASP A 1 47  ? -30.327 -12.263 38.849  0.80 42.60  ? 47  ASP A CG    1 
ATOM   685   O  OD1   A ASP A 1 47  ? -31.329 -11.006 39.394  0.20 44.90  ? 47  ASP A OD1   1 
ATOM   686   O  OD1   B ASP A 1 47  ? -30.664 -12.086 40.033  0.80 40.05  ? 47  ASP A OD1   1 
ATOM   687   O  OD2   A ASP A 1 47  ? -30.750 -12.919 38.484  0.20 39.63  ? 47  ASP A OD2   1 
ATOM   688   O  OD2   B ASP A 1 47  ? -31.023 -12.875 38.018  0.80 35.89  ? 47  ASP A OD2   1 
ATOM   689   N  N     A SER A 1 48  ? -26.652 -9.707  39.315  0.20 38.91  ? 48  SER A N     1 
ATOM   690   N  N     B SER A 1 48  ? -26.824 -9.671  39.107  0.80 39.35  ? 48  SER A N     1 
ATOM   691   C  CA    A SER A 1 48  ? -25.259 -9.279  39.261  0.20 36.07  ? 48  SER A CA    1 
ATOM   692   C  CA    B SER A 1 48  ? -25.486 -9.096  39.047  0.80 35.18  ? 48  SER A CA    1 
ATOM   693   C  C     A SER A 1 48  ? -24.497 -9.994  38.150  0.20 35.16  ? 48  SER A C     1 
ATOM   694   C  C     B SER A 1 48  ? -24.594 -9.814  38.035  0.80 35.32  ? 48  SER A C     1 
ATOM   695   O  O     A SER A 1 48  ? -23.718 -9.366  37.426  0.20 32.03  ? 48  SER A O     1 
ATOM   696   O  O     B SER A 1 48  ? -23.759 -9.171  37.400  0.80 31.31  ? 48  SER A O     1 
ATOM   697   C  CB    A SER A 1 48  ? -24.583 -9.518  40.611  0.20 37.18  ? 48  SER A CB    1 
ATOM   698   C  CB    B SER A 1 48  ? -24.843 -9.114  40.436  0.80 37.72  ? 48  SER A CB    1 
ATOM   699   O  OG    A SER A 1 48  ? -24.543 -10.901 40.927  0.20 37.82  ? 48  SER A OG    1 
ATOM   700   O  OG    B SER A 1 48  ? -24.817 -10.426 40.974  0.80 44.49  ? 48  SER A OG    1 
ATOM   701   N  N     A PHE A 1 49  ? -24.704 -11.305 38.002  0.20 32.63  ? 49  PHE A N     1 
ATOM   702   N  N     B PHE A 1 49  ? -24.746 -11.132 37.870  0.80 31.39  ? 49  PHE A N     1 
ATOM   703   C  CA    A PHE A 1 49  ? -23.945 -12.074 37.021  0.20 35.46  ? 49  PHE A CA    1 
ATOM   704   C  CA    B PHE A 1 49  ? -23.893 -11.851 36.926  0.80 35.47  ? 49  PHE A CA    1 
ATOM   705   C  C     A PHE A 1 49  ? -24.276 -11.686 35.586  0.20 34.87  ? 49  PHE A C     1 
ATOM   706   C  C     B PHE A 1 49  ? -24.185 -11.477 35.480  0.80 35.40  ? 49  PHE A C     1 
ATOM   707   O  O     A PHE A 1 49  ? -23.481 -11.970 34.683  0.20 32.20  ? 49  PHE A O     1 
ATOM   708   O  O     B PHE A 1 49  ? -23.354 -11.744 34.600  0.80 31.06  ? 49  PHE A O     1 
ATOM   709   C  CB    A PHE A 1 49  ? -24.181 -13.574 37.222  0.20 36.31  ? 49  PHE A CB    1 
ATOM   710   C  CB    B PHE A 1 49  ? -24.034 -13.366 37.108  0.80 36.23  ? 49  PHE A CB    1 
ATOM   711   C  CG    A PHE A 1 49  ? -25.603 -14.009 36.990  0.20 40.53  ? 49  PHE A CG    1 
ATOM   712   C  CG    B PHE A 1 49  ? -25.443 -13.893 36.942  0.80 41.31  ? 49  PHE A CG    1 
ATOM   713   C  CD1   A PHE A 1 49  ? -26.538 -13.948 38.011  0.20 39.36  ? 49  PHE A CD1   1 
ATOM   714   C  CD1   B PHE A 1 49  ? -25.922 -14.258 35.696  0.80 39.08  ? 49  PHE A CD1   1 
ATOM   715   C  CD2   A PHE A 1 49  ? -25.999 -14.496 35.755  0.20 39.08  ? 49  PHE A CD2   1 
ATOM   716   C  CD2   B PHE A 1 49  ? -26.272 -14.061 38.039  0.80 39.26  ? 49  PHE A CD2   1 
ATOM   717   C  CE1   A PHE A 1 49  ? -27.842 -14.359 37.801  0.20 40.29  ? 49  PHE A CE1   1 
ATOM   718   C  CE1   B PHE A 1 49  ? -27.200 -14.766 35.548  0.80 41.08  ? 49  PHE A CE1   1 
ATOM   719   C  CE2   A PHE A 1 49  ? -27.301 -14.904 35.540  0.20 41.34  ? 49  PHE A CE2   1 
ATOM   720   C  CE2   B PHE A 1 49  ? -27.549 -14.581 37.901  0.80 39.88  ? 49  PHE A CE2   1 
ATOM   721   C  CZ    A PHE A 1 49  ? -28.225 -14.834 36.564  0.20 44.39  ? 49  PHE A CZ    1 
ATOM   722   C  CZ    B PHE A 1 49  ? -28.020 -14.920 36.654  0.80 45.05  ? 49  PHE A CZ    1 
ATOM   723   N  N     A ASN A 1 50  ? -25.426 -11.048 35.355  0.20 36.21  ? 50  ASN A N     1 
ATOM   724   N  N     B ASN A 1 50  ? -25.342 -10.861 35.217  0.80 36.70  ? 50  ASN A N     1 
ATOM   725   C  CA    A ASN A 1 50  ? -25.765 -10.564 34.022  0.20 34.78  ? 50  ASN A CA    1 
ATOM   726   C  CA    B ASN A 1 50  ? -25.676 -10.397 33.878  0.80 35.22  ? 50  ASN A CA    1 
ATOM   727   C  C     A ASN A 1 50  ? -24.827 -9.467  33.538  0.20 32.81  ? 50  ASN A C     1 
ATOM   728   C  C     B ASN A 1 50  ? -24.798 -9.244  33.409  0.80 32.85  ? 50  ASN A C     1 
ATOM   729   O  O     A ASN A 1 50  ? -24.832 -9.159  32.341  0.20 30.89  ? 50  ASN A O     1 
ATOM   730   O  O     B ASN A 1 50  ? -24.895 -8.862  32.237  0.80 30.65  ? 50  ASN A O     1 
ATOM   731   C  CB    A ASN A 1 50  ? -27.207 -10.055 33.993  0.20 32.94  ? 50  ASN A CB    1 
ATOM   732   C  CB    B ASN A 1 50  ? -27.148 -9.977  33.808  0.80 31.60  ? 50  ASN A CB    1 
ATOM   733   C  CG    A ASN A 1 50  ? -28.222 -11.180 34.000  0.20 39.67  ? 50  ASN A CG    1 
ATOM   734   C  CG    B ASN A 1 50  ? -28.097 -11.158 33.849  0.80 39.91  ? 50  ASN A CG    1 
ATOM   735   O  OD1   A ASN A 1 50  ? -29.071 -11.261 34.888  0.20 41.58  ? 50  ASN A OD1   1 
ATOM   736   O  OD1   B ASN A 1 50  ? -28.936 -11.262 34.745  0.80 41.41  ? 50  ASN A OD1   1 
ATOM   737   N  ND2   A ASN A 1 50  ? -28.141 -12.057 33.004  0.20 34.04  ? 50  ASN A ND2   1 
ATOM   738   N  ND2   B ASN A 1 50  ? -27.980 -12.051 32.870  0.80 32.37  ? 50  ASN A ND2   1 
ATOM   739   N  N     A THR A 1 51  ? -24.032 -8.870  34.430  0.20 33.06  ? 51  THR A N     1 
ATOM   740   N  N     B THR A 1 51  ? -23.958 -8.671  34.280  0.80 33.40  ? 51  THR A N     1 
ATOM   741   C  CA    A THR A 1 51  ? -23.051 -7.882  33.995  0.20 29.30  ? 51  THR A CA    1 
ATOM   742   C  CA    B THR A 1 51  ? -22.992 -7.697  33.789  0.80 28.16  ? 51  THR A CA    1 
ATOM   743   C  C     A THR A 1 51  ? -22.002 -8.506  33.085  0.20 26.92  ? 51  THR A C     1 
ATOM   744   C  C     B THR A 1 51  ? -22.012 -8.358  32.835  0.80 24.92  ? 51  THR A C     1 
ATOM   745   O  O     A THR A 1 51  ? -21.460 -7.825  32.207  0.20 28.97  ? 51  THR A O     1 
ATOM   746   O  O     B THR A 1 51  ? -21.505 -7.702  31.922  0.80 29.12  ? 51  THR A O     1 
ATOM   747   C  CB    A THR A 1 51  ? -22.386 -7.231  35.208  0.20 33.19  ? 51  THR A CB    1 
ATOM   748   C  CB    B THR A 1 51  ? -22.233 -7.034  34.944  0.80 33.89  ? 51  THR A CB    1 
ATOM   749   O  OG1   A THR A 1 51  ? -21.960 -8.247  36.125  0.20 31.67  ? 51  THR A OG1   1 
ATOM   750   O  OG1   B THR A 1 51  ? -21.379 -7.993  35.574  0.80 37.93  ? 51  THR A OG1   1 
ATOM   751   C  CG2   A THR A 1 51  ? -23.359 -6.299  35.913  0.20 29.00  ? 51  THR A CG2   1 
ATOM   752   C  CG2   B THR A 1 51  ? -23.207 -6.478  35.976  0.80 27.49  ? 51  THR A CG2   1 
ATOM   753   N  N     A PHE A 1 52  ? -21.720 -9.797  33.265  0.20 26.95  ? 52  PHE A N     1 
ATOM   754   N  N     B PHE A 1 52  ? -21.774 -9.662  33.015  0.80 25.56  ? 52  PHE A N     1 
ATOM   755   C  CA    A PHE A 1 52  ? -20.731 -10.509 32.469  0.20 29.10  ? 52  PHE A CA    1 
ATOM   756   C  CA    B PHE A 1 52  ? -20.801 -10.422 32.239  0.80 28.41  ? 52  PHE A CA    1 
ATOM   757   C  C     A PHE A 1 52  ? -21.332 -11.570 31.559  0.20 31.02  ? 52  PHE A C     1 
ATOM   758   C  C     B PHE A 1 52  ? -21.425 -11.452 31.305  0.80 32.55  ? 52  PHE A C     1 
ATOM   759   O  O     A PHE A 1 52  ? -20.596 -12.160 30.758  0.20 29.91  ? 52  PHE A O     1 
ATOM   760   O  O     B PHE A 1 52  ? -20.754 -11.876 30.352  0.80 28.92  ? 52  PHE A O     1 
ATOM   761   C  CB    A PHE A 1 52  ? -19.686 -11.168 33.387  0.20 28.61  ? 52  PHE A CB    1 
ATOM   762   C  CB    B PHE A 1 52  ? -19.803 -11.128 33.185  0.80 28.54  ? 52  PHE A CB    1 
ATOM   763   C  CG    A PHE A 1 52  ? -18.620 -10.225 33.877  0.20 31.02  ? 52  PHE A CG    1 
ATOM   764   C  CG    B PHE A 1 52  ? -18.656 -10.243 33.643  0.80 31.60  ? 52  PHE A CG    1 
ATOM   765   C  CD1   A PHE A 1 52  ? -18.950 -9.104  34.619  0.20 31.75  ? 52  PHE A CD1   1 
ATOM   766   C  CD1   B PHE A 1 52  ? -18.890 -8.966  34.129  0.80 32.67  ? 52  PHE A CD1   1 
ATOM   767   C  CD2   A PHE A 1 52  ? -17.283 -10.468 33.601  0.20 32.77  ? 52  PHE A CD2   1 
ATOM   768   C  CD2   B PHE A 1 52  ? -17.341 -10.688 33.570  0.80 33.62  ? 52  PHE A CD2   1 
ATOM   769   C  CE1   A PHE A 1 52  ? -17.970 -8.239  35.072  0.20 32.06  ? 52  PHE A CE1   1 
ATOM   770   C  CE1   B PHE A 1 52  ? -17.841 -8.148  34.531  0.80 29.75  ? 52  PHE A CE1   1 
ATOM   771   C  CE2   A PHE A 1 52  ? -16.297 -9.606  34.050  0.20 32.68  ? 52  PHE A CE2   1 
ATOM   772   C  CE2   B PHE A 1 52  ? -16.283 -9.874  33.973  0.80 33.42  ? 52  PHE A CE2   1 
ATOM   773   C  CZ    A PHE A 1 52  ? -16.641 -8.490  34.788  0.20 30.92  ? 52  PHE A CZ    1 
ATOM   774   C  CZ    B PHE A 1 52  ? -16.537 -8.603  34.460  0.80 31.32  ? 52  PHE A CZ    1 
ATOM   775   N  N     A PHE A 1 53  ? -22.636 -11.829 31.650  0.20 29.17  ? 53  PHE A N     1 
ATOM   776   N  N     B PHE A 1 53  ? -22.687 -11.847 31.526  0.80 29.01  ? 53  PHE A N     1 
ATOM   777   C  CA    A PHE A 1 53  ? -23.265 -12.900 30.884  0.20 28.29  ? 53  PHE A CA    1 
ATOM   778   C  CA    B PHE A 1 53  ? -23.327 -12.904 30.743  0.80 27.83  ? 53  PHE A CA    1 
ATOM   779   C  C     A PHE A 1 53  ? -24.609 -12.430 30.352  0.20 31.75  ? 53  PHE A C     1 
ATOM   780   C  C     B PHE A 1 53  ? -24.693 -12.439 30.253  0.80 32.34  ? 53  PHE A C     1 
ATOM   781   O  O     A PHE A 1 53  ? -25.506 -12.098 31.133  0.20 29.81  ? 53  PHE A O     1 
ATOM   782   O  O     B PHE A 1 53  ? -25.549 -12.067 31.061  0.80 29.77  ? 53  PHE A O     1 
ATOM   783   C  CB    A PHE A 1 53  ? -23.452 -14.157 31.740  0.20 31.78  ? 53  PHE A CB    1 
ATOM   784   C  CB    B PHE A 1 53  ? -23.498 -14.190 31.560  0.80 32.07  ? 53  PHE A CB    1 
ATOM   785   C  CG    A PHE A 1 53  ? -22.170 -14.861 32.085  0.20 28.59  ? 53  PHE A CG    1 
ATOM   786   C  CG    B PHE A 1 53  ? -22.211 -14.846 31.987  0.80 28.53  ? 53  PHE A CG    1 
ATOM   787   C  CD1   A PHE A 1 53  ? -21.462 -14.525 33.228  0.20 25.78  ? 53  PHE A CD1   1 
ATOM   788   C  CD1   B PHE A 1 53  ? -21.545 -14.431 33.132  0.80 25.16  ? 53  PHE A CD1   1 
ATOM   789   C  CD2   A PHE A 1 53  ? -21.681 -15.870 31.272  0.20 33.06  ? 53  PHE A CD2   1 
ATOM   790   C  CD2   B PHE A 1 53  ? -21.690 -15.907 31.262  0.80 33.30  ? 53  PHE A CD2   1 
ATOM   791   C  CE1   A PHE A 1 53  ? -20.286 -15.178 33.550  0.20 32.57  ? 53  PHE A CE1   1 
ATOM   792   C  CE1   B PHE A 1 53  ? -20.376 -15.053 33.539  0.80 32.93  ? 53  PHE A CE1   1 
ATOM   793   C  CE2   A PHE A 1 53  ? -20.504 -16.527 31.586  0.20 31.88  ? 53  PHE A CE2   1 
ATOM   794   C  CE2   B PHE A 1 53  ? -20.511 -16.532 31.652  0.80 32.05  ? 53  PHE A CE2   1 
ATOM   795   C  CZ    A PHE A 1 53  ? -19.805 -16.181 32.727  0.20 30.55  ? 53  PHE A CZ    1 
ATOM   796   C  CZ    B PHE A 1 53  ? -19.852 -16.108 32.794  0.80 30.43  ? 53  PHE A CZ    1 
ATOM   797   N  N     A SER A 1 54  ? -24.749 -12.407 29.029  0.20 29.36  ? 54  SER A N     1 
ATOM   798   N  N     B SER A 1 54  ? -24.903 -12.482 28.935  0.80 29.22  ? 54  SER A N     1 
ATOM   799   C  CA    A SER A 1 54  ? -26.058 -12.247 28.418  0.20 29.31  ? 54  SER A CA    1 
ATOM   800   C  CA    B SER A 1 54  ? -26.231 -12.318 28.356  0.80 28.23  ? 54  SER A CA    1 
ATOM   801   C  C     A SER A 1 54  ? -26.819 -13.569 28.480  0.20 32.85  ? 54  SER A C     1 
ATOM   802   C  C     B SER A 1 54  ? -26.958 -13.657 28.313  0.80 33.48  ? 54  SER A C     1 
ATOM   803   O  O     A SER A 1 54  ? -26.257 -14.626 28.780  0.20 32.19  ? 54  SER A O     1 
ATOM   804   O  O     B SER A 1 54  ? -26.383 -14.712 28.593  0.80 32.35  ? 54  SER A O     1 
ATOM   805   C  CB    A SER A 1 54  ? -25.923 -11.773 26.973  0.20 31.36  ? 54  SER A CB    1 
ATOM   806   C  CB    B SER A 1 54  ? -26.138 -11.742 26.945  0.80 30.92  ? 54  SER A CB    1 
ATOM   807   O  OG    A SER A 1 54  ? -25.142 -12.684 26.219  0.20 32.52  ? 54  SER A OG    1 
ATOM   808   O  OG    B SER A 1 54  ? -25.539 -12.695 26.088  0.80 34.71  ? 54  SER A OG    1 
ATOM   809   N  N     A GLU A 1 55  ? -28.119 -13.506 28.195  0.20 35.32  ? 55  GLU A N     1 
ATOM   810   N  N     B GLU A 1 55  ? -28.247 -13.608 27.944  0.80 35.41  ? 55  GLU A N     1 
ATOM   811   C  CA    A GLU A 1 55  ? -28.980 -14.680 28.258  0.20 36.36  ? 55  GLU A CA    1 
ATOM   812   C  CA    B GLU A 1 55  ? -29.098 -14.791 27.871  0.80 36.22  ? 55  GLU A CA    1 
ATOM   813   C  C     A GLU A 1 55  ? -29.848 -14.757 27.012  0.20 37.75  ? 55  GLU A C     1 
ATOM   814   C  C     B GLU A 1 55  ? -29.866 -14.790 26.554  0.80 36.96  ? 55  GLU A C     1 
ATOM   815   O  O     A GLU A 1 55  ? -30.380 -13.743 26.551  0.20 39.26  ? 55  GLU A O     1 
ATOM   816   O  O     B GLU A 1 55  ? -30.334 -13.741 26.102  0.80 42.20  ? 55  GLU A O     1 
ATOM   817   C  CB    A GLU A 1 55  ? -29.867 -14.654 29.511  0.20 39.27  ? 55  GLU A CB    1 
ATOM   818   C  CB    B GLU A 1 55  ? -30.072 -14.841 29.066  0.80 39.66  ? 55  GLU A CB    1 
ATOM   819   C  CG    A GLU A 1 55  ? -29.093 -14.510 30.812  0.20 37.81  ? 55  GLU A CG    1 
ATOM   820   C  CG    B GLU A 1 55  ? -29.371 -14.666 30.410  0.80 36.23  ? 55  GLU A CG    1 
ATOM   821   C  CD    A GLU A 1 55  ? -29.961 -14.709 32.036  0.20 43.11  ? 55  GLU A CD    1 
ATOM   822   C  CD    B GLU A 1 55  ? -30.302 -14.770 31.596  0.80 44.03  ? 55  GLU A CD    1 
ATOM   823   O  OE1   A GLU A 1 55  ? -30.948 -15.468 31.947  0.20 42.68  ? 55  GLU A OE1   1 
ATOM   824   O  OE1   B GLU A 1 55  ? -31.387 -15.368 31.455  0.80 36.86  ? 55  GLU A OE1   1 
ATOM   825   O  OE2   A GLU A 1 55  ? -29.654 -14.104 33.086  0.20 40.10  ? 55  GLU A OE2   1 
ATOM   826   O  OE2   B GLU A 1 55  ? -29.936 -14.251 32.672  0.80 33.55  ? 55  GLU A OE2   1 
ATOM   827   N  N     A THR A 1 56  ? -29.988 -15.966 26.471  0.20 40.60  ? 56  THR A N     1 
ATOM   828   N  N     B THR A 1 56  ? -30.005 -15.974 25.946  0.80 40.96  ? 56  THR A N     1 
ATOM   829   C  CA    A THR A 1 56  ? -30.827 -16.214 25.311  0.20 43.75  ? 56  THR A CA    1 
ATOM   830   C  CA    B THR A 1 56  ? -30.531 -16.108 24.587  0.80 45.49  ? 56  THR A CA    1 
ATOM   831   C  C     A THR A 1 56  ? -32.170 -16.789 25.756  0.20 45.43  ? 56  THR A C     1 
ATOM   832   C  C     B THR A 1 56  ? -32.047 -16.298 24.522  0.80 53.45  ? 56  THR A C     1 
ATOM   833   O  O     A THR A 1 56  ? -32.418 -17.016 26.942  0.20 40.64  ? 56  THR A O     1 
ATOM   834   O  O     B THR A 1 56  ? -32.690 -15.802 23.588  0.80 53.11  ? 56  THR A O     1 
ATOM   835   C  CB    A THR A 1 56  ? -30.133 -17.159 24.327  0.20 41.40  ? 56  THR A CB    1 
ATOM   836   C  CB    B THR A 1 56  ? -29.866 -17.289 23.872  0.80 40.83  ? 56  THR A CB    1 
ATOM   837   O  OG1   A THR A 1 56  ? -30.164 -18.495 24.843  0.20 40.00  ? 56  THR A OG1   1 
ATOM   838   O  OG1   B THR A 1 56  ? -30.145 -18.498 24.589  0.80 39.35  ? 56  THR A OG1   1 
ATOM   839   C  CG2   A THR A 1 56  ? -28.686 -16.738 24.109  0.20 40.26  ? 56  THR A CG2   1 
ATOM   840   C  CG2   B THR A 1 56  ? -28.358 -17.090 23.769  0.80 38.18  ? 56  THR A CG2   1 
ATOM   841   N  N     A GLY A 1 57  ? -33.048 -17.035 24.779  0.20 47.26  ? 57  GLY A N     1 
ATOM   842   N  N     B GLY A 1 57  ? -32.634 -17.033 25.469  0.80 49.80  ? 57  GLY A N     1 
ATOM   843   C  CA    A GLY A 1 57  ? -34.382 -17.526 25.079  0.20 46.89  ? 57  GLY A CA    1 
ATOM   844   C  CA    B GLY A 1 57  ? -34.047 -17.382 25.442  0.80 47.40  ? 57  GLY A CA    1 
ATOM   845   C  C     A GLY A 1 57  ? -34.424 -18.955 25.579  0.20 48.37  ? 57  GLY A C     1 
ATOM   846   C  C     B GLY A 1 57  ? -34.294 -18.877 25.432  0.80 48.25  ? 57  GLY A C     1 
ATOM   847   O  O     A GLY A 1 57  ? -35.433 -19.364 26.165  0.20 51.89  ? 57  GLY A O     1 
ATOM   848   O  O     B GLY A 1 57  ? -35.342 -19.334 25.906  0.80 53.61  ? 57  GLY A O     1 
ATOM   849   N  N     A ALA A 1 58  ? -33.356 -19.721 25.363  0.20 47.57  ? 58  ALA A N     1 
ATOM   850   N  N     B ALA A 1 58  ? -33.350 -19.646 24.895  0.80 49.38  ? 58  ALA A N     1 
ATOM   851   C  CA    A ALA A 1 58  ? -33.273 -21.103 25.813  0.20 43.94  ? 58  ALA A CA    1 
ATOM   852   C  CA    B ALA A 1 58  ? -33.303 -21.088 25.075  0.80 42.69  ? 58  ALA A CA    1 
ATOM   853   C  C     A ALA A 1 58  ? -32.491 -21.249 27.115  0.20 41.65  ? 58  ALA A C     1 
ATOM   854   C  C     B ALA A 1 58  ? -32.568 -21.489 26.352  0.80 43.17  ? 58  ALA A C     1 
ATOM   855   O  O     A ALA A 1 58  ? -32.091 -22.363 27.469  0.20 38.30  ? 58  ALA A O     1 
ATOM   856   O  O     B ALA A 1 58  ? -32.354 -22.683 26.584  0.80 48.39  ? 58  ALA A O     1 
ATOM   857   C  CB    A ALA A 1 58  ? -32.651 -21.976 24.722  0.20 43.70  ? 58  ALA A CB    1 
ATOM   858   C  CB    B ALA A 1 58  ? -32.646 -21.747 23.860  0.80 44.97  ? 58  ALA A CB    1 
ATOM   859   N  N     A GLY A 1 59  ? -32.269 -20.150 27.833  0.20 42.65  ? 59  GLY A N     1 
ATOM   860   N  N     B GLY A 1 59  ? -32.174 -20.523 27.178  0.80 39.44  ? 59  GLY A N     1 
ATOM   861   C  CA    A GLY A 1 59  ? -31.533 -20.199 29.080  0.20 41.20  ? 59  GLY A CA    1 
ATOM   862   C  CA    B GLY A 1 59  ? -31.539 -20.805 28.449  0.80 45.29  ? 59  GLY A CA    1 
ATOM   863   C  C     A GLY A 1 59  ? -30.029 -20.252 28.939  0.20 37.96  ? 59  GLY A C     1 
ATOM   864   C  C     B GLY A 1 59  ? -30.029 -20.726 28.463  0.80 36.23  ? 59  GLY A C     1 
ATOM   865   O  O     A GLY A 1 59  ? -29.338 -20.496 29.935  0.20 38.00  ? 59  GLY A O     1 
ATOM   866   O  O     B GLY A 1 59  ? -29.415 -21.136 29.458  0.80 42.96  ? 59  GLY A O     1 
ATOM   867   N  N     A LYS A 1 60  ? -29.499 -20.032 27.739  0.20 36.40  ? 60  LYS A N     1 
ATOM   868   N  N     B LYS A 1 60  ? -29.414 -20.197 27.409  0.80 34.71  ? 60  LYS A N     1 
ATOM   869   C  CA    A LYS A 1 60  ? -28.060 -20.069 27.517  0.20 37.33  ? 60  LYS A CA    1 
ATOM   870   C  CA    B LYS A 1 60  ? -27.958 -20.142 27.283  0.80 37.16  ? 60  LYS A CA    1 
ATOM   871   C  C     A LYS A 1 60  ? -27.422 -18.778 28.018  0.20 36.19  ? 60  LYS A C     1 
ATOM   872   C  C     B LYS A 1 60  ? -27.421 -18.847 27.895  0.80 36.26  ? 60  LYS A C     1 
ATOM   873   O  O     A LYS A 1 60  ? -27.867 -17.680 27.669  0.20 37.60  ? 60  LYS A O     1 
ATOM   874   O  O     B LYS A 1 60  ? -27.951 -17.764 27.630  0.80 37.64  ? 60  LYS A O     1 
ATOM   875   C  CB    A LYS A 1 60  ? -27.769 -20.269 26.030  0.20 38.91  ? 60  LYS A CB    1 
ATOM   876   C  CB    B LYS A 1 60  ? -27.564 -20.235 25.804  0.80 39.19  ? 60  LYS A CB    1 
ATOM   877   C  CG    A LYS A 1 60  ? -26.320 -20.550 25.685  0.20 41.35  ? 60  LYS A CG    1 
ATOM   878   C  CG    B LYS A 1 60  ? -26.121 -20.633 25.514  0.80 42.70  ? 60  LYS A CG    1 
ATOM   879   C  CD    A LYS A 1 60  ? -26.156 -20.688 24.177  0.20 43.01  ? 60  LYS A CD    1 
ATOM   880   C  CD    B LYS A 1 60  ? -25.828 -20.475 24.015  0.80 43.29  ? 60  LYS A CD    1 
ATOM   881   C  CE    A LYS A 1 60  ? -24.725 -21.003 23.795  0.20 40.10  ? 60  LYS A CE    1 
ATOM   882   C  CE    B LYS A 1 60  ? -24.462 -20.984 23.657  0.80 40.54  ? 60  LYS A CE    1 
ATOM   883   N  NZ    A LYS A 1 60  ? -24.283 -22.307 24.357  0.20 43.50  ? 60  LYS A NZ    1 
ATOM   884   N  NZ    B LYS A 1 60  ? -24.329 -22.404 24.052  0.80 44.60  ? 60  LYS A NZ    1 
ATOM   885   N  N     A HIS A 1 61  ? -26.382 -18.910 28.839  0.20 29.73  ? 61  HIS A N     1 
ATOM   886   N  N     B HIS A 1 61  ? -26.377 -18.960 28.713  0.80 29.19  ? 61  HIS A N     1 
ATOM   887   C  CA    A HIS A 1 61  ? -25.675 -17.764 29.411  0.20 31.67  ? 61  HIS A CA    1 
ATOM   888   C  CA    B HIS A 1 61  ? -25.663 -17.808 29.250  0.80 31.70  ? 61  HIS A CA    1 
ATOM   889   C  C     A HIS A 1 61  ? -24.365 -17.589 28.649  0.20 31.16  ? 61  HIS A C     1 
ATOM   890   C  C     B HIS A 1 61  ? -24.342 -17.666 28.489  0.80 30.95  ? 61  HIS A C     1 
ATOM   891   O  O     A HIS A 1 61  ? -23.381 -18.284 28.913  0.20 32.67  ? 61  HIS A O     1 
ATOM   892   O  O     B HIS A 1 61  ? -23.556 -18.610 28.416  0.80 34.39  ? 61  HIS A O     1 
ATOM   893   C  CB    A HIS A 1 61  ? -25.440 -17.960 30.904  0.20 32.99  ? 61  HIS A CB    1 
ATOM   894   C  CB    B HIS A 1 61  ? -25.428 -17.956 30.751  0.80 32.85  ? 61  HIS A CB    1 
ATOM   895   C  CG    A HIS A 1 61  ? -26.703 -18.010 31.707  0.20 32.19  ? 61  HIS A CG    1 
ATOM   896   C  CG    B HIS A 1 61  ? -26.698 -18.006 31.550  0.80 31.61  ? 61  HIS A CG    1 
ATOM   897   N  ND1   A HIS A 1 61  ? -27.619 -19.033 31.588  0.20 38.36  ? 61  HIS A ND1   1 
ATOM   898   N  ND1   B HIS A 1 61  ? -27.580 -19.060 31.467  0.80 38.60  ? 61  HIS A ND1   1 
ATOM   899   C  CD2   A HIS A 1 61  ? -27.209 -17.156 32.627  0.20 38.29  ? 61  HIS A CD2   1 
ATOM   900   C  CD2   B HIS A 1 61  ? -27.251 -17.119 32.412  0.80 38.46  ? 61  HIS A CD2   1 
ATOM   901   C  CE1   A HIS A 1 61  ? -28.633 -18.810 32.406  0.20 36.93  ? 61  HIS A CE1   1 
ATOM   902   C  CE1   B HIS A 1 61  ? -28.615 -18.831 32.257  0.80 36.71  ? 61  HIS A CE1   1 
ATOM   903   N  NE2   A HIS A 1 61  ? -28.409 -17.678 33.048  0.20 38.51  ? 61  HIS A NE2   1 
ATOM   904   N  NE2   B HIS A 1 61  ? -28.442 -17.660 32.842  0.80 37.89  ? 61  HIS A NE2   1 
ATOM   905   N  N     A VAL A 1 62  ? -24.356 -16.656 27.709  0.20 29.59  ? 62  VAL A N     1 
ATOM   906   N  N     B VAL A 1 62  ? -24.120 -16.497 27.901  0.80 29.70  ? 62  VAL A N     1 
ATOM   907   C  CA    A VAL A 1 62  ? -23.220 -16.437 26.816  0.20 25.33  ? 62  VAL A CA    1 
ATOM   908   C  CA    B VAL A 1 62  ? -23.082 -16.286 26.892  0.80 23.25  ? 62  VAL A CA    1 
ATOM   909   C  C     A VAL A 1 62  ? -22.370 -15.308 27.386  0.20 29.56  ? 62  VAL A C     1 
ATOM   910   C  C     B VAL A 1 62  ? -22.208 -15.125 27.340  0.80 30.39  ? 62  VAL A C     1 
ATOM   911   O  O     A VAL A 1 62  ? -22.912 -14.235 27.687  0.20 27.63  ? 62  VAL A O     1 
ATOM   912   O  O     B VAL A 1 62  ? -22.721 -14.029 27.569  0.80 25.55  ? 62  VAL A O     1 
ATOM   913   C  CB    A VAL A 1 62  ? -23.684 -16.102 25.388  0.20 29.82  ? 62  VAL A CB    1 
ATOM   914   C  CB    B VAL A 1 62  ? -23.669 -15.997 25.499  0.80 29.76  ? 62  VAL A CB    1 
ATOM   915   C  CG1   A VAL A 1 62  ? -22.510 -16.160 24.421  0.20 29.58  ? 62  VAL A CG1   1 
ATOM   916   C  CG1   B VAL A 1 62  ? -22.547 -15.940 24.460  0.80 28.70  ? 62  VAL A CG1   1 
ATOM   917   C  CG2   A VAL A 1 62  ? -24.791 -17.051 24.957  0.20 30.18  ? 62  VAL A CG2   1 
ATOM   918   C  CG2   B VAL A 1 62  ? -24.708 -17.067 25.138  0.80 29.50  ? 62  VAL A CG2   1 
ATOM   919   N  N     A PRO A 1 63  ? -21.062 -15.501 27.554  0.20 31.36  ? 63  PRO A N     1 
ATOM   920   N  N     B PRO A 1 63  ? -20.887 -15.300 27.427  0.80 32.05  ? 63  PRO A N     1 
ATOM   921   C  CA    A PRO A 1 63  ? -20.215 -14.403 28.029  0.20 27.42  ? 63  PRO A CA    1 
ATOM   922   C  CA    B PRO A 1 63  ? -20.010 -14.185 27.806  0.80 28.05  ? 63  PRO A CA    1 
ATOM   923   C  C     A PRO A 1 63  ? -20.196 -13.258 27.031  0.20 25.29  ? 63  PRO A C     1 
ATOM   924   C  C     B PRO A 1 63  ? -20.157 -12.988 26.878  0.80 23.86  ? 63  PRO A C     1 
ATOM   925   O  O     A PRO A 1 63  ? -20.234 -13.464 25.815  0.20 25.98  ? 63  PRO A O     1 
ATOM   926   O  O     B PRO A 1 63  ? -20.239 -13.118 25.651  0.80 24.09  ? 63  PRO A O     1 
ATOM   927   C  CB    A PRO A 1 63  ? -18.832 -15.053 28.165  0.20 29.27  ? 63  PRO A CB    1 
ATOM   928   C  CB    B PRO A 1 63  ? -18.605 -14.796 27.704  0.80 28.44  ? 63  PRO A CB    1 
ATOM   929   C  CG    A PRO A 1 63  ? -19.104 -16.511 28.275  0.20 29.78  ? 63  PRO A CG    1 
ATOM   930   C  CG    B PRO A 1 63  ? -18.822 -16.236 27.986  0.80 29.64  ? 63  PRO A CG    1 
ATOM   931   C  CD    A PRO A 1 63  ? -20.312 -16.759 27.422  0.20 28.00  ? 63  PRO A CD    1 
ATOM   932   C  CD    B PRO A 1 63  ? -20.178 -16.588 27.413  0.80 27.46  ? 63  PRO A CD    1 
ATOM   933   N  N     A ARG A 1 64  ? -20.141 -12.037 27.559  0.20 26.64  ? 64  ARG A N     1 
ATOM   934   N  N     B ARG A 1 64  ? -20.186 -11.811 27.484  0.80 26.96  ? 64  ARG A N     1 
ATOM   935   C  CA    A ARG A 1 64  ? -20.010 -10.841 26.730  0.20 27.83  ? 64  ARG A CA    1 
ATOM   936   C  CA    B ARG A 1 64  ? -20.054 -10.564 26.743  0.80 28.18  ? 64  ARG A CA    1 
ATOM   937   C  C     A ARG A 1 64  ? -18.532 -10.604 26.411  0.20 25.44  ? 64  ARG A C     1 
ATOM   938   C  C     B ARG A 1 64  ? -18.559 -10.386 26.530  0.80 25.33  ? 64  ARG A C     1 
ATOM   939   O  O     A ARG A 1 64  ? -17.935 -9.589  26.767  0.20 26.43  ? 64  ARG A O     1 
ATOM   940   O  O     B ARG A 1 64  ? -17.857 -9.801  27.358  0.80 25.08  ? 64  ARG A O     1 
ATOM   941   C  CB    A ARG A 1 64  ? -20.632 -9.641  27.434  0.20 27.74  ? 64  ARG A CB    1 
ATOM   942   C  CB    B ARG A 1 64  ? -20.670 -9.402  27.512  0.80 27.90  ? 64  ARG A CB    1 
ATOM   943   C  CG    A ARG A 1 64  ? -22.056 -9.869  27.921  0.20 29.83  ? 64  ARG A CG    1 
ATOM   944   C  CG    B ARG A 1 64  ? -22.110 -9.624  27.931  0.80 30.60  ? 64  ARG A CG    1 
ATOM   945   C  CD    A ARG A 1 64  ? -22.546 -8.684  28.739  0.20 26.65  ? 64  ARG A CD    1 
ATOM   946   C  CD    B ARG A 1 64  ? -22.567 -8.474  28.803  0.80 25.90  ? 64  ARG A CD    1 
ATOM   947   N  NE    A ARG A 1 64  ? -23.847 -8.937  29.350  0.20 27.10  ? 64  ARG A NE    1 
ATOM   948   N  NE    B ARG A 1 64  ? -23.866 -8.730  29.418  0.80 26.57  ? 64  ARG A NE    1 
ATOM   949   C  CZ    A ARG A 1 64  ? -25.011 -8.663  28.778  0.20 27.64  ? 64  ARG A CZ    1 
ATOM   950   C  CZ    B ARG A 1 64  ? -25.032 -8.552  28.817  0.80 27.53  ? 64  ARG A CZ    1 
ATOM   951   N  NH1   A ARG A 1 64  ? -25.078 -8.132  27.567  0.20 27.77  ? 64  ARG A NH1   1 
ATOM   952   N  NH1   B ARG A 1 64  ? -25.106 -8.163  27.553  0.80 27.66  ? 64  ARG A NH1   1 
ATOM   953   N  NH2   A ARG A 1 64  ? -26.136 -8.922  29.439  0.20 32.64  ? 64  ARG A NH2   1 
ATOM   954   N  NH2   B ARG A 1 64  ? -26.154 -8.740  29.513  0.80 33.01  ? 64  ARG A NH2   1 
ATOM   955   N  N     A ALA A 1 65  ? -17.943 -11.584 25.729  0.20 24.00  ? 65  ALA A N     1 
ATOM   956   N  N     B ALA A 1 65  ? -18.060 -10.941 25.426  0.80 24.63  ? 65  ALA A N     1 
ATOM   957   C  CA    A ALA A 1 65  ? -16.503 -11.640 25.515  0.20 23.87  ? 65  ALA A CA    1 
ATOM   958   C  CA    B ALA A 1 65  ? -16.618 -11.020 25.218  0.80 22.24  ? 65  ALA A CA    1 
ATOM   959   C  C     A ALA A 1 65  ? -16.168 -11.658 24.030  0.20 23.63  ? 65  ALA A C     1 
ATOM   960   C  C     B ALA A 1 65  ? -16.296 -11.268 23.752  0.80 20.77  ? 65  ALA A C     1 
ATOM   961   O  O     A ALA A 1 65  ? -16.846 -12.319 23.235  0.20 23.75  ? 65  ALA A O     1 
ATOM   962   O  O     B ALA A 1 65  ? -17.011 -11.989 23.050  0.80 23.63  ? 65  ALA A O     1 
ATOM   963   C  CB    A ALA A 1 65  ? -15.896 -12.875 26.186  0.20 24.15  ? 65  ALA A CB    1 
ATOM   964   C  CB    B ALA A 1 65  ? -15.999 -12.129 26.076  0.80 23.27  ? 65  ALA A CB    1 
ATOM   965   N  N     A VAL A 1 66  ? -15.103 -10.945 23.670  0.20 24.85  ? 66  VAL A N     1 
ATOM   966   N  N     B VAL A 1 66  ? -15.172 -10.713 23.316  0.80 24.04  ? 66  VAL A N     1 
ATOM   967   C  CA    A VAL A 1 66  ? -14.549 -10.952 22.323  0.20 25.34  ? 66  VAL A CA    1 
ATOM   968   C  CA    B VAL A 1 66  ? -14.644 -10.955 21.982  0.80 25.00  ? 66  VAL A CA    1 
ATOM   969   C  C     A VAL A 1 66  ? -13.140 -11.529 22.396  0.20 24.63  ? 66  VAL A C     1 
ATOM   970   C  C     B VAL A 1 66  ? -13.163 -11.288 22.123  0.80 25.07  ? 66  VAL A C     1 
ATOM   971   O  O     A VAL A 1 66  ? -12.416 -11.299 23.371  0.20 21.52  ? 66  VAL A O     1 
ATOM   972   O  O     B VAL A 1 66  ? -12.447 -10.627 22.883  0.80 21.99  ? 66  VAL A O     1 
ATOM   973   C  CB    A VAL A 1 66  ? -14.540 -9.537  21.703  0.20 27.21  ? 66  VAL A CB    1 
ATOM   974   C  CB    B VAL A 1 66  ? -14.868 -9.734  21.065  0.80 29.35  ? 66  VAL A CB    1 
ATOM   975   C  CG1   A VAL A 1 66  ? -14.088 -9.577  20.244  0.20 31.90  ? 66  VAL A CG1   1 
ATOM   976   C  CG1   B VAL A 1 66  ? -14.593 -8.462  21.830  0.80 34.81  ? 66  VAL A CG1   1 
ATOM   977   C  CG2   A VAL A 1 66  ? -15.917 -8.894  21.817  0.20 26.00  ? 66  VAL A CG2   1 
ATOM   978   C  CG2   B VAL A 1 66  ? -13.988 -9.802  19.809  0.80 33.32  ? 66  VAL A CG2   1 
ATOM   979   N  N     A PHE A 1 67  ? -12.764 -12.297 21.373  0.20 23.29  ? 67  PHE A N     1 
ATOM   980   N  N     B PHE A 1 67  ? -12.722 -12.340 21.426  0.80 23.01  ? 67  PHE A N     1 
ATOM   981   C  CA    A PHE A 1 67  ? -11.436 -12.892 21.264  0.20 26.03  ? 67  PHE A CA    1 
ATOM   982   C  CA    B PHE A 1 67  ? -11.329 -12.746 21.362  0.80 26.42  ? 67  PHE A CA    1 
ATOM   983   C  C     A PHE A 1 67  ? -10.920 -12.612 19.860  0.20 23.63  ? 67  PHE A C     1 
ATOM   984   C  C     B PHE A 1 67  ? -10.787 -12.337 19.997  0.80 22.25  ? 67  PHE A C     1 
ATOM   985   O  O     A PHE A 1 67  ? -11.404 -13.205 18.890  0.20 26.60  ? 67  PHE A O     1 
ATOM   986   O  O     B PHE A 1 67  ? -11.478 -12.475 18.984  0.80 24.31  ? 67  PHE A O     1 
ATOM   987   C  CB    A PHE A 1 67  ? -11.471 -14.395 21.539  0.20 25.26  ? 67  PHE A CB    1 
ATOM   988   C  CB    B PHE A 1 67  ? -11.177 -14.261 21.542  0.80 24.67  ? 67  PHE A CB    1 
ATOM   989   C  CG    A PHE A 1 67  ? -11.793 -14.750 22.962  0.20 23.74  ? 67  PHE A CG    1 
ATOM   990   C  CG    B PHE A 1 67  ? -11.531 -14.767 22.916  0.80 22.84  ? 67  PHE A CG    1 
ATOM   991   C  CD1   A PHE A 1 67  ? -13.107 -14.872 23.385  0.20 28.41  ? 67  PHE A CD1   1 
ATOM   992   C  CD1   B PHE A 1 67  ? -12.819 -14.646 23.418  0.80 30.70  ? 67  PHE A CD1   1 
ATOM   993   C  CD2   A PHE A 1 67  ? -10.779 -14.978 23.876  0.20 24.84  ? 67  PHE A CD2   1 
ATOM   994   C  CD2   B PHE A 1 67  ? -10.580 -15.412 23.686  0.80 24.57  ? 67  PHE A CD2   1 
ATOM   995   C  CE1   A PHE A 1 67  ? -13.402 -15.205 24.698  0.20 25.22  ? 67  PHE A CE1   1 
ATOM   996   C  CE1   B PHE A 1 67  ? -13.140 -15.128 24.689  0.80 24.69  ? 67  PHE A CE1   1 
ATOM   997   C  CE2   A PHE A 1 67  ? -11.065 -15.312 25.187  0.20 24.53  ? 67  PHE A CE2   1 
ATOM   998   C  CE2   B PHE A 1 67  ? -10.891 -15.899 24.942  0.80 22.00  ? 67  PHE A CE2   1 
ATOM   999   C  CZ    A PHE A 1 67  ? -12.379 -15.425 25.598  0.20 27.26  ? 67  PHE A CZ    1 
ATOM   1000  C  CZ    B PHE A 1 67  ? -12.175 -15.759 25.444  0.80 27.33  ? 67  PHE A CZ    1 
ATOM   1001  N  N     A VAL A 1 68  ? -9.947  -11.711 19.745  0.20 23.67  ? 68  VAL A N     1 
ATOM   1002  N  N     B VAL A 1 68  ? -9.568  -11.814 19.964  0.80 22.27  ? 68  VAL A N     1 
ATOM   1003  C  CA    A VAL A 1 68  ? -9.422  -11.286 18.452  0.20 24.10  ? 68  VAL A CA    1 
ATOM   1004  C  CA    B VAL A 1 68  ? -8.993  -11.395 18.694  0.80 22.57  ? 68  VAL A CA    1 
ATOM   1005  C  C     A VAL A 1 68  ? -7.916  -11.505 18.438  0.20 26.27  ? 68  VAL A C     1 
ATOM   1006  C  C     B VAL A 1 68  ? -7.503  -11.710 18.680  0.80 25.94  ? 68  VAL A C     1 
ATOM   1007  O  O     A VAL A 1 68  ? -7.193  -10.973 19.291  0.20 23.29  ? 68  VAL A O     1 
ATOM   1008  O  O     B VAL A 1 68  ? -6.796  -11.512 19.674  0.80 21.24  ? 68  VAL A O     1 
ATOM   1009  C  CB    A VAL A 1 68  ? -9.773  -9.822  18.144  0.20 28.13  ? 68  VAL A CB    1 
ATOM   1010  C  CB    B VAL A 1 68  ? -9.256  -9.901  18.412  0.80 28.45  ? 68  VAL A CB    1 
ATOM   1011  C  CG1   A VAL A 1 68  ? -9.710  -8.981  19.406  0.20 28.03  ? 68  VAL A CG1   1 
ATOM   1012  C  CG1   B VAL A 1 68  ? -8.688  -9.043  19.510  0.80 36.36  ? 68  VAL A CG1   1 
ATOM   1013  C  CG2   A VAL A 1 68  ? -8.838  -9.270  17.074  0.20 29.23  ? 68  VAL A CG2   1 
ATOM   1014  C  CG2   B VAL A 1 68  ? -8.665  -9.494  17.060  0.80 29.74  ? 68  VAL A CG2   1 
ATOM   1015  N  N     A ASP A 1 69  ? -7.448  -12.279 17.462  0.20 25.21  ? 69  ASP A N     1 
ATOM   1016  N  N     B ASP A 1 69  ? -7.023  -12.182 17.534  0.80 23.95  ? 69  ASP A N     1 
ATOM   1017  C  CA    A ASP A 1 69  ? -6.031  -12.519 17.253  0.20 23.94  ? 69  ASP A CA    1 
ATOM   1018  C  CA    B ASP A 1 69  ? -5.607  -12.450 17.378  0.80 22.18  ? 69  ASP A CA    1 
ATOM   1019  C  C     A ASP A 1 69  ? -5.749  -12.441 15.760  0.20 26.21  ? 69  ASP A C     1 
ATOM   1020  C  C     B ASP A 1 69  ? -5.308  -12.434 15.891  0.80 24.29  ? 69  ASP A C     1 
ATOM   1021  O  O     A ASP A 1 69  ? -6.654  -12.559 14.930  0.20 27.19  ? 69  ASP A O     1 
ATOM   1022  O  O     B ASP A 1 69  ? -6.150  -12.817 15.076  0.80 29.74  ? 69  ASP A O     1 
ATOM   1023  C  CB    A ASP A 1 69  ? -5.599  -13.881 17.820  0.20 25.33  ? 69  ASP A CB    1 
ATOM   1024  C  CB    B ASP A 1 69  ? -5.214  -13.791 18.001  0.80 26.38  ? 69  ASP A CB    1 
ATOM   1025  C  CG    A ASP A 1 69  ? -4.092  -14.070 17.814  0.20 26.21  ? 69  ASP A CG    1 
ATOM   1026  C  CG    B ASP A 1 69  ? -3.731  -13.881 18.305  0.80 27.44  ? 69  ASP A CG    1 
ATOM   1027  O  OD1   A ASP A 1 69  ? -3.375  -13.141 17.385  0.20 24.34  ? 69  ASP A OD1   1 
ATOM   1028  O  OD1   B ASP A 1 69  ? -2.999  -12.906 18.018  0.80 26.23  ? 69  ASP A OD1   1 
ATOM   1029  O  OD2   A ASP A 1 69  ? -3.628  -15.152 18.238  0.20 26.85  ? 69  ASP A OD2   1 
ATOM   1030  O  OD2   B ASP A 1 69  ? -3.313  -14.929 18.858  0.80 27.83  ? 69  ASP A OD2   1 
ATOM   1031  N  N     A LEU A 1 70  ? -4.478  -12.227 15.425  0.20 26.25  ? 70  LEU A N     1 
ATOM   1032  N  N     B LEU A 1 70  ? -4.109  -11.981 15.548  0.80 26.55  ? 70  LEU A N     1 
ATOM   1033  C  CA    A LEU A 1 70  ? -4.064  -12.166 14.030  0.20 24.91  ? 70  LEU A CA    1 
ATOM   1034  C  CA    B LEU A 1 70  ? -3.815  -11.777 14.135  0.80 22.40  ? 70  LEU A CA    1 
ATOM   1035  C  C     A LEU A 1 70  ? -3.692  -13.529 13.463  0.20 29.04  ? 70  LEU A C     1 
ATOM   1036  C  C     B LEU A 1 70  ? -3.423  -13.058 13.409  0.80 29.73  ? 70  LEU A C     1 
ATOM   1037  O  O     A LEU A 1 70  ? -3.607  -13.676 12.239  0.20 29.19  ? 70  LEU A O     1 
ATOM   1038  O  O     B LEU A 1 70  ? -3.313  -13.039 12.180  0.80 29.77  ? 70  LEU A O     1 
ATOM   1039  C  CB    A LEU A 1 70  ? -2.886  -11.201 13.875  0.20 27.29  ? 70  LEU A CB    1 
ATOM   1040  C  CB    B LEU A 1 70  ? -2.730  -10.708 13.990  0.80 26.89  ? 70  LEU A CB    1 
ATOM   1041  C  CG    A LEU A 1 70  ? -3.174  -9.754  14.277  0.20 26.28  ? 70  LEU A CG    1 
ATOM   1042  C  CG    B LEU A 1 70  ? -3.277  -9.348  14.422  0.80 27.32  ? 70  LEU A CG    1 
ATOM   1043  C  CD1   A LEU A 1 70  ? -1.942  -8.884  14.105  0.20 27.70  ? 70  LEU A CD1   1 
ATOM   1044  C  CD1   B LEU A 1 70  ? -2.271  -8.214  14.343  0.80 24.30  ? 70  LEU A CD1   1 
ATOM   1045  C  CD2   A LEU A 1 70  ? -4.342  -9.201  13.474  0.20 31.78  ? 70  LEU A CD2   1 
ATOM   1046  C  CD2   B LEU A 1 70  ? -4.534  -9.009  13.621  0.80 33.21  ? 70  LEU A CD2   1 
ATOM   1047  N  N     A GLU A 1 71  ? -3.465  -14.521 14.319  0.20 29.30  ? 71  GLU A N     1 
ATOM   1048  N  N     B GLU A 1 71  ? -3.217  -14.157 14.118  0.80 27.70  ? 71  GLU A N     1 
ATOM   1049  C  CA    A GLU A 1 71  ? -3.269  -15.903 13.919  0.20 31.61  ? 71  GLU A CA    1 
ATOM   1050  C  CA    B GLU A 1 71  ? -3.048  -15.479 13.537  0.80 30.69  ? 71  GLU A CA    1 
ATOM   1051  C  C     A GLU A 1 71  ? -4.327  -16.776 14.586  0.20 33.31  ? 71  GLU A C     1 
ATOM   1052  C  C     B GLU A 1 71  ? -3.943  -16.444 14.299  0.80 34.85  ? 71  GLU A C     1 
ATOM   1053  O  O     A GLU A 1 71  ? -4.839  -16.424 15.653  0.20 33.76  ? 71  GLU A O     1 
ATOM   1054  O  O     B GLU A 1 71  ? -4.380  -16.137 15.413  0.80 35.03  ? 71  GLU A O     1 
ATOM   1055  C  CB    A GLU A 1 71  ? -1.869  -16.401 14.298  0.20 31.98  ? 71  GLU A CB    1 
ATOM   1056  C  CB    B GLU A 1 71  ? -1.574  -15.932 13.578  0.80 29.13  ? 71  GLU A CB    1 
ATOM   1057  C  CG    A GLU A 1 71  ? -1.586  -16.368 15.783  0.20 32.02  ? 71  GLU A CG    1 
ATOM   1058  C  CG    B GLU A 1 71  ? -0.898  -15.924 14.944  0.80 32.27  ? 71  GLU A CG    1 
ATOM   1059  C  CD    A GLU A 1 71  ? -1.104  -17.704 16.307  0.20 35.83  ? 71  GLU A CD    1 
ATOM   1060  C  CD    B GLU A 1 71  ? -0.850  -17.296 15.582  0.80 37.63  ? 71  GLU A CD    1 
ATOM   1061  O  OE1   A GLU A 1 71  ? -1.162  -18.691 15.545  0.20 34.46  ? 71  GLU A OE1   1 
ATOM   1062  O  OE1   B GLU A 1 71  ? -1.388  -18.236 14.967  0.80 31.20  ? 71  GLU A OE1   1 
ATOM   1063  O  OE2   A GLU A 1 71  ? -0.668  -17.766 17.476  0.20 33.07  ? 71  GLU A OE2   1 
ATOM   1064  O  OE2   B GLU A 1 71  ? -0.277  -17.437 16.695  0.80 36.89  ? 71  GLU A OE2   1 
ATOM   1065  N  N     A PRO A 1 72  ? -4.693  -17.909 13.980  0.20 32.78  ? 72  PRO A N     1 
ATOM   1066  N  N     B PRO A 1 72  ? -4.274  -17.603 13.717  0.80 31.45  ? 72  PRO A N     1 
ATOM   1067  C  CA    A PRO A 1 72  ? -5.826  -18.688 14.493  0.20 36.12  ? 72  PRO A CA    1 
ATOM   1068  C  CA    B PRO A 1 72  ? -5.345  -18.435 14.290  0.80 38.15  ? 72  PRO A CA    1 
ATOM   1069  C  C     A PRO A 1 72  ? -5.488  -19.767 15.511  0.20 35.72  ? 72  PRO A C     1 
ATOM   1070  C  C     B PRO A 1 72  ? -4.964  -19.421 15.387  0.80 36.74  ? 72  PRO A C     1 
ATOM   1071  O  O     A PRO A 1 72  ? -6.419  -20.298 16.132  0.20 35.51  ? 72  PRO A O     1 
ATOM   1072  O  O     B PRO A 1 72  ? -5.884  -19.947 16.030  0.80 38.31  ? 72  PRO A O     1 
ATOM   1073  C  CB    A PRO A 1 72  ? -6.386  -19.324 13.214  0.20 34.96  ? 72  PRO A CB    1 
ATOM   1074  C  CB    B PRO A 1 72  ? -5.860  -19.201 13.062  0.80 36.92  ? 72  PRO A CB    1 
ATOM   1075  C  CG    A PRO A 1 72  ? -5.165  -19.569 12.386  0.20 34.82  ? 72  PRO A CG    1 
ATOM   1076  C  CG    B PRO A 1 72  ? -4.641  -19.366 12.209  0.80 34.25  ? 72  PRO A CG    1 
ATOM   1077  C  CD    A PRO A 1 72  ? -4.228  -18.412 12.672  0.20 35.89  ? 72  PRO A CD    1 
ATOM   1078  C  CD    B PRO A 1 72  ? -3.888  -18.062 12.363  0.80 33.73  ? 72  PRO A CD    1 
ATOM   1079  N  N     A THR A 1 73  ? -4.207  -20.092 15.710  0.20 33.70  ? 73  THR A N     1 
ATOM   1080  N  N     B THR A 1 73  ? -3.670  -19.669 15.627  0.80 31.34  ? 73  THR A N     1 
ATOM   1081  C  CA    A THR A 1 73  ? -3.845  -21.289 16.468  0.20 34.29  ? 73  THR A CA    1 
ATOM   1082  C  CA    B THR A 1 73  ? -3.240  -20.840 16.398  0.80 37.63  ? 73  THR A CA    1 
ATOM   1083  C  C     A THR A 1 73  ? -4.343  -21.220 17.908  0.20 34.30  ? 73  THR A C     1 
ATOM   1084  C  C     B THR A 1 73  ? -3.866  -20.885 17.790  0.80 34.02  ? 73  THR A C     1 
ATOM   1085  O  O     A THR A 1 73  ? -4.914  -22.187 18.426  0.20 34.80  ? 73  THR A O     1 
ATOM   1086  O  O     B THR A 1 73  ? -4.288  -21.950 18.256  0.80 32.96  ? 73  THR A O     1 
ATOM   1087  C  CB    A THR A 1 73  ? -2.329  -21.491 16.439  0.20 35.51  ? 73  THR A CB    1 
ATOM   1088  C  CB    B THR A 1 73  ? -1.711  -20.859 16.525  0.80 31.91  ? 73  THR A CB    1 
ATOM   1089  O  OG1   A THR A 1 73  ? -1.891  -21.649 15.084  0.20 38.83  ? 73  THR A OG1   1 
ATOM   1090  O  OG1   B THR A 1 73  ? -1.111  -20.579 15.255  0.80 44.72  ? 73  THR A OG1   1 
ATOM   1091  C  CG2   A THR A 1 73  ? -1.939  -22.725 17.243  0.20 36.01  ? 73  THR A CG2   1 
ATOM   1092  C  CG2   B THR A 1 73  ? -1.230  -22.205 17.014  0.80 39.50  ? 73  THR A CG2   1 
ATOM   1093  N  N     A VAL A 1 74  ? -4.132  -20.084 18.573  0.20 34.05  ? 74  VAL A N     1 
ATOM   1094  N  N     B VAL A 1 74  ? -3.923  -19.748 18.478  0.80 33.72  ? 74  VAL A N     1 
ATOM   1095  C  CA    A VAL A 1 74  ? -4.495  -19.976 19.982  0.20 32.08  ? 74  VAL A CA    1 
ATOM   1096  C  CA    B VAL A 1 74  ? -4.315  -19.773 19.880  0.80 30.36  ? 74  VAL A CA    1 
ATOM   1097  C  C     A VAL A 1 74  ? -6.012  -19.963 20.152  0.20 33.86  ? 74  VAL A C     1 
ATOM   1098  C  C     B VAL A 1 74  ? -5.839  -19.770 20.027  0.80 33.39  ? 74  VAL A C     1 
ATOM   1099  O  O     A VAL A 1 74  ? -6.553  -20.607 21.059  0.20 35.58  ? 74  VAL A O     1 
ATOM   1100  O  O     B VAL A 1 74  ? -6.399  -20.503 20.851  0.80 36.44  ? 74  VAL A O     1 
ATOM   1101  C  CB    A VAL A 1 74  ? -3.838  -18.731 20.602  0.20 32.83  ? 74  VAL A CB    1 
ATOM   1102  C  CB    B VAL A 1 74  ? -3.659  -18.588 20.605  0.80 33.35  ? 74  VAL A CB    1 
ATOM   1103  C  CG1   A VAL A 1 74  ? -4.331  -18.517 22.021  0.20 29.26  ? 74  VAL A CG1   1 
ATOM   1104  C  CG1   B VAL A 1 74  ? -3.948  -18.646 22.085  0.80 30.18  ? 74  VAL A CG1   1 
ATOM   1105  C  CG2   A VAL A 1 74  ? -2.325  -18.868 20.572  0.20 32.99  ? 74  VAL A CG2   1 
ATOM   1106  C  CG2   B VAL A 1 74  ? -2.154  -18.563 20.324  0.80 33.85  ? 74  VAL A CG2   1 
ATOM   1107  N  N     A ILE A 1 75  ? -6.724  -19.238 19.287  0.20 32.55  ? 75  ILE A N     1 
ATOM   1108  N  N     B ILE A 1 75  ? -6.538  -18.953 19.234  0.80 29.98  ? 75  ILE A N     1 
ATOM   1109  C  CA    A ILE A 1 75  ? -8.176  -19.171 19.428  0.20 33.14  ? 75  ILE A CA    1 
ATOM   1110  C  CA    B ILE A 1 75  ? -7.998  -18.925 19.306  0.80 32.92  ? 75  ILE A CA    1 
ATOM   1111  C  C     A ILE A 1 75  ? -8.835  -20.458 18.940  0.20 37.49  ? 75  ILE A C     1 
ATOM   1112  C  C     B ILE A 1 75  ? -8.603  -20.254 18.843  0.80 38.07  ? 75  ILE A C     1 
ATOM   1113  O  O     A ILE A 1 75  ? -9.874  -20.870 19.473  0.20 35.50  ? 75  ILE A O     1 
ATOM   1114  O  O     B ILE A 1 75  ? -9.690  -20.643 19.298  0.80 34.62  ? 75  ILE A O     1 
ATOM   1115  C  CB    A ILE A 1 75  ? -8.728  -17.928 18.703  0.20 31.83  ? 75  ILE A CB    1 
ATOM   1116  C  CB    B ILE A 1 75  ? -8.525  -17.709 18.514  0.80 30.69  ? 75  ILE A CB    1 
ATOM   1117  C  CG1   A ILE A 1 75  ? -8.132  -16.655 19.306  0.20 31.34  ? 75  ILE A CG1   1 
ATOM   1118  C  CG1   B ILE A 1 75  ? -8.299  -16.433 19.339  0.80 31.97  ? 75  ILE A CG1   1 
ATOM   1119  C  CG2   A ILE A 1 75  ? -10.252 -17.881 18.785  0.20 33.80  ? 75  ILE A CG2   1 
ATOM   1120  C  CG2   B ILE A 1 75  ? -9.990  -17.876 18.125  0.80 35.08  ? 75  ILE A CG2   1 
ATOM   1121  C  CD1   A ILE A 1 75  ? -8.774  -15.375 18.808  0.20 29.66  ? 75  ILE A CD1   1 
ATOM   1122  C  CD1   B ILE A 1 75  ? -9.036  -15.200 18.849  0.80 29.90  ? 75  ILE A CD1   1 
ATOM   1123  N  N     A ASP A 1 76  ? -8.248  -21.124 17.939  0.20 35.30  ? 76  ASP A N     1 
ATOM   1124  N  N     B ASP A 1 76  ? -7.898  -20.998 17.983  0.80 33.89  ? 76  ASP A N     1 
ATOM   1125  C  CA    A ASP A 1 76  ? -8.763  -22.425 17.520  0.20 36.47  ? 76  ASP A CA    1 
ATOM   1126  C  CA    B ASP A 1 76  ? -8.367  -22.324 17.579  0.80 35.29  ? 76  ASP A CA    1 
ATOM   1127  C  C     A ASP A 1 76  ? -8.750  -23.443 18.651  0.20 40.43  ? 76  ASP A C     1 
ATOM   1128  C  C     B ASP A 1 76  ? -8.483  -23.281 18.762  0.80 41.15  ? 76  ASP A C     1 
ATOM   1129  O  O     A ASP A 1 76  ? -9.540  -24.392 18.624  0.20 37.78  ? 76  ASP A O     1 
ATOM   1130  O  O     B ASP A 1 76  ? -9.276  -24.229 18.716  0.80 35.24  ? 76  ASP A O     1 
ATOM   1131  C  CB    A ASP A 1 76  ? -7.965  -22.964 16.332  0.20 38.42  ? 76  ASP A CB    1 
ATOM   1132  C  CB    B ASP A 1 76  ? -7.435  -22.913 16.516  0.80 39.00  ? 76  ASP A CB    1 
ATOM   1133  C  CG    A ASP A 1 76  ? -8.371  -22.325 15.019  0.20 39.49  ? 76  ASP A CG    1 
ATOM   1134  C  CG    B ASP A 1 76  ? -7.746  -22.409 15.123  0.80 37.82  ? 76  ASP A CG    1 
ATOM   1135  O  OD1   A ASP A 1 76  ? -9.547  -21.915 14.897  0.20 40.07  ? 76  ASP A OD1   1 
ATOM   1136  O  OD1   B ASP A 1 76  ? -8.651  -21.557 14.999  0.80 43.37  ? 76  ASP A OD1   1 
ATOM   1137  O  OD2   A ASP A 1 76  ? -7.522  -22.240 14.105  0.20 36.63  ? 76  ASP A OD2   1 
ATOM   1138  O  OD2   B ASP A 1 76  ? -7.097  -22.863 14.154  0.80 39.00  ? 76  ASP A OD2   1 
ATOM   1139  N  N     A GLU A 1 77  ? -7.871  -23.268 19.639  0.20 40.65  ? 77  GLU A N     1 
ATOM   1140  N  N     B GLU A 1 77  ? -7.697  -23.068 19.820  0.80 41.93  ? 77  GLU A N     1 
ATOM   1141  C  CA    A GLU A 1 77  ? -7.923  -24.100 20.836  0.20 43.02  ? 77  GLU A CA    1 
ATOM   1142  C  CA    B GLU A 1 77  ? -7.816  -23.913 21.005  0.80 43.93  ? 77  GLU A CA    1 
ATOM   1143  C  C     A GLU A 1 77  ? -9.214  -23.859 21.607  0.20 44.29  ? 77  GLU A C     1 
ATOM   1144  C  C     B GLU A 1 77  ? -9.088  -23.612 21.794  0.80 46.13  ? 77  GLU A C     1 
ATOM   1145  O  O     A GLU A 1 77  ? -9.780  -24.789 22.193  0.20 40.79  ? 77  GLU A O     1 
ATOM   1146  O  O     B GLU A 1 77  ? -9.598  -24.492 22.505  0.80 39.54  ? 77  GLU A O     1 
ATOM   1147  C  CB    A GLU A 1 77  ? -6.710  -23.818 21.724  0.20 41.73  ? 77  GLU A CB    1 
ATOM   1148  C  CB    B GLU A 1 77  ? -6.593  -23.746 21.904  0.80 41.46  ? 77  GLU A CB    1 
ATOM   1149  C  CG    A GLU A 1 77  ? -6.484  -24.834 22.834  0.20 44.52  ? 77  GLU A CG    1 
ATOM   1150  C  CG    B GLU A 1 77  ? -5.372  -24.532 21.463  0.80 49.34  ? 77  GLU A CG    1 
ATOM   1151  C  CD    A GLU A 1 77  ? -5.805  -26.095 22.335  0.20 48.93  ? 77  GLU A CD    1 
ATOM   1152  C  CD    B GLU A 1 77  ? -4.248  -24.444 22.480  0.80 53.08  ? 77  GLU A CD    1 
ATOM   1153  O  OE1   A GLU A 1 77  ? -5.454  -26.141 21.137  0.20 44.59  ? 77  GLU A OE1   1 
ATOM   1154  O  OE1   B GLU A 1 77  ? -3.736  -23.323 22.713  0.80 42.35  ? 77  GLU A OE1   1 
ATOM   1155  O  OE2   A GLU A 1 77  ? -5.619  -27.036 23.136  0.20 49.98  ? 77  GLU A OE2   1 
ATOM   1156  O  OE2   B GLU A 1 77  ? -3.892  -25.492 23.062  0.80 69.32  ? 77  GLU A OE2   1 
ATOM   1157  N  N     A VAL A 1 78  ? -9.691  -22.612 21.619  0.20 42.90  ? 78  VAL A N     1 
ATOM   1158  N  N     B VAL A 1 78  ? -9.596  -22.377 21.703  0.80 44.08  ? 78  VAL A N     1 
ATOM   1159  C  CA    A VAL A 1 78  ? -10.945 -22.294 22.295  0.20 37.20  ? 78  VAL A CA    1 
ATOM   1160  C  CA    B VAL A 1 78  ? -10.882 -22.053 22.317  0.80 35.50  ? 78  VAL A CA    1 
ATOM   1161  C  C     A VAL A 1 78  ? -12.137 -22.768 21.473  0.20 43.02  ? 78  VAL A C     1 
ATOM   1162  C  C     B VAL A 1 78  ? -12.019 -22.656 21.501  0.80 43.12  ? 78  VAL A C     1 
ATOM   1163  O  O     A VAL A 1 78  ? -13.167 -23.160 22.034  0.20 45.30  ? 78  VAL A O     1 
ATOM   1164  O  O     B VAL A 1 78  ? -12.989 -23.182 22.058  0.80 45.69  ? 78  VAL A O     1 
ATOM   1165  C  CB    A VAL A 1 78  ? -11.022 -20.784 22.584  0.20 34.24  ? 78  VAL A CB    1 
ATOM   1166  C  CB    B VAL A 1 78  ? -11.036 -20.525 22.470  0.80 32.46  ? 78  VAL A CB    1 
ATOM   1167  C  CG1   A VAL A 1 78  ? -12.219 -20.460 23.473  0.20 37.02  ? 78  VAL A CG1   1 
ATOM   1168  C  CG1   B VAL A 1 78  ? -12.297 -20.169 23.269  0.80 36.57  ? 78  VAL A CG1   1 
ATOM   1169  C  CG2   A VAL A 1 78  ? -9.730  -20.302 23.222  0.20 33.88  ? 78  VAL A CG2   1 
ATOM   1170  C  CG2   B VAL A 1 78  ? -9.814  -19.938 23.138  0.80 32.19  ? 78  VAL A CG2   1 
ATOM   1171  N  N     A ARG A 1 79  ? -12.022 -22.748 20.143  0.20 43.22  ? 79  ARG A N     1 
ATOM   1172  N  N     B ARG A 1 79  ? -11.912 -22.601 20.168  0.80 43.66  ? 79  ARG A N     1 
ATOM   1173  C  CA    A ARG A 1 79  ? -13.113 -23.192 19.283  0.20 43.44  ? 79  ARG A CA    1 
ATOM   1174  C  CA    B ARG A 1 79  ? -12.945 -23.142 19.289  0.80 43.33  ? 79  ARG A CA    1 
ATOM   1175  C  C     A ARG A 1 79  ? -13.336 -24.696 19.353  0.20 48.51  ? 79  ARG A C     1 
ATOM   1176  C  C     B ARG A 1 79  ? -13.151 -24.639 19.486  0.80 48.82  ? 79  ARG A C     1 
ATOM   1177  O  O     A ARG A 1 79  ? -14.407 -25.168 18.957  0.20 53.81  ? 79  ARG A O     1 
ATOM   1178  O  O     B ARG A 1 79  ? -14.239 -25.144 19.191  0.80 55.69  ? 79  ARG A O     1 
ATOM   1179  C  CB    A ARG A 1 79  ? -12.841 -22.780 17.835  0.20 39.34  ? 79  ARG A CB    1 
ATOM   1180  C  CB    B ARG A 1 79  ? -12.596 -22.859 17.818  0.80 37.98  ? 79  ARG A CB    1 
ATOM   1181  C  CG    A ARG A 1 79  ? -12.866 -21.278 17.596  0.20 41.36  ? 79  ARG A CG    1 
ATOM   1182  C  CG    B ARG A 1 79  ? -12.741 -21.389 17.377  0.80 42.64  ? 79  ARG A CG    1 
ATOM   1183  C  CD    A ARG A 1 79  ? -12.403 -20.940 16.186  0.20 38.73  ? 79  ARG A CD    1 
ATOM   1184  C  CD    B ARG A 1 79  ? -12.027 -21.099 16.034  0.80 37.68  ? 79  ARG A CD    1 
ATOM   1185  N  NE    A ARG A 1 79  ? -12.554 -19.521 15.882  0.20 37.64  ? 79  ARG A NE    1 
ATOM   1186  N  NE    B ARG A 1 79  ? -12.266 -19.739 15.550  0.80 39.60  ? 79  ARG A NE    1 
ATOM   1187  C  CZ    A ARG A 1 79  ? -12.111 -18.944 14.773  0.20 37.90  ? 79  ARG A CZ    1 
ATOM   1188  C  CZ    B ARG A 1 79  ? -11.477 -19.087 14.703  0.80 41.35  ? 79  ARG A CZ    1 
ATOM   1189  N  NH1   A ARG A 1 79  ? -11.474 -19.635 13.841  0.20 43.32  ? 79  ARG A NH1   1 
ATOM   1190  N  NH1   B ARG A 1 79  ? -10.369 -19.637 14.224  0.80 40.84  ? 79  ARG A NH1   1 
ATOM   1191  N  NH2   A ARG A 1 79  ? -12.311 -17.641 14.595  0.20 35.55  ? 79  ARG A NH2   1 
ATOM   1192  N  NH2   B ARG A 1 79  ? -11.797 -17.846 14.334  0.80 36.96  ? 79  ARG A NH2   1 
ATOM   1193  N  N     A THR A 1 80  ? -12.356 -25.457 19.840  0.20 47.90  ? 80  THR A N     1 
ATOM   1194  N  N     B THR A 1 80  ? -12.143 -25.358 19.986  0.80 48.42  ? 80  THR A N     1 
ATOM   1195  C  CA    A THR A 1 80  ? -12.479 -26.903 19.953  0.20 49.85  ? 80  THR A CA    1 
ATOM   1196  C  CA    B THR A 1 80  ? -12.223 -26.807 20.130  0.80 50.71  ? 80  THR A CA    1 
ATOM   1197  C  C     A THR A 1 80  ? -12.295 -27.411 21.375  0.20 48.85  ? 80  THR A C     1 
ATOM   1198  C  C     B THR A 1 80  ? -12.045 -27.277 21.567  0.80 48.65  ? 80  THR A C     1 
ATOM   1199  O  O     A THR A 1 80  ? -12.306 -28.629 21.586  0.20 51.54  ? 80  THR A O     1 
ATOM   1200  O  O     B THR A 1 80  ? -11.975 -28.489 21.803  0.80 52.85  ? 80  THR A O     1 
ATOM   1201  C  CB    A THR A 1 80  ? -11.469 -27.602 19.033  0.20 48.59  ? 80  THR A CB    1 
ATOM   1202  C  CB    B THR A 1 80  ? -11.182 -27.495 19.237  0.80 48.50  ? 80  THR A CB    1 
ATOM   1203  O  OG1   A THR A 1 80  ? -10.136 -27.245 19.421  0.20 47.67  ? 80  THR A OG1   1 
ATOM   1204  O  OG1   B THR A 1 80  ? -9.876  -27.354 19.815  0.80 48.20  ? 80  THR A OG1   1 
ATOM   1205  C  CG2   A THR A 1 80  ? -11.698 -27.199 17.584  0.20 49.26  ? 80  THR A CG2   1 
ATOM   1206  C  CG2   B THR A 1 80  ? -11.181 -26.877 17.846  0.80 49.82  ? 80  THR A CG2   1 
ATOM   1207  N  N     A GLY A 1 81  ? -12.128 -26.524 22.351  0.20 48.13  ? 81  GLY A N     1 
ATOM   1208  N  N     B GLY A 1 81  ? -11.983 -26.364 22.533  0.80 48.03  ? 81  GLY A N     1 
ATOM   1209  C  CA    A GLY A 1 81  ? -11.943 -26.925 23.730  0.20 47.25  ? 81  GLY A CA    1 
ATOM   1210  C  CA    B GLY A 1 81  ? -11.728 -26.720 23.912  0.80 46.71  ? 81  GLY A CA    1 
ATOM   1211  C  C     A GLY A 1 81  ? -13.244 -27.339 24.390  0.20 47.11  ? 81  GLY A C     1 
ATOM   1212  C  C     B GLY A 1 81  ? -12.975 -27.174 24.657  0.80 45.40  ? 81  GLY A C     1 
ATOM   1213  O  O     A GLY A 1 81  ? -14.256 -27.600 23.735  0.20 48.45  ? 81  GLY A O     1 
ATOM   1214  O  O     B GLY A 1 81  ? -14.026 -27.450 24.078  0.80 47.22  ? 81  GLY A O     1 
ATOM   1215  N  N     A THR A 1 82  ? -13.206 -27.399 25.723  0.20 46.12  ? 82  THR A N     1 
ATOM   1216  N  N     B THR A 1 82  ? -12.835 -27.255 25.984  0.80 43.89  ? 82  THR A N     1 
ATOM   1217  C  CA    A THR A 1 82  ? -14.391 -27.794 26.477  0.20 49.48  ? 82  THR A CA    1 
ATOM   1218  C  CA    B THR A 1 82  ? -13.933 -27.706 26.836  0.80 49.27  ? 82  THR A CA    1 
ATOM   1219  C  C     A THR A 1 82  ? -15.480 -26.732 26.394  0.20 49.75  ? 82  THR A C     1 
ATOM   1220  C  C     B THR A 1 82  ? -15.110 -26.737 26.813  0.80 50.42  ? 82  THR A C     1 
ATOM   1221  O  O     A THR A 1 82  ? -16.661 -27.057 26.230  0.20 52.22  ? 82  THR A O     1 
ATOM   1222  O  O     B THR A 1 82  ? -16.265 -27.162 26.924  0.80 53.72  ? 82  THR A O     1 
ATOM   1223  C  CB    A THR A 1 82  ? -14.021 -28.071 27.935  0.20 52.75  ? 82  THR A CB    1 
ATOM   1224  C  CB    B THR A 1 82  ? -13.442 -27.883 28.276  0.80 56.03  ? 82  THR A CB    1 
ATOM   1225  O  OG1   A THR A 1 82  ? -13.031 -29.105 27.988  0.20 56.89  ? 82  THR A OG1   1 
ATOM   1226  O  OG1   B THR A 1 82  ? -12.310 -28.762 28.297  0.80 65.52  ? 82  THR A OG1   1 
ATOM   1227  C  CG2   A THR A 1 82  ? -15.245 -28.512 28.726  0.20 52.95  ? 82  THR A CG2   1 
ATOM   1228  C  CG2   B THR A 1 82  ? -14.544 -28.457 29.164  0.80 54.85  ? 82  THR A CG2   1 
ATOM   1229  N  N     A TYR A 1 83  ? -15.104 -25.455 26.498  0.20 49.74  ? 83  TYR A N     1 
ATOM   1230  N  N     B TYR A 1 83  ? -14.845 -25.439 26.688  0.80 50.94  ? 83  TYR A N     1 
ATOM   1231  C  CA    A TYR A 1 83  ? -16.057 -24.353 26.448  0.20 48.21  ? 83  TYR A CA    1 
ATOM   1232  C  CA    B TYR A 1 83  ? -15.891 -24.426 26.698  0.80 49.03  ? 83  TYR A CA    1 
ATOM   1233  C  C     A TYR A 1 83  ? -16.269 -23.820 25.036  0.20 46.06  ? 83  TYR A C     1 
ATOM   1234  C  C     B TYR A 1 83  ? -16.171 -23.877 25.306  0.80 45.88  ? 83  TYR A C     1 
ATOM   1235  O  O     A TYR A 1 83  ? -16.506 -22.617 24.859  0.20 47.99  ? 83  TYR A O     1 
ATOM   1236  O  O     B TYR A 1 83  ? -16.544 -22.707 25.165  0.80 51.20  ? 83  TYR A O     1 
ATOM   1237  C  CB    A TYR A 1 83  ? -15.609 -23.231 27.386  0.20 48.65  ? 83  TYR A CB    1 
ATOM   1238  C  CB    B TYR A 1 83  ? -15.523 -23.293 27.658  0.80 49.52  ? 83  TYR A CB    1 
ATOM   1239  C  CG    A TYR A 1 83  ? -15.682 -23.598 28.852  0.20 47.42  ? 83  TYR A CG    1 
ATOM   1240  C  CG    B TYR A 1 83  ? -15.686 -23.650 29.120  0.80 47.67  ? 83  TYR A CG    1 
ATOM   1241  C  CD1   A TYR A 1 83  ? -14.591 -24.157 29.504  0.20 46.07  ? 83  TYR A CD1   1 
ATOM   1242  C  CD1   B TYR A 1 83  ? -14.658 -24.260 29.827  0.80 44.97  ? 83  TYR A CD1   1 
ATOM   1243  C  CD2   A TYR A 1 83  ? -16.846 -23.390 29.583  0.20 50.84  ? 83  TYR A CD2   1 
ATOM   1244  C  CD2   B TYR A 1 83  ? -16.872 -23.376 29.795  0.80 51.82  ? 83  TYR A CD2   1 
ATOM   1245  C  CE1   A TYR A 1 83  ? -14.655 -24.496 30.843  0.20 44.49  ? 83  TYR A CE1   1 
ATOM   1246  C  CE1   B TYR A 1 83  ? -14.804 -24.588 31.160  0.80 43.47  ? 83  TYR A CE1   1 
ATOM   1247  C  CE2   A TYR A 1 83  ? -16.919 -23.725 30.922  0.20 45.74  ? 83  TYR A CE2   1 
ATOM   1248  C  CE2   B TYR A 1 83  ? -17.028 -23.697 31.129  0.80 45.39  ? 83  TYR A CE2   1 
ATOM   1249  C  CZ    A TYR A 1 83  ? -15.821 -24.278 31.547  0.20 46.13  ? 83  TYR A CZ    1 
ATOM   1250  C  CZ    B TYR A 1 83  ? -15.990 -24.305 31.808  0.80 46.93  ? 83  TYR A CZ    1 
ATOM   1251  O  OH    A TYR A 1 83  ? -15.890 -24.613 32.881  0.20 41.25  ? 83  TYR A OH    1 
ATOM   1252  O  OH    B TYR A 1 83  ? -16.135 -24.629 33.141  0.80 39.99  ? 83  TYR A OH    1 
ATOM   1253  N  N     A ARG A 1 84  ? -16.197 -24.686 24.022  0.20 44.20  ? 84  ARG A N     1 
ATOM   1254  N  N     B ARG A 1 84  ? -16.008 -24.703 24.271  0.80 42.40  ? 84  ARG A N     1 
ATOM   1255  C  CA    A ARG A 1 84  ? -16.417 -24.249 22.649  0.20 45.26  ? 84  ARG A CA    1 
ATOM   1256  C  CA    B ARG A 1 84  ? -16.220 -24.222 22.911  0.80 43.73  ? 84  ARG A CA    1 
ATOM   1257  C  C     A ARG A 1 84  ? -17.854 -23.805 22.407  0.20 46.09  ? 84  ARG A C     1 
ATOM   1258  C  C     B ARG A 1 84  ? -17.668 -23.802 22.692  0.80 46.03  ? 84  ARG A C     1 
ATOM   1259  O  O     A ARG A 1 84  ? -18.098 -23.007 21.495  0.20 46.35  ? 84  ARG A O     1 
ATOM   1260  O  O     B ARG A 1 84  ? -17.937 -22.822 21.987  0.80 47.08  ? 84  ARG A O     1 
ATOM   1261  C  CB    A ARG A 1 84  ? -16.039 -25.371 21.679  0.20 48.41  ? 84  ARG A CB    1 
ATOM   1262  C  CB    B ARG A 1 84  ? -15.806 -25.291 21.899  0.80 48.12  ? 84  ARG A CB    1 
ATOM   1263  C  CG    A ARG A 1 84  ? -17.218 -26.048 20.996  0.20 48.42  ? 84  ARG A CG    1 
ATOM   1264  C  CG    B ARG A 1 84  ? -16.797 -26.426 21.701  0.80 49.92  ? 84  ARG A CG    1 
ATOM   1265  C  CD    A ARG A 1 84  ? -16.922 -27.510 20.711  0.20 53.16  ? 84  ARG A CD    1 
ATOM   1266  C  CD    B ARG A 1 84  ? -16.122 -27.766 21.891  0.80 56.32  ? 84  ARG A CD    1 
ATOM   1267  N  NE    A ARG A 1 84  ? -16.630 -28.242 21.937  0.20 56.68  ? 84  ARG A NE    1 
ATOM   1268  N  NE    B ARG A 1 84  ? -17.059 -28.881 21.895  0.80 59.99  ? 84  ARG A NE    1 
ATOM   1269  C  CZ    A ARG A 1 84  ? -16.392 -29.545 21.997  0.20 62.34  ? 84  ARG A CZ    1 
ATOM   1270  C  CZ    B ARG A 1 84  ? -16.817 -30.052 22.469  0.80 67.53  ? 84  ARG A CZ    1 
ATOM   1271  N  NH1   A ARG A 1 84  ? -16.412 -30.302 20.911  0.20 65.40  ? 84  ARG A NH1   1 
ATOM   1272  N  NH1   B ARG A 1 84  ? -15.685 -30.281 23.119  0.80 62.17  ? 84  ARG A NH1   1 
ATOM   1273  N  NH2   A ARG A 1 84  ? -16.127 -30.103 23.175  0.20 61.87  ? 84  ARG A NH2   1 
ATOM   1274  N  NH2   B ARG A 1 84  ? -17.734 -31.014 22.395  0.80 71.61  ? 84  ARG A NH2   1 
ATOM   1275  N  N     A GLN A 1 85  ? -18.803 -24.292 23.203  0.20 47.62  ? 85  GLN A N     1 
ATOM   1276  N  N     B GLN A 1 85  ? -18.618 -24.514 23.305  0.80 48.85  ? 85  GLN A N     1 
ATOM   1277  C  CA    A GLN A 1 85  ? -20.206 -23.932 23.062  0.20 44.76  ? 85  GLN A CA    1 
ATOM   1278  C  CA    B GLN A 1 85  ? -20.023 -24.193 23.102  0.80 44.93  ? 85  GLN A CA    1 
ATOM   1279  C  C     A GLN A 1 85  ? -20.579 -22.692 23.861  0.20 41.86  ? 85  GLN A C     1 
ATOM   1280  C  C     B GLN A 1 85  ? -20.443 -22.936 23.843  0.80 42.25  ? 85  GLN A C     1 
ATOM   1281  O  O     A GLN A 1 85  ? -21.731 -22.250 23.793  0.20 38.29  ? 85  GLN A O     1 
ATOM   1282  O  O     B GLN A 1 85  ? -21.568 -22.461 23.642  0.80 37.99  ? 85  GLN A O     1 
ATOM   1283  C  CB    A GLN A 1 85  ? -21.094 -25.102 23.499  0.20 45.05  ? 85  GLN A CB    1 
ATOM   1284  C  CB    B GLN A 1 85  ? -20.898 -25.374 23.528  0.80 43.14  ? 85  GLN A CB    1 
ATOM   1285  C  CG    A GLN A 1 85  ? -20.628 -26.458 23.002  0.20 50.04  ? 85  GLN A CG    1 
ATOM   1286  C  CG    B GLN A 1 85  ? -20.844 -26.547 22.563  0.80 49.01  ? 85  GLN A CG    1 
ATOM   1287  C  CD    A GLN A 1 85  ? -21.378 -27.604 23.651  0.20 59.63  ? 85  GLN A CD    1 
ATOM   1288  C  CD    B GLN A 1 85  ? -21.848 -27.629 22.895  0.80 66.62  ? 85  GLN A CD    1 
ATOM   1289  O  OE1   A GLN A 1 85  ? -20.787 -28.623 24.012  0.20 53.91  ? 85  GLN A OE1   1 
ATOM   1290  O  OE1   B GLN A 1 85  ? -22.629 -27.497 23.838  0.80 65.79  ? 85  GLN A OE1   1 
ATOM   1291  N  NE2   A GLN A 1 85  ? -22.688 -27.445 23.802  0.20 65.55  ? 85  GLN A NE2   1 
ATOM   1292  N  NE2   B GLN A 1 85  ? -21.834 -28.711 22.116  0.80 62.37  ? 85  GLN A NE2   1 
ATOM   1293  N  N     A LEU A 1 86  ? -19.633 -22.117 24.605  0.20 39.09  ? 86  LEU A N     1 
ATOM   1294  N  N     B LEU A 1 86  ? -19.568 -22.386 24.682  0.80 37.96  ? 86  LEU A N     1 
ATOM   1295  C  CA    A LEU A 1 86  ? -19.964 -21.062 25.556  0.20 40.96  ? 86  LEU A CA    1 
ATOM   1296  C  CA    B LEU A 1 86  ? -19.943 -21.229 25.484  0.80 42.03  ? 86  LEU A CA    1 
ATOM   1297  C  C     A LEU A 1 86  ? -20.024 -19.692 24.887  0.20 32.36  ? 86  LEU A C     1 
ATOM   1298  C  C     B LEU A 1 86  ? -20.005 -19.965 24.632  0.80 31.82  ? 86  LEU A C     1 
ATOM   1299  O  O     A LEU A 1 86  ? -21.032 -18.987 24.994  0.20 31.58  ? 86  LEU A O     1 
ATOM   1300  O  O     B LEU A 1 86  ? -20.961 -19.193 24.725  0.80 28.56  ? 86  LEU A O     1 
ATOM   1301  C  CB    A LEU A 1 86  ? -18.946 -21.059 26.697  0.20 37.62  ? 86  LEU A CB    1 
ATOM   1302  C  CB    B LEU A 1 86  ? -18.955 -21.061 26.639  0.80 37.48  ? 86  LEU A CB    1 
ATOM   1303  C  CG    A LEU A 1 86  ? -19.256 -20.175 27.904  0.20 37.13  ? 86  LEU A CG    1 
ATOM   1304  C  CG    B LEU A 1 86  ? -19.375 -20.185 27.814  0.80 36.85  ? 86  LEU A CG    1 
ATOM   1305  C  CD1   A LEU A 1 86  ? -20.445 -20.720 28.688  0.20 39.43  ? 86  LEU A CD1   1 
ATOM   1306  C  CD1   B LEU A 1 86  ? -20.470 -20.866 28.641  0.80 39.36  ? 86  LEU A CD1   1 
ATOM   1307  C  CD2   A LEU A 1 86  ? -18.031 -20.041 28.795  0.20 37.37  ? 86  LEU A CD2   1 
ATOM   1308  C  CD2   B LEU A 1 86  ? -18.157 -19.875 28.672  0.80 36.89  ? 86  LEU A CD2   1 
ATOM   1309  N  N     A PHE A 1 87  ? -18.958 -19.301 24.194  0.20 35.62  ? 87  PHE A N     1 
ATOM   1310  N  N     B PHE A 1 87  ? -18.997 -19.743 23.790  0.80 36.90  ? 87  PHE A N     1 
ATOM   1311  C  CA    A PHE A 1 87  ? -18.853 -17.953 23.660  0.20 28.22  ? 87  PHE A CA    1 
ATOM   1312  C  CA    B PHE A 1 87  ? -18.866 -18.490 23.056  0.80 26.87  ? 87  PHE A CA    1 
ATOM   1313  C  C     A PHE A 1 87  ? -19.609 -17.824 22.340  0.20 32.28  ? 87  PHE A C     1 
ATOM   1314  C  C     B PHE A 1 87  ? -19.593 -18.550 21.721  0.80 33.85  ? 87  PHE A C     1 
ATOM   1315  O  O     A PHE A 1 87  ? -19.989 -18.811 21.705  0.20 34.55  ? 87  PHE A O     1 
ATOM   1316  O  O     B PHE A 1 87  ? -19.662 -19.598 21.077  0.80 41.88  ? 87  PHE A O     1 
ATOM   1317  C  CB    A PHE A 1 87  ? -17.385 -17.571 23.463  0.20 31.24  ? 87  PHE A CB    1 
ATOM   1318  C  CB    B PHE A 1 87  ? -17.382 -18.158 22.815  0.80 25.71  ? 87  PHE A CB    1 
ATOM   1319  C  CG    A PHE A 1 87  ? -16.539 -17.778 24.684  0.20 30.29  ? 87  PHE A CG    1 
ATOM   1320  C  CG    B PHE A 1 87  ? -16.577 -18.078 24.076  0.80 28.14  ? 87  PHE A CG    1 
ATOM   1321  C  CD1   A PHE A 1 87  ? -16.489 -16.817 25.678  0.20 29.82  ? 87  PHE A CD1   1 
ATOM   1322  C  CD1   B PHE A 1 87  ? -16.605 -16.940 24.857  0.80 32.99  ? 87  PHE A CD1   1 
ATOM   1323  C  CD2   A PHE A 1 87  ? -15.796 -18.937 24.840  0.20 31.42  ? 87  PHE A CD2   1 
ATOM   1324  C  CD2   B PHE A 1 87  ? -15.813 -19.157 24.496  0.80 31.14  ? 87  PHE A CD2   1 
ATOM   1325  C  CE1   A PHE A 1 87  ? -15.711 -17.006 26.803  0.20 32.28  ? 87  PHE A CE1   1 
ATOM   1326  C  CE1   B PHE A 1 87  ? -15.874 -16.867 26.020  0.80 30.75  ? 87  PHE A CE1   1 
ATOM   1327  C  CE2   A PHE A 1 87  ? -15.018 -19.134 25.962  0.20 34.14  ? 87  PHE A CE2   1 
ATOM   1328  C  CE2   B PHE A 1 87  ? -15.081 -19.094 25.659  0.80 33.97  ? 87  PHE A CE2   1 
ATOM   1329  C  CZ    A PHE A 1 87  ? -14.975 -18.168 26.946  0.20 31.72  ? 87  PHE A CZ    1 
ATOM   1330  C  CZ    B PHE A 1 87  ? -15.106 -17.947 26.423  0.80 33.28  ? 87  PHE A CZ    1 
ATOM   1331  N  N     A HIS A 1 88  ? -19.829 -16.578 21.932  0.20 32.32  ? 88  HIS A N     1 
ATOM   1332  N  N     B HIS A 1 88  ? -20.140 -17.409 21.317  0.80 29.11  ? 88  HIS A N     1 
ATOM   1333  C  CA    A HIS A 1 88  ? -20.405 -16.316 20.620  0.20 37.48  ? 88  HIS A CA    1 
ATOM   1334  C  CA    B HIS A 1 88  ? -20.595 -17.238 19.947  0.80 38.85  ? 88  HIS A CA    1 
ATOM   1335  C  C     A HIS A 1 88  ? -19.430 -16.772 19.541  0.20 36.82  ? 88  HIS A C     1 
ATOM   1336  C  C     B HIS A 1 88  ? -19.405 -17.380 18.999  0.80 37.16  ? 88  HIS A C     1 
ATOM   1337  O  O     A HIS A 1 88  ? -18.258 -16.378 19.570  0.20 34.72  ? 88  HIS A O     1 
ATOM   1338  O  O     B HIS A 1 88  ? -18.340 -16.809 19.259  0.80 36.51  ? 88  HIS A O     1 
ATOM   1339  C  CB    A HIS A 1 88  ? -20.710 -14.830 20.445  0.20 38.50  ? 88  HIS A CB    1 
ATOM   1340  C  CB    B HIS A 1 88  ? -21.215 -15.853 19.747  0.80 43.97  ? 88  HIS A CB    1 
ATOM   1341  C  CG    A HIS A 1 88  ? -21.840 -14.332 21.291  0.20 42.32  ? 88  HIS A CG    1 
ATOM   1342  C  CG    B HIS A 1 88  ? -22.464 -15.605 20.534  0.80 51.05  ? 88  HIS A CG    1 
ATOM   1343  N  ND1   A HIS A 1 88  ? -23.151 -14.702 21.077  0.20 46.35  ? 88  HIS A ND1   1 
ATOM   1344  N  ND1   B HIS A 1 88  ? -22.674 -14.435 21.235  0.80 47.92  ? 88  HIS A ND1   1 
ATOM   1345  C  CD2   A HIS A 1 88  ? -21.858 -13.473 22.337  0.20 36.60  ? 88  HIS A CD2   1 
ATOM   1346  C  CD2   B HIS A 1 88  ? -23.583 -16.349 20.699  0.80 49.62  ? 88  HIS A CD2   1 
ATOM   1347  C  CE1   A HIS A 1 88  ? -23.925 -14.103 21.964  0.20 45.72  ? 88  HIS A CE1   1 
ATOM   1348  C  CE1   B HIS A 1 88  ? -23.861 -14.478 21.813  0.80 47.04  ? 88  HIS A CE1   1 
ATOM   1349  N  NE2   A HIS A 1 88  ? -23.166 -13.350 22.739  0.20 38.99  ? 88  HIS A NE2   1 
ATOM   1350  N  NE2   B HIS A 1 88  ? -24.431 -15.631 21.509  0.80 50.01  ? 88  HIS A NE2   1 
ATOM   1351  N  N     A PRO A 1 89  ? -19.863 -17.593 18.581  0.20 37.50  ? 89  PRO A N     1 
ATOM   1352  N  N     B PRO A 1 89  ? -19.548 -18.104 17.887  0.80 37.70  ? 89  PRO A N     1 
ATOM   1353  C  CA    A PRO A 1 89  ? -18.935 -18.019 17.521  0.20 36.11  ? 89  PRO A CA    1 
ATOM   1354  C  CA    B PRO A 1 89  ? -18.426 -18.184 16.938  0.80 35.62  ? 89  PRO A CA    1 
ATOM   1355  C  C     A PRO A 1 89  ? -18.447 -16.875 16.653  0.20 33.01  ? 89  PRO A C     1 
ATOM   1356  C  C     B PRO A 1 89  ? -17.980 -16.829 16.422  0.80 30.27  ? 89  PRO A C     1 
ATOM   1357  O  O     A PRO A 1 89  ? -17.330 -16.943 16.126  0.20 31.29  ? 89  PRO A O     1 
ATOM   1358  O  O     B PRO A 1 89  ? -16.776 -16.600 16.277  0.80 31.92  ? 89  PRO A O     1 
ATOM   1359  C  CB    A PRO A 1 89  ? -19.764 -19.030 16.715  0.20 39.24  ? 89  PRO A CB    1 
ATOM   1360  C  CB    B PRO A 1 89  ? -18.981 -19.069 15.812  0.80 42.42  ? 89  PRO A CB    1 
ATOM   1361  C  CG    A PRO A 1 89  ? -21.183 -18.661 16.991  0.20 39.42  ? 89  PRO A CG    1 
ATOM   1362  C  CG    B PRO A 1 89  ? -20.056 -19.881 16.456  0.80 36.16  ? 89  PRO A CG    1 
ATOM   1363  C  CD    A PRO A 1 89  ? -21.206 -18.173 18.412  0.20 36.58  ? 89  PRO A CD    1 
ATOM   1364  C  CD    B PRO A 1 89  ? -20.673 -18.973 17.494  0.80 40.31  ? 89  PRO A CD    1 
ATOM   1365  N  N     A GLU A 1 90  ? -19.244 -15.816 16.497  0.20 33.42  ? 90  GLU A N     1 
ATOM   1366  N  N     B GLU A 1 90  ? -18.912 -15.911 16.172  0.80 32.73  ? 90  GLU A N     1 
ATOM   1367  C  CA    A GLU A 1 90  ? -18.839 -14.688 15.670  0.20 34.14  ? 90  GLU A CA    1 
ATOM   1368  C  CA    B GLU A 1 90  ? -18.557 -14.629 15.574  0.80 33.72  ? 90  GLU A CA    1 
ATOM   1369  C  C     A GLU A 1 90  ? -17.882 -13.742 16.386  0.20 32.94  ? 90  GLU A C     1 
ATOM   1370  C  C     B GLU A 1 90  ? -17.795 -13.712 16.523  0.80 32.98  ? 90  GLU A C     1 
ATOM   1371  O  O     A GLU A 1 90  ? -17.239 -12.920 15.725  0.20 32.04  ? 90  GLU A O     1 
ATOM   1372  O  O     B GLU A 1 90  ? -17.302 -12.672 16.074  0.80 32.21  ? 90  GLU A O     1 
ATOM   1373  C  CB    A GLU A 1 90  ? -20.069 -13.908 15.196  0.20 34.20  ? 90  GLU A CB    1 
ATOM   1374  C  CB    B GLU A 1 90  ? -19.809 -13.901 15.079  0.80 33.59  ? 90  GLU A CB    1 
ATOM   1375  C  CG    A GLU A 1 90  ? -20.854 -13.221 16.305  0.20 37.00  ? 90  GLU A CG    1 
ATOM   1376  C  CG    B GLU A 1 90  ? -20.653 -13.293 16.183  0.80 37.01  ? 90  GLU A CG    1 
ATOM   1377  C  CD    A GLU A 1 90  ? -21.887 -14.126 16.950  0.20 38.85  ? 90  GLU A CD    1 
ATOM   1378  C  CD    B GLU A 1 90  ? -21.715 -14.241 16.675  0.80 36.90  ? 90  GLU A CD    1 
ATOM   1379  O  OE1   A GLU A 1 90  ? -21.683 -15.357 16.963  0.20 42.18  ? 90  GLU A OE1   1 
ATOM   1380  O  OE1   B GLU A 1 90  ? -21.506 -15.469 16.566  0.80 46.09  ? 90  GLU A OE1   1 
ATOM   1381  O  OE2   A GLU A 1 90  ? -22.911 -13.605 17.439  0.20 47.04  ? 90  GLU A OE2   1 
ATOM   1382  O  OE2   B GLU A 1 90  ? -22.769 -13.768 17.150  0.80 48.86  ? 90  GLU A OE2   1 
ATOM   1383  N  N     A GLN A 1 91  ? -17.772 -13.831 17.709  0.20 28.11  ? 91  GLN A N     1 
ATOM   1384  N  N     B GLN A 1 91  ? -17.696 -14.047 17.812  0.80 25.77  ? 91  GLN A N     1 
ATOM   1385  C  CA    A GLN A 1 91  ? -16.856 -12.986 18.461  0.20 29.32  ? 91  GLN A CA    1 
ATOM   1386  C  CA    B GLN A 1 91  ? -16.896 -13.257 18.732  0.80 27.74  ? 91  GLN A CA    1 
ATOM   1387  C  C     A GLN A 1 91  ? -15.480 -13.620 18.634  0.20 29.02  ? 91  GLN A C     1 
ATOM   1388  C  C     B GLN A 1 91  ? -15.502 -13.848 18.939  0.80 29.11  ? 91  GLN A C     1 
ATOM   1389  O  O     A GLN A 1 91  ? -14.644 -13.072 19.360  0.20 26.64  ? 91  GLN A O     1 
ATOM   1390  O  O     B GLN A 1 91  ? -14.791 -13.447 19.865  0.80 27.34  ? 91  GLN A O     1 
ATOM   1391  C  CB    A GLN A 1 91  ? -17.453 -12.642 19.829  0.20 33.27  ? 91  GLN A CB    1 
ATOM   1392  C  CB    B GLN A 1 91  ? -17.628 -13.074 20.064  0.80 36.10  ? 91  GLN A CB    1 
ATOM   1393  C  CG    A GLN A 1 91  ? -18.752 -11.840 19.761  0.20 35.10  ? 91  GLN A CG    1 
ATOM   1394  C  CG    B GLN A 1 91  ? -18.873 -12.159 19.972  0.80 35.14  ? 91  GLN A CG    1 
ATOM   1395  C  CD    A GLN A 1 91  ? -18.583 -10.480 19.096  0.20 38.53  ? 91  GLN A CD    1 
ATOM   1396  C  CD    B GLN A 1 91  ? -18.647 -10.868 19.152  0.80 40.95  ? 91  GLN A CD    1 
ATOM   1397  O  OE1   A GLN A 1 91  ? -17.485 -9.918  19.066  0.20 34.51  ? 91  GLN A OE1   1 
ATOM   1398  O  OE1   B GLN A 1 91  ? -17.544 -10.295 19.123  0.80 38.02  ? 91  GLN A OE1   1 
ATOM   1399  N  NE2   A GLN A 1 91  ? -19.675 -9.946  18.560  0.20 38.58  ? 91  GLN A NE2   1 
ATOM   1400  N  NE2   B GLN A 1 91  ? -19.707 -10.408 18.486  0.80 42.10  ? 91  GLN A NE2   1 
ATOM   1401  N  N     A LEU A 1 92  ? -15.228 -14.757 17.988  0.20 26.01  ? 92  LEU A N     1 
ATOM   1402  N  N     B LEU A 1 92  ? -15.086 -14.767 18.073  0.80 25.13  ? 92  LEU A N     1 
ATOM   1403  C  CA    A LEU A 1 92  ? -13.914 -15.399 17.995  0.20 26.94  ? 92  LEU A CA    1 
ATOM   1404  C  CA    B LEU A 1 92  ? -13.707 -15.247 18.022  0.80 26.28  ? 92  LEU A CA    1 
ATOM   1405  C  C     A LEU A 1 92  ? -13.285 -15.119 16.634  0.20 28.24  ? 92  LEU A C     1 
ATOM   1406  C  C     B LEU A 1 92  ? -13.173 -14.910 16.636  0.80 28.30  ? 92  LEU A C     1 
ATOM   1407  O  O     A LEU A 1 92  ? -13.450 -15.883 15.683  0.20 28.14  ? 92  LEU A O     1 
ATOM   1408  O  O     B LEU A 1 92  ? -13.610 -15.509 15.646  0.80 26.56  ? 92  LEU A O     1 
ATOM   1409  C  CB    A LEU A 1 92  ? -14.033 -16.893 18.271  0.20 29.63  ? 92  LEU A CB    1 
ATOM   1410  C  CB    B LEU A 1 92  ? -13.641 -16.746 18.288  0.80 27.94  ? 92  LEU A CB    1 
ATOM   1411  C  CG    A LEU A 1 92  ? -14.959 -17.289 19.422  0.20 26.84  ? 92  LEU A CG    1 
ATOM   1412  C  CG    B LEU A 1 92  ? -14.438 -17.187 19.516  0.80 26.52  ? 92  LEU A CG    1 
ATOM   1413  C  CD1   A LEU A 1 92  ? -14.892 -18.787 19.666  0.20 33.34  ? 92  LEU A CD1   1 
ATOM   1414  C  CD1   B LEU A 1 92  ? -14.827 -18.638 19.407  0.80 33.50  ? 92  LEU A CD1   1 
ATOM   1415  C  CD2   A LEU A 1 92  ? -14.617 -16.516 20.685  0.20 29.55  ? 92  LEU A CD2   1 
ATOM   1416  C  CD2   B LEU A 1 92  ? -13.587 -16.951 20.751  0.80 32.34  ? 92  LEU A CD2   1 
ATOM   1417  N  N     A ILE A 1 93  ? -12.563 -14.005 16.544  0.20 26.11  ? 93  ILE A N     1 
ATOM   1418  N  N     B ILE A 1 93  ? -12.241 -13.956 16.559  0.80 24.04  ? 93  ILE A N     1 
ATOM   1419  C  CA    A ILE A 1 93  ? -12.063 -13.490 15.275  0.20 26.40  ? 93  ILE A CA    1 
ATOM   1420  C  CA    B ILE A 1 93  ? -11.845 -13.343 15.292  0.80 26.41  ? 93  ILE A CA    1 
ATOM   1421  C  C     A ILE A 1 93  ? -10.585 -13.835 15.150  0.20 28.37  ? 93  ILE A C     1 
ATOM   1422  C  C     B ILE A 1 93  ? -10.354 -13.567 15.064  0.80 29.11  ? 93  ILE A C     1 
ATOM   1423  O  O     A ILE A 1 93  ? -9.783  -13.508 16.035  0.20 26.13  ? 93  ILE A O     1 
ATOM   1424  O  O     B ILE A 1 93  ? -9.542  -13.305 15.960  0.80 25.03  ? 93  ILE A O     1 
ATOM   1425  C  CB    A ILE A 1 93  ? -12.296 -11.974 15.168  0.20 26.93  ? 93  ILE A CB    1 
ATOM   1426  C  CB    B ILE A 1 93  ? -12.174 -11.838 15.278  0.80 26.57  ? 93  ILE A CB    1 
ATOM   1427  C  CG1   A ILE A 1 93  ? -13.743 -11.637 15.546  0.20 30.97  ? 93  ILE A CG1   1 
ATOM   1428  C  CG1   B ILE A 1 93  ? -13.647 -11.610 15.648  0.80 31.35  ? 93  ILE A CG1   1 
ATOM   1429  C  CG2   A ILE A 1 93  ? -12.003 -11.491 13.765  0.20 29.33  ? 93  ILE A CG2   1 
ATOM   1430  C  CG2   B ILE A 1 93  ? -11.820 -11.222 13.925  0.80 29.31  ? 93  ILE A CG2   1 
ATOM   1431  C  CD1   A ILE A 1 93  ? -14.083 -10.166 15.432  0.20 29.69  ? 93  ILE A CD1   1 
ATOM   1432  C  CD1   B ILE A 1 93  ? -13.889 -10.280 16.311  0.80 27.12  ? 93  ILE A CD1   1 
ATOM   1433  N  N     A THR A 1 94  ? -10.222 -14.503 14.056  0.20 26.88  ? 94  THR A N     1 
ATOM   1434  N  N     B THR A 1 94  ? -9.990  -14.033 13.864  0.80 26.70  ? 94  THR A N     1 
ATOM   1435  C  CA    A THR A 1 94  ? -8.850  -14.936 13.822  0.20 29.68  ? 94  THR A CA    1 
ATOM   1436  C  CA    B THR A 1 94  ? -8.588  -14.301 13.551  0.80 25.97  ? 94  THR A CA    1 
ATOM   1437  C  C     A THR A 1 94  ? -8.420  -14.536 12.421  0.20 26.22  ? 94  THR A C     1 
ATOM   1438  C  C     B THR A 1 94  ? -8.225  -13.791 12.162  0.80 28.11  ? 94  THR A C     1 
ATOM   1439  O  O     A THR A 1 94  ? -9.153  -14.768 11.454  0.20 26.80  ? 94  THR A O     1 
ATOM   1440  O  O     B THR A 1 94  ? -9.043  -13.811 11.235  0.80 26.91  ? 94  THR A O     1 
ATOM   1441  C  CB    A THR A 1 94  ? -8.701  -16.454 13.986  0.20 31.86  ? 94  THR A CB    1 
ATOM   1442  C  CB    B THR A 1 94  ? -8.248  -15.798 13.614  0.80 33.91  ? 94  THR A CB    1 
ATOM   1443  O  OG1   A THR A 1 94  ? -9.486  -17.125 12.993  0.20 31.71  ? 94  THR A OG1   1 
ATOM   1444  O  OG1   B THR A 1 94  ? -9.096  -16.527 12.715  0.80 32.45  ? 94  THR A OG1   1 
ATOM   1445  C  CG2   A THR A 1 94  ? -9.156  -16.893 15.360  0.20 33.63  ? 94  THR A CG2   1 
ATOM   1446  C  CG2   B THR A 1 94  ? -8.422  -16.340 15.020  0.80 34.44  ? 94  THR A CG2   1 
ATOM   1447  N  N     A GLY A 1 95  ? -7.238  -13.939 12.315  0.20 28.81  ? 95  GLY A N     1 
ATOM   1448  N  N     B GLY A 1 95  ? -6.985  -13.321 12.038  0.80 28.24  ? 95  GLY A N     1 
ATOM   1449  C  CA    A GLY A 1 95  ? -6.615  -13.668 11.037  0.20 29.82  ? 95  GLY A CA    1 
ATOM   1450  C  CA    B GLY A 1 95  ? -6.337  -13.122 10.754  0.80 26.21  ? 95  GLY A CA    1 
ATOM   1451  C  C     A GLY A 1 95  ? -5.818  -14.860 10.553  0.20 31.94  ? 95  GLY A C     1 
ATOM   1452  C  C     B GLY A 1 95  ? -5.522  -14.348 10.375  0.80 32.12  ? 95  GLY A C     1 
ATOM   1453  O  O     A GLY A 1 95  ? -6.050  -16.002 10.956  0.20 33.52  ? 95  GLY A O     1 
ATOM   1454  O  O     B GLY A 1 95  ? -5.703  -15.435 10.930  0.80 31.95  ? 95  GLY A O     1 
ATOM   1455  N  N     A LYS A 1 96  ? -4.856  -14.587 9.679   0.20 30.20  ? 96  LYS A N     1 
ATOM   1456  N  N     B LYS A 1 96  ? -4.607  -14.175 9.417   0.80 26.12  ? 96  LYS A N     1 
ATOM   1457  C  CA    A LYS A 1 96  ? -4.005  -15.639 9.134   0.20 31.41  ? 96  LYS A CA    1 
ATOM   1458  C  CA    B LYS A 1 96  ? -3.807  -15.306 8.943   0.80 28.30  ? 96  LYS A CA    1 
ATOM   1459  C  C     A LYS A 1 96  ? -2.532  -15.448 9.452   0.20 33.65  ? 96  LYS A C     1 
ATOM   1460  C  C     B LYS A 1 96  ? -2.304  -15.106 9.113   0.80 36.29  ? 96  LYS A C     1 
ATOM   1461  O  O     A LYS A 1 96  ? -1.839  -16.423 9.751   0.20 37.94  ? 96  LYS A O     1 
ATOM   1462  O  O     B LYS A 1 96  ? -1.523  -15.973 8.699   0.80 37.49  ? 96  LYS A O     1 
ATOM   1463  C  CB    A LYS A 1 96  ? -4.188  -15.732 7.611   0.20 39.04  ? 96  LYS A CB    1 
ATOM   1464  C  CB    B LYS A 1 96  ? -4.120  -15.616 7.473   0.80 39.20  ? 96  LYS A CB    1 
ATOM   1465  C  CG    A LYS A 1 96  ? -5.643  -15.761 7.170   0.20 41.96  ? 96  LYS A CG    1 
ATOM   1466  C  CG    B LYS A 1 96  ? -5.417  -16.402 7.283   0.80 42.99  ? 96  LYS A CG    1 
ATOM   1467  C  CD    A LYS A 1 96  ? -5.781  -16.119 5.699   0.20 46.24  ? 96  LYS A CD    1 
ATOM   1468  C  CD    B LYS A 1 96  ? -5.424  -17.245 6.007   0.80 50.48  ? 96  LYS A CD    1 
ATOM   1469  C  CE    A LYS A 1 96  ? -5.465  -17.585 5.461   0.20 47.42  ? 96  LYS A CE    1 
ATOM   1470  C  CE    B LYS A 1 96  ? -5.183  -16.400 4.766   0.80 45.35  ? 96  LYS A CE    1 
ATOM   1471  N  NZ    A LYS A 1 96  ? -6.364  -18.479 6.245   0.20 42.69  ? 96  LYS A NZ    1 
ATOM   1472  N  NZ    B LYS A 1 96  ? -6.101  -15.220 4.686   0.80 49.39  ? 96  LYS A NZ    1 
ATOM   1473  N  N     A GLU A 1 97  ? -2.035  -14.216 9.395   0.20 32.02  ? 97  GLU A N     1 
ATOM   1474  N  N     B GLU A 1 97  ? -1.876  -14.008 9.727   0.80 29.82  ? 97  GLU A N     1 
ATOM   1475  C  CA    A GLU A 1 97  ? -0.627  -13.910 9.613   0.20 32.39  ? 97  GLU A CA    1 
ATOM   1476  C  CA    B GLU A 1 97  ? -0.467  -13.624 9.715   0.80 31.22  ? 97  GLU A CA    1 
ATOM   1477  C  C     A GLU A 1 97  ? -0.520  -12.998 10.825  0.20 32.39  ? 97  GLU A C     1 
ATOM   1478  C  C     B GLU A 1 97  ? -0.271  -12.628 10.842  0.80 32.76  ? 97  GLU A C     1 
ATOM   1479  O  O     A GLU A 1 97  ? -1.126  -11.921 10.848  0.20 31.75  ? 97  GLU A O     1 
ATOM   1480  O  O     B GLU A 1 97  ? -0.990  -11.625 10.902  0.80 32.20  ? 97  GLU A O     1 
ATOM   1481  C  CB    A GLU A 1 97  ? -0.024  -13.253 8.369   0.20 35.33  ? 97  GLU A CB    1 
ATOM   1482  C  CB    B GLU A 1 97  ? -0.102  -13.020 8.361   0.80 34.87  ? 97  GLU A CB    1 
ATOM   1483  C  CG    A GLU A 1 97  ? 1.465   -12.995 8.442   0.20 38.18  ? 97  GLU A CG    1 
ATOM   1484  C  CG    B GLU A 1 97  ? 1.243   -12.358 8.297   0.80 42.88  ? 97  GLU A CG    1 
ATOM   1485  C  CD    A GLU A 1 97  ? 2.015   -12.445 7.139   0.20 42.10  ? 97  GLU A CD    1 
ATOM   1486  C  CD    B GLU A 1 97  ? 1.549   -11.821 6.905   0.80 39.68  ? 97  GLU A CD    1 
ATOM   1487  O  OE1   A GLU A 1 97  ? 1.710   -13.020 6.073   0.20 41.50  ? 97  GLU A OE1   1 
ATOM   1488  O  OE1   B GLU A 1 97  ? 0.593   -11.454 6.183   0.80 41.28  ? 97  GLU A OE1   1 
ATOM   1489  O  OE2   A GLU A 1 97  ? 2.744   -11.432 7.181   0.20 43.15  ? 97  GLU A OE2   1 
ATOM   1490  O  OE2   B GLU A 1 97  ? 2.740   -11.779 6.533   0.80 49.46  ? 97  GLU A OE2   1 
ATOM   1491  N  N     A ASP A 1 98  ? 0.236   -13.428 11.831  0.20 29.55  ? 98  ASP A N     1 
ATOM   1492  N  N     B ASP A 1 98  ? 0.660   -12.905 11.749  0.80 27.93  ? 98  ASP A N     1 
ATOM   1493  C  CA    A ASP A 1 98  ? 0.310   -12.683 13.081  0.20 29.38  ? 98  ASP A CA    1 
ATOM   1494  C  CA    B ASP A 1 98  ? 0.696   -12.125 12.979  0.80 31.86  ? 98  ASP A CA    1 
ATOM   1495  C  C     A ASP A 1 98  ? 1.266   -11.501 12.920  0.20 27.75  ? 98  ASP A C     1 
ATOM   1496  C  C     B ASP A 1 98  ? 1.572   -10.886 12.819  0.80 27.67  ? 98  ASP A C     1 
ATOM   1497  O  O     A ASP A 1 98  ? 1.743   -11.197 11.823  0.20 31.26  ? 98  ASP A O     1 
ATOM   1498  O  O     B ASP A 1 98  ? 1.984   -10.507 11.713  0.80 30.64  ? 98  ASP A O     1 
ATOM   1499  C  CB    A ASP A 1 98  ? 0.694   -13.608 14.234  0.20 28.88  ? 98  ASP A CB    1 
ATOM   1500  C  CB    B ASP A 1 98  ? 1.125   -12.974 14.178  0.80 27.74  ? 98  ASP A CB    1 
ATOM   1501  C  CG    A ASP A 1 98  ? 2.107   -14.156 14.120  0.20 29.18  ? 98  ASP A CG    1 
ATOM   1502  C  CG    B ASP A 1 98  ? 2.543   -13.530 14.078  0.80 29.38  ? 98  ASP A CG    1 
ATOM   1503  O  OD1   A ASP A 1 98  ? 2.791   -13.913 13.101  0.20 33.38  ? 98  ASP A OD1   1 
ATOM   1504  O  OD1   B ASP A 1 98  ? 3.493   -12.858 13.585  0.80 22.34  ? 98  ASP A OD1   1 
ATOM   1505  O  OD2   A ASP A 1 98  ? 2.535   -14.845 15.069  0.20 30.66  ? 98  ASP A OD2   1 
ATOM   1506  O  OD2   B ASP A 1 98  ? 2.710   -14.661 14.579  0.80 34.36  ? 98  ASP A OD2   1 
ATOM   1507  N  N     A ALA A 1 99  ? 1.562   -10.821 14.024  0.20 26.20  ? 99  ALA A N     1 
ATOM   1508  N  N     B ALA A 1 99  ? 1.846   -10.236 13.943  0.80 23.09  ? 99  ALA A N     1 
ATOM   1509  C  CA    A ALA A 1 99  ? 2.324   -9.581  13.992  0.20 22.39  ? 99  ALA A CA    1 
ATOM   1510  C  CA    B ALA A 1 99  ? 2.564   -8.981  13.978  0.80 19.35  ? 99  ALA A CA    1 
ATOM   1511  C  C     A ALA A 1 99  ? 3.830   -9.793  14.058  0.20 24.76  ? 99  ALA A C     1 
ATOM   1512  C  C     B ALA A 1 99  ? 4.061   -9.167  14.182  0.80 22.85  ? 99  ALA A C     1 
ATOM   1513  O  O     A ALA A 1 99  ? 4.573   -8.808  14.039  0.20 26.33  ? 99  ALA A O     1 
ATOM   1514  O  O     B ALA A 1 99  ? 4.780   -8.172  14.287  0.80 30.85  ? 99  ALA A O     1 
ATOM   1515  C  CB    A ALA A 1 99  ? 1.883   -8.668  15.140  0.20 22.90  ? 99  ALA A CB    1 
ATOM   1516  C  CB    B ALA A 1 99  ? 1.976   -8.083  15.071  0.80 21.80  ? 99  ALA A CB    1 
ATOM   1517  N  N     A ALA A 1 100 ? 4.297   -11.043 14.130  0.20 25.75  ? 100 ALA A N     1 
ATOM   1518  N  N     B ALA A 1 100 ? 4.542   -10.410 14.213  0.80 26.03  ? 100 ALA A N     1 
ATOM   1519  C  CA    A ALA A 1 100 ? 5.729   -11.352 14.215  0.20 24.44  ? 100 ALA A CA    1 
ATOM   1520  C  CA    B ALA A 1 100 ? 5.973   -10.729 14.273  0.80 25.14  ? 100 ALA A CA    1 
ATOM   1521  C  C     A ALA A 1 100 ? 6.409   -10.588 15.351  0.20 26.88  ? 100 ALA A C     1 
ATOM   1522  C  C     B ALA A 1 100 ? 6.699   -9.963  15.385  0.80 28.20  ? 100 ALA A C     1 
ATOM   1523  O  O     A ALA A 1 100 ? 7.572   -10.187 15.236  0.20 26.39  ? 100 ALA A O     1 
ATOM   1524  O  O     B ALA A 1 100 ? 7.767   -9.380  15.177  0.80 24.41  ? 100 ALA A O     1 
ATOM   1525  C  CB    A ALA A 1 100 ? 6.433   -11.077 12.881  0.20 27.45  ? 100 ALA A CB    1 
ATOM   1526  C  CB    B ALA A 1 100 ? 6.637   -10.473 12.916  0.80 24.62  ? 100 ALA A CB    1 
ATOM   1527  N  N     A ASN A 1 101 ? 5.685   -10.385 16.456  0.20 24.06  ? 101 ASN A N     1 
ATOM   1528  N  N     B ASN A 1 101 ? 6.122   -9.985  16.588  0.80 24.11  ? 101 ASN A N     1 
ATOM   1529  C  CA    A ASN A 1 101 ? 6.179   -9.618  17.604  0.20 25.22  ? 101 ASN A CA    1 
ATOM   1530  C  CA    B ASN A 1 101 ? 6.717   -9.344  17.768  0.80 19.99  ? 101 ASN A CA    1 
ATOM   1531  C  C     A ASN A 1 101 ? 6.646   -8.227  17.181  0.20 25.02  ? 101 ASN A C     1 
ATOM   1532  C  C     B ASN A 1 101 ? 6.987   -7.851  17.545  0.80 28.23  ? 101 ASN A C     1 
ATOM   1533  O  O     A ASN A 1 101 ? 7.703   -7.751  17.603  0.20 26.78  ? 101 ASN A O     1 
ATOM   1534  O  O     B ASN A 1 101 ? 7.866   -7.271  18.201  0.80 24.91  ? 101 ASN A O     1 
ATOM   1535  C  CB    A ASN A 1 101 ? 7.293   -10.368 18.338  0.20 24.33  ? 101 ASN A CB    1 
ATOM   1536  C  CB    B ASN A 1 101 ? 8.020   -10.038 18.188  0.80 24.13  ? 101 ASN A CB    1 
ATOM   1537  C  CG    A ASN A 1 101 ? 6.938   -11.822 18.611  0.20 28.17  ? 101 ASN A CG    1 
ATOM   1538  C  CG    B ASN A 1 101 ? 7.838   -11.521 18.534  0.80 35.82  ? 101 ASN A CG    1 
ATOM   1539  O  OD1   A ASN A 1 101 ? 7.776   -12.712 18.478  0.20 28.82  ? 101 ASN A OD1   1 
ATOM   1540  O  OD1   B ASN A 1 101 ? 8.694   -12.350 18.227  0.80 29.47  ? 101 ASN A OD1   1 
ATOM   1541  N  ND2   A ASN A 1 101 ? 5.692   -12.066 18.989  0.20 30.43  ? 101 ASN A ND2   1 
ATOM   1542  N  ND2   B ASN A 1 101 ? 6.746   -11.848 19.197  0.80 28.19  ? 101 ASN A ND2   1 
ATOM   1543  N  N     A ASN A 1 102 ? 5.852   -7.571  16.335  0.20 23.43  ? 102 ASN A N     1 
ATOM   1544  N  N     B ASN A 1 102 ? 6.270   -7.215  16.613  0.80 25.31  ? 102 ASN A N     1 
ATOM   1545  C  CA    A ASN A 1 102 ? 6.186   -6.261  15.787  0.20 23.37  ? 102 ASN A CA    1 
ATOM   1546  C  CA    B ASN A 1 102 ? 6.587   -5.863  16.144  0.80 23.08  ? 102 ASN A CA    1 
ATOM   1547  C  C     A ASN A 1 102 ? 5.016   -5.316  16.020  0.20 23.60  ? 102 ASN A C     1 
ATOM   1548  C  C     B ASN A 1 102 ? 5.361   -4.973  16.347  0.80 22.14  ? 102 ASN A C     1 
ATOM   1549  O  O     A ASN A 1 102 ? 3.906   -5.569  15.539  0.20 23.65  ? 102 ASN A O     1 
ATOM   1550  O  O     B ASN A 1 102 ? 4.369   -5.100  15.618  0.80 25.37  ? 102 ASN A O     1 
ATOM   1551  C  CB    A ASN A 1 102 ? 6.519   -6.365  14.294  0.20 27.14  ? 102 ASN A CB    1 
ATOM   1552  C  CB    B ASN A 1 102 ? 7.036   -5.910  14.671  0.80 26.17  ? 102 ASN A CB    1 
ATOM   1553  C  CG    A ASN A 1 102 ? 7.159   -5.106  13.742  0.20 26.64  ? 102 ASN A CG    1 
ATOM   1554  C  CG    B ASN A 1 102 ? 7.400   -4.535  14.090  0.80 28.03  ? 102 ASN A CG    1 
ATOM   1555  O  OD1   A ASN A 1 102 ? 6.750   -3.989  14.061  0.20 24.22  ? 102 ASN A OD1   1 
ATOM   1556  O  OD1   B ASN A 1 102 ? 7.042   -3.480  14.617  0.80 22.14  ? 102 ASN A OD1   1 
ATOM   1557  N  ND2   A ASN A 1 102 ? 8.174   -5.285  12.904  0.20 27.83  ? 102 ASN A ND2   1 
ATOM   1558  N  ND2   B ASN A 1 102 ? 8.123   -4.558  12.967  0.80 30.96  ? 102 ASN A ND2   1 
ATOM   1559  N  N     A TYR A 1 103 ? 5.271   -4.225  16.749  0.20 24.46  ? 103 TYR A N     1 
ATOM   1560  N  N     B TYR A 1 103 ? 5.428   -4.086  17.352  0.80 21.63  ? 103 TYR A N     1 
ATOM   1561  C  CA    A TYR A 1 103 ? 4.215   -3.265  17.058  0.20 25.87  ? 103 TYR A CA    1 
ATOM   1562  C  CA    B TYR A 1 103 ? 4.368   -3.102  17.582  0.80 26.47  ? 103 TYR A CA    1 
ATOM   1563  C  C     A TYR A 1 103 ? 3.636   -2.644  15.792  0.20 25.55  ? 103 TYR A C     1 
ATOM   1564  C  C     B TYR A 1 103 ? 3.874   -2.449  16.294  0.80 25.37  ? 103 TYR A C     1 
ATOM   1565  O  O     A TYR A 1 103 ? 2.413   -2.527  15.652  0.20 25.13  ? 103 TYR A O     1 
ATOM   1566  O  O     B TYR A 1 103 ? 2.667   -2.269  16.097  0.80 25.18  ? 103 TYR A O     1 
ATOM   1567  C  CB    A TYR A 1 103 ? 4.756   -2.179  17.991  0.20 23.82  ? 103 TYR A CB    1 
ATOM   1568  C  CB    B TYR A 1 103 ? 4.862   -2.026  18.558  0.80 21.74  ? 103 TYR A CB    1 
ATOM   1569  C  CG    A TYR A 1 103 ? 3.799   -1.033  18.252  0.20 24.83  ? 103 TYR A CG    1 
ATOM   1570  C  CG    B TYR A 1 103 ? 3.915   -0.849  18.759  0.80 25.97  ? 103 TYR A CG    1 
ATOM   1571  C  CD1   A TYR A 1 103 ? 2.880   -1.092  19.293  0.20 25.13  ? 103 TYR A CD1   1 
ATOM   1572  C  CD1   B TYR A 1 103 ? 3.900   0.219   17.865  0.80 28.78  ? 103 TYR A CD1   1 
ATOM   1573  C  CD2   A TYR A 1 103 ? 3.826   0.115   17.467  0.20 27.51  ? 103 TYR A CD2   1 
ATOM   1574  C  CD2   B TYR A 1 103 ? 3.050   -0.799  19.859  0.80 23.74  ? 103 TYR A CD2   1 
ATOM   1575  C  CE1   A TYR A 1 103 ? 2.008   -0.043  19.538  0.20 25.38  ? 103 TYR A CE1   1 
ATOM   1576  C  CE1   B TYR A 1 103 ? 3.044   1.295   18.037  0.80 26.11  ? 103 TYR A CE1   1 
ATOM   1577  C  CE2   A TYR A 1 103 ? 2.956   1.166   17.704  0.20 26.99  ? 103 TYR A CE2   1 
ATOM   1578  C  CE2   B TYR A 1 103 ? 2.189   0.284   20.043  0.80 22.02  ? 103 TYR A CE2   1 
ATOM   1579  C  CZ    A TYR A 1 103 ? 2.051   1.081   18.740  0.20 29.53  ? 103 TYR A CZ    1 
ATOM   1580  C  CZ    B TYR A 1 103 ? 2.196   1.324   19.126  0.80 30.27  ? 103 TYR A CZ    1 
ATOM   1581  O  OH    A TYR A 1 103 ? 1.187   2.121   18.979  0.20 31.33  ? 103 TYR A OH    1 
ATOM   1582  O  OH    B TYR A 1 103 ? 1.369   2.397   19.277  0.80 33.87  ? 103 TYR A OH    1 
ATOM   1583  N  N     A ALA A 1 104 ? 4.500   -2.238  14.858  0.20 25.52  ? 104 ALA A N     1 
ATOM   1584  N  N     B ALA A 1 104 ? 4.795   -2.036  15.417  0.80 24.94  ? 104 ALA A N     1 
ATOM   1585  C  CA    A ALA A 1 104 ? 4.023   -1.559  13.657  0.20 26.97  ? 104 ALA A CA    1 
ATOM   1586  C  CA    B ALA A 1 104 ? 4.358   -1.301  14.237  0.80 25.57  ? 104 ALA A CA    1 
ATOM   1587  C  C     A ALA A 1 104 ? 3.159   -2.468  12.793  0.20 27.28  ? 104 ALA A C     1 
ATOM   1588  C  C     B ALA A 1 104 ? 3.505   -2.166  13.315  0.80 24.29  ? 104 ALA A C     1 
ATOM   1589  O  O     A ALA A 1 104 ? 2.272   -1.981  12.084  0.20 30.11  ? 104 ALA A O     1 
ATOM   1590  O  O     B ALA A 1 104 ? 2.561   -1.662  12.699  0.80 29.69  ? 104 ALA A O     1 
ATOM   1591  C  CB    A ALA A 1 104 ? 5.207   -1.026  12.851  0.20 27.69  ? 104 ALA A CB    1 
ATOM   1592  C  CB    B ALA A 1 104 ? 5.565   -0.728  13.484  0.80 27.81  ? 104 ALA A CB    1 
ATOM   1593  N  N     A ARG A 1 105 ? 3.402   -3.780  12.826  0.20 26.80  ? 105 ARG A N     1 
ATOM   1594  N  N     B ARG A 1 105 ? 3.802   -3.469  13.222  0.80 25.70  ? 105 ARG A N     1 
ATOM   1595  C  CA    A ARG A 1 105 ? 2.547   -4.702  12.085  0.20 27.55  ? 105 ARG A CA    1 
ATOM   1596  C  CA    B ARG A 1 105 ? 2.999   -4.361  12.386  0.80 26.38  ? 105 ARG A CA    1 
ATOM   1597  C  C     A ARG A 1 105 ? 1.177   -4.810  12.740  0.20 30.07  ? 105 ARG A C     1 
ATOM   1598  C  C     B ARG A 1 105 ? 1.599   -4.534  12.949  0.80 29.26  ? 105 ARG A C     1 
ATOM   1599  O  O     A ARG A 1 105 ? 0.145   -4.668  12.073  0.20 31.22  ? 105 ARG A O     1 
ATOM   1600  O  O     B ARG A 1 105 ? 0.624   -4.617  12.191  0.80 34.09  ? 105 ARG A O     1 
ATOM   1601  C  CB    A ARG A 1 105 ? 3.211   -6.076  11.984  0.20 26.83  ? 105 ARG A CB    1 
ATOM   1602  C  CB    B ARG A 1 105 ? 3.678   -5.725  12.254  0.80 27.25  ? 105 ARG A CB    1 
ATOM   1603  C  CG    A ARG A 1 105 ? 4.398   -6.116  11.033  0.20 32.36  ? 105 ARG A CG    1 
ATOM   1604  C  CG    B ARG A 1 105 ? 4.030   -6.122  10.829  0.80 34.68  ? 105 ARG A CG    1 
ATOM   1605  C  CD    A ARG A 1 105 ? 5.141   -7.441  11.097  0.20 31.73  ? 105 ARG A CD    1 
ATOM   1606  C  CD    B ARG A 1 105 ? 4.896   -7.369  10.769  0.80 32.89  ? 105 ARG A CD    1 
ATOM   1607  N  NE    A ARG A 1 105 ? 4.289   -8.583  10.784  0.20 29.36  ? 105 ARG A NE    1 
ATOM   1608  N  NE    B ARG A 1 105 ? 4.197   -8.461  10.102  0.80 31.18  ? 105 ARG A NE    1 
ATOM   1609  C  CZ    A ARG A 1 105 ? 4.067   -9.040  9.559   0.20 31.39  ? 105 ARG A CZ    1 
ATOM   1610  C  CZ    B ARG A 1 105 ? 4.073   -8.569  8.785   0.80 35.05  ? 105 ARG A CZ    1 
ATOM   1611  N  NH1   A ARG A 1 105 ? 4.596   -8.453  8.496   0.20 31.90  ? 105 ARG A NH1   1 
ATOM   1612  N  NH1   B ARG A 1 105 ? 4.623   -7.691  7.967   0.80 27.61  ? 105 ARG A NH1   1 
ATOM   1613  N  NH2   A ARG A 1 105 ? 3.299   -10.114 9.396   0.20 24.12  ? 105 ARG A NH2   1 
ATOM   1614  N  NH2   B ARG A 1 105 ? 3.372   -9.580  8.279   0.80 40.52  ? 105 ARG A NH2   1 
ATOM   1615  N  N     A GLY A 1 106 ? 1.149   -5.039  14.054  0.20 29.18  ? 106 GLY A N     1 
ATOM   1616  N  N     B GLY A 1 106 ? 1.476   -4.601  14.276  0.80 29.79  ? 106 GLY A N     1 
ATOM   1617  C  CA    A GLY A 1 106 ? -0.119  -5.122  14.757  0.20 27.44  ? 106 GLY A CA    1 
ATOM   1618  C  CA    B GLY A 1 106 ? 0.160   -4.728  14.876  0.80 27.16  ? 106 GLY A CA    1 
ATOM   1619  C  C     A GLY A 1 106 ? -0.923  -3.838  14.719  0.20 28.02  ? 106 GLY A C     1 
ATOM   1620  C  C     B GLY A 1 106 ? -0.643  -3.450  14.790  0.80 27.44  ? 106 GLY A C     1 
ATOM   1621  O  O     A GLY A 1 106 ? -2.157  -3.874  14.767  0.20 30.18  ? 106 GLY A O     1 
ATOM   1622  O  O     B GLY A 1 106 ? -1.863  -3.489  14.600  0.80 32.50  ? 106 GLY A O     1 
ATOM   1623  N  N     A HIS A 1 107 ? -0.249  -2.691  14.640  0.20 28.78  ? 107 HIS A N     1 
ATOM   1624  N  N     B HIS A 1 107 ? 0.027   -2.303  14.896  0.80 27.71  ? 107 HIS A N     1 
ATOM   1625  C  CA    A HIS A 1 107 ? -0.945  -1.412  14.689  0.20 27.37  ? 107 HIS A CA    1 
ATOM   1626  C  CA    B HIS A 1 107 ? -0.647  -1.018  14.910  0.80 22.92  ? 107 HIS A CA    1 
ATOM   1627  C  C     A HIS A 1 107 ? -1.261  -0.856  13.309  0.20 29.96  ? 107 HIS A C     1 
ATOM   1628  C  C     B HIS A 1 107 ? -0.897  -0.443  13.517  0.80 31.49  ? 107 HIS A C     1 
ATOM   1629  O  O     A HIS A 1 107 ? -2.340  -0.281  13.114  0.20 30.77  ? 107 HIS A O     1 
ATOM   1630  O  O     B HIS A 1 107 ? -1.992  0.063   13.257  0.80 31.33  ? 107 HIS A O     1 
ATOM   1631  C  CB    A HIS A 1 107 ? -0.123  -0.394  15.487  0.20 28.55  ? 107 HIS A CB    1 
ATOM   1632  C  CB    B HIS A 1 107 ? 0.155   -0.017  15.738  0.80 31.09  ? 107 HIS A CB    1 
ATOM   1633  C  CG    A HIS A 1 107 ? -0.876  0.856   15.820  0.20 30.01  ? 107 HIS A CG    1 
ATOM   1634  C  CG    B HIS A 1 107 ? -0.613  1.213   16.100  0.80 31.08  ? 107 HIS A CG    1 
ATOM   1635  N  ND1   A HIS A 1 107 ? -1.460  1.066   17.050  0.20 30.63  ? 107 HIS A ND1   1 
ATOM   1636  N  ND1   B HIS A 1 107 ? -1.330  1.323   17.271  0.80 30.94  ? 107 HIS A ND1   1 
ATOM   1637  C  CD2   A HIS A 1 107 ? -1.163  1.951   15.076  0.20 33.46  ? 107 HIS A CD2   1 
ATOM   1638  C  CD2   B HIS A 1 107 ? -0.786  2.384   15.440  0.80 37.39  ? 107 HIS A CD2   1 
ATOM   1639  C  CE1   A HIS A 1 107 ? -2.063  2.241   17.054  0.20 34.01  ? 107 HIS A CE1   1 
ATOM   1640  C  CE1   B HIS A 1 107 ? -1.905  2.511   17.322  0.80 35.95  ? 107 HIS A CE1   1 
ATOM   1641  N  NE2   A HIS A 1 107 ? -1.899  2.798   15.868  0.20 32.92  ? 107 HIS A NE2   1 
ATOM   1642  N  NE2   B HIS A 1 107 ? -1.593  3.173   16.223  0.80 33.72  ? 107 HIS A NE2   1 
ATOM   1643  N  N     A TYR A 1 108 ? -0.351  -1.018  12.349  0.20 28.77  ? 108 TYR A N     1 
ATOM   1644  N  N     B TYR A 1 108 ? 0.078   -0.498  12.608  0.80 27.12  ? 108 TYR A N     1 
ATOM   1645  C  CA    A TYR A 1 108 ? -0.487  -0.398  11.035  0.20 33.26  ? 108 TYR A CA    1 
ATOM   1646  C  CA    B TYR A 1 108 ? 0.009   0.335   11.410  0.80 38.35  ? 108 TYR A CA    1 
ATOM   1647  C  C     A TYR A 1 108 ? -0.700  -1.430  9.934   0.20 31.55  ? 108 TYR A C     1 
ATOM   1648  C  C     B TYR A 1 108 ? -0.331  -0.419  10.137  0.80 33.46  ? 108 TYR A C     1 
ATOM   1649  O  O     A TYR A 1 108 ? -1.819  -1.579  9.439   0.20 31.21  ? 108 TYR A O     1 
ATOM   1650  O  O     B TYR A 1 108 ? -1.083  0.101   9.312   0.80 44.97  ? 108 TYR A O     1 
ATOM   1651  C  CB    A TYR A 1 108 ? 0.734   0.471   10.719  0.20 32.67  ? 108 TYR A CB    1 
ATOM   1652  C  CB    B TYR A 1 108 ? 1.330   1.081   11.203  0.80 29.85  ? 108 TYR A CB    1 
ATOM   1653  C  CG    A TYR A 1 108 ? 0.943   1.620   11.680  0.20 31.01  ? 108 TYR A CG    1 
ATOM   1654  C  CG    B TYR A 1 108 ? 1.576   2.203   12.179  0.80 31.06  ? 108 TYR A CG    1 
ATOM   1655  C  CD1   A TYR A 1 108 ? 0.173   2.771   11.593  0.20 30.73  ? 108 TYR A CD1   1 
ATOM   1656  C  CD1   B TYR A 1 108 ? 0.880   3.403   12.079  0.80 32.72  ? 108 TYR A CD1   1 
ATOM   1657  C  CD2   A TYR A 1 108 ? 1.909   1.551   12.676  0.20 31.16  ? 108 TYR A CD2   1 
ATOM   1658  C  CD2   B TYR A 1 108 ? 2.513   2.070   13.194  0.80 29.89  ? 108 TYR A CD2   1 
ATOM   1659  C  CE1   A TYR A 1 108 ? 0.355   3.822   12.470  0.20 34.12  ? 108 TYR A CE1   1 
ATOM   1660  C  CE1   B TYR A 1 108 ? 1.105   4.434   12.967  0.80 39.53  ? 108 TYR A CE1   1 
ATOM   1661  C  CE2   A TYR A 1 108 ? 2.100   2.596   13.559  0.20 31.69  ? 108 TYR A CE2   1 
ATOM   1662  C  CE2   B TYR A 1 108 ? 2.747   3.095   14.082  0.80 33.54  ? 108 TYR A CE2   1 
ATOM   1663  C  CZ    A TYR A 1 108 ? 1.320   3.729   13.455  0.20 34.58  ? 108 TYR A CZ    1 
ATOM   1664  C  CZ    B TYR A 1 108 ? 2.037   4.276   13.970  0.80 37.23  ? 108 TYR A CZ    1 
ATOM   1665  O  OH    A TYR A 1 108 ? 1.506   4.771   14.331  0.20 32.88  ? 108 TYR A OH    1 
ATOM   1666  O  OH    B TYR A 1 108 ? 2.274   5.304   14.857  0.80 42.44  ? 108 TYR A OH    1 
ATOM   1667  N  N     A THR A 1 109 ? 0.355   -2.135  9.519   0.20 33.36  ? 109 THR A N     1 
ATOM   1668  N  N     B THR A 1 109 ? 0.209   -1.618  9.925   0.80 34.19  ? 109 THR A N     1 
ATOM   1669  C  CA    A THR A 1 109 ? 0.307   -2.850  8.246   0.20 33.84  ? 109 THR A CA    1 
ATOM   1670  C  CA    B THR A 1 109 ? -0.073  -2.320  8.679   0.80 37.22  ? 109 THR A CA    1 
ATOM   1671  C  C     A THR A 1 109 ? -0.633  -4.053  8.291   0.20 31.71  ? 109 THR A C     1 
ATOM   1672  C  C     B THR A 1 109 ? -1.083  -3.439  8.904   0.80 39.65  ? 109 THR A C     1 
ATOM   1673  O  O     A THR A 1 109 ? -1.319  -4.346  7.304   0.20 34.43  ? 109 THR A O     1 
ATOM   1674  O  O     B THR A 1 109 ? -2.287  -3.252  8.677   0.80 38.58  ? 109 THR A O     1 
ATOM   1675  C  CB    A THR A 1 109 ? 1.712   -3.286  7.833   0.20 36.91  ? 109 THR A CB    1 
ATOM   1676  C  CB    B THR A 1 109 ? 1.217   -2.865  8.071   0.80 37.46  ? 109 THR A CB    1 
ATOM   1677  O  OG1   A THR A 1 109 ? 2.378   -3.884  8.949   0.20 35.33  ? 109 THR A OG1   1 
ATOM   1678  O  OG1   B THR A 1 109 ? 1.716   -3.927  8.886   0.80 38.12  ? 109 THR A OG1   1 
ATOM   1679  C  CG2   A THR A 1 109 ? 2.508   -2.089  7.365   0.20 37.14  ? 109 THR A CG2   1 
ATOM   1680  C  CG2   B THR A 1 109 ? 2.273   -1.772  7.997   0.80 39.12  ? 109 THR A CG2   1 
ATOM   1681  N  N     A ILE A 1 110 ? -0.684  -4.759  9.416   0.20 30.51  ? 110 ILE A N     1 
ATOM   1682  N  N     B ILE A 1 110 ? -0.604  -4.585  9.395   0.80 29.66  ? 110 ILE A N     1 
ATOM   1683  C  CA    A ILE A 1 110 ? -1.447  -5.998  9.521   0.20 31.13  ? 110 ILE A CA    1 
ATOM   1684  C  CA    B ILE A 1 110 ? -1.434  -5.785  9.486   0.80 30.19  ? 110 ILE A CA    1 
ATOM   1685  C  C     A ILE A 1 110 ? -2.761  -5.799  10.271  0.20 31.59  ? 110 ILE A C     1 
ATOM   1686  C  C     B ILE A 1 110 ? -2.679  -5.529  10.332  0.80 30.55  ? 110 ILE A C     1 
ATOM   1687  O  O     A ILE A 1 110 ? -3.794  -6.338  9.871   0.20 34.47  ? 110 ILE A O     1 
ATOM   1688  O  O     B ILE A 1 110 ? -3.779  -5.980  9.992   0.80 32.98  ? 110 ILE A O     1 
ATOM   1689  C  CB    A ILE A 1 110 ? -0.583  -7.096  10.182  0.20 31.52  ? 110 ILE A CB    1 
ATOM   1690  C  CB    B ILE A 1 110 ? -0.600  -6.958  10.037  0.80 31.31  ? 110 ILE A CB    1 
ATOM   1691  C  CG1   A ILE A 1 110 ? 0.625   -7.420  9.298   0.20 36.80  ? 110 ILE A CG1   1 
ATOM   1692  C  CG1   B ILE A 1 110 ? 0.739   -7.062  9.283   0.80 37.93  ? 110 ILE A CG1   1 
ATOM   1693  C  CG2   A ILE A 1 110 ? -1.395  -8.348  10.444  0.20 34.66  ? 110 ILE A CG2   1 
ATOM   1694  C  CG2   B ILE A 1 110 ? -1.371  -8.259  9.941   0.80 36.04  ? 110 ILE A CG2   1 
ATOM   1695  C  CD1   A ILE A 1 110 ? 0.255   -8.002  7.946   0.20 36.90  ? 110 ILE A CD1   1 
ATOM   1696  C  CD1   B ILE A 1 110 ? 0.637   -7.640  7.872   0.80 36.68  ? 110 ILE A CD1   1 
ATOM   1697  N  N     A GLY A 1 111 ? -2.748  -5.023  11.357  0.20 32.21  ? 111 GLY A N     1 
ATOM   1698  N  N     B GLY A 1 111 ? -2.536  -4.786  11.431  0.80 32.24  ? 111 GLY A N     1 
ATOM   1699  C  CA    A GLY A 1 111 ? -3.964  -4.803  12.123  0.20 30.89  ? 111 GLY A CA    1 
ATOM   1700  C  CA    B GLY A 1 111 ? -3.682  -4.532  12.289  0.80 31.18  ? 111 GLY A CA    1 
ATOM   1701  C  C     A GLY A 1 111 ? -5.042  -4.047  11.373  0.20 33.40  ? 111 GLY A C     1 
ATOM   1702  C  C     B GLY A 1 111 ? -4.771  -3.730  11.608  0.80 32.84  ? 111 GLY A C     1 
ATOM   1703  O  O     A GLY A 1 111 ? -6.215  -4.120  11.753  0.20 33.41  ? 111 GLY A O     1 
ATOM   1704  O  O     B GLY A 1 111 ? -5.959  -3.918  11.887  0.80 35.27  ? 111 GLY A O     1 
ATOM   1705  N  N     A LYS A 1 112 ? -4.671  -3.333  10.309  0.20 32.21  ? 112 LYS A N     1 
ATOM   1706  N  N     B LYS A 1 112 ? -4.394  -2.839  10.692  0.80 32.31  ? 112 LYS A N     1 
ATOM   1707  C  CA    A LYS A 1 112 ? -5.642  -2.557  9.546   0.20 34.08  ? 112 LYS A CA    1 
ATOM   1708  C  CA    B LYS A 1 112 ? -5.404  -2.079  9.969   0.80 34.58  ? 112 LYS A CA    1 
ATOM   1709  C  C     A LYS A 1 112 ? -6.644  -3.452  8.823   0.20 34.24  ? 112 LYS A C     1 
ATOM   1710  C  C     B LYS A 1 112 ? -6.259  -2.963  9.073   0.80 36.27  ? 112 LYS A C     1 
ATOM   1711  O  O     A LYS A 1 112 ? -7.795  -3.050  8.616   0.20 32.86  ? 112 LYS A O     1 
ATOM   1712  O  O     B LYS A 1 112 ? -7.327  -2.527  8.637   0.80 33.61  ? 112 LYS A O     1 
ATOM   1713  C  CB    A LYS A 1 112 ? -4.898  -1.656  8.557   0.20 36.72  ? 112 LYS A CB    1 
ATOM   1714  C  CB    B LYS A 1 112 ? -4.741  -0.970  9.150   0.80 34.90  ? 112 LYS A CB    1 
ATOM   1715  C  CG    A LYS A 1 112 ? -5.757  -0.961  7.519   0.20 41.30  ? 112 LYS A CG    1 
ATOM   1716  C  CG    B LYS A 1 112 ? -5.691  0.154   8.776   0.80 52.01  ? 112 LYS A CG    1 
ATOM   1717  C  CD    A LYS A 1 112 ? -4.921  0.007   6.695   0.20 49.14  ? 112 LYS A CD    1 
ATOM   1718  C  CD    B LYS A 1 112 ? -4.949  1.426   8.410   0.80 58.36  ? 112 LYS A CD    1 
ATOM   1719  C  CE    A LYS A 1 112 ? -3.610  -0.626  6.251   0.20 41.82  ? 112 LYS A CE    1 
ATOM   1720  C  CE    B LYS A 1 112 ? -5.925  2.534   8.045   0.80 65.31  ? 112 LYS A CE    1 
ATOM   1721  N  NZ    A LYS A 1 112 ? -3.820  -1.810  5.376   0.20 43.84  ? 112 LYS A NZ    1 
ATOM   1722  N  NZ    B LYS A 1 112 ? -6.913  2.071   7.026   0.80 78.70  ? 112 LYS A NZ    1 
ATOM   1723  N  N     A GLU A 1 113 ? -6.241  -4.668  8.452   0.20 34.36  ? 113 GLU A N     1 
ATOM   1724  N  N     B GLU A 1 113 ? -5.832  -4.199  8.794   0.80 32.55  ? 113 GLU A N     1 
ATOM   1725  C  CA    A GLU A 1 113 ? -7.118  -5.532  7.671   0.20 35.55  ? 113 GLU A CA    1 
ATOM   1726  C  CA    B GLU A 1 113 ? -6.647  -5.054  7.940   0.80 35.54  ? 113 GLU A CA    1 
ATOM   1727  C  C     A GLU A 1 113 ? -8.304  -6.057  8.470   0.20 33.96  ? 113 GLU A C     1 
ATOM   1728  C  C     B GLU A 1 113 ? -7.837  -5.670  8.665   0.80 31.72  ? 113 GLU A C     1 
ATOM   1729  O  O     A GLU A 1 113 ? -9.282  -6.517  7.869   0.20 34.18  ? 113 GLU A O     1 
ATOM   1730  O  O     B GLU A 1 113 ? -8.687  -6.278  8.008   0.80 39.32  ? 113 GLU A O     1 
ATOM   1731  C  CB    A GLU A 1 113 ? -6.327  -6.714  7.110   0.20 38.22  ? 113 GLU A CB    1 
ATOM   1732  C  CB    B GLU A 1 113 ? -5.793  -6.167  7.330   0.80 40.18  ? 113 GLU A CB    1 
ATOM   1733  C  CG    A GLU A 1 113 ? -5.214  -6.326  6.155   0.20 43.77  ? 113 GLU A CG    1 
ATOM   1734  C  CG    B GLU A 1 113 ? -4.556  -5.663  6.599   0.80 39.79  ? 113 GLU A CG    1 
ATOM   1735  C  CD    A GLU A 1 113 ? -4.419  -7.525  5.674   0.20 52.60  ? 113 GLU A CD    1 
ATOM   1736  C  CD    B GLU A 1 113 ? -3.823  -6.758  5.829   0.80 56.96  ? 113 GLU A CD    1 
ATOM   1737  O  OE1   A GLU A 1 113 ? -4.465  -8.579  6.343   0.20 51.32  ? 113 GLU A OE1   1 
ATOM   1738  O  OE1   B GLU A 1 113 ? -4.100  -7.956  6.059   0.80 54.80  ? 113 GLU A OE1   1 
ATOM   1739  O  OE2   A GLU A 1 113 ? -3.750  -7.414  4.625   0.20 56.04  ? 113 GLU A OE2   1 
ATOM   1740  O  OE2   B GLU A 1 113 ? -2.967  -6.412  4.985   0.80 70.32  ? 113 GLU A OE2   1 
ATOM   1741  N  N     A ILE A 1 114 ? -8.255  -6.000  9.799   0.20 31.00  ? 114 ILE A N     1 
ATOM   1742  N  N     B ILE A 1 114 ? -7.936  -5.534  9.987   0.80 27.29  ? 114 ILE A N     1 
ATOM   1743  C  CA    A ILE A 1 114 ? -9.253  -6.701  10.599  0.20 30.34  ? 114 ILE A CA    1 
ATOM   1744  C  CA    B ILE A 1 114 ? -8.959  -6.277  10.714  0.80 27.95  ? 114 ILE A CA    1 
ATOM   1745  C  C     A ILE A 1 114 ? -9.771  -5.811  11.725  0.20 32.10  ? 114 ILE A C     1 
ATOM   1746  C  C     B ILE A 1 114 ? -9.695  -5.387  11.715  0.80 32.07  ? 114 ILE A C     1 
ATOM   1747  O  O     A ILE A 1 114 ? -10.521 -6.268  12.595  0.20 28.44  ? 114 ILE A O     1 
ATOM   1748  O  O     B ILE A 1 114 ? -10.687 -5.812  12.321  0.80 26.77  ? 114 ILE A O     1 
ATOM   1749  C  CB    A ILE A 1 114 ? -8.663  -8.021  11.138  0.20 32.66  ? 114 ILE A CB    1 
ATOM   1750  C  CB    B ILE A 1 114 ? -8.315  -7.503  11.402  0.80 35.32  ? 114 ILE A CB    1 
ATOM   1751  C  CG1   A ILE A 1 114 ? -9.766  -9.037  11.438  0.20 32.60  ? 114 ILE A CG1   1 
ATOM   1752  C  CG1   B ILE A 1 114 ? -9.368  -8.501  11.886  0.80 34.87  ? 114 ILE A CG1   1 
ATOM   1753  C  CG2   A ILE A 1 114 ? -7.791  -7.773  12.364  0.20 31.32  ? 114 ILE A CG2   1 
ATOM   1754  C  CG2   B ILE A 1 114 ? -7.386  -7.063  12.531  0.80 37.23  ? 114 ILE A CG2   1 
ATOM   1755  C  CD1   A ILE A 1 114 ? -9.234  -10.369 11.910  0.20 29.86  ? 114 ILE A CD1   1 
ATOM   1756  C  CD1   B ILE A 1 114 ? -8.786  -9.662  12.685  0.80 36.04  ? 114 ILE A CD1   1 
ATOM   1757  N  N     A ILE A 1 115 ? -9.403  -4.528  11.705  0.20 28.83  ? 115 ILE A N     1 
ATOM   1758  N  N     B ILE A 1 115 ? -9.244  -4.141  11.876  0.80 28.11  ? 115 ILE A N     1 
ATOM   1759  C  CA    A ILE A 1 115 ? -9.824  -3.636  12.783  0.20 30.03  ? 115 ILE A CA    1 
ATOM   1760  C  CA    B ILE A 1 115 ? -9.763  -3.302  12.960  0.80 28.89  ? 115 ILE A CA    1 
ATOM   1761  C  C     A ILE A 1 115 ? -11.312 -3.311  12.679  0.20 30.99  ? 115 ILE A C     1 
ATOM   1762  C  C     B ILE A 1 115 ? -11.253 -3.015  12.771  0.80 31.00  ? 115 ILE A C     1 
ATOM   1763  O  O     A ILE A 1 115 ? -11.987 -3.137  13.701  0.20 32.13  ? 115 ILE A O     1 
ATOM   1764  O  O     B ILE A 1 115 ? -12.027 -3.041  13.737  0.80 32.56  ? 115 ILE A O     1 
ATOM   1765  C  CB    A ILE A 1 115 ? -8.955  -2.361  12.796  0.20 30.40  ? 115 ILE A CB    1 
ATOM   1766  C  CB    B ILE A 1 115 ? -8.930  -2.006  13.096  0.80 29.83  ? 115 ILE A CB    1 
ATOM   1767  C  CG1   A ILE A 1 115 ? -9.355  -1.443  13.956  0.20 31.18  ? 115 ILE A CG1   1 
ATOM   1768  C  CG1   B ILE A 1 115 ? -9.491  -1.119  14.210  0.80 31.94  ? 115 ILE A CG1   1 
ATOM   1769  C  CG2   A ILE A 1 115 ? -9.043  -1.624  11.464  0.20 28.55  ? 115 ILE A CG2   1 
ATOM   1770  C  CG2   B ILE A 1 115 ? -8.833  -1.230  11.777  0.80 23.27  ? 115 ILE A CG2   1 
ATOM   1771  C  CD1   A ILE A 1 115 ? -9.275  -2.108  15.324  0.20 28.57  ? 115 ILE A CD1   1 
ATOM   1772  C  CD1   B ILE A 1 115 ? -9.535  -1.814  15.589  0.80 27.17  ? 115 ILE A CD1   1 
ATOM   1773  N  N     A ASP A 1 116 ? -11.855 -3.244  11.461  0.20 30.37  ? 116 ASP A N     1 
ATOM   1774  N  N     B ASP A 1 116 ? -11.688 -2.779  11.530  0.80 30.89  ? 116 ASP A N     1 
ATOM   1775  C  CA    A ASP A 1 116 ? -13.262 -2.892  11.298  0.20 32.27  ? 116 ASP A CA    1 
ATOM   1776  C  CA    B ASP A 1 116 ? -13.091 -2.435  11.292  0.80 33.74  ? 116 ASP A CA    1 
ATOM   1777  C  C     A ASP A 1 116 ? -14.182 -4.059  11.634  0.20 31.13  ? 116 ASP A C     1 
ATOM   1778  C  C     B ASP A 1 116 ? -14.002 -3.632  11.501  0.80 29.42  ? 116 ASP A C     1 
ATOM   1779  O  O     A ASP A 1 116 ? -15.259 -3.854  12.204  0.20 31.59  ? 116 ASP A O     1 
ATOM   1780  O  O     B ASP A 1 116 ? -15.140 -3.481  11.953  0.80 30.87  ? 116 ASP A O     1 
ATOM   1781  C  CB    A ASP A 1 116 ? -13.525 -2.404  9.872   0.20 33.03  ? 116 ASP A CB    1 
ATOM   1782  C  CB    B ASP A 1 116 ? -13.277 -1.891  9.879   0.80 34.53  ? 116 ASP A CB    1 
ATOM   1783  C  CG    A ASP A 1 116 ? -12.952 -1.026  9.614   0.20 36.68  ? 116 ASP A CG    1 
ATOM   1784  C  CG    B ASP A 1 116 ? -12.643 -0.541  9.694   0.80 35.15  ? 116 ASP A CG    1 
ATOM   1785  O  OD1   A ASP A 1 116 ? -12.981 -0.185  10.537  0.20 38.95  ? 116 ASP A OD1   1 
ATOM   1786  O  OD1   B ASP A 1 116 ? -12.736 0.289   10.621  0.80 43.38  ? 116 ASP A OD1   1 
ATOM   1787  O  OD2   A ASP A 1 116 ? -12.474 -0.783  8.486   0.20 39.07  ? 116 ASP A OD2   1 
ATOM   1788  O  OD2   B ASP A 1 116 ? -12.054 -0.318  8.621   0.80 45.98  ? 116 ASP A OD2   1 
ATOM   1789  N  N     A LEU A 1 117 ? -13.783 -5.285  11.288  0.20 29.75  ? 117 LEU A N     1 
ATOM   1790  N  N     B LEU A 1 117 ? -13.536 -4.828  11.149  0.80 28.86  ? 117 LEU A N     1 
ATOM   1791  C  CA    A LEU A 1 117 ? -14.608 -6.443  11.618  0.20 31.98  ? 117 LEU A CA    1 
ATOM   1792  C  CA    B LEU A 1 117 ? -14.307 -6.018  11.468  0.80 30.91  ? 117 LEU A CA    1 
ATOM   1793  C  C     A LEU A 1 117 ? -14.758 -6.598  13.126  0.20 33.57  ? 117 LEU A C     1 
ATOM   1794  C  C     B LEU A 1 117 ? -14.443 -6.181  12.976  0.80 36.26  ? 117 LEU A C     1 
ATOM   1795  O  O     A LEU A 1 117 ? -15.828 -6.980  13.616  0.20 29.83  ? 117 LEU A O     1 
ATOM   1796  O  O     B LEU A 1 117 ? -15.512 -6.565  13.478  0.80 30.89  ? 117 LEU A O     1 
ATOM   1797  C  CB    A LEU A 1 117 ? -14.015 -7.710  11.003  0.20 30.04  ? 117 LEU A CB    1 
ATOM   1798  C  CB    B LEU A 1 117 ? -13.649 -7.243  10.849  0.80 29.18  ? 117 LEU A CB    1 
ATOM   1799  C  CG    A LEU A 1 117 ? -14.679 -9.030  11.409  0.20 33.61  ? 117 LEU A CG    1 
ATOM   1800  C  CG    B LEU A 1 117 ? -14.346 -8.562  11.148  0.80 31.28  ? 117 LEU A CG    1 
ATOM   1801  C  CD1   A LEU A 1 117 ? -16.163 -9.031  11.064  0.20 33.40  ? 117 LEU A CD1   1 
ATOM   1802  C  CD1   B LEU A 1 117 ? -15.753 -8.568  10.581  0.80 39.24  ? 117 LEU A CD1   1 
ATOM   1803  C  CD2   A LEU A 1 117 ? -13.976 -10.219 10.769  0.20 31.79  ? 117 LEU A CD2   1 
ATOM   1804  C  CD2   B LEU A 1 117 ? -13.533 -9.722  10.607  0.80 35.23  ? 117 LEU A CD2   1 
ATOM   1805  N  N     A VAL A 1 118 ? -13.700 -6.295  13.882  0.20 31.35  ? 118 VAL A N     1 
ATOM   1806  N  N     B VAL A 1 118 ? -13.371 -5.876  13.716  0.80 27.34  ? 118 VAL A N     1 
ATOM   1807  C  CA    A VAL A 1 118 ? -13.780 -6.401  15.335  0.20 28.58  ? 118 VAL A CA    1 
ATOM   1808  C  CA    B VAL A 1 118 ? -13.399 -6.046  15.165  0.80 28.61  ? 118 VAL A CA    1 
ATOM   1809  C  C     A VAL A 1 118 ? -14.752 -5.370  15.896  0.20 29.48  ? 118 VAL A C     1 
ATOM   1810  C  C     B VAL A 1 118 ? -14.336 -5.028  15.809  0.80 28.60  ? 118 VAL A C     1 
ATOM   1811  O  O     A VAL A 1 118 ? -15.536 -5.668  16.806  0.20 27.15  ? 118 VAL A O     1 
ATOM   1812  O  O     B VAL A 1 118 ? -15.129 -5.365  16.701  0.80 28.05  ? 118 VAL A O     1 
ATOM   1813  C  CB    A VAL A 1 118 ? -12.379 -6.261  15.957  0.20 29.99  ? 118 VAL A CB    1 
ATOM   1814  C  CB    B VAL A 1 118 ? -11.970 -5.953  15.727  0.80 28.52  ? 118 VAL A CB    1 
ATOM   1815  C  CG1   A VAL A 1 118 ? -12.466 -6.296  17.476  0.20 28.52  ? 118 VAL A CG1   1 
ATOM   1816  C  CG1   B VAL A 1 118 ? -11.998 -5.893  17.261  0.80 29.65  ? 118 VAL A CG1   1 
ATOM   1817  C  CG2   A VAL A 1 118 ? -11.463 -7.361  15.446  0.20 26.90  ? 118 VAL A CG2   1 
ATOM   1818  C  CG2   B VAL A 1 118 ? -11.148 -7.133  15.236  0.80 24.41  ? 118 VAL A CG2   1 
ATOM   1819  N  N     A LEU A 1 119 ? -14.731 -4.148  15.356  0.20 27.83  ? 119 LEU A N     1 
ATOM   1820  N  N     B LEU A 1 119 ? -14.267 -3.769  15.361  0.80 24.09  ? 119 LEU A N     1 
ATOM   1821  C  CA    A LEU A 1 119 ? -15.598 -3.096  15.877  0.20 31.74  ? 119 LEU A CA    1 
ATOM   1822  C  CA    B LEU A 1 119 ? -15.193 -2.753  15.843  0.80 32.41  ? 119 LEU A CA    1 
ATOM   1823  C  C     A LEU A 1 119 ? -17.064 -3.374  15.564  0.20 32.75  ? 119 LEU A C     1 
ATOM   1824  C  C     B LEU A 1 119 ? -16.643 -3.131  15.552  0.80 33.67  ? 119 LEU A C     1 
ATOM   1825  O  O     A LEU A 1 119 ? -17.941 -3.085  16.385  0.20 30.40  ? 119 LEU A O     1 
ATOM   1826  O  O     B LEU A 1 119 ? -17.502 -2.981  16.425  0.80 25.28  ? 119 LEU A O     1 
ATOM   1827  C  CB    A LEU A 1 119 ? -15.173 -1.736  15.327  0.20 31.44  ? 119 LEU A CB    1 
ATOM   1828  C  CB    B LEU A 1 119 ? -14.847 -1.394  15.236  0.80 30.28  ? 119 LEU A CB    1 
ATOM   1829  C  CG    A LEU A 1 119 ? -13.871 -1.159  15.890  0.20 29.72  ? 119 LEU A CG    1 
ATOM   1830  C  CG    B LEU A 1 119 ? -13.456 -0.864  15.574  0.80 29.41  ? 119 LEU A CG    1 
ATOM   1831  C  CD1   A LEU A 1 119 ? -13.610 0.222   15.321  0.20 34.68  ? 119 LEU A CD1   1 
ATOM   1832  C  CD1   B LEU A 1 119 ? -13.155 0.421   14.778  0.80 33.24  ? 119 LEU A CD1   1 
ATOM   1833  C  CD2   A LEU A 1 119 ? -13.908 -1.113  17.412  0.20 30.62  ? 119 LEU A CD2   1 
ATOM   1834  C  CD2   B LEU A 1 119 ? -13.288 -0.658  17.078  0.80 34.83  ? 119 LEU A CD2   1 
ATOM   1835  N  N     A ASP A 1 120 ? -17.356 -3.936  14.386  0.20 31.35  ? 120 ASP A N     1 
ATOM   1836  N  N     B ASP A 1 120 ? -16.940 -3.655  14.353  0.80 30.79  ? 120 ASP A N     1 
ATOM   1837  C  CA    A ASP A 1 120 ? -18.736 -4.308  14.090  0.20 31.36  ? 120 ASP A CA    1 
ATOM   1838  C  CA    B ASP A 1 120 ? -18.331 -4.001  14.041  0.80 29.92  ? 120 ASP A CA    1 
ATOM   1839  C  C     A ASP A 1 120 ? -19.196 -5.480  14.950  0.20 31.74  ? 120 ASP A C     1 
ATOM   1840  C  C     B ASP A 1 120 ? -18.845 -5.143  14.921  0.80 32.37  ? 120 ASP A C     1 
ATOM   1841  O  O     A ASP A 1 120 ? -20.383 -5.574  15.283  0.20 29.64  ? 120 ASP A O     1 
ATOM   1842  O  O     B ASP A 1 120 ? -20.010 -5.132  15.343  0.80 31.01  ? 120 ASP A O     1 
ATOM   1843  C  CB    A ASP A 1 120 ? -18.894 -4.644  12.605  0.20 34.16  ? 120 ASP A CB    1 
ATOM   1844  C  CB    B ASP A 1 120 ? -18.488 -4.367  12.559  0.80 36.18  ? 120 ASP A CB    1 
ATOM   1845  C  CG    A ASP A 1 120 ? -18.768 -3.421  11.714  0.20 36.27  ? 120 ASP A CG    1 
ATOM   1846  C  CG    B ASP A 1 120 ? -18.316 -3.166  11.625  0.80 37.70  ? 120 ASP A CG    1 
ATOM   1847  O  OD1   A ASP A 1 120 ? -18.571 -2.310  12.247  0.20 41.59  ? 120 ASP A OD1   1 
ATOM   1848  O  OD1   B ASP A 1 120 ? -18.476 -2.015  12.084  0.80 44.18  ? 120 ASP A OD1   1 
ATOM   1849  O  OD2   A ASP A 1 120 ? -18.864 -3.572  10.477  0.20 38.50  ? 120 ASP A OD2   1 
ATOM   1850  O  OD2   B ASP A 1 120 ? -18.017 -3.375  10.426  0.80 38.91  ? 120 ASP A OD2   1 
ATOM   1851  N  N     A ARG A 1 121 ? -18.279 -6.377  15.319  0.20 28.90  ? 121 ARG A N     1 
ATOM   1852  N  N     B ARG A 1 121 ? -17.999 -6.141  15.199  0.80 29.94  ? 121 ARG A N     1 
ATOM   1853  C  CA    A ARG A 1 121 ? -18.632 -7.479  16.205  0.20 31.82  ? 121 ARG A CA    1 
ATOM   1854  C  CA    B ARG A 1 121 ? -18.407 -7.245  16.061  0.80 30.82  ? 121 ARG A CA    1 
ATOM   1855  C  C     A ARG A 1 121 ? -18.771 -7.021  17.651  0.20 32.65  ? 121 ARG A C     1 
ATOM   1856  C  C     B ARG A 1 121 ? -18.610 -6.781  17.501  0.80 32.52  ? 121 ARG A C     1 
ATOM   1857  O  O     A ARG A 1 121 ? -19.583 -7.581  18.396  0.20 33.85  ? 121 ARG A O     1 
ATOM   1858  O  O     B ARG A 1 121 ? -19.553 -7.227  18.165  0.80 33.81  ? 121 ARG A O     1 
ATOM   1859  C  CB    A ARG A 1 121 ? -17.593 -8.596  16.097  0.20 28.54  ? 121 ARG A CB    1 
ATOM   1860  C  CB    B ARG A 1 121 ? -17.392 -8.388  15.984  0.80 27.50  ? 121 ARG A CB    1 
ATOM   1861  C  CG    A ARG A 1 121 ? -17.603 -9.328  14.756  0.20 33.73  ? 121 ARG A CG    1 
ATOM   1862  C  CG    B ARG A 1 121 ? -17.347 -9.117  14.607  0.80 32.38  ? 121 ARG A CG    1 
ATOM   1863  C  CD    A ARG A 1 121 ? -18.799 -10.271 14.634  0.20 31.75  ? 121 ARG A CD    1 
ATOM   1864  C  CD    B ARG A 1 121 ? -18.523 -10.128 14.425  0.80 32.86  ? 121 ARG A CD    1 
ATOM   1865  N  NE    A ARG A 1 121 ? -18.909 -10.855 13.302  0.20 32.57  ? 121 ARG A NE    1 
ATOM   1866  N  NE    B ARG A 1 121 ? -18.636 -10.623 13.055  0.80 34.14  ? 121 ARG A NE    1 
ATOM   1867  C  CZ    A ARG A 1 121 ? -18.131 -11.825 12.838  0.20 36.13  ? 121 ARG A CZ    1 
ATOM   1868  C  CZ    B ARG A 1 121 ? -17.782 -11.464 12.481  0.80 40.81  ? 121 ARG A CZ    1 
ATOM   1869  N  NH1   A ARG A 1 121 ? -17.151 -12.336 13.567  0.20 32.35  ? 121 ARG A NH1   1 
ATOM   1870  N  NH1   B ARG A 1 121 ? -16.749 -11.964 13.145  0.80 31.83  ? 121 ARG A NH1   1 
ATOM   1871  N  NH2   A ARG A 1 121 ? -18.334 -12.287 11.606  0.20 34.30  ? 121 ARG A NH2   1 
ATOM   1872  N  NH2   B ARG A 1 121 ? -17.963 -11.806 11.202  0.80 27.60  ? 121 ARG A NH2   1 
ATOM   1873  N  N     A ILE A 1 122 ? -17.994 -6.015  18.062  0.20 28.55  ? 122 ILE A N     1 
ATOM   1874  N  N     B ILE A 1 122 ? -17.751 -5.876  17.992  0.80 26.01  ? 122 ILE A N     1 
ATOM   1875  C  CA    A ILE A 1 122 ? -18.180 -5.421  19.384  0.20 32.71  ? 122 ILE A CA    1 
ATOM   1876  C  CA    B ILE A 1 122 ? -17.970 -5.252  19.302  0.80 33.58  ? 122 ILE A CA    1 
ATOM   1877  C  C     A ILE A 1 122 ? -19.498 -4.658  19.444  0.20 33.01  ? 122 ILE A C     1 
ATOM   1878  C  C     B ILE A 1 122 ? -19.288 -4.479  19.324  0.80 33.36  ? 122 ILE A C     1 
ATOM   1879  O  O     A ILE A 1 122 ? -20.219 -4.709  20.450  0.20 32.69  ? 122 ILE A O     1 
ATOM   1880  O  O     B ILE A 1 122 ? -20.067 -4.566  20.286  0.80 33.90  ? 122 ILE A O     1 
ATOM   1881  C  CB    A ILE A 1 122 ? -16.983 -4.517  19.733  0.20 31.81  ? 122 ILE A CB    1 
ATOM   1882  C  CB    B ILE A 1 122 ? -16.778 -4.345  19.663  0.80 31.86  ? 122 ILE A CB    1 
ATOM   1883  C  CG1   A ILE A 1 122 ? -15.734 -5.362  19.996  0.20 28.57  ? 122 ILE A CG1   1 
ATOM   1884  C  CG1   B ILE A 1 122 ? -15.576 -5.198  20.075  0.80 28.39  ? 122 ILE A CG1   1 
ATOM   1885  C  CG2   A ILE A 1 122 ? -17.303 -3.629  20.933  0.20 28.11  ? 122 ILE A CG2   1 
ATOM   1886  C  CG2   B ILE A 1 122 ? -17.172 -3.330  20.767  0.80 26.77  ? 122 ILE A CG2   1 
ATOM   1887  C  CD1   A ILE A 1 122 ? -14.487 -4.544  20.281  0.20 29.33  ? 122 ILE A CD1   1 
ATOM   1888  C  CD1   B ILE A 1 122 ? -14.217 -4.463  20.019  0.80 27.87  ? 122 ILE A CD1   1 
ATOM   1889  N  N     A ARG A 1 123 ? -19.841 -3.948  18.365  0.20 33.66  ? 123 ARG A N     1 
ATOM   1890  N  N     B ARG A 1 123 ? -19.554 -3.703  18.267  0.80 35.11  ? 123 ARG A N     1 
ATOM   1891  C  CA    A ARG A 1 123 ? -21.086 -3.186  18.341  0.20 31.91  ? 123 ARG A CA    1 
ATOM   1892  C  CA    B ARG A 1 123 ? -20.805 -2.951  18.183  0.80 32.75  ? 123 ARG A CA    1 
ATOM   1893  C  C     A ARG A 1 123 ? -22.298 -4.092  18.501  0.20 34.42  ? 123 ARG A C     1 
ATOM   1894  C  C     B ARG A 1 123 ? -22.012 -3.859  18.366  0.80 33.76  ? 123 ARG A C     1 
ATOM   1895  O  O     A ARG A 1 123 ? -23.315 -3.672  19.066  0.20 31.08  ? 123 ARG A O     1 
ATOM   1896  O  O     B ARG A 1 123 ? -22.976 -3.496  19.058  0.80 29.08  ? 123 ARG A O     1 
ATOM   1897  C  CB    A ARG A 1 123 ? -21.189 -2.384  17.042  0.20 32.01  ? 123 ARG A CB    1 
ATOM   1898  C  CB    B ARG A 1 123 ? -20.876 -2.218  16.840  0.80 31.20  ? 123 ARG A CB    1 
ATOM   1899  C  CG    A ARG A 1 123 ? -22.235 -1.280  17.076  0.20 37.19  ? 123 ARG A CG    1 
ATOM   1900  C  CG    B ARG A 1 123 ? -22.218 -1.596  16.506  0.80 32.91  ? 123 ARG A CG    1 
ATOM   1901  C  CD    A ARG A 1 123 ? -22.330 -0.534  15.753  0.20 36.37  ? 123 ARG A CD    1 
ATOM   1902  C  CD    B ARG A 1 123 ? -22.535 -0.434  17.422  0.80 48.20  ? 123 ARG A CD    1 
ATOM   1903  N  NE    A ARG A 1 123 ? -21.019 -0.182  15.222  0.20 38.94  ? 123 ARG A NE    1 
ATOM   1904  N  NE    B ARG A 1 123 ? -21.530 0.619   17.330  0.80 49.45  ? 123 ARG A NE    1 
ATOM   1905  C  CZ    A ARG A 1 123 ? -20.477 -0.736  14.146  0.20 35.37  ? 123 ARG A CZ    1 
ATOM   1906  C  CZ    B ARG A 1 123 ? -21.544 1.721   18.065  0.80 52.30  ? 123 ARG A CZ    1 
ATOM   1907  N  NH1   A ARG A 1 123 ? -21.123 -1.649  13.438  0.20 36.92  ? 123 ARG A NH1   1 
ATOM   1908  N  NH1   B ARG A 1 123 ? -22.506 1.950   18.946  0.80 39.96  ? 123 ARG A NH1   1 
ATOM   1909  N  NH2   A ARG A 1 123 ? -19.257 -0.364  13.771  0.20 35.68  ? 123 ARG A NH2   1 
ATOM   1910  N  NH2   B ARG A 1 123 ? -20.571 2.618   17.910  0.80 45.38  ? 123 ARG A NH2   1 
ATOM   1911  N  N     A LYS A 1 124 ? -22.209 -5.335  18.023  0.20 32.21  ? 124 LYS A N     1 
ATOM   1912  N  N     B LYS A 1 124 ? -21.967 -5.057  17.776  0.80 28.79  ? 124 LYS A N     1 
ATOM   1913  C  CA    A LYS A 1 124 ? -23.306 -6.278  18.209  0.20 37.12  ? 124 LYS A CA    1 
ATOM   1914  C  CA    B LYS A 1 124 ? -23.082 -5.987  17.904  0.80 38.17  ? 124 LYS A CA    1 
ATOM   1915  C  C     A LYS A 1 124 ? -23.523 -6.605  19.683  0.20 36.68  ? 124 LYS A C     1 
ATOM   1916  C  C     B LYS A 1 124 ? -23.312 -6.383  19.362  0.80 35.73  ? 124 LYS A C     1 
ATOM   1917  O  O     A LYS A 1 124 ? -24.654 -6.891  20.092  0.20 38.14  ? 124 LYS A O     1 
ATOM   1918  O  O     B LYS A 1 124 ? -24.458 -6.438  19.824  0.80 40.53  ? 124 LYS A O     1 
ATOM   1919  C  CB    A LYS A 1 124 ? -23.038 -7.551  17.407  0.20 40.50  ? 124 LYS A CB    1 
ATOM   1920  C  CB    B LYS A 1 124 ? -22.828 -7.213  17.031  0.80 39.01  ? 124 LYS A CB    1 
ATOM   1921  C  CG    A LYS A 1 124 ? -24.177 -8.553  17.427  0.20 43.42  ? 124 LYS A CG    1 
ATOM   1922  C  CG    B LYS A 1 124 ? -23.927 -8.252  17.102  0.80 45.91  ? 124 LYS A CG    1 
ATOM   1923  C  CD    A LYS A 1 124 ? -23.926 -9.688  16.450  0.20 45.99  ? 124 LYS A CD    1 
ATOM   1924  C  CD    B LYS A 1 124 ? -23.654 -9.420  16.172  0.80 45.44  ? 124 LYS A CD    1 
ATOM   1925  C  CE    A LYS A 1 124 ? -25.098 -10.652 16.424  0.20 44.54  ? 124 LYS A CE    1 
ATOM   1926  C  CE    B LYS A 1 124 ? -24.709 -10.500 16.351  0.80 44.29  ? 124 LYS A CE    1 
ATOM   1927  N  NZ    A LYS A 1 124 ? -24.912 -11.726 15.411  0.20 51.54  ? 124 LYS A NZ    1 
ATOM   1928  N  NZ    B LYS A 1 124 ? -24.430 -11.675 15.488  0.80 54.72  ? 124 LYS A NZ    1 
ATOM   1929  N  N     A LEU A 1 125 ? -22.463 -6.565  20.493  0.20 33.38  ? 125 LEU A N     1 
ATOM   1930  N  N     B LEU A 1 125 ? -22.231 -6.662  20.099  0.80 36.23  ? 125 LEU A N     1 
ATOM   1931  C  CA    A LEU A 1 125 ? -22.614 -6.767  21.929  0.20 35.18  ? 125 LEU A CA    1 
ATOM   1932  C  CA    B LEU A 1 125 ? -22.340 -6.963  21.523  0.80 33.72  ? 125 LEU A CA    1 
ATOM   1933  C  C     A LEU A 1 125 ? -23.012 -5.482  22.643  0.20 34.68  ? 125 LEU A C     1 
ATOM   1934  C  C     B LEU A 1 125 ? -22.867 -5.765  22.298  0.80 35.06  ? 125 LEU A C     1 
ATOM   1935  O  O     A LEU A 1 125 ? -23.672 -5.536  23.688  0.20 32.20  ? 125 LEU A O     1 
ATOM   1936  O  O     B LEU A 1 125 ? -23.698 -5.913  23.204  0.80 34.38  ? 125 LEU A O     1 
ATOM   1937  C  CB    A LEU A 1 125 ? -21.318 -7.316  22.527  0.20 34.61  ? 125 LEU A CB    1 
ATOM   1938  C  CB    B LEU A 1 125 ? -20.977 -7.385  22.080  0.80 35.86  ? 125 LEU A CB    1 
ATOM   1939  C  CG    A LEU A 1 125 ? -20.886 -8.715  22.083  0.20 36.89  ? 125 LEU A CG    1 
ATOM   1940  C  CG    B LEU A 1 125 ? -20.403 -8.742  21.672  0.80 39.27  ? 125 LEU A CG    1 
ATOM   1941  C  CD1   A LEU A 1 125 ? -19.577 -9.117  22.754  0.20 33.32  ? 125 LEU A CD1   1 
ATOM   1942  C  CD1   B LEU A 1 125 ? -18.926 -8.840  22.046  0.80 30.85  ? 125 LEU A CD1   1 
ATOM   1943  C  CD2   A LEU A 1 125 ? -21.980 -9.728  22.379  0.20 37.07  ? 125 LEU A CD2   1 
ATOM   1944  C  CD2   B LEU A 1 125 ? -21.190 -9.855  22.341  0.80 35.31  ? 125 LEU A CD2   1 
ATOM   1945  N  N     A ALA A 1 126 ? -22.622 -4.326  22.100  0.20 31.50  ? 126 ALA A N     1 
ATOM   1946  N  N     B ALA A 1 126 ? -22.382 -4.570  21.967  0.80 29.56  ? 126 ALA A N     1 
ATOM   1947  C  CA    A ALA A 1 126 ? -23.006 -3.058  22.710  0.20 31.89  ? 126 ALA A CA    1 
ATOM   1948  C  CA    B ALA A 1 126 ? -22.829 -3.367  22.657  0.80 30.61  ? 126 ALA A CA    1 
ATOM   1949  C  C     A ALA A 1 126 ? -24.476 -2.740  22.470  0.20 36.15  ? 126 ALA A C     1 
ATOM   1950  C  C     B ALA A 1 126 ? -24.303 -3.090  22.398  0.80 36.95  ? 126 ALA A C     1 
ATOM   1951  O  O     A ALA A 1 126 ? -25.107 -2.079  23.302  0.20 33.25  ? 126 ALA A O     1 
ATOM   1952  O  O     B ALA A 1 126 ? -25.001 -2.591  23.289  0.80 33.32  ? 126 ALA A O     1 
ATOM   1953  C  CB    A ALA A 1 126 ? -22.124 -1.929  22.178  0.20 29.92  ? 126 ALA A CB    1 
ATOM   1954  C  CB    B ALA A 1 126 ? -21.972 -2.173  22.234  0.80 28.67  ? 126 ALA A CB    1 
ATOM   1955  N  N     A ASP A 1 127 ? -25.033 -3.191  21.341  0.20 36.05  ? 127 ASP A N     1 
ATOM   1956  N  N     B ASP A 1 127 ? -24.794 -3.412  21.196  0.80 35.28  ? 127 ASP A N     1 
ATOM   1957  C  CA    A ASP A 1 127 ? -26.454 -2.983  21.082  0.20 37.58  ? 127 ASP A CA    1 
ATOM   1958  C  CA    B ASP A 1 127 ? -26.202 -3.207  20.869  0.80 37.98  ? 127 ASP A CA    1 
ATOM   1959  C  C     A ASP A 1 127 ? -27.323 -3.789  22.037  0.20 37.21  ? 127 ASP A C     1 
ATOM   1960  C  C     B ASP A 1 127 ? -27.137 -4.047  21.732  0.80 37.69  ? 127 ASP A C     1 
ATOM   1961  O  O     A ASP A 1 127 ? -28.464 -3.401  22.314  0.20 37.55  ? 127 ASP A O     1 
ATOM   1962  O  O     B ASP A 1 127 ? -28.309 -3.687  21.883  0.80 37.31  ? 127 ASP A O     1 
ATOM   1963  C  CB    A ASP A 1 127 ? -26.788 -3.350  19.635  0.20 40.81  ? 127 ASP A CB    1 
ATOM   1964  C  CB    B ASP A 1 127 ? -26.458 -3.524  19.392  0.80 43.26  ? 127 ASP A CB    1 
ATOM   1965  C  CG    A ASP A 1 127 ? -26.189 -2.384  18.632  0.20 38.03  ? 127 ASP A CG    1 
ATOM   1966  C  CG    B ASP A 1 127 ? -26.172 -2.347  18.477  0.80 37.62  ? 127 ASP A CG    1 
ATOM   1967  O  OD1   A ASP A 1 127 ? -25.659 -1.335  19.056  0.20 43.54  ? 127 ASP A OD1   1 
ATOM   1968  O  OD1   B ASP A 1 127 ? -25.891 -1.242  18.988  0.80 44.75  ? 127 ASP A OD1   1 
ATOM   1969  O  OD2   A ASP A 1 127 ? -26.247 -2.675  17.419  0.20 43.69  ? 127 ASP A OD2   1 
ATOM   1970  O  OD2   B ASP A 1 127 ? -26.233 -2.528  17.243  0.80 45.14  ? 127 ASP A OD2   1 
ATOM   1971  N  N     A GLN A 1 128 ? -26.809 -4.909  22.543  0.20 35.87  ? 128 GLN A N     1 
ATOM   1972  N  N     B GLN A 1 128 ? -26.662 -5.168  22.276  0.80 35.70  ? 128 GLN A N     1 
ATOM   1973  C  CA    A GLN A 1 128 ? -27.537 -5.746  23.486  0.20 36.36  ? 128 GLN A CA    1 
ATOM   1974  C  CA    B GLN A 1 128 ? -27.472 -5.985  23.170  0.80 35.39  ? 128 GLN A CA    1 
ATOM   1975  C  C     A GLN A 1 128 ? -27.398 -5.273  24.927  0.20 36.79  ? 128 GLN A C     1 
ATOM   1976  C  C     B GLN A 1 128 ? -27.548 -5.428  24.583  0.80 37.85  ? 128 GLN A C     1 
ATOM   1977  O  O     A GLN A 1 128 ? -27.938 -5.921  25.831  0.20 35.53  ? 128 GLN A O     1 
ATOM   1978  O  O     B GLN A 1 128 ? -28.312 -5.953  25.399  0.80 40.22  ? 128 GLN A O     1 
ATOM   1979  C  CB    A GLN A 1 128 ? -27.062 -7.197  23.365  0.20 35.50  ? 128 GLN A CB    1 
ATOM   1980  C  CB    B GLN A 1 128 ? -26.931 -7.417  23.231  0.80 34.19  ? 128 GLN A CB    1 
ATOM   1981  C  CG    A GLN A 1 128 ? -27.124 -7.738  21.944  0.20 43.22  ? 128 GLN A CG    1 
ATOM   1982  C  CG    B GLN A 1 128 ? -27.390 -8.298  22.068  0.80 49.56  ? 128 GLN A CG    1 
ATOM   1983  C  CD    A GLN A 1 128 ? -26.514 -9.120  21.813  0.20 46.42  ? 128 GLN A CD    1 
ATOM   1984  C  CD    B GLN A 1 128 ? -26.800 -9.702  22.105  0.80 53.93  ? 128 GLN A CD    1 
ATOM   1985  O  OE1   A GLN A 1 128 ? -25.931 -9.459  20.783  0.20 46.45  ? 128 GLN A OE1   1 
ATOM   1986  O  OE1   B GLN A 1 128 ? -25.600 -9.882  22.328  0.80 52.15  ? 128 GLN A OE1   1 
ATOM   1987  N  NE2   A GLN A 1 128 ? -26.652 -9.928  22.858  0.20 50.72  ? 128 GLN A NE2   1 
ATOM   1988  N  NE2   B GLN A 1 128 ? -27.647 -10.707 21.885  0.80 56.35  ? 128 GLN A NE2   1 
ATOM   1989  N  N     A CYS A 1 129 ? -26.696 -4.169  25.165  0.20 35.24  ? 129 CYS A N     1 
ATOM   1990  N  N     B CYS A 1 129 ? -26.790 -4.389  24.900  0.80 33.18  ? 129 CYS A N     1 
ATOM   1991  C  CA    A CYS A 1 129 ? -26.549 -3.621  26.506  0.20 35.29  ? 129 CYS A CA    1 
ATOM   1992  C  CA    B CYS A 1 129 ? -26.706 -3.917  26.275  0.80 37.05  ? 129 CYS A CA    1 
ATOM   1993  C  C     A CYS A 1 129 ? -27.697 -2.672  26.818  0.20 36.05  ? 129 CYS A C     1 
ATOM   1994  C  C     B CYS A 1 129 ? -27.690 -2.775  26.502  0.80 36.58  ? 129 CYS A C     1 
ATOM   1995  O  O     A CYS A 1 129 ? -28.092 -1.857  25.979  0.20 34.39  ? 129 CYS A O     1 
ATOM   1996  O  O     B CYS A 1 129 ? -27.938 -1.963  25.607  0.80 34.67  ? 129 CYS A O     1 
ATOM   1997  C  CB    A CYS A 1 129 ? -25.217 -2.880  26.648  0.20 35.50  ? 129 CYS A CB    1 
ATOM   1998  C  CB    B CYS A 1 129 ? -25.277 -3.473  26.590  0.80 39.63  ? 129 CYS A CB    1 
ATOM   1999  S  SG    A CYS A 1 129 ? -23.743 -3.927  26.619  0.20 25.56  ? 129 CYS A SG    1 
ATOM   2000  S  SG    B CYS A 1 129 ? -24.036 -4.791  26.373  0.80 27.65  ? 129 CYS A SG    1 
ATOM   2001  N  N     A THR A 1 130 ? -28.234 -2.783  28.035  0.20 33.22  ? 130 THR A N     1 
ATOM   2002  N  N     B THR A 1 130 ? -28.265 -2.718  27.703  0.80 32.76  ? 130 THR A N     1 
ATOM   2003  C  CA    A THR A 1 130 ? -29.207 -1.798  28.494  0.20 37.16  ? 130 THR A CA    1 
ATOM   2004  C  CA    B THR A 1 130 ? -29.175 -1.621  28.008  0.80 37.51  ? 130 THR A CA    1 
ATOM   2005  C  C     A THR A 1 130 ? -28.511 -0.544  29.008  0.20 39.54  ? 130 THR A C     1 
ATOM   2006  C  C     B THR A 1 130 ? -28.509 -0.480  28.765  0.80 40.77  ? 130 THR A C     1 
ATOM   2007  O  O     A THR A 1 130 ? -29.013 0.571   28.822  0.20 43.33  ? 130 THR A O     1 
ATOM   2008  O  O     B THR A 1 130 ? -29.074 0.619   28.819  0.80 43.50  ? 130 THR A O     1 
ATOM   2009  C  CB    A THR A 1 130 ? -30.108 -2.394  29.581  0.20 35.67  ? 130 THR A CB    1 
ATOM   2010  C  CB    B THR A 1 130 ? -30.395 -2.124  28.802  0.80 35.34  ? 130 THR A CB    1 
ATOM   2011  O  OG1   A THR A 1 130 ? -29.313 -2.814  30.699  0.20 31.68  ? 130 THR A OG1   1 
ATOM   2012  O  OG1   B THR A 1 130 ? -29.987 -3.097  29.774  0.80 38.47  ? 130 THR A OG1   1 
ATOM   2013  C  CG2   A THR A 1 130 ? -30.891 -3.587  29.040  0.20 30.55  ? 130 THR A CG2   1 
ATOM   2014  C  CG2   B THR A 1 130 ? -31.421 -2.745  27.862  0.80 35.40  ? 130 THR A CG2   1 
ATOM   2015  N  N     A GLY A 1 131 ? -27.355 -0.710  29.644  0.20 33.90  ? 131 GLY A N     1 
ATOM   2016  N  N     B GLY A 1 131 ? -27.324 -0.706  29.331  0.80 33.29  ? 131 GLY A N     1 
ATOM   2017  C  CA    A GLY A 1 131 ? -26.570 0.405   30.131  0.20 31.55  ? 131 GLY A CA    1 
ATOM   2018  C  CA    B GLY A 1 131 ? -26.593 0.323   30.045  0.80 31.29  ? 131 GLY A CA    1 
ATOM   2019  C  C     A GLY A 1 131 ? -25.096 0.060   30.211  0.20 35.95  ? 131 GLY A C     1 
ATOM   2020  C  C     B GLY A 1 131 ? -25.103 0.019   30.092  0.80 36.46  ? 131 GLY A C     1 
ATOM   2021  O  O     A GLY A 1 131 ? -24.555 -0.130  31.305  0.20 33.29  ? 131 GLY A O     1 
ATOM   2022  O  O     B GLY A 1 131 ? -24.533 -0.167  31.173  0.80 33.35  ? 131 GLY A O     1 
ATOM   2023  N  N     A LEU A 1 132 ? -24.442 -0.040  29.054  0.20 30.77  ? 132 LEU A N     1 
ATOM   2024  N  N     B LEU A 1 132 ? -24.467 -0.035  28.920  0.80 30.44  ? 132 LEU A N     1 
ATOM   2025  C  CA    A LEU A 1 132 ? -23.022 -0.367  29.018  0.20 29.63  ? 132 LEU A CA    1 
ATOM   2026  C  CA    B LEU A 1 132 ? -23.062 -0.424  28.835  0.80 29.29  ? 132 LEU A CA    1 
ATOM   2027  C  C     A LEU A 1 132 ? -22.221 0.688   29.767  0.20 29.79  ? 132 LEU A C     1 
ATOM   2028  C  C     B LEU A 1 132 ? -22.185 0.541   29.622  0.80 29.06  ? 132 LEU A C     1 
ATOM   2029  O  O     A LEU A 1 132 ? -22.366 1.888   29.519  0.20 33.40  ? 132 LEU A O     1 
ATOM   2030  O  O     B LEU A 1 132 ? -22.270 1.759   29.444  0.80 33.89  ? 132 LEU A O     1 
ATOM   2031  C  CB    A LEU A 1 132 ? -22.544 -0.470  27.571  0.20 31.37  ? 132 LEU A CB    1 
ATOM   2032  C  CB    B LEU A 1 132 ? -22.625 -0.459  27.373  0.80 31.71  ? 132 LEU A CB    1 
ATOM   2033  C  CG    A LEU A 1 132 ? -21.063 -0.789  27.349  0.20 27.30  ? 132 LEU A CG    1 
ATOM   2034  C  CG    B LEU A 1 132 ? -21.122 -0.581  27.088  0.80 26.41  ? 132 LEU A CG    1 
ATOM   2035  C  CD1   A LEU A 1 132 ? -20.710 -2.149  27.930  0.20 28.91  ? 132 LEU A CD1   1 
ATOM   2036  C  CD1   B LEU A 1 132 ? -20.514 -1.790  27.781  0.80 28.44  ? 132 LEU A CD1   1 
ATOM   2037  C  CD2   A LEU A 1 132 ? -20.725 -0.735  25.866  0.20 30.67  ? 132 LEU A CD2   1 
ATOM   2038  C  CD2   B LEU A 1 132 ? -20.889 -0.653  25.578  0.80 30.83  ? 132 LEU A CD2   1 
ATOM   2039  N  N     A GLN A 1 133 ? -21.388 0.240   30.707  0.20 26.02  ? 133 GLN A N     1 
ATOM   2040  N  N     B GLN A 1 133 ? -21.368 0.007   30.525  0.80 22.24  ? 133 GLN A N     1 
ATOM   2041  C  CA    A GLN A 1 133 ? -20.592 1.153   31.512  0.20 31.87  ? 133 GLN A CA    1 
ATOM   2042  C  CA    B GLN A 1 133 ? -20.505 0.891   31.299  0.80 31.94  ? 133 GLN A CA    1 
ATOM   2043  C  C     A GLN A 1 133 ? -19.121 1.182   31.131  0.20 29.70  ? 133 GLN A C     1 
ATOM   2044  C  C     B GLN A 1 133 ? -19.094 0.978   30.746  0.80 27.85  ? 133 GLN A C     1 
ATOM   2045  O  O     A GLN A 1 133 ? -18.430 2.145   31.478  0.20 29.92  ? 133 GLN A O     1 
ATOM   2046  O  O     B GLN A 1 133 ? -18.442 2.020   30.910  0.80 27.76  ? 133 GLN A O     1 
ATOM   2047  C  CB    A GLN A 1 133 ? -20.717 0.809   33.005  0.20 35.33  ? 133 GLN A CB    1 
ATOM   2048  C  CB    B GLN A 1 133 ? -20.455 0.486   32.785  0.80 36.47  ? 133 GLN A CB    1 
ATOM   2049  C  CG    A GLN A 1 133 ? -20.505 -0.656  33.345  0.20 32.54  ? 133 GLN A CG    1 
ATOM   2050  C  CG    B GLN A 1 133 ? -20.566 -0.991  33.140  0.80 32.41  ? 133 GLN A CG    1 
ATOM   2051  C  CD    A GLN A 1 133 ? -20.260 -0.876  34.828  0.20 33.06  ? 133 GLN A CD    1 
ATOM   2052  C  CD    B GLN A 1 133 ? -20.582 -1.215  34.653  0.80 33.30  ? 133 GLN A CD    1 
ATOM   2053  O  OE1   A GLN A 1 133 ? -19.674 -0.027  35.499  0.20 33.42  ? 133 GLN A OE1   1 
ATOM   2054  O  OE1   B GLN A 1 133 ? -20.021 -0.427  35.407  0.80 34.44  ? 133 GLN A OE1   1 
ATOM   2055  N  NE2   A GLN A 1 133 ? -20.708 -2.014  35.347  0.20 30.04  ? 133 GLN A NE2   1 
ATOM   2056  N  NE2   B GLN A 1 133 ? -21.236 -2.286  35.097  0.80 30.42  ? 133 GLN A NE2   1 
ATOM   2057  N  N     A GLY A 1 134 ? -18.632 0.172   30.427  0.20 27.92  ? 134 GLY A N     1 
ATOM   2058  N  N     B GLY A 1 134 ? -18.612 -0.072  30.093  0.80 28.06  ? 134 GLY A N     1 
ATOM   2059  C  CA    A GLY A 1 134 ? -17.247 0.180   30.006  0.20 29.36  ? 134 GLY A CA    1 
ATOM   2060  C  CA    B GLY A 1 134 ? -17.320 0.023   29.413  0.80 26.29  ? 134 GLY A CA    1 
ATOM   2061  C  C     A GLY A 1 134 ? -16.833 -1.167  29.460  0.20 24.98  ? 134 GLY A C     1 
ATOM   2062  C  C     B GLY A 1 134 ? -16.679 -1.339  29.201  0.80 25.00  ? 134 GLY A C     1 
ATOM   2063  O  O     A GLY A 1 134 ? -17.626 -2.110  29.379  0.20 27.78  ? 134 GLY A O     1 
ATOM   2064  O  O     B GLY A 1 134 ? -17.369 -2.352  29.074  0.80 27.57  ? 134 GLY A O     1 
ATOM   2065  N  N     A PHE A 1 135 ? -15.557 -1.241  29.096  0.20 27.28  ? 135 PHE A N     1 
ATOM   2066  N  N     B PHE A 1 135 ? -15.337 -1.331  29.177  0.80 27.27  ? 135 PHE A N     1 
ATOM   2067  C  CA    A PHE A 1 135 ? -14.989 -2.418  28.459  0.20 25.28  ? 135 PHE A CA    1 
ATOM   2068  C  CA    B PHE A 1 135 ? -14.539 -2.410  28.595  0.80 26.23  ? 135 PHE A CA    1 
ATOM   2069  C  C     A PHE A 1 135 ? -13.868 -2.987  29.316  0.20 24.40  ? 135 PHE A C     1 
ATOM   2070  C  C     B PHE A 1 135 ? -13.401 -2.815  29.524  0.80 23.21  ? 135 PHE A C     1 
ATOM   2071  O  O     A PHE A 1 135 ? -13.187 -2.259  30.044  0.20 27.31  ? 135 PHE A O     1 
ATOM   2072  O  O     B PHE A 1 135 ? -12.768 -1.961  30.153  0.80 30.16  ? 135 PHE A O     1 
ATOM   2073  C  CB    A PHE A 1 135 ? -14.450 -2.084  27.056  0.20 25.48  ? 135 PHE A CB    1 
ATOM   2074  C  CB    B PHE A 1 135 ? -13.929 -1.989  27.224  0.80 21.96  ? 135 PHE A CB    1 
ATOM   2075  C  CG    A PHE A 1 135 ? -15.505 -1.597  26.100  0.20 23.82  ? 135 PHE A CG    1 
ATOM   2076  C  CG    B PHE A 1 135 ? -14.935 -1.434  26.238  0.80 21.23  ? 135 PHE A CG    1 
ATOM   2077  C  CD1   A PHE A 1 135 ? -15.885 -0.265  26.085  0.20 26.40  ? 135 PHE A CD1   1 
ATOM   2078  C  CD1   B PHE A 1 135 ? -15.736 -2.289  25.499  0.80 25.40  ? 135 PHE A CD1   1 
ATOM   2079  C  CD2   A PHE A 1 135 ? -16.120 -2.474  25.222  0.20 26.72  ? 135 PHE A CD2   1 
ATOM   2080  C  CD2   B PHE A 1 135 ? -15.061 -0.061  26.045  0.80 22.34  ? 135 PHE A CD2   1 
ATOM   2081  C  CE1   A PHE A 1 135 ? -16.859 0.186   25.209  0.20 28.27  ? 135 PHE A CE1   1 
ATOM   2082  C  CE1   B PHE A 1 135 ? -16.666 -1.793  24.592  0.80 28.06  ? 135 PHE A CE1   1 
ATOM   2083  C  CE2   A PHE A 1 135 ? -17.093 -2.031  24.344  0.20 26.65  ? 135 PHE A CE2   1 
ATOM   2084  C  CE2   B PHE A 1 135 ? -15.980 0.447   25.145  0.80 33.22  ? 135 PHE A CE2   1 
ATOM   2085  C  CZ    A PHE A 1 135 ? -17.463 -0.697  24.338  0.20 28.29  ? 135 PHE A CZ    1 
ATOM   2086  C  CZ    B PHE A 1 135 ? -16.792 -0.418  24.417  0.80 34.07  ? 135 PHE A CZ    1 
ATOM   2087  N  N     A LEU A 1 136 ? -13.693 -4.303  29.231  0.20 24.53  ? 136 LEU A N     1 
ATOM   2088  N  N     B LEU A 1 136 ? -13.136 -4.123  29.589  0.80 24.31  ? 136 LEU A N     1 
ATOM   2089  C  CA    A LEU A 1 136 ? -12.546 -4.988  29.807  0.20 24.56  ? 136 LEU A CA    1 
ATOM   2090  C  CA    B LEU A 1 136 ? -11.948 -4.686  30.228  0.80 23.07  ? 136 LEU A CA    1 
ATOM   2091  C  C     A LEU A 1 136 ? -11.648 -5.455  28.671  0.20 22.88  ? 136 LEU A C     1 
ATOM   2092  C  C     B LEU A 1 136 ? -11.101 -5.283  29.113  0.80 21.30  ? 136 LEU A C     1 
ATOM   2093  O  O     A LEU A 1 136 ? -12.127 -6.073  27.714  0.20 21.96  ? 136 LEU A O     1 
ATOM   2094  O  O     B LEU A 1 136 ? -11.564 -6.195  28.420  0.80 25.31  ? 136 LEU A O     1 
ATOM   2095  C  CB    A LEU A 1 136 ? -12.979 -6.174  30.670  0.20 22.80  ? 136 LEU A CB    1 
ATOM   2096  C  CB    B LEU A 1 136 ? -12.288 -5.782  31.240  0.80 23.22  ? 136 LEU A CB    1 
ATOM   2097  C  CG    A LEU A 1 136 ? -13.794 -5.847  31.927  0.20 25.93  ? 136 LEU A CG    1 
ATOM   2098  C  CG    B LEU A 1 136 ? -13.172 -5.517  32.474  0.80 24.78  ? 136 LEU A CG    1 
ATOM   2099  C  CD1   A LEU A 1 136 ? -14.049 -7.104  32.742  0.20 24.50  ? 136 LEU A CD1   1 
ATOM   2100  C  CD1   B LEU A 1 136 ? -14.570 -5.141  32.047  0.80 27.49  ? 136 LEU A CD1   1 
ATOM   2101  C  CD2   A LEU A 1 136 ? -13.092 -4.791  32.770  0.20 23.11  ? 136 LEU A CD2   1 
ATOM   2102  C  CD2   B LEU A 1 136 ? -13.208 -6.752  33.354  0.80 29.29  ? 136 LEU A CD2   1 
ATOM   2103  N  N     A VAL A 1 137 ? -10.355 -5.147  28.769  0.20 22.31  ? 137 VAL A N     1 
ATOM   2104  N  N     B VAL A 1 137 ? -9.870  -4.794  28.956  0.80 19.18  ? 137 VAL A N     1 
ATOM   2105  C  CA    A VAL A 1 137 ? -9.378  -5.470  27.734  0.20 23.03  ? 137 VAL A CA    1 
ATOM   2106  C  CA    B VAL A 1 137 ? -9.015  -5.151  27.812  0.80 22.86  ? 137 VAL A CA    1 
ATOM   2107  C  C     A VAL A 1 137 ? -8.252  -6.285  28.355  0.20 21.27  ? 137 VAL A C     1 
ATOM   2108  C  C     B VAL A 1 137 ? -7.788  -5.913  28.311  0.80 19.15  ? 137 VAL A C     1 
ATOM   2109  O  O     A VAL A 1 137 ? -7.767  -5.962  29.445  0.20 22.01  ? 137 VAL A O     1 
ATOM   2110  O  O     B VAL A 1 137 ? -6.965  -5.359  29.046  0.80 23.97  ? 137 VAL A O     1 
ATOM   2111  C  CB    A VAL A 1 137 ? -8.817  -4.198  27.063  0.20 23.94  ? 137 VAL A CB    1 
ATOM   2112  C  CB    B VAL A 1 137 ? -8.601  -3.902  27.019  0.80 25.18  ? 137 VAL A CB    1 
ATOM   2113  C  CG1   A VAL A 1 137 ? -7.933  -4.563  25.867  0.20 23.97  ? 137 VAL A CG1   1 
ATOM   2114  C  CG1   B VAL A 1 137 ? -7.656  -4.270  25.843  0.80 22.89  ? 137 VAL A CG1   1 
ATOM   2115  C  CG2   A VAL A 1 137 ? -9.947  -3.276  26.638  0.20 28.90  ? 137 VAL A CG2   1 
ATOM   2116  C  CG2   B VAL A 1 137 ? -9.832  -3.184  26.506  0.80 29.88  ? 137 VAL A CG2   1 
ATOM   2117  N  N     A PHE A 1 138 ? -7.836  -7.340  27.653  0.20 22.86  ? 138 PHE A N     1 
ATOM   2118  N  N     B PHE A 1 138 ? -7.637  -7.166  27.876  0.80 23.88  ? 138 PHE A N     1 
ATOM   2119  C  CA    A PHE A 1 138 ? -6.782  -8.242  28.104  0.20 22.52  ? 138 PHE A CA    1 
ATOM   2120  C  CA    B PHE A 1 138 ? -6.556  -8.052  28.312  0.80 20.96  ? 138 PHE A CA    1 
ATOM   2121  C  C     A PHE A 1 138 ? -5.755  -8.400  26.992  0.20 20.75  ? 138 PHE A C     1 
ATOM   2122  C  C     B PHE A 1 138 ? -5.525  -8.197  27.194  0.80 19.84  ? 138 PHE A C     1 
ATOM   2123  O  O     A PHE A 1 138 ? -6.122  -8.666  25.842  0.20 21.36  ? 138 PHE A O     1 
ATOM   2124  O  O     B PHE A 1 138 ? -5.889  -8.560  26.068  0.80 21.80  ? 138 PHE A O     1 
ATOM   2125  C  CB    A PHE A 1 138 ? -7.350  -9.616  28.480  0.20 21.42  ? 138 PHE A CB    1 
ATOM   2126  C  CB    B PHE A 1 138 ? -7.083  -9.454  28.640  0.80 19.90  ? 138 PHE A CB    1 
ATOM   2127  C  CG    A PHE A 1 138 ? -8.209  -9.611  29.715  0.20 24.40  ? 138 PHE A CG    1 
ATOM   2128  C  CG    B PHE A 1 138 ? -8.081  -9.526  29.774  0.80 24.69  ? 138 PHE A CG    1 
ATOM   2129  C  CD1   A PHE A 1 138 ? -9.503  -9.113  29.679  0.20 24.32  ? 138 PHE A CD1   1 
ATOM   2130  C  CD1   B PHE A 1 138 ? -9.306  -8.877  29.708  0.80 24.36  ? 138 PHE A CD1   1 
ATOM   2131  C  CD2   A PHE A 1 138 ? -7.732  -10.132 30.904  0.20 25.93  ? 138 PHE A CD2   1 
ATOM   2132  C  CD2   B PHE A 1 138 ? -7.824  -10.338 30.861  0.80 26.55  ? 138 PHE A CD2   1 
ATOM   2133  C  CE1   A PHE A 1 138 ? -10.295 -9.114  30.814  0.20 29.36  ? 138 PHE A CE1   1 
ATOM   2134  C  CE1   B PHE A 1 138 ? -10.223 -8.973  30.751  0.80 29.93  ? 138 PHE A CE1   1 
ATOM   2135  C  CE2   A PHE A 1 138 ? -8.521  -10.141 32.043  0.20 27.48  ? 138 PHE A CE2   1 
ATOM   2136  C  CE2   B PHE A 1 138 ? -8.747  -10.458 31.903  0.80 27.03  ? 138 PHE A CE2   1 
ATOM   2137  C  CZ    A PHE A 1 138 ? -9.803  -9.631  31.997  0.20 29.74  ? 138 PHE A CZ    1 
ATOM   2138  C  CZ    B PHE A 1 138 ? -9.943  -9.774  31.844  0.80 30.83  ? 138 PHE A CZ    1 
ATOM   2139  N  N     A HIS A 1 139 ? -4.478  -8.250  27.331  0.20 19.42  ? 139 HIS A N     1 
ATOM   2140  N  N     B HIS A 1 139 ? -4.242  -7.987  27.512  0.80 17.73  ? 139 HIS A N     1 
ATOM   2141  C  CA    A HIS A 1 139 ? -3.405  -8.354  26.344  0.20 21.48  ? 139 HIS A CA    1 
ATOM   2142  C  CA    B HIS A 1 139 ? -3.219  -8.027  26.464  0.80 22.01  ? 139 HIS A CA    1 
ATOM   2143  C  C     A HIS A 1 139 ? -2.075  -8.429  27.085  0.20 20.91  ? 139 HIS A C     1 
ATOM   2144  C  C     B HIS A 1 139 ? -1.819  -8.036  27.066  0.80 21.84  ? 139 HIS A C     1 
ATOM   2145  O  O     A HIS A 1 139 ? -2.020  -8.374  28.317  0.20 22.67  ? 139 HIS A O     1 
ATOM   2146  O  O     B HIS A 1 139 ? -1.593  -7.526  28.168  0.80 22.04  ? 139 HIS A O     1 
ATOM   2147  C  CB    A HIS A 1 139 ? -3.430  -7.176  25.364  0.20 20.49  ? 139 HIS A CB    1 
ATOM   2148  C  CB    B HIS A 1 139 ? -3.353  -6.822  25.515  0.80 19.57  ? 139 HIS A CB    1 
ATOM   2149  C  CG    A HIS A 1 139 ? -3.123  -5.854  25.999  0.20 21.70  ? 139 HIS A CG    1 
ATOM   2150  C  CG    B HIS A 1 139 ? -3.108  -5.506  26.187  0.80 22.61  ? 139 HIS A CG    1 
ATOM   2151  N  ND1   A HIS A 1 139 ? -1.877  -5.266  25.933  0.20 22.80  ? 139 HIS A ND1   1 
ATOM   2152  N  ND1   B HIS A 1 139 ? -2.021  -4.707  25.897  0.80 23.18  ? 139 HIS A ND1   1 
ATOM   2153  C  CD2   A HIS A 1 139 ? -3.901  -5.007  26.715  0.20 21.12  ? 139 HIS A CD2   1 
ATOM   2154  C  CD2   B HIS A 1 139 ? -3.799  -4.861  27.158  0.80 21.58  ? 139 HIS A CD2   1 
ATOM   2155  C  CE1   A HIS A 1 139 ? -1.902  -4.114  26.579  0.20 23.32  ? 139 HIS A CE1   1 
ATOM   2156  C  CE1   B HIS A 1 139 ? -2.059  -3.623  26.654  0.80 24.23  ? 139 HIS A CE1   1 
ATOM   2157  N  NE2   A HIS A 1 139 ? -3.117  -3.934  27.065  0.20 22.23  ? 139 HIS A NE2   1 
ATOM   2158  N  NE2   B HIS A 1 139 ? -3.121  -3.697  27.438  0.80 18.98  ? 139 HIS A NE2   1 
ATOM   2159  N  N     A SER A 1 140 ? -1.000  -8.559  26.316  0.20 21.22  ? 140 SER A N     1 
ATOM   2160  N  N     B SER A 1 140 ? -0.873  -8.579  26.300  0.80 20.86  ? 140 SER A N     1 
ATOM   2161  C  CA    A SER A 1 140 ? 0.356   -8.538  26.835  0.20 23.61  ? 140 SER A CA    1 
ATOM   2162  C  CA    B SER A 1 140 ? 0.539   -8.459  26.635  0.80 24.28  ? 140 SER A CA    1 
ATOM   2163  C  C     A SER A 1 140 ? 1.073   -7.284  26.355  0.20 20.08  ? 140 SER A C     1 
ATOM   2164  C  C     B SER A 1 140 ? 1.056   -7.069  26.288  0.80 19.43  ? 140 SER A C     1 
ATOM   2165  O  O     A SER A 1 140 ? 0.648   -6.625  25.402  0.20 23.19  ? 140 SER A O     1 
ATOM   2166  O  O     B SER A 1 140 ? 0.528   -6.396  25.396  0.80 23.49  ? 140 SER A O     1 
ATOM   2167  C  CB    A SER A 1 140 ? 1.135   -9.785  26.397  0.20 25.49  ? 140 SER A CB    1 
ATOM   2168  C  CB    B SER A 1 140 ? 1.380   -9.506  25.889  0.80 25.77  ? 140 SER A CB    1 
ATOM   2169  O  OG    A SER A 1 140 ? 1.217   -9.867  24.983  0.20 23.19  ? 140 SER A OG    1 
ATOM   2170  O  OG    B SER A 1 140 ? 1.318   -9.330  24.482  0.80 24.28  ? 140 SER A OG    1 
ATOM   2171  N  N     A PHE A 1 141 ? 2.170   -6.953  27.039  0.20 20.27  ? 141 PHE A N     1 
ATOM   2172  N  N     B PHE A 1 141 ? 2.087   -6.634  27.030  0.80 18.38  ? 141 PHE A N     1 
ATOM   2173  C  CA    A PHE A 1 141 ? 3.013   -5.837  26.626  0.20 24.30  ? 141 PHE A CA    1 
ATOM   2174  C  CA    B PHE A 1 141 ? 2.910   -5.504  26.592  0.80 23.78  ? 141 PHE A CA    1 
ATOM   2175  C  C     A PHE A 1 141 ? 4.061   -6.237  25.596  0.20 23.28  ? 141 PHE A C     1 
ATOM   2176  C  C     B PHE A 1 141 ? 3.831   -5.894  25.442  0.80 25.26  ? 141 PHE A C     1 
ATOM   2177  O  O     A PHE A 1 141 ? 4.409   -5.426  24.729  0.20 24.65  ? 141 PHE A O     1 
ATOM   2178  O  O     B PHE A 1 141 ? 4.156   -5.057  24.584  0.80 24.78  ? 141 PHE A O     1 
ATOM   2179  C  CB    A PHE A 1 141 ? 3.718   -5.225  27.840  0.20 25.78  ? 141 PHE A CB    1 
ATOM   2180  C  CB    B PHE A 1 141 ? 3.799   -5.001  27.727  0.80 25.91  ? 141 PHE A CB    1 
ATOM   2181  C  CG    A PHE A 1 141 ? 2.862   -4.275  28.633  0.20 24.39  ? 141 PHE A CG    1 
ATOM   2182  C  CG    B PHE A 1 141 ? 3.147   -4.015  28.658  0.80 25.04  ? 141 PHE A CG    1 
ATOM   2183  C  CD1   A PHE A 1 141 ? 1.762   -3.659  28.058  0.20 24.96  ? 141 PHE A CD1   1 
ATOM   2184  C  CD1   B PHE A 1 141 ? 1.884   -3.501  28.411  0.80 25.22  ? 141 PHE A CD1   1 
ATOM   2185  C  CD2   A PHE A 1 141 ? 3.170   -3.987  29.952  0.20 26.68  ? 141 PHE A CD2   1 
ATOM   2186  C  CD2   B PHE A 1 141 ? 3.845   -3.570  29.775  0.80 24.90  ? 141 PHE A CD2   1 
ATOM   2187  C  CE1   A PHE A 1 141 ? 0.980   -2.781  28.789  0.20 28.44  ? 141 PHE A CE1   1 
ATOM   2188  C  CE1   B PHE A 1 141 ? 1.311   -2.582  29.294  0.80 30.79  ? 141 PHE A CE1   1 
ATOM   2189  C  CE2   A PHE A 1 141 ? 2.393   -3.108  30.687  0.20 26.41  ? 141 PHE A CE2   1 
ATOM   2190  C  CE2   B PHE A 1 141 ? 3.285   -2.655  30.650  0.80 29.45  ? 141 PHE A CE2   1 
ATOM   2191  C  CZ    A PHE A 1 141 ? 1.297   -2.504  30.103  0.20 26.32  ? 141 PHE A CZ    1 
ATOM   2192  C  CZ    B PHE A 1 141 ? 2.025   -2.160  30.410  0.80 20.34  ? 141 PHE A CZ    1 
ATOM   2193  N  N     A GLY A 1 142 ? 4.571   -7.469  25.665  0.20 24.44  ? 142 GLY A N     1 
ATOM   2194  N  N     B GLY A 1 142 ? 4.287   -7.138  25.430  0.80 22.65  ? 142 GLY A N     1 
ATOM   2195  C  CA    A GLY A 1 142 ? 5.689   -7.850  24.819  0.20 24.65  ? 142 GLY A CA    1 
ATOM   2196  C  CA    B GLY A 1 142 ? 5.433   -7.520  24.619  0.80 26.62  ? 142 GLY A CA    1 
ATOM   2197  C  C     A GLY A 1 142 ? 5.306   -8.271  23.416  0.20 25.98  ? 142 GLY A C     1 
ATOM   2198  C  C     B GLY A 1 142 ? 5.138   -7.915  23.187  0.80 26.90  ? 142 GLY A C     1 
ATOM   2199  O  O     A GLY A 1 142 ? 6.115   -8.144  22.490  0.20 24.69  ? 142 GLY A O     1 
ATOM   2200  O  O     B GLY A 1 142 ? 5.971   -7.721  22.291  0.80 25.29  ? 142 GLY A O     1 
ATOM   2201  N  N     A GLY A 1 143 ? 4.093   -8.775  23.234  0.20 23.96  ? 143 GLY A N     1 
ATOM   2202  N  N     B GLY A 1 143 ? 3.969   -8.485  22.957  0.80 24.08  ? 143 GLY A N     1 
ATOM   2203  C  CA    A GLY A 1 143 ? 3.682   -9.281  21.943  0.20 23.96  ? 143 GLY A CA    1 
ATOM   2204  C  CA    B GLY A 1 143 ? 3.632   -8.945  21.630  0.80 24.43  ? 143 GLY A CA    1 
ATOM   2205  C  C     A GLY A 1 143 ? 3.494   -8.185  20.912  0.20 23.52  ? 143 GLY A C     1 
ATOM   2206  C  C     B GLY A 1 143 ? 3.356   -7.808  20.666  0.80 24.00  ? 143 GLY A C     1 
ATOM   2207  O  O     A GLY A 1 143 ? 3.529   -6.988  21.203  0.20 24.52  ? 143 GLY A O     1 
ATOM   2208  O  O     B GLY A 1 143 ? 2.976   -6.693  21.042  0.80 23.07  ? 143 GLY A O     1 
ATOM   2209  N  N     A GLY A 1 144 ? 3.297   -8.619  19.671  0.20 23.63  ? 144 GLY A N     1 
ATOM   2210  N  N     B GLY A 1 144 ? 3.559   -8.102  19.384  0.80 23.19  ? 144 GLY A N     1 
ATOM   2211  C  CA    A GLY A 1 144 ? 3.029   -7.712  18.572  0.20 24.25  ? 144 GLY A CA    1 
ATOM   2212  C  CA    B GLY A 1 144 ? 3.189   -7.143  18.356  0.80 25.58  ? 144 GLY A CA    1 
ATOM   2213  C  C     A GLY A 1 144 ? 1.552   -7.417  18.411  0.20 23.77  ? 144 GLY A C     1 
ATOM   2214  C  C     B GLY A 1 144 ? 1.692   -6.906  18.280  0.80 23.27  ? 144 GLY A C     1 
ATOM   2215  O  O     A GLY A 1 144 ? 1.162   -6.266  18.194  0.20 24.06  ? 144 GLY A O     1 
ATOM   2216  O  O     B GLY A 1 144 ? 1.243   -5.782  18.048  0.80 26.32  ? 144 GLY A O     1 
ATOM   2217  N  N     A THR A 1 145 ? 0.717   -8.455  18.508  0.20 21.20  ? 145 THR A N     1 
ATOM   2218  N  N     B THR A 1 145 ? 0.896   -7.960  18.459  0.80 23.08  ? 145 THR A N     1 
ATOM   2219  C  CA    A THR A 1 145 ? -0.726  -8.241  18.481  0.20 23.66  ? 145 THR A CA    1 
ATOM   2220  C  CA    B THR A 1 145 ? -0.550  -7.774  18.528  0.80 23.41  ? 145 THR A CA    1 
ATOM   2221  C  C     A THR A 1 145 ? -1.225  -7.655  19.798  0.20 24.08  ? 145 THR A C     1 
ATOM   2222  C  C     B THR A 1 145 ? -0.950  -7.161  19.868  0.80 24.88  ? 145 THR A C     1 
ATOM   2223  O  O     A THR A 1 145 ? -2.171  -6.860  19.805  0.20 25.93  ? 145 THR A O     1 
ATOM   2224  O  O     B THR A 1 145 ? -1.641  -6.132  19.914  0.80 23.56  ? 145 THR A O     1 
ATOM   2225  C  CB    A THR A 1 145 ? -1.444  -9.556  18.168  0.20 25.80  ? 145 THR A CB    1 
ATOM   2226  C  CB    B THR A 1 145 ? -1.240  -9.118  18.288  0.80 27.05  ? 145 THR A CB    1 
ATOM   2227  O  OG1   A THR A 1 145 ? -0.910  -10.116 16.962  0.20 22.63  ? 145 THR A OG1   1 
ATOM   2228  O  OG1   B THR A 1 145 ? -0.841  -9.632  17.014  0.80 21.31  ? 145 THR A OG1   1 
ATOM   2229  C  CG2   A THR A 1 145 ? -2.939  -9.330  17.986  0.20 23.74  ? 145 THR A CG2   1 
ATOM   2230  C  CG2   B THR A 1 145 ? -2.762  -8.988  18.325  0.80 26.25  ? 145 THR A CG2   1 
ATOM   2231  N  N     A GLY A 1 146 ? -0.593  -8.020  20.916  0.20 22.33  ? 146 GLY A N     1 
ATOM   2232  N  N     B GLY A 1 146 ? -0.477  -7.754  20.966  0.80 21.60  ? 146 GLY A N     1 
ATOM   2233  C  CA    A GLY A 1 146 ? -1.012  -7.487  22.202  0.20 23.87  ? 146 GLY A CA    1 
ATOM   2234  C  CA    B GLY A 1 146 ? -0.864  -7.279  22.288  0.80 24.13  ? 146 GLY A CA    1 
ATOM   2235  C  C     A GLY A 1 146 ? -0.643  -6.031  22.395  0.20 24.73  ? 146 GLY A C     1 
ATOM   2236  C  C     B GLY A 1 146 ? -0.505  -5.823  22.510  0.80 25.32  ? 146 GLY A C     1 
ATOM   2237  O  O     A GLY A 1 146 ? -1.358  -5.293  23.078  0.20 25.96  ? 146 GLY A O     1 
ATOM   2238  O  O     B GLY A 1 146 ? -1.257  -5.074  23.131  0.80 26.82  ? 146 GLY A O     1 
ATOM   2239  N  N     A SER A 1 147 ? 0.466   -5.595  21.803  0.20 22.65  ? 147 SER A N     1 
ATOM   2240  N  N     B SER A 1 147 ? 0.651   -5.401  22.008  0.80 21.97  ? 147 SER A N     1 
ATOM   2241  C  CA    A SER A 1 147 ? 0.921   -4.217  21.945  0.20 23.02  ? 147 SER A CA    1 
ATOM   2242  C  CA    B SER A 1 147 ? 1.003   -3.990  22.122  0.80 22.03  ? 147 SER A CA    1 
ATOM   2243  C  C     A SER A 1 147 ? 0.545   -3.330  20.768  0.20 25.44  ? 147 SER A C     1 
ATOM   2244  C  C     B SER A 1 147 ? 0.355   -3.171  21.012  0.80 25.35  ? 147 SER A C     1 
ATOM   2245  O  O     A SER A 1 147 ? 0.358   -2.124  20.955  0.20 25.15  ? 147 SER A O     1 
ATOM   2246  O  O     B SER A 1 147 ? -0.467  -2.289  21.277  0.80 22.84  ? 147 SER A O     1 
ATOM   2247  C  CB    A SER A 1 147 ? 2.440   -4.180  22.129  0.20 24.05  ? 147 SER A CB    1 
ATOM   2248  C  CB    B SER A 1 147 ? 2.522   -3.820  22.099  0.80 23.78  ? 147 SER A CB    1 
ATOM   2249  O  OG    A SER A 1 147 ? 3.082   -4.830  21.045  0.20 23.35  ? 147 SER A OG    1 
ATOM   2250  O  OG    B SER A 1 147 ? 3.025   -4.203  20.828  0.80 23.90  ? 147 SER A OG    1 
ATOM   2251  N  N     A GLY A 1 148 ? 0.431   -3.890  19.565  0.20 24.15  ? 148 GLY A N     1 
ATOM   2252  N  N     B GLY A 1 148 ? 0.680   -3.490  19.756  0.80 23.72  ? 148 GLY A N     1 
ATOM   2253  C  CA    A GLY A 1 148 ? 0.092   -3.105  18.394  0.20 23.66  ? 148 GLY A CA    1 
ATOM   2254  C  CA    B GLY A 1 148 ? 0.330   -2.600  18.659  0.80 21.88  ? 148 GLY A CA    1 
ATOM   2255  C  C     A GLY A 1 148 ? -1.394  -3.019  18.105  0.20 26.04  ? 148 GLY A C     1 
ATOM   2256  C  C     B GLY A 1 148 ? -1.152  -2.570  18.326  0.80 26.70  ? 148 GLY A C     1 
ATOM   2257  O  O     A GLY A 1 148 ? -1.921  -1.931  17.850  0.20 25.06  ? 148 GLY A O     1 
ATOM   2258  O  O     B GLY A 1 148 ? -1.732  -1.494  18.130  0.80 22.93  ? 148 GLY A O     1 
ATOM   2259  N  N     A PHE A 1 149 ? -2.084  -4.161  18.138  0.20 25.50  ? 149 PHE A N     1 
ATOM   2260  N  N     B PHE A 1 149 ? -1.780  -3.746  18.213  0.80 26.18  ? 149 PHE A N     1 
ATOM   2261  C  CA    A PHE A 1 149 ? -3.507  -4.169  17.818  0.20 27.47  ? 149 PHE A CA    1 
ATOM   2262  C  CA    B PHE A 1 149 ? -3.206  -3.762  17.909  0.80 28.18  ? 149 PHE A CA    1 
ATOM   2263  C  C     A PHE A 1 149 ? -4.360  -3.632  18.961  0.20 25.29  ? 149 PHE A C     1 
ATOM   2264  C  C     B PHE A 1 149 ? -4.035  -3.205  19.059  0.80 26.66  ? 149 PHE A C     1 
ATOM   2265  O  O     A PHE A 1 149 ? -5.450  -3.107  18.714  0.20 25.05  ? 149 PHE A O     1 
ATOM   2266  O  O     B PHE A 1 149 ? -5.053  -2.542  18.818  0.80 22.58  ? 149 PHE A O     1 
ATOM   2267  C  CB    A PHE A 1 149 ? -3.960  -5.582  17.445  0.20 25.67  ? 149 PHE A CB    1 
ATOM   2268  C  CB    B PHE A 1 149 ? -3.684  -5.174  17.557  0.80 25.58  ? 149 PHE A CB    1 
ATOM   2269  C  CG    A PHE A 1 149 ? -5.376  -5.651  16.942  0.20 25.00  ? 149 PHE A CG    1 
ATOM   2270  C  CG    B PHE A 1 149 ? -5.105  -5.212  17.076  0.80 24.74  ? 149 PHE A CG    1 
ATOM   2271  C  CD1   A PHE A 1 149 ? -5.662  -5.421  15.606  0.20 27.93  ? 149 PHE A CD1   1 
ATOM   2272  C  CD1   B PHE A 1 149 ? -5.408  -4.940  15.752  0.80 27.16  ? 149 PHE A CD1   1 
ATOM   2273  C  CD2   A PHE A 1 149 ? -6.419  -5.942  17.803  0.20 28.45  ? 149 PHE A CD2   1 
ATOM   2274  C  CD2   B PHE A 1 149 ? -6.144  -5.477  17.952  0.80 29.86  ? 149 PHE A CD2   1 
ATOM   2275  C  CE1   A PHE A 1 149 ? -6.962  -5.482  15.141  0.20 29.83  ? 149 PHE A CE1   1 
ATOM   2276  C  CE1   B PHE A 1 149 ? -6.716  -4.959  15.309  0.80 31.12  ? 149 PHE A CE1   1 
ATOM   2277  C  CE2   A PHE A 1 149 ? -7.720  -6.001  17.344  0.20 27.83  ? 149 PHE A CE2   1 
ATOM   2278  C  CE2   B PHE A 1 149 ? -7.454  -5.489  17.515  0.80 28.61  ? 149 PHE A CE2   1 
ATOM   2279  C  CZ    A PHE A 1 149 ? -7.994  -5.772  16.012  0.20 29.44  ? 149 PHE A CZ    1 
ATOM   2280  C  CZ    B PHE A 1 149 ? -7.745  -5.230  16.193  0.80 30.12  ? 149 PHE A CZ    1 
ATOM   2281  N  N     A THR A 1 150 ? -3.889  -3.744  20.205  0.20 25.05  ? 150 THR A N     1 
ATOM   2282  N  N     B THR A 1 150 ? -3.615  -3.439  20.306  0.80 24.05  ? 150 THR A N     1 
ATOM   2283  C  CA    A THR A 1 150 ? -4.676  -3.258  21.335  0.20 22.42  ? 150 THR A CA    1 
ATOM   2284  C  CA    B THR A 1 150 ? -4.394  -2.951  21.442  0.80 21.93  ? 150 THR A CA    1 
ATOM   2285  C  C     A THR A 1 150 ? -4.777  -1.736  21.323  0.20 25.63  ? 150 THR A C     1 
ATOM   2286  C  C     B THR A 1 150 ? -4.434  -1.427  21.468  0.80 26.27  ? 150 THR A C     1 
ATOM   2287  O  O     A THR A 1 150 ? -5.866  -1.177  21.498  0.20 25.11  ? 150 THR A O     1 
ATOM   2288  O  O     B THR A 1 150 ? -5.482  -0.836  21.752  0.80 25.28  ? 150 THR A O     1 
ATOM   2289  C  CB    A THR A 1 150 ? -4.069  -3.747  22.652  0.20 23.19  ? 150 THR A CB    1 
ATOM   2290  C  CB    B THR A 1 150 ? -3.828  -3.496  22.758  0.80 23.19  ? 150 THR A CB    1 
ATOM   2291  O  OG1   A THR A 1 150 ? -4.120  -5.179  22.702  0.20 21.59  ? 150 THR A OG1   1 
ATOM   2292  O  OG1   B THR A 1 150 ? -3.963  -4.922  22.796  0.80 21.27  ? 150 THR A OG1   1 
ATOM   2293  C  CG2   A THR A 1 150 ? -4.832  -3.175  23.843  0.20 22.47  ? 150 THR A CG2   1 
ATOM   2294  C  CG2   B THR A 1 150 ? -4.582  -2.905  23.969  0.80 21.63  ? 150 THR A CG2   1 
ATOM   2295  N  N     A SER A 1 151 ? -3.651  -1.049  21.108  0.20 27.22  ? 151 SER A N     1 
ATOM   2296  N  N     B SER A 1 151 ? -3.311  -0.763  21.162  0.80 26.79  ? 151 SER A N     1 
ATOM   2297  C  CA    A SER A 1 151 ? -3.660  0.411   21.122  0.20 27.29  ? 151 SER A CA    1 
ATOM   2298  C  CA    B SER A 1 151 ? -3.353  0.695   21.157  0.80 27.28  ? 151 SER A CA    1 
ATOM   2299  C  C     A SER A 1 151 ? -4.570  0.963   20.033  0.20 27.93  ? 151 SER A C     1 
ATOM   2300  C  C     B SER A 1 151 ? -4.216  1.209   20.011  0.80 27.66  ? 151 SER A C     1 
ATOM   2301  O  O     A SER A 1 151 ? -5.380  1.863   20.283  0.20 28.13  ? 151 SER A O     1 
ATOM   2302  O  O     B SER A 1 151 ? -4.955  2.179   20.185  0.80 29.02  ? 151 SER A O     1 
ATOM   2303  C  CB    A SER A 1 151 ? -2.239  0.950   20.964  0.20 29.26  ? 151 SER A CB    1 
ATOM   2304  C  CB    B SER A 1 151 ? -1.943  1.295   21.116  0.80 29.25  ? 151 SER A CB    1 
ATOM   2305  O  OG    A SER A 1 151 ? -1.719  0.637   19.685  0.20 31.70  ? 151 SER A OG    1 
ATOM   2306  O  OG    B SER A 1 151 ? -1.163  0.789   20.055  0.80 35.36  ? 151 SER A OG    1 
ATOM   2307  N  N     A LEU A 1 152 ? -4.451  0.429   18.813  0.20 26.74  ? 152 LEU A N     1 
ATOM   2308  N  N     B LEU A 1 152 ? -4.170  0.548   18.847  0.80 25.91  ? 152 LEU A N     1 
ATOM   2309  C  CA    A LEU A 1 152 ? -5.347  0.829   17.733  0.20 29.09  ? 152 LEU A CA    1 
ATOM   2310  C  CA    B LEU A 1 152 ? -5.065  0.913   17.750  0.80 29.67  ? 152 LEU A CA    1 
ATOM   2311  C  C     A LEU A 1 152 ? -6.801  0.587   18.109  0.20 29.22  ? 152 LEU A C     1 
ATOM   2312  C  C     B LEU A 1 152 ? -6.517  0.733   18.158  0.80 29.83  ? 152 LEU A C     1 
ATOM   2313  O  O     A LEU A 1 152 ? -7.679  1.398   17.790  0.20 28.72  ? 152 LEU A O     1 
ATOM   2314  O  O     B LEU A 1 152 ? -7.358  1.607   17.913  0.80 28.39  ? 152 LEU A O     1 
ATOM   2315  C  CB    A LEU A 1 152 ? -4.995  0.072   16.452  0.20 27.02  ? 152 LEU A CB    1 
ATOM   2316  C  CB    B LEU A 1 152 ? -4.762  0.076   16.504  0.80 26.31  ? 152 LEU A CB    1 
ATOM   2317  C  CG    A LEU A 1 152 ? -5.969  0.264   15.286  0.20 29.88  ? 152 LEU A CG    1 
ATOM   2318  C  CG    B LEU A 1 152 ? -5.699  0.341   15.306  0.80 30.78  ? 152 LEU A CG    1 
ATOM   2319  C  CD1   A LEU A 1 152 ? -6.047  1.731   14.898  0.20 31.29  ? 152 LEU A CD1   1 
ATOM   2320  C  CD1   B LEU A 1 152 ? -5.327  1.619   14.550  0.80 30.25  ? 152 LEU A CD1   1 
ATOM   2321  C  CD2   A LEU A 1 152 ? -5.575  -0.595  14.091  0.20 29.25  ? 152 LEU A CD2   1 
ATOM   2322  C  CD2   B LEU A 1 152 ? -5.726  -0.839  14.337  0.80 28.99  ? 152 LEU A CD2   1 
ATOM   2323  N  N     A LEU A 1 153 ? -7.075  -0.526  18.790  0.20 26.44  ? 153 LEU A N     1 
ATOM   2324  N  N     B LEU A 1 153 ? -6.830  -0.407  18.779  0.80 25.91  ? 153 LEU A N     1 
ATOM   2325  C  CA    A LEU A 1 153 ? -8.428  -0.784  19.268  0.20 26.78  ? 153 LEU A CA    1 
ATOM   2326  C  CA    B LEU A 1 153 ? -8.185  -0.644  19.266  0.80 26.40  ? 153 LEU A CA    1 
ATOM   2327  C  C     A LEU A 1 153 ? -8.845  0.241   20.315  0.20 27.79  ? 153 LEU A C     1 
ATOM   2328  C  C     B LEU A 1 153 ? -8.589  0.391   20.311  0.80 27.98  ? 153 LEU A C     1 
ATOM   2329  O  O     A LEU A 1 153 ? -9.958  0.778   20.258  0.20 25.94  ? 153 LEU A O     1 
ATOM   2330  O  O     B LEU A 1 153 ? -9.709  0.918   20.273  0.80 24.46  ? 153 LEU A O     1 
ATOM   2331  C  CB    A LEU A 1 153 ? -8.516  -2.201  19.829  0.20 28.17  ? 153 LEU A CB    1 
ATOM   2332  C  CB    B LEU A 1 153 ? -8.280  -2.053  19.846  0.80 28.27  ? 153 LEU A CB    1 
ATOM   2333  C  CG    A LEU A 1 153 ? -9.895  -2.684  20.277  0.20 23.30  ? 153 LEU A CG    1 
ATOM   2334  C  CG    B LEU A 1 153 ? -9.620  -2.482  20.452  0.80 22.61  ? 153 LEU A CG    1 
ATOM   2335  C  CD1   A LEU A 1 153 ? -10.909 -2.498  19.165  0.20 28.03  ? 153 LEU A CD1   1 
ATOM   2336  C  CD1   B LEU A 1 153 ? -10.674 -2.607  19.392  0.80 27.48  ? 153 LEU A CD1   1 
ATOM   2337  C  CD2   A LEU A 1 153 ? -9.811  -4.143  20.690  0.20 28.16  ? 153 LEU A CD2   1 
ATOM   2338  C  CD2   B LEU A 1 153 ? -9.422  -3.805  21.186  0.80 30.15  ? 153 LEU A CD2   1 
ATOM   2339  N  N     A MET A 1 154 ? -7.959  0.537   21.270  0.20 26.93  ? 154 MET A N     1 
ATOM   2340  N  N     B MET A 1 154 ? -7.685  0.706   21.245  0.80 25.68  ? 154 MET A N     1 
ATOM   2341  C  CA    A MET A 1 154 ? -8.274  1.528   22.293  0.20 30.52  ? 154 MET A CA    1 
ATOM   2342  C  CA    B MET A 1 154 ? -8.030  1.639   22.310  0.80 31.14  ? 154 MET A CA    1 
ATOM   2343  C  C     A MET A 1 154 ? -8.408  2.923   21.695  0.20 31.38  ? 154 MET A C     1 
ATOM   2344  C  C     B MET A 1 154 ? -8.296  3.026   21.743  0.80 31.67  ? 154 MET A C     1 
ATOM   2345  O  O     A MET A 1 154 ? -9.193  3.736   22.196  0.20 29.18  ? 154 MET A O     1 
ATOM   2346  O  O     B MET A 1 154 ? -9.199  3.729   22.206  0.80 29.03  ? 154 MET A O     1 
ATOM   2347  C  CB    A MET A 1 154 ? -7.207  1.511   23.387  0.20 26.87  ? 154 MET A CB    1 
ATOM   2348  C  CB    B MET A 1 154 ? -6.926  1.675   23.374  0.80 25.56  ? 154 MET A CB    1 
ATOM   2349  C  CG    A MET A 1 154 ? -7.073  0.173   24.101  0.20 27.81  ? 154 MET A CG    1 
ATOM   2350  C  CG    B MET A 1 154 ? -6.819  0.414   24.234  0.80 27.62  ? 154 MET A CG    1 
ATOM   2351  S  SD    A MET A 1 154 ? -8.402  -0.147  25.280  0.20 30.57  ? 154 MET A SD    1 
ATOM   2352  S  SD    B MET A 1 154 ? -8.102  0.240   25.497  0.80 40.41  ? 154 MET A SD    1 
ATOM   2353  C  CE    A MET A 1 154 ? -7.920  0.929   26.630  0.20 34.35  ? 154 MET A CE    1 
ATOM   2354  C  CE    B MET A 1 154 ? -7.251  0.825   26.974  0.80 33.93  ? 154 MET A CE    1 
ATOM   2355  N  N     A GLU A 1 155 ? -7.660  3.218   20.629  0.20 28.86  ? 155 GLU A N     1 
ATOM   2356  N  N     B GLU A 1 155 ? -7.542  3.424   20.716  0.80 28.49  ? 155 GLU A N     1 
ATOM   2357  C  CA    A GLU A 1 155 ? -7.823  4.499   19.950  0.20 29.12  ? 155 GLU A CA    1 
ATOM   2358  C  CA    B GLU A 1 155 ? -7.808  4.700   20.059  0.80 28.42  ? 155 GLU A CA    1 
ATOM   2359  C  C     A GLU A 1 155 ? -9.181  4.601   19.267  0.20 30.46  ? 155 GLU A C     1 
ATOM   2360  C  C     B GLU A 1 155 ? -9.220  4.730   19.483  0.80 30.36  ? 155 GLU A C     1 
ATOM   2361  O  O     A GLU A 1 155 ? -9.740  5.699   19.166  0.20 32.52  ? 155 GLU A O     1 
ATOM   2362  O  O     B GLU A 1 155 ? -9.978  5.682   19.713  0.80 31.33  ? 155 GLU A O     1 
ATOM   2363  C  CB    A GLU A 1 155 ? -6.694  4.707   18.936  0.20 30.65  ? 155 GLU A CB    1 
ATOM   2364  C  CB    B GLU A 1 155 ? -6.751  4.962   18.976  0.80 30.15  ? 155 GLU A CB    1 
ATOM   2365  C  CG    A GLU A 1 155 ? -5.328  4.986   19.561  0.20 37.08  ? 155 GLU A CG    1 
ATOM   2366  C  CG    B GLU A 1 155 ? -5.327  5.139   19.535  0.80 37.88  ? 155 GLU A CG    1 
ATOM   2367  C  CD    A GLU A 1 155 ? -4.209  5.075   18.531  0.20 41.08  ? 155 GLU A CD    1 
ATOM   2368  C  CD    B GLU A 1 155 ? -4.215  5.046   18.477  0.80 41.76  ? 155 GLU A CD    1 
ATOM   2369  O  OE1   A GLU A 1 155 ? -4.245  4.315   17.538  0.20 35.14  ? 155 GLU A OE1   1 
ATOM   2370  O  OE1   B GLU A 1 155 ? -4.499  5.174   17.266  0.80 42.08  ? 155 GLU A OE1   1 
ATOM   2371  O  OE2   A GLU A 1 155 ? -3.292  5.907   18.712  0.20 36.84  ? 155 GLU A OE2   1 
ATOM   2372  O  OE2   B GLU A 1 155 ? -3.042  4.845   18.866  0.80 38.46  ? 155 GLU A OE2   1 
ATOM   2373  N  N     A ARG A 1 156 ? -9.733  3.475   18.807  0.20 28.37  ? 156 ARG A N     1 
ATOM   2374  N  N     B ARG A 1 156 ? -9.618  3.665   18.781  0.80 27.64  ? 156 ARG A N     1 
ATOM   2375  C  CA    A ARG A 1 156 ? -11.025 3.499   18.130  0.20 32.63  ? 156 ARG A CA    1 
ATOM   2376  C  CA    B ARG A 1 156 ? -10.921 3.675   18.124  0.80 32.69  ? 156 ARG A CA    1 
ATOM   2377  C  C     A ARG A 1 156 ? -12.192 3.435   19.106  0.20 32.10  ? 156 ARG A C     1 
ATOM   2378  C  C     B ARG A 1 156 ? -12.057 3.627   19.138  0.80 31.75  ? 156 ARG A C     1 
ATOM   2379  O  O     A ARG A 1 156 ? -13.250 4.014   18.835  0.20 33.81  ? 156 ARG A O     1 
ATOM   2380  O  O     B ARG A 1 156 ? -13.079 4.294   18.955  0.80 33.31  ? 156 ARG A O     1 
ATOM   2381  C  CB    A ARG A 1 156 ? -11.122 2.344   17.133  0.20 31.01  ? 156 ARG A CB    1 
ATOM   2382  C  CB    B ARG A 1 156 ? -11.038 2.511   17.141  0.80 30.44  ? 156 ARG A CB    1 
ATOM   2383  C  CG    A ARG A 1 156 ? -10.183 2.462   15.943  0.20 33.82  ? 156 ARG A CG    1 
ATOM   2384  C  CG    B ARG A 1 156 ? -9.945  2.458   16.077  0.80 34.01  ? 156 ARG A CG    1 
ATOM   2385  C  CD    A ARG A 1 156 ? -10.602 3.594   15.021  0.20 39.33  ? 156 ARG A CD    1 
ATOM   2386  C  CD    B ARG A 1 156 ? -10.087 3.584   15.069  0.80 40.62  ? 156 ARG A CD    1 
ATOM   2387  N  NE    A ARG A 1 156 ? -11.906 3.345   14.419  0.20 40.69  ? 156 ARG A NE    1 
ATOM   2388  N  NE    B ARG A 1 156 ? -11.265 3.382   14.238  0.80 42.84  ? 156 ARG A NE    1 
ATOM   2389  C  CZ    A ARG A 1 156 ? -12.094 2.652   13.304  0.20 41.26  ? 156 ARG A CZ    1 
ATOM   2390  C  CZ    B ARG A 1 156 ? -11.258 2.737   13.080  0.80 44.04  ? 156 ARG A CZ    1 
ATOM   2391  N  NH1   A ARG A 1 156 ? -11.080 2.122   12.639  0.20 43.45  ? 156 ARG A NH1   1 
ATOM   2392  N  NH1   B ARG A 1 156 ? -10.134 2.270   12.554  0.80 40.03  ? 156 ARG A NH1   1 
ATOM   2393  N  NH2   A ARG A 1 156 ? -13.331 2.484   12.845  0.20 43.25  ? 156 ARG A NH2   1 
ATOM   2394  N  NH2   B ARG A 1 156 ? -12.406 2.554   12.435  0.80 45.20  ? 156 ARG A NH2   1 
ATOM   2395  N  N     A LEU A 1 157 ? -12.031 2.738   20.233  0.20 30.91  ? 157 LEU A N     1 
ATOM   2396  N  N     B LEU A 1 157 ? -11.899 2.845   20.212  0.80 30.81  ? 157 LEU A N     1 
ATOM   2397  C  CA    A LEU A 1 157 ? -13.112 2.660   21.208  0.20 33.24  ? 157 LEU A CA    1 
ATOM   2398  C  CA    B LEU A 1 157 ? -12.946 2.767   21.224  0.80 33.39  ? 157 LEU A CA    1 
ATOM   2399  C  C     A LEU A 1 157 ? -13.336 3.983   21.929  0.20 32.50  ? 157 LEU A C     1 
ATOM   2400  C  C     B LEU A 1 157 ? -13.195 4.121   21.881  0.80 31.86  ? 157 LEU A C     1 
ATOM   2401  O  O     A LEU A 1 157 ? -14.432 4.210   22.453  0.20 34.56  ? 157 LEU A O     1 
ATOM   2402  O  O     B LEU A 1 157 ? -14.328 4.416   22.277  0.80 34.25  ? 157 LEU A O     1 
ATOM   2403  C  CB    A LEU A 1 157 ? -12.836 1.547   22.223  0.20 33.94  ? 157 LEU A CB    1 
ATOM   2404  C  CB    B LEU A 1 157 ? -12.597 1.710   22.283  0.80 34.63  ? 157 LEU A CB    1 
ATOM   2405  C  CG    A LEU A 1 157 ? -12.864 0.114   21.684  0.20 33.30  ? 157 LEU A CG    1 
ATOM   2406  C  CG    B LEU A 1 157 ? -12.764 0.229   21.906  0.80 33.57  ? 157 LEU A CG    1 
ATOM   2407  C  CD1   A LEU A 1 157 ? -12.645 -0.892  22.799  0.20 28.33  ? 157 LEU A CD1   1 
ATOM   2408  C  CD1   B LEU A 1 157 ? -12.346 -0.674  23.037  0.80 29.67  ? 157 LEU A CD1   1 
ATOM   2409  C  CD2   A LEU A 1 157 ? -14.171 -0.168  20.961  0.20 34.51  ? 157 LEU A CD2   1 
ATOM   2410  C  CD2   B LEU A 1 157 ? -14.192 -0.100  21.495  0.80 35.16  ? 157 LEU A CD2   1 
ATOM   2411  N  N     A SER A 1 158 ? -12.331 4.860   21.968  0.20 30.21  ? 158 SER A N     1 
ATOM   2412  N  N     B SER A 1 158 ? -12.164 4.963   21.996  0.80 29.28  ? 158 SER A N     1 
ATOM   2413  C  CA    A SER A 1 158 ? -12.507 6.167   22.589  0.20 32.32  ? 158 SER A CA    1 
ATOM   2414  C  CA    B SER A 1 158 ? -12.365 6.272   22.612  0.80 31.62  ? 158 SER A CA    1 
ATOM   2415  C  C     A SER A 1 158 ? -13.293 7.130   21.712  0.20 39.21  ? 158 SER A C     1 
ATOM   2416  C  C     B SER A 1 158 ? -13.174 7.196   21.715  0.80 39.74  ? 158 SER A C     1 
ATOM   2417  O  O     A SER A 1 158 ? -13.816 8.125   22.224  0.20 38.17  ? 158 SER A O     1 
ATOM   2418  O  O     B SER A 1 158 ? -13.899 8.061   22.219  0.80 38.22  ? 158 SER A O     1 
ATOM   2419  C  CB    A SER A 1 158 ? -11.149 6.781   22.933  0.20 32.26  ? 158 SER A CB    1 
ATOM   2420  C  CB    B SER A 1 158 ? -11.028 6.921   22.965  0.80 31.91  ? 158 SER A CB    1 
ATOM   2421  O  OG    A SER A 1 158 ? -10.506 6.046   23.958  0.20 35.32  ? 158 SER A OG    1 
ATOM   2422  O  OG    B SER A 1 158 ? -10.467 6.340   24.131  0.80 36.22  ? 158 SER A OG    1 
ATOM   2423  N  N     A VAL A 1 159 ? -13.385 6.859   20.414  0.20 37.39  ? 159 VAL A N     1 
ATOM   2424  N  N     B VAL A 1 159 ? -13.070 7.024   20.397  0.80 39.53  ? 159 VAL A N     1 
ATOM   2425  C  CA    A VAL A 1 159 ? -14.171 7.687   19.504  0.20 35.10  ? 159 VAL A CA    1 
ATOM   2426  C  CA    B VAL A 1 159 ? -13.877 7.798   19.459  0.80 34.86  ? 159 VAL A CA    1 
ATOM   2427  C  C     A VAL A 1 159 ? -15.606 7.189   19.410  0.20 38.41  ? 159 VAL A C     1 
ATOM   2428  C  C     B VAL A 1 159 ? -15.301 7.265   19.418  0.80 38.24  ? 159 VAL A C     1 
ATOM   2429  O  O     A VAL A 1 159 ? -16.555 7.976   19.470  0.20 39.27  ? 159 VAL A O     1 
ATOM   2430  O  O     B VAL A 1 159 ? -16.266 8.030   19.519  0.80 39.63  ? 159 VAL A O     1 
ATOM   2431  C  CB    A VAL A 1 159 ? -13.498 7.730   18.114  0.20 39.43  ? 159 VAL A CB    1 
ATOM   2432  C  CB    B VAL A 1 159 ? -13.230 7.781   18.055  0.80 39.94  ? 159 VAL A CB    1 
ATOM   2433  C  CG1   A VAL A 1 159 ? -14.285 8.626   17.165  0.20 39.18  ? 159 VAL A CG1   1 
ATOM   2434  C  CG1   B VAL A 1 159 ? -14.044 8.611   17.071  0.80 38.11  ? 159 VAL A CG1   1 
ATOM   2435  C  CG2   A VAL A 1 159 ? -12.058 8.205   18.232  0.20 40.38  ? 159 VAL A CG2   1 
ATOM   2436  C  CG2   B VAL A 1 159 ? -11.787 8.275   18.111  0.80 41.36  ? 159 VAL A CG2   1 
ATOM   2437  N  N     A ASP A 1 160 ? -15.788 5.874   19.270  0.20 34.98  ? 160 ASP A N     1 
ATOM   2438  N  N     B ASP A 1 160 ? -15.459 5.942   19.290  0.80 33.68  ? 160 ASP A N     1 
ATOM   2439  C  CA    A ASP A 1 160 ? -17.127 5.303   19.208  0.20 37.05  ? 160 ASP A CA    1 
ATOM   2440  C  CA    B ASP A 1 160 ? -16.786 5.356   19.134  0.80 35.92  ? 160 ASP A CA    1 
ATOM   2441  C  C     A ASP A 1 160 ? -17.801 5.227   20.573  0.20 37.94  ? 160 ASP A C     1 
ATOM   2442  C  C     B ASP A 1 160 ? -17.548 5.210   20.448  0.80 38.92  ? 160 ASP A C     1 
ATOM   2443  O  O     A ASP A 1 160 ? -19.019 5.029   20.633  0.20 39.05  ? 160 ASP A O     1 
ATOM   2444  O  O     B ASP A 1 160 ? -18.774 5.084   20.412  0.80 38.55  ? 160 ASP A O     1 
ATOM   2445  C  CB    A ASP A 1 160 ? -17.083 3.904   18.586  0.20 37.51  ? 160 ASP A CB    1 
ATOM   2446  C  CB    B ASP A 1 160 ? -16.688 3.991   18.439  0.80 39.24  ? 160 ASP A CB    1 
ATOM   2447  C  CG    A ASP A 1 160 ? -16.522 3.906   17.176  0.20 40.93  ? 160 ASP A CG    1 
ATOM   2448  C  CG    B ASP A 1 160 ? -16.340 4.114   16.961  0.80 42.52  ? 160 ASP A CG    1 
ATOM   2449  O  OD1   A ASP A 1 160 ? -15.861 4.896   16.793  0.20 37.79  ? 160 ASP A OD1   1 
ATOM   2450  O  OD1   B ASP A 1 160 ? -16.919 4.995   16.292  0.80 48.34  ? 160 ASP A OD1   1 
ATOM   2451  O  OD2   A ASP A 1 160 ? -16.749 2.915   16.449  0.20 34.17  ? 160 ASP A OD2   1 
ATOM   2452  O  OD2   B ASP A 1 160 ? -15.483 3.348   16.470  0.80 42.43  ? 160 ASP A OD2   1 
ATOM   2453  N  N     A TYR A 1 161 ? -17.037 5.372   21.670  0.20 36.59  ? 161 TYR A N     1 
ATOM   2454  N  N     B TYR A 1 161 ? -16.860 5.222   21.594  0.80 36.85  ? 161 TYR A N     1 
ATOM   2455  C  CA    A TYR A 1 161 ? -17.567 5.296   23.037  0.20 33.80  ? 161 TYR A CA    1 
ATOM   2456  C  CA    B TYR A 1 161 ? -17.479 5.053   22.913  0.80 32.14  ? 161 TYR A CA    1 
ATOM   2457  C  C     A TYR A 1 161 ? -16.826 6.342   23.876  0.20 38.37  ? 161 TYR A C     1 
ATOM   2458  C  C     B TYR A 1 161 ? -16.849 6.038   23.899  0.80 38.25  ? 161 TYR A C     1 
ATOM   2459  O  O     A TYR A 1 161 ? -15.835 6.048   24.549  0.20 37.83  ? 161 TYR A O     1 
ATOM   2460  O  O     B TYR A 1 161 ? -16.302 5.662   24.935  0.80 39.66  ? 161 TYR A O     1 
ATOM   2461  C  CB    A TYR A 1 161 ? -17.416 3.893   23.624  0.20 33.98  ? 161 TYR A CB    1 
ATOM   2462  C  CB    B TYR A 1 161 ? -17.318 3.627   23.440  0.80 32.26  ? 161 TYR A CB    1 
ATOM   2463  C  CG    A TYR A 1 161 ? -17.909 2.788   22.718  0.20 33.79  ? 161 TYR A CG    1 
ATOM   2464  C  CG    B TYR A 1 161 ? -17.861 2.561   22.536  0.80 33.49  ? 161 TYR A CG    1 
ATOM   2465  C  CD1   A TYR A 1 161 ? -19.244 2.402   22.723  0.20 36.16  ? 161 TYR A CD1   1 
ATOM   2466  C  CD1   B TYR A 1 161 ? -19.185 2.149   22.634  0.80 36.38  ? 161 TYR A CD1   1 
ATOM   2467  C  CD2   A TYR A 1 161 ? -17.040 2.135   21.852  0.20 37.80  ? 161 TYR A CD2   1 
ATOM   2468  C  CD2   B TYR A 1 161 ? -17.057 1.971   21.564  0.80 39.12  ? 161 TYR A CD2   1 
ATOM   2469  C  CE1   A TYR A 1 161 ? -19.698 1.396   21.894  0.20 35.32  ? 161 TYR A CE1   1 
ATOM   2470  C  CE1   B TYR A 1 161 ? -19.688 1.181   21.803  0.80 35.82  ? 161 TYR A CE1   1 
ATOM   2471  C  CE2   A TYR A 1 161 ? -17.487 1.127   21.019  0.20 33.81  ? 161 TYR A CE2   1 
ATOM   2472  C  CE2   B TYR A 1 161 ? -17.556 0.998   20.728  0.80 33.52  ? 161 TYR A CE2   1 
ATOM   2473  C  CZ    A TYR A 1 161 ? -18.815 0.762   21.045  0.20 32.38  ? 161 TYR A CZ    1 
ATOM   2474  C  CZ    B TYR A 1 161 ? -18.869 0.608   20.850  0.80 31.17  ? 161 TYR A CZ    1 
ATOM   2475  O  OH    A TYR A 1 161 ? -19.262 -0.240  20.217  0.20 32.93  ? 161 TYR A OH    1 
ATOM   2476  O  OH    B TYR A 1 161 ? -19.372 -0.358  20.020  0.80 33.00  ? 161 TYR A OH    1 
ATOM   2477  N  N     A GLY A 1 162 ? -17.325 7.581   23.840  0.20 39.99  ? 162 GLY A N     1 
ATOM   2478  N  N     B GLY A 1 162 ? -16.936 7.330   23.575  0.80 37.08  ? 162 GLY A N     1 
ATOM   2479  C  CA    A GLY A 1 162 ? -16.665 8.669   24.541  0.20 41.78  ? 162 GLY A CA    1 
ATOM   2480  C  CA    B GLY A 1 162 ? -16.234 8.337   24.361  0.80 44.50  ? 162 GLY A CA    1 
ATOM   2481  C  C     A GLY A 1 162 ? -16.966 8.753   26.022  0.20 43.35  ? 162 GLY A C     1 
ATOM   2482  C  C     B GLY A 1 162 ? -16.578 8.327   25.841  0.80 43.75  ? 162 GLY A C     1 
ATOM   2483  O  O     A GLY A 1 162 ? -16.180 9.346   26.767  0.20 42.38  ? 162 GLY A O     1 
ATOM   2484  O  O     B GLY A 1 162 ? -15.716 8.568   26.689  0.80 50.46  ? 162 GLY A O     1 
ATOM   2485  N  N     A LYS A 1 163 ? -18.083 8.180   26.468  0.20 42.75  ? 163 LYS A N     1 
ATOM   2486  N  N     B LYS A 1 163 ? -17.833 8.052   26.178  0.80 43.12  ? 163 LYS A N     1 
ATOM   2487  C  CA    A LYS A 1 163 ? -18.488 8.249   27.866  0.20 44.22  ? 163 LYS A CA    1 
ATOM   2488  C  CA    B LYS A 1 163 ? -18.267 8.222   27.559  0.80 45.01  ? 163 LYS A CA    1 
ATOM   2489  C  C     A LYS A 1 163 ? -18.442 6.883   28.546  0.20 43.17  ? 163 LYS A C     1 
ATOM   2490  C  C     B LYS A 1 163 ? -18.017 7.000   28.439  0.80 45.34  ? 163 LYS A C     1 
ATOM   2491  O  O     A LYS A 1 163 ? -19.179 6.636   29.504  0.20 43.04  ? 163 LYS A O     1 
ATOM   2492  O  O     B LYS A 1 163 ? -18.266 7.073   29.648  0.80 45.00  ? 163 LYS A O     1 
ATOM   2493  C  CB    A LYS A 1 163 ? -19.885 8.857   27.986  0.20 47.31  ? 163 LYS A CB    1 
ATOM   2494  C  CB    B LYS A 1 163 ? -19.756 8.589   27.598  0.80 49.60  ? 163 LYS A CB    1 
ATOM   2495  N  N     A LYS A 1 164 ? -17.579 5.991   28.065  0.20 39.22  ? 164 LYS A N     1 
ATOM   2496  N  N     B LYS A 1 164 ? -17.517 5.896   27.885  0.80 38.65  ? 164 LYS A N     1 
ATOM   2497  C  CA    A LYS A 1 164 ? -17.426 4.657   28.626  0.20 37.66  ? 164 LYS A CA    1 
ATOM   2498  C  CA    B LYS A 1 164 ? -17.441 4.635   28.612  0.80 37.84  ? 164 LYS A CA    1 
ATOM   2499  C  C     A LYS A 1 164 ? -16.006 4.483   29.144  0.20 32.75  ? 164 LYS A C     1 
ATOM   2500  C  C     B LYS A 1 164 ? -16.049 4.407   29.192  0.80 32.58  ? 164 LYS A C     1 
ATOM   2501  O  O     A LYS A 1 164 ? -15.054 5.013   28.563  0.20 36.79  ? 164 LYS A O     1 
ATOM   2502  O  O     B LYS A 1 164 ? -15.041 4.870   28.650  0.80 36.91  ? 164 LYS A O     1 
ATOM   2503  C  CB    A LYS A 1 164 ? -17.745 3.580   27.584  0.20 36.76  ? 164 LYS A CB    1 
ATOM   2504  C  CB    B LYS A 1 164 ? -17.815 3.461   27.708  0.80 36.96  ? 164 LYS A CB    1 
ATOM   2505  C  CG    A LYS A 1 164 ? -19.112 3.735   26.939  0.20 33.35  ? 164 LYS A CG    1 
ATOM   2506  C  CG    B LYS A 1 164 ? -18.973 3.735   26.769  0.80 32.53  ? 164 LYS A CG    1 
ATOM   2507  C  CD    A LYS A 1 164 ? -20.214 3.754   27.985  0.20 35.57  ? 164 LYS A CD    1 
ATOM   2508  C  CD    B LYS A 1 164 ? -20.310 3.736   27.472  0.80 36.88  ? 164 LYS A CD    1 
ATOM   2509  C  CE    A LYS A 1 164 ? -21.565 4.056   27.360  0.20 41.34  ? 164 LYS A CE    1 
ATOM   2510  C  CE    B LYS A 1 164 ? -21.413 3.932   26.443  0.80 45.83  ? 164 LYS A CE    1 
ATOM   2511  N  NZ    A LYS A 1 164 ? -22.653 4.038   28.378  0.20 35.20  ? 164 LYS A NZ    1 
ATOM   2512  N  NZ    B LYS A 1 164 ? -22.763 3.979   27.060  0.80 43.25  ? 164 LYS A NZ    1 
ATOM   2513  N  N     A SER A 1 165 ? -15.867 3.744   30.239  0.20 32.44  ? 165 SER A N     1 
ATOM   2514  N  N     B SER A 1 165 ? -16.008 3.670   30.302  0.80 32.38  ? 165 SER A N     1 
ATOM   2515  C  CA    A SER A 1 165 ? -14.566 3.539   30.854  0.20 31.41  ? 165 SER A CA    1 
ATOM   2516  C  CA    B SER A 1 165 ? -14.761 3.393   30.998  0.80 31.11  ? 165 SER A CA    1 
ATOM   2517  C  C     A SER A 1 165 ? -13.846 2.356   30.217  0.20 28.20  ? 165 SER A C     1 
ATOM   2518  C  C     B SER A 1 165 ? -13.998 2.274   30.304  0.80 27.33  ? 165 SER A C     1 
ATOM   2519  O  O     A SER A 1 165 ? -14.447 1.509   29.554  0.20 30.57  ? 165 SER A O     1 
ATOM   2520  O  O     B SER A 1 165 ? -14.593 1.327   29.786  0.80 31.48  ? 165 SER A O     1 
ATOM   2521  C  CB    A SER A 1 165 ? -14.707 3.315   32.360  0.20 32.58  ? 165 SER A CB    1 
ATOM   2522  C  CB    B SER A 1 165 ? -15.031 2.996   32.450  0.80 34.57  ? 165 SER A CB    1 
ATOM   2523  O  OG    A SER A 1 165 ? -15.174 4.486   33.003  0.20 31.91  ? 165 SER A OG    1 
ATOM   2524  O  OG    B SER A 1 165 ? -15.757 3.998   33.142  0.80 32.91  ? 165 SER A OG    1 
ATOM   2525  N  N     A LYS A 1 166 ? -12.532 2.314   30.422  0.20 29.43  ? 166 LYS A N     1 
ATOM   2526  N  N     B LYS A 1 166 ? -12.675 2.373   30.314  0.80 29.36  ? 166 LYS A N     1 
ATOM   2527  C  CA    A LYS A 1 166 ? -11.705 1.235   29.902  0.20 27.30  ? 166 LYS A CA    1 
ATOM   2528  C  CA    B LYS A 1 166 ? -11.826 1.333   29.751  0.80 26.75  ? 166 LYS A CA    1 
ATOM   2529  C  C     A LYS A 1 166 ? -10.726 0.806   30.983  0.20 28.56  ? 166 LYS A C     1 
ATOM   2530  C  C     B LYS A 1 166 ? -10.771 0.963   30.779  0.80 28.57  ? 166 LYS A C     1 
ATOM   2531  O  O     A LYS A 1 166 ? -10.029 1.646   31.561  0.20 31.07  ? 166 LYS A O     1 
ATOM   2532  O  O     B LYS A 1 166 ? -10.038 1.833   31.258  0.80 33.72  ? 166 LYS A O     1 
ATOM   2533  C  CB    A LYS A 1 166 ? -10.955 1.666   28.633  0.20 32.46  ? 166 LYS A CB    1 
ATOM   2534  C  CB    B LYS A 1 166 ? -11.187 1.792   28.435  0.80 33.96  ? 166 LYS A CB    1 
ATOM   2535  C  CG    A LYS A 1 166 ? -11.860 2.238   27.544  0.20 34.44  ? 166 LYS A CG    1 
ATOM   2536  C  CG    B LYS A 1 166 ? -12.234 2.161   27.380  0.80 34.17  ? 166 LYS A CG    1 
ATOM   2537  C  CD    A LYS A 1 166 ? -11.125 2.387   26.224  0.20 34.39  ? 166 LYS A CD    1 
ATOM   2538  C  CD    B LYS A 1 166 ? -11.695 2.055   25.962  0.80 37.12  ? 166 LYS A CD    1 
ATOM   2539  C  CE    A LYS A 1 166 ? -11.879 3.292   25.262  0.20 34.02  ? 166 LYS A CE    1 
ATOM   2540  C  CE    B LYS A 1 166 ? -10.661 3.127   25.654  0.80 40.71  ? 166 LYS A CE    1 
ATOM   2541  N  NZ    A LYS A 1 166 ? -11.972 4.684   25.787  0.20 35.48  ? 166 LYS A NZ    1 
ATOM   2542  N  NZ    B LYS A 1 166 ? -11.111 4.499   26.036  0.80 34.01  ? 166 LYS A NZ    1 
ATOM   2543  N  N     A LEU A 1 167 ? -10.690 -0.494  31.264  0.20 26.62  ? 167 LEU A N     1 
ATOM   2544  N  N     B LEU A 1 167 ? -10.719 -0.318  31.132  0.80 25.72  ? 167 LEU A N     1 
ATOM   2545  C  CA    A LEU A 1 167 ? -9.796  -1.064  32.264  0.20 24.97  ? 167 LEU A CA    1 
ATOM   2546  C  CA    B LEU A 1 167 ? -9.770  -0.865  32.090  0.80 23.37  ? 167 LEU A CA    1 
ATOM   2547  C  C     A LEU A 1 167 ? -9.031  -2.211  31.624  0.20 26.54  ? 167 LEU A C     1 
ATOM   2548  C  C     B LEU A 1 167 ? -8.881  -1.886  31.395  0.80 27.24  ? 167 LEU A C     1 
ATOM   2549  O  O     A LEU A 1 167 ? -9.641  -3.146  31.094  0.20 22.12  ? 167 LEU A O     1 
ATOM   2550  O  O     B LEU A 1 167 ? -9.321  -2.582  30.475  0.80 30.28  ? 167 LEU A O     1 
ATOM   2551  C  CB    A LEU A 1 167 ? -10.565 -1.553  33.496  0.20 29.87  ? 167 LEU A CB    1 
ATOM   2552  C  CB    B LEU A 1 167 ? -10.485 -1.542  33.269  0.80 30.62  ? 167 LEU A CB    1 
ATOM   2553  C  CG    A LEU A 1 167 ? -11.161 -0.476  34.410  0.20 30.59  ? 167 LEU A CG    1 
ATOM   2554  C  CG    B LEU A 1 167 ? -10.667 -0.663  34.507  0.80 35.23  ? 167 LEU A CG    1 
ATOM   2555  C  CD1   A LEU A 1 167 ? -12.499 0.029   33.888  0.20 28.99  ? 167 LEU A CD1   1 
ATOM   2556  C  CD1   B LEU A 1 167 ? -11.293 0.670   34.129  0.80 31.19  ? 167 LEU A CD1   1 
ATOM   2557  C  CD2   A LEU A 1 167 ? -11.288 -0.990  35.834  0.20 27.27  ? 167 LEU A CD2   1 
ATOM   2558  C  CD2   B LEU A 1 167 ? -11.492 -1.370  35.550  0.80 27.06  ? 167 LEU A CD2   1 
ATOM   2559  N  N     A GLU A 1 168 ? -7.705  -2.144  31.677  0.20 27.28  ? 168 GLU A N     1 
ATOM   2560  N  N     B GLU A 1 168 ? -7.630  -1.990  31.852  0.80 27.03  ? 168 GLU A N     1 
ATOM   2561  C  CA    A GLU A 1 168 ? -6.857  -3.139  31.042  0.20 27.84  ? 168 GLU A CA    1 
ATOM   2562  C  CA    B GLU A 1 168 ? -6.675  -2.920  31.262  0.80 28.26  ? 168 GLU A CA    1 
ATOM   2563  C  C     A GLU A 1 168 ? -6.282  -4.099  32.073  0.20 26.17  ? 168 GLU A C     1 
ATOM   2564  C  C     B GLU A 1 168 ? -6.177  -3.940  32.269  0.80 26.21  ? 168 GLU A C     1 
ATOM   2565  O  O     A GLU A 1 168 ? -6.132  -3.764  33.251  0.20 26.01  ? 168 GLU A O     1 
ATOM   2566  O  O     B GLU A 1 168 ? -5.960  -3.620  33.444  0.80 25.47  ? 168 GLU A O     1 
ATOM   2567  C  CB    A GLU A 1 168 ? -5.715  -2.475  30.272  0.20 25.81  ? 168 GLU A CB    1 
ATOM   2568  C  CB    B GLU A 1 168 ? -5.454  -2.209  30.698  0.80 30.16  ? 168 GLU A CB    1 
ATOM   2569  C  CG    A GLU A 1 168 ? -6.113  -1.219  29.533  0.20 28.61  ? 168 GLU A CG    1 
ATOM   2570  C  CG    B GLU A 1 168 ? -5.642  -1.519  29.403  0.80 29.56  ? 168 GLU A CG    1 
ATOM   2571  C  CD    A GLU A 1 168 ? -4.951  -0.609  28.782  0.20 29.48  ? 168 GLU A CD    1 
ATOM   2572  C  CD    B GLU A 1 168 ? -4.388  -0.783  29.031  0.80 31.62  ? 168 GLU A CD    1 
ATOM   2573  O  OE1   A GLU A 1 168 ? -4.181  -1.371  28.162  0.20 26.87  ? 168 GLU A OE1   1 
ATOM   2574  O  OE1   B GLU A 1 168 ? -4.173  0.332   29.560  0.80 27.38  ? 168 GLU A OE1   1 
ATOM   2575  O  OE2   A GLU A 1 168 ? -4.801  0.628   28.823  0.20 29.60  ? 168 GLU A OE2   1 
ATOM   2576  O  OE2   B GLU A 1 168 ? -3.587  -1.348  28.262  0.80 28.34  ? 168 GLU A OE2   1 
ATOM   2577  N  N     A PHE A 1 169 ? -5.958  -5.305  31.607  0.20 24.01  ? 169 PHE A N     1 
ATOM   2578  N  N     B PHE A 1 169 ? -5.979  -5.169  31.785  0.80 24.42  ? 169 PHE A N     1 
ATOM   2579  C  CA    A PHE A 1 169 ? -5.311  -6.343  32.411  0.20 24.81  ? 169 PHE A CA    1 
ATOM   2580  C  CA    B PHE A 1 169 ? -5.153  -6.170  32.451  0.80 25.39  ? 169 PHE A CA    1 
ATOM   2581  C  C     A PHE A 1 169 ? -4.091  -6.786  31.610  0.20 25.12  ? 169 PHE A C     1 
ATOM   2582  C  C     B PHE A 1 169 ? -3.989  -6.411  31.503  0.80 25.74  ? 169 PHE A C     1 
ATOM   2583  O  O     A PHE A 1 169 ? -4.156  -7.757  30.850  0.20 24.90  ? 169 PHE A O     1 
ATOM   2584  O  O     B PHE A 1 169 ? -4.190  -6.894  30.381  0.80 24.35  ? 169 PHE A O     1 
ATOM   2585  C  CB    A PHE A 1 169 ? -6.262  -7.498  32.704  0.20 23.06  ? 169 PHE A CB    1 
ATOM   2586  C  CB    B PHE A 1 169 ? -5.922  -7.460  32.744  0.80 21.42  ? 169 PHE A CB    1 
ATOM   2587  C  CG    A PHE A 1 169 ? -7.368  -7.147  33.662  0.20 23.18  ? 169 PHE A CG    1 
ATOM   2588  C  CG    B PHE A 1 169 ? -6.953  -7.319  33.836  0.80 23.11  ? 169 PHE A CG    1 
ATOM   2589  C  CD1   A PHE A 1 169 ? -8.498  -6.474  33.225  0.20 25.65  ? 169 PHE A CD1   1 
ATOM   2590  C  CD1   B PHE A 1 169 ? -6.569  -7.255  35.163  0.80 19.32  ? 169 PHE A CD1   1 
ATOM   2591  C  CD2   A PHE A 1 169 ? -7.275  -7.489  34.999  0.20 23.74  ? 169 PHE A CD2   1 
ATOM   2592  C  CD2   B PHE A 1 169 ? -8.289  -7.228  33.528  0.80 23.86  ? 169 PHE A CD2   1 
ATOM   2593  C  CE1   A PHE A 1 169 ? -9.517  -6.148  34.112  0.20 24.12  ? 169 PHE A CE1   1 
ATOM   2594  C  CE1   B PHE A 1 169 ? -7.523  -7.109  36.175  0.80 26.83  ? 169 PHE A CE1   1 
ATOM   2595  C  CE2   A PHE A 1 169 ? -8.284  -7.167  35.886  0.20 24.75  ? 169 PHE A CE2   1 
ATOM   2596  C  CE2   B PHE A 1 169 ? -9.248  -7.082  34.534  0.80 26.07  ? 169 PHE A CE2   1 
ATOM   2597  C  CZ    A PHE A 1 169 ? -9.406  -6.496  35.441  0.20 25.86  ? 169 PHE A CZ    1 
ATOM   2598  C  CZ    B PHE A 1 169 ? -8.856  -7.021  35.853  0.80 26.04  ? 169 PHE A CZ    1 
ATOM   2599  N  N     A SER A 1 170 ? -2.985  -6.068  31.776  0.20 21.89  ? 170 SER A N     1 
ATOM   2600  N  N     B SER A 1 170 ? -2.783  -6.034  31.922  0.80 20.35  ? 170 SER A N     1 
ATOM   2601  C  CA    A SER A 1 170 ? -1.817  -6.246  30.928  0.20 19.99  ? 170 SER A CA    1 
ATOM   2602  C  CA    B SER A 1 170 ? -1.647  -5.982  31.005  0.80 18.44  ? 170 SER A CA    1 
ATOM   2603  C  C     A SER A 1 170 ? -0.853  -7.265  31.525  0.20 22.21  ? 170 SER A C     1 
ATOM   2604  C  C     B SER A 1 170 ? -0.528  -6.872  31.519  0.80 21.62  ? 170 SER A C     1 
ATOM   2605  O  O     A SER A 1 170 ? -0.939  -7.637  32.696  0.20 24.65  ? 170 SER A O     1 
ATOM   2606  O  O     B SER A 1 170 ? -0.174  -6.807  32.698  0.80 24.97  ? 170 SER A O     1 
ATOM   2607  C  CB    A SER A 1 170 ? -1.104  -4.913  30.719  0.20 24.78  ? 170 SER A CB    1 
ATOM   2608  C  CB    B SER A 1 170 ? -1.127  -4.556  30.857  0.80 25.92  ? 170 SER A CB    1 
ATOM   2609  O  OG    A SER A 1 170 ? -1.931  -3.994  30.035  0.20 25.04  ? 170 SER A OG    1 
ATOM   2610  O  OG    B SER A 1 170 ? -2.184  -3.622  30.789  0.80 32.14  ? 170 SER A OG    1 
ATOM   2611  N  N     A ILE A 1 171 ? 0.090   -7.708  30.699  0.20 22.31  ? 171 ILE A N     1 
ATOM   2612  N  N     B ILE A 1 171 ? 0.051   -7.675  30.640  0.80 22.21  ? 171 ILE A N     1 
ATOM   2613  C  CA    A ILE A 1 171 ? 1.116   -8.657  31.111  0.20 26.28  ? 171 ILE A CA    1 
ATOM   2614  C  CA    B ILE A 1 171 ? 1.092   -8.611  31.039  0.80 26.52  ? 171 ILE A CA    1 
ATOM   2615  C  C     A ILE A 1 171 ? 2.462   -7.956  31.004  0.20 24.67  ? 171 ILE A C     1 
ATOM   2616  C  C     B ILE A 1 171 ? 2.439   -7.958  30.735  0.80 24.99  ? 171 ILE A C     1 
ATOM   2617  O  O     A ILE A 1 171 ? 2.935   -7.662  29.898  0.20 23.79  ? 171 ILE A O     1 
ATOM   2618  O  O     B ILE A 1 171 ? 2.771   -7.698  29.573  0.80 22.98  ? 171 ILE A O     1 
ATOM   2619  C  CB    A ILE A 1 171 ? 1.091   -9.940  30.270  0.20 28.21  ? 171 ILE A CB    1 
ATOM   2620  C  CB    B ILE A 1 171 ? 0.929   -9.967  30.337  0.80 28.77  ? 171 ILE A CB    1 
ATOM   2621  C  CG1   A ILE A 1 171 ? -0.210  -10.703 30.516  0.20 26.68  ? 171 ILE A CG1   1 
ATOM   2622  C  CG1   B ILE A 1 171 ? -0.518  -10.482 30.498  0.80 27.24  ? 171 ILE A CG1   1 
ATOM   2623  C  CG2   A ILE A 1 171 ? 2.283   -10.817 30.613  0.20 27.66  ? 171 ILE A CG2   1 
ATOM   2624  C  CG2   B ILE A 1 171 ? 1.969   -10.967 30.860  0.80 29.96  ? 171 ILE A CG2   1 
ATOM   2625  C  CD1   A ILE A 1 171 ? -0.423  -11.074 31.973  0.20 26.87  ? 171 ILE A CD1   1 
ATOM   2626  C  CD1   B ILE A 1 171 ? -1.105  -10.374 31.943  0.80 24.14  ? 171 ILE A CD1   1 
ATOM   2627  N  N     A TYR A 1 172 ? 3.069   -7.677  32.146  0.20 26.17  ? 172 TYR A N     1 
ATOM   2628  N  N     B TYR A 1 172 ? 3.205   -7.687  31.777  0.80 26.28  ? 172 TYR A N     1 
ATOM   2629  C  CA    A TYR A 1 172 ? 4.412   -7.114  32.162  0.20 26.01  ? 172 TYR A CA    1 
ATOM   2630  C  CA    B TYR A 1 172 ? 4.495   -6.987  31.800  0.80 26.37  ? 172 TYR A CA    1 
ATOM   2631  C  C     A TYR A 1 172 ? 5.408   -8.208  31.790  0.20 27.28  ? 172 TYR A C     1 
ATOM   2632  C  C     B TYR A 1 172 ? 5.627   -8.002  31.635  0.80 27.96  ? 172 TYR A C     1 
ATOM   2633  O  O     A TYR A 1 172 ? 5.317   -9.324  32.318  0.20 25.92  ? 172 TYR A O     1 
ATOM   2634  O  O     B TYR A 1 172 ? 5.602   -9.052  32.294  0.80 27.78  ? 172 TYR A O     1 
ATOM   2635  C  CB    A TYR A 1 172 ? 4.712   -6.541  33.545  0.20 26.39  ? 172 TYR A CB    1 
ATOM   2636  C  CB    B TYR A 1 172 ? 4.610   -6.213  33.113  0.80 25.81  ? 172 TYR A CB    1 
ATOM   2637  C  CG    A TYR A 1 172 ? 5.975   -5.721  33.660  0.20 24.18  ? 172 TYR A CG    1 
ATOM   2638  C  CG    B TYR A 1 172 ? 5.919   -5.535  33.472  0.80 23.03  ? 172 TYR A CG    1 
ATOM   2639  C  CD1   A TYR A 1 172 ? 7.188   -6.321  33.965  0.20 24.05  ? 172 TYR A CD1   1 
ATOM   2640  C  CD1   B TYR A 1 172 ? 7.002   -6.271  33.923  0.80 23.36  ? 172 TYR A CD1   1 
ATOM   2641  C  CD2   A TYR A 1 172 ? 5.948   -4.343  33.498  0.20 26.66  ? 172 TYR A CD2   1 
ATOM   2642  C  CD2   B TYR A 1 172 ? 6.036   -4.152  33.449  0.80 26.72  ? 172 TYR A CD2   1 
ATOM   2643  C  CE1   A TYR A 1 172 ? 8.338   -5.577  34.088  0.20 26.92  ? 172 TYR A CE1   1 
ATOM   2644  C  CE1   B TYR A 1 172 ? 8.164   -5.666  34.292  0.80 26.10  ? 172 TYR A CE1   1 
ATOM   2645  C  CE2   A TYR A 1 172 ? 7.098   -3.588  33.619  0.20 28.69  ? 172 TYR A CE2   1 
ATOM   2646  C  CE2   B TYR A 1 172 ? 7.215   -3.529  33.819  0.80 28.83  ? 172 TYR A CE2   1 
ATOM   2647  C  CZ    A TYR A 1 172 ? 8.290   -4.212  33.914  0.20 27.74  ? 172 TYR A CZ    1 
ATOM   2648  C  CZ    B TYR A 1 172 ? 8.277   -4.298  34.240  0.80 27.10  ? 172 TYR A CZ    1 
ATOM   2649  O  OH    A TYR A 1 172 ? 9.442   -3.472  34.038  0.20 29.51  ? 172 TYR A OH    1 
ATOM   2650  O  OH    B TYR A 1 172 ? 9.466   -3.717  34.614  0.80 27.48  ? 172 TYR A OH    1 
ATOM   2651  N  N     A PRO A 1 173 ? 6.347   -7.945  30.882  0.20 26.94  ? 173 PRO A N     1 
ATOM   2652  N  N     B PRO A 1 173 ? 6.606   -7.756  30.754  0.80 26.78  ? 173 PRO A N     1 
ATOM   2653  C  CA    A PRO A 1 173 ? 7.226   -9.014  30.391  0.20 26.79  ? 173 PRO A CA    1 
ATOM   2654  C  CA    B PRO A 1 173 ? 7.526   -8.832  30.352  0.80 26.76  ? 173 PRO A CA    1 
ATOM   2655  C  C     A PRO A 1 173 ? 8.241   -9.449  31.438  0.20 27.53  ? 173 PRO A C     1 
ATOM   2656  C  C     B PRO A 1 173 ? 8.570   -9.192  31.400  0.80 27.40  ? 173 PRO A C     1 
ATOM   2657  O  O     A PRO A 1 173 ? 8.411   -8.836  32.494  0.20 26.56  ? 173 PRO A O     1 
ATOM   2658  O  O     B PRO A 1 173 ? 9.059   -8.354  32.162  0.80 24.69  ? 173 PRO A O     1 
ATOM   2659  C  CB    A PRO A 1 173 ? 7.912   -8.384  29.175  0.20 26.61  ? 173 PRO A CB    1 
ATOM   2660  C  CB    B PRO A 1 173 ? 8.202   -8.271  29.094  0.80 25.63  ? 173 PRO A CB    1 
ATOM   2661  C  CG    A PRO A 1 173 ? 7.865   -6.915  29.435  0.20 29.31  ? 173 PRO A CG    1 
ATOM   2662  C  CG    B PRO A 1 173 ? 8.164   -6.784  29.292  0.80 30.06  ? 173 PRO A CG    1 
ATOM   2663  C  CD    A PRO A 1 173 ? 6.586   -6.667  30.189  0.20 28.51  ? 173 PRO A CD    1 
ATOM   2664  C  CD    B PRO A 1 173 ? 6.850   -6.513  29.992  0.80 29.34  ? 173 PRO A CD    1 
ATOM   2665  N  N     A ALA A 1 174 ? 8.930   -10.548 31.119  0.20 26.94  ? 174 ALA A N     1 
ATOM   2666  N  N     B ALA A 1 174 ? 8.946   -10.463 31.385  0.80 26.09  ? 174 ALA A N     1 
ATOM   2667  C  CA    A ALA A 1 174 ? 9.916   -11.131 32.015  0.20 31.59  ? 174 ALA A CA    1 
ATOM   2668  C  CA    B ALA A 1 174 ? 9.938   -11.003 32.289  0.80 30.73  ? 174 ALA A CA    1 
ATOM   2669  C  C     A ALA A 1 174 ? 10.832  -12.033 31.208  0.20 35.05  ? 174 ALA A C     1 
ATOM   2670  C  C     B ALA A 1 174 ? 10.919  -11.864 31.506  0.80 33.71  ? 174 ALA A C     1 
ATOM   2671  O  O     A ALA A 1 174 ? 10.356  -12.694 30.274  0.20 36.85  ? 174 ALA A O     1 
ATOM   2672  O  O     B ALA A 1 174 ? 10.504  -12.640 30.639  0.80 35.46  ? 174 ALA A O     1 
ATOM   2673  C  CB    A ALA A 1 174 ? 9.246   -11.926 33.140  0.20 32.62  ? 174 ALA A CB    1 
ATOM   2674  C  CB    B ALA A 1 174 ? 9.275   -11.833 33.390  0.80 33.07  ? 174 ALA A CB    1 
ATOM   2675  N  N     A PRO A 1 175 ? 12.129  -12.090 31.523  0.20 38.43  ? 175 PRO A N     1 
ATOM   2676  N  N     B PRO A 1 175 ? 12.220  -11.744 31.782  0.80 36.38  ? 175 PRO A N     1 
ATOM   2677  C  CA    A PRO A 1 175 ? 13.037  -12.936 30.729  0.20 42.26  ? 175 PRO A CA    1 
ATOM   2678  C  CA    B PRO A 1 175 ? 13.211  -12.527 31.018  0.80 43.88  ? 175 PRO A CA    1 
ATOM   2679  C  C     A PRO A 1 175 ? 12.868  -14.426 30.979  0.20 41.55  ? 175 PRO A C     1 
ATOM   2680  C  C     B PRO A 1 175 ? 12.998  -14.031 31.074  0.80 39.39  ? 175 PRO A C     1 
ATOM   2681  O  O     A PRO A 1 175 ? 13.267  -15.224 30.121  0.20 44.28  ? 175 PRO A O     1 
ATOM   2682  O  O     B PRO A 1 175 ? 13.325  -14.729 30.104  0.80 46.36  ? 175 PRO A O     1 
ATOM   2683  C  CB    A PRO A 1 175 ? 14.428  -12.453 31.158  0.20 44.46  ? 175 PRO A CB    1 
ATOM   2684  C  CB    B PRO A 1 175 ? 14.542  -12.130 31.671  0.80 46.62  ? 175 PRO A CB    1 
ATOM   2685  C  CG    A PRO A 1 175 ? 14.224  -11.928 32.542  0.20 40.56  ? 175 PRO A CG    1 
ATOM   2686  C  CG    B PRO A 1 175 ? 14.301  -10.783 32.226  0.80 44.14  ? 175 PRO A CG    1 
ATOM   2687  C  CD    A PRO A 1 175 ? 12.848  -11.313 32.547  0.20 38.19  ? 175 PRO A CD    1 
ATOM   2688  C  CD    B PRO A 1 175 ? 12.856  -10.751 32.660  0.80 36.11  ? 175 PRO A CD    1 
ATOM   2689  N  N     A GLN A 1 176 ? 12.294  -14.828 32.116  0.20 45.02  ? 176 GLN A N     1 
ATOM   2690  N  N     B GLN A 1 176 ? 12.453  -14.546 32.178  0.80 45.13  ? 176 GLN A N     1 
ATOM   2691  C  CA    A GLN A 1 176 ? 12.129  -16.252 32.399  0.20 46.21  ? 176 GLN A CA    1 
ATOM   2692  C  CA    B GLN A 1 176 ? 12.315  -15.990 32.343  0.80 46.92  ? 176 GLN A CA    1 
ATOM   2693  C  C     A GLN A 1 176 ? 11.169  -16.910 31.414  0.20 49.76  ? 176 GLN A C     1 
ATOM   2694  C  C     B GLN A 1 176 ? 11.486  -16.611 31.220  0.80 52.02  ? 176 GLN A C     1 
ATOM   2695  O  O     A GLN A 1 176 ? 11.393  -18.049 30.988  0.20 50.89  ? 176 GLN A O     1 
ATOM   2696  O  O     B GLN A 1 176 ? 11.888  -17.619 30.627  0.80 56.99  ? 176 GLN A O     1 
ATOM   2697  C  CB    A GLN A 1 176 ? 11.640  -16.452 33.834  0.20 46.48  ? 176 GLN A CB    1 
ATOM   2698  C  CB    B GLN A 1 176 ? 11.697  -16.297 33.707  0.80 47.02  ? 176 GLN A CB    1 
ATOM   2699  C  CG    A GLN A 1 176 ? 12.714  -16.281 34.897  0.20 43.06  ? 176 GLN A CG    1 
ATOM   2700  C  CG    B GLN A 1 176 ? 12.553  -15.900 34.909  0.80 42.52  ? 176 GLN A CG    1 
ATOM   2701  C  CD    A GLN A 1 176 ? 13.119  -14.835 35.102  0.20 44.79  ? 176 GLN A CD    1 
ATOM   2702  C  CD    B GLN A 1 176 ? 12.509  -14.409 35.218  0.80 44.94  ? 176 GLN A CD    1 
ATOM   2703  O  OE1   A GLN A 1 176 ? 12.471  -13.917 34.599  0.20 44.33  ? 176 GLN A OE1   1 
ATOM   2704  O  OE1   B GLN A 1 176 ? 12.163  -13.591 34.363  0.80 46.89  ? 176 GLN A OE1   1 
ATOM   2705  N  NE2   A GLN A 1 176 ? 14.198  -14.626 35.848  0.20 41.67  ? 176 GLN A NE2   1 
ATOM   2706  N  NE2   B GLN A 1 176 ? 12.866  -14.050 36.448  0.80 47.58  ? 176 GLN A NE2   1 
ATOM   2707  N  N     A VAL A 1 177 ? 10.095  -16.214 31.048  0.20 44.75  ? 177 VAL A N     1 
ATOM   2708  N  N     B VAL A 1 177 ? 10.329  -16.022 30.904  0.80 45.13  ? 177 VAL A N     1 
ATOM   2709  C  CA    A VAL A 1 177 ? 9.134   -16.728 30.078  0.20 44.64  ? 177 VAL A CA    1 
ATOM   2710  C  CA    B VAL A 1 177 ? 9.396   -16.660 29.981  0.80 45.27  ? 177 VAL A CA    1 
ATOM   2711  C  C     A VAL A 1 177 ? 8.816   -15.633 29.069  0.20 43.89  ? 177 VAL A C     1 
ATOM   2712  C  C     B VAL A 1 177 ? 9.057   -15.767 28.784  0.80 45.52  ? 177 VAL A C     1 
ATOM   2713  O  O     A VAL A 1 177 ? 7.777   -14.969 29.159  0.20 38.43  ? 177 VAL A O     1 
ATOM   2714  O  O     B VAL A 1 177 ? 8.071   -16.012 28.099  0.80 54.01  ? 177 VAL A O     1 
ATOM   2715  C  CB    A VAL A 1 177 ? 7.860   -17.246 30.770  0.20 41.69  ? 177 VAL A CB    1 
ATOM   2716  C  CB    B VAL A 1 177 ? 8.116   -17.111 30.712  0.80 41.62  ? 177 VAL A CB    1 
ATOM   2717  C  CG1   A VAL A 1 177 ? 8.051   -18.685 31.215  0.20 43.82  ? 177 VAL A CG1   1 
ATOM   2718  C  CG1   B VAL A 1 177 ? 8.425   -18.238 31.683  0.80 45.67  ? 177 VAL A CG1   1 
ATOM   2719  C  CG2   A VAL A 1 177 ? 7.510   -16.367 31.966  0.20 38.32  ? 177 VAL A CG2   1 
ATOM   2720  C  CG2   B VAL A 1 177 ? 7.468   -15.933 31.454  0.80 37.31  ? 177 VAL A CG2   1 
ATOM   2721  N  N     A SER A 1 178 ? 9.707   -15.441 28.101  0.20 41.71  ? 178 SER A N     1 
ATOM   2722  N  N     B SER A 1 178 ? 9.863   -14.746 28.500  0.80 47.24  ? 178 SER A N     1 
ATOM   2723  C  CA    A SER A 1 178 ? 9.563   -14.407 27.088  0.20 38.19  ? 178 SER A CA    1 
ATOM   2724  C  CA    B SER A 1 178 ? 9.525   -13.839 27.409  0.80 41.27  ? 178 SER A CA    1 
ATOM   2725  C  C     A SER A 1 178 ? 9.488   -15.037 25.702  0.20 34.79  ? 178 SER A C     1 
ATOM   2726  C  C     B SER A 1 178 ? 9.737   -14.515 26.054  0.80 35.40  ? 178 SER A C     1 
ATOM   2727  O  O     A SER A 1 178 ? 9.670   -16.245 25.526  0.20 35.09  ? 178 SER A O     1 
ATOM   2728  O  O     B SER A 1 178 ? 10.271  -15.625 25.954  0.80 36.09  ? 178 SER A O     1 
ATOM   2729  C  CB    A SER A 1 178 ? 10.724  -13.407 27.149  0.20 37.74  ? 178 SER A CB    1 
ATOM   2730  C  CB    B SER A 1 178 ? 10.350  -12.552 27.492  0.80 39.42  ? 178 SER A CB    1 
ATOM   2731  O  OG    A SER A 1 178 ? 11.958  -14.051 26.888  0.20 37.59  ? 178 SER A OG    1 
ATOM   2732  O  OG    B SER A 1 178 ? 11.739  -12.829 27.505  0.80 46.38  ? 178 SER A OG    1 
ATOM   2733  N  N     A THR A 1 179 ? 9.223   -14.193 24.707  0.20 32.43  ? 179 THR A N     1 
ATOM   2734  N  N     B THR A 1 179 ? 9.303   -13.829 24.996  0.80 30.30  ? 179 THR A N     1 
ATOM   2735  C  CA    A THR A 1 179 ? 9.095   -14.640 23.324  0.20 29.35  ? 179 THR A CA    1 
ATOM   2736  C  CA    B THR A 1 179 ? 9.425   -14.352 23.641  0.80 30.55  ? 179 THR A CA    1 
ATOM   2737  C  C     A THR A 1 179 ? 10.096  -13.949 22.409  0.20 31.89  ? 179 THR A C     1 
ATOM   2738  C  C     B THR A 1 179 ? 10.379  -13.559 22.762  0.80 32.49  ? 179 THR A C     1 
ATOM   2739  O  O     A THR A 1 179 ? 10.896  -14.626 21.755  0.20 32.13  ? 179 THR A O     1 
ATOM   2740  O  O     B THR A 1 179 ? 11.072  -14.170 21.945  0.80 36.03  ? 179 THR A O     1 
ATOM   2741  C  CB    A THR A 1 179 ? 7.667   -14.400 22.819  0.20 31.24  ? 179 THR A CB    1 
ATOM   2742  C  CB    B THR A 1 179 ? 8.052   -14.420 22.948  0.80 31.98  ? 179 THR A CB    1 
ATOM   2743  O  OG1   A THR A 1 179 ? 6.746   -15.162 23.605  0.20 30.47  ? 179 THR A OG1   1 
ATOM   2744  O  OG1   B THR A 1 179 ? 7.532   -13.103 22.726  0.80 37.24  ? 179 THR A OG1   1 
ATOM   2745  C  CG2   A THR A 1 179 ? 7.552   -14.811 21.366  0.20 26.45  ? 179 THR A CG2   1 
ATOM   2746  C  CG2   B THR A 1 179 ? 7.067   -15.194 23.800  0.80 30.66  ? 179 THR A CG2   1 
ATOM   2747  N  N     A ALA A 1 180 ? 10.072  -12.622 22.341  0.20 29.43  ? 180 ALA A N     1 
ATOM   2748  N  N     B ALA A 1 180 ? 10.459  -12.231 22.914  0.80 29.81  ? 180 ALA A N     1 
ATOM   2749  C  CA    A ALA A 1 180 ? 10.930  -11.855 21.453  0.20 27.46  ? 180 ALA A CA    1 
ATOM   2750  C  CA    B ALA A 1 180 ? 11.203  -11.407 21.967  0.80 25.95  ? 180 ALA A CA    1 
ATOM   2751  C  C     A ALA A 1 180 ? 12.015  -11.138 22.246  0.20 25.55  ? 180 ALA A C     1 
ATOM   2752  C  C     B ALA A 1 180 ? 12.147  -10.427 22.657  0.80 21.46  ? 180 ALA A C     1 
ATOM   2753  O  O     A ALA A 1 180 ? 11.945  -11.006 23.469  0.20 26.69  ? 180 ALA A O     1 
ATOM   2754  O  O     B ALA A 1 180 ? 11.898  -9.947  23.762  0.80 22.31  ? 180 ALA A O     1 
ATOM   2755  C  CB    A ALA A 1 180 ? 10.111  -10.840 20.649  0.20 24.06  ? 180 ALA A CB    1 
ATOM   2756  C  CB    B ALA A 1 180 ? 10.261  -10.610 21.035  0.80 20.82  ? 180 ALA A CB    1 
ATOM   2757  N  N     A VAL A 1 181 ? 13.044  -10.683 21.527  0.20 26.06  ? 181 VAL A N     1 
ATOM   2758  N  N     B VAL A 1 181 ? 13.231  -10.098 21.949  0.80 26.87  ? 181 VAL A N     1 
ATOM   2759  C  CA    A VAL A 1 181 ? 14.030  -9.802  22.143  0.20 25.67  ? 181 VAL A CA    1 
ATOM   2760  C  CA    B VAL A 1 181 ? 14.188  -9.129  22.454  0.80 23.04  ? 181 VAL A CA    1 
ATOM   2761  C  C     A VAL A 1 181 ? 13.543  -8.362  22.148  0.20 21.66  ? 181 VAL A C     1 
ATOM   2762  C  C     B VAL A 1 181 ? 13.634  -7.711  22.428  0.80 22.31  ? 181 VAL A C     1 
ATOM   2763  O  O     A VAL A 1 181 ? 14.019  -7.553  22.951  0.20 24.41  ? 181 VAL A O     1 
ATOM   2764  O  O     B VAL A 1 181 ? 14.088  -6.862  23.202  0.80 26.75  ? 181 VAL A O     1 
ATOM   2765  C  CB    A VAL A 1 181 ? 15.392  -9.919  21.430  0.20 26.90  ? 181 VAL A CB    1 
ATOM   2766  C  CB    B VAL A 1 181 ? 15.488  -9.262  21.624  0.80 30.77  ? 181 VAL A CB    1 
ATOM   2767  C  CG1   A VAL A 1 181 ? 15.372  -9.191  20.094  0.20 26.71  ? 181 VAL A CG1   1 
ATOM   2768  C  CG1   B VAL A 1 181 ? 15.206  -8.950  20.174  0.80 26.82  ? 181 VAL A CG1   1 
ATOM   2769  C  CG2   A VAL A 1 181 ? 16.517  -9.407  22.317  0.20 25.84  ? 181 VAL A CG2   1 
ATOM   2770  C  CG2   B VAL A 1 181 ? 16.595  -8.382  22.158  0.80 27.60  ? 181 VAL A CG2   1 
ATOM   2771  N  N     A VAL A 1 182 ? 12.597  -8.028  21.281  0.20 23.06  ? 182 VAL A N     1 
ATOM   2772  N  N     B VAL A 1 182 ? 12.667  -7.424  21.555  0.80 19.54  ? 182 VAL A N     1 
ATOM   2773  C  CA    A VAL A 1 182 ? 12.125  -6.660  21.121  0.20 21.65  ? 182 VAL A CA    1 
ATOM   2774  C  CA    B VAL A 1 182 ? 12.172  -6.068  21.363  0.80 24.17  ? 182 VAL A CA    1 
ATOM   2775  C  C     A VAL A 1 182 ? 10.908  -6.376  22.008  0.20 23.45  ? 182 VAL A C     1 
ATOM   2776  C  C     B VAL A 1 182 ? 10.964  -5.800  22.263  0.80 23.27  ? 182 VAL A C     1 
ATOM   2777  O  O     A VAL A 1 182 ? 10.122  -5.476  21.709  0.20 22.83  ? 182 VAL A O     1 
ATOM   2778  O  O     B VAL A 1 182 ? 10.322  -4.747  22.150  0.80 26.71  ? 182 VAL A O     1 
ATOM   2779  C  CB    A VAL A 1 182 ? 11.827  -6.337  19.647  0.20 24.36  ? 182 VAL A CB    1 
ATOM   2780  C  CB    B VAL A 1 182 ? 11.794  -5.804  19.894  0.80 21.87  ? 182 VAL A CB    1 
ATOM   2781  C  CG1   A VAL A 1 182 ? 13.115  -6.414  18.810  0.20 25.26  ? 182 VAL A CG1   1 
ATOM   2782  C  CG1   B VAL A 1 182 ? 13.055  -5.739  18.977  0.80 28.20  ? 182 VAL A CG1   1 
ATOM   2783  C  CG2   A VAL A 1 182 ? 10.787  -7.278  19.087  0.20 26.52  ? 182 VAL A CG2   1 
ATOM   2784  C  CG2   B VAL A 1 182 ? 10.818  -6.848  19.413  0.80 27.43  ? 182 VAL A CG2   1 
ATOM   2785  N  N     A GLU A 1 183 ? 10.733  -7.130  23.093  0.20 21.84  ? 183 GLU A N     1 
ATOM   2786  N  N     B GLU A 1 183 ? 10.632  -6.738  23.153  0.80 22.34  ? 183 GLU A N     1 
ATOM   2787  C  CA    A GLU A 1 183 ? 9.599   -6.863  23.977  0.20 25.87  ? 183 GLU A CA    1 
ATOM   2788  C  CA    B GLU A 1 183 ? 9.513   -6.495  24.069  0.80 25.52  ? 183 GLU A CA    1 
ATOM   2789  C  C     A GLU A 1 183 ? 9.664   -5.497  24.661  0.20 23.95  ? 183 GLU A C     1 
ATOM   2790  C  C     B GLU A 1 183 ? 9.644   -5.201  24.874  0.80 23.64  ? 183 GLU A C     1 
ATOM   2791  O  O     A GLU A 1 183 ? 8.602   -4.859  24.794  0.20 25.55  ? 183 GLU A O     1 
ATOM   2792  O  O     B GLU A 1 183 ? 8.610   -4.547  25.095  0.80 25.06  ? 183 GLU A O     1 
ATOM   2793  C  CB    A GLU A 1 183 ? 9.466   -7.981  25.019  0.20 24.67  ? 183 GLU A CB    1 
ATOM   2794  C  CB    B GLU A 1 183 ? 9.311   -7.706  25.000  0.80 24.12  ? 183 GLU A CB    1 
ATOM   2795  C  CG    A GLU A 1 183 ? 9.201   -9.344  24.402  0.20 26.77  ? 183 GLU A CG    1 
ATOM   2796  C  CG    B GLU A 1 183 ? 8.750   -8.940  24.259  0.80 27.00  ? 183 GLU A CG    1 
ATOM   2797  C  CD    A GLU A 1 183 ? 8.933   -10.424 25.435  0.20 27.81  ? 183 GLU A CD    1 
ATOM   2798  C  CD    B GLU A 1 183 ? 8.262   -10.062 25.178  0.80 29.17  ? 183 GLU A CD    1 
ATOM   2799  O  OE1   A GLU A 1 183 ? 8.994   -10.124 26.646  0.20 26.15  ? 183 GLU A OE1   1 
ATOM   2800  O  OE1   B GLU A 1 183 ? 7.689   -9.767  26.246  0.80 24.50  ? 183 GLU A OE1   1 
ATOM   2801  O  OE2   A GLU A 1 183 ? 8.660   -11.575 25.031  0.20 26.27  ? 183 GLU A OE2   1 
ATOM   2802  O  OE2   B GLU A 1 183 ? 8.446   -11.253 24.821  0.80 25.52  ? 183 GLU A OE2   1 
ATOM   2803  N  N     A PRO A 1 184 ? 10.822  -4.998  25.123  0.20 23.43  ? 184 PRO A N     1 
ATOM   2804  N  N     B PRO A 1 184 ? 10.829  -4.762  25.321  0.80 22.51  ? 184 PRO A N     1 
ATOM   2805  C  CA    A PRO A 1 184 ? 10.831  -3.642  25.708  0.20 24.79  ? 184 PRO A CA    1 
ATOM   2806  C  CA    B PRO A 1 184 ? 10.906  -3.418  25.935  0.80 23.99  ? 184 PRO A CA    1 
ATOM   2807  C  C     A PRO A 1 184 ? 10.370  -2.551  24.753  0.20 26.27  ? 184 PRO A C     1 
ATOM   2808  C  C     B PRO A 1 184 ? 10.425  -2.296  25.024  0.80 26.25  ? 184 PRO A C     1 
ATOM   2809  O  O     A PRO A 1 184 ? 9.783   -1.558  25.204  0.20 26.80  ? 184 PRO A O     1 
ATOM   2810  O  O     B PRO A 1 184 ? 9.766   -1.367  25.505  0.80 27.40  ? 184 PRO A O     1 
ATOM   2811  C  CB    A PRO A 1 184 ? 12.298  -3.446  26.119  0.20 26.45  ? 184 PRO A CB    1 
ATOM   2812  C  CB    B PRO A 1 184 ? 12.399  -3.274  26.274  0.80 26.12  ? 184 PRO A CB    1 
ATOM   2813  C  CG    A PRO A 1 184 ? 12.800  -4.829  26.345  0.20 29.48  ? 184 PRO A CG    1 
ATOM   2814  C  CG    B PRO A 1 184 ? 12.860  -4.674  26.489  0.80 30.06  ? 184 PRO A CG    1 
ATOM   2815  C  CD    A PRO A 1 184 ? 12.133  -5.662  25.298  0.20 27.52  ? 184 PRO A CD    1 
ATOM   2816  C  CD    B PRO A 1 184 ? 12.118  -5.479  25.445  0.80 28.62  ? 184 PRO A CD    1 
ATOM   2817  N  N     A TYR A 1 185 ? 10.617  -2.698  23.448  0.20 24.79  ? 185 TYR A N     1 
ATOM   2818  N  N     B TYR A 1 185 ? 10.743  -2.351  23.723  0.80 24.34  ? 185 TYR A N     1 
ATOM   2819  C  CA    A TYR A 1 185 ? 10.143  -1.699  22.492  0.20 26.61  ? 185 TYR A CA    1 
ATOM   2820  C  CA    B TYR A 1 185 ? 10.251  -1.350  22.773  0.80 26.83  ? 185 TYR A CA    1 
ATOM   2821  C  C     A TYR A 1 185 ? 8.622   -1.682  22.415  0.20 23.39  ? 185 TYR A C     1 
ATOM   2822  C  C     B TYR A 1 185 ? 8.728   -1.339  22.713  0.80 23.53  ? 185 TYR A C     1 
ATOM   2823  O  O     A TYR A 1 185 ? 8.007   -0.610  22.387  0.20 24.06  ? 185 TYR A O     1 
ATOM   2824  O  O     B TYR A 1 185 ? 8.093   -0.282  22.841  0.80 23.76  ? 185 TYR A O     1 
ATOM   2825  C  CB    A TYR A 1 185 ? 10.725  -1.965  21.103  0.20 22.56  ? 185 TYR A CB    1 
ATOM   2826  C  CB    B TYR A 1 185 ? 10.791  -1.630  21.369  0.80 21.19  ? 185 TYR A CB    1 
ATOM   2827  C  CG    A TYR A 1 185 ? 12.123  -1.424  20.874  0.20 26.62  ? 185 TYR A CG    1 
ATOM   2828  C  CG    B TYR A 1 185 ? 12.232  -1.220  21.098  0.80 26.94  ? 185 TYR A CG    1 
ATOM   2829  C  CD1   A TYR A 1 185 ? 12.923  -1.018  21.934  0.20 27.88  ? 185 TYR A CD1   1 
ATOM   2830  C  CD1   B TYR A 1 185 ? 12.976  -0.484  22.019  0.80 28.06  ? 185 TYR A CD1   1 
ATOM   2831  C  CD2   A TYR A 1 185 ? 12.630  -1.299  19.587  0.20 25.11  ? 185 TYR A CD2   1 
ATOM   2832  C  CD2   B TYR A 1 185 ? 12.826  -1.540  19.894  0.80 24.30  ? 185 TYR A CD2   1 
ATOM   2833  C  CE1   A TYR A 1 185 ? 14.198  -0.519  21.718  0.20 28.68  ? 185 TYR A CE1   1 
ATOM   2834  C  CE1   B TYR A 1 185 ? 14.296  -0.106  21.745  0.80 28.69  ? 185 TYR A CE1   1 
ATOM   2835  C  CE2   A TYR A 1 185 ? 13.898  -0.802  19.362  0.20 27.65  ? 185 TYR A CE2   1 
ATOM   2836  C  CE2   B TYR A 1 185 ? 14.137  -1.165  19.609  0.80 30.16  ? 185 TYR A CE2   1 
ATOM   2837  C  CZ    A TYR A 1 185 ? 14.680  -0.417  20.428  0.20 26.12  ? 185 TYR A CZ    1 
ATOM   2838  C  CZ    B TYR A 1 185 ? 14.870  -0.462  20.533  0.80 25.59  ? 185 TYR A CZ    1 
ATOM   2839  O  OH    A TYR A 1 185 ? 15.947  0.078   20.195  0.20 26.93  ? 185 TYR A OH    1 
ATOM   2840  O  OH    B TYR A 1 185 ? 16.177  -0.097  20.227  0.80 26.01  ? 185 TYR A OH    1 
ATOM   2841  N  N     A ASN A 1 186 ? 8.001   -2.862  22.363  0.20 22.93  ? 186 ASN A N     1 
ATOM   2842  N  N     B ASN A 1 186 ? 8.132   -2.509  22.453  0.80 20.77  ? 186 ASN A N     1 
ATOM   2843  C  CA    A ASN A 1 186 ? 6.550   -2.935  22.232  0.20 23.62  ? 186 ASN A CA    1 
ATOM   2844  C  CA    B ASN A 1 186 ? 6.682   -2.617  22.323  0.80 23.02  ? 186 ASN A CA    1 
ATOM   2845  C  C     A ASN A 1 186 ? 5.854   -2.373  23.464  0.20 24.11  ? 186 ASN A C     1 
ATOM   2846  C  C     B ASN A 1 186 ? 5.979   -2.169  23.597  0.80 23.12  ? 186 ASN A C     1 
ATOM   2847  O  O     A ASN A 1 186 ? 4.817   -1.708  23.349  0.20 27.16  ? 186 ASN A O     1 
ATOM   2848  O  O     B ASN A 1 186 ? 4.911   -1.550  23.538  0.80 27.97  ? 186 ASN A O     1 
ATOM   2849  C  CB    A ASN A 1 186 ? 6.124   -4.381  21.990  0.20 24.70  ? 186 ASN A CB    1 
ATOM   2850  C  CB    B ASN A 1 186 ? 6.294   -4.056  21.981  0.80 25.44  ? 186 ASN A CB    1 
ATOM   2851  C  CG    A ASN A 1 186 ? 6.924   -5.047  20.886  0.20 24.86  ? 186 ASN A CG    1 
ATOM   2852  C  CG    B ASN A 1 186 ? 6.863   -4.519  20.640  0.80 23.74  ? 186 ASN A CG    1 
ATOM   2853  O  OD1   A ASN A 1 186 ? 7.172   -4.453  19.835  0.20 23.34  ? 186 ASN A OD1   1 
ATOM   2854  O  OD1   B ASN A 1 186 ? 7.231   -3.707  19.798  0.80 24.35  ? 186 ASN A OD1   1 
ATOM   2855  N  ND2   A ASN A 1 186 ? 7.336   -6.288  21.122  0.20 21.98  ? 186 ASN A ND2   1 
ATOM   2856  N  ND2   B ASN A 1 186 ? 6.917   -5.837  20.440  0.80 24.54  ? 186 ASN A ND2   1 
ATOM   2857  N  N     A SER A 1 187 ? 6.416   -2.622  24.648  0.20 26.89  ? 187 SER A N     1 
ATOM   2858  N  N     B SER A 1 187 ? 6.575   -2.461  24.753  0.80 27.91  ? 187 SER A N     1 
ATOM   2859  C  CA    A SER A 1 187 ? 5.775   -2.199  25.889  0.20 27.13  ? 187 SER A CA    1 
ATOM   2860  C  CA    B SER A 1 187 ? 5.982   -2.088  26.034  0.80 27.60  ? 187 SER A CA    1 
ATOM   2861  C  C     A SER A 1 187 ? 5.743   -0.679  26.013  0.20 28.24  ? 187 SER A C     1 
ATOM   2862  C  C     B SER A 1 187 ? 5.860   -0.572  26.172  0.80 29.13  ? 187 SER A C     1 
ATOM   2863  O  O     A SER A 1 187 ? 4.759   -0.110  26.503  0.20 25.32  ? 187 SER A O     1 
ATOM   2864  O  O     B SER A 1 187 ? 4.821   -0.051  26.606  0.80 24.83  ? 187 SER A O     1 
ATOM   2865  C  CB    A SER A 1 187 ? 6.504   -2.817  27.081  0.20 27.34  ? 187 SER A CB    1 
ATOM   2866  C  CB    B SER A 1 187 ? 6.829   -2.667  27.166  0.80 26.79  ? 187 SER A CB    1 
ATOM   2867  O  OG    A SER A 1 187 ? 6.707   -4.208  26.894  0.20 25.67  ? 187 SER A OG    1 
ATOM   2868  O  OG    B SER A 1 187 ? 6.887   -4.083  27.093  0.80 25.70  ? 187 SER A OG    1 
ATOM   2869  N  N     A ILE A 1 188 ? 6.812   -0.008  25.581  0.20 27.14  ? 188 ILE A N     1 
ATOM   2870  N  N     B ILE A 1 188 ? 6.930   0.149   25.825  0.80 27.53  ? 188 ILE A N     1 
ATOM   2871  C  CA    A ILE A 1 188 ? 6.870   1.447   25.683  0.20 26.40  ? 188 ILE A CA    1 
ATOM   2872  C  CA    B ILE A 1 188 ? 6.940   1.604   25.933  0.80 25.44  ? 188 ILE A CA    1 
ATOM   2873  C  C     A ILE A 1 188 ? 5.938   2.091   24.665  0.20 25.74  ? 188 ILE A C     1 
ATOM   2874  C  C     B ILE A 1 188 ? 6.064   2.227   24.853  0.80 24.62  ? 188 ILE A C     1 
ATOM   2875  O  O     A ILE A 1 188 ? 5.257   3.078   24.964  0.20 25.45  ? 188 ILE A O     1 
ATOM   2876  O  O     B ILE A 1 188 ? 5.339   3.193   25.102  0.80 25.25  ? 188 ILE A O     1 
ATOM   2877  C  CB    A ILE A 1 188 ? 8.322   1.935   25.511  0.20 29.09  ? 188 ILE A CB    1 
ATOM   2878  C  CB    B ILE A 1 188 ? 8.387   2.127   25.858  0.80 28.81  ? 188 ILE A CB    1 
ATOM   2879  C  CG1   A ILE A 1 188 ? 9.225   1.325   26.586  0.20 31.87  ? 188 ILE A CG1   1 
ATOM   2880  C  CG1   B ILE A 1 188 ? 9.236   1.556   26.999  0.80 33.61  ? 188 ILE A CG1   1 
ATOM   2881  C  CG2   A ILE A 1 188 ? 8.387   3.454   25.546  0.20 31.60  ? 188 ILE A CG2   1 
ATOM   2882  C  CG2   B ILE A 1 188 ? 8.419   3.648   25.829  0.80 33.48  ? 188 ILE A CG2   1 
ATOM   2883  C  CD1   A ILE A 1 188 ? 8.814   1.666   27.993  0.20 29.30  ? 188 ILE A CD1   1 
ATOM   2884  C  CD1   B ILE A 1 188 ? 8.669   1.792   28.327  0.80 31.17  ? 188 ILE A CD1   1 
ATOM   2885  N  N     A LEU A 1 189 ? 5.889   1.547   23.448  0.20 27.55  ? 189 LEU A N     1 
ATOM   2886  N  N     B LEU A 1 189 ? 6.125   1.704   23.630  0.80 26.85  ? 189 LEU A N     1 
ATOM   2887  C  CA    A LEU A 1 189 ? 5.013   2.114   22.427  0.20 26.57  ? 189 LEU A CA    1 
ATOM   2888  C  CA    B LEU A 1 189 ? 5.281   2.251   22.570  0.80 24.64  ? 189 LEU A CA    1 
ATOM   2889  C  C     A LEU A 1 189 ? 3.541   1.924   22.782  0.20 28.34  ? 189 LEU A C     1 
ATOM   2890  C  C     B LEU A 1 189 ? 3.793   2.159   22.926  0.80 29.99  ? 189 LEU A C     1 
ATOM   2891  O  O     A LEU A 1 189 ? 2.715   2.805   22.513  0.20 26.09  ? 189 LEU A O     1 
ATOM   2892  O  O     B LEU A 1 189 ? 3.042   3.134   22.780  0.80 28.33  ? 189 LEU A O     1 
ATOM   2893  C  CB    A LEU A 1 189 ? 5.323   1.489   21.069  0.20 24.54  ? 189 LEU A CB    1 
ATOM   2894  C  CB    B LEU A 1 189 ? 5.570   1.527   21.259  0.80 23.34  ? 189 LEU A CB    1 
ATOM   2895  C  CG    A LEU A 1 189 ? 6.744   1.710   20.548  0.20 27.80  ? 189 LEU A CG    1 
ATOM   2896  C  CG    B LEU A 1 189 ? 6.956   1.874   20.719  0.80 27.98  ? 189 LEU A CG    1 
ATOM   2897  C  CD1   A LEU A 1 189 ? 6.964   0.949   19.248  0.20 28.15  ? 189 LEU A CD1   1 
ATOM   2898  C  CD1   B LEU A 1 189 ? 7.460   0.825   19.727  0.80 29.40  ? 189 LEU A CD1   1 
ATOM   2899  C  CD2   A LEU A 1 189 ? 7.018   3.194   20.369  0.20 30.80  ? 189 LEU A CD2   1 
ATOM   2900  C  CD2   B LEU A 1 189 ? 6.890   3.248   20.085  0.80 31.59  ? 189 LEU A CD2   1 
ATOM   2901  N  N     A THR A 1 190 ? 3.189   0.785   23.384  0.20 27.07  ? 190 THR A N     1 
ATOM   2902  N  N     B THR A 1 190 ? 3.334   0.994   23.386  0.80 26.97  ? 190 THR A N     1 
ATOM   2903  C  CA    A THR A 1 190 ? 1.793   0.533   23.719  0.20 27.71  ? 190 THR A CA    1 
ATOM   2904  C  CA    B THR A 1 190 ? 1.900   0.889   23.636  0.80 27.15  ? 190 THR A CA    1 
ATOM   2905  C  C     A THR A 1 190 ? 1.360   1.232   25.002  0.20 29.29  ? 190 THR A C     1 
ATOM   2906  C  C     B THR A 1 190 ? 1.503   1.675   24.885  0.80 27.88  ? 190 THR A C     1 
ATOM   2907  O  O     A THR A 1 190 ? 0.155   1.389   25.228  0.20 28.79  ? 190 THR A O     1 
ATOM   2908  O  O     B THR A 1 190 ? 0.428   2.293   24.920  0.80 24.37  ? 190 THR A O     1 
ATOM   2909  C  CB    A THR A 1 190 ? 1.529   -0.973  23.837  0.20 27.76  ? 190 THR A CB    1 
ATOM   2910  C  CB    B THR A 1 190 ? 1.461   -0.580  23.726  0.80 27.39  ? 190 THR A CB    1 
ATOM   2911  O  OG1   A THR A 1 190 ? 0.116   -1.210  23.854  0.20 30.90  ? 190 THR A OG1   1 
ATOM   2912  O  OG1   B THR A 1 190 ? 0.032   -0.641  23.772  0.80 34.47  ? 190 THR A OG1   1 
ATOM   2913  C  CG2   A THR A 1 190 ? 2.136   -1.534  25.117  0.20 29.69  ? 190 THR A CG2   1 
ATOM   2914  C  CG2   B THR A 1 190 ? 2.019   -1.277  24.966  0.80 31.46  ? 190 THR A CG2   1 
ATOM   2915  N  N     A THR A 1 191 ? 2.305   1.651   25.844  0.20 28.35  ? 191 THR A N     1 
ATOM   2916  N  N     B THR A 1 191 ? 2.357   1.679   25.913  0.80 28.39  ? 191 THR A N     1 
ATOM   2917  C  CA    A THR A 1 191 ? 1.949   2.424   27.029  0.20 27.95  ? 191 THR A CA    1 
ATOM   2918  C  CA    B THR A 1 191 ? 2.089   2.494   27.095  0.80 27.77  ? 191 THR A CA    1 
ATOM   2919  C  C     A THR A 1 191 ? 1.813   3.907   26.702  0.20 27.63  ? 191 THR A C     1 
ATOM   2920  C  C     B THR A 1 191 ? 1.876   3.949   26.695  0.80 27.63  ? 191 THR A C     1 
ATOM   2921  O  O     A THR A 1 191 ? 1.066   4.622   27.376  0.20 26.86  ? 191 THR A O     1 
ATOM   2922  O  O     B THR A 1 191 ? 0.871   4.565   27.060  0.80 24.31  ? 191 THR A O     1 
ATOM   2923  C  CB    A THR A 1 191 ? 2.989   2.198   28.134  0.20 27.66  ? 191 THR A CB    1 
ATOM   2924  C  CB    B THR A 1 191 ? 3.239   2.364   28.102  0.80 26.47  ? 191 THR A CB    1 
ATOM   2925  O  OG1   A THR A 1 191 ? 3.113   0.793   28.394  0.20 26.81  ? 191 THR A OG1   1 
ATOM   2926  O  OG1   B THR A 1 191 ? 3.321   1.006   28.573  0.80 27.14  ? 191 THR A OG1   1 
ATOM   2927  C  CG2   A THR A 1 191 ? 2.579   2.900   29.429  0.20 29.95  ? 191 THR A CG2   1 
ATOM   2928  C  CG2   B THR A 1 191 ? 3.018   3.298   29.301  0.80 32.83  ? 191 THR A CG2   1 
ATOM   2929  N  N     A HIS A 1 192 ? 2.497   4.376   25.655  0.20 28.40  ? 192 HIS A N     1 
ATOM   2930  N  N     B HIS A 1 192 ? 2.779   4.487   25.868  0.80 28.63  ? 192 HIS A N     1 
ATOM   2931  C  CA    A HIS A 1 192 ? 2.394   5.776   25.256  0.20 29.36  ? 192 HIS A CA    1 
ATOM   2932  C  CA    B HIS A 1 192 ? 2.672   5.877   25.429  0.80 29.82  ? 192 HIS A CA    1 
ATOM   2933  C  C     A HIS A 1 192 ? 1.069   6.070   24.563  0.20 30.74  ? 192 HIS A C     1 
ATOM   2934  C  C     B HIS A 1 192 ? 1.351   6.147   24.723  0.80 30.95  ? 192 HIS A C     1 
ATOM   2935  O  O     A HIS A 1 192 ? 0.352   6.999   24.949  0.20 33.30  ? 192 HIS A O     1 
ATOM   2936  O  O     B HIS A 1 192 ? 0.669   7.133   25.022  0.80 34.91  ? 192 HIS A O     1 
ATOM   2937  C  CB    A HIS A 1 192 ? 3.561   6.153   24.340  0.20 28.70  ? 192 HIS A CB    1 
ATOM   2938  C  CB    B HIS A 1 192 ? 3.836   6.232   24.504  0.80 27.95  ? 192 HIS A CB    1 
ATOM   2939  C  CG    A HIS A 1 192 ? 3.404   7.490   23.684  0.20 32.21  ? 192 HIS A CG    1 
ATOM   2940  C  CG    B HIS A 1 192 ? 3.667   7.537   23.785  0.80 33.44  ? 192 HIS A CG    1 
ATOM   2941  N  ND1   A HIS A 1 192 ? 3.041   8.623   24.381  0.20 31.97  ? 192 HIS A ND1   1 
ATOM   2942  N  ND1   B HIS A 1 192 ? 3.440   8.729   24.444  0.80 33.06  ? 192 HIS A ND1   1 
ATOM   2943  C  CD2   A HIS A 1 192 ? 3.563   7.875   22.395  0.20 30.69  ? 192 HIS A CD2   1 
ATOM   2944  C  CD2   B HIS A 1 192 ? 3.710   7.841   22.464  0.80 30.30  ? 192 HIS A CD2   1 
ATOM   2945  C  CE1   A HIS A 1 192 ? 2.982   9.648   23.550  0.20 32.79  ? 192 HIS A CE1   1 
ATOM   2946  C  CE1   B HIS A 1 192 ? 3.346   9.708   23.561  0.80 32.79  ? 192 HIS A CE1   1 
ATOM   2947  N  NE2   A HIS A 1 192 ? 3.294   9.221   22.339  0.20 33.73  ? 192 HIS A NE2   1 
ATOM   2948  N  NE2   B HIS A 1 192 ? 3.502   9.194   22.352  0.80 33.60  ? 192 HIS A NE2   1 
ATOM   2949  N  N     A THR A 1 193 ? 0.730   5.292   23.533  0.20 26.83  ? 193 THR A N     1 
ATOM   2950  N  N     B THR A 1 193 ? 0.979   5.298   23.762  0.80 24.46  ? 193 THR A N     1 
ATOM   2951  C  CA    A THR A 1 193 ? -0.476  5.569   22.761  0.20 28.52  ? 193 THR A CA    1 
ATOM   2952  C  CA    B THR A 1 193 ? -0.189  5.606   22.944  0.80 26.29  ? 193 THR A CA    1 
ATOM   2953  C  C     A THR A 1 193 ? -1.752  5.218   23.515  0.20 31.20  ? 193 THR A C     1 
ATOM   2954  C  C     B THR A 1 193 ? -1.508  5.247   23.620  0.80 31.44  ? 193 THR A C     1 
ATOM   2955  O  O     A THR A 1 193 ? -2.833  5.654   23.107  0.20 30.48  ? 193 THR A O     1 
ATOM   2956  O  O     B THR A 1 193 ? -2.559  5.730   23.186  0.80 30.14  ? 193 THR A O     1 
ATOM   2957  C  CB    A THR A 1 193 ? -0.451  4.806   21.435  0.20 31.63  ? 193 THR A CB    1 
ATOM   2958  C  CB    B THR A 1 193 ? -0.110  4.887   21.594  0.80 32.00  ? 193 THR A CB    1 
ATOM   2959  O  OG1   A THR A 1 193 ? -0.262  3.408   21.690  0.20 31.84  ? 193 THR A OG1   1 
ATOM   2960  O  OG1   B THR A 1 193 ? 0.309   3.531   21.798  0.80 34.15  ? 193 THR A OG1   1 
ATOM   2961  C  CG2   A THR A 1 193 ? 0.671   5.313   20.557  0.20 31.75  ? 193 THR A CG2   1 
ATOM   2962  C  CG2   B THR A 1 193 ? 0.859   5.581   20.681  0.80 31.78  ? 193 THR A CG2   1 
ATOM   2963  N  N     A THR A 1 194 ? -1.658  4.444   24.594  0.20 29.02  ? 194 THR A N     1 
ATOM   2964  N  N     B THR A 1 194 ? -1.488  4.407   24.653  0.80 28.69  ? 194 THR A N     1 
ATOM   2965  C  CA    A THR A 1 194 ? -2.832  4.002   25.332  0.20 27.36  ? 194 THR A CA    1 
ATOM   2966  C  CA    B THR A 1 194 ? -2.717  4.006   25.327  0.80 27.04  ? 194 THR A CA    1 
ATOM   2967  C  C     A THR A 1 194 ? -2.972  4.684   26.687  0.20 30.01  ? 194 THR A C     1 
ATOM   2968  C  C     B THR A 1 194 ? -3.030  4.876   26.539  0.80 29.49  ? 194 THR A C     1 
ATOM   2969  O  O     A THR A 1 194 ? -3.972  4.461   27.379  0.20 31.72  ? 194 THR A O     1 
ATOM   2970  O  O     B THR A 1 194 ? -4.198  4.955   26.948  0.80 31.48  ? 194 THR A O     1 
ATOM   2971  C  CB    A THR A 1 194 ? -2.792  2.479   25.513  0.20 31.64  ? 194 THR A CB    1 
ATOM   2972  C  CB    B THR A 1 194 ? -2.622  2.524   25.736  0.80 32.09  ? 194 THR A CB    1 
ATOM   2973  O  OG1   A THR A 1 194 ? -2.099  1.885   24.407  0.20 32.10  ? 194 THR A OG1   1 
ATOM   2974  O  OG1   B THR A 1 194 ? -2.481  1.717   24.560  0.80 35.38  ? 194 THR A OG1   1 
ATOM   2975  C  CG2   A THR A 1 194 ? -4.198  1.908   25.565  0.20 29.90  ? 194 THR A CG2   1 
ATOM   2976  C  CG2   B THR A 1 194 ? -3.869  2.052   26.510  0.80 31.86  ? 194 THR A CG2   1 
ATOM   2977  N  N     A LEU A 1 195 ? -2.006  5.520   27.078  0.20 29.51  ? 195 LEU A N     1 
ATOM   2978  N  N     B LEU A 1 195 ? -2.022  5.575   27.075  0.80 29.50  ? 195 LEU A N     1 
ATOM   2979  C  CA    A LEU A 1 195 ? -2.057  6.177   28.379  0.20 33.59  ? 195 LEU A CA    1 
ATOM   2980  C  CA    B LEU A 1 195 ? -2.140  6.246   28.369  0.80 33.65  ? 195 LEU A CA    1 
ATOM   2981  C  C     A LEU A 1 195 ? -3.214  7.163   28.489  0.20 31.12  ? 195 LEU A C     1 
ATOM   2982  C  C     B LEU A 1 195 ? -3.359  7.161   28.429  0.80 30.73  ? 195 LEU A C     1 
ATOM   2983  O  O     A LEU A 1 195 ? -3.662  7.451   29.604  0.20 33.95  ? 195 LEU A O     1 
ATOM   2984  O  O     B LEU A 1 195 ? -4.209  7.026   29.315  0.80 29.92  ? 195 LEU A O     1 
ATOM   2985  C  CB    A LEU A 1 195 ? -0.734  6.896   28.651  0.20 30.22  ? 195 LEU A CB    1 
ATOM   2986  C  CB    B LEU A 1 195 ? -0.855  7.026   28.640  0.80 29.55  ? 195 LEU A CB    1 
ATOM   2987  C  CG    A LEU A 1 195 ? -0.437  7.327   30.088  0.20 37.16  ? 195 LEU A CG    1 
ATOM   2988  C  CG    B LEU A 1 195 ? -0.482  7.437   30.059  0.80 37.51  ? 195 LEU A CG    1 
ATOM   2989  C  CD1   A LEU A 1 195 ? -0.286  6.114   30.995  0.20 33.69  ? 195 LEU A CD1   1 
ATOM   2990  C  CD1   B LEU A 1 195 ? -0.631  6.275   31.031  0.80 33.76  ? 195 LEU A CD1   1 
ATOM   2991  C  CD2   A LEU A 1 195 ? 0.810   8.194   30.136  0.20 38.75  ? 195 LEU A CD2   1 
ATOM   2992  C  CD2   B LEU A 1 195 ? 0.944   7.939   30.053  0.80 39.88  ? 195 LEU A CD2   1 
ATOM   2993  N  N     A GLU A 1 196 ? -3.707  7.679   27.364  0.20 34.43  ? 196 GLU A N     1 
ATOM   2994  N  N     B GLU A 1 196 ? -3.478  8.084   27.474  0.80 34.92  ? 196 GLU A N     1 
ATOM   2995  C  CA    A GLU A 1 196 ? -4.802  8.641   27.367  0.20 33.92  ? 196 GLU A CA    1 
ATOM   2996  C  CA    B GLU A 1 196 ? -4.622  8.994   27.450  0.80 32.38  ? 196 GLU A CA    1 
ATOM   2997  C  C     A GLU A 1 196 ? -6.167  7.984   27.207  0.20 35.70  ? 196 GLU A C     1 
ATOM   2998  C  C     B GLU A 1 196 ? -5.959  8.263   27.359  0.80 37.72  ? 196 GLU A C     1 
ATOM   2999  O  O     A GLU A 1 196 ? -7.153  8.474   27.772  0.20 35.98  ? 196 GLU A O     1 
ATOM   3000  O  O     B GLU A 1 196 ? -6.984  8.819   27.773  0.80 36.89  ? 196 GLU A O     1 
ATOM   3001  C  CB    A GLU A 1 196 ? -4.592  9.671   26.252  0.20 38.18  ? 196 GLU A CB    1 
ATOM   3002  C  CB    B GLU A 1 196 ? -4.480  9.969   26.277  0.80 38.32  ? 196 GLU A CB    1 
ATOM   3003  C  CG    A GLU A 1 196 ? -5.654  10.754  26.175  0.20 41.99  ? 196 GLU A CG    1 
ATOM   3004  C  CG    B GLU A 1 196 ? -5.575  11.016  26.175  0.80 42.60  ? 196 GLU A CG    1 
ATOM   3005  C  CD    A GLU A 1 196 ? -5.437  11.701  25.008  0.20 46.17  ? 196 GLU A CD    1 
ATOM   3006  C  CD    B GLU A 1 196 ? -5.689  11.616  24.777  0.80 46.56  ? 196 GLU A CD    1 
ATOM   3007  O  OE1   A GLU A 1 196 ? -4.291  11.796  24.518  0.20 44.00  ? 196 GLU A OE1   1 
ATOM   3008  O  OE1   B GLU A 1 196 ? -4.733  11.483  23.986  0.80 45.26  ? 196 GLU A OE1   1 
ATOM   3009  O  OE2   A GLU A 1 196 ? -6.416  12.348  24.577  0.20 50.88  ? 196 GLU A OE2   1 
ATOM   3010  O  OE2   B GLU A 1 196 ? -6.741  12.219  24.473  0.80 52.17  ? 196 GLU A OE2   1 
ATOM   3011  N  N     A HIS A 1 197 ? -6.246  6.883   26.461  0.20 29.21  ? 197 HIS A N     1 
ATOM   3012  N  N     B HIS A 1 197 ? -5.973  7.019   26.876  0.80 25.88  ? 197 HIS A N     1 
ATOM   3013  C  CA    A HIS A 1 197 ? -7.504  6.202   26.190  0.20 33.29  ? 197 HIS A CA    1 
ATOM   3014  C  CA    B HIS A 1 197 ? -7.208  6.320   26.544  0.80 31.47  ? 197 HIS A CA    1 
ATOM   3015  C  C     A HIS A 1 197 ? -7.825  5.125   27.218  0.20 33.33  ? 197 HIS A C     1 
ATOM   3016  C  C     B HIS A 1 197 ? -7.639  5.279   27.568  0.80 34.08  ? 197 HIS A C     1 
ATOM   3017  O  O     A HIS A 1 197 ? -8.681  4.272   26.962  0.20 34.33  ? 197 HIS A O     1 
ATOM   3018  O  O     B HIS A 1 197 ? -8.701  4.681   27.398  0.80 39.09  ? 197 HIS A O     1 
ATOM   3019  C  CB    A HIS A 1 197 ? -7.479  5.594   24.787  0.20 31.26  ? 197 HIS A CB    1 
ATOM   3020  C  CB    B HIS A 1 197 ? -7.076  5.632   25.185  0.80 33.43  ? 197 HIS A CB    1 
ATOM   3021  C  CG    A HIS A 1 197 ? -6.987  6.535   23.735  0.20 34.42  ? 197 HIS A CG    1 
ATOM   3022  C  CG    B HIS A 1 197 ? -6.862  6.577   24.055  0.80 34.23  ? 197 HIS A CG    1 
ATOM   3023  N  ND1   A HIS A 1 197 ? -7.767  7.547   23.219  0.20 34.41  ? 197 HIS A ND1   1 
ATOM   3024  N  ND1   B HIS A 1 197 ? -7.773  7.555   23.724  0.80 33.85  ? 197 HIS A ND1   1 
ATOM   3025  C  CD2   A HIS A 1 197 ? -5.792  6.620   23.104  0.20 32.93  ? 197 HIS A CD2   1 
ATOM   3026  C  CD2   B HIS A 1 197 ? -5.837  6.699   23.181  0.80 32.79  ? 197 HIS A CD2   1 
ATOM   3027  C  CE1   A HIS A 1 197 ? -7.075  8.211   22.311  0.20 35.59  ? 197 HIS A CE1   1 
ATOM   3028  C  CE1   B HIS A 1 197 ? -7.323  8.233   22.684  0.80 35.33  ? 197 HIS A CE1   1 
ATOM   3029  N  NE2   A HIS A 1 197 ? -5.873  7.670   22.224  0.20 36.96  ? 197 HIS A NE2   1 
ATOM   3030  N  NE2   B HIS A 1 197 ? -6.150  7.734   22.335  0.80 37.80  ? 197 HIS A NE2   1 
ATOM   3031  N  N     A SER A 1 198 ? -7.153  5.138   28.364  0.20 29.87  ? 198 SER A N     1 
ATOM   3032  N  N     B SER A 1 198 ? -6.847  5.028   28.602  0.80 28.21  ? 198 SER A N     1 
ATOM   3033  C  CA    A SER A 1 198 ? -7.403  4.195   29.439  0.20 30.25  ? 198 SER A CA    1 
ATOM   3034  C  CA    B SER A 1 198 ? -7.121  3.979   29.571  0.80 29.84  ? 198 SER A CA    1 
ATOM   3035  C  C     A SER A 1 198 ? -7.714  4.956   30.719  0.20 28.56  ? 198 SER A C     1 
ATOM   3036  C  C     B SER A 1 198 ? -7.314  4.622   30.937  0.80 26.49  ? 198 SER A C     1 
ATOM   3037  O  O     A SER A 1 198 ? -7.353  6.126   30.874  0.20 28.84  ? 198 SER A O     1 
ATOM   3038  O  O     B SER A 1 198 ? -6.486  5.428   31.366  0.80 28.11  ? 198 SER A O     1 
ATOM   3039  C  CB    A SER A 1 198 ? -6.201  3.271   29.663  0.20 30.29  ? 198 SER A CB    1 
ATOM   3040  C  CB    B SER A 1 198 ? -5.972  2.968   29.606  0.80 30.38  ? 198 SER A CB    1 
ATOM   3041  O  OG    A SER A 1 198 ? -6.412  2.422   30.778  0.20 33.02  ? 198 SER A OG    1 
ATOM   3042  O  OG    B SER A 1 198 ? -6.283  1.852   30.416  0.80 37.25  ? 198 SER A OG    1 
ATOM   3043  N  N     A ASP A 1 199 ? -8.392  4.274   31.640  0.20 27.77  ? 199 ASP A N     1 
ATOM   3044  N  N     B ASP A 1 199 ? -8.405  4.280   31.617  0.80 27.74  ? 199 ASP A N     1 
ATOM   3045  C  CA    A ASP A 1 199 ? -8.745  4.837   32.938  0.20 22.67  ? 199 ASP A CA    1 
ATOM   3046  C  CA    B ASP A 1 199 ? -8.708  4.934   32.886  0.80 21.85  ? 199 ASP A CA    1 
ATOM   3047  C  C     A ASP A 1 199 ? -7.975  4.225   34.095  0.20 25.98  ? 199 ASP A C     1 
ATOM   3048  C  C     B ASP A 1 199 ? -8.060  4.260   34.084  0.80 25.79  ? 199 ASP A C     1 
ATOM   3049  O  O     A ASP A 1 199 ? -7.562  4.948   35.004  0.20 29.57  ? 199 ASP A O     1 
ATOM   3050  O  O     B ASP A 1 199 ? -7.925  4.886   35.145  0.80 30.31  ? 199 ASP A O     1 
ATOM   3051  C  CB    A ASP A 1 199 ? -10.248 4.673   33.199  0.20 32.00  ? 199 ASP A CB    1 
ATOM   3052  C  CB    B ASP A 1 199 ? -10.229 4.976   33.105  0.80 34.02  ? 199 ASP A CB    1 
ATOM   3053  C  CG    A ASP A 1 199 ? -11.085 5.684   32.441  0.20 33.18  ? 199 ASP A CG    1 
ATOM   3054  C  CG    B ASP A 1 199 ? -10.971 5.535   31.905  0.80 33.03  ? 199 ASP A CG    1 
ATOM   3055  O  OD1   A ASP A 1 199 ? -10.846 6.899   32.605  0.20 33.18  ? 199 ASP A OD1   1 
ATOM   3056  O  OD1   B ASP A 1 199 ? -10.725 6.703   31.542  0.80 38.45  ? 199 ASP A OD1   1 
ATOM   3057  O  OD2   A ASP A 1 199 ? -11.972 5.263   31.673  0.20 31.10  ? 199 ASP A OD2   1 
ATOM   3058  O  OD2   B ASP A 1 199 ? -11.776 4.800   31.307  0.80 29.37  ? 199 ASP A OD2   1 
ATOM   3059  N  N     A CYS A 1 200 ? -7.784  2.908   34.095  0.20 26.82  ? 200 CYS A N     1 
ATOM   3060  N  N     B CYS A 1 200 ? -7.692  2.997   33.947  0.80 27.01  ? 200 CYS A N     1 
ATOM   3061  C  CA    A CYS A 1 200 ? -7.055  2.236   35.169  0.20 23.04  ? 200 CYS A CA    1 
ATOM   3062  C  CA    B CYS A 1 200 ? -7.172  2.179   35.030  0.80 22.24  ? 200 CYS A CA    1 
ATOM   3063  C  C     A CYS A 1 200 ? -6.613  0.874   34.662  0.20 25.89  ? 200 CYS A C     1 
ATOM   3064  C  C     B CYS A 1 200 ? -6.573  0.939   34.386  0.80 25.46  ? 200 CYS A C     1 
ATOM   3065  O  O     A CYS A 1 200 ? -7.456  0.052   34.292  0.20 26.66  ? 200 CYS A O     1 
ATOM   3066  O  O     B CYS A 1 200 ? -7.177  0.369   33.475  0.80 28.77  ? 200 CYS A O     1 
ATOM   3067  C  CB    A CYS A 1 200 ? -7.928  2.089   36.418  0.20 24.06  ? 200 CYS A CB    1 
ATOM   3068  C  CB    B CYS A 1 200 ? -8.294  1.804   36.019  0.80 19.54  ? 200 CYS A CB    1 
ATOM   3069  S  SG    A CYS A 1 200 ? -7.085  1.304   37.811  0.20 24.04  ? 200 CYS A SG    1 
ATOM   3070  S  SG    B CYS A 1 200 ? -7.730  0.960   37.475  0.80 32.57  ? 200 CYS A SG    1 
ATOM   3071  N  N     A ALA A 1 201 ? -5.305  0.633   34.652  0.20 27.98  ? 201 ALA A N     1 
ATOM   3072  N  N     B ALA A 1 201 ? -5.383  0.545   34.831  0.80 28.09  ? 201 ALA A N     1 
ATOM   3073  C  CA    A ALA A 1 201 ? -4.734  -0.607  34.145  0.20 29.07  ? 201 ALA A CA    1 
ATOM   3074  C  CA    B ALA A 1 201 ? -4.672  -0.567  34.205  0.80 29.28  ? 201 ALA A CA    1 
ATOM   3075  C  C     A ALA A 1 201 ? -4.109  -1.403  35.281  0.20 28.60  ? 201 ALA A C     1 
ATOM   3076  C  C     B ALA A 1 201 ? -3.988  -1.385  35.281  0.80 29.00  ? 201 ALA A C     1 
ATOM   3077  O  O     A ALA A 1 201 ? -3.476  -0.834  36.176  0.20 28.67  ? 201 ALA A O     1 
ATOM   3078  O  O     B ALA A 1 201 ? -3.152  -0.851  36.017  0.80 30.15  ? 201 ALA A O     1 
ATOM   3079  C  CB    A ALA A 1 201 ? -3.682  -0.328  33.068  0.20 26.87  ? 201 ALA A CB    1 
ATOM   3080  C  CB    B ALA A 1 201 ? -3.644  -0.067  33.181  0.80 26.12  ? 201 ALA A CB    1 
ATOM   3081  N  N     A PHE A 1 202 ? -4.286  -2.724  35.235  0.20 24.80  ? 202 PHE A N     1 
ATOM   3082  N  N     B PHE A 1 202 ? -4.332  -2.677  35.354  0.80 24.59  ? 202 PHE A N     1 
ATOM   3083  C  CA    A PHE A 1 202 ? -3.725  -3.646  36.218  0.20 25.95  ? 202 PHE A CA    1 
ATOM   3084  C  CA    B PHE A 1 202 ? -3.729  -3.621  36.292  0.80 25.88  ? 202 PHE A CA    1 
ATOM   3085  C  C     A PHE A 1 202 ? -2.619  -4.455  35.547  0.20 27.18  ? 202 PHE A C     1 
ATOM   3086  C  C     B PHE A 1 202 ? -2.596  -4.372  35.594  0.80 27.29  ? 202 PHE A C     1 
ATOM   3087  O  O     A PHE A 1 202 ? -2.898  -5.345  34.735  0.20 27.04  ? 202 PHE A O     1 
ATOM   3088  O  O     B PHE A 1 202 ? -2.841  -5.275  34.784  0.80 27.13  ? 202 PHE A O     1 
ATOM   3089  C  CB    A PHE A 1 202 ? -4.804  -4.566  36.787  0.20 24.61  ? 202 PHE A CB    1 
ATOM   3090  C  CB    B PHE A 1 202 ? -4.771  -4.600  36.832  0.80 24.50  ? 202 PHE A CB    1 
ATOM   3091  C  CG    A PHE A 1 202 ? -5.936  -3.834  37.457  0.20 25.99  ? 202 PHE A CG    1 
ATOM   3092  C  CG    B PHE A 1 202 ? -5.819  -3.942  37.698  0.80 25.66  ? 202 PHE A CG    1 
ATOM   3093  C  CD1   A PHE A 1 202 ? -5.808  -3.379  38.758  0.20 24.65  ? 202 PHE A CD1   1 
ATOM   3094  C  CD1   B PHE A 1 202 ? -5.577  -3.714  39.039  0.80 23.72  ? 202 PHE A CD1   1 
ATOM   3095  C  CD2   A PHE A 1 202 ? -7.124  -3.601  36.784  0.20 24.66  ? 202 PHE A CD2   1 
ATOM   3096  C  CD2   B PHE A 1 202 ? -7.017  -3.514  37.151  0.80 24.70  ? 202 PHE A CD2   1 
ATOM   3097  C  CE1   A PHE A 1 202 ? -6.843  -2.701  39.378  0.20 25.36  ? 202 PHE A CE1   1 
ATOM   3098  C  CE1   B PHE A 1 202 ? -6.522  -3.084  39.833  0.80 24.54  ? 202 PHE A CE1   1 
ATOM   3099  C  CE2   A PHE A 1 202 ? -8.165  -2.923  37.398  0.20 26.84  ? 202 PHE A CE2   1 
ATOM   3100  C  CE2   B PHE A 1 202 ? -7.970  -2.880  37.937  0.80 27.86  ? 202 PHE A CE2   1 
ATOM   3101  C  CZ    A PHE A 1 202 ? -8.022  -2.473  38.696  0.20 27.37  ? 202 PHE A CZ    1 
ATOM   3102  C  CZ    B PHE A 1 202 ? -7.718  -2.667  39.280  0.80 27.30  ? 202 PHE A CZ    1 
ATOM   3103  N  N     A MET A 1 203 ? -1.371  -4.154  35.894  0.20 24.85  ? 203 MET A N     1 
ATOM   3104  N  N     B MET A 1 203 ? -1.366  -4.026  35.944  0.80 24.24  ? 203 MET A N     1 
ATOM   3105  C  CA    A MET A 1 203 ? -0.234  -4.861  35.323  0.20 26.98  ? 203 MET A CA    1 
ATOM   3106  C  CA    B MET A 1 203 ? -0.199  -4.692  35.390  0.80 26.76  ? 203 MET A CA    1 
ATOM   3107  C  C     A MET A 1 203 ? 0.035   -6.158  36.075  0.20 28.78  ? 203 MET A C     1 
ATOM   3108  C  C     B MET A 1 203 ? 0.101   -5.994  36.119  0.80 29.14  ? 203 MET A C     1 
ATOM   3109  O  O     A MET A 1 203 ? -0.058  -6.214  37.306  0.20 26.97  ? 203 MET A O     1 
ATOM   3110  O  O     B MET A 1 203 ? 0.097   -6.051  37.359  0.80 26.07  ? 203 MET A O     1 
ATOM   3111  C  CB    A MET A 1 203 ? 1.011   -3.978  35.347  0.20 27.63  ? 203 MET A CB    1 
ATOM   3112  C  CB    B MET A 1 203 ? 1.001   -3.768  35.450  0.80 27.30  ? 203 MET A CB    1 
ATOM   3113  C  CG    A MET A 1 203 ? 0.901   -2.742  34.474  0.20 31.96  ? 203 MET A CG    1 
ATOM   3114  C  CG    B MET A 1 203 ? 0.989   -2.753  34.339  0.80 32.46  ? 203 MET A CG    1 
ATOM   3115  S  SD    A MET A 1 203 ? 2.511   -2.034  34.079  0.20 36.41  ? 203 MET A SD    1 
ATOM   3116  S  SD    B MET A 1 203 ? 2.566   -1.906  34.279  0.80 39.15  ? 203 MET A SD    1 
ATOM   3117  C  CE    A MET A 1 203 ? 3.190   -1.755  35.714  0.20 30.50  ? 203 MET A CE    1 
ATOM   3118  C  CE    B MET A 1 203 ? 2.552   -1.063  35.859  0.80 29.28  ? 203 MET A CE    1 
ATOM   3119  N  N     A VAL A 1 204 ? 0.371   -7.203  35.321  0.20 26.00  ? 204 VAL A N     1 
ATOM   3120  N  N     B VAL A 1 204 ? 0.345   -7.041  35.335  0.80 25.69  ? 204 VAL A N     1 
ATOM   3121  C  CA    A VAL A 1 204 ? 0.636   -8.534  35.861  0.20 25.61  ? 204 VAL A CA    1 
ATOM   3122  C  CA    B VAL A 1 204 ? 0.737   -8.357  35.823  0.80 24.99  ? 204 VAL A CA    1 
ATOM   3123  C  C     A VAL A 1 204 ? 2.048   -8.917  35.431  0.20 26.31  ? 204 VAL A C     1 
ATOM   3124  C  C     B VAL A 1 204 ? 2.171   -8.593  35.356  0.80 27.01  ? 204 VAL A C     1 
ATOM   3125  O  O     A VAL A 1 204 ? 2.261   -9.366  34.298  0.20 26.07  ? 204 VAL A O     1 
ATOM   3126  O  O     B VAL A 1 204 ? 2.427   -8.713  34.149  0.80 25.71  ? 204 VAL A O     1 
ATOM   3127  C  CB    A VAL A 1 204 ? -0.388  -9.569  35.382  0.20 28.59  ? 204 VAL A CB    1 
ATOM   3128  C  CB    B VAL A 1 204 ? -0.201  -9.458  35.306  0.80 28.12  ? 204 VAL A CB    1 
ATOM   3129  C  CG1   A VAL A 1 204 ? -0.150  -10.907 36.064  0.20 30.76  ? 204 VAL A CG1   1 
ATOM   3130  C  CG1   B VAL A 1 204 ? 0.132   -10.789 35.951  0.80 31.57  ? 204 VAL A CG1   1 
ATOM   3131  C  CG2   A VAL A 1 204 ? -1.812  -9.075  35.632  0.20 30.90  ? 204 VAL A CG2   1 
ATOM   3132  C  CG2   B VAL A 1 204 ? -1.686  -9.077  35.543  0.80 31.30  ? 204 VAL A CG2   1 
ATOM   3133  N  N     A ASP A 1 205 ? 3.015   -8.744  36.330  0.20 24.96  ? 205 ASP A N     1 
ATOM   3134  N  N     B ASP A 1 205 ? 3.104   -8.634  36.307  0.80 25.00  ? 205 ASP A N     1 
ATOM   3135  C  CA    A ASP A 1 205 ? 4.398   -9.099  36.035  0.20 24.31  ? 205 ASP A CA    1 
ATOM   3136  C  CA    B ASP A 1 205 ? 4.534   -8.828  36.048  0.80 22.79  ? 205 ASP A CA    1 
ATOM   3137  C  C     A ASP A 1 205 ? 4.540   -10.613 35.927  0.20 25.96  ? 205 ASP A C     1 
ATOM   3138  C  C     B ASP A 1 205 ? 4.812   -10.328 36.013  0.80 25.21  ? 205 ASP A C     1 
ATOM   3139  O  O     A ASP A 1 205 ? 4.148   -11.352 36.835  0.20 23.79  ? 205 ASP A O     1 
ATOM   3140  O  O     B ASP A 1 205 ? 4.773   -10.998 37.051  0.80 25.55  ? 205 ASP A O     1 
ATOM   3141  C  CB    A ASP A 1 205 ? 5.322   -8.550  37.124  0.20 24.78  ? 205 ASP A CB    1 
ATOM   3142  C  CB    B ASP A 1 205 ? 5.344   -8.124  37.137  0.80 22.99  ? 205 ASP A CB    1 
ATOM   3143  C  CG    A ASP A 1 205 ? 6.795   -8.735  36.803  0.20 28.98  ? 205 ASP A CG    1 
ATOM   3144  C  CG    B ASP A 1 205 ? 6.857   -8.308  37.011  0.80 29.69  ? 205 ASP A CG    1 
ATOM   3145  O  OD1   A ASP A 1 205 ? 7.131   -9.111  35.658  0.20 27.01  ? 205 ASP A OD1   1 
ATOM   3146  O  OD1   B ASP A 1 205 ? 7.382   -9.016  36.110  0.80 25.78  ? 205 ASP A OD1   1 
ATOM   3147  O  OD2   A ASP A 1 205 ? 7.622   -8.501  37.709  0.20 30.98  ? 205 ASP A OD2   1 
ATOM   3148  O  OD2   B ASP A 1 205 ? 7.536   -7.708  37.865  0.80 32.02  ? 205 ASP A OD2   1 
ATOM   3149  N  N     A ASN A 1 206 ? 5.096   -11.078 34.805  0.20 25.25  ? 206 ASN A N     1 
ATOM   3150  N  N     B ASN A 1 206 ? 5.074   -10.857 34.816  0.80 24.79  ? 206 ASN A N     1 
ATOM   3151  C  CA    A ASN A 1 206 ? 5.286   -12.514 34.623  0.20 25.72  ? 206 ASN A CA    1 
ATOM   3152  C  CA    B ASN A 1 206 ? 5.315   -12.288 34.658  0.80 25.43  ? 206 ASN A CA    1 
ATOM   3153  C  C     A ASN A 1 206 ? 6.323   -13.062 35.595  0.20 26.99  ? 206 ASN A C     1 
ATOM   3154  C  C     B ASN A 1 206 ? 6.422   -12.788 35.578  0.80 26.86  ? 206 ASN A C     1 
ATOM   3155  O  O     A ASN A 1 206 ? 6.186   -14.190 36.085  0.20 26.38  ? 206 ASN A O     1 
ATOM   3156  O  O     B ASN A 1 206 ? 6.405   -13.956 35.994  0.80 26.88  ? 206 ASN A O     1 
ATOM   3157  C  CB    A ASN A 1 206 ? 5.693   -12.821 33.180  0.20 27.47  ? 206 ASN A CB    1 
ATOM   3158  C  CB    B ASN A 1 206 ? 5.661   -12.615 33.193  0.80 27.72  ? 206 ASN A CB    1 
ATOM   3159  C  CG    A ASN A 1 206 ? 4.501   -13.067 32.272  0.20 24.49  ? 206 ASN A CG    1 
ATOM   3160  C  CG    B ASN A 1 206 ? 4.457   -13.105 32.385  0.80 24.06  ? 206 ASN A CG    1 
ATOM   3161  O  OD1   A ASN A 1 206 ? 3.394   -13.343 32.738  0.20 27.78  ? 206 ASN A OD1   1 
ATOM   3162  O  OD1   B ASN A 1 206 ? 3.389   -13.387 32.935  0.80 28.25  ? 206 ASN A OD1   1 
ATOM   3163  N  ND2   A ASN A 1 206 ? 4.726   -12.980 30.964  0.20 25.73  ? 206 ASN A ND2   1 
ATOM   3164  N  ND2   B ASN A 1 206 ? 4.631   -13.206 31.065  0.80 25.73  ? 206 ASN A ND2   1 
ATOM   3165  N  N     A GLU A 1 207 ? 7.367   -12.282 35.888  0.20 24.48  ? 207 GLU A N     1 
ATOM   3166  N  N     B GLU A 1 207 ? 7.388   -11.932 35.922  0.80 22.11  ? 207 GLU A N     1 
ATOM   3167  C  CA    A GLU A 1 207 ? 8.383   -12.744 36.827  0.20 26.20  ? 207 GLU A CA    1 
ATOM   3168  C  CA    B GLU A 1 207 ? 8.420   -12.383 36.849  0.80 25.20  ? 207 GLU A CA    1 
ATOM   3169  C  C     A GLU A 1 207 ? 7.823   -12.870 38.237  0.20 25.46  ? 207 GLU A C     1 
ATOM   3170  C  C     B GLU A 1 207 ? 7.837   -12.624 38.233  0.80 24.99  ? 207 GLU A C     1 
ATOM   3171  O  O     A GLU A 1 207 ? 8.257   -13.740 38.999  0.20 24.75  ? 207 GLU A O     1 
ATOM   3172  O  O     B GLU A 1 207 ? 8.198   -13.592 38.907  0.80 23.80  ? 207 GLU A O     1 
ATOM   3173  C  CB    A GLU A 1 207 ? 9.583   -11.799 36.818  0.20 32.57  ? 207 GLU A CB    1 
ATOM   3174  C  CB    B GLU A 1 207 ? 9.556   -11.370 36.937  0.80 33.77  ? 207 GLU A CB    1 
ATOM   3175  C  CG    A GLU A 1 207 ? 10.809  -12.365 37.512  0.20 31.60  ? 207 GLU A CG    1 
ATOM   3176  C  CG    B GLU A 1 207 ? 10.735  -11.900 37.723  0.80 32.83  ? 207 GLU A CG    1 
ATOM   3177  C  CD    A GLU A 1 207 ? 11.893  -11.329 37.718  0.20 34.88  ? 207 GLU A CD    1 
ATOM   3178  C  CD    B GLU A 1 207 ? 11.928  -10.988 37.648  0.80 35.17  ? 207 GLU A CD    1 
ATOM   3179  O  OE1   A GLU A 1 207 ? 11.590  -10.119 37.640  0.20 33.50  ? 207 GLU A OE1   1 
ATOM   3180  O  OE1   B GLU A 1 207 ? 12.241  -10.526 36.530  0.80 37.67  ? 207 GLU A OE1   1 
ATOM   3181  O  OE2   A GLU A 1 207 ? 13.050  -11.730 37.959  0.20 31.08  ? 207 GLU A OE2   1 
ATOM   3182  O  OE2   B GLU A 1 207 ? 12.535  -10.725 38.705  0.80 41.86  ? 207 GLU A OE2   1 
ATOM   3183  N  N     A ALA A 1 208 ? 6.867   -12.013 38.599  0.20 25.85  ? 208 ALA A N     1 
ATOM   3184  N  N     B ALA A 1 208 ? 6.929   -11.750 38.662  0.80 25.76  ? 208 ALA A N     1 
ATOM   3185  C  CA    A ALA A 1 208 ? 6.240   -12.112 39.912  0.20 26.92  ? 208 ALA A CA    1 
ATOM   3186  C  CA    B ALA A 1 208 ? 6.317   -11.898 39.975  0.80 26.95  ? 208 ALA A CA    1 
ATOM   3187  C  C     A ALA A 1 208 ? 5.405   -13.381 40.024  0.20 26.10  ? 208 ALA A C     1 
ATOM   3188  C  C     B ALA A 1 208 ? 5.496   -13.181 40.048  0.80 25.87  ? 208 ALA A C     1 
ATOM   3189  O  O     A ALA A 1 208 ? 5.477   -14.099 41.028  0.20 27.91  ? 208 ALA A O     1 
ATOM   3190  O  O     B ALA A 1 208 ? 5.630   -13.963 40.995  0.80 27.96  ? 208 ALA A O     1 
ATOM   3191  C  CB    A ALA A 1 208 ? 5.383   -10.874 40.177  0.20 27.71  ? 208 ALA A CB    1 
ATOM   3192  C  CB    B ALA A 1 208 ? 5.457   -10.676 40.281  0.80 28.05  ? 208 ALA A CB    1 
ATOM   3193  N  N     A ILE A 1 209 ? 4.609   -13.678 38.993  0.20 24.48  ? 209 ILE A N     1 
ATOM   3194  N  N     B ILE A 1 209 ? 4.673   -13.432 39.027  0.80 23.82  ? 209 ILE A N     1 
ATOM   3195  C  CA    A ILE A 1 209 ? 3.801   -14.893 39.005  0.20 25.70  ? 209 ILE A CA    1 
ATOM   3196  C  CA    B ILE A 1 209 ? 3.817   -14.613 39.018  0.80 25.71  ? 209 ILE A CA    1 
ATOM   3197  C  C     A ILE A 1 209 ? 4.685   -16.125 38.863  0.20 26.80  ? 209 ILE A C     1 
ATOM   3198  C  C     B ILE A 1 209 ? 4.661   -15.876 38.916  0.80 26.72  ? 209 ILE A C     1 
ATOM   3199  O  O     A ILE A 1 209 ? 4.391   -17.179 39.439  0.20 27.31  ? 209 ILE A O     1 
ATOM   3200  O  O     B ILE A 1 209 ? 4.382   -16.881 39.576  0.80 26.75  ? 209 ILE A O     1 
ATOM   3201  C  CB    A ILE A 1 209 ? 2.733   -14.826 37.896  0.20 30.23  ? 209 ILE A CB    1 
ATOM   3202  C  CB    B ILE A 1 209 ? 2.801   -14.501 37.864  0.80 31.26  ? 209 ILE A CB    1 
ATOM   3203  C  CG1   A ILE A 1 209 ? 1.902   -13.546 38.029  0.20 26.19  ? 209 ILE A CG1   1 
ATOM   3204  C  CG1   B ILE A 1 209 ? 2.055   -13.158 37.932  0.80 24.97  ? 209 ILE A CG1   1 
ATOM   3205  C  CG2   A ILE A 1 209 ? 1.831   -16.053 37.936  0.20 29.26  ? 209 ILE A CG2   1 
ATOM   3206  C  CG2   B ILE A 1 209 ? 1.834   -15.697 37.851  0.80 31.36  ? 209 ILE A CG2   1 
ATOM   3207  C  CD1   A ILE A 1 209 ? 1.129   -13.446 39.327  0.20 29.47  ? 209 ILE A CD1   1 
ATOM   3208  C  CD1   B ILE A 1 209 ? 1.097   -13.021 39.101  0.80 29.39  ? 209 ILE A CD1   1 
ATOM   3209  N  N     A TYR A 1 210 ? 5.782   -16.015 38.109  0.20 24.93  ? 210 TYR A N     1 
ATOM   3210  N  N     B TYR A 1 210 ? 5.723   -15.834 38.104  0.80 24.25  ? 210 TYR A N     1 
ATOM   3211  C  CA    A TYR A 1 210 ? 6.697   -17.142 37.956  0.20 26.00  ? 210 TYR A CA    1 
ATOM   3212  C  CA    B TYR A 1 210 ? 6.663   -16.949 38.025  0.80 25.42  ? 210 TYR A CA    1 
ATOM   3213  C  C     A TYR A 1 210 ? 7.360   -17.500 39.282  0.20 28.55  ? 210 TYR A C     1 
ATOM   3214  C  C     B TYR A 1 210 ? 7.249   -17.286 39.396  0.80 28.25  ? 210 TYR A C     1 
ATOM   3215  O  O     A TYR A 1 210 ? 7.575   -18.682 39.576  0.20 28.02  ? 210 TYR A O     1 
ATOM   3216  O  O     B TYR A 1 210 ? 7.281   -18.454 39.802  0.80 27.05  ? 210 TYR A O     1 
ATOM   3217  C  CB    A TYR A 1 210 ? 7.750   -16.811 36.899  0.20 26.19  ? 210 TYR A CB    1 
ATOM   3218  C  CB    B TYR A 1 210 ? 7.767   -16.593 37.034  0.80 25.24  ? 210 TYR A CB    1 
ATOM   3219  C  CG    A TYR A 1 210 ? 8.553   -17.993 36.403  0.20 30.04  ? 210 TYR A CG    1 
ATOM   3220  C  CG    B TYR A 1 210 ? 8.687   -17.714 36.623  0.80 29.56  ? 210 TYR A CG    1 
ATOM   3221  C  CD1   A TYR A 1 210 ? 9.719   -18.387 37.046  0.20 34.74  ? 210 TYR A CD1   1 
ATOM   3222  C  CD1   B TYR A 1 210 ? 8.376   -18.515 35.539  0.80 30.62  ? 210 TYR A CD1   1 
ATOM   3223  C  CD2   A TYR A 1 210 ? 8.156   -18.698 35.275  0.20 32.17  ? 210 TYR A CD2   1 
ATOM   3224  C  CD2   B TYR A 1 210 ? 9.900   -17.925 37.272  0.80 37.00  ? 210 TYR A CD2   1 
ATOM   3225  C  CE1   A TYR A 1 210 ? 10.461  -19.459 36.585  0.20 35.57  ? 210 TYR A CE1   1 
ATOM   3226  C  CE1   B TYR A 1 210 ? 9.222   -19.514 35.126  0.80 38.59  ? 210 TYR A CE1   1 
ATOM   3227  C  CE2   A TYR A 1 210 ? 8.890   -19.771 34.808  0.20 37.37  ? 210 TYR A CE2   1 
ATOM   3228  C  CE2   B TYR A 1 210 ? 10.762  -18.933 36.863  0.80 36.03  ? 210 TYR A CE2   1 
ATOM   3229  C  CZ    A TYR A 1 210 ? 10.042  -20.148 35.466  0.20 38.06  ? 210 TYR A CZ    1 
ATOM   3230  C  CZ    B TYR A 1 210 ? 10.409  -19.726 35.790  0.80 35.54  ? 210 TYR A CZ    1 
ATOM   3231  O  OH    A TYR A 1 210 ? 10.771  -21.219 35.000  0.20 37.18  ? 210 TYR A OH    1 
ATOM   3232  O  OH    B TYR A 1 210 ? 11.233  -20.745 35.361  0.80 42.20  ? 210 TYR A OH    1 
ATOM   3233  N  N     A ASP A 1 211 ? 7.687   -16.495 40.097  0.20 25.43  ? 211 ASP A N     1 
ATOM   3234  N  N     B ASP A 1 211 ? 7.717   -16.271 40.124  0.80 24.68  ? 211 ASP A N     1 
ATOM   3235  C  CA    A ASP A 1 211 ? 8.351   -16.763 41.368  0.20 25.97  ? 211 ASP A CA    1 
ATOM   3236  C  CA    B ASP A 1 211 ? 8.358   -16.511 41.413  0.80 24.11  ? 211 ASP A CA    1 
ATOM   3237  C  C     A ASP A 1 211 ? 7.383   -17.348 42.388  0.20 30.25  ? 211 ASP A C     1 
ATOM   3238  C  C     B ASP A 1 211 ? 7.380   -17.072 42.432  0.80 30.42  ? 211 ASP A C     1 
ATOM   3239  O  O     A ASP A 1 211 ? 7.745   -18.264 43.137  0.20 29.95  ? 211 ASP A O     1 
ATOM   3240  O  O     B ASP A 1 211 ? 7.782   -17.839 43.314  0.80 27.53  ? 211 ASP A O     1 
ATOM   3241  C  CB    A ASP A 1 211 ? 8.996   -15.484 41.904  0.20 27.81  ? 211 ASP A CB    1 
ATOM   3242  C  CB    B ASP A 1 211 ? 8.992   -15.222 41.939  0.80 26.76  ? 211 ASP A CB    1 
ATOM   3243  C  CG    A ASP A 1 211 ? 10.202  -15.056 41.090  0.20 35.02  ? 211 ASP A CG    1 
ATOM   3244  C  CG    B ASP A 1 211 ? 10.311  -14.903 41.259  0.80 36.39  ? 211 ASP A CG    1 
ATOM   3245  O  OD1   A ASP A 1 211 ? 10.581  -15.795 40.157  0.20 34.19  ? 211 ASP A OD1   1 
ATOM   3246  O  OD1   B ASP A 1 211 ? 10.864  -15.798 40.587  0.80 37.82  ? 211 ASP A OD1   1 
ATOM   3247  O  OD2   A ASP A 1 211 ? 10.770  -13.982 41.381  0.20 40.02  ? 211 ASP A OD2   1 
ATOM   3248  O  OD2   B ASP A 1 211 ? 10.787  -13.757 41.392  0.80 41.79  ? 211 ASP A OD2   1 
ATOM   3249  N  N     A ILE A 1 212 ? 6.150   -16.836 42.432  0.20 28.18  ? 212 ILE A N     1 
ATOM   3250  N  N     B ILE A 1 212 ? 6.099   -16.706 42.323  0.80 27.63  ? 212 ILE A N     1 
ATOM   3251  C  CA    A ILE A 1 212 ? 5.165   -17.352 43.377  0.20 29.29  ? 212 ILE A CA    1 
ATOM   3252  C  CA    B ILE A 1 212 ? 5.095   -17.231 43.239  0.80 28.89  ? 212 ILE A CA    1 
ATOM   3253  C  C     A ILE A 1 212 ? 4.822   -18.801 43.057  0.20 31.50  ? 212 ILE A C     1 
ATOM   3254  C  C     B ILE A 1 212 ? 4.817   -18.703 42.950  0.80 31.42  ? 212 ILE A C     1 
ATOM   3255  O  O     A ILE A 1 212 ? 4.722   -19.643 43.959  0.20 32.19  ? 212 ILE A O     1 
ATOM   3256  O  O     B ILE A 1 212 ? 4.688   -19.514 43.878  0.80 32.07  ? 212 ILE A O     1 
ATOM   3257  C  CB    A ILE A 1 212 ? 3.911   -16.457 43.384  0.20 27.50  ? 212 ILE A CB    1 
ATOM   3258  C  CB    B ILE A 1 212 ? 3.827   -16.362 43.166  0.80 26.18  ? 212 ILE A CB    1 
ATOM   3259  C  CG1   A ILE A 1 212 ? 4.250   -15.069 43.933  0.20 32.14  ? 212 ILE A CG1   1 
ATOM   3260  C  CG1   B ILE A 1 212 ? 4.135   -14.978 43.744  0.80 33.14  ? 212 ILE A CG1   1 
ATOM   3261  C  CG2   A ILE A 1 212 ? 2.799   -17.093 44.207  0.20 30.53  ? 212 ILE A CG2   1 
ATOM   3262  C  CG2   B ILE A 1 212 ? 2.677   -17.005 43.926  0.80 30.32  ? 212 ILE A CG2   1 
ATOM   3263  C  CD1   A ILE A 1 212 ? 3.045   -14.155 44.074  0.20 29.31  ? 212 ILE A CD1   1 
ATOM   3264  C  CD1   B ILE A 1 212 ? 3.063   -13.934 43.491  0.80 28.67  ? 212 ILE A CD1   1 
ATOM   3265  N  N     A CYS A 1 213 ? 4.648   -19.122 41.771  0.20 28.80  ? 213 CYS A N     1 
ATOM   3266  N  N     B CYS A 1 213 ? 4.751   -19.083 41.668  0.80 28.25  ? 213 CYS A N     1 
ATOM   3267  C  CA    A CYS A 1 213 ? 4.358   -20.500 41.389  0.20 32.00  ? 213 CYS A CA    1 
ATOM   3268  C  CA    B CYS A 1 213 ? 4.592   -20.498 41.332  0.80 32.17  ? 213 CYS A CA    1 
ATOM   3269  C  C     A CYS A 1 213 ? 5.523   -21.432 41.703  0.20 32.65  ? 213 CYS A C     1 
ATOM   3270  C  C     B CYS A 1 213 ? 5.748   -21.335 41.869  0.80 32.19  ? 213 CYS A C     1 
ATOM   3271  O  O     A CYS A 1 213 ? 5.312   -22.631 41.918  0.20 32.37  ? 213 CYS A O     1 
ATOM   3272  O  O     B CYS A 1 213 ? 5.529   -22.431 42.397  0.80 33.12  ? 213 CYS A O     1 
ATOM   3273  C  CB    A CYS A 1 213 ? 4.001   -20.572 39.904  0.20 30.34  ? 213 CYS A CB    1 
ATOM   3274  C  CB    B CYS A 1 213 ? 4.468   -20.687 39.823  0.80 28.97  ? 213 CYS A CB    1 
ATOM   3275  S  SG    A CYS A 1 213 ? 2.458   -19.729 39.467  0.20 30.39  ? 213 CYS A SG    1 
ATOM   3276  S  SG    B CYS A 1 213 ? 2.923   -20.096 39.125  0.80 31.60  ? 213 CYS A SG    1 
ATOM   3277  N  N     A ARG A 1 214 ? 6.750   -20.905 41.736  0.20 31.85  ? 214 ARG A N     1 
ATOM   3278  N  N     B ARG A 1 214 ? 6.982   -20.838 41.732  0.80 31.74  ? 214 ARG A N     1 
ATOM   3279  C  CA    A ARG A 1 214 ? 7.907   -21.717 42.104  0.20 34.62  ? 214 ARG A CA    1 
ATOM   3280  C  CA    B ARG A 1 214 ? 8.153   -21.554 42.237  0.80 35.29  ? 214 ARG A CA    1 
ATOM   3281  C  C     A ARG A 1 214 ? 8.047   -21.848 43.616  0.20 36.78  ? 214 ARG A C     1 
ATOM   3282  C  C     B ARG A 1 214 ? 8.125   -21.670 43.755  0.80 37.24  ? 214 ARG A C     1 
ATOM   3283  O  O     A ARG A 1 214 ? 8.334   -22.939 44.122  0.20 35.97  ? 214 ARG A O     1 
ATOM   3284  O  O     B ARG A 1 214 ? 8.342   -22.753 44.308  0.80 36.15  ? 214 ARG A O     1 
ATOM   3285  C  CB    A ARG A 1 214 ? 9.188   -21.119 41.521  0.20 33.85  ? 214 ARG A CB    1 
ATOM   3286  C  CB    B ARG A 1 214 ? 9.441   -20.844 41.825  0.80 29.79  ? 214 ARG A CB    1 
ATOM   3287  C  CG    A ARG A 1 214 ? 9.559   -21.626 40.137  0.20 36.95  ? 214 ARG A CG    1 
ATOM   3288  C  CG    B ARG A 1 214 ? 9.722   -20.778 40.340  0.80 33.76  ? 214 ARG A CG    1 
ATOM   3289  C  CD    A ARG A 1 214 ? 11.022  -21.333 39.830  0.20 44.03  ? 214 ARG A CD    1 
ATOM   3290  C  CD    B ARG A 1 214 ? 11.144  -20.253 40.138  0.80 47.71  ? 214 ARG A CD    1 
ATOM   3291  N  NE    A ARG A 1 214 ? 11.901  -21.798 40.897  0.20 50.56  ? 214 ARG A NE    1 
ATOM   3292  N  NE    B ARG A 1 214 ? 12.058  -20.935 41.045  0.80 58.12  ? 214 ARG A NE    1 
ATOM   3293  C  CZ    A ARG A 1 214 ? 12.602  -22.923 40.860  0.20 49.37  ? 214 ARG A CZ    1 
ATOM   3294  C  CZ    B ARG A 1 214 ? 12.940  -21.857 40.683  0.80 58.48  ? 214 ARG A CZ    1 
ATOM   3295  N  NH1   A ARG A 1 214 ? 12.576  -23.720 39.804  0.20 49.20  ? 214 ARG A NH1   1 
ATOM   3296  N  NH1   B ARG A 1 214 ? 13.157  -22.145 39.409  0.80 56.78  ? 214 ARG A NH1   1 
ATOM   3297  N  NH2   A ARG A 1 214 ? 13.351  -23.256 41.907  0.20 49.77  ? 214 ARG A NH2   1 
ATOM   3298  N  NH2   B ARG A 1 214 ? 13.620  -22.506 41.623  0.80 54.66  ? 214 ARG A NH2   1 
ATOM   3299  N  N     A ARG A 1 215 ? 7.858   -20.748 44.348  0.20 33.37  ? 215 ARG A N     1 
ATOM   3300  N  N     B ARG A 1 215 ? 7.919   -20.543 44.442  0.80 32.84  ? 215 ARG A N     1 
ATOM   3301  C  CA    A ARG A 1 215 ? 8.103   -20.750 45.787  0.20 35.48  ? 215 ARG A CA    1 
ATOM   3302  C  CA    B ARG A 1 215 ? 8.020   -20.516 45.899  0.80 34.33  ? 215 ARG A CA    1 
ATOM   3303  C  C     A ARG A 1 215 ? 6.919   -21.320 46.561  0.20 39.73  ? 215 ARG A C     1 
ATOM   3304  C  C     B ARG A 1 215 ? 6.808   -21.174 46.545  0.80 39.95  ? 215 ARG A C     1 
ATOM   3305  O  O     A ARG A 1 215 ? 7.083   -22.239 47.371  0.20 45.81  ? 215 ARG A O     1 
ATOM   3306  O  O     B ARG A 1 215 ? 6.934   -22.184 47.247  0.80 47.40  ? 215 ARG A O     1 
ATOM   3307  C  CB    A ARG A 1 215 ? 8.422   -19.332 46.267  0.20 37.38  ? 215 ARG A CB    1 
ATOM   3308  C  CB    B ARG A 1 215 ? 8.168   -19.075 46.396  0.80 36.96  ? 215 ARG A CB    1 
ATOM   3309  C  CG    A ARG A 1 215 ? 9.722   -18.760 45.718  0.20 44.51  ? 215 ARG A CG    1 
ATOM   3310  C  CG    B ARG A 1 215 ? 9.550   -18.475 46.225  0.80 47.73  ? 215 ARG A CG    1 
ATOM   3311  C  CD    A ARG A 1 215 ? 10.006  -17.373 46.283  0.20 45.12  ? 215 ARG A CD    1 
ATOM   3312  C  CD    B ARG A 1 215 ? 9.656   -17.108 46.900  0.80 50.59  ? 215 ARG A CD    1 
ATOM   3313  N  NE    A ARG A 1 215 ? 9.081   -16.367 45.772  0.20 47.47  ? 215 ARG A NE    1 
ATOM   3314  N  NE    B ARG A 1 215 ? 8.870   -16.092 46.208  0.80 53.60  ? 215 ARG A NE    1 
ATOM   3315  C  CZ    A ARG A 1 215 ? 9.004   -15.120 46.218  0.20 43.03  ? 215 ARG A CZ    1 
ATOM   3316  C  CZ    B ARG A 1 215 ? 7.665   -15.681 46.583  0.80 45.53  ? 215 ARG A CZ    1 
ATOM   3317  N  NH1   A ARG A 1 215 ? 9.775   -14.690 47.204  0.20 42.75  ? 215 ARG A NH1   1 
ATOM   3318  N  NH1   B ARG A 1 215 ? 7.084   -16.147 47.676  0.80 46.98  ? 215 ARG A NH1   1 
ATOM   3319  N  NH2   A ARG A 1 215 ? 8.129   -14.286 45.664  0.20 38.22  ? 215 ARG A NH2   1 
ATOM   3320  N  NH2   B ARG A 1 215 ? 7.028   -14.780 45.840  0.80 45.14  ? 215 ARG A NH2   1 
ATOM   3321  N  N     A ASN A 1 216 ? 5.718   -20.788 46.326  0.20 38.24  ? 216 ASN A N     1 
ATOM   3322  N  N     B ASN A 1 216 ? 5.617   -20.617 46.317  0.80 38.77  ? 216 ASN A N     1 
ATOM   3323  C  CA    A ASN A 1 216 ? 4.564   -21.194 47.122  0.20 36.34  ? 216 ASN A CA    1 
ATOM   3324  C  CA    B ASN A 1 216 ? 4.445   -21.079 47.055  0.80 36.07  ? 216 ASN A CA    1 
ATOM   3325  C  C     A ASN A 1 216 ? 3.925   -22.479 46.614  0.20 37.29  ? 216 ASN A C     1 
ATOM   3326  C  C     B ASN A 1 216 ? 3.919   -22.403 46.526  0.80 37.08  ? 216 ASN A C     1 
ATOM   3327  O  O     A ASN A 1 216 ? 3.402   -23.260 47.417  0.20 43.08  ? 216 ASN A O     1 
ATOM   3328  O  O     B ASN A 1 216 ? 3.457   -23.240 47.309  0.80 43.89  ? 216 ASN A O     1 
ATOM   3329  C  CB    A ASN A 1 216 ? 3.523   -20.075 47.154  0.20 33.88  ? 216 ASN A CB    1 
ATOM   3330  C  CB    B ASN A 1 216 ? 3.340   -20.027 47.017  0.80 32.98  ? 216 ASN A CB    1 
ATOM   3331  C  CG    A ASN A 1 216 ? 4.025   -18.836 47.861  0.20 38.77  ? 216 ASN A CG    1 
ATOM   3332  C  CG    B ASN A 1 216 ? 3.717   -18.777 47.760  0.80 38.52  ? 216 ASN A CG    1 
ATOM   3333  O  OD1   A ASN A 1 216 ? 5.220   -18.545 47.849  0.20 43.73  ? 216 ASN A OD1   1 
ATOM   3334  O  OD1   B ASN A 1 216 ? 4.821   -18.263 47.597  0.80 47.30  ? 216 ASN A OD1   1 
ATOM   3335  N  ND2   A ASN A 1 216 ? 3.114   -18.101 48.490  0.20 37.21  ? 216 ASN A ND2   1 
ATOM   3336  N  ND2   B ASN A 1 216 ? 2.813   -18.285 48.601  0.80 37.50  ? 216 ASN A ND2   1 
ATOM   3337  N  N     A LEU A 1 217 ? 3.951   -22.719 45.304  0.20 33.38  ? 217 LEU A N     1 
ATOM   3338  N  N     B LEU A 1 217 ? 3.974   -22.617 45.214  0.80 32.86  ? 217 LEU A N     1 
ATOM   3339  C  CA    A LEU A 1 217 ? 3.283   -23.876 44.726  0.20 35.38  ? 217 LEU A CA    1 
ATOM   3340  C  CA    B LEU A 1 217 ? 3.381   -23.801 44.613  0.80 35.00  ? 217 LEU A CA    1 
ATOM   3341  C  C     A LEU A 1 217 ? 4.211   -25.057 44.482  0.20 36.52  ? 217 LEU A C     1 
ATOM   3342  C  C     B LEU A 1 217 ? 4.394   -24.891 44.310  0.80 35.38  ? 217 LEU A C     1 
ATOM   3343  O  O     A LEU A 1 217 ? 3.728   -26.127 44.099  0.20 40.07  ? 217 LEU A O     1 
ATOM   3344  O  O     B LEU A 1 217 ? 3.998   -25.974 43.875  0.80 41.06  ? 217 LEU A O     1 
ATOM   3345  C  CB    A LEU A 1 217 ? 2.597   -23.491 43.411  0.20 33.03  ? 217 LEU A CB    1 
ATOM   3346  C  CB    B LEU A 1 217 ? 2.624   -23.418 43.346  0.80 32.87  ? 217 LEU A CB    1 
ATOM   3347  C  CG    A LEU A 1 217 ? 1.508   -22.427 43.545  0.20 33.72  ? 217 LEU A CG    1 
ATOM   3348  C  CG    B LEU A 1 217 ? 1.562   -22.355 43.635  0.80 33.59  ? 217 LEU A CG    1 
ATOM   3349  C  CD1   A LEU A 1 217 ? 0.777   -22.238 42.226  0.20 34.56  ? 217 LEU A CD1   1 
ATOM   3350  C  CD1   B LEU A 1 217 ? 0.771   -22.024 42.383  0.80 35.15  ? 217 LEU A CD1   1 
ATOM   3351  C  CD2   A LEU A 1 217 ? 0.536   -22.797 44.664  0.20 33.34  ? 217 LEU A CD2   1 
ATOM   3352  C  CD2   B LEU A 1 217 ? 0.628   -22.811 44.784  0.80 33.24  ? 217 LEU A CD2   1 
ATOM   3353  N  N     A ASP A 1 218 ? 5.517   -24.890 44.696  0.20 37.91  ? 218 ASP A N     1 
ATOM   3354  N  N     B ASP A 1 218 ? 5.682   -24.636 44.532  0.80 36.97  ? 218 ASP A N     1 
ATOM   3355  C  CA    A ASP A 1 218 ? 6.494   -25.963 44.503  0.20 40.53  ? 218 ASP A CA    1 
ATOM   3356  C  CA    B ASP A 1 218 ? 6.724   -25.651 44.379  0.80 39.61  ? 218 ASP A CA    1 
ATOM   3357  C  C     A ASP A 1 218 ? 6.439   -26.509 43.077  0.20 39.93  ? 218 ASP A C     1 
ATOM   3358  C  C     B ASP A 1 218 ? 6.815   -26.180 42.950  0.80 41.22  ? 218 ASP A C     1 
ATOM   3359  O  O     A ASP A 1 218 ? 6.359   -27.718 42.849  0.20 39.33  ? 218 ASP A O     1 
ATOM   3360  O  O     B ASP A 1 218 ? 7.246   -27.314 42.728  0.80 37.43  ? 218 ASP A O     1 
ATOM   3361  C  CB    A ASP A 1 218 ? 6.296   -27.083 45.529  0.20 45.62  ? 218 ASP A CB    1 
ATOM   3362  C  CB    B ASP A 1 218 ? 6.516   -26.817 45.355  0.80 47.53  ? 218 ASP A CB    1 
ATOM   3363  C  CG    A ASP A 1 218 ? 6.793   -26.704 46.912  0.20 50.58  ? 218 ASP A CG    1 
ATOM   3364  C  CG    B ASP A 1 218 ? 6.687   -26.411 46.807  0.80 52.03  ? 218 ASP A CG    1 
ATOM   3365  O  OD1   A ASP A 1 218 ? 7.360   -25.600 47.063  0.20 48.98  ? 218 ASP A OD1   1 
ATOM   3366  O  OD1   B ASP A 1 218 ? 7.509   -25.506 47.086  0.80 49.39  ? 218 ASP A OD1   1 
ATOM   3367  O  OD2   A ASP A 1 218 ? 6.618   -27.516 47.847  0.20 47.69  ? 218 ASP A OD2   1 
ATOM   3368  O  OD2   B ASP A 1 218 ? 6.006   -27.014 47.670  0.80 50.95  ? 218 ASP A OD2   1 
ATOM   3369  N  N     A ILE A 1 219 ? 6.475   -25.599 42.108  0.20 39.69  ? 219 ILE A N     1 
ATOM   3370  N  N     B ILE A 1 219 ? 6.420   -25.375 41.967  0.80 39.84  ? 219 ILE A N     1 
ATOM   3371  C  CA    A ILE A 1 219 ? 6.549   -25.949 40.695  0.20 40.82  ? 219 ILE A CA    1 
ATOM   3372  C  CA    B ILE A 1 219 ? 6.506   -25.761 40.561  0.80 41.37  ? 219 ILE A CA    1 
ATOM   3373  C  C     A ILE A 1 219 ? 7.970   -25.686 40.222  0.20 39.46  ? 219 ILE A C     1 
ATOM   3374  C  C     B ILE A 1 219 ? 7.891   -25.369 40.056  0.80 38.50  ? 219 ILE A C     1 
ATOM   3375  O  O     A ILE A 1 219 ? 8.496   -24.580 40.402  0.20 38.78  ? 219 ILE A O     1 
ATOM   3376  O  O     B ILE A 1 219 ? 8.184   -24.186 39.875  0.80 37.63  ? 219 ILE A O     1 
ATOM   3377  C  CB    A ILE A 1 219 ? 5.529   -25.150 39.865  0.20 36.11  ? 219 ILE A CB    1 
ATOM   3378  C  CB    B ILE A 1 219 ? 5.394   -25.110 39.730  0.80 35.47  ? 219 ILE A CB    1 
ATOM   3379  C  CG1   A ILE A 1 219 ? 4.126   -25.302 40.451  0.20 38.16  ? 219 ILE A CG1   1 
ATOM   3380  C  CG1   B ILE A 1 219 ? 4.027   -25.564 40.230  0.80 38.53  ? 219 ILE A CG1   1 
ATOM   3381  C  CG2   A ILE A 1 219 ? 5.533   -25.618 38.422  0.20 39.71  ? 219 ILE A CG2   1 
ATOM   3382  C  CG2   B ILE A 1 219 ? 5.534   -25.476 38.254  0.80 39.84  ? 219 ILE A CG2   1 
ATOM   3383  C  CD1   A ILE A 1 219 ? 3.080   -24.487 39.730  0.20 35.82  ? 219 ILE A CD1   1 
ATOM   3384  C  CD1   B ILE A 1 219 ? 2.883   -24.938 39.489  0.80 37.08  ? 219 ILE A CD1   1 
ATOM   3385  N  N     A GLU A 1 220 ? 8.599   -26.703 39.631  0.20 45.76  ? 220 GLU A N     1 
ATOM   3386  N  N     B GLU A 1 220 ? 8.753   -26.364 39.840  0.80 48.13  ? 220 GLU A N     1 
ATOM   3387  C  CA    A GLU A 1 220 ? 9.999   -26.584 39.232  0.20 45.41  ? 220 GLU A CA    1 
ATOM   3388  C  CA    B GLU A 1 220 ? 10.159  -26.080 39.551  0.80 46.31  ? 220 GLU A CA    1 
ATOM   3389  C  C     A GLU A 1 220 ? 10.177  -25.512 38.162  0.20 44.21  ? 220 GLU A C     1 
ATOM   3390  C  C     B GLU A 1 220 ? 10.321  -25.268 38.267  0.80 44.36  ? 220 GLU A C     1 
ATOM   3391  O  O     A GLU A 1 220 ? 10.874  -24.512 38.370  0.20 43.31  ? 220 GLU A O     1 
ATOM   3392  O  O     B GLU A 1 220 ? 11.151  -24.353 38.204  0.80 42.19  ? 220 GLU A O     1 
ATOM   3393  C  CB    A GLU A 1 220 ? 10.518  -27.937 38.741  0.20 46.61  ? 220 GLU A CB    1 
ATOM   3394  C  CB    B GLU A 1 220 ? 10.949  -27.389 39.473  0.80 46.57  ? 220 GLU A CB    1 
ATOM   3395  N  N     A ARG A 1 221 ? 9.547   -25.705 37.005  0.20 41.70  ? 221 ARG A N     1 
ATOM   3396  N  N     B ARG A 1 221 ? 9.528   -25.573 37.240  0.80 41.39  ? 221 ARG A N     1 
ATOM   3397  C  CA    A ARG A 1 221 ? 9.619   -24.761 35.893  0.20 42.05  ? 221 ARG A CA    1 
ATOM   3398  C  CA    B ARG A 1 221 ? 9.572   -24.874 35.958  0.80 41.70  ? 221 ARG A CA    1 
ATOM   3399  C  C     A ARG A 1 221 ? 8.201   -24.557 35.375  0.20 42.91  ? 221 ARG A C     1 
ATOM   3400  C  C     B ARG A 1 221 ? 8.155   -24.510 35.526  0.80 43.57  ? 221 ARG A C     1 
ATOM   3401  O  O     A ARG A 1 221 ? 7.735   -25.300 34.500  0.20 39.98  ? 221 ARG A O     1 
ATOM   3402  O  O     B ARG A 1 221 ? 7.521   -25.240 34.749  0.80 39.02  ? 221 ARG A O     1 
ATOM   3403  C  CB    A ARG A 1 221 ? 10.560  -25.273 34.804  0.20 49.26  ? 221 ARG A CB    1 
ATOM   3404  C  CB    B ARG A 1 221 ? 10.279  -25.737 34.912  0.80 53.65  ? 221 ARG A CB    1 
ATOM   3405  C  CG    A ARG A 1 221 ? 10.892  -24.270 33.716  0.20 45.42  ? 221 ARG A CG    1 
ATOM   3406  C  CG    B ARG A 1 221 ? 9.890   -27.208 34.995  0.80 56.29  ? 221 ARG A CG    1 
ATOM   3407  C  CD    A ARG A 1 221 ? 11.863  -24.877 32.718  0.20 52.72  ? 221 ARG A CD    1 
ATOM   3408  C  CD    B ARG A 1 221 ? 10.688  -28.080 34.041  0.80 78.80  ? 221 ARG A CD    1 
ATOM   3409  N  NE    A ARG A 1 221 ? 11.975  -24.075 31.507  0.20 54.98  ? 221 ARG A NE    1 
ATOM   3410  N  NE    B ARG A 1 221 ? 9.950   -29.290 33.693  0.80 87.61  ? 221 ARG A NE    1 
ATOM   3411  C  CZ    A ARG A 1 221 ? 11.261  -24.277 30.408  0.20 54.36  ? 221 ARG A CZ    1 
ATOM   3412  C  CZ    B ARG A 1 221 ? 9.868   -30.368 34.461  0.80 96.63  ? 221 ARG A CZ    1 
ATOM   3413  N  NH1   A ARG A 1 221 ? 10.377  -25.258 30.329  0.20 55.72  ? 221 ARG A NH1   1 
ATOM   3414  N  NH1   B ARG A 1 221 ? 10.477  -30.428 35.635  0.80 95.76  ? 221 ARG A NH1   1 
ATOM   3415  N  NH2   A ARG A 1 221 ? 11.438  -23.474 29.363  0.20 51.94  ? 221 ARG A NH2   1 
ATOM   3416  N  NH2   B ARG A 1 221 ? 9.155   -31.410 34.043  0.80 96.14  ? 221 ARG A NH2   1 
ATOM   3417  N  N     A PRO A 1 222 ? 7.481   -23.566 35.902  0.20 40.07  ? 222 PRO A N     1 
ATOM   3418  N  N     B PRO A 1 222 ? 7.620   -23.385 36.017  0.80 39.92  ? 222 PRO A N     1 
ATOM   3419  C  CA    A PRO A 1 222 ? 6.066   -23.409 35.545  0.20 35.97  ? 222 PRO A CA    1 
ATOM   3420  C  CA    B PRO A 1 222 ? 6.243   -23.009 35.665  0.80 34.95  ? 222 PRO A CA    1 
ATOM   3421  C  C     A PRO A 1 222 ? 5.881   -23.036 34.083  0.20 36.38  ? 222 PRO A C     1 
ATOM   3422  C  C     B PRO A 1 222 ? 6.089   -22.785 34.167  0.80 36.71  ? 222 PRO A C     1 
ATOM   3423  O  O     A PRO A 1 222 ? 6.751   -22.431 33.452  0.20 38.52  ? 222 PRO A O     1 
ATOM   3424  O  O     B PRO A 1 222 ? 6.999   -22.294 33.497  0.80 39.56  ? 222 PRO A O     1 
ATOM   3425  C  CB    A PRO A 1 222 ? 5.587   -22.279 36.465  0.20 35.59  ? 222 PRO A CB    1 
ATOM   3426  C  CB    B PRO A 1 222 ? 6.015   -21.708 36.445  0.80 37.87  ? 222 PRO A CB    1 
ATOM   3427  C  CG    A PRO A 1 222 ? 6.619   -22.185 37.550  0.20 36.46  ? 222 PRO A CG    1 
ATOM   3428  C  CG    B PRO A 1 222 ? 7.047   -21.704 37.515  0.80 37.11  ? 222 PRO A CG    1 
ATOM   3429  C  CD    A PRO A 1 222 ? 7.911   -22.587 36.912  0.20 37.66  ? 222 PRO A CD    1 
ATOM   3430  C  CD    B PRO A 1 222 ? 8.235   -22.425 36.947  0.80 37.01  ? 222 PRO A CD    1 
ATOM   3431  N  N     A THR A 1 223 ? 4.724   -23.413 33.547  0.20 34.27  ? 223 THR A N     1 
ATOM   3432  N  N     B THR A 1 223 ? 4.932   -23.177 33.643  0.80 34.21  ? 223 THR A N     1 
ATOM   3433  C  CA    A THR A 1 223 ? 4.331   -23.094 32.182  0.20 31.82  ? 223 THR A CA    1 
ATOM   3434  C  CA    B THR A 1 223 ? 4.547   -22.902 32.266  0.80 30.73  ? 223 THR A CA    1 
ATOM   3435  C  C     A THR A 1 223 ? 3.249   -22.019 32.196  0.20 33.91  ? 223 THR A C     1 
ATOM   3436  C  C     B THR A 1 223 ? 3.436   -21.863 32.237  0.80 34.80  ? 223 THR A C     1 
ATOM   3437  O  O     A THR A 1 223 ? 2.855   -21.509 33.248  0.20 31.31  ? 223 THR A O     1 
ATOM   3438  O  O     B THR A 1 223 ? 2.881   -21.481 33.268  0.80 31.40  ? 223 THR A O     1 
ATOM   3439  C  CB    A THR A 1 223 ? 3.838   -24.344 31.451  0.20 32.80  ? 223 THR A CB    1 
ATOM   3440  C  CB    B THR A 1 223 ? 4.053   -24.163 31.557  0.80 31.23  ? 223 THR A CB    1 
ATOM   3441  O  OG1   A THR A 1 223 ? 2.647   -24.829 32.084  0.20 36.80  ? 223 THR A OG1   1 
ATOM   3442  O  OG1   B THR A 1 223 ? 2.798   -24.561 32.127  0.80 38.18  ? 223 THR A OG1   1 
ATOM   3443  C  CG2   A THR A 1 223 ? 4.904   -25.431 31.473  0.20 41.09  ? 223 THR A CG2   1 
ATOM   3444  C  CG2   B THR A 1 223 ? 5.073   -25.293 31.690  0.80 43.00  ? 223 THR A CG2   1 
ATOM   3445  N  N     A TYR A 1 224 ? 2.760   -21.683 31.001  0.20 33.18  ? 224 TYR A N     1 
ATOM   3446  N  N     B TYR A 1 224 ? 3.108   -21.430 31.020  0.80 31.26  ? 224 TYR A N     1 
ATOM   3447  C  CA    A TYR A 1 224 ? 1.711   -20.677 30.886  0.20 31.94  ? 224 TYR A CA    1 
ATOM   3448  C  CA    B TYR A 1 224 ? 1.952   -20.568 30.803  0.80 32.42  ? 224 TYR A CA    1 
ATOM   3449  C  C     A TYR A 1 224 ? 0.398   -21.155 31.492  0.20 33.59  ? 224 TYR A C     1 
ATOM   3450  C  C     B TYR A 1 224 ? 0.709   -21.084 31.521  0.80 34.58  ? 224 TYR A C     1 
ATOM   3451  O  O     A TYR A 1 224 ? -0.413  -20.334 31.935  0.20 28.88  ? 224 TYR A O     1 
ATOM   3452  O  O     B TYR A 1 224 ? -0.057  -20.300 32.095  0.80 29.12  ? 224 TYR A O     1 
ATOM   3453  C  CB    A TYR A 1 224 ? 1.522   -20.290 29.419  0.20 32.23  ? 224 TYR A CB    1 
ATOM   3454  C  CB    B TYR A 1 224 ? 1.688   -20.447 29.302  0.80 31.89  ? 224 TYR A CB    1 
ATOM   3455  C  CG    A TYR A 1 224 ? 2.648   -19.436 28.889  0.20 31.54  ? 224 TYR A CG    1 
ATOM   3456  C  CG    B TYR A 1 224 ? 2.677   -19.572 28.587  0.80 32.67  ? 224 TYR A CG    1 
ATOM   3457  C  CD1   A TYR A 1 224 ? 3.253   -18.484 29.697  0.20 29.28  ? 224 TYR A CD1   1 
ATOM   3458  C  CD1   B TYR A 1 224 ? 3.147   -18.409 29.173  0.80 30.42  ? 224 TYR A CD1   1 
ATOM   3459  C  CD2   A TYR A 1 224 ? 3.119   -19.590 27.591  0.20 33.15  ? 224 TYR A CD2   1 
ATOM   3460  C  CD2   B TYR A 1 224 ? 3.162   -19.922 27.330  0.80 32.62  ? 224 TYR A CD2   1 
ATOM   3461  C  CE1   A TYR A 1 224 ? 4.283   -17.701 29.230  0.20 32.54  ? 224 TYR A CE1   1 
ATOM   3462  C  CE1   B TYR A 1 224 ? 4.049   -17.604 28.519  0.80 32.52  ? 224 TYR A CE1   1 
ATOM   3463  C  CE2   A TYR A 1 224 ? 4.154   -18.809 27.112  0.20 34.30  ? 224 TYR A CE2   1 
ATOM   3464  C  CE2   B TYR A 1 224 ? 4.064   -19.124 26.672  0.80 34.58  ? 224 TYR A CE2   1 
ATOM   3465  C  CZ    A TYR A 1 224 ? 4.733   -17.866 27.938  0.20 34.81  ? 224 TYR A CZ    1 
ATOM   3466  C  CZ    B TYR A 1 224 ? 4.511   -17.970 27.271  0.80 37.90  ? 224 TYR A CZ    1 
ATOM   3467  O  OH    A TYR A 1 224 ? 5.766   -17.080 27.481  0.20 34.51  ? 224 TYR A OH    1 
ATOM   3468  O  OH    B TYR A 1 224 ? 5.420   -17.169 26.618  0.80 39.53  ? 224 TYR A OH    1 
ATOM   3469  N  N     A THR A 1 225 ? 0.169   -22.470 31.524  0.20 35.07  ? 225 THR A N     1 
ATOM   3470  N  N     B THR A 1 225 ? 0.483   -22.402 31.494  0.80 36.78  ? 225 THR A N     1 
ATOM   3471  C  CA    A THR A 1 225 ? -1.023  -22.986 32.187  0.20 31.64  ? 225 THR A CA    1 
ATOM   3472  C  CA    B THR A 1 225 ? -0.723  -22.948 32.114  0.80 31.59  ? 225 THR A CA    1 
ATOM   3473  C  C     A THR A 1 225 ? -0.979  -22.709 33.685  0.20 30.33  ? 225 THR A C     1 
ATOM   3474  C  C     B THR A 1 225 ? -0.749  -22.678 33.614  0.80 29.14  ? 225 THR A C     1 
ATOM   3475  O  O     A THR A 1 225 ? -2.000  -22.356 34.286  0.20 31.67  ? 225 THR A O     1 
ATOM   3476  O  O     B THR A 1 225 ? -1.800  -22.336 34.174  0.80 32.14  ? 225 THR A O     1 
ATOM   3477  C  CB    A THR A 1 225 ? -1.169  -24.485 31.921  0.20 35.05  ? 225 THR A CB    1 
ATOM   3478  C  CB    B THR A 1 225 ? -0.828  -24.451 31.847  0.80 34.60  ? 225 THR A CB    1 
ATOM   3479  O  OG1   A THR A 1 225 ? -1.231  -24.719 30.508  0.20 38.38  ? 225 THR A OG1   1 
ATOM   3480  O  OG1   B THR A 1 225 ? -0.881  -24.691 30.434  0.80 40.39  ? 225 THR A OG1   1 
ATOM   3481  C  CG2   A THR A 1 225 ? -2.435  -25.018 32.568  0.20 37.10  ? 225 THR A CG2   1 
ATOM   3482  C  CG2   B THR A 1 225 ? -2.086  -25.005 32.489  0.80 37.20  ? 225 THR A CG2   1 
ATOM   3483  N  N     A ASN A 1 226 ? 0.197   -22.850 34.302  0.20 32.14  ? 226 ASN A N     1 
ATOM   3484  N  N     B ASN A 1 226 ? 0.396   -22.824 34.288  0.80 32.50  ? 226 ASN A N     1 
ATOM   3485  C  CA    A ASN A 1 226 ? 0.318   -22.561 35.728  0.20 30.64  ? 226 ASN A CA    1 
ATOM   3486  C  CA    B ASN A 1 226 ? 0.442   -22.550 35.723  0.80 30.63  ? 226 ASN A CA    1 
ATOM   3487  C  C     A ASN A 1 226 ? 0.222   -21.065 36.000  0.20 29.43  ? 226 ASN A C     1 
ATOM   3488  C  C     B ASN A 1 226 ? 0.263   -21.064 36.001  0.80 29.44  ? 226 ASN A C     1 
ATOM   3489  O  O     A ASN A 1 226 ? -0.393  -20.645 36.988  0.20 30.98  ? 226 ASN A O     1 
ATOM   3490  O  O     B ASN A 1 226 ? -0.509  -20.671 36.890  0.80 31.22  ? 226 ASN A O     1 
ATOM   3491  C  CB    A ASN A 1 226 ? 1.634   -23.116 36.269  0.20 27.73  ? 226 ASN A CB    1 
ATOM   3492  C  CB    B ASN A 1 226 ? 1.762   -23.034 36.325  0.80 27.04  ? 226 ASN A CB    1 
ATOM   3493  C  CG    A ASN A 1 226 ? 1.796   -24.594 35.999  0.20 32.94  ? 226 ASN A CG    1 
ATOM   3494  C  CG    B ASN A 1 226 ? 2.058   -24.471 36.001  0.80 34.17  ? 226 ASN A CG    1 
ATOM   3495  O  OD1   A ASN A 1 226 ? 2.665   -25.003 35.230  0.20 33.46  ? 226 ASN A OD1   1 
ATOM   3496  O  OD1   B ASN A 1 226 ? 3.121   -24.790 35.459  0.80 31.38  ? 226 ASN A OD1   1 
ATOM   3497  N  ND2   A ASN A 1 226 ? 0.962   -25.406 36.633  0.20 31.77  ? 226 ASN A ND2   1 
ATOM   3498  N  ND2   B ASN A 1 226 ? 1.133   -25.352 36.336  0.80 31.28  ? 226 ASN A ND2   1 
ATOM   3499  N  N     A LEU A 1 227 ? 0.826   -20.247 35.134  0.20 28.58  ? 227 LEU A N     1 
ATOM   3500  N  N     B LEU A 1 227 ? 0.976   -20.222 35.246  0.80 28.45  ? 227 LEU A N     1 
ATOM   3501  C  CA    A LEU A 1 227 ? 0.763   -18.801 35.313  0.20 24.21  ? 227 LEU A CA    1 
ATOM   3502  C  CA    B LEU A 1 227 ? 0.876   -18.781 35.441  0.80 23.49  ? 227 LEU A CA    1 
ATOM   3503  C  C     A LEU A 1 227 ? -0.664  -18.290 35.159  0.20 26.17  ? 227 LEU A C     1 
ATOM   3504  C  C     B LEU A 1 227 ? -0.556  -18.301 35.277  0.80 26.09  ? 227 LEU A C     1 
ATOM   3505  O  O     A LEU A 1 227 ? -1.153  -17.526 36.000  0.20 24.76  ? 227 LEU A O     1 
ATOM   3506  O  O     B LEU A 1 227 ? -1.038  -17.489 36.072  0.80 24.76  ? 227 LEU A O     1 
ATOM   3507  C  CB    A LEU A 1 227 ? 1.689   -18.102 34.314  0.20 25.54  ? 227 LEU A CB    1 
ATOM   3508  C  CB    B LEU A 1 227 ? 1.786   -18.037 34.459  0.80 25.00  ? 227 LEU A CB    1 
ATOM   3509  C  CG    A LEU A 1 227 ? 3.180   -18.451 34.336  0.20 27.19  ? 227 LEU A CG    1 
ATOM   3510  C  CG    B LEU A 1 227 ? 3.255   -18.438 34.315  0.80 27.16  ? 227 LEU A CG    1 
ATOM   3511  C  CD1   A LEU A 1 227 ? 3.920   -17.656 33.266  0.20 27.79  ? 227 LEU A CD1   1 
ATOM   3512  C  CD1   B LEU A 1 227 ? 3.908   -17.560 33.240  0.80 27.75  ? 227 LEU A CD1   1 
ATOM   3513  C  CD2   A LEU A 1 227 ? 3.787   -18.195 35.699  0.20 25.45  ? 227 LEU A CD2   1 
ATOM   3514  C  CD2   B LEU A 1 227 ? 4.016   -18.317 35.602  0.80 24.38  ? 227 LEU A CD2   1 
ATOM   3515  N  N     A ASN A 1 228 ? -1.350  -18.708 34.092  0.20 25.99  ? 228 ASN A N     1 
ATOM   3516  N  N     B ASN A 1 228 ? -1.256  -18.809 34.257  0.80 25.09  ? 228 ASN A N     1 
ATOM   3517  C  CA    A ASN A 1 228 ? -2.688  -18.193 33.814  0.20 26.83  ? 228 ASN A CA    1 
ATOM   3518  C  CA    B ASN A 1 228 ? -2.566  -18.272 33.896  0.80 27.04  ? 228 ASN A CA    1 
ATOM   3519  C  C     A ASN A 1 228 ? -3.692  -18.613 34.877  0.20 26.63  ? 228 ASN A C     1 
ATOM   3520  C  C     B ASN A 1 228 ? -3.644  -18.695 34.872  0.80 26.56  ? 228 ASN A C     1 
ATOM   3521  O  O     A ASN A 1 228 ? -4.676  -17.903 35.106  0.20 28.64  ? 228 ASN A O     1 
ATOM   3522  O  O     B ASN A 1 228 ? -4.605  -17.951 35.084  0.80 28.80  ? 228 ASN A O     1 
ATOM   3523  C  CB    A ASN A 1 228 ? -3.158  -18.656 32.434  0.20 25.85  ? 228 ASN A CB    1 
ATOM   3524  C  CB    B ASN A 1 228 ? -2.941  -18.700 32.477  0.80 25.97  ? 228 ASN A CB    1 
ATOM   3525  C  CG    A ASN A 1 228 ? -2.310  -18.092 31.312  0.20 27.97  ? 228 ASN A CG    1 
ATOM   3526  C  CG    B ASN A 1 228 ? -2.047  -18.058 31.438  0.80 28.31  ? 228 ASN A CG    1 
ATOM   3527  O  OD1   A ASN A 1 228 ? -1.736  -17.011 31.437  0.20 24.80  ? 228 ASN A OD1   1 
ATOM   3528  O  OD1   B ASN A 1 228 ? -1.307  -17.132 31.750  0.80 24.08  ? 228 ASN A OD1   1 
ATOM   3529  N  ND2   A ASN A 1 228 ? -2.223  -18.825 30.209  0.20 25.48  ? 228 ASN A ND2   1 
ATOM   3530  N  ND2   B ASN A 1 228 ? -2.121  -18.533 30.202  0.80 24.62  ? 228 ASN A ND2   1 
ATOM   3531  N  N     A ARG A 1 229 ? -3.467  -19.751 35.533  0.20 25.53  ? 229 ARG A N     1 
ATOM   3532  N  N     B ARG A 1 229 ? -3.517  -19.873 35.467  0.80 25.02  ? 229 ARG A N     1 
ATOM   3533  C  CA    A ARG A 1 229 ? -4.385  -20.180 36.583  0.20 27.02  ? 229 ARG A CA    1 
ATOM   3534  C  CA    B ARG A 1 229 ? -4.490  -20.241 36.489  0.80 26.71  ? 229 ARG A CA    1 
ATOM   3535  C  C     A ARG A 1 229 ? -4.309  -19.252 37.789  0.20 28.24  ? 229 ARG A C     1 
ATOM   3536  C  C     B ARG A 1 229 ? -4.322  -19.380 37.727  0.80 27.99  ? 229 ARG A C     1 
ATOM   3537  O  O     A ARG A 1 229 ? -5.340  -18.827 38.322  0.20 27.71  ? 229 ARG A O     1 
ATOM   3538  O  O     B ARG A 1 229 ? -5.312  -18.994 38.357  0.80 27.58  ? 229 ARG A O     1 
ATOM   3539  C  CB    A ARG A 1 229 ? -4.090  -21.625 36.985  0.20 30.45  ? 229 ARG A CB    1 
ATOM   3540  C  CB    B ARG A 1 229 ? -4.377  -21.729 36.816  0.80 30.85  ? 229 ARG A CB    1 
ATOM   3541  C  CG    A ARG A 1 229 ? -4.610  -22.654 35.993  0.20 35.70  ? 229 ARG A CG    1 
ATOM   3542  C  CG    B ARG A 1 229 ? -5.538  -22.537 36.237  0.80 40.67  ? 229 ARG A CG    1 
ATOM   3543  C  CD    A ARG A 1 229 ? -4.748  -24.019 36.645  0.20 40.66  ? 229 ARG A CD    1 
ATOM   3544  C  CD    B ARG A 1 229 ? -5.173  -23.995 35.971  0.80 46.00  ? 229 ARG A CD    1 
ATOM   3545  N  NE    A ARG A 1 229 ? -3.468  -24.693 36.816  0.20 35.09  ? 229 ARG A NE    1 
ATOM   3546  N  NE    B ARG A 1 229 ? -5.093  -24.269 34.540  0.80 65.11  ? 229 ARG A NE    1 
ATOM   3547  C  CZ    A ARG A 1 229 ? -3.105  -25.779 36.149  0.20 28.82  ? 229 ARG A CZ    1 
ATOM   3548  C  CZ    B ARG A 1 229 ? -6.139  -24.516 33.762  0.80 63.31  ? 229 ARG A CZ    1 
ATOM   3549  N  NH1   A ARG A 1 229 ? -3.902  -26.339 35.253  0.20 35.95  ? 229 ARG A NH1   1 
ATOM   3550  N  NH1   B ARG A 1 229 ? -7.369  -24.558 34.249  0.80 50.22  ? 229 ARG A NH1   1 
ATOM   3551  N  NH2   A ARG A 1 229 ? -1.918  -26.324 36.393  0.20 29.02  ? 229 ARG A NH2   1 
ATOM   3552  N  NH2   B ARG A 1 229 ? -5.946  -24.718 32.461  0.80 50.84  ? 229 ARG A NH2   1 
ATOM   3553  N  N     A LEU A 1 230 ? -3.093  -18.922 38.229  0.20 28.36  ? 230 LEU A N     1 
ATOM   3554  N  N     B LEU A 1 230 ? -3.080  -19.042 38.074  0.80 28.23  ? 230 LEU A N     1 
ATOM   3555  C  CA    A LEU A 1 230 ? -2.940  -17.991 39.343  0.20 30.30  ? 230 LEU A CA    1 
ATOM   3556  C  CA    B LEU A 1 230 ? -2.847  -18.109 39.173  0.80 31.31  ? 230 LEU A CA    1 
ATOM   3557  C  C     A LEU A 1 230 ? -3.408  -16.591 38.964  0.20 27.80  ? 230 LEU A C     1 
ATOM   3558  C  C     B LEU A 1 230 ? -3.367  -16.711 38.843  0.80 27.91  ? 230 LEU A C     1 
ATOM   3559  O  O     A LEU A 1 230 ? -4.029  -15.897 39.779  0.20 27.25  ? 230 LEU A O     1 
ATOM   3560  O  O     B LEU A 1 230 ? -4.078  -16.098 39.649  0.80 27.22  ? 230 LEU A O     1 
ATOM   3561  C  CB    A LEU A 1 230 ? -1.483  -17.965 39.807  0.20 27.40  ? 230 LEU A CB    1 
ATOM   3562  C  CB    B LEU A 1 230 ? -1.357  -18.065 39.511  0.80 25.25  ? 230 LEU A CB    1 
ATOM   3563  C  CG    A LEU A 1 230 ? -1.152  -16.997 40.945  0.20 27.64  ? 230 LEU A CG    1 
ATOM   3564  C  CG    B LEU A 1 230 ? -1.022  -17.272 40.773  0.80 26.67  ? 230 LEU A CG    1 
ATOM   3565  C  CD1   A LEU A 1 230 ? -1.939  -17.345 42.202  0.20 30.56  ? 230 LEU A CD1   1 
ATOM   3566  C  CD1   B LEU A 1 230 ? -1.912  -17.730 41.918  0.80 32.13  ? 230 LEU A CD1   1 
ATOM   3567  C  CD2   A LEU A 1 230 ? 0.341   -16.997 41.228  0.20 31.23  ? 230 LEU A CD2   1 
ATOM   3568  C  CD2   B LEU A 1 230 ? 0.435   -17.453 41.134  0.80 32.95  ? 230 LEU A CD2   1 
ATOM   3569  N  N     A ILE A 1 231 ? -3.118  -16.157 37.734  0.20 27.75  ? 231 ILE A N     1 
ATOM   3570  N  N     B ILE A 1 231 ? -3.006  -16.181 37.667  0.80 27.46  ? 231 ILE A N     1 
ATOM   3571  C  CA    A ILE A 1 231 ? -3.559  -14.840 37.282  0.20 28.77  ? 231 ILE A CA    1 
ATOM   3572  C  CA    B ILE A 1 231 ? -3.487  -14.863 37.251  0.80 29.01  ? 231 ILE A CA    1 
ATOM   3573  C  C     A ILE A 1 231 ? -5.080  -14.770 37.234  0.20 25.13  ? 231 ILE A C     1 
ATOM   3574  C  C     B ILE A 1 231 ? -5.012  -14.820 37.225  0.80 24.91  ? 231 ILE A C     1 
ATOM   3575  O  O     A ILE A 1 231 ? -5.682  -13.769 37.640  0.20 25.93  ? 231 ILE A O     1 
ATOM   3576  O  O     B ILE A 1 231 ? -5.618  -13.795 37.554  0.80 25.63  ? 231 ILE A O     1 
ATOM   3577  C  CB    A ILE A 1 231 ? -2.933  -14.506 35.913  0.20 24.49  ? 231 ILE A CB    1 
ATOM   3578  C  CB    B ILE A 1 231 ? -2.888  -14.474 35.882  0.80 24.26  ? 231 ILE A CB    1 
ATOM   3579  C  CG1   A ILE A 1 231 ? -1.415  -14.359 36.038  0.20 26.79  ? 231 ILE A CG1   1 
ATOM   3580  C  CG1   B ILE A 1 231 ? -1.405  -14.113 36.014  0.80 26.34  ? 231 ILE A CG1   1 
ATOM   3581  C  CG2   A ILE A 1 231 ? -3.546  -13.232 35.341  0.20 29.20  ? 231 ILE A CG2   1 
ATOM   3582  C  CG2   B ILE A 1 231 ? -3.651  -13.285 35.280  0.80 29.49  ? 231 ILE A CG2   1 
ATOM   3583  C  CD1   A ILE A 1 231 ? -0.693  -14.280 34.705  0.20 28.50  ? 231 ILE A CD1   1 
ATOM   3584  C  CD1   B ILE A 1 231 ? -0.626  -14.164 34.688  0.80 28.94  ? 231 ILE A CD1   1 
ATOM   3585  N  N     A SER A 1 232 ? -5.726  -15.831 36.741  0.20 24.72  ? 232 SER A N     1 
ATOM   3586  N  N     B SER A 1 232 ? -5.661  -15.921 36.830  0.80 24.37  ? 232 SER A N     1 
ATOM   3587  C  CA    A SER A 1 232 ? -7.182  -15.831 36.644  0.20 26.51  ? 232 SER A CA    1 
ATOM   3588  C  CA    B SER A 1 232 ? -7.119  -15.906 36.731  0.80 25.82  ? 232 SER A CA    1 
ATOM   3589  C  C     A SER A 1 232 ? -7.841  -15.795 38.016  0.20 28.21  ? 232 SER A C     1 
ATOM   3590  C  C     B SER A 1 232 ? -7.777  -15.805 38.100  0.80 28.17  ? 232 SER A C     1 
ATOM   3591  O  O     A SER A 1 232 ? -8.913  -15.199 38.171  0.20 24.41  ? 232 SER A O     1 
ATOM   3592  O  O     B SER A 1 232 ? -8.847  -15.197 38.227  0.80 24.15  ? 232 SER A O     1 
ATOM   3593  C  CB    A SER A 1 232 ? -7.656  -17.055 35.864  0.20 29.15  ? 232 SER A CB    1 
ATOM   3594  C  CB    B SER A 1 232 ? -7.622  -17.157 36.018  0.80 29.49  ? 232 SER A CB    1 
ATOM   3595  O  OG    A SER A 1 232 ? -7.088  -18.239 36.396  0.20 28.60  ? 232 SER A OG    1 
ATOM   3596  O  OG    B SER A 1 232 ? -7.822  -18.213 36.942  0.80 35.02  ? 232 SER A OG    1 
ATOM   3597  N  N     A GLN A 1 233 ? -7.223  -16.430 39.015  0.20 28.95  ? 233 GLN A N     1 
ATOM   3598  N  N     B GLN A 1 233 ? -7.165  -16.421 39.115  0.80 28.88  ? 233 GLN A N     1 
ATOM   3599  C  CA    A GLN A 1 233 ? -7.741  -16.351 40.376  0.20 30.87  ? 233 GLN A CA    1 
ATOM   3600  C  CA    B GLN A 1 233 ? -7.634  -16.283 40.492  0.80 31.11  ? 233 GLN A CA    1 
ATOM   3601  C  C     A GLN A 1 233 ? -7.613  -14.942 40.940  0.20 30.84  ? 233 GLN A C     1 
ATOM   3602  C  C     B GLN A 1 233 ? -7.618  -14.825 40.938  0.80 30.93  ? 233 GLN A C     1 
ATOM   3603  O  O     A GLN A 1 233 ? -8.478  -14.500 41.705  0.20 28.84  ? 233 GLN A O     1 
ATOM   3604  O  O     B GLN A 1 233 ? -8.544  -14.363 41.619  0.80 28.43  ? 233 GLN A O     1 
ATOM   3605  C  CB    A GLN A 1 233 ? -7.012  -17.358 41.268  0.20 31.90  ? 233 GLN A CB    1 
ATOM   3606  C  CB    B GLN A 1 233 ? -6.753  -17.142 41.406  0.80 32.50  ? 233 GLN A CB    1 
ATOM   3607  C  CG    A GLN A 1 233 ? -7.531  -17.425 42.692  0.20 38.19  ? 233 GLN A CG    1 
ATOM   3608  C  CG    B GLN A 1 233 ? -7.412  -17.615 42.679  0.80 39.76  ? 233 GLN A CG    1 
ATOM   3609  C  CD    A GLN A 1 233 ? -8.983  -17.854 42.761  0.20 32.57  ? 233 GLN A CD    1 
ATOM   3610  C  CD    B GLN A 1 233 ? -8.722  -18.316 42.408  0.80 34.16  ? 233 GLN A CD    1 
ATOM   3611  O  OE1   A GLN A 1 233 ? -9.759  -17.321 43.552  0.20 37.48  ? 233 GLN A OE1   1 
ATOM   3612  O  OE1   B GLN A 1 233 ? -9.776  -17.818 42.776  0.80 38.81  ? 233 GLN A OE1   1 
ATOM   3613  N  NE2   A GLN A 1 233 ? -9.358  -18.822 41.928  0.20 33.88  ? 233 GLN A NE2   1 
ATOM   3614  N  NE2   B GLN A 1 233 ? -8.662  -19.472 41.742  0.80 35.69  ? 233 GLN A NE2   1 
ATOM   3615  N  N     A ILE A 1 234 ? -6.550  -14.223 40.573  0.20 26.52  ? 234 ILE A N     1 
ATOM   3616  N  N     B ILE A 1 234 ? -6.574  -14.085 40.558  0.80 26.10  ? 234 ILE A N     1 
ATOM   3617  C  CA    A ILE A 1 234 ? -6.382  -12.851 41.043  0.20 24.82  ? 234 ILE A CA    1 
ATOM   3618  C  CA    B ILE A 1 234 ? -6.441  -12.684 40.940  0.80 23.80  ? 234 ILE A CA    1 
ATOM   3619  C  C     A ILE A 1 234 ? -7.325  -11.912 40.300  0.20 28.15  ? 234 ILE A C     1 
ATOM   3620  C  C     B ILE A 1 234 ? -7.375  -11.802 40.121  0.80 28.71  ? 234 ILE A C     1 
ATOM   3621  O  O     A ILE A 1 234 ? -7.956  -11.038 40.908  0.20 29.80  ? 234 ILE A O     1 
ATOM   3622  O  O     B ILE A 1 234 ? -8.030  -10.900 40.666  0.80 30.41  ? 234 ILE A O     1 
ATOM   3623  C  CB    A ILE A 1 234 ? -4.912  -12.415 40.901  0.20 26.37  ? 234 ILE A CB    1 
ATOM   3624  C  CB    B ILE A 1 234 ? -4.966  -12.249 40.810  0.80 25.65  ? 234 ILE A CB    1 
ATOM   3625  C  CG1   A ILE A 1 234 ? -4.003  -13.335 41.723  0.20 30.60  ? 234 ILE A CG1   1 
ATOM   3626  C  CG1   B ILE A 1 234 ? -4.076  -13.145 41.680  0.80 31.22  ? 234 ILE A CG1   1 
ATOM   3627  C  CG2   A ILE A 1 234 ? -4.735  -10.974 41.345  0.20 30.98  ? 234 ILE A CG2   1 
ATOM   3628  C  CG2   B ILE A 1 234 ? -4.792  -10.808 41.219  0.80 31.80  ? 234 ILE A CG2   1 
ATOM   3629  C  CD1   A ILE A 1 234 ? -2.528  -13.023 41.580  0.20 29.28  ? 234 ILE A CD1   1 
ATOM   3630  C  CD1   B ILE A 1 234 ? -2.586  -12.957 41.438  0.80 29.27  ? 234 ILE A CD1   1 
ATOM   3631  N  N     A VAL A 1 235 ? -7.445  -12.078 38.979  0.20 27.51  ? 235 VAL A N     1 
ATOM   3632  N  N     B VAL A 1 235 ? -7.474  -12.050 38.809  0.80 27.05  ? 235 VAL A N     1 
ATOM   3633  C  CA    A VAL A 1 235 ? -8.384  -11.265 38.210  0.20 27.08  ? 235 VAL A CA    1 
ATOM   3634  C  CA    B VAL A 1 235 ? -8.435  -11.311 37.990  0.80 27.50  ? 235 VAL A CA    1 
ATOM   3635  C  C     A VAL A 1 235 ? -9.816  -11.507 38.673  0.20 27.97  ? 235 VAL A C     1 
ATOM   3636  C  C     B VAL A 1 235 ? -9.854  -11.490 38.524  0.80 27.92  ? 235 VAL A C     1 
ATOM   3637  O  O     A VAL A 1 235 ? -10.645 -10.588 38.665  0.20 26.52  ? 235 VAL A O     1 
ATOM   3638  O  O     B VAL A 1 235 ? -10.623 -10.526 38.619  0.80 26.38  ? 235 VAL A O     1 
ATOM   3639  C  CB    A VAL A 1 235 ? -8.211  -11.545 36.701  0.20 27.77  ? 235 VAL A CB    1 
ATOM   3640  C  CB    B VAL A 1 235 ? -8.318  -11.743 36.513  0.80 27.96  ? 235 VAL A CB    1 
ATOM   3641  C  CG1   A VAL A 1 235 ? -9.278  -10.822 35.888  0.20 24.42  ? 235 VAL A CG1   1 
ATOM   3642  C  CG1   B VAL A 1 235 ? -9.409  -11.087 35.658  0.80 22.82  ? 235 VAL A CG1   1 
ATOM   3643  C  CG2   A VAL A 1 235 ? -6.822  -11.130 36.249  0.20 25.65  ? 235 VAL A CG2   1 
ATOM   3644  C  CG2   B VAL A 1 235 ? -6.947  -11.409 36.001  0.80 26.29  ? 235 VAL A CG2   1 
ATOM   3645  N  N     A SER A 1 236 ? -10.128 -12.734 39.100  0.20 28.92  ? 236 SER A N     1 
ATOM   3646  N  N     B SER A 1 236 ? -10.219 -12.720 38.890  0.80 29.28  ? 236 SER A N     1 
ATOM   3647  C  CA    A SER A 1 236 ? -11.460 -13.015 39.627  0.20 28.61  ? 236 SER A CA    1 
ATOM   3648  C  CA    B SER A 1 236 ? -11.556 -12.962 39.422  0.80 27.85  ? 236 SER A CA    1 
ATOM   3649  C  C     A SER A 1 236 ? -11.757 -12.172 40.859  0.20 29.44  ? 236 SER A C     1 
ATOM   3650  C  C     B SER A 1 236 ? -11.812 -12.121 40.664  0.80 29.43  ? 236 SER A C     1 
ATOM   3651  O  O     A SER A 1 236 ? -12.860 -11.630 40.999  0.20 29.59  ? 236 SER A O     1 
ATOM   3652  O  O     B SER A 1 236 ? -12.871 -11.494 40.797  0.80 29.30  ? 236 SER A O     1 
ATOM   3653  C  CB    A SER A 1 236 ? -11.593 -14.501 39.960  0.20 31.43  ? 236 SER A CB    1 
ATOM   3654  C  CB    B SER A 1 236 ? -11.735 -14.445 39.740  0.80 32.41  ? 236 SER A CB    1 
ATOM   3655  O  OG    A SER A 1 236 ? -12.761 -14.744 40.726  0.20 20.38  ? 236 SER A OG    1 
ATOM   3656  O  OG    B SER A 1 236 ? -12.102 -15.152 38.571  0.80 46.31  ? 236 SER A OG    1 
ATOM   3657  N  N     A SER A 1 237 ? -10.781 -12.045 41.763  0.20 30.54  ? 237 SER A N     1 
ATOM   3658  N  N     B SER A 1 237 ? -10.839 -12.083 41.581  0.80 30.75  ? 237 SER A N     1 
ATOM   3659  C  CA    A SER A 1 237 ? -11.002 -11.283 42.989  0.20 31.48  ? 237 SER A CA    1 
ATOM   3660  C  CA    B SER A 1 237 ? -10.998 -11.306 42.808  0.80 32.39  ? 237 SER A CA    1 
ATOM   3661  C  C     A SER A 1 237 ? -11.087 -9.787  42.718  0.20 31.92  ? 237 SER A C     1 
ATOM   3662  C  C     B SER A 1 237 ? -11.190 -9.824  42.514  0.80 33.18  ? 237 SER A C     1 
ATOM   3663  O  O     A SER A 1 237 ? -11.702 -9.053  43.500  0.20 29.18  ? 237 SER A O     1 
ATOM   3664  O  O     B SER A 1 237 ? -11.930 -9.143  43.235  0.80 29.02  ? 237 SER A O     1 
ATOM   3665  C  CB    A SER A 1 237 ? -9.891  -11.577 43.995  0.20 28.84  ? 237 SER A CB    1 
ATOM   3666  C  CB    B SER A 1 237 ? -9.790  -11.515 43.715  0.80 27.77  ? 237 SER A CB    1 
ATOM   3667  O  OG    A SER A 1 237 ? -9.879  -12.949 44.350  0.20 32.61  ? 237 SER A OG    1 
ATOM   3668  O  OG    B SER A 1 237 ? -9.807  -12.822 44.259  0.80 33.14  ? 237 SER A OG    1 
ATOM   3669  N  N     A ILE A 1 238 ? -10.481 -9.313  41.628  0.20 25.89  ? 238 ILE A N     1 
ATOM   3670  N  N     B ILE A 1 238 ? -10.544 -9.306  41.463  0.80 25.00  ? 238 ILE A N     1 
ATOM   3671  C  CA    A ILE A 1 238 ? -10.567 -7.891  41.314  0.20 25.99  ? 238 ILE A CA    1 
ATOM   3672  C  CA    B ILE A 1 238 ? -10.724 -7.894  41.125  0.80 25.18  ? 238 ILE A CA    1 
ATOM   3673  C  C     A ILE A 1 238 ? -11.894 -7.562  40.635  0.20 29.06  ? 238 ILE A C     1 
ATOM   3674  C  C     B ILE A 1 238 ? -12.120 -7.644  40.560  0.80 29.58  ? 238 ILE A C     1 
ATOM   3675  O  O     A ILE A 1 238 ? -12.425 -6.458  40.805  0.20 27.46  ? 238 ILE A O     1 
ATOM   3676  O  O     B ILE A 1 238 ? -12.756 -6.625  40.861  0.80 26.87  ? 238 ILE A O     1 
ATOM   3677  C  CB    A ILE A 1 238 ? -9.370  -7.460  40.450  0.20 28.74  ? 238 ILE A CB    1 
ATOM   3678  C  CB    B ILE A 1 238 ? -9.635  -7.424  40.145  0.80 30.06  ? 238 ILE A CB    1 
ATOM   3679  C  CG1   A ILE A 1 238 ? -8.060  -7.870  41.123  0.20 25.85  ? 238 ILE A CG1   1 
ATOM   3680  C  CG1   B ILE A 1 238 ? -8.291  -7.259  40.856  0.80 24.76  ? 238 ILE A CG1   1 
ATOM   3681  C  CG2   A ILE A 1 238 ? -9.387  -5.957  40.222  0.20 23.56  ? 238 ILE A CG2   1 
ATOM   3682  C  CG2   B ILE A 1 238 ? -10.049 -6.117  39.496  0.80 24.92  ? 238 ILE A CG2   1 
ATOM   3683  C  CD1   A ILE A 1 238 ? -6.837  -7.669  40.247  0.20 24.71  ? 238 ILE A CD1   1 
ATOM   3684  C  CD1   B ILE A 1 238 ? -7.118  -7.163  39.857  0.80 23.75  ? 238 ILE A CD1   1 
ATOM   3685  N  N     A THR A 1 239 ? -12.455 -8.500  39.874  0.20 26.96  ? 239 THR A N     1 
ATOM   3686  N  N     B THR A 1 239 ? -12.616 -8.549  39.724  0.80 26.53  ? 239 THR A N     1 
ATOM   3687  C  CA    A THR A 1 239 ? -13.730 -8.299  39.200  0.20 29.00  ? 239 THR A CA    1 
ATOM   3688  C  CA    B THR A 1 239 ? -13.879 -8.307  39.041  0.80 29.05  ? 239 THR A CA    1 
ATOM   3689  C  C     A THR A 1 239 ? -14.900 -8.912  39.961  0.20 30.65  ? 239 THR A C     1 
ATOM   3690  C  C     B THR A 1 239 ? -15.088 -8.839  39.797  0.80 31.35  ? 239 THR A C     1 
ATOM   3691  O  O     A THR A 1 239 ? -16.025 -8.911  39.449  0.20 33.08  ? 239 THR A O     1 
ATOM   3692  O  O     B THR A 1 239 ? -16.223 -8.574  39.375  0.80 34.39  ? 239 THR A O     1 
ATOM   3693  C  CB    A THR A 1 239 ? -13.682 -8.877  37.783  0.20 28.57  ? 239 THR A CB    1 
ATOM   3694  C  CB    B THR A 1 239 ? -13.867 -8.936  37.640  0.80 28.07  ? 239 THR A CB    1 
ATOM   3695  O  OG1   A THR A 1 239 ? -13.587 -10.304 37.852  0.20 30.72  ? 239 THR A OG1   1 
ATOM   3696  O  OG1   B THR A 1 239 ? -13.883 -10.360 37.769  0.80 31.86  ? 239 THR A OG1   1 
ATOM   3697  C  CG2   A THR A 1 239 ? -12.483 -8.326  37.014  0.20 28.22  ? 239 THR A CG2   1 
ATOM   3698  C  CG2   B THR A 1 239 ? -12.624 -8.499  36.832  0.80 27.87  ? 239 THR A CG2   1 
ATOM   3699  N  N     A ALA A 1 240 ? -14.663 -9.434  41.169  0.20 29.40  ? 240 ALA A N     1 
ATOM   3700  N  N     B ALA A 1 240 ? -14.883 -9.578  40.896  0.80 29.74  ? 240 ALA A N     1 
ATOM   3701  C  CA    A ALA A 1 240 ? -15.741 -10.047 41.939  0.20 31.82  ? 240 ALA A CA    1 
ATOM   3702  C  CA    B ALA A 1 240 ? -16.014 -10.137 41.638  0.80 31.93  ? 240 ALA A CA    1 
ATOM   3703  C  C     A ALA A 1 240 ? -16.790 -9.034  42.379  0.20 30.13  ? 240 ALA A C     1 
ATOM   3704  C  C     B ALA A 1 240 ? -17.006 -9.052  42.056  0.80 29.35  ? 240 ALA A C     1 
ATOM   3705  O  O     A ALA A 1 240 ? -17.937 -9.417  42.627  0.20 30.32  ? 240 ALA A O     1 
ATOM   3706  O  O     B ALA A 1 240 ? -18.221 -9.279  42.051  0.80 28.71  ? 240 ALA A O     1 
ATOM   3707  C  CB    A ALA A 1 240 ? -15.172 -10.771 43.161  0.20 30.87  ? 240 ALA A CB    1 
ATOM   3708  C  CB    B ALA A 1 240 ? -15.514 -10.905 42.863  0.80 31.04  ? 240 ALA A CB    1 
ATOM   3709  N  N     A SER A 1 241 ? -16.426 -7.756  42.483  0.20 28.67  ? 241 SER A N     1 
ATOM   3710  N  N     B SER A 1 241 ? -16.509 -7.857  42.396  0.80 28.14  ? 241 SER A N     1 
ATOM   3711  C  CA    A SER A 1 241 ? -17.385 -6.727  42.864  0.20 32.08  ? 241 SER A CA    1 
ATOM   3712  C  CA    B SER A 1 241 ? -17.399 -6.770  42.798  0.80 32.11  ? 241 SER A CA    1 
ATOM   3713  C  C     A SER A 1 241 ? -18.272 -6.288  41.707  0.20 32.94  ? 241 SER A C     1 
ATOM   3714  C  C     B SER A 1 241 ? -18.327 -6.348  41.669  0.80 33.20  ? 241 SER A C     1 
ATOM   3715  O  O     A SER A 1 241 ? -19.231 -5.541  41.932  0.20 32.09  ? 241 SER A O     1 
ATOM   3716  O  O     B SER A 1 241 ? -19.420 -5.825  41.925  0.80 32.86  ? 241 SER A O     1 
ATOM   3717  C  CB    A SER A 1 241 ? -16.655 -5.514  43.442  0.20 32.32  ? 241 SER A CB    1 
ATOM   3718  C  CB    B SER A 1 241 ? -16.578 -5.573  43.275  0.80 32.27  ? 241 SER A CB    1 
ATOM   3719  O  OG    A SER A 1 241 ? -15.829 -4.904  42.469  0.20 33.17  ? 241 SER A OG    1 
ATOM   3720  O  OG    B SER A 1 241 ? -15.625 -5.200  42.300  0.80 35.08  ? 241 SER A OG    1 
ATOM   3721  N  N     A LEU A 1 242 ? -17.974 -6.723  40.483  0.20 28.25  ? 242 LEU A N     1 
ATOM   3722  N  N     B LEU A 1 242 ? -17.917 -6.563  40.419  0.80 27.14  ? 242 LEU A N     1 
ATOM   3723  C  CA    A LEU A 1 242 ? -18.828 -6.455  39.336  0.20 29.64  ? 242 LEU A CA    1 
ATOM   3724  C  CA    B LEU A 1 242 ? -18.762 -6.236  39.281  0.80 29.06  ? 242 LEU A CA    1 
ATOM   3725  C  C     A LEU A 1 242 ? -19.790 -7.596  39.034  0.20 33.99  ? 242 LEU A C     1 
ATOM   3726  C  C     B LEU A 1 242 ? -19.814 -7.305  39.011  0.80 34.99  ? 242 LEU A C     1 
ATOM   3727  O  O     A LEU A 1 242 ? -20.763 -7.389  38.300  0.20 35.24  ? 242 LEU A O     1 
ATOM   3728  O  O     B LEU A 1 242 ? -20.803 -7.019  38.328  0.80 37.45  ? 242 LEU A O     1 
ATOM   3729  C  CB    A LEU A 1 242 ? -17.975 -6.175  38.091  0.20 31.22  ? 242 LEU A CB    1 
ATOM   3730  C  CB    B LEU A 1 242 ? -17.897 -6.026  38.030  0.80 31.27  ? 242 LEU A CB    1 
ATOM   3731  C  CG    A LEU A 1 242 ? -16.920 -5.068  38.188  0.20 29.45  ? 242 LEU A CG    1 
ATOM   3732  C  CG    B LEU A 1 242 ? -16.796 -4.950  38.053  0.80 29.02  ? 242 LEU A CG    1 
ATOM   3733  C  CD1   A LEU A 1 242 ? -15.990 -5.103  36.977  0.20 30.48  ? 242 LEU A CD1   1 
ATOM   3734  C  CD1   B LEU A 1 242 ? -15.817 -5.124  36.860  0.80 30.01  ? 242 LEU A CD1   1 
ATOM   3735  C  CD2   A LEU A 1 242 ? -17.574 -3.700  38.323  0.20 29.57  ? 242 LEU A CD2   1 
ATOM   3736  C  CD2   B LEU A 1 242 ? -17.393 -3.544  38.070  0.80 28.19  ? 242 LEU A CD2   1 
ATOM   3737  N  N     A ARG A 1 243 ? -19.545 -8.785  39.585  0.20 31.60  ? 243 ARG A N     1 
ATOM   3738  N  N     B ARG A 1 243 ? -19.638 -8.516  39.553  0.80 31.89  ? 243 ARG A N     1 
ATOM   3739  C  CA    A ARG A 1 243 ? -20.338 -9.973  39.298  0.20 30.18  ? 243 ARG A CA    1 
ATOM   3740  C  CA    B ARG A 1 243 ? -20.436 -9.674  39.171  0.80 28.68  ? 243 ARG A CA    1 
ATOM   3741  C  C     A ARG A 1 243 ? -21.151 -10.449 40.492  0.20 32.58  ? 243 ARG A C     1 
ATOM   3742  C  C     B ARG A 1 243 ? -21.352 -10.176 40.273  0.80 32.14  ? 243 ARG A C     1 
ATOM   3743  O  O     A ARG A 1 243 ? -21.873 -11.446 40.374  0.20 30.57  ? 243 ARG A O     1 
ATOM   3744  O  O     B ARG A 1 243 ? -22.202 -11.036 40.004  0.80 29.75  ? 243 ARG A O     1 
ATOM   3745  C  CB    A ARG A 1 243 ? -19.424 -11.106 38.816  0.20 32.72  ? 243 ARG A CB    1 
ATOM   3746  C  CB    B ARG A 1 243 ? -19.519 -10.829 38.742  0.80 34.32  ? 243 ARG A CB    1 
ATOM   3747  C  CG    A ARG A 1 243 ? -18.610 -10.743 37.587  0.20 31.40  ? 243 ARG A CG    1 
ATOM   3748  C  CG    B ARG A 1 243 ? -18.537 -10.462 37.641  0.80 31.35  ? 243 ARG A CG    1 
ATOM   3749  C  CD    A ARG A 1 243 ? -17.629 -11.834 37.202  0.20 32.09  ? 243 ARG A CD    1 
ATOM   3750  C  CD    B ARG A 1 243 ? -17.695 -11.649 37.234  0.80 32.41  ? 243 ARG A CD    1 
ATOM   3751  N  NE    A ARG A 1 243 ? -16.537 -11.957 38.160  0.20 31.52  ? 243 ARG A NE    1 
ATOM   3752  N  NE    B ARG A 1 243 ? -16.569 -11.878 38.131  0.80 31.72  ? 243 ARG A NE    1 
ATOM   3753  C  CZ    A ARG A 1 243 ? -16.365 -12.990 38.972  0.20 27.70  ? 243 ARG A CZ    1 
ATOM   3754  C  CZ    B ARG A 1 243 ? -16.358 -13.001 38.804  0.80 27.11  ? 243 ARG A CZ    1 
ATOM   3755  N  NH1   A ARG A 1 243 ? -17.193 -14.022 38.964  0.20 28.17  ? 243 ARG A NH1   1 
ATOM   3756  N  NH1   B ARG A 1 243 ? -17.200 -14.018 38.732  0.80 27.14  ? 243 ARG A NH1   1 
ATOM   3757  N  NH2   A ARG A 1 243 ? -15.326 -12.995 39.803  0.20 29.45  ? 243 ARG A NH2   1 
ATOM   3758  N  NH2   B ARG A 1 243 ? -15.259 -13.114 39.548  0.80 29.01  ? 243 ARG A NH2   1 
ATOM   3759  N  N     A PHE A 1 244 ? -21.044 -9.775  41.635  0.20 29.99  ? 244 PHE A N     1 
ATOM   3760  N  N     B PHE A 1 244 ? -21.167 -9.699  41.501  0.80 28.80  ? 244 PHE A N     1 
ATOM   3761  C  CA    A PHE A 1 244 ? -21.754 -10.155 42.845  0.20 32.25  ? 244 PHE A CA    1 
ATOM   3762  C  CA    B PHE A 1 244 ? -21.886 -10.138 42.682  0.80 32.09  ? 244 PHE A CA    1 
ATOM   3763  C  C     A PHE A 1 244 ? -22.176 -8.892  43.581  0.20 33.78  ? 244 PHE A C     1 
ATOM   3764  C  C     B PHE A 1 244 ? -22.350 -8.890  43.420  0.80 34.09  ? 244 PHE A C     1 
ATOM   3765  O  O     A PHE A 1 244 ? -21.683 -7.796  43.305  0.20 32.65  ? 244 PHE A O     1 
ATOM   3766  O  O     B PHE A 1 244 ? -21.919 -7.771  43.122  0.80 32.38  ? 244 PHE A O     1 
ATOM   3767  C  CB    A PHE A 1 244 ? -20.892 -11.036 43.765  0.20 32.76  ? 244 PHE A CB    1 
ATOM   3768  C  CB    B PHE A 1 244 ? -21.010 -11.007 43.612  0.80 32.88  ? 244 PHE A CB    1 
ATOM   3769  C  CG    A PHE A 1 244 ? -20.400 -12.302 43.118  0.20 30.12  ? 244 PHE A CG    1 
ATOM   3770  C  CG    B PHE A 1 244 ? -20.545 -12.314 43.010  0.80 29.68  ? 244 PHE A CG    1 
ATOM   3771  C  CD1   A PHE A 1 244 ? -21.251 -13.380 42.935  0.20 31.13  ? 244 PHE A CD1   1 
ATOM   3772  C  CD1   B PHE A 1 244 ? -21.442 -13.342 42.744  0.80 30.50  ? 244 PHE A CD1   1 
ATOM   3773  C  CD2   A PHE A 1 244 ? -19.083 -12.418 42.706  0.20 34.05  ? 244 PHE A CD2   1 
ATOM   3774  C  CD2   B PHE A 1 244 ? -19.198 -12.527 42.740  0.80 34.60  ? 244 PHE A CD2   1 
ATOM   3775  C  CE1   A PHE A 1 244 ? -20.801 -14.548 42.346  0.20 33.73  ? 244 PHE A CE1   1 
ATOM   3776  C  CE1   B PHE A 1 244 ? -21.014 -14.550 42.204  0.80 33.87  ? 244 PHE A CE1   1 
ATOM   3777  C  CE2   A PHE A 1 244 ? -18.626 -13.584 42.117  0.20 31.41  ? 244 PHE A CE2   1 
ATOM   3778  C  CE2   B PHE A 1 244 ? -18.759 -13.735 42.202  0.80 31.12  ? 244 PHE A CE2   1 
ATOM   3779  C  CZ    A PHE A 1 244 ? -19.486 -14.649 41.936  0.20 31.34  ? 244 PHE A CZ    1 
ATOM   3780  C  CZ    B PHE A 1 244 ? -19.666 -14.743 41.928  0.80 31.38  ? 244 PHE A CZ    1 
ATOM   3781  N  N     A ASP A 1 245 ? -23.103 -9.058  44.521  0.20 33.74  ? 245 ASP A N     1 
ATOM   3782  N  N     B ASP A 1 245 ? -23.243 -9.084  44.388  0.80 33.86  ? 245 ASP A N     1 
ATOM   3783  C  CA    A ASP A 1 245 ? -23.541 -7.937  45.338  0.20 34.60  ? 245 ASP A CA    1 
ATOM   3784  C  CA    B ASP A 1 245 ? -23.657 -7.984  45.241  0.80 34.47  ? 245 ASP A CA    1 
ATOM   3785  C  C     A ASP A 1 245 ? -22.407 -7.471  46.246  0.20 37.06  ? 245 ASP A C     1 
ATOM   3786  C  C     B ASP A 1 245 ? -22.475 -7.515  46.087  0.80 37.57  ? 245 ASP A C     1 
ATOM   3787  O  O     A ASP A 1 245 ? -21.565 -8.260  46.684  0.20 35.52  ? 245 ASP A O     1 
ATOM   3788  O  O     B ASP A 1 245 ? -21.555 -8.283  46.388  0.80 35.29  ? 245 ASP A O     1 
ATOM   3789  C  CB    A ASP A 1 245 ? -24.761 -8.331  46.176  0.20 30.37  ? 245 ASP A CB    1 
ATOM   3790  C  CB    B ASP A 1 245 ? -24.822 -8.428  46.136  0.80 29.64  ? 245 ASP A CB    1 
ATOM   3791  C  CG    A ASP A 1 245 ? -25.346 -7.162  46.952  0.20 38.62  ? 245 ASP A CG    1 
ATOM   3792  C  CG    B ASP A 1 245 ? -25.676 -7.269  46.616  0.80 39.33  ? 245 ASP A CG    1 
ATOM   3793  O  OD1   A ASP A 1 245 ? -24.984 -6.002  46.664  0.20 38.59  ? 245 ASP A OD1   1 
ATOM   3794  O  OD1   B ASP A 1 245 ? -25.526 -6.141  46.102  0.80 41.56  ? 245 ASP A OD1   1 
ATOM   3795  O  OD2   A ASP A 1 245 ? -26.168 -7.407  47.858  0.20 36.63  ? 245 ASP A OD2   1 
ATOM   3796  O  OD2   B ASP A 1 245 ? -26.505 -7.494  47.518  0.80 36.82  ? 245 ASP A OD2   1 
ATOM   3797  N  N     A GLY A 1 246 ? -22.389 -6.173  46.521  0.20 33.96  ? 246 GLY A N     1 
ATOM   3798  N  N     B GLY A 1 246 ? -22.496 -6.242  46.463  0.80 33.74  ? 246 GLY A N     1 
ATOM   3799  C  CA    A GLY A 1 246 ? -21.360 -5.614  47.377  0.20 37.13  ? 246 GLY A CA    1 
ATOM   3800  C  CA    B GLY A 1 246 ? -21.429 -5.711  47.287  0.80 37.23  ? 246 GLY A CA    1 
ATOM   3801  C  C     A GLY A 1 246 ? -21.529 -4.117  47.500  0.20 37.00  ? 246 GLY A C     1 
ATOM   3802  C  C     B GLY A 1 246 ? -21.545 -4.212  47.445  0.80 36.90  ? 246 GLY A C     1 
ATOM   3803  O  O     A GLY A 1 246 ? -22.468 -3.524  46.958  0.20 41.78  ? 246 GLY A O     1 
ATOM   3804  O  O     B GLY A 1 246 ? -22.438 -3.566  46.888  0.80 41.62  ? 246 GLY A O     1 
ATOM   3805  N  N     A ALA A 1 247 ? -20.593 -3.508  48.228  0.20 35.67  ? 247 ALA A N     1 
ATOM   3806  N  N     B ALA A 1 247 ? -20.603 -3.662  48.219  0.80 35.42  ? 247 ALA A N     1 
ATOM   3807  C  CA    A ALA A 1 247 ? -20.617 -2.075  48.472  0.20 39.45  ? 247 ALA A CA    1 
ATOM   3808  C  CA    B ALA A 1 247 ? -20.611 -2.241  48.538  0.80 39.99  ? 247 ALA A CA    1 
ATOM   3809  C  C     A ALA A 1 247 ? -19.368 -1.347  48.000  0.20 36.82  ? 247 ALA A C     1 
ATOM   3810  C  C     B ALA A 1 247 ? -19.290 -1.548  48.227  0.80 36.82  ? 247 ALA A C     1 
ATOM   3811  O  O     A ALA A 1 247 ? -19.383 -0.112  47.941  0.20 39.09  ? 247 ALA A O     1 
ATOM   3812  O  O     B ALA A 1 247 ? -19.079 -0.414  48.674  0.80 39.71  ? 247 ALA A O     1 
ATOM   3813  C  CB    A ALA A 1 247 ? -20.825 -1.790  49.968  0.20 41.24  ? 247 ALA A CB    1 
ATOM   3814  C  CB    B ALA A 1 247 ? -20.970 -2.029  50.013  0.80 42.02  ? 247 ALA A CB    1 
ATOM   3815  N  N     A LEU A 1 248 ? -18.297 -2.061  47.666  0.20 35.27  ? 248 LEU A N     1 
ATOM   3816  N  N     B LEU A 1 248 ? -18.391 -2.190  47.489  0.80 35.29  ? 248 LEU A N     1 
ATOM   3817  C  CA    A LEU A 1 248 ? -17.046 -1.458  47.227  0.20 33.19  ? 248 LEU A CA    1 
ATOM   3818  C  CA    B LEU A 1 248 ? -17.119 -1.576  47.137  0.80 33.09  ? 248 LEU A CA    1 
ATOM   3819  C  C     A LEU A 1 248 ? -16.795 -1.818  45.769  0.20 32.28  ? 248 LEU A C     1 
ATOM   3820  C  C     B LEU A 1 248 ? -16.809 -1.905  45.682  0.80 32.20  ? 248 LEU A C     1 
ATOM   3821  O  O     A LEU A 1 248 ? -16.881 -2.993  45.394  0.20 31.59  ? 248 LEU A O     1 
ATOM   3822  O  O     B LEU A 1 248 ? -17.023 -3.039  45.240  0.80 30.68  ? 248 LEU A O     1 
ATOM   3823  C  CB    A LEU A 1 248 ? -15.879 -1.926  48.100  0.20 31.07  ? 248 LEU A CB    1 
ATOM   3824  C  CB    B LEU A 1 248 ? -16.000 -2.057  48.075  0.80 30.50  ? 248 LEU A CB    1 
ATOM   3825  C  CG    A LEU A 1 248 ? -14.487 -1.383  47.769  0.20 35.85  ? 248 LEU A CG    1 
ATOM   3826  C  CG    B LEU A 1 248 ? -14.652 -1.331  48.034  0.80 38.24  ? 248 LEU A CG    1 
ATOM   3827  C  CD1   A LEU A 1 248 ? -14.415 0.113   48.039  0.20 33.87  ? 248 LEU A CD1   1 
ATOM   3828  C  CD1   B LEU A 1 248 ? -14.869 0.153   48.222  0.80 34.12  ? 248 LEU A CD1   1 
ATOM   3829  C  CD2   A LEU A 1 248 ? -13.412 -2.126  48.554  0.20 31.77  ? 248 LEU A CD2   1 
ATOM   3830  C  CD2   B LEU A 1 248 ? -13.682 -1.871  49.100  0.80 31.83  ? 248 LEU A CD2   1 
ATOM   3831  N  N     A ASN A 1 249 ? -16.494 -0.804  44.952  0.20 31.86  ? 249 ASN A N     1 
ATOM   3832  N  N     B ASN A 1 249 ? -16.335 -0.905  44.929  0.80 31.37  ? 249 ASN A N     1 
ATOM   3833  C  CA    A ASN A 1 249 ? -16.173 -0.990  43.534  0.20 33.25  ? 249 ASN A CA    1 
ATOM   3834  C  CA    B ASN A 1 249 ? -15.976 -1.087  43.517  0.80 33.66  ? 249 ASN A CA    1 
ATOM   3835  C  C     A ASN A 1 249 ? -17.313 -1.685  42.789  0.20 33.20  ? 249 ASN A C     1 
ATOM   3836  C  C     B ASN A 1 249 ? -17.137 -1.675  42.714  0.80 33.45  ? 249 ASN A C     1 
ATOM   3837  O  O     A ASN A 1 249 ? -17.109 -2.654  42.055  0.20 32.99  ? 249 ASN A O     1 
ATOM   3838  O  O     B ASN A 1 249 ? -16.987 -2.656  41.985  0.80 33.61  ? 249 ASN A O     1 
ATOM   3839  C  CB    A ASN A 1 249 ? -14.859 -1.758  43.369  0.20 29.91  ? 249 ASN A CB    1 
ATOM   3840  C  CB    B ASN A 1 249 ? -14.734 -1.969  43.385  0.80 28.52  ? 249 ASN A CB    1 
ATOM   3841  C  CG    A ASN A 1 249 ? -13.676 -1.008  43.942  0.20 32.15  ? 249 ASN A CG    1 
ATOM   3842  C  CG    B ASN A 1 249 ? -13.469 -1.262  43.814  0.80 32.35  ? 249 ASN A CG    1 
ATOM   3843  O  OD1   A ASN A 1 249 ? -13.641 0.222   43.923  0.20 32.93  ? 249 ASN A OD1   1 
ATOM   3844  O  OD1   B ASN A 1 249 ? -13.482 -0.064  44.088  0.80 33.59  ? 249 ASN A OD1   1 
ATOM   3845  N  ND2   A ASN A 1 249 ? -12.699 -1.745  44.458  0.20 32.34  ? 249 ASN A ND2   1 
ATOM   3846  N  ND2   B ASN A 1 249 ? -12.358 -1.996  43.852  0.80 31.16  ? 249 ASN A ND2   1 
ATOM   3847  N  N     A VAL A 1 250 ? -18.531 -1.170  42.977  0.20 30.40  ? 250 VAL A N     1 
ATOM   3848  N  N     B VAL A 1 250 ? -18.317 -1.067  42.855  0.80 29.29  ? 250 VAL A N     1 
ATOM   3849  C  CA    A VAL A 1 250 ? -19.708 -1.798  42.380  0.20 32.09  ? 250 VAL A CA    1 
ATOM   3850  C  CA    B VAL A 1 250 ? -19.537 -1.686  42.345  0.80 32.03  ? 250 VAL A CA    1 
ATOM   3851  C  C     A VAL A 1 250 ? -19.830 -1.539  40.889  0.20 30.54  ? 250 VAL A C     1 
ATOM   3852  C  C     B VAL A 1 250 ? -19.794 -1.387  40.878  0.80 30.21  ? 250 VAL A C     1 
ATOM   3853  O  O     A VAL A 1 250 ? -20.627 -2.209  40.223  0.20 30.77  ? 250 VAL A O     1 
ATOM   3854  O  O     B VAL A 1 250 ? -20.618 -2.080  40.264  0.80 30.94  ? 250 VAL A O     1 
ATOM   3855  C  CB    A VAL A 1 250 ? -20.999 -1.333  43.082  0.20 31.53  ? 250 VAL A CB    1 
ATOM   3856  C  CB    B VAL A 1 250 ? -20.756 -1.276  43.206  0.80 32.10  ? 250 VAL A CB    1 
ATOM   3857  C  CG1   A VAL A 1 250 ? -20.985 -1.750  44.544  0.20 36.14  ? 250 VAL A CG1   1 
ATOM   3858  C  CG1   B VAL A 1 250 ? -20.329 -1.116  44.660  0.80 33.38  ? 250 VAL A CG1   1 
ATOM   3859  C  CG2   A VAL A 1 250 ? -21.161 0.172   42.956  0.20 34.78  ? 250 VAL A CG2   1 
ATOM   3860  C  CG2   B VAL A 1 250 ? -21.386 0.002   42.695  0.80 35.69  ? 250 VAL A CG2   1 
ATOM   3861  N  N     A ASP A 1 251 ? -19.068 -0.590  40.345  0.20 31.04  ? 251 ASP A N     1 
ATOM   3862  N  N     B ASP A 1 251 ? -19.127 -0.388  40.295  0.80 30.21  ? 251 ASP A N     1 
ATOM   3863  C  CA    A ASP A 1 251 ? -19.070 -0.324  38.912  0.20 35.00  ? 251 ASP A CA    1 
ATOM   3864  C  CA    B ASP A 1 251 ? -19.100 -0.241  38.842  0.80 34.95  ? 251 ASP A CA    1 
ATOM   3865  C  C     A ASP A 1 251 ? -17.668 0.108   38.493  0.20 29.74  ? 251 ASP A C     1 
ATOM   3866  C  C     B ASP A 1 251 ? -17.735 0.284   38.407  0.80 28.59  ? 251 ASP A C     1 
ATOM   3867  O  O     A ASP A 1 251 ? -16.762 0.234   39.322  0.20 30.25  ? 251 ASP A O     1 
ATOM   3868  O  O     B ASP A 1 251 ? -16.872 0.591   39.233  0.80 28.56  ? 251 ASP A O     1 
ATOM   3869  C  CB    A ASP A 1 251 ? -20.124 0.727   38.545  0.20 35.94  ? 251 ASP A CB    1 
ATOM   3870  C  CB    B ASP A 1 251 ? -20.233 0.659   38.327  0.80 36.65  ? 251 ASP A CB    1 
ATOM   3871  C  CG    A ASP A 1 251 ? -20.013 1.985   39.381  0.20 35.69  ? 251 ASP A CG    1 
ATOM   3872  C  CG    B ASP A 1 251 ? -20.286 2.015   39.010  0.80 38.31  ? 251 ASP A CG    1 
ATOM   3873  O  OD1   A ASP A 1 251 ? -19.255 1.975   40.372  0.20 35.38  ? 251 ASP A OD1   1 
ATOM   3874  O  OD1   B ASP A 1 251 ? -19.232 2.559   39.403  0.80 36.39  ? 251 ASP A OD1   1 
ATOM   3875  O  OD2   A ASP A 1 251 ? -20.682 2.987   39.044  0.20 36.22  ? 251 ASP A OD2   1 
ATOM   3876  O  OD2   B ASP A 1 251 ? -21.410 2.546   39.134  0.80 35.34  ? 251 ASP A OD2   1 
ATOM   3877  N  N     A LEU A 1 252 ? -17.491 0.330   37.187  0.20 34.43  ? 252 LEU A N     1 
ATOM   3878  N  N     B LEU A 1 252 ? -17.539 0.378   37.083  0.80 34.56  ? 252 LEU A N     1 
ATOM   3879  C  CA    A LEU A 1 252 ? -16.174 0.706   36.680  0.20 34.45  ? 252 LEU A CA    1 
ATOM   3880  C  CA    B LEU A 1 252 ? -16.218 0.729   36.560  0.80 34.73  ? 252 LEU A CA    1 
ATOM   3881  C  C     A LEU A 1 252 ? -15.801 2.130   37.070  0.20 32.92  ? 252 LEU A C     1 
ATOM   3882  C  C     B LEU A 1 252 ? -15.791 2.120   37.005  0.80 32.83  ? 252 LEU A C     1 
ATOM   3883  O  O     A LEU A 1 252 ? -14.612 2.437   37.215  0.20 31.61  ? 252 LEU A O     1 
ATOM   3884  O  O     B LEU A 1 252 ? -14.613 2.346   37.295  0.80 31.37  ? 252 LEU A O     1 
ATOM   3885  C  CB    A LEU A 1 252 ? -16.119 0.549   35.158  0.20 27.95  ? 252 LEU A CB    1 
ATOM   3886  C  CB    B LEU A 1 252 ? -16.189 0.623   35.029  0.80 27.16  ? 252 LEU A CB    1 
ATOM   3887  C  CG    A LEU A 1 252 ? -16.260 -0.874  34.615  0.20 31.19  ? 252 LEU A CG    1 
ATOM   3888  C  CG    B LEU A 1 252 ? -16.348 -0.790  34.455  0.80 31.10  ? 252 LEU A CG    1 
ATOM   3889  C  CD1   A LEU A 1 252 ? -15.937 -0.912  33.130  0.20 33.09  ? 252 LEU A CD1   1 
ATOM   3890  C  CD1   B LEU A 1 252 ? -16.102 -0.805  32.943  0.80 33.88  ? 252 LEU A CD1   1 
ATOM   3891  C  CD2   A LEU A 1 252 ? -15.369 -1.838  35.383  0.20 33.72  ? 252 LEU A CD2   1 
ATOM   3892  C  CD2   B LEU A 1 252 ? -15.424 -1.777  35.157  0.80 34.46  ? 252 LEU A CD2   1 
ATOM   3893  N  N     A THR A 1 253 ? -16.791 3.009   37.238  0.20 33.17  ? 253 THR A N     1 
ATOM   3894  N  N     B THR A 1 253 ? -16.733 3.067   37.068  0.80 33.08  ? 253 THR A N     1 
ATOM   3895  C  CA    A THR A 1 253 ? -16.500 4.382   37.641  0.20 31.61  ? 253 THR A CA    1 
ATOM   3896  C  CA    B THR A 1 253 ? -16.405 4.409   37.540  0.80 31.20  ? 253 THR A CA    1 
ATOM   3897  C  C     A THR A 1 253 ? -15.838 4.425   39.014  0.20 33.59  ? 253 THR A C     1 
ATOM   3898  C  C     B THR A 1 253 ? -15.811 4.376   38.947  0.80 33.62  ? 253 THR A C     1 
ATOM   3899  O  O     A THR A 1 253 ? -14.927 5.228   39.249  0.20 31.42  ? 253 THR A O     1 
ATOM   3900  O  O     B THR A 1 253 ? -14.860 5.110   39.245  0.80 30.84  ? 253 THR A O     1 
ATOM   3901  C  CB    A THR A 1 253 ? -17.786 5.213   37.636  0.20 36.55  ? 253 THR A CB    1 
ATOM   3902  C  CB    B THR A 1 253 ? -17.657 5.298   37.487  0.80 37.57  ? 253 THR A CB    1 
ATOM   3903  O  OG1   A THR A 1 253 ? -18.403 5.134   36.345  0.20 37.03  ? 253 THR A OG1   1 
ATOM   3904  O  OG1   B THR A 1 253 ? -18.107 5.410   36.128  0.80 38.01  ? 253 THR A OG1   1 
ATOM   3905  C  CG2   A THR A 1 253 ? -17.483 6.672   37.953  0.20 34.95  ? 253 THR A CG2   1 
ATOM   3906  C  CG2   B THR A 1 253 ? -17.359 6.698   38.020  0.80 34.99  ? 253 THR A CG2   1 
ATOM   3907  N  N     A GLU A 1 254 ? -16.272 3.556   39.930  0.20 34.74  ? 254 GLU A N     1 
ATOM   3908  N  N     B GLU A 1 254 ? -16.336 3.512   39.823  0.80 34.90  ? 254 GLU A N     1 
ATOM   3909  C  CA    A GLU A 1 254 ? -15.739 3.573   41.287  0.20 35.18  ? 254 GLU A CA    1 
ATOM   3910  C  CA    B GLU A 1 254 ? -15.872 3.515   41.207  0.80 35.78  ? 254 GLU A CA    1 
ATOM   3911  C  C     A GLU A 1 254 ? -14.288 3.111   41.348  0.20 33.13  ? 254 GLU A C     1 
ATOM   3912  C  C     B GLU A 1 254 ? -14.456 2.973   41.331  0.80 33.01  ? 254 GLU A C     1 
ATOM   3913  O  O     A GLU A 1 254 ? -13.576 3.475   42.291  0.20 31.30  ? 254 GLU A O     1 
ATOM   3914  O  O     B GLU A 1 254 ? -13.725 3.377   42.246  0.80 30.89  ? 254 GLU A O     1 
ATOM   3915  C  CB    A GLU A 1 254 ? -16.612 2.708   42.200  0.20 31.68  ? 254 GLU A CB    1 
ATOM   3916  C  CB    B GLU A 1 254 ? -16.826 2.719   42.104  0.80 30.79  ? 254 GLU A CB    1 
ATOM   3917  C  CG    A GLU A 1 254 ? -16.389 2.954   43.682  0.20 33.42  ? 254 GLU A CG    1 
ATOM   3918  C  CG    B GLU A 1 254 ? -16.655 3.054   43.582  0.80 33.32  ? 254 GLU A CG    1 
ATOM   3919  C  CD    A GLU A 1 254 ? -17.378 2.209   44.555  0.20 36.42  ? 254 GLU A CD    1 
ATOM   3920  C  CD    B GLU A 1 254 ? -17.446 2.143   44.504  0.80 36.68  ? 254 GLU A CD    1 
ATOM   3921  O  OE1   A GLU A 1 254 ? -18.481 1.885   44.063  0.20 33.92  ? 254 GLU A OE1   1 
ATOM   3922  O  OE1   B GLU A 1 254 ? -18.520 1.649   44.084  0.80 33.51  ? 254 GLU A OE1   1 
ATOM   3923  O  OE2   A GLU A 1 254 ? -17.049 1.942   45.733  0.20 37.92  ? 254 GLU A OE2   1 
ATOM   3924  O  OE2   B GLU A 1 254 ? -16.984 1.916   45.655  0.80 38.30  ? 254 GLU A OE2   1 
ATOM   3925  N  N     A PHE A 1 255 ? -13.834 2.321   40.370  0.20 34.78  ? 255 PHE A N     1 
ATOM   3926  N  N     B PHE A 1 255 ? -14.053 2.055   40.441  0.80 35.96  ? 255 PHE A N     1 
ATOM   3927  C  CA    A PHE A 1 255 ? -12.418 1.965   40.310  0.20 32.28  ? 255 PHE A CA    1 
ATOM   3928  C  CA    B PHE A 1 255 ? -12.645 1.662   40.372  0.80 33.64  ? 255 PHE A CA    1 
ATOM   3929  C  C     A PHE A 1 255 ? -11.553 3.201   40.104  0.20 32.23  ? 255 PHE A C     1 
ATOM   3930  C  C     B PHE A 1 255 ? -11.753 2.889   40.309  0.80 30.76  ? 255 PHE A C     1 
ATOM   3931  O  O     A PHE A 1 255 ? -10.481 3.327   40.706  0.20 33.73  ? 255 PHE A O     1 
ATOM   3932  O  O     B PHE A 1 255 ? -10.803 3.022   41.084  0.80 33.38  ? 255 PHE A O     1 
ATOM   3933  C  CB    A PHE A 1 255 ? -12.172 0.953   39.192  0.20 31.27  ? 255 PHE A CB    1 
ATOM   3934  C  CB    B PHE A 1 255 ? -12.384 0.777   39.150  0.80 31.07  ? 255 PHE A CB    1 
ATOM   3935  C  CG    A PHE A 1 255 ? -12.483 -0.464  39.575  0.20 31.06  ? 255 PHE A CG    1 
ATOM   3936  C  CG    B PHE A 1 255 ? -12.693 -0.674  39.359  0.80 30.90  ? 255 PHE A CG    1 
ATOM   3937  C  CD1   A PHE A 1 255 ? -13.791 -0.918  39.605  0.20 34.19  ? 255 PHE A CD1   1 
ATOM   3938  C  CD1   B PHE A 1 255 ? -13.962 -1.174  39.101  0.80 37.14  ? 255 PHE A CD1   1 
ATOM   3939  C  CD2   A PHE A 1 255 ? -11.466 -1.346  39.897  0.20 32.01  ? 255 PHE A CD2   1 
ATOM   3940  C  CD2   B PHE A 1 255 ? -11.708 -1.551  39.785  0.80 32.20  ? 255 PHE A CD2   1 
ATOM   3941  C  CE1   A PHE A 1 255 ? -14.078 -2.224  39.955  0.20 32.30  ? 255 PHE A CE1   1 
ATOM   3942  C  CE1   B PHE A 1 255 ? -14.248 -2.524  39.284  0.80 34.17  ? 255 PHE A CE1   1 
ATOM   3943  C  CE2   A PHE A 1 255 ? -11.747 -2.654  40.249  0.20 32.67  ? 255 PHE A CE2   1 
ATOM   3944  C  CE2   B PHE A 1 255 ? -11.987 -2.902  39.976  0.80 33.99  ? 255 PHE A CE2   1 
ATOM   3945  C  CZ    A PHE A 1 255 ? -13.053 -3.093  40.277  0.20 32.10  ? 255 PHE A CZ    1 
ATOM   3946  C  CZ    B PHE A 1 255 ? -13.253 -3.389  39.716  0.80 30.29  ? 255 PHE A CZ    1 
ATOM   3947  N  N     A GLN A 1 256 ? -12.004 4.126   39.256  0.20 33.87  ? 256 GLN A N     1 
ATOM   3948  N  N     B GLN A 1 256 ? -12.074 3.816   39.399  0.80 35.11  ? 256 GLN A N     1 
ATOM   3949  C  CA    A GLN A 1 256 ? -11.257 5.361   39.049  0.20 31.21  ? 256 GLN A CA    1 
ATOM   3950  C  CA    B GLN A 1 256 ? -11.273 5.025   39.217  0.80 29.46  ? 256 GLN A CA    1 
ATOM   3951  C  C     A GLN A 1 256 ? -11.369 6.290   40.250  0.20 31.30  ? 256 GLN A C     1 
ATOM   3952  C  C     B GLN A 1 256 ? -11.365 5.935   40.434  0.80 31.85  ? 256 GLN A C     1 
ATOM   3953  O  O     A GLN A 1 256 ? -10.438 7.051   40.531  0.20 31.63  ? 256 GLN A O     1 
ATOM   3954  O  O     B GLN A 1 256 ? -10.337 6.349   40.986  0.80 29.32  ? 256 GLN A O     1 
ATOM   3955  C  CB    A GLN A 1 256 ? -11.747 6.062   37.781  0.20 33.08  ? 256 GLN A CB    1 
ATOM   3956  C  CB    B GLN A 1 256 ? -11.730 5.770   37.956  0.80 33.39  ? 256 GLN A CB    1 
ATOM   3957  C  CG    A GLN A 1 256 ? -10.882 7.229   37.331  0.20 33.48  ? 256 GLN A CG    1 
ATOM   3958  C  CG    B GLN A 1 256 ? -11.976 4.885   36.740  0.80 37.01  ? 256 GLN A CG    1 
ATOM   3959  C  CD    A GLN A 1 256 ? -11.414 7.888   36.076  0.20 34.70  ? 256 GLN A CD    1 
ATOM   3960  C  CD    B GLN A 1 256 ? -12.544 5.657   35.559  0.80 43.38  ? 256 GLN A CD    1 
ATOM   3961  O  OE1   A GLN A 1 256 ? -12.602 7.795   35.771  0.20 36.77  ? 256 GLN A OE1   1 
ATOM   3962  O  OE1   B GLN A 1 256 ? -12.198 6.822   35.334  0.80 42.24  ? 256 GLN A OE1   1 
ATOM   3963  N  NE2   A GLN A 1 256 ? -10.533 8.553   35.335  0.20 34.36  ? 256 GLN A NE2   1 
ATOM   3964  N  NE2   B GLN A 1 256 ? -13.427 5.013   34.800  0.80 38.59  ? 256 GLN A NE2   1 
ATOM   3965  N  N     A THR A 1 257 ? -12.490 6.241   40.973  0.20 31.93  ? 257 THR A N     1 
ATOM   3966  N  N     B THR A 1 257 ? -12.596 6.254   40.862  0.80 31.65  ? 257 THR A N     1 
ATOM   3967  C  CA    A THR A 1 257 ? -12.648 7.104   42.140  0.20 33.34  ? 257 THR A CA    1 
ATOM   3968  C  CA    B THR A 1 257 ? -12.808 7.046   42.073  0.80 33.52  ? 257 THR A CA    1 
ATOM   3969  C  C     A THR A 1 257 ? -11.827 6.596   43.319  0.20 32.42  ? 257 THR A C     1 
ATOM   3970  C  C     B THR A 1 257 ? -11.949 6.543   43.225  0.80 32.23  ? 257 THR A C     1 
ATOM   3971  O  O     A THR A 1 257 ? -11.191 7.385   44.027  0.20 33.99  ? 257 THR A O     1 
ATOM   3972  O  O     B THR A 1 257 ? -11.291 7.327   43.917  0.80 34.03  ? 257 THR A O     1 
ATOM   3973  C  CB    A THR A 1 257 ? -14.125 7.209   42.520  0.20 35.82  ? 257 THR A CB    1 
ATOM   3974  C  CB    B THR A 1 257 ? -14.290 7.012   42.470  0.80 36.52  ? 257 THR A CB    1 
ATOM   3975  O  OG1   A THR A 1 257 ? -14.879 7.673   41.393  0.20 37.35  ? 257 THR A OG1   1 
ATOM   3976  O  OG1   B THR A 1 257 ? -15.075 7.718   41.501  0.80 37.95  ? 257 THR A OG1   1 
ATOM   3977  C  CG2   A THR A 1 257 ? -14.314 8.180   43.681  0.20 38.09  ? 257 THR A CG2   1 
ATOM   3978  C  CG2   B THR A 1 257 ? -14.509 7.637   43.858  0.80 39.81  ? 257 THR A CG2   1 
ATOM   3979  N  N     A ASN A 1 258 ? -11.817 5.281   43.540  0.20 32.23  ? 258 ASN A N     1 
ATOM   3980  N  N     B ASN A 1 258 ? -11.924 5.227   43.428  0.80 31.99  ? 258 ASN A N     1 
ATOM   3981  C  CA    A ASN A 1 258 ? -11.170 4.704   44.712  0.20 32.91  ? 258 ASN A CA    1 
ATOM   3982  C  CA    B ASN A 1 258 ? -11.243 4.669   44.590  0.80 33.00  ? 258 ASN A CA    1 
ATOM   3983  C  C     A ASN A 1 258 ? -9.686  4.425   44.522  0.20 32.08  ? 258 ASN A C     1 
ATOM   3984  C  C     B ASN A 1 258 ? -9.736  4.573   44.388  0.80 31.83  ? 258 ASN A C     1 
ATOM   3985  O  O     A ASN A 1 258 ? -8.979  4.238   45.518  0.20 30.81  ? 258 ASN A O     1 
ATOM   3986  O  O     B ASN A 1 258 ? -8.973  4.792   45.332  0.80 31.66  ? 258 ASN A O     1 
ATOM   3987  C  CB    A ASN A 1 258 ? -11.871 3.402   45.114  0.20 32.67  ? 258 ASN A CB    1 
ATOM   3988  C  CB    B ASN A 1 258 ? -11.822 3.293   44.920  0.80 32.05  ? 258 ASN A CB    1 
ATOM   3989  C  CG    A ASN A 1 258 ? -13.094 3.642   45.970  0.20 34.05  ? 258 ASN A CG    1 
ATOM   3990  C  CG    B ASN A 1 258 ? -13.232 3.378   45.451  0.80 35.58  ? 258 ASN A CG    1 
ATOM   3991  O  OD1   A ASN A 1 258 ? -13.183 4.646   46.675  0.20 31.83  ? 258 ASN A OD1   1 
ATOM   3992  O  OD1   B ASN A 1 258 ? -13.681 4.447   45.865  0.80 32.98  ? 258 ASN A OD1   1 
ATOM   3993  N  ND2   A ASN A 1 258 ? -14.044 2.716   45.918  0.20 35.19  ? 258 ASN A ND2   1 
ATOM   3994  N  ND2   B ASN A 1 258 ? -13.945 2.256   45.435  0.80 35.62  ? 258 ASN A ND2   1 
ATOM   3995  N  N     A LEU A 1 259 ? -9.195  4.383   43.284  0.20 33.53  ? 259 LEU A N     1 
ATOM   3996  N  N     B LEU A 1 259 ? -9.280  4.242   43.181  0.80 33.78  ? 259 LEU A N     1 
ATOM   3997  C  CA    A LEU A 1 259 ? -7.809  4.004   43.035  0.20 32.07  ? 259 LEU A CA    1 
ATOM   3998  C  CA    B LEU A 1 259 ? -7.887  3.858   42.998  0.80 32.22  ? 259 LEU A CA    1 
ATOM   3999  C  C     A LEU A 1 259 ? -7.034  4.964   42.143  0.20 32.34  ? 259 LEU A C     1 
ATOM   4000  C  C     B LEU A 1 259 ? -7.053  4.824   42.162  0.80 32.50  ? 259 LEU A C     1 
ATOM   4001  O  O     A LEU A 1 259 ? -5.798  4.915   42.160  0.20 28.88  ? 259 LEU A O     1 
ATOM   4002  O  O     B LEU A 1 259 ? -5.821  4.733   42.202  0.80 28.29  ? 259 LEU A O     1 
ATOM   4003  C  CB    A LEU A 1 259 ? -7.742  2.601   42.412  0.20 30.95  ? 259 LEU A CB    1 
ATOM   4004  C  CB    B LEU A 1 259 ? -7.810  2.462   42.365  0.80 30.96  ? 259 LEU A CB    1 
ATOM   4005  C  CG    A LEU A 1 259 ? -8.348  1.440   43.209  0.20 31.83  ? 259 LEU A CG    1 
ATOM   4006  C  CG    B LEU A 1 259 ? -8.406  1.292   43.161  0.80 31.88  ? 259 LEU A CG    1 
ATOM   4007  C  CD1   A LEU A 1 259 ? -8.210  0.133   42.440  0.20 32.03  ? 259 LEU A CD1   1 
ATOM   4008  C  CD1   B LEU A 1 259 ? -8.436  0.026   42.310  0.80 32.56  ? 259 LEU A CD1   1 
ATOM   4009  C  CD2   A LEU A 1 259 ? -7.704  1.325   44.579  0.20 32.91  ? 259 LEU A CD2   1 
ATOM   4010  C  CD2   B LEU A 1 259 ? -7.617  1.049   44.429  0.80 33.57  ? 259 LEU A CD2   1 
ATOM   4011  N  N     A VAL A 1 260 ? -7.694  5.828   41.384  0.20 31.86  ? 260 VAL A N     1 
ATOM   4012  N  N     B VAL A 1 260 ? -7.667  5.751   41.436  0.80 31.87  ? 260 VAL A N     1 
ATOM   4013  C  CA    A VAL A 1 260 ? -7.040  6.700   40.418  0.20 32.97  ? 260 VAL A CA    1 
ATOM   4014  C  CA    B VAL A 1 260 ? -6.916  6.620   40.534  0.80 33.12  ? 260 VAL A CA    1 
ATOM   4015  C  C     A VAL A 1 260 ? -7.234  8.145   40.861  0.20 31.35  ? 260 VAL A C     1 
ATOM   4016  C  C     B VAL A 1 260 ? -7.057  8.085   40.937  0.80 30.56  ? 260 VAL A C     1 
ATOM   4017  O  O     A VAL A 1 260 ? -8.257  8.764   40.570  0.20 34.38  ? 260 VAL A O     1 
ATOM   4018  O  O     B VAL A 1 260 ? -7.953  8.778   40.441  0.80 33.26  ? 260 VAL A O     1 
ATOM   4019  C  CB    A VAL A 1 260 ? -7.589  6.474   38.998  0.20 32.21  ? 260 VAL A CB    1 
ATOM   4020  C  CB    B VAL A 1 260 ? -7.354  6.393   39.077  0.80 32.80  ? 260 VAL A CB    1 
ATOM   4021  C  CG1   A VAL A 1 260 ? -6.900  7.393   38.003  0.20 33.50  ? 260 VAL A CG1   1 
ATOM   4022  C  CG1   B VAL A 1 260 ? -6.535  7.257   38.129  0.80 34.04  ? 260 VAL A CG1   1 
ATOM   4023  C  CG2   A VAL A 1 260 ? -7.408  5.019   38.590  0.20 28.87  ? 260 VAL A CG2   1 
ATOM   4024  C  CG2   B VAL A 1 260 ? -7.187  4.917   38.712  0.80 27.46  ? 260 VAL A CG2   1 
ATOM   4025  N  N     A PRO A 1 261 ? -6.261  8.723   41.572  0.20 36.07  ? 261 PRO A N     1 
ATOM   4026  N  N     B PRO A 1 261 ? -6.184  8.605   41.806  0.80 37.14  ? 261 PRO A N     1 
ATOM   4027  C  CA    A PRO A 1 261 ? -6.390  10.143  41.941  0.20 36.35  ? 261 PRO A CA    1 
ATOM   4028  C  CA    B PRO A 1 261 ? -6.307  10.017  42.213  0.80 36.58  ? 261 PRO A CA    1 
ATOM   4029  C  C     A PRO A 1 261 ? -6.146  11.077  40.770  0.20 37.99  ? 261 PRO A C     1 
ATOM   4030  C  C     B PRO A 1 261 ? -6.056  11.001  41.090  0.80 37.97  ? 261 PRO A C     1 
ATOM   4031  O  O     A PRO A 1 261 ? -6.862  12.075  40.614  0.20 40.05  ? 261 PRO A O     1 
ATOM   4032  O  O     B PRO A 1 261 ? -6.619  12.104  41.119  0.80 38.21  ? 261 PRO A O     1 
ATOM   4033  C  CB    A PRO A 1 261 ? -5.333  10.313  43.039  0.20 38.27  ? 261 PRO A CB    1 
ATOM   4034  C  CB    B PRO A 1 261 ? -5.250  10.161  43.320  0.80 38.87  ? 261 PRO A CB    1 
ATOM   4035  C  CG    A PRO A 1 261 ? -4.297  9.288   42.713  0.20 40.29  ? 261 PRO A CG    1 
ATOM   4036  C  CG    B PRO A 1 261 ? -4.295  9.031   43.087  0.80 43.44  ? 261 PRO A CG    1 
ATOM   4037  C  CD    A PRO A 1 261 ? -5.033  8.115   42.113  0.20 37.28  ? 261 PRO A CD    1 
ATOM   4038  C  CD    B PRO A 1 261 ? -5.136  7.903   42.563  0.80 39.85  ? 261 PRO A CD    1 
ATOM   4039  N  N     A TYR A 1 262 ? -5.149  10.779  39.939  0.20 34.95  ? 262 TYR A N     1 
ATOM   4040  N  N     B TYR A 1 262 ? -5.213  10.646  40.117  0.80 34.28  ? 262 TYR A N     1 
ATOM   4041  C  CA    A TYR A 1 262 ? -4.834  11.528  38.739  0.20 36.06  ? 262 TYR A CA    1 
ATOM   4042  C  CA    B TYR A 1 262 ? -4.889  11.480  38.974  0.80 34.94  ? 262 TYR A CA    1 
ATOM   4043  C  C     A TYR A 1 262 ? -4.831  10.597  37.533  0.20 35.82  ? 262 TYR A C     1 
ATOM   4044  C  C     B TYR A 1 262 ? -4.790  10.623  37.720  0.80 35.54  ? 262 TYR A C     1 
ATOM   4045  O  O     A TYR A 1 262 ? -4.430  9.434   37.643  0.20 36.65  ? 262 TYR A O     1 
ATOM   4046  O  O     B TYR A 1 262 ? -4.226  9.518   37.766  0.80 36.68  ? 262 TYR A O     1 
ATOM   4047  C  CB    A TYR A 1 262 ? -3.474  12.228  38.859  0.20 40.03  ? 262 TYR A CB    1 
ATOM   4048  C  CB    B TYR A 1 262 ? -3.580  12.243  39.202  0.80 41.11  ? 262 TYR A CB    1 
ATOM   4049  C  CG    A TYR A 1 262 ? -3.479  13.381  39.836  0.20 42.66  ? 262 TYR A CG    1 
ATOM   4050  C  CG    B TYR A 1 262 ? -3.779  13.343  40.205  0.80 42.86  ? 262 TYR A CG    1 
ATOM   4051  C  CD1   A TYR A 1 262 ? -3.924  14.639  39.450  0.20 41.95  ? 262 TYR A CD1   1 
ATOM   4052  C  CD1   B TYR A 1 262 ? -4.324  14.562  39.818  0.80 42.90  ? 262 TYR A CD1   1 
ATOM   4053  C  CD2   A TYR A 1 262 ? -3.045  13.211  41.144  0.20 41.50  ? 262 TYR A CD2   1 
ATOM   4054  C  CD2   B TYR A 1 262 ? -3.471  13.151  41.544  0.80 42.37  ? 262 TYR A CD2   1 
ATOM   4055  C  CE1   A TYR A 1 262 ? -3.936  15.697  40.340  0.20 41.92  ? 262 TYR A CE1   1 
ATOM   4056  C  CE1   B TYR A 1 262 ? -4.532  15.568  40.729  0.80 43.78  ? 262 TYR A CE1   1 
ATOM   4057  C  CE2   A TYR A 1 262 ? -3.052  14.265  42.041  0.20 43.92  ? 262 TYR A CE2   1 
ATOM   4058  C  CE2   B TYR A 1 262 ? -3.681  14.150  42.467  0.80 43.47  ? 262 TYR A CE2   1 
ATOM   4059  C  CZ    A TYR A 1 262 ? -3.498  15.505  41.632  0.20 43.54  ? 262 TYR A CZ    1 
ATOM   4060  C  CZ    B TYR A 1 262 ? -4.211  15.354  42.052  0.80 46.43  ? 262 TYR A CZ    1 
ATOM   4061  O  OH    A TYR A 1 262 ? -3.511  16.558  42.517  0.20 45.27  ? 262 TYR A OH    1 
ATOM   4062  O  OH    B TYR A 1 262 ? -4.420  16.354  42.961  0.80 46.38  ? 262 TYR A OH    1 
ATOM   4063  N  N     A PRO A 1 263 ? -5.268  11.081  36.367  0.20 35.56  ? 263 PRO A N     1 
ATOM   4064  N  N     B PRO A 1 263 ? -5.280  11.128  36.583  0.80 34.23  ? 263 PRO A N     1 
ATOM   4065  C  CA    A PRO A 1 263 ? -5.440  10.179  35.214  0.20 39.86  ? 263 PRO A CA    1 
ATOM   4066  C  CA    B PRO A 1 263 ? -5.505  10.251  35.415  0.80 41.29  ? 263 PRO A CA    1 
ATOM   4067  C  C     A PRO A 1 263 ? -4.161  9.494   34.760  0.20 35.23  ? 263 PRO A C     1 
ATOM   4068  C  C     B PRO A 1 263 ? -4.281  9.490   34.920  0.80 34.90  ? 263 PRO A C     1 
ATOM   4069  O  O     A PRO A 1 263 ? -4.224  8.350   34.291  0.20 34.62  ? 263 PRO A O     1 
ATOM   4070  O  O     B PRO A 1 263 ? -4.427  8.337   34.494  0.80 34.66  ? 263 PRO A O     1 
ATOM   4071  C  CB    A PRO A 1 263 ? -5.993  11.111  34.125  0.20 39.84  ? 263 PRO A CB    1 
ATOM   4072  C  CB    B PRO A 1 263 ? -6.024  11.226  34.346  0.80 39.78  ? 263 PRO A CB    1 
ATOM   4073  C  CG    A PRO A 1 263 ? -6.579  12.270  34.866  0.20 42.60  ? 263 PRO A CG    1 
ATOM   4074  C  CG    B PRO A 1 263 ? -6.480  12.430  35.089  0.80 43.90  ? 263 PRO A CG    1 
ATOM   4075  C  CD    A PRO A 1 263 ? -5.710  12.454  36.071  0.20 39.26  ? 263 PRO A CD    1 
ATOM   4076  C  CD    B PRO A 1 263 ? -5.606  12.531  36.293  0.80 39.48  ? 263 PRO A CD    1 
ATOM   4077  N  N     A ARG A 1 264 ? -3.003  10.148  34.880  0.20 32.49  ? 264 ARG A N     1 
ATOM   4078  N  N     B ARG A 1 264 ? -3.085  10.088  34.938  0.80 32.46  ? 264 ARG A N     1 
ATOM   4079  C  CA    A ARG A 1 264 ? -1.768  9.542   34.387  0.20 36.47  ? 264 ARG A CA    1 
ATOM   4080  C  CA    B ARG A 1 264 ? -1.933  9.405   34.351  0.80 36.79  ? 264 ARG A CA    1 
ATOM   4081  C  C     A ARG A 1 264 ? -1.337  8.368   35.256  0.20 34.88  ? 264 ARG A C     1 
ATOM   4082  C  C     B ARG A 1 264 ? -1.342  8.349   35.274  0.80 34.79  ? 264 ARG A C     1 
ATOM   4083  O  O     A ARG A 1 264 ? -0.954  7.314   34.737  0.20 35.90  ? 264 ARG A O     1 
ATOM   4084  O  O     B ARG A 1 264 ? -0.790  7.359   34.791  0.80 36.58  ? 264 ARG A O     1 
ATOM   4085  C  CB    A ARG A 1 264 ? -0.656  10.589  34.310  0.20 34.37  ? 264 ARG A CB    1 
ATOM   4086  C  CB    B ARG A 1 264 ? -0.844  10.413  33.957  0.80 35.29  ? 264 ARG A CB    1 
ATOM   4087  C  CG    A ARG A 1 264 ? -0.919  11.693  33.299  0.20 33.93  ? 264 ARG A CG    1 
ATOM   4088  C  CG    B ARG A 1 264 ? -1.038  11.011  32.565  0.80 35.55  ? 264 ARG A CG    1 
ATOM   4089  C  CD    A ARG A 1 264 ? 0.275   12.625  33.158  0.20 31.46  ? 264 ARG A CD    1 
ATOM   4090  C  CD    B ARG A 1 264 ? -0.110  12.205  32.323  0.80 31.35  ? 264 ARG A CD    1 
ATOM   4091  N  NE    A ARG A 1 264 ? 1.451   11.930  32.648  0.20 31.31  ? 264 ARG A NE    1 
ATOM   4092  N  NE    B ARG A 1 264 ? 1.297   11.844  32.415  0.80 31.21  ? 264 ARG A NE    1 
ATOM   4093  C  CZ    A ARG A 1 264 ? 1.663   11.661  31.367  0.20 32.33  ? 264 ARG A CZ    1 
ATOM   4094  C  CZ    B ARG A 1 264 ? 2.031   11.458  31.381  0.80 32.28  ? 264 ARG A CZ    1 
ATOM   4095  N  NH1   A ARG A 1 264 ? 0.789   12.003  30.435  0.20 32.79  ? 264 ARG A NH1   1 
ATOM   4096  N  NH1   B ARG A 1 264 ? 1.523   11.387  30.167  0.80 28.63  ? 264 ARG A NH1   1 
ATOM   4097  N  NH2   A ARG A 1 264 ? 2.779   11.031  31.012  0.20 32.93  ? 264 ARG A NH2   1 
ATOM   4098  N  NH2   B ARG A 1 264 ? 3.306   11.126  31.574  0.80 33.87  ? 264 ARG A NH2   1 
ATOM   4099  N  N     A ILE A 1 265 ? -1.390  8.527   36.577  0.20 35.26  ? 265 ILE A N     1 
ATOM   4100  N  N     B ILE A 1 265 ? -1.440  8.529   36.588  0.80 35.66  ? 265 ILE A N     1 
ATOM   4101  C  CA    A ILE A 1 265 ? -0.963  7.476   37.502  0.20 35.48  ? 265 ILE A CA    1 
ATOM   4102  C  CA    B ILE A 1 265 ? -0.895  7.540   37.508  0.80 35.55  ? 265 ILE A CA    1 
ATOM   4103  C  C     A ILE A 1 265 ? -2.191  6.611   37.774  0.20 29.82  ? 265 ILE A C     1 
ATOM   4104  C  C     B ILE A 1 265 ? -1.983  6.516   37.811  0.80 28.93  ? 265 ILE A C     1 
ATOM   4105  O  O     A ILE A 1 265 ? -2.946  6.830   38.723  0.20 30.34  ? 265 ILE A O     1 
ATOM   4106  O  O     B ILE A 1 265 ? -2.418  6.368   38.959  0.80 30.55  ? 265 ILE A O     1 
ATOM   4107  C  CB    A ILE A 1 265 ? -0.345  8.051   38.774  0.20 37.45  ? 265 ILE A CB    1 
ATOM   4108  C  CB    B ILE A 1 265 ? -0.358  8.212   38.782  0.80 38.08  ? 265 ILE A CB    1 
ATOM   4109  C  CG1   A ILE A 1 265 ? -1.141  9.264   39.260  0.20 34.52  ? 265 ILE A CG1   1 
ATOM   4110  C  CG1   B ILE A 1 265 ? -1.396  9.191   39.333  0.80 33.41  ? 265 ILE A CG1   1 
ATOM   4111  C  CG2   A ILE A 1 265 ? 1.103   8.444   38.520  0.20 34.04  ? 265 ILE A CG2   1 
ATOM   4112  C  CG2   B ILE A 1 265 ? 0.951   8.928   38.468  0.80 35.05  ? 265 ILE A CG2   1 
ATOM   4113  C  CD1   A ILE A 1 265 ? -0.520  9.962   40.448  0.20 42.64  ? 265 ILE A CD1   1 
ATOM   4114  C  CD1   B ILE A 1 265 ? -0.988  9.880   40.614  0.80 45.83  ? 265 ILE A CD1   1 
ATOM   4115  N  N     A HIS A 1 266 ? -2.394  5.610   36.920  0.20 26.23  ? 266 HIS A N     1 
ATOM   4116  N  N     B HIS A 1 266 ? -2.432  5.801   36.776  0.80 25.04  ? 266 HIS A N     1 
ATOM   4117  C  CA    A HIS A 1 266 ? -3.547  4.724   37.017  0.20 27.97  ? 266 HIS A CA    1 
ATOM   4118  C  CA    B HIS A 1 266 ? -3.608  4.943   36.866  0.80 27.74  ? 266 HIS A CA    1 
ATOM   4119  C  C     A HIS A 1 266 ? -3.115  3.266   36.981  0.20 24.85  ? 266 HIS A C     1 
ATOM   4120  C  C     B HIS A 1 266 ? -3.235  3.466   36.851  0.80 23.66  ? 266 HIS A C     1 
ATOM   4121  O  O     A HIS A 1 266 ? -3.770  2.420   36.369  0.20 28.23  ? 266 HIS A O     1 
ATOM   4122  O  O     B HIS A 1 266 ? -3.929  2.646   36.254  0.80 28.08  ? 266 HIS A O     1 
ATOM   4123  C  CB    A HIS A 1 266 ? -4.565  5.019   35.915  0.20 27.11  ? 266 HIS A CB    1 
ATOM   4124  C  CB    B HIS A 1 266 ? -4.625  5.268   35.765  0.80 26.42  ? 266 HIS A CB    1 
ATOM   4125  C  CG    A HIS A 1 266 ? -4.006  4.961   34.524  0.20 32.24  ? 266 HIS A CG    1 
ATOM   4126  C  CG    B HIS A 1 266 ? -4.147  5.049   34.353  0.80 33.74  ? 266 HIS A CG    1 
ATOM   4127  N  ND1   A HIS A 1 266 ? -4.038  6.040   33.666  0.20 29.74  ? 266 HIS A ND1   1 
ATOM   4128  N  ND1   B HIS A 1 266 ? -4.203  6.039   33.392  0.80 28.36  ? 266 HIS A ND1   1 
ATOM   4129  C  CD2   A HIS A 1 266 ? -3.428  3.950   33.833  0.20 28.01  ? 266 HIS A CD2   1 
ATOM   4130  C  CD2   B HIS A 1 266 ? -3.688  3.941   33.721  0.80 27.81  ? 266 HIS A CD2   1 
ATOM   4131  C  CE1   A HIS A 1 266 ? -3.493  5.700   32.512  0.20 31.44  ? 266 HIS A CE1   1 
ATOM   4132  C  CE1   B HIS A 1 266 ? -3.753  5.563   32.243  0.80 32.02  ? 266 HIS A CE1   1 
ATOM   4133  N  NE2   A HIS A 1 266 ? -3.116  4.436   32.587  0.20 31.27  ? 266 HIS A NE2   1 
ATOM   4134  N  NE2   B HIS A 1 266 ? -3.450  4.288   32.413  0.80 31.24  ? 266 HIS A NE2   1 
ATOM   4135  N  N     A PHE A 1 267 ? -2.012  2.945   37.661  0.20 24.81  ? 267 PHE A N     1 
ATOM   4136  N  N     B PHE A 1 267 ? -2.167  3.108   37.565  0.80 23.74  ? 267 PHE A N     1 
ATOM   4137  C  CA    A PHE A 1 267 ? -1.457  1.593   37.696  0.20 26.49  ? 267 PHE A CA    1 
ATOM   4138  C  CA    B PHE A 1 267 ? -1.622  1.751   37.584  0.80 25.91  ? 267 PHE A CA    1 
ATOM   4139  C  C     A PHE A 1 267 ? -1.368  1.141   39.150  0.20 26.44  ? 267 PHE A C     1 
ATOM   4140  C  C     B PHE A 1 267 ? -1.608  1.240   39.018  0.80 26.17  ? 267 PHE A C     1 
ATOM   4141  O  O     A PHE A 1 267 ? -0.306  1.248   39.784  0.20 26.87  ? 267 PHE A O     1 
ATOM   4142  O  O     B PHE A 1 267 ? -0.599  1.360   39.735  0.80 26.98  ? 267 PHE A O     1 
ATOM   4143  C  CB    A PHE A 1 267 ? -0.094  1.535   37.011  0.20 24.95  ? 267 PHE A CB    1 
ATOM   4144  C  CB    B PHE A 1 267 ? -0.229  1.708   36.970  0.80 24.36  ? 267 PHE A CB    1 
ATOM   4145  C  CG    A PHE A 1 267 ? -0.107  2.041   35.595  0.20 29.30  ? 267 PHE A CG    1 
ATOM   4146  C  CG    B PHE A 1 267 ? -0.188  2.209   35.554  0.80 29.72  ? 267 PHE A CG    1 
ATOM   4147  C  CD1   A PHE A 1 267 ? -0.440  1.197   34.545  0.20 26.75  ? 267 PHE A CD1   1 
ATOM   4148  C  CD1   B PHE A 1 267 ? -0.535  1.372   34.497  0.80 26.30  ? 267 PHE A CD1   1 
ATOM   4149  C  CD2   A PHE A 1 267 ? 0.211   3.361   35.314  0.20 28.98  ? 267 PHE A CD2   1 
ATOM   4150  C  CD2   B PHE A 1 267 ? 0.179   3.522   35.279  0.80 28.99  ? 267 PHE A CD2   1 
ATOM   4151  C  CE1   A PHE A 1 267 ? -0.453  1.661   33.240  0.20 25.81  ? 267 PHE A CE1   1 
ATOM   4152  C  CE1   B PHE A 1 267 ? -0.501  1.832   33.186  0.80 25.32  ? 267 PHE A CE1   1 
ATOM   4153  C  CE2   A PHE A 1 267 ? 0.198   3.830   34.011  0.20 29.44  ? 267 PHE A CE2   1 
ATOM   4154  C  CE2   B PHE A 1 267 ? 0.207   3.983   33.974  0.80 29.53  ? 267 PHE A CE2   1 
ATOM   4155  C  CZ    A PHE A 1 267 ? -0.134  2.979   32.974  0.20 28.21  ? 267 PHE A CZ    1 
ATOM   4156  C  CZ    B PHE A 1 267 ? -0.134  3.141   32.929  0.80 28.08  ? 267 PHE A CZ    1 
ATOM   4157  N  N     A PRO A 1 268 ? -2.463  0.639   39.712  0.20 27.54  ? 268 PRO A N     1 
ATOM   4158  N  N     B PRO A 1 268 ? -2.706  0.659   39.469  0.80 27.59  ? 268 PRO A N     1 
ATOM   4159  C  CA    A PRO A 1 268 ? -2.429  0.138   41.092  0.20 27.78  ? 268 PRO A CA    1 
ATOM   4160  C  CA    B PRO A 1 268 ? -2.758  0.113   40.828  0.80 28.31  ? 268 PRO A CA    1 
ATOM   4161  C  C     A PRO A 1 268 ? -1.590  -1.128  41.202  0.20 26.93  ? 268 PRO A C     1 
ATOM   4162  C  C     B PRO A 1 268 ? -2.047  -1.228  40.947  0.80 27.71  ? 268 PRO A C     1 
ATOM   4163  O  O     A PRO A 1 268 ? -1.249  -1.781  40.214  0.20 26.83  ? 268 PRO A O     1 
ATOM   4164  O  O     B PRO A 1 268 ? -1.896  -1.983  39.981  0.80 27.34  ? 268 PRO A O     1 
ATOM   4165  C  CB    A PRO A 1 268 ? -3.902  -0.141  41.409  0.20 27.15  ? 268 PRO A CB    1 
ATOM   4166  C  CB    B PRO A 1 268 ? -4.259  -0.022  41.099  0.80 27.22  ? 268 PRO A CB    1 
ATOM   4167  C  CG    A PRO A 1 268 ? -4.679  0.640   40.386  0.20 24.42  ? 268 PRO A CG    1 
ATOM   4168  C  CG    B PRO A 1 268 ? -4.912  -0.069  39.763  0.80 32.01  ? 268 PRO A CG    1 
ATOM   4169  C  CD    A PRO A 1 268 ? -3.824  0.632   39.156  0.20 27.67  ? 268 PRO A CD    1 
ATOM   4170  C  CD    B PRO A 1 268 ? -3.984  0.554   38.746  0.80 25.78  ? 268 PRO A CD    1 
ATOM   4171  N  N     A LEU A 1 269 ? -1.262  -1.471  42.446  0.20 26.02  ? 269 LEU A N     1 
ATOM   4172  N  N     B LEU A 1 269 ? -1.593  -1.502  42.166  0.80 26.38  ? 269 LEU A N     1 
ATOM   4173  C  CA    A LEU A 1 269 ? -0.469  -2.651  42.769  0.20 26.32  ? 269 LEU A CA    1 
ATOM   4174  C  CA    B LEU A 1 269 ? -0.882  -2.726  42.502  0.80 29.31  ? 269 LEU A CA    1 
ATOM   4175  C  C     A LEU A 1 269 ? -1.350  -3.655  43.501  0.20 28.06  ? 269 LEU A C     1 
ATOM   4176  C  C     B LEU A 1 269 ? -1.849  -3.719  43.134  0.80 29.17  ? 269 LEU A C     1 
ATOM   4177  O  O     A LEU A 1 269 ? -1.894  -3.346  44.568  0.20 25.20  ? 269 LEU A O     1 
ATOM   4178  O  O     B LEU A 1 269 ? -2.630  -3.353  44.025  0.80 28.24  ? 269 LEU A O     1 
ATOM   4179  C  CB    A LEU A 1 269 ? 0.740   -2.273  43.623  0.20 25.74  ? 269 LEU A CB    1 
ATOM   4180  C  CB    B LEU A 1 269 ? 0.262   -2.412  43.457  0.80 22.76  ? 269 LEU A CB    1 
ATOM   4181  C  CG    A LEU A 1 269 ? 1.570   -3.423  44.187  0.20 27.17  ? 269 LEU A CG    1 
ATOM   4182  C  CG    B LEU A 1 269 ? 1.179   -3.517  43.950  0.80 23.29  ? 269 LEU A CG    1 
ATOM   4183  C  CD1   A LEU A 1 269 ? 2.321   -4.148  43.078  0.20 30.81  ? 269 LEU A CD1   1 
ATOM   4184  C  CD1   B LEU A 1 269 ? 1.881   -4.196  42.777  0.80 32.99  ? 269 LEU A CD1   1 
ATOM   4185  C  CD2   A LEU A 1 269 ? 2.527   -2.904  45.249  0.20 33.10  ? 269 LEU A CD2   1 
ATOM   4186  C  CD2   B LEU A 1 269 ? 2.185   -2.900  44.901  0.80 33.75  ? 269 LEU A CD2   1 
ATOM   4187  N  N     A ALA A 1 270 ? -1.487  -4.850  42.934  0.20 26.36  ? 270 ALA A N     1 
ATOM   4188  N  N     B ALA A 1 270 ? -1.796  -4.970  42.687  0.80 25.94  ? 270 ALA A N     1 
ATOM   4189  C  CA    A ALA A 1 270 ? -2.329  -5.894  43.506  0.20 23.95  ? 270 ALA A CA    1 
ATOM   4190  C  CA    B ALA A 1 270 ? -2.595  -6.039  43.278  0.80 23.17  ? 270 ALA A CA    1 
ATOM   4191  C  C     A ALA A 1 270 ? -1.475  -6.893  44.276  0.20 26.81  ? 270 ALA A C     1 
ATOM   4192  C  C     B ALA A 1 270 ? -1.700  -6.958  44.100  0.80 26.45  ? 270 ALA A C     1 
ATOM   4193  O  O     A ALA A 1 270 ? -0.444  -7.356  43.776  0.20 26.70  ? 270 ALA A O     1 
ATOM   4194  O  O     B ALA A 1 270 ? -0.616  -7.349  43.649  0.80 26.33  ? 270 ALA A O     1 
ATOM   4195  C  CB    A ALA A 1 270 ? -3.127  -6.612  42.416  0.20 26.21  ? 270 ALA A CB    1 
ATOM   4196  C  CB    B ALA A 1 270 ? -3.326  -6.849  42.200  0.80 24.32  ? 270 ALA A CB    1 
ATOM   4197  N  N     A THR A 1 271 ? -1.907  -7.218  45.492  0.20 24.90  ? 271 THR A N     1 
ATOM   4198  N  N     B THR A 1 271 ? -2.153  -7.297  45.302  0.80 23.76  ? 271 THR A N     1 
ATOM   4199  C  CA    A THR A 1 271 ? -1.270  -8.230  46.323  0.20 27.98  ? 271 THR A CA    1 
ATOM   4200  C  CA    B THR A 1 271 ? -1.522  -8.314  46.130  0.80 27.67  ? 271 THR A CA    1 
ATOM   4201  C  C     A THR A 1 271 ? -2.336  -9.221  46.764  0.20 26.75  ? 271 THR A C     1 
ATOM   4202  C  C     B THR A 1 271 ? -2.583  -9.343  46.508  0.80 26.10  ? 271 THR A C     1 
ATOM   4203  O  O     A THR A 1 271 ? -3.387  -8.814  47.266  0.20 27.20  ? 271 THR A O     1 
ATOM   4204  O  O     B THR A 1 271 ? -3.766  -9.015  46.610  0.80 29.68  ? 271 THR A O     1 
ATOM   4205  C  CB    A THR A 1 271 ? -0.589  -7.606  47.548  0.20 32.46  ? 271 THR A CB    1 
ATOM   4206  C  CB    B THR A 1 271 ? -0.886  -7.701  47.393  0.80 34.23  ? 271 THR A CB    1 
ATOM   4207  O  OG1   A THR A 1 271 ? 0.337   -6.596  47.125  0.20 32.86  ? 271 THR A OG1   1 
ATOM   4208  O  OG1   B THR A 1 271 ? -0.240  -6.466  47.058  0.80 32.54  ? 271 THR A OG1   1 
ATOM   4209  C  CG2   A THR A 1 271 ? 0.151   -8.667  48.348  0.20 33.35  ? 271 THR A CG2   1 
ATOM   4210  C  CG2   B THR A 1 271 ? 0.137   -8.646  47.987  0.80 34.64  ? 271 THR A CG2   1 
ATOM   4211  N  N     A TYR A 1 272 ? -2.071  -10.512 46.573  0.20 30.21  ? 272 TYR A N     1 
ATOM   4212  N  N     B TYR A 1 272 ? -2.168  -10.599 46.693  0.80 30.64  ? 272 TYR A N     1 
ATOM   4213  C  CA    A TYR A 1 272 ? -3.032  -11.564 46.876  0.20 31.94  ? 272 TYR A CA    1 
ATOM   4214  C  CA    B TYR A 1 272 ? -3.129  -11.686 46.875  0.80 32.38  ? 272 TYR A CA    1 
ATOM   4215  C  C     A TYR A 1 272 ? -2.499  -12.461 47.987  0.20 26.72  ? 272 TYR A C     1 
ATOM   4216  C  C     B TYR A 1 272 ? -2.566  -12.733 47.835  0.80 26.09  ? 272 TYR A C     1 
ATOM   4217  O  O     A TYR A 1 272 ? -1.286  -12.584 48.181  0.20 29.13  ? 272 TYR A O     1 
ATOM   4218  O  O     B TYR A 1 272 ? -1.404  -13.122 47.724  0.80 26.71  ? 272 TYR A O     1 
ATOM   4219  C  CB    A TYR A 1 272 ? -3.349  -12.407 45.623  0.20 31.94  ? 272 TYR A CB    1 
ATOM   4220  C  CB    B TYR A 1 272 ? -3.479  -12.328 45.516  0.80 32.51  ? 272 TYR A CB    1 
ATOM   4221  C  CG    A TYR A 1 272 ? -4.437  -13.436 45.841  0.20 29.40  ? 272 TYR A CG    1 
ATOM   4222  C  CG    B TYR A 1 272 ? -4.503  -13.435 45.592  0.80 28.10  ? 272 TYR A CG    1 
ATOM   4223  C  CD1   A TYR A 1 272 ? -5.779  -13.087 45.753  0.20 31.55  ? 272 TYR A CD1   1 
ATOM   4224  C  CD1   B TYR A 1 272 ? -5.866  -13.155 45.550  0.80 32.02  ? 272 TYR A CD1   1 
ATOM   4225  C  CD2   A TYR A 1 272 ? -4.122  -14.755 46.146  0.20 30.29  ? 272 TYR A CD2   1 
ATOM   4226  C  CD2   B TYR A 1 272 ? -4.110  -14.757 45.730  0.80 29.27  ? 272 TYR A CD2   1 
ATOM   4227  C  CE1   A TYR A 1 272 ? -6.778  -14.022 45.962  0.20 28.36  ? 272 TYR A CE1   1 
ATOM   4228  C  CE1   B TYR A 1 272 ? -6.811  -14.161 45.642  0.80 27.25  ? 272 TYR A CE1   1 
ATOM   4229  C  CE2   A TYR A 1 272 ? -5.112  -15.695 46.359  0.20 31.03  ? 272 TYR A CE2   1 
ATOM   4230  C  CE2   B TYR A 1 272 ? -5.041  -15.773 45.820  0.80 31.00  ? 272 TYR A CE2   1 
ATOM   4231  C  CZ    A TYR A 1 272 ? -6.438  -15.323 46.265  0.20 31.19  ? 272 TYR A CZ    1 
ATOM   4232  C  CZ    B TYR A 1 272 ? -6.392  -15.466 45.779  0.80 34.43  ? 272 TYR A CZ    1 
ATOM   4233  O  OH    A TYR A 1 272 ? -7.425  -16.256 46.473  0.20 33.08  ? 272 TYR A OH    1 
ATOM   4234  O  OH    B TYR A 1 272 ? -7.313  -16.474 45.862  0.80 37.65  ? 272 TYR A OH    1 
ATOM   4235  N  N     A ALA A 1 273 ? -3.423  -13.090 48.718  0.20 29.93  ? 273 ALA A N     1 
ATOM   4236  N  N     B ALA A 1 273 ? -3.408  -13.223 48.748  0.80 30.07  ? 273 ALA A N     1 
ATOM   4237  C  CA    A ALA A 1 273 ? -3.091  -14.014 49.796  0.20 29.32  ? 273 ALA A CA    1 
ATOM   4238  C  CA    B ALA A 1 273 ? -2.972  -14.171 49.765  0.80 29.33  ? 273 ALA A CA    1 
ATOM   4239  C  C     A ALA A 1 273 ? -4.331  -14.798 50.211  0.20 26.05  ? 273 ALA A C     1 
ATOM   4240  C  C     B ALA A 1 273 ? -4.183  -14.923 50.288  0.80 25.38  ? 273 ALA A C     1 
ATOM   4241  O  O     A ALA A 1 273 ? -5.436  -14.243 50.227  0.20 29.18  ? 273 ALA A O     1 
ATOM   4242  O  O     B ALA A 1 273 ? -5.281  -14.359 50.334  0.80 29.87  ? 273 ALA A O     1 
ATOM   4243  C  CB    A ALA A 1 273 ? -2.515  -13.265 50.999  0.20 26.21  ? 273 ALA A CB    1 
ATOM   4244  C  CB    B ALA A 1 273 ? -2.262  -13.459 50.928  0.80 24.86  ? 273 ALA A CB    1 
ATOM   4245  N  N     A PRO A 1 274 ? -4.192  -16.083 50.559  0.20 26.97  ? 274 PRO A N     1 
ATOM   4246  N  N     B PRO A 1 274 ? -4.018  -16.187 50.697  0.80 26.56  ? 274 PRO A N     1 
ATOM   4247  C  CA    A PRO A 1 274 ? -2.965  -16.880 50.579  0.20 24.99  ? 274 PRO A CA    1 
ATOM   4248  C  CA    B PRO A 1 274 ? -2.803  -16.990 50.619  0.80 24.51  ? 274 PRO A CA    1 
ATOM   4249  C  C     A PRO A 1 274 ? -2.811  -17.758 49.345  0.20 29.09  ? 274 PRO A C     1 
ATOM   4250  C  C     B PRO A 1 274 ? -2.783  -17.800 49.345  0.80 29.24  ? 274 PRO A C     1 
ATOM   4251  O  O     A PRO A 1 274 ? -3.789  -18.118 48.697  0.20 28.66  ? 274 PRO A O     1 
ATOM   4252  O  O     B PRO A 1 274 ? -3.826  -18.138 48.806  0.80 28.62  ? 274 PRO A O     1 
ATOM   4253  C  CB    A PRO A 1 274 ? -3.136  -17.715 51.852  0.20 27.74  ? 274 PRO A CB    1 
ATOM   4254  C  CB    B PRO A 1 274 ? -2.906  -17.880 51.855  0.80 27.31  ? 274 PRO A CB    1 
ATOM   4255  C  CG    A PRO A 1 274 ? -4.654  -17.878 52.013  0.20 28.96  ? 274 PRO A CG    1 
ATOM   4256  C  CG    B PRO A 1 274 ? -4.392  -18.170 51.922  0.80 29.38  ? 274 PRO A CG    1 
ATOM   4257  C  CD    A PRO A 1 274 ? -5.321  -16.848 51.114  0.20 27.81  ? 274 PRO A CD    1 
ATOM   4258  C  CD    B PRO A 1 274 ? -5.083  -16.906 51.424  0.80 27.95  ? 274 PRO A CD    1 
ATOM   4259  N  N     A VAL A 1 275 ? -1.577  -18.113 49.001  0.20 28.82  ? 275 VAL A N     1 
ATOM   4260  N  N     B VAL A 1 275 ? -1.585  -18.091 48.843  0.80 28.82  ? 275 VAL A N     1 
ATOM   4261  C  CA    A VAL A 1 275 ? -1.281  -18.997 47.880  0.20 26.87  ? 275 VAL A CA    1 
ATOM   4262  C  CA    B VAL A 1 275 ? -1.376  -19.012 47.735  0.80 26.19  ? 275 VAL A CA    1 
ATOM   4263  C  C     A VAL A 1 275 ? -0.670  -20.266 48.458  0.20 30.00  ? 275 VAL A C     1 
ATOM   4264  C  C     B VAL A 1 275 ? -0.797  -20.290 48.328  0.80 30.19  ? 275 VAL A C     1 
ATOM   4265  O  O     A VAL A 1 275 ? 0.470   -20.255 48.937  0.20 29.83  ? 275 VAL A O     1 
ATOM   4266  O  O     B VAL A 1 275 ? 0.299   -20.274 48.900  0.80 29.42  ? 275 VAL A O     1 
ATOM   4267  C  CB    A VAL A 1 275 ? -0.341  -18.335 46.865  0.20 29.10  ? 275 VAL A CB    1 
ATOM   4268  C  CB    B VAL A 1 275 ? -0.439  -18.404 46.680  0.80 29.00  ? 275 VAL A CB    1 
ATOM   4269  C  CG1   A VAL A 1 275 ? -0.038  -19.291 45.727  0.20 28.29  ? 275 VAL A CG1   1 
ATOM   4270  C  CG1   B VAL A 1 275 ? -0.176  -19.393 45.577  0.80 28.10  ? 275 VAL A CG1   1 
ATOM   4271  C  CG2   A VAL A 1 275 ? -0.955  -17.045 46.344  0.20 30.28  ? 275 VAL A CG2   1 
ATOM   4272  C  CG2   B VAL A 1 275 ? -1.039  -17.118 46.137  0.80 30.93  ? 275 VAL A CG2   1 
ATOM   4273  N  N     A ILE A 1 276 ? -1.424  -21.362 48.418  0.20 27.73  ? 276 ILE A N     1 
ATOM   4274  N  N     B ILE A 1 276 ? -1.532  -21.394 48.220  0.80 26.77  ? 276 ILE A N     1 
ATOM   4275  C  CA    A ILE A 1 276 ? -1.013  -22.622 49.022  0.20 31.93  ? 276 ILE A CA    1 
ATOM   4276  C  CA    B ILE A 1 276 ? -1.160  -22.632 48.893  0.80 32.29  ? 276 ILE A CA    1 
ATOM   4277  C  C     A ILE A 1 276 ? -1.095  -23.720 47.972  0.20 31.39  ? 276 ILE A C     1 
ATOM   4278  C  C     B ILE A 1 276 ? -1.266  -23.783 47.906  0.80 31.22  ? 276 ILE A C     1 
ATOM   4279  O  O     A ILE A 1 276 ? -2.061  -23.787 47.205  0.20 33.38  ? 276 ILE A O     1 
ATOM   4280  O  O     B ILE A 1 276 ? -2.256  -23.892 47.175  0.80 34.00  ? 276 ILE A O     1 
ATOM   4281  C  CB    A ILE A 1 276 ? -1.885  -22.969 50.249  0.20 29.63  ? 276 ILE A CB    1 
ATOM   4282  C  CB    B ILE A 1 276 ? -2.041  -22.879 50.134  0.80 29.15  ? 276 ILE A CB    1 
ATOM   4283  C  CG1   A ILE A 1 276 ? -1.804  -21.852 51.290  0.20 29.60  ? 276 ILE A CG1   1 
ATOM   4284  C  CG1   B ILE A 1 276 ? -1.869  -21.725 51.122  0.80 28.83  ? 276 ILE A CG1   1 
ATOM   4285  C  CG2   A ILE A 1 276 ? -1.461  -24.298 50.857  0.20 31.93  ? 276 ILE A CG2   1 
ATOM   4286  C  CG2   B ILE A 1 276 ? -1.708  -24.217 50.781  0.80 31.07  ? 276 ILE A CG2   1 
ATOM   4287  C  CD1   A ILE A 1 276 ? -2.687  -22.081 52.507  0.20 29.87  ? 276 ILE A CD1   1 
ATOM   4288  C  CD1   B ILE A 1 276 ? -2.856  -21.761 52.300  0.80 27.95  ? 276 ILE A CD1   1 
ATOM   4289  N  N     A SER A 1 277 ? -0.075  -24.574 47.934  0.20 31.36  ? 277 SER A N     1 
ATOM   4290  N  N     B SER A 1 277 ? -0.242  -24.631 47.874  0.80 31.05  ? 277 SER A N     1 
ATOM   4291  C  CA    A SER A 1 277 ? -0.056  -25.680 46.988  0.20 34.12  ? 277 SER A CA    1 
ATOM   4292  C  CA    B SER A 1 277 ? -0.222  -25.739 46.929  0.80 34.10  ? 277 SER A CA    1 
ATOM   4293  C  C     A SER A 1 277 ? -1.217  -26.634 47.246  0.20 36.16  ? 277 SER A C     1 
ATOM   4294  C  C     B SER A 1 277 ? -1.351  -26.723 47.210  0.80 36.68  ? 277 SER A C     1 
ATOM   4295  O  O     A SER A 1 277 ? -1.638  -26.843 48.387  0.20 31.77  ? 277 SER A O     1 
ATOM   4296  O  O     B SER A 1 277 ? -1.618  -27.072 48.363  0.80 30.58  ? 277 SER A O     1 
ATOM   4297  C  CB    A SER A 1 277 ? 1.270   -26.435 47.081  0.20 34.04  ? 277 SER A CB    1 
ATOM   4298  C  CB    B SER A 1 277 ? 1.123   -26.464 46.994  0.80 33.79  ? 277 SER A CB    1 
ATOM   4299  O  OG    A SER A 1 277 ? 1.237   -27.614 46.298  0.20 35.08  ? 277 SER A OG    1 
ATOM   4300  O  OG    B SER A 1 277 ? 1.023   -27.733 46.379  0.80 34.69  ? 277 SER A OG    1 
ATOM   4301  N  N     A ALA A 1 278 ? -1.733  -27.221 46.163  0.20 34.38  ? 278 ALA A N     1 
ATOM   4302  N  N     B ALA A 1 278 ? -2.001  -27.185 46.139  0.80 33.17  ? 278 ALA A N     1 
ATOM   4303  C  CA    A ALA A 1 278 ? -2.832  -28.172 46.262  0.20 34.26  ? 278 ALA A CA    1 
ATOM   4304  C  CA    B ALA A 1 278 ? -3.032  -28.206 46.248  0.80 34.08  ? 278 ALA A CA    1 
ATOM   4305  C  C     A ALA A 1 278 ? -2.428  -29.480 46.928  0.20 36.76  ? 278 ALA A C     1 
ATOM   4306  C  C     B ALA A 1 278 ? -2.522  -29.507 46.858  0.80 36.70  ? 278 ALA A C     1 
ATOM   4307  O  O     A ALA A 1 278 ? -3.309  -30.246 47.328  0.20 34.93  ? 278 ALA A O     1 
ATOM   4308  O  O     B ALA A 1 278 ? -3.336  -30.363 47.210  0.80 34.11  ? 278 ALA A O     1 
ATOM   4309  C  CB    A ALA A 1 278 ? -3.407  -28.457 44.874  0.20 35.16  ? 278 ALA A CB    1 
ATOM   4310  C  CB    B ALA A 1 278 ? -3.641  -28.484 44.872  0.80 34.79  ? 278 ALA A CB    1 
ATOM   4311  N  N     A GLU A 1 279 ? -1.130  -29.755 47.062  0.20 39.21  ? 279 GLU A N     1 
ATOM   4312  N  N     B GLU A 1 279 ? -1.210  -29.696 46.982  0.80 39.05  ? 279 GLU A N     1 
ATOM   4313  C  CA    A GLU A 1 279 ? -0.691  -30.967 47.744  0.20 43.99  ? 279 GLU A CA    1 
ATOM   4314  C  CA    B GLU A 1 279 ? -0.715  -30.870 47.689  0.80 44.25  ? 279 GLU A CA    1 
ATOM   4315  C  C     A GLU A 1 279 ? -0.835  -30.878 49.258  0.20 40.25  ? 279 GLU A C     1 
ATOM   4316  C  C     B GLU A 1 279 ? -0.809  -30.719 49.203  0.80 40.09  ? 279 GLU A C     1 
ATOM   4317  O  O     A GLU A 1 279 ? -0.525  -31.854 49.946  0.20 41.19  ? 279 GLU A O     1 
ATOM   4318  O  O     B GLU A 1 279 ? -0.647  -31.709 49.920  0.80 40.74  ? 279 GLU A O     1 
ATOM   4319  C  CB    A GLU A 1 279 ? 0.762   -31.278 47.377  0.20 42.45  ? 279 GLU A CB    1 
ATOM   4320  C  CB    B GLU A 1 279 ? 0.729   -31.167 47.281  0.80 42.12  ? 279 GLU A CB    1 
ATOM   4321  C  CG    A GLU A 1 279 ? 0.995   -31.504 45.889  0.20 49.65  ? 279 GLU A CG    1 
ATOM   4322  C  CG    B GLU A 1 279 ? 0.920   -31.362 45.777  0.80 49.53  ? 279 GLU A CG    1 
ATOM   4323  C  CD    A GLU A 1 279 ? 0.374   -32.794 45.382  0.20 60.25  ? 279 GLU A CD    1 
ATOM   4324  C  CD    B GLU A 1 279 ? 0.407   -32.709 45.283  0.80 61.05  ? 279 GLU A CD    1 
ATOM   4325  O  OE1   A GLU A 1 279 ? 0.113   -33.697 46.207  0.20 56.24  ? 279 GLU A OE1   1 
ATOM   4326  O  OE1   B GLU A 1 279 ? 0.845   -33.749 45.827  0.80 63.90  ? 279 GLU A OE1   1 
ATOM   4327  O  OE2   A GLU A 1 279 ? 0.149   -32.907 44.158  0.20 60.99  ? 279 GLU A OE2   1 
ATOM   4328  O  OE2   B GLU A 1 279 ? -0.438  -32.726 44.357  0.80 61.40  ? 279 GLU A OE2   1 
ATOM   4329  N  N     A LYS A 1 280 ? -1.292  -29.746 49.786  0.20 39.14  ? 280 LYS A N     1 
ATOM   4330  N  N     B LYS A 1 280 ? -1.070  -29.511 49.696  0.80 37.72  ? 280 LYS A N     1 
ATOM   4331  C  CA    A LYS A 1 280 ? -1.532  -29.563 51.216  0.20 42.50  ? 280 LYS A CA    1 
ATOM   4332  C  CA    B LYS A 1 280 ? -1.269  -29.257 51.123  0.80 42.79  ? 280 LYS A CA    1 
ATOM   4333  C  C     A LYS A 1 280 ? -3.035  -29.379 51.411  0.20 41.51  ? 280 LYS A C     1 
ATOM   4334  C  C     B LYS A 1 280 ? -2.762  -29.083 51.406  0.80 41.42  ? 280 LYS A C     1 
ATOM   4335  O  O     A LYS A 1 280 ? -3.538  -28.261 51.531  0.20 40.68  ? 280 LYS A O     1 
ATOM   4336  O  O     B LYS A 1 280 ? -3.248  -27.996 51.719  0.80 40.56  ? 280 LYS A O     1 
ATOM   4337  C  CB    A LYS A 1 280 ? -0.734  -28.371 51.748  0.20 41.95  ? 280 LYS A CB    1 
ATOM   4338  C  CB    B LYS A 1 280 ? -0.473  -28.031 51.546  0.80 42.47  ? 280 LYS A CB    1 
ATOM   4339  C  CG    A LYS A 1 280 ? 0.741   -28.398 51.367  0.20 45.92  ? 280 LYS A CG    1 
ATOM   4340  C  CG    B LYS A 1 280 ? 0.879   -27.925 50.850  0.80 43.55  ? 280 LYS A CG    1 
ATOM   4341  C  CD    A LYS A 1 280 ? 1.462   -27.144 51.843  0.20 47.41  ? 280 LYS A CD    1 
ATOM   4342  C  CD    B LYS A 1 280 ? 1.901   -28.865 51.468  0.80 51.46  ? 280 LYS A CD    1 
ATOM   4343  C  CE    A LYS A 1 280 ? 2.921   -27.151 51.419  0.20 49.83  ? 280 LYS A CE    1 
ATOM   4344  C  CE    B LYS A 1 280 ? 2.303   -28.385 52.859  0.80 79.24  ? 280 LYS A CE    1 
ATOM   4345  N  NZ    A LYS A 1 280 ? 3.639   -25.932 51.886  0.20 54.13  ? 280 LYS A NZ    1 
ATOM   4346  N  NZ    B LYS A 1 280 ? 3.404   -29.196 53.460  0.80 93.93  ? 280 LYS A NZ    1 
ATOM   4347  N  N     A ALA A 1 281 ? -3.756  -30.499 51.448  0.20 41.96  ? 281 ALA A N     1 
ATOM   4348  N  N     B ALA A 1 281 ? -3.493  -30.199 51.301  0.80 41.33  ? 281 ALA A N     1 
ATOM   4349  C  CA    A ALA A 1 281 ? -5.214  -30.495 51.491  0.20 39.05  ? 281 ALA A CA    1 
ATOM   4350  C  CA    B ALA A 1 281 ? -4.954  -30.140 51.376  0.80 37.77  ? 281 ALA A CA    1 
ATOM   4351  C  C     A ALA A 1 281 ? -5.784  -30.446 52.905  0.20 44.19  ? 281 ALA A C     1 
ATOM   4352  C  C     B ALA A 1 281 ? -5.463  -29.950 52.804  0.80 45.38  ? 281 ALA A C     1 
ATOM   4353  O  O     A ALA A 1 281 ? -7.010  -30.455 53.061  0.20 41.57  ? 281 ALA A O     1 
ATOM   4354  O  O     B ALA A 1 281 ? -6.525  -29.348 53.007  0.80 44.86  ? 281 ALA A O     1 
ATOM   4355  C  CB    A ALA A 1 281 ? -5.762  -31.726 50.762  0.20 37.91  ? 281 ALA A CB    1 
ATOM   4356  C  CB    B ALA A 1 281 ? -5.561  -31.404 50.764  0.80 36.77  ? 281 ALA A CB    1 
ATOM   4357  N  N     A TYR A 1 282 ? -4.937  -30.400 53.933  0.20 42.98  ? 282 TYR A N     1 
ATOM   4358  N  N     B TYR A 1 282 ? -4.745  -30.466 53.801  0.80 41.83  ? 282 TYR A N     1 
ATOM   4359  C  CA    A TYR A 1 282 ? -5.389  -30.301 55.317  0.20 45.69  ? 282 TYR A CA    1 
ATOM   4360  C  CA    B TYR A 1 282 ? -5.172  -30.405 55.195  0.80 45.33  ? 282 TYR A CA    1 
ATOM   4361  C  C     A TYR A 1 282 ? -4.649  -29.187 56.045  0.20 48.96  ? 282 TYR A C     1 
ATOM   4362  C  C     B TYR A 1 282 ? -4.475  -29.289 55.965  0.80 49.26  ? 282 TYR A C     1 
ATOM   4363  O  O     A TYR A 1 282 ? -4.471  -29.242 57.265  0.20 52.44  ? 282 TYR A O     1 
ATOM   4364  O  O     B TYR A 1 282 ? -4.443  -29.320 57.201  0.80 52.65  ? 282 TYR A O     1 
ATOM   4365  C  CB    A TYR A 1 282 ? -5.208  -31.632 56.046  0.20 46.74  ? 282 TYR A CB    1 
ATOM   4366  C  CB    B TYR A 1 282 ? -4.913  -31.753 55.860  0.80 45.32  ? 282 TYR A CB    1 
ATOM   4367  C  CG    A TYR A 1 282 ? -5.970  -32.773 55.416  0.20 48.56  ? 282 TYR A CG    1 
ATOM   4368  C  CG    B TYR A 1 282 ? -5.888  -32.801 55.409  0.80 48.92  ? 282 TYR A CG    1 
ATOM   4369  C  CD1   A TYR A 1 282 ? -5.399  -33.545 54.413  0.20 42.27  ? 282 TYR A CD1   1 
ATOM   4370  C  CD1   B TYR A 1 282 ? -5.730  -33.451 54.195  0.80 42.10  ? 282 TYR A CD1   1 
ATOM   4371  C  CD2   A TYR A 1 282 ? -7.262  -33.074 55.822  0.20 43.90  ? 282 TYR A CD2   1 
ATOM   4372  C  CD2   B TYR A 1 282 ? -6.983  -33.128 56.196  0.80 44.30  ? 282 TYR A CD2   1 
ATOM   4373  C  CE1   A TYR A 1 282 ? -6.095  -34.587 53.834  0.20 41.55  ? 282 TYR A CE1   1 
ATOM   4374  C  CE1   B TYR A 1 282 ? -6.633  -34.402 53.783  0.80 40.31  ? 282 TYR A CE1   1 
ATOM   4375  C  CE2   A TYR A 1 282 ? -7.964  -34.112 55.249  0.20 43.60  ? 282 TYR A CE2   1 
ATOM   4376  C  CE2   B TYR A 1 282 ? -7.881  -34.070 55.796  0.80 44.71  ? 282 TYR A CE2   1 
ATOM   4377  C  CZ    A TYR A 1 282 ? -7.377  -34.866 54.256  0.20 40.25  ? 282 TYR A CZ    1 
ATOM   4378  C  CZ    B TYR A 1 282 ? -7.706  -34.708 54.590  0.80 40.65  ? 282 TYR A CZ    1 
ATOM   4379  O  OH    A TYR A 1 282 ? -8.075  -35.904 53.682  0.20 40.77  ? 282 TYR A OH    1 
ATOM   4380  O  OH    B TYR A 1 282 ? -8.617  -35.658 54.197  0.80 40.74  ? 282 TYR A OH    1 
ATOM   4381  N  N     A HIS A 1 283 ? -4.199  -28.180 55.298  0.20 43.33  ? 283 HIS A N     1 
ATOM   4382  N  N     B HIS A 1 283 ? -3.874  -28.337 55.247  0.80 38.94  ? 283 HIS A N     1 
ATOM   4383  C  CA    A HIS A 1 283 ? -3.402  -27.106 55.870  0.20 48.90  ? 283 HIS A CA    1 
ATOM   4384  C  CA    B HIS A 1 283 ? -3.137  -27.244 55.866  0.80 48.72  ? 283 HIS A CA    1 
ATOM   4385  C  C     A HIS A 1 283 ? -4.195  -26.342 56.922  0.20 50.42  ? 283 HIS A C     1 
ATOM   4386  C  C     B HIS A 1 283 ? -3.993  -26.540 56.910  0.80 48.86  ? 283 HIS A C     1 
ATOM   4387  O  O     A HIS A 1 283 ? -5.429  -26.318 56.912  0.20 52.28  ? 283 HIS A O     1 
ATOM   4388  O  O     B HIS A 1 283 ? -5.221  -26.471 56.798  0.80 53.31  ? 283 HIS A O     1 
ATOM   4389  C  CB    A HIS A 1 283 ? -2.937  -26.150 54.769  0.20 46.89  ? 283 HIS A CB    1 
ATOM   4390  C  CB    B HIS A 1 283 ? -2.690  -26.240 54.799  0.80 46.61  ? 283 HIS A CB    1 
ATOM   4391  C  CG    A HIS A 1 283 ? -4.059  -25.459 54.056  0.20 46.13  ? 283 HIS A CG    1 
ATOM   4392  C  CG    B HIS A 1 283 ? -3.820  -25.458 54.201  0.80 45.87  ? 283 HIS A CG    1 
ATOM   4393  N  ND1   A HIS A 1 283 ? -4.722  -24.373 54.587  0.20 45.83  ? 283 HIS A ND1   1 
ATOM   4394  N  ND1   B HIS A 1 283 ? -4.478  -25.855 53.056  0.80 46.70  ? 283 HIS A ND1   1 
ATOM   4395  C  CD2   A HIS A 1 283 ? -4.638  -25.703 52.856  0.20 45.82  ? 283 HIS A CD2   1 
ATOM   4396  C  CD2   B HIS A 1 283 ? -4.419  -24.310 54.600  0.80 45.38  ? 283 HIS A CD2   1 
ATOM   4397  C  CE1   A HIS A 1 283 ? -5.660  -23.977 53.745  0.20 44.92  ? 283 HIS A CE1   1 
ATOM   4398  C  CE1   B HIS A 1 283 ? -5.431  -24.982 52.774  0.80 45.79  ? 283 HIS A CE1   1 
ATOM   4399  N  NE2   A HIS A 1 283 ? -5.630  -24.767 52.686  0.20 43.71  ? 283 HIS A NE2   1 
ATOM   4400  N  NE2   B HIS A 1 283 ? -5.419  -24.038 53.698  0.80 45.46  ? 283 HIS A NE2   1 
ATOM   4401  N  N     A GLU A 1 284 ? -3.468  -25.719 57.844  0.20 56.87  ? 284 GLU A N     1 
ATOM   4402  N  N     B GLU A 1 284 ? -3.335  -26.029 57.944  0.80 57.91  ? 284 GLU A N     1 
ATOM   4403  C  CA    A GLU A 1 284 ? -4.095  -24.873 58.850  0.20 56.35  ? 284 GLU A CA    1 
ATOM   4404  C  CA    B GLU A 1 284 ? -4.024  -25.194 58.916  0.80 56.43  ? 284 GLU A CA    1 
ATOM   4405  C  C     A GLU A 1 284 ? -4.728  -23.656 58.187  0.20 52.87  ? 284 GLU A C     1 
ATOM   4406  C  C     B GLU A 1 284 ? -4.439  -23.889 58.247  0.80 53.29  ? 284 GLU A C     1 
ATOM   4407  O  O     A GLU A 1 284 ? -4.077  -22.948 57.412  0.20 54.94  ? 284 GLU A O     1 
ATOM   4408  O  O     B GLU A 1 284 ? -3.643  -23.260 57.541  0.80 60.12  ? 284 GLU A O     1 
ATOM   4409  C  CB    A GLU A 1 284 ? -3.064  -24.442 59.893  0.20 61.50  ? 284 GLU A CB    1 
ATOM   4410  C  CB    B GLU A 1 284 ? -3.122  -24.933 60.125  0.80 62.48  ? 284 GLU A CB    1 
ATOM   4411  C  CG    A GLU A 1 284 ? -1.615  -24.598 59.441  0.20 68.25  ? 284 GLU A CG    1 
ATOM   4412  C  CG    B GLU A 1 284 ? -1.829  -24.148 59.845  0.80 70.37  ? 284 GLU A CG    1 
ATOM   4413  C  CD    A GLU A 1 284 ? -1.235  -23.646 58.321  0.20 63.05  ? 284 GLU A CD    1 
ATOM   4414  C  CD    B GLU A 1 284 ? -0.741  -24.962 59.142  0.80 76.34  ? 284 GLU A CD    1 
ATOM   4415  O  OE1   A GLU A 1 284 ? -1.518  -22.436 58.446  0.20 56.04  ? 284 GLU A OE1   1 
ATOM   4416  O  OE1   B GLU A 1 284 ? -1.057  -25.980 58.486  0.80 71.46  ? 284 GLU A OE1   1 
ATOM   4417  O  OE2   A GLU A 1 284 ? -0.659  -24.111 57.314  0.20 59.56  ? 284 GLU A OE2   1 
ATOM   4418  O  OE2   B GLU A 1 284 ? 0.443   -24.575 59.245  0.80 86.79  ? 284 GLU A OE2   1 
ATOM   4419  N  N     A GLN A 1 285 ? -6.004  -23.419 58.481  0.20 50.76  ? 285 GLN A N     1 
ATOM   4420  N  N     B GLN A 1 285 ? -5.695  -23.495 58.432  0.80 50.71  ? 285 GLN A N     1 
ATOM   4421  C  CA    A GLN A 1 285 ? -6.717  -22.285 57.901  0.20 50.16  ? 285 GLN A CA    1 
ATOM   4422  C  CA    B GLN A 1 285 ? -6.178  -22.294 57.764  0.80 52.52  ? 285 GLN A CA    1 
ATOM   4423  C  C     A GLN A 1 285 ? -6.213  -20.996 58.537  0.20 45.90  ? 285 GLN A C     1 
ATOM   4424  C  C     B GLN A 1 285 ? -5.589  -21.052 58.429  0.80 45.57  ? 285 GLN A C     1 
ATOM   4425  O  O     A GLN A 1 285 ? -6.474  -20.732 59.714  0.20 44.29  ? 285 GLN A O     1 
ATOM   4426  O  O     B GLN A 1 285 ? -5.281  -21.046 59.624  0.80 50.89  ? 285 GLN A O     1 
ATOM   4427  C  CB    A GLN A 1 285 ? -8.222  -22.445 58.102  0.20 49.22  ? 285 GLN A CB    1 
ATOM   4428  C  CB    B GLN A 1 285 ? -7.710  -22.245 57.774  0.80 51.22  ? 285 GLN A CB    1 
ATOM   4429  C  CG    A GLN A 1 285 ? -8.834  -23.624 57.357  0.20 48.00  ? 285 GLN A CG    1 
ATOM   4430  C  CG    B GLN A 1 285 ? -8.403  -23.446 57.103  0.80 48.37  ? 285 GLN A CG    1 
ATOM   4431  C  CD    A GLN A 1 285 ? -8.891  -23.410 55.854  0.20 47.12  ? 285 GLN A CD    1 
ATOM   4432  C  CD    B GLN A 1 285 ? -8.384  -23.404 55.571  0.80 51.39  ? 285 GLN A CD    1 
ATOM   4433  O  OE1   A GLN A 1 285 ? -8.818  -22.280 55.371  0.20 43.37  ? 285 GLN A OE1   1 
ATOM   4434  O  OE1   B GLN A 1 285 ? -8.112  -22.367 54.958  0.80 41.80  ? 285 GLN A OE1   1 
ATOM   4435  N  NE2   A GLN A 1 285 ? -9.025  -24.500 55.107  0.20 47.38  ? 285 GLN A NE2   1 
ATOM   4436  N  NE2   B GLN A 1 285 ? -8.676  -24.544 54.951  0.80 48.46  ? 285 GLN A NE2   1 
ATOM   4437  N  N     A LEU A 1 286 ? -5.488  -20.193 57.759  0.20 40.51  ? 286 LEU A N     1 
ATOM   4438  N  N     B LEU A 1 286 ? -5.414  -19.999 57.633  0.80 39.42  ? 286 LEU A N     1 
ATOM   4439  C  CA    A LEU A 1 286 ? -4.934  -18.944 58.260  0.20 37.66  ? 286 LEU A CA    1 
ATOM   4440  C  CA    B LEU A 1 286 ? -4.837  -18.744 58.097  0.80 36.33  ? 286 LEU A CA    1 
ATOM   4441  C  C     A LEU A 1 286 ? -6.045  -18.017 58.749  0.20 38.37  ? 286 LEU A C     1 
ATOM   4442  C  C     B LEU A 1 286 ? -5.940  -17.774 58.500  0.80 39.05  ? 286 LEU A C     1 
ATOM   4443  O  O     A LEU A 1 286 ? -7.219  -18.165 58.397  0.20 37.06  ? 286 LEU A O     1 
ATOM   4444  O  O     B LEU A 1 286 ? -6.981  -17.694 57.843  0.80 33.59  ? 286 LEU A O     1 
ATOM   4445  C  CB    A LEU A 1 286 ? -4.108  -18.256 57.171  0.20 38.37  ? 286 LEU A CB    1 
ATOM   4446  C  CB    B LEU A 1 286 ? -3.956  -18.114 57.012  0.80 38.10  ? 286 LEU A CB    1 
ATOM   4447  C  CG    A LEU A 1 286 ? -2.943  -19.062 56.585  0.20 38.77  ? 286 LEU A CG    1 
ATOM   4448  C  CG    B LEU A 1 286 ? -2.454  -18.437 57.028  0.80 42.11  ? 286 LEU A CG    1 
ATOM   4449  C  CD1   A LEU A 1 286 ? -2.362  -18.372 55.357  0.20 34.69  ? 286 LEU A CD1   1 
ATOM   4450  C  CD1   B LEU A 1 286 ? -2.220  -19.941 56.952  0.80 37.21  ? 286 LEU A CD1   1 
ATOM   4451  C  CD2   A LEU A 1 286 ? -1.857  -19.295 57.628  0.20 39.90  ? 286 LEU A CD2   1 
ATOM   4452  C  CD2   B LEU A 1 286 ? -1.686  -17.704 55.913  0.80 36.35  ? 286 LEU A CD2   1 
ATOM   4453  N  N     A SER A 1 287 ? -5.661  -17.054 59.579  0.20 37.94  ? 287 SER A N     1 
ATOM   4454  N  N     B SER A 1 287 ? -5.692  -17.028 59.576  0.80 37.92  ? 287 SER A N     1 
ATOM   4455  C  CA    A SER A 1 287 ? -6.605  -16.109 60.154  0.20 34.78  ? 287 SER A CA    1 
ATOM   4456  C  CA    B SER A 1 287 ? -6.644  -16.062 60.107  0.80 34.59  ? 287 SER A CA    1 
ATOM   4457  C  C     A SER A 1 287 ? -6.696  -14.850 59.295  0.20 37.52  ? 287 SER A C     1 
ATOM   4458  C  C     B SER A 1 287 ? -6.702  -14.816 59.224  0.80 37.75  ? 287 SER A C     1 
ATOM   4459  O  O     A SER A 1 287 ? -5.937  -14.656 58.343  0.20 33.90  ? 287 SER A O     1 
ATOM   4460  O  O     B SER A 1 287 ? -5.856  -14.594 58.354  0.80 33.77  ? 287 SER A O     1 
ATOM   4461  C  CB    A SER A 1 287 ? -6.196  -15.749 61.582  0.20 33.34  ? 287 SER A CB    1 
ATOM   4462  C  CB    B SER A 1 287 ? -6.254  -15.659 61.526  0.80 33.31  ? 287 SER A CB    1 
ATOM   4463  O  OG    A SER A 1 287 ? -4.925  -15.123 61.600  0.20 33.59  ? 287 SER A OG    1 
ATOM   4464  O  OG    B SER A 1 287 ? -5.056  -14.902 61.505  0.80 32.70  ? 287 SER A OG    1 
ATOM   4465  N  N     A VAL A 1 288 ? -7.651  -13.985 59.646  0.20 34.52  ? 288 VAL A N     1 
ATOM   4466  N  N     B VAL A 1 288 ? -7.716  -13.984 59.480  0.80 34.30  ? 288 VAL A N     1 
ATOM   4467  C  CA    A VAL A 1 288 ? -7.781  -12.702 58.960  0.20 35.20  ? 288 VAL A CA    1 
ATOM   4468  C  CA    B VAL A 1 288 ? -7.844  -12.711 58.773  0.80 35.42  ? 288 VAL A CA    1 
ATOM   4469  C  C     A VAL A 1 288 ? -6.525  -11.863 59.161  0.20 37.27  ? 288 VAL A C     1 
ATOM   4470  C  C     B VAL A 1 288 ? -6.613  -11.838 59.002  0.80 38.49  ? 288 VAL A C     1 
ATOM   4471  O  O     A VAL A 1 288 ? -6.049  -11.197 58.232  0.20 30.66  ? 288 VAL A O     1 
ATOM   4472  O  O     B VAL A 1 288 ? -6.102  -11.198 58.069  0.80 29.74  ? 288 VAL A O     1 
ATOM   4473  C  CB    A VAL A 1 288 ? -9.045  -11.964 59.442  0.20 34.55  ? 288 VAL A CB    1 
ATOM   4474  C  CB    B VAL A 1 288 ? -9.143  -12.000 59.199  0.80 34.75  ? 288 VAL A CB    1 
ATOM   4475  C  CG1   A VAL A 1 288 ? -9.032  -10.517 58.975  0.20 32.59  ? 288 VAL A CG1   1 
ATOM   4476  C  CG1   B VAL A 1 288 ? -9.163  -10.576 58.689  0.80 32.07  ? 288 VAL A CG1   1 
ATOM   4477  C  CG2   A VAL A 1 288 ? -10.289 -12.669 58.935  0.20 35.26  ? 288 VAL A CG2   1 
ATOM   4478  C  CG2   B VAL A 1 288 ? -10.344 -12.762 58.671  0.80 35.91  ? 288 VAL A CG2   1 
ATOM   4479  N  N     A ALA A 1 289 ? -5.956  -11.897 60.369  0.20 34.04  ? 289 ALA A N     1 
ATOM   4480  N  N     B ALA A 1 289 ? -6.093  -11.819 60.235  0.80 34.24  ? 289 ALA A N     1 
ATOM   4481  C  CA    A ALA A 1 289 ? -4.739  -11.135 60.630  0.20 32.88  ? 289 ALA A CA    1 
ATOM   4482  C  CA    B ALA A 1 289 ? -4.893  -11.031 60.505  0.80 32.13  ? 289 ALA A CA    1 
ATOM   4483  C  C     A ALA A 1 289 ? -3.559  -11.686 59.839  0.20 34.23  ? 289 ALA A C     1 
ATOM   4484  C  C     B ALA A 1 289 ? -3.703  -11.554 59.710  0.80 34.29  ? 289 ALA A C     1 
ATOM   4485  O  O     A ALA A 1 289 ? -2.702  -10.922 59.381  0.20 35.02  ? 289 ALA A O     1 
ATOM   4486  O  O     B ALA A 1 289 ? -2.901  -10.770 59.192  0.80 35.02  ? 289 ALA A O     1 
ATOM   4487  C  CB    A ALA A 1 289 ? -4.430  -11.133 62.126  0.20 40.40  ? 289 ALA A CB    1 
ATOM   4488  C  CB    B ALA A 1 289 ? -4.578  -11.031 61.999  0.80 41.48  ? 289 ALA A CB    1 
ATOM   4489  N  N     A GLU A 1 290 ? -3.499  -13.008 59.664  0.20 33.40  ? 290 GLU A N     1 
ATOM   4490  N  N     B GLU A 1 290 ? -3.582  -12.877 59.588  0.80 33.15  ? 290 GLU A N     1 
ATOM   4491  C  CA    A GLU A 1 290 ? -2.387  -13.601 58.927  0.20 34.17  ? 290 GLU A CA    1 
ATOM   4492  C  CA    B GLU A 1 290 ? -2.437  -13.452 58.886  0.80 34.25  ? 290 GLU A CA    1 
ATOM   4493  C  C     A GLU A 1 290 ? -2.435  -13.231 57.449  0.20 33.31  ? 290 GLU A C     1 
ATOM   4494  C  C     B GLU A 1 290 ? -2.472  -13.120 57.395  0.80 33.35  ? 290 GLU A C     1 
ATOM   4495  O  O     A GLU A 1 290 ? -1.405  -12.883 56.858  0.20 33.93  ? 290 GLU A O     1 
ATOM   4496  O  O     B GLU A 1 290 ? -1.467  -12.675 56.824  0.80 34.12  ? 290 GLU A O     1 
ATOM   4497  C  CB    A GLU A 1 290 ? -2.386  -15.119 59.103  0.20 35.11  ? 290 GLU A CB    1 
ATOM   4498  C  CB    B GLU A 1 290 ? -2.395  -14.961 59.106  0.80 34.75  ? 290 GLU A CB    1 
ATOM   4499  C  CG    A GLU A 1 290 ? -1.632  -15.604 60.332  0.20 38.04  ? 290 GLU A CG    1 
ATOM   4500  C  CG    B GLU A 1 290 ? -1.634  -15.391 60.348  0.80 38.06  ? 290 GLU A CG    1 
ATOM   4501  C  CD    A GLU A 1 290 ? -1.711  -17.108 60.512  0.20 41.94  ? 290 GLU A CD    1 
ATOM   4502  C  CD    B GLU A 1 290 ? -2.032  -16.778 60.833  0.80 44.26  ? 290 GLU A CD    1 
ATOM   4503  O  OE1   A GLU A 1 290 ? -2.837  -17.648 60.552  0.20 39.69  ? 290 GLU A OE1   1 
ATOM   4504  O  OE1   B GLU A 1 290 ? -3.248  -17.068 60.907  0.80 40.87  ? 290 GLU A OE1   1 
ATOM   4505  O  OE2   A GLU A 1 290 ? -0.645  -17.753 60.605  0.20 44.92  ? 290 GLU A OE2   1 
ATOM   4506  O  OE2   B GLU A 1 290 ? -1.125  -17.580 61.139  0.80 48.44  ? 290 GLU A OE2   1 
ATOM   4507  N  N     A ILE A 1 291 ? -3.615  -13.295 56.833  0.20 29.63  ? 291 ILE A N     1 
ATOM   4508  N  N     B ILE A 1 291 ? -3.619  -13.325 56.745  0.80 29.48  ? 291 ILE A N     1 
ATOM   4509  C  CA    A ILE A 1 291 ? -3.707  -12.946 55.420  0.20 28.26  ? 291 ILE A CA    1 
ATOM   4510  C  CA    B ILE A 1 291 ? -3.668  -13.080 55.307  0.80 27.45  ? 291 ILE A CA    1 
ATOM   4511  C  C     A ILE A 1 291 ? -3.620  -11.435 55.226  0.20 31.26  ? 291 ILE A C     1 
ATOM   4512  C  C     B ILE A 1 291 ? -3.608  -11.587 55.015  0.80 30.97  ? 291 ILE A C     1 
ATOM   4513  O  O     A ILE A 1 291 ? -3.170  -10.969 54.172  0.20 32.92  ? 291 ILE A O     1 
ATOM   4514  O  O     B ILE A 1 291 ? -3.103  -11.175 53.962  0.80 33.55  ? 291 ILE A O     1 
ATOM   4515  C  CB    A ILE A 1 291 ? -4.991  -13.525 54.800  0.20 29.72  ? 291 ILE A CB    1 
ATOM   4516  C  CB    B ILE A 1 291 ? -4.913  -13.737 54.680  0.80 29.55  ? 291 ILE A CB    1 
ATOM   4517  C  CG1   A ILE A 1 291 ? -6.234  -12.865 55.397  0.20 28.46  ? 291 ILE A CG1   1 
ATOM   4518  C  CG1   B ILE A 1 291 ? -6.203  -13.092 55.187  0.80 27.60  ? 291 ILE A CG1   1 
ATOM   4519  C  CG2   A ILE A 1 291 ? -5.044  -15.034 54.990  0.20 26.29  ? 291 ILE A CG2   1 
ATOM   4520  C  CG2   B ILE A 1 291 ? -4.949  -15.217 54.961  0.80 25.54  ? 291 ILE A CG2   1 
ATOM   4521  C  CD1   A ILE A 1 291 ? -7.535  -13.372 54.808  0.20 28.45  ? 291 ILE A CD1   1 
ATOM   4522  C  CD1   B ILE A 1 291 ? -7.443  -13.760 54.638  0.80 28.21  ? 291 ILE A CD1   1 
ATOM   4523  N  N     A THR A 1 292 ? -4.021  -10.649 56.229  0.20 28.30  ? 292 THR A N     1 
ATOM   4524  N  N     B THR A 1 292 ? -4.087  -10.749 55.943  0.80 26.52  ? 292 THR A N     1 
ATOM   4525  C  CA    A THR A 1 292 ? -3.903  -9.198  56.122  0.20 31.47  ? 292 THR A CA    1 
ATOM   4526  C  CA    B THR A 1 292 ? -4.024  -9.307  55.729  0.80 30.13  ? 292 THR A CA    1 
ATOM   4527  C  C     A THR A 1 292 ? -2.444  -8.760  56.182  0.20 34.26  ? 292 THR A C     1 
ATOM   4528  C  C     B THR A 1 292 ? -2.593  -8.791  55.855  0.80 35.60  ? 292 THR A C     1 
ATOM   4529  O  O     A THR A 1 292 ? -2.019  -7.891  55.410  0.20 34.01  ? 292 THR A O     1 
ATOM   4530  O  O     B THR A 1 292 ? -2.155  -7.968  55.040  0.80 32.10  ? 292 THR A O     1 
ATOM   4531  C  CB    A THR A 1 292 ? -4.719  -8.516  57.223  0.20 33.01  ? 292 THR A CB    1 
ATOM   4532  C  CB    B THR A 1 292 ? -4.945  -8.577  56.707  0.80 32.22  ? 292 THR A CB    1 
ATOM   4533  O  OG1   A THR A 1 292 ? -6.110  -8.810  57.043  0.20 32.98  ? 292 THR A OG1   1 
ATOM   4534  O  OG1   B THR A 1 292 ? -6.288  -9.063  56.576  0.80 33.93  ? 292 THR A OG1   1 
ATOM   4535  C  CG2   A THR A 1 292 ? -4.520  -7.004  57.193  0.20 33.58  ? 292 THR A CG2   1 
ATOM   4536  C  CG2   B THR A 1 292 ? -4.947  -7.099  56.411  0.80 38.14  ? 292 THR A CG2   1 
ATOM   4537  N  N     A ASN A 1 293 ? -1.660  -9.354  57.087  0.20 32.92  ? 293 ASN A N     1 
ATOM   4538  N  N     B ASN A 1 293 ? -1.854  -9.250  56.874  0.80 31.94  ? 293 ASN A N     1 
ATOM   4539  C  CA    A ASN A 1 293 ? -0.232  -9.055  57.138  0.20 34.28  ? 293 ASN A CA    1 
ATOM   4540  C  CA    B ASN A 1 293 ? -0.426  -8.947  56.949  0.80 33.51  ? 293 ASN A CA    1 
ATOM   4541  C  C     A ASN A 1 293 ? 0.472   -9.469  55.854  0.20 33.56  ? 293 ASN A C     1 
ATOM   4542  C  C     B ASN A 1 293 ? 0.280   -9.338  55.662  0.80 33.02  ? 293 ASN A C     1 
ATOM   4543  O  O     A ASN A 1 293 ? 1.486   -8.869  55.482  0.20 36.41  ? 293 ASN A O     1 
ATOM   4544  O  O     B ASN A 1 293 ? 1.155   -8.613  55.179  0.80 35.78  ? 293 ASN A O     1 
ATOM   4545  C  CB    A ASN A 1 293 ? 0.417   -9.752  58.334  0.20 36.78  ? 293 ASN A CB    1 
ATOM   4546  C  CB    B ASN A 1 293 ? 0.234   -9.688  58.112  0.80 35.68  ? 293 ASN A CB    1 
ATOM   4547  C  CG    A ASN A 1 293 ? -0.144  -9.283  59.659  0.20 43.36  ? 293 ASN A CG    1 
ATOM   4548  C  CG    B ASN A 1 293 ? -0.261  -9.237  59.460  0.80 43.92  ? 293 ASN A CG    1 
ATOM   4549  O  OD1   A ASN A 1 293 ? -0.609  -8.150  59.784  0.20 47.98  ? 293 ASN A OD1   1 
ATOM   4550  O  OD1   B ASN A 1 293 ? -0.604  -8.072  59.654  0.80 48.69  ? 293 ASN A OD1   1 
ATOM   4551  N  ND2   A ASN A 1 293 ? -0.102  -10.155 60.659  0.20 45.12  ? 293 ASN A ND2   1 
ATOM   4552  N  ND2   B ASN A 1 293 ? -0.291  -10.162 60.411  0.80 45.72  ? 293 ASN A ND2   1 
ATOM   4553  N  N     A ALA A 1 294 ? -0.046  -10.491 55.168  0.20 30.30  ? 294 ALA A N     1 
ATOM   4554  N  N     B ALA A 1 294 ? -0.097  -10.485 55.089  0.80 30.05  ? 294 ALA A N     1 
ATOM   4555  C  CA    A ALA A 1 294 ? 0.546   -10.931 53.912  0.20 36.15  ? 294 ALA A CA    1 
ATOM   4556  C  CA    B ALA A 1 294 ? 0.612   -11.013 53.930  0.80 36.38  ? 294 ALA A CA    1 
ATOM   4557  C  C     A ALA A 1 294 ? 0.366   -9.918  52.790  0.20 36.22  ? 294 ALA A C     1 
ATOM   4558  C  C     B ALA A 1 294 ? 0.491   -10.105 52.716  0.80 36.54  ? 294 ALA A C     1 
ATOM   4559  O  O     A ALA A 1 294 ? 1.057   -10.025 51.771  0.20 36.50  ? 294 ALA A O     1 
ATOM   4560  O  O     B ALA A 1 294 ? 1.326   -10.190 51.811  0.80 36.87  ? 294 ALA A O     1 
ATOM   4561  C  CB    A ALA A 1 294 ? -0.047  -12.276 53.497  0.20 32.42  ? 294 ALA A CB    1 
ATOM   4562  C  CB    B ALA A 1 294 ? 0.098   -12.410 53.593  0.80 32.23  ? 294 ALA A CB    1 
ATOM   4563  N  N     A CYS A 1 295 ? -0.527  -8.938  52.953  0.20 34.12  ? 295 CYS A N     1 
ATOM   4564  N  N     B CYS A 1 295 ? -0.510  -9.221  52.689  0.80 35.07  ? 295 CYS A N     1 
ATOM   4565  C  CA    A CYS A 1 295 ? -0.710  -7.903  51.943  0.20 34.78  ? 295 CYS A CA    1 
ATOM   4566  C  CA    B CYS A 1 295 ? -0.685  -8.313  51.561  0.80 31.83  ? 295 CYS A CA    1 
ATOM   4567  C  C     A CYS A 1 295 ? 0.455   -6.929  51.876  0.20 36.61  ? 295 CYS A C     1 
ATOM   4568  C  C     B CYS A 1 295 ? 0.336   -7.186  51.540  0.80 38.12  ? 295 CYS A C     1 
ATOM   4569  O  O     A CYS A 1 295 ? 0.508   -6.123  50.942  0.20 38.12  ? 295 CYS A O     1 
ATOM   4570  O  O     B CYS A 1 295 ? 0.463   -6.515  50.512  0.80 38.58  ? 295 CYS A O     1 
ATOM   4571  C  CB    A CYS A 1 295 ? -1.994  -7.118  52.209  0.20 33.32  ? 295 CYS A CB    1 
ATOM   4572  C  CB    B CYS A 1 295 ? -2.098  -7.730  51.577  0.80 35.10  ? 295 CYS A CB    1 
ATOM   4573  S  SG    A CYS A 1 295 ? -3.507  -8.017  51.871  0.20 26.13  ? 295 CYS A SG    1 
ATOM   4574  S  SG    B CYS A 1 295 ? -3.341  -8.962  51.211  0.80 38.92  ? 295 CYS A SG    1 
ATOM   4575  N  N     A PHE A 1 296 ? 1.378   -6.976  52.836  0.20 35.29  ? 296 PHE A N     1 
ATOM   4576  N  N     B PHE A 1 296 ? 1.060   -6.962  52.635  0.80 32.90  ? 296 PHE A N     1 
ATOM   4577  C  CA    A PHE A 1 296 ? 2.512   -6.062  52.869  0.20 39.93  ? 296 PHE A CA    1 
ATOM   4578  C  CA    B PHE A 1 296 ? 2.111   -5.957  52.683  0.80 40.70  ? 296 PHE A CA    1 
ATOM   4579  C  C     A PHE A 1 296 ? 3.839   -6.801  52.759  0.20 41.14  ? 296 PHE A C     1 
ATOM   4580  C  C     B PHE A 1 296 ? 3.500   -6.574  52.595  0.80 39.34  ? 296 PHE A C     1 
ATOM   4581  O  O     A PHE A 1 296 ? 4.884   -6.261  53.138  0.20 44.16  ? 296 PHE A O     1 
ATOM   4582  O  O     B PHE A 1 296 ? 4.488   -5.910  52.928  0.80 45.15  ? 296 PHE A O     1 
ATOM   4583  C  CB    A PHE A 1 296 ? 2.459   -5.206  54.136  0.20 39.87  ? 296 PHE A CB    1 
ATOM   4584  C  CB    B PHE A 1 296 ? 1.967   -5.111  53.949  0.80 37.95  ? 296 PHE A CB    1 
ATOM   4585  C  CG    A PHE A 1 296 ? 1.194   -4.410  54.264  0.20 38.89  ? 296 PHE A CG    1 
ATOM   4586  C  CG    B PHE A 1 296 ? 0.633   -4.448  54.066  0.80 39.97  ? 296 PHE A CG    1 
ATOM   4587  C  CD1   A PHE A 1 296 ? 1.069   -3.179  53.642  0.20 36.84  ? 296 PHE A CD1   1 
ATOM   4588  C  CD1   B PHE A 1 296 ? 0.412   -3.198  53.513  0.80 34.76  ? 296 PHE A CD1   1 
ATOM   4589  C  CD2   A PHE A 1 296 ? 0.121   -4.901  54.990  0.20 39.22  ? 296 PHE A CD2   1 
ATOM   4590  C  CD2   B PHE A 1 296 ? -0.416  -5.086  54.709  0.80 36.54  ? 296 PHE A CD2   1 
ATOM   4591  C  CE1   A PHE A 1 296 ? -0.100  -2.448  53.749  0.20 39.91  ? 296 PHE A CE1   1 
ATOM   4592  C  CE1   B PHE A 1 296 ? -0.833  -2.591  53.612  0.80 38.79  ? 296 PHE A CE1   1 
ATOM   4593  C  CE2   A PHE A 1 296 ? -1.049  -4.173  55.102  0.20 39.36  ? 296 PHE A CE2   1 
ATOM   4594  C  CE2   B PHE A 1 296 ? -1.650  -4.485  54.812  0.80 38.28  ? 296 PHE A CE2   1 
ATOM   4595  C  CZ    A PHE A 1 296 ? -1.158  -2.944  54.483  0.20 38.38  ? 296 PHE A CZ    1 
ATOM   4596  C  CZ    B PHE A 1 296 ? -1.860  -3.235  54.265  0.80 36.09  ? 296 PHE A CZ    1 
ATOM   4597  N  N     A GLU A 1 297 ? 3.815   -8.035  52.251  0.20 40.39  ? 297 GLU A N     1 
ATOM   4598  N  N     B GLU A 1 297 ? 3.591   -7.840  52.167  0.80 39.70  ? 297 GLU A N     1 
ATOM   4599  C  CA    A GLU A 1 297 ? 5.021   -8.787  51.932  0.20 39.85  ? 297 GLU A CA    1 
ATOM   4600  C  CA    B GLU A 1 297 ? 4.871   -8.486  51.880  0.80 39.69  ? 297 GLU A CA    1 
ATOM   4601  C  C     A GLU A 1 297 ? 5.268   -8.724  50.435  0.20 38.39  ? 297 GLU A C     1 
ATOM   4602  C  C     B GLU A 1 297 ? 5.142   -8.403  50.389  0.80 37.78  ? 297 GLU A C     1 
ATOM   4603  O  O     A GLU A 1 297 ? 4.369   -9.072  49.653  0.20 33.39  ? 297 GLU A O     1 
ATOM   4604  O  O     B GLU A 1 297 ? 4.330   -8.907  49.593  0.80 32.35  ? 297 GLU A O     1 
ATOM   4605  C  CB    A GLU A 1 297 ? 4.887   -10.242 52.374  0.20 41.55  ? 297 GLU A CB    1 
ATOM   4606  C  CB    B GLU A 1 297 ? 4.870   -9.946  52.325  0.80 41.14  ? 297 GLU A CB    1 
ATOM   4607  C  CG    A GLU A 1 297 ? 4.386   -10.427 53.801  0.20 44.54  ? 297 GLU A CG    1 
ATOM   4608  C  CG    B GLU A 1 297 ? 4.857   -10.167 53.825  0.80 47.69  ? 297 GLU A CG    1 
ATOM   4609  C  CD    A GLU A 1 297 ? 5.409   -10.021 54.848  0.20 52.58  ? 297 GLU A CD    1 
ATOM   4610  C  CD    B GLU A 1 297 ? 6.190   -9.843  54.476  0.80 54.29  ? 297 GLU A CD    1 
ATOM   4611  O  OE1   A GLU A 1 297 ? 6.608   -9.927  54.511  0.20 54.65  ? 297 GLU A OE1   1 
ATOM   4612  O  OE1   B GLU A 1 297 ? 7.208   -9.744  53.753  0.80 62.21  ? 297 GLU A OE1   1 
ATOM   4613  O  OE2   A GLU A 1 297 ? 5.010   -9.796  56.011  0.20 53.14  ? 297 GLU A OE2   1 
ATOM   4614  O  OE2   B GLU A 1 297 ? 6.218   -9.684  55.715  0.80 62.88  ? 297 GLU A OE2   1 
ATOM   4615  N  N     A PRO A 1 298 ? 6.449   -8.284  49.995  0.20 40.00  ? 298 PRO A N     1 
ATOM   4616  N  N     B PRO A 1 298 ? 6.251   -7.795  49.971  0.80 41.56  ? 298 PRO A N     1 
ATOM   4617  C  CA    A PRO A 1 298 ? 6.691   -8.150  48.548  0.20 33.74  ? 298 PRO A CA    1 
ATOM   4618  C  CA    B PRO A 1 298 ? 6.543   -7.677  48.530  0.80 31.18  ? 298 PRO A CA    1 
ATOM   4619  C  C     A PRO A 1 298 ? 6.583   -9.457  47.779  0.20 34.14  ? 298 PRO A C     1 
ATOM   4620  C  C     B PRO A 1 298 ? 6.471   -8.983  47.742  0.80 30.45  ? 298 PRO A C     1 
ATOM   4621  O  O     A PRO A 1 298 ? 6.368   -9.422  46.561  0.20 35.43  ? 298 PRO A O     1 
ATOM   4622  O  O     B PRO A 1 298 ? 6.131   -8.949  46.550  0.80 34.83  ? 298 PRO A O     1 
ATOM   4623  C  CB    A PRO A 1 298 ? 8.114   -7.578  48.480  0.20 37.76  ? 298 PRO A CB    1 
ATOM   4624  C  CB    B PRO A 1 298 ? 7.959   -7.089  48.524  0.80 37.46  ? 298 PRO A CB    1 
ATOM   4625  C  CG    A PRO A 1 298 ? 8.337   -6.936  49.813  0.20 40.04  ? 298 PRO A CG    1 
ATOM   4626  C  CG    B PRO A 1 298 ? 8.010   -6.249  49.760  0.80 40.29  ? 298 PRO A CG    1 
ATOM   4627  C  CD    A PRO A 1 298 ? 7.576   -7.779  50.797  0.20 42.62  ? 298 PRO A CD    1 
ATOM   4628  C  CD    B PRO A 1 298 ? 7.181   -7.002  50.797  0.80 41.65  ? 298 PRO A CD    1 
ATOM   4629  N  N     A ALA A 1 299 ? 6.712   -10.607 48.445  0.20 37.77  ? 299 ALA A N     1 
ATOM   4630  N  N     B ALA A 1 299 ? 6.760   -10.134 48.360  0.80 38.09  ? 299 ALA A N     1 
ATOM   4631  C  CA    A ALA A 1 299 ? 6.668   -11.895 47.760  0.20 41.27  ? 299 ALA A CA    1 
ATOM   4632  C  CA    B ALA A 1 299 ? 6.750   -11.393 47.617  0.80 44.00  ? 299 ALA A CA    1 
ATOM   4633  C  C     A ALA A 1 299 ? 5.267   -12.303 47.323  0.20 34.55  ? 299 ALA A C     1 
ATOM   4634  C  C     B ALA A 1 299 ? 5.361   -11.762 47.104  0.80 36.33  ? 299 ALA A C     1 
ATOM   4635  O  O     A ALA A 1 299 ? 5.129   -13.348 46.678  0.20 35.03  ? 299 ALA A O     1 
ATOM   4636  O  O     B ALA A 1 299 ? 5.249   -12.482 46.107  0.80 34.50  ? 299 ALA A O     1 
ATOM   4637  C  CB    A ALA A 1 299 ? 7.257   -12.988 48.654  0.20 42.06  ? 299 ALA A CB    1 
ATOM   4638  C  CB    B ALA A 1 299 ? 7.291   -12.534 48.477  0.80 43.74  ? 299 ALA A CB    1 
ATOM   4639  N  N     A ASN A 1 300 ? 4.235   -11.526 47.646  0.20 31.28  ? 300 ASN A N     1 
ATOM   4640  N  N     B ASN A 1 300 ? 4.296   -11.298 47.756  0.80 29.55  ? 300 ASN A N     1 
ATOM   4641  C  CA    A ASN A 1 300 ? 2.866   -11.849 47.264  0.20 29.45  ? 300 ASN A CA    1 
ATOM   4642  C  CA    B ASN A 1 300 ? 2.957   -11.655 47.304  0.80 28.38  ? 300 ASN A CA    1 
ATOM   4643  C  C     A ASN A 1 300 ? 2.287   -10.855 46.266  0.20 31.60  ? 300 ASN A C     1 
ATOM   4644  C  C     B ASN A 1 300 ? 2.432   -10.732 46.212  0.80 31.71  ? 300 ASN A C     1 
ATOM   4645  O  O     A ASN A 1 300 ? 1.096   -10.934 45.943  0.20 31.18  ? 300 ASN A O     1 
ATOM   4646  O  O     B ASN A 1 300 ? 1.314   -10.943 45.727  0.80 31.66  ? 300 ASN A O     1 
ATOM   4647  C  CB    A ASN A 1 300 ? 1.978   -11.923 48.508  0.20 31.37  ? 300 ASN A CB    1 
ATOM   4648  C  CB    B ASN A 1 300 ? 1.983   -11.653 48.488  0.80 29.93  ? 300 ASN A CB    1 
ATOM   4649  C  CG    A ASN A 1 300 ? 2.447   -12.974 49.498  0.20 38.96  ? 300 ASN A CG    1 
ATOM   4650  C  CG    B ASN A 1 300 ? 2.341   -12.692 49.539  0.80 40.01  ? 300 ASN A CG    1 
ATOM   4651  O  OD1   A ASN A 1 300 ? 2.912   -14.047 49.107  0.20 42.94  ? 300 ASN A OD1   1 
ATOM   4652  O  OD1   B ASN A 1 300 ? 2.805   -13.789 49.211  0.80 45.52  ? 300 ASN A OD1   1 
ATOM   4653  N  ND2   A ASN A 1 300 ? 2.332   -12.670 50.787  0.20 35.02  ? 300 ASN A ND2   1 
ATOM   4654  N  ND2   B ASN A 1 300 ? 2.128   -12.353 50.810  0.80 34.26  ? 300 ASN A ND2   1 
ATOM   4655  N  N     A GLN A 1 301 ? 3.097   -9.928  45.763  0.20 31.48  ? 301 GLN A N     1 
ATOM   4656  N  N     B GLN A 1 301 ? 3.205   -9.725  45.815  0.80 31.25  ? 301 GLN A N     1 
ATOM   4657  C  CA    A GLN A 1 301 ? 2.597   -8.896  44.872  0.20 31.34  ? 301 GLN A CA    1 
ATOM   4658  C  CA    B GLN A 1 301 ? 2.734   -8.758  44.838  0.80 31.77  ? 301 GLN A CA    1 
ATOM   4659  C  C     A GLN A 1 301 ? 2.511   -9.406  43.436  0.20 30.54  ? 301 GLN A C     1 
ATOM   4660  C  C     B GLN A 1 301 ? 2.719   -9.343  43.431  0.80 31.29  ? 301 GLN A C     1 
ATOM   4661  O  O     A GLN A 1 301 ? 3.184   -10.362 43.041  0.20 27.83  ? 301 GLN A O     1 
ATOM   4662  O  O     B GLN A 1 301 ? 3.523   -10.214 43.082  0.80 24.74  ? 301 GLN A O     1 
ATOM   4663  C  CB    A GLN A 1 301 ? 3.493   -7.660  44.927  0.20 29.29  ? 301 GLN A CB    1 
ATOM   4664  C  CB    B GLN A 1 301 ? 3.612   -7.511  44.861  0.80 28.80  ? 301 GLN A CB    1 
ATOM   4665  C  CG    A GLN A 1 301 ? 3.691   -7.101  46.317  0.20 31.39  ? 301 GLN A CG    1 
ATOM   4666  C  CG    B GLN A 1 301 ? 3.220   -6.529  45.913  0.80 32.50  ? 301 GLN A CG    1 
ATOM   4667  C  CD    A GLN A 1 301 ? 4.346   -5.741  46.299  0.20 34.90  ? 301 GLN A CD    1 
ATOM   4668  C  CD    B GLN A 1 301 ? 4.408   -5.855  46.520  0.80 35.22  ? 301 GLN A CD    1 
ATOM   4669  O  OE1   A GLN A 1 301 ? 4.203   -4.960  47.238  0.20 32.10  ? 301 GLN A OE1   1 
ATOM   4670  O  OE1   B GLN A 1 301 ? 4.378   -5.459  47.681  0.80 38.30  ? 301 GLN A OE1   1 
ATOM   4671  N  NE2   A GLN A 1 301 ? 5.068   -5.446  45.224  0.20 33.89  ? 301 GLN A NE2   1 
ATOM   4672  N  NE2   B GLN A 1 301 ? 5.475   -5.716  45.741  0.80 37.90  ? 301 GLN A NE2   1 
ATOM   4673  N  N     A MET A 1 302 ? 1.663   -8.741  42.650  0.20 27.09  ? 302 MET A N     1 
ATOM   4674  N  N     B MET A 1 302 ? 1.786   -8.836  42.623  0.80 26.98  ? 302 MET A N     1 
ATOM   4675  C  CA    A MET A 1 302 ? 1.552   -9.041  41.230  0.20 26.20  ? 302 MET A CA    1 
ATOM   4676  C  CA    B MET A 1 302 ? 1.659   -9.169  41.213  0.80 25.86  ? 302 MET A CA    1 
ATOM   4677  C  C     A MET A 1 302 ? 2.615   -8.321  40.408  0.20 25.37  ? 302 MET A C     1 
ATOM   4678  C  C     B MET A 1 302 ? 2.649   -8.390  40.347  0.80 25.04  ? 302 MET A C     1 
ATOM   4679  O  O     A MET A 1 302 ? 2.858   -8.707  39.261  0.20 26.70  ? 302 MET A O     1 
ATOM   4680  O  O     B MET A 1 302 ? 2.811   -8.729  39.174  0.80 26.67  ? 302 MET A O     1 
ATOM   4681  C  CB    A MET A 1 302 ? 0.150   -8.675  40.731  0.20 29.96  ? 302 MET A CB    1 
ATOM   4682  C  CB    B MET A 1 302 ? 0.213   -8.901  40.766  0.80 29.93  ? 302 MET A CB    1 
ATOM   4683  C  CG    A MET A 1 302 ? -0.266  -9.362  39.442  0.20 35.21  ? 302 MET A CG    1 
ATOM   4684  C  CG    B MET A 1 302 ? -0.195  -9.446  39.411  0.80 35.75  ? 302 MET A CG    1 
ATOM   4685  S  SD    A MET A 1 302 ? -2.057  -9.404  39.215  0.20 46.43  ? 302 MET A SD    1 
ATOM   4686  S  SD    B MET A 1 302 ? -1.988  -9.471  39.171  0.80 47.62  ? 302 MET A SD    1 
ATOM   4687  C  CE    A MET A 1 302 ? -2.433  -7.663  39.020  0.20 35.67  ? 302 MET A CE    1 
ATOM   4688  C  CE    B MET A 1 302 ? -2.366  -7.736  38.891  0.80 36.46  ? 302 MET A CE    1 
ATOM   4689  N  N     A VAL A 1 303 ? 3.246   -7.291  40.972  0.20 28.38  ? 303 VAL A N     1 
ATOM   4690  N  N     B VAL A 1 303 ? 3.294   -7.358  40.902  0.80 28.31  ? 303 VAL A N     1 
ATOM   4691  C  CA    A VAL A 1 303 ? 4.360   -6.583  40.350  0.20 29.09  ? 303 VAL A CA    1 
ATOM   4692  C  CA    B VAL A 1 303 ? 4.356   -6.595  40.244  0.80 29.21  ? 303 VAL A CA    1 
ATOM   4693  C  C     A VAL A 1 303 ? 5.497   -6.524  41.362  0.20 32.79  ? 303 VAL A C     1 
ATOM   4694  C  C     B VAL A 1 303 ? 5.542   -6.526  41.200  0.80 33.40  ? 303 VAL A C     1 
ATOM   4695  O  O     A VAL A 1 303 ? 5.279   -6.169  42.526  0.20 29.76  ? 303 VAL A O     1 
ATOM   4696  O  O     B VAL A 1 303 ? 5.370   -6.243  42.392  0.80 29.42  ? 303 VAL A O     1 
ATOM   4697  C  CB    A VAL A 1 303 ? 3.962   -5.163  39.900  0.20 30.08  ? 303 VAL A CB    1 
ATOM   4698  C  CB    B VAL A 1 303 ? 3.901   -5.173  39.856  0.80 30.12  ? 303 VAL A CB    1 
ATOM   4699  C  CG1   A VAL A 1 303 ? 5.148   -4.453  39.255  0.20 29.79  ? 303 VAL A CG1   1 
ATOM   4700  C  CG1   B VAL A 1 303 ? 5.063   -4.374  39.228  0.80 29.95  ? 303 VAL A CG1   1 
ATOM   4701  C  CG2   A VAL A 1 303 ? 2.776   -5.214  38.944  0.20 26.83  ? 303 VAL A CG2   1 
ATOM   4702  C  CG2   B VAL A 1 303 ? 2.706   -5.223  38.915  0.80 26.70  ? 303 VAL A CG2   1 
ATOM   4703  N  N     A LYS A 1 304 ? 6.705   -6.871  40.923  0.20 31.78  ? 304 LYS A N     1 
ATOM   4704  N  N     B LYS A 1 304 ? 6.742   -6.775  40.681  0.80 31.88  ? 304 LYS A N     1 
ATOM   4705  C  CA    A LYS A 1 304 ? 7.864   -6.923  41.815  0.20 31.39  ? 304 LYS A CA    1 
ATOM   4706  C  CA    B LYS A 1 304 ? 7.944   -6.673  41.501  0.80 31.05  ? 304 LYS A CA    1 
ATOM   4707  C  C     A LYS A 1 304 ? 8.362   -5.507  42.075  0.20 34.53  ? 304 LYS A C     1 
ATOM   4708  C  C     B LYS A 1 304 ? 8.289   -5.209  41.763  0.80 36.62  ? 304 LYS A C     1 
ATOM   4709  O  O     A LYS A 1 304 ? 9.156   -4.948  41.315  0.20 33.24  ? 304 LYS A O     1 
ATOM   4710  O  O     B LYS A 1 304 ? 8.618   -4.463  40.832  0.80 31.76  ? 304 LYS A O     1 
ATOM   4711  C  CB    A LYS A 1 304 ? 8.961   -7.801  41.224  0.20 35.87  ? 304 LYS A CB    1 
ATOM   4712  C  CB    B LYS A 1 304 ? 9.108   -7.388  40.817  0.80 35.10  ? 304 LYS A CB    1 
ATOM   4713  C  CG    A LYS A 1 304 ? 8.538   -9.243  41.011  0.20 33.91  ? 304 LYS A CG    1 
ATOM   4714  C  CG    B LYS A 1 304 ? 8.930   -8.893  40.730  0.80 35.29  ? 304 LYS A CG    1 
ATOM   4715  C  CD    A LYS A 1 304 ? 9.723   -10.133 40.666  0.20 32.88  ? 304 LYS A CD    1 
ATOM   4716  C  CD    B LYS A 1 304 ? 9.847   -9.628  41.702  0.80 43.22  ? 304 LYS A CD    1 
ATOM   4717  C  CE    A LYS A 1 304 ? 10.730  -10.178 41.804  0.20 36.03  ? 304 LYS A CE    1 
ATOM   4718  C  CE    B LYS A 1 304 ? 9.483   -9.326  43.155  0.80 47.84  ? 304 LYS A CE    1 
ATOM   4719  N  NZ    A LYS A 1 304 ? 11.616  -11.368 41.715  0.20 25.78  ? 304 LYS A NZ    1 
ATOM   4720  N  NZ    B LYS A 1 304 ? 10.224  -10.170 44.149  0.80 58.21  ? 304 LYS A NZ    1 
ATOM   4721  N  N     A CYS A 1 305 ? 7.886   -4.919  43.172  0.20 31.99  ? 305 CYS A N     1 
ATOM   4722  N  N     B CYS A 1 305 ? 8.209   -4.810  43.031  0.80 30.65  ? 305 CYS A N     1 
ATOM   4723  C  CA    A CYS A 1 305 ? 8.356   -3.627  43.650  0.20 32.12  ? 305 CYS A CA    1 
ATOM   4724  C  CA    B CYS A 1 305 ? 8.630   -3.500  43.526  0.80 30.84  ? 305 CYS A CA    1 
ATOM   4725  C  C     A CYS A 1 305 ? 8.411   -3.673  45.171  0.20 34.68  ? 305 CYS A C     1 
ATOM   4726  C  C     B CYS A 1 305 ? 8.599   -3.569  45.048  0.80 34.84  ? 305 CYS A C     1 
ATOM   4727  O  O     A CYS A 1 305 ? 8.134   -4.705  45.791  0.20 32.55  ? 305 CYS A O     1 
ATOM   4728  O  O     B CYS A 1 305 ? 8.189   -4.577  45.630  0.80 31.63  ? 305 CYS A O     1 
ATOM   4729  C  CB    A CYS A 1 305 ? 7.462   -2.484  43.154  0.20 32.93  ? 305 CYS A CB    1 
ATOM   4730  C  CB    B CYS A 1 305 ? 7.745   -2.365  43.008  0.80 33.58  ? 305 CYS A CB    1 
ATOM   4731  S  SG    A CYS A 1 305 ? 5.726   -2.622  43.627  0.20 33.58  ? 305 CYS A SG    1 
ATOM   4732  S  SG    B CYS A 1 305 ? 6.007   -2.487  43.461  0.80 34.39  ? 305 CYS A SG    1 
ATOM   4733  N  N     A ASP A 1 306 ? 8.772   -2.546  45.780  0.20 37.47  ? 306 ASP A N     1 
ATOM   4734  N  N     B ASP A 1 306 ? 9.029   -2.482  45.697  0.80 37.66  ? 306 ASP A N     1 
ATOM   4735  C  CA    A ASP A 1 306 ? 8.921   -2.453  47.232  0.20 37.86  ? 306 ASP A CA    1 
ATOM   4736  C  CA    B ASP A 1 306 ? 9.140   -2.416  47.156  0.80 37.79  ? 306 ASP A CA    1 
ATOM   4737  C  C     A ASP A 1 306 ? 8.168   -1.231  47.745  0.20 35.79  ? 306 ASP A C     1 
ATOM   4738  C  C     B ASP A 1 306 ? 8.245   -1.308  47.704  0.80 35.73  ? 306 ASP A C     1 
ATOM   4739  O  O     A ASP A 1 306 ? 8.696   -0.106  47.686  0.20 40.17  ? 306 ASP A O     1 
ATOM   4740  O  O     B ASP A 1 306 ? 8.668   -0.146  47.792  0.80 40.16  ? 306 ASP A O     1 
ATOM   4741  C  CB    A ASP A 1 306 ? 10.392  -2.389  47.624  0.20 40.51  ? 306 ASP A CB    1 
ATOM   4742  C  CB    B ASP A 1 306 ? 10.595  -2.203  47.572  0.80 39.83  ? 306 ASP A CB    1 
ATOM   4743  C  CG    A ASP A 1 306 ? 10.615  -2.643  49.103  0.20 44.39  ? 306 ASP A CG    1 
ATOM   4744  C  CG    B ASP A 1 306 ? 10.828  -2.471  49.050  0.80 45.12  ? 306 ASP A CG    1 
ATOM   4745  O  OD1   A ASP A 1 306 ? 9.619   -2.844  49.830  0.20 42.85  ? 306 ASP A OD1   1 
ATOM   4746  O  OD1   B ASP A 1 306 ? 9.832   -2.599  49.794  0.80 42.45  ? 306 ASP A OD1   1 
ATOM   4747  O  OD2   A ASP A 1 306 ? 11.788  -2.650  49.537  0.20 43.82  ? 306 ASP A OD2   1 
ATOM   4748  O  OD2   B ASP A 1 306 ? 12.012  -2.567  49.464  0.80 42.49  ? 306 ASP A OD2   1 
ATOM   4749  N  N     A PRO A 1 307 ? 6.947   -1.406  48.260  0.20 36.84  ? 307 PRO A N     1 
ATOM   4750  N  N     B PRO A 1 307 ? 7.006   -1.624  48.102  0.80 35.08  ? 307 PRO A N     1 
ATOM   4751  C  CA    A PRO A 1 307 ? 6.186   -0.247  48.757  0.20 39.60  ? 307 PRO A CA    1 
ATOM   4752  C  CA    B PRO A 1 307 ? 6.089   -0.572  48.584  0.80 38.36  ? 307 PRO A CA    1 
ATOM   4753  C  C     A PRO A 1 307 ? 6.840   0.457   49.931  0.20 42.79  ? 307 PRO A C     1 
ATOM   4754  C  C     B PRO A 1 307 ? 6.550   0.134   49.846  0.80 42.49  ? 307 PRO A C     1 
ATOM   4755  O  O     A PRO A 1 307 ? 6.477   1.603   50.224  0.20 45.15  ? 307 PRO A O     1 
ATOM   4756  O  O     B PRO A 1 307 ? 6.116   1.265   50.098  0.80 48.24  ? 307 PRO A O     1 
ATOM   4757  C  CB    A PRO A 1 307 ? 4.833   -0.855  49.159  0.20 38.51  ? 307 PRO A CB    1 
ATOM   4758  C  CB    B PRO A 1 307 ? 4.775   -1.329  48.835  0.80 37.75  ? 307 PRO A CB    1 
ATOM   4759  C  CG    A PRO A 1 307 ? 4.768   -2.168  48.461  0.20 39.22  ? 307 PRO A CG    1 
ATOM   4760  C  CG    B PRO A 1 307 ? 4.887   -2.576  48.079  0.80 42.81  ? 307 PRO A CG    1 
ATOM   4761  C  CD    A PRO A 1 307 ? 6.183   -2.657  48.378  0.20 41.45  ? 307 PRO A CD    1 
ATOM   4762  C  CD    B PRO A 1 307 ? 6.353   -2.939  48.064  0.80 43.88  ? 307 PRO A CD    1 
ATOM   4763  N  N     A ARG A 1 308 ? 7.780   -0.191  50.622  0.20 43.93  ? 308 ARG A N     1 
ATOM   4764  N  N     B ARG A 1 308 ? 7.380   -0.499  50.671  0.80 39.53  ? 308 ARG A N     1 
ATOM   4765  C  CA    A ARG A 1 308 ? 8.514   0.487   51.686  0.20 47.55  ? 308 ARG A CA    1 
ATOM   4766  C  CA    B ARG A 1 308 ? 7.957   0.209   51.805  0.80 46.94  ? 308 ARG A CA    1 
ATOM   4767  C  C     A ARG A 1 308 ? 9.309   1.669   51.147  0.20 46.88  ? 308 ARG A C     1 
ATOM   4768  C  C     B ARG A 1 308 ? 8.810   1.393   51.364  0.80 47.38  ? 308 ARG A C     1 
ATOM   4769  O  O     A ARG A 1 308 ? 9.604   2.610   51.891  0.20 50.23  ? 308 ARG A O     1 
ATOM   4770  O  O     B ARG A 1 308 ? 9.051   2.299   52.166  0.80 52.57  ? 308 ARG A O     1 
ATOM   4771  C  CB    A ARG A 1 308 ? 9.448   -0.498  52.389  0.20 49.11  ? 308 ARG A CB    1 
ATOM   4772  C  CB    B ARG A 1 308 ? 8.774   -0.767  52.652  0.80 49.77  ? 308 ARG A CB    1 
ATOM   4773  C  CG    A ARG A 1 308 ? 8.796   -1.816  52.769  0.20 50.92  ? 308 ARG A CG    1 
ATOM   4774  C  CG    B ARG A 1 308 ? 8.014   -2.044  52.953  0.80 50.37  ? 308 ARG A CG    1 
ATOM   4775  C  CD    A ARG A 1 308 ? 9.847   -2.860  53.108  0.20 58.34  ? 308 ARG A CD    1 
ATOM   4776  C  CD    B ARG A 1 308 ? 8.905   -3.139  53.506  0.80 66.96  ? 308 ARG A CD    1 
ATOM   4777  N  NE    A ARG A 1 308 ? 9.277   -4.196  53.236  0.20 61.82  ? 308 ARG A NE    1 
ATOM   4778  N  NE    B ARG A 1 308 ? 8.230   -4.432  53.481  0.80 67.15  ? 308 ARG A NE    1 
ATOM   4779  C  CZ    A ARG A 1 308 ? 9.991   -5.300  53.409  0.20 58.07  ? 308 ARG A CZ    1 
ATOM   4780  C  CZ    B ARG A 1 308 ? 7.334   -4.828  54.376  0.80 70.25  ? 308 ARG A CZ    1 
ATOM   4781  N  NH1   A ARG A 1 308 ? 11.312  -5.265  53.476  0.20 52.76  ? 308 ARG A NH1   1 
ATOM   4782  N  NH1   B ARG A 1 308 ? 6.977   -4.051  55.387  0.80 75.50  ? 308 ARG A NH1   1 
ATOM   4783  N  NH2   A ARG A 1 308 ? 9.364   -6.469  53.513  0.20 50.20  ? 308 ARG A NH2   1 
ATOM   4784  N  NH2   B ARG A 1 308 ? 6.780   -6.032  54.253  0.80 55.68  ? 308 ARG A NH2   1 
ATOM   4785  N  N     A HIS A 1 309 ? 9.663   1.637   49.865  0.20 45.85  ? 309 HIS A N     1 
ATOM   4786  N  N     B HIS A 1 309 ? 9.265   1.410   50.106  0.80 44.12  ? 309 HIS A N     1 
ATOM   4787  C  CA    A HIS A 1 309 ? 10.421  2.704   49.229  0.20 48.82  ? 309 HIS A CA    1 
ATOM   4788  C  CA    B HIS A 1 309 ? 9.949   2.584   49.571  0.80 50.40  ? 309 HIS A CA    1 
ATOM   4789  C  C     A HIS A 1 309 ? 9.527   3.746   48.568  0.20 46.11  ? 309 HIS A C     1 
ATOM   4790  C  C     B HIS A 1 309 ? 8.964   3.724   49.328  0.80 44.72  ? 309 HIS A C     1 
ATOM   4791  O  O     A HIS A 1 309 ? 10.020  4.564   47.784  0.20 43.18  ? 309 HIS A O     1 
ATOM   4792  O  O     B HIS A 1 309 ? 9.103   4.817   49.890  0.80 52.09  ? 309 HIS A O     1 
ATOM   4793  C  CB    A HIS A 1 309 ? 11.389  2.115   48.198  0.20 50.18  ? 309 HIS A CB    1 
ATOM   4794  C  CB    B HIS A 1 309 ? 10.677  2.234   48.267  0.80 51.33  ? 309 HIS A CB    1 
ATOM   4795  C  CG    A HIS A 1 309 ? 12.330  1.098   48.767  0.20 50.90  ? 309 HIS A CG    1 
ATOM   4796  C  CG    B HIS A 1 309 ? 11.949  1.466   48.457  0.80 48.59  ? 309 HIS A CG    1 
ATOM   4797  N  ND1   A HIS A 1 309 ? 13.127  0.298   47.977  0.20 55.24  ? 309 HIS A ND1   1 
ATOM   4798  N  ND1   B HIS A 1 309 ? 12.676  0.964   47.398  0.80 55.24  ? 309 HIS A ND1   1 
ATOM   4799  C  CD2   A HIS A 1 309 ? 12.602  0.752   50.048  0.20 53.22  ? 309 HIS A CD2   1 
ATOM   4800  C  CD2   B HIS A 1 309 ? 12.630  1.123   49.577  0.80 55.42  ? 309 HIS A CD2   1 
ATOM   4801  C  CE1   A HIS A 1 309 ? 13.849  -0.498  48.746  0.20 54.48  ? 309 HIS A CE1   1 
ATOM   4802  C  CE1   B HIS A 1 309 ? 13.748  0.341   47.857  0.80 57.64  ? 309 HIS A CE1   1 
ATOM   4803  N  NE2   A HIS A 1 309 ? 13.549  -0.243  50.007  0.20 56.49  ? 309 HIS A NE2   1 
ATOM   4804  N  NE2   B HIS A 1 309 ? 13.743  0.422   49.176  0.80 62.09  ? 309 HIS A NE2   1 
ATOM   4805  N  N     A GLY A 1 310 ? 8.229   3.735   48.866  0.20 44.18  ? 310 GLY A N     1 
ATOM   4806  N  N     B GLY A 1 310 ? 7.957   3.480   48.499  0.80 44.22  ? 310 GLY A N     1 
ATOM   4807  C  CA    A GLY A 1 310 ? 7.302   4.690   48.299  0.20 43.15  ? 310 GLY A CA    1 
ATOM   4808  C  CA    B GLY A 1 310 ? 7.077   4.525   48.026  0.80 43.46  ? 310 GLY A CA    1 
ATOM   4809  C  C     A GLY A 1 310 ? 6.194   4.998   49.282  0.20 43.03  ? 310 GLY A C     1 
ATOM   4810  C  C     B GLY A 1 310 ? 6.042   4.947   49.047  0.80 42.91  ? 310 GLY A C     1 
ATOM   4811  O  O     A GLY A 1 310 ? 6.187   4.517   50.417  0.20 44.81  ? 310 GLY A O     1 
ATOM   4812  O  O     B GLY A 1 310 ? 6.206   4.775   50.257  0.80 44.58  ? 310 GLY A O     1 
ATOM   4813  N  N     A LYS A 1 311 ? 5.248   5.815   48.831  0.20 39.58  ? 311 LYS A N     1 
ATOM   4814  N  N     B LYS A 1 311 ? 4.960   5.529   48.540  0.80 38.79  ? 311 LYS A N     1 
ATOM   4815  C  CA    A LYS A 1 311 ? 4.111   6.222   49.638  0.20 40.33  ? 311 LYS A CA    1 
ATOM   4816  C  CA    B LYS A 1 311 ? 3.903   6.048   49.391  0.80 40.49  ? 311 LYS A CA    1 
ATOM   4817  C  C     A LYS A 1 311 ? 2.818   5.717   49.010  0.20 37.40  ? 311 LYS A C     1 
ATOM   4818  C  C     B LYS A 1 311 ? 2.547   5.719   48.782  0.80 37.48  ? 311 LYS A C     1 
ATOM   4819  O  O     A LYS A 1 311 ? 2.752   5.435   47.809  0.20 33.87  ? 311 LYS A O     1 
ATOM   4820  O  O     B LYS A 1 311 ? 2.387   5.697   47.558  0.80 33.42  ? 311 LYS A O     1 
ATOM   4821  C  CB    A LYS A 1 311 ? 4.062   7.748   49.799  0.20 41.89  ? 311 LYS A CB    1 
ATOM   4822  C  CB    B LYS A 1 311 ? 4.065   7.558   49.607  0.80 41.32  ? 311 LYS A CB    1 
ATOM   4823  C  CG    A LYS A 1 311 ? 5.264   8.332   50.526  0.20 45.02  ? 311 LYS A CG    1 
ATOM   4824  C  CG    B LYS A 1 311 ? 5.231   7.899   50.532  0.80 44.40  ? 311 LYS A CG    1 
ATOM   4825  C  CD    A LYS A 1 311 ? 5.142   9.840   50.675  0.20 51.65  ? 311 LYS A CD    1 
ATOM   4826  C  CD    B LYS A 1 311 ? 5.561   9.377   50.525  0.80 54.07  ? 311 LYS A CD    1 
ATOM   4827  C  CE    A LYS A 1 311 ? 6.346   10.426  51.398  0.20 54.77  ? 311 LYS A CE    1 
ATOM   4828  C  CE    B LYS A 1 311 ? 6.922   9.633   51.166  0.80 54.65  ? 311 LYS A CE    1 
ATOM   4829  N  NZ    A LYS A 1 311 ? 6.491   9.872   52.771  0.20 55.34  ? 311 LYS A NZ    1 
ATOM   4830  N  NZ    B LYS A 1 311 ? 7.010   9.053   52.535  0.80 62.39  ? 311 LYS A NZ    1 
ATOM   4831  N  N     A TYR A 1 312 ? 1.790   5.598   49.846  0.20 34.13  ? 312 TYR A N     1 
ATOM   4832  N  N     B TYR A 1 312 ? 1.584   5.439   49.656  0.80 31.59  ? 312 TYR A N     1 
ATOM   4833  C  CA    A TYR A 1 312 ? 0.477   5.134   49.425  0.20 34.72  ? 312 TYR A CA    1 
ATOM   4834  C  CA    B TYR A 1 312 ? 0.245   5.035   49.259  0.80 34.60  ? 312 TYR A CA    1 
ATOM   4835  C  C     A TYR A 1 312 ? -0.430  6.315   49.110  0.20 35.27  ? 312 TYR A C     1 
ATOM   4836  C  C     B TYR A 1 312 ? -0.643  6.240   48.980  0.80 35.01  ? 312 TYR A C     1 
ATOM   4837  O  O     A TYR A 1 312 ? -0.373  7.353   49.777  0.20 35.31  ? 312 TYR A O     1 
ATOM   4838  O  O     B TYR A 1 312 ? -0.599  7.241   49.705  0.80 35.08  ? 312 TYR A O     1 
ATOM   4839  C  CB    A TYR A 1 312 ? -0.166  4.261   50.505  0.20 34.61  ? 312 TYR A CB    1 
ATOM   4840  C  CB    B TYR A 1 312 ? -0.392  4.183   50.359  0.80 33.78  ? 312 TYR A CB    1 
ATOM   4841  C  CG    A TYR A 1 312 ? 0.397   2.860   50.574  0.20 32.40  ? 312 TYR A CG    1 
ATOM   4842  C  CG    B TYR A 1 312 ? 0.195   2.800   50.485  0.80 31.68  ? 312 TYR A CG    1 
ATOM   4843  C  CD1   A TYR A 1 312 ? -0.115  1.848   49.773  0.20 34.10  ? 312 TYR A CD1   1 
ATOM   4844  C  CD1   B TYR A 1 312 ? -0.283  1.760   49.704  0.80 34.46  ? 312 TYR A CD1   1 
ATOM   4845  C  CD2   A TYR A 1 312 ? 1.438   2.548   51.439  0.20 32.21  ? 312 TYR A CD2   1 
ATOM   4846  C  CD2   B TYR A 1 312 ? 1.213   2.525   51.395  0.80 30.95  ? 312 TYR A CD2   1 
ATOM   4847  C  CE1   A TYR A 1 312 ? 0.396   0.564   49.828  0.20 33.18  ? 312 TYR A CE1   1 
ATOM   4848  C  CE1   B TYR A 1 312 ? 0.242   0.482   49.808  0.80 33.30  ? 312 TYR A CE1   1 
ATOM   4849  C  CE2   A TYR A 1 312 ? 1.956   1.263   51.501  0.20 32.47  ? 312 TYR A CE2   1 
ATOM   4850  C  CE2   B TYR A 1 312 ? 1.745   1.235   51.508  0.80 31.65  ? 312 TYR A CE2   1 
ATOM   4851  C  CZ    A TYR A 1 312 ? 1.428   0.277   50.694  0.20 33.34  ? 312 TYR A CZ    1 
ATOM   4852  C  CZ    B TYR A 1 312 ? 1.247   0.223   50.710  0.80 33.10  ? 312 TYR A CZ    1 
ATOM   4853  O  OH    A TYR A 1 312 ? 1.935   -1.002  50.749  0.20 34.38  ? 312 TYR A OH    1 
ATOM   4854  O  OH    B TYR A 1 312 ? 1.743   -1.059  50.791  0.80 34.01  ? 312 TYR A OH    1 
ATOM   4855  N  N     A MET A 1 313 ? -1.267  6.146   48.085  0.20 32.52  ? 313 MET A N     1 
ATOM   4856  N  N     B MET A 1 313 ? -1.464  6.124   47.931  0.80 32.33  ? 313 MET A N     1 
ATOM   4857  C  CA    A MET A 1 313 ? -2.262  7.136   47.700  0.20 32.29  ? 313 MET A CA    1 
ATOM   4858  C  CA    B MET A 1 313 ? -2.533  7.072   47.627  0.80 31.09  ? 313 MET A CA    1 
ATOM   4859  C  C     A MET A 1 313 ? -3.690  6.613   47.751  0.20 35.08  ? 313 MET A C     1 
ATOM   4860  C  C     B MET A 1 313 ? -3.927  6.474   47.778  0.80 34.87  ? 313 MET A C     1 
ATOM   4861  O  O     A MET A 1 313 ? -4.624  7.421   47.804  0.20 38.28  ? 313 MET A O     1 
ATOM   4862  O  O     B MET A 1 313 ? -4.893  7.221   47.950  0.80 38.83  ? 313 MET A O     1 
ATOM   4863  C  CB    A MET A 1 313 ? -1.976  7.657   46.281  0.20 35.30  ? 313 MET A CB    1 
ATOM   4864  C  CB    B MET A 1 313 ? -2.392  7.607   46.190  0.80 34.88  ? 313 MET A CB    1 
ATOM   4865  C  CG    A MET A 1 313 ? -0.613  8.324   46.128  0.20 34.64  ? 313 MET A CG    1 
ATOM   4866  C  CG    B MET A 1 313 ? -1.047  8.265   45.861  0.80 35.38  ? 313 MET A CG    1 
ATOM   4867  S  SD    A MET A 1 313 ? -0.101  8.517   44.406  0.20 31.22  ? 313 MET A SD    1 
ATOM   4868  S  SD    B MET A 1 313 ? -0.817  8.539   44.076  0.80 37.15  ? 313 MET A SD    1 
ATOM   4869  C  CE    A MET A 1 313 ? 0.136   6.807   43.932  0.20 34.54  ? 313 MET A CE    1 
ATOM   4870  C  CE    B MET A 1 313 ? 0.237   7.155   43.654  0.80 36.82  ? 313 MET A CE    1 
ATOM   4871  N  N     A ALA A 1 314 ? -3.881  5.295   47.739  0.20 29.12  ? 314 ALA A N     1 
ATOM   4872  N  N     B ALA A 1 314 ? -4.048  5.156   47.702  0.80 27.86  ? 314 ALA A N     1 
ATOM   4873  C  CA    A ALA A 1 314 ? -5.194  4.671   47.820  0.20 30.42  ? 314 ALA A CA    1 
ATOM   4874  C  CA    B ALA A 1 314 ? -5.316  4.457   47.816  0.80 30.22  ? 314 ALA A CA    1 
ATOM   4875  C  C     A ALA A 1 314 ? -5.012  3.193   48.128  0.20 31.12  ? 314 ALA A C     1 
ATOM   4876  C  C     B ALA A 1 314 ? -5.010  3.027   48.229  0.80 31.25  ? 314 ALA A C     1 
ATOM   4877  O  O     A ALA A 1 314 ? -4.191  2.522   47.492  0.20 30.48  ? 314 ALA A O     1 
ATOM   4878  O  O     B ALA A 1 314 ? -3.906  2.521   48.008  0.80 31.01  ? 314 ALA A O     1 
ATOM   4879  C  CB    A ALA A 1 314 ? -5.980  4.862   46.525  0.20 29.73  ? 314 ALA A CB    1 
ATOM   4880  C  CB    B ALA A 1 314 ? -6.101  4.487   46.507  0.80 28.54  ? 314 ALA A CB    1 
ATOM   4881  N  N     A CYS A 1 315 ? -5.756  2.673   49.103  0.20 27.81  ? 315 CYS A N     1 
ATOM   4882  N  N     B CYS A 1 315 ? -5.994  2.387   48.849  0.80 25.16  ? 315 CYS A N     1 
ATOM   4883  C  CA    A CYS A 1 315 ? -5.591  1.291   49.533  0.20 29.55  ? 315 CYS A CA    1 
ATOM   4884  C  CA    B CYS A 1 315 ? -5.816  1.020   49.326  0.80 27.92  ? 315 CYS A CA    1 
ATOM   4885  C  C     A CYS A 1 315 ? -6.958  0.700   49.836  0.20 33.04  ? 315 CYS A C     1 
ATOM   4886  C  C     B CYS A 1 315 ? -7.191  0.431   49.616  0.80 33.10  ? 315 CYS A C     1 
ATOM   4887  O  O     A CYS A 1 315 ? -7.662  1.187   50.725  0.20 32.49  ? 315 CYS A O     1 
ATOM   4888  O  O     B CYS A 1 315 ? -7.853  0.845   50.575  0.80 32.61  ? 315 CYS A O     1 
ATOM   4889  C  CB    A CYS A 1 315 ? -4.680  1.206   50.760  0.20 35.54  ? 315 CYS A CB    1 
ATOM   4890  C  CB    B CYS A 1 315 ? -4.935  0.989   50.567  0.80 35.93  ? 315 CYS A CB    1 
ATOM   4891  S  SG    A CYS A 1 315 ? -4.240  -0.473  51.236  0.20 45.35  ? 315 CYS A SG    1 
ATOM   4892  S  SG    B CYS A 1 315 ? -4.357  -0.663  50.976  0.80 50.54  ? 315 CYS A SG    1 
ATOM   4893  N  N     A CYS A 1 316 ? -7.324  -0.350  49.107  0.20 26.63  ? 316 CYS A N     1 
ATOM   4894  N  N     B CYS A 1 316 ? -7.608  -0.520  48.785  0.80 24.26  ? 316 CYS A N     1 
ATOM   4895  C  CA    A CYS A 1 316 ? -8.614  -1.003  49.264  0.20 28.96  ? 316 CYS A CA    1 
ATOM   4896  C  CA    B CYS A 1 316 ? -8.844  -1.270  48.952  0.80 28.49  ? 316 CYS A CA    1 
ATOM   4897  C  C     A CYS A 1 316 ? -8.405  -2.493  49.485  0.20 31.46  ? 316 CYS A C     1 
ATOM   4898  C  C     B CYS A 1 316 ? -8.491  -2.721  49.242  0.80 33.73  ? 316 CYS A C     1 
ATOM   4899  O  O     A CYS A 1 316 ? -7.529  -3.105  48.865  0.20 28.20  ? 316 CYS A O     1 
ATOM   4900  O  O     B CYS A 1 316 ? -7.624  -3.291  48.570  0.80 27.70  ? 316 CYS A O     1 
ATOM   4901  C  CB    A CYS A 1 316 ? -9.508  -0.760  48.044  0.20 27.01  ? 316 CYS A CB    1 
ATOM   4902  C  CB    B CYS A 1 316 ? -9.712  -1.202  47.695  0.80 26.27  ? 316 CYS A CB    1 
ATOM   4903  S  SG    A CYS A 1 316 ? -9.867  0.989   47.739  0.20 29.00  ? 316 CYS A SG    1 
ATOM   4904  S  SG    B CYS A 1 316 ? -10.158 0.451   47.161  0.80 38.08  ? 316 CYS A SG    1 
ATOM   4905  N  N     A LEU A 1 317 ? -9.212  -3.068  50.372  0.20 27.42  ? 317 LEU A N     1 
ATOM   4906  N  N     B LEU A 1 317 ? -9.158  -3.310  50.232  0.80 26.35  ? 317 LEU A N     1 
ATOM   4907  C  CA    A LEU A 1 317 ? -9.103  -4.467  50.757  0.20 25.83  ? 317 LEU A CA    1 
ATOM   4908  C  CA    B LEU A 1 317 ? -9.005  -4.722  50.568  0.80 24.96  ? 317 LEU A CA    1 
ATOM   4909  C  C     A LEU A 1 317 ? -10.257 -5.271  50.176  0.20 25.31  ? 317 LEU A C     1 
ATOM   4910  C  C     B LEU A 1 317 ? -10.326 -5.437  50.331  0.80 25.25  ? 317 LEU A C     1 
ATOM   4911  O  O     A LEU A 1 317 ? -11.410 -4.827  50.187  0.20 28.62  ? 317 LEU A O     1 
ATOM   4912  O  O     B LEU A 1 317 ? -11.351 -5.080  50.927  0.80 29.13  ? 317 LEU A O     1 
ATOM   4913  C  CB    A LEU A 1 317 ? -9.083  -4.619  52.280  0.20 27.42  ? 317 LEU A CB    1 
ATOM   4914  C  CB    B LEU A 1 317 ? -8.532  -4.899  52.011  0.80 24.95  ? 317 LEU A CB    1 
ATOM   4915  C  CG    A LEU A 1 317 ? -7.696  -4.518  52.912  0.20 28.48  ? 317 LEU A CG    1 
ATOM   4916  C  CG    B LEU A 1 317 ? -7.194  -4.202  52.287  0.80 28.44  ? 317 LEU A CG    1 
ATOM   4917  C  CD1   A LEU A 1 317 ? -7.782  -4.547  54.426  0.20 20.70  ? 317 LEU A CD1   1 
ATOM   4918  C  CD1   B LEU A 1 317 ? -7.332  -3.183  53.405  0.80 33.97  ? 317 LEU A CD1   1 
ATOM   4919  C  CD2   A LEU A 1 317 ? -6.827  -5.651  52.401  0.20 27.63  ? 317 LEU A CD2   1 
ATOM   4920  C  CD2   B LEU A 1 317 ? -6.133  -5.227  52.624  0.80 29.52  ? 317 LEU A CD2   1 
ATOM   4921  N  N     A LEU A 1 318 ? -9.937  -6.462  49.677  0.20 24.38  ? 318 LEU A N     1 
ATOM   4922  N  N     B LEU A 1 318 ? -10.292 -6.460  49.477  0.80 22.44  ? 318 LEU A N     1 
ATOM   4923  C  CA    A LEU A 1 318 ? -10.923 -7.380  49.113  0.20 24.31  ? 318 LEU A CA    1 
ATOM   4924  C  CA    B LEU A 1 318 ? -11.472 -7.174  49.004  0.80 21.86  ? 318 LEU A CA    1 
ATOM   4925  C  C     A LEU A 1 318 ? -10.744 -8.732  49.798  0.20 26.28  ? 318 LEU A C     1 
ATOM   4926  C  C     B LEU A 1 318 ? -11.405 -8.605  49.523  0.80 26.53  ? 318 LEU A C     1 
ATOM   4927  O  O     A LEU A 1 318 ? -9.835  -9.495  49.459  0.20 21.07  ? 318 LEU A O     1 
ATOM   4928  O  O     B LEU A 1 318 ? -10.565 -9.394  49.075  0.80 24.64  ? 318 LEU A O     1 
ATOM   4929  C  CB    A LEU A 1 318 ? -10.769 -7.492  47.598  0.20 27.31  ? 318 LEU A CB    1 
ATOM   4930  C  CB    B LEU A 1 318 ? -11.525 -7.149  47.476  0.80 32.09  ? 318 LEU A CB    1 
ATOM   4931  C  CG    A LEU A 1 318 ? -10.963 -6.198  46.806  0.20 28.59  ? 318 LEU A CG    1 
ATOM   4932  C  CG    B LEU A 1 318 ? -11.529 -5.769  46.823  0.80 31.27  ? 318 LEU A CG    1 
ATOM   4933  C  CD1   A LEU A 1 318 ? -10.695 -6.434  45.327  0.20 30.99  ? 318 LEU A CD1   1 
ATOM   4934  C  CD1   B LEU A 1 318 ? -11.016 -5.868  45.389  0.80 36.33  ? 318 LEU A CD1   1 
ATOM   4935  C  CD2   A LEU A 1 318 ? -12.363 -5.630  47.019  0.20 31.74  ? 318 LEU A CD2   1 
ATOM   4936  C  CD2   B LEU A 1 318 ? -12.944 -5.198  46.855  0.80 31.66  ? 318 LEU A CD2   1 
ATOM   4937  N  N     A TYR A 1 319 ? -11.597 -9.016  50.776  0.20 22.40  ? 319 TYR A N     1 
ATOM   4938  N  N     B TYR A 1 319 ? -12.269 -8.939  50.477  0.80 25.48  ? 319 TYR A N     1 
ATOM   4939  C  CA    A TYR A 1 319 ? -11.624 -10.308 51.438  0.20 22.66  ? 319 TYR A CA    1 
ATOM   4940  C  CA    B TYR A 1 319 ? -12.223 -10.240 51.125  0.80 21.57  ? 319 TYR A CA    1 
ATOM   4941  C  C     A TYR A 1 319 ? -12.685 -11.193 50.798  0.20 22.38  ? 319 TYR A C     1 
ATOM   4942  C  C     B TYR A 1 319 ? -13.229 -11.194 50.501  0.80 22.21  ? 319 TYR A C     1 
ATOM   4943  O  O     A TYR A 1 319 ? -13.723 -10.712 50.337  0.20 24.48  ? 319 TYR A O     1 
ATOM   4944  O  O     B TYR A 1 319 ? -14.312 -10.796 50.060  0.80 24.23  ? 319 TYR A O     1 
ATOM   4945  C  CB    A TYR A 1 319 ? -11.906 -10.156 52.935  0.20 22.43  ? 319 TYR A CB    1 
ATOM   4946  C  CB    B TYR A 1 319 ? -12.504 -10.126 52.628  0.80 23.61  ? 319 TYR A CB    1 
ATOM   4947  C  CG    A TYR A 1 319 ? -10.814 -9.440  53.698  0.20 23.83  ? 319 TYR A CG    1 
ATOM   4948  C  CG    B TYR A 1 319 ? -11.403 -9.471  53.409  0.80 21.55  ? 319 TYR A CG    1 
ATOM   4949  C  CD1   A TYR A 1 319 ? -9.726  -10.137 54.206  0.20 23.45  ? 319 TYR A CD1   1 
ATOM   4950  C  CD1   B TYR A 1 319 ? -11.391 -8.102  53.608  0.80 19.93  ? 319 TYR A CD1   1 
ATOM   4951  C  CD2   A TYR A 1 319 ? -10.872 -8.069  53.912  0.20 22.57  ? 319 TYR A CD2   1 
ATOM   4952  C  CD2   B TYR A 1 319 ? -10.353 -10.225 53.941  0.80 20.84  ? 319 TYR A CD2   1 
ATOM   4953  C  CE1   A TYR A 1 319 ? -8.723  -9.488  54.904  0.20 24.62  ? 319 TYR A CE1   1 
ATOM   4954  C  CE1   B TYR A 1 319 ? -10.363 -7.486  54.321  0.80 22.14  ? 319 TYR A CE1   1 
ATOM   4955  C  CE2   A TYR A 1 319 ? -9.875  -7.410  54.611  0.20 21.93  ? 319 TYR A CE2   1 
ATOM   4956  C  CE2   B TYR A 1 319 ? -9.327  -9.617  54.656  0.80 24.17  ? 319 TYR A CE2   1 
ATOM   4957  C  CZ    A TYR A 1 319 ? -8.804  -8.126  55.104  0.20 25.12  ? 319 TYR A CZ    1 
ATOM   4958  C  CZ    B TYR A 1 319 ? -9.343  -8.243  54.840  0.80 24.95  ? 319 TYR A CZ    1 
ATOM   4959  O  OH    A TYR A 1 319 ? -7.808  -7.480  55.799  0.20 26.60  ? 319 TYR A OH    1 
ATOM   4960  O  OH    B TYR A 1 319 ? -8.345  -7.615  55.551  0.80 24.51  ? 319 TYR A OH    1 
ATOM   4961  N  N     A ARG A 1 320 ? -12.407 -12.496 50.760  0.20 21.87  ? 320 ARG A N     1 
ATOM   4962  N  N     B ARG A 1 320 ? -12.860 -12.472 50.475  0.80 22.36  ? 320 ARG A N     1 
ATOM   4963  C  CA    A ARG A 1 320 ? -13.342 -13.480 50.216  0.20 25.08  ? 320 ARG A CA    1 
ATOM   4964  C  CA    B ARG A 1 320 ? -13.760 -13.537 50.054  0.80 24.99  ? 320 ARG A CA    1 
ATOM   4965  C  C     A ARG A 1 320 ? -13.307 -14.716 51.105  0.20 27.06  ? 320 ARG A C     1 
ATOM   4966  C  C     B ARG A 1 320 ? -13.730 -14.637 51.100  0.80 28.71  ? 320 ARG A C     1 
ATOM   4967  O  O     A ARG A 1 320 ? -12.296 -15.424 51.144  0.20 26.37  ? 320 ARG A O     1 
ATOM   4968  O  O     B ARG A 1 320 ? -12.667 -15.208 51.366  0.80 29.06  ? 320 ARG A O     1 
ATOM   4969  C  CB    A ARG A 1 320 ? -12.998 -13.840 48.767  0.20 22.92  ? 320 ARG A CB    1 
ATOM   4970  C  CB    B ARG A 1 320 ? -13.358 -14.113 48.690  0.80 20.94  ? 320 ARG A CB    1 
ATOM   4971  C  CG    A ARG A 1 320 ? -13.260 -12.722 47.766  0.20 28.36  ? 320 ARG A CG    1 
ATOM   4972  C  CG    B ARG A 1 320 ? -13.264 -13.104 47.595  0.80 31.25  ? 320 ARG A CG    1 
ATOM   4973  C  CD    A ARG A 1 320 ? -12.843 -13.109 46.349  0.20 27.38  ? 320 ARG A CD    1 
ATOM   4974  C  CD    B ARG A 1 320 ? -12.841 -13.787 46.306  0.80 26.11  ? 320 ARG A CD    1 
ATOM   4975  N  NE    A ARG A 1 320 ? -13.784 -14.027 45.715  0.20 28.07  ? 320 ARG A NE    1 
ATOM   4976  N  NE    B ARG A 1 320 ? -13.960 -14.436 45.632  0.80 26.24  ? 320 ARG A NE    1 
ATOM   4977  C  CZ    A ARG A 1 320 ? -13.692 -14.439 44.456  0.20 32.62  ? 320 ARG A CZ    1 
ATOM   4978  C  CZ    B ARG A 1 320 ? -13.953 -14.759 44.344  0.80 34.45  ? 320 ARG A CZ    1 
ATOM   4979  N  NH1   A ARG A 1 320 ? -12.703 -14.046 43.671  0.20 28.80  ? 320 ARG A NH1   1 
ATOM   4980  N  NH1   B ARG A 1 320 ? -12.894 -14.531 43.582  0.80 29.66  ? 320 ARG A NH1   1 
ATOM   4981  N  NH2   A ARG A 1 320 ? -14.619 -15.262 43.973  0.20 31.72  ? 320 ARG A NH2   1 
ATOM   4982  N  NH2   B ARG A 1 320 ? -15.038 -15.309 43.805  0.80 31.04  ? 320 ARG A NH2   1 
ATOM   4983  N  N     A GLY A 1 321 ? -14.405 -14.974 51.825  0.20 25.33  ? 321 GLY A N     1 
ATOM   4984  N  N     B GLY A 1 321 ? -14.888 -14.939 51.694  0.80 22.39  ? 321 GLY A N     1 
ATOM   4985  C  CA    A GLY A 1 321 ? -14.540 -16.198 52.579  0.20 22.64  ? 321 GLY A CA    1 
ATOM   4986  C  CA    B GLY A 1 321 ? -15.045 -16.149 52.473  0.80 21.72  ? 321 GLY A CA    1 
ATOM   4987  C  C     A GLY A 1 321 ? -14.995 -15.933 54.000  0.20 22.91  ? 321 GLY A C     1 
ATOM   4988  C  C     B GLY A 1 321 ? -15.448 -15.842 53.909  0.80 20.83  ? 321 GLY A C     1 
ATOM   4989  O  O     A GLY A 1 321 ? -15.594 -14.894 54.301  0.20 25.38  ? 321 GLY A O     1 
ATOM   4990  O  O     B GLY A 1 321 ? -16.236 -14.922 54.162  0.80 24.85  ? 321 GLY A O     1 
ATOM   4991  N  N     A ASP A 1 322 ? -14.702 -16.895 54.877  0.20 23.61  ? 322 ASP A N     1 
ATOM   4992  N  N     B ASP A 1 322 ? -14.876 -16.603 54.845  0.80 22.51  ? 322 ASP A N     1 
ATOM   4993  C  CA    A ASP A 1 322 ? -15.124 -16.861 56.279  0.20 25.87  ? 322 ASP A CA    1 
ATOM   4994  C  CA    B ASP A 1 322 ? -15.327 -16.602 56.244  0.80 25.31  ? 322 ASP A CA    1 
ATOM   4995  C  C     A ASP A 1 322 ? -14.346 -15.764 57.001  0.20 24.30  ? 322 ASP A C     1 
ATOM   4996  C  C     B ASP A 1 322 ? -14.575 -15.511 57.000  0.80 22.09  ? 322 ASP A C     1 
ATOM   4997  O  O     A ASP A 1 322 ? -13.324 -15.999 57.649  0.20 29.17  ? 322 ASP A O     1 
ATOM   4998  O  O     B ASP A 1 322 ? -13.594 -15.753 57.703  0.80 29.05  ? 322 ASP A O     1 
ATOM   4999  C  CB    A ASP A 1 322 ? -14.910 -18.222 56.932  0.20 29.57  ? 322 ASP A CB    1 
ATOM   5000  C  CB    B ASP A 1 322 ? -15.120 -17.973 56.875  0.80 29.39  ? 322 ASP A CB    1 
ATOM   5001  C  CG    A ASP A 1 322 ? -15.338 -18.251 58.394  0.20 31.07  ? 322 ASP A CG    1 
ATOM   5002  C  CG    B ASP A 1 322 ? -15.495 -18.002 58.371  0.80 31.65  ? 322 ASP A CG    1 
ATOM   5003  O  OD1   A ASP A 1 322 ? -16.076 -17.343 58.831  0.20 28.72  ? 322 ASP A OD1   1 
ATOM   5004  O  OD1   B ASP A 1 322 ? -16.321 -17.172 58.815  0.80 29.03  ? 322 ASP A OD1   1 
ATOM   5005  O  OD2   A ASP A 1 322 ? -14.925 -19.186 59.110  0.20 32.01  ? 322 ASP A OD2   1 
ATOM   5006  O  OD2   B ASP A 1 322 ? -14.935 -18.842 59.102  0.80 31.78  ? 322 ASP A OD2   1 
ATOM   5007  N  N     A VAL A 1 323 ? -14.851 -14.537 56.884  0.20 26.40  ? 323 VAL A N     1 
ATOM   5008  N  N     B VAL A 1 323 ? -15.080 -14.287 56.870  0.80 27.44  ? 323 VAL A N     1 
ATOM   5009  C  CA    A VAL A 1 323 ? -14.203 -13.352 57.432  0.20 24.55  ? 323 VAL A CA    1 
ATOM   5010  C  CA    B VAL A 1 323 ? -14.368 -13.072 57.246  0.80 24.36  ? 323 VAL A CA    1 
ATOM   5011  C  C     A VAL A 1 323 ? -15.224 -12.580 58.257  0.20 30.78  ? 323 VAL A C     1 
ATOM   5012  C  C     B VAL A 1 323 ? -15.304 -12.210 58.088  0.80 32.84  ? 323 VAL A C     1 
ATOM   5013  O  O     A VAL A 1 323 ? -16.344 -12.336 57.795  0.20 26.72  ? 323 VAL A O     1 
ATOM   5014  O  O     B VAL A 1 323 ? -16.295 -11.683 57.573  0.80 25.46  ? 323 VAL A O     1 
ATOM   5015  C  CB    A VAL A 1 323 ? -13.619 -12.459 56.319  0.20 26.53  ? 323 VAL A CB    1 
ATOM   5016  C  CB    B VAL A 1 323 ? -13.887 -12.303 56.004  0.80 24.41  ? 323 VAL A CB    1 
ATOM   5017  C  CG1   A VAL A 1 323 ? -12.994 -11.211 56.909  0.20 25.79  ? 323 VAL A CG1   1 
ATOM   5018  C  CG1   B VAL A 1 323 ? -13.294 -10.971 56.387  0.80 24.83  ? 323 VAL A CG1   1 
ATOM   5019  C  CG2   A VAL A 1 323 ? -12.596 -13.228 55.503  0.20 28.26  ? 323 VAL A CG2   1 
ATOM   5020  C  CG2   B VAL A 1 323 ? -12.875 -13.136 55.237  0.80 29.96  ? 323 VAL A CG2   1 
ATOM   5021  N  N     A VAL A 1 324 ? -14.839 -12.199 59.466  0.20 28.50  ? 324 VAL A N     1 
ATOM   5022  N  N     B VAL A 1 324 ? -14.985 -12.048 59.370  0.80 29.18  ? 324 VAL A N     1 
ATOM   5023  C  CA    A VAL A 1 324 ? -15.672 -11.384 60.348  0.20 27.47  ? 324 VAL A CA    1 
ATOM   5024  C  CA    B VAL A 1 324 ? -15.825 -11.260 60.270  0.80 27.15  ? 324 VAL A CA    1 
ATOM   5025  C  C     A VAL A 1 324 ? -15.232 -9.931  60.210  0.20 24.23  ? 324 VAL A C     1 
ATOM   5026  C  C     B VAL A 1 324 ? -15.360 -9.805  60.262  0.80 22.83  ? 324 VAL A C     1 
ATOM   5027  O  O     A VAL A 1 324 ? -14.028 -9.652  60.313  0.20 28.73  ? 324 VAL A O     1 
ATOM   5028  O  O     B VAL A 1 324 ? -14.167 -9.530  60.471  0.80 28.49  ? 324 VAL A O     1 
ATOM   5029  C  CB    A VAL A 1 324 ? -15.569 -11.849 61.813  0.20 27.50  ? 324 VAL A CB    1 
ATOM   5030  C  CB    B VAL A 1 324 ? -15.827 -11.869 61.684  0.80 27.76  ? 324 VAL A CB    1 
ATOM   5031  C  CG1   A VAL A 1 324 ? -16.385 -10.940 62.719  0.20 31.24  ? 324 VAL A CG1   1 
ATOM   5032  C  CG1   B VAL A 1 324 ? -16.685 -11.041 62.624  0.80 31.94  ? 324 VAL A CG1   1 
ATOM   5033  C  CG2   A VAL A 1 324 ? -16.035 -13.292 61.940  0.20 27.68  ? 324 VAL A CG2   1 
ATOM   5034  C  CG2   B VAL A 1 324 ? -16.370 -13.301 61.617  0.80 24.86  ? 324 VAL A CG2   1 
ATOM   5035  N  N     A PRO A 1 325 ? -16.151 -8.993  59.966  0.20 27.51  ? 325 PRO A N     1 
ATOM   5036  N  N     B PRO A 1 325 ? -16.254 -8.850  59.980  0.80 27.43  ? 325 PRO A N     1 
ATOM   5037  C  CA    A PRO A 1 325 ? -15.737 -7.588  59.808  0.20 26.13  ? 325 PRO A CA    1 
ATOM   5038  C  CA    B PRO A 1 325 ? -15.815 -7.451  59.808  0.80 25.40  ? 325 PRO A CA    1 
ATOM   5039  C  C     A PRO A 1 325 ? -15.000 -7.030  61.013  0.20 32.45  ? 325 PRO A C     1 
ATOM   5040  C  C     B PRO A 1 325 ? -15.013 -6.895  60.977  0.80 33.02  ? 325 PRO A C     1 
ATOM   5041  O  O     A PRO A 1 325 ? -14.161 -6.134  60.850  0.20 27.98  ? 325 PRO A O     1 
ATOM   5042  O  O     B PRO A 1 325 ? -14.031 -6.174  60.748  0.80 26.74  ? 325 PRO A O     1 
ATOM   5043  C  CB    A PRO A 1 325 ? -17.067 -6.859  59.569  0.20 29.83  ? 325 PRO A CB    1 
ATOM   5044  C  CB    B PRO A 1 325 ? -17.138 -6.706  59.599  0.80 30.17  ? 325 PRO A CB    1 
ATOM   5045  C  CG    A PRO A 1 325 ? -17.965 -7.903  58.989  0.20 30.10  ? 325 PRO A CG    1 
ATOM   5046  C  CG    B PRO A 1 325 ? -18.035 -7.725  58.956  0.80 30.57  ? 325 PRO A CG    1 
ATOM   5047  C  CD    A PRO A 1 325 ? -17.577 -9.193  59.655  0.20 26.85  ? 325 PRO A CD    1 
ATOM   5048  C  CD    B PRO A 1 325 ? -17.632 -9.070  59.507  0.80 26.53  ? 325 PRO A CD    1 
ATOM   5049  N  N     A LYS A 1 326 ? -15.279 -7.537  62.218  0.20 29.79  ? 326 LYS A N     1 
ATOM   5050  N  N     B LYS A 1 326 ? -15.389 -7.214  62.223  0.80 28.55  ? 326 LYS A N     1 
ATOM   5051  C  CA    A LYS A 1 326 ? -14.565 -7.066  63.401  0.20 31.34  ? 326 LYS A CA    1 
ATOM   5052  C  CA    B LYS A 1 326 ? -14.597 -6.774  63.373  0.80 30.49  ? 326 LYS A CA    1 
ATOM   5053  C  C     A LYS A 1 326 ? -13.093 -7.461  63.358  0.20 33.50  ? 326 LYS A C     1 
ATOM   5054  C  C     B LYS A 1 326 ? -13.176 -7.350  63.355  0.80 33.64  ? 326 LYS A C     1 
ATOM   5055  O  O     A LYS A 1 326 ? -12.223 -6.680  63.762  0.20 30.22  ? 326 LYS A O     1 
ATOM   5056  O  O     B LYS A 1 326 ? -12.239 -6.701  63.841  0.80 30.03  ? 326 LYS A O     1 
ATOM   5057  C  CB    A LYS A 1 326 ? -15.228 -7.609  64.667  0.20 32.47  ? 326 LYS A CB    1 
ATOM   5058  C  CB    B LYS A 1 326 ? -15.313 -7.150  64.681  0.80 31.75  ? 326 LYS A CB    1 
ATOM   5059  C  CG    A LYS A 1 326 ? -14.560 -7.155  65.952  0.20 34.61  ? 326 LYS A CG    1 
ATOM   5060  C  CG    B LYS A 1 326 ? -15.455 -8.639  64.878  0.80 36.79  ? 326 LYS A CG    1 
ATOM   5061  C  CD    A LYS A 1 326 ? -15.125 -7.891  67.157  0.20 37.61  ? 326 LYS A CD    1 
ATOM   5062  C  CD    B LYS A 1 326 ? -16.038 -9.019  66.232  0.80 47.71  ? 326 LYS A CD    1 
ATOM   5063  C  CE    A LYS A 1 326 ? -14.937 -9.392  67.008  0.20 42.75  ? 326 LYS A CE    1 
ATOM   5064  C  CE    B LYS A 1 326 ? -16.192 -10.542 66.325  0.80 59.50  ? 326 LYS A CE    1 
ATOM   5065  N  NZ    A LYS A 1 326 ? -13.517 -9.754  66.731  0.20 35.63  ? 326 LYS A NZ    1 
ATOM   5066  N  NZ    B LYS A 1 326 ? -15.018 -11.284 65.745  0.80 51.25  ? 326 LYS A NZ    1 
ATOM   5067  N  N     A ASP A 1 327 ? -12.793 -8.671  62.876  0.20 32.10  ? 327 ASP A N     1 
ATOM   5068  N  N     B ASP A 1 327 ? -12.983 -8.556  62.800  0.80 32.97  ? 327 ASP A N     1 
ATOM   5069  C  CA    A ASP A 1 327 ? -11.398 -9.071  62.729  0.20 31.70  ? 327 ASP A CA    1 
ATOM   5070  C  CA    B ASP A 1 327 ? -11.630 -9.096  62.719  0.80 30.73  ? 327 ASP A CA    1 
ATOM   5071  C  C     A ASP A 1 327 ? -10.685 -8.222  61.684  0.20 33.07  ? 327 ASP A C     1 
ATOM   5072  C  C     B ASP A 1 327 ? -10.781 -8.325  61.707  0.80 33.33  ? 327 ASP A C     1 
ATOM   5073  O  O     A ASP A 1 327 ? -9.465  -8.040  61.763  0.20 33.10  ? 327 ASP A O     1 
ATOM   5074  O  O     B ASP A 1 327 ? -9.569  -8.174  61.907  0.80 32.92  ? 327 ASP A O     1 
ATOM   5075  C  CB    A ASP A 1 327 ? -11.305 -10.554 62.368  0.20 29.82  ? 327 ASP A CB    1 
ATOM   5076  C  CB    B ASP A 1 327 ? -11.644 -10.584 62.352  0.80 29.31  ? 327 ASP A CB    1 
ATOM   5077  C  CG    A ASP A 1 327 ? -11.733 -11.457 63.504  0.20 37.21  ? 327 ASP A CG    1 
ATOM   5078  C  CG    B ASP A 1 327 ? -12.132 -11.469 63.478  0.80 40.25  ? 327 ASP A CG    1 
ATOM   5079  O  OD1   A ASP A 1 327 ? -11.456 -11.110 64.672  0.20 33.03  ? 327 ASP A OD1   1 
ATOM   5080  O  OD1   B ASP A 1 327 ? -12.479 -10.933 64.549  0.80 31.45  ? 327 ASP A OD1   1 
ATOM   5081  O  OD2   A ASP A 1 327 ? -12.346 -12.511 63.228  0.20 33.97  ? 327 ASP A OD2   1 
ATOM   5082  O  OD2   B ASP A 1 327 ? -12.170 -12.705 63.280  0.80 33.68  ? 327 ASP A OD2   1 
ATOM   5083  N  N     A VAL A 1 328 ? -11.425 -7.698  60.704  0.20 27.08  ? 328 VAL A N     1 
ATOM   5084  N  N     B VAL A 1 328 ? -11.391 -7.845  60.619  0.80 25.74  ? 328 VAL A N     1 
ATOM   5085  C  CA    A VAL A 1 328 ? -10.835 -6.785  59.732  0.20 34.09  ? 328 VAL A CA    1 
ATOM   5086  C  CA    B VAL A 1 328 ? -10.656 -7.023  59.664  0.80 34.62  ? 328 VAL A CA    1 
ATOM   5087  C  C     A VAL A 1 328 ? -10.427 -5.481  60.406  0.20 35.84  ? 328 VAL A C     1 
ATOM   5088  C  C     B VAL A 1 328 ? -10.247 -5.705  60.308  0.80 36.68  ? 328 VAL A C     1 
ATOM   5089  O  O     A VAL A 1 328 ? -9.332  -4.958  60.167  0.20 34.36  ? 328 VAL A O     1 
ATOM   5090  O  O     B VAL A 1 328 ? -9.093  -5.269  60.190  0.80 32.47  ? 328 VAL A O     1 
ATOM   5091  C  CB    A VAL A 1 328 ? -11.814 -6.539  58.569  0.20 32.75  ? 328 VAL A CB    1 
ATOM   5092  C  CB    B VAL A 1 328 ? -11.495 -6.793  58.396  0.80 34.76  ? 328 VAL A CB    1 
ATOM   5093  C  CG1   A VAL A 1 328 ? -11.222 -5.551  57.576  0.20 33.40  ? 328 VAL A CG1   1 
ATOM   5094  C  CG1   B VAL A 1 328 ? -10.756 -5.866  57.432  0.80 34.14  ? 328 VAL A CG1   1 
ATOM   5095  C  CG2   A VAL A 1 328 ? -12.157 -7.849  57.883  0.20 28.93  ? 328 VAL A CG2   1 
ATOM   5096  C  CG2   B VAL A 1 328 ? -11.808 -8.118  57.739  0.80 27.60  ? 328 VAL A CG2   1 
ATOM   5097  N  N     A ASN A 1 329 ? -11.296 -4.939  61.265  0.20 35.52  ? 329 ASN A N     1 
ATOM   5098  N  N     B ASN A 1 329 ? -11.185 -5.063  61.017  0.80 36.45  ? 329 ASN A N     1 
ATOM   5099  C  CA    A ASN A 1 329 ? -10.980 -3.687  61.945  0.20 36.37  ? 329 ASN A CA    1 
ATOM   5100  C  CA    B ASN A 1 329 ? -10.880 -3.800  61.685  0.80 36.55  ? 329 ASN A CA    1 
ATOM   5101  C  C     A ASN A 1 329 ? -9.806  -3.841  62.902  0.20 36.33  ? 329 ASN A C     1 
ATOM   5102  C  C     B ASN A 1 329 ? -9.710  -3.957  62.646  0.80 36.55  ? 329 ASN A C     1 
ATOM   5103  O  O     A ASN A 1 329 ? -9.058  -2.881  63.121  0.20 39.22  ? 329 ASN A O     1 
ATOM   5104  O  O     B ASN A 1 329 ? -8.795  -3.124  62.665  0.80 39.51  ? 329 ASN A O     1 
ATOM   5105  C  CB    A ASN A 1 329 ? -12.208 -3.170  62.696  0.20 34.87  ? 329 ASN A CB    1 
ATOM   5106  C  CB    B ASN A 1 329 ? -12.115 -3.280  62.422  0.80 34.61  ? 329 ASN A CB    1 
ATOM   5107  C  CG    A ASN A 1 329 ? -13.381 -2.899  61.776  0.20 40.91  ? 329 ASN A CG    1 
ATOM   5108  C  CG    B ASN A 1 329 ? -13.268 -2.981  61.484  0.80 42.60  ? 329 ASN A CG    1 
ATOM   5109  O  OD1   A ASN A 1 329 ? -13.207 -2.678  60.576  0.20 39.13  ? 329 ASN A OD1   1 
ATOM   5110  O  OD1   B ASN A 1 329 ? -14.437 -3.209  61.817  0.80 47.57  ? 329 ASN A OD1   1 
ATOM   5111  N  ND2   A ASN A 1 329 ? -14.587 -2.912  62.335  0.20 42.09  ? 329 ASN A ND2   1 
ATOM   5112  N  ND2   B ASN A 1 329 ? -12.947 -2.477  60.296  0.80 39.25  ? 329 ASN A ND2   1 
ATOM   5113  N  N     A ALA A 1 330 ? -9.621  -5.033  63.474  0.20 34.96  ? 330 ALA A N     1 
ATOM   5114  N  N     B ALA A 1 330 ? -9.706  -5.039  63.429  0.80 34.82  ? 330 ALA A N     1 
ATOM   5115  C  CA    A ALA A 1 330 ? -8.530  -5.243  64.419  0.20 35.73  ? 330 ALA A CA    1 
ATOM   5116  C  CA    B ALA A 1 330 ? -8.589  -5.301  64.331  0.80 35.68  ? 330 ALA A CA    1 
ATOM   5117  C  C     A ALA A 1 330 ? -7.192  -5.425  63.710  0.20 36.55  ? 330 ALA A C     1 
ATOM   5118  C  C     B ALA A 1 330 ? -7.295  -5.554  63.562  0.80 35.53  ? 330 ALA A C     1 
ATOM   5119  O  O     A ALA A 1 330 ? -6.159  -4.952  64.198  0.20 40.59  ? 330 ALA A O     1 
ATOM   5120  O  O     B ALA A 1 330 ? -6.210  -5.165  64.012  0.80 41.05  ? 330 ALA A O     1 
ATOM   5121  C  CB    A ALA A 1 330 ? -8.832  -6.450  65.307  0.20 30.22  ? 330 ALA A CB    1 
ATOM   5122  C  CB    B ALA A 1 330 ? -8.921  -6.488  65.232  0.80 29.79  ? 330 ALA A CB    1 
ATOM   5123  N  N     A ALA A 1 331 ? -7.188  -6.109  62.563  0.20 36.38  ? 331 ALA A N     1 
ATOM   5124  N  N     B ALA A 1 331 ? -7.386  -6.210  62.405  0.80 36.09  ? 331 ALA A N     1 
ATOM   5125  C  CA    A ALA A 1 331 ? -5.942  -6.307  61.828  0.20 39.22  ? 331 ALA A CA    1 
ATOM   5126  C  CA    B ALA A 1 331 ? -6.201  -6.424  61.575  0.80 39.65  ? 331 ALA A CA    1 
ATOM   5127  C  C     A ALA A 1 331 ? -5.473  -5.022  61.157  0.20 39.03  ? 331 ALA A C     1 
ATOM   5128  C  C     B ALA A 1 331 ? -5.664  -5.104  61.034  0.80 37.40  ? 331 ALA A C     1 
ATOM   5129  O  O     A ALA A 1 331 ? -4.263  -4.791  61.040  0.20 42.54  ? 331 ALA A O     1 
ATOM   5130  O  O     B ALA A 1 331 ? -4.458  -4.838  61.088  0.80 42.44  ? 331 ALA A O     1 
ATOM   5131  C  CB    A ALA A 1 331 ? -6.114  -7.417  60.791  0.20 36.09  ? 331 ALA A CB    1 
ATOM   5132  C  CB    B ALA A 1 331 ? -6.534  -7.379  60.427  0.80 35.05  ? 331 ALA A CB    1 
ATOM   5133  N  N     A ILE A 1 332 ? -6.407  -4.181  60.711  0.20 40.07  ? 332 ILE A N     1 
ATOM   5134  N  N     B ILE A 1 332 ? -6.554  -4.265  60.506  0.80 40.53  ? 332 ILE A N     1 
ATOM   5135  C  CA    A ILE A 1 332 ? -6.033  -2.906  60.108  0.20 43.03  ? 332 ILE A CA    1 
ATOM   5136  C  CA    B ILE A 1 332 ? -6.146  -2.972  59.968  0.80 43.34  ? 332 ILE A CA    1 
ATOM   5137  C  C     A ILE A 1 332 ? -5.475  -1.959  61.164  0.20 46.24  ? 332 ILE A C     1 
ATOM   5138  C  C     B ILE A 1 332 ? -5.550  -2.101  61.068  0.80 46.76  ? 332 ILE A C     1 
ATOM   5139  O  O     A ILE A 1 332 ? -4.496  -1.241  60.919  0.20 45.77  ? 332 ILE A O     1 
ATOM   5140  O  O     B ILE A 1 332 ? -4.548  -1.404  60.855  0.80 45.28  ? 332 ILE A O     1 
ATOM   5141  C  CB    A ILE A 1 332 ? -7.240  -2.293  59.372  0.20 42.27  ? 332 ILE A CB    1 
ATOM   5142  C  CB    B ILE A 1 332 ? -7.346  -2.302  59.267  0.80 42.55  ? 332 ILE A CB    1 
ATOM   5143  C  CG1   A ILE A 1 332 ? -7.577  -3.105  58.120  0.20 38.41  ? 332 ILE A CG1   1 
ATOM   5144  C  CG1   B ILE A 1 332 ? -7.550  -2.908  57.873  0.80 37.54  ? 332 ILE A CG1   1 
ATOM   5145  C  CG2   A ILE A 1 332 ? -6.973  -0.845  59.000  0.20 42.72  ? 332 ILE A CG2   1 
ATOM   5146  C  CG2   B ILE A 1 332 ? -7.184  -0.793  59.190  0.80 42.37  ? 332 ILE A CG2   1 
ATOM   5147  C  CD1   A ILE A 1 332 ? -8.814  -2.609  57.397  0.20 29.83  ? 332 ILE A CD1   1 
ATOM   5148  C  CD1   B ILE A 1 332 ? -6.441  -2.606  56.905  0.80 42.27  ? 332 ILE A CD1   1 
ATOM   5149  N  N     A ALA A 1 333 ? -6.077  -1.950  62.358  0.20 42.28  ? 333 ALA A N     1 
ATOM   5150  N  N     B ALA A 1 333 ? -6.129  -2.160  62.274  0.80 42.41  ? 333 ALA A N     1 
ATOM   5151  C  CA    A ALA A 1 333 ? -5.617  -1.058  63.418  0.20 43.47  ? 333 ALA A CA    1 
ATOM   5152  C  CA    B ALA A 1 333 ? -5.616  -1.373  63.392  0.80 43.37  ? 333 ALA A CA    1 
ATOM   5153  C  C     A ALA A 1 333 ? -4.174  -1.354  63.806  0.20 44.63  ? 333 ALA A C     1 
ATOM   5154  C  C     B ALA A 1 333 ? -4.170  -1.733  63.714  0.80 42.28  ? 333 ALA A C     1 
ATOM   5155  O  O     A ALA A 1 333 ? -3.393  -0.432  64.069  0.20 48.23  ? 333 ALA A O     1 
ATOM   5156  O  O     B ALA A 1 333 ? -3.357  -0.849  64.007  0.80 47.45  ? 333 ALA A O     1 
ATOM   5157  C  CB    A ALA A 1 333 ? -6.537  -1.173  64.635  0.20 39.93  ? 333 ALA A CB    1 
ATOM   5158  C  CB    B ALA A 1 333 ? -6.507  -1.565  64.623  0.80 39.30  ? 333 ALA A CB    1 
ATOM   5159  N  N     A THR A 1 334 ? -3.799  -2.635  63.844  0.20 44.69  ? 334 THR A N     1 
ATOM   5160  N  N     B THR A 1 334 ? -3.822  -3.022  63.648  0.80 42.60  ? 334 THR A N     1 
ATOM   5161  C  CA    A THR A 1 334 ? -2.405  -2.983  64.101  0.20 49.33  ? 334 THR A CA    1 
ATOM   5162  C  CA    B THR A 1 334 ? -2.436  -3.416  63.895  0.80 48.97  ? 334 THR A CA    1 
ATOM   5163  C  C     A THR A 1 334 ? -1.506  -2.564  62.943  0.20 55.63  ? 334 THR A C     1 
ATOM   5164  C  C     B THR A 1 334 ? -1.515  -2.961  62.768  0.80 56.22  ? 334 THR A C     1 
ATOM   5165  O  O     A THR A 1 334 ? -0.339  -2.213  63.160  0.20 60.81  ? 334 THR A O     1 
ATOM   5166  O  O     B THR A 1 334 ? -0.427  -2.431  63.025  0.80 62.74  ? 334 THR A O     1 
ATOM   5167  C  CB    A THR A 1 334 ? -2.280  -4.485  64.363  0.20 50.43  ? 334 THR A CB    1 
ATOM   5168  C  CB    B THR A 1 334 ? -2.328  -4.929  64.063  0.80 51.55  ? 334 THR A CB    1 
ATOM   5169  O  OG1   A THR A 1 334 ? -3.201  -4.869  65.391  0.20 52.37  ? 334 THR A OG1   1 
ATOM   5170  O  OG1   B THR A 1 334 ? -2.597  -5.565  62.805  0.80 59.06  ? 334 THR A OG1   1 
ATOM   5171  C  CG2   A THR A 1 334 ? -0.869  -4.841  64.807  0.20 52.26  ? 334 THR A CG2   1 
ATOM   5172  C  CG2   B THR A 1 334 ? -3.313  -5.427  65.112  0.80 55.26  ? 334 THR A CG2   1 
ATOM   5173  N  N     A ILE A 1 335 ? -2.031  -2.578  61.716  0.20 51.59  ? 335 ILE A N     1 
ATOM   5174  N  N     B ILE A 1 335 ? -1.930  -3.154  61.514  0.80 49.93  ? 335 ILE A N     1 
ATOM   5175  C  CA    A ILE A 1 335 ? -1.237  -2.173  60.560  0.20 54.78  ? 335 ILE A CA    1 
ATOM   5176  C  CA    B ILE A 1 335 ? -1.075  -2.868  60.362  0.80 57.13  ? 335 ILE A CA    1 
ATOM   5177  C  C     A ILE A 1 335 ? -0.936  -0.679  60.610  0.20 57.14  ? 335 ILE A C     1 
ATOM   5178  C  C     B ILE A 1 335 ? -1.145  -1.384  60.029  0.80 56.47  ? 335 ILE A C     1 
ATOM   5179  O  O     A ILE A 1 335 ? 0.155   -0.239  60.226  0.20 57.60  ? 335 ILE A O     1 
ATOM   5180  O  O     B ILE A 1 335 ? -1.241  -0.991  58.859  0.80 64.87  ? 335 ILE A O     1 
ATOM   5181  C  CB    A ILE A 1 335 ? -1.957  -2.579  59.258  0.20 53.66  ? 335 ILE A CB    1 
ATOM   5182  C  CB    B ILE A 1 335 ? -1.467  -3.735  59.152  0.80 53.93  ? 335 ILE A CB    1 
ATOM   5183  C  CG1   A ILE A 1 335 ? -1.262  -3.781  58.614  0.20 53.94  ? 335 ILE A CG1   1 
ATOM   5184  C  CG1   B ILE A 1 335 ? -1.788  -5.147  59.621  0.80 53.21  ? 335 ILE A CG1   1 
ATOM   5185  C  CG2   A ILE A 1 335 ? -2.044  -1.414  58.275  0.20 54.06  ? 335 ILE A CG2   1 
ATOM   5186  C  CG2   B ILE A 1 335 ? -0.326  -3.822  58.150  0.80 56.66  ? 335 ILE A CG2   1 
ATOM   5187  C  CD1   A ILE A 1 335 ? -1.190  -4.997  59.509  0.20 53.31  ? 335 ILE A CD1   1 
ATOM   5188  C  CD1   B ILE A 1 335 ? -2.574  -5.927  58.625  0.80 47.96  ? 335 ILE A CD1   1 
ATOM   5189  N  N     A LYS A 1 336 ? -1.884  0.122   61.104  0.20 55.40  ? 336 LYS A N     1 
ATOM   5190  N  N     B LYS A 1 336 ? -1.105  -0.551  61.065  0.80 58.78  ? 336 LYS A N     1 
ATOM   5191  C  CA    A LYS A 1 336 ? -1.691  1.569   61.118  0.20 56.81  ? 336 LYS A CA    1 
ATOM   5192  C  CA    B LYS A 1 336 ? -0.965  0.887   60.921  0.80 61.03  ? 336 LYS A CA    1 
ATOM   5193  C  C     A LYS A 1 336 ? -0.663  2.000   62.157  0.20 58.35  ? 336 LYS A C     1 
ATOM   5194  C  C     B LYS A 1 336 ? 0.170   1.430   61.774  0.80 56.35  ? 336 LYS A C     1 
ATOM   5195  O  O     A LYS A 1 336 ? 0.046   2.991   61.946  0.20 55.20  ? 336 LYS A O     1 
ATOM   5196  O  O     B LYS A 1 336 ? 0.448   2.628   61.718  0.80 54.05  ? 336 LYS A O     1 
ATOM   5197  C  CB    A LYS A 1 336 ? -3.023  2.278   61.369  0.20 54.48  ? 336 LYS A CB    1 
ATOM   5198  C  CB    B LYS A 1 336 ? -2.267  1.606   61.305  0.80 55.80  ? 336 LYS A CB    1 
ATOM   5199  C  CG    A LYS A 1 336 ? -3.988  2.228   60.194  0.20 54.25  ? 336 LYS A CG    1 
ATOM   5200  C  CG    B LYS A 1 336 ? -3.310  1.657   60.205  0.80 58.20  ? 336 LYS A CG    1 
ATOM   5201  C  CD    A LYS A 1 336 ? -5.192  3.130   60.428  0.20 53.92  ? 336 LYS A CD    1 
ATOM   5202  C  CD    B LYS A 1 336 ? -4.633  2.193   60.738  0.80 53.11  ? 336 LYS A CD    1 
ATOM   5203  C  CE    A LYS A 1 336 ? -6.048  3.244   59.179  0.20 46.57  ? 336 LYS A CE    1 
ATOM   5204  C  CE    B LYS A 1 336 ? -4.425  3.437   61.595  0.80 63.60  ? 336 LYS A CE    1 
ATOM   5205  N  NZ    A LYS A 1 336 ? -7.152  4.227   59.346  0.20 47.29  ? 336 LYS A NZ    1 
ATOM   5206  N  NZ    B LYS A 1 336 ? -3.845  4.568   60.817  0.80 70.25  ? 336 LYS A NZ    1 
ATOM   5207  N  N     A THR A 1 337 ? -0.559  1.278   63.273  0.20 60.91  ? 337 THR A N     1 
ATOM   5208  N  N     B THR A 1 337 ? 0.818   0.589   62.575  0.80 61.97  ? 337 THR A N     1 
ATOM   5209  C  CA    A THR A 1 337 ? 0.321   1.697   64.358  0.20 61.34  ? 337 THR A CA    1 
ATOM   5210  C  CA    B THR A 1 337 ? 1.852   1.038   63.498  0.80 65.35  ? 337 THR A CA    1 
ATOM   5211  C  C     A THR A 1 337 ? 1.698   1.041   64.283  0.20 63.18  ? 337 THR A C     1 
ATOM   5212  C  C     B THR A 1 337 ? 3.041   0.086   63.456  0.80 67.16  ? 337 THR A C     1 
ATOM   5213  O  O     A THR A 1 337 ? 2.718   1.736   64.311  0.20 63.77  ? 337 THR A O     1 
ATOM   5214  O  O     B THR A 1 337 ? 4.196   0.515   63.564  0.80 70.78  ? 337 THR A O     1 
ATOM   5215  C  CB    A THR A 1 337 ? -0.329  1.396   65.715  0.20 58.82  ? 337 THR A CB    1 
ATOM   5216  C  CB    B THR A 1 337 ? 1.308   1.119   64.922  0.80 63.81  ? 337 THR A CB    1 
ATOM   5217  O  OG1   A THR A 1 337 ? -0.627  -0.002  65.811  0.20 54.54  ? 337 THR A OG1   1 
ATOM   5218  O  OG1   B THR A 1 337 ? 0.729   -0.141  65.292  0.80 69.25  ? 337 THR A OG1   1 
ATOM   5219  C  CG2   A THR A 1 337 ? -1.613  2.196   65.882  0.20 57.93  ? 337 THR A CG2   1 
ATOM   5220  C  CG2   B THR A 1 337 ? 0.255   2.221   65.042  0.80 61.19  ? 337 THR A CG2   1 
ATOM   5221  N  N     A LYS A 1 338 ? 1.744   -0.289  64.184  0.20 62.53  ? 338 LYS A N     1 
ATOM   5222  N  N     B LYS A 1 338 ? 2.766   -1.212  63.307  0.80 66.89  ? 338 LYS A N     1 
ATOM   5223  C  CA    A LYS A 1 338 ? 3.020   -0.993  64.276  0.20 64.92  ? 338 LYS A CA    1 
ATOM   5224  C  CA    B LYS A 1 338 ? 3.808   -2.232  63.285  0.80 69.32  ? 338 LYS A CA    1 
ATOM   5225  C  C     A LYS A 1 338 ? 3.886   -0.751  63.044  0.20 65.11  ? 338 LYS A C     1 
ATOM   5226  C  C     B LYS A 1 338 ? 4.376   -2.464  61.888  0.80 64.93  ? 338 LYS A C     1 
ATOM   5227  O  O     A LYS A 1 338 ? 5.057   -0.370  63.161  0.20 64.40  ? 338 LYS A O     1 
ATOM   5228  O  O     B LYS A 1 338 ? 5.153   -3.405  61.695  0.80 60.61  ? 338 LYS A O     1 
ATOM   5229  C  CB    A LYS A 1 338 ? 2.782   -2.491  64.475  0.20 64.21  ? 338 LYS A CB    1 
ATOM   5230  C  CB    B LYS A 1 338 ? 3.272   -3.546  63.862  0.80 70.37  ? 338 LYS A CB    1 
ATOM   5231  C  CG    A LYS A 1 338 ? 4.053   -3.326  64.418  0.20 66.84  ? 338 LYS A CG    1 
ATOM   5232  C  CG    B LYS A 1 338 ? 2.310   -4.295  62.952  0.80 63.77  ? 338 LYS A CG    1 
ATOM   5233  C  CD    A LYS A 1 338 ? 3.759   -4.813  64.551  0.20 61.72  ? 338 LYS A CD    1 
ATOM   5234  C  CD    B LYS A 1 338 ? 1.938   -5.646  63.547  0.80 60.32  ? 338 LYS A CD    1 
ATOM   5235  C  CE    A LYS A 1 338 ? 3.238   -5.153  65.935  0.20 56.76  ? 338 LYS A CE    1 
ATOM   5236  C  CE    B LYS A 1 338 ? 3.175   -6.492  63.804  0.80 65.20  ? 338 LYS A CE    1 
ATOM   5237  N  NZ    A LYS A 1 338 ? 2.982   -6.611  66.087  0.20 54.05  ? 338 LYS A NZ    1 
ATOM   5238  N  NZ    B LYS A 1 338 ? 3.982   -6.682  62.565  0.80 74.13  ? 338 LYS A NZ    1 
ATOM   5239  N  N     A ARG A 1 339 ? 3.332   -0.967  61.855  0.20 63.66  ? 339 ARG A N     1 
ATOM   5240  N  N     B ARG A 1 339 ? 4.005   -1.637  60.913  0.80 62.68  ? 339 ARG A N     1 
ATOM   5241  C  CA    A ARG A 1 339 ? 4.121   -0.953  60.632  0.20 62.85  ? 339 ARG A CA    1 
ATOM   5242  C  CA    B ARG A 1 339 ? 4.574   -1.717  59.577  0.80 64.63  ? 339 ARG A CA    1 
ATOM   5243  C  C     A ARG A 1 339 ? 4.211   0.454   60.051  0.20 60.42  ? 339 ARG A C     1 
ATOM   5244  C  C     B ARG A 1 339 ? 4.837   -0.315  59.047  0.80 62.52  ? 339 ARG A C     1 
ATOM   5245  O  O     A ARG A 1 339 ? 3.260   1.238   60.130  0.20 56.72  ? 339 ARG A O     1 
ATOM   5246  O  O     B ARG A 1 339 ? 4.205   0.659   59.469  0.80 59.08  ? 339 ARG A O     1 
ATOM   5247  C  CB    A ARG A 1 339 ? 3.526   -1.916  59.603  0.20 62.42  ? 339 ARG A CB    1 
ATOM   5248  C  CB    B ARG A 1 339 ? 3.664   -2.485  58.611  0.80 63.04  ? 339 ARG A CB    1 
ATOM   5249  C  CG    A ARG A 1 339 ? 3.171   -3.277  60.189  0.20 64.08  ? 339 ARG A CG    1 
ATOM   5250  C  CG    B ARG A 1 339 ? 3.889   -3.990  58.622  0.80 63.05  ? 339 ARG A CG    1 
ATOM   5251  C  CD    A ARG A 1 339 ? 3.101   -4.359  59.125  0.20 63.09  ? 339 ARG A CD    1 
ATOM   5252  C  CD    B ARG A 1 339 ? 3.158   -4.655  57.469  0.80 58.85  ? 339 ARG A CD    1 
ATOM   5253  N  NE    A ARG A 1 339 ? 2.687   -5.640  59.685  0.20 61.68  ? 339 ARG A NE    1 
ATOM   5254  N  NE    B ARG A 1 339 ? 4.020   -5.564  56.724  0.80 59.43  ? 339 ARG A NE    1 
ATOM   5255  C  CZ    A ARG A 1 339 ? 3.497   -6.484  60.311  0.20 62.30  ? 339 ARG A CZ    1 
ATOM   5256  C  CZ    B ARG A 1 339 ? 4.090   -6.872  56.933  0.80 53.95  ? 339 ARG A CZ    1 
ATOM   5257  N  NH1   A ARG A 1 339 ? 4.779   -6.208  60.490  0.20 60.25  ? 339 ARG A NH1   1 
ATOM   5258  N  NH1   B ARG A 1 339 ? 3.358   -7.463  57.862  0.80 55.30  ? 339 ARG A NH1   1 
ATOM   5259  N  NH2   A ARG A 1 339 ? 3.008   -7.632  60.772  0.20 56.08  ? 339 ARG A NH2   1 
ATOM   5260  N  NH2   B ARG A 1 339 ? 4.915   -7.604  56.189  0.80 46.02  ? 339 ARG A NH2   1 
ATOM   5261  N  N     A SER A 1 340 ? 5.370   0.765   59.469  0.20 59.17  ? 340 SER A N     1 
ATOM   5262  N  N     B SER A 1 340 ? 5.790   -0.227  58.117  0.80 69.88  ? 340 SER A N     1 
ATOM   5263  C  CA    A SER A 1 340 ? 5.627   2.072   58.865  0.20 57.12  ? 340 SER A CA    1 
ATOM   5264  C  CA    B SER A 1 340 ? 6.184   1.043   57.507  0.80 62.31  ? 340 SER A CA    1 
ATOM   5265  C  C     A SER A 1 340 ? 5.046   2.082   57.454  0.20 57.98  ? 340 SER A C     1 
ATOM   5266  C  C     B SER A 1 340 ? 5.241   1.329   56.343  0.80 59.84  ? 340 SER A C     1 
ATOM   5267  O  O     A SER A 1 340 ? 5.731   1.853   56.455  0.20 57.19  ? 340 SER A O     1 
ATOM   5268  O  O     B SER A 1 340 ? 5.557   1.112   55.170  0.80 59.12  ? 340 SER A O     1 
ATOM   5269  C  CB    A SER A 1 340 ? 7.119   2.377   58.857  0.20 51.46  ? 340 SER A CB    1 
ATOM   5270  C  CB    B SER A 1 340 ? 7.638   0.995   57.056  0.80 66.88  ? 340 SER A CB    1 
ATOM   5271  O  OG    A SER A 1 340 ? 7.636   2.436   60.173  0.20 50.43  ? 340 SER A OG    1 
ATOM   5272  O  OG    B SER A 1 340 ? 7.807   0.068   55.996  0.80 56.85  ? 340 SER A OG    1 
ATOM   5273  N  N     A ILE A 1 341 ? 3.751   2.361   57.380  0.20 53.98  ? 341 ILE A N     1 
ATOM   5274  N  N     B ILE A 1 341 ? 4.054   1.822   56.686  0.80 55.77  ? 341 ILE A N     1 
ATOM   5275  C  CA    A ILE A 1 341 ? 3.018   2.411   56.122  0.20 53.05  ? 341 ILE A CA    1 
ATOM   5276  C  CA    B ILE A 1 341 ? 3.022   2.175   55.717  0.80 52.89  ? 341 ILE A CA    1 
ATOM   5277  C  C     A ILE A 1 341 ? 2.638   3.868   55.892  0.20 48.81  ? 341 ILE A C     1 
ATOM   5278  C  C     B ILE A 1 341 ? 2.785   3.674   55.814  0.80 48.41  ? 341 ILE A C     1 
ATOM   5279  O  O     A ILE A 1 341 ? 1.695   4.384   56.501  0.20 50.46  ? 341 ILE A O     1 
ATOM   5280  O  O     B ILE A 1 341 ? 2.353   4.174   56.860  0.80 52.22  ? 341 ILE A O     1 
ATOM   5281  C  CB    A ILE A 1 341 ? 1.791   1.494   56.143  0.20 56.44  ? 341 ILE A CB    1 
ATOM   5282  C  CB    B ILE A 1 341 ? 1.721   1.397   55.960  0.80 57.71  ? 341 ILE A CB    1 
ATOM   5283  C  CG1   A ILE A 1 341 ? 2.239   0.042   56.323  0.20 53.21  ? 341 ILE A CG1   1 
ATOM   5284  C  CG1   B ILE A 1 341 ? 1.958   -0.098  55.761  0.80 52.50  ? 341 ILE A CG1   1 
ATOM   5285  C  CG2   A ILE A 1 341 ? 0.975   1.655   54.871  0.20 46.71  ? 341 ILE A CG2   1 
ATOM   5286  C  CG2   B ILE A 1 341 ? 0.601   1.911   55.052  0.80 44.53  ? 341 ILE A CG2   1 
ATOM   5287  C  CD1   A ILE A 1 341 ? 1.117   -0.912  56.630  0.20 54.69  ? 341 ILE A CD1   1 
ATOM   5288  C  CD1   B ILE A 1 341 ? 0.820   -0.939  56.266  0.80 55.81  ? 341 ILE A CD1   1 
ATOM   5289  N  N     A GLN A 1 342 ? 3.375   4.540   55.013  0.20 49.22  ? 342 GLN A N     1 
ATOM   5290  N  N     B GLN A 1 342 ? 3.067   4.388   54.730  0.80 48.56  ? 342 GLN A N     1 
ATOM   5291  C  CA    A GLN A 1 342 ? 3.240   5.978   54.833  0.20 48.41  ? 342 GLN A CA    1 
ATOM   5292  C  CA    B GLN A 1 342 ? 2.969   5.842   54.698  0.80 48.59  ? 342 GLN A CA    1 
ATOM   5293  C  C     A GLN A 1 342 ? 2.283   6.286   53.688  0.20 40.66  ? 342 GLN A C     1 
ATOM   5294  C  C     B GLN A 1 342 ? 2.068   6.247   53.543  0.80 38.65  ? 342 GLN A C     1 
ATOM   5295  O  O     A GLN A 1 342 ? 2.429   5.752   52.582  0.20 42.77  ? 342 GLN A O     1 
ATOM   5296  O  O     B GLN A 1 342 ? 2.342   5.907   52.386  0.80 43.34  ? 342 GLN A O     1 
ATOM   5297  C  CB    A GLN A 1 342 ? 4.603   6.617   54.560  0.20 50.39  ? 342 GLN A CB    1 
ATOM   5298  C  CB    B GLN A 1 342 ? 4.351   6.494   54.548  0.80 50.75  ? 342 GLN A CB    1 
ATOM   5299  C  CG    A GLN A 1 342 ? 5.690   6.250   55.561  0.20 52.44  ? 342 GLN A CG    1 
ATOM   5300  C  CG    B GLN A 1 342 ? 5.338   6.233   55.687  0.80 51.70  ? 342 GLN A CG    1 
ATOM   5301  C  CD    A GLN A 1 342 ? 7.040   6.847   55.198  0.20 59.34  ? 342 GLN A CD    1 
ATOM   5302  C  CD    B GLN A 1 342 ? 6.668   6.948   55.480  0.80 62.51  ? 342 GLN A CD    1 
ATOM   5303  O  OE1   A GLN A 1 342 ? 7.166   8.057   55.008  0.20 58.80  ? 342 GLN A OE1   1 
ATOM   5304  O  OE1   B GLN A 1 342 ? 7.531   6.487   54.724  0.80 55.05  ? 342 GLN A OE1   1 
ATOM   5305  N  NE2   A GLN A 1 342 ? 8.055   5.996   55.091  0.20 51.52  ? 342 GLN A NE2   1 
ATOM   5306  N  NE2   B GLN A 1 342 ? 6.836   8.084   56.150  0.80 59.77  ? 342 GLN A NE2   1 
ATOM   5307  N  N     A PHE A 1 343 ? 1.310   7.146   53.958  0.20 40.37  ? 343 PHE A N     1 
ATOM   5308  N  N     B PHE A 1 343 ? 1.005   6.970   53.851  0.80 39.91  ? 343 PHE A N     1 
ATOM   5309  C  CA    A PHE A 1 343 ? 0.447   7.717   52.936  0.20 40.87  ? 343 PHE A CA    1 
ATOM   5310  C  CA    B PHE A 1 343 ? 0.165   7.564   52.828  0.80 40.87  ? 343 PHE A CA    1 
ATOM   5311  C  C     A PHE A 1 343 ? 0.945   9.108   52.566  0.20 42.11  ? 343 PHE A C     1 
ATOM   5312  C  C     B PHE A 1 343 ? 0.695   8.946   52.471  0.80 41.81  ? 343 PHE A C     1 
ATOM   5313  O  O     A PHE A 1 343 ? 1.715   9.734   53.300  0.20 45.12  ? 343 PHE A O     1 
ATOM   5314  O  O     B PHE A 1 343 ? 1.511   9.529   53.188  0.80 45.97  ? 343 PHE A O     1 
ATOM   5315  C  CB    A PHE A 1 343 ? -1.005  7.791   53.421  0.20 41.27  ? 343 PHE A CB    1 
ATOM   5316  C  CB    B PHE A 1 343 ? -1.288  7.660   53.303  0.80 40.22  ? 343 PHE A CB    1 
ATOM   5317  C  CG    A PHE A 1 343 ? -1.741  6.482   53.351  0.20 45.60  ? 343 PHE A CG    1 
ATOM   5318  C  CG    B PHE A 1 343 ? -2.046  6.362   53.214  0.80 46.27  ? 343 PHE A CG    1 
ATOM   5319  C  CD1   A PHE A 1 343 ? -1.502  5.485   54.283  0.20 47.20  ? 343 PHE A CD1   1 
ATOM   5320  C  CD1   B PHE A 1 343 ? -1.758  5.311   54.069  0.80 47.93  ? 343 PHE A CD1   1 
ATOM   5321  C  CD2   A PHE A 1 343 ? -2.682  6.254   52.361  0.20 42.46  ? 343 PHE A CD2   1 
ATOM   5322  C  CD2   B PHE A 1 343 ? -3.044  6.193   52.274  0.80 41.85  ? 343 PHE A CD2   1 
ATOM   5323  C  CE1   A PHE A 1 343 ? -2.181  4.282   54.222  0.20 46.34  ? 343 PHE A CE1   1 
ATOM   5324  C  CE1   B PHE A 1 343 ? -2.452  4.116   53.988  0.80 47.16  ? 343 PHE A CE1   1 
ATOM   5325  C  CE2   A PHE A 1 343 ? -3.364  5.052   52.295  0.20 42.39  ? 343 PHE A CE2   1 
ATOM   5326  C  CE2   B PHE A 1 343 ? -3.740  4.995   52.188  0.80 43.22  ? 343 PHE A CE2   1 
ATOM   5327  C  CZ    A PHE A 1 343 ? -3.113  4.066   53.226  0.20 43.27  ? 343 PHE A CZ    1 
ATOM   5328  C  CZ    B PHE A 1 343 ? -3.445  3.961   53.042  0.80 41.56  ? 343 PHE A CZ    1 
ATOM   5329  N  N     A VAL A 1 344 ? 0.501   9.589   51.404  0.20 37.30  ? 344 VAL A N     1 
ATOM   5330  N  N     B VAL A 1 344 ? 0.231   9.465   51.334  0.80 34.32  ? 344 VAL A N     1 
ATOM   5331  C  CA    A VAL A 1 344 ? 0.831   10.957  51.023  0.20 43.22  ? 344 VAL A CA    1 
ATOM   5332  C  CA    B VAL A 1 344 ? 0.520   10.851  50.993  0.80 43.52  ? 344 VAL A CA    1 
ATOM   5333  C  C     A VAL A 1 344 ? 0.014   11.935  51.863  0.20 46.75  ? 344 VAL A C     1 
ATOM   5334  C  C     B VAL A 1 344 ? -0.319  11.769  51.875  0.80 47.34  ? 344 VAL A C     1 
ATOM   5335  O  O     A VAL A 1 344 ? -1.052  11.609  52.399  0.20 43.49  ? 344 VAL A O     1 
ATOM   5336  O  O     B VAL A 1 344 ? -1.453  11.442  52.259  0.80 38.33  ? 344 VAL A O     1 
ATOM   5337  C  CB    A VAL A 1 344 ? 0.607   11.187  49.520  0.20 39.99  ? 344 VAL A CB    1 
ATOM   5338  C  CB    B VAL A 1 344 ? 0.263   11.118  49.499  0.80 39.27  ? 344 VAL A CB    1 
ATOM   5339  C  CG1   A VAL A 1 344 ? 1.598   10.369  48.707  0.20 37.74  ? 344 VAL A CG1   1 
ATOM   5340  C  CG1   B VAL A 1 344 ? 1.316   10.419  48.646  0.80 36.87  ? 344 VAL A CG1   1 
ATOM   5341  C  CG2   A VAL A 1 344 ? -0.814  10.831  49.142  0.20 42.30  ? 344 VAL A CG2   1 
ATOM   5342  C  CG2   B VAL A 1 344 ? -1.143  10.667  49.122  0.80 41.77  ? 344 VAL A CG2   1 
ATOM   5343  N  N     A ASP A 1 345 ? 0.530   13.160  51.977  0.20 46.65  ? 345 ASP A N     1 
ATOM   5344  N  N     B ASP A 1 345 ? 0.243   12.938  52.201  0.80 49.73  ? 345 ASP A N     1 
ATOM   5345  C  CA    A ASP A 1 345 ? -0.062  14.142  52.879  0.20 51.58  ? 345 ASP A CA    1 
ATOM   5346  C  CA    B ASP A 1 345 ? -0.402  13.814  53.179  0.80 50.65  ? 345 ASP A CA    1 
ATOM   5347  C  C     A ASP A 1 345 ? -1.372  14.723  52.363  0.20 50.68  ? 345 ASP A C     1 
ATOM   5348  C  C     B ASP A 1 345 ? -1.746  14.332  52.684  0.80 51.52  ? 345 ASP A C     1 
ATOM   5349  O  O     A ASP A 1 345 ? -2.014  15.487  53.092  0.20 52.11  ? 345 ASP A O     1 
ATOM   5350  O  O     B ASP A 1 345 ? -2.634  14.626  53.494  0.80 52.78  ? 345 ASP A O     1 
ATOM   5351  C  CB    A ASP A 1 345 ? 0.934   15.273  53.141  0.20 54.79  ? 345 ASP A CB    1 
ATOM   5352  C  CB    B ASP A 1 345 ? 0.523   14.980  53.526  0.80 57.25  ? 345 ASP A CB    1 
ATOM   5353  C  CG    A ASP A 1 345 ? 2.205   14.785  53.807  0.20 55.90  ? 345 ASP A CG    1 
ATOM   5354  C  CG    B ASP A 1 345 ? 1.725   14.544  54.341  0.80 58.45  ? 345 ASP A CG    1 
ATOM   5355  O  OD1   A ASP A 1 345 ? 2.127   13.835  54.615  0.20 57.29  ? 345 ASP A OD1   1 
ATOM   5356  O  OD1   B ASP A 1 345 ? 1.538   13.809  55.336  0.80 59.96  ? 345 ASP A OD1   1 
ATOM   5357  O  OD2   A ASP A 1 345 ? 3.282   15.349  53.523  0.20 57.35  ? 345 ASP A OD2   1 
ATOM   5358  O  OD2   B ASP A 1 345 ? 2.856   14.933  53.983  0.80 58.09  ? 345 ASP A OD2   1 
ATOM   5359  N  N     A TRP A 1 346 ? -1.787  14.386  51.143  0.20 49.07  ? 346 TRP A N     1 
ATOM   5360  N  N     B TRP A 1 346 ? -1.925  14.436  51.369  0.80 48.89  ? 346 TRP A N     1 
ATOM   5361  C  CA    A TRP A 1 346 ? -3.009  14.924  50.560  0.20 48.47  ? 346 TRP A CA    1 
ATOM   5362  C  CA    B TRP A 1 346 ? -3.147  14.984  50.797  0.80 48.29  ? 346 TRP A CA    1 
ATOM   5363  C  C     A TRP A 1 346 ? -4.094  13.869  50.385  0.20 49.96  ? 346 TRP A C     1 
ATOM   5364  C  C     B TRP A 1 346 ? -4.250  13.951  50.631  0.80 50.32  ? 346 TRP A C     1 
ATOM   5365  O  O     A TRP A 1 346 ? -5.106  14.137  49.728  0.20 49.07  ? 346 TRP A O     1 
ATOM   5366  O  O     B TRP A 1 346 ? -5.324  14.286  50.120  0.80 49.18  ? 346 TRP A O     1 
ATOM   5367  C  CB    A TRP A 1 346 ? -2.703  15.595  49.219  0.20 46.99  ? 346 TRP A CB    1 
ATOM   5368  C  CB    B TRP A 1 346 ? -2.852  15.646  49.448  0.80 47.46  ? 346 TRP A CB    1 
ATOM   5369  C  CG    A TRP A 1 346 ? -1.898  14.749  48.280  0.20 44.83  ? 346 TRP A CG    1 
ATOM   5370  C  CG    B TRP A 1 346 ? -1.994  14.853  48.509  0.80 44.58  ? 346 TRP A CG    1 
ATOM   5371  C  CD1   A TRP A 1 346 ? -0.541  14.602  48.268  0.20 44.46  ? 346 TRP A CD1   1 
ATOM   5372  C  CD1   B TRP A 1 346 ? -0.639  14.939  48.371  0.80 44.65  ? 346 TRP A CD1   1 
ATOM   5373  C  CD2   A TRP A 1 346 ? -2.398  13.943  47.206  0.20 45.35  ? 346 TRP A CD2   1 
ATOM   5374  C  CD2   B TRP A 1 346 ? -2.434  13.888  47.546  0.80 45.87  ? 346 TRP A CD2   1 
ATOM   5375  N  NE1   A TRP A 1 346 ? -0.166  13.750  47.259  0.20 43.79  ? 346 TRP A NE1   1 
ATOM   5376  N  NE1   B TRP A 1 346 ? -0.206  14.075  47.398  0.80 43.69  ? 346 TRP A NE1   1 
ATOM   5377  C  CE2   A TRP A 1 346 ? -1.287  13.332  46.590  0.20 43.47  ? 346 TRP A CE2   1 
ATOM   5378  C  CE2   B TRP A 1 346 ? -1.288  13.421  46.869  0.80 43.82  ? 346 TRP A CE2   1 
ATOM   5379  C  CE3   A TRP A 1 346 ? -3.676  13.676  46.706  0.20 44.71  ? 346 TRP A CE3   1 
ATOM   5380  C  CE3   B TRP A 1 346 ? -3.682  13.369  47.191  0.80 42.58  ? 346 TRP A CE3   1 
ATOM   5381  C  CZ2   A TRP A 1 346 ? -1.416  12.471  45.502  0.20 38.90  ? 346 TRP A CZ2   1 
ATOM   5382  C  CZ2   B TRP A 1 346 ? -1.355  12.456  45.858  0.80 38.01  ? 346 TRP A CZ2   1 
ATOM   5383  C  CZ3   A TRP A 1 346 ? -3.801  12.821  45.623  0.20 44.39  ? 346 TRP A CZ3   1 
ATOM   5384  C  CZ3   B TRP A 1 346 ? -3.744  12.409  46.187  0.80 44.60  ? 346 TRP A CZ3   1 
ATOM   5385  C  CH2   A TRP A 1 346 ? -2.678  12.229  45.035  0.20 39.81  ? 346 TRP A CH2   1 
ATOM   5386  C  CH2   B TRP A 1 346 ? -2.589  11.967  45.534  0.80 39.30  ? 346 TRP A CH2   1 
ATOM   5387  N  N     A CYS A 1 347 ? -3.914  12.681  50.960  0.20 50.29  ? 347 CYS A N     1 
ATOM   5388  N  N     B CYS A 1 347 ? -4.018  12.711  51.047  0.80 50.40  ? 347 CYS A N     1 
ATOM   5389  C  CA    A CYS A 1 347 ? -4.897  11.620  50.848  0.20 53.40  ? 347 CYS A CA    1 
ATOM   5390  C  CA    B CYS A 1 347 ? -5.038  11.695  50.926  0.80 53.67  ? 347 CYS A CA    1 
ATOM   5391  C  C     A CYS A 1 347 ? -5.373  11.181  52.227  0.20 52.84  ? 347 CYS A C     1 
ATOM   5392  C  C     B CYS A 1 347 ? -5.416  11.161  52.299  0.80 52.70  ? 347 CYS A C     1 
ATOM   5393  O  O     A CYS A 1 347 ? -4.569  11.097  53.162  0.20 54.79  ? 347 CYS A O     1 
ATOM   5394  O  O     B CYS A 1 347 ? -4.546  11.004  53.164  0.80 54.88  ? 347 CYS A O     1 
ATOM   5395  C  CB    A CYS A 1 347 ? -4.321  10.410  50.096  0.20 49.93  ? 347 CYS A CB    1 
ATOM   5396  C  CB    B CYS A 1 347 ? -4.557  10.534  50.040  0.80 50.88  ? 347 CYS A CB    1 
ATOM   5397  S  SG    A CYS A 1 347 ? -4.179  10.637  48.309  0.20 41.19  ? 347 CYS A SG    1 
ATOM   5398  S  SG    B CYS A 1 347 ? -5.608  10.233  48.603  0.80 68.06  ? 347 CYS A SG    1 
ATOM   5399  N  N     A PRO A 1 348 ? -6.670  10.903  52.387  0.20 56.66  ? 348 PRO A N     1 
ATOM   5400  N  N     B PRO A 1 348 ? -6.698  10.892  52.534  0.80 56.85  ? 348 PRO A N     1 
ATOM   5401  C  CA    A PRO A 1 348 ? -7.169  10.408  53.678  0.20 57.24  ? 348 PRO A CA    1 
ATOM   5402  C  CA    B PRO A 1 348 ? -7.088  10.187  53.760  0.80 57.29  ? 348 PRO A CA    1 
ATOM   5403  C  C     A PRO A 1 348 ? -6.541  9.079   54.067  0.20 58.02  ? 348 PRO A C     1 
ATOM   5404  C  C     B PRO A 1 348 ? -6.320  8.879   53.894  0.80 58.41  ? 348 PRO A C     1 
ATOM   5405  O  O     A PRO A 1 348 ? -6.849  8.040   53.473  0.20 57.00  ? 348 PRO A O     1 
ATOM   5406  O  O     B PRO A 1 348 ? -6.089  8.168   52.914  0.80 55.89  ? 348 PRO A O     1 
ATOM   5407  C  CB    A PRO A 1 348 ? -8.679  10.266  53.442  0.20 57.71  ? 348 PRO A CB    1 
ATOM   5408  C  CB    B PRO A 1 348 ? -8.590  9.943   53.567  0.80 56.34  ? 348 PRO A CB    1 
ATOM   5409  C  CG    A PRO A 1 348 ? -8.975  11.168  52.283  0.20 61.01  ? 348 PRO A CG    1 
ATOM   5410  C  CG    B PRO A 1 348 ? -9.026  10.998  52.591  0.80 63.08  ? 348 PRO A CG    1 
ATOM   5411  C  CD    A PRO A 1 348 ? -7.756  11.114  51.414  0.20 53.55  ? 348 PRO A CD    1 
ATOM   5412  C  CD    B PRO A 1 348 ? -7.852  11.214  51.676  0.80 52.85  ? 348 PRO A CD    1 
ATOM   5413  N  N     A THR A 1 349 ? -5.657  9.104   55.064  0.20 58.12  ? 349 THR A N     1 
ATOM   5414  N  N     B THR A 1 349 ? -5.906  8.572   55.119  0.80 59.19  ? 349 THR A N     1 
ATOM   5415  C  CA    A THR A 1 349 ? -4.967  7.902   55.515  0.20 58.50  ? 349 THR A CA    1 
ATOM   5416  C  CA    B THR A 1 349 ? -5.210  7.324   55.412  0.80 60.37  ? 349 THR A CA    1 
ATOM   5417  C  C     A THR A 1 349 ? -5.961  6.876   56.044  0.20 56.68  ? 349 THR A C     1 
ATOM   5418  C  C     B THR A 1 349 ? -6.167  6.128   55.470  0.80 57.40  ? 349 THR A C     1 
ATOM   5419  O  O     A THR A 1 349 ? -6.354  6.927   57.214  0.20 60.92  ? 349 THR A O     1 
ATOM   5420  O  O     B THR A 1 349 ? -5.787  5.050   55.940  0.80 56.05  ? 349 THR A O     1 
ATOM   5421  C  CB    A THR A 1 349 ? -3.934  8.251   56.591  0.20 62.71  ? 349 THR A CB    1 
ATOM   5422  C  CB    B THR A 1 349 ? -4.425  7.478   56.725  0.80 63.84  ? 349 THR A CB    1 
ATOM   5423  O  OG1   A THR A 1 349 ? -3.031  9.243   56.085  0.20 55.76  ? 349 THR A OG1   1 
ATOM   5424  O  OG1   B THR A 1 349 ? -3.814  8.776   56.758  0.80 68.21  ? 349 THR A OG1   1 
ATOM   5425  C  CG2   A THR A 1 349 ? -3.143  7.015   57.000  0.20 57.06  ? 349 THR A CG2   1 
ATOM   5426  C  CG2   B THR A 1 349 ? -3.319  6.438   56.849  0.80 57.46  ? 349 THR A CG2   1 
ATOM   5427  N  N     A GLY A 1 350 ? -6.379  5.946   55.189  0.20 55.67  ? 350 GLY A N     1 
ATOM   5428  N  N     B GLY A 1 350 ? -7.391  6.289   54.968  0.80 53.98  ? 350 GLY A N     1 
ATOM   5429  C  CA    A GLY A 1 350 ? -7.348  4.947   55.592  0.20 51.57  ? 350 GLY A CA    1 
ATOM   5430  C  CA    B GLY A 1 350 ? -8.399  5.257   55.119  0.80 52.78  ? 350 GLY A CA    1 
ATOM   5431  C  C     A GLY A 1 350 ? -7.387  3.795   54.612  0.20 47.04  ? 350 GLY A C     1 
ATOM   5432  C  C     B GLY A 1 350 ? -8.203  4.095   54.155  0.80 53.90  ? 350 GLY A C     1 
ATOM   5433  O  O     A GLY A 1 350 ? -6.700  3.790   53.589  0.20 40.40  ? 350 GLY A O     1 
ATOM   5434  O  O     B GLY A 1 350 ? -7.881  4.273   52.981  0.80 44.32  ? 350 GLY A O     1 
ATOM   5435  N  N     A PHE A 1 351 ? -8.220  2.811   54.945  0.20 44.75  ? 351 PHE A N     1 
ATOM   5436  N  N     B PHE A 1 351 ? -8.397  2.890   54.680  0.80 45.14  ? 351 PHE A N     1 
ATOM   5437  C  CA    A PHE A 1 351 ? -8.377  1.597   54.157  0.20 38.33  ? 351 PHE A CA    1 
ATOM   5438  C  CA    B PHE A 1 351 ? -8.485  1.672   53.890  0.80 36.89  ? 351 PHE A CA    1 
ATOM   5439  C  C     A PHE A 1 351 ? -9.855  1.372   53.885  0.20 39.24  ? 351 PHE A C     1 
ATOM   5440  C  C     B PHE A 1 351 ? -9.954  1.374   53.631  0.80 39.07  ? 351 PHE A C     1 
ATOM   5441  O  O     A PHE A 1 351 ? -10.673 1.433   54.808  0.20 43.63  ? 351 PHE A O     1 
ATOM   5442  O  O     B PHE A 1 351 ? -10.770 1.404   54.555  0.80 45.05  ? 351 PHE A O     1 
ATOM   5443  C  CB    A PHE A 1 351 ? -7.793  0.381   54.886  0.20 39.45  ? 351 PHE A CB    1 
ATOM   5444  C  CB    B PHE A 1 351 ? -7.847  0.492   54.622  0.80 38.95  ? 351 PHE A CB    1 
ATOM   5445  C  CG    A PHE A 1 351 ? -6.325  0.492   55.187  0.20 37.46  ? 351 PHE A CG    1 
ATOM   5446  C  CG    B PHE A 1 351 ? -6.383  0.661   54.904  0.80 35.69  ? 351 PHE A CG    1 
ATOM   5447  C  CD1   A PHE A 1 351 ? -5.878  1.227   56.272  0.20 42.86  ? 351 PHE A CD1   1 
ATOM   5448  C  CD1   B PHE A 1 351 ? -5.953  1.375   56.006  0.80 42.13  ? 351 PHE A CD1   1 
ATOM   5449  C  CD2   A PHE A 1 351 ? -5.395  -0.156  54.397  0.20 42.08  ? 351 PHE A CD2   1 
ATOM   5450  C  CD2   B PHE A 1 351 ? -5.440  0.089   54.073  0.80 42.53  ? 351 PHE A CD2   1 
ATOM   5451  C  CE1   A PHE A 1 351 ? -4.528  1.325   56.553  0.20 46.30  ? 351 PHE A CE1   1 
ATOM   5452  C  CE1   B PHE A 1 351 ? -4.605  1.524   56.272  0.80 48.24  ? 351 PHE A CE1   1 
ATOM   5453  C  CE2   A PHE A 1 351 ? -4.043  -0.063  54.672  0.20 43.27  ? 351 PHE A CE2   1 
ATOM   5454  C  CE2   B PHE A 1 351 ? -4.088  0.235   54.330  0.80 44.27  ? 351 PHE A CE2   1 
ATOM   5455  C  CZ    A PHE A 1 351 ? -3.610  0.679   55.750  0.20 42.96  ? 351 PHE A CZ    1 
ATOM   5456  C  CZ    B PHE A 1 351 ? -3.669  0.955   55.428  0.80 40.99  ? 351 PHE A CZ    1 
ATOM   5457  N  N     A LYS A 1 352 ? -10.194 1.111   52.628  0.20 33.00  ? 352 LYS A N     1 
ATOM   5458  N  N     B LYS A 1 352 ? -10.289 1.084   52.384  0.80 31.31  ? 352 LYS A N     1 
ATOM   5459  C  CA    A LYS A 1 352 ? -11.552 0.755   52.243  0.20 35.43  ? 352 LYS A CA    1 
ATOM   5460  C  CA    B LYS A 1 352 ? -11.647 0.722   52.021  0.80 35.92  ? 352 LYS A CA    1 
ATOM   5461  C  C     A LYS A 1 352 ? -11.658 -0.760  52.151  0.20 32.51  ? 352 LYS A C     1 
ATOM   5462  C  C     B LYS A 1 352 ? -11.786 -0.793  52.051  0.80 32.52  ? 352 LYS A C     1 
ATOM   5463  O  O     A LYS A 1 352 ? -10.776 -1.414  51.584  0.20 33.58  ? 352 LYS A O     1 
ATOM   5464  O  O     B LYS A 1 352 ? -10.908 -1.511  51.562  0.80 34.02  ? 352 LYS A O     1 
ATOM   5465  C  CB    A LYS A 1 352 ? -11.934 1.406   50.912  0.20 36.32  ? 352 LYS A CB    1 
ATOM   5466  C  CB    B LYS A 1 352 ? -11.987 1.266   50.634  0.80 37.03  ? 352 LYS A CB    1 
ATOM   5467  C  CG    A LYS A 1 352 ? -12.124 2.910   51.000  0.20 37.11  ? 352 LYS A CG    1 
ATOM   5468  C  CG    B LYS A 1 352 ? -12.131 2.775   50.555  0.80 38.00  ? 352 LYS A CG    1 
ATOM   5469  C  CD    A LYS A 1 352 ? -12.719 3.467   49.719  0.20 39.63  ? 352 LYS A CD    1 
ATOM   5470  C  CD    B LYS A 1 352 ? -12.479 3.183   49.124  0.80 38.12  ? 352 LYS A CD    1 
ATOM   5471  C  CE    A LYS A 1 352 ? -13.056 4.941   49.868  0.20 43.65  ? 352 LYS A CE    1 
ATOM   5472  C  CE    B LYS A 1 352 ? -12.953 4.625   49.030  0.80 43.64  ? 352 LYS A CE    1 
ATOM   5473  N  NZ    A LYS A 1 352 ? -11.843 5.757   50.147  0.20 48.47  ? 352 LYS A NZ    1 
ATOM   5474  N  NZ    B LYS A 1 352 ? -11.914 5.594   49.466  0.80 49.69  ? 352 LYS A NZ    1 
ATOM   5475  N  N     A VAL A 1 353 ? -12.728 -1.316  52.713  0.20 29.91  ? 353 VAL A N     1 
ATOM   5476  N  N     B VAL A 1 353 ? -12.891 -1.280  52.620  0.80 28.84  ? 353 VAL A N     1 
ATOM   5477  C  CA    A VAL A 1 353 ? -12.882 -2.759  52.848  0.20 31.70  ? 353 VAL A CA    1 
ATOM   5478  C  CA    B VAL A 1 353 ? -13.058 -2.706  52.888  0.80 31.92  ? 353 VAL A CA    1 
ATOM   5479  C  C     A VAL A 1 353 ? -14.160 -3.198  52.148  0.20 30.13  ? 353 VAL A C     1 
ATOM   5480  C  C     B VAL A 1 353 ? -14.332 -3.215  52.224  0.80 29.92  ? 353 VAL A C     1 
ATOM   5481  O  O     A VAL A 1 353 ? -15.191 -2.520  52.227  0.20 33.73  ? 353 VAL A O     1 
ATOM   5482  O  O     B VAL A 1 353 ? -15.407 -2.622  52.382  0.80 34.44  ? 353 VAL A O     1 
ATOM   5483  C  CB    A VAL A 1 353 ? -12.895 -3.186  54.332  0.20 34.13  ? 353 VAL A CB    1 
ATOM   5484  C  CB    B VAL A 1 353 ? -13.074 -2.997  54.403  0.80 34.84  ? 353 VAL A CB    1 
ATOM   5485  C  CG1   A VAL A 1 353 ? -12.888 -4.698  54.453  0.20 29.94  ? 353 VAL A CG1   1 
ATOM   5486  C  CG1   B VAL A 1 353 ? -13.493 -4.436  54.670  0.80 30.89  ? 353 VAL A CG1   1 
ATOM   5487  C  CG2   A VAL A 1 353 ? -11.705 -2.584  55.069  0.20 31.10  ? 353 VAL A CG2   1 
ATOM   5488  C  CG2   B VAL A 1 353 ? -11.700 -2.715  55.012  0.80 31.05  ? 353 VAL A CG2   1 
ATOM   5489  N  N     A GLY A 1 354 ? -14.086 -4.333  51.457  0.20 31.53  ? 354 GLY A N     1 
ATOM   5490  N  N     B GLY A 1 354 ? -14.212 -4.315  51.499  0.80 31.65  ? 354 GLY A N     1 
ATOM   5491  C  CA    A GLY A 1 354 ? -15.250 -4.941  50.839  0.20 29.79  ? 354 GLY A CA    1 
ATOM   5492  C  CA    B GLY A 1 354 ? -15.377 -5.036  51.004  0.80 29.70  ? 354 GLY A CA    1 
ATOM   5493  C  C     A GLY A 1 354 ? -15.252 -6.443  51.035  0.20 27.05  ? 354 GLY A C     1 
ATOM   5494  C  C     B GLY A 1 354 ? -15.236 -6.506  51.326  0.80 26.89  ? 354 GLY A C     1 
ATOM   5495  O  O     A GLY A 1 354 ? -14.447 -7.152  50.426  0.20 25.75  ? 354 GLY A O     1 
ATOM   5496  O  O     B GLY A 1 354 ? -14.137 -7.050  51.307  0.80 25.18  ? 354 GLY A O     1 
ATOM   5497  N  N     A ILE A 1 355 ? -16.150 -6.944  51.878  0.20 28.78  ? 355 ILE A N     1 
ATOM   5498  N  N     B ILE A 1 355 ? -16.361 -7.144  51.647  0.80 29.99  ? 355 ILE A N     1 
ATOM   5499  C  CA    A ILE A 1 355 ? -16.132 -8.338  52.303  0.20 26.75  ? 355 ILE A CA    1 
ATOM   5500  C  CA    B ILE A 1 355 ? -16.362 -8.560  51.996  0.80 26.55  ? 355 ILE A CA    1 
ATOM   5501  C  C     A ILE A 1 355 ? -17.158 -9.124  51.498  0.20 27.69  ? 355 ILE A C     1 
ATOM   5502  C  C     B ILE A 1 355 ? -17.408 -9.291  51.160  0.80 28.26  ? 355 ILE A C     1 
ATOM   5503  O  O     A ILE A 1 355 ? -18.352 -8.799  51.506  0.20 27.51  ? 355 ILE A O     1 
ATOM   5504  O  O     B ILE A 1 355 ? -18.556 -8.844  51.061  0.80 26.32  ? 355 ILE A O     1 
ATOM   5505  C  CB    A ILE A 1 355 ? -16.400 -8.465  53.810  0.20 27.92  ? 355 ILE A CB    1 
ATOM   5506  C  CB    B ILE A 1 355 ? -16.618 -8.777  53.499  0.80 27.44  ? 355 ILE A CB    1 
ATOM   5507  C  CG1   A ILE A 1 355 ? -15.340 -7.695  54.598  0.20 27.65  ? 355 ILE A CG1   1 
ATOM   5508  C  CG1   B ILE A 1 355 ? -15.562 -8.037  54.327  0.80 28.47  ? 355 ILE A CG1   1 
ATOM   5509  C  CG2   A ILE A 1 355 ? -16.412 -9.923  54.218  0.20 26.85  ? 355 ILE A CG2   1 
ATOM   5510  C  CG2   B ILE A 1 355 ? -16.595 -10.249 53.810  0.80 26.81  ? 355 ILE A CG2   1 
ATOM   5511  C  CD1   A ILE A 1 355 ? -15.534 -7.744  56.099  0.20 27.83  ? 355 ILE A CD1   1 
ATOM   5512  C  CD1   B ILE A 1 355 ? -15.816 -8.059  55.838  0.80 31.02  ? 355 ILE A CD1   1 
ATOM   5513  N  N     A ASN A 1 356 ? -16.688 -10.155 50.802  0.20 25.27  ? 356 ASN A N     1 
ATOM   5514  N  N     B ASN A 1 356 ? -16.998 -10.395 50.539  0.80 24.79  ? 356 ASN A N     1 
ATOM   5515  C  CA    A ASN A 1 356 ? -17.534 -11.132 50.129  0.20 26.72  ? 356 ASN A CA    1 
ATOM   5516  C  CA    B ASN A 1 356 ? -17.876 -11.339 49.855  0.80 27.07  ? 356 ASN A CA    1 
ATOM   5517  C  C     A ASN A 1 356 ? -17.466 -12.420 50.936  0.20 25.72  ? 356 ASN A C     1 
ATOM   5518  C  C     B ASN A 1 356 ? -17.781 -12.632 50.645  0.80 24.22  ? 356 ASN A C     1 
ATOM   5519  O  O     A ASN A 1 356 ? -16.382 -12.982 51.122  0.20 26.48  ? 356 ASN A O     1 
ATOM   5520  O  O     B ASN A 1 356 ? -16.691 -13.191 50.790  0.80 29.20  ? 356 ASN A O     1 
ATOM   5521  C  CB    A ASN A 1 356 ? -17.074 -11.359 48.687  0.20 28.17  ? 356 ASN A CB    1 
ATOM   5522  C  CB    B ASN A 1 356 ? -17.448 -11.549 48.395  0.80 27.56  ? 356 ASN A CB    1 
ATOM   5523  C  CG    A ASN A 1 356 ? -18.042 -12.213 47.880  0.20 29.23  ? 356 ASN A CG    1 
ATOM   5524  C  CG    B ASN A 1 356 ? -18.327 -12.562 47.639  0.80 30.85  ? 356 ASN A CG    1 
ATOM   5525  O  OD1   A ASN A 1 356 ? -18.873 -12.936 48.434  0.20 30.93  ? 356 ASN A OD1   1 
ATOM   5526  O  OD1   B ASN A 1 356 ? -18.537 -13.702 48.076  0.80 28.89  ? 356 ASN A OD1   1 
ATOM   5527  N  ND2   A ASN A 1 356 ? -17.934 -12.133 46.559  0.20 30.86  ? 356 ASN A ND2   1 
ATOM   5528  N  ND2   B ASN A 1 356 ? -18.845 -12.137 46.490  0.80 34.40  ? 356 ASN A ND2   1 
ATOM   5529  N  N     A TYR A 1 357 ? -18.620 -12.881 51.424  0.20 26.96  ? 357 TYR A N     1 
ATOM   5530  N  N     B TYR A 1 357 ? -18.901 -13.085 51.196  0.80 27.63  ? 357 TYR A N     1 
ATOM   5531  C  CA    A TYR A 1 357 ? -18.673 -13.987 52.373  0.20 25.68  ? 357 TYR A CA    1 
ATOM   5532  C  CA    B TYR A 1 357 ? -18.802 -14.150 52.189  0.80 25.18  ? 357 TYR A CA    1 
ATOM   5533  C  C     A TYR A 1 357 ? -18.731 -15.354 51.699  0.20 27.52  ? 357 TYR A C     1 
ATOM   5534  C  C     B TYR A 1 357 ? -18.756 -15.543 51.588  0.80 27.93  ? 357 TYR A C     1 
ATOM   5535  O  O     A TYR A 1 357 ? -19.369 -16.272 52.229  0.20 28.51  ? 357 TYR A O     1 
ATOM   5536  O  O     B TYR A 1 357 ? -18.677 -16.516 52.343  0.80 26.71  ? 357 TYR A O     1 
ATOM   5537  C  CB    A TYR A 1 357 ? -19.867 -13.812 53.314  0.20 24.95  ? 357 TYR A CB    1 
ATOM   5538  C  CB    B TYR A 1 357 ? -19.956 -14.035 53.184  0.80 24.66  ? 357 TYR A CB    1 
ATOM   5539  C  CG    A TYR A 1 357 ? -19.881 -12.505 54.080  0.20 26.74  ? 357 TYR A CG    1 
ATOM   5540  C  CG    B TYR A 1 357 ? -19.857 -12.792 54.014  0.80 26.79  ? 357 TYR A CG    1 
ATOM   5541  C  CD1   A TYR A 1 357 ? -19.235 -12.386 55.304  0.20 27.92  ? 357 TYR A CD1   1 
ATOM   5542  C  CD1   B TYR A 1 357 ? -19.099 -12.773 55.177  0.80 29.12  ? 357 TYR A CD1   1 
ATOM   5543  C  CD2   A TYR A 1 357 ? -20.559 -11.397 53.588  0.20 25.40  ? 357 TYR A CD2   1 
ATOM   5544  C  CD2   B TYR A 1 357 ? -20.520 -11.633 53.642  0.80 24.56  ? 357 TYR A CD2   1 
ATOM   5545  C  CE1   A TYR A 1 357 ? -19.252 -11.195 56.014  0.20 26.23  ? 357 TYR A CE1   1 
ATOM   5546  C  CE1   B TYR A 1 357 ? -19.010 -11.632 55.958  0.80 25.15  ? 357 TYR A CE1   1 
ATOM   5547  C  CE2   A TYR A 1 357 ? -20.583 -10.203 54.290  0.20 28.55  ? 357 TYR A CE2   1 
ATOM   5548  C  CE2   B TYR A 1 357 ? -20.434 -10.490 54.417  0.80 29.40  ? 357 TYR A CE2   1 
ATOM   5549  C  CZ    A TYR A 1 357 ? -19.929 -10.108 55.502  0.20 27.76  ? 357 TYR A CZ    1 
ATOM   5550  C  CZ    B TYR A 1 357 ? -19.675 -10.500 55.571  0.80 27.61  ? 357 TYR A CZ    1 
ATOM   5551  O  OH    A TYR A 1 357 ? -19.953 -8.920  56.201  0.20 26.42  ? 357 TYR A OH    1 
ATOM   5552  O  OH    B TYR A 1 357 ? -19.586 -9.372  56.342  0.80 26.55  ? 357 TYR A OH    1 
ATOM   5553  N  N     A GLN A 1 358 ? -18.082 -15.523 50.548  0.20 26.95  ? 358 GLN A N     1 
ATOM   5554  N  N     B GLN A 1 358 ? -18.775 -15.667 50.264  0.80 25.16  ? 358 GLN A N     1 
ATOM   5555  C  CA    A GLN A 1 358 ? -17.988 -16.821 49.902  0.20 28.88  ? 358 GLN A CA    1 
ATOM   5556  C  CA    B GLN A 1 358 ? -18.519 -16.958 49.631  0.80 31.86  ? 358 GLN A CA    1 
ATOM   5557  C  C     A GLN A 1 358 ? -16.524 -17.175 49.679  0.20 28.61  ? 358 GLN A C     1 
ATOM   5558  C  C     B GLN A 1 358 ? -17.015 -17.159 49.472  0.80 28.40  ? 358 GLN A C     1 
ATOM   5559  O  O     A GLN A 1 358 ? -15.761 -16.338 49.178  0.20 28.23  ? 358 GLN A O     1 
ATOM   5560  O  O     B GLN A 1 358 ? -16.317 -16.231 49.044  0.80 30.54  ? 358 GLN A O     1 
ATOM   5561  C  CB    A GLN A 1 358 ? -18.744 -16.835 48.561  0.20 32.35  ? 358 GLN A CB    1 
ATOM   5562  C  CB    B GLN A 1 358 ? -19.211 -17.032 48.270  0.80 32.18  ? 358 GLN A CB    1 
ATOM   5563  C  CG    A GLN A 1 358 ? -18.812 -18.207 47.898  0.20 35.38  ? 358 GLN A CG    1 
ATOM   5564  C  CG    B GLN A 1 358 ? -19.289 -18.434 47.653  0.80 37.21  ? 358 GLN A CG    1 
ATOM   5565  C  CD    A GLN A 1 358 ? -19.624 -19.211 48.701  0.20 35.94  ? 358 GLN A CD    1 
ATOM   5566  C  CD    B GLN A 1 358 ? -20.280 -19.337 48.369  0.80 36.76  ? 358 GLN A CD    1 
ATOM   5567  O  OE1   A GLN A 1 358 ? -20.469 -18.836 49.516  0.20 32.43  ? 358 GLN A OE1   1 
ATOM   5568  O  OE1   B GLN A 1 358 ? -20.966 -18.913 49.298  0.80 33.04  ? 358 GLN A OE1   1 
ATOM   5569  N  NE2   A GLN A 1 358 ? -19.367 -20.495 48.477  0.20 36.13  ? 358 GLN A NE2   1 
ATOM   5570  N  NE2   B GLN A 1 358 ? -20.351 -20.591 47.942  0.80 42.68  ? 358 GLN A NE2   1 
ATOM   5571  N  N     A PRO A 1 359 ? -16.090 -18.377 50.048  0.20 29.05  ? 359 PRO A N     1 
ATOM   5572  N  N     B PRO A 1 359 ? -16.469 -18.320 49.830  0.80 27.52  ? 359 PRO A N     1 
ATOM   5573  C  CA    A PRO A 1 359 ? -14.685 -18.761 49.849  0.20 29.86  ? 359 PRO A CA    1 
ATOM   5574  C  CA    B PRO A 1 359 ? -15.024 -18.558 49.639  0.80 31.35  ? 359 PRO A CA    1 
ATOM   5575  C  C     A PRO A 1 359 ? -14.347 -18.838 48.372  0.20 31.45  ? 359 PRO A C     1 
ATOM   5576  C  C     B PRO A 1 359 ? -14.697 -18.664 48.162  0.80 31.55  ? 359 PRO A C     1 
ATOM   5577  O  O     A PRO A 1 359 ? -15.239 -19.044 47.535  0.20 29.24  ? 359 PRO A O     1 
ATOM   5578  O  O     B PRO A 1 359 ? -15.600 -18.913 47.347  0.80 26.71  ? 359 PRO A O     1 
ATOM   5579  C  CB    A PRO A 1 359 ? -14.599 -20.145 50.510  0.20 31.55  ? 359 PRO A CB    1 
ATOM   5580  C  CB    B PRO A 1 359 ? -14.789 -19.895 50.357  0.80 31.61  ? 359 PRO A CB    1 
ATOM   5581  C  CG    A PRO A 1 359 ? -15.754 -20.187 51.463  0.20 29.63  ? 359 PRO A CG    1 
ATOM   5582  C  CG    B PRO A 1 359 ? -16.120 -20.569 50.344  0.80 31.94  ? 359 PRO A CG    1 
ATOM   5583  C  CD    A PRO A 1 359 ? -16.839 -19.394 50.804  0.20 30.89  ? 359 PRO A CD    1 
ATOM   5584  C  CD    B PRO A 1 359 ? -17.143 -19.471 50.453  0.80 32.50  ? 359 PRO A CD    1 
ATOM   5585  N  N     A PRO A 1 360 ? -13.072 -18.675 48.011  0.20 31.91  ? 360 PRO A N     1 
ATOM   5586  N  N     B PRO A 1 360 ? -13.428 -18.494 47.774  0.80 34.02  ? 360 PRO A N     1 
ATOM   5587  C  CA    A PRO A 1 360 ? -12.691 -18.764 46.597  0.20 31.30  ? 360 PRO A CA    1 
ATOM   5588  C  CA    B PRO A 1 360 ? -13.094 -18.554 46.349  0.80 29.46  ? 360 PRO A CA    1 
ATOM   5589  C  C     A PRO A 1 360 ? -12.986 -20.143 46.026  0.20 33.31  ? 360 PRO A C     1 
ATOM   5590  C  C     B PRO A 1 360 ? -13.203 -19.975 45.817  0.80 34.07  ? 360 PRO A C     1 
ATOM   5591  O  O     A PRO A 1 360 ? -12.972 -21.152 46.735  0.20 30.69  ? 360 PRO A O     1 
ATOM   5592  O  O     B PRO A 1 360 ? -13.043 -20.958 46.548  0.80 30.23  ? 360 PRO A O     1 
ATOM   5593  C  CB    A PRO A 1 360 ? -11.183 -18.479 46.614  0.20 33.26  ? 360 PRO A CB    1 
ATOM   5594  C  CB    B PRO A 1 360 ? -11.641 -18.054 46.289  0.80 35.03  ? 360 PRO A CB    1 
ATOM   5595  C  CG    A PRO A 1 360 ? -10.938 -17.756 47.893  0.20 33.39  ? 360 PRO A CG    1 
ATOM   5596  C  CG    B PRO A 1 360 ? -11.264 -17.653 47.688  0.80 36.47  ? 360 PRO A CG    1 
ATOM   5597  C  CD    A PRO A 1 360 ? -11.933 -18.313 48.872  0.20 28.73  ? 360 PRO A CD    1 
ATOM   5598  C  CD    B PRO A 1 360 ? -12.222 -18.361 48.607  0.80 27.61  ? 360 PRO A CD    1 
ATOM   5599  N  N     A THR A 1 361 ? -13.253 -20.174 44.725  0.20 32.11  ? 361 THR A N     1 
ATOM   5600  N  N     B THR A 1 361 ? -13.477 -20.066 44.518  0.80 32.35  ? 361 THR A N     1 
ATOM   5601  C  CA    A THR A 1 361 ? -13.562 -21.406 44.011  0.20 31.50  ? 361 THR A CA    1 
ATOM   5602  C  CA    B THR A 1 361 ? -13.548 -21.325 43.798  0.80 30.82  ? 361 THR A CA    1 
ATOM   5603  C  C     A THR A 1 361 ? -12.296 -21.951 43.367  0.20 33.41  ? 361 THR A C     1 
ATOM   5604  C  C     B THR A 1 361 ? -12.158 -21.683 43.289  0.80 33.01  ? 361 THR A C     1 
ATOM   5605  O  O     A THR A 1 361 ? -11.571 -21.213 42.691  0.20 32.84  ? 361 THR A O     1 
ATOM   5606  O  O     B THR A 1 361 ? -11.363 -20.806 42.950  0.80 31.85  ? 361 THR A O     1 
ATOM   5607  C  CB    A THR A 1 361 ? -14.636 -21.165 42.947  0.20 32.53  ? 361 THR A CB    1 
ATOM   5608  C  CB    B THR A 1 361 ? -14.537 -21.208 42.628  0.80 32.36  ? 361 THR A CB    1 
ATOM   5609  O  OG1   A THR A 1 361 ? -15.909 -20.979 43.580  0.20 32.34  ? 361 THR A OG1   1 
ATOM   5610  O  OG1   B THR A 1 361 ? -15.850 -20.893 43.122  0.80 32.55  ? 361 THR A OG1   1 
ATOM   5611  C  CG2   A THR A 1 361 ? -14.723 -22.342 41.983  0.20 33.05  ? 361 THR A CG2   1 
ATOM   5612  C  CG2   B THR A 1 361 ? -14.614 -22.499 41.820  0.80 33.42  ? 361 THR A CG2   1 
ATOM   5613  N  N     A VAL A 1 362 ? -12.026 -23.229 43.583  0.20 34.01  ? 362 VAL A N     1 
ATOM   5614  N  N     B VAL A 1 362 ? -11.848 -22.973 43.260  0.80 35.97  ? 362 VAL A N     1 
ATOM   5615  C  CA    A VAL A 1 362 ? -10.891 -23.881 42.943  0.20 40.34  ? 362 VAL A CA    1 
ATOM   5616  C  CA    B VAL A 1 362 ? -10.655 -23.449 42.565  0.80 41.06  ? 362 VAL A CA    1 
ATOM   5617  C  C     A VAL A 1 362 ? -11.364 -24.515 41.643  0.20 37.77  ? 362 VAL A C     1 
ATOM   5618  C  C     B VAL A 1 362 ? -11.102 -24.295 41.387  0.80 38.04  ? 362 VAL A C     1 
ATOM   5619  O  O     A VAL A 1 362 ? -12.539 -24.862 41.484  0.20 38.54  ? 362 VAL A O     1 
ATOM   5620  O  O     B VAL A 1 362 ? -12.111 -25.005 41.464  0.80 38.12  ? 362 VAL A O     1 
ATOM   5621  C  CB    A VAL A 1 362 ? -10.234 -24.920 43.876  0.20 44.30  ? 362 VAL A CB    1 
ATOM   5622  C  CB    B VAL A 1 362 ? -9.698  -24.248 43.472  0.80 45.70  ? 362 VAL A CB    1 
ATOM   5623  C  CG1   A VAL A 1 362 ? -9.660  -24.237 45.111  0.20 37.92  ? 362 VAL A CG1   1 
ATOM   5624  C  CG1   B VAL A 1 362 ? -8.826  -23.306 44.298  0.80 37.22  ? 362 VAL A CG1   1 
ATOM   5625  C  CG2   A VAL A 1 362 ? -11.235 -25.996 44.262  0.20 41.15  ? 362 VAL A CG2   1 
ATOM   5626  C  CG2   B VAL A 1 362 ? -10.486 -25.211 44.352  0.80 47.60  ? 362 VAL A CG2   1 
ATOM   5627  N  N     A VAL A 1 363 ? -10.441 -24.657 40.698  0.20 37.76  ? 363 VAL A N     1 
ATOM   5628  N  N     B VAL A 1 363 ? -10.351 -24.214 40.297  0.80 38.03  ? 363 VAL A N     1 
ATOM   5629  C  CA    A VAL A 1 363 ? -10.764 -25.225 39.392  0.20 37.23  ? 363 VAL A CA    1 
ATOM   5630  C  CA    B VAL A 1 363 ? -10.673 -24.960 39.086  0.80 35.27  ? 363 VAL A CA    1 
ATOM   5631  C  C     A VAL A 1 363 ? -10.256 -26.661 39.341  0.20 39.94  ? 363 VAL A C     1 
ATOM   5632  C  C     B VAL A 1 363 ? -10.146 -26.382 39.247  0.80 39.86  ? 363 VAL A C     1 
ATOM   5633  O  O     A VAL A 1 363 ? -9.216  -26.972 39.941  0.20 36.92  ? 363 VAL A O     1 
ATOM   5634  O  O     B VAL A 1 363 ? -9.059  -26.580 39.813  0.80 33.66  ? 363 VAL A O     1 
ATOM   5635  C  CB    A VAL A 1 363 ? -10.176 -24.374 38.254  0.20 42.10  ? 363 VAL A CB    1 
ATOM   5636  C  CB    B VAL A 1 363 ? -10.094 -24.273 37.835  0.80 43.46  ? 363 VAL A CB    1 
ATOM   5637  C  CG1   A VAL A 1 363 ? -10.773 -22.975 38.281  0.20 40.06  ? 363 VAL A CG1   1 
ATOM   5638  C  CG1   B VAL A 1 363 ? -10.842 -22.974 37.549  0.80 45.48  ? 363 VAL A CG1   1 
ATOM   5639  C  CG2   A VAL A 1 363 ? -8.661  -24.305 38.360  0.20 42.60  ? 363 VAL A CG2   1 
ATOM   5640  C  CG2   B VAL A 1 363 ? -8.621  -23.982 38.018  0.80 44.40  ? 363 VAL A CG2   1 
ATOM   5641  N  N     A PRO A 1 364 ? -10.958 -27.573 38.662  0.20 42.38  ? 364 PRO A N     1 
ATOM   5642  N  N     B PRO A 1 364 ? -10.880 -27.397 38.795  0.80 42.72  ? 364 PRO A N     1 
ATOM   5643  C  CA    A PRO A 1 364 ? -10.455 -28.947 38.544  0.20 42.05  ? 364 PRO A CA    1 
ATOM   5644  C  CA    B PRO A 1 364 ? -10.329 -28.756 38.816  0.80 42.03  ? 364 PRO A CA    1 
ATOM   5645  C  C     A PRO A 1 364 ? -9.178  -29.009 37.722  0.20 42.57  ? 364 PRO A C     1 
ATOM   5646  C  C     B PRO A 1 364 ? -9.087  -28.835 37.943  0.80 42.07  ? 364 PRO A C     1 
ATOM   5647  O  O     A PRO A 1 364 ? -9.196  -28.784 36.508  0.20 43.42  ? 364 PRO A O     1 
ATOM   5648  O  O     B PRO A 1 364 ? -9.006  -28.210 36.882  0.80 41.49  ? 364 PRO A O     1 
ATOM   5649  C  CB    A PRO A 1 364 ? -11.610 -29.690 37.859  0.20 45.17  ? 364 PRO A CB    1 
ATOM   5650  C  CB    B PRO A 1 364 ? -11.473 -29.617 38.267  0.80 45.32  ? 364 PRO A CB    1 
ATOM   5651  C  CG    A PRO A 1 364 ? -12.382 -28.625 37.152  0.20 44.63  ? 364 PRO A CG    1 
ATOM   5652  C  CG    B PRO A 1 364 ? -12.381 -28.660 37.542  0.80 45.41  ? 364 PRO A CG    1 
ATOM   5653  C  CD    A PRO A 1 364 ? -12.268 -27.402 38.012  0.20 44.42  ? 364 PRO A CD    1 
ATOM   5654  C  CD    B PRO A 1 364 ? -12.260 -27.360 38.278  0.80 45.49  ? 364 PRO A CD    1 
ATOM   5655  N  N     A GLY A 1 365 ? -8.062  -29.307 38.379  0.20 43.27  ? 365 GLY A N     1 
ATOM   5656  N  N     B GLY A 1 365 ? -8.103  -29.594 38.407  0.80 43.11  ? 365 GLY A N     1 
ATOM   5657  C  CA    A GLY A 1 365 ? -6.767  -29.310 37.735  0.20 43.63  ? 365 GLY A CA    1 
ATOM   5658  C  CA    B GLY A 1 365 ? -6.835  -29.673 37.717  0.80 45.40  ? 365 GLY A CA    1 
ATOM   5659  C  C     A GLY A 1 365 ? -5.856  -28.161 38.107  0.20 41.36  ? 365 GLY A C     1 
ATOM   5660  C  C     B GLY A 1 365 ? -5.838  -28.594 38.076  0.80 43.28  ? 365 GLY A C     1 
ATOM   5661  O  O     A GLY A 1 365 ? -4.812  -27.992 37.467  0.20 41.44  ? 365 GLY A O     1 
ATOM   5662  O  O     B GLY A 1 365 ? -4.658  -28.729 37.730  0.80 39.96  ? 365 GLY A O     1 
ATOM   5663  N  N     A GLY A 1 366 ? -6.210  -27.368 39.120  0.20 37.42  ? 366 GLY A N     1 
ATOM   5664  N  N     B GLY A 1 366 ? -6.255  -27.564 38.804  0.80 35.49  ? 366 GLY A N     1 
ATOM   5665  C  CA    A GLY A 1 366 ? -5.387  -26.248 39.516  0.20 35.41  ? 366 GLY A CA    1 
ATOM   5666  C  CA    B GLY A 1 366 ? -5.383  -26.460 39.143  0.80 34.65  ? 366 GLY A CA    1 
ATOM   5667  C  C     A GLY A 1 366 ? -4.332  -26.617 40.543  0.20 37.36  ? 366 GLY A C     1 
ATOM   5668  C  C     B GLY A 1 366 ? -4.310  -26.828 40.161  0.80 39.08  ? 366 GLY A C     1 
ATOM   5669  O  O     A GLY A 1 366 ? -4.391  -27.664 41.186  0.20 36.03  ? 366 GLY A O     1 
ATOM   5670  O  O     B GLY A 1 366 ? -4.149  -27.973 40.585  0.80 41.11  ? 366 GLY A O     1 
ATOM   5671  N  N     A ASP A 1 367 ? -3.353  -25.728 40.691  0.20 33.51  ? 367 ASP A N     1 
ATOM   5672  N  N     B ASP A 1 367 ? -3.568  -25.800 40.564  0.80 32.78  ? 367 ASP A N     1 
ATOM   5673  C  CA    A ASP A 1 367 ? -2.261  -25.907 41.636  0.20 29.88  ? 367 ASP A CA    1 
ATOM   5674  C  CA    B ASP A 1 367 ? -2.426  -25.935 41.456  0.80 28.24  ? 367 ASP A CA    1 
ATOM   5675  C  C     A ASP A 1 367 ? -2.528  -25.243 42.982  0.20 34.46  ? 367 ASP A C     1 
ATOM   5676  C  C     B ASP A 1 367 ? -2.720  -25.520 42.892  0.80 35.02  ? 367 ASP A C     1 
ATOM   5677  O  O     A ASP A 1 367 ? -1.615  -25.163 43.810  0.20 31.64  ? 367 ASP A O     1 
ATOM   5678  O  O     B ASP A 1 367 ? -1.880  -25.757 43.766  0.80 30.65  ? 367 ASP A O     1 
ATOM   5679  C  CB    A ASP A 1 367 ? -0.959  -25.361 41.045  0.20 34.53  ? 367 ASP A CB    1 
ATOM   5680  C  CB    B ASP A 1 367 ? -1.259  -25.093 40.933  0.80 34.53  ? 367 ASP A CB    1 
ATOM   5681  C  CG    A ASP A 1 367 ? -0.728  -25.820 39.620  0.20 34.91  ? 367 ASP A CG    1 
ATOM   5682  C  CG    B ASP A 1 367 ? -0.761  -25.562 39.583  0.80 35.60  ? 367 ASP A CG    1 
ATOM   5683  O  OD1   A ASP A 1 367 ? -1.294  -26.861 39.226  0.20 29.06  ? 367 ASP A OD1   1 
ATOM   5684  O  OD1   B ASP A 1 367 ? -0.414  -26.755 39.465  0.80 35.40  ? 367 ASP A OD1   1 
ATOM   5685  O  OD2   A ASP A 1 367 ? 0.022   -25.137 38.893  0.20 33.84  ? 367 ASP A OD2   1 
ATOM   5686  O  OD2   B ASP A 1 367 ? -0.731  -24.741 38.638  0.80 31.38  ? 367 ASP A OD2   1 
ATOM   5687  N  N     A LEU A 1 368 ? -3.746  -24.763 43.215  0.20 33.61  ? 368 LEU A N     1 
ATOM   5688  N  N     B LEU A 1 368 ? -3.873  -24.908 43.153  0.80 33.48  ? 368 LEU A N     1 
ATOM   5689  C  CA    A LEU A 1 368 ? -4.106  -24.085 44.450  0.20 35.93  ? 368 LEU A CA    1 
ATOM   5690  C  CA    B LEU A 1 368 ? -4.154  -24.255 44.425  0.80 36.54  ? 368 LEU A CA    1 
ATOM   5691  C  C     A LEU A 1 368 ? -5.006  -24.972 45.302  0.20 34.45  ? 368 LEU A C     1 
ATOM   5692  C  C     B LEU A 1 368 ? -4.999  -25.131 45.342  0.80 34.45  ? 368 LEU A C     1 
ATOM   5693  O  O     A LEU A 1 368 ? -5.826  -25.734 44.783  0.20 37.64  ? 368 LEU A O     1 
ATOM   5694  O  O     B LEU A 1 368 ? -5.902  -25.835 44.885  0.80 38.28  ? 368 LEU A O     1 
ATOM   5695  C  CB    A LEU A 1 368 ? -4.820  -22.760 44.163  0.20 32.44  ? 368 LEU A CB    1 
ATOM   5696  C  CB    B LEU A 1 368 ? -4.887  -22.934 44.196  0.80 32.02  ? 368 LEU A CB    1 
ATOM   5697  C  CG    A LEU A 1 368 ? -4.035  -21.717 43.369  0.20 34.44  ? 368 LEU A CG    1 
ATOM   5698  C  CG    B LEU A 1 368 ? -4.064  -21.813 43.580  0.80 34.54  ? 368 LEU A CG    1 
ATOM   5699  C  CD1   A LEU A 1 368 ? -4.899  -20.493 43.111  0.20 34.54  ? 368 LEU A CD1   1 
ATOM   5700  C  CD1   B LEU A 1 368 ? -4.908  -20.554 43.497  0.80 33.88  ? 368 LEU A CD1   1 
ATOM   5701  C  CD2   A LEU A 1 368 ? -2.762  -21.335 44.105  0.20 35.64  ? 368 LEU A CD2   1 
ATOM   5702  C  CD2   B LEU A 1 368 ? -2.819  -21.588 44.409  0.80 37.09  ? 368 LEU A CD2   1 
ATOM   5703  N  N     A ALA A 1 369 ? -4.846  -24.863 46.617  0.20 32.72  ? 369 ALA A N     1 
ATOM   5704  N  N     B ALA A 1 369 ? -4.713  -25.065 46.643  0.80 32.25  ? 369 ALA A N     1 
ATOM   5705  C  CA    A ALA A 1 369 ? -5.665  -25.598 47.569  0.20 33.74  ? 369 ALA A CA    1 
ATOM   5706  C  CA    B ALA A 1 369 ? -5.592  -25.657 47.642  0.80 33.80  ? 369 ALA A CA    1 
ATOM   5707  C  C     A ALA A 1 369 ? -6.831  -24.736 48.035  0.20 32.22  ? 369 ALA A C     1 
ATOM   5708  C  C     B ALA A 1 369 ? -6.818  -24.779 47.849  0.80 31.38  ? 369 ALA A C     1 
ATOM   5709  O  O     A ALA A 1 369 ? -6.758  -23.504 48.032  0.20 31.35  ? 369 ALA A O     1 
ATOM   5710  O  O     B ALA A 1 369 ? -6.767  -23.554 47.698  0.80 30.08  ? 369 ALA A O     1 
ATOM   5711  C  CB    A ALA A 1 369 ? -4.840  -26.049 48.776  0.20 33.18  ? 369 ALA A CB    1 
ATOM   5712  C  CB    B ALA A 1 369 ? -4.862  -25.835 48.976  0.80 31.63  ? 369 ALA A CB    1 
ATOM   5713  N  N     A LYS A 1 370 ? -7.912  -25.401 48.438  0.20 37.10  ? 370 LYS A N     1 
ATOM   5714  N  N     B LYS A 1 370 ? -7.932  -25.418 48.200  0.80 38.07  ? 370 LYS A N     1 
ATOM   5715  C  CA    A LYS A 1 370 ? -9.074  -24.692 48.955  0.20 33.86  ? 370 LYS A CA    1 
ATOM   5716  C  CA    B LYS A 1 370 ? -9.092  -24.681 48.677  0.80 33.00  ? 370 LYS A CA    1 
ATOM   5717  C  C     A LYS A 1 370 ? -8.723  -23.963 50.247  0.20 32.44  ? 370 LYS A C     1 
ATOM   5718  C  C     B LYS A 1 370 ? -8.754  -23.940 49.966  0.80 31.20  ? 370 LYS A C     1 
ATOM   5719  O  O     A LYS A 1 370 ? -8.040  -24.505 51.120  0.20 33.55  ? 370 LYS A O     1 
ATOM   5720  O  O     B LYS A 1 370 ? -8.089  -24.481 50.853  0.80 33.10  ? 370 LYS A O     1 
ATOM   5721  C  CB    A LYS A 1 370 ? -10.223 -25.669 49.204  0.20 36.92  ? 370 LYS A CB    1 
ATOM   5722  C  CB    B LYS A 1 370 ? -10.254 -25.638 48.935  0.80 36.77  ? 370 LYS A CB    1 
ATOM   5723  C  CG    A LYS A 1 370 ? -10.745 -26.356 47.957  0.20 43.13  ? 370 LYS A CG    1 
ATOM   5724  C  CG    B LYS A 1 370 ? -10.875 -26.231 47.700  0.80 43.94  ? 370 LYS A CG    1 
ATOM   5725  C  CD    A LYS A 1 370 ? -11.874 -27.314 48.301  0.20 48.02  ? 370 LYS A CD    1 
ATOM   5726  C  CD    B LYS A 1 370 ? -12.187 -26.905 48.055  0.80 49.85  ? 370 LYS A CD    1 
ATOM   5727  C  CE    A LYS A 1 370 ? -12.438 -27.981 47.057  0.20 52.32  ? 370 LYS A CE    1 
ATOM   5728  C  CE    B LYS A 1 370 ? -12.828 -27.566 46.842  0.80 53.82  ? 370 LYS A CE    1 
ATOM   5729  N  NZ    A LYS A 1 370 ? -11.400 -28.755 46.322  0.20 55.55  ? 370 LYS A NZ    1 
ATOM   5730  N  NZ    B LYS A 1 370 ? -12.163 -28.851 46.490  0.80 55.85  ? 370 LYS A NZ    1 
ATOM   5731  N  N     A VAL A 1 371 ? -9.192  -22.721 50.365  0.20 31.61  ? 371 VAL A N     1 
ATOM   5732  N  N     B VAL A 1 371 ? -9.225  -22.699 50.085  0.80 29.62  ? 371 VAL A N     1 
ATOM   5733  C  CA    A VAL A 1 371 ? -8.983  -21.920 51.563  0.20 34.61  ? 371 VAL A CA    1 
ATOM   5734  C  CA    B VAL A 1 371 ? -9.032  -21.940 51.316  0.80 34.92  ? 371 VAL A CA    1 
ATOM   5735  C  C     A VAL A 1 371 ? -10.321 -21.346 52.012  0.20 32.63  ? 371 VAL A C     1 
ATOM   5736  C  C     B VAL A 1 371 ? -10.386 -21.455 51.829  0.80 32.12  ? 371 VAL A C     1 
ATOM   5737  O  O     A VAL A 1 371 ? -11.263 -21.210 51.228  0.20 31.12  ? 371 VAL A O     1 
ATOM   5738  O  O     B VAL A 1 371 ? -11.328 -21.246 51.060  0.80 30.87  ? 371 VAL A O     1 
ATOM   5739  C  CB    A VAL A 1 371 ? -7.953  -20.789 51.344  0.20 32.50  ? 371 VAL A CB    1 
ATOM   5740  C  CB    B VAL A 1 371 ? -8.050  -20.758 51.121  0.80 32.70  ? 371 VAL A CB    1 
ATOM   5741  C  CG1   A VAL A 1 371 ? -6.562  -21.370 51.098  0.20 32.89  ? 371 VAL A CG1   1 
ATOM   5742  C  CG1   B VAL A 1 371 ? -6.654  -21.267 50.688  0.80 32.94  ? 371 VAL A CG1   1 
ATOM   5743  C  CG2   A VAL A 1 371 ? -8.377  -19.900 50.186  0.20 30.43  ? 371 VAL A CG2   1 
ATOM   5744  C  CG2   B VAL A 1 371 ? -8.598  -19.769 50.111  0.80 30.23  ? 371 VAL A CG2   1 
ATOM   5745  N  N     A GLN A 1 372 ? -10.396 -21.014 53.301  0.20 34.77  ? 372 GLN A N     1 
ATOM   5746  N  N     B GLN A 1 372 ? -10.487 -21.295 53.151  0.80 35.30  ? 372 GLN A N     1 
ATOM   5747  C  CA    A GLN A 1 372 ? -11.621 -20.470 53.872  0.20 33.64  ? 372 GLN A CA    1 
ATOM   5748  C  CA    B GLN A 1 372 ? -11.726 -20.790 53.728  0.80 34.13  ? 372 GLN A CA    1 
ATOM   5749  C  C     A GLN A 1 372 ? -11.681 -18.950 53.833  0.20 29.36  ? 372 GLN A C     1 
ATOM   5750  C  C     B GLN A 1 372 ? -11.843 -19.278 53.634  0.80 28.14  ? 372 GLN A C     1 
ATOM   5751  O  O     A GLN A 1 372 ? -12.773 -18.387 53.967  0.20 29.17  ? 372 GLN A O     1 
ATOM   5752  O  O     B GLN A 1 372 ? -12.961 -18.754 53.666  0.80 29.56  ? 372 GLN A O     1 
ATOM   5753  C  CB    A GLN A 1 372 ? -11.789 -20.945 55.320  0.20 39.05  ? 372 GLN A CB    1 
ATOM   5754  C  CB    B GLN A 1 372 ? -11.855 -21.233 55.188  0.80 40.53  ? 372 GLN A CB    1 
ATOM   5755  C  CG    A GLN A 1 372 ? -12.106 -22.427 55.452  0.20 42.48  ? 372 GLN A CG    1 
ATOM   5756  C  CG    B GLN A 1 372 ? -12.160 -22.714 55.332  0.80 42.29  ? 372 GLN A CG    1 
ATOM   5757  C  CD    A GLN A 1 372 ? -13.480 -22.782 54.920  0.20 45.63  ? 372 GLN A CD    1 
ATOM   5758  C  CD    B GLN A 1 372 ? -13.317 -23.154 54.454  0.80 47.05  ? 372 GLN A CD    1 
ATOM   5759  O  OE1   A GLN A 1 372 ? -13.611 -23.549 53.966  0.20 48.42  ? 372 GLN A OE1   1 
ATOM   5760  O  OE1   B GLN A 1 372 ? -13.166 -24.030 53.598  0.80 50.87  ? 372 GLN A OE1   1 
ATOM   5761  N  NE2   A GLN A 1 372 ? -14.516 -22.231 55.543  0.20 47.89  ? 372 GLN A NE2   1 
ATOM   5762  N  NE2   B GLN A 1 372 ? -14.482 -22.549 54.660  0.80 52.01  ? 372 GLN A NE2   1 
ATOM   5763  N  N     A ARG A 1 373 ? -10.547 -18.272 53.663  0.20 27.12  ? 373 ARG A N     1 
ATOM   5764  N  N     B ARG A 1 373 ? -10.726 -18.565 53.528  0.80 26.57  ? 373 ARG A N     1 
ATOM   5765  C  CA    A ARG A 1 373 ? -10.538 -16.817 53.605  0.20 26.30  ? 373 ARG A CA    1 
ATOM   5766  C  CA    B ARG A 1 373 ? -10.775 -17.129 53.338  0.80 23.81  ? 373 ARG A CA    1 
ATOM   5767  C  C     A ARG A 1 373 ? -9.331  -16.352 52.804  0.20 24.97  ? 373 ARG A C     1 
ATOM   5768  C  C     B ARG A 1 373 ? -9.539  -16.685 52.568  0.80 24.86  ? 373 ARG A C     1 
ATOM   5769  O  O     A ARG A 1 373 ? -8.217  -16.844 53.008  0.20 24.77  ? 373 ARG A O     1 
ATOM   5770  O  O     B ARG A 1 373 ? -8.475  -17.315 52.628  0.80 24.09  ? 373 ARG A O     1 
ATOM   5771  C  CB    A ARG A 1 373 ? -10.524 -16.201 55.010  0.20 27.05  ? 373 ARG A CB    1 
ATOM   5772  C  CB    B ARG A 1 373 ? -10.877 -16.366 54.663  0.80 27.02  ? 373 ARG A CB    1 
ATOM   5773  C  CG    A ARG A 1 373 ? -9.432  -16.723 55.927  0.20 31.78  ? 373 ARG A CG    1 
ATOM   5774  C  CG    B ARG A 1 373 ? -9.686  -16.530 55.569  0.80 29.82  ? 373 ARG A CG    1 
ATOM   5775  C  CD    A ARG A 1 373 ? -9.519  -16.077 57.306  0.20 33.58  ? 373 ARG A CD    1 
ATOM   5776  C  CD    B ARG A 1 373 ? -10.031 -16.149 57.009  0.80 34.98  ? 373 ARG A CD    1 
ATOM   5777  N  NE    A ARG A 1 373 ? -10.733 -16.463 58.015  0.20 34.20  ? 373 ARG A NE    1 
ATOM   5778  N  NE    B ARG A 1 373 ? -10.959 -17.097 57.609  0.80 37.22  ? 373 ARG A NE    1 
ATOM   5779  C  CZ    A ARG A 1 373 ? -10.803 -17.457 58.891  0.20 36.62  ? 373 ARG A CZ    1 
ATOM   5780  C  CZ    B ARG A 1 373 ? -10.599 -18.200 58.254  0.80 41.15  ? 373 ARG A CZ    1 
ATOM   5781  N  NH1   A ARG A 1 373 ? -9.742  -18.187 59.194  0.20 39.65  ? 373 ARG A NH1   1 
ATOM   5782  N  NH1   B ARG A 1 373 ? -9.326  -18.541 58.385  0.80 44.36  ? 373 ARG A NH1   1 
ATOM   5783  N  NH2   A ARG A 1 373 ? -11.966 -17.723 59.479  0.20 32.98  ? 373 ARG A NH2   1 
ATOM   5784  N  NH2   B ARG A 1 373 ? -11.539 -18.978 58.784  0.80 39.90  ? 373 ARG A NH2   1 
ATOM   5785  N  N     A ALA A 1 374 ? -9.561  -15.410 51.894  0.20 25.47  ? 374 ALA A N     1 
ATOM   5786  N  N     B ALA A 1 374 ? -9.701  -15.582 51.852  0.80 25.22  ? 374 ALA A N     1 
ATOM   5787  C  CA    A ALA A 1 374 ? -8.526  -14.878 51.021  0.20 24.95  ? 374 ALA A CA    1 
ATOM   5788  C  CA    B ALA A 1 374 ? -8.651  -15.043 51.003  0.80 24.73  ? 374 ALA A CA    1 
ATOM   5789  C  C     A ALA A 1 374 ? -8.618  -13.358 51.005  0.20 25.75  ? 374 ALA A C     1 
ATOM   5790  C  C     B ALA A 1 374 ? -8.949  -13.568 50.812  0.80 26.80  ? 374 ALA A C     1 
ATOM   5791  O  O     A ALA A 1 374 ? -9.616  -12.769 51.430  0.20 24.92  ? 374 ALA A O     1 
ATOM   5792  O  O     B ALA A 1 374 ? -10.065 -13.101 51.079  0.80 26.63  ? 374 ALA A O     1 
ATOM   5793  C  CB    A ALA A 1 374 ? -8.649  -15.443 49.599  0.20 26.32  ? 374 ALA A CB    1 
ATOM   5794  C  CB    B ALA A 1 374 ? -8.575  -15.779 49.660  0.80 25.62  ? 374 ALA A CB    1 
ATOM   5795  N  N     A VAL A 1 375 ? -7.563  -12.718 50.506  0.20 24.17  ? 375 VAL A N     1 
ATOM   5796  N  N     B VAL A 1 375 ? -7.939  -12.836 50.356  0.80 23.59  ? 375 VAL A N     1 
ATOM   5797  C  CA    A VAL A 1 375 ? -7.483  -11.261 50.512  0.20 24.40  ? 375 VAL A CA    1 
ATOM   5798  C  CA    B VAL A 1 375 ? -8.046  -11.385 50.254  0.80 24.13  ? 375 VAL A CA    1 
ATOM   5799  C  C     A VAL A 1 375 ? -6.708  -10.806 49.282  0.20 25.73  ? 375 VAL A C     1 
ATOM   5800  C  C     B VAL A 1 375 ? -7.222  -10.936 49.063  0.80 21.62  ? 375 VAL A C     1 
ATOM   5801  O  O     A VAL A 1 375 ? -5.715  -11.429 48.889  0.20 26.13  ? 375 VAL A O     1 
ATOM   5802  O  O     B VAL A 1 375 ? -6.164  -11.506 48.768  0.80 28.97  ? 375 VAL A O     1 
ATOM   5803  C  CB    A VAL A 1 375 ? -6.843  -10.743 51.821  0.20 27.46  ? 375 VAL A CB    1 
ATOM   5804  C  CB    B VAL A 1 375 ? -7.602  -10.682 51.562  0.80 26.53  ? 375 VAL A CB    1 
ATOM   5805  C  CG1   A VAL A 1 375 ? -5.430  -11.275 51.975  0.20 27.01  ? 375 VAL A CG1   1 
ATOM   5806  C  CG1   B VAL A 1 375 ? -6.202  -11.128 51.992  0.80 30.76  ? 375 VAL A CG1   1 
ATOM   5807  C  CG2   A VAL A 1 375 ? -6.857  -9.229  51.866  0.20 23.22  ? 375 VAL A CG2   1 
ATOM   5808  C  CG2   B VAL A 1 375 ? -7.662  -9.161  51.426  0.80 27.20  ? 375 VAL A CG2   1 
ATOM   5809  N  N     A CYS A 1 376 ? -7.169  -9.710  48.668  0.20 25.21  ? 376 CYS A N     1 
ATOM   5810  N  N     B CYS A 1 376 ? -7.728  -9.921  48.366  0.80 23.76  ? 376 CYS A N     1 
ATOM   5811  C  CA    A CYS A 1 376 ? -6.546  -9.166  47.454  0.20 23.06  ? 376 CYS A CA    1 
ATOM   5812  C  CA    B CYS A 1 376 ? -6.990  -9.230  47.315  0.80 23.52  ? 376 CYS A CA    1 
ATOM   5813  C  C     A CYS A 1 376 ? -6.555  -7.641  47.554  0.20 24.89  ? 376 CYS A C     1 
ATOM   5814  C  C     B CYS A 1 376 ? -6.899  -7.767  47.708  0.80 25.32  ? 376 CYS A C     1 
ATOM   5815  O  O     A CYS A 1 376 ? -7.527  -6.990  47.162  0.20 28.67  ? 376 CYS A O     1 
ATOM   5816  O  O     B CYS A 1 376 ? -7.928  -7.125  47.950  0.80 32.67  ? 376 CYS A O     1 
ATOM   5817  C  CB    A CYS A 1 376 ? -7.260  -9.648  46.199  0.20 23.94  ? 376 CYS A CB    1 
ATOM   5818  C  CB    B CYS A 1 376 ? -7.685  -9.370  45.963  0.80 21.85  ? 376 CYS A CB    1 
ATOM   5819  S  SG    A CYS A 1 376 ? -6.443  -9.172  44.651  0.20 26.37  ? 376 CYS A SG    1 
ATOM   5820  S  SG    B CYS A 1 376 ? -6.883  -8.422  44.662  0.80 31.41  ? 376 CYS A SG    1 
ATOM   5821  N  N     A MET A 1 377 ? -5.458  -7.081  48.057  0.20 26.38  ? 377 MET A N     1 
ATOM   5822  N  N     B MET A 1 377 ? -5.682  -7.251  47.803  0.80 24.64  ? 377 MET A N     1 
ATOM   5823  C  CA    A MET A 1 377 ? -5.339  -5.640  48.231  0.20 27.39  ? 377 MET A CA    1 
ATOM   5824  C  CA    B MET A 1 377 ? -5.467  -5.841  48.085  0.80 26.44  ? 377 MET A CA    1 
ATOM   5825  C  C     A MET A 1 377 ? -5.006  -4.964  46.907  0.20 27.84  ? 377 MET A C     1 
ATOM   5826  C  C     B MET A 1 377 ? -5.106  -5.107  46.803  0.80 28.17  ? 377 MET A C     1 
ATOM   5827  O  O     A MET A 1 377 ? -4.074  -5.373  46.205  0.20 26.61  ? 377 MET A O     1 
ATOM   5828  O  O     B MET A 1 377 ? -4.170  -5.501  46.086  0.80 25.95  ? 377 MET A O     1 
ATOM   5829  C  CB    A MET A 1 377 ? -4.265  -5.319  49.273  0.20 29.62  ? 377 MET A CB    1 
ATOM   5830  C  CB    B MET A 1 377 ? -4.369  -5.629  49.134  0.80 29.73  ? 377 MET A CB    1 
ATOM   5831  C  CG    A MET A 1 377 ? -3.961  -3.833  49.424  0.20 30.43  ? 377 MET A CG    1 
ATOM   5832  C  CG    B MET A 1 377 ? -4.315  -4.183  49.649  0.80 30.54  ? 377 MET A CG    1 
ATOM   5833  S  SD    A MET A 1 377 ? -2.763  -3.481  50.732  0.20 34.93  ? 377 MET A SD    1 
ATOM   5834  S  SD    B MET A 1 377 ? -3.162  -3.897  51.010  0.80 35.19  ? 377 MET A SD    1 
ATOM   5835  C  CE    A MET A 1 377 ? -3.694  -3.951  52.187  0.20 36.75  ? 377 MET A CE    1 
ATOM   5836  C  CE    B MET A 1 377 ? -1.576  -4.002  50.172  0.80 32.56  ? 377 MET A CE    1 
ATOM   5837  N  N     A LEU A 1 378 ? -5.770  -3.928  46.567  0.20 25.80  ? 378 LEU A N     1 
ATOM   5838  N  N     B LEU A 1 378 ? -5.858  -4.052  46.510  0.80 25.18  ? 378 LEU A N     1 
ATOM   5839  C  CA    A LEU A 1 378 ? -5.523  -3.102  45.386  0.20 26.00  ? 378 LEU A CA    1 
ATOM   5840  C  CA    B LEU A 1 378 ? -5.522  -3.126  45.440  0.80 25.92  ? 378 LEU A CA    1 
ATOM   5841  C  C     A LEU A 1 378 ? -5.039  -1.743  45.879  0.20 27.44  ? 378 LEU A C     1 
ATOM   5842  C  C     B LEU A 1 378 ? -5.061  -1.827  46.074  0.80 27.91  ? 378 LEU A C     1 
ATOM   5843  O  O     A LEU A 1 378 ? -5.844  -0.898  46.283  0.20 30.26  ? 378 LEU A O     1 
ATOM   5844  O  O     B LEU A 1 378 ? -5.704  -1.320  47.003  0.80 28.24  ? 378 LEU A O     1 
ATOM   5845  C  CB    A LEU A 1 378 ? -6.778  -2.974  44.531  0.20 24.86  ? 378 LEU A CB    1 
ATOM   5846  C  CB    B LEU A 1 378 ? -6.710  -2.887  44.518  0.80 24.75  ? 378 LEU A CB    1 
ATOM   5847  C  CG    A LEU A 1 378 ? -7.411  -4.276  44.043  0.20 28.14  ? 378 LEU A CG    1 
ATOM   5848  C  CG    B LEU A 1 378 ? -7.393  -4.154  44.019  0.80 28.23  ? 378 LEU A CG    1 
ATOM   5849  C  CD1   A LEU A 1 378 ? -8.708  -3.989  43.307  0.20 30.50  ? 378 LEU A CD1   1 
ATOM   5850  C  CD1   B LEU A 1 378 ? -8.648  -3.801  43.257  0.80 31.04  ? 378 LEU A CD1   1 
ATOM   5851  C  CD2   A LEU A 1 378 ? -6.446  -5.045  43.155  0.20 25.17  ? 378 LEU A CD2   1 
ATOM   5852  C  CD2   B LEU A 1 378 ? -6.452  -4.987  43.156  0.80 25.07  ? 378 LEU A CD2   1 
ATOM   5853  N  N     A SER A 1 379 ? -3.724  -1.537  45.850  0.20 25.89  ? 379 SER A N     1 
ATOM   5854  N  N     B SER A 1 379 ? -3.922  -1.325  45.615  0.80 24.63  ? 379 SER A N     1 
ATOM   5855  C  CA    A SER A 1 379 ? -3.100  -0.347  46.413  0.20 27.81  ? 379 SER A CA    1 
ATOM   5856  C  CA    B SER A 1 379 ? -3.357  -0.107  46.158  0.80 27.24  ? 379 SER A CA    1 
ATOM   5857  C  C     A SER A 1 379 ? -2.381  0.428   45.320  0.20 28.14  ? 379 SER A C     1 
ATOM   5858  C  C     B SER A 1 379 ? -2.794  0.710   45.017  0.80 28.62  ? 379 SER A C     1 
ATOM   5859  O  O     A SER A 1 379 ? -1.597  -0.146  44.557  0.20 26.94  ? 379 SER A O     1 
ATOM   5860  O  O     B SER A 1 379 ? -2.472  0.182   43.954  0.80 28.06  ? 379 SER A O     1 
ATOM   5861  C  CB    A SER A 1 379 ? -2.123  -0.719  47.533  0.20 29.10  ? 379 SER A CB    1 
ATOM   5862  C  CB    B SER A 1 379 ? -2.278  -0.397  47.216  0.80 27.57  ? 379 SER A CB    1 
ATOM   5863  O  OG    A SER A 1 379 ? -1.075  -1.546  47.052  0.20 29.84  ? 379 SER A OG    1 
ATOM   5864  O  OG    B SER A 1 379 ? -1.123  -1.014  46.661  0.80 32.23  ? 379 SER A OG    1 
ATOM   5865  N  N     A ASN A 1 380 ? -2.646  1.730   45.251  0.20 28.59  ? 380 ASN A N     1 
ATOM   5866  N  N     B ASN A 1 380 ? -2.709  2.015   45.231  0.80 28.85  ? 380 ASN A N     1 
ATOM   5867  C  CA    A ASN A 1 380 ? -1.989  2.619   44.294  0.20 26.95  ? 380 ASN A CA    1 
ATOM   5868  C  CA    B ASN A 1 380 ? -1.956  2.888   44.338  0.80 25.80  ? 380 ASN A CA    1 
ATOM   5869  C  C     A ASN A 1 380 ? -0.834  3.299   45.019  0.20 30.00  ? 380 ASN A C     1 
ATOM   5870  C  C     B ASN A 1 380 ? -0.792  3.434   45.149  0.80 30.34  ? 380 ASN A C     1 
ATOM   5871  O  O     A ASN A 1 380 ? -1.027  4.294   45.722  0.20 31.13  ? 380 ASN A O     1 
ATOM   5872  O  O     B ASN A 1 380 ? -0.984  4.251   46.054  0.80 31.90  ? 380 ASN A O     1 
ATOM   5873  C  CB    A ASN A 1 380 ? -2.973  3.636   43.725  0.20 25.58  ? 380 ASN A CB    1 
ATOM   5874  C  CB    B ASN A 1 380 ? -2.815  4.003   43.750  0.80 24.31  ? 380 ASN A CB    1 
ATOM   5875  C  CG    A ASN A 1 380 ? -2.426  4.358   42.511  0.20 27.61  ? 380 ASN A CG    1 
ATOM   5876  C  CG    B ASN A 1 380 ? -2.249  4.518   42.451  0.80 27.27  ? 380 ASN A CG    1 
ATOM   5877  O  OD1   A ASN A 1 380 ? -1.233  4.279   42.212  0.20 26.46  ? 380 ASN A OD1   1 
ATOM   5878  O  OD1   B ASN A 1 380 ? -1.033  4.482   42.245  0.80 25.93  ? 380 ASN A OD1   1 
ATOM   5879  N  ND2   A ASN A 1 380 ? -3.295  5.068   41.803  0.20 28.82  ? 380 ASN A ND2   1 
ATOM   5880  N  ND2   B ASN A 1 380 ? -3.117  4.959   41.551  0.80 28.05  ? 380 ASN A ND2   1 
ATOM   5881  N  N     A THR A 1 381 ? 0.367   2.754   44.854  0.20 24.67  ? 381 THR A N     1 
ATOM   5882  N  N     B THR A 1 381 ? 0.401   2.928   44.862  0.80 23.64  ? 381 THR A N     1 
ATOM   5883  C  CA    A THR A 1 381 ? 1.564   3.278   45.491  0.20 30.73  ? 381 THR A CA    1 
ATOM   5884  C  CA    B THR A 1 381 ? 1.612   3.291   45.576  0.80 30.88  ? 381 THR A CA    1 
ATOM   5885  C  C     A THR A 1 381 ? 2.496   3.886   44.452  0.20 30.29  ? 381 THR A C     1 
ATOM   5886  C  C     B THR A 1 381 ? 2.643   3.782   44.578  0.80 30.14  ? 381 THR A C     1 
ATOM   5887  O  O     A THR A 1 381 ? 2.438   3.563   43.263  0.20 31.66  ? 381 THR A O     1 
ATOM   5888  O  O     B THR A 1 381 ? 2.801   3.194   43.505  0.80 29.92  ? 381 THR A O     1 
ATOM   5889  C  CB    A THR A 1 381 ? 2.303   2.183   46.269  0.20 31.66  ? 381 THR A CB    1 
ATOM   5890  C  CB    B THR A 1 381 ? 2.185   2.111   46.358  0.80 31.81  ? 381 THR A CB    1 
ATOM   5891  O  OG1   A THR A 1 381 ? 3.582   2.675   46.689  0.20 31.25  ? 381 THR A OG1   1 
ATOM   5892  O  OG1   B THR A 1 381 ? 3.570   2.354   46.634  0.80 29.74  ? 381 THR A OG1   1 
ATOM   5893  C  CG2   A THR A 1 381 ? 2.498   0.946   45.405  0.20 31.16  ? 381 THR A CG2   1 
ATOM   5894  C  CG2   B THR A 1 381 ? 2.039   0.814   45.573  0.80 31.43  ? 381 THR A CG2   1 
ATOM   5895  N  N     A THR A 1 382 ? 3.366   4.780   44.923  0.20 31.34  ? 382 THR A N     1 
ATOM   5896  N  N     B THR A 1 382 ? 3.361   4.846   44.942  0.80 31.32  ? 382 THR A N     1 
ATOM   5897  C  CA    A THR A 1 382 ? 4.389   5.361   44.064  0.20 32.88  ? 382 THR A CA    1 
ATOM   5898  C  CA    B THR A 1 382 ? 4.429   5.334   44.072  0.80 32.86  ? 382 THR A CA    1 
ATOM   5899  C  C     A THR A 1 382 ? 5.543   4.405   43.789  0.20 31.61  ? 382 THR A C     1 
ATOM   5900  C  C     B THR A 1 382 ? 5.519   4.292   43.822  0.80 31.74  ? 382 THR A C     1 
ATOM   5901  O  O     A THR A 1 382 ? 6.343   4.672   42.886  0.20 28.79  ? 382 THR A O     1 
ATOM   5902  O  O     B THR A 1 382 ? 6.307   4.462   42.885  0.80 27.66  ? 382 THR A O     1 
ATOM   5903  C  CB    A THR A 1 382 ? 4.933   6.652   44.684  0.20 35.34  ? 382 THR A CB    1 
ATOM   5904  C  CB    B THR A 1 382 ? 5.039   6.609   44.656  0.80 35.47  ? 382 THR A CB    1 
ATOM   5905  O  OG1   A THR A 1 382 ? 5.487   6.369   45.975  0.20 36.79  ? 382 THR A OG1   1 
ATOM   5906  O  OG1   B THR A 1 382 ? 5.509   6.358   45.983  0.80 36.80  ? 382 THR A OG1   1 
ATOM   5907  C  CG2   A THR A 1 382 ? 3.826   7.682   44.830  0.20 35.94  ? 382 THR A CG2   1 
ATOM   5908  C  CG2   B THR A 1 382 ? 4.008   7.705   44.710  0.80 35.49  ? 382 THR A CG2   1 
ATOM   5909  N  N     A ALA A 1 383 ? 5.637   3.296   44.527  0.20 29.78  ? 383 ALA A N     1 
ATOM   5910  N  N     B ALA A 1 383 ? 5.546   3.194   44.585  0.80 29.23  ? 383 ALA A N     1 
ATOM   5911  C  CA    A ALA A 1 383 ? 6.736   2.354   44.354  0.20 30.51  ? 383 ALA A CA    1 
ATOM   5912  C  CA    B ALA A 1 383 ? 6.559   2.158   44.400  0.80 29.82  ? 383 ALA A CA    1 
ATOM   5913  C  C     A ALA A 1 383 ? 6.632   1.540   43.071  0.20 31.02  ? 383 ALA A C     1 
ATOM   5914  C  C     B ALA A 1 383 ? 6.468   1.470   43.045  0.80 30.71  ? 383 ALA A C     1 
ATOM   5915  O  O     A ALA A 1 383 ? 7.614   0.891   42.692  0.20 29.64  ? 383 ALA A O     1 
ATOM   5916  O  O     B ALA A 1 383 ? 7.469   0.912   42.574  0.80 29.19  ? 383 ALA A O     1 
ATOM   5917  C  CB    A ALA A 1 383 ? 6.809   1.407   45.551  0.20 34.46  ? 383 ALA A CB    1 
ATOM   5918  C  CB    B ALA A 1 383 ? 6.446   1.106   45.501  0.80 34.72  ? 383 ALA A CB    1 
ATOM   5919  N  N     A ILE A 1 384 ? 5.481   1.556   42.395  0.20 31.98  ? 384 ILE A N     1 
ATOM   5920  N  N     B ILE A 1 384 ? 5.302   1.495   42.399  0.80 32.14  ? 384 ILE A N     1 
ATOM   5921  C  CA    A ILE A 1 384 ? 5.363   0.832   41.137  0.20 30.39  ? 384 ILE A CA    1 
ATOM   5922  C  CA    B ILE A 1 384 ? 5.195   0.920   41.064  0.80 30.19  ? 384 ILE A CA    1 
ATOM   5923  C  C     A ILE A 1 384 ? 6.219   1.466   40.045  0.20 30.35  ? 384 ILE A C     1 
ATOM   5924  C  C     B ILE A 1 384 ? 6.026   1.669   40.030  0.80 29.90  ? 384 ILE A C     1 
ATOM   5925  O  O     A ILE A 1 384 ? 6.539   0.805   39.050  0.20 28.02  ? 384 ILE A O     1 
ATOM   5926  O  O     B ILE A 1 384 ? 6.261   1.140   38.934  0.80 29.24  ? 384 ILE A O     1 
ATOM   5927  C  CB    A ILE A 1 384 ? 3.888   0.742   40.705  0.20 29.09  ? 384 ILE A CB    1 
ATOM   5928  C  CB    B ILE A 1 384 ? 3.715   0.853   40.645  0.80 28.85  ? 384 ILE A CB    1 
ATOM   5929  C  CG1   A ILE A 1 384 ? 3.701   -0.373  39.673  0.20 30.64  ? 384 ILE A CG1   1 
ATOM   5930  C  CG1   B ILE A 1 384 ? 3.507   -0.270  39.627  0.80 30.57  ? 384 ILE A CG1   1 
ATOM   5931  C  CG2   A ILE A 1 384 ? 3.402   2.080   40.166  0.20 33.83  ? 384 ILE A CG2   1 
ATOM   5932  C  CG2   B ILE A 1 384 ? 3.243   2.207   40.129  0.80 34.72  ? 384 ILE A CG2   1 
ATOM   5933  C  CD1   A ILE A 1 384 ? 2.286   -0.528  39.186  0.20 29.50  ? 384 ILE A CD1   1 
ATOM   5934  C  CD1   B ILE A 1 384 ? 2.137   -0.872  39.657  0.80 31.84  ? 384 ILE A CD1   1 
ATOM   5935  N  N     A ALA A 1 385 ? 6.624   2.729   40.215  0.20 30.03  ? 385 ALA A N     1 
ATOM   5936  N  N     B ALA A 1 385 ? 6.515   2.870   40.355  0.80 28.99  ? 385 ALA A N     1 
ATOM   5937  C  CA    A ALA A 1 385 ? 7.533   3.352   39.258  0.20 27.87  ? 385 ALA A CA    1 
ATOM   5938  C  CA    B ALA A 1 385 ? 7.463   3.539   39.461  0.80 28.35  ? 385 ALA A CA    1 
ATOM   5939  C  C     A ALA A 1 385 ? 8.871   2.630   39.179  0.20 30.48  ? 385 ALA A C     1 
ATOM   5940  C  C     B ALA A 1 385 ? 8.680   2.676   39.172  0.80 29.96  ? 385 ALA A C     1 
ATOM   5941  O  O     A ALA A 1 385 ? 9.633   2.861   38.231  0.20 31.94  ? 385 ALA A O     1 
ATOM   5942  O  O     B ALA A 1 385 ? 9.325   2.843   38.122  0.80 34.15  ? 385 ALA A O     1 
ATOM   5943  C  CB    A ALA A 1 385 ? 7.757   4.820   39.619  0.20 30.83  ? 385 ALA A CB    1 
ATOM   5944  C  CB    B ALA A 1 385 ? 7.908   4.866   40.068  0.80 30.80  ? 385 ALA A CB    1 
ATOM   5945  N  N     A GLU A 1 386 ? 9.185   1.777   40.159  0.20 31.82  ? 386 GLU A N     1 
ATOM   5946  N  N     B GLU A 1 386 ? 9.035   1.777   40.096  0.80 31.95  ? 386 GLU A N     1 
ATOM   5947  C  CA    A GLU A 1 386 ? 10.380  0.947   40.060  0.20 31.45  ? 386 GLU A CA    1 
ATOM   5948  C  CA    B GLU A 1 386 ? 10.202  0.921   39.890  0.80 31.18  ? 386 GLU A CA    1 
ATOM   5949  C  C     A GLU A 1 386 ? 10.270  -0.050  38.915  0.20 29.76  ? 386 GLU A C     1 
ATOM   5950  C  C     B GLU A 1 386 ? 10.029  0.014   38.685  0.80 29.41  ? 386 GLU A C     1 
ATOM   5951  O  O     A GLU A 1 386 ? 11.278  -0.371  38.272  0.20 29.26  ? 386 GLU A O     1 
ATOM   5952  O  O     B GLU A 1 386 ? 11.013  -0.294  37.992  0.80 29.83  ? 386 GLU A O     1 
ATOM   5953  C  CB    A GLU A 1 386 ? 10.621  0.208   41.376  0.20 30.45  ? 386 GLU A CB    1 
ATOM   5954  C  CB    B GLU A 1 386 ? 10.461  0.067   41.132  0.80 30.57  ? 386 GLU A CB    1 
ATOM   5955  C  CG    A GLU A 1 386 ? 10.906  1.115   42.556  0.20 33.88  ? 386 GLU A CG    1 
ATOM   5956  C  CG    B GLU A 1 386 ? 11.215  0.759   42.222  0.80 29.07  ? 386 GLU A CG    1 
ATOM   5957  C  CD    A GLU A 1 386 ? 11.042  0.349   43.863  0.20 41.14  ? 386 GLU A CD    1 
ATOM   5958  C  CD    B GLU A 1 386 ? 11.316  -0.101  43.478  0.80 48.84  ? 386 GLU A CD    1 
ATOM   5959  O  OE1   A GLU A 1 386 ? 10.338  -0.673  44.039  0.20 27.17  ? 386 GLU A OE1   1 
ATOM   5960  O  OE1   B GLU A 1 386 ? 11.492  -1.338  43.351  0.80 48.17  ? 386 GLU A OE1   1 
ATOM   5961  O  OE2   A GLU A 1 386 ? 11.862  0.768   44.708  0.20 40.49  ? 386 GLU A OE2   1 
ATOM   5962  O  OE2   B GLU A 1 386 ? 11.202  0.463   44.588  0.80 43.58  ? 386 GLU A OE2   1 
ATOM   5963  N  N     A ALA A 1 387 ? 9.060   -0.552  38.652  0.20 27.64  ? 387 ALA A N     1 
ATOM   5964  N  N     B ALA A 1 387 ? 8.796   -0.437  38.434  0.80 26.81  ? 387 ALA A N     1 
ATOM   5965  C  CA    A ALA A 1 387 ? 8.858   -1.464  37.532  0.20 31.38  ? 387 ALA A CA    1 
ATOM   5966  C  CA    B ALA A 1 387 ? 8.511   -1.252  37.257  0.80 31.42  ? 387 ALA A CA    1 
ATOM   5967  C  C     A ALA A 1 387 ? 8.989   -0.740  36.198  0.20 28.90  ? 387 ALA A C     1 
ATOM   5968  C  C     B ALA A 1 387 ? 8.773   -0.479  35.968  0.80 27.98  ? 387 ALA A C     1 
ATOM   5969  O  O     A ALA A 1 387 ? 9.532   -1.295  35.235  0.20 30.68  ? 387 ALA A O     1 
ATOM   5970  O  O     B ALA A 1 387 ? 9.375   -1.010  35.025  0.80 31.24  ? 387 ALA A O     1 
ATOM   5971  C  CB    A ALA A 1 387 ? 7.493   -2.139  37.648  0.20 30.05  ? 387 ALA A CB    1 
ATOM   5972  C  CB    B ALA A 1 387 ? 7.066   -1.745  37.309  0.80 30.48  ? 387 ALA A CB    1 
ATOM   5973  N  N     A TRP A 1 388 ? 8.488   0.498   36.118  0.20 27.86  ? 388 TRP A N     1 
ATOM   5974  N  N     B TRP A 1 388 ? 8.307   0.774   35.899  0.80 25.58  ? 388 TRP A N     1 
ATOM   5975  C  CA    A TRP A 1 388 ? 8.669   1.288   34.904  0.20 26.77  ? 388 TRP A CA    1 
ATOM   5976  C  CA    B TRP A 1 388 ? 8.549   1.579   34.706  0.80 24.68  ? 388 TRP A CA    1 
ATOM   5977  C  C     A TRP A 1 388 ? 10.139  1.588   34.650  0.20 29.39  ? 388 TRP A C     1 
ATOM   5978  C  C     B TRP A 1 388 ? 10.033  1.836   34.504  0.80 30.18  ? 388 TRP A C     1 
ATOM   5979  O  O     A TRP A 1 388 ? 10.569  1.652   33.491  0.20 30.74  ? 388 TRP A O     1 
ATOM   5980  O  O     B TRP A 1 388 ? 10.523  1.824   33.365  0.80 30.36  ? 388 TRP A O     1 
ATOM   5981  C  CB    A TRP A 1 388 ? 7.878   2.594   34.993  0.20 28.69  ? 388 TRP A CB    1 
ATOM   5982  C  CB    B TRP A 1 388 ? 7.798   2.906   34.788  0.80 27.56  ? 388 TRP A CB    1 
ATOM   5983  C  CG    A TRP A 1 388 ? 6.387   2.408   35.033  0.20 30.01  ? 388 TRP A CG    1 
ATOM   5984  C  CG    B TRP A 1 388 ? 6.295   2.744   34.789  0.80 30.38  ? 388 TRP A CG    1 
ATOM   5985  C  CD1   A TRP A 1 388 ? 5.550   2.701   36.072  0.20 31.70  ? 388 TRP A CD1   1 
ATOM   5986  C  CD1   B TRP A 1 388 ? 5.413   3.266   35.696  0.80 34.95  ? 388 TRP A CD1   1 
ATOM   5987  C  CD2   A TRP A 1 388 ? 5.560   1.885   33.988  0.20 30.24  ? 388 TRP A CD2   1 
ATOM   5988  C  CD2   B TRP A 1 388 ? 5.509   2.005   33.847  0.80 30.53  ? 388 TRP A CD2   1 
ATOM   5989  N  NE1   A TRP A 1 388 ? 4.254   2.395   35.736  0.20 30.18  ? 388 TRP A NE1   1 
ATOM   5990  N  NE1   B TRP A 1 388 ? 4.131   2.903   35.372  0.80 32.45  ? 388 TRP A NE1   1 
ATOM   5991  C  CE2   A TRP A 1 388 ? 4.233   1.893   34.461  0.20 26.74  ? 388 TRP A CE2   1 
ATOM   5992  C  CE2   B TRP A 1 388 ? 4.160   2.133   34.238  0.80 24.25  ? 388 TRP A CE2   1 
ATOM   5993  C  CE3   A TRP A 1 388 ? 5.813   1.411   32.697  0.20 29.61  ? 388 TRP A CE3   1 
ATOM   5994  C  CE3   B TRP A 1 388 ? 5.811   1.256   32.705  0.80 29.46  ? 388 TRP A CE3   1 
ATOM   5995  C  CZ2   A TRP A 1 388 ? 3.163   1.444   33.690  0.20 27.95  ? 388 TRP A CZ2   1 
ATOM   5996  C  CZ2   B TRP A 1 388 ? 3.120   1.533   33.532  0.80 27.66  ? 388 TRP A CZ2   1 
ATOM   5997  C  CZ3   A TRP A 1 388 ? 4.749   0.968   31.931  0.20 33.27  ? 388 TRP A CZ3   1 
ATOM   5998  C  CZ3   B TRP A 1 388 ? 4.774   0.663   32.001  0.80 35.20  ? 388 TRP A CZ3   1 
ATOM   5999  C  CH2   A TRP A 1 388 ? 3.440   0.987   32.430  0.20 29.72  ? 388 TRP A CH2   1 
ATOM   6000  C  CH2   B TRP A 1 388 ? 3.445   0.806   32.418  0.80 29.64  ? 388 TRP A CH2   1 
ATOM   6001  N  N     A ALA A 1 389 ? 10.923  1.773   35.715  0.20 28.20  ? 389 ALA A N     1 
ATOM   6002  N  N     B ALA A 1 389 ? 10.759  2.080   35.598  0.80 25.15  ? 389 ALA A N     1 
ATOM   6003  C  CA    A ALA A 1 389 ? 12.337  2.094   35.552  0.20 28.83  ? 389 ALA A CA    1 
ATOM   6004  C  CA    B ALA A 1 389 ? 12.177  2.411   35.496  0.80 28.14  ? 389 ALA A CA    1 
ATOM   6005  C  C     A ALA A 1 389 ? 13.126  0.899   35.030  0.20 31.24  ? 389 ALA A C     1 
ATOM   6006  C  C     B ALA A 1 389 ? 12.999  1.235   34.978  0.80 31.48  ? 389 ALA A C     1 
ATOM   6007  O  O     A ALA A 1 389 ? 14.081  1.068   34.262  0.20 28.84  ? 389 ALA A O     1 
ATOM   6008  O  O     B ALA A 1 389 ? 13.926  1.429   34.176  0.80 28.29  ? 389 ALA A O     1 
ATOM   6009  C  CB    A ALA A 1 389 ? 12.919  2.586   36.877  0.20 31.19  ? 389 ALA A CB    1 
ATOM   6010  C  CB    B ALA A 1 389 ? 12.699  2.883   36.853  0.80 31.09  ? 389 ALA A CB    1 
ATOM   6011  N  N     A ARG A 1 390 ? 12.758  -0.316  35.445  0.20 30.59  ? 390 ARG A N     1 
ATOM   6012  N  N     B ARG A 1 390 ? 12.709  0.014   35.442  0.80 29.94  ? 390 ARG A N     1 
ATOM   6013  C  CA    A ARG A 1 390 ? 13.446  -1.495  34.930  0.20 32.35  ? 390 ARG A CA    1 
ATOM   6014  C  CA    B ARG A 1 390 ? 13.433  -1.147  34.927  0.80 32.66  ? 390 ARG A CA    1 
ATOM   6015  C  C     A ARG A 1 390 ? 13.143  -1.712  33.455  0.20 33.56  ? 390 ARG A C     1 
ATOM   6016  C  C     B ARG A 1 390 ? 13.181  -1.317  33.440  0.80 35.06  ? 390 ARG A C     1 
ATOM   6017  O  O     A ARG A 1 390 ? 13.992  -2.222  32.715  0.20 32.93  ? 390 ARG A O     1 
ATOM   6018  O  O     B ARG A 1 390 ? 14.089  -1.670  32.679  0.80 33.27  ? 390 ARG A O     1 
ATOM   6019  C  CB    A ARG A 1 390 ? 13.062  -2.736  35.737  0.20 33.35  ? 390 ARG A CB    1 
ATOM   6020  C  CB    B ARG A 1 390 ? 13.028  -2.422  35.670  0.80 33.23  ? 390 ARG A CB    1 
ATOM   6021  C  CG    A ARG A 1 390 ? 13.399  -2.647  37.219  0.20 37.78  ? 390 ARG A CG    1 
ATOM   6022  C  CG    B ARG A 1 390 ? 13.326  -2.420  37.167  0.80 38.63  ? 390 ARG A CG    1 
ATOM   6023  C  CD    A ARG A 1 390 ? 13.278  -4.002  37.903  0.20 39.51  ? 390 ARG A CD    1 
ATOM   6024  C  CD    B ARG A 1 390 ? 13.195  -3.820  37.762  0.80 39.86  ? 390 ARG A CD    1 
ATOM   6025  N  NE    A ARG A 1 390 ? 11.931  -4.558  37.820  0.20 41.77  ? 390 ARG A NE    1 
ATOM   6026  N  NE    B ARG A 1 390 ? 11.908  -4.446  37.466  0.80 43.90  ? 390 ARG A NE    1 
ATOM   6027  C  CZ    A ARG A 1 390 ? 10.993  -4.393  38.743  0.20 36.17  ? 390 ARG A CZ    1 
ATOM   6028  C  CZ    B ARG A 1 390 ? 10.863  -4.447  38.284  0.80 36.47  ? 390 ARG A CZ    1 
ATOM   6029  N  NH1   A ARG A 1 390 ? 11.212  -3.674  39.831  0.20 34.59  ? 390 ARG A NH1   1 
ATOM   6030  N  NH1   B ARG A 1 390 ? 10.904  -3.843  39.462  0.80 33.77  ? 390 ARG A NH1   1 
ATOM   6031  N  NH2   A ARG A 1 390 ? 9.804   -4.964  38.569  0.20 35.90  ? 390 ARG A NH2   1 
ATOM   6032  N  NH2   B ARG A 1 390 ? 9.747   -5.067  37.909  0.80 42.17  ? 390 ARG A NH2   1 
ATOM   6033  N  N     A LEU A 1 391 ? 11.946  -1.328  33.011  0.20 30.25  ? 391 LEU A N     1 
ATOM   6034  N  N     B LEU A 1 391 ? 11.941  -1.075  33.019  0.80 30.38  ? 391 LEU A N     1 
ATOM   6035  C  CA    A LEU A 1 391 ? 11.584  -1.482  31.610  0.20 30.18  ? 391 LEU A CA    1 
ATOM   6036  C  CA    B LEU A 1 391 ? 11.588  -1.108  31.611  0.80 29.49  ? 391 LEU A CA    1 
ATOM   6037  C  C     A LEU A 1 391 ? 12.084  -0.321  30.762  0.20 31.04  ? 391 LEU A C     1 
ATOM   6038  C  C     B LEU A 1 391 ? 12.316  -0.019  30.836  0.80 31.60  ? 391 LEU A C     1 
ATOM   6039  O  O     A LEU A 1 391 ? 12.419  -0.519  29.590  0.20 27.16  ? 391 LEU A O     1 
ATOM   6040  O  O     B LEU A 1 391 ? 12.903  -0.282  29.781  0.80 26.38  ? 391 LEU A O     1 
ATOM   6041  C  CB    A LEU A 1 391 ? 10.069  -1.627  31.480  0.20 30.39  ? 391 LEU A CB    1 
ATOM   6042  C  CB    B LEU A 1 391 ? 10.077  -0.945  31.468  0.80 30.82  ? 391 LEU A CB    1 
ATOM   6043  C  CG    A LEU A 1 391 ? 9.486   -1.965  30.108  0.20 31.25  ? 391 LEU A CG    1 
ATOM   6044  C  CG    B LEU A 1 391 ? 9.375   -1.488  30.234  0.80 33.19  ? 391 LEU A CG    1 
ATOM   6045  C  CD1   A LEU A 1 391 ? 10.243  -3.113  29.457  0.20 26.62  ? 391 LEU A CD1   1 
ATOM   6046  C  CD1   B LEU A 1 391 ? 9.591   -2.983  30.142  0.80 29.27  ? 391 LEU A CD1   1 
ATOM   6047  C  CD2   A LEU A 1 391 ? 8.018   -2.312  30.264  0.20 30.75  ? 391 LEU A CD2   1 
ATOM   6048  C  CD2   B LEU A 1 391 ? 7.890   -1.168  30.336  0.80 37.61  ? 391 LEU A CD2   1 
ATOM   6049  N  N     A ASP A 1 392 ? 12.142  0.889   31.326  0.20 28.64  ? 392 ASP A N     1 
ATOM   6050  N  N     B ASP A 1 392 ? 12.276  1.221   31.338  0.80 27.46  ? 392 ASP A N     1 
ATOM   6051  C  CA    A ASP A 1 392 ? 12.679  2.020   30.576  0.20 32.77  ? 392 ASP A CA    1 
ATOM   6052  C  CA    B ASP A 1 392 ? 12.874  2.336   30.603  0.80 34.18  ? 392 ASP A CA    1 
ATOM   6053  C  C     A ASP A 1 392 ? 14.180  1.878   30.349  0.20 31.43  ? 392 ASP A C     1 
ATOM   6054  C  C     B ASP A 1 392 ? 14.379  2.131   30.410  0.80 32.66  ? 392 ASP A C     1 
ATOM   6055  O  O     A ASP A 1 392 ? 14.697  2.333   29.322  0.20 31.34  ? 392 ASP A O     1 
ATOM   6056  O  O     B ASP A 1 392 ? 14.937  2.485   29.361  0.80 31.22  ? 392 ASP A O     1 
ATOM   6057  C  CB    A ASP A 1 392 ? 12.368  3.334   31.297  0.20 28.35  ? 392 ASP A CB    1 
ATOM   6058  C  CB    B ASP A 1 392 ? 12.577  3.660   31.323  0.80 26.39  ? 392 ASP A CB    1 
ATOM   6059  C  CG    A ASP A 1 392 ? 10.905  3.737   31.184  0.20 31.13  ? 392 ASP A CG    1 
ATOM   6060  C  CG    B ASP A 1 392 ? 11.121  4.115   31.163  0.80 33.35  ? 392 ASP A CG    1 
ATOM   6061  O  OD1   A ASP A 1 392 ? 10.077  2.893   30.783  0.20 29.73  ? 392 ASP A OD1   1 
ATOM   6062  O  OD1   B ASP A 1 392 ? 10.451  3.738   30.180  0.80 36.08  ? 392 ASP A OD1   1 
ATOM   6063  O  OD2   A ASP A 1 392 ? 10.581  4.905   31.490  0.20 33.48  ? 392 ASP A OD2   1 
ATOM   6064  O  OD2   B ASP A 1 392 ? 10.637  4.885   32.022  0.80 35.86  ? 392 ASP A OD2   1 
ATOM   6065  N  N     A HIS A 1 393 ? 14.891  1.246   31.287  0.20 29.66  ? 393 HIS A N     1 
ATOM   6066  N  N     B HIS A 1 393 ? 15.047  1.534   31.400  0.80 27.38  ? 393 HIS A N     1 
ATOM   6067  C  CA    A HIS A 1 393 ? 16.328  1.047   31.124  0.20 31.30  ? 393 HIS A CA    1 
ATOM   6068  C  CA    B HIS A 1 393 ? 16.480  1.270   31.294  0.80 30.33  ? 393 HIS A CA    1 
ATOM   6069  C  C     A HIS A 1 393 ? 16.631  0.067   29.995  0.20 33.81  ? 393 HIS A C     1 
ATOM   6070  C  C     B HIS A 1 393 ? 16.801  0.330   30.128  0.80 36.39  ? 393 HIS A C     1 
ATOM   6071  O  O     A HIS A 1 393 ? 17.559  0.288   29.206  0.20 29.46  ? 393 HIS A O     1 
ATOM   6072  O  O     B HIS A 1 393 ? 17.747  0.569   29.365  0.80 27.21  ? 393 HIS A O     1 
ATOM   6073  C  CB    A HIS A 1 393 ? 16.939  0.560   32.437  0.20 33.21  ? 393 HIS A CB    1 
ATOM   6074  C  CB    B HIS A 1 393 ? 16.991  0.690   32.612  0.80 33.28  ? 393 HIS A CB    1 
ATOM   6075  C  CG    A HIS A 1 393 ? 18.406  0.278   32.350  0.20 39.33  ? 393 HIS A CG    1 
ATOM   6076  C  CG    B HIS A 1 393 ? 18.416  0.246   32.561  0.80 40.44  ? 393 HIS A CG    1 
ATOM   6077  N  ND1   A HIS A 1 393 ? 19.329  1.240   32.000  0.20 39.93  ? 393 HIS A ND1   1 
ATOM   6078  N  ND1   B HIS A 1 393 ? 19.426  1.039   32.057  0.80 41.25  ? 393 HIS A ND1   1 
ATOM   6079  C  CD2   A HIS A 1 393 ? 19.109  -0.859  32.562  0.20 37.65  ? 393 HIS A CD2   1 
ATOM   6080  C  CD2   B HIS A 1 393 ? 19.000  -0.916  32.939  0.80 38.37  ? 393 HIS A CD2   1 
ATOM   6081  C  CE1   A HIS A 1 393 ? 20.538  0.707   32.002  0.20 36.07  ? 393 HIS A CE1   1 
ATOM   6082  C  CE1   B HIS A 1 393 ? 20.570  0.385   32.130  0.80 36.11  ? 393 HIS A CE1   1 
ATOM   6083  N  NE2   A HIS A 1 393 ? 20.432  -0.565  32.340  0.20 37.01  ? 393 HIS A NE2   1 
ATOM   6084  N  NE2   B HIS A 1 393 ? 20.340  -0.802  32.664  0.80 36.95  ? 393 HIS A NE2   1 
ATOM   6085  N  N     A LYS A 1 394 ? 15.869  -1.028  29.908  0.20 31.84  ? 394 LYS A N     1 
ATOM   6086  N  N     B LYS A 1 394 ? 16.034  -0.759  29.988  0.80 32.40  ? 394 LYS A N     1 
ATOM   6087  C  CA    A LYS A 1 394 ? 16.041  -1.966  28.803  0.20 29.33  ? 394 LYS A CA    1 
ATOM   6088  C  CA    B LYS A 1 394 ? 16.285  -1.724  28.919  0.80 28.53  ? 394 LYS A CA    1 
ATOM   6089  C  C     A LYS A 1 394 ? 15.723  -1.312  27.466  0.20 28.70  ? 394 LYS A C     1 
ATOM   6090  C  C     B LYS A 1 394 ? 16.066  -1.098  27.551  0.80 29.44  ? 394 LYS A C     1 
ATOM   6091  O  O     A LYS A 1 394 ? 16.280  -1.703  26.434  0.20 29.56  ? 394 LYS A O     1 
ATOM   6092  O  O     B LYS A 1 394 ? 16.916  -1.215  26.662  0.80 26.71  ? 394 LYS A O     1 
ATOM   6093  C  CB    A LYS A 1 394 ? 15.159  -3.197  29.015  0.20 32.10  ? 394 LYS A CB    1 
ATOM   6094  C  CB    B LYS A 1 394 ? 15.393  -2.951  29.099  0.80 32.99  ? 394 LYS A CB    1 
ATOM   6095  C  CG    A LYS A 1 394 ? 15.473  -3.979  30.278  0.20 31.17  ? 394 LYS A CG    1 
ATOM   6096  C  CG    B LYS A 1 394 ? 15.797  -3.845  30.248  0.80 28.74  ? 394 LYS A CG    1 
ATOM   6097  C  CD    A LYS A 1 394 ? 14.463  -5.096  30.499  0.20 37.31  ? 394 LYS A CD    1 
ATOM   6098  C  CD    B LYS A 1 394 ? 14.951  -5.106  30.280  0.80 38.32  ? 394 LYS A CD    1 
ATOM   6099  C  CE    A LYS A 1 394 ? 14.707  -5.810  31.821  0.20 44.25  ? 394 LYS A CE    1 
ATOM   6100  C  CE    B LYS A 1 394 ? 15.103  -5.835  31.606  0.80 45.77  ? 394 LYS A CE    1 
ATOM   6101  N  NZ    A LYS A 1 394 ? 13.704  -6.885  32.067  0.20 43.18  ? 394 LYS A NZ    1 
ATOM   6102  N  NZ    B LYS A 1 394 ? 14.293  -7.087  31.643  0.80 49.60  ? 394 LYS A NZ    1 
ATOM   6103  N  N     A PHE A 1 395 ? 14.830  -0.320  27.464  0.20 31.71  ? 395 PHE A N     1 
ATOM   6104  N  N     B PHE A 1 395 ? 14.919  -0.440  27.364  0.80 32.28  ? 395 PHE A N     1 
ATOM   6105  C  CA    A PHE A 1 395 ? 14.581  0.455   26.253  0.20 29.55  ? 395 PHE A CA    1 
ATOM   6106  C  CA    B PHE A 1 395 ? 14.666  0.437   26.224  0.80 29.69  ? 395 PHE A CA    1 
ATOM   6107  C  C     A PHE A 1 395 ? 15.779  1.334   25.912  0.20 30.86  ? 395 PHE A C     1 
ATOM   6108  C  C     B PHE A 1 395 ? 15.877  1.306   25.893  0.80 31.11  ? 395 PHE A C     1 
ATOM   6109  O  O     A PHE A 1 395 ? 16.082  1.550   24.733  0.20 28.36  ? 395 PHE A O     1 
ATOM   6110  O  O     B PHE A 1 395 ? 16.386  1.287   24.764  0.80 27.55  ? 395 PHE A O     1 
ATOM   6111  C  CB    A PHE A 1 395 ? 13.321  1.305   26.430  0.20 28.06  ? 395 PHE A CB    1 
ATOM   6112  C  CB    B PHE A 1 395 ? 13.452  1.325   26.546  0.80 27.92  ? 395 PHE A CB    1 
ATOM   6113  C  CG    A PHE A 1 395 ? 12.915  2.062   25.196  0.20 25.80  ? 395 PHE A CG    1 
ATOM   6114  C  CG    B PHE A 1 395 ? 12.977  2.178   25.403  0.80 24.83  ? 395 PHE A CG    1 
ATOM   6115  C  CD1   A PHE A 1 395 ? 12.089  1.478   24.253  0.20 28.93  ? 395 PHE A CD1   1 
ATOM   6116  C  CD1   B PHE A 1 395 ? 13.645  3.347   25.050  0.80 30.19  ? 395 PHE A CD1   1 
ATOM   6117  C  CD2   A PHE A 1 395 ? 13.351  3.361   24.986  0.20 29.54  ? 395 PHE A CD2   1 
ATOM   6118  C  CD2   B PHE A 1 395 ? 11.828  1.843   24.721  0.80 23.01  ? 395 PHE A CD2   1 
ATOM   6119  C  CE1   A PHE A 1 395 ? 11.712  2.171   23.116  0.20 27.66  ? 395 PHE A CE1   1 
ATOM   6120  C  CE1   B PHE A 1 395 ? 13.196  4.136   24.013  0.80 26.39  ? 395 PHE A CE1   1 
ATOM   6121  C  CE2   A PHE A 1 395 ? 12.977  4.059   23.855  0.20 27.73  ? 395 PHE A CE2   1 
ATOM   6122  C  CE2   B PHE A 1 395 ? 11.372  2.628   23.680  0.80 30.72  ? 395 PHE A CE2   1 
ATOM   6123  C  CZ    A PHE A 1 395 ? 12.155  3.463   22.918  0.20 30.95  ? 395 PHE A CZ    1 
ATOM   6124  C  CZ    B PHE A 1 395 ? 12.053  3.778   23.327  0.80 31.13  ? 395 PHE A CZ    1 
ATOM   6125  N  N     A ASP A 1 396 ? 16.472  1.849   26.932  0.20 27.63  ? 396 ASP A N     1 
ATOM   6126  N  N     B ASP A 1 396 ? 16.327  2.095   26.875  0.80 26.88  ? 396 ASP A N     1 
ATOM   6127  C  CA    A ASP A 1 396 ? 17.608  2.728   26.680  0.20 32.31  ? 396 ASP A CA    1 
ATOM   6128  C  CA    B ASP A 1 396 ? 17.369  3.086   26.622  0.80 34.39  ? 396 ASP A CA    1 
ATOM   6129  C  C     A ASP A 1 396 ? 18.818  1.955   26.173  0.20 28.42  ? 396 ASP A C     1 
ATOM   6130  C  C     B ASP A 1 396 ? 18.640  2.427   26.102  0.80 29.29  ? 396 ASP A C     1 
ATOM   6131  O  O     A ASP A 1 396 ? 19.605  2.490   25.383  0.20 28.74  ? 396 ASP A O     1 
ATOM   6132  O  O     B ASP A 1 396 ? 19.299  2.966   25.204  0.80 25.61  ? 396 ASP A O     1 
ATOM   6133  C  CB    A ASP A 1 396 ? 17.983  3.499   27.947  0.20 29.24  ? 396 ASP A CB    1 
ATOM   6134  C  CB    B ASP A 1 396 ? 17.684  3.880   27.893  0.80 30.50  ? 396 ASP A CB    1 
ATOM   6135  C  CG    A ASP A 1 396 ? 16.828  4.314   28.505  0.20 29.90  ? 396 ASP A CG    1 
ATOM   6136  C  CG    B ASP A 1 396 ? 16.697  5.030   28.164  0.80 30.50  ? 396 ASP A CG    1 
ATOM   6137  O  OD1   A ASP A 1 396 ? 15.873  4.604   27.754  0.20 30.76  ? 396 ASP A OD1   1 
ATOM   6138  O  OD1   B ASP A 1 396 ? 15.780  5.298   27.351  0.80 28.60  ? 396 ASP A OD1   1 
ATOM   6139  O  OD2   A ASP A 1 396 ? 16.885  4.666   29.702  0.20 22.53  ? 396 ASP A OD2   1 
ATOM   6140  O  OD2   B ASP A 1 396 ? 16.857  5.676   29.219  0.80 30.62  ? 396 ASP A OD2   1 
ATOM   6141  N  N     A LEU A 1 397 ? 18.989  0.706   26.614  0.20 29.43  ? 397 LEU A N     1 
ATOM   6142  N  N     B LEU A 1 397 ? 19.004  1.271   26.667  0.80 27.42  ? 397 LEU A N     1 
ATOM   6143  C  CA    A LEU A 1 397 ? 20.163  -0.062  26.210  0.20 29.52  ? 397 LEU A CA    1 
ATOM   6144  C  CA    B LEU A 1 397 ? 20.233  0.582   26.265  0.80 30.37  ? 397 LEU A CA    1 
ATOM   6145  C  C     A LEU A 1 397 ? 20.142  -0.394  24.723  0.20 28.86  ? 397 LEU A C     1 
ATOM   6146  C  C     B LEU A 1 397 ? 20.232  0.244   24.779  0.80 29.79  ? 397 LEU A C     1 
ATOM   6147  O  O     A LEU A 1 397 ? 21.206  -0.519  24.105  0.20 28.41  ? 397 LEU A O     1 
ATOM   6148  O  O     B LEU A 1 397 ? 21.219  0.488   24.075  0.80 31.00  ? 397 LEU A O     1 
ATOM   6149  C  CB    A LEU A 1 397 ? 20.264  -1.341  27.042  0.20 30.24  ? 397 LEU A CB    1 
ATOM   6150  C  CB    B LEU A 1 397 ? 20.412  -0.691  27.093  0.80 28.81  ? 397 LEU A CB    1 
ATOM   6151  C  CG    A LEU A 1 397 ? 20.496  -1.170  28.545  0.20 31.00  ? 397 LEU A CG    1 
ATOM   6152  C  CG    B LEU A 1 397 ? 20.905  -0.611  28.541  0.80 33.08  ? 397 LEU A CG    1 
ATOM   6153  C  CD1   A LEU A 1 397 ? 20.431  -2.513  29.250  0.20 30.04  ? 397 LEU A CD1   1 
ATOM   6154  C  CD1   B LEU A 1 397 ? 21.016  -2.010  29.099  0.80 31.60  ? 397 LEU A CD1   1 
ATOM   6155  C  CD2   A LEU A 1 397 ? 21.827  -0.483  28.819  0.20 32.85  ? 397 LEU A CD2   1 
ATOM   6156  C  CD2   B LEU A 1 397 ? 22.243  0.129   28.629  0.80 32.19  ? 397 LEU A CD2   1 
ATOM   6157  N  N     A MET A 1 398 ? 18.955  -0.536  24.130  0.20 27.95  ? 398 MET A N     1 
ATOM   6158  N  N     B MET A 1 398 ? 19.138  -0.340  24.283  0.80 27.55  ? 398 MET A N     1 
ATOM   6159  C  CA    A MET A 1 398 ? 18.838  -0.801  22.701  0.20 26.27  ? 398 MET A CA    1 
ATOM   6160  C  CA    B MET A 1 398 ? 19.073  -0.650  22.862  0.80 26.17  ? 398 MET A CA    1 
ATOM   6161  C  C     A MET A 1 398 ? 18.721  0.472   21.873  0.20 30.09  ? 398 MET A C     1 
ATOM   6162  C  C     B MET A 1 398 ? 18.847  0.595   22.012  0.80 30.72  ? 398 MET A C     1 
ATOM   6163  O  O     A MET A 1 398 ? 19.380  0.592   20.833  0.20 29.28  ? 398 MET A O     1 
ATOM   6164  O  O     B MET A 1 398 ? 19.462  0.723   20.947  0.80 29.33  ? 398 MET A O     1 
ATOM   6165  C  CB    A MET A 1 398 ? 17.630  -1.697  22.415  0.20 26.63  ? 398 MET A CB    1 
ATOM   6166  C  CB    B MET A 1 398 ? 18.000  -1.698  22.580  0.80 24.21  ? 398 MET A CB    1 
ATOM   6167  C  CG    A MET A 1 398 ? 17.807  -3.150  22.815  0.20 30.29  ? 398 MET A CG    1 
ATOM   6168  C  CG    B MET A 1 398 ? 18.198  -2.998  23.357  0.80 33.50  ? 398 MET A CG    1 
ATOM   6169  S  SD    A MET A 1 398 ? 16.361  -4.151  22.410  0.20 28.41  ? 398 MET A SD    1 
ATOM   6170  S  SD    B MET A 1 398 ? 17.017  -4.308  22.942  0.80 34.93  ? 398 MET A SD    1 
ATOM   6171  C  CE    A MET A 1 398 ? 15.136  -3.428  23.497  0.20 26.79  ? 398 MET A CE    1 
ATOM   6172  C  CE    B MET A 1 398 ? 15.516  -3.534  23.530  0.80 25.64  ? 398 MET A CE    1 
ATOM   6173  N  N     A TYR A 1 399 ? 17.896  1.428   22.309  0.20 28.04  ? 399 TYR A N     1 
ATOM   6174  N  N     B TYR A 1 399 ? 18.009  1.538   22.459  0.80 27.39  ? 399 TYR A N     1 
ATOM   6175  C  CA    A TYR A 1 399 ? 17.618  2.602   21.486  0.20 29.18  ? 399 TYR A CA    1 
ATOM   6176  C  CA    B TYR A 1 399 ? 17.680  2.667   21.584  0.80 29.11  ? 399 TYR A CA    1 
ATOM   6177  C  C     A TYR A 1 399 ? 18.835  3.501   21.307  0.20 30.81  ? 399 TYR A C     1 
ATOM   6178  C  C     B TYR A 1 399 ? 18.865  3.614   21.378  0.80 30.52  ? 399 TYR A C     1 
ATOM   6179  O  O     A TYR A 1 399 ? 18.909  4.229   20.309  0.20 31.64  ? 399 TYR A O     1 
ATOM   6180  O  O     B TYR A 1 399 ? 18.949  4.282   20.337  0.80 31.51  ? 399 TYR A O     1 
ATOM   6181  C  CB    A TYR A 1 399 ? 16.458  3.403   22.081  0.20 31.69  ? 399 TYR A CB    1 
ATOM   6182  C  CB    B TYR A 1 399 ? 16.477  3.444   22.118  0.80 31.84  ? 399 TYR A CB    1 
ATOM   6183  C  CG    A TYR A 1 399 ? 15.975  4.518   21.181  0.20 30.90  ? 399 TYR A CG    1 
ATOM   6184  C  CG    B TYR A 1 399 ? 15.966  4.444   21.104  0.80 30.65  ? 399 TYR A CG    1 
ATOM   6185  C  CD1   A TYR A 1 399 ? 15.338  4.237   19.979  0.20 33.97  ? 399 TYR A CD1   1 
ATOM   6186  C  CD1   B TYR A 1 399 ? 15.474  4.016   19.875  0.80 33.89  ? 399 TYR A CD1   1 
ATOM   6187  C  CD2   A TYR A 1 399 ? 16.158  5.849   21.531  0.20 34.47  ? 399 TYR A CD2   1 
ATOM   6188  C  CD2   B TYR A 1 399 ? 15.997  5.809   21.359  0.80 34.24  ? 399 TYR A CD2   1 
ATOM   6189  C  CE1   A TYR A 1 399 ? 14.898  5.251   19.149  0.20 35.67  ? 399 TYR A CE1   1 
ATOM   6190  C  CE1   B TYR A 1 399 ? 15.020  4.923   18.928  0.80 34.29  ? 399 TYR A CE1   1 
ATOM   6191  C  CE2   A TYR A 1 399 ? 15.721  6.870   20.710  0.20 38.51  ? 399 TYR A CE2   1 
ATOM   6192  C  CE2   B TYR A 1 399 ? 15.546  6.723   20.420  0.80 40.21  ? 399 TYR A CE2   1 
ATOM   6193  C  CZ    A TYR A 1 399 ? 15.092  6.565   19.520  0.20 37.76  ? 399 TYR A CZ    1 
ATOM   6194  C  CZ    B TYR A 1 399 ? 15.058  6.273   19.207  0.80 37.85  ? 399 TYR A CZ    1 
ATOM   6195  O  OH    A TYR A 1 399 ? 14.657  7.580   18.699  0.20 42.98  ? 399 TYR A OH    1 
ATOM   6196  O  OH    B TYR A 1 399 ? 14.609  7.171   18.261  0.80 47.32  ? 399 TYR A OH    1 
ATOM   6197  N  N     A ALA A 1 400 ? 19.787  3.470   22.243  0.20 28.87  ? 400 ALA A N     1 
ATOM   6198  N  N     B ALA A 1 400 ? 19.774  3.695   22.353  0.80 28.74  ? 400 ALA A N     1 
ATOM   6199  C  CA    A ALA A 1 400 ? 21.015  4.239   22.081  0.20 32.12  ? 400 ALA A CA    1 
ATOM   6200  C  CA    B ALA A 1 400 ? 20.966  4.526   22.209  0.80 32.16  ? 400 ALA A CA    1 
ATOM   6201  C  C     A ALA A 1 400 ? 21.825  3.779   20.876  0.20 32.07  ? 400 ALA A C     1 
ATOM   6202  C  C     B ALA A 1 400 ? 21.775  4.152   20.968  0.80 32.29  ? 400 ALA A C     1 
ATOM   6203  O  O     A ALA A 1 400 ? 22.611  4.562   20.335  0.20 32.29  ? 400 ALA A O     1 
ATOM   6204  O  O     B ALA A 1 400 ? 22.352  5.028   20.317  0.80 35.63  ? 400 ALA A O     1 
ATOM   6205  C  CB    A ALA A 1 400 ? 21.861  4.140   23.349  0.20 28.47  ? 400 ALA A CB    1 
ATOM   6206  C  CB    B ALA A 1 400 ? 21.823  4.406   23.466  0.80 27.36  ? 400 ALA A CB    1 
ATOM   6207  N  N     A LYS A 1 401 ? 21.645  2.534   20.441  0.20 31.27  ? 401 LYS A N     1 
ATOM   6208  N  N     B LYS A 1 401 ? 21.825  2.868   20.623  0.80 30.97  ? 401 LYS A N     1 
ATOM   6209  C  CA    A LYS A 1 401 ? 22.323  1.995   19.269  0.20 31.88  ? 401 LYS A CA    1 
ATOM   6210  C  CA    B LYS A 1 401 ? 22.486  2.402   19.406  0.80 32.52  ? 401 LYS A CA    1 
ATOM   6211  C  C     A LYS A 1 401 ? 21.379  1.842   18.082  0.20 33.88  ? 401 LYS A C     1 
ATOM   6212  C  C     B LYS A 1 401 ? 21.533  2.285   18.221  0.80 36.17  ? 401 LYS A C     1 
ATOM   6213  O  O     A LYS A 1 401 ? 21.787  1.315   17.041  0.20 29.70  ? 401 LYS A O     1 
ATOM   6214  O  O     B LYS A 1 401 ? 21.987  1.995   17.105  0.80 34.58  ? 401 LYS A O     1 
ATOM   6215  C  CB    A LYS A 1 401 ? 22.971  0.647   19.602  0.20 28.37  ? 401 LYS A CB    1 
ATOM   6216  C  CB    B LYS A 1 401 ? 23.137  1.041   19.660  0.80 25.23  ? 401 LYS A CB    1 
ATOM   6217  C  CG    A LYS A 1 401 ? 24.383  0.738   20.174  0.20 35.50  ? 401 LYS A CG    1 
ATOM   6218  C  CG    B LYS A 1 401 ? 24.569  1.093   20.198  0.80 36.69  ? 401 LYS A CG    1 
ATOM   6219  C  CD    A LYS A 1 401 ? 24.410  1.448   21.513  0.20 37.49  ? 401 LYS A CD    1 
ATOM   6220  C  CD    B LYS A 1 401 ? 24.620  1.478   21.647  0.80 39.23  ? 401 LYS A CD    1 
ATOM   6221  C  CE    A LYS A 1 401 ? 25.832  1.654   22.006  0.20 38.39  ? 401 LYS A CE    1 
ATOM   6222  C  CE    B LYS A 1 401 ? 26.030  1.309   22.191  0.80 39.40  ? 401 LYS A CE    1 
ATOM   6223  N  NZ    A LYS A 1 401 ? 25.853  2.475   23.249  0.20 31.73  ? 401 LYS A NZ    1 
ATOM   6224  N  NZ    B LYS A 1 401 ? 26.094  1.622   23.652  0.80 33.10  ? 401 LYS A NZ    1 
ATOM   6225  N  N     A ARG A 1 402 ? 20.128  2.292   18.221  0.20 30.78  ? 402 ARG A N     1 
ATOM   6226  N  N     B ARG A 1 402 ? 20.234  2.496   18.449  0.80 31.18  ? 402 ARG A N     1 
ATOM   6227  C  CA    A ARG A 1 402 ? 19.108  2.192   17.173  0.20 29.99  ? 402 ARG A CA    1 
ATOM   6228  C  CA    B ARG A 1 402 ? 19.167  2.306   17.465  0.80 29.23  ? 402 ARG A CA    1 
ATOM   6229  C  C     A ARG A 1 402 ? 18.925  0.749   16.708  0.20 28.67  ? 402 ARG A C     1 
ATOM   6230  C  C     B ARG A 1 402 ? 19.024  0.843   17.052  0.80 27.64  ? 402 ARG A C     1 
ATOM   6231  O  O     A ARG A 1 402 ? 18.690  0.480   15.528  0.20 30.77  ? 402 ARG A O     1 
ATOM   6232  O  O     B ARG A 1 402 ? 18.652  0.548   15.915  0.80 31.33  ? 402 ARG A O     1 
ATOM   6233  C  CB    A ARG A 1 402 ? 19.432  3.109   15.990  0.20 35.39  ? 402 ARG A CB    1 
ATOM   6234  C  CB    B ARG A 1 402 ? 19.367  3.199   16.234  0.80 36.27  ? 402 ARG A CB    1 
ATOM   6235  C  CG    A ARG A 1 402 ? 19.327  4.601   16.295  0.20 36.53  ? 402 ARG A CG    1 
ATOM   6236  C  CG    B ARG A 1 402 ? 19.628  4.674   16.558  0.80 36.99  ? 402 ARG A CG    1 
ATOM   6237  C  CD    A ARG A 1 402 ? 17.936  4.978   16.795  0.20 39.68  ? 402 ARG A CD    1 
ATOM   6238  C  CD    B ARG A 1 402 ? 18.475  5.293   17.347  0.80 38.52  ? 402 ARG A CD    1 
ATOM   6239  N  NE    A ARG A 1 402 ? 17.710  6.420   16.772  0.20 42.01  ? 402 ARG A NE    1 
ATOM   6240  N  NE    B ARG A 1 402 ? 18.542  6.751   17.386  0.80 48.87  ? 402 ARG A NE    1 
ATOM   6241  C  CZ    A ARG A 1 402 ? 18.010  7.245   17.767  0.20 42.74  ? 402 ARG A CZ    1 
ATOM   6242  C  CZ    B ARG A 1 402 ? 18.811  7.469   18.469  0.80 39.05  ? 402 ARG A CZ    1 
ATOM   6243  N  NH1   A ARG A 1 402 ? 18.563  6.807   18.887  0.20 39.63  ? 402 ARG A NH1   1 
ATOM   6244  N  NH1   B ARG A 1 402 ? 19.035  6.898   19.643  0.80 38.88  ? 402 ARG A NH1   1 
ATOM   6245  N  NH2   A ARG A 1 402 ? 17.753  8.542   17.633  0.20 38.92  ? 402 ARG A NH2   1 
ATOM   6246  N  NH2   B ARG A 1 402 ? 18.846  8.796   18.374  0.80 37.56  ? 402 ARG A NH2   1 
ATOM   6247  N  N     A ALA A 1 403 ? 19.022  -0.189  17.646  0.20 26.51  ? 403 ALA A N     1 
ATOM   6248  N  N     B ALA A 1 403 ? 19.309  -0.079  17.971  0.80 24.27  ? 403 ALA A N     1 
ATOM   6249  C  CA    A ALA A 1 403 ? 18.893  -1.600  17.318  0.20 28.04  ? 403 ALA A CA    1 
ATOM   6250  C  CA    B ALA A 1 403 ? 19.204  -1.499  17.672  0.80 26.84  ? 403 ALA A CA    1 
ATOM   6251  C  C     A ALA A 1 403 ? 17.434  -1.967  17.080  0.20 27.81  ? 403 ALA A C     1 
ATOM   6252  C  C     B ALA A 1 403 ? 17.755  -1.885  17.385  0.80 28.53  ? 403 ALA A C     1 
ATOM   6253  O  O     A ALA A 1 403 ? 16.539  -1.509  17.794  0.20 28.19  ? 403 ALA A O     1 
ATOM   6254  O  O     B ALA A 1 403 ? 16.848  -1.517  18.135  0.80 30.16  ? 403 ALA A O     1 
ATOM   6255  C  CB    A ALA A 1 403 ? 19.476  -2.462  18.436  0.20 23.89  ? 403 ALA A CB    1 
ATOM   6256  C  CB    B ALA A 1 403 ? 19.764  -2.322  18.830  0.80 21.18  ? 403 ALA A CB    1 
ATOM   6257  N  N     A PHE A 1 404 ? 17.203  -2.794  16.056  0.20 26.18  ? 404 PHE A N     1 
ATOM   6258  N  N     B PHE A 1 404 ? 17.541  -2.622  16.289  0.80 25.71  ? 404 PHE A N     1 
ATOM   6259  C  CA    A PHE A 1 404 ? 15.877  -3.338  15.745  0.20 27.95  ? 404 PHE A CA    1 
ATOM   6260  C  CA    B PHE A 1 404 ? 16.253  -3.147  15.817  0.80 28.16  ? 404 PHE A CA    1 
ATOM   6261  C  C     A PHE A 1 404 ? 14.866  -2.248  15.396  0.20 27.08  ? 404 PHE A C     1 
ATOM   6262  C  C     B PHE A 1 404 ? 15.285  -2.072  15.327  0.80 27.07  ? 404 PHE A C     1 
ATOM   6263  O  O     A PHE A 1 404 ? 13.659  -2.438  15.558  0.20 26.04  ? 404 PHE A O     1 
ATOM   6264  O  O     B PHE A 1 404 ? 14.192  -2.421  14.847  0.80 25.26  ? 404 PHE A O     1 
ATOM   6265  C  CB    A PHE A 1 404 ? 15.337  -4.196  16.897  0.20 24.21  ? 404 PHE A CB    1 
ATOM   6266  C  CB    B PHE A 1 404 ? 15.521  -3.988  16.884  0.80 24.39  ? 404 PHE A CB    1 
ATOM   6267  C  CG    A PHE A 1 404 ? 16.256  -5.307  17.311  0.20 22.94  ? 404 PHE A CG    1 
ATOM   6268  C  CG    B PHE A 1 404 ? 16.359  -5.096  17.458  0.80 22.20  ? 404 PHE A CG    1 
ATOM   6269  C  CD1   A PHE A 1 404 ? 16.231  -6.523  16.655  0.20 23.68  ? 404 PHE A CD1   1 
ATOM   6270  C  CD1   B PHE A 1 404 ? 16.535  -6.279  16.770  0.80 23.28  ? 404 PHE A CD1   1 
ATOM   6271  C  CD2   A PHE A 1 404 ? 17.139  -5.138  18.363  0.20 23.04  ? 404 PHE A CD2   1 
ATOM   6272  C  CD2   B PHE A 1 404 ? 16.978  -4.949  18.680  0.80 22.03  ? 404 PHE A CD2   1 
ATOM   6273  C  CE1   A PHE A 1 404 ? 17.076  -7.553  17.035  0.20 25.15  ? 404 PHE A CE1   1 
ATOM   6274  C  CE1   B PHE A 1 404 ? 17.332  -7.295  17.288  0.80 22.96  ? 404 PHE A CE1   1 
ATOM   6275  C  CE2   A PHE A 1 404 ? 17.987  -6.164  18.749  0.20 27.82  ? 404 PHE A CE2   1 
ATOM   6276  C  CE2   B PHE A 1 404 ? 17.757  -5.967  19.215  0.80 31.01  ? 404 PHE A CE2   1 
ATOM   6277  C  CZ    A PHE A 1 404 ? 17.954  -7.375  18.083  0.20 24.35  ? 404 PHE A CZ    1 
ATOM   6278  C  CZ    B PHE A 1 404 ? 17.933  -7.146  18.513  0.80 25.47  ? 404 PHE A CZ    1 
ATOM   6279  N  N     A VAL A 1 405 ? 15.340  -1.101  14.913  0.20 27.18  ? 405 VAL A N     1 
ATOM   6280  N  N     B VAL A 1 405 ? 15.637  -0.785  15.420  0.80 27.20  ? 405 VAL A N     1 
ATOM   6281  C  CA    A VAL A 1 405 ? 14.437  -0.003  14.588  0.20 27.58  ? 405 VAL A CA    1 
ATOM   6282  C  CA    B VAL A 1 405 ? 14.691  0.272   15.075  0.80 28.93  ? 405 VAL A CA    1 
ATOM   6283  C  C     A VAL A 1 405 ? 13.948  -0.073  13.142  0.20 28.29  ? 405 VAL A C     1 
ATOM   6284  C  C     B VAL A 1 405 ? 14.240  0.159   13.626  0.80 29.09  ? 405 VAL A C     1 
ATOM   6285  O  O     A VAL A 1 405 ? 12.829  0.361   12.846  0.20 26.93  ? 405 VAL A O     1 
ATOM   6286  O  O     B VAL A 1 405 ? 13.097  0.498   13.294  0.80 25.58  ? 405 VAL A O     1 
ATOM   6287  C  CB    A VAL A 1 405 ? 15.120  1.345   14.883  0.20 28.71  ? 405 VAL A CB    1 
ATOM   6288  C  CB    B VAL A 1 405 ? 15.306  1.655   15.379  0.80 28.17  ? 405 VAL A CB    1 
ATOM   6289  C  CG1   A VAL A 1 405 ? 14.186  2.508   14.566  0.20 31.01  ? 405 VAL A CG1   1 
ATOM   6290  C  CG1   B VAL A 1 405 ? 14.509  2.769   14.686  0.80 32.73  ? 405 VAL A CG1   1 
ATOM   6291  C  CG2   A VAL A 1 405 ? 15.559  1.406   16.335  0.20 28.46  ? 405 VAL A CG2   1 
ATOM   6292  C  CG2   B VAL A 1 405 ? 15.348  1.899   16.882  0.80 27.41  ? 405 VAL A CG2   1 
ATOM   6293  N  N     A HIS A 1 406 ? 14.753  -0.629  12.233  0.20 26.45  ? 406 HIS A N     1 
ATOM   6294  N  N     B HIS A 1 406 ? 15.106  -0.343  12.744  0.80 26.84  ? 406 HIS A N     1 
ATOM   6295  C  CA    A HIS A 1 406 ? 14.341  -0.705  10.837  0.20 28.22  ? 406 HIS A CA    1 
ATOM   6296  C  CA    B HIS A 1 406 ? 14.754  -0.384  11.331  0.80 27.08  ? 406 HIS A CA    1 
ATOM   6297  C  C     A HIS A 1 406 ? 13.139  -1.621  10.635  0.20 29.97  ? 406 HIS A C     1 
ATOM   6298  C  C     B HIS A 1 406 ? 13.538  -1.274  11.069  0.80 32.50  ? 406 HIS A C     1 
ATOM   6299  O  O     A HIS A 1 406 ? 12.441  -1.485  9.625   0.20 28.76  ? 406 HIS A O     1 
ATOM   6300  O  O     B HIS A 1 406 ? 12.772  -1.000  10.136  0.80 25.86  ? 406 HIS A O     1 
ATOM   6301  C  CB    A HIS A 1 406 ? 15.509  -1.171  9.963   0.20 29.01  ? 406 HIS A CB    1 
ATOM   6302  C  CB    B HIS A 1 406 ? 15.967  -0.834  10.505  0.80 26.21  ? 406 HIS A CB    1 
ATOM   6303  C  CG    A HIS A 1 406 ? 15.906  -2.595  10.195  0.20 26.69  ? 406 HIS A CG    1 
ATOM   6304  C  CG    B HIS A 1 406 ? 16.301  -2.281  10.680  0.80 25.69  ? 406 HIS A CG    1 
ATOM   6305  N  ND1   A HIS A 1 406 ? 16.672  -2.988  11.271  0.20 27.41  ? 406 HIS A ND1   1 
ATOM   6306  N  ND1   B HIS A 1 406 ? 16.938  -2.768  11.801  0.80 29.29  ? 406 HIS A ND1   1 
ATOM   6307  C  CD2   A HIS A 1 406 ? 15.644  -3.721  9.489   0.20 27.69  ? 406 HIS A CD2   1 
ATOM   6308  C  CD2   B HIS A 1 406 ? 16.056  -3.351  9.890   0.80 25.87  ? 406 HIS A CD2   1 
ATOM   6309  C  CE1   A HIS A 1 406 ? 16.865  -4.293  11.218  0.20 28.56  ? 406 HIS A CE1   1 
ATOM   6310  C  CE1   B HIS A 1 406 ? 17.092  -4.076  11.683  0.80 29.72  ? 406 HIS A CE1   1 
ATOM   6311  N  NE2   A HIS A 1 406 ? 16.251  -4.762  10.147  0.20 27.18  ? 406 HIS A NE2   1 
ATOM   6312  N  NE2   B HIS A 1 406 ? 16.567  -4.452  10.530  0.80 26.14  ? 406 HIS A NE2   1 
ATOM   6313  N  N     A TRP A 1 407 ? 12.880  -2.546  11.567  0.20 25.08  ? 407 TRP A N     1 
ATOM   6314  N  N     B TRP A 1 407 ? 13.328  -2.325  11.884  0.80 23.89  ? 407 TRP A N     1 
ATOM   6315  C  CA    A TRP A 1 407 ? 11.701  -3.398  11.450  0.20 28.50  ? 407 TRP A CA    1 
ATOM   6316  C  CA    B TRP A 1 407 ? 12.164  -3.192  11.701  0.80 26.69  ? 407 TRP A CA    1 
ATOM   6317  C  C     A TRP A 1 407 ? 10.419  -2.614  11.695  0.20 29.84  ? 407 TRP A C     1 
ATOM   6318  C  C     B TRP A 1 407 ? 10.860  -2.438  11.926  0.80 32.81  ? 407 TRP A C     1 
ATOM   6319  O  O     A TRP A 1 407 ? 9.386   -2.909  11.082  0.20 28.76  ? 407 TRP A O     1 
ATOM   6320  O  O     B TRP A 1 407 ? 9.837   -2.769  11.313  0.80 28.16  ? 407 TRP A O     1 
ATOM   6321  C  CB    A TRP A 1 407 ? 11.787  -4.575  12.424  0.20 27.81  ? 407 TRP A CB    1 
ATOM   6322  C  CB    B TRP A 1 407 ? 12.219  -4.393  12.652  0.80 27.11  ? 407 TRP A CB    1 
ATOM   6323  C  CG    A TRP A 1 407 ? 12.926  -5.502  12.161  0.20 32.60  ? 407 TRP A CG    1 
ATOM   6324  C  CG    B TRP A 1 407 ? 13.216  -5.419  12.314  0.80 35.45  ? 407 TRP A CG    1 
ATOM   6325  C  CD1   A TRP A 1 407 ? 13.982  -5.761  12.988  0.20 29.59  ? 407 TRP A CD1   1 
ATOM   6326  C  CD1   B TRP A 1 407 ? 14.311  -5.779  13.049  0.80 29.69  ? 407 TRP A CD1   1 
ATOM   6327  C  CD2   A TRP A 1 407 ? 13.132  -6.295  10.986  0.20 30.03  ? 407 TRP A CD2   1 
ATOM   6328  C  CD2   B TRP A 1 407 ? 13.227  -6.240  11.146  0.80 29.51  ? 407 TRP A CD2   1 
ATOM   6329  N  NE1   A TRP A 1 407 ? 14.832  -6.667  12.399  0.20 28.52  ? 407 TRP A NE1   1 
ATOM   6330  N  NE1   B TRP A 1 407 ? 15.008  -6.769  12.401  0.80 28.25  ? 407 TRP A NE1   1 
ATOM   6331  C  CE2   A TRP A 1 407 ? 14.332  -7.010  11.170  0.20 31.69  ? 407 TRP A CE2   1 
ATOM   6332  C  CE2   B TRP A 1 407 ? 14.365  -7.068  11.230  0.80 31.92  ? 407 TRP A CE2   1 
ATOM   6333  C  CE3   A TRP A 1 407 ? 12.418  -6.468  9.796   0.20 36.86  ? 407 TRP A CE3   1 
ATOM   6334  C  CE3   B TRP A 1 407 ? 12.390  -6.350  10.029  0.80 38.15  ? 407 TRP A CE3   1 
ATOM   6335  C  CZ2   A TRP A 1 407 ? 14.835  -7.883  10.209  0.20 31.59  ? 407 TRP A CZ2   1 
ATOM   6336  C  CZ2   B TRP A 1 407 ? 14.686  -7.992  10.247  0.80 31.77  ? 407 TRP A CZ2   1 
ATOM   6337  C  CZ3   A TRP A 1 407 ? 12.918  -7.337  8.843   0.20 37.95  ? 407 TRP A CZ3   1 
ATOM   6338  C  CZ3   B TRP A 1 407 ? 12.709  -7.272  9.051   0.80 38.53  ? 407 TRP A CZ3   1 
ATOM   6339  C  CH2   A TRP A 1 407 ? 14.115  -8.033  9.055   0.20 38.95  ? 407 TRP A CH2   1 
ATOM   6340  C  CH2   B TRP A 1 407 ? 13.847  -8.083  9.166   0.80 41.97  ? 407 TRP A CH2   1 
ATOM   6341  N  N     A TYR A 1 408 ? 10.466  -1.617  12.580  0.20 26.00  ? 408 TYR A N     1 
ATOM   6342  N  N     B TYR A 1 408 ? 10.876  -1.434  12.806  0.80 20.81  ? 408 TYR A N     1 
ATOM   6343  C  CA    A TYR A 1 408 ? 9.282   -0.819  12.881  0.20 29.58  ? 408 TYR A CA    1 
ATOM   6344  C  CA    B TYR A 1 408 ? 9.690   -0.627  13.074  0.80 32.14  ? 408 TYR A CA    1 
ATOM   6345  C  C     A TYR A 1 408 ? 9.034   0.234   11.809  0.20 30.12  ? 408 TYR A C     1 
ATOM   6346  C  C     B TYR A 1 408 ? 9.509   0.458   12.025  0.80 28.26  ? 408 TYR A C     1 
ATOM   6347  O  O     A TYR A 1 408 ? 7.901   0.404   11.347  0.20 31.72  ? 408 TYR A O     1 
ATOM   6348  O  O     B TYR A 1 408 ? 8.392   0.695   11.552  0.80 27.05  ? 408 TYR A O     1 
ATOM   6349  C  CB    A TYR A 1 408 ? 9.433   -0.159  14.252  0.20 27.17  ? 408 TYR A CB    1 
ATOM   6350  C  CB    B TYR A 1 408 ? 9.803   -0.001  14.458  0.80 25.53  ? 408 TYR A CB    1 
ATOM   6351  C  CG    A TYR A 1 408 ? 9.445   -1.135  15.406  0.20 26.68  ? 408 TYR A CG    1 
ATOM   6352  C  CG    B TYR A 1 408 ? 9.813   -1.011  15.584  0.80 25.67  ? 408 TYR A CG    1 
ATOM   6353  C  CD1   A TYR A 1 408 ? 10.610  -1.792  15.774  0.20 27.49  ? 408 TYR A CD1   1 
ATOM   6354  C  CD1   B TYR A 1 408 ? 10.952  -1.758  15.870  0.80 28.31  ? 408 TYR A CD1   1 
ATOM   6355  C  CD2   A TYR A 1 408 ? 8.289   -1.389  16.136  0.20 27.45  ? 408 TYR A CD2   1 
ATOM   6356  C  CD2   B TYR A 1 408 ? 8.685   -1.198  16.380  0.80 30.00  ? 408 TYR A CD2   1 
ATOM   6357  C  CE1   A TYR A 1 408 ? 10.627  -2.682  16.830  0.20 27.12  ? 408 TYR A CE1   1 
ATOM   6358  C  CE1   B TYR A 1 408 ? 10.965  -2.670  16.899  0.80 27.45  ? 408 TYR A CE1   1 
ATOM   6359  C  CE2   A TYR A 1 408 ? 8.296   -2.276  17.193  0.20 25.13  ? 408 TYR A CE2   1 
ATOM   6360  C  CE2   B TYR A 1 408 ? 8.690   -2.105  17.402  0.80 24.33  ? 408 TYR A CE2   1 
ATOM   6361  C  CZ    A TYR A 1 408 ? 9.466   -2.920  17.537  0.20 25.23  ? 408 TYR A CZ    1 
ATOM   6362  C  CZ    B TYR A 1 408 ? 9.828   -2.834  17.666  0.80 25.27  ? 408 TYR A CZ    1 
ATOM   6363  O  OH    A TYR A 1 408 ? 9.477   -3.807  18.591  0.20 27.44  ? 408 TYR A OH    1 
ATOM   6364  O  OH    B TYR A 1 408 ? 9.821   -3.745  18.705  0.80 28.48  ? 408 TYR A OH    1 
ATOM   6365  N  N     A VAL A 1 409 ? 10.084  0.949   11.398  0.20 32.30  ? 409 VAL A N     1 
ATOM   6366  N  N     B VAL A 1 409 ? 10.604  1.120   11.654  0.80 33.88  ? 409 VAL A N     1 
ATOM   6367  C  CA    A VAL A 1 409 ? 9.924   1.996   10.393  0.20 34.35  ? 409 VAL A CA    1 
ATOM   6368  C  CA    B VAL A 1 409 ? 10.557  2.112   10.586  0.80 38.81  ? 409 VAL A CA    1 
ATOM   6369  C  C     A VAL A 1 409 ? 9.485   1.408   9.058   0.20 33.95  ? 409 VAL A C     1 
ATOM   6370  C  C     B VAL A 1 409 ? 10.123  1.466   9.276   0.80 31.62  ? 409 VAL A C     1 
ATOM   6371  O  O     A VAL A 1 409 ? 8.772   2.061   8.286   0.20 35.10  ? 409 VAL A O     1 
ATOM   6372  O  O     B VAL A 1 409 ? 9.365   2.058   8.498   0.80 37.29  ? 409 VAL A O     1 
ATOM   6373  C  CB    A VAL A 1 409 ? 11.229  2.807   10.261  0.20 36.65  ? 409 VAL A CB    1 
ATOM   6374  C  CB    B VAL A 1 409 ? 11.923  2.817   10.470  0.80 40.11  ? 409 VAL A CB    1 
ATOM   6375  C  CG1   A VAL A 1 409 ? 11.049  3.966   9.291   0.20 34.97  ? 409 VAL A CG1   1 
ATOM   6376  C  CG1   B VAL A 1 409 ? 12.074  3.528   9.131   0.80 37.18  ? 409 VAL A CG1   1 
ATOM   6377  C  CG2   A VAL A 1 409 ? 11.668  3.319   11.628  0.20 35.57  ? 409 VAL A CG2   1 
ATOM   6378  C  CG2   B VAL A 1 409 ? 12.092  3.800   11.628  0.80 39.15  ? 409 VAL A CG2   1 
ATOM   6379  N  N     A GLY A 1 410 ? 9.876   0.171   8.770   0.20 31.84  ? 410 GLY A N     1 
ATOM   6380  N  N     B GLY A 1 410 ? 10.563  0.228   9.025   0.80 29.89  ? 410 GLY A N     1 
ATOM   6381  C  CA    A GLY A 1 410 ? 9.472   -0.475  7.541   0.20 34.30  ? 410 GLY A CA    1 
ATOM   6382  C  CA    B GLY A 1 410 ? 10.154  -0.472  7.817   0.80 32.87  ? 410 GLY A CA    1 
ATOM   6383  C  C     A GLY A 1 410 ? 8.037   -0.950  7.485   0.20 35.99  ? 410 GLY A C     1 
ATOM   6384  C  C     B GLY A 1 410 ? 8.683   -0.842  7.762   0.80 40.03  ? 410 GLY A C     1 
ATOM   6385  O  O     A GLY A 1 410 ? 7.611   -1.462  6.445   0.20 31.43  ? 410 GLY A O     1 
ATOM   6386  O  O     B GLY A 1 410 ? 8.201   -1.241  6.694   0.80 30.68  ? 410 GLY A O     1 
ATOM   6387  N  N     A GLU A 1 411 ? 7.272   -0.795  8.568   0.20 34.17  ? 411 GLU A N     1 
ATOM   6388  N  N     B GLU A 1 411 ? 7.967   -0.727  8.879   0.80 39.03  ? 411 GLU A N     1 
ATOM   6389  C  CA    A GLU A 1 411 ? 5.897   -1.279  8.603   0.20 34.66  ? 411 GLU A CA    1 
ATOM   6390  C  CA    B GLU A 1 411 ? 6.544   -1.028  8.945   0.80 32.81  ? 411 GLU A CA    1 
ATOM   6391  C  C     A GLU A 1 411 ? 4.919   -0.167  8.973   0.20 35.87  ? 411 GLU A C     1 
ATOM   6392  C  C     B GLU A 1 411 ? 5.717   0.244   9.124   0.80 36.02  ? 411 GLU A C     1 
ATOM   6393  O  O     A GLU A 1 411 ? 4.027   -0.369  9.804   0.20 37.30  ? 411 GLU A O     1 
ATOM   6394  O  O     B GLU A 1 411 ? 4.708   0.254   9.828   0.80 43.68  ? 411 GLU A O     1 
ATOM   6395  C  CB    A GLU A 1 411 ? 5.769   -2.447  9.585   0.20 34.72  ? 411 GLU A CB    1 
ATOM   6396  C  CB    B GLU A 1 411 ? 6.250   -2.022  10.069  0.80 34.42  ? 411 GLU A CB    1 
ATOM   6397  C  CG    A GLU A 1 411 ? 6.613   -3.668  9.239   0.20 33.31  ? 411 GLU A CG    1 
ATOM   6398  C  CG    B GLU A 1 411 ? 6.713   -3.451  9.807   0.80 32.56  ? 411 GLU A CG    1 
ATOM   6399  C  CD    A GLU A 1 411 ? 5.884   -4.666  8.358   0.20 35.66  ? 411 GLU A CD    1 
ATOM   6400  C  CD    B GLU A 1 411 ? 5.857   -4.185  8.791   0.80 37.21  ? 411 GLU A CD    1 
ATOM   6401  O  OE1   A GLU A 1 411 ? 4.736   -4.389  7.958   0.20 34.38  ? 411 GLU A OE1   1 
ATOM   6402  O  OE1   B GLU A 1 411 ? 4.859   -3.608  8.311   0.80 41.24  ? 411 GLU A OE1   1 
ATOM   6403  O  OE2   A GLU A 1 411 ? 6.455   -5.741  8.077   0.20 37.44  ? 411 GLU A OE2   1 
ATOM   6404  O  OE2   B GLU A 1 411 ? 6.164   -5.357  8.491   0.80 37.50  ? 411 GLU A OE2   1 
ATOM   6405  N  N     A GLY A 1 412 ? 5.082   1.007   8.368   0.20 36.29  ? 412 GLY A N     1 
ATOM   6406  N  N     B GLY A 1 412 ? 6.149   1.338   8.503   0.80 37.42  ? 412 GLY A N     1 
ATOM   6407  C  CA    A GLY A 1 412 ? 4.109   2.074   8.515   0.20 34.91  ? 412 GLY A CA    1 
ATOM   6408  C  CA    B GLY A 1 412 ? 5.336   2.538   8.450   0.80 44.94  ? 412 GLY A CA    1 
ATOM   6409  C  C     A GLY A 1 412 ? 4.283   2.962   9.727   0.20 37.71  ? 412 GLY A C     1 
ATOM   6410  C  C     B GLY A 1 412 ? 5.388   3.432   9.668   0.80 44.26  ? 412 GLY A C     1 
ATOM   6411  O  O     A GLY A 1 412 ? 3.305   3.550   10.198  0.20 33.30  ? 412 GLY A O     1 
ATOM   6412  O  O     B GLY A 1 412 ? 4.648   4.418   9.723   0.80 40.04  ? 412 GLY A O     1 
ATOM   6413  N  N     A MET A 1 413 ? 5.505   3.093   10.236  0.20 39.74  ? 413 MET A N     1 
ATOM   6414  N  N     B MET A 1 413 ? 6.227   3.121   10.646  0.80 40.46  ? 413 MET A N     1 
ATOM   6415  C  CA    A MET A 1 413 ? 5.774   3.841   11.453  0.20 39.56  ? 413 MET A CA    1 
ATOM   6416  C  CA    B MET A 1 413 ? 6.403   3.970   11.809  0.80 44.45  ? 413 MET A CA    1 
ATOM   6417  C  C     A MET A 1 413 ? 6.981   4.744   11.240  0.20 37.98  ? 413 MET A C     1 
ATOM   6418  C  C     B MET A 1 413 ? 7.520   4.971   11.554  0.80 35.89  ? 413 MET A C     1 
ATOM   6419  O  O     A MET A 1 413 ? 7.908   4.398   10.504  0.20 39.50  ? 413 MET A O     1 
ATOM   6420  O  O     B MET A 1 413 ? 8.498   4.671   10.865  0.80 44.47  ? 413 MET A O     1 
ATOM   6421  C  CB    A MET A 1 413 ? 6.016   2.886   12.633  0.20 35.65  ? 413 MET A CB    1 
ATOM   6422  C  CB    B MET A 1 413 ? 6.733   3.125   13.040  0.80 33.74  ? 413 MET A CB    1 
ATOM   6423  C  CG    A MET A 1 413 ? 6.263   3.562   13.967  0.20 40.41  ? 413 MET A CG    1 
ATOM   6424  C  CG    B MET A 1 413 ? 6.106   3.648   14.315  0.80 41.97  ? 413 MET A CG    1 
ATOM   6425  S  SD    A MET A 1 413 ? 6.512   2.355   15.279  0.20 37.52  ? 413 MET A SD    1 
ATOM   6426  S  SD    B MET A 1 413 ? 6.427   2.559   15.707  0.80 42.92  ? 413 MET A SD    1 
ATOM   6427  C  CE    A MET A 1 413 ? 6.962   3.430   16.637  0.20 32.93  ? 413 MET A CE    1 
ATOM   6428  C  CE    B MET A 1 413 ? 7.747   3.437   16.507  0.80 35.49  ? 413 MET A CE    1 
ATOM   6429  N  N     A GLU A 1 414 ? 6.960   5.909   11.882  0.20 39.05  ? 414 GLU A N     1 
ATOM   6430  N  N     B GLU A 1 414 ? 7.368   6.170   12.106  0.80 39.87  ? 414 GLU A N     1 
ATOM   6431  C  CA    A GLU A 1 414 ? 8.063   6.855   11.803  0.20 39.60  ? 414 GLU A CA    1 
ATOM   6432  C  CA    B GLU A 1 414 ? 8.440   7.154   12.058  0.80 36.67  ? 414 GLU A CA    1 
ATOM   6433  C  C     A GLU A 1 414 ? 9.011   6.670   12.982  0.20 39.68  ? 414 GLU A C     1 
ATOM   6434  C  C     B GLU A 1 414 ? 9.273   7.081   13.332  0.80 40.50  ? 414 GLU A C     1 
ATOM   6435  O  O     A GLU A 1 414 ? 8.605   6.264   14.074  0.20 38.89  ? 414 GLU A O     1 
ATOM   6436  O  O     B GLU A 1 414 ? 8.741   6.914   14.436  0.80 38.02  ? 414 GLU A O     1 
ATOM   6437  C  CB    A GLU A 1 414 ? 7.551   8.297   11.769  0.20 44.34  ? 414 GLU A CB    1 
ATOM   6438  C  CB    B GLU A 1 414 ? 7.891   8.567   11.859  0.80 42.77  ? 414 GLU A CB    1 
ATOM   6439  C  CG    A GLU A 1 414 ? 6.588   8.593   10.632  0.20 52.99  ? 414 GLU A CG    1 
ATOM   6440  C  CG    B GLU A 1 414 ? 7.421   8.852   10.441  0.80 56.73  ? 414 GLU A CG    1 
ATOM   6441  C  CD    A GLU A 1 414 ? 6.285   10.074  10.493  0.20 66.05  ? 414 GLU A CD    1 
ATOM   6442  C  CD    B GLU A 1 414 ? 6.858   10.255  10.273  0.80 67.63  ? 414 GLU A CD    1 
ATOM   6443  O  OE1   A GLU A 1 414 ? 7.113   10.896  10.937  0.20 65.49  ? 414 GLU A OE1   1 
ATOM   6444  O  OE1   B GLU A 1 414 ? 5.975   10.645  11.067  0.80 69.12  ? 414 GLU A OE1   1 
ATOM   6445  O  OE2   A GLU A 1 414 ? 5.217   10.415  9.940   0.20 67.41  ? 414 GLU A OE2   1 
ATOM   6446  O  OE2   B GLU A 1 414 ? 7.301   10.969  9.346   0.80 68.28  ? 414 GLU A OE2   1 
ATOM   6447  N  N     A GLU A 1 415 ? 10.289  6.977   12.746  0.20 37.55  ? 415 GLU A N     1 
ATOM   6448  N  N     B GLU A 1 415 ? 10.593  7.193   13.165  0.80 36.00  ? 415 GLU A N     1 
ATOM   6449  C  CA    A GLU A 1 415 ? 11.297  6.825   13.790  0.20 38.08  ? 415 GLU A CA    1 
ATOM   6450  C  CA    B GLU A 1 415 ? 11.521  7.046   14.282  0.80 38.51  ? 415 GLU A CA    1 
ATOM   6451  C  C     A GLU A 1 415 ? 11.072  7.801   14.940  0.20 39.71  ? 415 GLU A C     1 
ATOM   6452  C  C     B GLU A 1 415 ? 11.265  8.064   15.389  0.80 41.22  ? 415 GLU A C     1 
ATOM   6453  O  O     A GLU A 1 415 ? 11.466  7.518   16.078  0.20 39.11  ? 415 GLU A O     1 
ATOM   6454  O  O     B GLU A 1 415 ? 11.641  7.818   16.540  0.80 40.98  ? 415 GLU A O     1 
ATOM   6455  C  CB    A GLU A 1 415 ? 12.695  7.010   13.190  0.20 39.34  ? 415 GLU A CB    1 
ATOM   6456  C  CB    B GLU A 1 415 ? 12.967  7.164   13.773  0.80 42.54  ? 415 GLU A CB    1 
ATOM   6457  C  CG    A GLU A 1 415 ? 13.838  6.901   14.188  0.20 40.33  ? 415 GLU A CG    1 
ATOM   6458  C  CG    B GLU A 1 415 ? 14.021  6.837   14.823  0.80 37.48  ? 415 GLU A CG    1 
ATOM   6459  C  CD    A GLU A 1 415 ? 15.196  7.104   13.548  0.20 45.68  ? 415 GLU A CD    1 
ATOM   6460  C  CD    B GLU A 1 415 ? 15.431  6.822   14.271  0.80 48.93  ? 415 GLU A CD    1 
ATOM   6461  O  OE1   A GLU A 1 415 ? 15.466  6.477   12.500  0.20 43.76  ? 415 GLU A OE1   1 
ATOM   6462  O  OE1   B GLU A 1 415 ? 15.603  6.565   13.056  0.80 48.05  ? 415 GLU A OE1   1 
ATOM   6463  O  OE2   A GLU A 1 415 ? 15.994  7.896   14.092  0.20 44.29  ? 415 GLU A OE2   1 
ATOM   6464  O  OE2   B GLU A 1 415 ? 16.372  7.057   15.063  0.80 54.81  ? 415 GLU A OE2   1 
ATOM   6465  N  N     A GLY A 1 416 ? 10.433  8.942   14.671  0.20 35.91  ? 416 GLY A N     1 
ATOM   6466  N  N     B GLY A 1 416 ? 10.637  9.199   15.072  0.80 34.47  ? 416 GLY A N     1 
ATOM   6467  C  CA    A GLY A 1 416 ? 10.225  9.944   15.701  0.20 39.20  ? 416 GLY A CA    1 
ATOM   6468  C  CA    B GLY A 1 416 ? 10.319  10.178  16.095  0.80 40.36  ? 416 GLY A CA    1 
ATOM   6469  C  C     A GLY A 1 416 ? 9.259   9.526   16.790  0.20 35.23  ? 416 GLY A C     1 
ATOM   6470  C  C     B GLY A 1 416 ? 9.313   9.682   17.109  0.80 35.04  ? 416 GLY A C     1 
ATOM   6471  O  O     A GLY A 1 416 ? 9.272   10.120  17.873  0.20 39.29  ? 416 GLY A O     1 
ATOM   6472  O  O     B GLY A 1 416 ? 9.275   10.196  18.235  0.80 40.00  ? 416 GLY A O     1 
ATOM   6473  N  N     A GLU A 1 417 ? 8.422   8.519   16.529  0.20 34.67  ? 417 GLU A N     1 
ATOM   6474  N  N     B GLU A 1 417 ? 8.494   8.693   16.743  0.80 33.87  ? 417 GLU A N     1 
ATOM   6475  C  CA    A GLU A 1 417 ? 7.478   8.064   17.545  0.20 34.45  ? 417 GLU A CA    1 
ATOM   6476  C  CA    B GLU A 1 417 ? 7.569   8.118   17.717  0.80 33.90  ? 417 GLU A CA    1 
ATOM   6477  C  C     A GLU A 1 417 ? 8.191   7.388   18.710  0.20 34.78  ? 417 GLU A C     1 
ATOM   6478  C  C     B GLU A 1 417 ? 8.319   7.428   18.849  0.80 34.44  ? 417 GLU A C     1 
ATOM   6479  O  O     A GLU A 1 417 ? 7.684   7.402   19.839  0.20 38.94  ? 417 GLU A O     1 
ATOM   6480  O  O     B GLU A 1 417 ? 7.851   7.423   19.997  0.80 40.45  ? 417 GLU A O     1 
ATOM   6481  C  CB    A GLU A 1 417 ? 6.451   7.116   16.923  0.20 35.06  ? 417 GLU A CB    1 
ATOM   6482  C  CB    B GLU A 1 417 ? 6.609   7.145   17.033  0.80 34.34  ? 417 GLU A CB    1 
ATOM   6483  C  CG    A GLU A 1 417 ? 5.292   6.758   17.846  0.20 38.19  ? 417 GLU A CG    1 
ATOM   6484  C  CG    B GLU A 1 417 ? 5.681   6.411   18.004  0.80 39.99  ? 417 GLU A CG    1 
ATOM   6485  C  CD    A GLU A 1 417 ? 4.334   5.758   17.229  0.20 38.14  ? 417 GLU A CD    1 
ATOM   6486  C  CD    B GLU A 1 417 ? 4.399   5.935   17.356  0.80 37.86  ? 417 GLU A CD    1 
ATOM   6487  O  OE1   A GLU A 1 417 ? 4.497   5.433   16.033  0.20 37.13  ? 417 GLU A OE1   1 
ATOM   6488  O  OE1   B GLU A 1 417 ? 4.232   6.153   16.134  0.80 39.31  ? 417 GLU A OE1   1 
ATOM   6489  O  OE2   A GLU A 1 417 ? 3.417   5.294   17.942  0.20 40.98  ? 417 GLU A OE2   1 
ATOM   6490  O  OE2   B GLU A 1 417 ? 3.552   5.346   18.071  0.80 41.82  ? 417 GLU A OE2   1 
ATOM   6491  N  N     A PHE A 1 418 ? 9.361   6.794   18.459  0.20 35.23  ? 418 PHE A N     1 
ATOM   6492  N  N     B PHE A 1 418 ? 9.482   6.851   18.547  0.80 35.37  ? 418 PHE A N     1 
ATOM   6493  C  CA    A PHE A 1 418 ? 10.136  6.195   19.541  0.20 36.44  ? 418 PHE A CA    1 
ATOM   6494  C  CA    B PHE A 1 418 ? 10.339  6.289   19.587  0.80 37.21  ? 418 PHE A CA    1 
ATOM   6495  C  C     A PHE A 1 418 ? 10.576  7.244   20.555  0.20 36.14  ? 418 PHE A C     1 
ATOM   6496  C  C     B PHE A 1 418 ? 10.691  7.328   20.645  0.80 36.85  ? 418 PHE A C     1 
ATOM   6497  O  O     A PHE A 1 418 ? 10.532  7.003   21.767  0.20 31.41  ? 418 PHE A O     1 
ATOM   6498  O  O     B PHE A 1 418 ? 10.530  7.086   21.848  0.80 31.18  ? 418 PHE A O     1 
ATOM   6499  C  CB    A PHE A 1 418 ? 11.352  5.463   18.973  0.20 34.92  ? 418 PHE A CB    1 
ATOM   6500  C  CB    B PHE A 1 418 ? 11.614  5.728   18.960  0.80 34.16  ? 418 PHE A CB    1 
ATOM   6501  C  CG    A PHE A 1 418 ? 11.047  4.091   18.444  0.20 34.28  ? 418 PHE A CG    1 
ATOM   6502  C  CG    B PHE A 1 418 ? 11.506  4.298   18.532  0.80 34.95  ? 418 PHE A CG    1 
ATOM   6503  C  CD1   A PHE A 1 418 ? 11.129  2.984   19.271  0.20 33.08  ? 418 PHE A CD1   1 
ATOM   6504  C  CD1   B PHE A 1 418 ? 11.136  3.974   17.235  0.80 36.27  ? 418 PHE A CD1   1 
ATOM   6505  C  CD2   A PHE A 1 418 ? 10.688  3.907   17.119  0.20 35.27  ? 418 PHE A CD2   1 
ATOM   6506  C  CD2   B PHE A 1 418 ? 11.794  3.275   19.417  0.80 34.43  ? 418 PHE A CD2   1 
ATOM   6507  C  CE1   A PHE A 1 418 ? 10.856  1.718   18.790  0.20 29.68  ? 418 PHE A CE1   1 
ATOM   6508  C  CE1   B PHE A 1 418 ? 11.047  2.647   16.834  0.80 34.19  ? 418 PHE A CE1   1 
ATOM   6509  C  CE2   A PHE A 1 418 ? 10.412  2.643   16.631  0.20 32.07  ? 418 PHE A CE2   1 
ATOM   6510  C  CE2   B PHE A 1 418 ? 11.701  1.950   19.024  0.80 35.21  ? 418 PHE A CE2   1 
ATOM   6511  C  CZ    A PHE A 1 418 ? 10.497  1.548   17.467  0.20 31.44  ? 418 PHE A CZ    1 
ATOM   6512  C  CZ    B PHE A 1 418 ? 11.330  1.639   17.728  0.80 31.74  ? 418 PHE A CZ    1 
ATOM   6513  N  N     A SER A 1 419 ? 11.014  8.411   20.077  0.20 32.95  ? 419 SER A N     1 
ATOM   6514  N  N     B SER A 1 419 ? 11.218  8.478   20.218  0.80 31.73  ? 419 SER A N     1 
ATOM   6515  C  CA    A SER A 1 419 ? 11.476  9.455   20.987  0.20 32.83  ? 419 SER A CA    1 
ATOM   6516  C  CA    B SER A 1 419 ? 11.654  9.488   21.177  0.80 32.00  ? 419 SER A CA    1 
ATOM   6517  C  C     A SER A 1 419 ? 10.312  10.081  21.746  0.20 34.59  ? 419 SER A C     1 
ATOM   6518  C  C     B SER A 1 419 ? 10.470  10.079  21.933  0.80 35.29  ? 419 SER A C     1 
ATOM   6519  O  O     A SER A 1 419 ? 10.433  10.380  22.940  0.20 30.53  ? 419 SER A O     1 
ATOM   6520  O  O     B SER A 1 419 ? 10.579  10.383  23.125  0.80 29.41  ? 419 SER A O     1 
ATOM   6521  C  CB    A SER A 1 419 ? 12.249  10.523  20.214  0.20 34.16  ? 419 SER A CB    1 
ATOM   6522  C  CB    B SER A 1 419 ? 12.434  10.601  20.472  0.80 32.90  ? 419 SER A CB    1 
ATOM   6523  O  OG    A SER A 1 419 ? 13.347  9.956   19.518  0.20 44.57  ? 419 SER A OG    1 
ATOM   6524  O  OG    B SER A 1 419 ? 13.570  10.083  19.795  0.80 49.03  ? 419 SER A OG    1 
ATOM   6525  N  N     A GLU A 1 420 ? 9.179   10.290  21.071  0.20 31.00  ? 420 GLU A N     1 
ATOM   6526  N  N     B GLU A 1 420 ? 9.330   10.250  21.257  0.80 29.55  ? 420 GLU A N     1 
ATOM   6527  C  CA    A GLU A 1 420 ? 8.010   10.846  21.745  0.20 37.12  ? 420 GLU A CA    1 
ATOM   6528  C  CA    B GLU A 1 420 ? 8.176   10.840  21.928  0.80 38.15  ? 420 GLU A CA    1 
ATOM   6529  C  C     A GLU A 1 420 ? 7.487   9.895   22.815  0.20 34.39  ? 420 GLU A C     1 
ATOM   6530  C  C     B GLU A 1 420 ? 7.581   9.876   22.956  0.80 34.77  ? 420 GLU A C     1 
ATOM   6531  O  O     A GLU A 1 420 ? 7.106   10.328  23.910  0.20 32.86  ? 420 GLU A O     1 
ATOM   6532  O  O     B GLU A 1 420 ? 7.138   10.302  24.029  0.80 32.69  ? 420 GLU A O     1 
ATOM   6533  C  CB    A GLU A 1 420 ? 6.917   11.163  20.722  0.20 38.96  ? 420 GLU A CB    1 
ATOM   6534  C  CB    B GLU A 1 420 ? 7.134   11.283  20.893  0.80 39.58  ? 420 GLU A CB    1 
ATOM   6535  C  CG    A GLU A 1 420 ? 5.596   11.603  21.340  0.20 35.31  ? 420 GLU A CG    1 
ATOM   6536  C  CG    B GLU A 1 420 ? 6.200   10.193  20.375  0.80 40.04  ? 420 GLU A CG    1 
ATOM   6537  C  CD    A GLU A 1 420 ? 4.519   11.865  20.304  0.20 41.56  ? 420 GLU A CD    1 
ATOM   6538  C  CD    B GLU A 1 420 ? 5.039   10.745  19.552  0.80 51.99  ? 420 GLU A CD    1 
ATOM   6539  O  OE1   A GLU A 1 420 ? 4.857   12.324  19.192  0.20 49.92  ? 420 GLU A OE1   1 
ATOM   6540  O  OE1   B GLU A 1 420 ? 5.218   11.786  18.879  0.80 54.37  ? 420 GLU A OE1   1 
ATOM   6541  O  OE2   A GLU A 1 420 ? 3.334   11.606  20.599  0.20 36.80  ? 420 GLU A OE2   1 
ATOM   6542  O  OE2   B GLU A 1 420 ? 3.944   10.141  19.584  0.80 43.61  ? 420 GLU A OE2   1 
ATOM   6543  N  N     A ALA A 1 421 ? 7.473   8.592   22.523  0.20 31.00  ? 421 ALA A N     1 
ATOM   6544  N  N     B ALA A 1 421 ? 7.601   8.569   22.671  0.80 30.28  ? 421 ALA A N     1 
ATOM   6545  C  CA    A ALA A 1 421 ? 7.009   7.620   23.506  0.20 32.90  ? 421 ALA A CA    1 
ATOM   6546  C  CA    B ALA A 1 421 ? 7.132   7.600   23.657  0.80 33.16  ? 421 ALA A CA    1 
ATOM   6547  C  C     A ALA A 1 421 ? 7.949   7.547   24.702  0.20 32.06  ? 421 ALA A C     1 
ATOM   6548  C  C     B ALA A 1 421 ? 8.057   7.557   24.864  0.80 32.42  ? 421 ALA A C     1 
ATOM   6549  O  O     A ALA A 1 421 ? 7.500   7.358   25.839  0.20 31.00  ? 421 ALA A O     1 
ATOM   6550  O  O     B ALA A 1 421 ? 7.591   7.459   26.006  0.80 30.91  ? 421 ALA A O     1 
ATOM   6551  C  CB    A ALA A 1 421 ? 6.862   6.243   22.857  0.20 25.89  ? 421 ALA A CB    1 
ATOM   6552  C  CB    B ALA A 1 421 ? 7.003   6.210   23.023  0.80 24.16  ? 421 ALA A CB    1 
ATOM   6553  N  N     A ARG A 1 422 ? 9.256   7.696   24.471  0.20 29.19  ? 422 ARG A N     1 
ATOM   6554  N  N     B ARG A 1 422 ? 9.372   7.624   24.638  0.80 28.35  ? 422 ARG A N     1 
ATOM   6555  C  CA    A ARG A 1 422 ? 10.214  7.564   25.565  0.20 31.48  ? 422 ARG A CA    1 
ATOM   6556  C  CA    B ARG A 1 422 ? 10.304  7.590   25.760  0.80 31.65  ? 422 ARG A CA    1 
ATOM   6557  C  C     A ARG A 1 422 ? 10.115  8.733   26.537  0.20 32.14  ? 422 ARG A C     1 
ATOM   6558  C  C     B ARG A 1 422 ? 10.203  8.856   26.599  0.80 32.32  ? 422 ARG A C     1 
ATOM   6559  O  O     A ARG A 1 422 ? 10.198  8.541   27.755  0.20 30.67  ? 422 ARG A O     1 
ATOM   6560  O  O     B ARG A 1 422 ? 10.369  8.804   27.822  0.80 30.60  ? 422 ARG A O     1 
ATOM   6561  C  CB    A ARG A 1 422 ? 11.635  7.442   25.011  0.20 30.97  ? 422 ARG A CB    1 
ATOM   6562  C  CB    B ARG A 1 422 ? 11.733  7.394   25.249  0.80 31.33  ? 422 ARG A CB    1 
ATOM   6563  C  CG    A ARG A 1 422 ? 12.711  7.288   26.083  0.20 30.93  ? 422 ARG A CG    1 
ATOM   6564  C  CG    B ARG A 1 422 ? 12.814  7.390   26.339  0.80 30.56  ? 422 ARG A CG    1 
ATOM   6565  C  CD    A ARG A 1 422 ? 12.418  6.110   27.004  0.20 30.54  ? 422 ARG A CD    1 
ATOM   6566  C  CD    B ARG A 1 422 ? 12.628  6.237   27.325  0.80 31.17  ? 422 ARG A CD    1 
ATOM   6567  N  NE    A ARG A 1 422 ? 13.460  5.917   28.008  0.20 31.95  ? 422 ARG A NE    1 
ATOM   6568  N  NE    B ARG A 1 422 ? 13.584  6.286   28.430  0.80 34.60  ? 422 ARG A NE    1 
ATOM   6569  C  CZ    A ARG A 1 422 ? 13.454  6.468   29.214  0.20 32.30  ? 422 ARG A CZ    1 
ATOM   6570  C  CZ    B ARG A 1 422 ? 13.383  6.926   29.576  0.80 32.59  ? 422 ARG A CZ    1 
ATOM   6571  N  NH1   A ARG A 1 422 ? 12.467  7.254   29.611  0.20 31.34  ? 422 ARG A NH1   1 
ATOM   6572  N  NH1   B ARG A 1 422 ? 12.260  7.581   29.817  0.80 30.92  ? 422 ARG A NH1   1 
ATOM   6573  N  NH2   A ARG A 1 422 ? 14.464  6.223   30.044  0.20 29.28  ? 422 ARG A NH2   1 
ATOM   6574  N  NH2   B ARG A 1 422 ? 14.325  6.894   30.510  0.80 28.45  ? 422 ARG A NH2   1 
ATOM   6575  N  N     A GLU A 1 423 ? 9.945   9.953   26.020  0.20 30.75  ? 423 GLU A N     1 
ATOM   6576  N  N     B GLU A 1 423 ? 9.945   9.991   25.949  0.80 30.78  ? 423 GLU A N     1 
ATOM   6577  C  CA    A GLU A 1 423 ? 9.803   11.109  26.898  0.20 32.48  ? 423 GLU A CA    1 
ATOM   6578  C  CA    B GLU A 1 423 ? 9.740   11.255  26.646  0.80 31.97  ? 423 GLU A CA    1 
ATOM   6579  C  C     A GLU A 1 423 ? 8.466   11.095  27.629  0.20 33.97  ? 423 GLU A C     1 
ATOM   6580  C  C     B GLU A 1 423 ? 8.488   11.201  27.517  0.80 34.28  ? 423 GLU A C     1 
ATOM   6581  O  O     A GLU A 1 423 ? 8.347   11.686  28.708  0.20 31.60  ? 423 GLU A O     1 
ATOM   6582  O  O     B GLU A 1 423 ? 8.452   11.786  28.604  0.80 31.12  ? 423 GLU A O     1 
ATOM   6583  C  CB    A GLU A 1 423 ? 9.962   12.401  26.097  0.20 35.32  ? 423 GLU A CB    1 
ATOM   6584  C  CB    B GLU A 1 423 ? 9.653   12.380  25.607  0.80 35.60  ? 423 GLU A CB    1 
ATOM   6585  C  CG    A GLU A 1 423 ? 11.325  12.563  25.448  0.20 35.54  ? 423 GLU A CG    1 
ATOM   6586  C  CG    B GLU A 1 423 ? 9.502   13.801  26.139  0.80 52.06  ? 423 GLU A CG    1 
ATOM   6587  C  CD    A GLU A 1 423 ? 11.434  13.831  24.629  0.20 37.47  ? 423 GLU A CD    1 
ATOM   6588  C  CD    B GLU A 1 423 ? 9.381   14.839  25.013  0.80 57.92  ? 423 GLU A CD    1 
ATOM   6589  O  OE1   A GLU A 1 423 ? 10.522  14.679  24.723  0.20 44.19  ? 423 GLU A OE1   1 
ATOM   6590  O  OE1   B GLU A 1 423 ? 9.085   14.449  23.860  0.80 57.97  ? 423 GLU A OE1   1 
ATOM   6591  O  OE2   A GLU A 1 423 ? 12.428  13.981  23.888  0.20 35.27  ? 423 GLU A OE2   1 
ATOM   6592  O  OE2   B GLU A 1 423 ? 9.584   16.045  25.281  0.80 62.16  ? 423 GLU A OE2   1 
ATOM   6593  N  N     A ASP A 1 424 ? 7.453   10.436  27.060  0.20 34.48  ? 424 ASP A N     1 
ATOM   6594  N  N     B ASP A 1 424 ? 7.452   10.492  27.057  0.80 34.75  ? 424 ASP A N     1 
ATOM   6595  C  CA    A ASP A 1 424 ? 6.193   10.266  27.775  0.20 33.74  ? 424 ASP A CA    1 
ATOM   6596  C  CA    B ASP A 1 424 ? 6.241   10.336  27.858  0.80 33.80  ? 424 ASP A CA    1 
ATOM   6597  C  C     A ASP A 1 424 ? 6.385   9.383   29.002  0.20 32.13  ? 424 ASP A C     1 
ATOM   6598  C  C     B ASP A 1 424 ? 6.530   9.522   29.116  0.80 32.39  ? 424 ASP A C     1 
ATOM   6599  O  O     A ASP A 1 424 ? 5.822   9.658   30.069  0.20 32.95  ? 424 ASP A O     1 
ATOM   6600  O  O     B ASP A 1 424 ? 6.070   9.875   30.211  0.80 32.54  ? 424 ASP A O     1 
ATOM   6601  C  CB    A ASP A 1 424 ? 5.136   9.679   26.836  0.20 31.74  ? 424 ASP A CB    1 
ATOM   6602  C  CB    B ASP A 1 424 ? 5.148   9.685   27.001  0.80 31.57  ? 424 ASP A CB    1 
ATOM   6603  C  CG    A ASP A 1 424 ? 3.737   9.696   27.434  0.20 34.90  ? 424 ASP A CG    1 
ATOM   6604  C  CG    B ASP A 1 424 ? 3.731   9.926   27.531  0.80 35.65  ? 424 ASP A CG    1 
ATOM   6605  O  OD1   A ASP A 1 424 ? 3.528   10.349  28.479  0.20 33.00  ? 424 ASP A OD1   1 
ATOM   6606  O  OD1   B ASP A 1 424 ? 3.534   10.756  28.439  0.80 33.21  ? 424 ASP A OD1   1 
ATOM   6607  O  OD2   A ASP A 1 424 ? 2.841   9.050   26.851  0.20 32.76  ? 424 ASP A OD2   1 
ATOM   6608  O  OD2   B ASP A 1 424 ? 2.804   9.270   27.015  0.80 32.97  ? 424 ASP A OD2   1 
ATOM   6609  N  N     A MET A 1 425 ? 7.188   8.324   28.873  0.20 31.31  ? 425 MET A N     1 
ATOM   6610  N  N     B MET A 1 425 ? 7.322   8.453   28.988  0.80 31.54  ? 425 MET A N     1 
ATOM   6611  C  CA    A MET A 1 425 ? 7.531   7.510   30.035  0.20 28.27  ? 425 MET A CA    1 
ATOM   6612  C  CA    B MET A 1 425 ? 7.698   7.658   30.158  0.80 27.06  ? 425 MET A CA    1 
ATOM   6613  C  C     A MET A 1 425 ? 8.461   8.256   30.982  0.20 28.28  ? 425 MET A C     1 
ATOM   6614  C  C     B MET A 1 425 ? 8.559   8.455   31.132  0.80 26.64  ? 425 MET A C     1 
ATOM   6615  O  O     A MET A 1 425 ? 8.406   8.040   32.198  0.20 32.42  ? 425 MET A O     1 
ATOM   6616  O  O     B MET A 1 425 ? 8.480   8.244   32.348  0.80 32.79  ? 425 MET A O     1 
ATOM   6617  C  CB    A MET A 1 425 ? 8.177   6.198   29.591  0.20 30.98  ? 425 MET A CB    1 
ATOM   6618  C  CB    B MET A 1 425 ? 8.444   6.394   29.730  0.80 31.79  ? 425 MET A CB    1 
ATOM   6619  C  CG    A MET A 1 425 ? 7.467   5.517   28.438  0.20 29.91  ? 425 MET A CG    1 
ATOM   6620  C  CG    B MET A 1 425 ? 7.669   5.478   28.820  0.80 28.74  ? 425 MET A CG    1 
ATOM   6621  S  SD    A MET A 1 425 ? 5.780   5.042   28.838  0.20 26.03  ? 425 MET A SD    1 
ATOM   6622  S  SD    B MET A 1 425 ? 6.158   4.937   29.598  0.80 32.90  ? 425 MET A SD    1 
ATOM   6623  C  CE    A MET A 1 425 ? 6.088   3.769   30.060  0.20 30.10  ? 425 MET A CE    1 
ATOM   6624  C  CE    B MET A 1 425 ? 6.823   4.239   31.111  0.80 31.84  ? 425 MET A CE    1 
ATOM   6625  N  N     A ALA A 1 426 ? 9.334   9.114   30.446  0.20 32.22  ? 426 ALA A N     1 
ATOM   6626  N  N     B ALA A 1 426 ? 9.455   9.308   30.618  0.80 32.55  ? 426 ALA A N     1 
ATOM   6627  C  CA    A ALA A 1 426 ? 10.184  9.935   31.302  0.20 30.98  ? 426 ALA A CA    1 
ATOM   6628  C  CA    B ALA A 1 426 ? 10.206  10.201  31.497  0.80 30.93  ? 426 ALA A CA    1 
ATOM   6629  C  C     A ALA A 1 426 ? 9.347   10.865  32.170  0.20 33.39  ? 426 ALA A C     1 
ATOM   6630  C  C     B ALA A 1 426 ? 9.258   11.072  32.312  0.80 33.83  ? 426 ALA A C     1 
ATOM   6631  O  O     A ALA A 1 426 ? 9.598   10.998  33.374  0.20 34.04  ? 426 ALA A O     1 
ATOM   6632  O  O     B ALA A 1 426 ? 9.412   11.211  33.533  0.80 34.55  ? 426 ALA A O     1 
ATOM   6633  C  CB    A ALA A 1 426 ? 11.170  10.738  30.455  0.20 29.23  ? 426 ALA A CB    1 
ATOM   6634  C  CB    B ALA A 1 426 ? 11.163  11.070  30.683  0.80 27.24  ? 426 ALA A CB    1 
ATOM   6635  N  N     A ALA A 1 427 ? 8.340   11.511  31.576  0.20 32.64  ? 427 ALA A N     1 
ATOM   6636  N  N     B ALA A 1 427 ? 8.254   11.649  31.647  0.80 32.85  ? 427 ALA A N     1 
ATOM   6637  C  CA    A ALA A 1 427 ? 7.438   12.352  32.354  0.20 33.08  ? 427 ALA A CA    1 
ATOM   6638  C  CA    B ALA A 1 427 ? 7.258   12.451  32.349  0.80 33.17  ? 427 ALA A CA    1 
ATOM   6639  C  C     A ALA A 1 427 ? 6.595   11.530  33.318  0.20 33.20  ? 427 ALA A C     1 
ATOM   6640  C  C     B ALA A 1 427 ? 6.476   11.618  33.356  0.80 33.43  ? 427 ALA A C     1 
ATOM   6641  O  O     A ALA A 1 427 ? 6.175   12.044  34.361  0.20 33.50  ? 427 ALA A O     1 
ATOM   6642  O  O     B ALA A 1 427 ? 6.147   12.107  34.443  0.80 33.22  ? 427 ALA A O     1 
ATOM   6643  C  CB    A ALA A 1 427 ? 6.539   13.163  31.421  0.20 29.82  ? 427 ALA A CB    1 
ATOM   6644  C  CB    B ALA A 1 427 ? 6.305   13.101  31.347  0.80 28.85  ? 427 ALA A CB    1 
ATOM   6645  N  N     A LEU A 1 428 ? 6.330   10.262  32.989  0.20 30.43  ? 428 LEU A N     1 
ATOM   6646  N  N     B LEU A 1 428 ? 6.145   10.367  33.010  0.80 30.20  ? 428 LEU A N     1 
ATOM   6647  C  CA    A LEU A 1 428 ? 5.595   9.401   33.912  0.20 32.99  ? 428 LEU A CA    1 
ATOM   6648  C  CA    B LEU A 1 428 ? 5.376   9.533   33.936  0.80 32.65  ? 428 LEU A CA    1 
ATOM   6649  C  C     A LEU A 1 428 ? 6.426   9.098   35.151  0.20 33.46  ? 428 LEU A C     1 
ATOM   6650  C  C     B LEU A 1 428 ? 6.194   9.206   35.176  0.80 33.68  ? 428 LEU A C     1 
ATOM   6651  O  O     A LEU A 1 428 ? 5.895   9.051   36.267  0.20 32.25  ? 428 LEU A O     1 
ATOM   6652  O  O     B LEU A 1 428 ? 5.685   9.276   36.300  0.80 31.56  ? 428 LEU A O     1 
ATOM   6653  C  CB    A LEU A 1 428 ? 5.180   8.107   33.211  0.20 30.54  ? 428 LEU A CB    1 
ATOM   6654  C  CB    B LEU A 1 428 ? 4.915   8.249   33.245  0.80 28.69  ? 428 LEU A CB    1 
ATOM   6655  C  CG    A LEU A 1 428 ? 4.374   7.098   34.030  0.20 35.10  ? 428 LEU A CG    1 
ATOM   6656  C  CG    B LEU A 1 428 ? 4.031   7.270   34.017  0.80 37.30  ? 428 LEU A CG    1 
ATOM   6657  C  CD1   A LEU A 1 428 ? 3.015   7.670   34.403  0.20 32.92  ? 428 LEU A CD1   1 
ATOM   6658  C  CD1   B LEU A 1 428 ? 2.707   7.916   34.340  0.80 33.08  ? 428 LEU A CD1   1 
ATOM   6659  C  CD2   A LEU A 1 428 ? 4.220   5.792   33.267  0.20 33.21  ? 428 LEU A CD2   1 
ATOM   6660  C  CD2   B LEU A 1 428 ? 3.819   6.004   33.218  0.80 34.61  ? 428 LEU A CD2   1 
ATOM   6661  N  N     A GLU A 1 429 ? 7.736   8.895   34.975  0.20 31.22  ? 429 GLU A N     1 
ATOM   6662  N  N     B GLU A 1 429 ? 7.473   8.866   34.990  0.80 29.97  ? 429 GLU A N     1 
ATOM   6663  C  CA    A GLU A 1 429 ? 8.617   8.722   36.125  0.20 33.61  ? 429 GLU A CA    1 
ATOM   6664  C  CA    B GLU A 1 429 ? 8.348   8.626   36.133  0.80 33.11  ? 429 GLU A CA    1 
ATOM   6665  C  C     A GLU A 1 429 ? 8.695   9.990   36.965  0.20 34.90  ? 429 GLU A C     1 
ATOM   6666  C  C     B GLU A 1 429 ? 8.418   9.853   37.036  0.80 35.83  ? 429 GLU A C     1 
ATOM   6667  O  O     A GLU A 1 429 ? 8.987   9.920   38.164  0.20 33.89  ? 429 GLU A O     1 
ATOM   6668  O  O     B GLU A 1 429 ? 8.319   9.735   38.264  0.80 29.82  ? 429 GLU A O     1 
ATOM   6669  C  CB    A GLU A 1 429 ? 10.016  8.304   35.665  0.20 36.02  ? 429 GLU A CB    1 
ATOM   6670  C  CB    B GLU A 1 429 ? 9.749   8.220   35.655  0.80 36.78  ? 429 GLU A CB    1 
ATOM   6671  C  CG    A GLU A 1 429 ? 10.090  6.910   35.050  0.20 36.28  ? 429 GLU A CG    1 
ATOM   6672  C  CG    B GLU A 1 429 ? 9.853   6.810   35.039  0.80 36.63  ? 429 GLU A CG    1 
ATOM   6673  C  CD    A GLU A 1 429 ? 11.521  6.449   34.812  0.20 38.30  ? 429 GLU A CD    1 
ATOM   6674  C  CD    B GLU A 1 429 ? 11.274  6.227   35.120  0.80 38.69  ? 429 GLU A CD    1 
ATOM   6675  O  OE1   A GLU A 1 429 ? 12.452  7.080   35.362  0.20 34.14  ? 429 GLU A OE1   1 
ATOM   6676  O  OE1   B GLU A 1 429 ? 11.834  6.162   36.232  0.80 36.20  ? 429 GLU A OE1   1 
ATOM   6677  O  OE2   A GLU A 1 429 ? 11.716  5.458   34.073  0.20 36.72  ? 429 GLU A OE2   1 
ATOM   6678  O  OE2   B GLU A 1 429 ? 11.848  5.841   34.072  0.80 39.56  ? 429 GLU A OE2   1 
ATOM   6679  N  N     A LYS A 1 430 ? 8.438   11.151  36.362  0.20 31.96  ? 430 LYS A N     1 
ATOM   6680  N  N     B LYS A 1 430 ? 8.562   11.043  36.444  0.80 30.91  ? 430 LYS A N     1 
ATOM   6681  C  CA    A LYS A 1 430 ? 8.401   12.395  37.119  0.20 35.74  ? 430 LYS A CA    1 
ATOM   6682  C  CA    B LYS A 1 430 ? 8.555   12.273  37.232  0.80 35.34  ? 430 LYS A CA    1 
ATOM   6683  C  C     A LYS A 1 430 ? 7.043   12.642  37.761  0.20 36.39  ? 430 LYS A C     1 
ATOM   6684  C  C     B LYS A 1 430 ? 7.214   12.497  37.930  0.80 37.31  ? 430 LYS A C     1 
ATOM   6685  O  O     A LYS A 1 430 ? 6.957   13.426  38.712  0.20 35.54  ? 430 LYS A O     1 
ATOM   6686  O  O     B LYS A 1 430 ? 7.188   13.026  39.048  0.80 35.08  ? 430 LYS A O     1 
ATOM   6687  C  CB    A LYS A 1 430 ? 8.774   13.574  36.218  0.20 40.41  ? 430 LYS A CB    1 
ATOM   6688  C  CB    B LYS A 1 430 ? 8.909   13.467  36.341  0.80 41.12  ? 430 LYS A CB    1 
ATOM   6689  C  CG    A LYS A 1 430 ? 10.028  13.344  35.388  0.20 36.26  ? 430 LYS A CG    1 
ATOM   6690  C  CG    B LYS A 1 430 ? 9.213   14.749  37.103  0.80 43.87  ? 430 LYS A CG    1 
ATOM   6691  C  CD    A LYS A 1 430 ? 11.197  12.884  36.245  0.20 42.67  ? 430 LYS A CD    1 
ATOM   6692  C  CD    B LYS A 1 430 ? 9.920   15.781  36.220  0.80 66.25  ? 430 LYS A CD    1 
ATOM   6693  C  CE    A LYS A 1 430 ? 12.398  12.508  35.388  0.20 34.45  ? 430 LYS A CE    1 
ATOM   6694  C  CE    B LYS A 1 430 ? 9.109   16.125  34.970  0.80 68.81  ? 430 LYS A CE    1 
ATOM   6695  N  NZ    A LYS A 1 430 ? 12.113  11.361  34.477  0.20 29.01  ? 430 LYS A NZ    1 
ATOM   6696  N  NZ    B LYS A 1 430 ? 9.773   17.183  34.141  0.80 52.43  ? 430 LYS A NZ    1 
ATOM   6697  N  N     A ASP A 1 431 ? 5.984   11.998  37.265  0.20 33.16  ? 431 ASP A N     1 
ATOM   6698  N  N     B ASP A 1 431 ? 6.098   12.106  37.300  0.80 32.77  ? 431 ASP A N     1 
ATOM   6699  C  CA    A ASP A 1 431 ? 4.687   12.087  37.932  0.20 31.92  ? 431 ASP A CA    1 
ATOM   6700  C  CA    B ASP A 1 431 ? 4.795   12.199  37.971  0.80 31.48  ? 431 ASP A CA    1 
ATOM   6701  C  C     A ASP A 1 431 ? 4.723   11.400  39.292  0.20 31.63  ? 431 ASP A C     1 
ATOM   6702  C  C     B ASP A 1 431 ? 4.793   11.444  39.295  0.80 31.23  ? 431 ASP A C     1 
ATOM   6703  O  O     A ASP A 1 431 ? 4.140   11.900  40.262  0.20 37.93  ? 431 ASP A O     1 
ATOM   6704  O  O     B ASP A 1 431 ? 4.241   11.925  40.295  0.80 38.15  ? 431 ASP A O     1 
ATOM   6705  C  CB    A ASP A 1 431 ? 3.598   11.474  37.051  0.20 31.10  ? 431 ASP A CB    1 
ATOM   6706  C  CB    B ASP A 1 431 ? 3.686   11.666  37.059  0.80 30.54  ? 431 ASP A CB    1 
ATOM   6707  C  CG    A ASP A 1 431 ? 3.397   12.234  35.754  0.20 35.13  ? 431 ASP A CG    1 
ATOM   6708  C  CG    B ASP A 1 431 ? 3.434   12.561  35.863  0.80 35.98  ? 431 ASP A CG    1 
ATOM   6709  O  OD1   A ASP A 1 431 ? 3.389   13.482  35.788  0.20 32.73  ? 431 ASP A OD1   1 
ATOM   6710  O  OD1   B ASP A 1 431 ? 4.025   13.654  35.822  0.80 35.93  ? 431 ASP A OD1   1 
ATOM   6711  O  OD2   A ASP A 1 431 ? 3.245   11.583  34.699  0.20 32.06  ? 431 ASP A OD2   1 
ATOM   6712  O  OD2   B ASP A 1 431 ? 2.651   12.178  34.966  0.80 35.89  ? 431 ASP A OD2   1 
ATOM   6713  N  N     A TYR A 1 432 ? 5.403   10.254  39.383  0.20 33.35  ? 432 TYR A N     1 
ATOM   6714  N  N     B TYR A 1 432 ? 5.407   10.260  39.326  0.80 33.14  ? 432 TYR A N     1 
ATOM   6715  C  CA    A TYR A 1 432 ? 5.526   9.567   40.663  0.20 33.76  ? 432 TYR A CA    1 
ATOM   6716  C  CA    B TYR A 1 432 ? 5.520   9.522   40.579  0.80 33.61  ? 432 TYR A CA    1 
ATOM   6717  C  C     A TYR A 1 432 ? 6.465   10.304  41.609  0.20 40.17  ? 432 TYR A C     1 
ATOM   6718  C  C     B TYR A 1 432 ? 6.461   10.227  41.547  0.80 40.33  ? 432 TYR A C     1 
ATOM   6719  O  O     A TYR A 1 432 ? 6.295   10.226  42.831  0.20 39.74  ? 432 TYR A O     1 
ATOM   6720  O  O     B TYR A 1 432 ? 6.214   10.238  42.760  0.80 39.39  ? 432 TYR A O     1 
ATOM   6721  C  CB    A TYR A 1 432 ? 6.008   8.132   40.448  0.20 34.78  ? 432 TYR A CB    1 
ATOM   6722  C  CB    B TYR A 1 432 ? 5.986   8.092   40.308  0.80 34.85  ? 432 TYR A CB    1 
ATOM   6723  C  CG    A TYR A 1 432 ? 4.972   7.222   39.826  0.20 32.52  ? 432 TYR A CG    1 
ATOM   6724  C  CG    B TYR A 1 432 ? 4.905   7.234   39.689  0.80 32.30  ? 432 TYR A CG    1 
ATOM   6725  C  CD1   A TYR A 1 432 ? 3.989   6.627   40.607  0.20 34.96  ? 432 TYR A CD1   1 
ATOM   6726  C  CD1   B TYR A 1 432 ? 3.824   6.811   40.456  0.80 36.07  ? 432 TYR A CD1   1 
ATOM   6727  C  CD2   A TYR A 1 432 ? 4.979   6.952   38.461  0.20 33.08  ? 432 TYR A CD2   1 
ATOM   6728  C  CD2   B TYR A 1 432 ? 4.956   6.849   38.346  0.80 32.94  ? 432 TYR A CD2   1 
ATOM   6729  C  CE1   A TYR A 1 432 ? 3.039   5.795   40.050  0.20 32.33  ? 432 TYR A CE1   1 
ATOM   6730  C  CE1   B TYR A 1 432 ? 2.824   6.041   39.924  0.80 31.88  ? 432 TYR A CE1   1 
ATOM   6731  C  CE2   A TYR A 1 432 ? 4.028   6.117   37.893  0.20 33.24  ? 432 TYR A CE2   1 
ATOM   6732  C  CE2   B TYR A 1 432 ? 3.937   6.061   37.792  0.80 33.12  ? 432 TYR A CE2   1 
ATOM   6733  C  CZ    A TYR A 1 432 ? 3.062   5.541   38.695  0.20 33.94  ? 432 TYR A CZ    1 
ATOM   6734  C  CZ    B TYR A 1 432 ? 2.874   5.661   38.599  0.80 34.49  ? 432 TYR A CZ    1 
ATOM   6735  O  OH    A TYR A 1 432 ? 2.111   4.711   38.146  0.20 32.85  ? 432 TYR A OH    1 
ATOM   6736  O  OH    B TYR A 1 432 ? 1.843   4.890   38.104  0.80 33.20  ? 432 TYR A OH    1 
ATOM   6737  N  N     A GLU A 1 433 ? 7.453   11.024  41.070  0.20 36.67  ? 433 GLU A N     1 
ATOM   6738  N  N     B GLU A 1 433 ? 7.529   10.839  41.029  0.80 35.69  ? 433 GLU A N     1 
ATOM   6739  C  CA    A GLU A 1 433 ? 8.368   11.771  41.927  0.20 41.18  ? 433 GLU A CA    1 
ATOM   6740  C  CA    B GLU A 1 433 ? 8.498   11.501  41.901  0.80 41.63  ? 433 GLU A CA    1 
ATOM   6741  C  C     A GLU A 1 433 ? 7.713   13.023  42.498  0.20 39.19  ? 433 GLU A C     1 
ATOM   6742  C  C     B GLU A 1 433 ? 7.862   12.659  42.660  0.80 40.03  ? 433 GLU A C     1 
ATOM   6743  O  O     A GLU A 1 433 ? 8.021   13.419  43.628  0.20 43.01  ? 433 GLU A O     1 
ATOM   6744  O  O     B GLU A 1 433 ? 7.992   12.752  43.887  0.80 43.93  ? 433 GLU A O     1 
ATOM   6745  C  CB    A GLU A 1 433 ? 9.634   12.139  41.153  0.20 38.77  ? 433 GLU A CB    1 
ATOM   6746  C  CB    B GLU A 1 433 ? 9.702   11.982  41.092  0.80 38.04  ? 433 GLU A CB    1 
ATOM   6747  C  CG    A GLU A 1 433 ? 10.498  10.948  40.776  0.20 46.90  ? 433 GLU A CG    1 
ATOM   6748  C  CG    B GLU A 1 433 ? 10.589  10.852  40.609  0.80 47.30  ? 433 GLU A CG    1 
ATOM   6749  C  CD    A GLU A 1 433 ? 11.715  11.343  39.963  0.20 57.37  ? 433 GLU A CD    1 
ATOM   6750  C  CD    B GLU A 1 433 ? 11.941  11.336  40.128  0.80 59.61  ? 433 GLU A CD    1 
ATOM   6751  O  OE1   A GLU A 1 433 ? 11.982  12.557  39.840  0.20 56.56  ? 433 GLU A OE1   1 
ATOM   6752  O  OE1   B GLU A 1 433 ? 12.104  12.561  39.935  0.80 56.99  ? 433 GLU A OE1   1 
ATOM   6753  O  OE2   A GLU A 1 433 ? 12.404  10.439  39.443  0.20 60.44  ? 433 GLU A OE2   1 
ATOM   6754  O  OE2   B GLU A 1 433 ? 12.844  10.489  39.946  0.80 67.82  ? 433 GLU A OE2   1 
ATOM   6755  N  N     A GLU A 1 434 ? 6.810   13.655  41.743  0.20 36.52  ? 434 GLU A N     1 
ATOM   6756  N  N     B GLU A 1 434 ? 7.164   13.551  41.947  0.80 32.81  ? 434 GLU A N     1 
ATOM   6757  C  CA    A GLU A 1 434 ? 6.150   14.860  42.237  0.20 37.52  ? 434 GLU A CA    1 
ATOM   6758  C  CA    B GLU A 1 434 ? 6.513   14.686  42.602  0.80 35.27  ? 434 GLU A CA    1 
ATOM   6759  C  C     A GLU A 1 434 ? 5.149   14.546  43.341  0.20 43.00  ? 434 GLU A C     1 
ATOM   6760  C  C     B GLU A 1 434 ? 5.604   14.231  43.739  0.80 45.50  ? 434 GLU A C     1 
ATOM   6761  O  O     A GLU A 1 434 ? 4.900   15.392  44.207  0.20 41.55  ? 434 GLU A O     1 
ATOM   6762  O  O     B GLU A 1 434 ? 5.627   14.812  44.830  0.80 48.65  ? 434 GLU A O     1 
ATOM   6763  C  CB    A GLU A 1 434 ? 5.458   15.594  41.087  0.20 38.85  ? 434 GLU A CB    1 
ATOM   6764  C  CB    B GLU A 1 434 ? 5.717   15.510  41.585  0.80 36.28  ? 434 GLU A CB    1 
ATOM   6765  C  CG    A GLU A 1 434 ? 6.421   16.221  40.087  0.20 43.89  ? 434 GLU A CG    1 
ATOM   6766  C  CG    B GLU A 1 434 ? 6.556   16.116  40.456  0.80 46.36  ? 434 GLU A CG    1 
ATOM   6767  C  CD    A GLU A 1 434 ? 5.706   16.851  38.908  0.20 45.32  ? 434 GLU A CD    1 
ATOM   6768  C  CD    B GLU A 1 434 ? 5.697   16.826  39.424  0.80 46.73  ? 434 GLU A CD    1 
ATOM   6769  O  OE1   A GLU A 1 434 ? 4.458   16.904  38.925  0.20 42.92  ? 434 GLU A OE1   1 
ATOM   6770  O  OE1   B GLU A 1 434 ? 4.617   17.340  39.794  0.80 46.78  ? 434 GLU A OE1   1 
ATOM   6771  O  OE2   A GLU A 1 434 ? 6.394   17.292  37.963  0.20 50.01  ? 434 GLU A OE2   1 
ATOM   6772  O  OE2   B GLU A 1 434 ? 6.091   16.863  38.243  0.80 50.88  ? 434 GLU A OE2   1 
ATOM   6773  N  N     A VAL A 1 435 ? 4.561   13.350  43.327  0.20 40.59  ? 435 VAL A N     1 
ATOM   6774  N  N     B VAL A 1 435 ? 4.803   13.188  43.508  0.80 39.59  ? 435 VAL A N     1 
ATOM   6775  C  CA    A VAL A 1 435 ? 3.685   12.951  44.422  0.20 43.77  ? 435 VAL A CA    1 
ATOM   6776  C  CA    B VAL A 1 435 ? 3.928   12.687  44.566  0.80 45.78  ? 435 VAL A CA    1 
ATOM   6777  C  C     A VAL A 1 435 ? 4.504   12.533  45.637  0.20 44.83  ? 435 VAL A C     1 
ATOM   6778  C  C     B VAL A 1 435 ? 4.757   12.140  45.723  0.80 45.74  ? 435 VAL A C     1 
ATOM   6779  O  O     A VAL A 1 435 ? 4.158   12.863  46.777  0.20 45.94  ? 435 VAL A O     1 
ATOM   6780  O  O     B VAL A 1 435 ? 4.444   12.379  46.897  0.80 47.19  ? 435 VAL A O     1 
ATOM   6781  C  CB    A VAL A 1 435 ? 2.735   11.830  43.963  0.20 38.38  ? 435 VAL A CB    1 
ATOM   6782  C  CB    B VAL A 1 435 ? 2.951   11.636  44.002  0.80 37.14  ? 435 VAL A CB    1 
ATOM   6783  C  CG1   A VAL A 1 435 ? 1.945   11.292  45.143  0.20 41.11  ? 435 VAL A CG1   1 
ATOM   6784  C  CG1   B VAL A 1 435 ? 2.351   10.808  45.122  0.80 41.77  ? 435 VAL A CG1   1 
ATOM   6785  C  CG2   A VAL A 1 435 ? 1.796   12.343  42.884  0.20 38.76  ? 435 VAL A CG2   1 
ATOM   6786  C  CG2   B VAL A 1 435 ? 1.846   12.324  43.215  0.80 37.59  ? 435 VAL A CG2   1 
ATOM   6787  N  N     A GLY A 1 436 ? 5.601   11.813  45.413  0.20 45.73  ? 436 GLY A N     1 
ATOM   6788  N  N     B GLY A 1 436 ? 5.832   11.413  45.415  0.80 46.88  ? 436 GLY A N     1 
ATOM   6789  C  CA    A GLY A 1 436 ? 6.467   11.384  46.493  0.20 47.55  ? 436 GLY A CA    1 
ATOM   6790  C  CA    B GLY A 1 436 ? 6.777   11.012  46.439  0.80 46.55  ? 436 GLY A CA    1 
ATOM   6791  C  C     A GLY A 1 436 ? 6.995   9.976   46.308  0.20 51.45  ? 436 GLY A C     1 
ATOM   6792  C  C     B GLY A 1 436 ? 7.341   9.610   46.306  0.80 54.43  ? 436 GLY A C     1 
ATOM   6793  O  O     A GLY A 1 436 ? 6.501   9.035   46.938  0.20 52.96  ? 436 GLY A O     1 
ATOM   6794  O  O     B GLY A 1 436 ? 6.663   8.625   46.614  0.80 55.04  ? 436 GLY A O     1 
ATOM   6795  N  N     A VAL A 1 437 ? 8.000   9.818   45.452  0.20 52.99  ? 437 VAL A N     1 
ATOM   6796  N  N     B VAL A 1 437 ? 8.590   9.509   45.861  0.80 55.85  ? 437 VAL A N     1 
ATOM   6797  C  CA    A VAL A 1 437 ? 8.578   8.505   45.188  0.20 52.80  ? 437 VAL A CA    1 
ATOM   6798  C  CA    B VAL A 1 437 ? 9.291   8.231   45.796  0.80 55.02  ? 437 VAL A CA    1 
ATOM   6799  C  C     A VAL A 1 437 ? 9.414   8.057   46.381  0.20 55.16  ? 437 VAL A C     1 
ATOM   6800  C  C     B VAL A 1 437 ? 10.786  8.499   45.679  0.80 64.33  ? 437 VAL A C     1 
ATOM   6801  O  O     A VAL A 1 437 ? 9.681   8.841   47.293  0.20 56.61  ? 437 VAL A O     1 
ATOM   6802  O  O     B VAL A 1 437 ? 11.198  9.609   45.336  0.80 64.12  ? 437 VAL A O     1 
ATOM   6803  C  CB    A VAL A 1 437 ? 9.422   8.510   43.896  0.20 53.12  ? 437 VAL A CB    1 
ATOM   6804  C  CB    B VAL A 1 437 ? 8.792   7.358   44.624  0.80 56.61  ? 437 VAL A CB    1 
ATOM   6805  C  CG1   A VAL A 1 437 ? 10.889  8.787   44.209  0.20 55.81  ? 437 VAL A CG1   1 
ATOM   6806  C  CG1   B VAL A 1 437 ? 9.116   8.012   43.286  0.80 53.53  ? 437 VAL A CG1   1 
ATOM   6807  C  CG2   A VAL A 1 437 ? 9.262   7.195   43.144  0.20 49.16  ? 437 VAL A CG2   1 
ATOM   6808  C  CG2   B VAL A 1 437 ? 9.402   5.959   44.700  0.80 57.81  ? 437 VAL A CG2   1 
ATOM   6809  N  N     A MET B 2 1   ? 1.675   -17.099 8.254   0.20 48.51  ? 1   MET B N     1 
ATOM   6810  N  N     B MET B 2 1   ? 3.551   -17.899 10.890  0.80 62.43  ? 1   MET B N     1 
ATOM   6811  C  CA    A MET B 2 1   ? 2.966   -17.675 7.893   0.20 50.84  ? 1   MET B CA    1 
ATOM   6812  C  CA    B MET B 2 1   ? 2.647   -18.355 9.839   0.80 50.79  ? 1   MET B CA    1 
ATOM   6813  C  C     A MET B 2 1   ? 2.930   -19.198 7.964   0.20 51.79  ? 1   MET B C     1 
ATOM   6814  C  C     B MET B 2 1   ? 3.037   -19.745 9.342   0.80 53.98  ? 1   MET B C     1 
ATOM   6815  O  O     A MET B 2 1   ? 2.985   -19.774 9.051   0.20 53.51  ? 1   MET B O     1 
ATOM   6816  O  O     B MET B 2 1   ? 3.198   -20.660 10.154  0.80 54.86  ? 1   MET B O     1 
ATOM   6817  C  CB    A MET B 2 1   ? 4.072   -17.145 8.809   0.20 54.60  ? 1   MET B CB    1 
ATOM   6818  C  CB    B MET B 2 1   ? 2.615   -17.350 8.688   0.80 58.20  ? 1   MET B CB    1 
ATOM   6819  C  CG    A MET B 2 1   ? 4.323   -15.652 8.703   0.20 53.03  ? 1   MET B CG    1 
ATOM   6820  C  CG    B MET B 2 1   ? 3.841   -16.456 8.624   0.80 59.74  ? 1   MET B CG    1 
ATOM   6821  S  SD    A MET B 2 1   ? 4.570   -15.103 7.008   0.20 53.87  ? 1   MET B SD    1 
ATOM   6822  S  SD    B MET B 2 1   ? 3.515   -14.918 7.753   0.80 65.30  ? 1   MET B SD    1 
ATOM   6823  C  CE    A MET B 2 1   ? 5.270   -13.483 7.290   0.20 44.05  ? 1   MET B CE    1 
ATOM   6824  C  CE    B MET B 2 1   ? 2.844   -15.538 6.226   0.80 40.90  ? 1   MET B CE    1 
ATOM   6825  N  N     A ARG B 2 2   ? 2.845   -19.850 6.804   0.20 40.10  ? 2   ARG B N     1 
ATOM   6826  N  N     B ARG B 2 2   ? 3.204   -19.910 8.024   0.80 56.29  ? 2   ARG B N     1 
ATOM   6827  C  CA    A ARG B 2 2   ? 2.809   -21.306 6.770   0.20 42.95  ? 2   ARG B CA    1 
ATOM   6828  C  CA    B ARG B 2 2   ? 3.223   -21.258 7.466   0.80 42.27  ? 2   ARG B CA    1 
ATOM   6829  C  C     A ARG B 2 2   ? 3.652   -21.876 5.635   0.20 36.73  ? 2   ARG B C     1 
ATOM   6830  C  C     B ARG B 2 2   ? 4.223   -21.457 6.318   0.80 41.14  ? 2   ARG B C     1 
ATOM   6831  O  O     A ARG B 2 2   ? 4.335   -22.888 5.817   0.20 39.46  ? 2   ARG B O     1 
ATOM   6832  O  O     B ARG B 2 2   ? 5.396   -21.734 6.589   0.80 38.58  ? 2   ARG B O     1 
ATOM   6833  C  CB    A ARG B 2 2   ? 1.365   -21.804 6.647   0.20 37.88  ? 2   ARG B CB    1 
ATOM   6834  C  CB    B ARG B 2 2   ? 1.792   -21.642 7.052   0.80 33.24  ? 2   ARG B CB    1 
ATOM   6835  C  CG    A ARG B 2 2   ? 0.540   -21.665 7.914   0.20 45.97  ? 2   ARG B CG    1 
ATOM   6836  C  CG    B ARG B 2 2   ? 1.006   -20.504 6.414   0.80 42.07  ? 2   ARG B CG    1 
ATOM   6837  C  CD    A ARG B 2 2   ? 0.994   -22.644 8.985   0.20 49.64  ? 2   ARG B CD    1 
ATOM   6838  C  CD    B ARG B 2 2   ? -0.496  -20.612 6.690   0.80 41.84  ? 2   ARG B CD    1 
ATOM   6839  N  NE    A ARG B 2 2   ? 0.214   -22.505 10.209  0.20 56.39  ? 2   ARG B NE    1 
ATOM   6840  N  NE    B ARG B 2 2   ? -0.844  -20.054 7.995   0.80 55.21  ? 2   ARG B NE    1 
ATOM   6841  C  CZ    A ARG B 2 2   ? 0.326   -23.299 11.266  0.20 51.05  ? 2   ARG B CZ    1 
ATOM   6842  C  CZ    B ARG B 2 2   ? -2.074  -19.994 8.491   0.80 59.78  ? 2   ARG B CZ    1 
ATOM   6843  N  NH1   A ARG B 2 2   ? 1.171   -24.317 11.280  0.20 55.81  ? 2   ARG B NH1   1 
ATOM   6844  N  NH1   B ARG B 2 2   ? -3.111  -20.486 7.832   0.80 65.13  ? 2   ARG B NH1   1 
ATOM   6845  N  NH2   A ARG B 2 2   ? -0.428  -23.064 12.335  0.20 52.11  ? 2   ARG B NH2   1 
ATOM   6846  N  NH2   B ARG B 2 2   ? -2.270  -19.421 9.678   0.80 39.67  ? 2   ARG B NH2   1 
ATOM   6847  N  N     A GLU B 2 3   ? 3.621   -21.241 4.467   0.20 35.48  ? 3   GLU B N     1 
ATOM   6848  N  N     B GLU B 2 3   ? 3.798   -21.316 5.052   0.80 33.70  ? 3   GLU B N     1 
ATOM   6849  C  CA    A GLU B 2 3   ? 4.196   -21.817 3.255   0.20 33.10  ? 3   GLU B CA    1 
ATOM   6850  C  CA    B GLU B 2 3   ? 4.484   -21.975 3.928   0.80 31.81  ? 3   GLU B CA    1 
ATOM   6851  C  C     A GLU B 2 3   ? 5.595   -21.265 3.003   0.20 32.48  ? 3   GLU B C     1 
ATOM   6852  C  C     B GLU B 2 3   ? 5.783   -21.302 3.492   0.80 30.28  ? 3   GLU B C     1 
ATOM   6853  O  O     A GLU B 2 3   ? 5.815   -20.052 3.085   0.20 30.37  ? 3   GLU B O     1 
ATOM   6854  O  O     B GLU B 2 3   ? 5.876   -20.071 3.409   0.80 29.01  ? 3   GLU B O     1 
ATOM   6855  C  CB    A GLU B 2 3   ? 3.297   -21.538 2.049   0.20 33.25  ? 3   GLU B CB    1 
ATOM   6856  C  CB    B GLU B 2 3   ? 3.573   -22.060 2.699   0.80 32.30  ? 3   GLU B CB    1 
ATOM   6857  C  CG    A GLU B 2 3   ? 1.801   -21.576 2.354   0.20 39.53  ? 3   GLU B CG    1 
ATOM   6858  C  CG    B GLU B 2 3   ? 2.388   -23.003 2.846   0.80 33.43  ? 3   GLU B CG    1 
ATOM   6859  C  CD    A GLU B 2 3   ? 1.254   -22.982 2.526   0.20 40.47  ? 3   GLU B CD    1 
ATOM   6860  C  CD    B GLU B 2 3   ? 1.191   -22.311 3.458   0.80 37.24  ? 3   GLU B CD    1 
ATOM   6861  O  OE1   A GLU B 2 3   ? 2.036   -23.954 2.430   0.20 35.00  ? 3   GLU B OE1   1 
ATOM   6862  O  OE1   B GLU B 2 3   ? 1.044   -21.091 3.223   0.80 36.26  ? 3   GLU B OE1   1 
ATOM   6863  O  OE2   A GLU B 2 3   ? 0.030   -23.112 2.753   0.20 31.99  ? 3   GLU B OE2   1 
ATOM   6864  O  OE2   B GLU B 2 3   ? 0.404   -22.984 4.162   0.80 37.42  ? 3   GLU B OE2   1 
ATOM   6865  N  N     A ILE B 2 4   ? 6.529   -22.158 2.680   0.20 31.17  ? 4   ILE B N     1 
ATOM   6866  N  N     B ILE B 2 4   ? 6.758   -22.134 3.123   0.80 29.12  ? 4   ILE B N     1 
ATOM   6867  C  CA    A ILE B 2 4   ? 7.898   -21.798 2.322   0.20 29.92  ? 4   ILE B CA    1 
ATOM   6868  C  CA    B ILE B 2 4   ? 8.045   -21.686 2.589   0.80 27.96  ? 4   ILE B CA    1 
ATOM   6869  C  C     A ILE B 2 4   ? 8.198   -22.380 0.948   0.20 32.66  ? 4   ILE B C     1 
ATOM   6870  C  C     B ILE B 2 4   ? 8.250   -22.304 1.213   0.80 32.61  ? 4   ILE B C     1 
ATOM   6871  O  O     A ILE B 2 4   ? 7.899   -23.551 0.687   0.20 36.70  ? 4   ILE B O     1 
ATOM   6872  O  O     B ILE B 2 4   ? 7.991   -23.495 1.016   0.80 36.62  ? 4   ILE B O     1 
ATOM   6873  C  CB    A ILE B 2 4   ? 8.914   -22.306 3.363   0.20 31.44  ? 4   ILE B CB    1 
ATOM   6874  C  CB    B ILE B 2 4   ? 9.211   -22.069 3.528   0.80 31.41  ? 4   ILE B CB    1 
ATOM   6875  C  CG1   A ILE B 2 4   ? 8.712   -21.594 4.704   0.20 32.20  ? 4   ILE B CG1   1 
ATOM   6876  C  CG1   B ILE B 2 4   ? 9.127   -21.280 4.837   0.80 31.50  ? 4   ILE B CG1   1 
ATOM   6877  C  CG2   A ILE B 2 4   ? 10.345  -22.126 2.860   0.20 31.32  ? 4   ILE B CG2   1 
ATOM   6878  C  CG2   B ILE B 2 4   ? 10.572  -21.865 2.839   0.80 29.95  ? 4   ILE B CG2   1 
ATOM   6879  C  CD1   A ILE B 2 4   ? 9.751   -21.947 5.749   0.20 35.05  ? 4   ILE B CD1   1 
ATOM   6880  C  CD1   B ILE B 2 4   ? 10.121  -21.724 5.882   0.80 35.36  ? 4   ILE B CD1   1 
ATOM   6881  N  N     A VAL B 2 5   ? 8.783   -21.567 0.075   0.20 31.35  ? 5   VAL B N     1 
ATOM   6882  N  N     B VAL B 2 5   ? 8.717   -21.492 0.269   0.80 30.55  ? 5   VAL B N     1 
ATOM   6883  C  CA    A VAL B 2 5   ? 9.171   -21.990 -1.266  0.20 33.32  ? 5   VAL B CA    1 
ATOM   6884  C  CA    B VAL B 2 5   ? 9.134   -21.956 -1.048  0.80 33.80  ? 5   VAL B CA    1 
ATOM   6885  C  C     A VAL B 2 5   ? 10.676  -22.232 -1.261  0.20 34.64  ? 5   VAL B C     1 
ATOM   6886  C  C     B VAL B 2 5   ? 10.655  -21.998 -1.080  0.80 34.94  ? 5   VAL B C     1 
ATOM   6887  O  O     A VAL B 2 5   ? 11.466  -21.287 -1.168  0.20 34.14  ? 5   VAL B O     1 
ATOM   6888  O  O     B VAL B 2 5   ? 11.317  -20.998 -0.772  0.80 28.89  ? 5   VAL B O     1 
ATOM   6889  C  CB    A VAL B 2 5   ? 8.776   -20.952 -2.324  0.20 32.04  ? 5   VAL B CB    1 
ATOM   6890  C  CB    B VAL B 2 5   ? 8.580   -21.046 -2.155  0.80 30.57  ? 5   VAL B CB    1 
ATOM   6891  C  CG1   A VAL B 2 5   ? 9.337   -21.342 -3.688  0.20 33.19  ? 5   VAL B CG1   1 
ATOM   6892  C  CG1   B VAL B 2 5   ? 9.283   -21.335 -3.500  0.80 33.35  ? 5   VAL B CG1   1 
ATOM   6893  C  CG2   A VAL B 2 5   ? 7.264   -20.809 -2.384  0.20 36.29  ? 5   VAL B CG2   1 
ATOM   6894  C  CG2   B VAL B 2 5   ? 7.067   -21.222 -2.259  0.80 35.24  ? 5   VAL B CG2   1 
ATOM   6895  N  N     A HIS B 2 6   ? 11.070  -23.499 -1.370  0.20 34.04  ? 6   HIS B N     1 
ATOM   6896  N  N     B HIS B 2 6   ? 11.201  -23.151 -1.467  0.80 34.13  ? 6   HIS B N     1 
ATOM   6897  C  CA    A HIS B 2 6   ? 12.473  -23.890 -1.386  0.20 32.17  ? 6   HIS B CA    1 
ATOM   6898  C  CA    B HIS B 2 6   ? 12.630  -23.425 -1.511  0.80 31.23  ? 6   HIS B CA    1 
ATOM   6899  C  C     A HIS B 2 6   ? 13.012  -23.833 -2.810  0.20 33.29  ? 6   HIS B C     1 
ATOM   6900  C  C     B HIS B 2 6   ? 13.090  -23.428 -2.963  0.80 32.68  ? 6   HIS B C     1 
ATOM   6901  O  O     A HIS B 2 6   ? 12.379  -24.341 -3.739  0.20 35.84  ? 6   HIS B O     1 
ATOM   6902  O  O     B HIS B 2 6   ? 12.496  -24.120 -3.794  0.80 36.53  ? 6   HIS B O     1 
ATOM   6903  C  CB    A HIS B 2 6   ? 12.636  -25.299 -0.815  0.20 33.17  ? 6   HIS B CB    1 
ATOM   6904  C  CB    B HIS B 2 6   ? 12.914  -24.783 -0.859  0.80 29.18  ? 6   HIS B CB    1 
ATOM   6905  C  CG    A HIS B 2 6   ? 14.017  -25.860 -0.957  0.20 33.56  ? 6   HIS B CG    1 
ATOM   6906  C  CG    B HIS B 2 6   ? 14.256  -25.363 -1.192  0.80 36.43  ? 6   HIS B CG    1 
ATOM   6907  N  ND1   A HIS B 2 6   ? 14.965  -25.763 0.038   0.20 36.34  ? 6   HIS B ND1   1 
ATOM   6908  N  ND1   B HIS B 2 6   ? 15.280  -25.434 -0.273  0.80 41.63  ? 6   HIS B ND1   1 
ATOM   6909  C  CD2   A HIS B 2 6   ? 14.609  -26.528 -1.976  0.20 35.35  ? 6   HIS B CD2   1 
ATOM   6910  C  CD2   B HIS B 2 6   ? 14.738  -25.914 -2.334  0.80 34.50  ? 6   HIS B CD2   1 
ATOM   6911  C  CE1   A HIS B 2 6   ? 16.082  -26.345 -0.362  0.20 36.83  ? 6   HIS B CE1   1 
ATOM   6912  C  CE1   B HIS B 2 6   ? 16.340  -25.989 -0.838  0.80 35.22  ? 6   HIS B CE1   1 
ATOM   6913  N  NE2   A HIS B 2 6   ? 15.893  -26.817 -1.581  0.20 34.20  ? 6   HIS B NE2   1 
ATOM   6914  N  NE2   B HIS B 2 6   ? 16.036  -26.291 -2.086  0.80 34.40  ? 6   HIS B NE2   1 
ATOM   6915  N  N     A ILE B 2 7   ? 14.176  -23.207 -2.977  0.20 33.03  ? 7   ILE B N     1 
ATOM   6916  N  N     B ILE B 2 7   ? 14.134  -22.655 -3.268  0.80 30.11  ? 7   ILE B N     1 
ATOM   6917  C  CA    A ILE B 2 7   ? 14.848  -23.123 -4.267  0.20 33.35  ? 7   ILE B CA    1 
ATOM   6918  C  CA    B ILE B 2 7   ? 14.817  -22.698 -4.561  0.80 33.57  ? 7   ILE B CA    1 
ATOM   6919  C  C     A ILE B 2 7   ? 16.285  -23.590 -4.088  0.20 34.69  ? 7   ILE B C     1 
ATOM   6920  C  C     B ILE B 2 7   ? 16.248  -23.153 -4.321  0.80 35.57  ? 7   ILE B C     1 
ATOM   6921  O  O     A ILE B 2 7   ? 16.862  -23.488 -3.001  0.20 27.86  ? 7   ILE B O     1 
ATOM   6922  O  O     B ILE B 2 7   ? 16.922  -22.639 -3.421  0.80 23.81  ? 7   ILE B O     1 
ATOM   6923  C  CB    A ILE B 2 7   ? 14.809  -21.689 -4.855  0.20 36.37  ? 7   ILE B CB    1 
ATOM   6924  C  CB    B ILE B 2 7   ? 14.813  -21.324 -5.260  0.80 36.45  ? 7   ILE B CB    1 
ATOM   6925  C  CG1   A ILE B 2 7   ? 13.395  -21.112 -4.791  0.20 37.32  ? 7   ILE B CG1   1 
ATOM   6926  C  CG1   B ILE B 2 7   ? 13.390  -20.820 -5.491  0.80 36.91  ? 7   ILE B CG1   1 
ATOM   6927  C  CG2   A ILE B 2 7   ? 15.303  -21.670 -6.296  0.20 38.03  ? 7   ILE B CG2   1 
ATOM   6928  C  CG2   B ILE B 2 7   ? 15.612  -21.368 -6.561  0.80 39.03  ? 7   ILE B CG2   1 
ATOM   6929  C  CD1   A ILE B 2 7   ? 13.252  -19.775 -5.494  0.20 37.66  ? 7   ILE B CD1   1 
ATOM   6930  C  CD1   B ILE B 2 7   ? 13.126  -19.461 -4.863  0.80 41.86  ? 7   ILE B CD1   1 
ATOM   6931  N  N     A GLN B 2 8   ? 16.860  -24.122 -5.166  0.20 36.01  ? 8   GLN B N     1 
ATOM   6932  N  N     B GLN B 2 8   ? 16.726  -24.095 -5.133  0.80 36.42  ? 8   GLN B N     1 
ATOM   6933  C  CA    A GLN B 2 8   ? 18.266  -24.491 -5.200  0.20 34.64  ? 8   GLN B CA    1 
ATOM   6934  C  CA    B GLN B 2 8   ? 18.125  -24.496 -5.105  0.80 34.61  ? 8   GLN B CA    1 
ATOM   6935  C  C     A GLN B 2 8   ? 18.812  -24.215 -6.592  0.20 34.68  ? 8   GLN B C     1 
ATOM   6936  C  C     B GLN B 2 8   ? 18.723  -24.288 -6.489  0.80 34.63  ? 8   GLN B C     1 
ATOM   6937  O  O     A GLN B 2 8   ? 18.139  -24.481 -7.592  0.20 36.75  ? 8   GLN B O     1 
ATOM   6938  O  O     B GLN B 2 8   ? 18.147  -24.735 -7.485  0.80 36.95  ? 8   GLN B O     1 
ATOM   6939  C  CB    A GLN B 2 8   ? 18.465  -25.962 -4.824  0.20 36.33  ? 8   GLN B CB    1 
ATOM   6940  C  CB    B GLN B 2 8   ? 18.269  -25.947 -4.658  0.80 37.53  ? 8   GLN B CB    1 
ATOM   6941  C  CG    A GLN B 2 8   ? 17.564  -26.923 -5.574  0.20 35.76  ? 8   GLN B CG    1 
ATOM   6942  C  CG    B GLN B 2 8   ? 17.249  -26.871 -5.267  0.80 34.87  ? 8   GLN B CG    1 
ATOM   6943  C  CD    A GLN B 2 8   ? 17.555  -28.295 -4.945  0.20 34.42  ? 8   GLN B CD    1 
ATOM   6944  C  CD    B GLN B 2 8   ? 17.238  -28.208 -4.596  0.80 34.98  ? 8   GLN B CD    1 
ATOM   6945  O  OE1   A GLN B 2 8   ? 17.502  -28.426 -3.725  0.20 35.07  ? 8   GLN B OE1   1 
ATOM   6946  O  OE1   B GLN B 2 8   ? 16.760  -28.345 -3.472  0.80 34.93  ? 8   GLN B OE1   1 
ATOM   6947  N  NE2   A GLN B 2 8   ? 17.616  -29.327 -5.774  0.20 35.36  ? 8   GLN B NE2   1 
ATOM   6948  N  NE2   B GLN B 2 8   ? 17.741  -29.221 -5.289  0.80 34.96  ? 8   GLN B NE2   1 
ATOM   6949  N  N     A ALA B 2 9   ? 20.026  -23.671 -6.652  0.20 33.00  ? 9   ALA B N     1 
ATOM   6950  N  N     B ALA B 2 9   ? 19.875  -23.618 -6.545  0.80 32.50  ? 9   ALA B N     1 
ATOM   6951  C  CA    A ALA B 2 9   ? 20.641  -23.281 -7.911  0.20 32.63  ? 9   ALA B CA    1 
ATOM   6952  C  CA    B ALA B 2 9   ? 20.427  -23.119 -7.796  0.80 31.22  ? 9   ALA B CA    1 
ATOM   6953  C  C     A ALA B 2 9   ? 22.088  -23.749 -7.958  0.20 34.25  ? 9   ALA B C     1 
ATOM   6954  C  C     B ALA B 2 9   ? 21.886  -23.534 -7.941  0.80 34.43  ? 9   ALA B C     1 
ATOM   6955  O  O     A ALA B 2 9   ? 22.744  -23.904 -6.924  0.20 30.60  ? 9   ALA B O     1 
ATOM   6956  O  O     B ALA B 2 9   ? 22.694  -23.296 -7.042  0.80 28.69  ? 9   ALA B O     1 
ATOM   6957  C  CB    A ALA B 2 9   ? 20.578  -21.761 -8.118  0.20 34.36  ? 9   ALA B CB    1 
ATOM   6958  C  CB    B ALA B 2 9   ? 20.300  -21.596 -7.864  0.80 34.56  ? 9   ALA B CB    1 
ATOM   6959  N  N     A GLY B 2 10  ? 22.579  -23.977 -9.175  0.20 36.28  ? 10  GLY B N     1 
ATOM   6960  N  N     B GLY B 2 10  ? 22.229  -24.136 -9.081  0.80 37.43  ? 10  GLY B N     1 
ATOM   6961  C  CA    A GLY B 2 10  ? 23.957  -24.382 -9.375  0.20 33.07  ? 10  GLY B CA    1 
ATOM   6962  C  CA    B GLY B 2 10  ? 23.611  -24.489 -9.347  0.80 31.71  ? 10  GLY B CA    1 
ATOM   6963  C  C     A GLY B 2 10  ? 24.240  -25.803 -8.939  0.20 34.18  ? 10  GLY B C     1 
ATOM   6964  C  C     B GLY B 2 10  ? 24.031  -25.780 -8.673  0.80 33.56  ? 10  GLY B C     1 
ATOM   6965  O  O     A GLY B 2 10  ? 23.381  -26.461 -8.344  0.20 36.98  ? 10  GLY B O     1 
ATOM   6966  O  O     B GLY B 2 10  ? 23.257  -26.457 -7.994  0.80 38.86  ? 10  GLY B O     1 
ATOM   6967  N  N     A GLN B 2 11  ? 25.448  -26.291 -9.230  0.20 34.51  ? 11  GLN B N     1 
ATOM   6968  N  N     B GLN B 2 11  ? 25.310  -26.116 -8.853  0.80 33.05  ? 11  GLN B N     1 
ATOM   6969  C  CA    A GLN B 2 11  ? 25.808  -27.649 -8.837  0.20 35.99  ? 11  GLN B CA    1 
ATOM   6970  C  CA    B GLN B 2 11  ? 25.790  -27.432 -8.441  0.80 34.40  ? 11  GLN B CA    1 
ATOM   6971  C  C     A GLN B 2 11  ? 25.854  -27.794 -7.320  0.20 34.36  ? 11  GLN B C     1 
ATOM   6972  C  C     B GLN B 2 11  ? 25.753  -27.601 -6.925  0.80 33.55  ? 11  GLN B C     1 
ATOM   6973  O  O     A GLN B 2 11  ? 25.420  -28.816 -6.776  0.20 36.76  ? 11  GLN B O     1 
ATOM   6974  O  O     B GLN B 2 11  ? 25.168  -28.564 -6.415  0.80 37.26  ? 11  GLN B O     1 
ATOM   6975  C  CB    A GLN B 2 11  ? 27.154  -28.040 -9.451  0.20 33.98  ? 11  GLN B CB    1 
ATOM   6976  C  CB    B GLN B 2 11  ? 27.207  -27.675 -8.963  0.80 30.93  ? 11  GLN B CB    1 
ATOM   6977  C  CG    A GLN B 2 11  ? 27.119  -28.308 -10.949 0.20 39.63  ? 11  GLN B CG    1 
ATOM   6978  C  CG    B GLN B 2 11  ? 27.738  -29.032 -8.556  0.80 30.38  ? 11  GLN B CG    1 
ATOM   6979  C  CD    A GLN B 2 11  ? 27.378  -27.065 -11.780 0.20 36.99  ? 11  GLN B CD    1 
ATOM   6980  C  CD    B GLN B 2 11  ? 27.247  -30.126 -9.486  0.80 61.86  ? 11  GLN B CD    1 
ATOM   6981  O  OE1   A GLN B 2 11  ? 28.493  -26.540 -11.812 0.20 19.75  ? 11  GLN B OE1   1 
ATOM   6982  O  OE1   B GLN B 2 11  ? 26.977  -29.876 -10.666 0.80 62.13  ? 11  GLN B OE1   1 
ATOM   6983  N  NE2   A GLN B 2 11  ? 26.346  -26.591 -12.462 0.20 39.27  ? 11  GLN B NE2   1 
ATOM   6984  N  NE2   B GLN B 2 11  ? 27.119  -31.343 -8.963  0.80 67.88  ? 11  GLN B NE2   1 
ATOM   6985  N  N     A CYS B 2 12  ? 26.374  -26.782 -6.621  0.20 35.61  ? 12  CYS B N     1 
ATOM   6986  N  N     B CYS B 2 12  ? 26.398  -26.692 -6.185  0.80 36.96  ? 12  CYS B N     1 
ATOM   6987  C  CA    A CYS B 2 12  ? 26.493  -26.869 -5.169  0.20 35.00  ? 12  CYS B CA    1 
ATOM   6988  C  CA    B CYS B 2 12  ? 26.371  -26.797 -4.729  0.80 36.75  ? 12  CYS B CA    1 
ATOM   6989  C  C     A CYS B 2 12  ? 25.133  -26.772 -4.488  0.20 34.40  ? 12  CYS B C     1 
ATOM   6990  C  C     B CYS B 2 12  ? 24.951  -26.648 -4.198  0.80 32.77  ? 12  CYS B C     1 
ATOM   6991  O  O     A CYS B 2 12  ? 24.860  -27.506 -3.531  0.20 33.07  ? 12  CYS B O     1 
ATOM   6992  O  O     B CYS B 2 12  ? 24.538  -27.387 -3.302  0.80 33.88  ? 12  CYS B O     1 
ATOM   6993  C  CB    A CYS B 2 12  ? 27.429  -25.776 -4.654  0.20 33.73  ? 12  CYS B CB    1 
ATOM   6994  C  CB    B CYS B 2 12  ? 27.289  -25.752 -4.090  0.80 34.93  ? 12  CYS B CB    1 
ATOM   6995  S  SG    A CYS B 2 12  ? 27.219  -25.362 -2.900  0.20 33.02  ? 12  CYS B SG    1 
ATOM   6996  S  SG    B CYS B 2 12  ? 27.412  -25.879 -2.259  0.80 31.81  ? 12  CYS B SG    1 
ATOM   6997  N  N     A GLY B 2 13  ? 24.270  -25.872 -4.961  0.20 33.46  ? 13  GLY B N     1 
ATOM   6998  N  N     B GLY B 2 13  ? 24.188  -25.709 -4.749  0.80 33.93  ? 13  GLY B N     1 
ATOM   6999  C  CA    A GLY B 2 13  ? 22.978  -25.697 -4.315  0.20 34.19  ? 13  GLY B CA    1 
ATOM   7000  C  CA    B GLY B 2 13  ? 22.836  -25.498 -4.260  0.80 34.89  ? 13  GLY B CA    1 
ATOM   7001  C  C     A GLY B 2 13  ? 22.098  -26.927 -4.431  0.20 34.68  ? 13  GLY B C     1 
ATOM   7002  C  C     B GLY B 2 13  ? 21.977  -26.738 -4.386  0.80 35.45  ? 13  GLY B C     1 
ATOM   7003  O  O     A GLY B 2 13  ? 21.509  -27.380 -3.444  0.20 31.59  ? 13  GLY B O     1 
ATOM   7004  O  O     B GLY B 2 13  ? 21.229  -27.087 -3.464  0.80 29.88  ? 13  GLY B O     1 
ATOM   7005  N  N     A ASN B 2 14  ? 21.994  -27.482 -5.642  0.20 30.22  ? 14  ASN B N     1 
ATOM   7006  N  N     B ASN B 2 14  ? 22.089  -27.435 -5.521  0.80 29.57  ? 14  ASN B N     1 
ATOM   7007  C  CA    A ASN B 2 14  ? 21.216  -28.701 -5.831  0.20 31.40  ? 14  ASN B CA    1 
ATOM   7008  C  CA    B ASN B 2 14  ? 21.307  -28.643 -5.736  0.80 30.80  ? 14  ASN B CA    1 
ATOM   7009  C  C     A ASN B 2 14  ? 21.813  -29.868 -5.060  0.20 32.93  ? 14  ASN B C     1 
ATOM   7010  C  C     B ASN B 2 14  ? 21.814  -29.824 -4.924  0.80 32.81  ? 14  ASN B C     1 
ATOM   7011  O  O     A ASN B 2 14  ? 21.084  -30.778 -4.645  0.20 35.96  ? 14  ASN B O     1 
ATOM   7012  O  O     B ASN B 2 14  ? 21.005  -30.636 -4.457  0.80 36.08  ? 14  ASN B O     1 
ATOM   7013  C  CB    A ASN B 2 14  ? 21.122  -29.036 -7.320  0.20 34.72  ? 14  ASN B CB    1 
ATOM   7014  C  CB    B ASN B 2 14  ? 21.280  -28.981 -7.224  0.80 34.60  ? 14  ASN B CB    1 
ATOM   7015  C  CG    A ASN B 2 14  ? 20.358  -27.991 -8.101  0.20 35.66  ? 14  ASN B CG    1 
ATOM   7016  C  CG    B ASN B 2 14  ? 20.203  -28.225 -7.952  0.80 35.89  ? 14  ASN B CG    1 
ATOM   7017  O  OD1   A ASN B 2 14  ? 19.161  -28.138 -8.354  0.20 39.45  ? 14  ASN B OD1   1 
ATOM   7018  O  OD1   B ASN B 2 14  ? 19.013  -28.537 -7.815  0.80 41.92  ? 14  ASN B OD1   1 
ATOM   7019  N  ND2   A ASN B 2 14  ? 21.042  -26.920 -8.480  0.20 37.44  ? 14  ASN B ND2   1 
ATOM   7020  N  ND2   B ASN B 2 14  ? 20.596  -27.213 -8.710  0.80 39.34  ? 14  ASN B ND2   1 
ATOM   7021  N  N     A GLN B 2 15  ? 23.130  -29.856 -4.848  0.20 31.61  ? 15  GLN B N     1 
ATOM   7022  N  N     B GLN B 2 15  ? 23.128  -29.936 -4.723  0.80 31.10  ? 15  GLN B N     1 
ATOM   7023  C  CA    A GLN B 2 15  ? 23.775  -30.948 -4.128  0.20 32.95  ? 15  GLN B CA    1 
ATOM   7024  C  CA    B GLN B 2 15  ? 23.646  -31.081 -3.986  0.80 31.79  ? 15  GLN B CA    1 
ATOM   7025  C  C     A GLN B 2 15  ? 23.386  -30.937 -2.655  0.20 35.59  ? 15  GLN B C     1 
ATOM   7026  C  C     B GLN B 2 15  ? 23.315  -30.978 -2.505  0.80 35.72  ? 15  GLN B C     1 
ATOM   7027  O  O     A GLN B 2 15  ? 22.937  -31.954 -2.114  0.20 34.84  ? 15  GLN B O     1 
ATOM   7028  O  O     B GLN B 2 15  ? 22.948  -31.977 -1.881  0.80 34.61  ? 15  GLN B O     1 
ATOM   7029  C  CB    A GLN B 2 15  ? 25.294  -30.855 -4.291  0.20 35.96  ? 15  GLN B CB    1 
ATOM   7030  C  CB    B GLN B 2 15  ? 25.159  -31.222 -4.183  0.80 36.93  ? 15  GLN B CB    1 
ATOM   7031  C  CG    A GLN B 2 15  ? 26.017  -32.179 -4.131  0.20 40.05  ? 15  GLN B CG    1 
ATOM   7032  C  CG    B GLN B 2 15  ? 25.745  -32.425 -3.437  0.80 38.84  ? 15  GLN B CG    1 
ATOM   7033  C  CD    A GLN B 2 15  ? 25.647  -33.176 -5.212  0.20 43.19  ? 15  GLN B CD    1 
ATOM   7034  C  CD    B GLN B 2 15  ? 25.039  -33.739 -3.769  0.80 54.01  ? 15  GLN B CD    1 
ATOM   7035  O  OE1   A GLN B 2 15  ? 25.587  -34.381 -4.967  0.20 51.92  ? 15  GLN B OE1   1 
ATOM   7036  O  OE1   B GLN B 2 15  ? 24.781  -34.038 -4.939  0.80 56.76  ? 15  GLN B OE1   1 
ATOM   7037  N  NE2   A GLN B 2 15  ? 25.403  -32.678 -6.418  0.20 46.12  ? 15  GLN B NE2   1 
ATOM   7038  N  NE2   B GLN B 2 15  ? 24.710  -34.522 -2.737  0.80 40.48  ? 15  GLN B NE2   1 
ATOM   7039  N  N     A ILE B 2 16  ? 23.549  -29.792 -1.989  0.20 34.04  ? 16  ILE B N     1 
ATOM   7040  N  N     B ILE B 2 16  ? 23.439  -29.785 -1.920  0.80 34.03  ? 16  ILE B N     1 
ATOM   7041  C  CA    A ILE B 2 16  ? 23.166  -29.704 -0.584  0.20 32.17  ? 16  ILE B CA    1 
ATOM   7042  C  CA    B ILE B 2 16  ? 23.081  -29.666 -0.511  0.80 32.05  ? 16  ILE B CA    1 
ATOM   7043  C  C     A ILE B 2 16  ? 21.651  -29.651 -0.440  0.20 35.61  ? 16  ILE B C     1 
ATOM   7044  C  C     B ILE B 2 16  ? 21.565  -29.566 -0.345  0.80 35.79  ? 16  ILE B C     1 
ATOM   7045  O  O     A ILE B 2 16  ? 21.104  -30.062 0.590   0.20 32.63  ? 16  ILE B O     1 
ATOM   7046  O  O     B ILE B 2 16  ? 21.026  -29.972 0.690   0.80 32.15  ? 16  ILE B O     1 
ATOM   7047  C  CB    A ILE B 2 16  ? 23.839  -28.490 0.084   0.20 34.75  ? 16  ILE B CB    1 
ATOM   7048  C  CB    B ILE B 2 16  ? 23.799  -28.476 0.154   0.80 34.86  ? 16  ILE B CB    1 
ATOM   7049  C  CG1   A ILE B 2 16  ? 23.410  -27.190 -0.600  0.20 32.98  ? 16  ILE B CG1   1 
ATOM   7050  C  CG1   B ILE B 2 16  ? 23.229  -27.142 -0.330  0.80 31.84  ? 16  ILE B CG1   1 
ATOM   7051  C  CG2   A ILE B 2 16  ? 25.354  -28.639 0.061   0.20 34.41  ? 16  ILE B CG2   1 
ATOM   7052  C  CG2   B ILE B 2 16  ? 25.303  -28.553 -0.077  0.80 34.44  ? 16  ILE B CG2   1 
ATOM   7053  C  CD1   A ILE B 2 16  ? 23.999  -25.945 0.032   0.20 35.77  ? 16  ILE B CD1   1 
ATOM   7054  C  CD1   B ILE B 2 16  ? 23.664  -25.957 0.519   0.80 37.84  ? 16  ILE B CD1   1 
ATOM   7055  N  N     A GLY B 2 17  ? 20.948  -29.150 -1.457  0.20 33.32  ? 17  GLY B N     1 
ATOM   7056  N  N     B GLY B 2 17  ? 20.858  -29.037 -1.345  0.80 32.84  ? 17  GLY B N     1 
ATOM   7057  C  CA    A GLY B 2 17  ? 19.497  -29.112 -1.389  0.20 36.98  ? 17  GLY B CA    1 
ATOM   7058  C  CA    B GLY B 2 17  ? 19.407  -29.006 -1.274  0.80 37.62  ? 17  GLY B CA    1 
ATOM   7059  C  C     A GLY B 2 17  ? 18.876  -30.492 -1.465  0.20 36.21  ? 17  GLY B C     1 
ATOM   7060  C  C     B GLY B 2 17  ? 18.805  -30.395 -1.270  0.80 36.01  ? 17  GLY B C     1 
ATOM   7061  O  O     A GLY B 2 17  ? 17.858  -30.760 -0.822  0.20 36.67  ? 17  GLY B O     1 
ATOM   7062  O  O     B GLY B 2 17  ? 17.887  -30.680 -0.501  0.80 36.10  ? 17  GLY B O     1 
ATOM   7063  N  N     A ALA B 2 18  ? 19.480  -31.388 -2.250  0.20 36.03  ? 18  ALA B N     1 
ATOM   7064  N  N     B ALA B 2 18  ? 19.336  -31.287 -2.112  0.80 36.13  ? 18  ALA B N     1 
ATOM   7065  C  CA    A ALA B 2 18  ? 18.981  -32.757 -2.330  0.20 36.96  ? 18  ALA B CA    1 
ATOM   7066  C  CA    B ALA B 2 18  ? 18.824  -32.650 -2.183  0.80 36.62  ? 18  ALA B CA    1 
ATOM   7067  C  C     A ALA B 2 18  ? 19.160  -33.485 -1.005  0.20 38.52  ? 18  ALA B C     1 
ATOM   7068  C  C     B ALA B 2 18  ? 19.006  -33.380 -0.861  0.80 38.37  ? 18  ALA B C     1 
ATOM   7069  O  O     A ALA B 2 18  ? 18.244  -34.176 -0.544  0.20 39.63  ? 18  ALA B O     1 
ATOM   7070  O  O     B ALA B 2 18  ? 18.121  -34.134 -0.436  0.80 39.63  ? 18  ALA B O     1 
ATOM   7071  C  CB    A ALA B 2 18  ? 19.687  -33.509 -3.459  0.20 35.76  ? 18  ALA B CB    1 
ATOM   7072  C  CB    B ALA B 2 18  ? 19.516  -33.409 -3.319  0.80 35.91  ? 18  ALA B CB    1 
ATOM   7073  N  N     A LYS B 2 19  ? 20.332  -33.342 -0.378  0.20 38.15  ? 19  LYS B N     1 
ATOM   7074  N  N     B LYS B 2 19  ? 20.152  -33.175 -0.199  0.80 38.16  ? 19  LYS B N     1 
ATOM   7075  C  CA    A LYS B 2 19  ? 20.551  -33.926 0.940   0.20 39.00  ? 19  LYS B CA    1 
ATOM   7076  C  CA    B LYS B 2 19  ? 20.385  -33.790 1.105   0.80 38.86  ? 19  LYS B CA    1 
ATOM   7077  C  C     A LYS B 2 19  ? 19.614  -33.338 1.985   0.20 41.04  ? 19  LYS B C     1 
ATOM   7078  C  C     B LYS B 2 19  ? 19.445  -33.226 2.164   0.80 41.75  ? 19  LYS B C     1 
ATOM   7079  O  O     A LYS B 2 19  ? 19.347  -33.989 3.001   0.20 41.99  ? 19  LYS B O     1 
ATOM   7080  O  O     B LYS B 2 19  ? 19.012  -33.952 3.069   0.80 42.80  ? 19  LYS B O     1 
ATOM   7081  C  CB    A LYS B 2 19  ? 22.005  -33.725 1.373   0.20 36.67  ? 19  LYS B CB    1 
ATOM   7082  C  CB    B LYS B 2 19  ? 21.835  -33.586 1.531   0.80 33.96  ? 19  LYS B CB    1 
ATOM   7083  C  CG    A LYS B 2 19  ? 23.045  -34.183 0.351   0.20 44.12  ? 19  LYS B CG    1 
ATOM   7084  C  CG    B LYS B 2 19  ? 22.847  -34.348 0.691   0.80 48.48  ? 19  LYS B CG    1 
ATOM   7085  C  CD    A LYS B 2 19  ? 23.751  -35.466 0.782   0.20 46.96  ? 19  LYS B CD    1 
ATOM   7086  C  CD    B LYS B 2 19  ? 22.629  -35.842 0.842   0.80 51.06  ? 19  LYS B CD    1 
ATOM   7087  C  CE    A LYS B 2 19  ? 22.833  -36.677 0.696   0.20 49.36  ? 19  LYS B CE    1 
ATOM   7088  C  CE    B LYS B 2 19  ? 23.620  -36.650 0.023   0.80 52.91  ? 19  LYS B CE    1 
ATOM   7089  N  NZ    A LYS B 2 19  ? 23.505  -37.928 1.149   0.20 45.93  ? 19  LYS B NZ    1 
ATOM   7090  N  NZ    B LYS B 2 19  ? 23.350  -38.101 0.197   0.80 44.37  ? 19  LYS B NZ    1 
ATOM   7091  N  N     A PHE B 2 20  ? 19.117  -32.119 1.759   0.20 38.22  ? 20  PHE B N     1 
ATOM   7092  N  N     B PHE B 2 20  ? 19.141  -31.929 2.081   0.80 37.18  ? 20  PHE B N     1 
ATOM   7093  C  CA    A PHE B 2 20  ? 18.127  -31.542 2.661   0.20 39.82  ? 20  PHE B CA    1 
ATOM   7094  C  CA    B PHE B 2 20  ? 18.169  -31.333 2.992   0.80 40.17  ? 20  PHE B CA    1 
ATOM   7095  C  C     A PHE B 2 20  ? 16.794  -32.272 2.552   0.20 39.54  ? 20  PHE B C     1 
ATOM   7096  C  C     B PHE B 2 20  ? 16.836  -32.061 2.917   0.80 38.84  ? 20  PHE B C     1 
ATOM   7097  O  O     A PHE B 2 20  ? 16.168  -32.587 3.570   0.20 40.24  ? 20  PHE B O     1 
ATOM   7098  O  O     B PHE B 2 20  ? 16.235  -32.384 3.949   0.80 40.39  ? 20  PHE B O     1 
ATOM   7099  C  CB    A PHE B 2 20  ? 17.956  -30.053 2.361   0.20 38.66  ? 20  PHE B CB    1 
ATOM   7100  C  CB    B PHE B 2 20  ? 17.999  -29.852 2.657   0.80 39.16  ? 20  PHE B CB    1 
ATOM   7101  C  CG    A PHE B 2 20  ? 16.895  -29.383 3.187   0.20 41.19  ? 20  PHE B CG    1 
ATOM   7102  C  CG    B PHE B 2 20  ? 16.895  -29.171 3.414   0.80 42.52  ? 20  PHE B CG    1 
ATOM   7103  C  CD1   A PHE B 2 20  ? 17.110  -29.112 4.529   0.20 38.16  ? 20  PHE B CD1   1 
ATOM   7104  C  CD1   B PHE B 2 20  ? 16.991  -28.971 4.780   0.80 38.41  ? 20  PHE B CD1   1 
ATOM   7105  C  CD2   A PHE B 2 20  ? 15.687  -29.013 2.619   0.20 38.03  ? 20  PHE B CD2   1 
ATOM   7106  C  CD2   B PHE B 2 20  ? 15.771  -28.705 2.750   0.80 37.78  ? 20  PHE B CD2   1 
ATOM   7107  C  CE1   A PHE B 2 20  ? 16.136  -28.491 5.289   0.20 36.51  ? 20  PHE B CE1   1 
ATOM   7108  C  CE1   B PHE B 2 20  ? 15.973  -28.330 5.473   0.80 35.00  ? 20  PHE B CE1   1 
ATOM   7109  C  CE2   A PHE B 2 20  ? 14.712  -28.391 3.374   0.20 38.97  ? 20  PHE B CE2   1 
ATOM   7110  C  CE2   B PHE B 2 20  ? 14.760  -28.063 3.439   0.80 39.36  ? 20  PHE B CE2   1 
ATOM   7111  C  CZ    A PHE B 2 20  ? 14.938  -28.130 4.711   0.20 36.03  ? 20  PHE B CZ    1 
ATOM   7112  C  CZ    B PHE B 2 20  ? 14.867  -27.878 4.799   0.80 35.53  ? 20  PHE B CZ    1 
ATOM   7113  N  N     A TRP B 2 21  ? 16.349  -32.559 1.326   0.20 40.62  ? 21  TRP B N     1 
ATOM   7114  N  N     B TRP B 2 21  ? 16.379  -32.363 1.702   0.80 42.03  ? 21  TRP B N     1 
ATOM   7115  C  CA    A TRP B 2 21  ? 15.092  -33.273 1.140   0.20 38.15  ? 21  TRP B CA    1 
ATOM   7116  C  CA    B TRP B 2 21  ? 15.070  -32.982 1.535   0.80 40.36  ? 21  TRP B CA    1 
ATOM   7117  C  C     A TRP B 2 21  ? 15.202  -34.749 1.501   0.20 41.62  ? 21  TRP B C     1 
ATOM   7118  C  C     B TRP B 2 21  ? 15.076  -34.448 1.951   0.80 43.17  ? 21  TRP B C     1 
ATOM   7119  O  O     A TRP B 2 21  ? 14.171  -35.409 1.673   0.20 41.49  ? 21  TRP B O     1 
ATOM   7120  O  O     B TRP B 2 21  ? 14.086  -34.938 2.503   0.80 40.44  ? 21  TRP B O     1 
ATOM   7121  C  CB    A TRP B 2 21  ? 14.608  -33.118 -0.301  0.20 36.72  ? 21  TRP B CB    1 
ATOM   7122  C  CB    B TRP B 2 21  ? 14.605  -32.811 0.097   0.80 33.25  ? 21  TRP B CB    1 
ATOM   7123  C  CG    A TRP B 2 21  ? 14.220  -31.715 -0.641  0.20 38.17  ? 21  TRP B CG    1 
ATOM   7124  C  CG    B TRP B 2 21  ? 14.153  -31.412 -0.192  0.80 36.61  ? 21  TRP B CG    1 
ATOM   7125  C  CD1   A TRP B 2 21  ? 14.865  -30.869 -1.495  0.20 40.97  ? 21  TRP B CD1   1 
ATOM   7126  C  CD1   B TRP B 2 21  ? 14.804  -30.471 -0.936  0.80 42.50  ? 21  TRP B CD1   1 
ATOM   7127  C  CD2   A TRP B 2 21  ? 13.102  -30.987 -0.121  0.20 37.39  ? 21  TRP B CD2   1 
ATOM   7128  C  CD2   B TRP B 2 21  ? 12.953  -30.789 0.279   0.80 36.47  ? 21  TRP B CD2   1 
ATOM   7129  N  NE1   A TRP B 2 21  ? 14.213  -29.660 -1.544  0.20 39.95  ? 21  TRP B NE1   1 
ATOM   7130  N  NE1   B TRP B 2 21  ? 14.080  -29.305 -0.964  0.80 38.34  ? 21  TRP B NE1   1 
ATOM   7131  C  CE2   A TRP B 2 21  ? 13.128  -29.708 -0.709  0.20 35.76  ? 21  TRP B CE2   1 
ATOM   7132  C  CE2   B TRP B 2 21  ? 12.936  -29.476 -0.229  0.80 31.67  ? 21  TRP B CE2   1 
ATOM   7133  C  CE3   A TRP B 2 21  ? 12.081  -31.294 0.784   0.20 40.26  ? 21  TRP B CE3   1 
ATOM   7134  C  CE3   B TRP B 2 21  ? 11.890  -31.216 1.084   0.80 41.29  ? 21  TRP B CE3   1 
ATOM   7135  C  CZ2   A TRP B 2 21  ? 12.172  -28.737 -0.423  0.20 38.03  ? 21  TRP B CZ2   1 
ATOM   7136  C  CZ2   B TRP B 2 21  ? 11.899  -28.585 0.040   0.80 40.23  ? 21  TRP B CZ2   1 
ATOM   7137  C  CZ3   A TRP B 2 21  ? 11.133  -30.327 1.068   0.20 37.08  ? 21  TRP B CZ3   1 
ATOM   7138  C  CZ3   B TRP B 2 21  ? 10.859  -30.330 1.349   0.80 33.53  ? 21  TRP B CZ3   1 
ATOM   7139  C  CH2   A TRP B 2 21  ? 11.184  -29.065 0.465   0.20 37.55  ? 21  TRP B CH2   1 
ATOM   7140  C  CH2   B TRP B 2 21  ? 10.869  -29.032 0.825   0.80 36.70  ? 21  TRP B CH2   1 
ATOM   7141  N  N     A GLU B 2 22  ? 16.419  -35.279 1.617   0.20 42.23  ? 22  GLU B N     1 
ATOM   7142  N  N     B GLU B 2 22  ? 16.174  -35.167 1.702   0.80 42.07  ? 22  GLU B N     1 
ATOM   7143  C  CA    A GLU B 2 22  ? 16.619  -36.654 2.051   0.20 43.01  ? 22  GLU B CA    1 
ATOM   7144  C  CA    B GLU B 2 22  ? 16.295  -36.523 2.230   0.80 40.52  ? 22  GLU B CA    1 
ATOM   7145  C  C     A GLU B 2 22  ? 16.718  -36.790 3.563   0.20 44.41  ? 22  GLU B C     1 
ATOM   7146  C  C     B GLU B 2 22  ? 16.248  -36.524 3.751   0.80 45.77  ? 22  GLU B C     1 
ATOM   7147  O  O     A GLU B 2 22  ? 16.460  -37.878 4.091   0.20 46.82  ? 22  GLU B O     1 
ATOM   7148  O  O     B GLU B 2 22  ? 15.640  -37.409 4.365   0.80 44.94  ? 22  GLU B O     1 
ATOM   7149  C  CB    A GLU B 2 22  ? 17.887  -37.237 1.417   0.20 43.67  ? 22  GLU B CB    1 
ATOM   7150  C  CB    B GLU B 2 22  ? 17.600  -37.170 1.758   0.80 41.77  ? 22  GLU B CB    1 
ATOM   7151  C  CG    A GLU B 2 22  ? 17.853  -37.321 -0.100  0.20 48.06  ? 22  GLU B CG    1 
ATOM   7152  C  CG    B GLU B 2 22  ? 17.772  -37.266 0.251   0.80 48.18  ? 22  GLU B CG    1 
ATOM   7153  C  CD    A GLU B 2 22  ? 19.150  -37.852 -0.683  0.20 50.50  ? 22  GLU B CD    1 
ATOM   7154  C  CD    B GLU B 2 22  ? 19.107  -37.882 -0.147  0.80 51.08  ? 22  GLU B CD    1 
ATOM   7155  O  OE1   A GLU B 2 22  ? 20.021  -38.293 0.097   0.20 51.17  ? 22  GLU B OE1   1 
ATOM   7156  O  OE1   B GLU B 2 22  ? 19.659  -38.678 0.647   0.80 53.78  ? 22  GLU B OE1   1 
ATOM   7157  O  OE2   A GLU B 2 22  ? 19.297  -37.826 -1.924  0.20 48.21  ? 22  GLU B OE2   1 
ATOM   7158  O  OE2   B GLU B 2 22  ? 19.605  -37.563 -1.251  0.80 49.32  ? 22  GLU B OE2   1 
ATOM   7159  N  N     A VAL B 2 23  ? 17.085  -35.723 4.268   0.20 41.91  ? 23  VAL B N     1 
ATOM   7160  N  N     B VAL B 2 23  ? 16.887  -35.538 4.378   0.80 41.54  ? 23  VAL B N     1 
ATOM   7161  C  CA    A VAL B 2 23  ? 17.222  -35.806 5.716   0.20 43.98  ? 23  VAL B CA    1 
ATOM   7162  C  CA    B VAL B 2 23  ? 17.022  -35.554 5.830   0.80 44.27  ? 23  VAL B CA    1 
ATOM   7163  C  C     A VAL B 2 23  ? 15.931  -35.418 6.435   0.20 43.38  ? 23  VAL B C     1 
ATOM   7164  C  C     B VAL B 2 23  ? 15.691  -35.234 6.499   0.80 43.13  ? 23  VAL B C     1 
ATOM   7165  O  O     A VAL B 2 23  ? 15.642  -35.954 7.509   0.20 45.49  ? 23  VAL B O     1 
ATOM   7166  O  O     B VAL B 2 23  ? 15.271  -35.936 7.426   0.80 46.30  ? 23  VAL B O     1 
ATOM   7167  C  CB    A VAL B 2 23  ? 18.409  -34.948 6.195   0.20 42.52  ? 23  VAL B CB    1 
ATOM   7168  C  CB    B VAL B 2 23  ? 18.137  -34.591 6.276   0.80 42.60  ? 23  VAL B CB    1 
ATOM   7169  C  CG1   A VAL B 2 23  ? 18.123  -33.462 6.013   0.20 41.59  ? 23  VAL B CG1   1 
ATOM   7170  C  CG1   B VAL B 2 23  ? 18.103  -34.395 7.773   0.80 44.22  ? 23  VAL B CG1   1 
ATOM   7171  C  CG2   A VAL B 2 23  ? 18.751  -35.263 7.647   0.20 41.27  ? 23  VAL B CG2   1 
ATOM   7172  C  CG2   B VAL B 2 23  ? 19.491  -35.144 5.864   0.80 39.51  ? 23  VAL B CG2   1 
ATOM   7173  N  N     A ILE B 2 24  ? 15.135  -34.512 5.866   0.20 40.98  ? 24  ILE B N     1 
ATOM   7174  N  N     B ILE B 2 24  ? 15.003  -34.179 6.050   0.80 39.60  ? 24  ILE B N     1 
ATOM   7175  C  CA    A ILE B 2 24  ? 13.892  -34.117 6.521   0.20 45.82  ? 24  ILE B CA    1 
ATOM   7176  C  CA    B ILE B 2 24  ? 13.755  -33.833 6.737   0.80 46.67  ? 24  ILE B CA    1 
ATOM   7177  C  C     A ILE B 2 24  ? 12.749  -35.073 6.188   0.20 46.34  ? 24  ILE B C     1 
ATOM   7178  C  C     B ILE B 2 24  ? 12.624  -34.779 6.339   0.80 47.86  ? 24  ILE B C     1 
ATOM   7179  O  O     A ILE B 2 24  ? 11.830  -35.239 6.998   0.20 45.24  ? 24  ILE B O     1 
ATOM   7180  O  O     B ILE B 2 24  ? 11.672  -34.966 7.109   0.80 44.34  ? 24  ILE B O     1 
ATOM   7181  C  CB    A ILE B 2 24  ? 13.514  -32.668 6.166   0.20 41.10  ? 24  ILE B CB    1 
ATOM   7182  C  CB    B ILE B 2 24  ? 13.347  -32.364 6.505   0.80 38.51  ? 24  ILE B CB    1 
ATOM   7183  C  CG1   A ILE B 2 24  ? 13.206  -32.533 4.674   0.20 42.04  ? 24  ILE B CG1   1 
ATOM   7184  C  CG1   B ILE B 2 24  ? 13.091  -32.084 5.027   0.80 44.11  ? 24  ILE B CG1   1 
ATOM   7185  C  CG2   A ILE B 2 24  ? 14.620  -31.709 6.583   0.20 40.85  ? 24  ILE B CG2   1 
ATOM   7186  C  CG2   B ILE B 2 24  ? 14.389  -31.415 7.076   0.80 38.91  ? 24  ILE B CG2   1 
ATOM   7187  C  CD1   A ILE B 2 24  ? 12.624  -31.191 4.297   0.20 40.61  ? 24  ILE B CD1   1 
ATOM   7188  C  CD1   B ILE B 2 24  ? 12.333  -30.790 4.801   0.80 37.32  ? 24  ILE B CD1   1 
ATOM   7189  N  N     A SER B 2 25  ? 12.779  -35.706 5.012   0.20 43.80  ? 25  SER B N     1 
ATOM   7190  N  N     B SER B 2 25  ? 12.692  -35.383 5.148   0.80 42.58  ? 25  SER B N     1 
ATOM   7191  C  CA    A SER B 2 25  ? 11.764  -36.704 4.692   0.20 46.08  ? 25  SER B CA    1 
ATOM   7192  C  CA    B SER B 2 25  ? 11.692  -36.385 4.791   0.80 46.01  ? 25  SER B CA    1 
ATOM   7193  C  C     A SER B 2 25  ? 11.893  -37.919 5.600   0.20 49.11  ? 25  SER B C     1 
ATOM   7194  C  C     B SER B 2 25  ? 11.740  -37.562 5.750   0.80 48.72  ? 25  SER B C     1 
ATOM   7195  O  O     A SER B 2 25  ? 10.886  -38.527 5.982   0.20 50.05  ? 25  SER B O     1 
ATOM   7196  O  O     B SER B 2 25  ? 10.699  -38.042 6.210   0.80 50.93  ? 25  SER B O     1 
ATOM   7197  C  CB    A SER B 2 25  ? 11.869  -37.114 3.224   0.20 44.74  ? 25  SER B CB    1 
ATOM   7198  C  CB    B SER B 2 25  ? 11.895  -36.869 3.359   0.80 43.65  ? 25  SER B CB    1 
ATOM   7199  O  OG    A SER B 2 25  ? 11.593  -36.022 2.365   0.20 39.85  ? 25  SER B OG    1 
ATOM   7200  O  OG    B SER B 2 25  ? 11.545  -35.872 2.417   0.80 38.91  ? 25  SER B OG    1 
ATOM   7201  N  N     A ASP B 2 26  ? 13.125  -38.285 5.958   0.20 49.65  ? 26  ASP B N     1 
ATOM   7202  N  N     B ASP B 2 26  ? 12.943  -38.043 6.066   0.80 50.99  ? 26  ASP B N     1 
ATOM   7203  C  CA    A ASP B 2 26  ? 13.321  -39.370 6.912   0.20 50.29  ? 26  ASP B CA    1 
ATOM   7204  C  CA    B ASP B 2 26  ? 13.057  -39.117 7.044   0.80 50.31  ? 26  ASP B CA    1 
ATOM   7205  C  C     A ASP B 2 26  ? 12.865  -38.972 8.311   0.20 52.22  ? 26  ASP B C     1 
ATOM   7206  C  C     B ASP B 2 26  ? 12.536  -38.678 8.411   0.80 53.47  ? 26  ASP B C     1 
ATOM   7207  O  O     A ASP B 2 26  ? 12.381  -39.821 9.069   0.20 51.87  ? 26  ASP B O     1 
ATOM   7208  O  O     B ASP B 2 26  ? 11.912  -39.470 9.131   0.80 49.22  ? 26  ASP B O     1 
ATOM   7209  C  CB    A ASP B 2 26  ? 14.789  -39.794 6.927   0.20 50.72  ? 26  ASP B CB    1 
ATOM   7210  C  CB    B ASP B 2 26  ? 14.508  -39.587 7.138   0.80 51.55  ? 26  ASP B CB    1 
ATOM   7211  C  CG    A ASP B 2 26  ? 15.060  -40.923 7.900   0.20 54.22  ? 26  ASP B CG    1 
ATOM   7212  C  CG    B ASP B 2 26  ? 14.737  -40.520 8.306   0.80 53.02  ? 26  ASP B CG    1 
ATOM   7213  O  OD1   A ASP B 2 26  ? 14.684  -42.075 7.598   0.20 52.71  ? 26  ASP B OD1   1 
ATOM   7214  O  OD1   B ASP B 2 26  ? 14.228  -41.661 8.266   0.80 55.76  ? 26  ASP B OD1   1 
ATOM   7215  O  OD2   A ASP B 2 26  ? 15.649  -40.656 8.969   0.20 56.49  ? 26  ASP B OD2   1 
ATOM   7216  O  OD2   B ASP B 2 26  ? 15.415  -40.106 9.270   0.80 57.41  ? 26  ASP B OD2   1 
ATOM   7217  N  N     A GLU B 2 27  ? 13.004  -37.693 8.670   0.20 49.85  ? 27  GLU B N     1 
ATOM   7218  N  N     B GLU B 2 27  ? 12.770  -37.417 8.786   0.80 50.23  ? 27  GLU B N     1 
ATOM   7219  C  CA    A GLU B 2 27  ? 12.545  -37.236 9.979   0.20 49.89  ? 27  GLU B CA    1 
ATOM   7220  C  CA    B GLU B 2 27  ? 12.284  -36.946 10.081  0.80 50.54  ? 27  GLU B CA    1 
ATOM   7221  C  C     A GLU B 2 27  ? 11.024  -37.262 10.066  0.20 48.66  ? 27  GLU B C     1 
ATOM   7222  C  C     B GLU B 2 27  ? 10.763  -36.837 10.110  0.80 46.47  ? 27  GLU B C     1 
ATOM   7223  O  O     A GLU B 2 27  ? 10.457  -37.766 11.042  0.20 49.87  ? 27  GLU B O     1 
ATOM   7224  O  O     B GLU B 2 27  ? 10.156  -37.002 11.174  0.80 51.62  ? 27  GLU B O     1 
ATOM   7225  C  CB    A GLU B 2 27  ? 13.077  -35.830 10.265  0.20 49.33  ? 27  GLU B CB    1 
ATOM   7226  C  CB    B GLU B 2 27  ? 12.918  -35.594 10.436  0.80 49.90  ? 27  GLU B CB    1 
ATOM   7227  C  CG    A GLU B 2 27  ? 14.580  -35.763 10.501  0.20 45.34  ? 27  GLU B CG    1 
ATOM   7228  C  CG    B GLU B 2 27  ? 14.433  -35.636 10.703  0.80 45.09  ? 27  GLU B CG    1 
ATOM   7229  C  CD    A GLU B 2 27  ? 15.081  -34.343 10.698  0.20 43.13  ? 27  GLU B CD    1 
ATOM   7230  C  CD    B GLU B 2 27  ? 14.973  -34.331 11.280  0.80 43.93  ? 27  GLU B CD    1 
ATOM   7231  O  OE1   A GLU B 2 27  ? 14.247  -33.417 10.793  0.20 39.48  ? 27  GLU B OE1   1 
ATOM   7232  O  OE1   B GLU B 2 27  ? 14.188  -33.554 11.857  0.80 41.85  ? 27  GLU B OE1   1 
ATOM   7233  O  OE2   A GLU B 2 27  ? 16.313  -34.152 10.756  0.20 45.35  ? 27  GLU B OE2   1 
ATOM   7234  O  OE2   B GLU B 2 27  ? 16.188  -34.079 11.158  0.80 46.04  ? 27  GLU B OE2   1 
ATOM   7235  N  N     A HIS B 2 28  ? 10.345  -36.721 9.053   0.20 46.11  ? 28  HIS B N     1 
ATOM   7236  N  N     B HIS B 2 28  ? 10.133  -36.576 8.965   0.80 44.70  ? 28  HIS B N     1 
ATOM   7237  C  CA    A HIS B 2 28  ? 8.889   -36.697 9.053   0.20 50.21  ? 28  HIS B CA    1 
ATOM   7238  C  CA    B HIS B 2 28  ? 8.696   -36.344 8.892   0.80 51.10  ? 28  HIS B CA    1 
ATOM   7239  C  C     A HIS B 2 28  ? 8.273   -38.051 8.727   0.20 50.72  ? 28  HIS B C     1 
ATOM   7240  C  C     B HIS B 2 28  ? 7.906   -37.562 8.422   0.80 51.95  ? 28  HIS B C     1 
ATOM   7241  O  O     A HIS B 2 28  ? 7.082   -38.252 8.986   0.20 51.29  ? 28  HIS B O     1 
ATOM   7242  O  O     B HIS B 2 28  ? 6.719   -37.431 8.096   0.80 47.37  ? 28  HIS B O     1 
ATOM   7243  C  CB    A HIS B 2 28  ? 8.380   -35.651 8.059   0.20 45.91  ? 28  HIS B CB    1 
ATOM   7244  C  CB    B HIS B 2 28  ? 8.403   -35.165 7.971   0.80 43.68  ? 28  HIS B CB    1 
ATOM   7245  C  CG    A HIS B 2 28  ? 8.629   -34.239 8.486   0.20 44.31  ? 28  HIS B CG    1 
ATOM   7246  C  CG    B HIS B 2 28  ? 8.604   -33.832 8.613   0.80 44.36  ? 28  HIS B CG    1 
ATOM   7247  N  ND1   A HIS B 2 28  ? 7.689   -33.488 9.157   0.20 38.99  ? 28  HIS B ND1   1 
ATOM   7248  N  ND1   B HIS B 2 28  ? 9.699   -33.035 8.351   0.80 38.65  ? 28  HIS B ND1   1 
ATOM   7249  C  CD2   A HIS B 2 28  ? 9.710   -33.438 8.332   0.20 41.61  ? 28  HIS B CD2   1 
ATOM   7250  C  CD2   B HIS B 2 28  ? 7.845   -33.151 9.501   0.80 35.28  ? 28  HIS B CD2   1 
ATOM   7251  C  CE1   A HIS B 2 28  ? 8.180   -32.287 9.401   0.20 44.66  ? 28  HIS B CE1   1 
ATOM   7252  C  CE1   B HIS B 2 28  ? 9.606   -31.920 9.053   0.80 40.33  ? 28  HIS B CE1   1 
ATOM   7253  N  NE2   A HIS B 2 28  ? 9.406   -32.230 8.909   0.20 41.87  ? 28  HIS B NE2   1 
ATOM   7254  N  NE2   B HIS B 2 28  ? 8.492   -31.967 9.763   0.80 50.10  ? 28  HIS B NE2   1 
ATOM   7255  N  N     A GLY B 2 29  ? 9.047   -38.976 8.167   0.20 51.69  ? 29  GLY B N     1 
ATOM   7256  N  N     B GLY B 2 29  ? 8.530   -38.735 8.376   0.80 50.65  ? 29  GLY B N     1 
ATOM   7257  C  CA    A GLY B 2 29  ? 8.531   -40.289 7.839   0.20 53.02  ? 29  GLY B CA    1 
ATOM   7258  C  CA    B GLY B 2 29  ? 7.831   -39.927 7.942   0.80 54.80  ? 29  GLY B CA    1 
ATOM   7259  C  C     A GLY B 2 29  ? 7.936   -40.363 6.449   0.20 53.76  ? 29  GLY B C     1 
ATOM   7260  C  C     B GLY B 2 29  ? 7.456   -39.958 6.479   0.80 53.89  ? 29  GLY B C     1 
ATOM   7261  O  O     A GLY B 2 29  ? 6.837   -40.893 6.262   0.20 54.44  ? 29  GLY B O     1 
ATOM   7262  O  O     B GLY B 2 29  ? 6.533   -40.682 6.104   0.80 52.26  ? 29  GLY B O     1 
ATOM   7263  N  N     A ILE B 2 30  ? 8.655   -39.831 5.464   0.20 53.24  ? 30  ILE B N     1 
ATOM   7264  N  N     B ILE B 2 30  ? 8.140   -39.191 5.636   0.80 51.15  ? 30  ILE B N     1 
ATOM   7265  C  CA    A ILE B 2 30  ? 8.238   -39.862 4.068   0.20 54.31  ? 30  ILE B CA    1 
ATOM   7266  C  CA    B ILE B 2 30  ? 7.895   -39.193 4.198   0.80 55.39  ? 30  ILE B CA    1 
ATOM   7267  C  C     A ILE B 2 30  ? 9.252   -40.685 3.287   0.20 54.90  ? 30  ILE B C     1 
ATOM   7268  C  C     B ILE B 2 30  ? 8.905   -40.119 3.533   0.80 51.96  ? 30  ILE B C     1 
ATOM   7269  O  O     A ILE B 2 30  ? 10.462  -40.454 3.395   0.20 51.89  ? 30  ILE B O     1 
ATOM   7270  O  O     B ILE B 2 30  ? 10.108  -40.049 3.817   0.80 51.26  ? 30  ILE B O     1 
ATOM   7271  C  CB    A ILE B 2 30  ? 8.109   -38.446 3.477   0.20 53.72  ? 30  ILE B CB    1 
ATOM   7272  C  CB    B ILE B 2 30  ? 7.975   -37.772 3.614   0.80 52.85  ? 30  ILE B CB    1 
ATOM   7273  C  CG1   A ILE B 2 30  ? 7.065   -37.638 4.251   0.20 54.52  ? 30  ILE B CG1   1 
ATOM   7274  C  CG1   B ILE B 2 30  ? 7.130   -36.809 4.451   0.80 54.98  ? 30  ILE B CG1   1 
ATOM   7275  C  CG2   A ILE B 2 30  ? 7.744   -38.512 2.001   0.20 54.16  ? 30  ILE B CG2   1 
ATOM   7276  C  CG2   B ILE B 2 30  ? 7.500   -37.768 2.172   0.80 51.77  ? 30  ILE B CG2   1 
ATOM   7277  C  CD1   A ILE B 2 30  ? 6.839   -36.246 3.700   0.20 50.62  ? 30  ILE B CD1   1 
ATOM   7278  C  CD1   B ILE B 2 30  ? 5.675   -37.217 4.568   0.80 58.09  ? 30  ILE B CD1   1 
ATOM   7279  N  N     A ASP B 2 31  ? 8.760   -41.644 2.515   0.20 58.17  ? 31  ASP B N     1 
ATOM   7280  N  N     B ASP B 2 31  ? 8.423   -40.986 2.656   0.80 58.30  ? 31  ASP B N     1 
ATOM   7281  C  CA    A ASP B 2 31  ? 9.599   -42.481 1.670   0.20 58.06  ? 31  ASP B CA    1 
ATOM   7282  C  CA    B ASP B 2 31  ? 9.249   -41.960 1.960   0.80 56.77  ? 31  ASP B CA    1 
ATOM   7283  C  C     A ASP B 2 31  ? 9.853   -41.786 0.340   0.20 58.97  ? 31  ASP B C     1 
ATOM   7284  C  C     B ASP B 2 31  ? 9.672   -41.420 0.598   0.80 59.95  ? 31  ASP B C     1 
ATOM   7285  O  O     A ASP B 2 31  ? 9.218   -40.779 0.017   0.20 60.18  ? 31  ASP B O     1 
ATOM   7286  O  O     B ASP B 2 31  ? 9.219   -40.355 0.168   0.80 61.44  ? 31  ASP B O     1 
ATOM   7287  C  CB    A ASP B 2 31  ? 8.935   -43.847 1.483   0.20 59.63  ? 31  ASP B CB    1 
ATOM   7288  C  CB    B ASP B 2 31  ? 8.485   -43.285 1.825   0.80 60.48  ? 31  ASP B CB    1 
ATOM   7289  C  CG    A ASP B 2 31  ? 7.479   -43.745 1.066   0.20 62.08  ? 31  ASP B CG    1 
ATOM   7290  C  CG    B ASP B 2 31  ? 7.514   -43.294 0.659   0.80 62.77  ? 31  ASP B CG    1 
ATOM   7291  O  OD1   A ASP B 2 31  ? 7.080   -42.702 0.509   0.20 62.73  ? 31  ASP B OD1   1 
ATOM   7292  O  OD1   B ASP B 2 31  ? 6.860   -42.260 0.408   0.80 64.40  ? 31  ASP B OD1   1 
ATOM   7293  O  OD2   A ASP B 2 31  ? 6.728   -44.715 1.302   0.20 63.49  ? 31  ASP B OD2   1 
ATOM   7294  O  OD2   B ASP B 2 31  ? 7.405   -44.346 -0.007  0.80 62.27  ? 31  ASP B OD2   1 
ATOM   7295  N  N     A PRO B 2 32  ? 10.804  -42.284 -0.459  0.20 57.15  ? 32  PRO B N     1 
ATOM   7296  N  N     B PRO B 2 32  ? 10.578  -42.115 -0.104  0.80 55.82  ? 32  PRO B N     1 
ATOM   7297  C  CA    A PRO B 2 32  ? 11.051  -41.663 -1.773  0.20 57.10  ? 32  PRO B CA    1 
ATOM   7298  C  CA    B PRO B 2 32  ? 10.962  -41.656 -1.453  0.80 56.71  ? 32  PRO B CA    1 
ATOM   7299  C  C     A PRO B 2 32  ? 9.829   -41.608 -2.676  0.20 59.06  ? 32  PRO B C     1 
ATOM   7300  C  C     B PRO B 2 32  ? 9.791   -41.439 -2.398  0.80 58.05  ? 32  PRO B C     1 
ATOM   7301  O  O     A PRO B 2 32  ? 9.803   -40.787 -3.601  0.20 60.46  ? 32  PRO B O     1 
ATOM   7302  O  O     B PRO B 2 32  ? 9.865   -40.557 -3.262  0.80 59.47  ? 32  PRO B O     1 
ATOM   7303  C  CB    A PRO B 2 32  ? 12.151  -42.547 -2.374  0.20 57.34  ? 32  PRO B CB    1 
ATOM   7304  C  CB    B PRO B 2 32  ? 11.883  -42.778 -1.944  0.80 57.61  ? 32  PRO B CB    1 
ATOM   7305  C  CG    A PRO B 2 32  ? 12.885  -43.065 -1.189  0.20 57.57  ? 32  PRO B CG    1 
ATOM   7306  C  CG    B PRO B 2 32  ? 12.526  -43.285 -0.691  0.80 57.81  ? 32  PRO B CG    1 
ATOM   7307  C  CD    A PRO B 2 32  ? 11.849  -43.269 -0.117  0.20 57.26  ? 32  PRO B CD    1 
ATOM   7308  C  CD    B PRO B 2 32  ? 11.478  -43.177 0.389   0.80 54.40  ? 32  PRO B CD    1 
ATOM   7309  N  N     A THR B 2 33  ? 8.819   -42.443 -2.442  0.20 63.22  ? 33  THR B N     1 
ATOM   7310  N  N     B THR B 2 33  ? 8.708   -42.206 -2.261  0.80 63.98  ? 33  THR B N     1 
ATOM   7311  C  CA    A THR B 2 33  ? 7.604   -42.431 -3.247  0.20 64.92  ? 33  THR B CA    1 
ATOM   7312  C  CA    B THR B 2 33  ? 7.538   -42.009 -3.109  0.80 64.58  ? 33  THR B CA    1 
ATOM   7313  C  C     A THR B 2 33  ? 6.601   -41.375 -2.793  0.20 64.06  ? 33  THR B C     1 
ATOM   7314  C  C     B THR B 2 33  ? 6.695   -40.819 -2.673  0.80 64.82  ? 33  THR B C     1 
ATOM   7315  O  O     A THR B 2 33  ? 5.487   -41.333 -3.328  0.20 63.33  ? 33  THR B O     1 
ATOM   7316  O  O     B THR B 2 33  ? 5.950   -40.267 -3.491  0.80 68.64  ? 33  THR B O     1 
ATOM   7317  C  CB    A THR B 2 33  ? 6.942   -43.811 -3.225  0.20 69.47  ? 33  THR B CB    1 
ATOM   7318  C  CB    B THR B 2 33  ? 6.676   -43.275 -3.119  0.80 70.34  ? 33  THR B CB    1 
ATOM   7319  O  OG1   A THR B 2 33  ? 6.601   -44.159 -1.877  0.20 64.86  ? 33  THR B OG1   1 
ATOM   7320  O  OG1   B THR B 2 33  ? 7.510   -44.420 -3.344  0.80 74.45  ? 33  THR B OG1   1 
ATOM   7321  C  CG2   A THR B 2 33  ? 7.883   -44.864 -3.796  0.20 70.85  ? 33  THR B CG2   1 
ATOM   7322  C  CG2   B THR B 2 33  ? 5.622   -43.201 -4.221  0.80 68.81  ? 33  THR B CG2   1 
ATOM   7323  N  N     A GLY B 2 34  ? 6.964   -40.532 -1.828  0.20 62.34  ? 34  GLY B N     1 
ATOM   7324  N  N     B GLY B 2 34  ? 6.801   -40.404 -1.413  0.80 62.27  ? 34  GLY B N     1 
ATOM   7325  C  CA    A GLY B 2 34  ? 6.088   -39.484 -1.351  0.20 61.32  ? 34  GLY B CA    1 
ATOM   7326  C  CA    B GLY B 2 34  ? 6.027   -39.298 -0.889  0.80 61.87  ? 34  GLY B CA    1 
ATOM   7327  C  C     A GLY B 2 34  ? 5.029   -39.921 -0.363  0.20 58.31  ? 34  GLY B C     1 
ATOM   7328  C  C     B GLY B 2 34  ? 4.987   -39.690 0.134   0.80 53.70  ? 34  GLY B C     1 
ATOM   7329  O  O     A GLY B 2 34  ? 4.187   -39.098 0.017   0.20 58.94  ? 34  GLY B O     1 
ATOM   7330  O  O     B GLY B 2 34  ? 4.433   -38.807 0.796   0.80 61.53  ? 34  GLY B O     1 
ATOM   7331  N  N     A SER B 2 35  ? 5.041   -41.179 0.065   0.20 62.05  ? 35  SER B N     1 
ATOM   7332  N  N     B SER B 2 35  ? 4.708   -40.980 0.290   0.80 62.21  ? 35  SER B N     1 
ATOM   7333  C  CA    A SER B 2 35  ? 4.044   -41.693 0.990   0.20 62.12  ? 35  SER B CA    1 
ATOM   7334  C  CA    B SER B 2 35  ? 3.689   -41.428 1.226   0.80 61.59  ? 35  SER B CA    1 
ATOM   7335  C  C     A SER B 2 35  ? 4.524   -41.549 2.429   0.20 60.06  ? 35  SER B C     1 
ATOM   7336  C  C     B SER B 2 35  ? 4.191   -41.323 2.662   0.80 60.07  ? 35  SER B C     1 
ATOM   7337  O  O     A SER B 2 35  ? 5.720   -41.629 2.719   0.20 59.15  ? 35  SER B O     1 
ATOM   7338  O  O     B SER B 2 35  ? 5.382   -41.469 2.942   0.80 57.11  ? 35  SER B O     1 
ATOM   7339  C  CB    A SER B 2 35  ? 3.739   -43.162 0.690   0.20 65.62  ? 35  SER B CB    1 
ATOM   7340  C  CB    B SER B 2 35  ? 3.287   -42.871 0.920   0.80 67.37  ? 35  SER B CB    1 
ATOM   7341  O  OG    A SER B 2 35  ? 3.399   -43.346 -0.674  0.20 65.07  ? 35  SER B OG    1 
ATOM   7342  O  OG    B SER B 2 35  ? 3.394   -43.151 -0.468  0.80 65.67  ? 35  SER B OG    1 
ATOM   7343  N  N     A TYR B 2 36  ? 3.573   -41.337 3.335   0.20 59.88  ? 36  TYR B N     1 
ATOM   7344  N  N     B TYR B 2 36  ? 3.261   -41.080 3.581   0.80 58.45  ? 36  TYR B N     1 
ATOM   7345  C  CA    A TYR B 2 36  ? 3.872   -41.183 4.754   0.20 60.53  ? 36  TYR B CA    1 
ATOM   7346  C  CA    B TYR B 2 36  ? 3.596   -40.894 4.986   0.80 61.27  ? 36  TYR B CA    1 
ATOM   7347  C  C     A TYR B 2 36  ? 3.814   -42.551 5.423   0.20 63.13  ? 36  TYR B C     1 
ATOM   7348  C  C     B TYR B 2 36  ? 3.657   -42.244 5.692   0.80 64.25  ? 36  TYR B C     1 
ATOM   7349  O  O     A TYR B 2 36  ? 2.742   -43.156 5.527   0.20 65.53  ? 36  TYR B O     1 
ATOM   7350  O  O     B TYR B 2 36  ? 2.664   -42.980 5.722   0.80 66.26  ? 36  TYR B O     1 
ATOM   7351  C  CB    A TYR B 2 36  ? 2.899   -40.209 5.412   0.20 61.52  ? 36  TYR B CB    1 
ATOM   7352  C  CB    B TYR B 2 36  ? 2.579   -39.985 5.671   0.80 63.89  ? 36  TYR B CB    1 
ATOM   7353  C  CG    A TYR B 2 36  ? 3.007   -40.169 6.920   0.20 58.44  ? 36  TYR B CG    1 
ATOM   7354  C  CG    B TYR B 2 36  ? 2.749   -39.951 7.170   0.80 58.54  ? 36  TYR B CG    1 
ATOM   7355  C  CD1   A TYR B 2 36  ? 4.015   -39.446 7.545   0.20 56.74  ? 36  TYR B CD1   1 
ATOM   7356  C  CD1   B TYR B 2 36  ? 3.849   -39.332 7.747   0.80 56.79  ? 36  TYR B CD1   1 
ATOM   7357  C  CD2   A TYR B 2 36  ? 2.101   -40.854 7.719   0.20 57.34  ? 36  TYR B CD2   1 
ATOM   7358  C  CD2   B TYR B 2 36  ? 1.818   -40.546 8.007   0.80 56.95  ? 36  TYR B CD2   1 
ATOM   7359  C  CE1   A TYR B 2 36  ? 4.118   -39.408 8.923   0.20 55.91  ? 36  TYR B CE1   1 
ATOM   7360  C  CE1   B TYR B 2 36  ? 4.013   -39.299 9.116   0.80 55.66  ? 36  TYR B CE1   1 
ATOM   7361  C  CE2   A TYR B 2 36  ? 2.196   -40.822 9.097   0.20 58.50  ? 36  TYR B CE2   1 
ATOM   7362  C  CE2   B TYR B 2 36  ? 1.972   -40.520 9.378   0.80 58.98  ? 36  TYR B CE2   1 
ATOM   7363  C  CZ    A TYR B 2 36  ? 3.206   -40.098 9.693   0.20 57.64  ? 36  TYR B CZ    1 
ATOM   7364  C  CZ    B TYR B 2 36  ? 3.070   -39.896 9.926   0.80 57.35  ? 36  TYR B CZ    1 
ATOM   7365  O  OH    A TYR B 2 36  ? 3.303   -40.063 11.065  0.20 59.26  ? 36  TYR B OH    1 
ATOM   7366  O  OH    B TYR B 2 36  ? 3.228   -39.871 11.289  0.80 60.20  ? 36  TYR B OH    1 
ATOM   7367  N  N     A HIS B 2 37  ? 4.968   -43.038 5.878   0.20 60.82  ? 37  HIS B N     1 
ATOM   7368  N  N     B HIS B 2 37  ? 4.816   -42.558 6.278   0.80 58.92  ? 37  HIS B N     1 
ATOM   7369  C  CA    A HIS B 2 37  ? 5.031   -44.294 6.614   0.20 61.88  ? 37  HIS B CA    1 
ATOM   7370  C  CA    B HIS B 2 37  ? 5.028   -43.817 6.982   0.80 58.62  ? 37  HIS B CA    1 
ATOM   7371  C  C     A HIS B 2 37  ? 5.666   -44.076 7.981   0.20 61.45  ? 37  HIS B C     1 
ATOM   7372  C  C     B HIS B 2 37  ? 5.400   -43.604 8.445   0.80 61.99  ? 37  HIS B C     1 
ATOM   7373  O  O     A HIS B 2 37  ? 6.621   -44.770 8.347   0.20 61.72  ? 37  HIS B O     1 
ATOM   7374  O  O     B HIS B 2 37  ? 5.885   -44.532 9.101   0.80 62.79  ? 37  HIS B O     1 
ATOM   7375  C  CB    A HIS B 2 37  ? 5.809   -45.348 5.824   0.20 66.18  ? 37  HIS B CB    1 
ATOM   7376  C  CB    B HIS B 2 37  ? 6.108   -44.647 6.285   0.80 64.82  ? 37  HIS B CB    1 
ATOM   7377  C  CG    A HIS B 2 37  ? 5.038   -45.944 4.687   0.20 69.86  ? 37  HIS B CG    1 
ATOM   7378  C  CG    B HIS B 2 37  ? 5.666   -45.253 4.990   0.80 67.09  ? 37  HIS B CG    1 
ATOM   7379  N  ND1   A HIS B 2 37  ? 4.720   -45.235 3.549   0.20 69.97  ? 37  HIS B ND1   1 
ATOM   7380  N  ND1   B HIS B 2 37  ? 5.112   -44.509 3.970   0.80 68.23  ? 37  HIS B ND1   1 
ATOM   7381  C  CD2   A HIS B 2 37  ? 4.521   -47.184 4.515   0.20 70.76  ? 37  HIS B CD2   1 
ATOM   7382  C  CD2   B HIS B 2 37  ? 5.697   -46.533 4.547   0.80 76.88  ? 37  HIS B CD2   1 
ATOM   7383  C  CE1   A HIS B 2 37  ? 4.041   -46.013 2.724   0.20 69.90  ? 37  HIS B CE1   1 
ATOM   7384  C  CE1   B HIS B 2 37  ? 4.823   -45.304 2.954   0.80 71.90  ? 37  HIS B CE1   1 
ATOM   7385  N  NE2   A HIS B 2 37  ? 3.906   -47.200 3.286   0.20 69.94  ? 37  HIS B NE2   1 
ATOM   7386  N  NE2   B HIS B 2 37  ? 5.166   -46.537 3.280   0.80 78.83  ? 37  HIS B NE2   1 
ATOM   7387  N  N     A GLY B 2 38  ? 5.145   -43.115 8.737   0.20 60.24  ? 38  GLY B N     1 
ATOM   7388  N  N     B GLY B 2 38  ? 5.187   -42.402 8.972   0.80 59.28  ? 38  GLY B N     1 
ATOM   7389  C  CA    A GLY B 2 38  ? 5.650   -42.790 10.051  0.20 59.41  ? 38  GLY B CA    1 
ATOM   7390  C  CA    B GLY B 2 38  ? 5.609   -42.112 10.323  0.80 58.97  ? 38  GLY B CA    1 
ATOM   7391  C  C     A GLY B 2 38  ? 4.812   -43.391 11.161  0.20 61.04  ? 38  GLY B C     1 
ATOM   7392  C  C     B GLY B 2 38  ? 4.671   -42.676 11.369  0.80 60.42  ? 38  GLY B C     1 
ATOM   7393  O  O     A GLY B 2 38  ? 4.035   -44.331 10.957  0.20 61.67  ? 38  GLY B O     1 
ATOM   7394  O  O     B GLY B 2 38  ? 3.514   -42.997 11.105  0.80 66.55  ? 38  GLY B O     1 
ATOM   7395  N  N     A ASP B 2 39  ? 4.973   -42.834 12.359  0.20 62.08  ? 39  ASP B N     1 
ATOM   7396  N  N     B ASP B 2 39  ? 5.197   -42.789 12.587  0.80 62.48  ? 39  ASP B N     1 
ATOM   7397  C  CA    A ASP B 2 39  ? 4.243   -43.309 13.528  0.20 64.12  ? 39  ASP B CA    1 
ATOM   7398  C  CA    B ASP B 2 39  ? 4.462   -43.333 13.719  0.80 64.27  ? 39  ASP B CA    1 
ATOM   7399  C  C     A ASP B 2 39  ? 4.167   -42.224 14.593  0.20 65.20  ? 39  ASP B C     1 
ATOM   7400  C  C     B ASP B 2 39  ? 4.086   -42.264 14.739  0.80 65.43  ? 39  ASP B C     1 
ATOM   7401  O  O     A ASP B 2 39  ? 4.391   -42.489 15.779  0.20 66.63  ? 39  ASP B O     1 
ATOM   7402  O  O     B ASP B 2 39  ? 3.711   -42.602 15.866  0.80 69.08  ? 39  ASP B O     1 
ATOM   7403  C  CB    A ASP B 2 39  ? 4.900   -44.573 14.088  0.20 66.23  ? 39  ASP B CB    1 
ATOM   7404  C  CB    B ASP B 2 39  ? 5.285   -44.434 14.391  0.80 68.23  ? 39  ASP B CB    1 
ATOM   7405  C  CG    A ASP B 2 39  ? 6.411   -44.460 14.166  0.20 68.06  ? 39  ASP B CG    1 
ATOM   7406  C  CG    B ASP B 2 39  ? 6.577   -43.906 14.992  0.80 73.72  ? 39  ASP B CG    1 
ATOM   7407  O  OD1   A ASP B 2 39  ? 6.945   -43.373 13.861  0.20 66.82  ? 39  ASP B OD1   1 
ATOM   7408  O  OD1   B ASP B 2 39  ? 6.542   -43.427 16.147  0.80 80.86  ? 39  ASP B OD1   1 
ATOM   7409  O  OD2   A ASP B 2 39  ? 7.064   -45.462 14.527  0.20 66.28  ? 39  ASP B OD2   1 
ATOM   7410  O  OD2   B ASP B 2 39  ? 7.625   -43.957 14.309  0.80 70.99  ? 39  ASP B OD2   1 
ATOM   7411  N  N     A SER B 2 40  ? 3.850   -41.000 14.177  0.20 64.95  ? 40  SER B N     1 
ATOM   7412  N  N     B SER B 2 40  ? 4.179   -40.987 14.376  0.80 66.56  ? 40  SER B N     1 
ATOM   7413  C  CA    A SER B 2 40  ? 3.745   -39.874 15.093  0.20 59.61  ? 40  SER B CA    1 
ATOM   7414  C  CA    B SER B 2 40  ? 3.886   -39.891 15.290  0.80 58.72  ? 40  SER B CA    1 
ATOM   7415  C  C     A SER B 2 40  ? 2.952   -38.767 14.416  0.20 60.24  ? 40  SER B C     1 
ATOM   7416  C  C     B SER B 2 40  ? 3.193   -38.769 14.535  0.80 59.73  ? 40  SER B C     1 
ATOM   7417  O  O     A SER B 2 40  ? 3.188   -38.455 13.247  0.20 59.72  ? 40  SER B O     1 
ATOM   7418  O  O     B SER B 2 40  ? 3.673   -38.337 13.484  0.80 61.16  ? 40  SER B O     1 
ATOM   7419  C  CB    A SER B 2 40  ? 5.127   -39.357 15.510  0.20 59.92  ? 40  SER B CB    1 
ATOM   7420  C  CB    B SER B 2 40  ? 5.164   -39.360 15.948  0.80 59.94  ? 40  SER B CB    1 
ATOM   7421  O  OG    A SER B 2 40  ? 5.013   -38.225 16.355  0.20 62.14  ? 40  SER B OG    1 
ATOM   7422  O  OG    B SER B 2 40  ? 4.906   -38.167 16.670  0.80 63.48  ? 40  SER B OG    1 
ATOM   7423  N  N     A ASP B 2 41  ? 2.016   -38.177 15.160  0.20 64.20  ? 41  ASP B N     1 
ATOM   7424  N  N     B ASP B 2 41  ? 2.072   -38.294 15.080  0.80 64.68  ? 41  ASP B N     1 
ATOM   7425  C  CA    A ASP B 2 41  ? 1.213   -37.085 14.626  0.20 62.33  ? 41  ASP B CA    1 
ATOM   7426  C  CA    B ASP B 2 41  ? 1.374   -37.163 14.482  0.80 62.45  ? 41  ASP B CA    1 
ATOM   7427  C  C     A ASP B 2 41  ? 1.980   -35.771 14.563  0.20 59.37  ? 41  ASP B C     1 
ATOM   7428  C  C     B ASP B 2 41  ? 2.187   -35.877 14.561  0.80 59.34  ? 41  ASP B C     1 
ATOM   7429  O  O     A ASP B 2 41  ? 1.596   -34.879 13.797  0.20 55.40  ? 41  ASP B O     1 
ATOM   7430  O  O     B ASP B 2 41  ? 1.940   -34.954 13.776  0.80 52.86  ? 41  ASP B O     1 
ATOM   7431  C  CB    A ASP B 2 41  ? -0.054  -36.907 15.466  0.20 66.79  ? 41  ASP B CB    1 
ATOM   7432  C  CB    B ASP B 2 41  ? 0.010   -36.964 15.155  0.80 67.81  ? 41  ASP B CB    1 
ATOM   7433  C  CG    A ASP B 2 41  ? -0.932  -38.146 15.467  0.20 67.53  ? 41  ASP B CG    1 
ATOM   7434  C  CG    B ASP B 2 41  ? -1.050  -37.938 14.646  0.80 68.47  ? 41  ASP B CG    1 
ATOM   7435  O  OD1   A ASP B 2 41  ? -0.482  -39.195 15.977  0.20 64.52  ? 41  ASP B OD1   1 
ATOM   7436  O  OD1   B ASP B 2 41  ? -1.499  -37.794 13.488  0.80 58.19  ? 41  ASP B OD1   1 
ATOM   7437  O  OD2   A ASP B 2 41  ? -2.071  -38.070 14.958  0.20 64.08  ? 41  ASP B OD2   1 
ATOM   7438  O  OD2   B ASP B 2 41  ? -1.435  -38.849 15.409  0.80 70.49  ? 41  ASP B OD2   1 
ATOM   7439  N  N     A LEU B 2 42  ? 3.057   -35.633 15.339  0.20 59.27  ? 42  LEU B N     1 
ATOM   7440  N  N     B LEU B 2 42  ? 3.155   -35.796 15.481  0.80 59.30  ? 42  LEU B N     1 
ATOM   7441  C  CA    A LEU B 2 42  ? 3.860   -34.417 15.315  0.20 59.02  ? 42  LEU B CA    1 
ATOM   7442  C  CA    B LEU B 2 42  ? 4.009   -34.615 15.564  0.80 59.77  ? 42  LEU B CA    1 
ATOM   7443  C  C     A LEU B 2 42  ? 4.613   -34.230 14.004  0.20 56.79  ? 42  LEU B C     1 
ATOM   7444  C  C     B LEU B 2 42  ? 4.802   -34.378 14.283  0.80 58.12  ? 42  LEU B C     1 
ATOM   7445  O  O     A LEU B 2 42  ? 5.143   -33.140 13.765  0.20 55.78  ? 42  LEU B O     1 
ATOM   7446  O  O     B LEU B 2 42  ? 5.336   -33.280 14.089  0.80 57.18  ? 42  LEU B O     1 
ATOM   7447  C  CB    A LEU B 2 42  ? 4.851   -34.422 16.481  0.20 59.01  ? 42  LEU B CB    1 
ATOM   7448  C  CB    B LEU B 2 42  ? 4.964   -34.734 16.753  0.80 58.69  ? 42  LEU B CB    1 
ATOM   7449  C  CG    A LEU B 2 42  ? 4.260   -34.573 17.884  0.20 62.54  ? 42  LEU B CG    1 
ATOM   7450  C  CG    B LEU B 2 42  ? 4.374   -34.476 18.140  0.80 63.83  ? 42  LEU B CG    1 
ATOM   7451  C  CD1   A LEU B 2 42  ? 5.365   -34.602 18.929  0.20 62.22  ? 42  LEU B CD1   1 
ATOM   7452  C  CD1   B LEU B 2 42  ? 5.472   -34.505 19.193  0.80 62.82  ? 42  LEU B CD1   1 
ATOM   7453  C  CD2   A LEU B 2 42  ? 3.271   -33.456 18.179  0.20 61.21  ? 42  LEU B CD2   1 
ATOM   7454  C  CD2   B LEU B 2 42  ? 3.632   -33.150 18.175  0.80 62.12  ? 42  LEU B CD2   1 
ATOM   7455  N  N     A GLN B 2 43  ? 4.673   -35.256 13.155  0.20 53.66  ? 43  GLN B N     1 
ATOM   7456  N  N     B GLN B 2 43  ? 4.893   -35.376 13.405  0.80 52.68  ? 43  GLN B N     1 
ATOM   7457  C  CA    A GLN B 2 43  ? 5.380   -35.147 11.886  0.20 52.12  ? 43  GLN B CA    1 
ATOM   7458  C  CA    B GLN B 2 43  ? 5.546   -35.189 12.120  0.80 52.22  ? 43  GLN B CA    1 
ATOM   7459  C  C     A GLN B 2 43  ? 4.532   -34.515 10.790  0.20 51.65  ? 43  GLN B C     1 
ATOM   7460  C  C     B GLN B 2 43  ? 4.643   -34.534 11.082  0.80 52.48  ? 43  GLN B C     1 
ATOM   7461  O  O     A GLN B 2 43  ? 5.091   -33.977 9.828   0.20 47.20  ? 43  GLN B O     1 
ATOM   7462  O  O     B GLN B 2 43  ? 5.138   -34.123 10.029  0.80 46.86  ? 43  GLN B O     1 
ATOM   7463  C  CB    A GLN B 2 43  ? 5.859   -36.529 11.436  0.20 52.39  ? 43  GLN B CB    1 
ATOM   7464  C  CB    B GLN B 2 43  ? 6.046   -36.538 11.598  0.80 52.18  ? 43  GLN B CB    1 
ATOM   7465  C  CG    A GLN B 2 43  ? 6.769   -37.222 12.439  0.20 53.91  ? 43  GLN B CG    1 
ATOM   7466  C  CG    B GLN B 2 43  ? 6.770   -37.359 12.654  0.80 53.77  ? 43  GLN B CG    1 
ATOM   7467  C  CD    A GLN B 2 43  ? 7.019   -38.679 12.096  0.20 57.51  ? 43  GLN B CD    1 
ATOM   7468  C  CD    B GLN B 2 43  ? 6.937   -38.813 12.255  0.80 58.14  ? 43  GLN B CD    1 
ATOM   7469  O  OE1   A GLN B 2 43  ? 6.153   -39.358 11.544  0.20 57.03  ? 43  GLN B OE1   1 
ATOM   7470  O  OE1   B GLN B 2 43  ? 5.963   -39.561 12.174  0.80 53.74  ? 43  GLN B OE1   1 
ATOM   7471  N  NE2   A GLN B 2 43  ? 8.211   -39.168 12.424  0.20 57.67  ? 43  GLN B NE2   1 
ATOM   7472  N  NE2   B GLN B 2 43  ? 8.177   -39.220 11.999  0.80 60.01  ? 43  GLN B NE2   1 
ATOM   7473  N  N     A LEU B 2 44  ? 3.206   -34.558 10.914  0.20 50.73  ? 44  LEU B N     1 
ATOM   7474  N  N     B LEU B 2 44  ? 3.339   -34.406 11.349  0.80 50.14  ? 44  LEU B N     1 
ATOM   7475  C  CA    A LEU B 2 44  ? 2.313   -34.056 9.878   0.20 47.50  ? 44  LEU B CA    1 
ATOM   7476  C  CA    B LEU B 2 44  ? 2.409   -33.927 10.336  0.80 44.55  ? 44  LEU B CA    1 
ATOM   7477  C  C     A LEU B 2 44  ? 1.597   -32.769 10.264  0.20 49.61  ? 44  LEU B C     1 
ATOM   7478  C  C     B LEU B 2 44  ? 1.761   -32.584 10.644  0.80 48.93  ? 44  LEU B C     1 
ATOM   7479  O  O     A LEU B 2 44  ? 0.791   -32.268 9.473   0.20 51.27  ? 44  LEU B O     1 
ATOM   7480  O  O     B LEU B 2 44  ? 1.181   -31.986 9.733   0.80 50.14  ? 44  LEU B O     1 
ATOM   7481  C  CB    A LEU B 2 44  ? 1.280   -35.129 9.509   0.20 51.79  ? 44  LEU B CB    1 
ATOM   7482  C  CB    B LEU B 2 44  ? 1.300   -34.964 10.100  0.80 52.77  ? 44  LEU B CB    1 
ATOM   7483  C  CG    A LEU B 2 44  ? 1.836   -36.422 8.907   0.20 53.36  ? 44  LEU B CG    1 
ATOM   7484  C  CG    B LEU B 2 44  ? 1.225   -35.537 8.684   0.80 55.52  ? 44  LEU B CG    1 
ATOM   7485  C  CD1   A LEU B 2 44  ? 0.711   -37.389 8.566   0.20 52.35  ? 44  LEU B CD1   1 
ATOM   7486  C  CD1   B LEU B 2 44  ? 2.549   -36.180 8.306   0.80 46.36  ? 44  LEU B CD1   1 
ATOM   7487  C  CD2   A LEU B 2 44  ? 2.677   -36.123 7.678   0.20 50.70  ? 44  LEU B CD2   1 
ATOM   7488  C  CD2   B LEU B 2 44  ? 0.089   -36.536 8.552   0.80 52.85  ? 44  LEU B CD2   1 
ATOM   7489  N  N     A GLU B 2 45  ? 1.864   -32.219 11.451  0.20 50.03  ? 45  GLU B N     1 
ATOM   7490  N  N     B GLU B 2 45  ? 1.842   -32.094 11.884  0.80 48.60  ? 45  GLU B N     1 
ATOM   7491  C  CA    A GLU B 2 45  ? 1.196   -30.987 11.862  0.20 52.91  ? 45  GLU B CA    1 
ATOM   7492  C  CA    B GLU B 2 45  ? 1.143   -30.860 12.240  0.80 53.80  ? 45  GLU B CA    1 
ATOM   7493  C  C     A GLU B 2 45  ? 1.608   -29.818 10.975  0.20 52.23  ? 45  GLU B C     1 
ATOM   7494  C  C     B GLU B 2 45  ? 1.567   -29.699 11.348  0.80 53.11  ? 45  GLU B C     1 
ATOM   7495  O  O     A GLU B 2 45  ? 0.760   -29.150 10.371  0.20 52.18  ? 45  GLU B O     1 
ATOM   7496  O  O     B GLU B 2 45  ? 0.725   -28.938 10.857  0.80 54.66  ? 45  GLU B O     1 
ATOM   7497  C  CB    A GLU B 2 45  ? 1.502   -30.686 13.332  0.20 51.01  ? 45  GLU B CB    1 
ATOM   7498  C  CB    B GLU B 2 45  ? 1.388   -30.515 13.708  0.80 48.07  ? 45  GLU B CB    1 
ATOM   7499  C  CG    A GLU B 2 45  ? 0.957   -31.721 14.301  0.20 59.28  ? 45  GLU B CG    1 
ATOM   7500  C  CG    B GLU B 2 45  ? 0.798   -31.517 14.683  0.80 61.59  ? 45  GLU B CG    1 
ATOM   7501  C  CD    A GLU B 2 45  ? 1.142   -31.319 15.751  0.20 62.46  ? 45  GLU B CD    1 
ATOM   7502  C  CD    B GLU B 2 45  ? 0.230   -30.854 15.922  0.80 70.04  ? 45  GLU B CD    1 
ATOM   7503  O  OE1   A GLU B 2 45  ? 1.719   -30.241 16.004  0.20 60.11  ? 45  GLU B OE1   1 
ATOM   7504  O  OE1   B GLU B 2 45  ? 0.081   -29.614 15.909  0.80 79.21  ? 45  GLU B OE1   1 
ATOM   7505  O  OE2   A GLU B 2 45  ? 0.707   -32.082 16.640  0.20 67.54  ? 45  GLU B OE2   1 
ATOM   7506  O  OE2   B GLU B 2 45  ? -0.072  -31.568 16.905  0.80 77.23  ? 45  GLU B OE2   1 
ATOM   7507  N  N     A ARG B 2 46  ? 2.910   -29.558 10.882  0.20 51.44  ? 46  ARG B N     1 
ATOM   7508  N  N     B ARG B 2 46  ? 2.872   -29.549 11.120  0.80 51.84  ? 46  ARG B N     1 
ATOM   7509  C  CA    A ARG B 2 46  ? 3.451   -28.485 10.054  0.20 47.67  ? 46  ARG B CA    1 
ATOM   7510  C  CA    B ARG B 2 46  ? 3.400   -28.423 10.359  0.80 46.70  ? 46  ARG B CA    1 
ATOM   7511  C  C     A ARG B 2 46  ? 4.182   -29.046 8.836   0.20 47.60  ? 46  ARG B C     1 
ATOM   7512  C  C     B ARG B 2 46  ? 4.081   -28.879 9.068   0.80 48.65  ? 46  ARG B C     1 
ATOM   7513  O  O     A ARG B 2 46  ? 5.248   -28.565 8.452   0.20 45.16  ? 46  ARG B O     1 
ATOM   7514  O  O     B ARG B 2 46  ? 4.958   -28.191 8.541   0.80 43.55  ? 46  ARG B O     1 
ATOM   7515  C  CB    A ARG B 2 46  ? 4.373   -27.586 10.874  0.20 49.78  ? 46  ARG B CB    1 
ATOM   7516  C  CB    B ARG B 2 46  ? 4.349   -27.599 11.230  0.80 50.46  ? 46  ARG B CB    1 
ATOM   7517  C  CG    A ARG B 2 46  ? 3.746   -27.085 12.172  0.20 50.42  ? 46  ARG B CG    1 
ATOM   7518  C  CG    B ARG B 2 46  ? 3.638   -26.967 12.429  0.80 48.95  ? 46  ARG B CG    1 
ATOM   7519  C  CD    A ARG B 2 46  ? 4.666   -26.137 12.926  0.20 53.22  ? 46  ARG B CD    1 
ATOM   7520  C  CD    B ARG B 2 46  ? 4.554   -26.112 13.272  0.80 54.11  ? 46  ARG B CD    1 
ATOM   7521  N  NE    A ARG B 2 46  ? 4.782   -24.841 12.267  0.20 54.92  ? 46  ARG B NE    1 
ATOM   7522  N  NE    B ARG B 2 46  ? 3.907   -24.860 13.648  0.80 60.71  ? 46  ARG B NE    1 
ATOM   7523  C  CZ    A ARG B 2 46  ? 5.466   -23.811 12.750  0.20 54.55  ? 46  ARG B CZ    1 
ATOM   7524  C  CZ    B ARG B 2 46  ? 4.094   -23.706 13.022  0.80 64.75  ? 46  ARG B CZ    1 
ATOM   7525  N  NH1   A ARG B 2 46  ? 6.111   -23.889 13.902  0.20 51.06  ? 46  ARG B NH1   1 
ATOM   7526  N  NH1   B ARG B 2 46  ? 4.934   -23.600 12.004  0.80 58.48  ? 46  ARG B NH1   1 
ATOM   7527  N  NH2   A ARG B 2 46  ? 5.501   -22.675 12.061  0.20 55.78  ? 46  ARG B NH2   1 
ATOM   7528  N  NH2   B ARG B 2 46  ? 3.424   -22.631 13.427  0.80 69.06  ? 46  ARG B NH2   1 
ATOM   7529  N  N     A ILE B 2 47  ? 3.607   -30.077 8.215   0.20 47.89  ? 47  ILE B N     1 
ATOM   7530  N  N     B ILE B 2 47  ? 3.660   -30.030 8.537   0.80 49.36  ? 47  ILE B N     1 
ATOM   7531  C  CA    A ILE B 2 47  ? 4.257   -30.701 7.068   0.20 46.51  ? 47  ILE B CA    1 
ATOM   7532  C  CA    B ILE B 2 47  ? 4.210   -30.521 7.277   0.80 46.54  ? 47  ILE B CA    1 
ATOM   7533  C  C     A ILE B 2 47  ? 4.081   -29.855 5.811   0.20 45.05  ? 47  ILE B C     1 
ATOM   7534  C  C     B ILE B 2 47  ? 3.937   -29.533 6.155   0.80 46.75  ? 47  ILE B C     1 
ATOM   7535  O  O     A ILE B 2 47  ? 4.924   -29.900 4.908   0.20 44.08  ? 47  ILE B O     1 
ATOM   7536  O  O     B ILE B 2 47  ? 4.690   -29.470 5.174   0.80 45.07  ? 47  ILE B O     1 
ATOM   7537  C  CB    A ILE B 2 47  ? 3.725   -32.132 6.867   0.20 49.56  ? 47  ILE B CB    1 
ATOM   7538  C  CB    B ILE B 2 47  ? 3.639   -31.917 6.951   0.80 50.74  ? 47  ILE B CB    1 
ATOM   7539  C  CG1   A ILE B 2 47  ? 4.568   -32.879 5.831   0.20 47.07  ? 47  ILE B CG1   1 
ATOM   7540  C  CG1   B ILE B 2 47  ? 4.507   -32.608 5.905   0.80 46.58  ? 47  ILE B CG1   1 
ATOM   7541  C  CG2   A ILE B 2 47  ? 2.258   -32.116 6.457   0.20 46.89  ? 47  ILE B CG2   1 
ATOM   7542  C  CG2   B ILE B 2 47  ? 2.188   -31.826 6.482   0.80 45.81  ? 47  ILE B CG2   1 
ATOM   7543  C  CD1   A ILE B 2 47  ? 6.013   -33.045 6.236   0.20 44.78  ? 47  ILE B CD1   1 
ATOM   7544  C  CD1   B ILE B 2 47  ? 5.831   -33.055 6.458   0.80 44.36  ? 47  ILE B CD1   1 
ATOM   7545  N  N     A ASN B 2 48  ? 3.009   -29.061 5.735   0.20 42.55  ? 48  ASN B N     1 
ATOM   7546  N  N     B ASN B 2 48  ? 2.873   -28.735 6.289   0.80 42.62  ? 48  ASN B N     1 
ATOM   7547  C  CA    A ASN B 2 48  ? 2.773   -28.217 4.570   0.20 43.30  ? 48  ASN B CA    1 
ATOM   7548  C  CA    B ASN B 2 48  ? 2.503   -27.758 5.274   0.80 39.52  ? 48  ASN B CA    1 
ATOM   7549  C  C     A ASN B 2 48  ? 3.786   -27.088 4.444   0.20 42.66  ? 48  ASN B C     1 
ATOM   7550  C  C     B ASN B 2 48  ? 3.576   -26.704 5.061   0.80 41.03  ? 48  ASN B C     1 
ATOM   7551  O  O     A ASN B 2 48  ? 3.824   -26.429 3.399   0.20 40.50  ? 48  ASN B O     1 
ATOM   7552  O  O     B ASN B 2 48  ? 3.616   -26.091 3.987   0.80 45.30  ? 48  ASN B O     1 
ATOM   7553  C  CB    A ASN B 2 48  ? 1.358   -27.636 4.620   0.20 40.03  ? 48  ASN B CB    1 
ATOM   7554  C  CB    B ASN B 2 48  ? 1.190   -27.079 5.662   0.80 45.34  ? 48  ASN B CB    1 
ATOM   7555  N  N     A VAL B 2 49  ? 4.603   -26.853 5.474   0.20 41.36  ? 49  VAL B N     1 
ATOM   7556  N  N     B VAL B 2 49  ? 4.449   -26.484 6.047   0.80 32.89  ? 49  VAL B N     1 
ATOM   7557  C  CA    A VAL B 2 49  ? 5.596   -25.784 5.409   0.20 38.21  ? 49  VAL B CA    1 
ATOM   7558  C  CA    B VAL B 2 49  ? 5.493   -25.471 5.899   0.80 35.44  ? 49  VAL B CA    1 
ATOM   7559  C  C     A VAL B 2 49  ? 6.573   -26.027 4.265   0.20 38.28  ? 49  VAL B C     1 
ATOM   7560  C  C     B VAL B 2 49  ? 6.375   -25.771 4.691   0.80 39.91  ? 49  VAL B C     1 
ATOM   7561  O  O     A VAL B 2 49  ? 6.938   -25.098 3.534   0.20 37.77  ? 49  VAL B O     1 
ATOM   7562  O  O     B VAL B 2 49  ? 6.717   -24.868 3.913   0.80 34.03  ? 49  VAL B O     1 
ATOM   7563  C  CB    A VAL B 2 49  ? 6.320   -25.649 6.761   0.20 38.12  ? 49  VAL B CB    1 
ATOM   7564  C  CB    B VAL B 2 49  ? 6.323   -25.371 7.189   0.80 39.02  ? 49  VAL B CB    1 
ATOM   7565  C  CG1   A VAL B 2 49  ? 7.343   -24.532 6.707   0.20 36.92  ? 49  VAL B CG1   1 
ATOM   7566  C  CG1   B VAL B 2 49  ? 7.475   -24.414 6.997   0.80 36.56  ? 49  VAL B CG1   1 
ATOM   7567  C  CG2   A VAL B 2 49  ? 5.312   -25.396 7.873   0.20 41.50  ? 49  VAL B CG2   1 
ATOM   7568  C  CG2   B VAL B 2 49  ? 5.438   -24.924 8.354   0.80 41.61  ? 49  VAL B CG2   1 
ATOM   7569  N  N     A TYR B 2 50  ? 7.000   -27.277 4.079   0.20 39.70  ? 50  TYR B N     1 
ATOM   7570  N  N     B TYR B 2 50  ? 6.755   -27.036 4.506   0.80 36.70  ? 50  TYR B N     1 
ATOM   7571  C  CA    A TYR B 2 50  ? 7.936   -27.628 3.017   0.20 39.81  ? 50  TYR B CA    1 
ATOM   7572  C  CA    B TYR B 2 50  ? 7.668   -27.387 3.428   0.80 38.65  ? 50  TYR B CA    1 
ATOM   7573  C  C     A TYR B 2 50  ? 7.384   -28.670 2.052   0.20 41.40  ? 50  TYR B C     1 
ATOM   7574  C  C     B TYR B 2 50  ? 7.051   -28.236 2.327   0.80 41.21  ? 50  TYR B C     1 
ATOM   7575  O  O     A TYR B 2 50  ? 8.161   -29.253 1.286   0.20 40.48  ? 50  TYR B O     1 
ATOM   7576  O  O     B TYR B 2 50  ? 7.592   -28.249 1.220   0.80 37.55  ? 50  TYR B O     1 
ATOM   7577  C  CB    A TYR B 2 50  ? 9.254   -28.138 3.608   0.20 40.74  ? 50  TYR B CB    1 
ATOM   7578  C  CB    B TYR B 2 50  ? 8.898   -28.120 3.983   0.80 42.11  ? 50  TYR B CB    1 
ATOM   7579  C  CG    A TYR B 2 50  ? 10.147  -27.068 4.194   0.20 38.89  ? 50  TYR B CG    1 
ATOM   7580  C  CG    B TYR B 2 50  ? 9.952   -27.194 4.552   0.80 42.26  ? 50  TYR B CG    1 
ATOM   7581  C  CD1   A TYR B 2 50  ? 10.967  -26.299 3.379   0.20 36.74  ? 50  TYR B CD1   1 
ATOM   7582  C  CD1   B TYR B 2 50  ? 10.699  -26.368 3.724   0.80 34.42  ? 50  TYR B CD1   1 
ATOM   7583  C  CD2   A TYR B 2 50  ? 10.184  -26.840 5.563   0.20 38.31  ? 50  TYR B CD2   1 
ATOM   7584  C  CD2   B TYR B 2 50  ? 10.191  -27.140 5.916   0.80 38.21  ? 50  TYR B CD2   1 
ATOM   7585  C  CE1   A TYR B 2 50  ? 11.792  -25.327 3.910   0.20 36.15  ? 50  TYR B CE1   1 
ATOM   7586  C  CE1   B TYR B 2 50  ? 11.667  -25.520 4.238   0.80 37.02  ? 50  TYR B CE1   1 
ATOM   7587  C  CE2   A TYR B 2 50  ? 11.005  -25.869 6.103   0.20 36.10  ? 50  TYR B CE2   1 
ATOM   7588  C  CE2   B TYR B 2 50  ? 11.152  -26.294 6.439   0.80 37.54  ? 50  TYR B CE2   1 
ATOM   7589  C  CZ    A TYR B 2 50  ? 11.807  -25.117 5.273   0.20 37.85  ? 50  TYR B CZ    1 
ATOM   7590  C  CZ    B TYR B 2 50  ? 11.886  -25.489 5.601   0.80 38.01  ? 50  TYR B CZ    1 
ATOM   7591  O  OH    A TYR B 2 50  ? 12.627  -24.150 5.806   0.20 37.75  ? 50  TYR B OH    1 
ATOM   7592  O  OH    B TYR B 2 50  ? 12.842  -24.654 6.133   0.80 37.78  ? 50  TYR B OH    1 
ATOM   7593  N  N     A TYR B 2 51  ? 6.078   -28.934 2.066   0.20 43.21  ? 51  TYR B N     1 
ATOM   7594  N  N     B TYR B 2 51  ? 5.951   -28.942 2.589   0.80 41.15  ? 51  TYR B N     1 
ATOM   7595  C  CA    A TYR B 2 51  ? 5.507   -29.975 1.222   0.20 45.87  ? 51  TYR B CA    1 
ATOM   7596  C  CA    B TYR B 2 51  ? 5.351   -29.834 1.606   0.80 46.12  ? 51  TYR B CA    1 
ATOM   7597  C  C     A TYR B 2 51  ? 4.136   -29.554 0.713   0.20 48.27  ? 51  TYR B C     1 
ATOM   7598  C  C     B TYR B 2 51  ? 3.940   -29.380 1.263   0.80 47.77  ? 51  TYR B C     1 
ATOM   7599  O  O     A TYR B 2 51  ? 3.410   -28.804 1.372   0.20 46.80  ? 51  TYR B O     1 
ATOM   7600  O  O     B TYR B 2 51  ? 3.183   -28.956 2.142   0.80 47.87  ? 51  TYR B O     1 
ATOM   7601  C  CB    A TYR B 2 51  ? 5.390   -31.310 1.971   0.20 44.42  ? 51  TYR B CB    1 
ATOM   7602  C  CB    B TYR B 2 51  ? 5.304   -31.280 2.111   0.80 43.78  ? 51  TYR B CB    1 
ATOM   7603  C  CG    A TYR B 2 51  ? 6.714   -32.002 2.204   0.20 48.08  ? 51  TYR B CG    1 
ATOM   7604  C  CG    B TYR B 2 51  ? 6.647   -31.863 2.492   0.80 49.14  ? 51  TYR B CG    1 
ATOM   7605  C  CD1   A TYR B 2 51  ? 7.497   -31.693 3.310   0.20 44.63  ? 51  TYR B CD1   1 
ATOM   7606  C  CD1   B TYR B 2 51  ? 7.231   -31.567 3.717   0.80 43.40  ? 51  TYR B CD1   1 
ATOM   7607  C  CD2   A TYR B 2 51  ? 7.181   -32.965 1.319   0.20 46.14  ? 51  TYR B CD2   1 
ATOM   7608  C  CD2   B TYR B 2 51  ? 7.321   -32.725 1.633   0.80 46.03  ? 51  TYR B CD2   1 
ATOM   7609  C  CE1   A TYR B 2 51  ? 8.707   -32.322 3.525   0.20 45.94  ? 51  TYR B CE1   1 
ATOM   7610  C  CE1   B TYR B 2 51  ? 8.451   -32.104 4.076   0.80 41.60  ? 51  TYR B CE1   1 
ATOM   7611  C  CE2   A TYR B 2 51  ? 8.388   -33.601 1.528   0.20 46.19  ? 51  TYR B CE2   1 
ATOM   7612  C  CE2   B TYR B 2 51  ? 8.540   -33.268 1.981   0.80 43.93  ? 51  TYR B CE2   1 
ATOM   7613  C  CZ    A TYR B 2 51  ? 9.148   -33.276 2.630   0.20 45.48  ? 51  TYR B CZ    1 
ATOM   7614  C  CZ    B TYR B 2 51  ? 9.107   -32.953 3.199   0.80 51.60  ? 51  TYR B CZ    1 
ATOM   7615  O  OH    A TYR B 2 51  ? 10.352  -33.906 2.840   0.20 41.50  ? 51  TYR B OH    1 
ATOM   7616  O  OH    B TYR B 2 51  ? 10.327  -33.496 3.545   0.80 42.33  ? 51  TYR B OH    1 
ATOM   7617  N  N     A ASN B 2 52  ? 3.792   -30.052 -0.472  0.20 49.95  ? 52  ASN B N     1 
ATOM   7618  N  N     B ASN B 2 52  ? 3.599   -29.465 -0.021  0.80 49.97  ? 52  ASN B N     1 
ATOM   7619  C  CA    A ASN B 2 52  ? 2.484   -29.851 -1.083  0.20 53.30  ? 52  ASN B CA    1 
ATOM   7620  C  CA    B ASN B 2 52  ? 2.220   -29.342 -0.463  0.80 53.19  ? 52  ASN B CA    1 
ATOM   7621  C  C     A ASN B 2 52  ? 1.779   -31.197 -1.176  0.20 55.93  ? 52  ASN B C     1 
ATOM   7622  C  C     B ASN B 2 52  ? 1.538   -30.700 -0.382  0.80 56.12  ? 52  ASN B C     1 
ATOM   7623  O  O     A ASN B 2 52  ? 2.250   -32.100 -1.875  0.20 57.06  ? 52  ASN B O     1 
ATOM   7624  O  O     B ASN B 2 52  ? 2.186   -31.749 -0.435  0.80 53.67  ? 52  ASN B O     1 
ATOM   7625  C  CB    A ASN B 2 52  ? 2.613   -29.216 -2.468  0.20 53.78  ? 52  ASN B CB    1 
ATOM   7626  C  CB    B ASN B 2 52  ? 2.136   -28.811 -1.896  0.80 53.99  ? 52  ASN B CB    1 
ATOM   7627  C  CG    A ASN B 2 52  ? 2.844   -27.722 -2.404  0.20 51.74  ? 52  ASN B CG    1 
ATOM   7628  C  CG    B ASN B 2 52  ? 2.469   -27.331 -2.001  0.80 53.39  ? 52  ASN B CG    1 
ATOM   7629  O  OD1   A ASN B 2 52  ? 2.321   -27.039 -1.523  0.20 51.05  ? 52  ASN B OD1   1 
ATOM   7630  O  OD1   B ASN B 2 52  ? 2.069   -26.528 -1.158  0.80 52.25  ? 52  ASN B OD1   1 
ATOM   7631  N  ND2   A ASN B 2 52  ? 3.627   -27.203 -3.343  0.20 47.97  ? 52  ASN B ND2   1 
ATOM   7632  N  ND2   B ASN B 2 52  ? 3.199   -26.964 -3.051  0.80 46.42  ? 52  ASN B ND2   1 
ATOM   7633  N  N     A GLU B 2 53  ? 0.656   -31.327 -0.476  0.20 58.78  ? 53  GLU B N     1 
ATOM   7634  N  N     B GLU B 2 53  ? 0.219   -30.673 -0.246  0.80 61.59  ? 53  GLU B N     1 
ATOM   7635  C  CA    A GLU B 2 53  ? -0.078  -32.583 -0.476  0.20 60.84  ? 53  GLU B CA    1 
ATOM   7636  C  CA    B GLU B 2 53  ? -0.577  -31.888 -0.169  0.80 62.05  ? 53  GLU B CA    1 
ATOM   7637  C  C     A GLU B 2 53  ? -0.786  -32.792 -1.809  0.20 62.13  ? 53  GLU B C     1 
ATOM   7638  C  C     B GLU B 2 53  ? -1.136  -32.183 -1.554  0.80 64.07  ? 53  GLU B C     1 
ATOM   7639  O  O     A GLU B 2 53  ? -1.333  -31.854 -2.396  0.20 63.91  ? 53  GLU B O     1 
ATOM   7640  O  O     B GLU B 2 53  ? -1.822  -31.340 -2.145  0.80 65.68  ? 53  GLU B O     1 
ATOM   7641  C  CB    A GLU B 2 53  ? -1.090  -32.607 0.669   0.20 62.57  ? 53  GLU B CB    1 
ATOM   7642  C  CB    B GLU B 2 53  ? -1.700  -31.741 0.856   0.80 64.42  ? 53  GLU B CB    1 
ATOM   7643  C  CG    A GLU B 2 53  ? -1.856  -33.914 0.789   0.20 64.27  ? 53  GLU B CG    1 
ATOM   7644  C  CG    B GLU B 2 53  ? -2.299  -33.055 1.326   0.80 64.67  ? 53  GLU B CG    1 
ATOM   7645  C  CD    A GLU B 2 53  ? -2.798  -33.932 1.974   0.20 66.55  ? 53  GLU B CD    1 
ATOM   7646  C  CD    B GLU B 2 53  ? -3.374  -32.856 2.379   0.80 77.82  ? 53  GLU B CD    1 
ATOM   7647  O  OE1   A GLU B 2 53  ? -2.921  -32.891 2.654   0.20 75.05  ? 53  GLU B OE1   1 
ATOM   7648  O  OE1   B GLU B 2 53  ? -3.823  -31.702 2.566   0.80 68.10  ? 53  GLU B OE1   1 
ATOM   7649  O  OE2   A GLU B 2 53  ? -3.413  -34.988 2.227   0.20 64.32  ? 53  GLU B OE2   1 
ATOM   7650  O  OE2   B GLU B 2 53  ? -3.766  -33.853 3.022   0.80 85.78  ? 53  GLU B OE2   1 
ATOM   7651  N  N     A ALA B 2 54  ? -0.765  -34.030 -2.287  0.20 61.86  ? 54  ALA B N     1 
ATOM   7652  N  N     B ALA B 2 54  ? -0.822  -33.361 -2.078  0.80 61.26  ? 54  ALA B N     1 
ATOM   7653  C  CA    A ALA B 2 54  ? -1.448  -34.433 -3.506  0.20 62.56  ? 54  ALA B CA    1 
ATOM   7654  C  CA    B ALA B 2 54  ? -1.341  -33.803 -3.360  0.80 61.24  ? 54  ALA B CA    1 
ATOM   7655  C  C     A ALA B 2 54  ? -2.434  -35.554 -3.187  0.20 62.73  ? 54  ALA B C     1 
ATOM   7656  C  C     B ALA B 2 54  ? -2.495  -34.776 -3.153  0.80 62.21  ? 54  ALA B C     1 
ATOM   7657  O  O     A ALA B 2 54  ? -2.564  -35.992 -2.041  0.20 62.73  ? 54  ALA B O     1 
ATOM   7658  O  O     B ALA B 2 54  ? -2.810  -35.185 -2.032  0.80 60.36  ? 54  ALA B O     1 
ATOM   7659  C  CB    A ALA B 2 54  ? -0.444  -34.870 -4.577  0.20 63.33  ? 54  ALA B CB    1 
ATOM   7660  C  CB    B ALA B 2 54  ? -0.234  -34.450 -4.198  0.80 64.85  ? 54  ALA B CB    1 
ATOM   7661  N  N     A THR B 2 55  ? -3.134  -36.017 -4.218  0.20 64.64  ? 55  THR B N     1 
ATOM   7662  N  N     B THR B 2 55  ? -3.134  -35.138 -4.261  0.80 67.59  ? 55  THR B N     1 
ATOM   7663  C  CA    A THR B 2 55  ? -4.087  -37.102 -4.043  0.20 62.22  ? 55  THR B CA    1 
ATOM   7664  C  CA    B THR B 2 55  ? -4.205  -36.122 -4.221  0.80 64.05  ? 55  THR B CA    1 
ATOM   7665  C  C     A THR B 2 55  ? -3.358  -38.424 -3.821  0.20 62.78  ? 55  THR B C     1 
ATOM   7666  C  C     B THR B 2 55  ? -3.664  -37.478 -3.786  0.80 63.13  ? 55  THR B C     1 
ATOM   7667  O  O     A THR B 2 55  ? -2.209  -38.606 -4.235  0.20 61.49  ? 55  THR B O     1 
ATOM   7668  O  O     B THR B 2 55  ? -2.515  -37.836 -4.064  0.80 63.53  ? 55  THR B O     1 
ATOM   7669  C  CB    A THR B 2 55  ? -5.008  -37.212 -5.258  0.20 62.33  ? 55  THR B CB    1 
ATOM   7670  C  CB    B THR B 2 55  ? -4.876  -36.243 -5.587  0.80 68.70  ? 55  THR B CB    1 
ATOM   7671  N  N     A GLY B 2 56  ? -4.042  -39.351 -3.157  0.20 62.29  ? 56  GLY B N     1 
ATOM   7672  N  N     B GLY B 2 56  ? -4.508  -38.235 -3.092  0.80 62.59  ? 56  GLY B N     1 
ATOM   7673  C  CA    A GLY B 2 56  ? -3.447  -40.636 -2.852  0.20 59.42  ? 56  GLY B CA    1 
ATOM   7674  C  CA    B GLY B 2 56  ? -4.114  -39.532 -2.584  0.80 62.34  ? 56  GLY B CA    1 
ATOM   7675  C  C     A GLY B 2 56  ? -2.449  -40.608 -1.719  0.20 62.84  ? 56  GLY B C     1 
ATOM   7676  C  C     B GLY B 2 56  ? -3.304  -39.498 -1.310  0.80 65.52  ? 56  GLY B C     1 
ATOM   7677  O  O     A GLY B 2 56  ? -1.533  -41.437 -1.692  0.20 57.07  ? 56  GLY B O     1 
ATOM   7678  O  O     B GLY B 2 56  ? -2.739  -40.531 -0.931  0.80 66.76  ? 56  GLY B O     1 
ATOM   7679  N  N     A ASN B 2 57  ? -2.602  -39.670 -0.780  0.20 64.06  ? 57  ASN B N     1 
ATOM   7680  N  N     B ASN B 2 57  ? -3.235  -38.347 -0.637  0.80 59.64  ? 57  ASN B N     1 
ATOM   7681  C  CA    A ASN B 2 57  ? -1.700  -39.528 0.365   0.20 62.83  ? 57  ASN B CA    1 
ATOM   7682  C  CA    B ASN B 2 57  ? -2.449  -38.172 0.585   0.80 66.36  ? 57  ASN B CA    1 
ATOM   7683  C  C     A ASN B 2 57  ? -0.256  -39.317 -0.089  0.20 62.27  ? 57  ASN B C     1 
ATOM   7684  C  C     B ASN B 2 57  ? -0.962  -38.431 0.321   0.80 65.73  ? 57  ASN B C     1 
ATOM   7685  O  O     A ASN B 2 57  ? 0.670   -39.992 0.366   0.20 60.51  ? 57  ASN B O     1 
ATOM   7686  O  O     B ASN B 2 57  ? -0.334  -39.315 0.912   0.80 61.42  ? 57  ASN B O     1 
ATOM   7687  C  CB    A ASN B 2 57  ? -1.811  -40.729 1.308   0.20 60.51  ? 57  ASN B CB    1 
ATOM   7688  C  CB    B ASN B 2 57  ? -2.979  -39.062 1.716   0.80 65.52  ? 57  ASN B CB    1 
ATOM   7689  N  N     A LYS B 2 58  ? -0.067  -38.365 -0.999  0.20 61.34  ? 58  LYS B N     1 
ATOM   7690  N  N     B LYS B 2 58  ? -0.412  -37.642 -0.600  0.80 62.53  ? 58  LYS B N     1 
ATOM   7691  C  CA    A LYS B 2 58  ? 1.250   -38.006 -1.500  0.20 62.66  ? 58  LYS B CA    1 
ATOM   7692  C  CA    B LYS B 2 58  ? 1.009   -37.655 -0.918  0.80 60.39  ? 58  LYS B CA    1 
ATOM   7693  C  C     A LYS B 2 58  ? 1.687   -36.660 -0.934  0.20 61.86  ? 58  LYS B C     1 
ATOM   7694  C  C     B LYS B 2 58  ? 1.548   -36.231 -0.852  0.80 62.87  ? 58  LYS B C     1 
ATOM   7695  O  O     A LYS B 2 58  ? 0.868   -35.844 -0.501  0.20 61.31  ? 58  LYS B O     1 
ATOM   7696  O  O     B LYS B 2 58  ? 0.898   -35.290 -1.319  0.80 63.13  ? 58  LYS B O     1 
ATOM   7697  C  CB    A LYS B 2 58  ? 1.269   -37.951 -3.033  0.20 62.26  ? 58  LYS B CB    1 
ATOM   7698  C  CB    B LYS B 2 58  ? 1.275   -38.264 -2.306  0.80 64.56  ? 58  LYS B CB    1 
ATOM   7699  C  CG    A LYS B 2 58  ? 1.204   -39.308 -3.715  0.20 62.79  ? 58  LYS B CG    1 
ATOM   7700  C  CG    B LYS B 2 58  ? 1.524   -39.774 -2.298  0.80 68.19  ? 58  LYS B CG    1 
ATOM   7701  C  CD    A LYS B 2 58  ? 1.581   -39.195 -5.183  0.20 50.21  ? 58  LYS B CD    1 
ATOM   7702  C  CD    B LYS B 2 58  ? 0.264   -40.555 -1.957  0.80 67.43  ? 58  LYS B CD    1 
ATOM   7703  C  CE    A LYS B 2 58  ? 1.395   -40.517 -5.909  0.20 54.75  ? 58  LYS B CE    1 
ATOM   7704  C  CE    B LYS B 2 58  ? 0.551   -42.025 -1.712  0.80 60.65  ? 58  LYS B CE    1 
ATOM   7705  N  NZ    A LYS B 2 58  ? -0.033  -40.936 -5.925  0.20 48.26  ? 58  LYS B NZ    1 
ATOM   7706  N  NZ    B LYS B 2 58  ? -0.641  -42.701 -1.129  0.80 68.77  ? 58  LYS B NZ    1 
ATOM   7707  N  N     A TYR B 2 59  ? 3.000   -36.440 -0.946  0.20 61.07  ? 59  TYR B N     1 
ATOM   7708  N  N     B TYR B 2 59  ? 2.739   -36.081 -0.274  0.80 65.21  ? 59  TYR B N     1 
ATOM   7709  C  CA    A TYR B 2 59  ? 3.596   -35.196 -0.464  0.20 57.59  ? 59  TYR B CA    1 
ATOM   7710  C  CA    B TYR B 2 59  ? 3.325   -34.778 0.023   0.80 57.08  ? 59  TYR B CA    1 
ATOM   7711  C  C     A TYR B 2 59  ? 4.741   -34.829 -1.398  0.20 56.06  ? 59  TYR B C     1 
ATOM   7712  C  C     B TYR B 2 59  ? 4.482   -34.507 -0.928  0.80 57.42  ? 59  TYR B C     1 
ATOM   7713  O  O     A TYR B 2 59  ? 5.792   -35.476 -1.378  0.20 54.89  ? 59  TYR B O     1 
ATOM   7714  O  O     B TYR B 2 59  ? 5.468   -35.251 -0.939  0.80 51.75  ? 59  TYR B O     1 
ATOM   7715  C  CB    A TYR B 2 59  ? 4.090   -35.334 0.976   0.20 56.44  ? 59  TYR B CB    1 
ATOM   7716  C  CB    B TYR B 2 59  ? 3.800   -34.718 1.473   0.80 54.51  ? 59  TYR B CB    1 
ATOM   7717  C  CG    A TYR B 2 59  ? 2.984   -35.478 1.996   0.20 56.80  ? 59  TYR B CG    1 
ATOM   7718  C  CG    B TYR B 2 59  ? 2.739   -35.077 2.487   0.80 55.87  ? 59  TYR B CG    1 
ATOM   7719  C  CD1   A TYR B 2 59  ? 2.359   -34.359 2.531   0.20 57.80  ? 59  TYR B CD1   1 
ATOM   7720  C  CD1   B TYR B 2 59  ? 2.585   -36.385 2.928   0.80 60.74  ? 59  TYR B CD1   1 
ATOM   7721  C  CD2   A TYR B 2 59  ? 2.567   -36.730 2.429   0.20 59.54  ? 59  TYR B CD2   1 
ATOM   7722  C  CD2   B TYR B 2 59  ? 1.898   -34.105 3.013   0.80 60.14  ? 59  TYR B CD2   1 
ATOM   7723  C  CE1   A TYR B 2 59  ? 1.348   -34.482 3.466   0.20 59.62  ? 59  TYR B CE1   1 
ATOM   7724  C  CE1   B TYR B 2 59  ? 1.620   -36.716 3.865   0.80 61.00  ? 59  TYR B CE1   1 
ATOM   7725  C  CE2   A TYR B 2 59  ? 1.557   -36.864 3.365   0.20 60.88  ? 59  TYR B CE2   1 
ATOM   7726  C  CE2   B TYR B 2 59  ? 0.929   -34.425 3.948   0.80 59.55  ? 59  TYR B CE2   1 
ATOM   7727  C  CZ    A TYR B 2 59  ? 0.951   -35.736 3.879   0.20 60.22  ? 59  TYR B CZ    1 
ATOM   7728  C  CZ    B TYR B 2 59  ? 0.793   -35.730 4.368   0.80 59.84  ? 59  TYR B CZ    1 
ATOM   7729  O  OH    A TYR B 2 59  ? -0.055  -35.859 4.809   0.20 62.54  ? 59  TYR B OH    1 
ATOM   7730  O  OH    B TYR B 2 59  ? -0.171  -36.048 5.296   0.80 66.08  ? 59  TYR B OH    1 
ATOM   7731  N  N     A VAL B 2 60  ? 4.537   -33.802 -2.209  0.20 53.94  ? 60  VAL B N     1 
ATOM   7732  N  N     B VAL B 2 60  ? 4.365   -33.441 -1.705  0.80 55.14  ? 60  VAL B N     1 
ATOM   7733  C  CA    A VAL B 2 60  ? 5.536   -33.330 -3.164  0.20 52.68  ? 60  VAL B CA    1 
ATOM   7734  C  CA    B VAL B 2 60  ? 5.357   -33.049 -2.704  0.80 55.37  ? 60  VAL B CA    1 
ATOM   7735  C  C     A VAL B 2 60  ? 6.173   -32.064 -2.603  0.20 49.16  ? 60  VAL B C     1 
ATOM   7736  C  C     B VAL B 2 60  ? 6.129   -31.854 -2.158  0.80 49.08  ? 60  VAL B C     1 
ATOM   7737  O  O     A VAL B 2 60  ? 5.443   -31.134 -2.231  0.20 49.20  ? 60  VAL B O     1 
ATOM   7738  O  O     B VAL B 2 60  ? 5.507   -30.894 -1.688  0.80 47.90  ? 60  VAL B O     1 
ATOM   7739  C  CB    A VAL B 2 60  ? 4.915   -33.063 -4.547  0.20 54.47  ? 60  VAL B CB    1 
ATOM   7740  C  CB    B VAL B 2 60  ? 4.698   -32.703 -4.054  0.80 54.54  ? 60  VAL B CB    1 
ATOM   7741  C  CG1   A VAL B 2 60  ? 5.958   -32.502 -5.500  0.20 52.50  ? 60  VAL B CG1   1 
ATOM   7742  C  CG1   B VAL B 2 60  ? 5.702   -32.072 -5.001  0.80 54.60  ? 60  VAL B CG1   1 
ATOM   7743  C  CG2   A VAL B 2 60  ? 4.308   -34.339 -5.106  0.20 53.75  ? 60  VAL B CG2   1 
ATOM   7744  C  CG2   B VAL B 2 60  ? 4.090   -33.954 -4.677  0.80 55.19  ? 60  VAL B CG2   1 
ATOM   7745  N  N     A PRO B 2 61  ? 7.501   -31.988 -2.516  0.20 46.85  ? 61  PRO B N     1 
ATOM   7746  N  N     B PRO B 2 61  ? 7.461   -31.881 -2.174  0.80 46.52  ? 61  PRO B N     1 
ATOM   7747  C  CA    A PRO B 2 61  ? 8.137   -30.786 -1.968  0.20 43.46  ? 61  PRO B CA    1 
ATOM   7748  C  CA    B PRO B 2 61  ? 8.235   -30.769 -1.605  0.80 43.44  ? 61  PRO B CA    1 
ATOM   7749  C  C     A PRO B 2 61  ? 7.843   -29.554 -2.810  0.20 41.35  ? 61  PRO B C     1 
ATOM   7750  C  C     B PRO B 2 61  ? 7.995   -29.459 -2.342  0.80 42.99  ? 61  PRO B C     1 
ATOM   7751  O  O     A PRO B 2 61  ? 7.716   -29.622 -4.033  0.20 40.35  ? 61  PRO B O     1 
ATOM   7752  O  O     B PRO B 2 61  ? 8.027   -29.398 -3.571  0.80 34.69  ? 61  PRO B O     1 
ATOM   7753  C  CB    A PRO B 2 61  ? 9.630   -31.135 -1.991  0.20 44.29  ? 61  PRO B CB    1 
ATOM   7754  C  CB    B PRO B 2 61  ? 9.685   -31.244 -1.757  0.80 45.04  ? 61  PRO B CB    1 
ATOM   7755  C  CG    A PRO B 2 61  ? 9.670   -32.631 -1.986  0.20 46.74  ? 61  PRO B CG    1 
ATOM   7756  C  CG    B PRO B 2 61  ? 9.582   -32.727 -1.680  0.80 46.51  ? 61  PRO B CG    1 
ATOM   7757  C  CD    A PRO B 2 61  ? 8.479   -33.054 -2.794  0.20 50.77  ? 61  PRO B CD    1 
ATOM   7758  C  CD    B PRO B 2 61  ? 8.304   -33.063 -2.416  0.80 51.69  ? 61  PRO B CD    1 
ATOM   7759  N  N     A ARG B 2 62  ? 7.725   -28.416 -2.136  0.20 39.50  ? 62  ARG B N     1 
ATOM   7760  N  N     B ARG B 2 62  ? 7.750   -28.398 -1.573  0.80 35.90  ? 62  ARG B N     1 
ATOM   7761  C  CA    A ARG B 2 62  ? 7.593   -27.130 -2.821  0.20 35.91  ? 62  ARG B CA    1 
ATOM   7762  C  CA    B ARG B 2 62  ? 7.647   -27.068 -2.160  0.80 31.64  ? 62  ARG B CA    1 
ATOM   7763  C  C     A ARG B 2 62  ? 8.960   -26.611 -3.251  0.20 40.07  ? 62  ARG B C     1 
ATOM   7764  C  C     B ARG B 2 62  ? 9.051   -26.628 -2.564  0.80 45.92  ? 62  ARG B C     1 
ATOM   7765  O  O     A ARG B 2 62  ? 9.363   -25.497 -2.914  0.20 34.20  ? 62  ARG B O     1 
ATOM   7766  O  O     B ARG B 2 62  ? 9.670   -25.786 -1.906  0.80 36.12  ? 62  ARG B O     1 
ATOM   7767  C  CB    A ARG B 2 62  ? 6.879   -26.122 -1.926  0.20 43.06  ? 62  ARG B CB    1 
ATOM   7768  C  CB    B ARG B 2 62  ? 7.005   -26.085 -1.174  0.80 44.70  ? 62  ARG B CB    1 
ATOM   7769  C  CG    A ARG B 2 62  ? 6.317   -24.913 -2.675  0.20 42.09  ? 62  ARG B CG    1 
ATOM   7770  C  CG    B ARG B 2 62  ? 6.277   -24.922 -1.841  0.80 44.63  ? 62  ARG B CG    1 
ATOM   7771  C  CD    A ARG B 2 62  ? 5.559   -23.965 -1.758  0.20 44.22  ? 62  ARG B CD    1 
ATOM   7772  C  CD    B ARG B 2 62  ? 5.444   -24.096 -0.850  0.80 46.20  ? 62  ARG B CD    1 
ATOM   7773  N  NE    A ARG B 2 62  ? 4.306   -24.532 -1.274  0.20 45.28  ? 62  ARG B NE    1 
ATOM   7774  N  NE    B ARG B 2 62  ? 4.352   -24.847 -0.238  0.80 48.77  ? 62  ARG B NE    1 
ATOM   7775  C  CZ    A ARG B 2 62  ? 4.132   -25.053 -0.067  0.20 46.03  ? 62  ARG B CZ    1 
ATOM   7776  C  CZ    B ARG B 2 62  ? 4.420   -25.424 0.955   0.80 41.26  ? 62  ARG B CZ    1 
ATOM   7777  N  NH1   A ARG B 2 62  ? 5.118   -25.099 0.815   0.20 41.30  ? 62  ARG B NH1   1 
ATOM   7778  N  NH1   B ARG B 2 62  ? 5.515   -25.351 1.695   0.80 42.11  ? 62  ARG B NH1   1 
ATOM   7779  N  NH2   A ARG B 2 62  ? 2.940   -25.540 0.263   0.20 41.92  ? 62  ARG B NH2   1 
ATOM   7780  N  NH2   B ARG B 2 62  ? 3.368   -26.093 1.414   0.80 43.50  ? 62  ARG B NH2   1 
ATOM   7781  N  N     A ALA B 2 63  ? 9.693   -27.443 -3.986  0.20 36.04  ? 63  ALA B N     1 
ATOM   7782  N  N     B ALA B 2 63  ? 9.561   -27.213 -3.645  0.80 32.71  ? 63  ALA B N     1 
ATOM   7783  C  CA    A ALA B 2 63  ? 11.060  -27.155 -4.389  0.20 34.62  ? 63  ALA B CA    1 
ATOM   7784  C  CA    B ALA B 2 63  ? 10.968  -27.115 -3.999  0.80 33.21  ? 63  ALA B CA    1 
ATOM   7785  C  C     A ALA B 2 63  ? 11.120  -26.853 -5.881  0.20 40.04  ? 63  ALA B C     1 
ATOM   7786  C  C     B ALA B 2 63  ? 11.097  -26.841 -5.486  0.80 40.29  ? 63  ALA B C     1 
ATOM   7787  O  O     A ALA B 2 63  ? 10.316  -27.360 -6.670  0.20 38.64  ? 63  ALA B O     1 
ATOM   7788  O  O     B ALA B 2 63  ? 10.427  -27.479 -6.306  0.80 39.22  ? 63  ALA B O     1 
ATOM   7789  C  CB    A ALA B 2 63  ? 11.988  -28.326 -4.055  0.20 36.93  ? 63  ALA B CB    1 
ATOM   7790  C  CB    B ALA B 2 63  ? 11.713  -28.402 -3.627  0.80 33.16  ? 63  ALA B CB    1 
ATOM   7791  N  N     A ILE B 2 64  ? 12.084  -26.017 -6.258  0.20 38.62  ? 64  ILE B N     1 
ATOM   7792  N  N     B ILE B 2 64  ? 11.965  -25.897 -5.823  0.80 42.42  ? 64  ILE B N     1 
ATOM   7793  C  CA    A ILE B 2 64  ? 12.291  -25.609 -7.642  0.20 36.00  ? 64  ILE B CA    1 
ATOM   7794  C  CA    B ILE B 2 64  ? 12.219  -25.485 -7.195  0.80 32.12  ? 64  ILE B CA    1 
ATOM   7795  C  C     A ILE B 2 64  ? 13.776  -25.762 -7.934  0.20 37.61  ? 64  ILE B C     1 
ATOM   7796  C  C     B ILE B 2 64  ? 13.704  -25.690 -7.460  0.80 37.30  ? 64  ILE B C     1 
ATOM   7797  O  O     A ILE B 2 64  ? 14.592  -24.973 -7.444  0.20 36.28  ? 64  ILE B O     1 
ATOM   7798  O  O     B ILE B 2 64  ? 14.539  -25.340 -6.620  0.80 31.15  ? 64  ILE B O     1 
ATOM   7799  C  CB    A ILE B 2 64  ? 11.825  -24.170 -7.901  0.20 37.89  ? 64  ILE B CB    1 
ATOM   7800  C  CB    B ILE B 2 64  ? 11.800  -24.021 -7.414  0.80 39.07  ? 64  ILE B CB    1 
ATOM   7801  C  CG1   A ILE B 2 64  ? 10.328  -24.037 -7.611  0.20 41.39  ? 64  ILE B CG1   1 
ATOM   7802  C  CG1   B ILE B 2 64  ? 10.297  -23.870 -7.153  0.80 41.43  ? 64  ILE B CG1   1 
ATOM   7803  C  CG2   A ILE B 2 64  ? 12.136  -23.756 -9.330  0.20 38.54  ? 64  ILE B CG2   1 
ATOM   7804  C  CG2   B ILE B 2 64  ? 12.191  -23.526 -8.802  0.80 35.88  ? 64  ILE B CG2   1 
ATOM   7805  C  CD1   A ILE B 2 64  ? 9.806   -22.630 -7.731  0.20 40.29  ? 64  ILE B CD1   1 
ATOM   7806  C  CD1   B ILE B 2 64  ? 9.777   -22.500 -7.437  0.80 40.12  ? 64  ILE B CD1   1 
ATOM   7807  N  N     A LEU B 2 65  ? 14.128  -26.777 -8.721  0.20 39.07  ? 65  LEU B N     1 
ATOM   7808  N  N     B LEU B 2 65  ? 14.029  -26.277 -8.608  0.80 37.82  ? 65  LEU B N     1 
ATOM   7809  C  CA    A LEU B 2 65  ? 15.519  -27.065 -9.049  0.20 38.48  ? 65  LEU B CA    1 
ATOM   7810  C  CA    B LEU B 2 65  ? 15.394  -26.687 -8.923  0.80 38.11  ? 65  LEU B CA    1 
ATOM   7811  C  C     A LEU B 2 65  ? 15.952  -26.242 -10.255 0.20 39.87  ? 65  LEU B C     1 
ATOM   7812  C  C     B LEU B 2 65  ? 15.836  -26.006 -10.211 0.80 39.59  ? 65  LEU B C     1 
ATOM   7813  O  O     A LEU B 2 65  ? 15.299  -26.276 -11.303 0.20 38.53  ? 65  LEU B O     1 
ATOM   7814  O  O     B LEU B 2 65  ? 15.181  -26.153 -11.248 0.80 37.62  ? 65  LEU B O     1 
ATOM   7815  C  CB    A LEU B 2 65  ? 15.711  -28.555 -9.338  0.20 41.17  ? 65  LEU B CB    1 
ATOM   7816  C  CB    B LEU B 2 65  ? 15.484  -28.209 -9.051  0.80 38.56  ? 65  LEU B CB    1 
ATOM   7817  C  CG    A LEU B 2 65  ? 15.477  -29.572 -8.219  0.20 40.51  ? 65  LEU B CG    1 
ATOM   7818  C  CG    B LEU B 2 65  ? 15.207  -29.084 -7.827  0.80 36.63  ? 65  LEU B CG    1 
ATOM   7819  C  CD1   A LEU B 2 65  ? 14.003  -29.931 -8.063  0.20 44.66  ? 65  LEU B CD1   1 
ATOM   7820  C  CD1   B LEU B 2 65  ? 13.711  -29.207 -7.501  0.80 46.16  ? 65  LEU B CD1   1 
ATOM   7821  C  CD2   A LEU B 2 65  ? 16.310  -30.819 -8.469  0.20 45.54  ? 65  LEU B CD2   1 
ATOM   7822  C  CD2   B LEU B 2 65  ? 15.805  -30.469 -8.018  0.80 46.58  ? 65  LEU B CD2   1 
ATOM   7823  N  N     A VAL B 2 66  ? 17.054  -25.508 -10.106 0.20 40.28  ? 66  VAL B N     1 
ATOM   7824  N  N     B VAL B 2 66  ? 16.952  -25.274 -10.151 0.80 40.61  ? 66  VAL B N     1 
ATOM   7825  C  CA    A VAL B 2 66  ? 17.584  -24.646 -11.156 0.20 40.64  ? 66  VAL B CA    1 
ATOM   7826  C  CA    B VAL B 2 66  ? 17.415  -24.459 -11.270 0.80 40.50  ? 66  VAL B CA    1 
ATOM   7827  C  C     A VAL B 2 66  ? 19.067  -24.946 -11.331 0.20 40.62  ? 66  VAL B C     1 
ATOM   7828  C  C     B VAL B 2 66  ? 18.918  -24.647 -11.454 0.80 40.97  ? 66  VAL B C     1 
ATOM   7829  O  O     A VAL B 2 66  ? 19.777  -25.189 -10.348 0.20 37.01  ? 66  VAL B O     1 
ATOM   7830  O  O     B VAL B 2 66  ? 19.666  -24.740 -10.475 0.80 35.93  ? 66  VAL B O     1 
ATOM   7831  C  CB    A VAL B 2 66  ? 17.371  -23.151 -10.829 0.20 39.16  ? 66  VAL B CB    1 
ATOM   7832  C  CB    B VAL B 2 66  ? 17.056  -22.969 -11.056 0.80 39.46  ? 66  VAL B CB    1 
ATOM   7833  C  CG1   A VAL B 2 66  ? 17.769  -22.277 -12.012 0.20 41.40  ? 66  VAL B CG1   1 
ATOM   7834  C  CG1   B VAL B 2 66  ? 17.277  -22.564 -9.608  0.80 46.98  ? 66  VAL B CG1   1 
ATOM   7835  C  CG2   A VAL B 2 66  ? 15.927  -22.883 -10.419 0.20 38.68  ? 66  VAL B CG2   1 
ATOM   7836  C  CG2   B VAL B 2 66  ? 17.842  -22.055 -12.001 0.80 41.19  ? 66  VAL B CG2   1 
ATOM   7837  N  N     A ASP B 2 67  ? 19.528  -24.938 -12.581 0.20 45.27  ? 67  ASP B N     1 
ATOM   7838  N  N     B ASP B 2 67  ? 19.356  -24.712 -12.713 0.80 46.19  ? 67  ASP B N     1 
ATOM   7839  C  CA    A ASP B 2 67  ? 20.950  -25.008 -12.907 0.20 42.46  ? 67  ASP B CA    1 
ATOM   7840  C  CA    B ASP B 2 67  ? 20.779  -24.715 -13.045 0.80 41.77  ? 67  ASP B CA    1 
ATOM   7841  C  C     A ASP B 2 67  ? 21.123  -24.771 -14.399 0.20 47.07  ? 67  ASP B C     1 
ATOM   7842  C  C     B ASP B 2 67  ? 20.946  -24.327 -14.508 0.80 48.58  ? 67  ASP B C     1 
ATOM   7843  O  O     A ASP B 2 67  ? 20.264  -25.146 -15.202 0.20 47.42  ? 67  ASP B O     1 
ATOM   7844  O  O     B ASP B 2 67  ? 20.066  -24.582 -15.334 0.80 47.10  ? 67  ASP B O     1 
ATOM   7845  C  CB    A ASP B 2 67  ? 21.569  -26.356 -12.516 0.20 43.53  ? 67  ASP B CB    1 
ATOM   7846  C  CB    B ASP B 2 67  ? 21.422  -26.085 -12.787 0.80 42.80  ? 67  ASP B CB    1 
ATOM   7847  C  CG    A ASP B 2 67  ? 23.086  -26.303 -12.451 0.20 43.76  ? 67  ASP B CG    1 
ATOM   7848  C  CG    B ASP B 2 67  ? 22.921  -25.995 -12.546 0.80 43.96  ? 67  ASP B CG    1 
ATOM   7849  O  OD1   A ASP B 2 67  ? 23.662  -25.235 -12.747 0.20 41.19  ? 67  ASP B OD1   1 
ATOM   7850  O  OD1   B ASP B 2 67  ? 23.554  -25.024 -13.014 0.80 41.18  ? 67  ASP B OD1   1 
ATOM   7851  O  OD2   A ASP B 2 67  ? 23.704  -27.328 -12.097 0.20 43.53  ? 67  ASP B OD2   1 
ATOM   7852  O  OD2   B ASP B 2 67  ? 23.467  -26.903 -11.880 0.80 42.27  ? 67  ASP B OD2   1 
ATOM   7853  N  N     A LEU B 2 68  ? 22.246  -24.146 -14.761 0.20 45.13  ? 68  LEU B N     1 
ATOM   7854  N  N     B LEU B 2 68  ? 22.079  -23.701 -14.824 0.80 44.89  ? 68  LEU B N     1 
ATOM   7855  C  CA    A LEU B 2 68  ? 22.534  -23.918 -16.172 0.20 45.40  ? 68  LEU B CA    1 
ATOM   7856  C  CA    B LEU B 2 68  ? 22.416  -23.505 -16.225 0.80 42.16  ? 68  LEU B CA    1 
ATOM   7857  C  C     A LEU B 2 68  ? 23.087  -25.170 -16.840 0.20 49.58  ? 68  LEU B C     1 
ATOM   7858  C  C     B LEU B 2 68  ? 23.042  -24.749 -16.841 0.80 49.96  ? 68  LEU B C     1 
ATOM   7859  O  O     A LEU B 2 68  ? 22.665  -25.523 -17.946 0.20 51.64  ? 68  LEU B O     1 
ATOM   7860  O  O     B LEU B 2 68  ? 23.201  -24.809 -18.065 0.80 51.76  ? 68  LEU B O     1 
ATOM   7861  C  CB    A LEU B 2 68  ? 23.510  -22.752 -16.331 0.20 45.78  ? 68  LEU B CB    1 
ATOM   7862  C  CB    B LEU B 2 68  ? 23.358  -22.309 -16.382 0.80 43.39  ? 68  LEU B CB    1 
ATOM   7863  C  CG    A LEU B 2 68  ? 22.925  -21.355 -16.124 0.20 45.55  ? 68  LEU B CG    1 
ATOM   7864  C  CG    B LEU B 2 68  ? 22.707  -20.942 -16.179 0.80 45.99  ? 68  LEU B CG    1 
ATOM   7865  C  CD1   A LEU B 2 68  ? 24.000  -20.293 -16.294 0.20 44.21  ? 68  LEU B CD1   1 
ATOM   7866  C  CD1   B LEU B 2 68  ? 23.760  -19.841 -16.146 0.80 45.11  ? 68  LEU B CD1   1 
ATOM   7867  C  CD2   A LEU B 2 68  ? 21.771  -21.113 -17.084 0.20 45.77  ? 68  LEU B CD2   1 
ATOM   7868  C  CD2   B LEU B 2 68  ? 21.678  -20.678 -17.268 0.80 44.85  ? 68  LEU B CD2   1 
ATOM   7869  N  N     A GLU B 2 69  ? 24.023  -25.850 -16.194 0.20 49.97  ? 69  GLU B N     1 
ATOM   7870  N  N     B GLU B 2 69  ? 23.389  -25.731 -16.018 0.80 47.40  ? 69  GLU B N     1 
ATOM   7871  C  CA    A GLU B 2 69  ? 24.604  -27.056 -16.770 0.20 53.73  ? 69  GLU B CA    1 
ATOM   7872  C  CA    B GLU B 2 69  ? 23.983  -26.987 -16.449 0.80 51.01  ? 69  GLU B CA    1 
ATOM   7873  C  C     A GLU B 2 69  ? 23.593  -28.193 -16.706 0.20 53.86  ? 69  GLU B C     1 
ATOM   7874  C  C     B GLU B 2 69  ? 22.935  -28.087 -16.380 0.80 55.09  ? 69  GLU B C     1 
ATOM   7875  O  O     A GLU B 2 69  ? 23.117  -28.526 -15.612 0.20 52.86  ? 69  GLU B O     1 
ATOM   7876  O  O     B GLU B 2 69  ? 22.490  -28.442 -15.274 0.80 48.39  ? 69  GLU B O     1 
ATOM   7877  C  CB    A GLU B 2 69  ? 25.883  -27.440 -16.033 0.20 55.21  ? 69  GLU B CB    1 
ATOM   7878  C  CB    B GLU B 2 69  ? 25.181  -27.334 -15.562 0.80 52.98  ? 69  GLU B CB    1 
ATOM   7879  C  CG    A GLU B 2 69  ? 27.051  -27.787 -16.950 0.20 64.98  ? 69  GLU B CG    1 
ATOM   7880  C  CG    B GLU B 2 69  ? 25.634  -28.780 -15.637 0.80 53.86  ? 69  GLU B CG    1 
ATOM   7881  C  CD    A GLU B 2 69  ? 26.772  -28.984 -17.842 0.20 62.35  ? 69  GLU B CD    1 
ATOM   7882  C  CD    B GLU B 2 69  ? 26.718  -28.997 -16.672 0.80 67.20  ? 69  GLU B CD    1 
ATOM   7883  O  OE1   A GLU B 2 69  ? 26.040  -29.900 -17.408 0.20 58.10  ? 69  GLU B OE1   1 
ATOM   7884  O  OE1   B GLU B 2 69  ? 27.347  -28.003 -17.097 0.80 67.95  ? 69  GLU B OE1   1 
ATOM   7885  O  OE2   A GLU B 2 69  ? 27.283  -29.008 -18.983 0.20 56.40  ? 69  GLU B OE2   1 
ATOM   7886  O  OE2   B GLU B 2 69  ? 26.942  -30.165 -17.056 0.80 73.91  ? 69  GLU B OE2   1 
ATOM   7887  N  N     A PRO B 2 70  ? 23.238  -28.815 -17.836 0.20 56.77  ? 70  PRO B N     1 
ATOM   7888  N  N     B PRO B 2 70  ? 22.511  -28.655 -17.511 0.80 58.47  ? 70  PRO B N     1 
ATOM   7889  C  CA    A PRO B 2 70  ? 22.235  -29.891 -17.810 0.20 55.06  ? 70  PRO B CA    1 
ATOM   7890  C  CA    B PRO B 2 70  ? 21.490  -29.714 -17.458 0.80 55.22  ? 70  PRO B CA    1 
ATOM   7891  C  C     A PRO B 2 70  ? 22.718  -31.184 -17.175 0.20 54.93  ? 70  PRO B C     1 
ATOM   7892  C  C     B PRO B 2 70  ? 21.950  -30.969 -16.739 0.80 53.18  ? 70  PRO B C     1 
ATOM   7893  O  O     A PRO B 2 70  ? 21.936  -32.137 -17.094 0.20 56.22  ? 70  PRO B O     1 
ATOM   7894  O  O     B PRO B 2 70  ? 21.103  -31.709 -16.223 0.80 56.08  ? 70  PRO B O     1 
ATOM   7895  C  CB    A PRO B 2 70  ? 21.915  -30.098 -19.298 0.20 55.25  ? 70  PRO B CB    1 
ATOM   7896  C  CB    B PRO B 2 70  ? 21.197  -29.992 -18.939 0.80 60.05  ? 70  PRO B CB    1 
ATOM   7897  C  CG    A PRO B 2 70  ? 23.145  -29.648 -20.008 0.20 56.62  ? 70  PRO B CG    1 
ATOM   7898  C  CG    B PRO B 2 70  ? 22.428  -29.557 -19.653 0.80 52.17  ? 70  PRO B CG    1 
ATOM   7899  C  CD    A PRO B 2 70  ? 23.682  -28.502 -19.205 0.20 55.01  ? 70  PRO B CD    1 
ATOM   7900  C  CD    B PRO B 2 70  ? 22.957  -28.383 -18.888 0.80 55.68  ? 70  PRO B CD    1 
ATOM   7901  N  N     A GLY B 2 71  ? 23.970  -31.260 -16.723 0.20 54.86  ? 71  GLY B N     1 
ATOM   7902  N  N     B GLY B 2 71  ? 23.260  -31.224 -16.677 0.80 53.29  ? 71  GLY B N     1 
ATOM   7903  C  CA    A GLY B 2 71  ? 24.462  -32.474 -16.098 0.20 55.53  ? 71  GLY B CA    1 
ATOM   7904  C  CA    B GLY B 2 71  ? 23.744  -32.436 -16.036 0.80 55.91  ? 71  GLY B CA    1 
ATOM   7905  C  C     A GLY B 2 71  ? 24.021  -32.690 -14.667 0.20 55.76  ? 71  GLY B C     1 
ATOM   7906  C  C     B GLY B 2 71  ? 23.344  -32.552 -14.578 0.80 54.64  ? 71  GLY B C     1 
ATOM   7907  O  O     A GLY B 2 71  ? 24.283  -33.760 -14.109 0.20 55.02  ? 71  GLY B O     1 
ATOM   7908  O  O     B GLY B 2 71  ? 23.251  -33.661 -14.043 0.80 58.44  ? 71  GLY B O     1 
ATOM   7909  N  N     A THR B 2 72  ? 23.360  -31.703 -14.061 0.20 53.83  ? 72  THR B N     1 
ATOM   7910  N  N     B THR B 2 72  ? 23.107  -31.416 -13.915 0.80 52.83  ? 72  THR B N     1 
ATOM   7911  C  CA    A THR B 2 72  ? 22.930  -31.809 -12.672 0.20 53.54  ? 72  THR B CA    1 
ATOM   7912  C  CA    B THR B 2 72  ? 22.674  -31.449 -12.521 0.80 52.42  ? 72  THR B CA    1 
ATOM   7913  C  C     A THR B 2 72  ? 21.575  -32.488 -12.527 0.20 55.46  ? 72  THR B C     1 
ATOM   7914  C  C     B THR B 2 72  ? 21.284  -32.060 -12.389 0.80 54.73  ? 72  THR B C     1 
ATOM   7915  O  O     A THR B 2 72  ? 21.353  -33.209 -11.547 0.20 55.25  ? 72  THR B O     1 
ATOM   7916  O  O     B THR B 2 72  ? 20.996  -32.759 -11.410 0.80 53.50  ? 72  THR B O     1 
ATOM   7917  C  CB    A THR B 2 72  ? 22.874  -30.419 -12.031 0.20 53.46  ? 72  THR B CB    1 
ATOM   7918  C  CB    B THR B 2 72  ? 22.691  -30.038 -11.930 0.80 54.83  ? 72  THR B CB    1 
ATOM   7919  O  OG1   A THR B 2 72  ? 24.094  -29.716 -12.300 0.20 51.82  ? 72  THR B OG1   1 
ATOM   7920  O  OG1   B THR B 2 72  ? 23.944  -29.405 -12.218 0.80 51.58  ? 72  THR B OG1   1 
ATOM   7921  C  CG2   A THR B 2 72  ? 22.687  -30.529 -10.524 0.20 47.22  ? 72  THR B CG2   1 
ATOM   7922  C  CG2   B THR B 2 72  ? 22.498  -30.089 -10.420 0.80 43.45  ? 72  THR B CG2   1 
ATOM   7923  N  N     A MET B 2 73  ? 20.667  -32.281 -13.484 0.20 55.47  ? 73  MET B N     1 
ATOM   7924  N  N     B MET B 2 73  ? 20.411  -31.806 -13.367 0.80 54.65  ? 73  MET B N     1 
ATOM   7925  C  CA    A MET B 2 73  ? 19.347  -32.897 -13.401 0.20 56.68  ? 73  MET B CA    1 
ATOM   7926  C  CA    B MET B 2 73  ? 19.057  -32.350 -13.328 0.80 56.39  ? 73  MET B CA    1 
ATOM   7927  C  C     A MET B 2 73  ? 19.435  -34.418 -13.385 0.20 57.75  ? 73  MET B C     1 
ATOM   7928  C  C     B MET B 2 73  ? 19.077  -33.870 -13.217 0.80 58.75  ? 73  MET B C     1 
ATOM   7929  O  O     A MET B 2 73  ? 18.618  -35.079 -12.735 0.20 57.33  ? 73  MET B O     1 
ATOM   7930  O  O     B MET B 2 73  ? 18.415  -34.450 -12.349 0.80 55.88  ? 73  MET B O     1 
ATOM   7931  C  CB    A MET B 2 73  ? 18.473  -32.426 -14.566 0.20 59.00  ? 73  MET B CB    1 
ATOM   7932  C  CB    B MET B 2 73  ? 18.286  -31.903 -14.575 0.80 61.04  ? 73  MET B CB    1 
ATOM   7933  C  CG    A MET B 2 73  ? 19.054  -32.715 -15.943 0.20 59.45  ? 73  MET B CG    1 
ATOM   7934  C  CG    B MET B 2 73  ? 16.871  -32.468 -14.708 0.80 65.18  ? 73  MET B CG    1 
ATOM   7935  S  SD    A MET B 2 73  ? 18.015  -32.151 -17.306 0.20 63.51  ? 73  MET B SD    1 
ATOM   7936  S  SD    B MET B 2 73  ? 15.964  -31.805 -16.132 0.80 77.97  ? 73  MET B SD    1 
ATOM   7937  C  CE    A MET B 2 73  ? 18.981  -32.689 -18.713 0.20 57.95  ? 73  MET B CE    1 
ATOM   7938  C  CE    B MET B 2 73  ? 16.950  -32.411 -17.503 0.80 67.24  ? 73  MET B CE    1 
ATOM   7939  N  N     A ASP B 2 74  ? 20.417  -34.988 -14.085 0.20 57.18  ? 74  ASP B N     1 
ATOM   7940  N  N     B ASP B 2 74  ? 19.844  -34.532 -14.089 0.80 55.68  ? 74  ASP B N     1 
ATOM   7941  C  CA    A ASP B 2 74  ? 20.564  -36.439 -14.102 0.20 57.86  ? 74  ASP B CA    1 
ATOM   7942  C  CA    B ASP B 2 74  ? 19.892  -35.990 -14.082 0.80 56.66  ? 74  ASP B CA    1 
ATOM   7943  C  C     A ASP B 2 74  ? 21.074  -36.959 -12.764 0.20 56.58  ? 74  ASP B C     1 
ATOM   7944  C  C     B ASP B 2 74  ? 20.434  -36.527 -12.763 0.80 54.26  ? 74  ASP B C     1 
ATOM   7945  O  O     A ASP B 2 74  ? 20.645  -38.022 -12.300 0.20 56.82  ? 74  ASP B O     1 
ATOM   7946  O  O     B ASP B 2 74  ? 19.990  -37.575 -12.283 0.80 58.07  ? 74  ASP B O     1 
ATOM   7947  C  CB    A ASP B 2 74  ? 21.501  -36.855 -15.236 0.20 57.17  ? 74  ASP B CB    1 
ATOM   7948  C  CB    B ASP B 2 74  ? 20.743  -36.492 -15.250 0.80 59.56  ? 74  ASP B CB    1 
ATOM   7949  C  CG    A ASP B 2 74  ? 21.046  -36.337 -16.588 0.20 60.56  ? 74  ASP B CG    1 
ATOM   7950  C  CG    B ASP B 2 74  ? 20.091  -36.240 -16.600 0.80 64.79  ? 74  ASP B CG    1 
ATOM   7951  O  OD1   A ASP B 2 74  ? 19.951  -35.739 -16.658 0.20 63.06  ? 74  ASP B OD1   1 
ATOM   7952  O  OD1   B ASP B 2 74  ? 20.033  -35.067 -17.026 0.80 66.38  ? 74  ASP B OD1   1 
ATOM   7953  O  OD2   A ASP B 2 74  ? 21.783  -36.523 -17.580 0.20 61.79  ? 74  ASP B OD2   1 
ATOM   7954  O  OD2   B ASP B 2 74  ? 19.637  -37.218 -17.235 0.80 68.90  ? 74  ASP B OD2   1 
ATOM   7955  N  N     A SER B 2 75  ? 21.987  -36.222 -12.126 0.20 54.41  ? 75  SER B N     1 
ATOM   7956  N  N     B SER B 2 75  ? 21.400  -35.824 -12.166 0.80 55.19  ? 75  SER B N     1 
ATOM   7957  C  CA    A SER B 2 75  ? 22.545  -36.673 -10.855 0.20 56.01  ? 75  SER B CA    1 
ATOM   7958  C  CA    B SER B 2 75  ? 21.993  -36.292 -10.917 0.80 56.52  ? 75  SER B CA    1 
ATOM   7959  C  C     A SER B 2 75  ? 21.524  -36.593 -9.727  0.20 57.42  ? 75  SER B C     1 
ATOM   7960  C  C     B SER B 2 75  ? 20.978  -36.280 -9.776  0.80 56.13  ? 75  SER B C     1 
ATOM   7961  O  O     A SER B 2 75  ? 21.576  -37.399 -8.790  0.20 59.15  ? 75  SER B O     1 
ATOM   7962  O  O     B SER B 2 75  ? 20.900  -37.238 -8.998  0.80 57.08  ? 75  SER B O     1 
ATOM   7963  C  CB    A SER B 2 75  ? 23.787  -35.852 -10.509 0.20 57.06  ? 75  SER B CB    1 
ATOM   7964  C  CB    B SER B 2 75  ? 23.210  -35.437 -10.566 0.80 58.84  ? 75  SER B CB    1 
ATOM   7965  O  OG    A SER B 2 75  ? 23.516  -34.463 -10.582 0.20 58.63  ? 75  SER B OG    1 
ATOM   7966  O  OG    B SER B 2 75  ? 22.871  -34.059 -10.525 0.80 60.31  ? 75  SER B OG    1 
ATOM   7967  N  N     A VAL B 2 76  ? 20.595  -35.639 -9.792  0.20 55.60  ? 76  VAL B N     1 
ATOM   7968  N  N     B VAL B 2 76  ? 20.191  -35.210 -9.658  0.80 55.25  ? 76  VAL B N     1 
ATOM   7969  C  CA    A VAL B 2 76  ? 19.582  -35.528 -8.748  0.20 57.34  ? 76  VAL B CA    1 
ATOM   7970  C  CA    B VAL B 2 76  ? 19.201  -35.156 -8.587  0.80 57.81  ? 76  VAL B CA    1 
ATOM   7971  C  C     A VAL B 2 76  ? 18.565  -36.657 -8.868  0.20 57.43  ? 76  VAL B C     1 
ATOM   7972  C  C     B VAL B 2 76  ? 18.121  -36.209 -8.807  0.80 58.23  ? 76  VAL B C     1 
ATOM   7973  O  O     A VAL B 2 76  ? 18.138  -37.234 -7.860  0.20 57.17  ? 76  VAL B O     1 
ATOM   7974  O  O     B VAL B 2 76  ? 17.686  -36.873 -7.858  0.80 57.51  ? 76  VAL B O     1 
ATOM   7975  C  CB    A VAL B 2 76  ? 18.904  -34.147 -8.800  0.20 55.33  ? 76  VAL B CB    1 
ATOM   7976  C  CB    B VAL B 2 76  ? 18.597  -33.746 -8.473  0.80 54.79  ? 76  VAL B CB    1 
ATOM   7977  C  CG1   A VAL B 2 76  ? 17.863  -34.028 -7.699  0.20 52.70  ? 76  VAL B CG1   1 
ATOM   7978  C  CG1   B VAL B 2 76  ? 17.826  -33.619 -7.173  0.80 49.94  ? 76  VAL B CG1   1 
ATOM   7979  C  CG2   A VAL B 2 76  ? 19.939  -33.042 -8.674  0.20 53.73  ? 76  VAL B CG2   1 
ATOM   7980  C  CG2   B VAL B 2 76  ? 19.683  -32.690 -8.551  0.80 53.08  ? 76  VAL B CG2   1 
ATOM   7981  N  N     A ARG B 2 77  ? 18.166  -36.996 -10.097 0.20 58.14  ? 77  ARG B N     1 
ATOM   7982  N  N     B ARG B 2 77  ? 17.672  -36.380 -10.057 0.80 59.81  ? 77  ARG B N     1 
ATOM   7983  C  CA    A ARG B 2 77  ? 17.172  -38.049 -10.287 0.20 57.06  ? 77  ARG B CA    1 
ATOM   7984  C  CA    B ARG B 2 77  ? 16.668  -37.400 -10.357 0.80 54.93  ? 77  ARG B CA    1 
ATOM   7985  C  C     A ARG B 2 77  ? 17.727  -39.415 -9.901  0.20 56.73  ? 77  ARG B C     1 
ATOM   7986  C  C     B ARG B 2 77  ? 17.157  -38.791 -9.969  0.80 56.98  ? 77  ARG B C     1 
ATOM   7987  O  O     A ARG B 2 77  ? 16.997  -40.258 -9.366  0.20 57.61  ? 77  ARG B O     1 
ATOM   7988  O  O     B ARG B 2 77  ? 16.380  -39.615 -9.472  0.80 59.46  ? 77  ARG B O     1 
ATOM   7989  C  CB    A ARG B 2 77  ? 16.683  -38.062 -11.736 0.20 56.78  ? 77  ARG B CB    1 
ATOM   7990  C  CB    B ARG B 2 77  ? 16.304  -37.370 -11.841 0.80 57.08  ? 77  ARG B CB    1 
ATOM   7991  C  CG    A ARG B 2 77  ? 15.912  -36.819 -12.152 0.20 56.84  ? 77  ARG B CG    1 
ATOM   7992  C  CG    B ARG B 2 77  ? 15.527  -36.148 -12.306 0.80 56.72  ? 77  ARG B CG    1 
ATOM   7993  C  CD    A ARG B 2 77  ? 15.282  -37.003 -13.526 0.20 58.41  ? 77  ARG B CD    1 
ATOM   7994  C  CD    B ARG B 2 77  ? 15.242  -36.250 -13.807 0.80 63.42  ? 77  ARG B CD    1 
ATOM   7995  N  NE    A ARG B 2 77  ? 14.682  -35.771 -14.027 0.20 58.68  ? 77  ARG B NE    1 
ATOM   7996  N  NE    B ARG B 2 77  ? 14.678  -35.032 -14.381 0.80 56.17  ? 77  ARG B NE    1 
ATOM   7997  C  CZ    A ARG B 2 77  ? 15.295  -34.913 -14.831 0.20 55.64  ? 77  ARG B CZ    1 
ATOM   7998  C  CZ    B ARG B 2 77  ? 13.379  -34.778 -14.471 0.80 66.56  ? 77  ARG B CZ    1 
ATOM   7999  N  NH1   A ARG B 2 77  ? 16.530  -35.124 -15.255 0.20 56.96  ? 77  ARG B NH1   1 
ATOM   8000  N  NH1   B ARG B 2 77  ? 12.473  -35.623 -13.999 0.80 56.77  ? 77  ARG B NH1   1 
ATOM   8001  N  NH2   A ARG B 2 77  ? 14.652  -33.817 -15.222 0.20 52.08  ? 77  ARG B NH2   1 
ATOM   8002  N  NH2   B ARG B 2 77  ? 12.977  -33.649 -15.052 0.80 60.92  ? 77  ARG B NH2   1 
ATOM   8003  N  N     A SER B 2 78  ? 19.015  -39.653 -10.159 0.20 57.78  ? 78  SER B N     1 
ATOM   8004  N  N     B SER B 2 78  ? 18.444  -39.066 -10.179 0.80 56.52  ? 78  SER B N     1 
ATOM   8005  C  CA    A SER B 2 78  ? 19.620  -40.939 -9.830  0.20 58.18  ? 78  SER B CA    1 
ATOM   8006  C  CA    B SER B 2 78  ? 19.013  -40.383 -9.919  0.80 59.97  ? 78  SER B CA    1 
ATOM   8007  C  C     A SER B 2 78  ? 19.744  -41.167 -8.329  0.20 57.59  ? 78  SER B C     1 
ATOM   8008  C  C     B SER B 2 78  ? 19.232  -40.662 -8.436  0.80 59.38  ? 78  SER B C     1 
ATOM   8009  O  O     A SER B 2 78  ? 20.070  -42.286 -7.916  0.20 54.63  ? 78  SER B O     1 
ATOM   8010  O  O     B SER B 2 78  ? 19.695  -41.755 -8.090  0.80 55.76  ? 78  SER B O     1 
ATOM   8011  C  CB    A SER B 2 78  ? 20.998  -41.057 -10.485 0.20 59.53  ? 78  SER B CB    1 
ATOM   8012  C  CB    B SER B 2 78  ? 20.332  -40.536 -10.678 0.80 61.93  ? 78  SER B CB    1 
ATOM   8013  O  OG    A SER B 2 78  ? 21.881  -40.060 -10.003 0.20 56.87  ? 78  SER B OG    1 
ATOM   8014  O  OG    B SER B 2 78  ? 20.125  -40.373 -12.071 0.80 62.52  ? 78  SER B OG    1 
ATOM   8015  N  N     A GLY B 2 79  ? 19.494  -40.147 -7.509  0.20 58.26  ? 79  GLY B N     1 
ATOM   8016  N  N     B GLY B 2 79  ? 18.918  -39.713 -7.563  0.80 60.54  ? 79  GLY B N     1 
ATOM   8017  C  CA    A GLY B 2 79  ? 19.546  -40.300 -6.076  0.20 57.45  ? 79  GLY B CA    1 
ATOM   8018  C  CA    B GLY B 2 79  ? 18.997  -39.933 -6.139  0.80 57.12  ? 79  GLY B CA    1 
ATOM   8019  C  C     A GLY B 2 79  ? 18.338  -41.032 -5.536  0.20 56.40  ? 79  GLY B C     1 
ATOM   8020  C  C     B GLY B 2 79  ? 17.775  -40.650 -5.617  0.80 55.28  ? 79  GLY B C     1 
ATOM   8021  O  O     A GLY B 2 79  ? 17.400  -41.388 -6.263  0.20 59.68  ? 79  GLY B O     1 
ATOM   8022  O  O     B GLY B 2 79  ? 16.779  -40.862 -6.324  0.80 63.45  ? 79  GLY B O     1 
ATOM   8023  N  N     A PRO B 2 80  ? 18.355  -41.276 -4.223  0.20 56.24  ? 80  PRO B N     1 
ATOM   8024  N  N     B PRO B 2 80  ? 17.837  -41.040 -4.342  0.80 56.15  ? 80  PRO B N     1 
ATOM   8025  C  CA    A PRO B 2 80  ? 17.223  -41.995 -3.606  0.20 57.62  ? 80  PRO B CA    1 
ATOM   8026  C  CA    B PRO B 2 80  ? 16.717  -41.809 -3.763  0.80 58.56  ? 80  PRO B CA    1 
ATOM   8027  C  C     A PRO B 2 80  ? 15.910  -41.234 -3.685  0.20 59.57  ? 80  PRO B C     1 
ATOM   8028  C  C     B PRO B 2 80  ? 15.414  -41.027 -3.713  0.80 62.93  ? 80  PRO B C     1 
ATOM   8029  O  O     A PRO B 2 80  ? 14.901  -41.787 -4.143  0.20 60.19  ? 80  PRO B O     1 
ATOM   8030  O  O     B PRO B 2 80  ? 14.376  -41.517 -4.182  0.80 59.87  ? 80  PRO B O     1 
ATOM   8031  C  CB    A PRO B 2 80  ? 17.691  -42.193 -2.156  0.20 58.08  ? 80  PRO B CB    1 
ATOM   8032  C  CB    B PRO B 2 80  ? 17.235  -42.166 -2.364  0.80 58.50  ? 80  PRO B CB    1 
ATOM   8033  C  CG    A PRO B 2 80  ? 19.184  -42.064 -2.207  0.20 57.89  ? 80  PRO B CG    1 
ATOM   8034  C  CG    B PRO B 2 80  ? 18.243  -41.098 -2.051  0.80 57.83  ? 80  PRO B CG    1 
ATOM   8035  C  CD    A PRO B 2 80  ? 19.457  -41.051 -3.274  0.20 56.05  ? 80  PRO B CD    1 
ATOM   8036  C  CD    B PRO B 2 80  ? 18.908  -40.787 -3.363  0.80 56.39  ? 80  PRO B CD    1 
ATOM   8037  N  N     A PHE B 2 81  ? 15.892  -39.977 -3.244  0.20 56.87  ? 81  PHE B N     1 
ATOM   8038  N  N     B PHE B 2 81  ? 15.436  -39.817 -3.150  0.80 58.08  ? 81  PHE B N     1 
ATOM   8039  C  CA    A PHE B 2 81  ? 14.693  -39.140 -3.271  0.20 55.98  ? 81  PHE B CA    1 
ATOM   8040  C  CA    B PHE B 2 81  ? 14.277  -38.935 -3.167  0.80 56.76  ? 81  PHE B CA    1 
ATOM   8041  C  C     A PHE B 2 81  ? 14.647  -38.256 -4.510  0.20 53.69  ? 81  PHE B C     1 
ATOM   8042  C  C     B PHE B 2 81  ? 14.217  -38.086 -4.429  0.80 52.54  ? 81  PHE B C     1 
ATOM   8043  O  O     A PHE B 2 81  ? 14.214  -37.104 -4.441  0.20 51.52  ? 81  PHE B O     1 
ATOM   8044  O  O     B PHE B 2 81  ? 13.633  -36.998 -4.410  0.80 47.24  ? 81  PHE B O     1 
ATOM   8045  C  CB    A PHE B 2 81  ? 14.612  -38.287 -2.009  0.20 52.23  ? 81  PHE B CB    1 
ATOM   8046  C  CB    B PHE B 2 81  ? 14.268  -38.041 -1.926  0.80 50.80  ? 81  PHE B CB    1 
ATOM   8047  C  CG    A PHE B 2 81  ? 14.321  -39.068 -0.759  0.20 51.32  ? 81  PHE B CG    1 
ATOM   8048  C  CG    B PHE B 2 81  ? 14.073  -38.783 -0.631  0.80 50.17  ? 81  PHE B CG    1 
ATOM   8049  C  CD1   A PHE B 2 81  ? 15.323  -39.776 -0.117  0.20 52.82  ? 81  PHE B CD1   1 
ATOM   8050  C  CD1   B PHE B 2 81  ? 15.120  -39.475 -0.046  0.80 52.91  ? 81  PHE B CD1   1 
ATOM   8051  C  CD2   A PHE B 2 81  ? 13.047  -39.081 -0.217  0.20 51.07  ? 81  PHE B CD2   1 
ATOM   8052  C  CD2   B PHE B 2 81  ? 12.850  -38.762 0.017   0.80 49.12  ? 81  PHE B CD2   1 
ATOM   8053  C  CE1   A PHE B 2 81  ? 15.058  -40.490 1.037   0.20 51.79  ? 81  PHE B CE1   1 
ATOM   8054  C  CE1   B PHE B 2 81  ? 14.946  -40.148 1.152   0.80 50.93  ? 81  PHE B CE1   1 
ATOM   8055  C  CE2   A PHE B 2 81  ? 12.775  -39.794 0.937   0.20 53.51  ? 81  PHE B CE2   1 
ATOM   8056  C  CE2   B PHE B 2 81  ? 12.669  -39.437 1.215   0.80 52.91  ? 81  PHE B CE2   1 
ATOM   8057  C  CZ    A PHE B 2 81  ? 13.783  -40.499 1.564   0.20 52.85  ? 81  PHE B CZ    1 
ATOM   8058  C  CZ    B PHE B 2 81  ? 13.721  -40.129 1.782   0.80 52.92  ? 81  PHE B CZ    1 
ATOM   8059  N  N     A GLY B 2 82  ? 15.085  -38.774 -5.660  0.20 52.54  ? 82  GLY B N     1 
ATOM   8060  N  N     B GLY B 2 82  ? 14.817  -38.553 -5.529  0.80 51.41  ? 82  GLY B N     1 
ATOM   8061  C  CA    A GLY B 2 82  ? 15.156  -37.952 -6.855  0.20 52.48  ? 82  GLY B CA    1 
ATOM   8062  C  CA    B GLY B 2 82  ? 14.802  -37.797 -6.770  0.80 50.01  ? 82  GLY B CA    1 
ATOM   8063  C  C     A GLY B 2 82  ? 13.853  -37.836 -7.614  0.20 56.28  ? 82  GLY B C     1 
ATOM   8064  C  C     B GLY B 2 82  ? 13.476  -37.801 -7.500  0.80 57.12  ? 82  GLY B C     1 
ATOM   8065  O  O     A GLY B 2 82  ? 13.571  -36.789 -8.204  0.20 55.98  ? 82  GLY B O     1 
ATOM   8066  O  O     B GLY B 2 82  ? 13.194  -36.869 -8.260  0.80 55.91  ? 82  GLY B O     1 
ATOM   8067  N  N     A GLN B 2 83  ? 13.043  -38.895 -7.617  0.20 56.89  ? 83  GLN B N     1 
ATOM   8068  N  N     B GLN B 2 83  ? 12.649  -38.826 -7.285  0.80 57.40  ? 83  GLN B N     1 
ATOM   8069  C  CA    A GLN B 2 83  ? 11.788  -38.882 -8.357  0.20 58.96  ? 83  GLN B CA    1 
ATOM   8070  C  CA    B GLN B 2 83  ? 11.351  -38.935 -7.940  0.80 60.14  ? 83  GLN B CA    1 
ATOM   8071  C  C     A GLN B 2 83  ? 10.654  -38.204 -7.600  0.20 58.64  ? 83  GLN B C     1 
ATOM   8072  C  C     B GLN B 2 83  ? 10.217  -38.353 -7.103  0.80 57.87  ? 83  GLN B C     1 
ATOM   8073  O  O     A GLN B 2 83  ? 9.611   -37.929 -8.203  0.20 58.81  ? 83  GLN B O     1 
ATOM   8074  O  O     B GLN B 2 83  ? 9.069   -38.801 -7.230  0.80 65.14  ? 83  GLN B O     1 
ATOM   8075  C  CB    A GLN B 2 83  ? 11.377  -40.313 -8.720  0.20 59.90  ? 83  GLN B CB    1 
ATOM   8076  C  CB    B GLN B 2 83  ? 11.059  -40.396 -8.286  0.80 59.35  ? 83  GLN B CB    1 
ATOM   8077  C  CG    A GLN B 2 83  ? 12.408  -41.072 -9.545  0.20 58.11  ? 83  GLN B CG    1 
ATOM   8078  C  CG    B GLN B 2 83  ? 12.215  -41.133 -8.957  0.80 58.07  ? 83  GLN B CG    1 
ATOM   8079  C  CD    A GLN B 2 83  ? 12.597  -40.494 -10.937 0.20 59.58  ? 83  GLN B CD    1 
ATOM   8080  C  CD    B GLN B 2 83  ? 12.579  -40.574 -10.323 0.80 62.55  ? 83  GLN B CD    1 
ATOM   8081  O  OE1   A GLN B 2 83  ? 11.707  -39.839 -11.478 0.20 59.77  ? 83  GLN B OE1   1 
ATOM   8082  O  OE1   B GLN B 2 83  ? 11.780  -39.889 -10.965 0.80 64.02  ? 83  GLN B OE1   1 
ATOM   8083  N  NE2   A GLN B 2 83  ? 13.764  -40.736 -11.522 0.20 58.13  ? 83  GLN B NE2   1 
ATOM   8084  N  NE2   B GLN B 2 83  ? 13.794  -40.871 -10.776 0.80 59.65  ? 83  GLN B NE2   1 
ATOM   8085  N  N     A ILE B 2 84  ? 10.828  -37.922 -6.305  0.20 57.41  ? 84  ILE B N     1 
ATOM   8086  N  N     B ILE B 2 84  ? 10.503  -37.369 -6.250  0.80 58.71  ? 84  ILE B N     1 
ATOM   8087  C  CA    A ILE B 2 84  ? 9.755   -37.310 -5.530  0.20 58.80  ? 84  ILE B CA    1 
ATOM   8088  C  CA    B ILE B 2 84  ? 9.470   -36.726 -5.447  0.80 59.47  ? 84  ILE B CA    1 
ATOM   8089  C  C     A ILE B 2 84  ? 9.535   -35.853 -5.922  0.20 55.65  ? 84  ILE B C     1 
ATOM   8090  C  C     B ILE B 2 84  ? 9.232   -35.269 -5.840  0.80 55.91  ? 84  ILE B C     1 
ATOM   8091  O  O     A ILE B 2 84  ? 8.435   -35.322 -5.723  0.20 54.45  ? 84  ILE B O     1 
ATOM   8092  O  O     B ILE B 2 84  ? 8.121   -34.761 -5.616  0.80 52.46  ? 84  ILE B O     1 
ATOM   8093  C  CB    A ILE B 2 84  ? 10.039  -37.440 -4.019  0.20 56.43  ? 84  ILE B CB    1 
ATOM   8094  C  CB    B ILE B 2 84  ? 9.779   -36.833 -3.936  0.80 57.07  ? 84  ILE B CB    1 
ATOM   8095  C  CG1   A ILE B 2 84  ? 8.775   -37.152 -3.206  0.20 57.72  ? 84  ILE B CG1   1 
ATOM   8096  C  CG1   B ILE B 2 84  ? 8.519   -36.576 -3.105  0.80 56.61  ? 84  ILE B CG1   1 
ATOM   8097  C  CG2   A ILE B 2 84  ? 11.163  -36.506 -3.594  0.20 56.57  ? 84  ILE B CG2   1 
ATOM   8098  C  CG2   B ILE B 2 84  ? 10.854  -35.840 -3.525  0.80 59.27  ? 84  ILE B CG2   1 
ATOM   8099  C  CD1   A ILE B 2 84  ? 8.986   -37.199 -1.710  0.20 55.27  ? 84  ILE B CD1   1 
ATOM   8100  C  CD1   B ILE B 2 84  ? 7.281   -37.275 -3.628  0.80 62.29  ? 84  ILE B CD1   1 
ATOM   8101  N  N     A PHE B 2 85  ? 10.543  -35.192 -6.486  0.20 53.17  ? 85  PHE B N     1 
ATOM   8102  N  N     B PHE B 2 85  ? 10.214  -34.589 -6.430  0.80 54.04  ? 85  PHE B N     1 
ATOM   8103  C  CA    A PHE B 2 85  ? 10.370  -33.816 -6.926  0.20 51.17  ? 85  PHE B CA    1 
ATOM   8104  C  CA    B PHE B 2 85  ? 10.017  -33.201 -6.823  0.80 50.16  ? 85  PHE B CA    1 
ATOM   8105  C  C     A PHE B 2 85  ? 9.417   -33.755 -8.114  0.20 51.34  ? 85  PHE B C     1 
ATOM   8106  C  C     B PHE B 2 85  ? 9.081   -33.120 -8.025  0.80 52.84  ? 85  PHE B C     1 
ATOM   8107  O  O     A PHE B 2 85  ? 9.364   -34.665 -8.945  0.20 52.43  ? 85  PHE B O     1 
ATOM   8108  O  O     B PHE B 2 85  ? 8.954   -34.065 -8.805  0.80 49.46  ? 85  PHE B O     1 
ATOM   8109  C  CB    A PHE B 2 85  ? 11.714  -33.194 -7.305  0.20 48.23  ? 85  PHE B CB    1 
ATOM   8110  C  CB    B PHE B 2 85  ? 11.359  -32.542 -7.142  0.80 41.83  ? 85  PHE B CB    1 
ATOM   8111  C  CG    A PHE B 2 85  ? 12.749  -33.274 -6.221  0.20 50.33  ? 85  PHE B CG    1 
ATOM   8112  C  CG    B PHE B 2 85  ? 12.400  -32.749 -6.077  0.80 51.40  ? 85  PHE B CG    1 
ATOM   8113  C  CD1   A PHE B 2 85  ? 12.623  -32.520 -5.066  0.20 52.24  ? 85  PHE B CD1   1 
ATOM   8114  C  CD1   B PHE B 2 85  ? 12.301  -32.098 -4.854  0.80 53.43  ? 85  PHE B CD1   1 
ATOM   8115  C  CD2   A PHE B 2 85  ? 13.856  -34.094 -6.362  0.20 52.65  ? 85  PHE B CD2   1 
ATOM   8116  C  CD2   B PHE B 2 85  ? 13.469  -33.603 -6.289  0.80 51.85  ? 85  PHE B CD2   1 
ATOM   8117  C  CE1   A PHE B 2 85  ? 13.576  -32.591 -4.067  0.20 49.58  ? 85  PHE B CE1   1 
ATOM   8118  C  CE1   B PHE B 2 85  ? 13.255  -32.297 -3.865  0.80 49.04  ? 85  PHE B CE1   1 
ATOM   8119  C  CE2   A PHE B 2 85  ? 14.815  -34.167 -5.368  0.20 50.56  ? 85  PHE B CE2   1 
ATOM   8120  C  CE2   B PHE B 2 85  ? 14.430  -33.803 -5.310  0.80 49.87  ? 85  PHE B CE2   1 
ATOM   8121  C  CZ    A PHE B 2 85  ? 14.674  -33.416 -4.220  0.20 50.03  ? 85  PHE B CZ    1 
ATOM   8122  C  CZ    B PHE B 2 85  ? 14.323  -33.152 -4.096  0.80 52.05  ? 85  PHE B CZ    1 
ATOM   8123  N  N     A ARG B 2 86  ? 8.657   -32.670 -8.184  0.20 51.80  ? 86  ARG B N     1 
ATOM   8124  N  N     B ARG B 2 86  ? 8.408   -31.986 -8.162  0.80 50.84  ? 86  ARG B N     1 
ATOM   8125  C  CA    A ARG B 2 86  ? 7.714   -32.492 -9.279  0.20 48.72  ? 86  ARG B CA    1 
ATOM   8126  C  CA    B ARG B 2 86  ? 7.513   -31.800 -9.295  0.80 46.98  ? 86  ARG B CA    1 
ATOM   8127  C  C     A ARG B 2 86  ? 8.473   -32.326 -10.591 0.20 49.35  ? 86  ARG B C     1 
ATOM   8128  C  C     B ARG B 2 86  ? 8.327   -31.666 -10.573 0.80 50.34  ? 86  ARG B C     1 
ATOM   8129  O  O     A ARG B 2 86  ? 9.416   -31.527 -10.657 0.20 49.33  ? 86  ARG B O     1 
ATOM   8130  O  O     B ARG B 2 86  ? 9.169   -30.759 -10.668 0.80 44.73  ? 86  ARG B O     1 
ATOM   8131  C  CB    A ARG B 2 86  ? 6.822   -31.281 -9.021  0.20 50.99  ? 86  ARG B CB    1 
ATOM   8132  C  CB    B ARG B 2 86  ? 6.626   -30.571 -9.103  0.80 51.68  ? 86  ARG B CB    1 
ATOM   8133  C  CG    A ARG B 2 86  ? 5.791   -31.016 -10.102 0.20 49.69  ? 86  ARG B CG    1 
ATOM   8134  C  CG    B ARG B 2 86  ? 5.303   -30.863 -8.413  0.80 54.27  ? 86  ARG B CG    1 
ATOM   8135  C  CD    A ARG B 2 86  ? 4.953   -29.793 -9.767  0.20 52.74  ? 86  ARG B CD    1 
ATOM   8136  C  CD    B ARG B 2 86  ? 4.325   -29.709 -8.577  0.80 57.19  ? 86  ARG B CD    1 
ATOM   8137  N  NE    A ARG B 2 86  ? 4.210   -29.975 -8.525  0.20 57.07  ? 86  ARG B NE    1 
ATOM   8138  N  NE    B ARG B 2 86  ? 3.030   -30.018 -7.981  0.80 65.91  ? 86  ARG B NE    1 
ATOM   8139  C  CZ    A ARG B 2 86  ? 3.487   -29.032 -7.936  0.20 58.89  ? 86  ARG B CZ    1 
ATOM   8140  C  CZ    B ARG B 2 86  ? 2.721   -29.807 -6.709  0.80 63.35  ? 86  ARG B CZ    1 
ATOM   8141  N  NH1   A ARG B 2 86  ? 3.387   -27.816 -8.447  0.20 56.36  ? 86  ARG B NH1   1 
ATOM   8142  N  NH1   B ARG B 2 86  ? 3.585   -29.258 -5.871  0.80 65.77  ? 86  ARG B NH1   1 
ATOM   8143  N  NH2   A ARG B 2 86  ? 2.850   -29.317 -6.804  0.20 62.10  ? 86  ARG B NH2   1 
ATOM   8144  N  NH2   B ARG B 2 86  ? 1.515   -30.157 -6.267  0.80 65.39  ? 86  ARG B NH2   1 
ATOM   8145  N  N     A PRO B 2 87  ? 8.106   -33.060 -11.644 0.20 50.37  ? 87  PRO B N     1 
ATOM   8146  N  N     B PRO B 2 87  ? 8.123   -32.538 -11.568 0.80 51.17  ? 87  PRO B N     1 
ATOM   8147  C  CA    A PRO B 2 87  ? 8.855   -32.951 -12.908 0.20 49.07  ? 87  PRO B CA    1 
ATOM   8148  C  CA    B PRO B 2 87  ? 8.876   -32.409 -12.829 0.80 48.34  ? 87  PRO B CA    1 
ATOM   8149  C  C     A PRO B 2 87  ? 8.777   -31.576 -13.545 0.20 49.27  ? 87  PRO B C     1 
ATOM   8150  C  C     B PRO B 2 87  ? 8.713   -31.054 -13.485 0.80 50.00  ? 87  PRO B C     1 
ATOM   8151  O  O     A PRO B 2 87  ? 9.706   -31.182 -14.260 0.20 50.77  ? 87  PRO B O     1 
ATOM   8152  O  O     B PRO B 2 87  ? 9.652   -30.556 -14.122 0.80 52.35  ? 87  PRO B O     1 
ATOM   8153  C  CB    A PRO B 2 87  ? 8.201   -34.019 -13.796 0.20 47.29  ? 87  PRO B CB    1 
ATOM   8154  C  CB    B PRO B 2 87  ? 8.292   -33.531 -13.698 0.80 46.11  ? 87  PRO B CB    1 
ATOM   8155  C  CG    A PRO B 2 87  ? 7.537   -34.965 -12.841 0.20 50.44  ? 87  PRO B CG    1 
ATOM   8156  C  CG    B PRO B 2 87  ? 7.782   -34.539 -12.715 0.80 52.10  ? 87  PRO B CG    1 
ATOM   8157  C  CD    A PRO B 2 87  ? 7.083   -34.117 -11.694 0.20 51.77  ? 87  PRO B CD    1 
ATOM   8158  C  CD    B PRO B 2 87  ? 7.279   -33.745 -11.540 0.80 52.52  ? 87  PRO B CD    1 
ATOM   8159  N  N     A ASP B 2 88  ? 7.696   -30.830 -13.305 0.20 50.27  ? 88  ASP B N     1 
ATOM   8160  N  N     B ASP B 2 88  ? 7.541   -30.439 -13.337 0.80 51.06  ? 88  ASP B N     1 
ATOM   8161  C  CA    A ASP B 2 88  ? 7.551   -29.520 -13.931 0.20 49.76  ? 88  ASP B CA    1 
ATOM   8162  C  CA    B ASP B 2 88  ? 7.325   -29.073 -13.796 0.80 49.40  ? 88  ASP B CA    1 
ATOM   8163  C  C     A ASP B 2 88  ? 8.538   -28.509 -13.362 0.20 49.79  ? 88  ASP B C     1 
ATOM   8164  C  C     B ASP B 2 88  ? 8.249   -28.079 -13.094 0.80 50.16  ? 88  ASP B C     1 
ATOM   8165  O  O     A ASP B 2 88  ? 8.948   -27.580 -14.069 0.20 50.11  ? 88  ASP B O     1 
ATOM   8166  O  O     B ASP B 2 88  ? 8.448   -26.969 -13.603 0.80 51.11  ? 88  ASP B O     1 
ATOM   8167  C  CB    A ASP B 2 88  ? 6.119   -29.014 -13.758 0.20 54.58  ? 88  ASP B CB    1 
ATOM   8168  C  CB    B ASP B 2 88  ? 5.847   -28.714 -13.576 0.80 56.91  ? 88  ASP B CB    1 
ATOM   8169  C  CG    A ASP B 2 88  ? 5.085   -30.095 -14.004 0.20 50.88  ? 88  ASP B CG    1 
ATOM   8170  C  CG    B ASP B 2 88  ? 5.518   -27.282 -13.945 0.80 58.42  ? 88  ASP B CG    1 
ATOM   8171  O  OD1   A ASP B 2 88  ? 5.027   -31.055 -13.206 0.20 44.97  ? 88  ASP B OD1   1 
ATOM   8172  O  OD1   B ASP B 2 88  ? 5.249   -27.022 -15.138 0.80 75.44  ? 88  ASP B OD1   1 
ATOM   8173  O  OD2   A ASP B 2 88  ? 4.331   -29.982 -14.992 0.20 54.12  ? 88  ASP B OD2   1 
ATOM   8174  O  OD2   B ASP B 2 88  ? 5.515   -26.419 -13.038 0.80 55.57  ? 88  ASP B OD2   1 
ATOM   8175  N  N     A ASN B 2 89  ? 8.934   -28.669 -12.096 0.20 47.48  ? 89  ASN B N     1 
ATOM   8176  N  N     B ASN B 2 89  ? 8.834   -28.455 -11.952 0.80 46.94  ? 89  ASN B N     1 
ATOM   8177  C  CA    A ASN B 2 89  ? 9.834   -27.709 -11.469 0.20 46.70  ? 89  ASN B CA    1 
ATOM   8178  C  CA    B ASN B 2 89  ? 9.669   -27.558 -11.162 0.80 45.31  ? 89  ASN B CA    1 
ATOM   8179  C  C     A ASN B 2 89  ? 11.252  -27.788 -12.020 0.20 49.11  ? 89  ASN B C     1 
ATOM   8180  C  C     B ASN B 2 89  ? 11.163  -27.727 -11.438 0.80 49.52  ? 89  ASN B C     1 
ATOM   8181  O  O     A ASN B 2 89  ? 11.987  -26.798 -11.944 0.20 45.79  ? 89  ASN B O     1 
ATOM   8182  O  O     B ASN B 2 89  ? 11.987  -27.260 -10.643 0.80 45.93  ? 89  ASN B O     1 
ATOM   8183  C  CB    A ASN B 2 89  ? 9.860   -27.916 -9.955  0.20 45.97  ? 89  ASN B CB    1 
ATOM   8184  C  CB    B ASN B 2 89  ? 9.392   -27.753 -9.670  0.80 46.45  ? 89  ASN B CB    1 
ATOM   8185  C  CG    A ASN B 2 89  ? 8.492   -27.768 -9.324  0.20 47.79  ? 89  ASN B CG    1 
ATOM   8186  C  CG    B ASN B 2 89  ? 8.048   -27.187 -9.244  0.80 48.89  ? 89  ASN B CG    1 
ATOM   8187  O  OD1   A ASN B 2 89  ? 8.157   -28.471 -8.371  0.20 48.89  ? 89  ASN B OD1   1 
ATOM   8188  O  OD1   B ASN B 2 89  ? 7.182   -26.929 -10.077 0.80 51.06  ? 89  ASN B OD1   1 
ATOM   8189  N  ND2   A ASN B 2 89  ? 7.690   -26.854 -9.856  0.20 48.87  ? 89  ASN B ND2   1 
ATOM   8190  N  ND2   B ASN B 2 89  ? 7.870   -26.990 -7.937  0.80 43.63  ? 89  ASN B ND2   1 
ATOM   8191  N  N     A PHE B 2 90  ? 11.653  -28.938 -12.564 0.20 48.43  ? 90  PHE B N     1 
ATOM   8192  N  N     B PHE B 2 90  ? 11.531  -28.383 -12.538 0.80 50.71  ? 90  PHE B N     1 
ATOM   8193  C  CA    A PHE B 2 90  ? 12.985  -29.091 -13.137 0.20 47.05  ? 90  PHE B CA    1 
ATOM   8194  C  CA    B PHE B 2 90  ? 12.918  -28.460 -12.986 0.80 45.75  ? 90  PHE B CA    1 
ATOM   8195  C  C     A PHE B 2 90  ? 13.191  -28.142 -14.309 0.20 47.97  ? 90  PHE B C     1 
ATOM   8196  C  C     B PHE B 2 90  ? 13.122  -27.415 -14.076 0.80 50.19  ? 90  PHE B C     1 
ATOM   8197  O  O     A PHE B 2 90  ? 12.644  -28.359 -15.394 0.20 49.24  ? 90  PHE B O     1 
ATOM   8198  O  O     B PHE B 2 90  ? 12.421  -27.434 -15.093 0.80 53.46  ? 90  PHE B O     1 
ATOM   8199  C  CB    A PHE B 2 90  ? 13.213  -30.533 -13.593 0.20 47.94  ? 90  PHE B CB    1 
ATOM   8200  C  CB    B PHE B 2 90  ? 13.255  -29.853 -13.520 0.80 46.01  ? 90  PHE B CB    1 
ATOM   8201  C  CG    A PHE B 2 90  ? 13.503  -31.488 -12.474 0.20 47.89  ? 90  PHE B CG    1 
ATOM   8202  C  CG    B PHE B 2 90  ? 13.389  -30.913 -12.458 0.80 43.91  ? 90  PHE B CG    1 
ATOM   8203  C  CD1   A PHE B 2 90  ? 12.477  -32.002 -11.699 0.20 47.28  ? 90  PHE B CD1   1 
ATOM   8204  C  CD1   B PHE B 2 90  ? 12.278  -31.366 -11.756 0.80 46.70  ? 90  PHE B CD1   1 
ATOM   8205  C  CD2   A PHE B 2 90  ? 14.803  -31.886 -12.206 0.20 46.76  ? 90  PHE B CD2   1 
ATOM   8206  C  CD2   B PHE B 2 90  ? 14.621  -31.493 -12.198 0.80 43.78  ? 90  PHE B CD2   1 
ATOM   8207  C  CE1   A PHE B 2 90  ? 12.742  -32.887 -10.672 0.20 47.30  ? 90  PHE B CE1   1 
ATOM   8208  C  CE1   B PHE B 2 90  ? 12.403  -32.357 -10.796 0.80 45.99  ? 90  PHE B CE1   1 
ATOM   8209  C  CE2   A PHE B 2 90  ? 15.075  -32.770 -11.182 0.20 50.66  ? 90  PHE B CE2   1 
ATOM   8210  C  CE2   B PHE B 2 90  ? 14.753  -32.481 -11.239 0.80 50.84  ? 90  PHE B CE2   1 
ATOM   8211  C  CZ    A PHE B 2 90  ? 14.044  -33.271 -10.412 0.20 50.57  ? 90  PHE B CZ    1 
ATOM   8212  C  CZ    B PHE B 2 90  ? 13.641  -32.913 -10.536 0.80 51.01  ? 90  PHE B CZ    1 
ATOM   8213  N  N     A VAL B 2 91  ? 13.973  -27.087 -14.100 0.20 47.04  ? 91  VAL B N     1 
ATOM   8214  N  N     B VAL B 2 91  ? 14.068  -26.503 -13.866 0.80 45.08  ? 91  VAL B N     1 
ATOM   8215  C  CA    A VAL B 2 91  ? 14.344  -26.149 -15.154 0.20 47.73  ? 91  VAL B CA    1 
ATOM   8216  C  CA    B VAL B 2 91  ? 14.328  -25.413 -14.800 0.80 43.65  ? 91  VAL B CA    1 
ATOM   8217  C  C     A VAL B 2 91  ? 15.863  -26.146 -15.255 0.20 50.05  ? 91  VAL B C     1 
ATOM   8218  C  C     B VAL B 2 91  ? 15.826  -25.387 -15.077 0.80 52.45  ? 91  VAL B C     1 
ATOM   8219  O  O     A VAL B 2 91  ? 16.554  -25.759 -14.304 0.20 47.36  ? 91  VAL B O     1 
ATOM   8220  O  O     B VAL B 2 91  ? 16.611  -24.938 -14.231 0.80 44.41  ? 91  VAL B O     1 
ATOM   8221  C  CB    A VAL B 2 91  ? 13.791  -24.737 -14.894 0.20 45.31  ? 91  VAL B CB    1 
ATOM   8222  C  CB    B VAL B 2 91  ? 13.845  -24.058 -14.267 0.80 43.01  ? 91  VAL B CB    1 
ATOM   8223  C  CG1   A VAL B 2 91  ? 13.890  -24.376 -13.419 0.20 42.87  ? 91  VAL B CG1   1 
ATOM   8224  C  CG1   B VAL B 2 91  ? 13.952  -23.006 -15.353 0.80 43.00  ? 91  VAL B CG1   1 
ATOM   8225  C  CG2   A VAL B 2 91  ? 14.517  -23.712 -15.755 0.20 44.84  ? 91  VAL B CG2   1 
ATOM   8226  C  CG2   B VAL B 2 91  ? 12.408  -24.154 -13.741 0.80 39.54  ? 91  VAL B CG2   1 
ATOM   8227  N  N     A PHE B 2 92  ? 16.380  -26.599 -16.395 0.20 50.06  ? 92  PHE B N     1 
ATOM   8228  N  N     B PHE B 2 92  ? 16.227  -25.856 -16.259 0.80 48.38  ? 92  PHE B N     1 
ATOM   8229  C  CA    A PHE B 2 92  ? 17.814  -26.722 -16.606 0.20 49.88  ? 92  PHE B CA    1 
ATOM   8230  C  CA    B PHE B 2 92  ? 17.637  -26.058 -16.566 0.80 48.55  ? 92  PHE B CA    1 
ATOM   8231  C  C     A PHE B 2 92  ? 18.171  -26.193 -17.985 0.20 51.33  ? 92  PHE B C     1 
ATOM   8232  C  C     B PHE B 2 92  ? 17.972  -25.463 -17.925 0.80 53.22  ? 92  PHE B C     1 
ATOM   8233  O  O     A PHE B 2 92  ? 17.453  -26.440 -18.959 0.20 48.89  ? 92  PHE B O     1 
ATOM   8234  O  O     B PHE B 2 92  ? 17.232  -25.658 -18.894 0.80 45.08  ? 92  PHE B O     1 
ATOM   8235  C  CB    A PHE B 2 92  ? 18.278  -28.179 -16.458 0.20 53.28  ? 92  PHE B CB    1 
ATOM   8236  C  CB    B PHE B 2 92  ? 17.990  -27.548 -16.505 0.80 52.48  ? 92  PHE B CB    1 
ATOM   8237  C  CG    A PHE B 2 92  ? 18.298  -28.666 -15.035 0.20 54.34  ? 92  PHE B CG    1 
ATOM   8238  C  CG    B PHE B 2 92  ? 17.912  -28.121 -15.112 0.80 54.72  ? 92  PHE B CG    1 
ATOM   8239  C  CD1   A PHE B 2 92  ? 17.128  -29.052 -14.402 0.20 54.65  ? 92  PHE B CD1   1 
ATOM   8240  C  CD1   B PHE B 2 92  ? 16.701  -28.528 -14.582 0.80 57.85  ? 92  PHE B CD1   1 
ATOM   8241  C  CD2   A PHE B 2 92  ? 19.488  -28.738 -14.330 0.20 52.61  ? 92  PHE B CD2   1 
ATOM   8242  C  CD2   B PHE B 2 92  ? 19.046  -28.225 -14.322 0.80 54.02  ? 92  PHE B CD2   1 
ATOM   8243  C  CE1   A PHE B 2 92  ? 17.144  -29.495 -13.093 0.20 50.51  ? 92  PHE B CE1   1 
ATOM   8244  C  CE1   B PHE B 2 92  ? 16.627  -29.036 -13.296 0.80 52.30  ? 92  PHE B CE1   1 
ATOM   8245  C  CE2   A PHE B 2 92  ? 19.509  -29.184 -13.021 0.20 52.45  ? 92  PHE B CE2   1 
ATOM   8246  C  CE2   B PHE B 2 92  ? 18.971  -28.737 -13.036 0.80 51.88  ? 92  PHE B CE2   1 
ATOM   8247  C  CZ    A PHE B 2 92  ? 18.335  -29.561 -12.402 0.20 49.60  ? 92  PHE B CZ    1 
ATOM   8248  C  CZ    B PHE B 2 92  ? 17.762  -29.139 -12.525 0.80 44.64  ? 92  PHE B CZ    1 
ATOM   8249  N  N     A GLY B 2 93  ? 19.284  -25.465 -18.060 0.20 51.24  ? 93  GLY B N     1 
ATOM   8250  N  N     B GLY B 2 93  ? 19.084  -24.727 -17.982 0.80 52.05  ? 93  GLY B N     1 
ATOM   8251  C  CA    A GLY B 2 93  ? 19.731  -24.887 -19.307 0.20 51.87  ? 93  GLY B CA    1 
ATOM   8252  C  CA    B GLY B 2 93  ? 19.525  -24.079 -19.197 0.80 49.20  ? 93  GLY B CA    1 
ATOM   8253  C  C     A GLY B 2 93  ? 20.551  -25.854 -20.137 0.20 53.78  ? 93  GLY B C     1 
ATOM   8254  C  C     B GLY B 2 93  ? 20.351  -25.003 -20.072 0.80 56.77  ? 93  GLY B C     1 
ATOM   8255  O  O     A GLY B 2 93  ? 20.764  -27.014 -19.783 0.20 52.30  ? 93  GLY B O     1 
ATOM   8256  O  O     B GLY B 2 93  ? 20.459  -26.209 -19.838 0.80 52.70  ? 93  GLY B O     1 
ATOM   8257  N  N     A GLN B 2 94  ? 21.024  -25.349 -21.275 0.20 55.27  ? 94  GLN B N     1 
ATOM   8258  N  N     B GLN B 2 94  ? 20.951  -24.409 -21.103 0.80 48.15  ? 94  GLN B N     1 
ATOM   8259  C  CA    A GLN B 2 94  ? 21.835  -26.126 -22.204 0.20 57.15  ? 94  GLN B CA    1 
ATOM   8260  C  CA    B GLN B 2 94  ? 21.749  -25.176 -22.066 0.80 60.55  ? 94  GLN B CA    1 
ATOM   8261  C  C     A GLN B 2 94  ? 23.329  -25.902 -22.017 0.20 59.26  ? 94  GLN B C     1 
ATOM   8262  C  C     B GLN B 2 94  ? 23.206  -25.221 -21.616 0.80 60.13  ? 94  GLN B C     1 
ATOM   8263  O  O     A GLN B 2 94  ? 24.113  -26.847 -22.150 0.20 57.00  ? 94  GLN B O     1 
ATOM   8264  O  O     B GLN B 2 94  ? 23.696  -26.261 -21.166 0.80 61.80  ? 94  GLN B O     1 
ATOM   8265  C  CB    A GLN B 2 94  ? 21.446  -25.792 -23.648 0.20 55.33  ? 94  GLN B CB    1 
ATOM   8266  C  CB    B GLN B 2 94  ? 21.607  -24.578 -23.466 0.80 57.13  ? 94  GLN B CB    1 
ATOM   8267  N  N     A SER B 2 95  ? 23.740  -24.677 -21.705 0.20 60.22  ? 95  SER B N     1 
ATOM   8268  N  N     B SER B 2 95  ? 23.905  -24.098 -21.730 0.80 62.35  ? 95  SER B N     1 
ATOM   8269  C  CA    A SER B 2 95  ? 25.141  -24.339 -21.501 0.20 63.79  ? 95  SER B CA    1 
ATOM   8270  C  CA    B SER B 2 95  ? 25.300  -24.009 -21.324 0.80 66.03  ? 95  SER B CA    1 
ATOM   8271  C  C     A SER B 2 95  ? 25.376  -23.956 -20.046 0.20 60.65  ? 95  SER B C     1 
ATOM   8272  C  C     B SER B 2 95  ? 25.411  -23.437 -19.918 0.80 62.36  ? 95  SER B C     1 
ATOM   8273  O  O     A SER B 2 95  ? 24.598  -23.197 -19.460 0.20 57.12  ? 95  SER B O     1 
ATOM   8274  O  O     B SER B 2 95  ? 24.723  -22.470 -19.572 0.80 55.52  ? 95  SER B O     1 
ATOM   8275  C  CB    A SER B 2 95  ? 25.569  -23.189 -22.416 0.20 63.85  ? 95  SER B CB    1 
ATOM   8276  C  CB    B SER B 2 95  ? 26.106  -23.143 -22.290 0.80 64.84  ? 95  SER B CB    1 
ATOM   8277  O  OG    A SER B 2 95  ? 24.834  -22.010 -22.131 0.20 62.15  ? 95  SER B OG    1 
ATOM   8278  O  OG    B SER B 2 95  ? 27.400  -22.900 -21.766 0.80 70.78  ? 95  SER B OG    1 
ATOM   8279  N  N     A GLY B 2 96  ? 26.453  -24.480 -19.471 0.20 57.60  ? 96  GLY B N     1 
ATOM   8280  N  N     B GLY B 2 96  ? 26.297  -24.029 -19.121 0.80 55.44  ? 96  GLY B N     1 
ATOM   8281  C  CA    A GLY B 2 96  ? 26.801  -24.182 -18.100 0.20 55.30  ? 96  GLY B CA    1 
ATOM   8282  C  CA    B GLY B 2 96  ? 26.558  -23.560 -17.776 0.80 56.03  ? 96  GLY B CA    1 
ATOM   8283  C  C     A GLY B 2 96  ? 27.305  -22.760 -17.927 0.20 52.00  ? 96  GLY B C     1 
ATOM   8284  C  C     B GLY B 2 96  ? 27.183  -22.181 -17.739 0.80 52.64  ? 96  GLY B C     1 
ATOM   8285  O  O     A GLY B 2 96  ? 27.366  -21.957 -18.859 0.20 53.43  ? 96  GLY B O     1 
ATOM   8286  O  O     B GLY B 2 96  ? 27.064  -21.406 -18.694 0.80 53.96  ? 96  GLY B O     1 
ATOM   8287  N  N     A ALA B 2 97  ? 27.676  -22.449 -16.685 0.20 46.31  ? 97  ALA B N     1 
ATOM   8288  N  N     B ALA B 2 97  ? 27.864  -21.863 -16.640 0.80 43.80  ? 97  ALA B N     1 
ATOM   8289  C  CA    A ALA B 2 97  ? 28.173  -21.123 -16.347 0.20 42.14  ? 97  ALA B CA    1 
ATOM   8290  C  CA    B ALA B 2 97  ? 28.413  -20.532 -16.444 0.80 37.23  ? 97  ALA B CA    1 
ATOM   8291  C  C     A ALA B 2 97  ? 29.689  -21.022 -16.404 0.20 40.32  ? 97  ALA B C     1 
ATOM   8292  C  C     B ALA B 2 97  ? 29.923  -20.502 -16.293 0.80 39.49  ? 97  ALA B C     1 
ATOM   8293  O  O     A ALA B 2 97  ? 30.216  -19.909 -16.507 0.20 45.06  ? 97  ALA B O     1 
ATOM   8294  O  O     B ALA B 2 97  ? 30.486  -19.407 -16.192 0.80 49.63  ? 97  ALA B O     1 
ATOM   8295  C  CB    A ALA B 2 97  ? 27.691  -20.714 -14.950 0.20 39.59  ? 97  ALA B CB    1 
ATOM   8296  C  CB    B ALA B 2 97  ? 27.774  -19.864 -15.213 0.80 40.04  ? 97  ALA B CB    1 
ATOM   8297  N  N     A GLY B 2 98  ? 30.398  -22.146 -16.338 0.20 42.41  ? 98  GLY B N     1 
ATOM   8298  N  N     B GLY B 2 98  ? 30.589  -21.654 -16.265 0.80 43.67  ? 98  GLY B N     1 
ATOM   8299  C  CA    A GLY B 2 98  ? 31.849  -22.117 -16.420 0.20 41.02  ? 98  GLY B CA    1 
ATOM   8300  C  CA    B GLY B 2 98  ? 32.043  -21.721 -16.165 0.80 39.37  ? 98  GLY B CA    1 
ATOM   8301  C  C     A GLY B 2 98  ? 32.520  -21.437 -15.251 0.20 38.70  ? 98  GLY B C     1 
ATOM   8302  C  C     B GLY B 2 98  ? 32.678  -20.891 -15.069 0.80 39.37  ? 98  GLY B C     1 
ATOM   8303  O  O     A GLY B 2 98  ? 33.581  -20.827 -15.422 0.20 39.93  ? 98  GLY B O     1 
ATOM   8304  O  O     B GLY B 2 98  ? 33.700  -20.232 -15.310 0.80 40.37  ? 98  GLY B O     1 
ATOM   8305  N  N     A ASN B 2 99  ? 31.925  -21.527 -14.060 0.20 39.35  ? 99  ASN B N     1 
ATOM   8306  N  N     B ASN B 2 99  ? 32.098  -20.906 -13.867 0.80 41.47  ? 99  ASN B N     1 
ATOM   8307  C  CA    A ASN B 2 99  ? 32.456  -20.898 -12.849 0.20 39.93  ? 99  ASN B CA    1 
ATOM   8308  C  CA    B ASN B 2 99  ? 32.627  -20.167 -12.713 0.80 40.06  ? 99  ASN B CA    1 
ATOM   8309  C  C     A ASN B 2 99  ? 32.638  -19.392 -13.024 0.20 36.85  ? 99  ASN B C     1 
ATOM   8310  C  C     B ASN B 2 99  ? 32.666  -18.664 -12.966 0.80 35.03  ? 99  ASN B C     1 
ATOM   8311  O  O     A ASN B 2 99  ? 33.562  -18.800 -12.461 0.20 33.48  ? 99  ASN B O     1 
ATOM   8312  O  O     B ASN B 2 99  ? 33.431  -17.939 -12.330 0.80 37.71  ? 99  ASN B O     1 
ATOM   8313  C  CB    A ASN B 2 99  ? 33.775  -21.545 -12.415 0.20 41.04  ? 99  ASN B CB    1 
ATOM   8314  C  CB    B ASN B 2 99  ? 34.016  -20.666 -12.304 0.80 43.62  ? 99  ASN B CB    1 
ATOM   8315  C  CG    A ASN B 2 99  ? 33.638  -23.031 -12.155 0.20 41.65  ? 99  ASN B CG    1 
ATOM   8316  C  CG    B ASN B 2 99  ? 33.969  -22.021 -11.641 0.80 39.80  ? 99  ASN B CG    1 
ATOM   8317  O  OD1   A ASN B 2 99  ? 32.604  -23.500 -11.675 0.20 37.69  ? 99  ASN B OD1   1 
ATOM   8318  O  OD1   B ASN B 2 99  ? 33.038  -22.326 -10.892 0.80 37.64  ? 99  ASN B OD1   1 
ATOM   8319  N  ND2   A ASN B 2 99  ? 34.685  -23.784 -12.474 0.20 42.21  ? 99  ASN B ND2   1 
ATOM   8320  N  ND2   B ASN B 2 99  ? 34.973  -22.848 -11.916 0.80 42.88  ? 99  ASN B ND2   1 
ATOM   8321  N  N     A ASN B 2 100 ? 31.758  -18.764 -13.800 0.20 36.62  ? 100 ASN B N     1 
ATOM   8322  N  N     B ASN B 2 100 ? 31.832  -18.185 -13.879 0.80 33.60  ? 100 ASN B N     1 
ATOM   8323  C  CA    A ASN B 2 100 ? 31.830  -17.338 -14.098 0.20 37.94  ? 100 ASN B CA    1 
ATOM   8324  C  CA    B ASN B 2 100 ? 31.829  -16.787 -14.300 0.80 40.85  ? 100 ASN B CA    1 
ATOM   8325  C  C     A ASN B 2 100 ? 30.571  -16.667 -13.570 0.20 37.31  ? 100 ASN B C     1 
ATOM   8326  C  C     B ASN B 2 100 ? 30.550  -16.153 -13.766 0.80 40.61  ? 100 ASN B C     1 
ATOM   8327  O  O     A ASN B 2 100 ? 29.457  -17.055 -13.940 0.20 36.34  ? 100 ASN B O     1 
ATOM   8328  O  O     B ASN B 2 100 ? 29.479  -16.311 -14.357 0.80 33.44  ? 100 ASN B O     1 
ATOM   8329  C  CB    A ASN B 2 100 ? 31.985  -17.104 -15.605 0.20 37.64  ? 100 ASN B CB    1 
ATOM   8330  C  CB    B ASN B 2 100 ? 31.940  -16.683 -15.821 0.80 36.21  ? 100 ASN B CB    1 
ATOM   8331  C  CG    A ASN B 2 100 ? 32.357  -15.670 -15.945 0.20 38.63  ? 100 ASN B CG    1 
ATOM   8332  C  CG    B ASN B 2 100 ? 32.117  -15.257 -16.309 0.80 40.76  ? 100 ASN B CG    1 
ATOM   8333  O  OD1   A ASN B 2 100 ? 31.989  -14.732 -15.240 0.20 36.85  ? 100 ASN B OD1   1 
ATOM   8334  O  OD1   B ASN B 2 100 ? 31.733  -14.303 -15.641 0.80 35.49  ? 100 ASN B OD1   1 
ATOM   8335  N  ND2   A ASN B 2 100 ? 33.089  -15.497 -17.040 0.20 39.46  ? 100 ASN B ND2   1 
ATOM   8336  N  ND2   B ASN B 2 100 ? 32.694  -15.111 -17.500 0.80 38.01  ? 100 ASN B ND2   1 
ATOM   8337  N  N     A TRP B 2 101 ? 30.752  -15.655 -12.715 0.20 35.99  ? 101 TRP B N     1 
ATOM   8338  N  N     B TRP B 2 101 ? 30.687  -15.439 -12.640 0.80 35.93  ? 101 TRP B N     1 
ATOM   8339  C  CA    A TRP B 2 101 ? 29.615  -14.959 -12.120 0.20 35.30  ? 101 TRP B CA    1 
ATOM   8340  C  CA    B TRP B 2 101 ? 29.579  -14.714 -12.020 0.80 35.10  ? 101 TRP B CA    1 
ATOM   8341  C  C     A TRP B 2 101 ? 28.880  -14.096 -13.138 0.20 39.50  ? 101 TRP B C     1 
ATOM   8342  C  C     B TRP B 2 101 ? 28.798  -13.890 -13.037 0.80 40.58  ? 101 TRP B C     1 
ATOM   8343  O  O     A TRP B 2 101 ? 27.666  -13.898 -13.015 0.20 36.07  ? 101 TRP B O     1 
ATOM   8344  O  O     B TRP B 2 101 ? 27.565  -13.811 -12.964 0.80 36.00  ? 101 TRP B O     1 
ATOM   8345  C  CB    A TRP B 2 101 ? 30.088  -14.099 -10.946 0.20 30.87  ? 101 TRP B CB    1 
ATOM   8346  C  CB    B TRP B 2 101 ? 30.128  -13.805 -10.920 0.80 28.98  ? 101 TRP B CB    1 
ATOM   8347  C  CG    A TRP B 2 101 ? 28.978  -13.565 -10.077 0.20 33.75  ? 101 TRP B CG    1 
ATOM   8348  C  CG    B TRP B 2 101 ? 29.094  -13.226 -9.949  0.80 33.72  ? 101 TRP B CG    1 
ATOM   8349  C  CD1   A TRP B 2 101 ? 28.445  -14.163 -8.974  0.20 33.42  ? 101 TRP B CD1   1 
ATOM   8350  C  CD1   B TRP B 2 101 ? 28.627  -13.807 -8.808  0.80 33.94  ? 101 TRP B CD1   1 
ATOM   8351  C  CD2   A TRP B 2 101 ? 28.283  -12.322 -10.234 0.20 31.40  ? 101 TRP B CD2   1 
ATOM   8352  C  CD2   B TRP B 2 101 ? 28.461  -11.944 -10.033 0.80 31.81  ? 101 TRP B CD2   1 
ATOM   8353  N  NE1   A TRP B 2 101 ? 27.456  -13.373 -8.436  0.20 33.16  ? 101 TRP B NE1   1 
ATOM   8354  N  NE1   B TRP B 2 101 ? 27.728  -12.971 -8.177  0.80 31.99  ? 101 TRP B NE1   1 
ATOM   8355  C  CE2   A TRP B 2 101 ? 27.338  -12.236 -9.190  0.20 34.13  ? 101 TRP B CE2   1 
ATOM   8356  C  CE2   B TRP B 2 101 ? 27.611  -11.820 -8.909  0.80 34.38  ? 101 TRP B CE2   1 
ATOM   8357  C  CE3   A TRP B 2 101 ? 28.366  -11.274 -11.155 0.20 32.87  ? 101 TRP B CE3   1 
ATOM   8358  C  CE3   B TRP B 2 101 ? 28.524  -10.889 -10.947 0.80 33.21  ? 101 TRP B CE3   1 
ATOM   8359  C  CZ2   A TRP B 2 101 ? 26.483  -11.146 -9.046  0.20 33.54  ? 101 TRP B CZ2   1 
ATOM   8360  C  CZ2   B TRP B 2 101 ? 26.829  -10.687 -8.687  0.80 36.75  ? 101 TRP B CZ2   1 
ATOM   8361  C  CZ3   A TRP B 2 101 ? 27.518  -10.192 -11.008 0.20 34.85  ? 101 TRP B CZ3   1 
ATOM   8362  C  CZ3   B TRP B 2 101 ? 27.756  -9.760  -10.718 0.80 34.98  ? 101 TRP B CZ3   1 
ATOM   8363  C  CH2   A TRP B 2 101 ? 26.590  -10.136 -9.962  0.20 34.05  ? 101 TRP B CH2   1 
ATOM   8364  C  CH2   B TRP B 2 101 ? 26.922  -9.666  -9.595  0.80 28.13  ? 101 TRP B CH2   1 
ATOM   8365  N  N     A ALA B 2 102 ? 29.590  -13.575 -14.143 0.20 36.22  ? 102 ALA B N     1 
ATOM   8366  N  N     B ALA B 2 102 ? 29.497  -13.283 -14.006 0.80 36.67  ? 102 ALA B N     1 
ATOM   8367  C  CA    A ALA B 2 102 ? 28.945  -12.711 -15.128 0.20 39.72  ? 102 ALA B CA    1 
ATOM   8368  C  CA    B ALA B 2 102 ? 28.823  -12.402 -14.955 0.80 39.89  ? 102 ALA B CA    1 
ATOM   8369  C  C     A ALA B 2 102 ? 28.075  -13.505 -16.093 0.20 40.75  ? 102 ALA B C     1 
ATOM   8370  C  C     B ALA B 2 102 ? 27.928  -13.177 -15.916 0.80 41.68  ? 102 ALA B C     1 
ATOM   8371  O  O     A ALA B 2 102 ? 27.038  -13.005 -16.543 0.20 42.79  ? 102 ALA B O     1 
ATOM   8372  O  O     B ALA B 2 102 ? 26.885  -12.662 -16.328 0.80 43.73  ? 102 ALA B O     1 
ATOM   8373  C  CB    A ALA B 2 102 ? 29.994  -11.909 -15.897 0.20 43.23  ? 102 ALA B CB    1 
ATOM   8374  C  CB    B ALA B 2 102 ? 29.843  -11.574 -15.732 0.80 44.67  ? 102 ALA B CB    1 
ATOM   8375  N  N     A LYS B 2 103 ? 28.478  -14.734 -16.424 0.20 39.75  ? 103 LYS B N     1 
ATOM   8376  N  N     B LYS B 2 103 ? 28.315  -14.403 -16.285 0.80 39.86  ? 103 LYS B N     1 
ATOM   8377  C  CA    A LYS B 2 103 ? 27.657  -15.573 -17.292 0.20 39.56  ? 103 LYS B CA    1 
ATOM   8378  C  CA    B LYS B 2 103 ? 27.428  -15.252 -17.079 0.80 37.58  ? 103 LYS B CA    1 
ATOM   8379  C  C     A LYS B 2 103 ? 26.350  -15.958 -16.611 0.20 42.33  ? 103 LYS B C     1 
ATOM   8380  C  C     B LYS B 2 103 ? 26.176  -15.621 -16.294 0.80 43.78  ? 103 LYS B C     1 
ATOM   8381  O  O     A LYS B 2 103 ? 25.302  -16.037 -17.262 0.20 42.80  ? 103 LYS B O     1 
ATOM   8382  O  O     B LYS B 2 103 ? 25.070  -15.670 -16.849 0.80 38.03  ? 103 LYS B O     1 
ATOM   8383  C  CB    A LYS B 2 103 ? 28.434  -16.823 -17.704 0.20 43.48  ? 103 LYS B CB    1 
ATOM   8384  C  CB    B LYS B 2 103 ? 28.163  -16.516 -17.526 0.80 43.98  ? 103 LYS B CB    1 
ATOM   8385  C  CG    A LYS B 2 103 ? 29.597  -16.554 -18.647 0.20 42.26  ? 103 LYS B CG    1 
ATOM   8386  C  CG    B LYS B 2 103 ? 29.131  -16.301 -18.690 0.80 42.68  ? 103 LYS B CG    1 
ATOM   8387  C  CD    A LYS B 2 103 ? 30.342  -17.838 -18.975 0.20 43.94  ? 103 LYS B CD    1 
ATOM   8388  C  CD    B LYS B 2 103 ? 29.645  -17.630 -19.218 0.80 43.92  ? 103 LYS B CD    1 
ATOM   8389  C  CE    A LYS B 2 103 ? 31.350  -17.627 -20.093 0.20 47.66  ? 103 LYS B CE    1 
ATOM   8390  C  CE    B LYS B 2 103 ? 30.259  -17.483 -20.607 0.80 49.78  ? 103 LYS B CE    1 
ATOM   8391  N  NZ    A LYS B 2 103 ? 30.680  -17.192 -21.349 0.20 48.95  ? 103 LYS B NZ    1 
ATOM   8392  N  NZ    B LYS B 2 103 ? 31.471  -16.622 -20.588 0.80 51.39  ? 103 LYS B NZ    1 
ATOM   8393  N  N     A GLY B 2 104 ? 26.391  -16.203 -15.299 0.20 39.01  ? 104 GLY B N     1 
ATOM   8394  N  N     B GLY B 2 104 ? 26.330  -15.905 -15.003 0.80 39.59  ? 104 GLY B N     1 
ATOM   8395  C  CA    A GLY B 2 104 ? 25.183  -16.562 -14.580 0.20 38.16  ? 104 GLY B CA    1 
ATOM   8396  C  CA    B GLY B 2 104 ? 25.163  -16.169 -14.180 0.80 36.47  ? 104 GLY B CA    1 
ATOM   8397  C  C     A GLY B 2 104 ? 24.272  -15.400 -14.257 0.20 38.43  ? 104 GLY B C     1 
ATOM   8398  C  C     B GLY B 2 104 ? 24.274  -14.952 -14.018 0.80 38.60  ? 104 GLY B C     1 
ATOM   8399  O  O     A GLY B 2 104 ? 23.069  -15.605 -14.074 0.20 38.82  ? 104 GLY B O     1 
ATOM   8400  O  O     B GLY B 2 104 ? 23.044  -15.063 -14.033 0.80 40.81  ? 104 GLY B O     1 
ATOM   8401  N  N     A HIS B 2 105 ? 24.810  -14.183 -14.198 0.20 35.62  ? 105 HIS B N     1 
ATOM   8402  N  N     B HIS B 2 105 ? 24.872  -13.775 -13.879 0.80 34.97  ? 105 HIS B N     1 
ATOM   8403  C  CA    A HIS B 2 105 ? 24.040  -13.030 -13.749 0.20 38.15  ? 105 HIS B CA    1 
ATOM   8404  C  CA    B HIS B 2 105 ? 24.099  -12.614 -13.458 0.80 37.93  ? 105 HIS B CA    1 
ATOM   8405  C  C     A HIS B 2 105 ? 23.510  -12.162 -14.881 0.20 40.73  ? 105 HIS B C     1 
ATOM   8406  C  C     B HIS B 2 105 ? 23.611  -11.758 -14.616 0.80 41.77  ? 105 HIS B C     1 
ATOM   8407  O  O     A HIS B 2 105 ? 22.453  -11.542 -14.721 0.20 40.43  ? 105 HIS B O     1 
ATOM   8408  O  O     B HIS B 2 105 ? 22.524  -11.169 -14.527 0.80 40.98  ? 105 HIS B O     1 
ATOM   8409  C  CB    A HIS B 2 105 ? 24.889  -12.160 -12.815 0.20 35.95  ? 105 HIS B CB    1 
ATOM   8410  C  CB    B HIS B 2 105 ? 24.930  -11.752 -12.506 0.80 33.70  ? 105 HIS B CB    1 
ATOM   8411  C  CG    A HIS B 2 105 ? 24.090  -11.193 -11.998 0.20 38.58  ? 105 HIS B CG    1 
ATOM   8412  C  CG    B HIS B 2 105 ? 24.111  -10.885 -11.599 0.80 41.42  ? 105 HIS B CG    1 
ATOM   8413  N  ND1   A HIS B 2 105 ? 23.431  -11.560 -10.844 0.20 36.37  ? 105 HIS B ND1   1 
ATOM   8414  N  ND1   B HIS B 2 105 ? 23.877  -9.551  -11.855 0.80 43.88  ? 105 HIS B ND1   1 
ATOM   8415  C  CD2   A HIS B 2 105 ? 23.842  -9.872  -12.169 0.20 40.96  ? 105 HIS B CD2   1 
ATOM   8416  C  CD2   B HIS B 2 105 ? 23.476  -11.160 -10.434 0.80 36.05  ? 105 HIS B CD2   1 
ATOM   8417  C  CE1   A HIS B 2 105 ? 22.814  -10.508 -10.338 0.20 37.04  ? 105 HIS B CE1   1 
ATOM   8418  C  CE1   B HIS B 2 105 ? 23.133  -9.044  -10.887 0.80 33.91  ? 105 HIS B CE1   1 
ATOM   8419  N  NE2   A HIS B 2 105 ? 23.047  -9.471  -11.123 0.20 35.69  ? 105 HIS B NE2   1 
ATOM   8420  N  NE2   B HIS B 2 105 ? 22.878  -9.999  -10.013 0.80 37.81  ? 105 HIS B NE2   1 
ATOM   8421  N  N     A TYR B 2 106 ? 24.203  -12.093 -16.018 0.20 41.27  ? 106 TYR B N     1 
ATOM   8422  N  N     B TYR B 2 106 ? 24.373  -11.677 -15.703 0.80 43.43  ? 106 TYR B N     1 
ATOM   8423  C  CA    A TYR B 2 106 ? 23.830  -11.158 -17.072 0.20 40.78  ? 106 TYR B CA    1 
ATOM   8424  C  CA    B TYR B 2 106 ? 24.102  -10.686 -16.734 0.80 43.26  ? 106 TYR B CA    1 
ATOM   8425  C  C     A TYR B 2 106 ? 23.524  -11.800 -18.416 0.20 41.66  ? 106 TYR B C     1 
ATOM   8426  C  C     B TYR B 2 106 ? 23.713  -11.256 -18.087 0.80 38.33  ? 106 TYR B C     1 
ATOM   8427  O  O     A TYR B 2 106 ? 22.760  -11.220 -19.190 0.20 45.72  ? 106 TYR B O     1 
ATOM   8428  O  O     B TYR B 2 106 ? 22.947  -10.607 -18.805 0.80 42.15  ? 106 TYR B O     1 
ATOM   8429  C  CB    A TYR B 2 106 ? 24.934  -10.109 -17.273 0.20 43.48  ? 106 TYR B CB    1 
ATOM   8430  C  CB    B TYR B 2 106 ? 25.322  -9.780  -16.920 0.80 46.17  ? 106 TYR B CB    1 
ATOM   8431  C  CG    A TYR B 2 106 ? 25.098  -9.160  -16.108 0.20 44.10  ? 106 TYR B CG    1 
ATOM   8432  C  CG    B TYR B 2 106 ? 25.462  -8.712  -15.865 0.80 44.78  ? 106 TYR B CG    1 
ATOM   8433  C  CD1   A TYR B 2 106 ? 24.156  -8.169  -15.857 0.20 42.32  ? 106 TYR B CD1   1 
ATOM   8434  C  CD1   B TYR B 2 106 ? 24.393  -7.881  -15.537 0.80 42.82  ? 106 TYR B CD1   1 
ATOM   8435  C  CD2   A TYR B 2 106 ? 26.198  -9.248  -15.265 0.20 42.30  ? 106 TYR B CD2   1 
ATOM   8436  C  CD2   B TYR B 2 106 ? 26.662  -8.536  -15.196 0.80 42.82  ? 106 TYR B CD2   1 
ATOM   8437  C  CE1   A TYR B 2 106 ? 24.303  -7.298  -14.795 0.20 44.52  ? 106 TYR B CE1   1 
ATOM   8438  C  CE1   B TYR B 2 106 ? 24.528  -6.895  -14.574 0.80 46.61  ? 106 TYR B CE1   1 
ATOM   8439  C  CE2   A TYR B 2 106 ? 26.353  -8.382  -14.201 0.20 42.32  ? 106 TYR B CE2   1 
ATOM   8440  C  CE2   B TYR B 2 106 ? 26.807  -7.562  -14.237 0.80 45.69  ? 106 TYR B CE2   1 
ATOM   8441  C  CZ    A TYR B 2 106 ? 25.405  -7.409  -13.971 0.20 43.75  ? 106 TYR B CZ    1 
ATOM   8442  C  CZ    B TYR B 2 106 ? 25.745  -6.746  -13.925 0.80 46.45  ? 106 TYR B CZ    1 
ATOM   8443  O  OH    A TYR B 2 106 ? 25.562  -6.547  -12.911 0.20 46.84  ? 106 TYR B OH    1 
ATOM   8444  O  OH    B TYR B 2 106 ? 25.923  -5.775  -12.967 0.80 50.14  ? 106 TYR B OH    1 
ATOM   8445  N  N     A THR B 2 107 ? 24.090  -12.967 -18.721 0.20 39.30  ? 107 THR B N     1 
ATOM   8446  N  N     B THR B 2 107 ? 24.206  -12.436 -18.461 0.80 38.66  ? 107 THR B N     1 
ATOM   8447  C  CA    A THR B 2 107 ? 23.910  -13.554 -20.044 0.20 41.62  ? 107 THR B CA    1 
ATOM   8448  C  CA    B THR B 2 107 ? 23.984  -12.949 -19.807 0.80 40.88  ? 107 THR B CA    1 
ATOM   8449  C  C     A THR B 2 107 ? 23.167  -14.883 -19.980 0.20 42.76  ? 107 THR B C     1 
ATOM   8450  C  C     B THR B 2 107 ? 23.172  -14.241 -19.794 0.80 41.01  ? 107 THR B C     1 
ATOM   8451  O  O     A THR B 2 107 ? 21.945  -14.927 -20.160 0.20 45.28  ? 107 THR B O     1 
ATOM   8452  O  O     B THR B 2 107 ? 21.938  -14.201 -19.817 0.80 47.37  ? 107 THR B O     1 
ATOM   8453  C  CB    A THR B 2 107 ? 25.263  -13.745 -20.734 0.20 42.74  ? 107 THR B CB    1 
ATOM   8454  C  CB    B THR B 2 107 ? 25.330  -13.158 -20.512 0.80 40.07  ? 107 THR B CB    1 
ATOM   8455  O  OG1   A THR B 2 107 ? 26.016  -14.751 -20.046 0.20 47.84  ? 107 THR B OG1   1 
ATOM   8456  O  OG1   B THR B 2 107 ? 26.135  -14.068 -19.758 0.80 49.23  ? 107 THR B OG1   1 
ATOM   8457  C  CG2   A THR B 2 107 ? 26.052  -12.441 -20.735 0.20 40.87  ? 107 THR B CG2   1 
ATOM   8458  C  CG2   B THR B 2 107 ? 26.083  -11.841 -20.632 0.80 37.10  ? 107 THR B CG2   1 
ATOM   8459  N  N     A GLU B 2 108 ? 23.900  -15.971 -19.727 0.20 43.56  ? 108 GLU B N     1 
ATOM   8460  N  N     B GLU B 2 108 ? 23.855  -15.388 -19.748 0.80 40.19  ? 108 GLU B N     1 
ATOM   8461  C  CA    A GLU B 2 108 ? 23.294  -17.300 -19.754 0.20 44.08  ? 108 GLU B CA    1 
ATOM   8462  C  CA    B GLU B 2 108 ? 23.176  -16.684 -19.793 0.80 41.48  ? 108 GLU B CA    1 
ATOM   8463  C  C     A GLU B 2 108 ? 22.205  -17.438 -18.697 0.20 46.51  ? 108 GLU B C     1 
ATOM   8464  C  C     B GLU B 2 108 ? 22.102  -16.793 -18.716 0.80 47.46  ? 108 GLU B C     1 
ATOM   8465  O  O     A GLU B 2 108 ? 21.177  -18.085 -18.932 0.20 46.82  ? 108 GLU B O     1 
ATOM   8466  O  O     B GLU B 2 108 ? 20.963  -17.189 -18.992 0.80 52.07  ? 108 GLU B O     1 
ATOM   8467  C  CB    A GLU B 2 108 ? 24.369  -18.370 -19.557 0.20 47.66  ? 108 GLU B CB    1 
ATOM   8468  C  CB    B GLU B 2 108 ? 24.199  -17.810 -19.627 0.80 44.92  ? 108 GLU B CB    1 
ATOM   8469  C  CG    A GLU B 2 108 ? 25.601  -18.189 -20.434 0.20 52.77  ? 108 GLU B CG    1 
ATOM   8470  C  CG    B GLU B 2 108 ? 25.384  -17.737 -20.579 0.80 55.27  ? 108 GLU B CG    1 
ATOM   8471  C  CD    A GLU B 2 108 ? 25.294  -18.308 -21.914 0.20 60.95  ? 108 GLU B CD    1 
ATOM   8472  C  CD    B GLU B 2 108 ? 25.129  -18.477 -21.873 0.80 62.10  ? 108 GLU B CD    1 
ATOM   8473  O  OE1   A GLU B 2 108 ? 24.309  -18.993 -22.269 0.20 59.86  ? 108 GLU B OE1   1 
ATOM   8474  O  OE1   B GLU B 2 108 ? 24.182  -19.297 -21.910 0.80 59.25  ? 108 GLU B OE1   1 
ATOM   8475  O  OE2   A GLU B 2 108 ? 26.038  -17.715 -22.724 0.20 61.65  ? 108 GLU B OE2   1 
ATOM   8476  O  OE2   B GLU B 2 108 ? 25.875  -18.241 -22.849 0.80 64.82  ? 108 GLU B OE2   1 
ATOM   8477  N  N     A GLY B 2 109 ? 22.412  -16.837 -17.522 0.20 45.29  ? 109 GLY B N     1 
ATOM   8478  N  N     B GLY B 2 109 ? 22.455  -16.454 -17.472 0.80 46.29  ? 109 GLY B N     1 
ATOM   8479  C  CA    A GLY B 2 109 ? 21.409  -16.898 -16.474 0.20 40.19  ? 109 GLY B CA    1 
ATOM   8480  C  CA    B GLY B 2 109 ? 21.502  -16.571 -16.379 0.80 36.83  ? 109 GLY B CA    1 
ATOM   8481  C  C     A GLY B 2 109 ? 20.196  -16.024 -16.709 0.20 46.49  ? 109 GLY B C     1 
ATOM   8482  C  C     B GLY B 2 109 ? 20.327  -15.625 -16.505 0.80 46.63  ? 109 GLY B C     1 
ATOM   8483  O  O     A GLY B 2 109 ? 19.129  -16.307 -16.156 0.20 49.55  ? 109 GLY B O     1 
ATOM   8484  O  O     B GLY B 2 109 ? 19.208  -15.966 -16.105 0.80 52.64  ? 109 GLY B O     1 
ATOM   8485  N  N     A ALA B 2 110 ? 20.331  -14.971 -17.520 0.20 44.82  ? 110 ALA B N     1 
ATOM   8486  N  N     B ALA B 2 110 ? 20.557  -14.428 -17.051 0.80 43.11  ? 110 ALA B N     1 
ATOM   8487  C  CA    A ALA B 2 110 ? 19.212  -14.064 -17.757 0.20 47.51  ? 110 ALA B CA    1 
ATOM   8488  C  CA    B ALA B 2 110 ? 19.467  -13.476 -17.225 0.80 45.08  ? 110 ALA B CA    1 
ATOM   8489  C  C     A ALA B 2 110 ? 18.178  -14.675 -18.694 0.20 49.91  ? 110 ALA B C     1 
ATOM   8490  C  C     B ALA B 2 110 ? 18.422  -13.994 -18.202 0.80 52.76  ? 110 ALA B C     1 
ATOM   8491  O  O     A ALA B 2 110 ? 16.973  -14.483 -18.499 0.20 50.96  ? 110 ALA B O     1 
ATOM   8492  O  O     B ALA B 2 110 ? 17.231  -13.698 -18.051 0.80 55.52  ? 110 ALA B O     1 
ATOM   8493  C  CB    A ALA B 2 110 ? 19.719  -12.736 -18.318 0.20 41.98  ? 110 ALA B CB    1 
ATOM   8494  C  CB    B ALA B 2 110 ? 20.006  -12.127 -17.699 0.80 37.58  ? 110 ALA B CB    1 
ATOM   8495  N  N     A GLU B 2 111 ? 18.624  -15.404 -19.719 0.20 51.20  ? 111 GLU B N     1 
ATOM   8496  N  N     B GLU B 2 111 ? 18.839  -14.777 -19.197 0.80 47.03  ? 111 GLU B N     1 
ATOM   8497  C  CA    A GLU B 2 111 ? 17.689  -16.049 -20.635 0.20 54.01  ? 111 GLU B CA    1 
ATOM   8498  C  CA    B GLU B 2 111 ? 17.891  -15.273 -20.188 0.80 52.23  ? 111 GLU B CA    1 
ATOM   8499  C  C     A GLU B 2 111 ? 16.859  -17.128 -19.951 0.20 52.30  ? 111 GLU B C     1 
ATOM   8500  C  C     B GLU B 2 111 ? 16.917  -16.277 -19.586 0.80 50.84  ? 111 GLU B C     1 
ATOM   8501  O  O     A GLU B 2 111 ? 15.805  -17.506 -20.474 0.20 51.51  ? 111 GLU B O     1 
ATOM   8502  O  O     B GLU B 2 111 ? 15.780  -16.398 -20.059 0.80 54.75  ? 111 GLU B O     1 
ATOM   8503  C  CB    A GLU B 2 111 ? 18.444  -16.648 -21.823 0.20 57.42  ? 111 GLU B CB    1 
ATOM   8504  C  CB    B GLU B 2 111 ? 18.648  -15.901 -21.360 0.80 57.19  ? 111 GLU B CB    1 
ATOM   8505  C  CG    A GLU B 2 111 ? 18.860  -15.630 -22.877 0.20 64.85  ? 111 GLU B CG    1 
ATOM   8506  C  CG    B GLU B 2 111 ? 17.827  -16.059 -22.628 0.80 71.90  ? 111 GLU B CG    1 
ATOM   8507  C  CD    A GLU B 2 111 ? 17.699  -15.188 -23.752 0.20 70.53  ? 111 GLU B CD    1 
ATOM   8508  C  CD    B GLU B 2 111 ? 18.509  -15.452 -23.841 0.80 74.21  ? 111 GLU B CD    1 
ATOM   8509  O  OE1   A GLU B 2 111 ? 16.801  -16.016 -24.018 0.20 66.17  ? 111 GLU B OE1   1 
ATOM   8510  O  OE1   B GLU B 2 111 ? 19.661  -14.983 -23.706 0.80 71.65  ? 111 GLU B OE1   1 
ATOM   8511  O  OE2   A GLU B 2 111 ? 17.684  -14.011 -24.173 0.20 65.26  ? 111 GLU B OE2   1 
ATOM   8512  O  OE2   B GLU B 2 111 ? 17.890  -15.437 -24.928 0.80 86.86  ? 111 GLU B OE2   1 
ATOM   8513  N  N     A LEU B 2 112 ? 17.304  -17.625 -18.799 0.20 48.44  ? 112 LEU B N     1 
ATOM   8514  N  N     B LEU B 2 112 ? 17.336  -16.995 -18.547 0.80 46.32  ? 112 LEU B N     1 
ATOM   8515  C  CA    A LEU B 2 112 ? 16.599  -18.666 -18.067 0.20 48.20  ? 112 LEU B CA    1 
ATOM   8516  C  CA    B LEU B 2 112 ? 16.533  -18.058 -17.957 0.80 47.24  ? 112 LEU B CA    1 
ATOM   8517  C  C     A LEU B 2 112 ? 15.883  -18.138 -16.831 0.20 50.66  ? 112 LEU B C     1 
ATOM   8518  C  C     B LEU B 2 112 ? 15.693  -17.585 -16.776 0.80 51.67  ? 112 LEU B C     1 
ATOM   8519  O  O     A LEU B 2 112 ? 15.166  -18.899 -16.173 0.20 48.14  ? 112 LEU B O     1 
ATOM   8520  O  O     B LEU B 2 112 ? 14.828  -18.336 -16.305 0.80 46.53  ? 112 LEU B O     1 
ATOM   8521  C  CB    A LEU B 2 112 ? 17.579  -19.777 -17.667 0.20 49.04  ? 112 LEU B CB    1 
ATOM   8522  C  CB    B LEU B 2 112 ? 17.457  -19.203 -17.515 0.80 49.29  ? 112 LEU B CB    1 
ATOM   8523  C  CG    A LEU B 2 112 ? 17.023  -21.167 -17.346 0.20 50.49  ? 112 LEU B CG    1 
ATOM   8524  C  CG    B LEU B 2 112 ? 16.906  -20.556 -17.057 0.80 48.74  ? 112 LEU B CG    1 
ATOM   8525  C  CD1   A LEU B 2 112 ? 16.462  -21.827 -18.598 0.20 50.98  ? 112 LEU B CD1   1 
ATOM   8526  C  CD1   B LEU B 2 112 ? 16.221  -21.290 -18.202 0.80 56.32  ? 112 LEU B CD1   1 
ATOM   8527  C  CD2   A LEU B 2 112 ? 18.093  -22.040 -16.706 0.20 49.81  ? 112 LEU B CD2   1 
ATOM   8528  C  CD2   B LEU B 2 112 ? 18.024  -21.407 -16.472 0.80 50.12  ? 112 LEU B CD2   1 
ATOM   8529  N  N     A VAL B 2 113 ? 16.047  -16.853 -16.503 0.20 49.43  ? 113 VAL B N     1 
ATOM   8530  N  N     B VAL B 2 113 ? 15.905  -16.354 -16.305 0.80 48.78  ? 113 VAL B N     1 
ATOM   8531  C  CA    A VAL B 2 113 ? 15.477  -16.336 -15.263 0.20 47.55  ? 113 VAL B CA    1 
ATOM   8532  C  CA    B VAL B 2 113 ? 15.364  -15.966 -15.009 0.80 47.38  ? 113 VAL B CA    1 
ATOM   8533  C  C     A VAL B 2 113 ? 13.963  -16.200 -15.375 0.20 50.85  ? 113 VAL B C     1 
ATOM   8534  C  C     B VAL B 2 113 ? 13.849  -15.805 -15.070 0.80 53.33  ? 113 VAL B C     1 
ATOM   8535  O  O     A VAL B 2 113 ? 13.252  -16.289 -14.366 0.20 46.28  ? 113 VAL B O     1 
ATOM   8536  O  O     B VAL B 2 113 ? 13.162  -15.987 -14.056 0.80 43.27  ? 113 VAL B O     1 
ATOM   8537  C  CB    A VAL B 2 113 ? 16.144  -14.999 -14.881 0.20 45.26  ? 113 VAL B CB    1 
ATOM   8538  C  CB    B VAL B 2 113 ? 16.064  -14.692 -14.499 0.80 42.12  ? 113 VAL B CB    1 
ATOM   8539  C  CG1   A VAL B 2 113 ? 15.599  -13.850 -15.720 0.20 47.74  ? 113 VAL B CG1   1 
ATOM   8540  C  CG1   B VAL B 2 113 ? 15.569  -13.452 -15.242 0.80 45.04  ? 113 VAL B CG1   1 
ATOM   8541  C  CG2   A VAL B 2 113 ? 15.960  -14.717 -13.401 0.20 43.59  ? 113 VAL B CG2   1 
ATOM   8542  C  CG2   B VAL B 2 113 ? 15.868  -14.554 -13.005 0.80 44.25  ? 113 VAL B CG2   1 
ATOM   8543  N  N     A ASP B 2 114 ? 13.440  -16.004 -16.588 0.20 50.17  ? 114 ASP B N     1 
ATOM   8544  N  N     B ASP B 2 114 ? 13.296  -15.494 -16.247 0.80 50.51  ? 114 ASP B N     1 
ATOM   8545  C  CA    A ASP B 2 114 ? 11.997  -15.859 -16.751 0.20 50.05  ? 114 ASP B CA    1 
ATOM   8546  C  CA    B ASP B 2 114 ? 11.843  -15.405 -16.365 0.80 50.44  ? 114 ASP B CA    1 
ATOM   8547  C  C     A ASP B 2 114 ? 11.288  -17.200 -16.613 0.20 50.22  ? 114 ASP B C     1 
ATOM   8548  C  C     B ASP B 2 114 ? 11.191  -16.776 -16.222 0.80 51.46  ? 114 ASP B C     1 
ATOM   8549  O  O     A ASP B 2 114 ? 10.175  -17.268 -16.077 0.20 51.98  ? 114 ASP B O     1 
ATOM   8550  O  O     B ASP B 2 114 ? 10.118  -16.898 -15.619 0.80 54.00  ? 114 ASP B O     1 
ATOM   8551  C  CB    A ASP B 2 114 ? 11.683  -15.215 -18.101 0.20 54.18  ? 114 ASP B CB    1 
ATOM   8552  C  CB    B ASP B 2 114 ? 11.457  -14.759 -17.695 0.80 55.65  ? 114 ASP B CB    1 
ATOM   8553  C  CG    A ASP B 2 114 ? 12.068  -13.749 -18.149 0.20 53.01  ? 114 ASP B CG    1 
ATOM   8554  C  CG    B ASP B 2 114 ? 11.810  -13.287 -17.751 0.80 52.06  ? 114 ASP B CG    1 
ATOM   8555  O  OD1   A ASP B 2 114 ? 11.818  -13.037 -17.154 0.20 53.20  ? 114 ASP B OD1   1 
ATOM   8556  O  OD1   B ASP B 2 114 ? 12.252  -12.743 -16.719 0.80 55.26  ? 114 ASP B OD1   1 
ATOM   8557  O  OD2   A ASP B 2 114 ? 12.623  -13.310 -19.178 0.20 56.87  ? 114 ASP B OD2   1 
ATOM   8558  O  OD2   B ASP B 2 114 ? 11.647  -12.673 -18.827 0.80 61.81  ? 114 ASP B OD2   1 
ATOM   8559  N  N     A SER B 2 115 ? 11.915  -18.278 -17.087 0.20 47.14  ? 115 SER B N     1 
ATOM   8560  N  N     B SER B 2 115 ? 11.828  -17.823 -16.752 0.80 44.11  ? 115 SER B N     1 
ATOM   8561  C  CA    A SER B 2 115 ? 11.311  -19.599 -16.951 0.20 50.62  ? 115 SER B CA    1 
ATOM   8562  C  CA    B SER B 2 115 ? 11.237  -19.155 -16.668 0.80 50.53  ? 115 SER B CA    1 
ATOM   8563  C  C     A SER B 2 115 ? 11.244  -20.026 -15.490 0.20 50.02  ? 115 SER B C     1 
ATOM   8564  C  C     B SER B 2 115 ? 11.204  -19.659 -15.229 0.80 50.94  ? 115 SER B C     1 
ATOM   8565  O  O     A SER B 2 115 ? 10.271  -20.662 -15.068 0.20 48.00  ? 115 SER B O     1 
ATOM   8566  O  O     B SER B 2 115 ? 10.248  -20.329 -14.823 0.80 47.31  ? 115 SER B O     1 
ATOM   8567  C  CB    A SER B 2 115 ? 12.091  -20.622 -17.777 0.20 51.42  ? 115 SER B CB    1 
ATOM   8568  C  CB    B SER B 2 115 ? 11.996  -20.126 -17.570 0.80 52.12  ? 115 SER B CB    1 
ATOM   8569  O  OG    A SER B 2 115 ? 12.079  -20.281 -19.153 0.20 53.83  ? 115 SER B OG    1 
ATOM   8570  O  OG    B SER B 2 115 ? 11.786  -19.810 -18.939 0.80 55.68  ? 115 SER B OG    1 
ATOM   8571  N  N     A VAL B 2 116 ? 12.265  -19.683 -14.704 0.20 49.22  ? 116 VAL B N     1 
ATOM   8572  N  N     B VAL B 2 116 ? 12.237  -19.349 -14.443 0.80 51.59  ? 116 VAL B N     1 
ATOM   8573  C  CA    A VAL B 2 116 ? 12.253  -20.023 -13.284 0.20 45.11  ? 116 VAL B CA    1 
ATOM   8574  C  CA    B VAL B 2 116 ? 12.218  -19.710 -13.027 0.80 42.27  ? 116 VAL B CA    1 
ATOM   8575  C  C     A VAL B 2 116 ? 11.176  -19.231 -12.554 0.20 46.60  ? 116 VAL B C     1 
ATOM   8576  C  C     B VAL B 2 116 ? 11.111  -18.956 -12.305 0.80 47.38  ? 116 VAL B C     1 
ATOM   8577  O  O     A VAL B 2 116 ? 10.461  -19.774 -11.703 0.20 43.11  ? 116 VAL B O     1 
ATOM   8578  O  O     B VAL B 2 116 ? 10.416  -19.516 -11.452 0.80 41.41  ? 116 VAL B O     1 
ATOM   8579  C  CB    A VAL B 2 116 ? 13.644  -19.791 -12.666 0.20 46.08  ? 116 VAL B CB    1 
ATOM   8580  C  CB    B VAL B 2 116 ? 13.596  -19.448 -12.386 0.80 45.61  ? 116 VAL B CB    1 
ATOM   8581  C  CG1   A VAL B 2 116 ? 13.631  -20.139 -11.186 0.20 44.10  ? 116 VAL B CG1   1 
ATOM   8582  C  CG1   B VAL B 2 116 ? 13.590  -19.853 -10.913 0.80 43.80  ? 116 VAL B CG1   1 
ATOM   8583  C  CG2   A VAL B 2 116 ? 14.698  -20.607 -13.404 0.20 42.98  ? 116 VAL B CG2   1 
ATOM   8584  C  CG2   B VAL B 2 116 ? 14.698  -20.185 -13.162 0.80 43.22  ? 116 VAL B CG2   1 
ATOM   8585  N  N     A LEU B 2 117 ? 11.040  -17.940 -12.876 0.20 46.79  ? 117 LEU B N     1 
ATOM   8586  N  N     B LEU B 2 117 ? 10.926  -17.676 -12.636 0.80 45.50  ? 117 LEU B N     1 
ATOM   8587  C  CA    A LEU B 2 117 ? 10.039  -17.108 -12.213 0.20 47.24  ? 117 LEU B CA    1 
ATOM   8588  C  CA    B LEU B 2 117 ? 9.906   -16.880 -11.962 0.80 46.77  ? 117 LEU B CA    1 
ATOM   8589  C  C     A LEU B 2 117 ? 8.632   -17.653 -12.425 0.20 50.93  ? 117 LEU B C     1 
ATOM   8590  C  C     B LEU B 2 117 ? 8.506   -17.424 -12.207 0.80 52.55  ? 117 LEU B C     1 
ATOM   8591  O  O     A LEU B 2 117 ? 7.819   -17.666 -11.494 0.20 50.38  ? 117 LEU B O     1 
ATOM   8592  O  O     B LEU B 2 117 ? 7.639   -17.307 -11.334 0.80 51.75  ? 117 LEU B O     1 
ATOM   8593  C  CB    A LEU B 2 117 ? 10.129  -15.667 -12.715 0.20 48.13  ? 117 LEU B CB    1 
ATOM   8594  C  CB    B LEU B 2 117 ? 9.992   -15.423 -12.412 0.80 47.30  ? 117 LEU B CB    1 
ATOM   8595  C  CG    A LEU B 2 117 ? 11.345  -14.831 -12.309 0.20 47.84  ? 117 LEU B CG    1 
ATOM   8596  C  CG    B LEU B 2 117 ? 10.873  -14.506 -11.568 0.80 53.03  ? 117 LEU B CG    1 
ATOM   8597  C  CD1   A LEU B 2 117 ? 11.243  -13.431 -12.894 0.20 48.89  ? 117 LEU B CD1   1 
ATOM   8598  C  CD1   B LEU B 2 117 ? 10.785  -13.081 -12.074 0.80 49.56  ? 117 LEU B CD1   1 
ATOM   8599  C  CD2   A LEU B 2 117 ? 11.488  -14.772 -10.799 0.20 49.81  ? 117 LEU B CD2   1 
ATOM   8600  C  CD2   B LEU B 2 117 ? 10.457  -14.591 -10.101 0.80 51.28  ? 117 LEU B CD2   1 
ATOM   8601  N  N     A ASP B 2 118 ? 8.326   -18.105 -13.644 0.20 50.22  ? 118 ASP B N     1 
ATOM   8602  N  N     B ASP B 2 118 ? 8.262   -18.016 -13.380 0.80 50.73  ? 118 ASP B N     1 
ATOM   8603  C  CA    A ASP B 2 118 ? 7.010   -18.679 -13.909 0.20 48.83  ? 118 ASP B CA    1 
ATOM   8604  C  CA    B ASP B 2 118 ? 6.938   -18.563 -13.662 0.80 48.01  ? 118 ASP B CA    1 
ATOM   8605  C  C     A ASP B 2 118 ? 6.752   -19.893 -13.026 0.20 47.62  ? 118 ASP B C     1 
ATOM   8606  C  C     B ASP B 2 118 ? 6.588   -19.687 -12.698 0.80 47.55  ? 118 ASP B C     1 
ATOM   8607  O  O     A ASP B 2 118 ? 5.619   -20.121 -12.585 0.20 47.39  ? 118 ASP B O     1 
ATOM   8608  O  O     B ASP B 2 118 ? 5.455   -19.765 -12.212 0.80 46.81  ? 118 ASP B O     1 
ATOM   8609  C  CB    A ASP B 2 118 ? 6.886   -19.054 -15.387 0.20 49.88  ? 118 ASP B CB    1 
ATOM   8610  C  CB    B ASP B 2 118 ? 6.862   -19.052 -15.109 0.80 49.44  ? 118 ASP B CB    1 
ATOM   8611  C  CG    A ASP B 2 118 ? 6.975   -17.848 -16.303 0.20 53.72  ? 118 ASP B CG    1 
ATOM   8612  C  CG    B ASP B 2 118 ? 6.772   -17.912 -16.105 0.80 53.30  ? 118 ASP B CG    1 
ATOM   8613  O  OD1   A ASP B 2 118 ? 6.587   -16.742 -15.873 0.20 54.45  ? 118 ASP B OD1   1 
ATOM   8614  O  OD1   B ASP B 2 118 ? 6.100   -16.904 -15.801 0.80 55.69  ? 118 ASP B OD1   1 
ATOM   8615  O  OD2   A ASP B 2 118 ? 7.433   -18.007 -17.455 0.20 61.71  ? 118 ASP B OD2   1 
ATOM   8616  O  OD2   B ASP B 2 118 ? 7.374   -18.020 -17.192 0.80 63.51  ? 118 ASP B OD2   1 
ATOM   8617  N  N     A VAL B 2 119 ? 7.793   -20.681 -12.752 0.20 45.04  ? 119 VAL B N     1 
ATOM   8618  N  N     B VAL B 2 119 ? 7.545   -20.567 -12.403 0.80 41.45  ? 119 VAL B N     1 
ATOM   8619  C  CA    A VAL B 2 119 ? 7.645   -21.814 -11.846 0.20 44.67  ? 119 VAL B CA    1 
ATOM   8620  C  CA    B VAL B 2 119 ? 7.249   -21.654 -11.482 0.80 43.42  ? 119 VAL B CA    1 
ATOM   8621  C  C     A VAL B 2 119 ? 7.416   -21.326 -10.421 0.20 46.33  ? 119 VAL B C     1 
ATOM   8622  C  C     B VAL B 2 119 ? 7.198   -21.146 -10.045 0.80 45.73  ? 119 VAL B C     1 
ATOM   8623  O  O     A VAL B 2 119 ? 6.626   -21.911 -9.669  0.20 46.62  ? 119 VAL B O     1 
ATOM   8624  O  O     B VAL B 2 119 ? 6.430   -21.670 -9.231  0.80 45.90  ? 119 VAL B O     1 
ATOM   8625  C  CB    A VAL B 2 119 ? 8.872   -22.738 -11.944 0.20 44.78  ? 119 VAL B CB    1 
ATOM   8626  C  CB    B VAL B 2 119 ? 8.254   -22.810 -11.648 0.80 44.08  ? 119 VAL B CB    1 
ATOM   8627  C  CG1   A VAL B 2 119 ? 8.722   -23.926 -11.011 0.20 44.96  ? 119 VAL B CG1   1 
ATOM   8628  C  CG1   B VAL B 2 119 ? 9.621   -22.433 -11.143 0.80 50.18  ? 119 VAL B CG1   1 
ATOM   8629  C  CG2   A VAL B 2 119 ? 9.067   -23.204 -13.377 0.20 45.28  ? 119 VAL B CG2   1 
ATOM   8630  C  CG2   B VAL B 2 119 ? 7.762   -24.035 -10.920 0.80 48.26  ? 119 VAL B CG2   1 
ATOM   8631  N  N     A VAL B 2 120 ? 8.096   -20.246 -10.027 0.20 49.29  ? 120 VAL B N     1 
ATOM   8632  N  N     B VAL B 2 120 ? 7.985   -20.120 -9.707  0.80 52.21  ? 120 VAL B N     1 
ATOM   8633  C  CA    A VAL B 2 120 ? 7.880   -19.679 -8.698  0.20 46.27  ? 120 VAL B CA    1 
ATOM   8634  C  CA    B VAL B 2 120 ? 7.891   -19.541 -8.369  0.80 44.41  ? 120 VAL B CA    1 
ATOM   8635  C  C     A VAL B 2 120 ? 6.451   -19.169 -8.566  0.20 47.32  ? 120 VAL B C     1 
ATOM   8636  C  C     B VAL B 2 120 ? 6.499   -18.968 -8.141  0.80 47.46  ? 120 VAL B C     1 
ATOM   8637  O  O     A VAL B 2 120 ? 5.824   -19.304 -7.507  0.20 45.76  ? 120 VAL B O     1 
ATOM   8638  O  O     B VAL B 2 120 ? 5.906   -19.156 -7.073  0.80 41.49  ? 120 VAL B O     1 
ATOM   8639  C  CB    A VAL B 2 120 ? 8.907   -18.566 -8.414  0.20 46.01  ? 120 VAL B CB    1 
ATOM   8640  C  CB    B VAL B 2 120 ? 8.978   -18.471 -8.151  0.80 46.01  ? 120 VAL B CB    1 
ATOM   8641  C  CG1   A VAL B 2 120 ? 8.686   -17.981 -7.027  0.20 47.41  ? 120 VAL B CG1   1 
ATOM   8642  C  CG1   B VAL B 2 120 ? 8.781   -17.804 -6.793  0.80 48.15  ? 120 VAL B CG1   1 
ATOM   8643  C  CG2   A VAL B 2 120 ? 10.325  -19.099 -8.548  0.20 48.34  ? 120 VAL B CG2   1 
ATOM   8644  C  CG2   B VAL B 2 120 ? 10.369  -19.076 -8.243  0.80 49.38  ? 120 VAL B CG2   1 
ATOM   8645  N  N     A ARG B 2 121 ? 5.911   -18.583 -9.638  0.20 48.22  ? 121 ARG B N     1 
ATOM   8646  N  N     B ARG B 2 121 ? 5.954   -18.265 -9.142  0.80 49.47  ? 121 ARG B N     1 
ATOM   8647  C  CA    A ARG B 2 121 ? 4.531   -18.105 -9.605  0.20 50.00  ? 121 ARG B CA    1 
ATOM   8648  C  CA    B ARG B 2 121 ? 4.602   -17.717 -9.025  0.80 50.44  ? 121 ARG B CA    1 
ATOM   8649  C  C     A ARG B 2 121 ? 3.552   -19.260 -9.436  0.20 48.46  ? 121 ARG B C     1 
ATOM   8650  C  C     B ARG B 2 121 ? 3.571   -18.820 -8.833  0.80 49.65  ? 121 ARG B C     1 
ATOM   8651  O  O     A ARG B 2 121 ? 2.556   -19.138 -8.714  0.20 53.96  ? 121 ARG B O     1 
ATOM   8652  O  O     B ARG B 2 121 ? 2.675   -18.705 -7.986  0.80 55.33  ? 121 ARG B O     1 
ATOM   8653  C  CB    A ARG B 2 121 ? 4.216   -17.317 -10.878 0.20 49.20  ? 121 ARG B CB    1 
ATOM   8654  C  CB    B ARG B 2 121 ? 4.252   -16.887 -10.261 0.80 50.51  ? 121 ARG B CB    1 
ATOM   8655  C  CG    A ARG B 2 121 ? 5.072   -16.074 -11.081 0.20 51.72  ? 121 ARG B CG    1 
ATOM   8656  C  CG    B ARG B 2 121 ? 5.013   -15.577 -10.387 0.80 53.75  ? 121 ARG B CG    1 
ATOM   8657  C  CD    A ARG B 2 121 ? 4.824   -15.448 -12.448 0.20 54.24  ? 121 ARG B CD    1 
ATOM   8658  C  CD    B ARG B 2 121 ? 4.424   -14.710 -11.495 0.80 51.73  ? 121 ARG B CD    1 
ATOM   8659  N  NE    A ARG B 2 121 ? 5.729   -14.337 -12.721 0.20 54.47  ? 121 ARG B NE    1 
ATOM   8660  N  NE    B ARG B 2 121 ? 5.053   -13.396 -11.579 0.80 54.06  ? 121 ARG B NE    1 
ATOM   8661  C  CZ    A ARG B 2 121 ? 5.746   -13.642 -13.850 0.20 56.18  ? 121 ARG B CZ    1 
ATOM   8662  C  CZ    B ARG B 2 121 ? 6.096   -13.110 -12.348 0.80 60.24  ? 121 ARG B CZ    1 
ATOM   8663  N  NH1   A ARG B 2 121 ? 4.915   -13.915 -14.843 0.20 53.27  ? 121 ARG B NH1   1 
ATOM   8664  N  NH1   B ARG B 2 121 ? 6.667   -14.029 -13.111 0.80 54.16  ? 121 ARG B NH1   1 
ATOM   8665  N  NH2   A ARG B 2 121 ? 6.620   -12.648 -13.988 0.20 54.71  ? 121 ARG B NH2   1 
ATOM   8666  N  NH2   B ARG B 2 121 ? 6.581   -11.872 -12.351 0.80 64.27  ? 121 ARG B NH2   1 
ATOM   8667  N  N     A LYS B 2 122 ? 3.822   -20.392 -10.090 0.20 48.20  ? 122 LYS B N     1 
ATOM   8668  N  N     B LYS B 2 122 ? 3.676   -19.895 -9.614  0.80 45.97  ? 122 LYS B N     1 
ATOM   8669  C  CA    A LYS B 2 122 ? 2.929   -21.542 -9.977  0.20 49.07  ? 122 LYS B CA    1 
ATOM   8670  C  CA    B LYS B 2 122 ? 2.733   -21.000 -9.472  0.80 47.46  ? 122 LYS B CA    1 
ATOM   8671  C  C     A LYS B 2 122 ? 2.888   -22.072 -8.549  0.20 49.83  ? 122 LYS B C     1 
ATOM   8672  C  C     B LYS B 2 122 ? 2.808   -21.612 -8.080  0.80 49.60  ? 122 LYS B C     1 
ATOM   8673  O  O     A LYS B 2 122 ? 1.827   -22.480 -8.060  0.20 52.30  ? 122 LYS B O     1 
ATOM   8674  O  O     B LYS B 2 122 ? 1.776   -21.899 -7.463  0.80 52.83  ? 122 LYS B O     1 
ATOM   8675  C  CB    A LYS B 2 122 ? 3.367   -22.644 -10.942 0.20 50.64  ? 122 LYS B CB    1 
ATOM   8676  C  CB    B LYS B 2 122 ? 3.005   -22.057 -10.541 0.80 48.64  ? 122 LYS B CB    1 
ATOM   8677  C  CG    A LYS B 2 122 ? 2.505   -23.896 -10.886 0.20 51.10  ? 122 LYS B CG    1 
ATOM   8678  C  CG    B LYS B 2 122 ? 1.981   -23.172 -10.591 0.80 51.02  ? 122 LYS B CG    1 
ATOM   8679  C  CD    A LYS B 2 122 ? 3.147   -25.046 -11.644 0.20 54.80  ? 122 LYS B CD    1 
ATOM   8680  C  CD    B LYS B 2 122 ? 0.615   -22.651 -11.015 0.80 66.98  ? 122 LYS B CD    1 
ATOM   8681  C  CE    A LYS B 2 122 ? 4.474   -25.444 -11.017 0.20 49.72  ? 122 LYS B CE    1 
ATOM   8682  C  CE    B LYS B 2 122 ? 0.647   -22.081 -12.430 0.80 69.69  ? 122 LYS B CE    1 
ATOM   8683  N  NZ    A LYS B 2 122 ? 5.108   -26.584 -11.731 0.20 51.41  ? 122 LYS B NZ    1 
ATOM   8684  N  NZ    B LYS B 2 122 ? -0.662  -21.483 -12.817 0.80 66.89  ? 122 LYS B NZ    1 
ATOM   8685  N  N     A GLU B 2 123 ? 4.031   -22.075 -7.862  0.20 49.46  ? 123 GLU B N     1 
ATOM   8686  N  N     B GLU B 2 123 ? 4.019   -21.815 -7.560  0.80 49.84  ? 123 GLU B N     1 
ATOM   8687  C  CA    A GLU B 2 123 ? 4.062   -22.576 -6.493  0.20 47.99  ? 123 GLU B CA    1 
ATOM   8688  C  CA    B GLU B 2 123 ? 4.143   -22.395 -6.227  0.80 46.49  ? 123 GLU B CA    1 
ATOM   8689  C  C     A GLU B 2 123 ? 3.533   -21.543 -5.506  0.20 50.79  ? 123 GLU B C     1 
ATOM   8690  C  C     B GLU B 2 123 ? 3.687   -21.422 -5.147  0.80 52.20  ? 123 GLU B C     1 
ATOM   8691  O  O     A GLU B 2 123 ? 2.851   -21.900 -4.540  0.20 51.52  ? 123 GLU B O     1 
ATOM   8692  O  O     B GLU B 2 123 ? 3.217   -21.852 -4.086  0.80 52.79  ? 123 GLU B O     1 
ATOM   8693  C  CB    A GLU B 2 123 ? 5.484   -22.996 -6.117  0.20 47.16  ? 123 GLU B CB    1 
ATOM   8694  C  CB    B GLU B 2 123 ? 5.585   -22.834 -5.979  0.80 46.92  ? 123 GLU B CB    1 
ATOM   8695  C  CG    A GLU B 2 123 ? 6.006   -24.204 -6.882  0.20 47.85  ? 123 GLU B CG    1 
ATOM   8696  C  CG    B GLU B 2 123 ? 5.955   -24.142 -6.654  0.80 47.37  ? 123 GLU B CG    1 
ATOM   8697  C  CD    A GLU B 2 123 ? 5.378   -25.512 -6.429  0.20 49.21  ? 123 GLU B CD    1 
ATOM   8698  C  CD    B GLU B 2 123 ? 5.494   -25.358 -5.875  0.80 48.25  ? 123 GLU B CD    1 
ATOM   8699  O  OE1   A GLU B 2 123 ? 4.687   -25.520 -5.389  0.20 52.48  ? 123 GLU B OE1   1 
ATOM   8700  O  OE1   B GLU B 2 123 ? 5.109   -25.198 -4.699  0.80 56.25  ? 123 GLU B OE1   1 
ATOM   8701  O  OE2   A GLU B 2 123 ? 5.579   -26.537 -7.115  0.20 51.69  ? 123 GLU B OE2   1 
ATOM   8702  O  OE2   B GLU B 2 123 ? 5.515   -26.476 -6.432  0.80 51.22  ? 123 GLU B OE2   1 
ATOM   8703  N  N     A SER B 2 124 ? 3.831   -20.260 -5.735  0.20 50.70  ? 124 SER B N     1 
ATOM   8704  N  N     B SER B 2 124 ? 3.807   -20.116 -5.400  0.80 51.18  ? 124 SER B N     1 
ATOM   8705  C  CA    A SER B 2 124 ? 3.388   -19.220 -4.810  0.20 48.94  ? 124 SER B CA    1 
ATOM   8706  C  CA    B SER B 2 124 ? 3.402   -19.121 -4.415  0.80 47.76  ? 124 SER B CA    1 
ATOM   8707  C  C     A SER B 2 124 ? 1.874   -19.044 -4.850  0.20 53.00  ? 124 SER B C     1 
ATOM   8708  C  C     B SER B 2 124 ? 1.885   -18.980 -4.335  0.80 53.43  ? 124 SER B C     1 
ATOM   8709  O  O     A SER B 2 124 ? 1.245   -18.807 -3.812  0.20 51.04  ? 124 SER B O     1 
ATOM   8710  O  O     B SER B 2 124 ? 1.331   -18.891 -3.236  0.80 51.81  ? 124 SER B O     1 
ATOM   8711  C  CB    A SER B 2 124 ? 4.089   -17.899 -5.127  0.20 47.17  ? 124 SER B CB    1 
ATOM   8712  C  CB    B SER B 2 124 ? 4.042   -17.771 -4.739  0.80 45.54  ? 124 SER B CB    1 
ATOM   8713  O  OG    A SER B 2 124 ? 5.484   -17.987 -4.888  0.20 47.74  ? 124 SER B OG    1 
ATOM   8714  O  OG    B SER B 2 124 ? 5.401   -17.735 -4.333  0.80 45.82  ? 124 SER B OG    1 
ATOM   8715  N  N     A GLU B 2 125 ? 1.271   -19.150 -6.038  0.20 53.97  ? 125 GLU B N     1 
ATOM   8716  N  N     B GLU B 2 125 ? 1.197   -18.955 -5.482  0.80 54.91  ? 125 GLU B N     1 
ATOM   8717  C  CA    A GLU B 2 125 ? -0.180  -19.029 -6.142  0.20 54.23  ? 125 GLU B CA    1 
ATOM   8718  C  CA    B GLU B 2 125 ? -0.248  -18.744 -5.476  0.80 53.57  ? 125 GLU B CA    1 
ATOM   8719  C  C     A GLU B 2 125 ? -0.893  -20.160 -5.414  0.20 53.44  ? 125 GLU B C     1 
ATOM   8720  C  C     B GLU B 2 125 ? -1.003  -19.886 -4.808  0.80 51.72  ? 125 GLU B C     1 
ATOM   8721  O  O     A GLU B 2 125 ? -1.983  -19.954 -4.869  0.20 57.15  ? 125 GLU B O     1 
ATOM   8722  O  O     B GLU B 2 125 ? -2.138  -19.683 -4.362  0.80 60.05  ? 125 GLU B O     1 
ATOM   8723  C  CB    A GLU B 2 125 ? -0.606  -18.995 -7.610  0.20 56.83  ? 125 GLU B CB    1 
ATOM   8724  C  CB    B GLU B 2 125 ? -0.756  -18.542 -6.903  0.80 55.31  ? 125 GLU B CB    1 
ATOM   8725  C  CG    A GLU B 2 125 ? -0.259  -17.703 -8.334  0.20 63.45  ? 125 GLU B CG    1 
ATOM   8726  C  CG    B GLU B 2 125 ? -0.425  -17.173 -7.482  0.80 62.96  ? 125 GLU B CG    1 
ATOM   8727  C  CD    A GLU B 2 125 ? -0.658  -17.729 -9.799  0.20 66.45  ? 125 GLU B CD    1 
ATOM   8728  C  CD    B GLU B 2 125 ? -0.891  -17.011 -8.921  0.80 72.69  ? 125 GLU B CD    1 
ATOM   8729  O  OE1   A GLU B 2 125 ? -1.261  -18.734 -10.237 0.20 63.55  ? 125 GLU B OE1   1 
ATOM   8730  O  OE1   B GLU B 2 125 ? -1.560  -17.930 -9.444  0.80 75.71  ? 125 GLU B OE1   1 
ATOM   8731  O  OE2   A GLU B 2 125 ? -0.368  -16.746 -10.512 0.20 61.30  ? 125 GLU B OE2   1 
ATOM   8732  O  OE2   B GLU B 2 125 ? -0.583  -15.963 -9.530  0.80 71.04  ? 125 GLU B OE2   1 
ATOM   8733  N  N     A SER B 2 126 ? -0.296  -21.352 -5.387  0.20 54.95  ? 126 SER B N     1 
ATOM   8734  N  N     B SER B 2 126 ? -0.398  -21.070 -4.716  0.80 53.44  ? 126 SER B N     1 
ATOM   8735  C  CA    A SER B 2 126 ? -0.856  -22.504 -4.693  0.20 55.67  ? 126 SER B CA    1 
ATOM   8736  C  CA    B SER B 2 126 ? -0.998  -22.226 -4.065  0.80 56.82  ? 126 SER B CA    1 
ATOM   8737  C  C     A SER B 2 126 ? -0.569  -22.489 -3.193  0.20 55.50  ? 126 SER B C     1 
ATOM   8738  C  C     B SER B 2 126 ? -0.634  -22.326 -2.585  0.80 58.21  ? 126 SER B C     1 
ATOM   8739  O  O     A SER B 2 126 ? -0.605  -23.549 -2.555  0.20 55.16  ? 126 SER B O     1 
ATOM   8740  O  O     B SER B 2 126 ? -0.789  -23.398 -1.986  0.80 57.44  ? 126 SER B O     1 
ATOM   8741  C  CB    A SER B 2 126 ? -0.326  -23.798 -5.318  0.20 56.69  ? 126 SER B CB    1 
ATOM   8742  C  CB    B SER B 2 126 ? -0.588  -23.509 -4.792  0.80 58.94  ? 126 SER B CB    1 
ATOM   8743  O  OG    A SER B 2 126 ? -0.921  -24.939 -4.725  0.20 60.64  ? 126 SER B OG    1 
ATOM   8744  O  OG    B SER B 2 126 ? -1.218  -23.602 -6.054  0.80 57.27  ? 126 SER B OG    1 
ATOM   8745  N  N     A CYS B 2 127 ? -0.285  -21.319 -2.626  0.20 53.48  ? 127 CYS B N     1 
ATOM   8746  N  N     B CYS B 2 127 ? -0.148  -21.241 -1.991  0.80 50.90  ? 127 CYS B N     1 
ATOM   8747  C  CA    A CYS B 2 127 ? -0.010  -21.163 -1.205  0.20 48.35  ? 127 CYS B CA    1 
ATOM   8748  C  CA    B CYS B 2 127 ? 0.146   -21.188 -0.568  0.80 46.63  ? 127 CYS B CA    1 
ATOM   8749  C  C     A CYS B 2 127 ? -1.130  -20.368 -0.548  0.20 45.68  ? 127 CYS B C     1 
ATOM   8750  C  C     B CYS B 2 127 ? -0.936  -20.380 0.135   0.80 46.70  ? 127 CYS B C     1 
ATOM   8751  O  O     A CYS B 2 127 ? -1.595  -19.365 -1.097  0.20 48.40  ? 127 CYS B O     1 
ATOM   8752  O  O     B CYS B 2 127 ? -1.346  -19.322 -0.352  0.80 41.09  ? 127 CYS B O     1 
ATOM   8753  C  CB    A CYS B 2 127 ? 1.329   -20.455 -0.977  0.20 45.95  ? 127 CYS B CB    1 
ATOM   8754  C  CB    B CYS B 2 127 ? 1.521   -20.565 -0.309  0.80 43.65  ? 127 CYS B CB    1 
ATOM   8755  S  SG    A CYS B 2 127 ? 2.786   -21.396 -1.493  0.20 44.57  ? 127 CYS B SG    1 
ATOM   8756  S  SG    B CYS B 2 127 ? 2.944   -21.562 -0.867  0.80 42.92  ? 127 CYS B SG    1 
ATOM   8757  N  N     A ASP B 2 128 ? -1.555  -20.815 0.635   0.20 45.05  ? 128 ASP B N     1 
ATOM   8758  N  N     B ASP B 2 128 ? -1.389  -20.884 1.286   0.80 42.54  ? 128 ASP B N     1 
ATOM   8759  C  CA    A ASP B 2 128 ? -2.630  -20.124 1.341   0.20 42.83  ? 128 ASP B CA    1 
ATOM   8760  C  CA    B ASP B 2 128 ? -2.439  -20.201 2.037   0.80 41.33  ? 128 ASP B CA    1 
ATOM   8761  C  C     A ASP B 2 128 ? -2.104  -18.912 2.103   0.20 42.04  ? 128 ASP B C     1 
ATOM   8762  C  C     B ASP B 2 128 ? -1.992  -18.807 2.468   0.80 41.97  ? 128 ASP B C     1 
ATOM   8763  O  O     A ASP B 2 128 ? -2.684  -17.823 2.026   0.20 43.99  ? 128 ASP B O     1 
ATOM   8764  O  O     B ASP B 2 128 ? -2.694  -17.816 2.234   0.80 44.17  ? 128 ASP B O     1 
ATOM   8765  C  CB    A ASP B 2 128 ? -3.346  -21.094 2.282   0.20 43.36  ? 128 ASP B CB    1 
ATOM   8766  C  CB    B ASP B 2 128 ? -2.838  -21.046 3.248   0.80 47.02  ? 128 ASP B CB    1 
ATOM   8767  C  CG    A ASP B 2 128 ? -4.674  -20.554 2.771   0.20 43.65  ? 128 ASP B CG    1 
ATOM   8768  C  CG    B ASP B 2 128 ? -3.882  -20.371 4.106   0.80 45.64  ? 128 ASP B CG    1 
ATOM   8769  O  OD1   A ASP B 2 128 ? -5.575  -20.335 1.933   0.20 36.52  ? 128 ASP B OD1   1 
ATOM   8770  O  OD1   B ASP B 2 128 ? -4.961  -20.038 3.572   0.80 45.73  ? 128 ASP B OD1   1 
ATOM   8771  O  OD2   A ASP B 2 128 ? -4.819  -20.353 3.995   0.20 45.39  ? 128 ASP B OD2   1 
ATOM   8772  O  OD2   B ASP B 2 128 ? -3.623  -20.174 5.311   0.80 55.61  ? 128 ASP B OD2   1 
ATOM   8773  N  N     A CYS B 2 129 ? -1.008  -19.081 2.845   0.20 44.03  ? 129 CYS B N     1 
ATOM   8774  N  N     B CYS B 2 129 ? -0.818  -18.712 3.102   0.80 45.03  ? 129 CYS B N     1 
ATOM   8775  C  CA    A CYS B 2 129 ? -0.340  -17.969 3.527   0.20 42.17  ? 129 CYS B CA    1 
ATOM   8776  C  CA    B CYS B 2 129 ? -0.226  -17.418 3.458   0.80 42.09  ? 129 CYS B CA    1 
ATOM   8777  C  C     A CYS B 2 129 ? 1.163   -18.218 3.449   0.20 38.82  ? 129 CYS B C     1 
ATOM   8778  C  C     B CYS B 2 129 ? 1.292   -17.617 3.524   0.80 34.58  ? 129 CYS B C     1 
ATOM   8779  O  O     A CYS B 2 129 ? 1.719   -18.959 4.266   0.20 40.19  ? 129 CYS B O     1 
ATOM   8780  O  O     B CYS B 2 129 ? 1.851   -17.897 4.587   0.80 35.77  ? 129 CYS B O     1 
ATOM   8781  C  CB    A CYS B 2 129 ? -0.808  -17.826 4.971   0.20 40.09  ? 129 CYS B CB    1 
ATOM   8782  C  CB    B CYS B 2 129 ? -0.786  -16.886 4.769   0.80 40.82  ? 129 CYS B CB    1 
ATOM   8783  S  SG    A CYS B 2 129 ? -0.291  -16.275 5.759   0.20 35.85  ? 129 CYS B SG    1 
ATOM   8784  S  SG    B CYS B 2 129 ? -0.357  -15.166 5.103   0.80 42.69  ? 129 CYS B SG    1 
ATOM   8785  N  N     A LEU B 2 130 ? 1.813   -17.585 2.475   0.20 39.29  ? 130 LEU B N     1 
ATOM   8786  N  N     B LEU B 2 130 ? 1.938   -17.484 2.368   0.80 39.55  ? 130 LEU B N     1 
ATOM   8787  C  CA    A LEU B 2 130 ? 3.221   -17.829 2.192   0.20 35.72  ? 130 LEU B CA    1 
ATOM   8788  C  CA    B LEU B 2 130 ? 3.374   -17.708 2.260   0.80 35.48  ? 130 LEU B CA    1 
ATOM   8789  C  C     A LEU B 2 130 ? 4.113   -17.085 3.181   0.20 32.32  ? 130 LEU B C     1 
ATOM   8790  C  C     B LEU B 2 130 ? 4.150   -16.765 3.172   0.80 30.06  ? 130 LEU B C     1 
ATOM   8791  O  O     A LEU B 2 130 ? 3.916   -15.892 3.430   0.20 35.76  ? 130 LEU B O     1 
ATOM   8792  O  O     B LEU B 2 130 ? 3.929   -15.553 3.156   0.80 35.94  ? 130 LEU B O     1 
ATOM   8793  C  CB    A LEU B 2 130 ? 3.542   -17.388 0.762   0.20 36.72  ? 130 LEU B CB    1 
ATOM   8794  C  CB    B LEU B 2 130 ? 3.802   -17.506 0.804   0.80 36.39  ? 130 LEU B CB    1 
ATOM   8795  C  CG    A LEU B 2 130 ? 4.935   -17.648 0.188   0.20 37.53  ? 130 LEU B CG    1 
ATOM   8796  C  CG    B LEU B 2 130 ? 5.279   -17.306 0.489   0.80 36.69  ? 130 LEU B CG    1 
ATOM   8797  C  CD1   A LEU B 2 130 ? 5.201   -19.136 0.098   0.20 35.14  ? 130 LEU B CD1   1 
ATOM   8798  C  CD1   B LEU B 2 130 ? 5.862   -18.579 -0.085  0.80 37.90  ? 130 LEU B CD1   1 
ATOM   8799  C  CD2   A LEU B 2 130 ? 5.058   -16.998 -1.184  0.20 38.38  ? 130 LEU B CD2   1 
ATOM   8800  C  CD2   B LEU B 2 130 ? 5.416   -16.162 -0.504  0.80 45.24  ? 130 LEU B CD2   1 
ATOM   8801  N  N     A GLN B 2 131 ? 5.102   -17.789 3.737   0.20 32.19  ? 131 GLN B N     1 
ATOM   8802  N  N     B GLN B 2 131 ? 5.089   -17.321 3.945   0.80 30.45  ? 131 GLN B N     1 
ATOM   8803  C  CA    A GLN B 2 131 ? 6.103   -17.127 4.577   0.20 36.16  ? 131 GLN B CA    1 
ATOM   8804  C  CA    B GLN B 2 131 ? 5.929   -16.515 4.825   0.80 34.89  ? 131 GLN B CA    1 
ATOM   8805  C  C     A GLN B 2 131 ? 7.086   -16.338 3.716   0.20 34.81  ? 131 GLN B C     1 
ATOM   8806  C  C     B GLN B 2 131 ? 7.273   -16.117 4.219   0.80 36.20  ? 131 GLN B C     1 
ATOM   8807  O  O     A GLN B 2 131 ? 7.101   -15.104 3.733   0.20 32.03  ? 131 GLN B O     1 
ATOM   8808  O  O     B GLN B 2 131 ? 7.856   -15.117 4.654   0.80 31.67  ? 131 GLN B O     1 
ATOM   8809  C  CB    A GLN B 2 131 ? 6.845   -18.155 5.438   0.20 37.21  ? 131 GLN B CB    1 
ATOM   8810  C  CB    B GLN B 2 131 ? 6.182   -17.246 6.146   0.80 32.26  ? 131 GLN B CB    1 
ATOM   8811  C  CG    A GLN B 2 131 ? 5.973   -18.992 6.357   0.20 39.03  ? 131 GLN B CG    1 
ATOM   8812  C  CG    B GLN B 2 131 ? 6.965   -18.529 6.041   0.80 40.79  ? 131 GLN B CG    1 
ATOM   8813  C  CD    A GLN B 2 131 ? 6.795   -19.882 7.272   0.20 38.87  ? 131 GLN B CD    1 
ATOM   8814  C  CD    B GLN B 2 131 ? 7.540   -18.940 7.377   0.80 40.92  ? 131 GLN B CD    1 
ATOM   8815  O  OE1   A GLN B 2 131 ? 7.946   -19.573 7.580   0.20 37.74  ? 131 GLN B OE1   1 
ATOM   8816  O  OE1   B GLN B 2 131 ? 8.140   -18.125 8.072   0.80 36.36  ? 131 GLN B OE1   1 
ATOM   8817  N  NE2   A GLN B 2 131 ? 6.211   -20.995 7.706   0.20 39.50  ? 131 GLN B NE2   1 
ATOM   8818  N  NE2   B GLN B 2 131 ? 7.344   -20.199 7.754   0.80 39.99  ? 131 GLN B NE2   1 
ATOM   8819  N  N     A GLY B 2 132 ? 7.915   -17.043 2.952   0.20 34.02  ? 132 GLY B N     1 
ATOM   8820  N  N     B GLY B 2 132 ? 7.790   -16.856 3.249   0.80 33.72  ? 132 GLY B N     1 
ATOM   8821  C  CA    A GLY B 2 132 ? 8.903   -16.388 2.119   0.20 31.98  ? 132 GLY B CA    1 
ATOM   8822  C  CA    B GLY B 2 132 ? 9.004   -16.395 2.601   0.80 32.89  ? 132 GLY B CA    1 
ATOM   8823  C  C     A GLY B 2 132 ? 9.560   -17.335 1.139   0.20 30.56  ? 132 GLY B C     1 
ATOM   8824  C  C     B GLY B 2 132 ? 9.683   -17.511 1.828   0.80 29.26  ? 132 GLY B C     1 
ATOM   8825  O  O     A GLY B 2 132 ? 8.871   -18.111 0.471   0.20 30.62  ? 132 GLY B O     1 
ATOM   8826  O  O     B GLY B 2 132 ? 9.083   -18.543 1.528   0.80 26.17  ? 132 GLY B O     1 
ATOM   8827  N  N     A PHE B 2 133 ? 10.891  -17.285 1.044   0.20 32.12  ? 133 PHE B N     1 
ATOM   8828  N  N     B PHE B 2 133 ? 10.950  -17.267 1.517   0.80 32.60  ? 133 PHE B N     1 
ATOM   8829  C  CA    A PHE B 2 133 ? 11.637  -18.111 0.104   0.20 30.47  ? 133 PHE B CA    1 
ATOM   8830  C  CA    B PHE B 2 133 ? 11.694  -18.125 0.618   0.80 28.16  ? 133 PHE B CA    1 
ATOM   8831  C  C     A PHE B 2 133 ? 12.947  -18.564 0.737   0.20 32.15  ? 133 PHE B C     1 
ATOM   8832  C  C     B PHE B 2 133 ? 12.982  -18.575 1.285   0.80 32.27  ? 133 PHE B C     1 
ATOM   8833  O  O     A PHE B 2 133 ? 13.644  -17.767 1.371   0.20 28.31  ? 133 PHE B O     1 
ATOM   8834  O  O     B PHE B 2 133 ? 13.529  -17.891 2.152   0.80 26.76  ? 133 PHE B O     1 
ATOM   8835  C  CB    A PHE B 2 133 ? 11.927  -17.352 -1.198  0.20 32.87  ? 133 PHE B CB    1 
ATOM   8836  C  CB    B PHE B 2 133 ? 12.035  -17.397 -0.694  0.80 32.72  ? 133 PHE B CB    1 
ATOM   8837  C  CG    A PHE B 2 133 ? 10.694  -16.875 -1.910  0.20 33.29  ? 133 PHE B CG    1 
ATOM   8838  C  CG    B PHE B 2 133 ? 10.839  -16.880 -1.430  0.80 33.27  ? 133 PHE B CG    1 
ATOM   8839  C  CD1   A PHE B 2 133 ? 10.060  -17.684 -2.837  0.20 33.12  ? 133 PHE B CD1   1 
ATOM   8840  C  CD1   B PHE B 2 133 ? 10.145  -17.697 -2.317  0.80 33.09  ? 133 PHE B CD1   1 
ATOM   8841  C  CD2   A PHE B 2 133 ? 10.167  -15.618 -1.651  0.20 33.58  ? 133 PHE B CD2   1 
ATOM   8842  C  CD2   B PHE B 2 133 ? 10.399  -15.574 -1.238  0.80 32.60  ? 133 PHE B CD2   1 
ATOM   8843  C  CE1   A PHE B 2 133 ? 8.921   -17.252 -3.492  0.20 32.16  ? 133 PHE B CE1   1 
ATOM   8844  C  CE1   B PHE B 2 133 ? 9.024   -17.219 -2.996  0.80 31.55  ? 133 PHE B CE1   1 
ATOM   8845  C  CE2   A PHE B 2 133 ? 9.030   -15.181 -2.303  0.20 34.15  ? 133 PHE B CE2   1 
ATOM   8846  C  CE2   B PHE B 2 133 ? 9.287   -15.097 -1.912  0.80 32.60  ? 133 PHE B CE2   1 
ATOM   8847  C  CZ    A PHE B 2 133 ? 8.407   -16.000 -3.225  0.20 35.18  ? 133 PHE B CZ    1 
ATOM   8848  C  CZ    B PHE B 2 133 ? 8.601   -15.922 -2.792  0.80 33.78  ? 133 PHE B CZ    1 
ATOM   8849  N  N     A GLN B 2 134 ? 13.279  -19.842 0.549   0.20 31.65  ? 134 GLN B N     1 
ATOM   8850  N  N     B GLN B 2 134 ? 13.483  -19.722 0.856   0.80 33.25  ? 134 GLN B N     1 
ATOM   8851  C  CA    A GLN B 2 134 ? 14.490  -20.447 1.096   0.20 30.08  ? 134 GLN B CA    1 
ATOM   8852  C  CA    B GLN B 2 134 ? 14.843  -20.087 1.184   0.80 30.18  ? 134 GLN B CA    1 
ATOM   8853  C  C     A GLN B 2 134 ? 15.346  -20.962 -0.054  0.20 30.11  ? 134 GLN B C     1 
ATOM   8854  C  C     B GLN B 2 134 ? 15.560  -20.449 -0.112  0.80 27.36  ? 134 GLN B C     1 
ATOM   8855  O  O     A GLN B 2 134 ? 14.931  -21.870 -0.782  0.20 29.83  ? 134 GLN B O     1 
ATOM   8856  O  O     B GLN B 2 134 ? 14.941  -20.881 -1.092  0.80 28.56  ? 134 GLN B O     1 
ATOM   8857  C  CB    A GLN B 2 134 ? 14.152  -21.582 2.066   0.20 31.28  ? 134 GLN B CB    1 
ATOM   8858  C  CB    B GLN B 2 134 ? 14.908  -21.215 2.232   0.80 29.50  ? 134 GLN B CB    1 
ATOM   8859  C  CG    A GLN B 2 134 ? 15.332  -22.494 2.393   0.20 32.82  ? 134 GLN B CG    1 
ATOM   8860  C  CG    B GLN B 2 134 ? 14.505  -22.611 1.778   0.80 32.85  ? 134 GLN B CG    1 
ATOM   8861  C  CD    A GLN B 2 134 ? 14.972  -23.607 3.366   0.20 36.43  ? 134 GLN B CD    1 
ATOM   8862  C  CD    B GLN B 2 134 ? 14.518  -23.621 2.930   0.80 36.05  ? 134 GLN B CD    1 
ATOM   8863  O  OE1   A GLN B 2 134 ? 14.440  -23.356 4.448   0.20 37.48  ? 134 GLN B OE1   1 
ATOM   8864  O  OE1   B GLN B 2 134 ? 14.388  -23.255 4.102   0.80 39.47  ? 134 GLN B OE1   1 
ATOM   8865  N  NE2   A GLN B 2 134 ? 15.267  -24.845 2.984   0.20 39.48  ? 134 GLN B NE2   1 
ATOM   8866  N  NE2   B GLN B 2 134 ? 14.677  -24.896 2.595   0.80 43.92  ? 134 GLN B NE2   1 
ATOM   8867  N  N     A LEU B 2 135 ? 16.538  -20.389 -0.210  0.20 27.79  ? 135 LEU B N     1 
ATOM   8868  N  N     B LEU B 2 135 ? 16.860  -20.200 -0.128  0.80 27.91  ? 135 LEU B N     1 
ATOM   8869  C  CA    A LEU B 2 135 ? 17.434  -20.707 -1.314  0.20 28.14  ? 135 LEU B CA    1 
ATOM   8870  C  CA    B LEU B 2 135 ? 17.681  -20.457 -1.304  0.80 27.58  ? 135 LEU B CA    1 
ATOM   8871  C  C     A LEU B 2 135 ? 18.711  -21.356 -0.795  0.20 28.14  ? 135 LEU B C     1 
ATOM   8872  C  C     B LEU B 2 135 ? 18.994  -21.081 -0.865  0.80 26.37  ? 135 LEU B C     1 
ATOM   8873  O  O     A LEU B 2 135 ? 19.238  -20.966 0.252   0.20 29.46  ? 135 LEU B O     1 
ATOM   8874  O  O     B LEU B 2 135 ? 19.665  -20.545 0.020   0.80 25.04  ? 135 LEU B O     1 
ATOM   8875  C  CB    A LEU B 2 135 ? 17.780  -19.443 -2.113  0.20 32.40  ? 135 LEU B CB    1 
ATOM   8876  C  CB    B LEU B 2 135 ? 17.954  -19.164 -2.078  0.80 33.56  ? 135 LEU B CB    1 
ATOM   8877  C  CG    A LEU B 2 135 ? 18.867  -19.552 -3.185  0.20 32.00  ? 135 LEU B CG    1 
ATOM   8878  C  CG    B LEU B 2 135 ? 18.803  -19.341 -3.334  0.80 32.55  ? 135 LEU B CG    1 
ATOM   8879  C  CD1   A LEU B 2 135 ? 18.415  -20.436 -4.340  0.20 33.15  ? 135 LEU B CD1   1 
ATOM   8880  C  CD1   B LEU B 2 135 ? 17.921  -19.277 -4.580  0.80 38.24  ? 135 LEU B CD1   1 
ATOM   8881  C  CD2   A LEU B 2 135 ? 19.272  -18.172 -3.683  0.20 33.82  ? 135 LEU B CD2   1 
ATOM   8882  C  CD2   B LEU B 2 135 ? 19.934  -18.315 -3.398  0.80 35.66  ? 135 LEU B CD2   1 
ATOM   8883  N  N     A THR B 2 136 ? 19.206  -22.350 -1.530  0.20 31.31  ? 136 THR B N     1 
ATOM   8884  N  N     B THR B 2 136 ? 19.358  -22.208 -1.475  0.80 31.83  ? 136 THR B N     1 
ATOM   8885  C  CA    A THR B 2 136 ? 20.483  -22.994 -1.242  0.20 29.44  ? 136 THR B CA    1 
ATOM   8886  C  CA    B THR B 2 136 ? 20.655  -22.830 -1.260  0.80 28.94  ? 136 THR B CA    1 
ATOM   8887  C  C     A THR B 2 136 ? 21.360  -22.875 -2.478  0.20 32.58  ? 136 THR B C     1 
ATOM   8888  C  C     B THR B 2 136 ? 21.529  -22.623 -2.489  0.80 33.86  ? 136 THR B C     1 
ATOM   8889  O  O     A THR B 2 136 ? 20.956  -23.295 -3.568  0.20 30.57  ? 136 THR B O     1 
ATOM   8890  O  O     B THR B 2 136 ? 21.053  -22.732 -3.626  0.80 31.64  ? 136 THR B O     1 
ATOM   8891  C  CB    A THR B 2 136 ? 20.291  -24.461 -0.856  0.20 31.91  ? 136 THR B CB    1 
ATOM   8892  C  CB    B THR B 2 136 ? 20.517  -24.323 -0.969  0.80 31.73  ? 136 THR B CB    1 
ATOM   8893  O  OG1   A THR B 2 136 ? 19.813  -25.199 -1.988  0.20 35.24  ? 136 THR B OG1   1 
ATOM   8894  O  OG1   B THR B 2 136 ? 19.861  -24.973 -2.067  0.80 36.50  ? 136 THR B OG1   1 
ATOM   8895  C  CG2   A THR B 2 136 ? 19.286  -24.583 0.274   0.20 31.38  ? 136 THR B CG2   1 
ATOM   8896  C  CG2   B THR B 2 136 ? 19.718  -24.545 0.301   0.80 30.27  ? 136 THR B CG2   1 
ATOM   8897  N  N     A HIS B 2 137 ? 22.555  -22.309 -2.311  0.20 29.34  ? 137 HIS B N     1 
ATOM   8898  N  N     B HIS B 2 137 ? 22.805  -22.318 -2.256  0.80 28.17  ? 137 HIS B N     1 
ATOM   8899  C  CA    A HIS B 2 137 ? 23.414  -22.001 -3.447  0.20 29.99  ? 137 HIS B CA    1 
ATOM   8900  C  CA    B HIS B 2 137 ? 23.754  -22.032 -3.326  0.80 29.02  ? 137 HIS B CA    1 
ATOM   8901  C  C     A HIS B 2 137 ? 24.832  -21.752 -2.952  0.20 32.21  ? 137 HIS B C     1 
ATOM   8902  C  C     B HIS B 2 137 ? 25.145  -21.891 -2.724  0.80 35.53  ? 137 HIS B C     1 
ATOM   8903  O  O     A HIS B 2 137 ? 25.077  -21.597 -1.753  0.20 29.96  ? 137 HIS B O     1 
ATOM   8904  O  O     B HIS B 2 137 ? 25.304  -21.750 -1.503  0.80 28.21  ? 137 HIS B O     1 
ATOM   8905  C  CB    A HIS B 2 137 ? 22.891  -20.788 -4.220  0.20 33.32  ? 137 HIS B CB    1 
ATOM   8906  C  CB    B HIS B 2 137 ? 23.374  -20.767 -4.114  0.80 35.75  ? 137 HIS B CB    1 
ATOM   8907  C  CG    A HIS B 2 137 ? 23.060  -19.488 -3.494  0.20 29.85  ? 137 HIS B CG    1 
ATOM   8908  C  CG    B HIS B 2 137 ? 23.388  -19.502 -3.306  0.80 30.16  ? 137 HIS B CG    1 
ATOM   8909  N  ND1   A HIS B 2 137 ? 23.319  -18.301 -4.144  0.20 28.16  ? 137 HIS B ND1   1 
ATOM   8910  N  ND1   B HIS B 2 137 ? 23.604  -18.264 -3.873  0.80 26.27  ? 137 HIS B ND1   1 
ATOM   8911  C  CD2   A HIS B 2 137 ? 23.006  -19.189 -2.174  0.20 29.37  ? 137 HIS B CD2   1 
ATOM   8912  C  CD2   B HIS B 2 137 ? 23.195  -19.280 -1.983  0.80 29.12  ? 137 HIS B CD2   1 
ATOM   8913  C  CE1   A HIS B 2 137 ? 23.418  -17.327 -3.257  0.20 28.34  ? 137 HIS B CE1   1 
ATOM   8914  C  CE1   B HIS B 2 137 ? 23.553  -17.336 -2.934  0.80 27.65  ? 137 HIS B CE1   1 
ATOM   8915  N  NE2   A HIS B 2 137 ? 23.233  -17.840 -2.054  0.20 29.12  ? 137 HIS B NE2   1 
ATOM   8916  N  NE2   B HIS B 2 137 ? 23.308  -17.926 -1.778  0.80 28.98  ? 137 HIS B NE2   1 
ATOM   8917  N  N     A SER B 2 138 ? 25.766  -21.708 -3.901  0.20 31.68  ? 138 SER B N     1 
ATOM   8918  N  N     B SER B 2 138 ? 26.152  -21.964 -3.595  0.80 28.82  ? 138 SER B N     1 
ATOM   8919  C  CA    A SER B 2 138 ? 27.153  -21.363 -3.627  0.20 30.55  ? 138 SER B CA    1 
ATOM   8920  C  CA    B SER B 2 138 ? 27.496  -21.520 -3.274  0.80 32.68  ? 138 SER B CA    1 
ATOM   8921  C  C     A SER B 2 138 ? 27.442  -19.934 -4.064  0.20 30.84  ? 138 SER B C     1 
ATOM   8922  C  C     B SER B 2 138 ? 27.707  -20.112 -3.813  0.80 31.00  ? 138 SER B C     1 
ATOM   8923  O  O     A SER B 2 138 ? 26.726  -19.346 -4.879  0.20 28.79  ? 138 SER B O     1 
ATOM   8924  O  O     B SER B 2 138 ? 27.043  -19.668 -4.756  0.80 30.16  ? 138 SER B O     1 
ATOM   8925  C  CB    A SER B 2 138 ? 28.115  -22.320 -4.340  0.20 32.59  ? 138 SER B CB    1 
ATOM   8926  C  CB    B SER B 2 138 ? 28.555  -22.458 -3.866  0.80 30.04  ? 138 SER B CB    1 
ATOM   8927  O  OG    A SER B 2 138 ? 27.978  -22.242 -5.749  0.20 31.81  ? 138 SER B OG    1 
ATOM   8928  O  OG    B SER B 2 138 ? 28.546  -22.388 -5.282  0.80 33.16  ? 138 SER B OG    1 
ATOM   8929  N  N     A LEU B 2 139 ? 28.516  -19.378 -3.509  0.20 28.55  ? 139 LEU B N     1 
ATOM   8930  N  N     B LEU B 2 139 ? 28.645  -19.405 -3.200  0.80 27.80  ? 139 LEU B N     1 
ATOM   8931  C  CA    A LEU B 2 139 ? 28.966  -18.045 -3.872  0.20 27.20  ? 139 LEU B CA    1 
ATOM   8932  C  CA    B LEU B 2 139 ? 29.011  -18.089 -3.690  0.80 26.08  ? 139 LEU B CA    1 
ATOM   8933  C  C     A LEU B 2 139 ? 30.222  -18.051 -4.731  0.20 28.61  ? 139 LEU B C     1 
ATOM   8934  C  C     B LEU B 2 139 ? 30.204  -18.135 -4.632  0.80 28.64  ? 139 LEU B C     1 
ATOM   8935  O  O     A LEU B 2 139 ? 30.601  -16.994 -5.247  0.20 29.09  ? 139 LEU B O     1 
ATOM   8936  O  O     B LEU B 2 139 ? 30.509  -17.119 -5.269  0.80 28.80  ? 139 LEU B O     1 
ATOM   8937  C  CB    A LEU B 2 139 ? 29.220  -17.209 -2.610  0.20 32.79  ? 139 LEU B CB    1 
ATOM   8938  C  CB    B LEU B 2 139 ? 29.323  -17.155 -2.522  0.80 33.26  ? 139 LEU B CB    1 
ATOM   8939  C  CG    A LEU B 2 139 ? 28.087  -17.192 -1.580  0.20 31.62  ? 139 LEU B CG    1 
ATOM   8940  C  CG    B LEU B 2 139 ? 28.178  -16.945 -1.521  0.80 32.56  ? 139 LEU B CG    1 
ATOM   8941  C  CD1   A LEU B 2 139 ? 28.417  -16.247 -0.436  0.20 34.60  ? 139 LEU B CD1   1 
ATOM   8942  C  CD1   B LEU B 2 139 ? 28.575  -15.896 -0.499  0.80 36.03  ? 139 LEU B CD1   1 
ATOM   8943  C  CD2   A LEU B 2 139 ? 26.767  -16.812 -2.232  0.20 29.04  ? 139 LEU B CD2   1 
ATOM   8944  C  CD2   B LEU B 2 139 ? 26.902  -16.530 -2.226  0.80 28.24  ? 139 LEU B CD2   1 
ATOM   8945  N  N     A GLY B 2 140 ? 30.867  -19.202 -4.905  0.20 27.27  ? 140 GLY B N     1 
ATOM   8946  N  N     B GLY B 2 140 ? 30.876  -19.281 -4.737  0.80 26.32  ? 140 GLY B N     1 
ATOM   8947  C  CA    A GLY B 2 140 ? 32.135  -19.254 -5.611  0.20 28.73  ? 140 GLY B CA    1 
ATOM   8948  C  CA    B GLY B 2 140 ? 32.145  -19.344 -5.448  0.80 28.54  ? 140 GLY B CA    1 
ATOM   8949  C  C     A GLY B 2 140 ? 32.024  -19.591 -7.083  0.20 35.14  ? 140 GLY B C     1 
ATOM   8950  C  C     B GLY B 2 140 ? 32.074  -19.699 -6.909  0.80 36.33  ? 140 GLY B C     1 
ATOM   8951  O  O     A GLY B 2 140 ? 32.956  -19.337 -7.854  0.20 32.82  ? 140 GLY B O     1 
ATOM   8952  O  O     B GLY B 2 140 ? 33.086  -19.596 -7.611  0.80 32.93  ? 140 GLY B O     1 
ATOM   8953  N  N     A GLY B 2 141 ? 30.899  -20.163 -7.485  0.20 31.87  ? 141 GLY B N     1 
ATOM   8954  N  N     B GLY B 2 141 ? 30.909  -20.121 -7.389  0.80 31.81  ? 141 GLY B N     1 
ATOM   8955  C  CA    A GLY B 2 141 ? 30.668  -20.557 -8.861  0.20 30.47  ? 141 GLY B CA    1 
ATOM   8956  C  CA    B GLY B 2 141 ? 30.725  -20.519 -8.763  0.80 30.25  ? 141 GLY B CA    1 
ATOM   8957  C  C     A GLY B 2 141 ? 30.064  -19.451 -9.693  0.20 28.88  ? 141 GLY B C     1 
ATOM   8958  C  C     B GLY B 2 141 ? 30.067  -19.440 -9.587  0.80 28.25  ? 141 GLY B C     1 
ATOM   8959  O  O     A GLY B 2 141 ? 30.361  -18.267 -9.507  0.20 33.37  ? 141 GLY B O     1 
ATOM   8960  O  O     B GLY B 2 141 ? 30.107  -18.252 -9.255  0.80 35.60  ? 141 GLY B O     1 
ATOM   8961  N  N     A GLY B 2 142 ? 29.200  -19.841 -10.628 0.20 33.47  ? 142 GLY B N     1 
ATOM   8962  N  N     B GLY B 2 142 ? 29.454  -19.860 -10.694 0.80 33.74  ? 142 GLY B N     1 
ATOM   8963  C  CA    A GLY B 2 142 ? 28.565  -18.885 -11.515 0.20 33.46  ? 142 GLY B CA    1 
ATOM   8964  C  CA    B GLY B 2 142 ? 28.863  -18.920 -11.625 0.80 31.67  ? 142 GLY B CA    1 
ATOM   8965  C  C     A GLY B 2 142 ? 27.051  -18.966 -11.528 0.20 35.31  ? 142 GLY B C     1 
ATOM   8966  C  C     B GLY B 2 142 ? 27.352  -18.808 -11.522 0.80 36.73  ? 142 GLY B C     1 
ATOM   8967  O  O     A GLY B 2 142 ? 26.374  -17.935 -11.561 0.20 33.77  ? 142 GLY B O     1 
ATOM   8968  O  O     B GLY B 2 142 ? 26.803  -17.702 -11.573 0.80 31.22  ? 142 GLY B O     1 
ATOM   8969  N  N     A THR B 2 143 ? 26.505  -20.185 -11.510 0.20 34.18  ? 143 THR B N     1 
ATOM   8970  N  N     B THR B 2 143 ? 26.675  -19.952 -11.368 0.80 34.97  ? 143 THR B N     1 
ATOM   8971  C  CA    A THR B 2 143 ? 25.055  -20.359 -11.522 0.20 34.15  ? 143 THR B CA    1 
ATOM   8972  C  CA    B THR B 2 143 ? 25.217  -20.036 -11.406 0.80 34.12  ? 143 THR B CA    1 
ATOM   8973  C  C     A THR B 2 143 ? 24.460  -20.155 -10.134 0.20 29.91  ? 143 THR B C     1 
ATOM   8974  C  C     B THR B 2 143 ? 24.590  -19.703 -10.052 0.80 26.60  ? 143 THR B C     1 
ATOM   8975  O  O     A THR B 2 143 ? 23.534  -19.357 -9.959  0.20 30.76  ? 143 THR B O     1 
ATOM   8976  O  O     B THR B 2 143 ? 23.830  -18.737 -9.943  0.80 32.79  ? 143 THR B O     1 
ATOM   8977  C  CB    A THR B 2 143 ? 24.688  -21.746 -12.053 0.20 36.92  ? 143 THR B CB    1 
ATOM   8978  C  CB    B THR B 2 143 ? 24.789  -21.436 -11.870 0.80 36.96  ? 143 THR B CB    1 
ATOM   8979  O  OG1   A THR B 2 143 ? 25.147  -21.881 -13.403 0.20 38.51  ? 143 THR B OG1   1 
ATOM   8980  O  OG1   B THR B 2 143 ? 25.195  -21.634 -13.228 0.80 38.27  ? 143 THR B OG1   1 
ATOM   8981  C  CG2   A THR B 2 143 ? 23.179  -21.955 -12.012 0.20 36.76  ? 143 THR B CG2   1 
ATOM   8982  C  CG2   B THR B 2 143 ? 23.276  -21.615 -11.769 0.80 37.66  ? 143 THR B CG2   1 
ATOM   8983  N  N     A GLY B 2 144 ? 24.967  -20.883 -9.138  0.20 30.34  ? 144 GLY B N     1 
ATOM   8984  N  N     B GLY B 2 144 ? 24.889  -20.495 -9.021  0.80 32.79  ? 144 GLY B N     1 
ATOM   8985  C  CA    A GLY B 2 144 ? 24.499  -20.683 -7.778  0.20 31.49  ? 144 GLY B CA    1 
ATOM   8986  C  CA    B GLY B 2 144 ? 24.327  -20.209 -7.699  0.80 26.81  ? 144 GLY B CA    1 
ATOM   8987  C  C     A GLY B 2 144 ? 24.844  -19.321 -7.218  0.20 30.33  ? 144 GLY B C     1 
ATOM   8988  C  C     B GLY B 2 144 ? 24.611  -18.793 -7.241  0.80 31.84  ? 144 GLY B C     1 
ATOM   8989  O  O     A GLY B 2 144 ? 24.185  -18.860 -6.280  0.20 31.89  ? 144 GLY B O     1 
ATOM   8990  O  O     B GLY B 2 144 ? 23.734  -18.119 -6.689  0.80 34.06  ? 144 GLY B O     1 
ATOM   8991  N  N     A SER B 2 145 ? 25.853  -18.657 -7.783  0.20 32.18  ? 145 SER B N     1 
ATOM   8992  N  N     B SER B 2 145 ? 25.834  -18.310 -7.495  0.80 33.62  ? 145 SER B N     1 
ATOM   8993  C  CA    A SER B 2 145 ? 26.271  -17.330 -7.341  0.20 31.83  ? 145 SER B CA    1 
ATOM   8994  C  CA    B SER B 2 145 ? 26.254  -16.968 -7.087  0.80 30.89  ? 145 SER B CA    1 
ATOM   8995  C  C     A SER B 2 145 ? 25.668  -16.220 -8.197  0.20 32.89  ? 145 SER B C     1 
ATOM   8996  C  C     B SER B 2 145 ? 25.695  -15.889 -8.006  0.80 33.24  ? 145 SER B C     1 
ATOM   8997  O  O     A SER B 2 145 ? 25.021  -15.308 -7.669  0.20 33.20  ? 145 SER B O     1 
ATOM   8998  O  O     B SER B 2 145 ? 25.097  -14.908 -7.540  0.80 31.00  ? 145 SER B O     1 
ATOM   8999  C  CB    A SER B 2 145 ? 27.801  -17.229 -7.363  0.20 33.53  ? 145 SER B CB    1 
ATOM   9000  C  CB    B SER B 2 145 ? 27.783  -16.877 -7.089  0.80 30.58  ? 145 SER B CB    1 
ATOM   9001  O  OG    A SER B 2 145 ? 28.289  -17.276 -8.697  0.20 33.44  ? 145 SER B OG    1 
ATOM   9002  O  OG    B SER B 2 145 ? 28.272  -17.019 -8.431  0.80 38.25  ? 145 SER B OG    1 
ATOM   9003  N  N     A GLY B 2 146 ? 25.891  -16.268 -9.516  0.20 34.23  ? 146 GLY B N     1 
ATOM   9004  N  N     B GLY B 2 146 ? 25.929  -16.030 -9.311  0.80 35.11  ? 146 GLY B N     1 
ATOM   9005  C  CA    A GLY B 2 146 ? 25.389  -15.206 -10.374 0.20 34.42  ? 146 GLY B CA    1 
ATOM   9006  C  CA    B GLY B 2 146 ? 25.506  -15.036 -10.275 0.80 34.21  ? 146 GLY B CA    1 
ATOM   9007  C  C     A GLY B 2 146 ? 23.895  -15.309 -10.616 0.20 32.58  ? 146 GLY B C     1 
ATOM   9008  C  C     B GLY B 2 146 ? 24.019  -15.070 -10.566 0.80 31.82  ? 146 GLY B C     1 
ATOM   9009  O  O     A GLY B 2 146 ? 23.161  -14.335 -10.446 0.20 35.25  ? 146 GLY B O     1 
ATOM   9010  O  O     B GLY B 2 146 ? 23.343  -14.046 -10.461 0.80 36.60  ? 146 GLY B O     1 
ATOM   9011  N  N     A MET B 2 147 ? 23.423  -16.495 -11.006 0.20 35.29  ? 147 MET B N     1 
ATOM   9012  N  N     B MET B 2 147 ? 23.490  -16.230 -10.948 0.80 35.54  ? 147 MET B N     1 
ATOM   9013  C  CA    A MET B 2 147 ? 21.995  -16.674 -11.237 0.20 33.37  ? 147 MET B CA    1 
ATOM   9014  C  CA    B MET B 2 147 ? 22.055  -16.315 -11.207 0.80 32.30  ? 147 MET B CA    1 
ATOM   9015  C  C     A MET B 2 147 ? 21.233  -16.916 -9.942  0.20 33.30  ? 147 MET B C     1 
ATOM   9016  C  C     B MET B 2 147 ? 21.244  -16.357 -9.921  0.80 34.27  ? 147 MET B C     1 
ATOM   9017  O  O     A MET B 2 147 ? 20.039  -16.605 -9.863  0.20 32.90  ? 147 MET B O     1 
ATOM   9018  O  O     B MET B 2 147 ? 20.075  -15.955 -9.916  0.80 35.52  ? 147 MET B O     1 
ATOM   9019  C  CB    A MET B 2 147 ? 21.762  -17.829 -12.208 0.20 34.22  ? 147 MET B CB    1 
ATOM   9020  C  CB    B MET B 2 147 ? 21.731  -17.545 -12.055 0.80 32.82  ? 147 MET B CB    1 
ATOM   9021  C  CG    A MET B 2 147 ? 20.321  -17.930 -12.686 0.20 41.16  ? 147 MET B CG    1 
ATOM   9022  C  CG    B MET B 2 147 ? 20.279  -17.591 -12.534 0.80 42.43  ? 147 MET B CG    1 
ATOM   9023  S  SD    A MET B 2 147 ? 19.984  -19.400 -13.669 0.20 42.32  ? 147 MET B SD    1 
ATOM   9024  S  SD    B MET B 2 147 ? 19.832  -19.172 -13.273 0.80 44.33  ? 147 MET B SD    1 
ATOM   9025  C  CE    A MET B 2 147 ? 18.268  -19.136 -14.115 0.20 40.17  ? 147 MET B CE    1 
ATOM   9026  C  CE    B MET B 2 147 ? 18.248  -18.774 -14.001 0.80 38.95  ? 147 MET B CE    1 
ATOM   9027  N  N     A GLY B 2 148 ? 21.894  -17.470 -8.925  0.20 31.17  ? 148 GLY B N     1 
ATOM   9028  N  N     B GLY B 2 148 ? 21.828  -16.839 -8.826  0.80 33.39  ? 148 GLY B N     1 
ATOM   9029  C  CA    A GLY B 2 148 ? 21.241  -17.609 -7.635  0.20 31.27  ? 148 GLY B CA    1 
ATOM   9030  C  CA    B GLY B 2 148 ? 21.082  -16.852 -7.577  0.80 27.89  ? 148 GLY B CA    1 
ATOM   9031  C  C     A GLY B 2 148 ? 20.850  -16.269 -7.045  0.20 31.03  ? 148 GLY B C     1 
ATOM   9032  C  C     B GLY B 2 148 ? 20.778  -15.453 -7.079  0.80 31.47  ? 148 GLY B C     1 
ATOM   9033  O  O     A GLY B 2 148 ? 19.784  -16.134 -6.438  0.20 30.79  ? 148 GLY B O     1 
ATOM   9034  O  O     B GLY B 2 148 ? 19.649  -15.159 -6.676  0.80 32.32  ? 148 GLY B O     1 
ATOM   9035  N  N     A THR B 2 149 ? 21.701  -15.257 -7.230  0.20 31.60  ? 149 THR B N     1 
ATOM   9036  N  N     B THR B 2 149 ? 21.785  -14.572 -7.103  0.80 29.76  ? 149 THR B N     1 
ATOM   9037  C  CA    A THR B 2 149 ? 21.408  -13.915 -6.745  0.20 30.43  ? 149 THR B CA    1 
ATOM   9038  C  CA    B THR B 2 149 ? 21.588  -13.197 -6.658  0.80 27.78  ? 149 THR B CA    1 
ATOM   9039  C  C     A THR B 2 149 ? 20.461  -13.165 -7.671  0.20 33.75  ? 149 THR B C     1 
ATOM   9040  C  C     B THR B 2 149 ? 20.630  -12.450 -7.579  0.80 37.78  ? 149 THR B C     1 
ATOM   9041  O  O     A THR B 2 149 ? 19.644  -12.367 -7.197  0.20 33.94  ? 149 THR B O     1 
ATOM   9042  O  O     B THR B 2 149 ? 19.819  -11.641 -7.112  0.80 35.00  ? 149 THR B O     1 
ATOM   9043  C  CB    A THR B 2 149 ? 22.705  -13.122 -6.571  0.20 33.00  ? 149 THR B CB    1 
ATOM   9044  C  CB    B THR B 2 149 ? 22.933  -12.462 -6.553  0.80 33.56  ? 149 THR B CB    1 
ATOM   9045  O  OG1   A THR B 2 149 ? 23.491  -13.213 -7.768  0.20 33.29  ? 149 THR B OG1   1 
ATOM   9046  O  OG1   B THR B 2 149 ? 23.701  -12.627 -7.762  0.80 31.94  ? 149 THR B OG1   1 
ATOM   9047  C  CG2   A THR B 2 149 ? 23.508  -13.664 -5.398  0.20 31.20  ? 149 THR B CG2   1 
ATOM   9048  C  CG2   B THR B 2 149 ? 23.737  -12.999 -5.381  0.80 33.03  ? 149 THR B CG2   1 
ATOM   9049  N  N     A LEU B 2 150 ? 20.554  -13.397 -8.984  0.20 35.65  ? 150 LEU B N     1 
ATOM   9050  N  N     B LEU B 2 150 ? 20.699  -12.709 -8.887  0.80 35.99  ? 150 LEU B N     1 
ATOM   9051  C  CA    A LEU B 2 150 ? 19.625  -12.756 -9.910  0.20 35.16  ? 150 LEU B CA    1 
ATOM   9052  C  CA    B LEU B 2 150 ? 19.715  -12.139 -9.807  0.80 36.04  ? 150 LEU B CA    1 
ATOM   9053  C  C     A LEU B 2 150 ? 18.188  -13.171 -9.627  0.20 35.94  ? 150 LEU B C     1 
ATOM   9054  C  C     B LEU B 2 150 ? 18.301  -12.581 -9.440  0.80 36.84  ? 150 LEU B C     1 
ATOM   9055  O  O     A LEU B 2 150 ? 17.264  -12.367 -9.796  0.20 36.68  ? 150 LEU B O     1 
ATOM   9056  O  O     B LEU B 2 150 ? 17.383  -11.757 -9.337  0.80 35.82  ? 150 LEU B O     1 
ATOM   9057  C  CB    A LEU B 2 150 ? 20.006  -13.089 -11.353 0.20 36.12  ? 150 LEU B CB    1 
ATOM   9058  C  CB    B LEU B 2 150 ? 20.050  -12.539 -11.246 0.80 36.81  ? 150 LEU B CB    1 
ATOM   9059  C  CG    A LEU B 2 150 ? 19.202  -12.385 -12.448 0.20 38.76  ? 150 LEU B CG    1 
ATOM   9060  C  CG    B LEU B 2 150 ? 19.184  -11.903 -12.339 0.80 38.53  ? 150 LEU B CG    1 
ATOM   9061  C  CD1   A LEU B 2 150 ? 19.396  -10.877 -12.379 0.20 37.68  ? 150 LEU B CD1   1 
ATOM   9062  C  CD1   B LEU B 2 150 ? 19.497  -10.423 -12.488 0.80 37.20  ? 150 LEU B CD1   1 
ATOM   9063  C  CD2   A LEU B 2 150 ? 19.584  -12.915 -13.823 0.20 40.89  ? 150 LEU B CD2   1 
ATOM   9064  C  CD2   B LEU B 2 150 ? 19.361  -12.624 -13.673 0.80 41.32  ? 150 LEU B CD2   1 
ATOM   9065  N  N     A LEU B 2 151 ? 17.981  -14.416 -9.191  0.20 33.26  ? 151 LEU B N     1 
ATOM   9066  N  N     B LEU B 2 151 ? 18.112  -13.885 -9.224  0.80 33.29  ? 151 LEU B N     1 
ATOM   9067  C  CA    A LEU B 2 151 ? 16.648  -14.844 -8.784  0.20 36.23  ? 151 LEU B CA    1 
ATOM   9068  C  CA    B LEU B 2 151 ? 16.790  -14.405 -8.895  0.80 35.63  ? 151 LEU B CA    1 
ATOM   9069  C  C     A LEU B 2 151 ? 16.223  -14.162 -7.490  0.20 37.93  ? 151 LEU B C     1 
ATOM   9070  C  C     B LEU B 2 151 ? 16.282  -13.824 -7.583  0.80 39.51  ? 151 LEU B C     1 
ATOM   9071  O  O     A LEU B 2 151 ? 15.043  -13.844 -7.311  0.20 36.44  ? 151 LEU B O     1 
ATOM   9072  O  O     B LEU B 2 151 ? 15.106  -13.458 -7.473  0.80 34.40  ? 151 LEU B O     1 
ATOM   9073  C  CB    A LEU B 2 151 ? 16.608  -16.363 -8.630  0.20 36.71  ? 151 LEU B CB    1 
ATOM   9074  C  CB    B LEU B 2 151 ? 16.838  -15.926 -8.815  0.80 38.30  ? 151 LEU B CB    1 
ATOM   9075  C  CG    A LEU B 2 151 ? 16.566  -17.160 -9.934  0.20 37.07  ? 151 LEU B CG    1 
ATOM   9076  C  CG    B LEU B 2 151 ? 15.503  -16.611 -8.573  0.80 33.66  ? 151 LEU B CG    1 
ATOM   9077  C  CD1   A LEU B 2 151 ? 16.775  -18.637 -9.665  0.20 34.61  ? 151 LEU B CD1   1 
ATOM   9078  C  CD1   B LEU B 2 151 ? 14.535  -16.254 -9.688  0.80 41.58  ? 151 LEU B CD1   1 
ATOM   9079  C  CD2   A LEU B 2 151 ? 15.240  -16.927 -10.632 0.20 38.09  ? 151 LEU B CD2   1 
ATOM   9080  C  CD2   B LEU B 2 151 ? 15.716  -18.108 -8.510  0.80 41.56  ? 151 LEU B CD2   1 
ATOM   9081  N  N     A ILE B 2 152 ? 17.172  -13.924 -6.581  0.20 36.21  ? 152 ILE B N     1 
ATOM   9082  N  N     B ILE B 2 152 ? 17.160  -13.728 -6.579  0.80 36.47  ? 152 ILE B N     1 
ATOM   9083  C  CA    A ILE B 2 152 ? 16.848  -13.259 -5.319  0.20 38.48  ? 152 ILE B CA    1 
ATOM   9084  C  CA    B ILE B 2 152 ? 16.793  -13.087 -5.317  0.80 38.82  ? 152 ILE B CA    1 
ATOM   9085  C  C     A ILE B 2 152 ? 16.254  -11.881 -5.581  0.20 39.06  ? 152 ILE B C     1 
ATOM   9086  C  C     B ILE B 2 152 ? 16.245  -11.689 -5.569  0.80 39.26  ? 152 ILE B C     1 
ATOM   9087  O  O     A ILE B 2 152 ? 15.238  -11.500 -4.989  0.20 40.56  ? 152 ILE B O     1 
ATOM   9088  O  O     B ILE B 2 152 ? 15.202  -11.306 -5.029  0.80 41.19  ? 152 ILE B O     1 
ATOM   9089  C  CB    A ILE B 2 152 ? 18.095  -13.168 -4.423  0.20 35.49  ? 152 ILE B CB    1 
ATOM   9090  C  CB    B ILE B 2 152 ? 18.000  -13.047 -4.365  0.80 35.36  ? 152 ILE B CB    1 
ATOM   9091  C  CG1   A ILE B 2 152 ? 18.544  -14.560 -3.982  0.20 34.46  ? 152 ILE B CG1   1 
ATOM   9092  C  CG1   B ILE B 2 152 ? 18.311  -14.448 -3.844  0.80 34.60  ? 152 ILE B CG1   1 
ATOM   9093  C  CG2   A ILE B 2 152 ? 17.819  -12.288 -3.216  0.20 38.01  ? 152 ILE B CG2   1 
ATOM   9094  C  CG2   B ILE B 2 152 ? 17.747  -12.073 -3.232  0.80 38.51  ? 152 ILE B CG2   1 
ATOM   9095  C  CD1   A ILE B 2 152 ? 19.830  -14.558 -3.188  0.20 33.43  ? 152 ILE B CD1   1 
ATOM   9096  C  CD1   B ILE B 2 152 ? 19.484  -14.498 -2.895  0.80 32.76  ? 152 ILE B CD1   1 
ATOM   9097  N  N     A SER B 2 153 ? 16.875  -11.116 -6.481  0.20 37.10  ? 153 SER B N     1 
ATOM   9098  N  N     B SER B 2 153 ? 16.937  -10.908 -6.403  0.80 36.66  ? 153 SER B N     1 
ATOM   9099  C  CA    A SER B 2 153 ? 16.415  -9.753  -6.729  0.20 39.60  ? 153 SER B CA    1 
ATOM   9100  C  CA    B SER B 2 153 ? 16.538  -9.517  -6.611  0.80 39.37  ? 153 SER B CA    1 
ATOM   9101  C  C     A SER B 2 153 ? 15.105  -9.737  -7.508  0.20 42.90  ? 153 SER B C     1 
ATOM   9102  C  C     B SER B 2 153 ? 15.176  -9.413  -7.284  0.80 45.24  ? 153 SER B C     1 
ATOM   9103  O  O     A SER B 2 153 ? 14.216  -8.929  -7.218  0.20 41.52  ? 153 SER B O     1 
ATOM   9104  O  O     B SER B 2 153 ? 14.375  -8.540  -6.934  0.80 39.42  ? 153 SER B O     1 
ATOM   9105  C  CB    A SER B 2 153 ? 17.493  -8.962  -7.471  0.20 41.18  ? 153 SER B CB    1 
ATOM   9106  C  CB    B SER B 2 153 ? 17.586  -8.776  -7.438  0.80 41.21  ? 153 SER B CB    1 
ATOM   9107  O  OG    A SER B 2 153 ? 17.147  -7.591  -7.561  0.20 41.90  ? 153 SER B OG    1 
ATOM   9108  O  OG    B SER B 2 153 ? 18.603  -8.247  -6.612  0.80 44.56  ? 153 SER B OG    1 
ATOM   9109  N  N     A LYS B 2 154 ? 14.966  -10.617 -8.503  0.20 39.77  ? 154 LYS B N     1 
ATOM   9110  N  N     B LYS B 2 154 ? 14.909  -10.268 -8.273  0.80 40.23  ? 154 LYS B N     1 
ATOM   9111  C  CA    A LYS B 2 154 ? 13.739  -10.643 -9.295  0.20 40.07  ? 154 LYS B CA    1 
ATOM   9112  C  CA    B LYS B 2 154 ? 13.619  -10.214 -8.951  0.80 37.93  ? 154 LYS B CA    1 
ATOM   9113  C  C     A LYS B 2 154 ? 12.553  -11.117 -8.464  0.20 42.09  ? 154 LYS B C     1 
ATOM   9114  C  C     B LYS B 2 154 ? 12.496  -10.701 -8.046  0.80 43.53  ? 154 LYS B C     1 
ATOM   9115  O  O     A LYS B 2 154 ? 11.442  -10.591 -8.600  0.20 43.38  ? 154 LYS B O     1 
ATOM   9116  O  O     B LYS B 2 154 ? 11.362  -10.218 -8.147  0.80 43.13  ? 154 LYS B O     1 
ATOM   9117  C  CB    A LYS B 2 154 ? 13.924  -11.530 -10.526 0.20 42.85  ? 154 LYS B CB    1 
ATOM   9118  C  CB    B LYS B 2 154 ? 13.667  -11.039 -10.233 0.80 41.77  ? 154 LYS B CB    1 
ATOM   9119  C  CG    A LYS B 2 154 ? 14.898  -10.971 -11.551 0.20 43.15  ? 154 LYS B CG    1 
ATOM   9120  C  CG    B LYS B 2 154 ? 14.703  -10.564 -11.241 0.80 45.40  ? 154 LYS B CG    1 
ATOM   9121  C  CD    A LYS B 2 154 ? 14.465  -9.593  -12.025 0.20 46.17  ? 154 LYS B CD    1 
ATOM   9122  C  CD    B LYS B 2 154 ? 14.420  -9.143  -11.702 0.80 46.74  ? 154 LYS B CD    1 
ATOM   9123  C  CE    A LYS B 2 154 ? 15.469  -9.002  -13.002 0.20 47.02  ? 154 LYS B CE    1 
ATOM   9124  C  CE    B LYS B 2 154 ? 15.457  -8.688  -12.711 0.80 48.27  ? 154 LYS B CE    1 
ATOM   9125  N  NZ    A LYS B 2 154 ? 15.080  -7.631  -13.431 0.20 45.47  ? 154 LYS B NZ    1 
ATOM   9126  N  NZ    B LYS B 2 154 ? 15.595  -9.675  -13.815 0.80 51.87  ? 154 LYS B NZ    1 
ATOM   9127  N  N     A ILE B 2 155 ? 12.766  -12.112 -7.600  0.20 42.02  ? 155 ILE B N     1 
ATOM   9128  N  N     B ILE B 2 155 ? 12.788  -11.652 -7.159  0.80 42.54  ? 155 ILE B N     1 
ATOM   9129  C  CA    A ILE B 2 155 ? 11.693  -12.569 -6.724  0.20 39.27  ? 155 ILE B CA    1 
ATOM   9130  C  CA    B ILE B 2 155 ? 11.782  -12.108 -6.206  0.80 38.16  ? 155 ILE B CA    1 
ATOM   9131  C  C     A ILE B 2 155 ? 11.409  -11.529 -5.647  0.20 41.00  ? 155 ILE B C     1 
ATOM   9132  C  C     B ILE B 2 155 ? 11.436  -10.992 -5.231  0.80 38.84  ? 155 ILE B C     1 
ATOM   9133  O  O     A ILE B 2 155 ? 10.281  -11.430 -5.147  0.20 40.95  ? 155 ILE B O     1 
ATOM   9134  O  O     B ILE B 2 155 ? 10.264  -10.655 -5.038  0.80 41.89  ? 155 ILE B O     1 
ATOM   9135  C  CB    A ILE B 2 155 ? 12.058  -13.944 -6.131  0.20 41.88  ? 155 ILE B CB    1 
ATOM   9136  C  CB    B ILE B 2 155 ? 12.279  -13.362 -5.469  0.80 43.91  ? 155 ILE B CB    1 
ATOM   9137  C  CG1   A ILE B 2 155 ? 12.181  -14.978 -7.252  0.20 38.99  ? 155 ILE B CG1   1 
ATOM   9138  C  CG1   B ILE B 2 155 ? 12.340  -14.555 -6.427  0.80 42.64  ? 155 ILE B CG1   1 
ATOM   9139  C  CG2   A ILE B 2 155 ? 11.025  -14.399 -5.113  0.20 40.46  ? 155 ILE B CG2   1 
ATOM   9140  C  CG2   B ILE B 2 155 ? 11.406  -13.653 -4.265  0.80 38.81  ? 155 ILE B CG2   1 
ATOM   9141  C  CD1   A ILE B 2 155 ? 12.868  -16.259 -6.839  0.20 38.63  ? 155 ILE B CD1   1 
ATOM   9142  C  CD1   B ILE B 2 155 ? 12.706  -15.846 -5.736  0.80 40.69  ? 155 ILE B CD1   1 
ATOM   9143  N  N     A ARG B 2 156 ? 12.413  -10.727 -5.288  0.20 41.99  ? 156 ARG B N     1 
ATOM   9144  N  N     B ARG B 2 156 ? 12.458  -10.394 -4.614  0.80 39.47  ? 156 ARG B N     1 
ATOM   9145  C  CA    A ARG B 2 156 ? 12.202  -9.631  -4.347  0.20 42.23  ? 156 ARG B CA    1 
ATOM   9146  C  CA    B ARG B 2 156 ? 12.270  -9.263  -3.713  0.80 44.16  ? 156 ARG B CA    1 
ATOM   9147  C  C     A ARG B 2 156 ? 11.206  -8.620  -4.903  0.20 44.84  ? 156 ARG B C     1 
ATOM   9148  C  C     B ARG B 2 156 ? 11.583  -8.085  -4.398  0.80 48.46  ? 156 ARG B C     1 
ATOM   9149  O  O     A ARG B 2 156 ? 10.292  -8.175  -4.198  0.20 44.26  ? 156 ARG B O     1 
ATOM   9150  O  O     B ARG B 2 156 ? 10.961  -7.262  -3.715  0.80 51.18  ? 156 ARG B O     1 
ATOM   9151  C  CB    A ARG B 2 156 ? 13.537  -8.953  -4.036  0.20 42.67  ? 156 ARG B CB    1 
ATOM   9152  C  CB    B ARG B 2 156 ? 13.630  -8.852  -3.130  0.80 45.85  ? 156 ARG B CB    1 
ATOM   9153  C  CG    A ARG B 2 156 ? 13.521  -8.023  -2.832  0.20 45.58  ? 156 ARG B CG    1 
ATOM   9154  C  CG    B ARG B 2 156 ? 13.678  -7.502  -2.415  0.80 45.25  ? 156 ARG B CG    1 
ATOM   9155  C  CD    A ARG B 2 156 ? 13.574  -8.811  -1.537  0.20 43.83  ? 156 ARG B CD    1 
ATOM   9156  C  CD    B ARG B 2 156 ? 14.456  -7.589  -1.108  0.80 45.77  ? 156 ARG B CD    1 
ATOM   9157  N  NE    A ARG B 2 156 ? 13.874  -7.964  -0.389  0.20 45.57  ? 156 ARG B NE    1 
ATOM   9158  N  NE    B ARG B 2 156 ? 13.713  -8.360  -0.119  0.80 47.06  ? 156 ARG B NE    1 
ATOM   9159  C  CZ    A ARG B 2 156 ? 14.022  -8.413  0.850   0.20 44.87  ? 156 ARG B CZ    1 
ATOM   9160  C  CZ    B ARG B 2 156 ? 13.978  -8.380  1.180   0.80 46.79  ? 156 ARG B CZ    1 
ATOM   9161  N  NH1   A ARG B 2 156 ? 13.903  -9.699  1.135   0.20 36.01  ? 156 ARG B NH1   1 
ATOM   9162  N  NH1   B ARG B 2 156 ? 14.997  -7.706  1.691   0.80 45.54  ? 156 ARG B NH1   1 
ATOM   9163  N  NH2   A ARG B 2 156 ? 14.295  -7.550  1.825   0.20 42.56  ? 156 ARG B NH2   1 
ATOM   9164  N  NH2   B ARG B 2 156 ? 13.186  -9.079  1.989   0.80 44.44  ? 156 ARG B NH2   1 
ATOM   9165  N  N     A GLU B 2 157 ? 11.369  -8.248  -6.177  0.20 45.49  ? 157 GLU B N     1 
ATOM   9166  N  N     B GLU B 2 157 ? 11.658  -7.995  -5.728  0.80 45.13  ? 157 GLU B N     1 
ATOM   9167  C  CA    A GLU B 2 157 ? 10.511  -7.232  -6.778  0.20 47.67  ? 157 GLU B CA    1 
ATOM   9168  C  CA    B GLU B 2 157 ? 10.880  -6.984  -6.436  0.80 47.17  ? 157 GLU B CA    1 
ATOM   9169  C  C     A GLU B 2 157 ? 9.070   -7.708  -6.911  0.20 47.20  ? 157 GLU B C     1 
ATOM   9170  C  C     B GLU B 2 157 ? 9.399   -7.340  -6.452  0.80 48.74  ? 157 GLU B C     1 
ATOM   9171  O  O     A GLU B 2 157 ? 8.149   -6.885  -6.930  0.20 46.23  ? 157 GLU B O     1 
ATOM   9172  O  O     B GLU B 2 157 ? 8.545   -6.457  -6.318  0.80 45.02  ? 157 GLU B O     1 
ATOM   9173  C  CB    A GLU B 2 157 ? 11.059  -6.826  -8.149  0.20 50.65  ? 157 GLU B CB    1 
ATOM   9174  C  CB    B GLU B 2 157 ? 11.397  -6.807  -7.867  0.80 51.54  ? 157 GLU B CB    1 
ATOM   9175  C  CG    A GLU B 2 157 ? 12.479  -6.281  -8.123  0.20 53.97  ? 157 GLU B CG    1 
ATOM   9176  C  CG    B GLU B 2 157 ? 12.534  -5.799  -8.023  0.80 55.52  ? 157 GLU B CG    1 
ATOM   9177  C  CD    A GLU B 2 157 ? 13.004  -5.947  -9.508  0.20 58.30  ? 157 GLU B CD    1 
ATOM   9178  C  CD    B GLU B 2 157 ? 12.637  -5.249  -9.438  0.80 61.80  ? 157 GLU B CD    1 
ATOM   9179  O  OE1   A GLU B 2 157 ? 12.191  -5.879  -10.454 0.20 60.23  ? 157 GLU B OE1   1 
ATOM   9180  O  OE1   B GLU B 2 157 ? 11.587  -4.887  -10.014 0.80 65.38  ? 157 GLU B OE1   1 
ATOM   9181  O  OE2   A GLU B 2 157 ? 14.231  -5.757  -9.653  0.20 60.40  ? 157 GLU B OE2   1 
ATOM   9182  O  OE2   B GLU B 2 157 ? 13.764  -5.182  -9.976  0.80 67.30  ? 157 GLU B OE2   1 
ATOM   9183  N  N     A GLU B 2 158 ? 8.852   -9.019  -7.006  0.20 46.51  ? 158 GLU B N     1 
ATOM   9184  N  N     B GLU B 2 158 ? 9.075   -8.627  -6.605  0.80 46.90  ? 158 GLU B N     1 
ATOM   9185  C  CA    A GLU B 2 158 ? 7.505   -9.550  -7.162  0.20 46.46  ? 158 GLU B CA    1 
ATOM   9186  C  CA    B GLU B 2 158 ? 7.692   -9.066  -6.736  0.80 46.60  ? 158 GLU B CA    1 
ATOM   9187  C  C     A GLU B 2 158 ? 6.867   -9.954  -5.841  0.20 46.76  ? 158 GLU B C     1 
ATOM   9188  C  C     B GLU B 2 158 ? 7.052   -9.486  -5.420  0.80 47.14  ? 158 GLU B C     1 
ATOM   9189  O  O     A GLU B 2 158 ? 5.646   -10.140 -5.791  0.20 47.27  ? 158 GLU B O     1 
ATOM   9190  O  O     B GLU B 2 158 ? 5.820   -9.519  -5.334  0.80 48.85  ? 158 GLU B O     1 
ATOM   9191  C  CB    A GLU B 2 158 ? 7.517   -10.747 -8.119  0.20 47.15  ? 158 GLU B CB    1 
ATOM   9192  C  CB    B GLU B 2 158 ? 7.594   -10.229 -7.730  0.80 46.04  ? 158 GLU B CB    1 
ATOM   9193  C  CG    A GLU B 2 158 ? 8.052   -10.411 -9.504  0.20 49.35  ? 158 GLU B CG    1 
ATOM   9194  C  CG    B GLU B 2 158 ? 6.190   -10.447 -8.264  0.80 58.24  ? 158 GLU B CG    1 
ATOM   9195  C  CD    A GLU B 2 158 ? 7.878   -11.543 -10.499 0.20 52.06  ? 158 GLU B CD    1 
ATOM   9196  C  CD    B GLU B 2 158 ? 6.137   -11.458 -9.388  0.80 57.49  ? 158 GLU B CD    1 
ATOM   9197  O  OE1   A GLU B 2 158 ? 7.089   -12.470 -10.222 0.20 52.94  ? 158 GLU B OE1   1 
ATOM   9198  O  OE1   B GLU B 2 158 ? 7.196   -11.736 -9.992  0.80 54.89  ? 158 GLU B OE1   1 
ATOM   9199  O  OE2   A GLU B 2 158 ? 8.532   -11.502 -11.563 0.20 51.97  ? 158 GLU B OE2   1 
ATOM   9200  O  OE2   B GLU B 2 158 ? 5.031   -11.971 -9.671  0.80 58.45  ? 158 GLU B OE2   1 
ATOM   9201  N  N     A TYR B 2 159 ? 7.656   -10.094 -4.777  0.20 45.48  ? 159 TYR B N     1 
ATOM   9202  N  N     B TYR B 2 159 ? 7.848   -9.808  -4.404  0.80 44.43  ? 159 TYR B N     1 
ATOM   9203  C  CA    A TYR B 2 159 ? 7.144   -10.400 -3.440  0.20 43.56  ? 159 TYR B CA    1 
ATOM   9204  C  CA    B TYR B 2 159 ? 7.346   -10.199 -3.086  0.80 43.71  ? 159 TYR B CA    1 
ATOM   9205  C  C     A TYR B 2 159 ? 7.942   -9.597  -2.422  0.20 41.14  ? 159 TYR B C     1 
ATOM   9206  C  C     B TYR B 2 159 ? 8.066   -9.388  -2.016  0.80 37.45  ? 159 TYR B C     1 
ATOM   9207  O  O     A TYR B 2 159 ? 8.737   -10.149 -1.652  0.20 41.28  ? 159 TYR B O     1 
ATOM   9208  O  O     B TYR B 2 159 ? 8.800   -9.937  -1.188  0.80 41.48  ? 159 TYR B O     1 
ATOM   9209  C  CB    A TYR B 2 159 ? 7.231   -11.900 -3.147  0.20 43.03  ? 159 TYR B CB    1 
ATOM   9210  C  CB    B TYR B 2 159 ? 7.533   -11.698 -2.853  0.80 43.26  ? 159 TYR B CB    1 
ATOM   9211  C  CG    A TYR B 2 159 ? 6.708   -12.789 -4.252  0.20 44.49  ? 159 TYR B CG    1 
ATOM   9212  C  CG    B TYR B 2 159 ? 6.793   -12.572 -3.838  0.80 43.82  ? 159 TYR B CG    1 
ATOM   9213  C  CD1   A TYR B 2 159 ? 5.362   -13.124 -4.325  0.20 45.07  ? 159 TYR B CD1   1 
ATOM   9214  C  CD1   B TYR B 2 159 ? 5.481   -12.961 -3.603  0.80 43.81  ? 159 TYR B CD1   1 
ATOM   9215  C  CD2   A TYR B 2 159 ? 7.564   -13.299 -5.219  0.20 43.82  ? 159 TYR B CD2   1 
ATOM   9216  C  CD2   B TYR B 2 159 ? 7.406   -13.005 -5.008  0.80 43.01  ? 159 TYR B CD2   1 
ATOM   9217  C  CE1   A TYR B 2 159 ? 4.883   -13.940 -5.334  0.20 46.22  ? 159 TYR B CE1   1 
ATOM   9218  C  CE1   B TYR B 2 159 ? 4.797   -13.756 -4.504  0.80 45.03  ? 159 TYR B CE1   1 
ATOM   9219  C  CE2   A TYR B 2 159 ? 7.096   -14.116 -6.230  0.20 45.81  ? 159 TYR B CE2   1 
ATOM   9220  C  CE2   B TYR B 2 159 ? 6.733   -13.805 -5.914  0.80 47.93  ? 159 TYR B CE2   1 
ATOM   9221  C  CZ    A TYR B 2 159 ? 5.756   -14.434 -6.284  0.20 48.70  ? 159 TYR B CZ    1 
ATOM   9222  C  CZ    B TYR B 2 159 ? 5.427   -14.176 -5.656  0.80 48.39  ? 159 TYR B CZ    1 
ATOM   9223  O  OH    A TYR B 2 159 ? 5.291   -15.247 -7.292  0.20 50.62  ? 159 TYR B OH    1 
ATOM   9224  O  OH    B TYR B 2 159 ? 4.753   -14.969 -6.555  0.80 58.82  ? 159 TYR B OH    1 
ATOM   9225  N  N     A PRO B 2 160 ? 7.747   -8.275  -2.387  0.20 42.94  ? 160 PRO B N     1 
ATOM   9226  N  N     B PRO B 2 160 ? 7.872   -8.066  -2.000  0.80 42.58  ? 160 PRO B N     1 
ATOM   9227  C  CA    A PRO B 2 160 ? 8.563   -7.440  -1.490  0.20 44.27  ? 160 PRO B CA    1 
ATOM   9228  C  CA    B PRO B 2 160 ? 8.703   -7.211  -1.136  0.80 44.00  ? 160 PRO B CA    1 
ATOM   9229  C  C     A PRO B 2 160 ? 8.214   -7.602  -0.023  0.20 45.51  ? 160 PRO B C     1 
ATOM   9230  C  C     B PRO B 2 160 ? 8.375   -7.307  0.344   0.80 47.59  ? 160 PRO B C     1 
ATOM   9231  O  O     A PRO B 2 160 ? 9.005   -7.185  0.833   0.20 48.03  ? 160 PRO B O     1 
ATOM   9232  O  O     B PRO B 2 160 ? 9.123   -6.749  1.157   0.80 52.42  ? 160 PRO B O     1 
ATOM   9233  C  CB    A PRO B 2 160 ? 8.268   -6.016  -1.978  0.20 44.68  ? 160 PRO B CB    1 
ATOM   9234  C  CB    B PRO B 2 160 ? 8.427   -5.801  -1.672  0.80 44.92  ? 160 PRO B CB    1 
ATOM   9235  C  CG    A PRO B 2 160 ? 6.887   -6.102  -2.531  0.20 42.13  ? 160 PRO B CG    1 
ATOM   9236  C  CG    B PRO B 2 160 ? 7.055   -5.883  -2.240  0.80 39.98  ? 160 PRO B CG    1 
ATOM   9237  C  CD    A PRO B 2 160 ? 6.752   -7.481  -3.131  0.20 44.86  ? 160 PRO B CD    1 
ATOM   9238  C  CD    B PRO B 2 160 ? 6.884   -7.284  -2.769  0.80 45.81  ? 160 PRO B CD    1 
ATOM   9239  N  N     A ASP B 2 161 ? 7.065   -8.191  0.297   0.20 44.35  ? 161 ASP B N     1 
ATOM   9240  N  N     B ASP B 2 161 ? 7.296   -7.985  0.732   0.80 44.32  ? 161 ASP B N     1 
ATOM   9241  C  CA    A ASP B 2 161 ? 6.621   -8.354  1.673   0.20 43.01  ? 161 ASP B CA    1 
ATOM   9242  C  CA    B ASP B 2 161 ? 6.946   -8.088  2.139   0.80 42.02  ? 161 ASP B CA    1 
ATOM   9243  C  C     A ASP B 2 161 ? 6.925   -9.739  2.233   0.20 41.78  ? 161 ASP B C     1 
ATOM   9244  C  C     B ASP B 2 161 ? 7.186   -9.482  2.704   0.80 40.69  ? 161 ASP B C     1 
ATOM   9245  O  O     A ASP B 2 161 ? 6.444   -10.072 3.319   0.20 39.40  ? 161 ASP B O     1 
ATOM   9246  O  O     B ASP B 2 161 ? 6.820   -9.740  3.849   0.80 40.09  ? 161 ASP B O     1 
ATOM   9247  C  CB    A ASP B 2 161 ? 5.122   -8.070  1.774   0.20 46.66  ? 161 ASP B CB    1 
ATOM   9248  C  CB    B ASP B 2 161 ? 5.490   -7.669  2.355   0.80 47.64  ? 161 ASP B CB    1 
ATOM   9249  C  CG    A ASP B 2 161 ? 4.315   -8.838  0.744   0.20 47.14  ? 161 ASP B CG    1 
ATOM   9250  C  CG    B ASP B 2 161 ? 4.500   -8.657  1.772   0.80 47.65  ? 161 ASP B CG    1 
ATOM   9251  O  OD1   A ASP B 2 161 ? 4.749   -8.902  -0.428  0.20 41.36  ? 161 ASP B OD1   1 
ATOM   9252  O  OD1   B ASP B 2 161 ? 4.794   -9.282  0.728   0.80 48.95  ? 161 ASP B OD1   1 
ATOM   9253  O  OD2   A ASP B 2 161 ? 3.251   -9.384  1.105   0.20 46.41  ? 161 ASP B OD2   1 
ATOM   9254  O  OD2   B ASP B 2 161 ? 3.418   -8.815  2.369   0.80 53.95  ? 161 ASP B OD2   1 
ATOM   9255  N  N     A ARG B 2 162 ? 7.701   -10.550 1.521   0.20 38.83  ? 162 ARG B N     1 
ATOM   9256  N  N     B ARG B 2 162 ? 7.780   -10.384 1.936   0.80 35.06  ? 162 ARG B N     1 
ATOM   9257  C  CA    A ARG B 2 162 ? 8.040   -11.896 1.958   0.20 36.69  ? 162 ARG B CA    1 
ATOM   9258  C  CA    B ARG B 2 162 ? 8.084   -11.728 2.402   0.80 33.53  ? 162 ARG B CA    1 
ATOM   9259  C  C     A ARG B 2 162 ? 9.531   -11.992 2.255   0.20 38.06  ? 162 ARG B C     1 
ATOM   9260  C  C     B ARG B 2 162 ? 9.568   -11.851 2.734   0.80 36.34  ? 162 ARG B C     1 
ATOM   9261  O  O     A ARG B 2 162 ? 10.353  -11.323 1.622   0.20 36.37  ? 162 ARG B O     1 
ATOM   9262  O  O     B ARG B 2 162 ? 10.405  -11.092 2.239   0.80 43.03  ? 162 ARG B O     1 
ATOM   9263  C  CB    A ARG B 2 162 ? 7.648   -12.935 0.902   0.20 38.01  ? 162 ARG B CB    1 
ATOM   9264  C  CB    B ARG B 2 162 ? 7.704   -12.774 1.350   0.80 36.45  ? 162 ARG B CB    1 
ATOM   9265  C  CG    A ARG B 2 162 ? 6.181   -12.902 0.480   0.20 40.97  ? 162 ARG B CG    1 
ATOM   9266  C  CG    B ARG B 2 162 ? 6.336   -12.594 0.710   0.80 42.71  ? 162 ARG B CG    1 
ATOM   9267  C  CD    A ARG B 2 162 ? 5.235   -13.337 1.601   0.20 36.98  ? 162 ARG B CD    1 
ATOM   9268  C  CD    B ARG B 2 162 ? 5.209   -12.845 1.707   0.80 33.66  ? 162 ARG B CD    1 
ATOM   9269  N  NE    A ARG B 2 162 ? 4.950   -12.266 2.549   0.20 45.07  ? 162 ARG B NE    1 
ATOM   9270  N  NE    B ARG B 2 162 ? 4.815   -11.636 2.423   0.80 51.77  ? 162 ARG B NE    1 
ATOM   9271  C  CZ    A ARG B 2 162 ? 4.143   -12.384 3.596   0.20 44.42  ? 162 ARG B CZ    1 
ATOM   9272  C  CZ    B ARG B 2 162 ? 4.021   -11.619 3.487   0.80 42.19  ? 162 ARG B CZ    1 
ATOM   9273  N  NH1   A ARG B 2 162 ? 3.511   -13.516 3.859   0.20 43.25  ? 162 ARG B NH1   1 
ATOM   9274  N  NH1   B ARG B 2 162 ? 3.527   -12.735 4.000   0.80 45.91  ? 162 ARG B NH1   1 
ATOM   9275  N  NH2   A ARG B 2 162 ? 3.965   -11.338 4.398   0.20 46.20  ? 162 ARG B NH2   1 
ATOM   9276  N  NH2   B ARG B 2 162 ? 3.722   -10.454 4.057   0.80 50.13  ? 162 ARG B NH2   1 
ATOM   9277  N  N     A ILE B 2 163 ? 9.870   -12.845 3.219   0.20 33.10  ? 163 ILE B N     1 
ATOM   9278  N  N     B ILE B 2 163 ? 9.890   -12.855 3.541   0.80 32.71  ? 163 ILE B N     1 
ATOM   9279  C  CA    A ILE B 2 163 ? 11.239  -12.962 3.710   0.20 33.69  ? 163 ILE B CA    1 
ATOM   9280  C  CA    B ILE B 2 163 ? 11.247  -13.028 4.057   0.80 35.09  ? 163 ILE B CA    1 
ATOM   9281  C  C     A ILE B 2 163 ? 12.061  -13.807 2.746   0.20 30.22  ? 163 ILE B C     1 
ATOM   9282  C  C     B ILE B 2 163 ? 12.099  -13.775 3.041   0.80 29.18  ? 163 ILE B C     1 
ATOM   9283  O  O     A ILE B 2 163 ? 11.555  -14.754 2.133   0.20 32.69  ? 163 ILE B O     1 
ATOM   9284  O  O     B ILE B 2 163 ? 11.707  -14.833 2.538   0.80 33.63  ? 163 ILE B O     1 
ATOM   9285  C  CB    A ILE B 2 163 ? 11.245  -13.556 5.130   0.20 31.28  ? 163 ILE B CB    1 
ATOM   9286  C  CB    B ILE B 2 163 ? 11.226  -13.778 5.398   0.80 30.40  ? 163 ILE B CB    1 
ATOM   9287  C  CG1   A ILE B 2 163 ? 10.318  -12.749 6.040   0.20 33.55  ? 163 ILE B CG1   1 
ATOM   9288  C  CG1   B ILE B 2 163 ? 10.616  -12.904 6.495   0.80 34.52  ? 163 ILE B CG1   1 
ATOM   9289  C  CG2   A ILE B 2 163 ? 12.654  -13.583 5.709   0.20 31.39  ? 163 ILE B CG2   1 
ATOM   9290  C  CG2   B ILE B 2 163 ? 12.618  -14.230 5.785   0.80 31.22  ? 163 ILE B CG2   1 
ATOM   9291  C  CD1   A ILE B 2 163 ? 10.672  -11.281 6.123   0.20 31.24  ? 163 ILE B CD1   1 
ATOM   9292  C  CD1   B ILE B 2 163 ? 11.323  -11.595 6.696   0.80 27.04  ? 163 ILE B CD1   1 
ATOM   9293  N  N     A MET B 2 164 ? 13.340  -13.465 2.609   0.20 30.79  ? 164 MET B N     1 
ATOM   9294  N  N     B MET B 2 164 ? 13.294  -13.253 2.773   0.80 30.32  ? 164 MET B N     1 
ATOM   9295  C  CA    A MET B 2 164 ? 14.263  -14.173 1.728   0.20 29.84  ? 164 MET B CA    1 
ATOM   9296  C  CA    B MET B 2 164 ? 14.259  -13.916 1.906   0.80 29.94  ? 164 MET B CA    1 
ATOM   9297  C  C     A MET B 2 164 ? 15.397  -14.731 2.578   0.20 28.98  ? 164 MET B C     1 
ATOM   9298  C  C     B MET B 2 164 ? 15.428  -14.389 2.754   0.80 28.75  ? 164 MET B C     1 
ATOM   9299  O  O     A MET B 2 164 ? 16.170  -13.968 3.168   0.20 27.60  ? 164 MET B O     1 
ATOM   9300  O  O     B MET B 2 164 ? 16.104  -13.578 3.396   0.80 24.42  ? 164 MET B O     1 
ATOM   9301  C  CB    A MET B 2 164 ? 14.795  -13.244 0.637   0.20 29.10  ? 164 MET B CB    1 
ATOM   9302  C  CB    B MET B 2 164 ? 14.751  -12.992 0.800   0.80 27.60  ? 164 MET B CB    1 
ATOM   9303  C  CG    A MET B 2 164 ? 15.651  -13.928 -0.420  0.20 32.79  ? 164 MET B CG    1 
ATOM   9304  C  CG    B MET B 2 164 ? 15.913  -13.585 0.026   0.80 34.70  ? 164 MET B CG    1 
ATOM   9305  S  SD    A MET B 2 164 ? 14.736  -15.105 -1.437  0.20 32.99  ? 164 MET B SD    1 
ATOM   9306  S  SD    B MET B 2 164 ? 15.465  -15.123 -0.790  0.80 42.01  ? 164 MET B SD    1 
ATOM   9307  C  CE    A MET B 2 164 ? 13.446  -14.054 -2.103  0.20 34.60  ? 164 MET B CE    1 
ATOM   9308  C  CE    B MET B 2 164 ? 14.404  -14.482 -2.080  0.80 37.55  ? 164 MET B CE    1 
ATOM   9309  N  N     A ASN B 2 165 ? 15.485  -16.056 2.651   0.20 28.56  ? 165 ASN B N     1 
ATOM   9310  N  N     B ASN B 2 165 ? 15.667  -15.693 2.725   0.80 25.51  ? 165 ASN B N     1 
ATOM   9311  C  CA    A ASN B 2 165 ? 16.532  -16.746 3.392   0.20 29.67  ? 165 ASN B CA    1 
ATOM   9312  C  CA    B ASN B 2 165 ? 16.611  -16.388 3.581   0.80 29.69  ? 165 ASN B CA    1 
ATOM   9313  C  C     A ASN B 2 165 ? 17.365  -17.561 2.416   0.20 30.50  ? 165 ASN B C     1 
ATOM   9314  C  C     B ASN B 2 165 ? 17.479  -17.273 2.697   0.80 30.56  ? 165 ASN B C     1 
ATOM   9315  O  O     A ASN B 2 165 ? 16.815  -18.288 1.582   0.20 29.41  ? 165 ASN B O     1 
ATOM   9316  O  O     B ASN B 2 165 ? 16.975  -17.916 1.770   0.80 30.33  ? 165 ASN B O     1 
ATOM   9317  C  CB    A ASN B 2 165 ? 15.942  -17.652 4.477   0.20 30.52  ? 165 ASN B CB    1 
ATOM   9318  C  CB    B ASN B 2 165 ? 15.845  -17.198 4.639   0.80 30.90  ? 165 ASN B CB    1 
ATOM   9319  C  CG    A ASN B 2 165 ? 17.008  -18.401 5.256   0.20 31.22  ? 165 ASN B CG    1 
ATOM   9320  C  CG    B ASN B 2 165 ? 16.674  -18.291 5.272   0.80 30.86  ? 165 ASN B CG    1 
ATOM   9321  O  OD1   A ASN B 2 165 ? 17.263  -19.579 5.011   0.20 31.92  ? 165 ASN B OD1   1 
ATOM   9322  O  OD1   B ASN B 2 165 ? 16.243  -19.439 5.340   0.80 38.55  ? 165 ASN B OD1   1 
ATOM   9323  N  ND2   A ASN B 2 165 ? 17.639  -17.717 6.201   0.20 32.60  ? 165 ASN B ND2   1 
ATOM   9324  N  ND2   B ASN B 2 165 ? 17.858  -17.943 5.754   0.80 35.87  ? 165 ASN B ND2   1 
ATOM   9325  N  N     A THR B 2 166 ? 18.685  -17.431 2.512   0.20 30.92  ? 166 THR B N     1 
ATOM   9326  N  N     B THR B 2 166 ? 18.786  -17.275 2.943   0.80 30.52  ? 166 THR B N     1 
ATOM   9327  C  CA    A THR B 2 166 ? 19.601  -18.152 1.644   0.20 28.80  ? 166 THR B CA    1 
ATOM   9328  C  CA    B THR B 2 166 ? 19.693  -18.073 2.128   0.80 30.00  ? 166 THR B CA    1 
ATOM   9329  C  C     A THR B 2 166 ? 20.555  -18.992 2.481   0.20 27.72  ? 166 THR B C     1 
ATOM   9330  C  C     B THR B 2 166 ? 20.598  -18.913 3.012   0.80 31.02  ? 166 THR B C     1 
ATOM   9331  O  O     A THR B 2 166 ? 20.915  -18.621 3.603   0.20 30.29  ? 166 THR B O     1 
ATOM   9332  O  O     B THR B 2 166 ? 20.932  -18.534 4.144   0.80 26.44  ? 166 THR B O     1 
ATOM   9333  C  CB    A THR B 2 166 ? 20.403  -17.197 0.741   0.20 30.26  ? 166 THR B CB    1 
ATOM   9334  C  CB    B THR B 2 166 ? 20.578  -17.211 1.179   0.80 29.68  ? 166 THR B CB    1 
ATOM   9335  O  OG1   A THR B 2 166 ? 21.321  -16.430 1.530   0.20 27.80  ? 166 THR B OG1   1 
ATOM   9336  O  OG1   B THR B 2 166 ? 21.571  -16.499 1.930   0.80 27.70  ? 166 THR B OG1   1 
ATOM   9337  C  CG2   A THR B 2 166 ? 19.468  -16.253 0.000   0.20 31.94  ? 166 THR B CG2   1 
ATOM   9338  C  CG2   B THR B 2 166 ? 19.734  -16.227 0.381   0.80 34.00  ? 166 THR B CG2   1 
ATOM   9339  N  N     A PHE B 2 167 ? 20.949  -20.136 1.927   0.20 27.06  ? 167 PHE B N     1 
ATOM   9340  N  N     B PHE B 2 167 ? 20.964  -20.077 2.479   0.80 28.42  ? 167 PHE B N     1 
ATOM   9341  C  CA    A PHE B 2 167 ? 21.922  -21.037 2.541   0.20 26.75  ? 167 PHE B CA    1 
ATOM   9342  C  CA    B PHE B 2 167 ? 22.084  -20.875 2.960   0.80 25.80  ? 167 PHE B CA    1 
ATOM   9343  C  C     A PHE B 2 167 ? 23.198  -20.976 1.706   0.20 27.43  ? 167 PHE B C     1 
ATOM   9344  C  C     B PHE B 2 167 ? 23.161  -20.732 1.893   0.80 26.87  ? 167 PHE B C     1 
ATOM   9345  O  O     A PHE B 2 167 ? 23.508  -21.886 0.936   0.20 26.72  ? 167 PHE B O     1 
ATOM   9346  O  O     B PHE B 2 167 ? 22.967  -21.172 0.754   0.80 29.14  ? 167 PHE B O     1 
ATOM   9347  C  CB    A PHE B 2 167 ? 21.373  -22.468 2.630   0.20 27.52  ? 167 PHE B CB    1 
ATOM   9348  C  CB    B PHE B 2 167 ? 21.691  -22.338 3.159   0.80 29.18  ? 167 PHE B CB    1 
ATOM   9349  C  CG    A PHE B 2 167 ? 20.394  -22.674 3.750   0.20 31.38  ? 167 PHE B CG    1 
ATOM   9350  C  CG    B PHE B 2 167 ? 20.563  -22.544 4.137   0.80 31.33  ? 167 PHE B CG    1 
ATOM   9351  C  CD1   A PHE B 2 167 ? 20.829  -23.081 5.000   0.20 30.10  ? 167 PHE B CD1   1 
ATOM   9352  C  CD1   B PHE B 2 167 ? 19.241  -22.352 3.753   0.80 26.62  ? 167 PHE B CD1   1 
ATOM   9353  C  CD2   A PHE B 2 167 ? 19.040  -22.465 3.552   0.20 27.64  ? 167 PHE B CD2   1 
ATOM   9354  C  CD2   B PHE B 2 167 ? 20.825  -22.959 5.429   0.80 31.72  ? 167 PHE B CD2   1 
ATOM   9355  C  CE1   A PHE B 2 167 ? 19.930  -23.275 6.036   0.20 32.70  ? 167 PHE B CE1   1 
ATOM   9356  C  CE1   B PHE B 2 167 ? 18.196  -22.548 4.669   0.80 29.53  ? 167 PHE B CE1   1 
ATOM   9357  C  CE2   A PHE B 2 167 ? 18.135  -22.657 4.586   0.20 29.83  ? 167 PHE B CE2   1 
ATOM   9358  C  CE2   B PHE B 2 167 ? 19.794  -23.162 6.344   0.80 33.33  ? 167 PHE B CE2   1 
ATOM   9359  C  CZ    A PHE B 2 167 ? 18.581  -23.062 5.827   0.20 32.28  ? 167 PHE B CZ    1 
ATOM   9360  C  CZ    B PHE B 2 167 ? 18.477  -22.956 5.959   0.80 32.28  ? 167 PHE B CZ    1 
ATOM   9361  N  N     A SER B 2 168 ? 23.950  -19.890 1.879   0.20 28.98  ? 168 SER B N     1 
ATOM   9362  N  N     B SER B 2 168 ? 24.285  -20.104 2.248   0.80 27.45  ? 168 SER B N     1 
ATOM   9363  C  CA    A SER B 2 168 ? 25.100  -19.606 1.032   0.20 24.80  ? 168 SER B CA    1 
ATOM   9364  C  CA    B SER B 2 168 ? 25.254  -19.624 1.262   0.80 23.35  ? 168 SER B CA    1 
ATOM   9365  C  C     A SER B 2 168 ? 26.308  -20.446 1.433   0.20 26.54  ? 168 SER B C     1 
ATOM   9366  C  C     B SER B 2 168 ? 26.631  -20.176 1.607   0.80 25.34  ? 168 SER B C     1 
ATOM   9367  O  O     A SER B 2 168 ? 26.563  -20.675 2.619   0.20 27.30  ? 168 SER B O     1 
ATOM   9368  O  O     B SER B 2 168 ? 27.213  -19.803 2.629   0.80 22.53  ? 168 SER B O     1 
ATOM   9369  C  CB    A SER B 2 168 ? 25.457  -18.121 1.105   0.20 28.42  ? 168 SER B CB    1 
ATOM   9370  C  CB    B SER B 2 168 ? 25.282  -18.093 1.226   0.80 28.38  ? 168 SER B CB    1 
ATOM   9371  O  OG    A SER B 2 168 ? 24.342  -17.302 0.793   0.20 30.62  ? 168 SER B OG    1 
ATOM   9372  O  OG    B SER B 2 168 ? 24.026  -17.527 0.889   0.80 32.35  ? 168 SER B OG    1 
ATOM   9373  N  N     A VAL B 2 169 ? 27.062  -20.889 0.432   0.20 29.38  ? 169 VAL B N     1 
ATOM   9374  N  N     B VAL B 2 169 ? 27.158  -21.045 0.754   0.80 29.86  ? 169 VAL B N     1 
ATOM   9375  C  CA    A VAL B 2 169 ? 28.252  -21.706 0.635   0.20 28.54  ? 169 VAL B CA    1 
ATOM   9376  C  CA    B VAL B 2 169 ? 28.395  -21.765 1.031   0.80 26.77  ? 169 VAL B CA    1 
ATOM   9377  C  C     A VAL B 2 169 ? 29.469  -20.852 0.308   0.20 27.71  ? 169 VAL B C     1 
ATOM   9378  C  C     B VAL B 2 169 ? 29.555  -20.923 0.503   0.80 26.82  ? 169 VAL B C     1 
ATOM   9379  O  O     A VAL B 2 169 ? 29.633  -20.399 -0.832  0.20 31.35  ? 169 VAL B O     1 
ATOM   9380  O  O     B VAL B 2 169 ? 29.597  -20.600 -0.687  0.80 31.98  ? 169 VAL B O     1 
ATOM   9381  C  CB    A VAL B 2 169 ? 28.219  -22.983 -0.219  0.20 27.31  ? 169 VAL B CB    1 
ATOM   9382  C  CB    B VAL B 2 169 ? 28.371  -23.168 0.400   0.80 26.32  ? 169 VAL B CB    1 
ATOM   9383  C  CG1   A VAL B 2 169 ? 29.565  -23.683 -0.177  0.20 29.33  ? 169 VAL B CG1   1 
ATOM   9384  C  CG1   B VAL B 2 169 ? 29.675  -23.891 0.619   0.80 27.19  ? 169 VAL B CG1   1 
ATOM   9385  C  CG2   A VAL B 2 169 ? 27.124  -23.911 0.272   0.20 28.74  ? 169 VAL B CG2   1 
ATOM   9386  C  CG2   B VAL B 2 169 ? 27.241  -23.981 0.990   0.80 31.52  ? 169 VAL B CG2   1 
ATOM   9387  N  N     A MET B 2 170 ? 30.314  -20.624 1.312   0.20 29.23  ? 170 MET B N     1 
ATOM   9388  N  N     B MET B 2 170 ? 30.477  -20.534 1.405   0.80 29.59  ? 170 MET B N     1 
ATOM   9389  C  CA    A MET B 2 170 ? 31.523  -19.830 1.154   0.20 30.19  ? 170 MET B CA    1 
ATOM   9390  C  CA    B MET B 2 170 ? 31.563  -19.614 1.060   0.80 30.48  ? 170 MET B CA    1 
ATOM   9391  C  C     A MET B 2 170 ? 32.626  -20.676 0.521   0.20 27.44  ? 170 MET B C     1 
ATOM   9392  C  C     B MET B 2 170 ? 32.785  -20.402 0.604   0.80 25.98  ? 170 MET B C     1 
ATOM   9393  O  O     A MET B 2 170 ? 32.806  -21.838 0.898   0.20 27.96  ? 170 MET B O     1 
ATOM   9394  O  O     B MET B 2 170 ? 33.107  -21.433 1.212   0.80 26.55  ? 170 MET B O     1 
ATOM   9395  C  CB    A MET B 2 170 ? 31.995  -19.298 2.506   0.20 30.10  ? 170 MET B CB    1 
ATOM   9396  C  CB    B MET B 2 170 ? 31.951  -18.759 2.276   0.80 33.40  ? 170 MET B CB    1 
ATOM   9397  C  CG    A MET B 2 170 ? 30.934  -18.555 3.287   0.20 32.39  ? 170 MET B CG    1 
ATOM   9398  C  CG    B MET B 2 170 ? 30.813  -18.449 3.208   0.80 32.57  ? 170 MET B CG    1 
ATOM   9399  S  SD    A MET B 2 170 ? 30.411  -17.050 2.454   0.20 26.88  ? 170 MET B SD    1 
ATOM   9400  S  SD    B MET B 2 170 ? 29.604  -17.348 2.466   0.80 60.44  ? 170 MET B SD    1 
ATOM   9401  C  CE    A MET B 2 170 ? 29.071  -16.516 3.523   0.20 34.89  ? 170 MET B CE    1 
ATOM   9402  C  CE    B MET B 2 170 ? 30.405  -15.759 2.670   0.80 41.12  ? 170 MET B CE    1 
ATOM   9403  N  N     A PRO B 2 171 ? 33.368  -20.128 -0.435  0.20 28.92  ? 171 PRO B N     1 
ATOM   9404  N  N     B PRO B 2 171 ? 33.505  -19.936 -0.416  0.80 29.36  ? 171 PRO B N     1 
ATOM   9405  C  CA    A PRO B 2 171 ? 34.466  -20.880 -1.051  0.20 27.67  ? 171 PRO B CA    1 
ATOM   9406  C  CA    B PRO B 2 171 ? 34.591  -20.749 -0.981  0.80 27.37  ? 171 PRO B CA    1 
ATOM   9407  C  C     A PRO B 2 171 ? 35.708  -20.884 -0.168  0.20 27.93  ? 171 PRO B C     1 
ATOM   9408  C  C     B PRO B 2 171 ? 35.820  -20.826 -0.089  0.80 27.59  ? 171 PRO B C     1 
ATOM   9409  O  O     A PRO B 2 171 ? 35.811  -20.159 0.820   0.20 28.23  ? 171 PRO B O     1 
ATOM   9410  O  O     B PRO B 2 171 ? 36.140  -19.898 0.653   0.80 28.93  ? 171 PRO B O     1 
ATOM   9411  C  CB    A PRO B 2 171 ? 34.722  -20.122 -2.358  0.20 26.54  ? 171 PRO B CB    1 
ATOM   9412  C  CB    B PRO B 2 171 ? 34.926  -20.032 -2.292  0.80 25.53  ? 171 PRO B CB    1 
ATOM   9413  C  CG    A PRO B 2 171 ? 34.330  -18.722 -2.049  0.20 26.07  ? 171 PRO B CG    1 
ATOM   9414  C  CG    B PRO B 2 171 ? 34.561  -18.623 -2.071  0.80 24.39  ? 171 PRO B CG    1 
ATOM   9415  C  CD    A PRO B 2 171 ? 33.162  -18.820 -1.083  0.20 27.90  ? 171 PRO B CD    1 
ATOM   9416  C  CD    B PRO B 2 171 ? 33.304  -18.681 -1.167  0.80 28.20  ? 171 PRO B CD    1 
ATOM   9417  N  N     A SER B 2 172 ? 36.668  -21.724 -0.558  0.20 30.40  ? 172 SER B N     1 
ATOM   9418  N  N     B SER B 2 172 ? 36.545  -21.942 -0.212  0.80 30.62  ? 172 SER B N     1 
ATOM   9419  C  CA    A SER B 2 172 ? 37.943  -21.821 0.141   0.20 29.73  ? 172 SER B CA    1 
ATOM   9420  C  CA    B SER B 2 172 ? 37.841  -22.115 0.436   0.80 29.38  ? 172 SER B CA    1 
ATOM   9421  C  C     A SER B 2 172 ? 38.952  -22.588 -0.704  0.20 31.20  ? 172 SER B C     1 
ATOM   9422  C  C     B SER B 2 172 ? 38.852  -22.689 -0.549  0.80 31.43  ? 172 SER B C     1 
ATOM   9423  O  O     A SER B 2 172 ? 38.584  -23.553 -1.387  0.20 28.02  ? 172 SER B O     1 
ATOM   9424  O  O     B SER B 2 172 ? 38.546  -23.678 -1.244  0.80 26.42  ? 172 SER B O     1 
ATOM   9425  C  CB    A SER B 2 172 ? 37.774  -22.506 1.497   0.20 29.72  ? 172 SER B CB    1 
ATOM   9426  C  CB    B SER B 2 172 ? 37.738  -23.040 1.637   0.80 31.35  ? 172 SER B CB    1 
ATOM   9427  O  OG    A SER B 2 172 ? 39.015  -22.586 2.178   0.20 27.19  ? 172 SER B OG    1 
ATOM   9428  O  OG    B SER B 2 172 ? 39.033  -23.471 2.037   0.80 29.14  ? 172 SER B OG    1 
ATOM   9429  N  N     A PRO B 2 173 ? 40.230  -22.197 -0.678  0.20 31.00  ? 173 PRO B N     1 
ATOM   9430  N  N     B PRO B 2 173 ? 40.071  -22.138 -0.608  0.80 30.93  ? 173 PRO B N     1 
ATOM   9431  C  CA    A PRO B 2 173 ? 41.238  -22.927 -1.464  0.20 32.22  ? 173 PRO B CA    1 
ATOM   9432  C  CA    B PRO B 2 173 ? 41.131  -22.766 -1.418  0.80 31.93  ? 173 PRO B CA    1 
ATOM   9433  C  C     A PRO B 2 173 ? 41.498  -24.340 -0.969  0.20 33.72  ? 173 PRO B C     1 
ATOM   9434  C  C     B PRO B 2 173 ? 41.439  -24.197 -1.018  0.80 33.62  ? 173 PRO B C     1 
ATOM   9435  O  O     A PRO B 2 173 ? 42.078  -25.138 -1.718  0.20 35.38  ? 173 PRO B O     1 
ATOM   9436  O  O     B PRO B 2 173 ? 41.972  -24.951 -1.844  0.80 35.80  ? 173 PRO B O     1 
ATOM   9437  C  CB    A PRO B 2 173 ? 42.496  -22.055 -1.326  0.20 34.93  ? 173 PRO B CB    1 
ATOM   9438  C  CB    B PRO B 2 173 ? 42.347  -21.856 -1.180  0.80 36.22  ? 173 PRO B CB    1 
ATOM   9439  C  CG    A PRO B 2 173 ? 42.008  -20.719 -0.853  0.20 33.56  ? 173 PRO B CG    1 
ATOM   9440  C  CG    B PRO B 2 173 ? 41.792  -20.556 -0.716  0.80 35.09  ? 173 PRO B CG    1 
ATOM   9441  C  CD    A PRO B 2 173 ? 40.788  -21.000 -0.030  0.20 28.87  ? 173 PRO B CD    1 
ATOM   9442  C  CD    B PRO B 2 173 ? 40.519  -20.892 0.038   0.80 26.41  ? 173 PRO B CD    1 
ATOM   9443  N  N     A LYS B 2 174 ? 41.101  -24.677 0.260   0.20 32.09  ? 174 LYS B N     1 
ATOM   9444  N  N     B LYS B 2 174 ? 41.141  -24.589 0.224   0.80 32.20  ? 174 LYS B N     1 
ATOM   9445  C  CA    A LYS B 2 174 ? 41.348  -26.016 0.784   0.20 33.12  ? 174 LYS B CA    1 
ATOM   9446  C  CA    B LYS B 2 174 ? 41.393  -25.953 0.674   0.80 32.71  ? 174 LYS B CA    1 
ATOM   9447  C  C     A LYS B 2 174 ? 40.485  -27.075 0.108   0.20 37.24  ? 174 LYS B C     1 
ATOM   9448  C  C     B LYS B 2 174 ? 40.482  -26.970 -0.006  0.80 37.64  ? 174 LYS B C     1 
ATOM   9449  O  O     A LYS B 2 174 ? 40.857  -28.253 0.112   0.20 36.90  ? 174 LYS B O     1 
ATOM   9450  O  O     B LYS B 2 174 ? 40.830  -28.156 -0.064  0.80 36.79  ? 174 LYS B O     1 
ATOM   9451  C  CB    A LYS B 2 174 ? 41.115  -26.044 2.298   0.20 36.90  ? 174 LYS B CB    1 
ATOM   9452  C  CB    B LYS B 2 174 ? 41.223  -26.049 2.199   0.80 37.24  ? 174 LYS B CB    1 
ATOM   9453  C  CG    A LYS B 2 174 ? 42.069  -25.164 3.097   0.20 33.98  ? 174 LYS B CG    1 
ATOM   9454  C  CG    B LYS B 2 174 ? 42.201  -25.191 3.007   0.80 33.59  ? 174 LYS B CG    1 
ATOM   9455  C  CD    A LYS B 2 174 ? 41.823  -25.290 4.596   0.20 41.12  ? 174 LYS B CD    1 
ATOM   9456  C  CD    B LYS B 2 174 ? 42.055  -25.409 4.510   0.80 43.17  ? 174 LYS B CD    1 
ATOM   9457  C  CE    A LYS B 2 174 ? 42.761  -24.387 5.389   0.20 40.22  ? 174 LYS B CE    1 
ATOM   9458  C  CE    B LYS B 2 174 ? 43.122  -24.631 5.281   0.80 41.08  ? 174 LYS B CE    1 
ATOM   9459  N  NZ    A LYS B 2 174 ? 44.193  -24.740 5.190   0.20 34.42  ? 174 LYS B NZ    1 
ATOM   9460  N  NZ    B LYS B 2 174 ? 42.930  -24.797 6.749   0.80 46.18  ? 174 LYS B NZ    1 
ATOM   9461  N  N     A VAL B 2 175 ? 39.351  -26.688 -0.466  0.20 33.53  ? 175 VAL B N     1 
ATOM   9462  N  N     B VAL B 2 175 ? 39.334  -26.541 -0.525  0.80 33.12  ? 175 VAL B N     1 
ATOM   9463  C  CA    A VAL B 2 175 ? 38.469  -27.616 -1.168  0.20 36.86  ? 175 VAL B CA    1 
ATOM   9464  C  CA    B VAL B 2 175 ? 38.375  -27.443 -1.144  0.80 37.25  ? 175 VAL B CA    1 
ATOM   9465  C  C     A VAL B 2 175 ? 38.600  -27.471 -2.677  0.20 36.88  ? 175 VAL B C     1 
ATOM   9466  C  C     B VAL B 2 175 ? 38.281  -27.223 -2.649  0.80 34.89  ? 175 VAL B C     1 
ATOM   9467  O  O     A VAL B 2 175 ? 38.850  -28.448 -3.384  0.20 38.95  ? 175 VAL B O     1 
ATOM   9468  O  O     B VAL B 2 175 ? 38.163  -28.186 -3.409  0.80 40.09  ? 175 VAL B O     1 
ATOM   9469  C  CB    A VAL B 2 175 ? 37.007  -27.418 -0.708  0.20 35.22  ? 175 VAL B CB    1 
ATOM   9470  C  CB    B VAL B 2 175 ? 36.984  -27.322 -0.476  0.80 34.39  ? 175 VAL B CB    1 
ATOM   9471  C  CG1   A VAL B 2 175 ? 36.071  -28.318 -1.503  0.20 33.18  ? 175 VAL B CG1   1 
ATOM   9472  C  CG1   B VAL B 2 175 ? 36.001  -28.304 -1.110  0.80 32.85  ? 175 VAL B CG1   1 
ATOM   9473  C  CG2   A VAL B 2 175 ? 36.881  -27.691 0.779   0.20 35.22  ? 175 VAL B CG2   1 
ATOM   9474  C  CG2   B VAL B 2 175 ? 37.087  -27.568 1.010   0.80 35.83  ? 175 VAL B CG2   1 
ATOM   9475  N  N     A SER B 2 176 ? 38.440  -26.253 -3.188  0.20 40.04  ? 176 SER B N     1 
ATOM   9476  N  N     B SER B 2 176 ? 38.357  -25.978 -3.108  0.80 41.77  ? 176 SER B N     1 
ATOM   9477  C  CA    A SER B 2 176 ? 38.628  -25.960 -4.606  0.20 37.16  ? 176 SER B CA    1 
ATOM   9478  C  CA    B SER B 2 176 ? 38.373  -25.690 -4.541  0.80 35.16  ? 176 SER B CA    1 
ATOM   9479  C  C     A SER B 2 176 ? 39.573  -24.773 -4.722  0.20 42.82  ? 176 SER B C     1 
ATOM   9480  C  C     B SER B 2 176 ? 39.538  -24.768 -4.868  0.80 43.33  ? 176 SER B C     1 
ATOM   9481  O  O     A SER B 2 176 ? 39.191  -23.638 -4.419  0.20 41.54  ? 176 SER B O     1 
ATOM   9482  O  O     B SER B 2 176 ? 39.537  -23.594 -4.480  0.80 42.49  ? 176 SER B O     1 
ATOM   9483  C  CB    A SER B 2 176 ? 37.295  -25.670 -5.294  0.20 41.92  ? 176 SER B CB    1 
ATOM   9484  C  CB    B SER B 2 176 ? 37.054  -25.073 -4.999  0.80 43.91  ? 176 SER B CB    1 
ATOM   9485  O  OG    A SER B 2 176 ? 37.485  -25.411 -6.674  0.20 44.64  ? 176 SER B OG    1 
ATOM   9486  O  OG    B SER B 2 176 ? 37.046  -24.947 -6.412  0.80 47.59  ? 176 SER B OG    1 
ATOM   9487  N  N     A ASP B 2 177 ? 40.804  -25.035 -5.156  0.20 41.40  ? 177 ASP B N     1 
ATOM   9488  N  N     B ASP B 2 177 ? 40.523  -25.303 -5.587  0.80 43.90  ? 177 ASP B N     1 
ATOM   9489  C  CA    A ASP B 2 177 ? 41.821  -23.992 -5.289  0.20 42.67  ? 177 ASP B CA    1 
ATOM   9490  C  CA    B ASP B 2 177 ? 41.652  -24.519 -6.094  0.80 52.15  ? 177 ASP B CA    1 
ATOM   9491  C  C     A ASP B 2 177 ? 41.716  -23.313 -6.657  0.20 43.74  ? 177 ASP B C     1 
ATOM   9492  C  C     B ASP B 2 177 ? 41.280  -23.894 -7.442  0.80 42.96  ? 177 ASP B C     1 
ATOM   9493  O  O     A ASP B 2 177 ? 42.613  -23.381 -7.497  0.20 38.96  ? 177 ASP B O     1 
ATOM   9494  O  O     B ASP B 2 177 ? 41.769  -24.273 -8.508  0.80 58.45  ? 177 ASP B O     1 
ATOM   9495  C  CB    A ASP B 2 177 ? 43.210  -24.578 -5.061  0.20 39.76  ? 177 ASP B CB    1 
ATOM   9496  C  CB    B ASP B 2 177 ? 42.897  -25.392 -6.200  0.80 46.36  ? 177 ASP B CB    1 
ATOM   9497  C  CG    A ASP B 2 177 ? 44.280  -23.511 -4.925  0.20 33.03  ? 177 ASP B CG    1 
ATOM   9498  C  CG    B ASP B 2 177 ? 42.604  -26.759 -6.795  0.80 48.08  ? 177 ASP B CG    1 
ATOM   9499  O  OD1   A ASP B 2 177 ? 43.931  -22.313 -4.960  0.20 28.76  ? 177 ASP B OD1   1 
ATOM   9500  O  OD1   B ASP B 2 177 ? 41.440  -27.207 -6.709  0.80 52.48  ? 177 ASP B OD1   1 
ATOM   9501  O  OD2   A ASP B 2 177 ? 45.468  -23.870 -4.775  0.20 30.70  ? 177 ASP B OD2   1 
ATOM   9502  O  OD2   B ASP B 2 177 ? 43.536  -27.395 -7.338  0.80 51.22  ? 177 ASP B OD2   1 
ATOM   9503  N  N     A THR B 2 178 ? 40.582  -22.649 -6.867  0.20 42.60  ? 178 THR B N     1 
ATOM   9504  N  N     B THR B 2 178 ? 40.379  -22.912 -7.369  0.80 43.82  ? 178 THR B N     1 
ATOM   9505  C  CA    A THR B 2 178 ? 40.323  -21.875 -8.073  0.20 39.79  ? 178 THR B CA    1 
ATOM   9506  C  CA    B THR B 2 178 ? 39.923  -22.137 -8.520  0.80 38.93  ? 178 THR B CA    1 
ATOM   9507  C  C     A THR B 2 178 ? 40.351  -20.395 -7.719  0.20 38.34  ? 178 THR B C     1 
ATOM   9508  C  C     B THR B 2 178 ? 40.020  -20.670 -8.134  0.80 39.64  ? 178 THR B C     1 
ATOM   9509  O  O     A THR B 2 178 ? 39.746  -19.979 -6.726  0.20 35.87  ? 178 THR B O     1 
ATOM   9510  O  O     B THR B 2 178 ? 39.257  -20.198 -7.287  0.80 38.74  ? 178 THR B O     1 
ATOM   9511  C  CB    A THR B 2 178 ? 38.975  -22.249 -8.693  0.20 42.21  ? 178 THR B CB    1 
ATOM   9512  C  CB    B THR B 2 178 ? 38.490  -22.501 -8.915  0.80 45.72  ? 178 THR B CB    1 
ATOM   9513  O  OG1   A THR B 2 178 ? 38.910  -23.669 -8.878  0.20 44.95  ? 178 THR B OG1   1 
ATOM   9514  O  OG1   B THR B 2 178 ? 38.375  -23.923 -9.065  0.80 47.75  ? 178 THR B OG1   1 
ATOM   9515  C  CG2   A THR B 2 178 ? 38.802  -21.563 -10.039 0.20 37.92  ? 178 THR B CG2   1 
ATOM   9516  C  CG2   B THR B 2 178 ? 38.106  -21.817 -10.224 0.80 38.45  ? 178 THR B CG2   1 
ATOM   9517  N  N     A VAL B 2 179 ? 41.052  -19.602 -8.534  0.20 37.24  ? 179 VAL B N     1 
ATOM   9518  N  N     B VAL B 2 179 ? 40.950  -19.941 -8.754  0.80 38.87  ? 179 VAL B N     1 
ATOM   9519  C  CA    A VAL B 2 179 ? 41.275  -18.196 -8.201  0.20 33.19  ? 179 VAL B CA    1 
ATOM   9520  C  CA    B VAL B 2 179 ? 41.356  -18.647 -8.204  0.80 33.41  ? 179 VAL B CA    1 
ATOM   9521  C  C     A VAL B 2 179 ? 40.131  -17.284 -8.614  0.20 29.21  ? 179 VAL B C     1 
ATOM   9522  C  C     B VAL B 2 179 ? 40.361  -17.518 -8.436  0.80 27.98  ? 179 VAL B C     1 
ATOM   9523  O  O     A VAL B 2 179 ? 40.154  -16.094 -8.278  0.20 28.01  ? 179 VAL B O     1 
ATOM   9524  O  O     B VAL B 2 179 ? 40.515  -16.454 -7.830  0.80 30.13  ? 179 VAL B O     1 
ATOM   9525  C  CB    A VAL B 2 179 ? 42.582  -17.689 -8.840  0.20 32.41  ? 179 VAL B CB    1 
ATOM   9526  C  CB    B VAL B 2 179 ? 42.732  -18.249 -8.775  0.80 33.60  ? 179 VAL B CB    1 
ATOM   9527  C  CG1   A VAL B 2 179 ? 43.765  -18.484 -8.318  0.20 32.47  ? 179 VAL B CG1   1 
ATOM   9528  C  CG1   B VAL B 2 179 ? 43.830  -18.992 -8.051  0.80 32.73  ? 179 VAL B CG1   1 
ATOM   9529  C  CG2   A VAL B 2 179 ? 42.500  -17.784 -10.355 0.20 35.69  ? 179 VAL B CG2   1 
ATOM   9530  C  CG2   B VAL B 2 179 ? 42.799  -18.571 -10.250 0.80 33.39  ? 179 VAL B CG2   1 
ATOM   9531  N  N     A VAL B 2 180 ? 39.128  -17.794 -9.337  0.20 29.12  ? 180 VAL B N     1 
ATOM   9532  N  N     B VAL B 2 180 ? 39.349  -17.688 -9.295  0.80 28.11  ? 180 VAL B N     1 
ATOM   9533  C  CA    A VAL B 2 180 ? 37.966  -16.977 -9.675  0.20 31.06  ? 180 VAL B CA    1 
ATOM   9534  C  CA    B VAL B 2 180 ? 38.409  -16.590 -9.532  0.80 29.12  ? 180 VAL B CA    1 
ATOM   9535  C  C     A VAL B 2 180 ? 36.871  -17.068 -8.621  0.20 29.41  ? 180 VAL B C     1 
ATOM   9536  C  C     B VAL B 2 180 ? 37.281  -16.561 -8.506  0.80 28.61  ? 180 VAL B C     1 
ATOM   9537  O  O     A VAL B 2 180 ? 35.805  -16.459 -8.787  0.20 26.67  ? 180 VAL B O     1 
ATOM   9538  O  O     B VAL B 2 180 ? 36.471  -15.620 -8.504  0.80 25.03  ? 180 VAL B O     1 
ATOM   9539  C  CB    A VAL B 2 180 ? 37.396  -17.361 -11.057 0.20 34.95  ? 180 VAL B CB    1 
ATOM   9540  C  CB    B VAL B 2 180 ? 37.823  -16.640 -10.960 0.80 35.15  ? 180 VAL B CB    1 
ATOM   9541  C  CG1   A VAL B 2 180 ? 38.492  -17.325 -12.112 0.20 33.13  ? 180 VAL B CG1   1 
ATOM   9542  C  CG1   B VAL B 2 180 ? 38.890  -16.245 -11.999 0.80 29.44  ? 180 VAL B CG1   1 
ATOM   9543  C  CG2   A VAL B 2 180 ? 36.736  -18.729 -11.001 0.20 33.70  ? 180 VAL B CG2   1 
ATOM   9544  C  CG2   B VAL B 2 180 ? 37.235  -18.020 -11.260 0.80 37.51  ? 180 VAL B CG2   1 
ATOM   9545  N  N     A GLU B 2 181 ? 37.100  -17.803 -7.540  0.20 29.28  ? 181 GLU B N     1 
ATOM   9546  N  N     B GLU B 2 181 ? 37.219  -17.546 -7.620  0.80 27.41  ? 181 GLU B N     1 
ATOM   9547  C  CA    A GLU B 2 181 ? 36.096  -17.942 -6.493  0.20 30.81  ? 181 GLU B CA    1 
ATOM   9548  C  CA    B GLU B 2 181 ? 36.129  -17.652 -6.654  0.80 30.56  ? 181 GLU B CA    1 
ATOM   9549  C  C     A GLU B 2 181 ? 36.008  -16.694 -5.614  0.20 30.46  ? 181 GLU B C     1 
ATOM   9550  C  C     B GLU B 2 181 ? 36.076  -16.506 -5.636  0.80 30.68  ? 181 GLU B C     1 
ATOM   9551  O  O     A GLU B 2 181 ? 34.894  -16.264 -5.293  0.20 32.20  ? 181 GLU B O     1 
ATOM   9552  O  O     B GLU B 2 181 ? 34.986  -16.205 -5.135  0.80 32.97  ? 181 GLU B O     1 
ATOM   9553  C  CB    A GLU B 2 181 ? 36.376  -19.184 -5.644  0.20 32.53  ? 181 GLU B CB    1 
ATOM   9554  C  CB    B GLU B 2 181 ? 36.198  -19.004 -5.934  0.80 32.90  ? 181 GLU B CB    1 
ATOM   9555  C  CG    A GLU B 2 181 ? 36.339  -20.481 -6.435  0.20 35.30  ? 181 GLU B CG    1 
ATOM   9556  C  CG    B GLU B 2 181 ? 36.089  -20.229 -6.868  0.80 32.93  ? 181 GLU B CG    1 
ATOM   9557  C  CD    A GLU B 2 181 ? 36.566  -21.697 -5.564  0.20 37.56  ? 181 GLU B CD    1 
ATOM   9558  C  CD    B GLU B 2 181 ? 35.783  -21.517 -6.113  0.80 37.14  ? 181 GLU B CD    1 
ATOM   9559  O  OE1   A GLU B 2 181 ? 37.214  -21.558 -4.504  0.20 32.41  ? 181 GLU B OE1   1 
ATOM   9560  O  OE1   B GLU B 2 181 ? 35.675  -21.451 -4.876  0.80 42.67  ? 181 GLU B OE1   1 
ATOM   9561  O  OE2   A GLU B 2 181 ? 36.086  -22.789 -5.936  0.20 36.96  ? 181 GLU B OE2   1 
ATOM   9562  O  OE2   B GLU B 2 181 ? 35.634  -22.592 -6.747  0.80 34.73  ? 181 GLU B OE2   1 
ATOM   9563  N  N     A PRO B 2 182 ? 37.124  -16.086 -5.187  0.20 29.07  ? 182 PRO B N     1 
ATOM   9564  N  N     B PRO B 2 182 ? 37.190  -15.853 -5.269  0.80 28.68  ? 182 PRO B N     1 
ATOM   9565  C  CA    A PRO B 2 182 ? 37.000  -14.808 -4.465  0.20 27.47  ? 182 PRO B CA    1 
ATOM   9566  C  CA    B PRO B 2 182 ? 37.036  -14.615 -4.480  0.80 27.08  ? 182 PRO B CA    1 
ATOM   9567  C  C     A PRO B 2 182 ? 36.327  -13.724 -5.284  0.20 29.98  ? 182 PRO B C     1 
ATOM   9568  C  C     B PRO B 2 182 ? 36.268  -13.538 -5.220  0.80 30.58  ? 182 PRO B C     1 
ATOM   9569  O  O     A PRO B 2 182 ? 35.646  -12.862 -4.714  0.20 27.61  ? 182 PRO B O     1 
ATOM   9570  O  O     B PRO B 2 182 ? 35.467  -12.831 -4.597  0.80 26.97  ? 182 PRO B O     1 
ATOM   9571  C  CB    A PRO B 2 182 ? 38.453  -14.445 -4.134  0.20 28.26  ? 182 PRO B CB    1 
ATOM   9572  C  CB    B PRO B 2 182 ? 38.477  -14.187 -4.191  0.80 27.84  ? 182 PRO B CB    1 
ATOM   9573  C  CG    A PRO B 2 182 ? 39.169  -15.743 -4.120  0.20 27.25  ? 182 PRO B CG    1 
ATOM   9574  C  CG    B PRO B 2 182 ? 39.274  -15.447 -4.262  0.80 25.17  ? 182 PRO B CG    1 
ATOM   9575  C  CD    A PRO B 2 182 ? 38.517  -16.576 -5.177  0.20 32.06  ? 182 PRO B CD    1 
ATOM   9576  C  CD    B PRO B 2 182 ? 38.581  -16.356 -5.247  0.80 33.15  ? 182 PRO B CD    1 
ATOM   9577  N  N     A TYR B 2 183 ? 36.504  -13.738 -6.607  0.20 28.08  ? 183 TYR B N     1 
ATOM   9578  N  N     B TYR B 2 183 ? 36.489  -13.386 -6.533  0.80 28.02  ? 183 TYR B N     1 
ATOM   9579  C  CA    A TYR B 2 183 ? 35.795  -12.799 -7.471  0.20 28.52  ? 183 TYR B CA    1 
ATOM   9580  C  CA    B TYR B 2 183 ? 35.669  -12.467 -7.316  0.80 27.08  ? 183 TYR B CA    1 
ATOM   9581  C  C     A TYR B 2 183 ? 34.288  -12.986 -7.349  0.20 28.24  ? 183 TYR B C     1 
ATOM   9582  C  C     B TYR B 2 183 ? 34.198  -12.823 -7.167  0.80 28.07  ? 183 TYR B C     1 
ATOM   9583  O  O     A TYR B 2 183 ? 33.549  -12.040 -7.055  0.20 29.67  ? 183 TYR B O     1 
ATOM   9584  O  O     B TYR B 2 183 ? 33.376  -11.986 -6.783  0.80 30.30  ? 183 TYR B O     1 
ATOM   9585  C  CB    A TYR B 2 183 ? 36.235  -12.988 -8.924  0.20 30.85  ? 183 TYR B CB    1 
ATOM   9586  C  CB    B TYR B 2 183 ? 36.034  -12.508 -8.806  0.80 29.90  ? 183 TYR B CB    1 
ATOM   9587  C  CG    A TYR B 2 183 ? 37.452  -12.188 -9.341  0.20 31.45  ? 183 TYR B CG    1 
ATOM   9588  C  CG    B TYR B 2 183 ? 37.391  -11.970 -9.251  0.80 32.11  ? 183 TYR B CG    1 
ATOM   9589  C  CD1   A TYR B 2 183 ? 37.816  -11.027 -8.671  0.20 30.95  ? 183 TYR B CD1   1 
ATOM   9590  C  CD1   B TYR B 2 183 ? 38.132  -11.083 -8.477  0.80 31.07  ? 183 TYR B CD1   1 
ATOM   9591  C  CD2   A TYR B 2 183 ? 38.226  -12.589 -10.420 0.20 32.47  ? 183 TYR B CD2   1 
ATOM   9592  C  CD2   B TYR B 2 183 ? 37.902  -12.334 -10.484 0.80 32.25  ? 183 TYR B CD2   1 
ATOM   9593  C  CE1   A TYR B 2 183 ? 38.924  -10.294 -9.061  0.20 30.75  ? 183 TYR B CE1   1 
ATOM   9594  C  CE1   B TYR B 2 183 ? 39.366  -10.605 -8.927  0.80 29.46  ? 183 TYR B CE1   1 
ATOM   9595  C  CE2   A TYR B 2 183 ? 39.334  -11.865 -10.817 0.20 30.61  ? 183 TYR B CE2   1 
ATOM   9596  C  CE2   B TYR B 2 183 ? 39.118  -11.859 -10.939 0.80 29.99  ? 183 TYR B CE2   1 
ATOM   9597  C  CZ    A TYR B 2 183 ? 39.679  -10.719 -10.136 0.20 33.02  ? 183 TYR B CZ    1 
ATOM   9598  C  CZ    B TYR B 2 183 ? 39.846  -10.999 -10.165 0.80 34.22  ? 183 TYR B CZ    1 
ATOM   9599  O  OH    A TYR B 2 183 ? 40.783  -9.997  -10.534 0.20 31.22  ? 183 TYR B OH    1 
ATOM   9600  O  OH    B TYR B 2 183 ? 41.058  -10.544 -10.649 0.80 31.00  ? 183 TYR B OH    1 
ATOM   9601  N  N     A ASN B 2 184 ? 33.815  -14.214 -7.574  0.20 26.29  ? 184 ASN B N     1 
ATOM   9602  N  N     B ASN B 2 184 ? 33.849  -14.077 -7.474  0.80 25.66  ? 184 ASN B N     1 
ATOM   9603  C  CA    A ASN B 2 184 ? 32.378  -14.463 -7.559  0.20 28.75  ? 184 ASN B CA    1 
ATOM   9604  C  CA    B ASN B 2 184 ? 32.436  -14.455 -7.525  0.80 28.81  ? 184 ASN B CA    1 
ATOM   9605  C  C     A ASN B 2 184 ? 31.809  -14.395 -6.148  0.20 29.46  ? 184 ASN B C     1 
ATOM   9606  C  C     B ASN B 2 184 ? 31.758  -14.256 -6.176  0.80 29.49  ? 184 ASN B C     1 
ATOM   9607  O  O     A ASN B 2 184 ? 30.617  -14.117 -5.977  0.20 29.12  ? 184 ASN B O     1 
ATOM   9608  O  O     B ASN B 2 184 ? 30.605  -13.814 -6.112  0.80 28.68  ? 184 ASN B O     1 
ATOM   9609  C  CB    A ASN B 2 184 ? 32.077  -15.821 -8.192  0.20 28.15  ? 184 ASN B CB    1 
ATOM   9610  C  CB    B ASN B 2 184 ? 32.287  -15.907 -7.975  0.80 26.77  ? 184 ASN B CB    1 
ATOM   9611  C  CG    A ASN B 2 184 ? 32.753  -15.993 -9.539  0.20 30.56  ? 184 ASN B CG    1 
ATOM   9612  C  CG    B ASN B 2 184 ? 32.856  -16.156 -9.358  0.80 30.25  ? 184 ASN B CG    1 
ATOM   9613  O  OD1   A ASN B 2 184 ? 33.095  -15.015 -10.203 0.20 30.74  ? 184 ASN B OD1   1 
ATOM   9614  O  OD1   B ASN B 2 184 ? 32.886  -15.266 -10.206 0.80 30.91  ? 184 ASN B OD1   1 
ATOM   9615  N  ND2   A ASN B 2 184 ? 32.950  -17.239 -9.947  0.20 30.29  ? 184 ASN B ND2   1 
ATOM   9616  N  ND2   B ASN B 2 184 ? 33.289  -17.376 -9.593  0.80 30.36  ? 184 ASN B ND2   1 
ATOM   9617  N  N     A ALA B 2 185 ? 32.635  -14.647 -5.130  0.20 27.28  ? 185 ALA B N     1 
ATOM   9618  N  N     B ALA B 2 185 ? 32.454  -14.575 -5.082  0.80 27.17  ? 185 ALA B N     1 
ATOM   9619  C  CA    A ALA B 2 185 ? 32.150  -14.557 -3.757  0.20 29.48  ? 185 ALA B CA    1 
ATOM   9620  C  CA    B ALA B 2 185 ? 31.816  -14.465 -3.774  0.80 29.80  ? 185 ALA B CA    1 
ATOM   9621  C  C     A ALA B 2 185 ? 31.918  -13.108 -3.348  0.20 30.57  ? 185 ALA B C     1 
ATOM   9622  C  C     B ALA B 2 185 ? 31.679  -13.010 -3.341  0.80 31.42  ? 185 ALA B C     1 
ATOM   9623  O  O     A ALA B 2 185 ? 30.925  -12.798 -2.680  0.20 29.91  ? 185 ALA B O     1 
ATOM   9624  O  O     B ALA B 2 185 ? 30.665  -12.629 -2.748  0.80 30.21  ? 185 ALA B O     1 
ATOM   9625  C  CB    A ALA B 2 185 ? 33.134  -15.236 -2.805  0.20 27.94  ? 185 ALA B CB    1 
ATOM   9626  C  CB    B ALA B 2 185 ? 32.594  -15.269 -2.738  0.80 25.06  ? 185 ALA B CB    1 
ATOM   9627  N  N     A THR B 2 186 ? 32.820  -12.205 -3.739  0.20 29.37  ? 186 THR B N     1 
ATOM   9628  N  N     B THR B 2 186 ? 32.677  -12.178 -3.630  0.80 29.42  ? 186 THR B N     1 
ATOM   9629  C  CA    A THR B 2 186 ? 32.643  -10.795 -3.410  0.20 27.49  ? 186 THR B CA    1 
ATOM   9630  C  CA    B THR B 2 186 ? 32.590  -10.770 -3.255  0.80 26.78  ? 186 THR B CA    1 
ATOM   9631  C  C     A THR B 2 186 ? 31.447  -10.203 -4.145  0.20 30.36  ? 186 THR B C     1 
ATOM   9632  C  C     B THR B 2 186 ? 31.459  -10.070 -4.000  0.80 30.23  ? 186 THR B C     1 
ATOM   9633  O  O     A THR B 2 186 ? 30.655  -9.459  -3.555  0.20 33.67  ? 186 THR B O     1 
ATOM   9634  O  O     B THR B 2 186 ? 30.690  -9.305  -3.407  0.80 34.89  ? 186 THR B O     1 
ATOM   9635  C  CB    A THR B 2 186 ? 33.917  -10.016 -3.740  0.20 31.86  ? 186 THR B CB    1 
ATOM   9636  C  CB    B THR B 2 186 ? 33.930  -10.083 -3.522  0.80 32.62  ? 186 THR B CB    1 
ATOM   9637  O  OG1   A THR B 2 186 ? 35.021  -10.585 -3.026  0.20 30.76  ? 186 THR B OG1   1 
ATOM   9638  O  OG1   B THR B 2 186 ? 34.925  -10.646 -2.656  0.80 29.71  ? 186 THR B OG1   1 
ATOM   9639  C  CG2   A THR B 2 186 ? 33.768  -8.554  -3.347  0.20 32.81  ? 186 THR B CG2   1 
ATOM   9640  C  CG2   B THR B 2 186 ? 33.834  -8.582  -3.272  0.80 32.80  ? 186 THR B CG2   1 
ATOM   9641  N  N     A LEU B 2 187 ? 31.302  -10.518 -5.435  0.20 29.74  ? 187 LEU B N     1 
ATOM   9642  N  N     B LEU B 2 187 ? 31.346  -10.320 -5.307  0.80 29.65  ? 187 LEU B N     1 
ATOM   9643  C  CA    A LEU B 2 187 ? 30.130  -10.069 -6.177  0.20 31.07  ? 187 LEU B CA    1 
ATOM   9644  C  CA    B LEU B 2 187 ? 30.281  -9.706  -6.090  0.80 30.42  ? 187 LEU B CA    1 
ATOM   9645  C  C     A LEU B 2 187 ? 28.851  -10.677 -5.615  0.20 28.87  ? 187 LEU B C     1 
ATOM   9646  C  C     B LEU B 2 187 ? 28.909  -10.118 -5.578  0.80 25.68  ? 187 LEU B C     1 
ATOM   9647  O  O     A LEU B 2 187 ? 27.781  -10.066 -5.706  0.20 32.39  ? 187 LEU B O     1 
ATOM   9648  O  O     B LEU B 2 187 ? 27.960  -9.333  -5.658  0.80 31.59  ? 187 LEU B O     1 
ATOM   9649  C  CB    A LEU B 2 187 ? 30.279  -10.418 -7.660  0.20 27.89  ? 187 LEU B CB    1 
ATOM   9650  C  CB    B LEU B 2 187 ? 30.423  -10.084 -7.561  0.80 26.91  ? 187 LEU B CB    1 
ATOM   9651  C  CG    A LEU B 2 187 ? 31.366  -9.696  -8.467  0.20 30.96  ? 187 LEU B CG    1 
ATOM   9652  C  CG    B LEU B 2 187 ? 31.721  -9.638  -8.254  0.80 29.28  ? 187 LEU B CG    1 
ATOM   9653  C  CD1   A LEU B 2 187 ? 31.641  -10.436 -9.766  0.20 30.09  ? 187 LEU B CD1   1 
ATOM   9654  C  CD1   B LEU B 2 187 ? 31.658  -10.021 -9.711  0.80 29.52  ? 187 LEU B CD1   1 
ATOM   9655  C  CD2   A LEU B 2 187 ? 30.961  -8.257  -8.749  0.20 28.65  ? 187 LEU B CD2   1 
ATOM   9656  C  CD2   B LEU B 2 187 ? 31.912  -8.153  -8.077  0.80 26.05  ? 187 LEU B CD2   1 
ATOM   9657  N  N     A SER B 2 188 ? 28.940  -11.876 -5.030  0.20 31.19  ? 188 SER B N     1 
ATOM   9658  N  N     B SER B 2 188 ? 28.790  -11.347 -5.071  0.80 30.47  ? 188 SER B N     1 
ATOM   9659  C  CA    A SER B 2 188 ? 27.763  -12.500 -4.436  0.20 31.44  ? 188 SER B CA    1 
ATOM   9660  C  CA    B SER B 2 188 ? 27.542  -11.846 -4.512  0.80 32.59  ? 188 SER B CA    1 
ATOM   9661  C  C     A SER B 2 188 ? 27.400  -11.845 -3.111  0.20 30.31  ? 188 SER B C     1 
ATOM   9662  C  C     B SER B 2 188 ? 27.257  -11.237 -3.151  0.80 29.38  ? 188 SER B C     1 
ATOM   9663  O  O     A SER B 2 188 ? 26.219  -11.619 -2.830  0.20 30.25  ? 188 SER B O     1 
ATOM   9664  O  O     B SER B 2 188 ? 26.126  -10.813 -2.888  0.80 30.56  ? 188 SER B O     1 
ATOM   9665  C  CB    A SER B 2 188 ? 27.999  -13.997 -4.238  0.20 30.84  ? 188 SER B CB    1 
ATOM   9666  C  CB    B SER B 2 188 ? 27.588  -13.368 -4.399  0.80 31.17  ? 188 SER B CB    1 
ATOM   9667  O  OG    A SER B 2 188 ? 28.218  -14.653 -5.476  0.20 31.48  ? 188 SER B OG    1 
ATOM   9668  O  OG    B SER B 2 188 ? 27.303  -13.977 -5.643  0.80 42.68  ? 188 SER B OG    1 
ATOM   9669  N  N     A VAL B 2 189 ? 28.401  -11.543 -2.280  0.20 31.55  ? 189 VAL B N     1 
ATOM   9670  N  N     B VAL B 2 189 ? 28.270  -11.180 -2.282  0.80 31.47  ? 189 VAL B N     1 
ATOM   9671  C  CA    A VAL B 2 189 ? 28.134  -10.909 -0.992  0.20 31.54  ? 189 VAL B CA    1 
ATOM   9672  C  CA    B VAL B 2 189 ? 28.084  -10.600 -0.956  0.80 31.79  ? 189 VAL B CA    1 
ATOM   9673  C  C     A VAL B 2 189 ? 27.542  -9.521  -1.189  0.20 30.79  ? 189 VAL B C     1 
ATOM   9674  C  C     B VAL B 2 189 ? 27.559  -9.178  -1.074  0.80 30.60  ? 189 VAL B C     1 
ATOM   9675  O  O     A VAL B 2 189 ? 26.685  -9.087  -0.411  0.20 29.40  ? 189 VAL B O     1 
ATOM   9676  O  O     B VAL B 2 189 ? 26.650  -8.776  -0.345  0.80 28.70  ? 189 VAL B O     1 
ATOM   9677  C  CB    A VAL B 2 189 ? 29.423  -10.872 -0.145  0.20 30.79  ? 189 VAL B CB    1 
ATOM   9678  C  CB    B VAL B 2 189 ? 29.399  -10.668 -0.156  0.80 30.59  ? 189 VAL B CB    1 
ATOM   9679  C  CG1   A VAL B 2 189 ? 29.234  -10.010 1.093   0.20 33.57  ? 189 VAL B CG1   1 
ATOM   9680  C  CG1   B VAL B 2 189 ? 29.325  -9.799  1.081   0.80 34.10  ? 189 VAL B CG1   1 
ATOM   9681  C  CG2   A VAL B 2 189 ? 29.826  -12.282 0.254   0.20 31.67  ? 189 VAL B CG2   1 
ATOM   9682  C  CG2   B VAL B 2 189 ? 29.695  -12.108 0.226   0.80 31.76  ? 189 VAL B CG2   1 
ATOM   9683  N  N     A HIS B 2 190 ? 27.963  -8.814  -2.241  0.20 31.30  ? 190 HIS B N     1 
ATOM   9684  N  N     B HIS B 2 190 ? 28.100  -8.410  -2.019  0.80 29.63  ? 190 HIS B N     1 
ATOM   9685  C  CA    A HIS B 2 190 ? 27.423  -7.484  -2.506  0.20 31.85  ? 190 HIS B CA    1 
ATOM   9686  C  CA    B HIS B 2 190 ? 27.555  -7.096  -2.345  0.80 30.14  ? 190 HIS B CA    1 
ATOM   9687  C  C     A HIS B 2 190 ? 25.922  -7.525  -2.775  0.20 35.19  ? 190 HIS B C     1 
ATOM   9688  C  C     B HIS B 2 190 ? 26.032  -7.145  -2.498  0.80 35.85  ? 190 HIS B C     1 
ATOM   9689  O  O     A HIS B 2 190 ? 25.218  -6.546  -2.503  0.20 38.00  ? 190 HIS B O     1 
ATOM   9690  O  O     B HIS B 2 190 ? 25.312  -6.323  -1.920  0.80 40.36  ? 190 HIS B O     1 
ATOM   9691  C  CB    A HIS B 2 190 ? 28.163  -6.847  -3.683  0.20 36.20  ? 190 HIS B CB    1 
ATOM   9692  C  CB    B HIS B 2 190 ? 28.238  -6.584  -3.620  0.80 36.36  ? 190 HIS B CB    1 
ATOM   9693  C  CG    A HIS B 2 190 ? 27.654  -5.489  -4.056  0.20 40.94  ? 190 HIS B CG    1 
ATOM   9694  C  CG    B HIS B 2 190 ? 27.864  -5.187  -4.009  0.80 42.23  ? 190 HIS B CG    1 
ATOM   9695  N  ND1   A HIS B 2 190 ? 27.451  -4.489  -3.130  0.20 41.07  ? 190 HIS B ND1   1 
ATOM   9696  N  ND1   B HIS B 2 190 ? 27.908  -4.127  -3.129  0.80 42.58  ? 190 HIS B ND1   1 
ATOM   9697  C  CD2   A HIS B 2 190 ? 27.313  -4.963  -5.257  0.20 41.62  ? 190 HIS B CD2   1 
ATOM   9698  C  CD2   B HIS B 2 190 ? 27.476  -4.669  -5.199  0.80 42.52  ? 190 HIS B CD2   1 
ATOM   9699  C  CE1   A HIS B 2 190 ? 27.004  -3.407  -3.742  0.20 40.22  ? 190 HIS B CE1   1 
ATOM   9700  C  CE1   B HIS B 2 190 ? 27.544  -3.021  -3.752  0.80 36.09  ? 190 HIS B CE1   1 
ATOM   9701  N  NE2   A HIS B 2 190 ? 26.911  -3.668  -5.033  0.20 46.47  ? 190 HIS B NE2   1 
ATOM   9702  N  NE2   B HIS B 2 190 ? 27.276  -3.322  -5.009  0.80 49.35  ? 190 HIS B NE2   1 
ATOM   9703  N  N     A GLN B 2 191 ? 25.412  -8.643  -3.296  0.20 31.66  ? 191 GLN B N     1 
ATOM   9704  N  N     B GLN B 2 191 ? 25.520  -8.139  -3.235  0.80 33.77  ? 191 GLN B N     1 
ATOM   9705  C  CA    A GLN B 2 191 ? 23.987  -8.773  -3.569  0.20 31.93  ? 191 GLN B CA    1 
ATOM   9706  C  CA    B GLN B 2 191 ? 24.077  -8.244  -3.433  0.80 29.31  ? 191 GLN B CA    1 
ATOM   9707  C  C     A GLN B 2 191 ? 23.212  -9.403  -2.420  0.20 32.38  ? 191 GLN B C     1 
ATOM   9708  C  C     B GLN B 2 191 ? 23.377  -8.732  -2.169  0.80 33.29  ? 191 GLN B C     1 
ATOM   9709  O  O     A GLN B 2 191 ? 21.999  -9.181  -2.316  0.20 33.69  ? 191 GLN B O     1 
ATOM   9710  O  O     B GLN B 2 191 ? 22.288  -8.247  -1.838  0.80 31.97  ? 191 GLN B O     1 
ATOM   9711  C  CB    A GLN B 2 191 ? 23.759  -9.600  -4.840  0.20 33.26  ? 191 GLN B CB    1 
ATOM   9712  C  CB    B GLN B 2 191 ? 23.763  -9.183  -4.599  0.80 33.00  ? 191 GLN B CB    1 
ATOM   9713  C  CG    A GLN B 2 191 ? 24.354  -8.995  -6.107  0.20 33.76  ? 191 GLN B CG    1 
ATOM   9714  C  CG    B GLN B 2 191 ? 24.369  -8.771  -5.949  0.80 33.98  ? 191 GLN B CG    1 
ATOM   9715  C  CD    A GLN B 2 191 ? 23.662  -7.712  -6.540  0.20 37.57  ? 191 GLN B CD    1 
ATOM   9716  C  CD    B GLN B 2 191 ? 23.582  -7.672  -6.647  0.80 37.81  ? 191 GLN B CD    1 
ATOM   9717  O  OE1   A GLN B 2 191 ? 22.622  -7.333  -5.998  0.20 37.47  ? 191 GLN B OE1   1 
ATOM   9718  O  OE1   B GLN B 2 191 ? 22.355  -7.739  -6.757  0.80 38.83  ? 191 GLN B OE1   1 
ATOM   9719  N  NE2   A GLN B 2 191 ? 24.239  -7.036  -7.527  0.20 37.80  ? 191 GLN B NE2   1 
ATOM   9720  N  NE2   B GLN B 2 191 ? 24.290  -6.652  -7.129  0.80 38.31  ? 191 GLN B NE2   1 
ATOM   9721  N  N     A LEU B 2 192 ? 23.876  -10.183 -1.561  0.20 30.00  ? 192 LEU B N     1 
ATOM   9722  N  N     B LEU B 2 192 ? 23.989  -9.689  -1.448  0.80 28.02  ? 192 LEU B N     1 
ATOM   9723  C  CA    A LEU B 2 192 ? 23.191  -10.772 -0.413  0.20 29.67  ? 192 LEU B CA    1 
ATOM   9724  C  CA    B LEU B 2 192 ? 23.333  -10.297 -0.283  0.80 30.07  ? 192 LEU B CA    1 
ATOM   9725  C  C     A LEU B 2 192 ? 22.926  -9.743  0.680   0.20 31.47  ? 192 LEU B C     1 
ATOM   9726  C  C     B LEU B 2 192 ? 23.130  -9.288  0.840   0.80 30.70  ? 192 LEU B C     1 
ATOM   9727  O  O     A LEU B 2 192 ? 21.949  -9.874  1.427   0.20 31.02  ? 192 LEU B O     1 
ATOM   9728  O  O     B LEU B 2 192 ? 22.135  -9.360  1.574   0.80 31.73  ? 192 LEU B O     1 
ATOM   9729  C  CB    A LEU B 2 192 ? 24.006  -11.938 0.148   0.20 29.16  ? 192 LEU B CB    1 
ATOM   9730  C  CB    B LEU B 2 192 ? 24.148  -11.486 0.231   0.80 27.07  ? 192 LEU B CB    1 
ATOM   9731  C  CG    A LEU B 2 192 ? 24.101  -13.200 -0.715  0.20 30.44  ? 192 LEU B CG    1 
ATOM   9732  C  CG    B LEU B 2 192 ? 24.318  -12.712 -0.672  0.80 30.70  ? 192 LEU B CG    1 
ATOM   9733  C  CD1   A LEU B 2 192 ? 25.066  -14.210 -0.104  0.20 32.27  ? 192 LEU B CD1   1 
ATOM   9734  C  CD1   B LEU B 2 192 ? 25.299  -13.707 -0.057  0.80 36.97  ? 192 LEU B CD1   1 
ATOM   9735  C  CD2   A LEU B 2 192 ? 22.729  -13.829 -0.912  0.20 29.83  ? 192 LEU B CD2   1 
ATOM   9736  C  CD2   B LEU B 2 192 ? 22.987  -13.397 -0.949  0.80 30.63  ? 192 LEU B CD2   1 
ATOM   9737  N  N     A VAL B 2 193 ? 23.778  -8.722  0.797   0.20 31.88  ? 193 VAL B N     1 
ATOM   9738  N  N     B VAL B 2 193 ? 24.077  -8.365  1.013   0.80 32.62  ? 193 VAL B N     1 
ATOM   9739  C  CA    A VAL B 2 193 ? 23.572  -7.703  1.822   0.20 32.48  ? 193 VAL B CA    1 
ATOM   9740  C  CA    B VAL B 2 193 ? 23.928  -7.325  2.026   0.80 32.54  ? 193 VAL B CA    1 
ATOM   9741  C  C     A VAL B 2 193 ? 22.349  -6.854  1.495   0.20 36.08  ? 193 VAL B C     1 
ATOM   9742  C  C     B VAL B 2 193 ? 22.661  -6.514  1.777   0.80 36.30  ? 193 VAL B C     1 
ATOM   9743  O  O     A VAL B 2 193 ? 21.581  -6.471  2.388   0.20 33.13  ? 193 VAL B O     1 
ATOM   9744  O  O     B VAL B 2 193 ? 22.000  -6.063  2.722   0.80 34.38  ? 193 VAL B O     1 
ATOM   9745  C  CB    A VAL B 2 193 ? 24.836  -6.835  1.976   0.20 34.38  ? 193 VAL B CB    1 
ATOM   9746  C  CB    B VAL B 2 193 ? 25.193  -6.436  2.047   0.80 34.11  ? 193 VAL B CB    1 
ATOM   9747  C  CG1   A VAL B 2 193 ? 24.607  -5.735  3.000   0.20 35.95  ? 193 VAL B CG1   1 
ATOM   9748  C  CG1   B VAL B 2 193 ? 24.970  -5.194  2.884   0.80 40.28  ? 193 VAL B CG1   1 
ATOM   9749  C  CG2   A VAL B 2 193 ? 26.032  -7.688  2.374   0.20 32.76  ? 193 VAL B CG2   1 
ATOM   9750  C  CG2   B VAL B 2 193 ? 26.390  -7.222  2.587   0.80 31.24  ? 193 VAL B CG2   1 
ATOM   9751  N  N     A GLU B 2 194 ? 22.136  -6.561  0.212   0.20 33.95  ? 194 GLU B N     1 
ATOM   9752  N  N     B GLU B 2 194 ? 22.271  -6.356  0.512   0.80 32.81  ? 194 GLU B N     1 
ATOM   9753  C  CA    A GLU B 2 194 ? 21.097  -5.626  -0.202  0.20 38.47  ? 194 GLU B CA    1 
ATOM   9754  C  CA    B GLU B 2 194 ? 21.116  -5.527  0.194   0.80 36.20  ? 194 GLU B CA    1 
ATOM   9755  C  C     A GLU B 2 194 ? 19.730  -6.274  -0.378  0.20 39.79  ? 194 GLU B C     1 
ATOM   9756  C  C     B GLU B 2 194 ? 19.808  -6.304  0.099   0.80 41.26  ? 194 GLU B C     1 
ATOM   9757  O  O     A GLU B 2 194 ? 18.710  -5.628  -0.109  0.20 42.77  ? 194 GLU B O     1 
ATOM   9758  O  O     B GLU B 2 194 ? 18.748  -5.744  0.404   0.80 46.07  ? 194 GLU B O     1 
ATOM   9759  C  CB    A GLU B 2 194 ? 21.498  -4.947  -1.518  0.20 40.69  ? 194 GLU B CB    1 
ATOM   9760  C  CB    B GLU B 2 194 ? 21.351  -4.785  -1.128  0.80 43.63  ? 194 GLU B CB    1 
ATOM   9761  C  CG    A GLU B 2 194 ? 22.907  -4.369  -1.535  0.20 41.40  ? 194 GLU B CG    1 
ATOM   9762  C  CG    B GLU B 2 194 ? 22.622  -3.943  -1.159  0.80 41.78  ? 194 GLU B CG    1 
ATOM   9763  C  CD    A GLU B 2 194 ? 23.012  -3.021  -0.842  0.20 46.57  ? 194 GLU B CD    1 
ATOM   9764  C  CD    B GLU B 2 194 ? 22.582  -2.760  -0.195  0.80 50.74  ? 194 GLU B CD    1 
ATOM   9765  O  OE1   A GLU B 2 194 ? 21.968  -2.479  -0.418  0.20 50.06  ? 194 GLU B OE1   1 
ATOM   9766  O  OE1   B GLU B 2 194 ? 21.489  -2.187  0.019   0.80 50.18  ? 194 GLU B OE1   1 
ATOM   9767  O  OE2   A GLU B 2 194 ? 24.143  -2.502  -0.724  0.20 45.56  ? 194 GLU B OE2   1 
ATOM   9768  O  OE2   B GLU B 2 194 ? 23.649  -2.401  0.345   0.80 58.46  ? 194 GLU B OE2   1 
ATOM   9769  N  N     A ASN B 2 195 ? 19.675  -7.530  -0.823  0.20 37.95  ? 195 ASN B N     1 
ATOM   9770  N  N     B ASN B 2 195 ? 19.838  -7.576  -0.306  0.80 34.52  ? 195 ASN B N     1 
ATOM   9771  C  CA    A ASN B 2 195 ? 18.423  -8.127  -1.266  0.20 40.30  ? 195 ASN B CA    1 
ATOM   9772  C  CA    B ASN B 2 195 ? 18.626  -8.231  -0.787  0.80 39.72  ? 195 ASN B CA    1 
ATOM   9773  C  C     A ASN B 2 195 ? 17.888  -9.219  -0.351  0.20 36.28  ? 195 ASN B C     1 
ATOM   9774  C  C     B ASN B 2 195 ? 18.204  -9.484  -0.032  0.80 36.70  ? 195 ASN B C     1 
ATOM   9775  O  O     A ASN B 2 195 ? 16.746  -9.651  -0.543  0.20 35.89  ? 195 ASN B O     1 
ATOM   9776  O  O     B ASN B 2 195 ? 17.240  -10.133 -0.450  0.80 31.76  ? 195 ASN B O     1 
ATOM   9777  C  CB    A ASN B 2 195 ? 18.584  -8.703  -2.681  0.20 38.94  ? 195 ASN B CB    1 
ATOM   9778  C  CB    B ASN B 2 195 ? 18.773  -8.575  -2.278  0.80 37.75  ? 195 ASN B CB    1 
ATOM   9779  C  CG    A ASN B 2 195 ? 19.053  -7.667  -3.685  0.20 46.57  ? 195 ASN B CG    1 
ATOM   9780  C  CG    B ASN B 2 195 ? 18.470  -7.390  -3.177  0.80 49.79  ? 195 ASN B CG    1 
ATOM   9781  O  OD1   A ASN B 2 195 ? 20.084  -7.841  -4.336  0.20 41.22  ? 195 ASN B OD1   1 
ATOM   9782  O  OD1   B ASN B 2 195 ? 19.163  -7.146  -4.172  0.80 52.16  ? 195 ASN B OD1   1 
ATOM   9783  N  ND2   A ASN B 2 195 ? 18.293  -6.583  -3.820  0.20 46.49  ? 195 ASN B ND2   1 
ATOM   9784  N  ND2   B ASN B 2 195 ? 17.429  -6.641  -2.830  0.80 44.94  ? 195 ASN B ND2   1 
ATOM   9785  N  N     A THR B 2 196 ? 18.664  -9.684  0.621   0.20 35.56  ? 196 THR B N     1 
ATOM   9786  N  N     B THR B 2 196 ? 18.874  -9.858  1.050   0.80 36.44  ? 196 THR B N     1 
ATOM   9787  C  CA    A THR B 2 196 ? 18.236  -10.765 1.496   0.20 33.66  ? 196 THR B CA    1 
ATOM   9788  C  CA    B THR B 2 196 ? 18.385  -10.955 1.872   0.80 34.20  ? 196 THR B CA    1 
ATOM   9789  C  C     A THR B 2 196 ? 18.032  -10.252 2.915   0.20 30.73  ? 196 THR B C     1 
ATOM   9790  C  C     B THR B 2 196 ? 18.083  -10.449 3.272   0.80 29.25  ? 196 THR B C     1 
ATOM   9791  O  O     A THR B 2 196 ? 18.635  -9.258  3.329   0.20 30.44  ? 196 THR B O     1 
ATOM   9792  O  O     B THR B 2 196 ? 18.697  -9.493  3.751   0.80 30.47  ? 196 THR B O     1 
ATOM   9793  C  CB    A THR B 2 196 ? 19.253  -11.912 1.498   0.20 31.34  ? 196 THR B CB    1 
ATOM   9794  C  CB    B THR B 2 196 ? 19.376  -12.133 1.942   0.80 31.25  ? 196 THR B CB    1 
ATOM   9795  O  OG1   A THR B 2 196 ? 20.512  -11.438 1.988   0.20 33.87  ? 196 THR B OG1   1 
ATOM   9796  O  OG1   B THR B 2 196 ? 20.526  -11.779 2.726   0.80 32.82  ? 196 THR B OG1   1 
ATOM   9797  C  CG2   A THR B 2 196 ? 19.433  -12.461 0.092   0.20 29.56  ? 196 THR B CG2   1 
ATOM   9798  C  CG2   B THR B 2 196 ? 19.791  -12.541 0.543   0.80 29.13  ? 196 THR B CG2   1 
ATOM   9799  N  N     A ASP B 2 197 ? 17.165  -10.944 3.657   0.20 32.77  ? 197 ASP B N     1 
ATOM   9800  N  N     B ASP B 2 197 ? 17.107  -11.090 3.916   0.80 33.71  ? 197 ASP B N     1 
ATOM   9801  C  CA    A ASP B 2 197 ? 16.864  -10.582 5.036   0.20 33.04  ? 197 ASP B CA    1 
ATOM   9802  C  CA    B ASP B 2 197 ? 16.811  -10.753 5.301   0.80 33.83  ? 197 ASP B CA    1 
ATOM   9803  C  C     A ASP B 2 197 ? 17.581  -11.453 6.060   0.20 27.72  ? 197 ASP B C     1 
ATOM   9804  C  C     B ASP B 2 197 ? 17.737  -11.479 6.262   0.80 26.94  ? 197 ASP B C     1 
ATOM   9805  O  O     A ASP B 2 197 ? 17.750  -11.017 7.205   0.20 31.22  ? 197 ASP B O     1 
ATOM   9806  O  O     B ASP B 2 197 ? 18.132  -10.913 7.287   0.80 31.71  ? 197 ASP B O     1 
ATOM   9807  C  CB    A ASP B 2 197 ? 15.350  -10.650 5.281   0.20 31.39  ? 197 ASP B CB    1 
ATOM   9808  C  CB    B ASP B 2 197 ? 15.349  -11.069 5.611   0.80 27.95  ? 197 ASP B CB    1 
ATOM   9809  C  CG    A ASP B 2 197 ? 14.560  -9.789  4.304   0.20 34.17  ? 197 ASP B CG    1 
ATOM   9810  C  CG    B ASP B 2 197 ? 14.405  -10.196 4.824   0.80 35.13  ? 197 ASP B CG    1 
ATOM   9811  O  OD1   A ASP B 2 197 ? 14.802  -8.562  4.245   0.20 22.46  ? 197 ASP B OD1   1 
ATOM   9812  O  OD1   B ASP B 2 197 ? 14.297  -9.003  5.171   0.80 40.56  ? 197 ASP B OD1   1 
ATOM   9813  O  OD2   A ASP B 2 197 ? 13.703  -10.345 3.584   0.20 32.93  ? 197 ASP B OD2   1 
ATOM   9814  O  OD2   B ASP B 2 197 ? 13.825  -10.684 3.824   0.80 33.87  ? 197 ASP B OD2   1 
ATOM   9815  N  N     A GLU B 2 198 ? 18.000  -12.661 5.688   0.20 27.10  ? 198 GLU B N     1 
ATOM   9816  N  N     B GLU B 2 198 ? 18.054  -12.742 5.979   0.80 26.43  ? 198 GLU B N     1 
ATOM   9817  C  CA    A GLU B 2 198 ? 18.757  -13.524 6.587   0.20 27.02  ? 198 GLU B CA    1 
ATOM   9818  C  CA    B GLU B 2 198 ? 18.881  -13.541 6.877   0.80 26.31  ? 198 GLU B CA    1 
ATOM   9819  C  C     A GLU B 2 198 ? 19.495  -14.572 5.763   0.20 29.27  ? 198 GLU B C     1 
ATOM   9820  C  C     B GLU B 2 198 ? 19.693  -14.534 6.060   0.80 28.75  ? 198 GLU B C     1 
ATOM   9821  O  O     A GLU B 2 198 ? 18.948  -15.096 4.790   0.20 29.68  ? 198 GLU B O     1 
ATOM   9822  O  O     B GLU B 2 198 ? 19.131  -15.259 5.233   0.80 32.00  ? 198 GLU B O     1 
ATOM   9823  C  CB    A GLU B 2 198 ? 17.839  -14.185 7.629   0.20 27.55  ? 198 GLU B CB    1 
ATOM   9824  C  CB    B GLU B 2 198 ? 18.015  -14.283 7.913   0.80 26.31  ? 198 GLU B CB    1 
ATOM   9825  C  CG    A GLU B 2 198 ? 16.565  -14.795 7.061   0.20 31.00  ? 198 GLU B CG    1 
ATOM   9826  C  CG    B GLU B 2 198 ? 16.573  -13.846 7.931   0.80 33.22  ? 198 GLU B CG    1 
ATOM   9827  C  CD    A GLU B 2 198 ? 15.556  -15.163 8.139   0.20 32.16  ? 198 GLU B CD    1 
ATOM   9828  C  CD    B GLU B 2 198 ? 15.691  -14.762 8.730   0.80 33.20  ? 198 GLU B CD    1 
ATOM   9829  O  OE1   A GLU B 2 198 ? 15.293  -14.323 9.027   0.20 31.27  ? 198 GLU B OE1   1 
ATOM   9830  O  OE1   B GLU B 2 198 ? 15.968  -14.948 9.927   0.80 40.37  ? 198 GLU B OE1   1 
ATOM   9831  O  OE2   A GLU B 2 198 ? 15.028  -16.294 8.100   0.20 33.35  ? 198 GLU B OE2   1 
ATOM   9832  O  OE2   B GLU B 2 198 ? 14.730  -15.297 8.152   0.80 34.80  ? 198 GLU B OE2   1 
ATOM   9833  N  N     A THR B 2 199 ? 20.739  -14.863 6.151   0.20 25.87  ? 199 THR B N     1 
ATOM   9834  N  N     B THR B 2 199 ? 21.005  -14.572 6.287   0.80 23.66  ? 199 THR B N     1 
ATOM   9835  C  CA    A THR B 2 199 ? 21.592  -15.784 5.405   0.20 26.70  ? 199 THR B CA    1 
ATOM   9836  C  CA    B THR B 2 199 ? 21.904  -15.424 5.515   0.80 26.44  ? 199 THR B CA    1 
ATOM   9837  C  C     A THR B 2 199 ? 22.410  -16.627 6.372   0.20 25.78  ? 199 THR B C     1 
ATOM   9838  C  C     B THR B 2 199 ? 22.712  -16.295 6.461   0.80 24.88  ? 199 THR B C     1 
ATOM   9839  O  O     A THR B 2 199 ? 22.972  -16.099 7.336   0.20 28.78  ? 199 THR B O     1 
ATOM   9840  O  O     B THR B 2 199 ? 23.445  -15.774 7.309   0.80 31.26  ? 199 THR B O     1 
ATOM   9841  C  CB    A THR B 2 199 ? 22.525  -15.026 4.446   0.20 27.24  ? 199 THR B CB    1 
ATOM   9842  C  CB    B THR B 2 199 ? 22.834  -14.585 4.632   0.80 26.21  ? 199 THR B CB    1 
ATOM   9843  O  OG1   A THR B 2 199 ? 21.766  -14.485 3.356   0.20 26.98  ? 199 THR B OG1   1 
ATOM   9844  O  OG1   B THR B 2 199 ? 22.059  -13.922 3.623   0.80 27.99  ? 199 THR B OG1   1 
ATOM   9845  C  CG2   A THR B 2 199 ? 23.610  -15.947 3.893   0.20 26.87  ? 199 THR B CG2   1 
ATOM   9846  C  CG2   B THR B 2 199 ? 23.898  -15.470 3.973   0.80 27.14  ? 199 THR B CG2   1 
ATOM   9847  N  N     A TYR B 2 200 ? 22.462  -17.937 6.118   0.20 25.12  ? 200 TYR B N     1 
ATOM   9848  N  N     B TYR B 2 200 ? 22.569  -17.613 6.318   0.80 22.02  ? 200 TYR B N     1 
ATOM   9849  C  CA    A TYR B 2 200 ? 23.281  -18.868 6.889   0.20 27.08  ? 200 TYR B CA    1 
ATOM   9850  C  CA    B TYR B 2 200 ? 23.383  -18.579 7.044   0.80 27.61  ? 200 TYR B CA    1 
ATOM   9851  C  C     A TYR B 2 200 ? 24.590  -19.085 6.139   0.20 25.79  ? 200 TYR B C     1 
ATOM   9852  C  C     B TYR B 2 200 ? 24.697  -18.749 6.297   0.80 23.56  ? 200 TYR B C     1 
ATOM   9853  O  O     A TYR B 2 200 ? 24.594  -19.647 5.038   0.20 26.83  ? 200 TYR B O     1 
ATOM   9854  O  O     B TYR B 2 200 ? 24.694  -19.155 5.130   0.80 28.81  ? 200 TYR B O     1 
ATOM   9855  C  CB    A TYR B 2 200 ? 22.559  -20.197 7.100   0.20 26.97  ? 200 TYR B CB    1 
ATOM   9856  C  CB    B TYR B 2 200 ? 22.675  -19.929 7.157   0.80 26.48  ? 200 TYR B CB    1 
ATOM   9857  C  CG    A TYR B 2 200 ? 21.315  -20.111 7.954   0.20 25.70  ? 200 TYR B CG    1 
ATOM   9858  C  CG    B TYR B 2 200 ? 21.479  -19.938 8.087   0.80 24.97  ? 200 TYR B CG    1 
ATOM   9859  C  CD1   A TYR B 2 200 ? 21.394  -20.161 9.339   0.20 29.86  ? 200 TYR B CD1   1 
ATOM   9860  C  CD1   B TYR B 2 200 ? 21.636  -20.160 9.452   0.80 29.94  ? 200 TYR B CD1   1 
ATOM   9861  C  CD2   A TYR B 2 200 ? 20.061  -19.988 7.374   0.20 29.41  ? 200 TYR B CD2   1 
ATOM   9862  C  CD2   B TYR B 2 200 ? 20.197  -19.721 7.602   0.80 29.79  ? 200 TYR B CD2   1 
ATOM   9863  C  CE1   A TYR B 2 200 ? 20.257  -20.085 10.124  0.20 28.71  ? 200 TYR B CE1   1 
ATOM   9864  C  CE1   B TYR B 2 200 ? 20.539  -20.164 10.308  0.80 29.00  ? 200 TYR B CE1   1 
ATOM   9865  C  CE2   A TYR B 2 200 ? 18.919  -19.911 8.148   0.20 30.32  ? 200 TYR B CE2   1 
ATOM   9866  C  CE2   B TYR B 2 200 ? 19.105  -19.720 8.446   0.80 30.45  ? 200 TYR B CE2   1 
ATOM   9867  C  CZ    A TYR B 2 200 ? 19.023  -19.961 9.522   0.20 28.78  ? 200 TYR B CZ    1 
ATOM   9868  C  CZ    B TYR B 2 200 ? 19.281  -19.949 9.795   0.80 26.89  ? 200 TYR B CZ    1 
ATOM   9869  O  OH    A TYR B 2 200 ? 17.885  -19.886 10.294  0.20 30.36  ? 200 TYR B OH    1 
ATOM   9870  O  OH    B TYR B 2 200 ? 18.181  -19.953 10.642  0.80 30.39  ? 200 TYR B OH    1 
ATOM   9871  N  N     A CYS B 2 201 ? 25.698  -18.656 6.739   0.20 28.57  ? 201 CYS B N     1 
ATOM   9872  N  N     B CYS B 2 201 ? 25.813  -18.449 6.957   0.80 28.96  ? 201 CYS B N     1 
ATOM   9873  C  CA    A CYS B 2 201 ? 27.013  -18.820 6.128   0.20 28.70  ? 201 CYS B CA    1 
ATOM   9874  C  CA    B CYS B 2 201 ? 27.126  -18.513 6.315   0.80 28.52  ? 201 CYS B CA    1 
ATOM   9875  C  C     A CYS B 2 201 ? 27.474  -20.263 6.293   0.20 29.45  ? 201 CYS B C     1 
ATOM   9876  C  C     B CYS B 2 201 ? 27.757  -19.870 6.605   0.80 30.42  ? 201 CYS B C     1 
ATOM   9877  O  O     A CYS B 2 201 ? 27.544  -20.770 7.416   0.20 26.60  ? 201 CYS B O     1 
ATOM   9878  O  O     B CYS B 2 201 ? 28.231  -20.126 7.721   0.80 26.29  ? 201 CYS B O     1 
ATOM   9879  C  CB    A CYS B 2 201 ? 28.018  -17.864 6.763   0.20 26.88  ? 201 CYS B CB    1 
ATOM   9880  C  CB    B CYS B 2 201 ? 28.016  -17.371 6.792   0.80 25.57  ? 201 CYS B CB    1 
ATOM   9881  S  SG    A CYS B 2 201 ? 27.470  -16.151 6.833   0.20 34.33  ? 201 CYS B SG    1 
ATOM   9882  S  SG    B CYS B 2 201 ? 27.595  -15.773 6.053   0.80 41.97  ? 201 CYS B SG    1 
ATOM   9883  N  N     A ILE B 2 202 ? 27.789  -20.922 5.184   0.20 27.53  ? 202 ILE B N     1 
ATOM   9884  N  N     B ILE B 2 202 ? 27.770  -20.735 5.591   0.80 31.38  ? 202 ILE B N     1 
ATOM   9885  C  CA    A ILE B 2 202 ? 28.238  -22.313 5.196   0.20 25.43  ? 202 ILE B CA    1 
ATOM   9886  C  CA    B ILE B 2 202 ? 28.330  -22.078 5.681   0.80 21.60  ? 202 ILE B CA    1 
ATOM   9887  C  C     A ILE B 2 202 ? 29.613  -22.332 4.539   0.20 27.93  ? 202 ILE B C     1 
ATOM   9888  C  C     B ILE B 2 202 ? 29.645  -22.047 4.926   0.80 31.02  ? 202 ILE B C     1 
ATOM   9889  O  O     A ILE B 2 202 ? 29.746  -22.543 3.332   0.20 29.02  ? 202 ILE B O     1 
ATOM   9890  O  O     B ILE B 2 202 ? 29.657  -21.815 3.714   0.80 24.86  ? 202 ILE B O     1 
ATOM   9891  C  CB    A ILE B 2 202 ? 27.256  -23.252 4.489   0.20 25.65  ? 202 ILE B CB    1 
ATOM   9892  C  CB    B ILE B 2 202 ? 27.382  -23.138 5.096   0.80 25.13  ? 202 ILE B CB    1 
ATOM   9893  C  CG1   A ILE B 2 202 ? 25.853  -23.099 5.084   0.20 27.07  ? 202 ILE B CG1   1 
ATOM   9894  C  CG1   B ILE B 2 202 ? 25.975  -22.991 5.697   0.80 29.27  ? 202 ILE B CG1   1 
ATOM   9895  C  CG2   A ILE B 2 202 ? 27.721  -24.695 4.604   0.20 26.54  ? 202 ILE B CG2   1 
ATOM   9896  C  CG2   B ILE B 2 202 ? 27.949  -24.531 5.324   0.80 26.99  ? 202 ILE B CG2   1 
ATOM   9897  C  CD1   A ILE B 2 202 ? 24.823  -24.027 4.479   0.20 26.26  ? 202 ILE B CD1   1 
ATOM   9898  C  CD1   B ILE B 2 202 ? 25.503  -24.190 6.489   0.80 28.74  ? 202 ILE B CD1   1 
ATOM   9899  N  N     A ASP B 2 203 ? 30.653  -22.108 5.340   0.20 28.04  ? 203 ASP B N     1 
ATOM   9900  N  N     B ASP B 2 203 ? 30.743  -22.271 5.633   0.80 26.98  ? 203 ASP B N     1 
ATOM   9901  C  CA    A ASP B 2 203 ? 32.011  -21.977 4.826   0.20 28.17  ? 203 ASP B CA    1 
ATOM   9902  C  CA    B ASP B 2 203 ? 32.081  -21.952 5.139   0.80 28.03  ? 203 ASP B CA    1 
ATOM   9903  C  C     A ASP B 2 203 ? 32.628  -23.350 4.591   0.20 28.94  ? 203 ASP B C     1 
ATOM   9904  C  C     B ASP B 2 203 ? 32.835  -23.245 4.853   0.80 29.17  ? 203 ASP B C     1 
ATOM   9905  O  O     A ASP B 2 203 ? 32.638  -24.198 5.488   0.20 31.00  ? 203 ASP B O     1 
ATOM   9906  O  O     B ASP B 2 203 ? 33.189  -23.982 5.781   0.80 30.57  ? 203 ASP B O     1 
ATOM   9907  C  CB    A ASP B 2 203 ? 32.860  -21.170 5.810   0.20 28.52  ? 203 ASP B CB    1 
ATOM   9908  C  CB    B ASP B 2 203 ? 32.810  -21.107 6.177   0.80 28.38  ? 203 ASP B CB    1 
ATOM   9909  C  CG    A ASP B 2 203 ? 34.313  -21.033 5.376   0.20 29.66  ? 203 ASP B CG    1 
ATOM   9910  C  CG    B ASP B 2 203 ? 34.128  -20.581 5.689   0.80 29.58  ? 203 ASP B CG    1 
ATOM   9911  O  OD1   A ASP B 2 203 ? 34.646  -21.335 4.211   0.20 26.68  ? 203 ASP B OD1   1 
ATOM   9912  O  OD1   B ASP B 2 203 ? 34.415  -20.666 4.471   0.80 25.46  ? 203 ASP B OD1   1 
ATOM   9913  O  OD2   A ASP B 2 203 ? 35.132  -20.614 6.219   0.20 29.57  ? 203 ASP B OD2   1 
ATOM   9914  O  OD2   B ASP B 2 203 ? 34.872  -20.065 6.544   0.80 27.51  ? 203 ASP B OD2   1 
ATOM   9915  N  N     A ASN B 2 204 ? 33.156  -23.563 3.383   0.20 29.67  ? 204 ASN B N     1 
ATOM   9916  N  N     B ASN B 2 204 ? 33.118  -23.508 3.576   0.80 29.11  ? 204 ASN B N     1 
ATOM   9917  C  CA    A ASN B 2 204 ? 33.850  -24.813 3.084   0.20 33.33  ? 204 ASN B CA    1 
ATOM   9918  C  CA    B ASN B 2 204 ? 33.864  -24.725 3.240   0.80 34.10  ? 204 ASN B CA    1 
ATOM   9919  C  C     A ASN B 2 204 ? 35.153  -24.955 3.861   0.20 33.68  ? 204 ASN B C     1 
ATOM   9920  C  C     B ASN B 2 204 ? 35.248  -24.775 3.886   0.80 34.44  ? 204 ASN B C     1 
ATOM   9921  O  O     A ASN B 2 204 ? 35.617  -26.081 4.071   0.20 32.24  ? 204 ASN B O     1 
ATOM   9922  O  O     B ASN B 2 204 ? 35.818  -25.864 4.008   0.80 31.74  ? 204 ASN B O     1 
ATOM   9923  C  CB    A ASN B 2 204 ? 34.144  -24.922 1.587   0.20 32.50  ? 204 ASN B CB    1 
ATOM   9924  C  CB    B ASN B 2 204 ? 34.023  -24.874 1.731   0.80 32.68  ? 204 ASN B CB    1 
ATOM   9925  C  CG    A ASN B 2 204 ? 32.886  -25.026 0.747   0.20 31.39  ? 204 ASN B CG    1 
ATOM   9926  C  CG    B ASN B 2 204 ? 32.854  -25.591 1.087   0.80 33.54  ? 204 ASN B CG    1 
ATOM   9927  O  OD1   A ASN B 2 204 ? 31.842  -25.479 1.220   0.20 28.63  ? 204 ASN B OD1   1 
ATOM   9928  O  OD1   B ASN B 2 204 ? 32.023  -26.205 1.768   0.80 27.19  ? 204 ASN B OD1   1 
ATOM   9929  N  ND2   A ASN B 2 204 ? 32.981  -24.612 -0.513  0.20 30.96  ? 204 ASN B ND2   1 
ATOM   9930  N  ND2   B ASN B 2 204 ? 32.799  -25.538 -0.238  0.80 34.58  ? 204 ASN B ND2   1 
ATOM   9931  N  N     A GLU B 2 205 ? 35.757  -23.841 4.284   0.20 32.13  ? 205 GLU B N     1 
ATOM   9932  N  N     B GLU B 2 205 ? 35.815  -23.632 4.284   0.80 32.33  ? 205 GLU B N     1 
ATOM   9933  C  CA    A GLU B 2 205 ? 37.006  -23.912 5.036   0.20 32.24  ? 205 GLU B CA    1 
ATOM   9934  C  CA    B GLU B 2 205 ? 37.035  -23.684 5.086   0.80 32.20  ? 205 GLU B CA    1 
ATOM   9935  C  C     A GLU B 2 205 ? 36.792  -24.567 6.396   0.20 33.15  ? 205 GLU B C     1 
ATOM   9936  C  C     B GLU B 2 205 ? 36.757  -24.318 6.444   0.80 33.59  ? 205 GLU B C     1 
ATOM   9937  O  O     A GLU B 2 205 ? 37.549  -25.462 6.792   0.20 34.59  ? 205 GLU B O     1 
ATOM   9938  O  O     B GLU B 2 205 ? 37.579  -25.078 6.966   0.80 34.76  ? 205 GLU B O     1 
ATOM   9939  C  CB    A GLU B 2 205 ? 37.596  -22.513 5.198   0.20 29.64  ? 205 GLU B CB    1 
ATOM   9940  C  CB    B GLU B 2 205 ? 37.627  -22.287 5.259   0.80 29.00  ? 205 GLU B CB    1 
ATOM   9941  C  CG    A GLU B 2 205 ? 38.854  -22.458 6.045   0.20 33.51  ? 205 GLU B CG    1 
ATOM   9942  C  CG    B GLU B 2 205 ? 38.841  -22.246 6.176   0.80 33.46  ? 205 GLU B CG    1 
ATOM   9943  C  CD    A GLU B 2 205 ? 40.099  -22.177 5.223   0.20 34.94  ? 205 GLU B CD    1 
ATOM   9944  C  CD    B GLU B 2 205 ? 40.095  -21.733 5.470   0.80 37.07  ? 205 GLU B CD    1 
ATOM   9945  O  OE1   A GLU B 2 205 ? 40.115  -22.519 4.022   0.20 30.07  ? 205 GLU B OE1   1 
ATOM   9946  O  OE1   B GLU B 2 205 ? 40.043  -21.504 4.248   0.80 29.80  ? 205 GLU B OE1   1 
ATOM   9947  O  OE2   A GLU B 2 205 ? 41.061  -21.607 5.779   0.20 37.60  ? 205 GLU B OE2   1 
ATOM   9948  O  OE2   B GLU B 2 205 ? 41.135  -21.560 6.141   0.80 39.27  ? 205 GLU B OE2   1 
ATOM   9949  N  N     A ALA B 2 206 ? 35.766  -24.129 7.129   0.20 29.75  ? 206 ALA B N     1 
ATOM   9950  N  N     B ALA B 2 206 ? 35.596  -24.022 7.023   0.80 28.46  ? 206 ALA B N     1 
ATOM   9951  C  CA    A ALA B 2 206 ? 35.474  -24.737 8.423   0.20 34.03  ? 206 ALA B CA    1 
ATOM   9952  C  CA    B ALA B 2 206 ? 35.223  -24.653 8.283   0.80 35.02  ? 206 ALA B CA    1 
ATOM   9953  C  C     A ALA B 2 206 ? 35.039  -26.189 8.266   0.20 30.82  ? 206 ALA B C     1 
ATOM   9954  C  C     B ALA B 2 206 ? 34.957  -26.143 8.095   0.80 29.91  ? 206 ALA B C     1 
ATOM   9955  O  O     A ALA B 2 206 ? 35.408  -27.045 9.079   0.20 33.49  ? 206 ALA B O     1 
ATOM   9956  O  O     B ALA B 2 206 ? 35.481  -26.977 8.844   0.80 33.23  ? 206 ALA B O     1 
ATOM   9957  C  CB    A ALA B 2 206 ? 34.403  -23.929 9.153   0.20 30.80  ? 206 ALA B CB    1 
ATOM   9958  C  CB    B ALA B 2 206 ? 33.997  -23.956 8.863   0.80 29.41  ? 206 ALA B CB    1 
ATOM   9959  N  N     A LEU B 2 207 ? 34.251  -26.485 7.228   0.20 30.70  ? 207 LEU B N     1 
ATOM   9960  N  N     B LEU B 2 207 ? 34.130  -26.490 7.105   0.80 30.46  ? 207 LEU B N     1 
ATOM   9961  C  CA    A LEU B 2 207 ? 33.854  -27.865 6.967   0.20 31.16  ? 207 LEU B CA    1 
ATOM   9962  C  CA    B LEU B 2 207 ? 33.756  -27.884 6.891   0.80 30.84  ? 207 LEU B CA    1 
ATOM   9963  C  C     A LEU B 2 207 ? 35.065  -28.746 6.687   0.20 32.26  ? 207 LEU B C     1 
ATOM   9964  C  C     B LEU B 2 207 ? 34.985  -28.758 6.651   0.80 32.16  ? 207 LEU B C     1 
ATOM   9965  O  O     A LEU B 2 207 ? 35.078  -29.926 7.060   0.20 33.33  ? 207 LEU B O     1 
ATOM   9966  O  O     B LEU B 2 207 ? 35.107  -29.847 7.223   0.80 32.88  ? 207 LEU B O     1 
ATOM   9967  C  CB    A LEU B 2 207 ? 32.877  -27.916 5.790   0.20 28.49  ? 207 LEU B CB    1 
ATOM   9968  C  CB    B LEU B 2 207 ? 32.785  -27.978 5.712   0.80 27.86  ? 207 LEU B CB    1 
ATOM   9969  C  CG    A LEU B 2 207 ? 31.541  -27.189 5.965   0.20 33.30  ? 207 LEU B CG    1 
ATOM   9970  C  CG    B LEU B 2 207 ? 31.475  -27.198 5.886   0.80 33.47  ? 207 LEU B CG    1 
ATOM   9971  C  CD1   A LEU B 2 207 ? 30.731  -27.232 4.677   0.20 32.10  ? 207 LEU B CD1   1 
ATOM   9972  C  CD1   B LEU B 2 207 ? 30.590  -27.325 4.651   0.80 31.83  ? 207 LEU B CD1   1 
ATOM   9973  C  CD2   A LEU B 2 207 ? 30.751  -27.787 7.114   0.20 31.20  ? 207 LEU B CD2   1 
ATOM   9974  C  CD2   B LEU B 2 207 ? 30.732  -27.655 7.133   0.80 30.94  ? 207 LEU B CD2   1 
ATOM   9975  N  N     A TYR B 2 208 ? 36.091  -28.193 6.040   0.20 33.98  ? 208 TYR B N     1 
ATOM   9976  N  N     B TYR B 2 208 ? 35.915  -28.287 5.824   0.80 34.40  ? 208 TYR B N     1 
ATOM   9977  C  CA    A TYR B 2 208 ? 37.304  -28.961 5.785   0.20 31.85  ? 208 TYR B CA    1 
ATOM   9978  C  CA    B TYR B 2 208 ? 37.129  -29.058 5.573   0.80 30.04  ? 208 TYR B CA    1 
ATOM   9979  C  C     A TYR B 2 208 ? 38.127  -29.127 7.056   0.20 36.62  ? 208 TYR B C     1 
ATOM   9980  C  C     B TYR B 2 208 ? 37.977  -29.179 6.830   0.80 36.24  ? 208 TYR B C     1 
ATOM   9981  O  O     A TYR B 2 208 ? 38.674  -30.206 7.311   0.20 37.42  ? 208 TYR B O     1 
ATOM   9982  O  O     B TYR B 2 208 ? 38.534  -30.249 7.108   0.80 36.59  ? 208 TYR B O     1 
ATOM   9983  C  CB    A TYR B 2 208 ? 38.131  -28.285 4.691   0.20 38.10  ? 208 TYR B CB    1 
ATOM   9984  C  CB    B TYR B 2 208 ? 37.941  -28.416 4.449   0.80 39.47  ? 208 TYR B CB    1 
ATOM   9985  C  CG    A TYR B 2 208 ? 39.410  -29.014 4.345   0.20 36.12  ? 208 TYR B CG    1 
ATOM   9986  C  CG    B TYR B 2 208 ? 39.270  -29.101 4.218   0.80 35.24  ? 208 TYR B CG    1 
ATOM   9987  C  CD1   A TYR B 2 208 ? 39.412  -30.049 3.419   0.20 40.29  ? 208 TYR B CD1   1 
ATOM   9988  C  CD1   B TYR B 2 208 ? 39.363  -30.202 3.384   0.80 40.38  ? 208 TYR B CD1   1 
ATOM   9989  C  CD2   A TYR B 2 208 ? 40.616  -28.664 4.939   0.20 39.00  ? 208 TYR B CD2   1 
ATOM   9990  C  CD2   B TYR B 2 208 ? 40.426  -28.654 4.847   0.80 38.70  ? 208 TYR B CD2   1 
ATOM   9991  C  CE1   A TYR B 2 208 ? 40.579  -30.718 3.099   0.20 44.61  ? 208 TYR B CE1   1 
ATOM   9992  C  CE1   B TYR B 2 208 ? 40.574  -30.842 3.176   0.80 44.90  ? 208 TYR B CE1   1 
ATOM   9993  C  CE2   A TYR B 2 208 ? 41.786  -29.327 4.626   0.20 43.32  ? 208 TYR B CE2   1 
ATOM   9994  C  CE2   B TYR B 2 208 ? 41.638  -29.285 4.648   0.80 43.53  ? 208 TYR B CE2   1 
ATOM   9995  C  CZ    A TYR B 2 208 ? 41.762  -30.352 3.705   0.20 45.00  ? 208 TYR B CZ    1 
ATOM   9996  C  CZ    B TYR B 2 208 ? 41.706  -30.377 3.809   0.80 45.03  ? 208 TYR B CZ    1 
ATOM   9997  O  OH    A TYR B 2 208 ? 42.925  -31.016 3.388   0.20 50.49  ? 208 TYR B OH    1 
ATOM   9998  O  OH    B TYR B 2 208 ? 42.913  -31.013 3.602   0.80 51.61  ? 208 TYR B OH    1 
ATOM   9999  N  N     A ASP B 2 209 ? 38.226  -28.068 7.864   0.20 34.70  ? 209 ASP B N     1 
ATOM   10000 N  N     B ASP B 2 209 ? 38.104  -28.084 7.588   0.80 34.32  ? 209 ASP B N     1 
ATOM   10001 C  CA    A ASP B 2 209 ? 38.998  -28.147 9.098   0.20 38.85  ? 209 ASP B CA    1 
ATOM   10002 C  CA    B ASP B 2 209 ? 38.884  -28.120 8.818   0.80 38.74  ? 209 ASP B CA    1 
ATOM   10003 C  C     A ASP B 2 209 ? 38.369  -29.111 10.097  0.20 38.76  ? 209 ASP B C     1 
ATOM   10004 C  C     B ASP B 2 209 ? 38.265  -29.079 9.829   0.80 39.91  ? 209 ASP B C     1 
ATOM   10005 O  O     A ASP B 2 209 ? 39.083  -29.714 10.905  0.20 37.08  ? 209 ASP B O     1 
ATOM   10006 O  O     B ASP B 2 209 ? 38.988  -29.793 10.530  0.80 32.82  ? 209 ASP B O     1 
ATOM   10007 C  CB    A ASP B 2 209 ? 39.145  -26.755 9.718   0.20 39.61  ? 209 ASP B CB    1 
ATOM   10008 C  CB    B ASP B 2 209 ? 39.015  -26.710 9.414   0.80 39.78  ? 209 ASP B CB    1 
ATOM   10009 C  CG    A ASP B 2 209 ? 39.981  -25.813 8.860   0.20 40.47  ? 209 ASP B CG    1 
ATOM   10010 C  CG    B ASP B 2 209 ? 40.039  -25.825 8.668   0.80 40.92  ? 209 ASP B CG    1 
ATOM   10011 O  OD1   A ASP B 2 209 ? 40.556  -26.269 7.847   0.20 40.75  ? 209 ASP B OD1   1 
ATOM   10012 O  OD1   B ASP B 2 209 ? 40.909  -26.363 7.943   0.80 40.52  ? 209 ASP B OD1   1 
ATOM   10013 O  OD2   A ASP B 2 209 ? 40.059  -24.612 9.200   0.20 39.54  ? 209 ASP B OD2   1 
ATOM   10014 O  OD2   B ASP B 2 209 ? 39.973  -24.579 8.818   0.80 40.09  ? 209 ASP B OD2   1 
ATOM   10015 N  N     A ILE B 2 210 ? 37.044  -29.271 10.056  0.20 35.32  ? 210 ILE B N     1 
ATOM   10016 N  N     B ILE B 2 210 ? 36.926  -29.114 9.907   0.80 34.66  ? 210 ILE B N     1 
ATOM   10017 C  CA    A ILE B 2 210 ? 36.376  -30.207 10.957  0.20 38.62  ? 210 ILE B CA    1 
ATOM   10018 C  CA    B ILE B 2 210 ? 36.235  -30.030 10.814  0.80 38.46  ? 210 ILE B CA    1 
ATOM   10019 C  C     A ILE B 2 210 ? 36.623  -31.644 10.512  0.20 39.92  ? 210 ILE B C     1 
ATOM   10020 C  C     B ILE B 2 210 ? 36.525  -31.479 10.441  0.80 39.57  ? 210 ILE B C     1 
ATOM   10021 O  O     A ILE B 2 210 ? 36.963  -32.513 11.324  0.20 41.30  ? 210 ILE B O     1 
ATOM   10022 O  O     B ILE B 2 210 ? 36.935  -32.286 11.285  0.80 40.99  ? 210 ILE B O     1 
ATOM   10023 C  CB    A ILE B 2 210 ? 34.871  -29.894 11.038  0.20 36.45  ? 210 ILE B CB    1 
ATOM   10024 C  CB    B ILE B 2 210 ? 34.718  -29.760 10.813  0.80 35.81  ? 210 ILE B CB    1 
ATOM   10025 C  CG1   A ILE B 2 210 ? 34.637  -28.575 11.779  0.20 36.97  ? 210 ILE B CG1   1 
ATOM   10026 C  CG1   B ILE B 2 210 ? 34.389  -28.414 11.464  0.80 38.71  ? 210 ILE B CG1   1 
ATOM   10027 C  CG2   A ILE B 2 210 ? 34.123  -31.036 11.715  0.20 38.08  ? 210 ILE B CG2   1 
ATOM   10028 C  CG2   B ILE B 2 210 ? 33.978  -30.896 11.524  0.80 37.87  ? 210 ILE B CG2   1 
ATOM   10029 C  CD1   A ILE B 2 210 ? 33.200  -28.102 11.742  0.20 33.01  ? 210 ILE B CD1   1 
ATOM   10030 C  CD1   B ILE B 2 210 ? 32.947  -27.982 11.250  0.80 28.45  ? 210 ILE B CD1   1 
ATOM   10031 N  N     A CYS B 2 211 ? 36.454  -31.917 9.217   0.20 41.71  ? 211 CYS B N     1 
ATOM   10032 N  N     B CYS B 2 211 ? 36.280  -31.838 9.180   0.80 42.36  ? 211 CYS B N     1 
ATOM   10033 C  CA    A CYS B 2 211 ? 36.642  -33.276 8.719   0.20 41.25  ? 211 CYS B CA    1 
ATOM   10034 C  CA    B CYS B 2 211 ? 36.551  -33.199 8.729   0.80 41.17  ? 211 CYS B CA    1 
ATOM   10035 C  C     A CYS B 2 211 ? 38.098  -33.714 8.824   0.20 41.94  ? 211 CYS B C     1 
ATOM   10036 C  C     B CYS B 2 211 ? 38.014  -33.574 8.967   0.80 40.80  ? 211 CYS B C     1 
ATOM   10037 O  O     A CYS B 2 211 ? 38.380  -34.886 9.098   0.20 46.40  ? 211 CYS B O     1 
ATOM   10038 O  O     B CYS B 2 211 ? 38.313  -34.557 9.653   0.80 45.51  ? 211 CYS B O     1 
ATOM   10039 C  CB    A CYS B 2 211 ? 36.159  -33.378 7.272   0.20 40.84  ? 211 CYS B CB    1 
ATOM   10040 C  CB    B CYS B 2 211 ? 36.182  -33.345 7.246   0.80 40.80  ? 211 CYS B CB    1 
ATOM   10041 S  SG    A CYS B 2 211 ? 34.386  -33.112 7.042   0.20 40.64  ? 211 CYS B SG    1 
ATOM   10042 S  SG    B CYS B 2 211 ? 34.417  -33.117 6.801   0.80 40.24  ? 211 CYS B SG    1 
ATOM   10043 N  N     A PHE B 2 212 ? 39.038  -32.789 8.615   0.20 44.82  ? 212 PHE B N     1 
ATOM   10044 N  N     B PHE B 2 212 ? 38.945  -32.780 8.432   0.80 45.35  ? 212 PHE B N     1 
ATOM   10045 C  CA    A PHE B 2 212 ? 40.448  -33.164 8.588   0.20 44.18  ? 212 PHE B CA    1 
ATOM   10046 C  CA    B PHE B 2 212 ? 40.358  -33.159 8.468   0.80 43.94  ? 212 PHE B CA    1 
ATOM   10047 C  C     A PHE B 2 212 ? 41.038  -33.265 9.989   0.20 45.66  ? 212 PHE B C     1 
ATOM   10048 C  C     B PHE B 2 212 ? 40.909  -33.182 9.891   0.80 45.69  ? 212 PHE B C     1 
ATOM   10049 O  O     A PHE B 2 212 ? 41.794  -34.199 10.280  0.20 46.47  ? 212 PHE B O     1 
ATOM   10050 O  O     B PHE B 2 212 ? 41.387  -34.218 10.369  0.80 46.34  ? 212 PHE B O     1 
ATOM   10051 C  CB    A PHE B 2 212 ? 41.241  -32.157 7.753   0.20 43.07  ? 212 PHE B CB    1 
ATOM   10052 C  CB    B PHE B 2 212 ? 41.192  -32.208 7.601   0.80 42.54  ? 212 PHE B CB    1 
ATOM   10053 C  CG    A PHE B 2 212 ? 42.710  -32.466 7.661   0.20 49.87  ? 212 PHE B CG    1 
ATOM   10054 C  CG    B PHE B 2 212 ? 42.670  -32.523 7.610   0.80 50.03  ? 212 PHE B CG    1 
ATOM   10055 C  CD1   A PHE B 2 212 ? 43.174  -33.439 6.790   0.20 51.21  ? 212 PHE B CD1   1 
ATOM   10056 C  CD1   B PHE B 2 212 ? 43.194  -33.472 6.750   0.80 51.37  ? 212 PHE B CD1   1 
ATOM   10057 C  CD2   A PHE B 2 212 ? 43.628  -31.778 8.438   0.20 52.38  ? 212 PHE B CD2   1 
ATOM   10058 C  CD2   B PHE B 2 212 ? 43.531  -31.880 8.489   0.80 53.19  ? 212 PHE B CD2   1 
ATOM   10059 C  CE1   A PHE B 2 212 ? 44.526  -33.724 6.702   0.20 50.38  ? 212 PHE B CE1   1 
ATOM   10060 C  CE1   B PHE B 2 212 ? 44.552  -33.771 6.762   0.80 50.41  ? 212 PHE B CE1   1 
ATOM   10061 C  CE2   A PHE B 2 212 ? 44.981  -32.059 8.354   0.20 48.62  ? 212 PHE B CE2   1 
ATOM   10062 C  CE2   B PHE B 2 212 ? 44.889  -32.179 8.506   0.80 48.54  ? 212 PHE B CE2   1 
ATOM   10063 C  CZ    A PHE B 2 212 ? 45.429  -33.032 7.484   0.20 47.04  ? 212 PHE B CZ    1 
ATOM   10064 C  CZ    B PHE B 2 212 ? 45.396  -33.124 7.640   0.80 46.76  ? 212 PHE B CZ    1 
ATOM   10065 N  N     A ARG B 2 213 ? 40.716  -32.318 10.868  0.20 44.32  ? 213 ARG B N     1 
ATOM   10066 N  N     B ARG B 2 213 ? 40.885  -32.037 10.575  0.80 44.66  ? 213 ARG B N     1 
ATOM   10067 C  CA    A ARG B 2 213 ? 41.349  -32.284 12.181  0.20 43.46  ? 213 ARG B CA    1 
ATOM   10068 C  CA    B ARG B 2 213 ? 41.593  -31.925 11.845  0.80 41.88  ? 213 ARG B CA    1 
ATOM   10069 C  C     A ARG B 2 213 ? 40.509  -32.985 13.245  0.20 45.66  ? 213 ARG B C     1 
ATOM   10070 C  C     B ARG B 2 213 ? 40.863  -32.618 12.989  0.80 45.90  ? 213 ARG B C     1 
ATOM   10071 O  O     A ARG B 2 213 ? 41.037  -33.779 14.029  0.20 47.62  ? 213 ARG B O     1 
ATOM   10072 O  O     B ARG B 2 213 ? 41.515  -33.178 13.879  0.80 48.50  ? 213 ARG B O     1 
ATOM   10073 C  CB    A ARG B 2 213 ? 41.629  -30.837 12.592  0.20 45.85  ? 213 ARG B CB    1 
ATOM   10074 C  CB    B ARG B 2 213 ? 41.833  -30.453 12.189  0.80 44.27  ? 213 ARG B CB    1 
ATOM   10075 C  CG    A ARG B 2 213 ? 42.622  -30.121 11.695  0.20 46.38  ? 213 ARG B CG    1 
ATOM   10076 C  CG    B ARG B 2 213 ? 42.847  -29.764 11.290  0.80 48.93  ? 213 ARG B CG    1 
ATOM   10077 C  CD    A ARG B 2 213 ? 42.980  -28.752 12.251  0.20 50.85  ? 213 ARG B CD    1 
ATOM   10078 C  CD    B ARG B 2 213 ? 43.250  -28.388 11.818  0.80 53.59  ? 213 ARG B CD    1 
ATOM   10079 N  NE    A ARG B 2 213 ? 43.896  -28.036 11.370  0.20 51.73  ? 213 ARG B NE    1 
ATOM   10080 N  NE    B ARG B 2 213 ? 42.192  -27.393 11.683  0.80 59.18  ? 213 ARG B NE    1 
ATOM   10081 C  CZ    A ARG B 2 213 ? 45.215  -28.168 11.394  0.20 49.82  ? 213 ARG B CZ    1 
ATOM   10082 C  CZ    B ARG B 2 213 ? 41.398  -27.005 12.672  0.80 55.67  ? 213 ARG B CZ    1 
ATOM   10083 N  NH1   A ARG B 2 213 ? 45.815  -28.967 12.261  0.20 49.61  ? 213 ARG B NH1   1 
ATOM   10084 N  NH1   B ARG B 2 213 ? 41.518  -27.505 13.891  0.80 63.43  ? 213 ARG B NH1   1 
ATOM   10085 N  NH2   A ARG B 2 213 ? 45.950  -27.486 10.520  0.20 44.85  ? 213 ARG B NH2   1 
ATOM   10086 N  NH2   B ARG B 2 213 ? 40.460  -26.091 12.433  0.80 59.82  ? 213 ARG B NH2   1 
ATOM   10087 N  N     A THR B 2 214 ? 39.205  -32.704 13.290  0.20 43.35  ? 214 THR B N     1 
ATOM   10088 N  N     B THR B 2 214 ? 39.530  -32.604 12.985  0.80 43.20  ? 214 THR B N     1 
ATOM   10089 C  CA    A THR B 2 214 ? 38.359  -33.314 14.309  0.20 44.91  ? 214 THR B CA    1 
ATOM   10090 C  CA    B THR B 2 214 ? 38.748  -33.132 14.097  0.80 45.21  ? 214 THR B CA    1 
ATOM   10091 C  C     A THR B 2 214 ? 37.959  -34.735 13.926  0.20 46.06  ? 214 THR B C     1 
ATOM   10092 C  C     B THR B 2 214 ? 38.169  -34.516 13.829  0.80 46.19  ? 214 THR B C     1 
ATOM   10093 O  O     A THR B 2 214 ? 38.140  -35.671 14.712  0.20 47.50  ? 214 THR B O     1 
ATOM   10094 O  O     B THR B 2 214 ? 38.249  -35.389 14.700  0.80 47.70  ? 214 THR B O     1 
ATOM   10095 C  CB    A THR B 2 214 ? 37.120  -32.452 14.548  0.20 43.75  ? 214 THR B CB    1 
ATOM   10096 C  CB    B THR B 2 214 ? 37.622  -32.153 14.449  0.80 44.36  ? 214 THR B CB    1 
ATOM   10097 O  OG1   A THR B 2 214 ? 37.508  -31.220 15.170  0.20 43.42  ? 214 THR B OG1   1 
ATOM   10098 O  OG1   B THR B 2 214 ? 38.198  -30.918 14.897  0.80 42.10  ? 214 THR B OG1   1 
ATOM   10099 C  CG2   A THR B 2 214 ? 36.131  -33.178 15.447  0.20 46.03  ? 214 THR B CG2   1 
ATOM   10100 C  CG2   B THR B 2 214 ? 36.731  -32.717 15.543  0.80 49.15  ? 214 THR B CG2   1 
ATOM   10101 N  N     A LEU B 2 215 ? 37.418  -34.916 12.721  0.20 43.72  ? 215 LEU B N     1 
ATOM   10102 N  N     B LEU B 2 215 ? 37.609  -34.754 12.644  0.80 42.70  ? 215 LEU B N     1 
ATOM   10103 C  CA    A LEU B 2 215 ? 36.970  -36.232 12.280  0.20 48.20  ? 215 LEU B CA    1 
ATOM   10104 C  CA    B LEU B 2 215 ? 37.006  -36.042 12.307  0.80 48.68  ? 215 LEU B CA    1 
ATOM   10105 C  C     A LEU B 2 215 ? 38.108  -37.120 11.792  0.20 48.64  ? 215 LEU B C     1 
ATOM   10106 C  C     B LEU B 2 215 ? 37.993  -37.050 11.722  0.80 48.68  ? 215 LEU B C     1 
ATOM   10107 O  O     A LEU B 2 215 ? 37.886  -38.320 11.591  0.20 48.84  ? 215 LEU B O     1 
ATOM   10108 O  O     B LEU B 2 215 ? 37.581  -38.162 11.379  0.80 49.57  ? 215 LEU B O     1 
ATOM   10109 C  CB    A LEU B 2 215 ? 35.924  -36.085 11.172  0.20 44.92  ? 215 LEU B CB    1 
ATOM   10110 C  CB    B LEU B 2 215 ? 35.850  -35.850 11.316  0.80 44.46  ? 215 LEU B CB    1 
ATOM   10111 C  CG    A LEU B 2 215 ? 34.684  -35.259 11.526  0.20 45.00  ? 215 LEU B CG    1 
ATOM   10112 C  CG    B LEU B 2 215 ? 34.606  -35.120 11.817  0.80 43.95  ? 215 LEU B CG    1 
ATOM   10113 C  CD1   A LEU B 2 215 ? 33.727  -35.191 10.347  0.20 44.52  ? 215 LEU B CD1   1 
ATOM   10114 C  CD1   B LEU B 2 215 ? 33.541  -35.102 10.737  0.80 43.51  ? 215 LEU B CD1   1 
ATOM   10115 C  CD2   A LEU B 2 215 ? 33.991  -35.828 12.753  0.20 48.06  ? 215 LEU B CD2   1 
ATOM   10116 C  CD2   B LEU B 2 215 ? 34.086  -35.776 13.079  0.80 48.08  ? 215 LEU B CD2   1 
ATOM   10117 N  N     A LYS B 2 216 ? 39.306  -36.567 11.598  0.20 48.96  ? 216 LYS B N     1 
ATOM   10118 N  N     B LYS B 2 216 ? 39.268  -36.691 11.575  0.80 49.10  ? 216 LYS B N     1 
ATOM   10119 C  CA    A LYS B 2 216 ? 40.477  -37.320 11.144  0.20 49.94  ? 216 LYS B CA    1 
ATOM   10120 C  CA    B LYS B 2 216 ? 40.334  -37.595 11.149  0.80 49.86  ? 216 LYS B CA    1 
ATOM   10121 C  C     A LYS B 2 216 ? 40.218  -37.986 9.789   0.20 51.92  ? 216 LYS B C     1 
ATOM   10122 C  C     B LYS B 2 216 ? 40.193  -38.081 9.708   0.80 52.12  ? 216 LYS B C     1 
ATOM   10123 O  O     A LYS B 2 216 ? 40.336  -39.202 9.625   0.20 53.00  ? 216 LYS B O     1 
ATOM   10124 O  O     B LYS B 2 216 ? 40.934  -38.982 9.296   0.80 53.84  ? 216 LYS B O     1 
ATOM   10125 C  CB    A LYS B 2 216 ? 40.910  -38.352 12.192  0.20 53.47  ? 216 LYS B CB    1 
ATOM   10126 C  CB    B LYS B 2 216 ? 40.440  -38.816 12.074  0.80 52.86  ? 216 LYS B CB    1 
ATOM   10127 C  CG    A LYS B 2 216 ? 42.223  -38.024 12.886  0.20 54.81  ? 216 LYS B CG    1 
ATOM   10128 C  CG    B LYS B 2 216 ? 40.473  -38.484 13.565  0.80 60.28  ? 216 LYS B CG    1 
ATOM   10129 C  CD    A LYS B 2 216 ? 42.128  -36.725 13.668  0.20 55.65  ? 216 LYS B CD    1 
ATOM   10130 C  CD    B LYS B 2 216 ? 41.748  -37.751 13.946  0.80 56.67  ? 216 LYS B CD    1 
ATOM   10131 C  CE    A LYS B 2 216 ? 43.450  -36.377 14.337  0.20 55.15  ? 216 LYS B CE    1 
ATOM   10132 C  CE    B LYS B 2 216 ? 41.815  -37.500 15.442  0.80 68.62  ? 216 LYS B CE    1 
ATOM   10133 N  NZ    A LYS B 2 216 ? 43.861  -37.409 15.328  0.20 59.49  ? 216 LYS B NZ    1 
ATOM   10134 N  NZ    B LYS B 2 216 ? 41.754  -38.772 16.218  0.80 76.79  ? 216 LYS B NZ    1 
ATOM   10135 N  N     A LEU B 2 217 ? 39.859  -37.158 8.812   0.20 49.42  ? 217 LEU B N     1 
ATOM   10136 N  N     B LEU B 2 217 ? 39.277  -37.521 8.922   0.80 46.62  ? 217 LEU B N     1 
ATOM   10137 C  CA    A LEU B 2 217 ? 39.719  -37.581 7.422   0.20 49.95  ? 217 LEU B CA    1 
ATOM   10138 C  CA    B LEU B 2 217 ? 39.128  -37.931 7.527   0.80 48.56  ? 217 LEU B CA    1 
ATOM   10139 C  C     A LEU B 2 217 ? 40.840  -36.924 6.627   0.20 52.43  ? 217 LEU B C     1 
ATOM   10140 C  C     B LEU B 2 217 ? 40.260  -37.316 6.713   0.80 51.56  ? 217 LEU B C     1 
ATOM   10141 O  O     A LEU B 2 217 ? 40.862  -35.699 6.468   0.20 52.20  ? 217 LEU B O     1 
ATOM   10142 O  O     B LEU B 2 217 ? 40.253  -36.112 6.439   0.80 55.75  ? 217 LEU B O     1 
ATOM   10143 C  CB    A LEU B 2 217 ? 38.347  -37.209 6.864   0.20 51.29  ? 217 LEU B CB    1 
ATOM   10144 C  CB    B LEU B 2 217 ? 37.763  -37.508 6.988   0.80 52.65  ? 217 LEU B CB    1 
ATOM   10145 C  CG    A LEU B 2 217 ? 37.155  -37.941 7.484   0.20 49.70  ? 217 LEU B CG    1 
ATOM   10146 C  CG    B LEU B 2 217 ? 36.559  -37.874 7.860   0.80 50.59  ? 217 LEU B CG    1 
ATOM   10147 C  CD1   A LEU B 2 217 ? 35.848  -37.482 6.854   0.20 49.39  ? 217 LEU B CD1   1 
ATOM   10148 C  CD1   B LEU B 2 217 ? 35.249  -37.359 7.268   0.80 46.22  ? 217 LEU B CD1   1 
ATOM   10149 C  CD2   A LEU B 2 217 ? 37.323  -39.445 7.342   0.20 51.82  ? 217 LEU B CD2   1 
ATOM   10150 C  CD2   B LEU B 2 217 ? 36.488  -39.379 8.084   0.80 57.10  ? 217 LEU B CD2   1 
ATOM   10151 N  N     A THR B 2 218 ? 41.774  -37.741 6.134   0.20 55.60  ? 218 THR B N     1 
ATOM   10152 N  N     B THR B 2 218 ? 41.234  -38.141 6.318   0.80 57.97  ? 218 THR B N     1 
ATOM   10153 C  CA    A THR B 2 218 ? 42.941  -37.197 5.446   0.20 53.90  ? 218 THR B CA    1 
ATOM   10154 C  CA    B THR B 2 218 ? 42.449  -37.611 5.704   0.80 53.18  ? 218 THR B CA    1 
ATOM   10155 C  C     A THR B 2 218 ? 42.556  -36.535 4.128   0.20 56.46  ? 218 THR B C     1 
ATOM   10156 C  C     B THR B 2 218 ? 42.153  -36.892 4.393   0.80 54.60  ? 218 THR B C     1 
ATOM   10157 O  O     A THR B 2 218 ? 43.146  -35.518 3.743   0.20 54.99  ? 218 THR B O     1 
ATOM   10158 O  O     B THR B 2 218 ? 42.810  -35.898 4.058   0.80 58.98  ? 218 THR B O     1 
ATOM   10159 C  CB    A THR B 2 218 ? 43.973  -38.301 5.211   0.20 59.22  ? 218 THR B CB    1 
ATOM   10160 C  CB    B THR B 2 218 ? 43.460  -38.736 5.475   0.80 59.87  ? 218 THR B CB    1 
ATOM   10161 O  OG1   A THR B 2 218 ? 43.369  -39.378 4.482   0.20 54.72  ? 218 THR B OG1   1 
ATOM   10162 O  OG1   B THR B 2 218 ? 43.529  -39.565 6.640   0.80 62.71  ? 218 THR B OG1   1 
ATOM   10163 C  CG2   A THR B 2 218 ? 44.505  -38.826 6.538   0.20 56.35  ? 218 THR B CG2   1 
ATOM   10164 C  CG2   B THR B 2 218 ? 44.844  -38.154 5.197   0.80 62.38  ? 218 THR B CG2   1 
ATOM   10165 N  N     A THR B 2 219 ? 41.574  -37.093 3.421   0.20 54.65  ? 219 THR B N     1 
ATOM   10166 N  N     B THR B 2 219 ? 41.174  -37.380 3.631   0.80 53.60  ? 219 THR B N     1 
ATOM   10167 C  CA    A THR B 2 219 ? 41.121  -36.565 2.134   0.20 52.83  ? 219 THR B CA    1 
ATOM   10168 C  CA    B THR B 2 219 ? 40.834  -36.817 2.326   0.80 51.10  ? 219 THR B CA    1 
ATOM   10169 C  C     A THR B 2 219 ? 39.601  -36.468 2.151   0.20 53.90  ? 219 THR B C     1 
ATOM   10170 C  C     B THR B 2 219 ? 39.334  -36.557 2.281   0.80 54.15  ? 219 THR B C     1 
ATOM   10171 O  O     A THR B 2 219 ? 38.901  -37.380 1.689   0.20 53.91  ? 219 THR B O     1 
ATOM   10172 O  O     B THR B 2 219 ? 38.552  -37.425 1.869   0.80 54.66  ? 219 THR B O     1 
ATOM   10173 C  CB    A THR B 2 219 ? 41.607  -37.436 0.974   0.20 56.86  ? 219 THR B CB    1 
ATOM   10174 C  CB    B THR B 2 219 ? 41.270  -37.745 1.195   0.80 59.59  ? 219 THR B CB    1 
ATOM   10175 O  OG1   A THR B 2 219 ? 41.274  -38.807 1.228   0.20 60.55  ? 219 THR B OG1   1 
ATOM   10176 O  OG1   B THR B 2 219 ? 40.696  -39.043 1.397   0.80 63.04  ? 219 THR B OG1   1 
ATOM   10177 C  CG2   A THR B 2 219 ? 43.114  -37.307 0.803   0.20 54.85  ? 219 THR B CG2   1 
ATOM   10178 C  CG2   B THR B 2 219 ? 42.782  -37.869 1.166   0.80 52.77  ? 219 THR B CG2   1 
ATOM   10179 N  N     A PRO B 2 220 ? 39.056  -35.375 2.681   0.20 52.84  ? 220 PRO B N     1 
ATOM   10180 N  N     B PRO B 2 220 ? 38.894  -35.372 2.702   0.80 53.25  ? 220 PRO B N     1 
ATOM   10181 C  CA    A PRO B 2 220 ? 37.598  -35.217 2.703   0.20 52.32  ? 220 PRO B CA    1 
ATOM   10182 C  CA    B PRO B 2 220 ? 37.454  -35.088 2.723   0.80 52.94  ? 220 PRO B CA    1 
ATOM   10183 C  C     A PRO B 2 220 ? 37.036  -34.979 1.310   0.20 47.29  ? 220 PRO B C     1 
ATOM   10184 C  C     B PRO B 2 220 ? 36.873  -34.932 1.325   0.80 47.09  ? 220 PRO B C     1 
ATOM   10185 O  O     A PRO B 2 220 ? 37.665  -34.349 0.456   0.20 45.92  ? 220 PRO B O     1 
ATOM   10186 O  O     B PRO B 2 220 ? 37.487  -34.345 0.430   0.80 45.50  ? 220 PRO B O     1 
ATOM   10187 C  CB    A PRO B 2 220 ? 37.384  -33.991 3.602   0.20 48.04  ? 220 PRO B CB    1 
ATOM   10188 C  CB    B PRO B 2 220 ? 37.364  -33.774 3.513   0.80 47.85  ? 220 PRO B CB    1 
ATOM   10189 C  CG    A PRO B 2 220 ? 38.672  -33.819 4.351   0.20 47.49  ? 220 PRO B CG    1 
ATOM   10190 C  CG    B PRO B 2 220 ? 38.626  -33.710 4.300   0.80 47.33  ? 220 PRO B CG    1 
ATOM   10191 C  CD    A PRO B 2 220 ? 39.737  -34.296 3.413   0.20 50.07  ? 220 PRO B CD    1 
ATOM   10192 C  CD    B PRO B 2 220 ? 39.664  -34.331 3.403   0.80 50.02  ? 220 PRO B CD    1 
ATOM   10193 N  N     A THR B 2 221 ? 35.831  -35.491 1.090   0.20 43.57  ? 221 THR B N     1 
ATOM   10194 N  N     B THR B 2 221 ? 35.673  -35.469 1.150   0.80 42.88  ? 221 THR B N     1 
ATOM   10195 C  CA    A THR B 2 221 ? 35.124  -35.352 -0.173  0.20 45.01  ? 221 THR B CA    1 
ATOM   10196 C  CA    B THR B 2 221 ? 34.901  -35.366 -0.079  0.80 44.98  ? 221 THR B CA    1 
ATOM   10197 C  C     A THR B 2 221 ? 33.909  -34.449 0.011   0.20 42.68  ? 221 THR B C     1 
ATOM   10198 C  C     B THR B 2 221 ? 33.733  -34.410 0.144   0.80 42.50  ? 221 THR B C     1 
ATOM   10199 O  O     A THR B 2 221 ? 33.631  -33.949 1.105   0.20 40.88  ? 221 THR B O     1 
ATOM   10200 O  O     B THR B 2 221 ? 33.457  -33.984 1.268   0.80 40.12  ? 221 THR B O     1 
ATOM   10201 C  CB    A THR B 2 221 ? 34.699  -36.720 -0.713  0.20 49.45  ? 221 THR B CB    1 
ATOM   10202 C  CB    B THR B 2 221 ? 34.399  -36.754 -0.514  0.80 51.68  ? 221 THR B CB    1 
ATOM   10203 O  OG1   A THR B 2 221 ? 33.755  -37.316 0.188   0.20 44.28  ? 221 THR B OG1   1 
ATOM   10204 O  OG1   B THR B 2 221 ? 35.422  -37.732 -0.281  0.80 55.66  ? 221 THR B OG1   1 
ATOM   10205 C  CG2   A THR B 2 221 ? 35.906  -37.636 -0.863  0.20 50.21  ? 221 THR B CG2   1 
ATOM   10206 C  CG2   B THR B 2 221 ? 34.053  -36.776 -1.990  0.80 46.67  ? 221 THR B CG2   1 
ATOM   10207 N  N     A TYR B 2 222 ? 33.172  -34.249 -1.085  0.20 40.72  ? 222 TYR B N     1 
ATOM   10208 N  N     B TYR B 2 222 ? 33.050  -34.058 -0.950  0.80 40.25  ? 222 TYR B N     1 
ATOM   10209 C  CA    A TYR B 2 222 ? 31.932  -33.486 -1.016  0.20 39.65  ? 222 TYR B CA    1 
ATOM   10210 C  CA    B TYR B 2 222 ? 31.849  -33.240 -0.828  0.80 39.27  ? 222 TYR B CA    1 
ATOM   10211 C  C     A TYR B 2 222 ? 30.849  -34.211 -0.228  0.20 41.93  ? 222 TYR B C     1 
ATOM   10212 C  C     B TYR B 2 222 ? 30.775  -33.966 -0.033  0.80 43.00  ? 222 TYR B C     1 
ATOM   10213 O  O     A TYR B 2 222 ? 29.887  -33.568 0.206   0.20 41.67  ? 222 TYR B O     1 
ATOM   10214 O  O     B TYR B 2 222 ? 30.043  -33.342 0.743   0.80 42.27  ? 222 TYR B O     1 
ATOM   10215 C  CB    A TYR B 2 222 ? 31.424  -33.170 -2.423  0.20 40.98  ? 222 TYR B CB    1 
ATOM   10216 C  CB    B TYR B 2 222 ? 31.334  -32.847 -2.212  0.80 42.29  ? 222 TYR B CB    1 
ATOM   10217 C  CG    A TYR B 2 222 ? 32.044  -31.937 -3.039  0.20 35.28  ? 222 TYR B CG    1 
ATOM   10218 C  CG    B TYR B 2 222 ? 32.120  -31.718 -2.831  0.80 34.36  ? 222 TYR B CG    1 
ATOM   10219 C  CD1   A TYR B 2 222 ? 32.456  -30.871 -2.247  0.20 37.74  ? 222 TYR B CD1   1 
ATOM   10220 C  CD1   B TYR B 2 222 ? 32.369  -30.551 -2.115  0.80 37.18  ? 222 TYR B CD1   1 
ATOM   10221 C  CD2   A TYR B 2 222 ? 32.216  -31.837 -4.413  0.20 37.56  ? 222 TYR B CD2   1 
ATOM   10222 C  CD2   B TYR B 2 222 ? 32.638  -31.827 -4.113  0.80 37.20  ? 222 TYR B CD2   1 
ATOM   10223 C  CE1   A TYR B 2 222 ? 33.021  -29.742 -2.808  0.20 37.21  ? 222 TYR B CE1   1 
ATOM   10224 C  CE1   B TYR B 2 222 ? 33.096  -29.521 -2.661  0.80 36.48  ? 222 TYR B CE1   1 
ATOM   10225 C  CE2   A TYR B 2 222 ? 32.779  -30.715 -4.983  0.20 36.87  ? 222 TYR B CE2   1 
ATOM   10226 C  CE2   B TYR B 2 222 ? 33.368  -30.803 -4.672  0.80 37.91  ? 222 TYR B CE2   1 
ATOM   10227 C  CZ    A TYR B 2 222 ? 33.182  -29.672 -4.178  0.20 37.74  ? 222 TYR B CZ    1 
ATOM   10228 C  CZ    B TYR B 2 222 ? 33.598  -29.656 -3.946  0.80 38.85  ? 222 TYR B CZ    1 
ATOM   10229 O  OH    A TYR B 2 222 ? 33.743  -28.555 -4.746  0.20 34.36  ? 222 TYR B OH    1 
ATOM   10230 O  OH    B TYR B 2 222 ? 34.322  -28.637 -4.498  0.80 34.13  ? 222 TYR B OH    1 
ATOM   10231 N  N     A GLY B 2 223 ? 30.977  -35.523 -0.037  0.20 40.73  ? 223 GLY B N     1 
ATOM   10232 N  N     B GLY B 2 223 ? 30.684  -35.289 -0.197  0.80 39.26  ? 223 GLY B N     1 
ATOM   10233 C  CA    A GLY B 2 223 ? 30.018  -36.260 0.757   0.20 40.59  ? 223 GLY B CA    1 
ATOM   10234 C  CA    B GLY B 2 223 ? 29.780  -36.071 0.627   0.80 40.34  ? 223 GLY B CA    1 
ATOM   10235 C  C     A GLY B 2 223 ? 30.208  -36.037 2.243   0.20 44.50  ? 223 GLY B C     1 
ATOM   10236 C  C     B GLY B 2 223 ? 30.042  -35.892 2.110   0.80 45.42  ? 223 GLY B C     1 
ATOM   10237 O  O     A GLY B 2 223 ? 29.234  -35.931 2.994   0.20 41.21  ? 223 GLY B O     1 
ATOM   10238 O  O     B GLY B 2 223 ? 29.109  -35.716 2.895   0.80 40.55  ? 223 GLY B O     1 
ATOM   10239 N  N     A ASP B 2 224 ? 31.466  -35.963 2.682   0.20 44.98  ? 224 ASP B N     1 
ATOM   10240 N  N     B ASP B 2 224 ? 31.317  -35.919 2.511   0.80 46.18  ? 224 ASP B N     1 
ATOM   10241 C  CA    A ASP B 2 224 ? 31.737  -35.711 4.093   0.20 42.35  ? 224 ASP B CA    1 
ATOM   10242 C  CA    B ASP B 2 224 ? 31.662  -35.704 3.913   0.80 41.89  ? 224 ASP B CA    1 
ATOM   10243 C  C     A ASP B 2 224 ? 31.388  -34.279 4.471   0.20 43.35  ? 224 ASP B C     1 
ATOM   10244 C  C     B ASP B 2 224 ? 31.292  -34.300 4.361   0.80 43.80  ? 224 ASP B C     1 
ATOM   10245 O  O     A ASP B 2 224 ? 30.915  -34.024 5.585   0.20 38.52  ? 224 ASP B O     1 
ATOM   10246 O  O     B ASP B 2 224 ? 30.764  -34.114 5.464   0.80 37.84  ? 224 ASP B O     1 
ATOM   10247 C  CB    A ASP B 2 224 ? 33.204  -36.005 4.410   0.20 43.05  ? 224 ASP B CB    1 
ATOM   10248 C  CB    B ASP B 2 224 ? 33.157  -35.937 4.139   0.80 43.10  ? 224 ASP B CB    1 
ATOM   10249 C  CG    A ASP B 2 224 ? 33.640  -37.378 3.939   0.20 48.96  ? 224 ASP B CG    1 
ATOM   10250 C  CG    B ASP B 2 224 ? 33.614  -37.295 3.661   0.80 50.54  ? 224 ASP B CG    1 
ATOM   10251 O  OD1   A ASP B 2 224 ? 32.782  -38.281 3.854   0.20 48.31  ? 224 ASP B OD1   1 
ATOM   10252 O  OD1   B ASP B 2 224 ? 33.082  -38.301 4.164   0.80 48.96  ? 224 ASP B OD1   1 
ATOM   10253 O  OD2   A ASP B 2 224 ? 34.842  -37.549 3.648   0.20 47.35  ? 224 ASP B OD2   1 
ATOM   10254 O  OD2   B ASP B 2 224 ? 34.498  -37.350 2.775   0.80 45.42  ? 224 ASP B OD2   1 
ATOM   10255 N  N     A LEU B 2 225 ? 31.621  -33.331 3.561   0.20 38.92  ? 225 LEU B N     1 
ATOM   10256 N  N     B LEU B 2 225 ? 31.602  -33.296 3.535   0.80 38.53  ? 225 LEU B N     1 
ATOM   10257 C  CA    A LEU B 2 225 ? 31.300  -31.935 3.841   0.20 41.55  ? 225 LEU B CA    1 
ATOM   10258 C  CA    B LEU B 2 225 ? 31.282  -31.916 3.887   0.80 41.63  ? 225 LEU B CA    1 
ATOM   10259 C  C     A LEU B 2 225 ? 29.792  -31.717 3.879   0.20 38.48  ? 225 LEU B C     1 
ATOM   10260 C  C     B LEU B 2 225 ? 29.778  -31.717 4.022   0.80 38.25  ? 225 LEU B C     1 
ATOM   10261 O  O     A LEU B 2 225 ? 29.269  -31.086 4.805   0.20 38.68  ? 225 LEU B O     1 
ATOM   10262 O  O     B LEU B 2 225 ? 29.313  -31.042 4.948   0.80 38.81  ? 225 LEU B O     1 
ATOM   10263 C  CB    A LEU B 2 225 ? 31.949  -31.025 2.796   0.20 41.94  ? 225 LEU B CB    1 
ATOM   10264 C  CB    B LEU B 2 225 ? 31.847  -30.951 2.838   0.80 42.26  ? 225 LEU B CB    1 
ATOM   10265 C  CG    A LEU B 2 225 ? 33.473  -31.090 2.654   0.20 40.26  ? 225 LEU B CG    1 
ATOM   10266 C  CG    B LEU B 2 225 ? 33.355  -30.947 2.543   0.80 40.67  ? 225 LEU B CG    1 
ATOM   10267 C  CD1   A LEU B 2 225 ? 33.964  -30.052 1.657   0.20 37.00  ? 225 LEU B CD1   1 
ATOM   10268 C  CD1   B LEU B 2 225 ? 33.733  -29.749 1.685   0.80 36.34  ? 225 LEU B CD1   1 
ATOM   10269 C  CD2   A LEU B 2 225 ? 34.154  -30.906 4.002   0.20 36.22  ? 225 LEU B CD2   1 
ATOM   10270 C  CD2   B LEU B 2 225 ? 34.169  -30.953 3.832   0.80 36.09  ? 225 LEU B CD2   1 
ATOM   10271 N  N     A ASN B 2 226 ? 29.076  -32.230 2.875   0.20 39.29  ? 226 ASN B N     1 
ATOM   10272 N  N     B ASN B 2 226 ? 29.005  -32.284 3.094   0.80 39.32  ? 226 ASN B N     1 
ATOM   10273 C  CA    A ASN B 2 226 ? 27.626  -32.083 2.837   0.20 40.70  ? 226 ASN B CA    1 
ATOM   10274 C  CA    B ASN B 2 226 ? 27.562  -32.072 3.085   0.80 41.64  ? 226 ASN B CA    1 
ATOM   10275 C  C     A ASN B 2 226 ? 26.935  -32.871 3.943   0.20 38.18  ? 226 ASN B C     1 
ATOM   10276 C  C     B ASN B 2 226 ? 26.857  -32.843 4.193   0.80 38.32  ? 226 ASN B C     1 
ATOM   10277 O  O     A ASN B 2 226 ? 25.761  -32.614 4.228   0.20 38.12  ? 226 ASN B O     1 
ATOM   10278 O  O     B ASN B 2 226 ? 25.736  -32.482 4.565   0.80 36.45  ? 226 ASN B O     1 
ATOM   10279 C  CB    A ASN B 2 226 ? 27.092  -32.509 1.468   0.20 38.20  ? 226 ASN B CB    1 
ATOM   10280 C  CB    B ASN B 2 226 ? 26.993  -32.448 1.718   0.80 38.36  ? 226 ASN B CB    1 
ATOM   10281 C  CG    A ASN B 2 226 ? 27.562  -31.595 0.351   0.20 35.99  ? 226 ASN B CG    1 
ATOM   10282 C  CG    B ASN B 2 226 ? 27.573  -31.607 0.596   0.80 35.71  ? 226 ASN B CG    1 
ATOM   10283 O  OD1   A ASN B 2 226 ? 28.493  -30.810 0.526   0.20 37.58  ? 226 ASN B OD1   1 
ATOM   10284 O  OD1   B ASN B 2 226 ? 28.178  -30.565 0.831   0.80 39.77  ? 226 ASN B OD1   1 
ATOM   10285 N  ND2   A ASN B 2 226 ? 26.919  -31.693 -0.806  0.20 34.29  ? 226 ASN B ND2   1 
ATOM   10286 N  ND2   B ASN B 2 226 ? 27.378  -32.049 -0.630  0.80 31.95  ? 226 ASN B ND2   1 
ATOM   10287 N  N     A HIS B 2 227 ? 27.633  -33.822 4.568   0.20 36.68  ? 227 HIS B N     1 
ATOM   10288 N  N     B HIS B 2 227 ? 27.484  -33.885 4.738   0.80 35.34  ? 227 HIS B N     1 
ATOM   10289 C  CA    A HIS B 2 227 ? 27.079  -34.488 5.742   0.20 41.79  ? 227 HIS B CA    1 
ATOM   10290 C  CA    B HIS B 2 227 ? 26.931  -34.522 5.928   0.80 41.88  ? 227 HIS B CA    1 
ATOM   10291 C  C     A HIS B 2 227 ? 26.888  -33.499 6.884   0.20 41.85  ? 227 HIS B C     1 
ATOM   10292 C  C     B HIS B 2 227 ? 26.853  -33.522 7.070   0.80 42.18  ? 227 HIS B C     1 
ATOM   10293 O  O     A HIS B 2 227 ? 25.897  -33.570 7.621   0.20 42.29  ? 227 HIS B O     1 
ATOM   10294 O  O     B HIS B 2 227 ? 25.848  -33.459 7.789   0.80 42.87  ? 227 HIS B O     1 
ATOM   10295 C  CB    A HIS B 2 227 ? 27.991  -35.638 6.171   0.20 45.87  ? 227 HIS B CB    1 
ATOM   10296 C  CB    B HIS B 2 227 ? 27.783  -35.730 6.314   0.80 46.15  ? 227 HIS B CB    1 
ATOM   10297 C  CG    A HIS B 2 227 ? 27.516  -36.371 7.386   0.20 47.83  ? 227 HIS B CG    1 
ATOM   10298 C  CG    B HIS B 2 227 ? 27.455  -36.308 7.654   0.80 48.05  ? 227 HIS B CG    1 
ATOM   10299 N  ND1   A HIS B 2 227 ? 26.341  -37.091 7.410   0.20 49.93  ? 227 HIS B ND1   1 
ATOM   10300 N  ND1   B HIS B 2 227 ? 26.267  -36.958 7.916   0.80 48.75  ? 227 HIS B ND1   1 
ATOM   10301 C  CD2   A HIS B 2 227 ? 28.060  -36.498 8.619   0.20 50.51  ? 227 HIS B CD2   1 
ATOM   10302 C  CD2   B HIS B 2 227 ? 28.167  -36.345 8.804   0.80 50.33  ? 227 HIS B CD2   1 
ATOM   10303 C  CE1   A HIS B 2 227 ? 26.181  -37.630 8.606   0.20 50.97  ? 227 HIS B CE1   1 
ATOM   10304 C  CE1   B HIS B 2 227 ? 26.262  -37.368 9.171   0.80 53.28  ? 227 HIS B CE1   1 
ATOM   10305 N  NE2   A HIS B 2 227 ? 27.211  -37.285 9.359   0.20 54.60  ? 227 HIS B NE2   1 
ATOM   10306 N  NE2   B HIS B 2 227 ? 27.402  -37.007 9.733   0.80 57.32  ? 227 HIS B NE2   1 
ATOM   10307 N  N     A LEU B 2 228 ? 27.824  -32.562 7.038   0.20 39.14  ? 228 LEU B N     1 
ATOM   10308 N  N     B LEU B 2 228 ? 27.896  -32.705 7.224   0.80 39.01  ? 228 LEU B N     1 
ATOM   10309 C  CA    A LEU B 2 228 ? 27.673  -31.504 8.029   0.20 37.13  ? 228 LEU B CA    1 
ATOM   10310 C  CA    B LEU B 2 228 ? 27.859  -31.620 8.196   0.80 36.64  ? 228 LEU B CA    1 
ATOM   10311 C  C     A LEU B 2 228 ? 26.669  -30.449 7.584   0.20 37.54  ? 228 LEU B C     1 
ATOM   10312 C  C     B LEU B 2 228 ? 26.772  -30.610 7.850   0.80 38.21  ? 228 LEU B C     1 
ATOM   10313 O  O     A LEU B 2 228 ? 26.015  -29.827 8.429   0.20 37.01  ? 228 LEU B O     1 
ATOM   10314 O  O     B LEU B 2 228 ? 25.994  -30.201 8.718   0.80 36.91  ? 228 LEU B O     1 
ATOM   10315 C  CB    A LEU B 2 228 ? 29.027  -30.854 8.313   0.20 38.54  ? 228 LEU B CB    1 
ATOM   10316 C  CB    B LEU B 2 228 ? 29.225  -30.943 8.268   0.80 39.02  ? 228 LEU B CB    1 
ATOM   10317 C  CG    A LEU B 2 228 ? 30.131  -31.784 8.822   0.20 35.86  ? 228 LEU B CG    1 
ATOM   10318 C  CG    B LEU B 2 228 ? 30.340  -31.828 8.833   0.80 34.96  ? 228 LEU B CG    1 
ATOM   10319 C  CD1   A LEU B 2 228 ? 31.436  -31.022 9.003   0.20 36.50  ? 228 LEU B CD1   1 
ATOM   10320 C  CD1   B LEU B 2 228 ? 31.678  -31.123 8.716   0.80 37.59  ? 228 LEU B CD1   1 
ATOM   10321 C  CD2   A LEU B 2 228 ? 29.709  -32.445 10.125  0.20 41.08  ? 228 LEU B CD2   1 
ATOM   10322 C  CD2   B LEU B 2 228 ? 30.045  -32.176 10.287  0.80 42.03  ? 228 LEU B CD2   1 
ATOM   10323 N  N     A VAL B 2 229 ? 26.533  -30.234 6.273   0.20 36.11  ? 229 VAL B N     1 
ATOM   10324 N  N     B VAL B 2 229 ? 26.709  -30.194 6.582   0.80 34.83  ? 229 VAL B N     1 
ATOM   10325 C  CA    A VAL B 2 229 ? 25.582  -29.246 5.772   0.20 36.20  ? 229 VAL B CA    1 
ATOM   10326 C  CA    B VAL B 2 229 ? 25.697  -29.227 6.158   0.80 36.58  ? 229 VAL B CA    1 
ATOM   10327 C  C     A VAL B 2 229 ? 24.152  -29.748 5.934   0.20 38.00  ? 229 VAL B C     1 
ATOM   10328 C  C     B VAL B 2 229 ? 24.300  -29.756 6.451   0.80 37.88  ? 229 VAL B C     1 
ATOM   10329 O  O     A VAL B 2 229 ? 23.237  -28.971 6.232   0.20 34.42  ? 229 VAL B O     1 
ATOM   10330 O  O     B VAL B 2 229 ? 23.443  -29.037 6.978   0.80 34.39  ? 229 VAL B O     1 
ATOM   10331 C  CB    A VAL B 2 229 ? 25.897  -28.901 4.305   0.20 35.23  ? 229 VAL B CB    1 
ATOM   10332 C  CB    B VAL B 2 229 ? 25.865  -28.890 4.666   0.80 34.12  ? 229 VAL B CB    1 
ATOM   10333 C  CG1   A VAL B 2 229 ? 24.923  -27.855 3.777   0.20 34.24  ? 229 VAL B CG1   1 
ATOM   10334 C  CG1   B VAL B 2 229 ? 24.752  -27.958 4.193   0.80 35.59  ? 229 VAL B CG1   1 
ATOM   10335 C  CG2   A VAL B 2 229 ? 27.333  -28.417 4.170   0.20 37.68  ? 229 VAL B CG2   1 
ATOM   10336 C  CG2   B VAL B 2 229 ? 27.234  -28.272 4.412   0.80 38.59  ? 229 VAL B CG2   1 
ATOM   10337 N  N     A SER B 2 230 ? 23.934  -31.051 5.738   0.20 35.68  ? 230 SER B N     1 
ATOM   10338 N  N     B SER B 2 230 ? 24.049  -31.025 6.114   0.80 33.15  ? 230 SER B N     1 
ATOM   10339 C  CA    A SER B 2 230 ? 22.584  -31.593 5.859   0.20 40.31  ? 230 SER B CA    1 
ATOM   10340 C  CA    B SER B 2 230 ? 22.693  -31.554 6.242   0.80 41.71  ? 230 SER B CA    1 
ATOM   10341 C  C     A SER B 2 230 ? 22.117  -31.587 7.309   0.20 37.08  ? 230 SER B C     1 
ATOM   10342 C  C     B SER B 2 230 ? 22.244  -31.565 7.699   0.80 36.93  ? 230 SER B C     1 
ATOM   10343 O  O     A SER B 2 230 ? 20.952  -31.283 7.590   0.20 39.61  ? 230 SER B O     1 
ATOM   10344 O  O     B SER B 2 230 ? 21.078  -31.281 7.999   0.80 40.99  ? 230 SER B O     1 
ATOM   10345 C  CB    A SER B 2 230 ? 22.529  -33.005 5.277   0.20 40.59  ? 230 SER B CB    1 
ATOM   10346 C  CB    B SER B 2 230 ? 22.610  -32.953 5.621   0.80 42.53  ? 230 SER B CB    1 
ATOM   10347 O  OG    A SER B 2 230 ? 23.320  -33.904 6.034   0.20 39.61  ? 230 SER B OG    1 
ATOM   10348 O  OG    B SER B 2 230 ? 23.538  -33.848 6.211   0.80 40.19  ? 230 SER B OG    1 
ATOM   10349 N  N     A ALA B 2 231 ? 23.013  -31.912 8.244   0.20 36.16  ? 231 ALA B N     1 
ATOM   10350 N  N     B ALA B 2 231 ? 23.164  -31.848 8.623   0.80 34.48  ? 231 ALA B N     1 
ATOM   10351 C  CA    A ALA B 2 231 ? 22.658  -31.867 9.659   0.20 38.53  ? 231 ALA B CA    1 
ATOM   10352 C  CA    B ALA B 2 231 ? 22.827  -31.816 10.043  0.80 39.45  ? 231 ALA B CA    1 
ATOM   10353 C  C     A ALA B 2 231 ? 22.475  -30.435 10.143  0.20 40.43  ? 231 ALA B C     1 
ATOM   10354 C  C     B ALA B 2 231 ? 22.524  -30.393 10.502  0.80 42.15  ? 231 ALA B C     1 
ATOM   10355 O  O     A ALA B 2 231 ? 21.698  -30.191 11.074  0.20 36.35  ? 231 ALA B O     1 
ATOM   10356 O  O     B ALA B 2 231 ? 21.607  -30.172 11.304  0.80 34.83  ? 231 ALA B O     1 
ATOM   10357 C  CB    A ALA B 2 231 ? 23.724  -32.578 10.493  0.20 36.61  ? 231 ALA B CB    1 
ATOM   10358 C  CB    B ALA B 2 231 ? 23.969  -32.418 10.865  0.80 34.01  ? 231 ALA B CB    1 
ATOM   10359 N  N     A THR B 2 232 ? 23.179  -29.479 9.529   0.20 38.98  ? 232 THR B N     1 
ATOM   10360 N  N     B THR B 2 232 ? 23.274  -29.416 9.983   0.80 40.28  ? 232 THR B N     1 
ATOM   10361 C  CA    A THR B 2 232 ? 23.009  -28.079 9.902   0.20 37.47  ? 232 THR B CA    1 
ATOM   10362 C  CA    B THR B 2 232 ? 23.079  -28.016 10.352  0.80 35.75  ? 232 THR B CA    1 
ATOM   10363 C  C     A THR B 2 232 ? 21.687  -27.528 9.381   0.20 37.39  ? 232 THR B C     1 
ATOM   10364 C  C     B THR B 2 232 ? 21.735  -27.492 9.857   0.80 39.24  ? 232 THR B C     1 
ATOM   10365 O  O     A THR B 2 232 ? 20.960  -26.845 10.114  0.20 37.54  ? 232 THR B O     1 
ATOM   10366 O  O     B THR B 2 232 ? 20.978  -26.873 10.619  0.80 36.26  ? 232 THR B O     1 
ATOM   10367 C  CB    A THR B 2 232 ? 24.181  -27.248 9.375   0.20 36.56  ? 232 THR B CB    1 
ATOM   10368 C  CB    B THR B 2 232 ? 24.226  -27.177 9.782   0.80 37.60  ? 232 THR B CB    1 
ATOM   10369 O  OG1   A THR B 2 232 ? 25.410  -27.753 9.916   0.20 37.01  ? 232 THR B OG1   1 
ATOM   10370 O  OG1   B THR B 2 232 ? 25.454  -27.546 10.426  0.80 37.60  ? 232 THR B OG1   1 
ATOM   10371 C  CG2   A THR B 2 232 ? 24.023  -25.785 9.769   0.20 34.17  ? 232 THR B CG2   1 
ATOM   10372 C  CG2   B THR B 2 232 ? 23.968  -25.681 9.964   0.80 33.92  ? 232 THR B CG2   1 
ATOM   10373 N  N     A MET B 2 233 ? 21.358  -27.817 8.121   0.20 35.41  ? 233 MET B N     1 
ATOM   10374 N  N     B MET B 2 233 ? 21.425  -27.724 8.577   0.80 34.75  ? 233 MET B N     1 
ATOM   10375 C  CA    A MET B 2 233 ? 20.082  -27.390 7.559   0.20 35.97  ? 233 MET B CA    1 
ATOM   10376 C  CA    B MET B 2 233 ? 20.161  -27.245 8.024   0.80 36.46  ? 233 MET B CA    1 
ATOM   10377 C  C     A MET B 2 233 ? 18.895  -28.123 8.164   0.20 35.42  ? 233 MET B C     1 
ATOM   10378 C  C     B MET B 2 233 ? 18.976  -27.902 8.711   0.80 35.52  ? 233 MET B C     1 
ATOM   10379 O  O     A MET B 2 233 ? 17.758  -27.683 7.968   0.20 33.21  ? 233 MET B O     1 
ATOM   10380 O  O     B MET B 2 233 ? 17.949  -27.253 8.946   0.80 34.14  ? 233 MET B O     1 
ATOM   10381 C  CB    A MET B 2 233 ? 20.079  -27.584 6.044   0.20 35.50  ? 233 MET B CB    1 
ATOM   10382 C  CB    B MET B 2 233 ? 20.107  -27.506 6.522   0.80 34.68  ? 233 MET B CB    1 
ATOM   10383 C  CG    A MET B 2 233 ? 21.030  -26.663 5.303   0.20 34.92  ? 233 MET B CG    1 
ATOM   10384 C  CG    B MET B 2 233 ? 21.111  -26.709 5.727   0.80 35.06  ? 233 MET B CG    1 
ATOM   10385 S  SD    A MET B 2 233 ? 20.865  -26.816 3.517   0.20 36.94  ? 233 MET B SD    1 
ATOM   10386 S  SD    B MET B 2 233 ? 20.983  -27.118 3.988   0.80 37.83  ? 233 MET B SD    1 
ATOM   10387 C  CE    A MET B 2 233 ? 19.120  -26.477 3.316   0.20 37.91  ? 233 MET B CE    1 
ATOM   10388 C  CE    B MET B 2 233 ? 19.353  -26.494 3.602   0.80 39.48  ? 233 MET B CE    1 
ATOM   10389 N  N     A SER B 2 234 ? 19.126  -29.226 8.877   0.20 34.69  ? 234 SER B N     1 
ATOM   10390 N  N     B SER B 2 234 ? 19.088  -29.195 9.025   0.80 34.41  ? 234 SER B N     1 
ATOM   10391 C  CA    A SER B 2 234 ? 18.054  -29.931 9.566   0.20 39.06  ? 234 SER B CA    1 
ATOM   10392 C  CA    B SER B 2 234 ? 18.045  -29.838 9.818   0.80 39.83  ? 234 SER B CA    1 
ATOM   10393 C  C     A SER B 2 234 ? 17.824  -29.418 10.977  0.20 38.47  ? 234 SER B C     1 
ATOM   10394 C  C     B SER B 2 234 ? 17.883  -29.148 11.161  0.80 39.47  ? 234 SER B C     1 
ATOM   10395 O  O     A SER B 2 234 ? 16.764  -29.689 11.551  0.20 35.44  ? 234 SER B O     1 
ATOM   10396 O  O     B SER B 2 234 ? 16.758  -28.904 11.609  0.80 36.49  ? 234 SER B O     1 
ATOM   10397 C  CB    A SER B 2 234 ? 18.346  -31.433 9.626   0.20 37.73  ? 234 SER B CB    1 
ATOM   10398 C  CB    B SER B 2 234 ? 18.356  -31.315 10.037  0.80 36.94  ? 234 SER B CB    1 
ATOM   10399 O  OG    A SER B 2 234 ? 17.345  -32.108 10.369  0.20 40.61  ? 234 SER B OG    1 
ATOM   10400 O  OG    B SER B 2 234 ? 17.454  -31.848 10.994  0.80 38.49  ? 234 SER B OG    1 
ATOM   10401 N  N     A GLY B 2 235 ? 18.785  -28.694 11.547  0.20 36.61  ? 235 GLY B N     1 
ATOM   10402 N  N     B GLY B 2 235 ? 19.000  -28.813 11.808  0.80 36.01  ? 235 GLY B N     1 
ATOM   10403 C  CA    A GLY B 2 235 ? 18.632  -28.140 12.877  0.20 37.15  ? 235 GLY B CA    1 
ATOM   10404 C  CA    B GLY B 2 235 ? 18.929  -28.202 13.125  0.80 36.15  ? 235 GLY B CA    1 
ATOM   10405 C  C     A GLY B 2 235 ? 18.079  -26.731 12.868  0.20 39.43  ? 235 GLY B C     1 
ATOM   10406 C  C     B GLY B 2 235 ? 18.305  -26.819 13.102  0.80 40.95  ? 235 GLY B C     1 
ATOM   10407 O  O     A GLY B 2 235 ? 17.246  -26.380 13.708  0.20 37.31  ? 235 GLY B O     1 
ATOM   10408 O  O     B GLY B 2 235 ? 17.372  -26.539 13.858  0.80 37.16  ? 235 GLY B O     1 
ATOM   10409 N  N     A VAL B 2 236 ? 18.533  -25.909 11.917  0.20 38.50  ? 236 VAL B N     1 
ATOM   10410 N  N     B VAL B 2 236 ? 18.807  -25.932 12.234  0.80 40.18  ? 236 VAL B N     1 
ATOM   10411 C  CA    A VAL B 2 236 ? 18.059  -24.532 11.825  0.20 36.08  ? 236 VAL B CA    1 
ATOM   10412 C  CA    B VAL B 2 236 ? 18.325  -24.553 12.251  0.80 34.61  ? 236 VAL B CA    1 
ATOM   10413 C  C     A VAL B 2 236 ? 16.641  -24.431 11.285  0.20 35.37  ? 236 VAL B C     1 
ATOM   10414 C  C     B VAL B 2 236 ? 16.853  -24.450 11.862  0.80 31.79  ? 236 VAL B C     1 
ATOM   10415 O  O     A VAL B 2 236 ? 16.065  -23.337 11.289  0.20 35.92  ? 236 VAL B O     1 
ATOM   10416 O  O     B VAL B 2 236 ? 16.193  -23.481 12.248  0.80 35.60  ? 236 VAL B O     1 
ATOM   10417 C  CB    A VAL B 2 236 ? 19.002  -23.682 10.947  0.20 34.18  ? 236 VAL B CB    1 
ATOM   10418 C  CB    B VAL B 2 236 ? 19.172  -23.634 11.346  0.80 32.64  ? 236 VAL B CB    1 
ATOM   10419 C  CG1   A VAL B 2 236 ? 20.411  -23.689 11.518  0.20 36.22  ? 236 VAL B CG1   1 
ATOM   10420 C  CG1   B VAL B 2 236 ? 20.566  -23.463 11.910  0.80 36.33  ? 236 VAL B CG1   1 
ATOM   10421 C  CG2   A VAL B 2 236 ? 18.998  -24.190 9.515   0.20 36.99  ? 236 VAL B CG2   1 
ATOM   10422 C  CG2   B VAL B 2 236 ? 19.232  -24.167 9.928   0.80 38.41  ? 236 VAL B CG2   1 
ATOM   10423 N  N     A THR B 2 237 ? 16.065  -25.537 10.810  0.20 35.02  ? 237 THR B N     1 
ATOM   10424 N  N     B THR B 2 237 ? 16.319  -25.406 11.098  0.80 35.09  ? 237 THR B N     1 
ATOM   10425 C  CA    A THR B 2 237 ? 14.683  -25.560 10.345  0.20 36.41  ? 237 THR B CA    1 
ATOM   10426 C  CA    B THR B 2 237 ? 14.916  -25.386 10.700  0.80 34.51  ? 237 THR B CA    1 
ATOM   10427 C  C     A THR B 2 237 ? 13.804  -26.473 11.190  0.20 37.59  ? 237 THR B C     1 
ATOM   10428 C  C     B THR B 2 237 ? 14.025  -26.207 11.625  0.80 36.53  ? 237 THR B C     1 
ATOM   10429 O  O     A THR B 2 237 ? 12.683  -26.794 10.775  0.20 39.51  ? 237 THR B O     1 
ATOM   10430 O  O     B THR B 2 237 ? 12.863  -26.454 11.281  0.80 39.24  ? 237 THR B O     1 
ATOM   10431 C  CB    A THR B 2 237 ? 14.611  -25.987 8.874   0.20 37.87  ? 237 THR B CB    1 
ATOM   10432 C  CB    B THR B 2 237 ? 14.744  -25.901 9.265   0.80 40.11  ? 237 THR B CB    1 
ATOM   10433 O  OG1   A THR B 2 237 ? 15.083  -27.334 8.737   0.20 35.58  ? 237 THR B OG1   1 
ATOM   10434 O  OG1   B THR B 2 237 ? 15.110  -27.287 9.205   0.80 34.39  ? 237 THR B OG1   1 
ATOM   10435 C  CG2   A THR B 2 237 ? 15.453  -25.065 8.005   0.20 34.84  ? 237 THR B CG2   1 
ATOM   10436 C  CG2   B THR B 2 237 ? 15.580  -25.085 8.277   0.80 34.71  ? 237 THR B CG2   1 
ATOM   10437 N  N     A THR B 2 238 ? 14.281  -26.899 12.363  0.20 36.18  ? 238 THR B N     1 
ATOM   10438 N  N     B THR B 2 238 ? 14.538  -26.625 12.784  0.80 34.15  ? 238 THR B N     1 
ATOM   10439 C  CA    A THR B 2 238 ? 13.497  -27.793 13.211  0.20 38.97  ? 238 THR B CA    1 
ATOM   10440 C  CA    B THR B 2 238 ? 13.774  -27.493 13.678  0.80 40.29  ? 238 THR B CA    1 
ATOM   10441 C  C     A THR B 2 238 ? 12.219  -27.118 13.693  0.20 41.56  ? 238 THR B C     1 
ATOM   10442 C  C     B THR B 2 238 ? 12.499  -26.817 14.167  0.80 40.42  ? 238 THR B C     1 
ATOM   10443 O  O     A THR B 2 238 ? 11.115  -27.641 13.499  0.20 42.03  ? 238 THR B O     1 
ATOM   10444 O  O     B THR B 2 238 ? 11.423  -27.426 14.178  0.80 41.63  ? 238 THR B O     1 
ATOM   10445 C  CB    A THR B 2 238 ? 14.342  -28.259 14.398  0.20 39.56  ? 238 THR B CB    1 
ATOM   10446 C  CB    B THR B 2 238 ? 14.646  -27.911 14.861  0.80 40.09  ? 238 THR B CB    1 
ATOM   10447 O  OG1   A THR B 2 238 ? 15.310  -29.216 13.951  0.20 37.68  ? 238 THR B OG1   1 
ATOM   10448 O  OG1   B THR B 2 238 ? 15.646  -28.831 14.409  0.80 38.59  ? 238 THR B OG1   1 
ATOM   10449 C  CG2   A THR B 2 238 ? 13.463  -28.885 15.475  0.20 38.79  ? 238 THR B CG2   1 
ATOM   10450 C  CG2   B THR B 2 238 ? 13.804  -28.567 15.955  0.80 33.94  ? 238 THR B CG2   1 
ATOM   10451 N  N     A CYS B 2 239 ? 12.347  -25.948 14.318  0.20 40.73  ? 239 CYS B N     1 
ATOM   10452 N  N     B CYS B 2 239 ? 12.595  -25.556 14.581  0.80 44.64  ? 239 CYS B N     1 
ATOM   10453 C  CA    A CYS B 2 239 ? 11.182  -25.252 14.850  0.20 40.64  ? 239 CYS B CA    1 
ATOM   10454 C  CA    B CYS B 2 239 ? 11.417  -24.881 15.112  0.80 38.29  ? 239 CYS B CA    1 
ATOM   10455 C  C     A CYS B 2 239 ? 10.317  -24.627 13.765  0.20 43.14  ? 239 CYS B C     1 
ATOM   10456 C  C     B CYS B 2 239 ? 10.378  -24.633 14.026  0.80 44.05  ? 239 CYS B C     1 
ATOM   10457 O  O     A CYS B 2 239 ? 9.325   -23.967 14.094  0.20 41.53  ? 239 CYS B O     1 
ATOM   10458 O  O     B CYS B 2 239 ? 9.179   -24.610 14.316  0.80 40.93  ? 239 CYS B O     1 
ATOM   10459 C  CB    A CYS B 2 239 ? 11.629  -24.189 15.853  0.20 38.31  ? 239 CYS B CB    1 
ATOM   10460 C  CB    B CYS B 2 239 ? 11.817  -23.572 15.789  0.80 35.96  ? 239 CYS B CB    1 
ATOM   10461 S  SG    A CYS B 2 239 ? 12.612  -24.861 17.212  0.20 38.40  ? 239 CYS B SG    1 
ATOM   10462 S  SG    B CYS B 2 239 ? 12.898  -23.774 17.209  0.80 52.38  ? 239 CYS B SG    1 
ATOM   10463 N  N     A LEU B 2 240 ? 10.669  -24.808 12.492  0.20 38.96  ? 240 LEU B N     1 
ATOM   10464 N  N     B LEU B 2 240 ? 10.806  -24.471 12.771  0.80 35.95  ? 240 LEU B N     1 
ATOM   10465 C  CA    A LEU B 2 240 ? 9.783   -24.471 11.387  0.20 42.24  ? 240 LEU B CA    1 
ATOM   10466 C  CA    B LEU B 2 240 ? 9.851   -24.254 11.688  0.80 43.25  ? 240 LEU B CA    1 
ATOM   10467 C  C     A LEU B 2 240 ? 8.969   -25.664 10.910  0.20 43.14  ? 240 LEU B C     1 
ATOM   10468 C  C     B LEU B 2 240 ? 8.975   -25.474 11.420  0.80 43.01  ? 240 LEU B C     1 
ATOM   10469 O  O     A LEU B 2 240 ? 7.899   -25.473 10.323  0.20 46.61  ? 240 LEU B O     1 
ATOM   10470 O  O     B LEU B 2 240 ? 7.861   -25.319 10.913  0.80 46.13  ? 240 LEU B O     1 
ATOM   10471 C  CB    A LEU B 2 240 ? 10.588  -23.910 10.209  0.20 37.13  ? 240 LEU B CB    1 
ATOM   10472 C  CB    B LEU B 2 240 ? 10.587  -23.866 10.400  0.80 36.61  ? 240 LEU B CB    1 
ATOM   10473 C  CG    A LEU B 2 240 ? 11.305  -22.575 10.412  0.20 37.08  ? 240 LEU B CG    1 
ATOM   10474 C  CG    B LEU B 2 240 ? 11.267  -22.496 10.354  0.80 36.84  ? 240 LEU B CG    1 
ATOM   10475 C  CD1   A LEU B 2 240 ? 12.151  -22.228 9.194   0.20 40.54  ? 240 LEU B CD1   1 
ATOM   10476 C  CD1   B LEU B 2 240 ? 12.320  -22.453 9.254   0.80 41.28  ? 240 LEU B CD1   1 
ATOM   10477 C  CD2   A LEU B 2 240 ? 10.298  -21.477 10.689  0.20 41.44  ? 240 LEU B CD2   1 
ATOM   10478 C  CD2   B LEU B 2 240 ? 10.242  -21.406 10.124  0.80 43.04  ? 240 LEU B CD2   1 
ATOM   10479 N  N     A ARG B 2 241 ? 9.450   -26.883 11.154  0.20 44.46  ? 241 ARG B N     1 
ATOM   10480 N  N     B ARG B 2 241 ? 9.438   -26.676 11.768  0.80 45.78  ? 241 ARG B N     1 
ATOM   10481 C  CA    A ARG B 2 241 ? 8.787   -28.098 10.701  0.20 43.44  ? 241 ARG B CA    1 
ATOM   10482 C  CA    B ARG B 2 241 ? 8.809   -27.904 11.303  0.80 45.10  ? 241 ARG B CA    1 
ATOM   10483 C  C     A ARG B 2 241 ? 8.032   -28.823 11.806  0.20 48.73  ? 241 ARG B C     1 
ATOM   10484 C  C     B ARG B 2 241 ? 8.117   -28.711 12.388  0.80 49.81  ? 241 ARG B C     1 
ATOM   10485 O  O     A ARG B 2 241 ? 7.209   -29.693 11.501  0.20 48.66  ? 241 ARG B O     1 
ATOM   10486 O  O     B ARG B 2 241 ? 7.304   -29.578 12.056  0.80 53.35  ? 241 ARG B O     1 
ATOM   10487 C  CB    A ARG B 2 241 ? 9.812   -29.057 10.084  0.20 40.59  ? 241 ARG B CB    1 
ATOM   10488 C  CB    B ARG B 2 241 ? 9.849   -28.804 10.622  0.80 36.64  ? 241 ARG B CB    1 
ATOM   10489 C  CG    A ARG B 2 241 ? 10.532  -28.482 8.876   0.20 40.14  ? 241 ARG B CG    1 
ATOM   10490 C  CG    B ARG B 2 241 ? 10.540  -28.117 9.471   0.80 41.28  ? 241 ARG B CG    1 
ATOM   10491 C  CD    A ARG B 2 241 ? 11.615  -29.415 8.356   0.20 37.27  ? 241 ARG B CD    1 
ATOM   10492 C  CD    B ARG B 2 241 ? 11.583  -28.999 8.809   0.80 34.63  ? 241 ARG B CD    1 
ATOM   10493 N  NE    A ARG B 2 241 ? 12.765  -29.498 9.249   0.20 37.95  ? 241 ARG B NE    1 
ATOM   10494 N  NE    B ARG B 2 241 ? 12.800  -29.159 9.599   0.80 35.56  ? 241 ARG B NE    1 
ATOM   10495 C  CZ    A ARG B 2 241 ? 13.045  -30.543 10.016  0.20 39.11  ? 241 ARG B CZ    1 
ATOM   10496 C  CZ    B ARG B 2 241 ? 13.162  -30.291 10.184  0.80 39.01  ? 241 ARG B CZ    1 
ATOM   10497 N  NH1   A ARG B 2 241 ? 12.266  -31.612 10.039  0.20 38.59  ? 241 ARG B NH1   1 
ATOM   10498 N  NH1   B ARG B 2 241 ? 12.387  -31.361 10.156  0.80 37.39  ? 241 ARG B NH1   1 
ATOM   10499 N  NH2   A ARG B 2 241 ? 14.139  -30.519 10.772  0.20 37.02  ? 241 ARG B NH2   1 
ATOM   10500 N  NH2   B ARG B 2 241 ? 14.341  -30.360 10.794  0.80 36.14  ? 241 ARG B NH2   1 
ATOM   10501 N  N     A PHE B 2 242 ? 8.292   -28.493 13.064  0.20 45.36  ? 242 PHE B N     1 
ATOM   10502 N  N     B PHE B 2 242 ? 8.433   -28.478 13.655  0.80 45.08  ? 242 PHE B N     1 
ATOM   10503 C  CA    A PHE B 2 242 ? 7.654   -29.107 14.216  0.20 48.72  ? 242 PHE B CA    1 
ATOM   10504 C  CA    B PHE B 2 242 ? 7.759   -29.188 14.728  0.80 48.44  ? 242 PHE B CA    1 
ATOM   10505 C  C     A PHE B 2 242 ? 6.974   -28.035 15.060  0.20 47.89  ? 242 PHE B C     1 
ATOM   10506 C  C     B PHE B 2 242 ? 7.089   -28.191 15.665  0.80 48.76  ? 242 PHE B C     1 
ATOM   10507 O  O     A PHE B 2 242 ? 7.352   -26.860 15.003  0.20 47.53  ? 242 PHE B O     1 
ATOM   10508 O  O     B PHE B 2 242 ? 7.535   -27.044 15.766  0.80 44.83  ? 242 PHE B O     1 
ATOM   10509 C  CB    A PHE B 2 242 ? 8.683   -29.876 15.058  0.20 46.39  ? 242 PHE B CB    1 
ATOM   10510 C  CB    B PHE B 2 242 ? 8.742   -30.069 15.510  0.80 47.34  ? 242 PHE B CB    1 
ATOM   10511 C  CG    A PHE B 2 242 ? 9.289   -31.052 14.344  0.20 47.11  ? 242 PHE B CG    1 
ATOM   10512 C  CG    B PHE B 2 242 ? 9.363   -31.156 14.686  0.80 47.17  ? 242 PHE B CG    1 
ATOM   10513 C  CD1   A PHE B 2 242 ? 8.595   -32.246 14.238  0.20 45.92  ? 242 PHE B CD1   1 
ATOM   10514 C  CD1   B PHE B 2 242 ? 8.604   -32.227 14.246  0.80 45.77  ? 242 PHE B CD1   1 
ATOM   10515 C  CD2   A PHE B 2 242 ? 10.550  -30.962 13.775  0.20 45.85  ? 242 PHE B CD2   1 
ATOM   10516 C  CD2   B PHE B 2 242 ? 10.706  -31.109 14.347  0.80 48.29  ? 242 PHE B CD2   1 
ATOM   10517 C  CE1   A PHE B 2 242 ? 9.147   -33.329 13.580  0.20 48.88  ? 242 PHE B CE1   1 
ATOM   10518 C  CE1   B PHE B 2 242 ? 9.173   -33.231 13.486  0.80 49.16  ? 242 PHE B CE1   1 
ATOM   10519 C  CE2   A PHE B 2 242 ? 11.107  -32.042 13.117  0.20 41.75  ? 242 PHE B CE2   1 
ATOM   10520 C  CE2   B PHE B 2 242 ? 11.279  -32.108 13.588  0.80 38.10  ? 242 PHE B CE2   1 
ATOM   10521 C  CZ    A PHE B 2 242 ? 10.405  -33.227 13.018  0.20 45.29  ? 242 PHE B CZ    1 
ATOM   10522 C  CZ    B PHE B 2 242 ? 10.513  -33.169 13.153  0.80 45.34  ? 242 PHE B CZ    1 
ATOM   10523 N  N     A PRO B 2 243 ? 5.951   -28.405 15.852  0.20 52.04  ? 243 PRO B N     1 
ATOM   10524 N  N     B PRO B 2 243 ? 6.008   -28.598 16.367  0.80 53.48  ? 243 PRO B N     1 
ATOM   10525 C  CA    A PRO B 2 243 ? 5.196   -27.392 16.609  0.20 51.88  ? 243 PRO B CA    1 
ATOM   10526 C  CA    B PRO B 2 243 ? 5.239   -27.637 17.175  0.80 53.75  ? 243 PRO B CA    1 
ATOM   10527 C  C     A PRO B 2 243 ? 6.042   -26.603 17.599  0.20 54.24  ? 243 PRO B C     1 
ATOM   10528 C  C     B PRO B 2 243 ? 6.048   -26.970 18.278  0.80 54.23  ? 243 PRO B C     1 
ATOM   10529 O  O     A PRO B 2 243 ? 6.532   -25.516 17.273  0.20 55.67  ? 243 PRO B O     1 
ATOM   10530 O  O     B PRO B 2 243 ? 6.161   -25.740 18.309  0.80 54.92  ? 243 PRO B O     1 
ATOM   10531 C  CB    A PRO B 2 243 ? 4.123   -28.221 17.331  0.20 53.12  ? 243 PRO B CB    1 
ATOM   10532 C  CB    B PRO B 2 243 ? 4.113   -28.496 17.769  0.80 52.24  ? 243 PRO B CB    1 
ATOM   10533 C  CG    A PRO B 2 243 ? 4.647   -29.624 17.332  0.20 52.75  ? 243 PRO B CG    1 
ATOM   10534 C  CG    B PRO B 2 243 ? 4.015   -29.680 16.882  0.80 52.82  ? 243 PRO B CG    1 
ATOM   10535 C  CD    A PRO B 2 243 ? 5.399   -29.757 16.047  0.20 53.72  ? 243 PRO B CD    1 
ATOM   10536 C  CD    B PRO B 2 243 ? 5.408   -29.943 16.397  0.80 55.71  ? 243 PRO B CD    1 
ATOM   10537 N  N     A GLY B 2 244 ? 6.208   -27.127 18.810  0.20 55.32  ? 244 GLY B N     1 
ATOM   10538 N  N     B GLY B 2 244 ? 6.601   -27.768 19.190  0.80 58.50  ? 244 GLY B N     1 
ATOM   10539 C  CA    A GLY B 2 244 ? 6.957   -26.442 19.841  0.20 57.57  ? 244 GLY B CA    1 
ATOM   10540 C  CA    B GLY B 2 244 ? 7.356   -27.218 20.304  0.80 55.93  ? 244 GLY B CA    1 
ATOM   10541 C  C     A GLY B 2 244 ? 6.143   -25.361 20.532  0.20 61.89  ? 244 GLY B C     1 
ATOM   10542 C  C     B GLY B 2 244 ? 6.557   -26.191 21.080  0.80 62.97  ? 244 GLY B C     1 
ATOM   10543 O  O     A GLY B 2 244 ? 5.028   -25.016 20.136  0.20 59.74  ? 244 GLY B O     1 
ATOM   10544 O  O     B GLY B 2 244 ? 5.360   -26.363 21.343  0.80 68.36  ? 244 GLY B O     1 
ATOM   10545 N  N     A GLN B 2 245 ? 6.727   -24.814 21.601  0.20 65.26  ? 245 GLN B N     1 
ATOM   10546 N  N     B GLN B 2 245 ? 7.229   -25.101 21.452  0.80 68.74  ? 245 GLN B N     1 
ATOM   10547 C  CA    A GLN B 2 245 ? 6.046   -23.770 22.362  0.20 64.82  ? 245 GLN B CA    1 
ATOM   10548 C  CA    B GLN B 2 245 ? 6.585   -23.949 22.075  0.80 65.71  ? 245 GLN B CA    1 
ATOM   10549 C  C     A GLN B 2 245 ? 5.920   -22.487 21.552  0.20 64.06  ? 245 GLN B C     1 
ATOM   10550 C  C     B GLN B 2 245 ? 6.876   -22.632 21.373  0.80 63.56  ? 245 GLN B C     1 
ATOM   10551 O  O     A GLN B 2 245 ? 4.876   -21.824 21.585  0.20 63.16  ? 245 GLN B O     1 
ATOM   10552 O  O     B GLN B 2 245 ? 6.172   -21.648 21.637  0.80 66.68  ? 245 GLN B O     1 
ATOM   10553 C  CB    A GLN B 2 245 ? 6.784   -23.504 23.675  0.20 63.53  ? 245 GLN B CB    1 
ATOM   10554 C  CB    B GLN B 2 245 ? 7.003   -23.824 23.550  0.80 64.21  ? 245 GLN B CB    1 
ATOM   10555 C  CG    A GLN B 2 245 ? 6.118   -22.453 24.557  0.20 63.11  ? 245 GLN B CG    1 
ATOM   10556 C  CG    B GLN B 2 245 ? 6.137   -24.614 24.524  0.80 57.33  ? 245 GLN B CG    1 
ATOM   10557 C  CD    A GLN B 2 245 ? 6.890   -22.178 25.836  0.20 56.63  ? 245 GLN B CD    1 
ATOM   10558 C  CD    B GLN B 2 245 ? 5.043   -23.767 25.158  0.80 72.23  ? 245 GLN B CD    1 
ATOM   10559 O  OE1   A GLN B 2 245 ? 6.372   -22.359 26.938  0.20 47.75  ? 245 GLN B OE1   1 
ATOM   10560 O  OE1   B GLN B 2 245 ? 4.895   -22.584 24.844  0.80 72.79  ? 245 GLN B OE1   1 
ATOM   10561 N  NE2   A GLN B 2 245 ? 8.132   -21.731 25.694  0.20 54.10  ? 245 GLN B NE2   1 
ATOM   10562 N  NE2   B GLN B 2 245 ? 4.276   -24.370 26.062  0.80 60.89  ? 245 GLN B NE2   1 
ATOM   10563 N  N     A LEU B 2 246 ? 6.969   -22.118 20.823  0.20 62.26  ? 246 LEU B N     1 
ATOM   10564 N  N     B LEU B 2 246 ? 7.883   -22.572 20.504  0.80 60.06  ? 246 LEU B N     1 
ATOM   10565 C  CA    A LEU B 2 246 ? 6.950   -20.926 19.989  0.20 59.57  ? 246 LEU B CA    1 
ATOM   10566 C  CA    B LEU B 2 246 ? 8.151   -21.385 19.696  0.80 63.21  ? 246 LEU B CA    1 
ATOM   10567 C  C     A LEU B 2 246 ? 6.439   -21.266 18.596  0.20 58.33  ? 246 LEU B C     1 
ATOM   10568 C  C     B LEU B 2 246 ? 7.263   -21.445 18.462  0.80 60.99  ? 246 LEU B C     1 
ATOM   10569 O  O     A LEU B 2 246 ? 6.725   -22.340 18.059  0.20 59.77  ? 246 LEU B O     1 
ATOM   10570 O  O     B LEU B 2 246 ? 7.521   -22.217 17.534  0.80 62.84  ? 246 LEU B O     1 
ATOM   10571 C  CB    A LEU B 2 246 ? 8.347   -20.309 19.888  0.20 58.21  ? 246 LEU B CB    1 
ATOM   10572 C  CB    B LEU B 2 246 ? 9.625   -21.309 19.307  0.80 62.23  ? 246 LEU B CB    1 
ATOM   10573 C  CG    A LEU B 2 246 ? 8.971   -19.724 21.154  0.20 54.95  ? 246 LEU B CG    1 
ATOM   10574 C  CG    B LEU B 2 246 ? 10.572  -20.587 20.269  0.80 60.11  ? 246 LEU B CG    1 
ATOM   10575 C  CD1   A LEU B 2 246 ? 10.385  -19.242 20.870  0.20 54.19  ? 246 LEU B CD1   1 
ATOM   10576 C  CD1   B LEU B 2 246 ? 11.987  -20.522 19.707  0.80 54.66  ? 246 LEU B CD1   1 
ATOM   10577 C  CD2   A LEU B 2 246 ? 8.114   -18.592 21.699  0.20 50.79  ? 246 LEU B CD2   1 
ATOM   10578 C  CD2   B LEU B 2 246 ? 10.050  -19.190 20.578  0.80 55.45  ? 246 LEU B CD2   1 
ATOM   10579 N  N     A ASN B 2 247 ? 5.679   -20.343 18.018  0.20 56.14  ? 247 ASN B N     1 
ATOM   10580 N  N     B ASN B 2 247 ? 6.202   -20.636 18.451  0.80 56.59  ? 247 ASN B N     1 
ATOM   10581 C  CA    A ASN B 2 247 ? 5.231   -20.460 16.632  0.20 54.66  ? 247 ASN B CA    1 
ATOM   10582 C  CA    B ASN B 2 247 ? 5.365   -20.507 17.266  0.80 55.04  ? 247 ASN B CA    1 
ATOM   10583 C  C     A ASN B 2 247 ? 6.150   -19.651 15.718  0.20 50.71  ? 247 ASN B C     1 
ATOM   10584 C  C     B ASN B 2 247 ? 6.222   -19.941 16.141  0.80 48.98  ? 247 ASN B C     1 
ATOM   10585 O  O     A ASN B 2 247 ? 5.739   -18.728 15.016  0.20 48.85  ? 247 ASN B O     1 
ATOM   10586 O  O     B ASN B 2 247 ? 6.208   -18.736 15.878  0.80 53.04  ? 247 ASN B O     1 
ATOM   10587 C  CB    A ASN B 2 247 ? 3.778   -20.012 16.507  0.20 56.85  ? 247 ASN B CB    1 
ATOM   10588 C  CB    B ASN B 2 247 ? 4.157   -19.617 17.553  0.80 58.95  ? 247 ASN B CB    1 
ATOM   10589 C  CG    A ASN B 2 247 ? 3.215   -20.242 15.121  0.20 52.98  ? 247 ASN B CG    1 
ATOM   10590 C  CG    B ASN B 2 247 ? 2.914   -20.068 16.815  0.80 59.23  ? 247 ASN B CG    1 
ATOM   10591 O  OD1   A ASN B 2 247 ? 3.733   -21.053 14.354  0.20 53.98  ? 247 ASN B OD1   1 
ATOM   10592 O  OD1   B ASN B 2 247 ? 2.999   -20.643 15.727  0.80 56.60  ? 247 ASN B OD1   1 
ATOM   10593 N  ND2   A ASN B 2 247 ? 2.151   -19.522 14.789  0.20 49.41  ? 247 ASN B ND2   1 
ATOM   10594 N  ND2   B ASN B 2 247 ? 1.747   -19.807 17.402  0.80 52.15  ? 247 ASN B ND2   1 
ATOM   10595 N  N     A ALA B 2 248 ? 7.427   -20.020 15.749  0.20 51.61  ? 248 ALA B N     1 
ATOM   10596 N  N     B ALA B 2 248 ? 6.975   -20.809 15.477  0.80 53.71  ? 248 ALA B N     1 
ATOM   10597 C  CA    A ALA B 2 248 ? 8.449   -19.263 15.041  0.20 47.48  ? 248 ALA B CA    1 
ATOM   10598 C  CA    B ALA B 2 248 ? 8.156   -20.396 14.731  0.80 52.96  ? 248 ALA B CA    1 
ATOM   10599 C  C     A ALA B 2 248 ? 8.297   -19.408 13.531  0.20 44.49  ? 248 ALA B C     1 
ATOM   10600 C  C     B ALA B 2 248 ? 7.842   -19.929 13.316  0.80 41.94  ? 248 ALA B C     1 
ATOM   10601 O  O     A ALA B 2 248 ? 7.995   -20.490 13.019  0.20 43.22  ? 248 ALA B O     1 
ATOM   10602 O  O     B ALA B 2 248 ? 7.047   -20.547 12.601  0.80 45.25  ? 248 ALA B O     1 
ATOM   10603 C  CB    A ALA B 2 248 ? 9.839   -19.724 15.474  0.20 47.42  ? 248 ALA B CB    1 
ATOM   10604 C  CB    B ALA B 2 248 ? 9.157   -21.547 14.674  0.80 46.41  ? 248 ALA B CB    1 
ATOM   10605 N  N     A ASP B 2 249 ? 8.507   -18.301 12.818  0.20 40.92  ? 249 ASP B N     1 
ATOM   10606 N  N     B ASP B 2 249 ? 8.500   -18.843 12.908  0.80 42.63  ? 249 ASP B N     1 
ATOM   10607 C  CA    A ASP B 2 249 ? 8.541   -18.326 11.360  0.20 40.97  ? 249 ASP B CA    1 
ATOM   10608 C  CA    B ASP B 2 249 ? 8.501   -18.429 11.511  0.80 41.25  ? 249 ASP B CA    1 
ATOM   10609 C  C     A ASP B 2 249 ? 9.790   -17.615 10.854  0.20 37.94  ? 249 ASP B C     1 
ATOM   10610 C  C     B ASP B 2 249 ? 9.724   -17.560 11.252  0.80 39.37  ? 249 ASP B C     1 
ATOM   10611 O  O     A ASP B 2 249 ? 10.700  -17.318 11.635  0.20 37.25  ? 249 ASP B O     1 
ATOM   10612 O  O     B ASP B 2 249 ? 10.398  -17.092 12.176  0.80 33.19  ? 249 ASP B O     1 
ATOM   10613 C  CB    A ASP B 2 249 ? 7.274   -17.695 10.767  0.20 40.00  ? 249 ASP B CB    1 
ATOM   10614 C  CB    B ASP B 2 249 ? 7.211   -17.695 11.129  0.80 40.13  ? 249 ASP B CB    1 
ATOM   10615 C  CG    A ASP B 2 249 ? 7.004   -16.295 11.298  0.20 39.24  ? 249 ASP B CG    1 
ATOM   10616 C  CG    B ASP B 2 249 ? 7.014   -16.414 11.905  0.80 40.02  ? 249 ASP B CG    1 
ATOM   10617 O  OD1   A ASP B 2 249 ? 7.914   -15.441 11.247  0.20 36.01  ? 249 ASP B OD1   1 
ATOM   10618 O  OD1   B ASP B 2 249 ? 7.899   -15.534 11.870  0.80 36.51  ? 249 ASP B OD1   1 
ATOM   10619 O  OD2   A ASP B 2 249 ? 5.867   -16.039 11.746  0.20 38.75  ? 249 ASP B OD2   1 
ATOM   10620 O  OD2   B ASP B 2 249 ? 5.960   -16.279 12.548  0.80 47.45  ? 249 ASP B OD2   1 
ATOM   10621 N  N     A LEU B 2 250 ? 9.840   -17.333 9.551   0.20 36.72  ? 250 LEU B N     1 
ATOM   10622 N  N     B LEU B 2 250 ? 9.973   -17.318 9.965   0.80 36.43  ? 250 LEU B N     1 
ATOM   10623 C  CA    A LEU B 2 250 ? 10.996  -16.669 8.961   0.20 34.29  ? 250 LEU B CA    1 
ATOM   10624 C  CA    B LEU B 2 250 ? 11.211  -16.671 9.549   0.80 32.88  ? 250 LEU B CA    1 
ATOM   10625 C  C     A LEU B 2 250 ? 11.071  -15.187 9.305   0.20 33.38  ? 250 LEU B C     1 
ATOM   10626 C  C     B LEU B 2 250 ? 11.227  -15.189 9.889   0.80 32.42  ? 250 LEU B C     1 
ATOM   10627 O  O     A LEU B 2 250 ? 12.159  -14.603 9.236   0.20 29.97  ? 250 LEU B O     1 
ATOM   10628 O  O     B LEU B 2 250 ? 12.306  -14.604 10.050  0.80 29.60  ? 250 LEU B O     1 
ATOM   10629 C  CB    A LEU B 2 250 ? 10.984  -16.843 7.441   0.20 34.98  ? 250 LEU B CB    1 
ATOM   10630 C  CB    B LEU B 2 250 ? 11.414  -16.857 8.045   0.80 35.45  ? 250 LEU B CB    1 
ATOM   10631 C  CG    A LEU B 2 250 ? 11.257  -18.259 6.931   0.20 33.17  ? 250 LEU B CG    1 
ATOM   10632 C  CG    B LEU B 2 250 ? 11.581  -18.272 7.489   0.80 35.61  ? 250 LEU B CG    1 
ATOM   10633 C  CD1   A LEU B 2 250 ? 11.124  -18.332 5.418   0.20 35.60  ? 250 LEU B CD1   1 
ATOM   10634 C  CD1   B LEU B 2 250 ? 11.717  -18.218 5.988   0.80 36.13  ? 250 LEU B CD1   1 
ATOM   10635 C  CD2   A LEU B 2 250 ? 12.637  -18.721 7.373   0.20 35.39  ? 250 LEU B CD2   1 
ATOM   10636 C  CD2   B LEU B 2 250 ? 12.790  -18.957 8.117   0.80 34.85  ? 250 LEU B CD2   1 
ATOM   10637 N  N     A ARG B 2 251 ? 9.949   -14.564 9.663   0.20 33.64  ? 251 ARG B N     1 
ATOM   10638 N  N     B ARG B 2 251 ? 10.060  -14.553 9.970   0.80 33.90  ? 251 ARG B N     1 
ATOM   10639 C  CA    A ARG B 2 251 ? 9.974   -13.169 10.084  0.20 32.24  ? 251 ARG B CA    1 
ATOM   10640 C  CA    B ARG B 2 251 ? 10.050  -13.113 10.203  0.80 32.18  ? 251 ARG B CA    1 
ATOM   10641 C  C     A ARG B 2 251 ? 10.262  -13.039 11.574  0.20 32.49  ? 251 ARG B C     1 
ATOM   10642 C  C     B ARG B 2 251 ? 10.342  -12.786 11.662  0.80 33.16  ? 251 ARG B C     1 
ATOM   10643 O  O     A ARG B 2 251 ? 10.990  -12.128 11.983  0.20 28.27  ? 251 ARG B O     1 
ATOM   10644 O  O     B ARG B 2 251 ? 11.037  -11.806 11.950  0.80 26.26  ? 251 ARG B O     1 
ATOM   10645 C  CB    A ARG B 2 251 ? 8.649   -12.482 9.740   0.20 32.77  ? 251 ARG B CB    1 
ATOM   10646 C  CB    B ARG B 2 251 ? 8.713   -12.511 9.771   0.80 32.86  ? 251 ARG B CB    1 
ATOM   10647 C  CG    A ARG B 2 251 ? 8.708   -10.956 9.778   0.20 31.53  ? 251 ARG B CG    1 
ATOM   10648 C  CG    B ARG B 2 251 ? 8.623   -10.999 9.981   0.80 31.40  ? 251 ARG B CG    1 
ATOM   10649 C  CD    A ARG B 2 251 ? 7.371   -10.336 9.396   0.20 33.80  ? 251 ARG B CD    1 
ATOM   10650 C  CD    B ARG B 2 251 ? 7.321   -10.422 9.437   0.80 33.88  ? 251 ARG B CD    1 
ATOM   10651 N  NE    A ARG B 2 251 ? 6.883   -10.839 8.117   0.20 36.46  ? 251 ARG B NE    1 
ATOM   10652 N  NE    B ARG B 2 251 ? 7.234   -10.553 7.988   0.80 37.38  ? 251 ARG B NE    1 
ATOM   10653 C  CZ    A ARG B 2 251 ? 6.955   -10.178 6.969   0.20 33.40  ? 251 ARG B CZ    1 
ATOM   10654 C  CZ    B ARG B 2 251 ? 7.873   -9.766  7.134   0.80 33.11  ? 251 ARG B CZ    1 
ATOM   10655 N  NH1   A ARG B 2 251 ? 7.479   -8.965  6.901   0.20 28.69  ? 251 ARG B NH1   1 
ATOM   10656 N  NH1   B ARG B 2 251 ? 8.687   -8.811  7.552   0.80 34.43  ? 251 ARG B NH1   1 
ATOM   10657 N  NH2   A ARG B 2 251 ? 6.485   -10.746 5.863   0.20 34.46  ? 251 ARG B NH2   1 
ATOM   10658 N  NH2   B ARG B 2 251 ? 7.705   -9.953  5.831   0.80 42.56  ? 251 ARG B NH2   1 
ATOM   10659 N  N     A LYS B 2 252 ? 9.706   -13.936 12.394  0.20 31.43  ? 252 LYS B N     1 
ATOM   10660 N  N     B LYS B 2 252 ? 9.815   -13.583 12.595  0.80 28.92  ? 252 LYS B N     1 
ATOM   10661 C  CA    A LYS B 2 252 ? 10.057  -13.958 13.812  0.20 31.98  ? 252 LYS B CA    1 
ATOM   10662 C  CA    B LYS B 2 252 ? 10.175  -13.408 14.002  0.80 29.74  ? 252 LYS B CA    1 
ATOM   10663 C  C     A LYS B 2 252 ? 11.554  -14.167 14.001  0.20 33.74  ? 252 LYS B C     1 
ATOM   10664 C  C     B LYS B 2 252 ? 11.654  -13.691 14.234  0.80 33.91  ? 252 LYS B C     1 
ATOM   10665 O  O     A LYS B 2 252 ? 12.157  -13.600 14.920  0.20 31.14  ? 252 LYS B O     1 
ATOM   10666 O  O     B LYS B 2 252 ? 12.293  -13.027 15.056  0.80 31.68  ? 252 LYS B O     1 
ATOM   10667 C  CB    A LYS B 2 252 ? 9.272   -15.051 14.536  0.20 34.62  ? 252 LYS B CB    1 
ATOM   10668 C  CB    B LYS B 2 252 ? 9.325   -14.308 14.887  0.80 35.20  ? 252 LYS B CB    1 
ATOM   10669 C  CG    A LYS B 2 252 ? 7.782   -14.774 14.664  0.20 35.38  ? 252 LYS B CG    1 
ATOM   10670 C  CG    B LYS B 2 252 ? 7.909   -13.823 15.050  0.80 30.43  ? 252 LYS B CG    1 
ATOM   10671 C  CD    A LYS B 2 252 ? 7.120   -15.795 15.577  0.20 36.77  ? 252 LYS B CD    1 
ATOM   10672 C  CD    B LYS B 2 252 ? 7.201   -14.556 16.170  0.80 32.19  ? 252 LYS B CD    1 
ATOM   10673 C  CE    A LYS B 2 252 ? 5.617   -15.598 15.644  0.20 38.21  ? 252 LYS B CE    1 
ATOM   10674 C  CE    B LYS B 2 252 ? 5.722   -14.292 16.105  0.80 36.85  ? 252 LYS B CE    1 
ATOM   10675 N  NZ    A LYS B 2 252 ? 4.953   -15.844 14.332  0.20 39.36  ? 252 LYS B NZ    1 
ATOM   10676 N  NZ    B LYS B 2 252 ? 5.172   -15.056 14.944  0.80 45.99  ? 252 LYS B NZ    1 
ATOM   10677 N  N     A LEU B 2 253 ? 12.168  -14.980 13.140  0.20 33.14  ? 253 LEU B N     1 
ATOM   10678 N  N     B LEU B 2 253 ? 12.208  -14.687 13.531  0.80 34.44  ? 253 LEU B N     1 
ATOM   10679 C  CA    A LEU B 2 253 ? 13.620  -15.119 13.162  0.20 32.55  ? 253 LEU B CA    1 
ATOM   10680 C  CA    B LEU B 2 253 ? 13.644  -14.937 13.601  0.80 32.80  ? 253 LEU B CA    1 
ATOM   10681 C  C     A LEU B 2 253 ? 14.295  -13.805 12.791  0.20 28.42  ? 253 LEU B C     1 
ATOM   10682 C  C     B LEU B 2 253 ? 14.424  -13.680 13.240  0.80 27.28  ? 253 LEU B C     1 
ATOM   10683 O  O     A LEU B 2 253 ? 15.191  -13.333 13.499  0.20 27.60  ? 253 LEU B O     1 
ATOM   10684 O  O     B LEU B 2 253 ? 15.337  -13.274 13.965  0.80 26.18  ? 253 LEU B O     1 
ATOM   10685 C  CB    A LEU B 2 253 ? 14.054  -16.237 12.212  0.20 36.02  ? 253 LEU B CB    1 
ATOM   10686 C  CB    B LEU B 2 253 ? 14.026  -16.099 12.678  0.80 37.40  ? 253 LEU B CB    1 
ATOM   10687 C  CG    A LEU B 2 253 ? 15.555  -16.529 12.142  0.20 33.00  ? 253 LEU B CG    1 
ATOM   10688 C  CG    B LEU B 2 253 ? 15.524  -16.445 12.652  0.80 34.01  ? 253 LEU B CG    1 
ATOM   10689 C  CD1   A LEU B 2 253 ? 16.045  -17.131 13.450  0.20 36.13  ? 253 LEU B CD1   1 
ATOM   10690 C  CD1   B LEU B 2 253 ? 15.996  -16.812 14.060  0.80 33.77  ? 253 LEU B CD1   1 
ATOM   10691 C  CD2   A LEU B 2 253 ? 15.876  -17.451 10.978  0.20 32.39  ? 253 LEU B CD2   1 
ATOM   10692 C  CD2   B LEU B 2 253 ? 15.858  -17.563 11.660  0.80 36.26  ? 253 LEU B CD2   1 
ATOM   10693 N  N     A ALA B 2 254 ? 13.854  -13.185 11.692  0.20 28.78  ? 254 ALA B N     1 
ATOM   10694 N  N     B ALA B 2 254 ? 14.022  -13.014 12.152  0.80 27.99  ? 254 ALA B N     1 
ATOM   10695 C  CA    A ALA B 2 254 ? 14.502  -11.971 11.206  0.20 28.20  ? 254 ALA B CA    1 
ATOM   10696 C  CA    B ALA B 2 254 ? 14.724  -11.830 11.669  0.80 28.22  ? 254 ALA B CA    1 
ATOM   10697 C  C     A ALA B 2 254 ? 14.384  -10.827 12.206  0.20 28.12  ? 254 ALA B C     1 
ATOM   10698 C  C     B ALA B 2 254 ? 14.608  -10.661 12.639  0.80 29.35  ? 254 ALA B C     1 
ATOM   10699 O  O     A ALA B 2 254 ? 15.361  -10.114 12.459  0.20 27.63  ? 254 ALA B O     1 
ATOM   10700 O  O     B ALA B 2 254 ? 15.595  -9.953  12.888  0.80 27.77  ? 254 ALA B O     1 
ATOM   10701 C  CB    A ALA B 2 254 ? 13.907  -11.558 9.860   0.20 30.09  ? 254 ALA B CB    1 
ATOM   10702 C  CB    B ALA B 2 254 ? 14.183  -11.430 10.295  0.80 29.26  ? 254 ALA B CB    1 
ATOM   10703 N  N     A VAL B 2 255 ? 13.195  -10.631 12.780  0.20 26.76  ? 255 VAL B N     1 
ATOM   10704 N  N     B VAL B 2 255 ? 13.404  -10.427 13.176  0.80 24.68  ? 255 VAL B N     1 
ATOM   10705 C  CA    A VAL B 2 255 ? 12.995  -9.483  13.658  0.20 26.94  ? 255 VAL B CA    1 
ATOM   10706 C  CA    B VAL B 2 255 ? 13.188  -9.309  14.093  0.80 25.56  ? 255 VAL B CA    1 
ATOM   10707 C  C     A VAL B 2 255 ? 13.846  -9.603  14.916  0.20 24.68  ? 255 VAL B C     1 
ATOM   10708 C  C     B VAL B 2 255 ? 14.089  -9.437  15.310  0.80 23.49  ? 255 VAL B C     1 
ATOM   10709 O  O     A VAL B 2 255 ? 14.338  -8.595  15.435  0.20 25.16  ? 255 VAL B O     1 
ATOM   10710 O  O     B VAL B 2 255 ? 14.705  -8.463  15.751  0.80 29.03  ? 255 VAL B O     1 
ATOM   10711 C  CB    A VAL B 2 255 ? 11.499  -9.319  13.997  0.20 24.69  ? 255 VAL B CB    1 
ATOM   10712 C  CB    B VAL B 2 255 ? 11.704  -9.231  14.512  0.80 23.69  ? 255 VAL B CB    1 
ATOM   10713 C  CG1   A VAL B 2 255 ? 11.287  -8.155  14.956  0.20 26.59  ? 255 VAL B CG1   1 
ATOM   10714 C  CG1   B VAL B 2 255 ? 11.519  -8.182  15.599  0.80 26.06  ? 255 VAL B CG1   1 
ATOM   10715 C  CG2   A VAL B 2 255 ? 10.690  -9.099  12.732  0.20 29.20  ? 255 VAL B CG2   1 
ATOM   10716 C  CG2   B VAL B 2 255 ? 10.829  -8.914  13.334  0.80 26.62  ? 255 VAL B CG2   1 
ATOM   10717 N  N     A ASN B 2 256 ? 14.056  -10.821 15.414  0.20 25.27  ? 256 ASN B N     1 
ATOM   10718 N  N     B ASN B 2 256 ? 14.165  -10.641 15.883  0.80 23.44  ? 256 ASN B N     1 
ATOM   10719 C  CA    A ASN B 2 256 ? 14.744  -11.030 16.683  0.20 24.97  ? 256 ASN B CA    1 
ATOM   10720 C  CA    B ASN B 2 256 ? 14.911  -10.865 17.116  0.80 23.59  ? 256 ASN B CA    1 
ATOM   10721 C  C     A ASN B 2 256 ? 16.177  -11.530 16.533  0.20 28.09  ? 256 ASN B C     1 
ATOM   10722 C  C     B ASN B 2 256 ? 16.420  -11.030 16.919  0.80 27.99  ? 256 ASN B C     1 
ATOM   10723 O  O     A ASN B 2 256 ? 16.849  -11.746 17.547  0.20 27.65  ? 256 ASN B O     1 
ATOM   10724 O  O     B ASN B 2 256 ? 17.175  -10.827 17.880  0.80 30.67  ? 256 ASN B O     1 
ATOM   10725 C  CB    A ASN B 2 256 ? 13.942  -11.999 17.552  0.20 28.30  ? 256 ASN B CB    1 
ATOM   10726 C  CB    B ASN B 2 256 ? 14.350  -12.093 17.835  0.80 28.09  ? 256 ASN B CB    1 
ATOM   10727 C  CG    A ASN B 2 256 ? 12.612  -11.417 17.981  0.20 26.62  ? 256 ASN B CG    1 
ATOM   10728 C  CG    B ASN B 2 256 ? 12.999  -11.816 18.503  0.80 23.88  ? 256 ASN B CG    1 
ATOM   10729 O  OD1   A ASN B 2 256 ? 12.566  -10.432 18.718  0.20 24.14  ? 256 ASN B OD1   1 
ATOM   10730 O  OD1   B ASN B 2 256 ? 12.912  -11.041 19.448  0.80 29.90  ? 256 ASN B OD1   1 
ATOM   10731 N  ND2   A ASN B 2 256 ? 11.522  -12.015 17.513  0.20 29.83  ? 256 ASN B ND2   1 
ATOM   10732 N  ND2   B ASN B 2 256 ? 11.945  -12.463 18.015  0.80 34.41  ? 256 ASN B ND2   1 
ATOM   10733 N  N     A MET B 2 257 ? 16.661  -11.722 15.306  0.20 26.30  ? 257 MET B N     1 
ATOM   10734 N  N     B MET B 2 257 ? 16.882  -11.384 15.715  0.80 24.34  ? 257 MET B N     1 
ATOM   10735 C  CA    A MET B 2 257 ? 18.060  -12.053 15.074  0.20 26.94  ? 257 MET B CA    1 
ATOM   10736 C  CA    B MET B 2 257 ? 18.289  -11.718 15.487  0.80 26.93  ? 257 MET B CA    1 
ATOM   10737 C  C     A MET B 2 257 ? 18.788  -11.028 14.218  0.20 24.79  ? 257 MET B C     1 
ATOM   10738 C  C     B MET B 2 257 ? 19.081  -10.624 14.780  0.80 27.54  ? 257 MET B C     1 
ATOM   10739 O  O     A MET B 2 257 ? 20.021  -11.081 14.140  0.20 27.87  ? 257 MET B O     1 
ATOM   10740 O  O     B MET B 2 257 ? 20.318  -10.612 14.886  0.80 25.63  ? 257 MET B O     1 
ATOM   10741 C  CB    A MET B 2 257 ? 18.195  -13.435 14.414  0.20 27.31  ? 257 MET B CB    1 
ATOM   10742 C  CB    B MET B 2 257 ? 18.413  -13.001 14.654  0.80 27.49  ? 257 MET B CB    1 
ATOM   10743 C  CG    A MET B 2 257 ? 17.812  -14.608 15.305  0.20 29.79  ? 257 MET B CG    1 
ATOM   10744 C  CG    B MET B 2 257 ? 18.116  -14.304 15.384  0.80 28.65  ? 257 MET B CG    1 
ATOM   10745 S  SD    A MET B 2 257 ? 18.947  -14.885 16.675  0.20 31.48  ? 257 MET B SD    1 
ATOM   10746 S  SD    B MET B 2 257 ? 19.216  -14.663 16.756  0.80 32.34  ? 257 MET B SD    1 
ATOM   10747 C  CE    A MET B 2 257 ? 20.435  -15.366 15.801  0.20 28.09  ? 257 MET B CE    1 
ATOM   10748 C  CE    B MET B 2 257 ? 20.763  -14.938 15.879  0.80 28.57  ? 257 MET B CE    1 
ATOM   10749 N  N     A VAL B 2 258 ? 18.073  -10.102 13.584  0.20 25.32  ? 258 VAL B N     1 
ATOM   10750 N  N     B VAL B 2 258 ? 18.412  -9.704  14.085  0.80 25.09  ? 258 VAL B N     1 
ATOM   10751 C  CA    A VAL B 2 258 ? 18.686  -9.092  12.724  0.20 25.03  ? 258 VAL B CA    1 
ATOM   10752 C  CA    B VAL B 2 258 ? 19.072  -8.719  13.226  0.80 27.03  ? 258 VAL B CA    1 
ATOM   10753 C  C     A VAL B 2 258 ? 18.456  -7.714  13.334  0.20 25.64  ? 258 VAL B C     1 
ATOM   10754 C  C     B VAL B 2 258 ? 18.883  -7.295  13.738  0.80 24.79  ? 258 VAL B C     1 
ATOM   10755 O  O     A VAL B 2 258 ? 17.424  -7.083  13.065  0.20 25.09  ? 258 VAL B O     1 
ATOM   10756 O  O     B VAL B 2 258 ? 17.938  -6.619  13.310  0.80 27.16  ? 258 VAL B O     1 
ATOM   10757 C  CB    A VAL B 2 258 ? 18.127  -9.164  11.293  0.20 28.01  ? 258 VAL B CB    1 
ATOM   10758 C  CB    B VAL B 2 258 ? 18.540  -8.810  11.792  0.80 26.83  ? 258 VAL B CB    1 
ATOM   10759 C  CG1   A VAL B 2 258 ? 18.819  -8.150  10.392  0.20 27.21  ? 258 VAL B CG1   1 
ATOM   10760 C  CG1   B VAL B 2 258 ? 19.346  -7.889  10.858  0.80 24.72  ? 258 VAL B CG1   1 
ATOM   10761 C  CG2   A VAL B 2 258 ? 18.281  -10.567 10.733  0.20 28.39  ? 258 VAL B CG2   1 
ATOM   10762 C  CG2   B VAL B 2 258 ? 18.551  -10.262 11.316  0.80 26.58  ? 258 VAL B CG2   1 
ATOM   10763 N  N     A PRO B 2 259 ? 19.379  -7.210  14.160  0.20 25.07  ? 259 PRO B N     1 
ATOM   10764 N  N     B PRO B 2 259 ? 19.771  -6.774  14.593  0.80 21.86  ? 259 PRO B N     1 
ATOM   10765 C  CA    A PRO B 2 259 ? 19.197  -5.858  14.709  0.20 27.32  ? 259 PRO B CA    1 
ATOM   10766 C  CA    B PRO B 2 259 ? 19.564  -5.420  15.134  0.80 23.83  ? 259 PRO B CA    1 
ATOM   10767 C  C     A PRO B 2 259 ? 19.424  -4.765  13.686  0.20 24.96  ? 259 PRO B C     1 
ATOM   10768 C  C     B PRO B 2 259 ? 19.904  -4.300  14.165  0.80 26.68  ? 259 PRO B C     1 
ATOM   10769 O  O     A PRO B 2 259 ? 18.774  -3.715  13.762  0.20 27.66  ? 259 PRO B O     1 
ATOM   10770 O  O     B PRO B 2 259 ? 19.565  -3.138  14.437  0.80 24.29  ? 259 PRO B O     1 
ATOM   10771 C  CB    A PRO B 2 259 ? 20.232  -5.799  15.838  0.20 23.17  ? 259 PRO B CB    1 
ATOM   10772 C  CB    B PRO B 2 259 ? 20.479  -5.386  16.358  0.80 25.18  ? 259 PRO B CB    1 
ATOM   10773 C  CG    A PRO B 2 259 ? 21.300  -6.741  15.399  0.20 26.79  ? 259 PRO B CG    1 
ATOM   10774 C  CG    B PRO B 2 259 ? 21.534  -6.406  16.079  0.80 28.27  ? 259 PRO B CG    1 
ATOM   10775 C  CD    A PRO B 2 259 ? 20.601  -7.856  14.669  0.20 23.95  ? 259 PRO B CD    1 
ATOM   10776 C  CD    B PRO B 2 259 ? 20.903  -7.469  15.222  0.80 23.96  ? 259 PRO B CD    1 
ATOM   10777 N  N     A PHE B 2 260 ? 20.333  -4.972  12.739  0.20 26.58  ? 260 PHE B N     1 
ATOM   10778 N  N     B PHE B 2 260 ? 20.574  -4.599  13.055  0.80 24.36  ? 260 PHE B N     1 
ATOM   10779 C  CA    A PHE B 2 260 ? 20.604  -4.013  11.683  0.20 30.50  ? 260 PHE B CA    1 
ATOM   10780 C  CA    B PHE B 2 260 ? 20.959  -3.572  12.097  0.80 32.68  ? 260 PHE B CA    1 
ATOM   10781 C  C     A PHE B 2 260 ? 20.468  -4.706  10.335  0.20 26.41  ? 260 PHE B C     1 
ATOM   10782 C  C     B PHE B 2 260 ? 20.864  -4.207  10.717  0.80 23.46  ? 260 PHE B C     1 
ATOM   10783 O  O     A PHE B 2 260 ? 20.923  -5.846  10.176  0.20 27.13  ? 260 PHE B O     1 
ATOM   10784 O  O     B PHE B 2 260 ? 21.304  -5.354  10.551  0.80 27.79  ? 260 PHE B O     1 
ATOM   10785 C  CB    A PHE B 2 260 ? 22.005  -3.411  11.833  0.20 28.60  ? 260 PHE B CB    1 
ATOM   10786 C  CB    B PHE B 2 260 ? 22.359  -3.048  12.360  0.80 33.06  ? 260 PHE B CB    1 
ATOM   10787 C  CG    A PHE B 2 260 ? 22.284  -2.885  13.210  0.20 28.30  ? 260 PHE B CG    1 
ATOM   10788 C  CG    B PHE B 2 260 ? 22.525  -2.493  13.735  0.80 24.43  ? 260 PHE B CG    1 
ATOM   10789 C  CD1   A PHE B 2 260 ? 21.791  -1.653  13.607  0.20 29.49  ? 260 PHE B CD1   1 
ATOM   10790 C  CD1   B PHE B 2 260 ? 22.014  -1.246  14.053  0.80 32.65  ? 260 PHE B CD1   1 
ATOM   10791 C  CD2   A PHE B 2 260 ? 23.029  -3.626  14.108  0.20 26.96  ? 260 PHE B CD2   1 
ATOM   10792 C  CD2   B PHE B 2 260 ? 23.171  -3.219  14.711  0.80 28.31  ? 260 PHE B CD2   1 
ATOM   10793 C  CE1   A PHE B 2 260 ? 22.041  -1.168  14.877  0.20 29.87  ? 260 PHE B CE1   1 
ATOM   10794 C  CE1   B PHE B 2 260 ? 22.156  -0.732  15.319  0.80 29.67  ? 260 PHE B CE1   1 
ATOM   10795 C  CE2   A PHE B 2 260 ? 23.283  -3.148  15.378  0.20 31.62  ? 260 PHE B CE2   1 
ATOM   10796 C  CE2   B PHE B 2 260 ? 23.317  -2.707  15.987  0.80 35.42  ? 260 PHE B CE2   1 
ATOM   10797 C  CZ    A PHE B 2 260 ? 22.788  -1.917  15.764  0.20 27.81  ? 260 PHE B CZ    1 
ATOM   10798 C  CZ    B PHE B 2 260 ? 22.814  -1.468  16.287  0.80 24.83  ? 260 PHE B CZ    1 
ATOM   10799 N  N     A PRO B 2 261 ? 19.851  -4.047  9.352   0.20 28.79  ? 261 PRO B N     1 
ATOM   10800 N  N     B PRO B 2 261 ? 20.277  -3.514  9.741   0.80 29.19  ? 261 PRO B N     1 
ATOM   10801 C  CA    A PRO B 2 261 ? 19.489  -4.752  8.110   0.20 29.47  ? 261 PRO B CA    1 
ATOM   10802 C  CA    B PRO B 2 261 ? 19.805  -4.216  8.536   0.80 28.87  ? 261 PRO B CA    1 
ATOM   10803 C  C     A PRO B 2 261 ? 20.671  -5.348  7.366   0.20 27.02  ? 261 PRO B C     1 
ATOM   10804 C  C     B PRO B 2 261 ? 20.868  -5.032  7.824   0.80 27.68  ? 261 PRO B C     1 
ATOM   10805 O  O     A PRO B 2 261 ? 20.498  -6.351  6.660   0.20 27.41  ? 261 PRO B O     1 
ATOM   10806 O  O     B PRO B 2 261 ? 20.587  -6.167  7.417   0.80 25.07  ? 261 PRO B O     1 
ATOM   10807 C  CB    A PRO B 2 261 ? 18.786  -3.664  7.282   0.20 28.22  ? 261 PRO B CB    1 
ATOM   10808 C  CB    B PRO B 2 261 ? 19.258  -3.079  7.659   0.80 30.32  ? 261 PRO B CB    1 
ATOM   10809 C  CG    A PRO B 2 261 ? 19.207  -2.363  7.897   0.20 30.71  ? 261 PRO B CG    1 
ATOM   10810 C  CG    B PRO B 2 261 ? 19.620  -1.793  8.357   0.80 34.82  ? 261 PRO B CG    1 
ATOM   10811 C  CD    A PRO B 2 261 ? 19.407  -2.644  9.349   0.20 28.06  ? 261 PRO B CD    1 
ATOM   10812 C  CD    B PRO B 2 261 ? 19.822  -2.118  9.789   0.80 28.38  ? 261 PRO B CD    1 
ATOM   10813 N  N     A ARG B 2 262 ? 21.867  -4.778  7.508   0.20 29.13  ? 262 ARG B N     1 
ATOM   10814 N  N     B ARG B 2 262 ? 22.096  -4.515  7.704   0.80 28.14  ? 262 ARG B N     1 
ATOM   10815 C  CA    A ARG B 2 262 ? 23.047  -5.300  6.832   0.20 26.46  ? 262 ARG B CA    1 
ATOM   10816 C  CA    B ARG B 2 262 ? 23.126  -5.197  6.923   0.80 26.24  ? 262 ARG B CA    1 
ATOM   10817 C  C     A ARG B 2 262 ? 23.731  -6.426  7.597   0.20 27.80  ? 262 ARG B C     1 
ATOM   10818 C  C     B ARG B 2 262 ? 23.779  -6.354  7.671   0.80 27.66  ? 262 ARG B C     1 
ATOM   10819 O  O     A ARG B 2 262 ? 24.588  -7.108  7.026   0.20 28.02  ? 262 ARG B O     1 
ATOM   10820 O  O     B ARG B 2 262 ? 24.301  -7.274  7.032   0.80 26.54  ? 262 ARG B O     1 
ATOM   10821 C  CB    A ARG B 2 262 ? 24.055  -4.171  6.578   0.20 29.23  ? 262 ARG B CB    1 
ATOM   10822 C  CB    B ARG B 2 262 ? 24.195  -4.186  6.483   0.80 28.80  ? 262 ARG B CB    1 
ATOM   10823 C  CG    A ARG B 2 262 ? 23.542  -3.085  5.644   0.20 31.61  ? 262 ARG B CG    1 
ATOM   10824 C  CG    B ARG B 2 262 ? 23.690  -3.161  5.462   0.80 31.24  ? 262 ARG B CG    1 
ATOM   10825 C  CD    A ARG B 2 262 ? 24.524  -1.931  5.539   0.20 32.70  ? 262 ARG B CD    1 
ATOM   10826 C  CD    B ARG B 2 262 ? 24.500  -1.874  5.497   0.80 32.35  ? 262 ARG B CD    1 
ATOM   10827 N  NE    A ARG B 2 262 ? 25.819  -2.364  5.029   0.20 37.25  ? 262 ARG B NE    1 
ATOM   10828 N  NE    B ARG B 2 262 ? 25.924  -2.123  5.323   0.80 36.34  ? 262 ARG B NE    1 
ATOM   10829 C  CZ    A ARG B 2 262 ? 26.123  -2.452  3.742   0.20 44.46  ? 262 ARG B CZ    1 
ATOM   10830 C  CZ    B ARG B 2 262 ? 26.546  -2.127  4.153   0.80 47.26  ? 262 ARG B CZ    1 
ATOM   10831 N  NH1   A ARG B 2 262 ? 25.244  -2.147  2.801   0.20 43.67  ? 262 ARG B NH1   1 
ATOM   10832 N  NH1   B ARG B 2 262 ? 25.898  -1.876  3.025   0.80 49.77  ? 262 ARG B NH1   1 
ATOM   10833 N  NH2   A ARG B 2 262 ? 27.340  -2.857  3.388   0.20 38.92  ? 262 ARG B NH2   1 
ATOM   10834 N  NH2   B ARG B 2 262 ? 27.848  -2.394  4.111   0.80 42.76  ? 262 ARG B NH2   1 
ATOM   10835 N  N     A LEU B 2 263 ? 23.375  -6.645  8.862   0.20 26.63  ? 263 LEU B N     1 
ATOM   10836 N  N     B LEU B 2 263 ? 23.736  -6.351  9.002   0.80 29.65  ? 263 LEU B N     1 
ATOM   10837 C  CA    A LEU B 2 263 ? 24.005  -7.687  9.670   0.20 26.58  ? 263 LEU B CA    1 
ATOM   10838 C  CA    B LEU B 2 263 ? 24.385  -7.389  9.803   0.80 28.41  ? 263 LEU B CA    1 
ATOM   10839 C  C     A LEU B 2 263 ? 23.045  -8.867  9.816   0.20 28.35  ? 263 LEU B C     1 
ATOM   10840 C  C     B LEU B 2 263 ? 23.411  -8.549  9.984   0.80 26.74  ? 263 LEU B C     1 
ATOM   10841 O  O     A LEU B 2 263 ? 22.475  -9.130  10.878  0.20 29.02  ? 263 LEU B O     1 
ATOM   10842 O  O     B LEU B 2 263 ? 22.860  -8.796  11.063  0.80 31.11  ? 263 LEU B O     1 
ATOM   10843 C  CB    A LEU B 2 263 ? 24.427  -7.126  11.028  0.20 29.45  ? 263 LEU B CB    1 
ATOM   10844 C  CB    B LEU B 2 263 ? 24.854  -6.822  11.140  0.80 31.28  ? 263 LEU B CB    1 
ATOM   10845 C  CG    A LEU B 2 263 ? 25.313  -5.875  11.035  0.20 31.99  ? 263 LEU B CG    1 
ATOM   10846 C  CG    B LEU B 2 263 ? 25.702  -5.537  11.080  0.80 31.72  ? 263 LEU B CG    1 
ATOM   10847 C  CD1   A LEU B 2 263 ? 25.885  -5.620  12.423  0.20 31.20  ? 263 LEU B CD1   1 
ATOM   10848 C  CD1   B LEU B 2 263 ? 26.348  -5.236  12.421  0.80 29.46  ? 263 LEU B CD1   1 
ATOM   10849 C  CD2   A LEU B 2 263 ? 26.429  -5.981  10.007  0.20 32.41  ? 263 LEU B CD2   1 
ATOM   10850 C  CD2   B LEU B 2 263 ? 26.761  -5.617  9.979   0.80 33.54  ? 263 LEU B CD2   1 
ATOM   10851 N  N     A HIS B 2 264 ? 22.874  -9.584  8.704   0.20 27.62  ? 264 HIS B N     1 
ATOM   10852 N  N     B HIS B 2 264 ? 23.179  -9.251  8.879   0.80 28.90  ? 264 HIS B N     1 
ATOM   10853 C  CA    A HIS B 2 264 ? 21.964  -10.720 8.632   0.20 27.06  ? 264 HIS B CA    1 
ATOM   10854 C  CA    B HIS B 2 264 ? 22.210  -10.335 8.851   0.80 27.31  ? 264 HIS B CA    1 
ATOM   10855 C  C     A HIS B 2 264 ? 22.679  -11.989 8.177   0.20 26.10  ? 264 HIS B C     1 
ATOM   10856 C  C     B HIS B 2 264 ? 22.853  -11.647 8.413   0.80 23.67  ? 264 HIS B C     1 
ATOM   10857 O  O     A HIS B 2 264 ? 22.068  -12.873 7.571   0.20 26.06  ? 264 HIS B O     1 
ATOM   10858 O  O     B HIS B 2 264 ? 22.192  -12.507 7.829   0.80 27.05  ? 264 HIS B O     1 
ATOM   10859 C  CB    A HIS B 2 264 ? 20.780  -10.408 7.716   0.20 27.64  ? 264 HIS B CB    1 
ATOM   10860 C  CB    B HIS B 2 264 ? 21.010  -9.969  7.975   0.80 27.49  ? 264 HIS B CB    1 
ATOM   10861 C  CG    A HIS B 2 264 ? 21.170  -10.051 6.314   0.20 28.71  ? 264 HIS B CG    1 
ATOM   10862 C  CG    B HIS B 2 264 ? 21.353  -9.650  6.547   0.80 29.88  ? 264 HIS B CG    1 
ATOM   10863 N  ND1   A HIS B 2 264 ? 21.375  -8.750  5.906   0.20 27.71  ? 264 HIS B ND1   1 
ATOM   10864 N  ND1   B HIS B 2 264 ? 21.312  -8.368  6.040   0.80 27.77  ? 264 HIS B ND1   1 
ATOM   10865 C  CD2   A HIS B 2 264 ? 21.383  -10.824 5.222   0.20 29.30  ? 264 HIS B CD2   1 
ATOM   10866 C  CD2   B HIS B 2 264 ? 21.705  -10.450 5.513   0.80 28.17  ? 264 HIS B CD2   1 
ATOM   10867 C  CE1   A HIS B 2 264 ? 21.697  -8.737  4.625   0.20 27.11  ? 264 HIS B CE1   1 
ATOM   10868 C  CE1   B HIS B 2 264 ? 21.628  -8.391  4.757   0.80 25.11  ? 264 HIS B CE1   1 
ATOM   10869 N  NE2   A HIS B 2 264 ? 21.709  -9.982  4.185   0.20 27.89  ? 264 HIS B NE2   1 
ATOM   10870 N  NE2   B HIS B 2 264 ? 21.865  -9.643  4.409   0.80 28.48  ? 264 HIS B NE2   1 
ATOM   10871 N  N     A PHE B 2 265 ? 23.974  -12.093 8.469   0.20 25.73  ? 265 PHE B N     1 
ATOM   10872 N  N     B PHE B 2 265 ? 24.136  -11.827 8.748   0.80 25.36  ? 265 PHE B N     1 
ATOM   10873 C  CA    A PHE B 2 265 ? 24.776  -13.268 8.143   0.20 29.21  ? 265 PHE B CA    1 
ATOM   10874 C  CA    B PHE B 2 265 ? 24.930  -12.996 8.369   0.80 30.40  ? 265 PHE B CA    1 
ATOM   10875 C  C     A PHE B 2 265 ? 25.033  -14.037 9.432   0.20 29.46  ? 265 PHE B C     1 
ATOM   10876 C  C     B PHE B 2 265 ? 25.204  -13.832 9.613   0.80 30.00  ? 265 PHE B C     1 
ATOM   10877 O  O     A PHE B 2 265 ? 25.715  -13.537 10.334  0.20 28.20  ? 265 PHE B O     1 
ATOM   10878 O  O     B PHE B 2 265 ? 25.938  -13.398 10.507  0.80 27.45  ? 265 PHE B O     1 
ATOM   10879 C  CB    A PHE B 2 265 ? 26.085  -12.867 7.464   0.20 29.16  ? 265 PHE B CB    1 
ATOM   10880 C  CB    B PHE B 2 265 ? 26.235  -12.562 7.693   0.80 29.23  ? 265 PHE B CB    1 
ATOM   10881 C  CG    A PHE B 2 265 ? 25.892  -12.191 6.140   0.20 29.76  ? 265 PHE B CG    1 
ATOM   10882 C  CG    B PHE B 2 265 ? 26.017  -11.758 6.446   0.80 29.05  ? 265 PHE B CG    1 
ATOM   10883 C  CD1   A PHE B 2 265 ? 25.777  -12.937 4.976   0.20 26.10  ? 265 PHE B CD1   1 
ATOM   10884 C  CD1   B PHE B 2 265 ? 25.855  -12.387 5.217   0.80 27.78  ? 265 PHE B CD1   1 
ATOM   10885 C  CD2   A PHE B 2 265 ? 25.810  -10.812 6.058   0.20 27.82  ? 265 PHE B CD2   1 
ATOM   10886 C  CD2   B PHE B 2 265 ? 25.928  -10.379 6.503   0.80 24.86  ? 265 PHE B CD2   1 
ATOM   10887 C  CE1   A PHE B 2 265 ? 25.590  -12.318 3.759   0.20 30.21  ? 265 PHE B CE1   1 
ATOM   10888 C  CE1   B PHE B 2 265 ? 25.622  -11.652 4.081   0.80 30.73  ? 265 PHE B CE1   1 
ATOM   10889 C  CE2   A PHE B 2 265 ? 25.625  -10.188 4.841   0.20 28.48  ? 265 PHE B CE2   1 
ATOM   10890 C  CE2   B PHE B 2 265 ? 25.697  -9.640  5.358   0.80 30.11  ? 265 PHE B CE2   1 
ATOM   10891 C  CZ    A PHE B 2 265 ? 25.516  -10.942 3.690   0.20 29.89  ? 265 PHE B CZ    1 
ATOM   10892 C  CZ    B PHE B 2 265 ? 25.552  -10.279 4.150   0.80 28.45  ? 265 PHE B CZ    1 
ATOM   10893 N  N     A PHE B 2 266 ? 24.490  -15.247 9.515   0.20 28.77  ? 266 PHE B N     1 
ATOM   10894 N  N     B PHE B 2 266 ? 24.622  -15.031 9.666   0.80 29.16  ? 266 PHE B N     1 
ATOM   10895 C  CA    A PHE B 2 266 ? 24.523  -16.041 10.735  0.20 27.63  ? 266 PHE B CA    1 
ATOM   10896 C  CA    B PHE B 2 266 ? 24.674  -15.880 10.849  0.80 27.20  ? 266 PHE B CA    1 
ATOM   10897 C  C     A PHE B 2 266 ? 25.658  -17.056 10.687  0.20 29.42  ? 266 PHE B C     1 
ATOM   10898 C  C     B PHE B 2 266 ? 25.794  -16.907 10.766  0.80 29.84  ? 266 PHE B C     1 
ATOM   10899 O  O     A PHE B 2 266 ? 25.970  -17.609 9.628   0.20 29.36  ? 266 PHE B O     1 
ATOM   10900 O  O     B PHE B 2 266 ? 26.051  -17.488 9.704   0.80 29.89  ? 266 PHE B O     1 
ATOM   10901 C  CB    A PHE B 2 266 ? 23.191  -16.766 10.949  0.20 25.40  ? 266 PHE B CB    1 
ATOM   10902 C  CB    B PHE B 2 266 ? 23.349  -16.619 11.059  0.80 24.46  ? 266 PHE B CB    1 
ATOM   10903 C  CG    A PHE B 2 266 ? 21.996  -15.850 10.993  0.20 27.10  ? 266 PHE B CG    1 
ATOM   10904 C  CG    B PHE B 2 266 ? 22.176  -15.704 11.248  0.80 26.98  ? 266 PHE B CG    1 
ATOM   10905 C  CD1   A PHE B 2 266 ? 22.124  -14.533 11.408  0.20 28.30  ? 266 PHE B CD1   1 
ATOM   10906 C  CD1   B PHE B 2 266 ? 22.329  -14.494 11.918  0.80 25.60  ? 266 PHE B CD1   1 
ATOM   10907 C  CD2   A PHE B 2 266 ? 20.742  -16.310 10.622  0.20 27.60  ? 266 PHE B CD2   1 
ATOM   10908 C  CD2   B PHE B 2 266 ? 20.924  -16.049 10.754  0.80 27.92  ? 266 PHE B CD2   1 
ATOM   10909 C  CE1   A PHE B 2 266 ? 21.022  -13.691 11.448  0.20 29.50  ? 266 PHE B CE1   1 
ATOM   10910 C  CE1   B PHE B 2 266 ? 21.238  -13.641 12.085  0.80 31.56  ? 266 PHE B CE1   1 
ATOM   10911 C  CE2   A PHE B 2 266 ? 19.642  -15.477 10.659  0.20 31.68  ? 266 PHE B CE2   1 
ATOM   10912 C  CE2   B PHE B 2 266 ? 19.844  -15.211 10.919  0.80 33.86  ? 266 PHE B CE2   1 
ATOM   10913 C  CZ    A PHE B 2 266 ? 19.781  -14.164 11.073  0.20 29.48  ? 266 PHE B CZ    1 
ATOM   10914 C  CZ    B PHE B 2 266 ? 19.998  -14.001 11.577  0.80 30.24  ? 266 PHE B CZ    1 
ATOM   10915 N  N     A MET B 2 267 ? 26.271  -17.298 11.849  0.20 28.25  ? 267 MET B N     1 
ATOM   10916 N  N     B MET B 2 267 ? 26.434  -17.136 11.911  0.80 27.63  ? 267 MET B N     1 
ATOM   10917 C  CA    A MET B 2 267 ? 27.308  -18.307 12.011  0.20 26.88  ? 267 MET B CA    1 
ATOM   10918 C  CA    B MET B 2 267 ? 27.371  -18.225 12.136  0.80 26.34  ? 267 MET B CA    1 
ATOM   10919 C  C     A MET B 2 267 ? 26.689  -19.541 12.659  0.20 32.49  ? 267 MET B C     1 
ATOM   10920 C  C     B MET B 2 267 ? 26.630  -19.410 12.743  0.80 33.25  ? 267 MET B C     1 
ATOM   10921 O  O     A MET B 2 267 ? 26.446  -19.540 13.876  0.20 31.03  ? 267 MET B O     1 
ATOM   10922 O  O     B MET B 2 267 ? 26.219  -19.336 13.916  0.80 29.11  ? 267 MET B O     1 
ATOM   10923 C  CB    A MET B 2 267 ? 28.457  -17.765 12.868  0.20 30.77  ? 267 MET B CB    1 
ATOM   10924 C  CB    B MET B 2 267 ? 28.480  -17.740 13.074  0.80 30.73  ? 267 MET B CB    1 
ATOM   10925 C  CG    A MET B 2 267 ? 29.736  -18.590 12.818  0.20 36.46  ? 267 MET B CG    1 
ATOM   10926 C  CG    B MET B 2 267 ? 29.408  -18.788 13.660  0.80 37.56  ? 267 MET B CG    1 
ATOM   10927 S  SD    A MET B 2 267 ? 31.022  -17.962 13.924  0.20 40.32  ? 267 MET B SD    1 
ATOM   10928 S  SD    B MET B 2 267 ? 30.751  -17.999 14.602  0.80 50.45  ? 267 MET B SD    1 
ATOM   10929 C  CE    A MET B 2 267 ? 30.995  -16.216 13.531  0.20 31.70  ? 267 MET B CE    1 
ATOM   10930 C  CE    B MET B 2 267 ? 30.485  -16.271 14.226  0.80 34.25  ? 267 MET B CE    1 
ATOM   10931 N  N     A PRO B 2 268 ? 26.409  -20.604 11.909  0.20 27.86  ? 268 PRO B N     1 
ATOM   10932 N  N     B PRO B 2 268 ? 26.413  -20.500 12.010  0.80 26.98  ? 268 PRO B N     1 
ATOM   10933 C  CA    A PRO B 2 268 ? 25.758  -21.777 12.493  0.20 31.19  ? 268 PRO B CA    1 
ATOM   10934 C  CA    B PRO B 2 268 ? 25.785  -21.682 12.603  0.80 31.19  ? 268 PRO B CA    1 
ATOM   10935 C  C     A PRO B 2 268 ? 26.741  -22.832 12.974  0.20 33.32  ? 268 PRO B C     1 
ATOM   10936 C  C     B PRO B 2 268 ? 26.812  -22.581 13.276  0.80 34.35  ? 268 PRO B C     1 
ATOM   10937 O  O     A PRO B 2 268 ? 27.843  -22.998 12.445  0.20 29.89  ? 268 PRO B O     1 
ATOM   10938 O  O     B PRO B 2 268 ? 28.015  -22.500 13.024  0.80 27.84  ? 268 PRO B O     1 
ATOM   10939 C  CB    A PRO B 2 268 ? 24.917  -22.312 11.324  0.20 31.81  ? 268 PRO B CB    1 
ATOM   10940 C  CB    B PRO B 2 268 ? 25.152  -22.395 11.397  0.80 32.13  ? 268 PRO B CB    1 
ATOM   10941 C  CG    A PRO B 2 268 ? 25.632  -21.829 10.074  0.20 29.90  ? 268 PRO B CG    1 
ATOM   10942 C  CG    B PRO B 2 268 ? 25.759  -21.744 10.168  0.80 29.83  ? 268 PRO B CG    1 
ATOM   10943 C  CD    A PRO B 2 268 ? 26.652  -20.783 10.469  0.20 29.77  ? 268 PRO B CD    1 
ATOM   10944 C  CD    B PRO B 2 268 ? 26.786  -20.752 10.611  0.80 29.88  ? 268 PRO B CD    1 
ATOM   10945 N  N     A GLY B 2 269 ? 26.309  -23.560 14.008  0.20 30.41  ? 269 GLY B N     1 
ATOM   10946 N  N     B GLY B 2 269 ? 26.304  -23.456 14.138  0.80 29.81  ? 269 GLY B N     1 
ATOM   10947 C  CA    A GLY B 2 269 ? 27.095  -24.645 14.553  0.20 33.40  ? 269 GLY B CA    1 
ATOM   10948 C  CA    B GLY B 2 269 ? 27.150  -24.392 14.851  0.80 33.35  ? 269 GLY B CA    1 
ATOM   10949 C  C     A GLY B 2 269 ? 26.223  -25.853 14.832  0.20 36.38  ? 269 GLY B C     1 
ATOM   10950 C  C     B GLY B 2 269 ? 26.344  -25.570 15.345  0.80 36.53  ? 269 GLY B C     1 
ATOM   10951 O  O     A GLY B 2 269 ? 24.993  -25.789 14.758  0.20 36.15  ? 269 GLY B O     1 
ATOM   10952 O  O     B GLY B 2 269 ? 25.152  -25.446 15.647  0.80 33.78  ? 269 GLY B O     1 
ATOM   10953 N  N     A PHE B 2 270 ? 26.885  -26.960 15.160  0.20 35.92  ? 270 PHE B N     1 
ATOM   10954 N  N     B PHE B 2 270 ? 27.008  -26.724 15.442  0.80 34.91  ? 270 PHE B N     1 
ATOM   10955 C  CA    A PHE B 2 270 ? 26.193  -28.216 15.403  0.20 38.62  ? 270 PHE B CA    1 
ATOM   10956 C  CA    B PHE B 2 270 ? 26.332  -27.989 15.685  0.80 37.94  ? 270 PHE B CA    1 
ATOM   10957 C  C     A PHE B 2 270 ? 27.020  -29.072 16.351  0.20 41.57  ? 270 PHE B C     1 
ATOM   10958 C  C     B PHE B 2 270 ? 27.142  -28.836 16.658  0.80 41.32  ? 270 PHE B C     1 
ATOM   10959 O  O     A PHE B 2 270 ? 28.252  -29.091 16.269  0.20 40.70  ? 270 PHE B O     1 
ATOM   10960 O  O     B PHE B 2 270 ? 28.376  -28.800 16.665  0.80 40.67  ? 270 PHE B O     1 
ATOM   10961 C  CB    A PHE B 2 270 ? 25.933  -28.969 14.092  0.20 41.24  ? 270 PHE B CB    1 
ATOM   10962 C  CB    B PHE B 2 270 ? 26.113  -28.753 14.364  0.80 42.15  ? 270 PHE B CB    1 
ATOM   10963 C  CG    A PHE B 2 270 ? 24.985  -30.126 14.232  0.20 38.66  ? 270 PHE B CG    1 
ATOM   10964 C  CG    B PHE B 2 270 ? 25.149  -29.904 14.471  0.80 37.50  ? 270 PHE B CG    1 
ATOM   10965 C  CD1   A PHE B 2 270 ? 23.622  -29.943 14.069  0.20 39.75  ? 270 PHE B CD1   1 
ATOM   10966 C  CD1   B PHE B 2 270 ? 25.585  -31.160 14.872  0.80 41.37  ? 270 PHE B CD1   1 
ATOM   10967 C  CD2   A PHE B 2 270 ? 25.456  -31.395 14.526  0.20 41.50  ? 270 PHE B CD2   1 
ATOM   10968 C  CD2   B PHE B 2 270 ? 23.806  -29.730 14.166  0.80 39.27  ? 270 PHE B CD2   1 
ATOM   10969 C  CE1   A PHE B 2 270 ? 22.744  -31.005 14.198  0.20 43.33  ? 270 PHE B CE1   1 
ATOM   10970 C  CE1   B PHE B 2 270 ? 24.700  -32.222 14.976  0.80 43.53  ? 270 PHE B CE1   1 
ATOM   10971 C  CE2   A PHE B 2 270 ? 24.585  -32.461 14.657  0.20 43.15  ? 270 PHE B CE2   1 
ATOM   10972 C  CE2   B PHE B 2 270 ? 22.912  -30.788 14.263  0.80 44.59  ? 270 PHE B CE2   1 
ATOM   10973 C  CZ    A PHE B 2 270 ? 23.227  -32.266 14.492  0.20 40.96  ? 270 PHE B CZ    1 
ATOM   10974 C  CZ    B PHE B 2 270 ? 23.359  -32.038 14.670  0.80 41.31  ? 270 PHE B CZ    1 
ATOM   10975 N  N     A ALA B 2 271 ? 26.332  -29.781 17.248  0.20 42.11  ? 271 ALA B N     1 
ATOM   10976 N  N     B ALA B 2 271 ? 26.429  -29.610 17.481  0.80 42.03  ? 271 ALA B N     1 
ATOM   10977 C  CA    A ALA B 2 271 ? 26.969  -30.676 18.197  0.20 44.06  ? 271 ALA B CA    1 
ATOM   10978 C  CA    B ALA B 2 271 ? 27.036  -30.581 18.373  0.80 44.05  ? 271 ALA B CA    1 
ATOM   10979 C  C     A ALA B 2 271 ? 26.055  -31.872 18.416  0.20 47.95  ? 271 ALA B C     1 
ATOM   10980 C  C     B ALA B 2 271 ? 26.073  -31.752 18.497  0.80 48.60  ? 271 ALA B C     1 
ATOM   10981 O  O     A ALA B 2 271 ? 24.832  -31.695 18.513  0.20 45.74  ? 271 ALA B O     1 
ATOM   10982 O  O     B ALA B 2 271 ? 24.854  -31.533 18.559  0.80 46.16  ? 271 ALA B O     1 
ATOM   10983 C  CB    A ALA B 2 271 ? 27.258  -29.985 19.533  0.20 44.09  ? 271 ALA B CB    1 
ATOM   10984 C  CB    B ALA B 2 271 ? 27.339  -29.994 19.755  0.80 43.56  ? 271 ALA B CB    1 
ATOM   10985 N  N     A PRO B 2 272 ? 26.605  -33.090 18.493  0.20 47.07  ? 272 PRO B N     1 
ATOM   10986 N  N     B PRO B 2 272 ? 26.570  -32.996 18.515  0.80 47.08  ? 272 PRO B N     1 
ATOM   10987 C  CA    A PRO B 2 272 ? 28.023  -33.444 18.365  0.20 46.97  ? 272 PRO B CA    1 
ATOM   10988 C  CA    B PRO B 2 272 ? 27.973  -33.403 18.406  0.80 46.96  ? 272 PRO B CA    1 
ATOM   10989 C  C     A PRO B 2 272 ? 28.444  -33.619 16.912  0.20 47.15  ? 272 PRO B C     1 
ATOM   10990 C  C     B PRO B 2 272 ? 28.423  -33.456 16.962  0.80 46.87  ? 272 PRO B C     1 
ATOM   10991 O  O     A PRO B 2 272 ? 27.607  -33.818 16.035  0.20 46.70  ? 272 PRO B O     1 
ATOM   10992 O  O     B PRO B 2 272 ? 27.611  -33.640 16.059  0.80 46.53  ? 272 PRO B O     1 
ATOM   10993 C  CB    A PRO B 2 272 ? 28.108  -34.759 19.145  0.20 50.10  ? 272 PRO B CB    1 
ATOM   10994 C  CB    B PRO B 2 272 ? 27.966  -34.800 19.032  0.80 50.29  ? 272 PRO B CB    1 
ATOM   10995 C  CG    A PRO B 2 272 ? 26.781  -35.408 18.870  0.20 49.24  ? 272 PRO B CG    1 
ATOM   10996 C  CG    B PRO B 2 272 ? 26.635  -35.349 18.606  0.80 49.03  ? 272 PRO B CG    1 
ATOM   10997 C  CD    A PRO B 2 272 ? 25.783  -34.268 18.830  0.20 47.53  ? 272 PRO B CD    1 
ATOM   10998 C  CD    B PRO B 2 272 ? 25.687  -34.165 18.698  0.80 47.59  ? 272 PRO B CD    1 
ATOM   10999 N  N     A LEU B 2 273 ? 29.743  -33.552 16.633  0.20 48.09  ? 273 LEU B N     1 
ATOM   11000 N  N     B LEU B 2 273 ? 29.720  -33.302 16.716  0.80 47.74  ? 273 LEU B N     1 
ATOM   11001 C  CA    A LEU B 2 273 ? 30.261  -33.760 15.288  0.20 49.77  ? 273 LEU B CA    1 
ATOM   11002 C  CA    B LEU B 2 273 ? 30.266  -33.539 15.391  0.80 49.37  ? 273 LEU B CA    1 
ATOM   11003 C  C     A LEU B 2 273 ? 30.490  -35.248 15.055  0.20 54.06  ? 273 LEU B C     1 
ATOM   11004 C  C     B LEU B 2 273 ? 30.395  -35.037 15.154  0.80 54.40  ? 273 LEU B C     1 
ATOM   11005 O  O     A LEU B 2 273 ? 31.183  -35.906 15.838  0.20 56.23  ? 273 LEU B O     1 
ATOM   11006 O  O     B LEU B 2 273 ? 30.849  -35.780 16.028  0.80 57.49  ? 273 LEU B O     1 
ATOM   11007 C  CB    A LEU B 2 273 ? 31.561  -32.982 15.086  0.20 45.09  ? 273 LEU B CB    1 
ATOM   11008 C  CB    B LEU B 2 273 ? 31.624  -32.858 15.245  0.80 44.35  ? 273 LEU B CB    1 
ATOM   11009 C  CG    A LEU B 2 273 ? 31.450  -31.462 15.212  0.20 46.51  ? 273 LEU B CG    1 
ATOM   11010 C  CG    B LEU B 2 273 ? 31.578  -31.330 15.298  0.80 46.72  ? 273 LEU B CG    1 
ATOM   11011 C  CD1   A LEU B 2 273 ? 32.825  -30.817 15.147  0.20 44.30  ? 273 LEU B CD1   1 
ATOM   11012 C  CD1   B LEU B 2 273 ? 32.986  -30.764 15.235  0.80 44.56  ? 273 LEU B CD1   1 
ATOM   11013 C  CD2   A LEU B 2 273 ? 30.538  -30.900 14.131  0.20 44.55  ? 273 LEU B CD2   1 
ATOM   11014 C  CD2   B LEU B 2 273 ? 30.717  -30.776 14.169  0.80 44.59  ? 273 LEU B CD2   1 
ATOM   11015 N  N     A THR B 2 274 ? 29.911  -35.772 13.976  0.20 55.94  ? 274 THR B N     1 
ATOM   11016 N  N     B THR B 2 274 ? 29.988  -35.477 13.965  0.80 56.40  ? 274 THR B N     1 
ATOM   11017 C  CA    A THR B 2 274 ? 29.976  -37.194 13.675  0.20 58.41  ? 274 THR B CA    1 
ATOM   11018 C  CA    B THR B 2 274 ? 29.920  -36.895 13.647  0.80 59.01  ? 274 THR B CA    1 
ATOM   11019 C  C     A THR B 2 274 ? 30.152  -37.396 12.177  0.20 60.08  ? 274 THR B C     1 
ATOM   11020 C  C     B THR B 2 274 ? 30.299  -37.122 12.190  0.80 60.94  ? 274 THR B C     1 
ATOM   11021 O  O     A THR B 2 274 ? 29.475  -36.751 11.372  0.20 56.55  ? 274 THR B O     1 
ATOM   11022 O  O     B THR B 2 274 ? 30.156  -36.231 11.347  0.80 57.25  ? 274 THR B O     1 
ATOM   11023 C  CB    A THR B 2 274 ? 28.711  -37.924 14.152  0.20 57.83  ? 274 THR B CB    1 
ATOM   11024 C  CB    B THR B 2 274 ? 28.513  -37.459 13.918  0.80 55.59  ? 274 THR B CB    1 
ATOM   11025 O  OG1   A THR B 2 274 ? 28.494  -37.652 15.542  0.20 52.20  ? 274 THR B OG1   1 
ATOM   11026 O  OG1   B THR B 2 274 ? 28.473  -38.845 13.556  0.80 68.85  ? 274 THR B OG1   1 
ATOM   11027 C  CG2   A THR B 2 274 ? 28.851  -39.427 13.953  0.20 63.49  ? 274 THR B CG2   1 
ATOM   11028 C  CG2   B THR B 2 274 ? 27.466  -36.697 13.114  0.80 55.88  ? 274 THR B CG2   1 
ATOM   11029 N  N     A SER B 2 275 ? 31.064  -38.295 11.813  0.20 59.27  ? 275 SER B N     1 
ATOM   11030 N  N     B SER B 2 275 ? 30.784  -38.330 11.903  0.80 59.76  ? 275 SER B N     1 
ATOM   11031 C  CA    A SER B 2 275 ? 31.277  -38.641 10.417  0.20 59.91  ? 275 SER B CA    1 
ATOM   11032 C  CA    B SER B 2 275 ? 31.128  -38.730 10.550  0.80 60.07  ? 275 SER B CA    1 
ATOM   11033 C  C     A SER B 2 275 ? 30.200  -39.607 9.938   0.20 62.90  ? 275 SER B C     1 
ATOM   11034 C  C     B SER B 2 275 ? 29.933  -39.426 9.895   0.80 63.18  ? 275 SER B C     1 
ATOM   11035 O  O     A SER B 2 275 ? 29.631  -40.374 10.720  0.20 63.93  ? 275 SER B O     1 
ATOM   11036 O  O     B SER B 2 275 ? 28.874  -39.601 10.501  0.80 66.17  ? 275 SER B O     1 
ATOM   11037 C  CB    A SER B 2 275 ? 32.657  -39.270 10.225  0.20 58.47  ? 275 SER B CB    1 
ATOM   11038 C  CB    B SER B 2 275 ? 32.362  -39.629 10.562  0.80 57.43  ? 275 SER B CB    1 
ATOM   11039 O  OG    A SER B 2 275 ? 33.674  -38.448 10.768  0.20 56.37  ? 275 SER B OG    1 
ATOM   11040 O  OG    B SER B 2 275 ? 32.744  -39.990 9.245   0.80 69.83  ? 275 SER B OG    1 
ATOM   11041 N  N     A ARG B 2 276 ? 29.925  -39.566 8.637   0.20 63.35  ? 276 ARG B N     1 
ATOM   11042 N  N     B ARG B 2 276 ? 30.100  -39.833 8.639   0.80 63.62  ? 276 ARG B N     1 
ATOM   11043 C  CA    A ARG B 2 276 ? 28.932  -40.462 8.064   0.20 64.29  ? 276 ARG B CA    1 
ATOM   11044 C  CA    B ARG B 2 276 ? 29.009  -40.449 7.893   0.80 64.04  ? 276 ARG B CA    1 
ATOM   11045 C  C     A ARG B 2 276 ? 29.442  -41.900 8.076   0.20 71.16  ? 276 ARG B C     1 
ATOM   11046 C  C     B ARG B 2 276 ? 28.864  -41.942 8.166   0.80 74.58  ? 276 ARG B C     1 
ATOM   11047 O  O     A ARG B 2 276 ? 30.640  -42.162 7.935   0.20 66.54  ? 276 ARG B O     1 
ATOM   11048 O  O     B ARG B 2 276 ? 28.013  -42.586 7.543   0.80 84.05  ? 276 ARG B O     1 
ATOM   11049 C  CB    A ARG B 2 276 ? 28.577  -40.037 6.636   0.20 60.94  ? 276 ARG B CB    1 
ATOM   11050 C  CB    B ARG B 2 276 ? 29.189  -40.205 6.389   0.80 58.55  ? 276 ARG B CB    1 
ATOM   11051 C  CG    A ARG B 2 276 ? 29.731  -40.091 5.644   0.20 59.60  ? 276 ARG B CG    1 
ATOM   11052 C  CG    B ARG B 2 276 ? 30.637  -40.178 5.916   0.80 62.23  ? 276 ARG B CG    1 
ATOM   11053 C  CD    A ARG B 2 276 ? 29.260  -39.796 4.222   0.20 50.64  ? 276 ARG B CD    1 
ATOM   11054 C  CD    B ARG B 2 276 ? 31.153  -41.565 5.552   0.80 69.81  ? 276 ARG B CD    1 
ATOM   11055 N  NE    A ARG B 2 276 ? 30.343  -39.915 3.252   0.20 50.17  ? 276 ARG B NE    1 
ATOM   11056 N  NE    B ARG B 2 276 ? 32.585  -41.556 5.267   0.80 75.13  ? 276 ARG B NE    1 
ATOM   11057 C  CZ    A ARG B 2 276 ? 30.196  -39.796 1.939   0.20 45.70  ? 276 ARG B CZ    1 
ATOM   11058 C  CZ    B ARG B 2 276 ? 33.118  -41.233 4.096   0.80 62.16  ? 276 ARG B CZ    1 
ATOM   11059 N  NH1   A ARG B 2 276 ? 29.014  -39.555 1.394   0.20 30.36  ? 276 ARG B NH1   1 
ATOM   11060 N  NH1   B ARG B 2 276 ? 32.365  -40.879 3.067   0.80 65.32  ? 276 ARG B NH1   1 
ATOM   11061 N  NH2   A ARG B 2 276 ? 31.260  -39.924 1.151   0.20 47.52  ? 276 ARG B NH2   1 
ATOM   11062 N  NH2   B ARG B 2 276 ? 34.441  -41.255 3.956   0.80 60.02  ? 276 ARG B NH2   1 
ATOM   11063 N  N     A GLY B 2 277 ? 28.514  -42.836 8.263   0.20 75.12  ? 277 GLY B N     1 
ATOM   11064 N  N     B GLY B 2 277 ? 29.654  -42.501 9.082   0.80 71.20  ? 277 GLY B N     1 
ATOM   11065 C  CA    A GLY B 2 277 ? 28.854  -44.245 8.291   0.20 74.60  ? 277 GLY B CA    1 
ATOM   11066 C  CA    B GLY B 2 277 ? 29.580  -43.922 9.367   0.80 75.49  ? 277 GLY B CA    1 
ATOM   11067 C  C     A GLY B 2 277 ? 29.034  -44.797 9.690   0.20 72.52  ? 277 GLY B C     1 
ATOM   11068 C  C     B GLY B 2 277 ? 29.644  -44.270 10.841  0.80 72.91  ? 277 GLY B C     1 
ATOM   11069 O  O     A GLY B 2 277 ? 28.639  -45.933 9.972   0.20 67.09  ? 277 GLY B O     1 
ATOM   11070 O  O     B GLY B 2 277 ? 29.090  -45.287 11.271  0.80 76.15  ? 277 GLY B O     1 
ATOM   11071 N  N     A SER B 2 278 ? 29.629  -44.003 10.575  0.20 72.65  ? 278 SER B N     1 
ATOM   11072 N  N     B SER B 2 278 ? 30.318  -43.433 11.624  0.80 71.60  ? 278 SER B N     1 
ATOM   11073 C  CA    A SER B 2 278 ? 29.872  -44.428 11.949  0.20 71.99  ? 278 SER B CA    1 
ATOM   11074 C  CA    B SER B 2 278 ? 30.484  -43.672 13.054  0.80 70.87  ? 278 SER B CA    1 
ATOM   11075 C  C     A SER B 2 278 ? 28.658  -44.157 12.835  0.20 70.41  ? 278 SER B C     1 
ATOM   11076 C  C     B SER B 2 278 ? 29.215  -43.329 13.833  0.80 67.29  ? 278 SER B C     1 
ATOM   11077 O  O     A SER B 2 278 ? 28.784  -44.016 14.052  0.20 65.51  ? 278 SER B O     1 
ATOM   11078 O  O     B SER B 2 278 ? 28.547  -42.337 13.544  0.80 61.01  ? 278 SER B O     1 
ATOM   11079 C  CB    A SER B 2 278 ? 31.105  -43.722 12.517  0.20 70.28  ? 278 SER B CB    1 
ATOM   11080 C  CB    B SER B 2 278 ? 31.665  -42.861 13.592  0.80 76.95  ? 278 SER B CB    1 
ATOM   11081 O  OG    A SER B 2 278 ? 32.255  -43.992 11.735  0.20 69.33  ? 278 SER B OG    1 
ATOM   11082 O  OG    B SER B 2 278 ? 32.862  -43.181 12.902  0.80 72.88  ? 278 SER B OG    1 
ATOM   11083 N  N     A LEU B 2 284 ? 25.956  -38.129 25.249  0.20 61.68  ? 284 LEU B N     1 
ATOM   11084 N  N     B LEU B 2 284 ? 25.661  -38.163 25.162  0.80 61.18  ? 284 LEU B N     1 
ATOM   11085 C  CA    A LEU B 2 284 ? 26.350  -36.748 25.510  0.20 64.57  ? 284 LEU B CA    1 
ATOM   11086 C  CA    B LEU B 2 284 ? 26.148  -36.833 25.514  0.80 65.05  ? 284 LEU B CA    1 
ATOM   11087 C  C     A LEU B 2 284 ? 25.386  -36.072 26.479  0.20 61.39  ? 284 LEU B C     1 
ATOM   11088 C  C     B LEU B 2 284 ? 25.275  -36.177 26.575  0.80 61.49  ? 284 LEU B C     1 
ATOM   11089 O  O     A LEU B 2 284 ? 24.179  -36.035 26.245  0.20 61.43  ? 284 LEU B O     1 
ATOM   11090 O  O     B LEU B 2 284 ? 24.056  -36.338 26.576  0.80 63.36  ? 284 LEU B O     1 
ATOM   11091 C  CB    A LEU B 2 284 ? 26.427  -35.950 24.204  0.20 63.97  ? 284 LEU B CB    1 
ATOM   11092 C  CB    B LEU B 2 284 ? 26.223  -35.929 24.278  0.80 64.23  ? 284 LEU B CB    1 
ATOM   11093 C  CG    A LEU B 2 284 ? 27.732  -36.019 23.403  0.20 63.37  ? 284 LEU B CG    1 
ATOM   11094 C  CG    B LEU B 2 284 ? 27.354  -36.204 23.285  0.80 64.93  ? 284 LEU B CG    1 
ATOM   11095 C  CD1   A LEU B 2 284 ? 28.920  -35.648 24.280  0.20 60.89  ? 284 LEU B CD1   1 
ATOM   11096 C  CD1   B LEU B 2 284 ? 26.895  -37.185 22.218  0.80 72.81  ? 284 LEU B CD1   1 
ATOM   11097 C  CD2   A LEU B 2 284 ? 27.935  -37.388 22.766  0.20 66.56  ? 284 LEU B CD2   1 
ATOM   11098 C  CD2   B LEU B 2 284 ? 27.879  -34.913 22.658  0.80 58.18  ? 284 LEU B CD2   1 
ATOM   11099 N  N     A THR B 2 285 ? 25.929  -35.536 27.568  0.20 57.48  ? 285 THR B N     1 
ATOM   11100 N  N     B THR B 2 285 ? 25.905  -35.430 27.472  0.80 56.93  ? 285 THR B N     1 
ATOM   11101 C  CA    A THR B 2 285 ? 25.118  -34.868 28.571  0.20 60.37  ? 285 THR B CA    1 
ATOM   11102 C  CA    B THR B 2 285 ? 25.208  -34.741 28.545  0.80 60.57  ? 285 THR B CA    1 
ATOM   11103 C  C     A THR B 2 285 ? 24.785  -33.444 28.130  0.20 60.28  ? 285 THR B C     1 
ATOM   11104 C  C     B THR B 2 285 ? 24.950  -33.291 28.158  0.80 60.99  ? 285 THR B C     1 
ATOM   11105 O  O     A THR B 2 285 ? 25.323  -32.921 27.150  0.20 59.21  ? 285 THR B O     1 
ATOM   11106 O  O     B THR B 2 285 ? 25.666  -32.714 27.339  0.80 60.81  ? 285 THR B O     1 
ATOM   11107 C  CB    A THR B 2 285 ? 25.835  -34.855 29.920  0.20 59.16  ? 285 THR B CB    1 
ATOM   11108 C  CB    B THR B 2 285 ? 26.019  -34.806 29.839  0.80 59.15  ? 285 THR B CB    1 
ATOM   11109 O  OG1   A THR B 2 285 ? 27.112  -34.220 29.779  0.20 60.34  ? 285 THR B OG1   1 
ATOM   11110 O  OG1   B THR B 2 285 ? 27.194  -33.999 29.705  0.80 61.12  ? 285 THR B OG1   1 
ATOM   11111 C  CG2   A THR B 2 285 ? 26.035  -36.274 30.429  0.20 60.02  ? 285 THR B CG2   1 
ATOM   11112 C  CG2   B THR B 2 285 ? 26.436  -36.235 30.121  0.80 59.65  ? 285 THR B CG2   1 
ATOM   11113 N  N     A VAL B 2 286 ? 23.881  -32.813 28.874  0.20 59.41  ? 286 VAL B N     1 
ATOM   11114 N  N     B VAL B 2 286 ? 23.914  -32.710 28.755  0.80 59.75  ? 286 VAL B N     1 
ATOM   11115 C  CA    A VAL B 2 286 ? 23.436  -31.451 28.579  0.20 58.70  ? 286 VAL B CA    1 
ATOM   11116 C  CA    B VAL B 2 286 ? 23.522  -31.326 28.477  0.80 59.07  ? 286 VAL B CA    1 
ATOM   11117 C  C     A VAL B 2 286 ? 24.579  -30.452 28.757  0.20 56.65  ? 286 VAL B C     1 
ATOM   11118 C  C     B VAL B 2 286 ? 24.685  -30.368 28.734  0.80 56.77  ? 286 VAL B C     1 
ATOM   11119 O  O     A VAL B 2 286 ? 24.771  -29.601 27.876  0.20 54.85  ? 286 VAL B O     1 
ATOM   11120 O  O     B VAL B 2 286 ? 24.920  -29.471 27.905  0.80 54.66  ? 286 VAL B O     1 
ATOM   11121 C  CB    A VAL B 2 286 ? 22.219  -31.065 29.438  0.20 57.05  ? 286 VAL B CB    1 
ATOM   11122 C  CB    B VAL B 2 286 ? 22.274  -30.917 29.285  0.80 56.69  ? 286 VAL B CB    1 
ATOM   11123 C  CG1   A VAL B 2 286 ? 21.753  -29.656 29.098  0.20 53.21  ? 286 VAL B CG1   1 
ATOM   11124 C  CG1   B VAL B 2 286 ? 21.949  -29.446 29.069  0.80 52.07  ? 286 VAL B CG1   1 
ATOM   11125 C  CG2   A VAL B 2 286 ? 21.091  -32.068 29.244  0.20 57.72  ? 286 VAL B CG2   1 
ATOM   11126 C  CG2   B VAL B 2 286 ? 21.082  -31.788 28.906  0.80 57.41  ? 286 VAL B CG2   1 
ATOM   11127 N  N     A PRO B 2 287 ? 25.355  -30.489 29.851  0.20 58.17  ? 287 PRO B N     1 
ATOM   11128 N  N     B PRO B 2 287 ? 25.439  -30.493 29.838  0.80 58.31  ? 287 PRO B N     1 
ATOM   11129 C  CA    A PRO B 2 287 ? 26.482  -29.543 29.953  0.20 55.56  ? 287 PRO B CA    1 
ATOM   11130 C  CA    B PRO B 2 287 ? 26.621  -29.623 29.992  0.80 55.34  ? 287 PRO B CA    1 
ATOM   11131 C  C     A PRO B 2 287 ? 27.515  -29.707 28.851  0.20 57.88  ? 287 PRO B C     1 
ATOM   11132 C  C     B PRO B 2 287 ? 27.667  -29.806 28.902  0.80 58.52  ? 287 PRO B C     1 
ATOM   11133 O  O     A PRO B 2 287 ? 28.193  -28.733 28.501  0.20 56.98  ? 287 PRO B O     1 
ATOM   11134 O  O     B PRO B 2 287 ? 28.421  -28.866 28.623  0.80 57.57  ? 287 PRO B O     1 
ATOM   11135 C  CB    A PRO B 2 287 ? 27.076  -29.851 31.335  0.20 57.62  ? 287 PRO B CB    1 
ATOM   11136 C  CB    B PRO B 2 287 ? 27.165  -30.019 31.370  0.80 57.80  ? 287 PRO B CB    1 
ATOM   11137 C  CG    A PRO B 2 287 ? 25.956  -30.443 32.099  0.20 56.88  ? 287 PRO B CG    1 
ATOM   11138 C  CG    B PRO B 2 287 ? 25.978  -30.527 32.099  0.80 56.83  ? 287 PRO B CG    1 
ATOM   11139 C  CD    A PRO B 2 287 ? 25.196  -31.257 31.101  0.20 55.38  ? 287 PRO B CD    1 
ATOM   11140 C  CD    B PRO B 2 287 ? 25.176  -31.262 31.074  0.80 55.19  ? 287 PRO B CD    1 
ATOM   11141 N  N     A GLU B 2 288 ? 27.658  -30.910 28.293  0.20 55.49  ? 288 GLU B N     1 
ATOM   11142 N  N     B GLU B 2 288 ? 27.743  -30.982 28.276  0.80 55.39  ? 288 GLU B N     1 
ATOM   11143 C  CA    A GLU B 2 288 ? 28.579  -31.104 27.179  0.20 54.75  ? 288 GLU B CA    1 
ATOM   11144 C  CA    B GLU B 2 288 ? 28.702  -31.160 27.191  0.80 54.52  ? 288 GLU B CA    1 
ATOM   11145 C  C     A GLU B 2 288 ? 28.023  -30.545 25.877  0.20 55.48  ? 288 GLU B C     1 
ATOM   11146 C  C     B GLU B 2 288 ? 28.229  -30.457 25.929  0.80 55.91  ? 288 GLU B C     1 
ATOM   11147 O  O     A GLU B 2 288 ? 28.788  -30.032 25.053  0.20 53.94  ? 288 GLU B O     1 
ATOM   11148 O  O     B GLU B 2 288 ? 29.041  -29.916 25.172  0.80 53.29  ? 288 GLU B O     1 
ATOM   11149 C  CB    A GLU B 2 288 ? 28.907  -32.589 27.019  0.20 55.84  ? 288 GLU B CB    1 
ATOM   11150 C  CB    B GLU B 2 288 ? 28.929  -32.645 26.920  0.80 55.69  ? 288 GLU B CB    1 
ATOM   11151 C  CG    A GLU B 2 288 ? 29.779  -33.155 28.131  0.20 57.43  ? 288 GLU B CG    1 
ATOM   11152 C  CG    B GLU B 2 288 ? 30.375  -33.100 27.081  0.80 56.90  ? 288 GLU B CG    1 
ATOM   11153 C  CD    A GLU B 2 288 ? 29.924  -34.662 28.049  0.20 59.51  ? 288 GLU B CD    1 
ATOM   11154 C  CD    B GLU B 2 288 ? 30.523  -34.608 26.959  0.80 63.97  ? 288 GLU B CD    1 
ATOM   11155 O  OE1   A GLU B 2 288 ? 28.913  -35.346 27.782  0.20 58.69  ? 288 GLU B OE1   1 
ATOM   11156 O  OE1   B GLU B 2 288 ? 29.491  -35.312 27.026  0.80 63.43  ? 288 GLU B OE1   1 
ATOM   11157 O  OE2   A GLU B 2 288 ? 31.052  -35.162 28.246  0.20 63.03  ? 288 GLU B OE2   1 
ATOM   11158 O  OE2   B GLU B 2 288 ? 31.667  -35.089 26.796  0.80 64.17  ? 288 GLU B OE2   1 
ATOM   11159 N  N     A LEU B 2 289 ? 26.705  -30.629 25.676  0.20 56.18  ? 289 LEU B N     1 
ATOM   11160 N  N     B LEU B 2 289 ? 26.916  -30.457 25.692  0.80 57.13  ? 289 LEU B N     1 
ATOM   11161 C  CA    A LEU B 2 289 ? 26.106  -30.079 24.464  0.20 52.74  ? 289 LEU B CA    1 
ATOM   11162 C  CA    B LEU B 2 289 ? 26.356  -29.782 24.527  0.80 53.14  ? 289 LEU B CA    1 
ATOM   11163 C  C     A LEU B 2 289 ? 26.201  -28.560 24.437  0.20 51.27  ? 289 LEU B C     1 
ATOM   11164 C  C     B LEU B 2 289 ? 26.561  -28.276 24.616  0.80 51.51  ? 289 LEU B C     1 
ATOM   11165 O  O     A LEU B 2 289 ? 26.515  -27.971 23.397  0.20 51.59  ? 289 LEU B O     1 
ATOM   11166 O  O     B LEU B 2 289 ? 27.178  -27.668 23.735  0.80 53.16  ? 289 LEU B O     1 
ATOM   11167 C  CB    A LEU B 2 289 ? 24.650  -30.524 24.347  0.20 50.01  ? 289 LEU B CB    1 
ATOM   11168 C  CB    B LEU B 2 289 ? 24.870  -30.121 24.397  0.80 49.99  ? 289 LEU B CB    1 
ATOM   11169 C  CG    A LEU B 2 289 ? 24.407  -31.995 24.012  0.20 51.28  ? 289 LEU B CG    1 
ATOM   11170 C  CG    B LEU B 2 289 ? 24.518  -31.463 23.759  0.80 50.24  ? 289 LEU B CG    1 
ATOM   11171 C  CD1   A LEU B 2 289 ? 22.916  -32.283 23.935  0.20 48.94  ? 289 LEU B CD1   1 
ATOM   11172 C  CD1   B LEU B 2 289 ? 23.027  -31.749 23.896  0.80 48.07  ? 289 LEU B CD1   1 
ATOM   11173 C  CD2   A LEU B 2 289 ? 25.095  -32.358 22.708  0.20 48.98  ? 289 LEU B CD2   1 
ATOM   11174 C  CD2   B LEU B 2 289 ? 24.931  -31.453 22.302  0.80 45.07  ? 289 LEU B CD2   1 
ATOM   11175 N  N     A THR B 2 290 ? 25.926  -27.907 25.569  0.20 49.20  ? 290 THR B N     1 
ATOM   11176 N  N     B THR B 2 290 ? 26.066  -27.659 25.692  0.80 47.67  ? 290 THR B N     1 
ATOM   11177 C  CA    A THR B 2 290 ? 26.043  -26.454 25.626  0.20 51.59  ? 290 THR B CA    1 
ATOM   11178 C  CA    B THR B 2 290 ? 26.144  -26.207 25.834  0.80 52.20  ? 290 THR B CA    1 
ATOM   11179 C  C     A THR B 2 290 ? 27.493  -26.006 25.498  0.20 53.46  ? 290 THR B C     1 
ATOM   11180 C  C     B THR B 2 290 ? 27.579  -25.693 25.817  0.80 54.22  ? 290 THR B C     1 
ATOM   11181 O  O     A THR B 2 290 ? 27.760  -24.910 24.992  0.20 52.88  ? 290 THR B O     1 
ATOM   11182 O  O     B THR B 2 290 ? 27.793  -24.505 25.550  0.80 55.99  ? 290 THR B O     1 
ATOM   11183 C  CB    A THR B 2 290 ? 25.438  -25.922 26.928  0.20 49.21  ? 290 THR B CB    1 
ATOM   11184 C  CB    B THR B 2 290 ? 25.446  -25.755 27.127  0.80 47.99  ? 290 THR B CB    1 
ATOM   11185 O  OG1   A THR B 2 290 ? 26.200  -26.401 28.043  0.20 53.52  ? 290 THR B OG1   1 
ATOM   11186 O  OG1   B THR B 2 290 ? 26.257  -26.095 28.262  0.80 53.83  ? 290 THR B OG1   1 
ATOM   11187 C  CG2   A THR B 2 290 ? 23.993  -26.383 27.075  0.20 44.81  ? 290 THR B CG2   1 
ATOM   11188 C  CG2   B THR B 2 290 ? 24.090  -26.435 27.269  0.80 43.16  ? 290 THR B CG2   1 
ATOM   11189 N  N     A GLN B 2 291 ? 28.436  -26.838 25.944  0.20 54.06  ? 291 GLN B N     1 
ATOM   11190 N  N     B GLN B 2 291 ? 28.560  -26.555 26.095  0.80 53.99  ? 291 GLN B N     1 
ATOM   11191 C  CA    A GLN B 2 291 ? 29.853  -26.508 25.832  0.20 56.58  ? 291 GLN B CA    1 
ATOM   11192 C  CA    B GLN B 2 291 ? 29.971  -26.195 25.991  0.80 57.73  ? 291 GLN B CA    1 
ATOM   11193 C  C     A GLN B 2 291 ? 30.352  -26.644 24.399  0.20 54.28  ? 291 GLN B C     1 
ATOM   11194 C  C     B GLN B 2 291 ? 30.494  -26.315 24.564  0.80 55.26  ? 291 GLN B C     1 
ATOM   11195 O  O     A GLN B 2 291 ? 31.130  -25.806 23.928  0.20 53.02  ? 291 GLN B O     1 
ATOM   11196 O  O     B GLN B 2 291 ? 31.198  -25.419 24.085  0.80 53.28  ? 291 GLN B O     1 
ATOM   11197 C  CB    A GLN B 2 291 ? 30.670  -27.403 26.767  0.20 58.41  ? 291 GLN B CB    1 
ATOM   11198 C  CB    B GLN B 2 291 ? 30.812  -27.069 26.929  0.80 58.46  ? 291 GLN B CB    1 
ATOM   11199 C  CG    A GLN B 2 291 ? 32.176  -27.230 26.646  0.20 64.34  ? 291 GLN B CG    1 
ATOM   11200 C  CG    B GLN B 2 291 ? 32.294  -26.715 26.956  0.80 68.98  ? 291 GLN B CG    1 
ATOM   11201 C  CD    A GLN B 2 291 ? 32.945  -28.180 27.546  0.20 67.45  ? 291 GLN B CD    1 
ATOM   11202 C  CD    B GLN B 2 291 ? 33.064  -27.478 28.024  0.80 73.67  ? 291 GLN B CD    1 
ATOM   11203 O  OE1   A GLN B 2 291 ? 32.354  -28.973 28.280  0.20 66.60  ? 291 GLN B OE1   1 
ATOM   11204 O  OE1   B GLN B 2 291 ? 32.472  -28.087 28.918  0.80 71.92  ? 291 GLN B OE1   1 
ATOM   11205 N  NE2   A GLN B 2 291 ? 34.270  -28.103 27.494  0.20 67.42  ? 291 GLN B NE2   1 
ATOM   11206 N  NE2   B GLN B 2 291 ? 34.391  -27.445 27.936  0.80 65.17  ? 291 GLN B NE2   1 
ATOM   11207 N  N     A GLN B 2 292 ? 29.915  -27.685 23.689  0.20 52.53  ? 292 GLN B N     1 
ATOM   11208 N  N     B GLN B 2 292 ? 30.159  -27.408 23.874  0.80 51.57  ? 292 GLN B N     1 
ATOM   11209 C  CA    A GLN B 2 292 ? 30.399  -27.931 22.337  0.20 52.43  ? 292 GLN B CA    1 
ATOM   11210 C  CA    B GLN B 2 292 ? 30.592  -27.574 22.490  0.80 53.53  ? 292 GLN B CA    1 
ATOM   11211 C  C     A GLN B 2 292 ? 29.764  -27.015 21.302  0.20 50.98  ? 292 GLN B C     1 
ATOM   11212 C  C     B GLN B 2 292 ? 29.990  -26.498 21.598  0.80 53.57  ? 292 GLN B C     1 
ATOM   11213 O  O     A GLN B 2 292 ? 30.368  -26.786 20.250  0.20 47.35  ? 292 GLN B O     1 
ATOM   11214 O  O     B GLN B 2 292 ? 30.663  -25.979 20.698  0.80 44.68  ? 292 GLN B O     1 
ATOM   11215 C  CB    A GLN B 2 292 ? 30.162  -29.394 21.949  0.20 52.27  ? 292 GLN B CB    1 
ATOM   11216 C  CB    B GLN B 2 292 ? 30.209  -28.966 21.974  0.80 53.92  ? 292 GLN B CB    1 
ATOM   11217 C  CG    A GLN B 2 292 ? 30.976  -30.389 22.765  0.20 52.04  ? 292 GLN B CG    1 
ATOM   11218 C  CG    B GLN B 2 292 ? 30.930  -30.126 22.655  0.80 52.18  ? 292 GLN B CG    1 
ATOM   11219 C  CD    A GLN B 2 292 ? 30.814  -31.820 22.283  0.20 51.92  ? 292 GLN B CD    1 
ATOM   11220 C  CD    B GLN B 2 292 ? 30.752  -31.447 21.914  0.80 51.71  ? 292 GLN B CD    1 
ATOM   11221 O  OE1   A GLN B 2 292 ? 31.197  -32.765 22.974  0.20 52.33  ? 292 GLN B OE1   1 
ATOM   11222 O  OE1   B GLN B 2 292 ? 30.338  -31.471 20.754  0.80 52.42  ? 292 GLN B OE1   1 
ATOM   11223 N  NE2   A GLN B 2 292 ? 30.250  -31.986 21.092  0.20 49.97  ? 292 GLN B NE2   1 
ATOM   11224 N  NE2   B GLN B 2 292 ? 31.069  -32.552 22.583  0.80 52.19  ? 292 GLN B NE2   1 
ATOM   11225 N  N     A MET B 2 293 ? 28.568  -26.486 21.569  0.20 50.96  ? 293 MET B N     1 
ATOM   11226 N  N     B MET B 2 293 ? 28.727  -26.140 21.849  0.80 52.54  ? 293 MET B N     1 
ATOM   11227 C  CA    A MET B 2 293 ? 27.934  -25.579 20.615  0.20 50.72  ? 293 MET B CA    1 
ATOM   11228 C  CA    B MET B 2 293 ? 28.017  -25.181 21.008  0.80 51.74  ? 293 MET B CA    1 
ATOM   11229 C  C     A MET B 2 293 ? 28.763  -24.316 20.420  0.20 49.16  ? 293 MET B C     1 
ATOM   11230 C  C     B MET B 2 293 ? 28.700  -23.824 20.969  0.80 49.96  ? 293 MET B C     1 
ATOM   11231 O  O     A MET B 2 293 ? 29.089  -23.941 19.288  0.20 50.44  ? 293 MET B O     1 
ATOM   11232 O  O     B MET B 2 293 ? 28.509  -23.065 20.013  0.80 51.55  ? 293 MET B O     1 
ATOM   11233 C  CB    A MET B 2 293 ? 26.522  -25.222 21.079  0.20 48.81  ? 293 MET B CB    1 
ATOM   11234 C  CB    B MET B 2 293 ? 26.584  -25.006 21.508  0.80 48.14  ? 293 MET B CB    1 
ATOM   11235 C  CG    A MET B 2 293 ? 25.446  -26.177 20.605  0.20 45.74  ? 293 MET B CG    1 
ATOM   11236 C  CG    B MET B 2 293 ? 25.556  -25.827 20.782  0.80 45.88  ? 293 MET B CG    1 
ATOM   11237 S  SD    A MET B 2 293 ? 23.803  -25.456 20.782  0.20 53.93  ? 293 MET B SD    1 
ATOM   11238 S  SD    B MET B 2 293 ? 23.935  -25.083 21.038  0.80 59.07  ? 293 MET B SD    1 
ATOM   11239 C  CE    A MET B 2 293 ? 23.770  -25.115 22.539  0.20 50.71  ? 293 MET B CE    1 
ATOM   11240 C  CE    B MET B 2 293 ? 23.927  -24.870 22.815  0.80 51.84  ? 293 MET B CE    1 
ATOM   11241 N  N     A PHE B 2 294 ? 29.113  -23.645 21.517  0.20 49.52  ? 294 PHE B N     1 
ATOM   11242 N  N     B PHE B 2 294 ? 29.460  -23.480 22.006  0.80 49.79  ? 294 PHE B N     1 
ATOM   11243 C  CA    A PHE B 2 294 ? 29.871  -22.401 21.460  0.20 50.03  ? 294 PHE B CA    1 
ATOM   11244 C  CA    B PHE B 2 294 ? 30.188  -22.219 22.050  0.80 52.48  ? 294 PHE B CA    1 
ATOM   11245 C  C     A PHE B 2 294 ? 31.347  -22.613 21.148  0.20 45.38  ? 294 PHE B C     1 
ATOM   11246 C  C     B PHE B 2 294 ? 31.686  -22.417 21.854  0.80 47.69  ? 294 PHE B C     1 
ATOM   11247 O  O     A PHE B 2 294 ? 32.075  -21.627 20.987  0.20 45.71  ? 294 PHE B O     1 
ATOM   11248 O  O     B PHE B 2 294 ? 32.485  -21.576 22.280  0.80 49.21  ? 294 PHE B O     1 
ATOM   11249 C  CB    A PHE B 2 294 ? 29.728  -21.642 22.782  0.20 47.29  ? 294 PHE B CB    1 
ATOM   11250 C  CB    B PHE B 2 294 ? 29.900  -21.493 23.361  0.80 47.19  ? 294 PHE B CB    1 
ATOM   11251 C  CG    A PHE B 2 294 ? 28.323  -21.194 23.075  0.20 45.58  ? 294 PHE B CG    1 
ATOM   11252 C  CG    B PHE B 2 294 ? 28.513  -20.910 23.435  0.80 44.27  ? 294 PHE B CG    1 
ATOM   11253 C  CD1   A PHE B 2 294 ? 27.868  -19.965 22.629  0.20 43.40  ? 294 PHE B CD1   1 
ATOM   11254 C  CD1   B PHE B 2 294 ? 27.427  -21.702 23.772  0.80 50.32  ? 294 PHE B CD1   1 
ATOM   11255 C  CD2   A PHE B 2 294 ? 27.459  -22.001 23.797  0.20 49.42  ? 294 PHE B CD2   1 
ATOM   11256 C  CD2   B PHE B 2 294 ? 28.299  -19.569 23.160  0.80 42.23  ? 294 PHE B CD2   1 
ATOM   11257 C  CE1   A PHE B 2 294 ? 26.577  -19.549 22.896  0.20 42.21  ? 294 PHE B CE1   1 
ATOM   11258 C  CE1   B PHE B 2 294 ? 26.151  -21.164 23.838  0.80 45.97  ? 294 PHE B CE1   1 
ATOM   11259 C  CE2   A PHE B 2 294 ? 26.166  -21.590 24.068  0.20 46.95  ? 294 PHE B CE2   1 
ATOM   11260 C  CE2   B PHE B 2 294 ? 27.030  -19.027 23.226  0.80 43.48  ? 294 PHE B CE2   1 
ATOM   11261 C  CZ    A PHE B 2 294 ? 25.726  -20.362 23.616  0.20 42.75  ? 294 PHE B CZ    1 
ATOM   11262 C  CZ    B PHE B 2 294 ? 25.956  -19.828 23.561  0.80 40.66  ? 294 PHE B CZ    1 
ATOM   11263 N  N     A ASP B 2 295 ? 31.803  -23.859 21.063  0.20 47.32  ? 295 ASP B N     1 
ATOM   11264 N  N     B ASP B 2 295 ? 32.078  -23.517 21.222  0.80 47.42  ? 295 ASP B N     1 
ATOM   11265 C  CA    A ASP B 2 295 ? 33.198  -24.130 20.744  0.20 42.54  ? 295 ASP B CA    1 
ATOM   11266 C  CA    B ASP B 2 295 ? 33.471  -23.811 20.920  0.80 38.84  ? 295 ASP B CA    1 
ATOM   11267 C  C     A ASP B 2 295 ? 33.474  -23.823 19.276  0.20 42.70  ? 295 ASP B C     1 
ATOM   11268 C  C     B ASP B 2 295 ? 33.741  -23.512 19.450  0.80 42.12  ? 295 ASP B C     1 
ATOM   11269 O  O     A ASP B 2 295 ? 32.664  -24.132 18.398  0.20 43.00  ? 295 ASP B O     1 
ATOM   11270 O  O     B ASP B 2 295 ? 32.942  -23.866 18.578  0.80 42.36  ? 295 ASP B O     1 
ATOM   11271 C  CB    A ASP B 2 295 ? 33.533  -25.590 21.056  0.20 44.64  ? 295 ASP B CB    1 
ATOM   11272 C  CB    B ASP B 2 295 ? 33.788  -25.275 21.237  0.80 42.97  ? 295 ASP B CB    1 
ATOM   11273 C  CG    A ASP B 2 295 ? 35.028  -25.847 21.151  0.20 47.62  ? 295 ASP B CG    1 
ATOM   11274 C  CG    B ASP B 2 295 ? 35.266  -25.594 21.145  0.80 48.21  ? 295 ASP B CG    1 
ATOM   11275 O  OD1   A ASP B 2 295 ? 35.802  -25.221 20.398  0.20 44.94  ? 295 ASP B OD1   1 
ATOM   11276 O  OD1   B ASP B 2 295 ? 35.874  -25.373 20.078  0.80 44.22  ? 295 ASP B OD1   1 
ATOM   11277 O  OD2   A ASP B 2 295 ? 35.428  -26.686 21.986  0.20 51.13  ? 295 ASP B OD2   1 
ATOM   11278 O  OD2   B ASP B 2 295 ? 35.821  -26.079 22.151  0.80 58.04  ? 295 ASP B OD2   1 
ATOM   11279 N  N     A SER B 2 296 ? 34.633  -23.214 19.014  0.20 43.81  ? 296 SER B N     1 
ATOM   11280 N  N     B SER B 2 296 ? 34.885  -22.872 19.183  0.80 45.89  ? 296 SER B N     1 
ATOM   11281 C  CA    A SER B 2 296 ? 35.014  -22.876 17.646  0.20 41.48  ? 296 SER B CA    1 
ATOM   11282 C  CA    B SER B 2 296 ? 35.202  -22.425 17.828  0.80 42.00  ? 296 SER B CA    1 
ATOM   11283 C  C     A SER B 2 296 ? 35.237  -24.110 16.782  0.20 39.30  ? 296 SER B C     1 
ATOM   11284 C  C     B SER B 2 296 ? 35.253  -23.582 16.842  0.80 37.49  ? 296 SER B C     1 
ATOM   11285 O  O     A SER B 2 296 ? 35.232  -23.998 15.551  0.20 39.28  ? 296 SER B O     1 
ATOM   11286 O  O     B SER B 2 296 ? 34.938  -23.402 15.659  0.80 37.66  ? 296 SER B O     1 
ATOM   11287 C  CB    A SER B 2 296 ? 36.274  -22.010 17.647  0.20 41.87  ? 296 SER B CB    1 
ATOM   11288 C  CB    B SER B 2 296 ? 36.531  -21.672 17.818  0.80 42.68  ? 296 SER B CB    1 
ATOM   11289 O  OG    A SER B 2 296 ? 37.368  -22.698 18.231  0.20 51.74  ? 296 SER B OG    1 
ATOM   11290 O  OG    B SER B 2 296 ? 37.613  -22.527 18.155  0.80 54.79  ? 296 SER B OG    1 
ATOM   11291 N  N     A LYS B 2 297 ? 35.434  -25.280 17.395  0.20 38.31  ? 297 LYS B N     1 
ATOM   11292 N  N     B LYS B 2 297 ? 35.624  -24.775 17.307  0.80 35.12  ? 297 LYS B N     1 
ATOM   11293 C  CA    A LYS B 2 297 ? 35.596  -26.509 16.628  0.20 42.32  ? 297 LYS B CA    1 
ATOM   11294 C  CA    B LYS B 2 297 ? 35.760  -25.919 16.414  0.80 43.79  ? 297 LYS B CA    1 
ATOM   11295 C  C     A LYS B 2 297 ? 34.310  -26.933 15.935  0.20 37.84  ? 297 LYS B C     1 
ATOM   11296 C  C     B LYS B 2 297 ? 34.422  -26.521 16.020  0.80 36.30  ? 297 LYS B C     1 
ATOM   11297 O  O     A LYS B 2 297 ? 34.370  -27.658 14.936  0.20 38.49  ? 297 LYS B O     1 
ATOM   11298 O  O     B LYS B 2 297 ? 34.388  -27.358 15.113  0.80 37.95  ? 297 LYS B O     1 
ATOM   11299 C  CB    A LYS B 2 297 ? 36.091  -27.635 17.537  0.20 43.81  ? 297 LYS B CB    1 
ATOM   11300 C  CB    B LYS B 2 297 ? 36.638  -26.995 17.060  0.80 45.67  ? 297 LYS B CB    1 
ATOM   11301 C  CG    A LYS B 2 297 ? 37.603  -27.738 17.634  0.20 47.64  ? 297 LYS B CG    1 
ATOM   11302 C  CG    B LYS B 2 297 ? 37.927  -26.450 17.646  0.80 51.67  ? 297 LYS B CG    1 
ATOM   11303 C  CD    A LYS B 2 297 ? 38.210  -28.096 16.285  0.20 50.08  ? 297 LYS B CD    1 
ATOM   11304 C  CD    B LYS B 2 297 ? 38.928  -27.550 17.961  0.80 58.37  ? 297 LYS B CD    1 
ATOM   11305 C  CE    A LYS B 2 297 ? 39.717  -28.259 16.375  0.20 47.68  ? 297 LYS B CE    1 
ATOM   11306 C  CE    B LYS B 2 297 ? 40.210  -26.952 18.523  0.80 64.44  ? 297 LYS B CE    1 
ATOM   11307 N  NZ    A LYS B 2 297 ? 40.310  -28.634 15.059  0.20 45.48  ? 297 LYS B NZ    1 
ATOM   11308 N  NZ    B LYS B 2 297 ? 40.791  -25.937 17.598  0.80 64.40  ? 297 LYS B NZ    1 
ATOM   11309 N  N     A ASN B 2 298 ? 33.153  -26.499 16.437  0.20 37.88  ? 298 ASN B N     1 
ATOM   11310 N  N     B ASN B 2 298 ? 33.329  -26.123 16.672  0.80 36.22  ? 298 ASN B N     1 
ATOM   11311 C  CA    A ASN B 2 298 ? 31.868  -26.896 15.879  0.20 37.32  ? 298 ASN B CA    1 
ATOM   11312 C  CA    B ASN B 2 298 ? 31.995  -26.596 16.333  0.80 37.67  ? 298 ASN B CA    1 
ATOM   11313 C  C     A ASN B 2 298 ? 31.263  -25.855 14.947  0.20 36.78  ? 298 ASN B C     1 
ATOM   11314 C  C     B ASN B 2 298 ? 31.213  -25.591 15.503  0.80 38.39  ? 298 ASN B C     1 
ATOM   11315 O  O     A ASN B 2 298 ? 30.335  -26.185 14.200  0.20 33.82  ? 298 ASN B O     1 
ATOM   11316 O  O     B ASN B 2 298 ? 29.992  -25.727 15.377  0.80 40.43  ? 298 ASN B O     1 
ATOM   11317 C  CB    A ASN B 2 298 ? 30.876  -27.198 17.009  0.20 40.33  ? 298 ASN B CB    1 
ATOM   11318 C  CB    B ASN B 2 298 ? 31.208  -26.930 17.600  0.80 41.83  ? 298 ASN B CB    1 
ATOM   11319 C  CG    A ASN B 2 298 ? 31.318  -28.360 17.880  0.20 40.62  ? 298 ASN B CG    1 
ATOM   11320 C  CG    B ASN B 2 298 ? 31.713  -28.179 18.284  0.80 38.33  ? 298 ASN B CG    1 
ATOM   11321 O  OD1   A ASN B 2 298 ? 32.275  -28.249 18.645  0.20 38.74  ? 298 ASN B OD1   1 
ATOM   11322 O  OD1   B ASN B 2 298 ? 32.632  -28.122 19.088  0.80 39.28  ? 298 ASN B OD1   1 
ATOM   11323 N  ND2   A ASN B 2 298 ? 30.614  -29.479 17.774  0.20 41.88  ? 298 ASN B ND2   1 
ATOM   11324 N  ND2   B ASN B 2 298 ? 31.109  -29.313 17.969  0.80 39.68  ? 298 ASN B ND2   1 
ATOM   11325 N  N     A MET B 2 299 ? 31.759  -24.620 14.971  0.20 31.31  ? 299 MET B N     1 
ATOM   11326 N  N     B MET B 2 299 ? 31.873  -24.574 14.966  0.80 30.53  ? 299 MET B N     1 
ATOM   11327 C  CA    A MET B 2 299 ? 31.212  -23.579 14.110  0.20 34.74  ? 299 MET B CA    1 
ATOM   11328 C  CA    B MET B 2 299 ? 31.210  -23.608 14.109  0.80 34.69  ? 299 MET B CA    1 
ATOM   11329 C  C     A MET B 2 299 ? 31.455  -23.919 12.645  0.20 32.86  ? 299 MET B C     1 
ATOM   11330 C  C     B MET B 2 299 ? 31.327  -24.048 12.657  0.80 32.10  ? 299 MET B C     1 
ATOM   11331 O  O     A MET B 2 299 ? 32.585  -24.211 12.242  0.20 35.52  ? 299 MET B O     1 
ATOM   11332 O  O     B MET B 2 299 ? 32.289  -24.720 12.267  0.80 38.16  ? 299 MET B O     1 
ATOM   11333 C  CB    A MET B 2 299 ? 31.840  -22.226 14.450  0.20 34.81  ? 299 MET B CB    1 
ATOM   11334 C  CB    B MET B 2 299 ? 31.812  -22.211 14.285  0.80 33.84  ? 299 MET B CB    1 
ATOM   11335 C  CG    A MET B 2 299 ? 31.573  -21.749 15.869  0.20 51.14  ? 299 MET B CG    1 
ATOM   11336 C  CG    B MET B 2 299 ? 31.556  -21.581 15.647  0.80 52.49  ? 299 MET B CG    1 
ATOM   11337 S  SD    A MET B 2 299 ? 29.818  -21.547 16.223  0.20 128.72 ? 299 MET B SD    1 
ATOM   11338 S  SD    B MET B 2 299 ? 29.808  -21.569 16.073  0.80 122.59 ? 299 MET B SD    1 
ATOM   11339 C  CE    A MET B 2 299 ? 29.884  -20.999 17.925  0.20 53.77  ? 299 MET B CE    1 
ATOM   11340 C  CE    B MET B 2 299 ? 29.900  -21.046 17.775  0.80 54.00  ? 299 MET B CE    1 
ATOM   11341 N  N     A MET B 2 300 ? 30.387  -23.879 11.850  0.20 32.70  ? 300 MET B N     1 
ATOM   11342 N  N     B MET B 2 300 ? 30.329  -23.675 11.863  0.80 32.32  ? 300 MET B N     1 
ATOM   11343 C  CA    A MET B 2 300 ? 30.462  -24.155 10.421  0.20 31.23  ? 300 MET B CA    1 
ATOM   11344 C  CA    B MET B 2 300 ? 30.340  -23.901 10.427  0.80 30.56  ? 300 MET B CA    1 
ATOM   11345 C  C     A MET B 2 300 ? 31.048  -22.995 9.626   0.20 33.10  ? 300 MET B C     1 
ATOM   11346 C  C     B MET B 2 300 ? 30.890  -22.705 9.667   0.80 34.60  ? 300 MET B C     1 
ATOM   11347 O  O     A MET B 2 300 ? 31.013  -23.029 8.392   0.20 31.58  ? 300 MET B O     1 
ATOM   11348 O  O     B MET B 2 300 ? 30.861  -22.704 8.435   0.80 30.61  ? 300 MET B O     1 
ATOM   11349 C  CB    A MET B 2 300 ? 29.074  -24.503 9.875   0.20 30.44  ? 300 MET B CB    1 
ATOM   11350 C  CB    B MET B 2 300 ? 28.933  -24.226 9.916   0.80 29.23  ? 300 MET B CB    1 
ATOM   11351 C  CG    A MET B 2 300 ? 28.417  -25.699 10.551  0.20 37.10  ? 300 MET B CG    1 
ATOM   11352 C  CG    B MET B 2 300 ? 28.296  -25.439 10.585  0.80 38.30  ? 300 MET B CG    1 
ATOM   11353 S  SD    A MET B 2 300 ? 29.343  -27.231 10.334  0.20 38.55  ? 300 MET B SD    1 
ATOM   11354 S  SD    B MET B 2 300 ? 29.327  -26.913 10.445  0.80 40.97  ? 300 MET B SD    1 
ATOM   11355 C  CE    A MET B 2 300 ? 28.349  -28.363 11.303  0.20 38.60  ? 300 MET B CE    1 
ATOM   11356 C  CE    B MET B 2 300 ? 28.544  -27.980 11.651  0.80 39.78  ? 300 MET B CE    1 
ATOM   11357 N  N     A ALA B 2 301 ? 31.568  -21.972 10.299  0.20 32.76  ? 301 ALA B N     1 
ATOM   11358 N  N     B ALA B 2 301 ? 31.347  -21.677 10.375  0.80 32.09  ? 301 ALA B N     1 
ATOM   11359 C  CA    A ALA B 2 301 ? 32.234  -20.855 9.649   0.20 31.66  ? 301 ALA B CA    1 
ATOM   11360 C  CA    B ALA B 2 301 ? 32.066  -20.556 9.790   0.80 32.53  ? 301 ALA B CA    1 
ATOM   11361 C  C     A ALA B 2 301 ? 33.584  -20.643 10.313  0.20 32.58  ? 301 ALA B C     1 
ATOM   11362 C  C     B ALA B 2 301 ? 33.442  -20.509 10.433  0.80 32.75  ? 301 ALA B C     1 
ATOM   11363 O  O     A ALA B 2 301 ? 33.688  -20.661 11.543  0.20 30.70  ? 301 ALA B O     1 
ATOM   11364 O  O     B ALA B 2 301 ? 33.556  -20.552 11.661  0.80 29.95  ? 301 ALA B O     1 
ATOM   11365 C  CB    A ALA B 2 301 ? 31.394  -19.574 9.728   0.20 31.21  ? 301 ALA B CB    1 
ATOM   11366 C  CB    B ALA B 2 301 ? 31.312  -19.237 10.004  0.80 29.83  ? 301 ALA B CB    1 
ATOM   11367 N  N     A ALA B 2 302 ? 34.617  -20.444 9.494   0.20 31.82  ? 302 ALA B N     1 
ATOM   11368 N  N     B ALA B 2 302 ? 34.487  -20.414 9.606   0.80 32.03  ? 302 ALA B N     1 
ATOM   11369 C  CA    A ALA B 2 302 ? 35.978  -20.312 9.999   0.20 32.35  ? 302 ALA B CA    1 
ATOM   11370 C  CA    B ALA B 2 302 ? 35.861  -20.563 10.088  0.80 31.73  ? 302 ALA B CA    1 
ATOM   11371 C  C     A ALA B 2 302 ? 36.152  -19.013 10.774  0.20 32.91  ? 302 ALA B C     1 
ATOM   11372 C  C     B ALA B 2 302 ? 36.314  -19.267 10.759  0.80 32.66  ? 302 ALA B C     1 
ATOM   11373 O  O     A ALA B 2 302 ? 36.817  -18.084 10.304  0.20 33.49  ? 302 ALA B O     1 
ATOM   11374 O  O     B ALA B 2 302 ? 37.106  -18.487 10.230  0.80 36.34  ? 302 ALA B O     1 
ATOM   11375 C  CB    A ALA B 2 302 ? 36.983  -20.387 8.849   0.20 33.12  ? 302 ALA B CB    1 
ATOM   11376 C  CB    B ALA B 2 302 ? 36.785  -20.952 8.943   0.80 36.62  ? 302 ALA B CB    1 
ATOM   11377 N  N     A CYS B 2 303 ? 35.547  -18.932 11.957  0.20 32.09  ? 303 CYS B N     1 
ATOM   11378 N  N     B CYS B 2 303 ? 35.786  -19.040 11.960  0.80 32.09  ? 303 CYS B N     1 
ATOM   11379 C  CA    A CYS B 2 303 ? 35.641  -17.746 12.796  0.20 31.82  ? 303 CYS B CA    1 
ATOM   11380 C  CA    B CYS B 2 303 ? 36.177  -17.875 12.732  0.80 30.96  ? 303 CYS B CA    1 
ATOM   11381 C  C     A CYS B 2 303 ? 35.646  -18.181 14.251  0.20 34.18  ? 303 CYS B C     1 
ATOM   11382 C  C     B CYS B 2 303 ? 36.065  -18.220 14.206  0.80 32.35  ? 303 CYS B C     1 
ATOM   11383 O  O     A CYS B 2 303 ? 34.732  -18.886 14.689  0.20 32.83  ? 303 CYS B O     1 
ATOM   11384 O  O     B CYS B 2 303 ? 35.446  -19.218 14.591  0.80 36.81  ? 303 CYS B O     1 
ATOM   11385 C  CB    A CYS B 2 303 ? 34.474  -16.782 12.549  0.20 35.11  ? 303 CYS B CB    1 
ATOM   11386 C  CB    B CYS B 2 303 ? 35.342  -16.642 12.369  0.80 33.80  ? 303 CYS B CB    1 
ATOM   11387 S  SG    A CYS B 2 303 ? 34.024  -16.526 10.822  0.20 19.40  ? 303 CYS B SG    1 
ATOM   11388 S  SG    B CYS B 2 303 ? 33.619  -16.713 12.869  0.80 47.73  ? 303 CYS B SG    1 
ATOM   11389 N  N     A ASP B 2 304 ? 36.666  -17.766 14.989  0.20 32.63  ? 304 ASP B N     1 
ATOM   11390 N  N     B ASP B 2 304 ? 36.674  -17.377 15.029  0.80 33.06  ? 304 ASP B N     1 
ATOM   11391 C  CA    A ASP B 2 304 ? 36.690  -18.003 16.426  0.20 31.33  ? 304 ASP B CA    1 
ATOM   11392 C  CA    B ASP B 2 304 ? 36.750  -17.613 16.463  0.80 29.48  ? 304 ASP B CA    1 
ATOM   11393 C  C     A ASP B 2 304 ? 35.773  -16.996 17.109  0.20 33.71  ? 304 ASP B C     1 
ATOM   11394 C  C     B ASP B 2 304 ? 35.740  -16.718 17.164  0.80 34.21  ? 304 ASP B C     1 
ATOM   11395 O  O     A ASP B 2 304 ? 36.044  -15.791 17.054  0.20 32.54  ? 304 ASP B O     1 
ATOM   11396 O  O     B ASP B 2 304 ? 35.899  -15.489 17.141  0.80 32.01  ? 304 ASP B O     1 
ATOM   11397 C  CB    A ASP B 2 304 ? 38.112  -17.890 16.967  0.20 35.02  ? 304 ASP B CB    1 
ATOM   11398 C  CB    B ASP B 2 304 ? 38.169  -17.327 16.965  0.80 34.88  ? 304 ASP B CB    1 
ATOM   11399 C  CG    A ASP B 2 304 ? 38.258  -18.476 18.364  0.20 38.52  ? 304 ASP B CG    1 
ATOM   11400 C  CG    B ASP B 2 304 ? 38.455  -17.939 18.322  0.80 40.18  ? 304 ASP B CG    1 
ATOM   11401 O  OD1   A ASP B 2 304 ? 37.373  -18.240 19.212  0.20 36.90  ? 304 ASP B OD1   1 
ATOM   11402 O  OD1   B ASP B 2 304 ? 37.515  -18.432 18.986  0.80 37.16  ? 304 ASP B OD1   1 
ATOM   11403 O  OD2   A ASP B 2 304 ? 39.259  -19.180 18.614  0.20 36.79  ? 304 ASP B OD2   1 
ATOM   11404 O  OD2   B ASP B 2 304 ? 39.637  -17.928 18.727  0.80 40.67  ? 304 ASP B OD2   1 
ATOM   11405 N  N     A PRO B 2 305 ? 34.687  -17.436 17.752  0.20 26.72  ? 305 PRO B N     1 
ATOM   11406 N  N     B PRO B 2 305 ? 34.682  -17.271 17.767  0.80 25.50  ? 305 PRO B N     1 
ATOM   11407 C  CA    A PRO B 2 305 ? 33.739  -16.473 18.336  0.20 33.41  ? 305 PRO B CA    1 
ATOM   11408 C  CA    B PRO B 2 305 ? 33.740  -16.422 18.516  0.80 33.68  ? 305 PRO B CA    1 
ATOM   11409 C  C     A PRO B 2 305 ? 34.310  -15.674 19.494  0.20 33.40  ? 305 PRO B C     1 
ATOM   11410 C  C     B PRO B 2 305 ? 34.405  -15.630 19.629  0.80 33.31  ? 305 PRO B C     1 
ATOM   11411 O  O     A PRO B 2 305 ? 33.750  -14.624 19.832  0.20 32.00  ? 305 PRO B O     1 
ATOM   11412 O  O     B PRO B 2 305 ? 33.932  -14.542 19.979  0.80 31.36  ? 305 PRO B O     1 
ATOM   11413 C  CB    A PRO B 2 305 ? 32.578  -17.363 18.793  0.20 35.39  ? 305 PRO B CB    1 
ATOM   11414 C  CB    B PRO B 2 305 ? 32.732  -17.437 19.069  0.80 35.75  ? 305 PRO B CB    1 
ATOM   11415 C  CG    A PRO B 2 305 ? 33.206  -18.702 19.031  0.20 34.77  ? 305 PRO B CG    1 
ATOM   11416 C  CG    B PRO B 2 305 ? 32.814  -18.605 18.146  0.80 41.09  ? 305 PRO B CG    1 
ATOM   11417 C  CD    A PRO B 2 305 ? 34.269  -18.831 17.975  0.20 31.64  ? 305 PRO B CD    1 
ATOM   11418 C  CD    B PRO B 2 305 ? 34.238  -18.675 17.691  0.80 28.72  ? 305 PRO B CD    1 
ATOM   11419 N  N     A ARG B 2 306 ? 35.399  -16.130 20.112  0.20 35.83  ? 306 ARG B N     1 
ATOM   11420 N  N     B ARG B 2 306 ? 35.495  -16.153 20.199  0.80 35.90  ? 306 ARG B N     1 
ATOM   11421 C  CA    A ARG B 2 306 ? 36.010  -15.403 21.215  0.20 37.74  ? 306 ARG B CA    1 
ATOM   11422 C  CA    B ARG B 2 306 ? 36.228  -15.452 21.244  0.80 37.65  ? 306 ARG B CA    1 
ATOM   11423 C  C     A ARG B 2 306 ? 36.862  -14.230 20.748  0.20 36.36  ? 306 ARG B C     1 
ATOM   11424 C  C     B ARG B 2 306 ? 37.060  -14.301 20.705  0.80 36.31  ? 306 ARG B C     1 
ATOM   11425 O  O     A ARG B 2 306 ? 37.443  -13.536 21.588  0.20 38.97  ? 306 ARG B O     1 
ATOM   11426 O  O     B ARG B 2 306 ? 37.694  -13.603 21.499  0.80 40.43  ? 306 ARG B O     1 
ATOM   11427 C  CB    A ARG B 2 306 ? 36.850  -16.353 22.072  0.20 41.06  ? 306 ARG B CB    1 
ATOM   11428 C  CB    B ARG B 2 306 ? 37.121  -16.427 22.016  0.80 40.81  ? 306 ARG B CB    1 
ATOM   11429 C  CG    A ARG B 2 306 ? 36.039  -17.459 22.727  0.20 48.08  ? 306 ARG B CG    1 
ATOM   11430 C  CG    B ARG B 2 306 ? 36.414  -17.175 23.151  0.80 50.60  ? 306 ARG B CG    1 
ATOM   11431 C  CD    A ARG B 2 306 ? 36.866  -18.224 23.746  0.20 50.65  ? 306 ARG B CD    1 
ATOM   11432 C  CD    B ARG B 2 306 ? 35.626  -18.371 22.638  0.80 50.31  ? 306 ARG B CD    1 
ATOM   11433 N  NE    A ARG B 2 306 ? 36.124  -19.341 24.319  0.20 57.90  ? 306 ARG B NE    1 
ATOM   11434 N  NE    B ARG B 2 306 ? 34.617  -18.831 23.587  0.80 78.75  ? 306 ARG B NE    1 
ATOM   11435 C  CZ    A ARG B 2 306 ? 35.321  -19.247 25.370  0.20 58.48  ? 306 ARG B CZ    1 
ATOM   11436 C  CZ    B ARG B 2 306 ? 34.848  -19.681 24.580  0.80 61.53  ? 306 ARG B CZ    1 
ATOM   11437 N  NH1   A ARG B 2 306 ? 35.132  -18.097 25.995  0.20 55.25  ? 306 ARG B NH1   1 
ATOM   11438 N  NH1   B ARG B 2 306 ? 36.058  -20.162 24.810  0.80 65.81  ? 306 ARG B NH1   1 
ATOM   11439 N  NH2   A ARG B 2 306 ? 34.691  -20.335 25.804  0.20 60.53  ? 306 ARG B NH2   1 
ATOM   11440 N  NH2   B ARG B 2 306 ? 33.837  -20.058 25.358  0.80 63.22  ? 306 ARG B NH2   1 
ATOM   11441 N  N     A HIS B 2 307 ? 36.950  -13.997 19.439  0.20 32.79  ? 307 HIS B N     1 
ATOM   11442 N  N     B HIS B 2 307 ? 37.070  -14.080 19.393  0.80 32.49  ? 307 HIS B N     1 
ATOM   11443 C  CA    A HIS B 2 307 ? 37.567  -12.792 18.905  0.20 31.55  ? 307 HIS B CA    1 
ATOM   11444 C  CA    B HIS B 2 307 ? 37.663  -12.896 18.786  0.80 31.15  ? 307 HIS B CA    1 
ATOM   11445 C  C     A HIS B 2 307 ? 36.576  -11.647 18.739  0.20 34.96  ? 307 HIS B C     1 
ATOM   11446 C  C     B HIS B 2 307 ? 36.654  -11.776 18.577  0.80 35.36  ? 307 HIS B C     1 
ATOM   11447 O  O     A HIS B 2 307 ? 37.000  -10.501 18.554  0.20 36.16  ? 307 HIS B O     1 
ATOM   11448 O  O     B HIS B 2 307 ? 36.987  -10.764 17.950  0.80 38.63  ? 307 HIS B O     1 
ATOM   11449 C  CB    A HIS B 2 307 ? 38.236  -13.095 17.557  0.20 32.13  ? 307 HIS B CB    1 
ATOM   11450 C  CB    B HIS B 2 307 ? 38.307  -13.255 17.441  0.80 31.46  ? 307 HIS B CB    1 
ATOM   11451 C  CG    A HIS B 2 307 ? 39.309  -14.137 17.638  0.20 35.64  ? 307 HIS B CG    1 
ATOM   11452 C  CG    B HIS B 2 307 ? 39.551  -14.074 17.569  0.80 36.78  ? 307 HIS B CG    1 
ATOM   11453 N  ND1   A HIS B 2 307 ? 39.872  -14.716 16.520  0.20 34.80  ? 307 HIS B ND1   1 
ATOM   11454 N  ND1   B HIS B 2 307 ? 40.248  -14.546 16.476  0.80 34.82  ? 307 HIS B ND1   1 
ATOM   11455 C  CD2   A HIS B 2 307 ? 39.925  -14.702 18.704  0.20 35.04  ? 307 HIS B CD2   1 
ATOM   11456 C  CD2   B HIS B 2 307 ? 40.233  -14.494 18.662  0.80 33.84  ? 307 HIS B CD2   1 
ATOM   11457 C  CE1   A HIS B 2 307 ? 40.784  -15.595 16.895  0.20 33.51  ? 307 HIS B CE1   1 
ATOM   11458 C  CE1   B HIS B 2 307 ? 41.301  -15.228 16.892  0.80 31.46  ? 307 HIS B CE1   1 
ATOM   11459 N  NE2   A HIS B 2 307 ? 40.835  -15.606 18.215  0.20 36.79  ? 307 HIS B NE2   1 
ATOM   11460 N  NE2   B HIS B 2 307 ? 41.312  -15.214 18.214  0.80 41.55  ? 307 HIS B NE2   1 
ATOM   11461 N  N     A GLY B 2 308 ? 35.275  -11.923 18.800  0.20 32.42  ? 308 GLY B N     1 
ATOM   11462 N  N     B GLY B 2 308 ? 35.423  -11.943 19.062  0.80 32.89  ? 308 GLY B N     1 
ATOM   11463 C  CA    A GLY B 2 308 ? 34.279  -10.871 18.712  0.20 28.84  ? 308 GLY B CA    1 
ATOM   11464 C  CA    B GLY B 2 308 ? 34.402  -10.938 18.860  0.80 28.47  ? 308 GLY B CA    1 
ATOM   11465 C  C     A GLY B 2 308 ? 33.212  -10.988 19.785  0.20 26.38  ? 308 GLY B C     1 
ATOM   11466 C  C     B GLY B 2 308 ? 33.328  -10.974 19.934  0.80 25.56  ? 308 GLY B C     1 
ATOM   11467 O  O     A GLY B 2 308 ? 33.467  -11.551 20.858  0.20 28.46  ? 308 GLY B O     1 
ATOM   11468 O  O     B GLY B 2 308 ? 33.551  -11.475 21.043  0.80 27.74  ? 308 GLY B O     1 
ATOM   11469 N  N     A ARG B 2 309 ? 32.012  -10.475 19.512  0.20 27.02  ? 309 ARG B N     1 
ATOM   11470 N  N     B ARG B 2 309 ? 32.148  -10.466 19.598  0.80 26.87  ? 309 ARG B N     1 
ATOM   11471 C  CA    A ARG B 2 309 ? 30.929  -10.499 20.481  0.20 26.96  ? 309 ARG B CA    1 
ATOM   11472 C  CA    B ARG B 2 309 ? 31.074  -10.312 20.571  0.80 25.62  ? 309 ARG B CA    1 
ATOM   11473 C  C     A ARG B 2 309 ? 29.644  -10.958 19.807  0.20 28.58  ? 309 ARG B C     1 
ATOM   11474 C  C     B ARG B 2 309 ? 29.771  -10.773 19.948  0.80 28.07  ? 309 ARG B C     1 
ATOM   11475 O  O     A ARG B 2 309 ? 29.438  -10.746 18.607  0.20 28.84  ? 309 ARG B O     1 
ATOM   11476 O  O     B ARG B 2 309 ? 29.471  -10.425 18.799  0.80 29.13  ? 309 ARG B O     1 
ATOM   11477 C  CB    A ARG B 2 309 ? 30.724  -9.121  21.118  0.20 31.14  ? 309 ARG B CB    1 
ATOM   11478 C  CB    B ARG B 2 309 ? 30.954  -8.860  21.031  0.80 31.58  ? 309 ARG B CB    1 
ATOM   11479 C  CG    A ARG B 2 309 ? 31.795  -8.720  22.128  0.20 32.98  ? 309 ARG B CG    1 
ATOM   11480 C  CG    B ARG B 2 309 ? 31.905  -8.467  22.154  0.80 32.43  ? 309 ARG B CG    1 
ATOM   11481 C  CD    A ARG B 2 309 ? 31.469  -7.366  22.749  0.20 39.97  ? 309 ARG B CD    1 
ATOM   11482 C  CD    B ARG B 2 309 ? 31.714  -6.995  22.531  0.80 42.53  ? 309 ARG B CD    1 
ATOM   11483 N  NE    A ARG B 2 309 ? 32.420  -6.985  23.787  0.20 46.96  ? 309 ARG B NE    1 
ATOM   11484 N  NE    B ARG B 2 309 ? 32.406  -6.660  23.771  0.80 48.38  ? 309 ARG B NE    1 
ATOM   11485 C  CZ    A ARG B 2 309 ? 32.221  -7.153  25.087  0.20 47.05  ? 309 ARG B CZ    1 
ATOM   11486 C  CZ    B ARG B 2 309 ? 32.814  -5.442  24.106  0.80 59.20  ? 309 ARG B CZ    1 
ATOM   11487 N  NH1   A ARG B 2 309 ? 31.104  -7.689  25.553  0.20 36.89  ? 309 ARG B NH1   1 
ATOM   11488 N  NH1   B ARG B 2 309 ? 32.635  -4.404  23.303  0.80 43.77  ? 309 ARG B NH1   1 
ATOM   11489 N  NH2   A ARG B 2 309 ? 33.169  -6.780  25.942  0.20 44.38  ? 309 ARG B NH2   1 
ATOM   11490 N  NH2   B ARG B 2 309 ? 33.426  -5.262  25.273  0.80 60.23  ? 309 ARG B NH2   1 
ATOM   11491 N  N     A TYR B 2 310 ? 28.776  -11.583 20.597  0.20 31.34  ? 310 TYR B N     1 
ATOM   11492 N  N     B TYR B 2 310 ? 29.017  -11.568 20.702  0.80 31.32  ? 310 TYR B N     1 
ATOM   11493 C  CA    A TYR B 2 310 ? 27.498  -12.082 20.107  0.20 30.83  ? 310 TYR B CA    1 
ATOM   11494 C  CA    B TYR B 2 310 ? 27.684  -11.981 20.281  0.80 31.27  ? 310 TYR B CA    1 
ATOM   11495 C  C     A TYR B 2 310 ? 26.455  -10.975 20.178  0.20 31.87  ? 310 TYR B C     1 
ATOM   11496 C  C     B TYR B 2 310 ? 26.719  -10.816 20.414  0.80 33.90  ? 310 TYR B C     1 
ATOM   11497 O  O     A TYR B 2 310 ? 26.168  -10.458 21.262  0.20 30.18  ? 310 TYR B O     1 
ATOM   11498 O  O     B TYR B 2 310 ? 26.591  -10.229 21.493  0.80 28.52  ? 310 TYR B O     1 
ATOM   11499 C  CB    A TYR B 2 310 ? 27.028  -13.287 20.921  0.20 32.02  ? 310 TYR B CB    1 
ATOM   11500 C  CB    B TYR B 2 310 ? 27.198  -13.156 21.124  0.80 32.52  ? 310 TYR B CB    1 
ATOM   11501 C  CG    A TYR B 2 310 ? 27.774  -14.573 20.654  0.20 30.67  ? 310 TYR B CG    1 
ATOM   11502 C  CG    B TYR B 2 310 ? 27.924  -14.452 20.861  0.80 30.04  ? 310 TYR B CG    1 
ATOM   11503 C  CD1   A TYR B 2 310 ? 27.658  -15.225 19.437  0.20 32.06  ? 310 TYR B CD1   1 
ATOM   11504 C  CD1   B TYR B 2 310 ? 27.756  -15.121 19.668  0.80 31.00  ? 310 TYR B CD1   1 
ATOM   11505 C  CD2   A TYR B 2 310 ? 28.571  -15.151 21.634  0.20 33.84  ? 310 TYR B CD2   1 
ATOM   11506 C  CD2   B TYR B 2 310 ? 28.757  -15.017 21.824  0.80 33.69  ? 310 TYR B CD2   1 
ATOM   11507 C  CE1   A TYR B 2 310 ? 28.332  -16.406 19.194  0.20 39.64  ? 310 TYR B CE1   1 
ATOM   11508 C  CE1   B TYR B 2 310 ? 28.413  -16.308 19.422  0.80 41.23  ? 310 TYR B CE1   1 
ATOM   11509 C  CE2   A TYR B 2 310 ? 29.248  -16.333 21.402  0.20 37.89  ? 310 TYR B CE2   1 
ATOM   11510 C  CE2   B TYR B 2 310 ? 29.416  -16.214 21.589  0.80 38.69  ? 310 TYR B CE2   1 
ATOM   11511 C  CZ    A TYR B 2 310 ? 29.125  -16.956 20.179  0.20 37.75  ? 310 TYR B CZ    1 
ATOM   11512 C  CZ    B TYR B 2 310 ? 29.238  -16.851 20.382  0.80 37.38  ? 310 TYR B CZ    1 
ATOM   11513 O  OH    A TYR B 2 310 ? 29.792  -18.134 19.937  0.20 40.97  ? 310 TYR B OH    1 
ATOM   11514 O  OH    B TYR B 2 310 ? 29.873  -18.037 20.118  0.80 41.71  ? 310 TYR B OH    1 
ATOM   11515 N  N     A LEU B 2 311 ? 25.885  -10.619 19.027  0.20 29.12  ? 311 LEU B N     1 
ATOM   11516 N  N     B LEU B 2 311 ? 26.050  -10.476 19.316  0.80 28.46  ? 311 LEU B N     1 
ATOM   11517 C  CA    A LEU B 2 311 ? 24.729  -9.729  19.029  0.20 30.38  ? 311 LEU B CA    1 
ATOM   11518 C  CA    B LEU B 2 311 ? 24.952  -9.526  19.381  0.80 28.67  ? 311 LEU B CA    1 
ATOM   11519 C  C     A LEU B 2 311 ? 23.478  -10.475 19.481  0.20 30.47  ? 311 LEU B C     1 
ATOM   11520 C  C     B LEU B 2 311 ? 23.666  -10.226 19.804  0.80 31.44  ? 311 LEU B C     1 
ATOM   11521 O  O     A LEU B 2 311 ? 22.803  -10.058 20.430  0.20 29.12  ? 311 LEU B O     1 
ATOM   11522 O  O     B LEU B 2 311 ? 22.936  -9.734  20.670  0.80 29.41  ? 311 LEU B O     1 
ATOM   11523 C  CB    A LEU B 2 311 ? 24.523  -9.123  17.639  0.20 30.04  ? 311 LEU B CB    1 
ATOM   11524 C  CB    B LEU B 2 311 ? 24.761  -8.856  18.024  0.80 29.50  ? 311 LEU B CB    1 
ATOM   11525 C  CG    A LEU B 2 311 ? 25.625  -8.214  17.087  0.20 31.74  ? 311 LEU B CG    1 
ATOM   11526 C  CG    B LEU B 2 311 ? 25.961  -8.184  17.369  0.80 33.10  ? 311 LEU B CG    1 
ATOM   11527 C  CD1   A LEU B 2 311 ? 25.347  -7.872  15.631  0.20 30.52  ? 311 LEU B CD1   1 
ATOM   11528 C  CD1   B LEU B 2 311 ? 25.555  -7.500  16.066  0.80 32.69  ? 311 LEU B CD1   1 
ATOM   11529 C  CD2   A LEU B 2 311 ? 25.753  -6.947  17.918  0.20 29.51  ? 311 LEU B CD2   1 
ATOM   11530 C  CD2   B LEU B 2 311 ? 26.579  -7.198  18.331  0.80 30.63  ? 311 LEU B CD2   1 
ATOM   11531 N  N     A THR B 2 312 ? 23.160  -11.587 18.817  0.20 29.35  ? 312 THR B N     1 
ATOM   11532 N  N     B THR B 2 312 ? 23.392  -11.382 19.197  0.80 28.29  ? 312 THR B N     1 
ATOM   11533 C  CA    A THR B 2 312 ? 22.024  -12.424 19.177  0.20 28.30  ? 312 THR B CA    1 
ATOM   11534 C  CA    B THR B 2 312 ? 22.184  -12.164 19.407  0.80 28.72  ? 312 THR B CA    1 
ATOM   11535 C  C     A THR B 2 312 ? 22.401  -13.888 18.986  0.20 29.89  ? 312 THR B C     1 
ATOM   11536 C  C     B THR B 2 312 ? 22.529  -13.621 19.137  0.80 29.91  ? 312 THR B C     1 
ATOM   11537 O  O     A THR B 2 312 ? 23.334  -14.221 18.247  0.20 29.01  ? 312 THR B O     1 
ATOM   11538 O  O     B THR B 2 312 ? 23.376  -13.932 18.283  0.80 30.04  ? 312 THR B O     1 
ATOM   11539 C  CB    A THR B 2 312 ? 20.774  -12.093 18.346  0.20 28.56  ? 312 THR B CB    1 
ATOM   11540 C  CB    B THR B 2 312 ? 21.027  -11.724 18.494  0.80 28.15  ? 312 THR B CB    1 
ATOM   11541 O  OG1   A THR B 2 312 ? 21.116  -12.057 16.955  0.20 27.42  ? 312 THR B OG1   1 
ATOM   11542 O  OG1   B THR B 2 312 ? 21.440  -11.800 17.122  0.80 28.13  ? 312 THR B OG1   1 
ATOM   11543 C  CG2   A THR B 2 312 ? 20.178  -10.750 18.761  0.20 28.40  ? 312 THR B CG2   1 
ATOM   11544 C  CG2   B THR B 2 312 ? 20.564  -10.296 18.807  0.80 26.63  ? 312 THR B CG2   1 
ATOM   11545 N  N     A VAL B 2 313 ? 21.657  -14.761 19.661  0.20 28.39  ? 313 VAL B N     1 
ATOM   11546 N  N     B VAL B 2 313 ? 21.889  -14.512 19.887  0.80 26.05  ? 313 VAL B N     1 
ATOM   11547 C  CA    A VAL B 2 313 ? 21.918  -16.199 19.645  0.20 28.52  ? 313 VAL B CA    1 
ATOM   11548 C  CA    B VAL B 2 313 ? 22.138  -15.947 19.786  0.80 28.11  ? 313 VAL B CA    1 
ATOM   11549 C  C     A VAL B 2 313 ? 20.593  -16.938 19.774  0.20 31.13  ? 313 VAL B C     1 
ATOM   11550 C  C     B VAL B 2 313 ? 20.821  -16.688 19.966  0.80 33.13  ? 313 VAL B C     1 
ATOM   11551 O  O     A VAL B 2 313 ? 19.783  -16.628 20.653  0.20 32.26  ? 313 VAL B O     1 
ATOM   11552 O  O     B VAL B 2 313 ? 19.997  -16.322 20.815  0.80 32.90  ? 313 VAL B O     1 
ATOM   11553 C  CB    A VAL B 2 313 ? 22.884  -16.619 20.774  0.20 33.64  ? 313 VAL B CB    1 
ATOM   11554 C  CB    B VAL B 2 313 ? 23.160  -16.429 20.842  0.80 35.11  ? 313 VAL B CB    1 
ATOM   11555 C  CG1   A VAL B 2 313 ? 22.697  -18.089 21.125  0.20 30.80  ? 313 VAL B CG1   1 
ATOM   11556 C  CG1   B VAL B 2 313 ? 23.444  -17.910 20.676  0.80 32.05  ? 313 VAL B CG1   1 
ATOM   11557 C  CG2   A VAL B 2 313 ? 24.324  -16.352 20.373  0.20 30.78  ? 313 VAL B CG2   1 
ATOM   11558 C  CG2   B VAL B 2 313 ? 24.445  -15.629 20.775  0.80 27.09  ? 313 VAL B CG2   1 
ATOM   11559 N  N     A ALA B 2 314 ? 20.375  -17.917 18.897  0.20 28.64  ? 314 ALA B N     1 
ATOM   11560 N  N     B ALA B 2 314 ? 20.625  -17.731 19.165  0.80 26.67  ? 314 ALA B N     1 
ATOM   11561 C  CA    A ALA B 2 314 ? 19.216  -18.804 18.956  0.20 27.18  ? 314 ALA B CA    1 
ATOM   11562 C  CA    B ALA B 2 314 ? 19.547  -18.687 19.370  0.80 26.78  ? 314 ALA B CA    1 
ATOM   11563 C  C     A ALA B 2 314 ? 19.720  -20.242 18.995  0.20 33.40  ? 314 ALA B C     1 
ATOM   11564 C  C     B ALA B 2 314 ? 20.127  -20.092 19.423  0.80 37.16  ? 314 ALA B C     1 
ATOM   11565 O  O     A ALA B 2 314 ? 20.277  -20.737 18.008  0.20 29.53  ? 314 ALA B O     1 
ATOM   11566 O  O     B ALA B 2 314 ? 21.054  -20.424 18.678  0.80 31.08  ? 314 ALA B O     1 
ATOM   11567 C  CB    A ALA B 2 314 ? 18.284  -18.577 17.767  0.20 29.71  ? 314 ALA B CB    1 
ATOM   11568 C  CB    B ALA B 2 314 ? 18.484  -18.592 18.277  0.80 24.69  ? 314 ALA B CB    1 
ATOM   11569 N  N     A ALA B 2 315 ? 19.527  -20.908 20.131  0.20 32.03  ? 315 ALA B N     1 
ATOM   11570 N  N     B ALA B 2 315 ? 19.589  -20.908 20.323  0.80 31.80  ? 315 ALA B N     1 
ATOM   11571 C  CA    A ALA B 2 315 ? 20.000  -22.270 20.343  0.20 30.70  ? 315 ALA B CA    1 
ATOM   11572 C  CA    B ALA B 2 315 ? 19.949  -22.312 20.434  0.80 30.15  ? 315 ALA B CA    1 
ATOM   11573 C  C     A ALA B 2 315 ? 18.811  -23.212 20.459  0.20 37.37  ? 315 ALA B C     1 
ATOM   11574 C  C     B ALA B 2 315 ? 18.691  -23.154 20.287  0.80 37.70  ? 315 ALA B C     1 
ATOM   11575 O  O     A ALA B 2 315 ? 17.878  -22.951 21.227  0.20 39.22  ? 315 ALA B O     1 
ATOM   11576 O  O     B ALA B 2 315 ? 17.590  -22.723 20.650  0.80 40.57  ? 315 ALA B O     1 
ATOM   11577 C  CB    A ALA B 2 315 ? 20.869  -22.360 21.600  0.20 36.58  ? 315 ALA B CB    1 
ATOM   11578 C  CB    B ALA B 2 315 ? 20.636  -22.623 21.777  0.80 36.62  ? 315 ALA B CB    1 
ATOM   11579 N  N     A ILE B 2 316 ? 18.849  -24.306 19.702  0.20 36.71  ? 316 ILE B N     1 
ATOM   11580 N  N     B ILE B 2 316 ? 18.859  -24.343 19.719  0.80 36.42  ? 316 ILE B N     1 
ATOM   11581 C  CA    A ILE B 2 316 ? 17.784  -25.301 19.690  0.20 38.24  ? 316 ILE B CA    1 
ATOM   11582 C  CA    B ILE B 2 316 ? 17.791  -25.326 19.592  0.80 38.21  ? 316 ILE B CA    1 
ATOM   11583 C  C     A ILE B 2 316 ? 18.381  -26.654 20.049  0.20 41.47  ? 316 ILE B C     1 
ATOM   11584 C  C     B ILE B 2 316 ? 18.350  -26.647 20.095  0.80 41.69  ? 316 ILE B C     1 
ATOM   11585 O  O     A ILE B 2 316 ? 19.447  -27.025 19.542  0.20 38.93  ? 316 ILE B O     1 
ATOM   11586 O  O     B ILE B 2 316 ? 19.226  -27.242 19.453  0.80 39.59  ? 316 ILE B O     1 
ATOM   11587 C  CB    A ILE B 2 316 ? 17.063  -25.347 18.326  0.20 41.11  ? 316 ILE B CB    1 
ATOM   11588 C  CB    B ILE B 2 316 ? 17.267  -25.458 18.154  0.80 41.46  ? 316 ILE B CB    1 
ATOM   11589 C  CG1   A ILE B 2 316 ? 16.064  -26.511 18.265  0.20 40.71  ? 316 ILE B CG1   1 
ATOM   11590 C  CG1   B ILE B 2 316 ? 16.770  -24.102 17.640  0.80 44.38  ? 316 ILE B CG1   1 
ATOM   11591 C  CG2   A ILE B 2 316 ? 18.067  -25.397 17.178  0.20 40.30  ? 316 ILE B CG2   1 
ATOM   11592 C  CG2   B ILE B 2 316 ? 16.123  -26.468 18.099  0.80 40.90  ? 316 ILE B CG2   1 
ATOM   11593 C  CD1   A ILE B 2 316 ? 16.551  -27.717 17.474  0.20 39.16  ? 316 ILE B CD1   1 
ATOM   11594 C  CD1   B ILE B 2 316 ? 16.376  -24.101 16.170  0.80 49.00  ? 316 ILE B CD1   1 
ATOM   11595 N  N     A PHE B 2 317 ? 17.702  -27.378 20.935  0.20 38.09  ? 317 PHE B N     1 
ATOM   11596 N  N     B PHE B 2 317 ? 17.878  -27.077 21.264  0.80 35.24  ? 317 PHE B N     1 
ATOM   11597 C  CA    A PHE B 2 317 ? 18.078  -28.723 21.340  0.20 38.76  ? 317 PHE B CA    1 
ATOM   11598 C  CA    B PHE B 2 317 ? 18.174  -28.394 21.809  0.80 37.96  ? 317 PHE B CA    1 
ATOM   11599 C  C     A PHE B 2 317 ? 17.087  -29.730 20.768  0.20 40.94  ? 317 PHE B C     1 
ATOM   11600 C  C     B PHE B 2 317 ? 17.141  -29.388 21.304  0.80 35.17  ? 317 PHE B C     1 
ATOM   11601 O  O     A PHE B 2 317 ? 15.943  -29.395 20.450  0.20 42.02  ? 317 PHE B O     1 
ATOM   11602 O  O     B PHE B 2 317 ? 15.955  -29.067 21.209  0.80 47.98  ? 317 PHE B O     1 
ATOM   11603 C  CB    A PHE B 2 317 ? 18.126  -28.843 22.869  0.20 39.97  ? 317 PHE B CB    1 
ATOM   11604 C  CB    B PHE B 2 317 ? 18.168  -28.358 23.339  0.80 35.79  ? 317 PHE B CB    1 
ATOM   11605 C  CG    A PHE B 2 317 ? 19.207  -28.018 23.513  0.20 43.04  ? 317 PHE B CG    1 
ATOM   11606 C  CG    B PHE B 2 317 ? 19.317  -27.590 23.936  0.80 46.11  ? 317 PHE B CG    1 
ATOM   11607 C  CD1   A PHE B 2 317 ? 19.037  -26.656 23.710  0.20 40.69  ? 317 PHE B CD1   1 
ATOM   11608 C  CD1   B PHE B 2 317 ? 19.254  -26.212 24.063  0.80 40.00  ? 317 PHE B CD1   1 
ATOM   11609 C  CD2   A PHE B 2 317 ? 20.390  -28.607 23.931  0.20 40.61  ? 317 PHE B CD2   1 
ATOM   11610 C  CD2   B PHE B 2 317 ? 20.458  -28.248 24.375  0.80 38.20  ? 317 PHE B CD2   1 
ATOM   11611 C  CE1   A PHE B 2 317 ? 20.029  -25.898 24.304  0.20 42.59  ? 317 PHE B CE1   1 
ATOM   11612 C  CE1   B PHE B 2 317 ? 20.304  -25.505 24.609  0.80 43.26  ? 317 PHE B CE1   1 
ATOM   11613 C  CE2   A PHE B 2 317 ? 21.384  -27.854 24.526  0.20 42.58  ? 317 PHE B CE2   1 
ATOM   11614 C  CE2   B PHE B 2 317 ? 21.507  -27.545 24.918  0.80 44.19  ? 317 PHE B CE2   1 
ATOM   11615 C  CZ    A PHE B 2 317 ? 21.203  -26.498 24.713  0.20 43.77  ? 317 PHE B CZ    1 
ATOM   11616 C  CZ    B PHE B 2 317 ? 21.429  -26.173 25.039  0.80 45.21  ? 317 PHE B CZ    1 
ATOM   11617 N  N     A ARG B 2 318 ? 17.543  -30.974 20.629  0.20 42.09  ? 318 ARG B N     1 
ATOM   11618 N  N     B ARG B 2 318 ? 17.603  -30.581 20.935  0.80 43.39  ? 318 ARG B N     1 
ATOM   11619 C  CA    A ARG B 2 318 ? 16.711  -32.054 20.107  0.20 45.32  ? 318 ARG B CA    1 
ATOM   11620 C  CA    B ARG B 2 318 ? 16.729  -31.628 20.431  0.80 45.02  ? 318 ARG B CA    1 
ATOM   11621 C  C     A ARG B 2 318 ? 17.033  -33.337 20.857  0.20 47.49  ? 318 ARG B C     1 
ATOM   11622 C  C     B ARG B 2 318 ? 16.978  -32.909 21.211  0.80 48.76  ? 318 ARG B C     1 
ATOM   11623 O  O     A ARG B 2 318 ? 18.179  -33.797 20.843  0.20 44.62  ? 318 ARG B O     1 
ATOM   11624 O  O     B ARG B 2 318 ? 18.128  -33.277 21.469  0.80 41.60  ? 318 ARG B O     1 
ATOM   11625 C  CB    A ARG B 2 318 ? 16.923  -32.244 18.600  0.20 42.59  ? 318 ARG B CB    1 
ATOM   11626 C  CB    B ARG B 2 318 ? 16.939  -31.872 18.923  0.80 43.20  ? 318 ARG B CB    1 
ATOM   11627 C  CG    A ARG B 2 318 ? 16.108  -31.287 17.740  0.20 42.34  ? 318 ARG B CG    1 
ATOM   11628 C  CG    B ARG B 2 318 ? 16.534  -30.683 18.046  0.80 40.57  ? 318 ARG B CG    1 
ATOM   11629 C  CD    A ARG B 2 318 ? 16.611  -31.248 16.306  0.20 43.87  ? 318 ARG B CD    1 
ATOM   11630 C  CD    B ARG B 2 318 ? 16.499  -31.056 16.576  0.80 44.54  ? 318 ARG B CD    1 
ATOM   11631 N  NE    A ARG B 2 318 ? 16.429  -32.516 15.609  0.20 44.11  ? 318 ARG B NE    1 
ATOM   11632 N  NE    B ARG B 2 318 ? 15.438  -32.010 16.280  0.80 41.63  ? 318 ARG B NE    1 
ATOM   11633 C  CZ    A ARG B 2 318 ? 15.463  -32.758 14.733  0.20 44.30  ? 318 ARG B CZ    1 
ATOM   11634 C  CZ    B ARG B 2 318 ? 15.222  -32.541 15.085  0.80 44.97  ? 318 ARG B CZ    1 
ATOM   11635 N  NH1   A ARG B 2 318 ? 14.569  -31.837 14.419  0.20 42.78  ? 318 ARG B NH1   1 
ATOM   11636 N  NH1   B ARG B 2 318 ? 15.978  -32.233 14.047  0.80 39.64  ? 318 ARG B NH1   1 
ATOM   11637 N  NH2   A ARG B 2 318 ? 15.395  -33.954 14.155  0.20 44.18  ? 318 ARG B NH2   1 
ATOM   11638 N  NH2   B ARG B 2 318 ? 14.223  -33.408 14.930  0.80 44.90  ? 318 ARG B NH2   1 
ATOM   11639 N  N     A GLY B 2 319 ? 16.021  -33.913 21.502  0.20 47.34  ? 319 GLY B N     1 
ATOM   11640 N  N     B GLY B 2 319 ? 15.898  -33.578 21.595  0.80 46.43  ? 319 GLY B N     1 
ATOM   11641 C  CA    A GLY B 2 319 ? 16.197  -35.140 22.254  0.20 51.12  ? 319 GLY B CA    1 
ATOM   11642 C  CA    B GLY B 2 319 ? 15.982  -34.814 22.338  0.80 52.85  ? 319 GLY B CA    1 
ATOM   11643 C  C     A GLY B 2 319 ? 15.466  -35.130 23.581  0.20 51.03  ? 319 GLY B C     1 
ATOM   11644 C  C     B GLY B 2 319 ? 15.176  -34.737 23.613  0.80 50.38  ? 319 GLY B C     1 
ATOM   11645 O  O     A GLY B 2 319 ? 14.883  -34.113 23.967  0.20 49.44  ? 319 GLY B O     1 
ATOM   11646 O  O     B GLY B 2 319 ? 14.381  -33.815 23.824  0.80 49.11  ? 319 GLY B O     1 
ATOM   11647 N  N     A ARG B 2 320 ? 15.488  -36.259 24.288  0.20 53.23  ? 320 ARG B N     1 
ATOM   11648 N  N     B ARG B 2 320 ? 15.392  -35.722 24.484  0.80 55.08  ? 320 ARG B N     1 
ATOM   11649 C  CA    A ARG B 2 320 ? 14.842  -36.365 25.593  0.20 52.67  ? 320 ARG B CA    1 
ATOM   11650 C  CA    B ARG B 2 320 ? 14.677  -35.840 25.750  0.80 51.69  ? 320 ARG B CA    1 
ATOM   11651 C  C     A ARG B 2 320 ? 15.786  -35.827 26.660  0.20 50.15  ? 320 ARG B C     1 
ATOM   11652 C  C     B ARG B 2 320 ? 15.593  -35.379 26.876  0.80 48.05  ? 320 ARG B C     1 
ATOM   11653 O  O     A ARG B 2 320 ? 16.781  -36.473 27.006  0.20 49.36  ? 320 ARG B O     1 
ATOM   11654 O  O     B ARG B 2 320 ? 16.650  -35.977 27.109  0.80 48.43  ? 320 ARG B O     1 
ATOM   11655 C  CB    A ARG B 2 320 ? 14.449  -37.810 25.885  0.20 53.23  ? 320 ARG B CB    1 
ATOM   11656 C  CB    B ARG B 2 320 ? 14.217  -37.280 25.980  0.80 51.79  ? 320 ARG B CB    1 
ATOM   11657 C  CG    A ARG B 2 320 ? 13.267  -38.312 25.074  0.20 54.25  ? 320 ARG B CG    1 
ATOM   11658 C  CG    B ARG B 2 320 ? 13.361  -37.487 27.211  0.80 60.25  ? 320 ARG B CG    1 
ATOM   11659 C  CD    A ARG B 2 320 ? 12.051  -37.422 25.272  0.20 55.42  ? 320 ARG B CD    1 
ATOM   11660 C  CD    B ARG B 2 320 ? 12.969  -38.954 27.342  0.80 66.96  ? 320 ARG B CD    1 
ATOM   11661 N  NE    A ARG B 2 320 ? 10.828  -38.047 24.785  0.20 55.47  ? 320 ARG B NE    1 
ATOM   11662 N  NE    B ARG B 2 320 ? 12.335  -39.464 26.130  0.80 64.92  ? 320 ARG B NE    1 
ATOM   11663 C  CZ    A ARG B 2 320 ? 10.384  -37.956 23.539  0.20 56.16  ? 320 ARG B CZ    1 
ATOM   11664 C  CZ    B ARG B 2 320 ? 11.024  -39.501 25.929  0.80 72.53  ? 320 ARG B CZ    1 
ATOM   11665 N  NH1   A ARG B 2 320 ? 11.050  -37.283 22.615  0.20 48.04  ? 320 ARG B NH1   1 
ATOM   11666 N  NH1   B ARG B 2 320 ? 10.170  -39.067 26.844  0.80 60.72  ? 320 ARG B NH1   1 
ATOM   11667 N  NH2   A ARG B 2 320 ? 9.243   -38.557 23.212  0.20 57.24  ? 320 ARG B NH2   1 
ATOM   11668 N  NH2   B ARG B 2 320 ? 10.557  -39.985 24.782  0.80 70.12  ? 320 ARG B NH2   1 
ATOM   11669 N  N     A MET B 2 321 ? 15.474  -34.643 27.184  0.20 48.91  ? 321 MET B N     1 
ATOM   11670 N  N     B MET B 2 321 ? 15.182  -34.326 27.576  0.80 48.59  ? 321 MET B N     1 
ATOM   11671 C  CA    A MET B 2 321 ? 16.280  -34.024 28.223  0.20 50.41  ? 321 MET B CA    1 
ATOM   11672 C  CA    B MET B 2 321 ? 16.047  -33.700 28.563  0.80 47.88  ? 321 MET B CA    1 
ATOM   11673 C  C     A MET B 2 321 ? 15.394  -33.094 29.037  0.20 53.25  ? 321 MET B C     1 
ATOM   11674 C  C     B MET B 2 321 ? 15.215  -32.792 29.453  0.80 55.64  ? 321 MET B C     1 
ATOM   11675 O  O     A MET B 2 321 ? 14.312  -32.694 28.600  0.20 55.21  ? 321 MET B O     1 
ATOM   11676 O  O     B MET B 2 321 ? 14.085  -32.424 29.119  0.80 58.17  ? 321 MET B O     1 
ATOM   11677 C  CB    A MET B 2 321 ? 17.471  -33.258 27.633  0.20 53.37  ? 321 MET B CB    1 
ATOM   11678 C  CB    B MET B 2 321 ? 17.156  -32.896 27.886  0.80 55.12  ? 321 MET B CB    1 
ATOM   11679 C  CG    A MET B 2 321 ? 17.088  -31.989 26.887  0.20 51.72  ? 321 MET B CG    1 
ATOM   11680 C  CG    B MET B 2 321 ? 16.620  -31.712 27.099  0.80 47.84  ? 321 MET B CG    1 
ATOM   11681 S  SD    A MET B 2 321 ? 18.479  -31.264 25.996  0.20 49.51  ? 321 MET B SD    1 
ATOM   11682 S  SD    B MET B 2 321 ? 17.844  -31.022 25.971  0.80 51.81  ? 321 MET B SD    1 
ATOM   11683 C  CE    A MET B 2 321 ? 18.727  -32.489 24.713  0.20 46.28  ? 321 MET B CE    1 
ATOM   11684 C  CE    B MET B 2 321 ? 17.814  -32.230 24.642  0.80 38.45  ? 321 MET B CE    1 
ATOM   11685 N  N     A SER B 2 322 ? 15.869  -32.755 30.233  0.20 54.97  ? 322 SER B N     1 
ATOM   11686 N  N     B SER B 2 322 ? 15.805  -32.420 30.584  0.80 55.45  ? 322 SER B N     1 
ATOM   11687 C  CA    A SER B 2 322 ? 15.125  -31.880 31.128  0.20 55.22  ? 322 SER B CA    1 
ATOM   11688 C  CA    B SER B 2 322 ? 15.153  -31.519 31.521  0.80 53.38  ? 322 SER B CA    1 
ATOM   11689 C  C     A SER B 2 322 ? 15.196  -30.439 30.640  0.20 59.10  ? 322 SER B C     1 
ATOM   11690 C  C     B SER B 2 322 ? 15.192  -30.089 30.994  0.80 60.42  ? 322 SER B C     1 
ATOM   11691 O  O     A SER B 2 322 ? 16.283  -29.915 30.377  0.20 57.86  ? 322 SER B O     1 
ATOM   11692 O  O     B SER B 2 322 ? 16.256  -29.577 30.629  0.80 57.59  ? 322 SER B O     1 
ATOM   11693 C  CB    A SER B 2 322 ? 15.673  -31.983 32.550  0.20 56.60  ? 322 SER B CB    1 
ATOM   11694 C  CB    B SER B 2 322 ? 15.830  -31.600 32.887  0.80 57.74  ? 322 SER B CB    1 
ATOM   11695 O  OG    A SER B 2 322 ? 14.996  -31.093 33.419  0.20 57.69  ? 322 SER B OG    1 
ATOM   11696 O  OG    B SER B 2 322 ? 15.428  -30.527 33.718  0.80 58.27  ? 322 SER B OG    1 
ATOM   11697 N  N     A MET B 2 323 ? 14.032  -29.797 30.527  0.20 61.84  ? 323 MET B N     1 
ATOM   11698 N  N     B MET B 2 323 ? 14.021  -29.449 30.945  0.80 63.86  ? 323 MET B N     1 
ATOM   11699 C  CA    A MET B 2 323 ? 14.000  -28.399 30.114  0.20 61.20  ? 323 MET B CA    1 
ATOM   11700 C  CA    B MET B 2 323 ? 13.967  -28.032 30.603  0.80 62.07  ? 323 MET B CA    1 
ATOM   11701 C  C     A MET B 2 323 ? 14.544  -27.480 31.200  0.20 61.23  ? 323 MET B C     1 
ATOM   11702 C  C     B MET B 2 323 ? 14.760  -27.195 31.597  0.80 62.03  ? 323 MET B C     1 
ATOM   11703 O  O     A MET B 2 323 ? 15.042  -26.391 30.895  0.20 59.44  ? 323 MET B O     1 
ATOM   11704 O  O     B MET B 2 323 ? 15.309  -26.148 31.233  0.80 59.20  ? 323 MET B O     1 
ATOM   11705 C  CB    A MET B 2 323 ? 12.575  -27.994 29.739  0.20 65.16  ? 323 MET B CB    1 
ATOM   11706 C  CB    B MET B 2 323 ? 12.511  -27.565 30.550  0.80 70.93  ? 323 MET B CB    1 
ATOM   11707 C  CG    A MET B 2 323 ? 11.943  -28.862 28.663  0.20 63.66  ? 323 MET B CG    1 
ATOM   11708 C  CG    B MET B 2 323 ? 12.311  -26.105 30.152  0.80 67.90  ? 323 MET B CG    1 
ATOM   11709 S  SD    A MET B 2 323 ? 10.267  -28.334 28.259  0.20 73.15  ? 323 MET B SD    1 
ATOM   11710 S  SD    B MET B 2 323 ? 11.983  -25.900 28.393  0.80 83.85  ? 323 MET B SD    1 
ATOM   11711 C  CE    A MET B 2 323 ? 9.775   -29.601 27.093  0.20 55.07  ? 323 MET B CE    1 
ATOM   11712 C  CE    B MET B 2 323 ? 10.566  -26.977 28.185  0.80 68.69  ? 323 MET B CE    1 
ATOM   11713 N  N     A LYS B 2 324 ? 14.456  -27.896 32.466  0.20 61.66  ? 324 LYS B N     1 
ATOM   11714 N  N     B LYS B 2 324 ? 14.839  -27.643 32.852  0.80 62.91  ? 324 LYS B N     1 
ATOM   11715 C  CA    A LYS B 2 324 ? 15.007  -27.085 33.547  0.20 60.51  ? 324 LYS B CA    1 
ATOM   11716 C  CA    B LYS B 2 324 ? 15.610  -26.918 33.854  0.80 59.43  ? 324 LYS B CA    1 
ATOM   11717 C  C     A LYS B 2 324 ? 16.530  -27.097 33.523  0.20 58.01  ? 324 LYS B C     1 
ATOM   11718 C  C     B LYS B 2 324 ? 17.108  -27.113 33.653  0.80 57.17  ? 324 LYS B C     1 
ATOM   11719 O  O     A LYS B 2 324 ? 17.169  -26.062 33.748  0.20 58.54  ? 324 LYS B O     1 
ATOM   11720 O  O     B LYS B 2 324 ? 17.887  -26.175 33.845  0.80 58.78  ? 324 LYS B O     1 
ATOM   11721 C  CB    A LYS B 2 324 ? 14.485  -27.580 34.897  0.20 61.93  ? 324 LYS B CB    1 
ATOM   11722 C  CB    B LYS B 2 324 ? 15.193  -27.361 35.260  0.80 64.60  ? 324 LYS B CB    1 
ATOM   11723 C  CG    A LYS B 2 324 ? 15.122  -26.895 36.097  0.20 63.55  ? 324 LYS B CG    1 
ATOM   11724 C  CG    B LYS B 2 324 ? 15.799  -26.536 36.393  0.80 62.73  ? 324 LYS B CG    1 
ATOM   11725 C  CD    A LYS B 2 324 ? 14.551  -27.418 37.406  0.20 62.67  ? 324 LYS B CD    1 
ATOM   11726 C  CD    B LYS B 2 324 ? 15.355  -27.058 37.756  0.80 67.89  ? 324 LYS B CD    1 
ATOM   11727 C  CE    A LYS B 2 324 ? 15.332  -26.885 38.597  0.20 65.04  ? 324 LYS B CE    1 
ATOM   11728 C  CE    B LYS B 2 324 ? 15.987  -26.270 38.895  0.80 66.88  ? 324 LYS B CE    1 
ATOM   11729 N  NZ    A LYS B 2 324 ? 15.372  -25.397 38.619  0.20 61.82  ? 324 LYS B NZ    1 
ATOM   11730 N  NZ    B LYS B 2 324 ? 15.534  -26.755 40.232  0.80 65.10  ? 324 LYS B NZ    1 
ATOM   11731 N  N     A GLU B 2 325 ? 17.130  -28.259 33.251  0.20 55.68  ? 325 GLU B N     1 
ATOM   11732 N  N     B GLU B 2 325 ? 17.527  -28.320 33.265  0.80 54.06  ? 325 GLU B N     1 
ATOM   11733 C  CA    A GLU B 2 325 ? 18.585  -28.345 33.186  0.20 57.13  ? 325 GLU B CA    1 
ATOM   11734 C  CA    B GLU B 2 325 ? 18.952  -28.583 33.086  0.80 56.63  ? 325 GLU B CA    1 
ATOM   11735 C  C     A GLU B 2 325 ? 19.143  -27.495 32.053  0.20 57.66  ? 325 GLU B C     1 
ATOM   11736 C  C     B GLU B 2 325 ? 19.523  -27.747 31.947  0.80 58.78  ? 325 GLU B C     1 
ATOM   11737 O  O     A GLU B 2 325 ? 20.235  -26.929 32.181  0.20 56.85  ? 325 GLU B O     1 
ATOM   11738 O  O     B GLU B 2 325 ? 20.653  -27.252 32.033  0.80 59.02  ? 325 GLU B O     1 
ATOM   11739 C  CB    A GLU B 2 325 ? 19.017  -29.802 33.022  0.20 56.13  ? 325 GLU B CB    1 
ATOM   11740 C  CB    B GLU B 2 325 ? 19.185  -30.072 32.828  0.80 54.87  ? 325 GLU B CB    1 
ATOM   11741 C  CG    A GLU B 2 325 ? 20.520  -30.019 33.070  0.20 59.64  ? 325 GLU B CG    1 
ATOM   11742 C  CG    B GLU B 2 325 ? 20.628  -30.522 33.011  0.80 61.18  ? 325 GLU B CG    1 
ATOM   11743 C  CD    A GLU B 2 325 ? 20.908  -31.465 32.825  0.20 61.26  ? 325 GLU B CD    1 
ATOM   11744 C  CD    B GLU B 2 325 ? 20.896  -31.877 32.380  0.80 62.52  ? 325 GLU B CD    1 
ATOM   11745 O  OE1   A GLU B 2 325 ? 19.999  -32.309 32.673  0.20 61.19  ? 325 GLU B OE1   1 
ATOM   11746 O  OE1   B GLU B 2 325 ? 19.927  -32.533 31.940  0.80 60.25  ? 325 GLU B OE1   1 
ATOM   11747 O  OE2   A GLU B 2 325 ? 22.121  -31.756 32.780  0.20 64.32  ? 325 GLU B OE2   1 
ATOM   11748 O  OE2   B GLU B 2 325 ? 22.076  -32.282 32.311  0.80 68.38  ? 325 GLU B OE2   1 
ATOM   11749 N  N     A VAL B 2 326 ? 18.411  -27.390 30.944  0.20 55.36  ? 326 VAL B N     1 
ATOM   11750 N  N     B VAL B 2 326 ? 18.752  -27.579 30.872  0.80 54.98  ? 326 VAL B N     1 
ATOM   11751 C  CA    A VAL B 2 326 ? 18.868  -26.579 29.821  0.20 52.94  ? 326 VAL B CA    1 
ATOM   11752 C  CA    B VAL B 2 326 ? 19.168  -26.700 29.787  0.80 51.45  ? 326 VAL B CA    1 
ATOM   11753 C  C     A VAL B 2 326 ? 18.911  -25.106 30.210  0.20 54.68  ? 326 VAL B C     1 
ATOM   11754 C  C     B VAL B 2 326 ? 19.187  -25.254 30.259  0.80 54.20  ? 326 VAL B C     1 
ATOM   11755 O  O     A VAL B 2 326 ? 19.884  -24.400 29.922  0.20 53.07  ? 326 VAL B O     1 
ATOM   11756 O  O     B VAL B 2 326 ? 20.163  -24.528 30.040  0.80 52.67  ? 326 VAL B O     1 
ATOM   11757 C  CB    A VAL B 2 326 ? 17.971  -26.811 28.592  0.20 54.25  ? 326 VAL B CB    1 
ATOM   11758 C  CB    B VAL B 2 326 ? 18.250  -26.882 28.567  0.80 54.84  ? 326 VAL B CB    1 
ATOM   11759 C  CG1   A VAL B 2 326 ? 18.384  -25.893 27.457  0.20 50.34  ? 326 VAL B CG1   1 
ATOM   11760 C  CG1   B VAL B 2 326 ? 18.360  -25.684 27.649  0.80 50.17  ? 326 VAL B CG1   1 
ATOM   11761 C  CG2   A VAL B 2 326 ? 18.037  -28.265 28.155  0.20 52.37  ? 326 VAL B CG2   1 
ATOM   11762 C  CG2   B VAL B 2 326 ? 18.616  -28.147 27.825  0.80 52.29  ? 326 VAL B CG2   1 
ATOM   11763 N  N     A ASP B 2 327 ? 17.856  -24.623 30.874  0.20 55.59  ? 327 ASP B N     1 
ATOM   11764 N  N     B ASP B 2 327 ? 18.102  -24.815 30.911  0.80 56.40  ? 327 ASP B N     1 
ATOM   11765 C  CA    A ASP B 2 327 ? 17.818  -23.224 31.290  0.20 52.51  ? 327 ASP B CA    1 
ATOM   11766 C  CA    B ASP B 2 327 ? 18.048  -23.455 31.438  0.80 51.04  ? 327 ASP B CA    1 
ATOM   11767 C  C     A ASP B 2 327 ? 18.943  -22.909 32.268  0.20 53.74  ? 327 ASP B C     1 
ATOM   11768 C  C     B ASP B 2 327 ? 19.214  -23.185 32.380  0.80 52.91  ? 327 ASP B C     1 
ATOM   11769 O  O     A ASP B 2 327 ? 19.562  -21.842 32.190  0.20 52.91  ? 327 ASP B O     1 
ATOM   11770 O  O     B ASP B 2 327 ? 19.804  -22.099 32.353  0.80 51.47  ? 327 ASP B O     1 
ATOM   11771 C  CB    A ASP B 2 327 ? 16.461  -22.896 31.911  0.20 55.22  ? 327 ASP B CB    1 
ATOM   11772 C  CB    B ASP B 2 327 ? 16.719  -23.217 32.159  0.80 53.65  ? 327 ASP B CB    1 
ATOM   11773 C  CG    A ASP B 2 327 ? 15.322  -22.991 30.913  0.20 57.27  ? 327 ASP B CG    1 
ATOM   11774 C  CG    B ASP B 2 327 ? 15.548  -23.029 31.204  0.80 57.17  ? 327 ASP B CG    1 
ATOM   11775 O  OD1   A ASP B 2 327 ? 15.582  -22.891 29.697  0.20 58.32  ? 327 ASP B OD1   1 
ATOM   11776 O  OD1   B ASP B 2 327 ? 15.696  -23.294 29.994  0.80 59.23  ? 327 ASP B OD1   1 
ATOM   11777 O  OD2   A ASP B 2 327 ? 14.165  -23.160 31.347  0.20 62.70  ? 327 ASP B OD2   1 
ATOM   11778 O  OD2   B ASP B 2 327 ? 14.468  -22.613 31.674  0.80 67.53  ? 327 ASP B OD2   1 
ATOM   11779 N  N     A GLU B 2 328 ? 19.221  -23.826 33.197  0.20 54.34  ? 328 GLU B N     1 
ATOM   11780 N  N     B GLU B 2 328 ? 19.566  -24.165 33.216  0.80 53.06  ? 328 GLU B N     1 
ATOM   11781 C  CA    A GLU B 2 328 ? 20.313  -23.610 34.140  0.20 56.68  ? 328 GLU B CA    1 
ATOM   11782 C  CA    B GLU B 2 328 ? 20.656  -23.966 34.166  0.80 57.55  ? 328 GLU B CA    1 
ATOM   11783 C  C     A GLU B 2 328 ? 21.662  -23.623 33.432  0.20 57.25  ? 328 GLU B C     1 
ATOM   11784 C  C     B GLU B 2 328 ? 22.004  -23.905 33.457  0.80 59.08  ? 328 GLU B C     1 
ATOM   11785 O  O     A GLU B 2 328 ? 22.566  -22.861 33.793  0.20 55.16  ? 328 GLU B O     1 
ATOM   11786 O  O     B GLU B 2 328 ? 22.833  -23.040 33.767  0.80 54.73  ? 328 GLU B O     1 
ATOM   11787 C  CB    A GLU B 2 328 ? 20.276  -24.671 35.240  0.20 58.02  ? 328 GLU B CB    1 
ATOM   11788 C  CB    B GLU B 2 328 ? 20.660  -25.074 35.221  0.80 57.43  ? 328 GLU B CB    1 
ATOM   11789 C  CG    A GLU B 2 328 ? 19.090  -24.557 36.185  0.20 61.35  ? 328 GLU B CG    1 
ATOM   11790 C  CG    B GLU B 2 328 ? 19.663  -24.883 36.365  0.80 63.40  ? 328 GLU B CG    1 
ATOM   11791 C  CD    A GLU B 2 328 ? 19.073  -25.655 37.234  0.20 64.10  ? 328 GLU B CD    1 
ATOM   11792 C  CD    B GLU B 2 328 ? 20.024  -25.697 37.608  0.80 67.18  ? 328 GLU B CD    1 
ATOM   11793 O  OE1   A GLU B 2 328 ? 19.662  -26.728 36.985  0.20 60.68  ? 328 GLU B OE1   1 
ATOM   11794 O  OE1   B GLU B 2 328 ? 21.230  -25.945 37.837  0.80 59.71  ? 328 GLU B OE1   1 
ATOM   11795 O  OE2   A GLU B 2 328 ? 18.472  -25.444 38.310  0.20 64.62  ? 328 GLU B OE2   1 
ATOM   11796 O  OE2   B GLU B 2 328 ? 19.101  -26.088 38.358  0.80 67.76  ? 328 GLU B OE2   1 
ATOM   11797 N  N     A GLN B 2 329 ? 21.813  -24.477 32.416  0.20 56.91  ? 329 GLN B N     1 
ATOM   11798 N  N     B GLN B 2 329 ? 22.244  -24.816 32.505  0.80 58.93  ? 329 GLN B N     1 
ATOM   11799 C  CA    A GLN B 2 329 ? 23.091  -24.579 31.722  0.20 54.62  ? 329 GLN B CA    1 
ATOM   11800 C  CA    B GLN B 2 329 ? 23.535  -24.840 31.826  0.80 52.40  ? 329 GLN B CA    1 
ATOM   11801 C  C     A GLN B 2 329 ? 23.310  -23.409 30.771  0.20 54.88  ? 329 GLN B C     1 
ATOM   11802 C  C     B GLN B 2 329 ? 23.709  -23.627 30.923  0.80 56.07  ? 329 GLN B C     1 
ATOM   11803 O  O     A GLN B 2 329 ? 24.437  -22.919 30.639  0.20 53.69  ? 329 GLN B O     1 
ATOM   11804 O  O     B GLN B 2 329 ? 24.795  -23.039 30.877  0.80 52.22  ? 329 GLN B O     1 
ATOM   11805 C  CB    A GLN B 2 329 ? 23.173  -25.904 30.965  0.20 56.00  ? 329 GLN B CB    1 
ATOM   11806 C  CB    B GLN B 2 329 ? 23.696  -26.133 31.032  0.80 55.72  ? 329 GLN B CB    1 
ATOM   11807 C  CG    A GLN B 2 329 ? 24.506  -26.614 31.121  0.20 56.39  ? 329 GLN B CG    1 
ATOM   11808 C  CG    B GLN B 2 329 ? 23.956  -27.348 31.906  0.80 57.30  ? 329 GLN B CG    1 
ATOM   11809 C  CD    A GLN B 2 329 ? 24.760  -27.062 32.549  0.20 58.42  ? 329 GLN B CD    1 
ATOM   11810 C  CD    B GLN B 2 329 ? 25.144  -27.152 32.835  0.80 59.44  ? 329 GLN B CD    1 
ATOM   11811 O  OE1   A GLN B 2 329 ? 25.895  -27.046 33.025  0.20 58.88  ? 329 GLN B OE1   1 
ATOM   11812 O  OE1   B GLN B 2 329 ? 26.291  -27.059 32.391  0.80 61.98  ? 329 GLN B OE1   1 
ATOM   11813 N  NE2   A GLN B 2 329 ? 23.700  -27.472 33.237  0.20 57.96  ? 329 GLN B NE2   1 
ATOM   11814 N  NE2   B GLN B 2 329 ? 24.871  -27.082 34.132  0.80 64.23  ? 329 GLN B NE2   1 
ATOM   11815 N  N     A MET B 2 330 ? 22.249  -22.950 30.102  0.20 52.18  ? 330 MET B N     1 
ATOM   11816 N  N     B MET B 2 330 ? 22.652  -23.232 30.202  0.80 52.54  ? 330 MET B N     1 
ATOM   11817 C  CA    A MET B 2 330 ? 22.385  -21.807 29.204  0.20 51.74  ? 330 MET B CA    1 
ATOM   11818 C  CA    B MET B 2 330 ? 22.731  -22.016 29.398  0.80 51.47  ? 330 MET B CA    1 
ATOM   11819 C  C     A MET B 2 330 ? 22.748  -20.543 29.972  0.20 54.54  ? 330 MET B C     1 
ATOM   11820 C  C     B MET B 2 330 ? 23.074  -20.815 30.264  0.80 54.87  ? 330 MET B C     1 
ATOM   11821 O  O     A MET B 2 330 ? 23.541  -19.725 29.491  0.20 54.10  ? 330 MET B O     1 
ATOM   11822 O  O     B MET B 2 330 ? 23.875  -19.959 29.865  0.80 53.47  ? 330 MET B O     1 
ATOM   11823 C  CB    A MET B 2 330 ? 21.095  -21.603 28.408  0.20 45.85  ? 330 MET B CB    1 
ATOM   11824 C  CB    B MET B 2 330 ? 21.418  -21.774 28.648  0.80 44.63  ? 330 MET B CB    1 
ATOM   11825 C  CG    A MET B 2 330 ? 20.836  -22.676 27.361  0.20 50.01  ? 330 MET B CG    1 
ATOM   11826 C  CG    B MET B 2 330 ? 21.254  -22.612 27.387  0.80 51.26  ? 330 MET B CG    1 
ATOM   11827 S  SD    A MET B 2 330 ? 22.140  -22.764 26.117  0.20 50.56  ? 330 MET B SD    1 
ATOM   11828 S  SD    B MET B 2 330 ? 22.655  -22.465 26.252  0.80 49.23  ? 330 MET B SD    1 
ATOM   11829 C  CE    A MET B 2 330 ? 22.067  -21.107 25.445  0.20 47.01  ? 330 MET B CE    1 
ATOM   11830 C  CE    B MET B 2 330 ? 22.810  -20.684 26.123  0.80 43.49  ? 330 MET B CE    1 
ATOM   11831 N  N     A LEU B 2 331 ? 22.181  -20.366 31.168  0.20 53.61  ? 331 LEU B N     1 
ATOM   11832 N  N     B LEU B 2 331 ? 22.472  -20.735 31.453  0.80 53.21  ? 331 LEU B N     1 
ATOM   11833 C  CA    A LEU B 2 331 ? 22.561  -19.229 31.999  0.20 55.56  ? 331 LEU B CA    1 
ATOM   11834 C  CA    B LEU B 2 331 ? 22.842  -19.707 32.419  0.80 56.32  ? 331 LEU B CA    1 
ATOM   11835 C  C     A LEU B 2 331 ? 24.015  -19.320 32.441  0.20 56.28  ? 331 LEU B C     1 
ATOM   11836 C  C     B LEU B 2 331 ? 24.341  -19.740 32.700  0.80 56.13  ? 331 LEU B C     1 
ATOM   11837 O  O     A LEU B 2 331 ? 24.687  -18.290 32.567  0.20 58.04  ? 331 LEU B O     1 
ATOM   11838 O  O     B LEU B 2 331 ? 25.016  -18.706 32.661  0.80 58.09  ? 331 LEU B O     1 
ATOM   11839 C  CB    A LEU B 2 331 ? 21.641  -19.133 33.216  0.20 55.66  ? 331 LEU B CB    1 
ATOM   11840 C  CB    B LEU B 2 331 ? 22.044  -19.904 33.711  0.80 58.03  ? 331 LEU B CB    1 
ATOM   11841 C  CG    A LEU B 2 331 ? 20.228  -18.606 32.966  0.20 55.90  ? 331 LEU B CG    1 
ATOM   11842 C  CG    B LEU B 2 331 ? 21.586  -18.673 34.492  0.80 61.84  ? 331 LEU B CG    1 
ATOM   11843 C  CD1   A LEU B 2 331 ? 19.408  -18.642 34.246  0.20 53.77  ? 331 LEU B CD1   1 
ATOM   11844 C  CD1   B LEU B 2 331 ? 20.422  -18.000 33.785  0.80 59.00  ? 331 LEU B CD1   1 
ATOM   11845 C  CD2   A LEU B 2 331 ? 20.281  -17.193 32.401  0.20 55.22  ? 331 LEU B CD2   1 
ATOM   11846 C  CD2   B LEU B 2 331 ? 21.205  -19.052 35.922  0.80 63.94  ? 331 LEU B CD2   1 
ATOM   11847 N  N     A ASN B 2 332 ? 24.518  -20.536 32.674  0.20 55.97  ? 332 ASN B N     1 
ATOM   11848 N  N     B ASN B 2 332 ? 24.876  -20.935 32.970  0.80 53.25  ? 332 ASN B N     1 
ATOM   11849 C  CA    A ASN B 2 332 ? 25.908  -20.699 33.090  0.20 57.57  ? 332 ASN B CA    1 
ATOM   11850 C  CA    B ASN B 2 332 ? 26.296  -21.083 33.276  0.80 58.02  ? 332 ASN B CA    1 
ATOM   11851 C  C     A ASN B 2 332 ? 26.871  -20.258 31.995  0.20 59.61  ? 332 ASN B C     1 
ATOM   11852 C  C     B ASN B 2 332 ? 27.167  -20.550 32.145  0.80 60.29  ? 332 ASN B C     1 
ATOM   11853 O  O     A ASN B 2 332 ? 27.881  -19.603 32.277  0.20 60.88  ? 332 ASN B O     1 
ATOM   11854 O  O     B ASN B 2 332 ? 28.001  -19.662 32.354  0.80 60.89  ? 332 ASN B O     1 
ATOM   11855 C  CB    A ASN B 2 332 ? 26.173  -22.153 33.480  0.20 59.43  ? 332 ASN B CB    1 
ATOM   11856 C  CB    B ASN B 2 332 ? 26.620  -22.553 33.556  0.80 60.28  ? 332 ASN B CB    1 
ATOM   11857 C  CG    A ASN B 2 332 ? 27.604  -22.384 33.931  0.20 62.06  ? 332 ASN B CG    1 
ATOM   11858 C  CG    B ASN B 2 332 ? 26.344  -22.950 34.997  0.80 68.02  ? 332 ASN B CG    1 
ATOM   11859 O  OD1   A ASN B 2 332 ? 28.264  -21.474 34.433  0.20 61.64  ? 332 ASN B OD1   1 
ATOM   11860 O  OD1   B ASN B 2 332 ? 26.520  -22.149 35.919  0.80 73.66  ? 332 ASN B OD1   1 
ATOM   11861 N  ND2   A ASN B 2 332 ? 28.091  -23.607 33.752  0.20 62.62  ? 332 ASN B ND2   1 
ATOM   11862 N  ND2   B ASN B 2 332 ? 25.917  -24.195 35.197  0.80 56.16  ? 332 ASN B ND2   1 
ATOM   11863 N  N     A VAL B 2 333 ? 26.578  -20.612 30.741  0.20 57.30  ? 333 VAL B N     1 
ATOM   11864 N  N     B VAL B 2 333 ? 26.982  -21.085 30.932  0.80 53.08  ? 333 VAL B N     1 
ATOM   11865 C  CA    A VAL B 2 333 ? 27.443  -20.214 29.633  0.20 58.12  ? 333 VAL B CA    1 
ATOM   11866 C  CA    B VAL B 2 333 ? 27.777  -20.657 29.780  0.80 60.21  ? 333 VAL B CA    1 
ATOM   11867 C  C     A VAL B 2 333 ? 27.455  -18.698 29.485  0.20 58.60  ? 333 VAL B C     1 
ATOM   11868 C  C     B VAL B 2 333 ? 27.656  -19.156 29.551  0.80 58.67  ? 333 VAL B C     1 
ATOM   11869 O  O     A VAL B 2 333 ? 28.486  -18.097 29.160  0.20 58.63  ? 333 VAL B O     1 
ATOM   11870 O  O     B VAL B 2 333 ? 28.610  -18.509 29.101  0.80 58.76  ? 333 VAL B O     1 
ATOM   11871 C  CB    A VAL B 2 333 ? 26.998  -20.908 28.331  0.20 53.72  ? 333 VAL B CB    1 
ATOM   11872 C  CB    B VAL B 2 333 ? 27.366  -21.449 28.520  0.80 51.64  ? 333 VAL B CB    1 
ATOM   11873 C  CG1   A VAL B 2 333 ? 27.947  -20.567 27.193  0.20 54.99  ? 333 VAL B CG1   1 
ATOM   11874 C  CG1   B VAL B 2 333 ? 28.293  -21.129 27.358  0.80 55.81  ? 333 VAL B CG1   1 
ATOM   11875 C  CG2   A VAL B 2 333 ? 26.922  -22.412 28.531  0.20 56.68  ? 333 VAL B CG2   1 
ATOM   11876 C  CG2   B VAL B 2 333 ? 27.377  -22.937 28.807  0.80 60.32  ? 333 VAL B CG2   1 
ATOM   11877 N  N     A GLN B 2 334 ? 26.314  -18.055 29.732  0.20 56.28  ? 334 GLN B N     1 
ATOM   11878 N  N     B GLN B 2 334 ? 26.496  -18.574 29.860  0.80 56.16  ? 334 GLN B N     1 
ATOM   11879 C  CA    A GLN B 2 334 ? 26.218  -16.606 29.638  0.20 56.59  ? 334 GLN B CA    1 
ATOM   11880 C  CA    B GLN B 2 334 ? 26.306  -17.142 29.680  0.80 54.17  ? 334 GLN B CA    1 
ATOM   11881 C  C     A GLN B 2 334 ? 26.822  -15.890 30.840  0.20 61.68  ? 334 GLN B C     1 
ATOM   11882 C  C     B GLN B 2 334 ? 27.001  -16.315 30.759  0.80 63.21  ? 334 GLN B C     1 
ATOM   11883 O  O     A GLN B 2 334 ? 26.910  -14.657 30.825  0.20 59.98  ? 334 GLN B O     1 
ATOM   11884 O  O     B GLN B 2 334 ? 27.169  -15.103 30.580  0.80 61.67  ? 334 GLN B O     1 
ATOM   11885 C  CB    A GLN B 2 334 ? 24.753  -16.195 29.466  0.20 58.47  ? 334 GLN B CB    1 
ATOM   11886 C  CB    B GLN B 2 334 ? 24.808  -16.823 29.647  0.80 61.22  ? 334 GLN B CB    1 
ATOM   11887 C  CG    A GLN B 2 334 ? 24.085  -16.819 28.248  0.20 50.90  ? 334 GLN B CG    1 
ATOM   11888 C  CG    B GLN B 2 334 ? 24.432  -15.550 28.891  0.80 55.33  ? 334 GLN B CG    1 
ATOM   11889 C  CD    A GLN B 2 334 ? 22.580  -16.630 28.236  0.20 49.54  ? 334 GLN B CD    1 
ATOM   11890 C  CD    B GLN B 2 334 ? 22.927  -15.413 28.709  0.80 56.76  ? 334 GLN B CD    1 
ATOM   11891 O  OE1   A GLN B 2 334 ? 22.082  -15.513 28.085  0.20 46.23  ? 334 GLN B OE1   1 
ATOM   11892 O  OE1   B GLN B 2 334 ? 22.353  -14.345 28.937  0.80 60.81  ? 334 GLN B OE1   1 
ATOM   11893 N  NE2   A GLN B 2 334 ? 21.846  -17.725 28.396  0.20 45.16  ? 334 GLN B NE2   1 
ATOM   11894 N  NE2   B GLN B 2 334 ? 22.279  -16.502 28.299  0.80 49.41  ? 334 GLN B NE2   1 
ATOM   11895 N  N     A ASN B 2 335 ? 27.240  -16.623 31.871  0.20 61.05  ? 335 ASN B N     1 
ATOM   11896 N  N     B ASN B 2 335 ? 27.416  -16.937 31.866  0.80 60.69  ? 335 ASN B N     1 
ATOM   11897 C  CA    A ASN B 2 335 ? 27.904  -16.043 33.033  0.20 62.73  ? 335 ASN B CA    1 
ATOM   11898 C  CA    B ASN B 2 335 ? 28.128  -16.222 32.921  0.80 62.97  ? 335 ASN B CA    1 
ATOM   11899 C  C     A ASN B 2 335 ? 29.420  -16.184 32.967  0.20 62.09  ? 335 ASN B C     1 
ATOM   11900 C  C     B ASN B 2 335 ? 29.642  -16.269 32.746  0.80 61.67  ? 335 ASN B C     1 
ATOM   11901 O  O     A ASN B 2 335 ? 30.144  -15.214 33.212  0.20 66.21  ? 335 ASN B O     1 
ATOM   11902 O  O     B ASN B 2 335 ? 30.321  -15.264 32.981  0.80 67.73  ? 335 ASN B O     1 
ATOM   11903 C  CB    A ASN B 2 335 ? 27.375  -16.686 34.321  0.20 62.83  ? 335 ASN B CB    1 
ATOM   11904 C  CB    B ASN B 2 335 ? 27.753  -16.785 34.295  0.80 62.05  ? 335 ASN B CB    1 
ATOM   11905 C  CG    A ASN B 2 335 ? 25.914  -16.370 34.572  0.20 64.18  ? 335 ASN B CG    1 
ATOM   11906 C  CG    B ASN B 2 335 ? 26.331  -16.440 34.699  0.80 65.42  ? 335 ASN B CG    1 
ATOM   11907 O  OD1   A ASN B 2 335 ? 25.401  -15.351 34.109  0.20 62.05  ? 335 ASN B OD1   1 
ATOM   11908 O  OD1   B ASN B 2 335 ? 25.640  -17.239 35.336  0.80 66.91  ? 335 ASN B OD1   1 
ATOM   11909 N  ND2   A ASN B 2 335 ? 25.236  -17.243 35.308  0.20 65.51  ? 335 ASN B ND2   1 
ATOM   11910 N  ND2   B ASN B 2 335 ? 25.883  -15.246 34.324  0.80 60.62  ? 335 ASN B ND2   1 
ATOM   11911 N  N     A LYS B 2 336 ? 29.918  -17.379 32.641  0.20 63.09  ? 336 LYS B N     1 
ATOM   11912 N  N     B LYS B 2 336 ? 30.189  -17.418 32.341  0.80 63.57  ? 336 LYS B N     1 
ATOM   11913 C  CA    A LYS B 2 336 ? 31.356  -17.575 32.503  0.20 65.17  ? 336 LYS B CA    1 
ATOM   11914 C  CA    B LYS B 2 336 ? 31.633  -17.528 32.151  0.80 68.01  ? 336 LYS B CA    1 
ATOM   11915 C  C     A LYS B 2 336 ? 31.911  -16.921 31.244  0.20 64.28  ? 336 LYS B C     1 
ATOM   11916 C  C     B LYS B 2 336 ? 32.103  -16.798 30.896  0.80 65.45  ? 336 LYS B C     1 
ATOM   11917 O  O     A LYS B 2 336 ? 33.103  -16.599 31.202  0.20 64.74  ? 336 LYS B O     1 
ATOM   11918 O  O     B LYS B 2 336 ? 33.260  -16.367 30.829  0.80 66.64  ? 336 LYS B O     1 
ATOM   11919 C  CB    A LYS B 2 336 ? 31.688  -19.068 32.498  0.20 64.22  ? 336 LYS B CB    1 
ATOM   11920 C  CB    B LYS B 2 336 ? 32.042  -19.001 32.088  0.80 62.70  ? 336 LYS B CB    1 
ATOM   11921 C  CG    A LYS B 2 336 ? 31.232  -19.818 33.741  0.20 67.55  ? 336 LYS B CG    1 
ATOM   11922 C  CG    B LYS B 2 336 ? 31.755  -19.783 33.361  0.80 70.43  ? 336 LYS B CG    1 
ATOM   11923 C  CD    A LYS B 2 336 ? 31.560  -21.301 33.636  0.20 70.47  ? 336 LYS B CD    1 
ATOM   11924 C  CD    B LYS B 2 336 ? 31.932  -21.282 33.139  0.80 72.21  ? 336 LYS B CD    1 
ATOM   11925 C  CE    A LYS B 2 336 ? 30.911  -21.925 32.408  0.20 63.54  ? 336 LYS B CE    1 
ATOM   11926 C  CE    B LYS B 2 336 ? 31.811  -22.057 34.445  0.80 75.96  ? 336 LYS B CE    1 
ATOM   11927 N  NZ    A LYS B 2 336 ? 31.269  -23.361 32.248  0.20 57.49  ? 336 LYS B NZ    1 
ATOM   11928 N  NZ    B LYS B 2 336 ? 30.540  -21.757 35.162  0.80 70.15  ? 336 LYS B NZ    1 
ATOM   11929 N  N     A ASN B 2 337 ? 31.080  -16.721 30.224  0.20 59.61  ? 337 ASN B N     1 
ATOM   11930 N  N     B ASN B 2 337 ? 31.234  -16.655 29.894  0.80 58.19  ? 337 ASN B N     1 
ATOM   11931 C  CA    A ASN B 2 337 ? 31.482  -16.094 28.972  0.20 54.62  ? 337 ASN B CA    1 
ATOM   11932 C  CA    B ASN B 2 337 ? 31.573  -15.982 28.647  0.80 52.73  ? 337 ASN B CA    1 
ATOM   11933 C  C     A ASN B 2 337 ? 30.708  -14.801 28.744  0.20 54.63  ? 337 ASN B C     1 
ATOM   11934 C  C     B ASN B 2 337 ? 30.976  -14.580 28.567  0.80 56.39  ? 337 ASN B C     1 
ATOM   11935 O  O     A ASN B 2 337 ? 30.322  -14.474 27.619  0.20 50.61  ? 337 ASN B O     1 
ATOM   11936 O  O     B ASN B 2 337 ? 30.692  -14.087 27.469  0.80 50.59  ? 337 ASN B O     1 
ATOM   11937 C  CB    A ASN B 2 337 ? 31.287  -17.051 27.799  0.20 53.74  ? 337 ASN B CB    1 
ATOM   11938 C  CB    B ASN B 2 337 ? 31.111  -16.820 27.458  0.80 52.41  ? 337 ASN B CB    1 
ATOM   11939 C  CG    A ASN B 2 337 ? 31.974  -18.384 28.016  0.20 58.79  ? 337 ASN B CG    1 
ATOM   11940 C  CG    B ASN B 2 337 ? 31.648  -18.233 27.498  0.80 60.91  ? 337 ASN B CG    1 
ATOM   11941 O  OD1   A ASN B 2 337 ? 33.068  -18.447 28.576  0.20 59.17  ? 337 ASN B OD1   1 
ATOM   11942 O  OD1   B ASN B 2 337 ? 32.670  -18.538 26.881  0.80 61.76  ? 337 ASN B OD1   1 
ATOM   11943 N  ND2   A ASN B 2 337 ? 31.330  -19.460 27.577  0.20 57.65  ? 337 ASN B ND2   1 
ATOM   11944 N  ND2   B ASN B 2 337 ? 30.957  -19.109 28.219  0.80 55.54  ? 337 ASN B ND2   1 
ATOM   11945 N  N     A SER B 2 338 ? 30.477  -14.047 29.821  0.20 54.60  ? 338 SER B N     1 
ATOM   11946 N  N     B SER B 2 338 ? 30.797  -13.926 29.718  0.80 55.79  ? 338 SER B N     1 
ATOM   11947 C  CA    A SER B 2 338 ? 29.676  -12.831 29.731  0.20 49.90  ? 338 SER B CA    1 
ATOM   11948 C  CA    B SER B 2 338 ? 30.063  -12.664 29.776  0.80 47.74  ? 338 SER B CA    1 
ATOM   11949 C  C     A SER B 2 338 ? 30.355  -11.736 28.918  0.20 44.77  ? 338 SER B C     1 
ATOM   11950 C  C     B SER B 2 338 ? 30.669  -11.602 28.864  0.80 44.00  ? 338 SER B C     1 
ATOM   11951 O  O     A SER B 2 338 ? 29.666  -10.849 28.404  0.20 43.61  ? 338 SER B O     1 
ATOM   11952 O  O     B SER B 2 338 ? 29.939  -10.825 28.239  0.80 42.80  ? 338 SER B O     1 
ATOM   11953 C  CB    A SER B 2 338 ? 29.354  -12.314 31.134  0.20 56.06  ? 338 SER B CB    1 
ATOM   11954 C  CB    B SER B 2 338 ? 30.025  -12.168 31.218  0.80 57.90  ? 338 SER B CB    1 
ATOM   11955 O  OG    A SER B 2 338 ? 30.539  -12.094 31.878  0.20 58.42  ? 338 SER B OG    1 
ATOM   11956 O  OG    B SER B 2 338 ? 31.330  -12.185 31.770  0.80 58.59  ? 338 SER B OG    1 
ATOM   11957 N  N     A SER B 2 339 ? 31.682  -11.773 28.787  0.20 43.49  ? 339 SER B N     1 
ATOM   11958 N  N     B SER B 2 339 ? 31.995  -11.538 28.780  0.80 39.77  ? 339 SER B N     1 
ATOM   11959 C  CA    A SER B 2 339 ? 32.387  -10.748 28.031  0.20 45.37  ? 339 SER B CA    1 
ATOM   11960 C  CA    B SER B 2 339 ? 32.624  -10.510 27.961  0.80 46.07  ? 339 SER B CA    1 
ATOM   11961 C  C     A SER B 2 339 ? 32.251  -10.920 26.523  0.20 42.90  ? 339 SER B C     1 
ATOM   11962 C  C     B SER B 2 339 ? 32.533  -10.797 26.464  0.80 43.74  ? 339 SER B C     1 
ATOM   11963 O  O     A SER B 2 339 ? 32.682  -10.035 25.777  0.20 46.99  ? 339 SER B O     1 
ATOM   11964 O  O     B SER B 2 339 ? 33.100  -10.034 25.673  0.80 50.57  ? 339 SER B O     1 
ATOM   11965 C  CB    A SER B 2 339 ? 33.871  -10.736 28.412  0.20 48.00  ? 339 SER B CB    1 
ATOM   11966 C  CB    B SER B 2 339 ? 34.091  -10.328 28.374  0.80 48.11  ? 339 SER B CB    1 
ATOM   11967 O  OG    A SER B 2 339 ? 34.516  -11.929 28.001  0.20 49.97  ? 339 SER B OG    1 
ATOM   11968 O  OG    B SER B 2 339 ? 34.852  -11.493 28.115  0.80 53.69  ? 339 SER B OG    1 
ATOM   11969 N  N     A TYR B 2 340 ? 31.666  -12.026 26.057  0.20 37.12  ? 340 TYR B N     1 
ATOM   11970 N  N     B TYR B 2 340 ? 31.843  -11.866 26.054  0.80 35.18  ? 340 TYR B N     1 
ATOM   11971 C  CA    A TYR B 2 340 ? 31.493  -12.281 24.633  0.20 37.42  ? 340 TYR B CA    1 
ATOM   11972 C  CA    B TYR B 2 340 ? 31.628  -12.166 24.643  0.80 37.17  ? 340 TYR B CA    1 
ATOM   11973 C  C     A TYR B 2 340 ? 30.049  -12.086 24.180  0.20 37.70  ? 340 TYR B C     1 
ATOM   11974 C  C     B TYR B 2 340 ? 30.210  -11.869 24.176  0.80 38.74  ? 340 TYR B C     1 
ATOM   11975 O  O     A TYR B 2 340 ? 29.658  -12.595 23.124  0.20 31.13  ? 340 TYR B O     1 
ATOM   11976 O  O     B TYR B 2 340 ? 29.891  -12.124 23.012  0.80 26.89  ? 340 TYR B O     1 
ATOM   11977 C  CB    A TYR B 2 340 ? 31.978  -13.688 24.286  0.20 39.03  ? 340 TYR B CB    1 
ATOM   11978 C  CB    B TYR B 2 340 ? 31.971  -13.631 24.348  0.80 39.07  ? 340 TYR B CB    1 
ATOM   11979 C  CG    A TYR B 2 340 ? 33.406  -13.942 24.712  0.20 40.05  ? 340 TYR B CG    1 
ATOM   11980 C  CG    B TYR B 2 340 ? 33.384  -14.003 24.737  0.80 39.78  ? 340 TYR B CG    1 
ATOM   11981 C  CD1   A TYR B 2 340 ? 34.469  -13.470 23.955  0.20 42.32  ? 340 TYR B CD1   1 
ATOM   11982 C  CD1   B TYR B 2 340 ? 34.470  -13.463 24.064  0.80 42.41  ? 340 TYR B CD1   1 
ATOM   11983 C  CD2   A TYR B 2 340 ? 33.689  -14.642 25.876  0.20 43.10  ? 340 TYR B CD2   1 
ATOM   11984 C  CD2   B TYR B 2 340 ? 33.629  -14.885 25.777  0.80 41.91  ? 340 TYR B CD2   1 
ATOM   11985 C  CE1   A TYR B 2 340 ? 35.777  -13.694 24.342  0.20 44.20  ? 340 TYR B CE1   1 
ATOM   11986 C  CE1   B TYR B 2 340 ? 35.766  -13.793 24.416  0.80 44.35  ? 340 TYR B CE1   1 
ATOM   11987 C  CE2   A TYR B 2 340 ? 34.994  -14.871 26.272  0.20 50.27  ? 340 TYR B CE2   1 
ATOM   11988 C  CE2   B TYR B 2 340 ? 34.920  -15.226 26.134  0.80 52.67  ? 340 TYR B CE2   1 
ATOM   11989 C  CZ    A TYR B 2 340 ? 36.034  -14.395 25.500  0.20 46.30  ? 340 TYR B CZ    1 
ATOM   11990 C  CZ    B TYR B 2 340 ? 35.986  -14.676 25.450  0.80 46.40  ? 340 TYR B CZ    1 
ATOM   11991 O  OH    A TYR B 2 340 ? 37.335  -14.619 25.888  0.20 49.47  ? 340 TYR B OH    1 
ATOM   11992 O  OH    B TYR B 2 340 ? 37.279  -15.002 25.799  0.80 51.60  ? 340 TYR B OH    1 
ATOM   11993 N  N     A PHE B 2 341 ? 29.249  -11.365 24.965  0.20 37.98  ? 341 PHE B N     1 
ATOM   11994 N  N     B PHE B 2 341 ? 29.345  -11.368 25.054  0.80 38.26  ? 341 PHE B N     1 
ATOM   11995 C  CA    A PHE B 2 341 ? 27.887  -10.996 24.605  0.20 33.55  ? 341 PHE B CA    1 
ATOM   11996 C  CA    B PHE B 2 341 ? 28.012  -10.911 24.690  0.80 33.45  ? 341 PHE B CA    1 
ATOM   11997 C  C     A PHE B 2 341 ? 27.738  -9.491  24.757  0.20 33.71  ? 341 PHE B C     1 
ATOM   11998 C  C     B PHE B 2 341 ? 27.995  -9.396  24.806  0.80 34.36  ? 341 PHE B C     1 
ATOM   11999 O  O     A PHE B 2 341 ? 28.285  -8.902  25.694  0.20 39.78  ? 341 PHE B O     1 
ATOM   12000 O  O     B PHE B 2 341 ? 28.690  -8.832  25.655  0.80 42.49  ? 341 PHE B O     1 
ATOM   12001 C  CB    A PHE B 2 341 ? 26.855  -11.720 25.482  0.20 34.06  ? 341 PHE B CB    1 
ATOM   12002 C  CB    B PHE B 2 341 ? 26.953  -11.549 25.597  0.80 33.94  ? 341 PHE B CB    1 
ATOM   12003 C  CG    A PHE B 2 341 ? 26.814  -13.203 25.267  0.20 33.56  ? 341 PHE B CG    1 
ATOM   12004 C  CG    B PHE B 2 341 ? 26.921  -13.044 25.507  0.80 32.40  ? 341 PHE B CG    1 
ATOM   12005 C  CD1   A PHE B 2 341 ? 25.988  -13.752 24.301  0.20 31.93  ? 341 PHE B CD1   1 
ATOM   12006 C  CD1   B PHE B 2 341 ? 27.777  -13.812 26.268  0.80 30.85  ? 341 PHE B CD1   1 
ATOM   12007 C  CD2   A PHE B 2 341 ? 27.606  -14.048 26.025  0.20 34.07  ? 341 PHE B CD2   1 
ATOM   12008 C  CD2   B PHE B 2 341 ? 26.071  -13.680 24.621  0.80 30.98  ? 341 PHE B CD2   1 
ATOM   12009 C  CE1   A PHE B 2 341 ? 25.951  -15.118 24.095  0.20 35.97  ? 341 PHE B CE1   1 
ATOM   12010 C  CE1   B PHE B 2 341 ? 27.782  -15.189 26.167  0.80 38.41  ? 341 PHE B CE1   1 
ATOM   12011 C  CE2   A PHE B 2 341 ? 27.575  -15.416 25.825  0.20 39.65  ? 341 PHE B CE2   1 
ATOM   12012 C  CE2   B PHE B 2 341 ? 26.067  -15.056 24.516  0.80 37.01  ? 341 PHE B CE2   1 
ATOM   12013 C  CZ    A PHE B 2 341 ? 26.745  -15.952 24.859  0.20 40.73  ? 341 PHE B CZ    1 
ATOM   12014 C  CZ    B PHE B 2 341 ? 26.919  -15.813 25.297  0.80 44.05  ? 341 PHE B CZ    1 
ATOM   12015 N  N     A VAL B 2 342 ? 27.011  -8.867  23.832  0.20 29.89  ? 342 VAL B N     1 
ATOM   12016 N  N     B VAL B 2 342 ? 27.256  -8.724  23.936  0.80 28.84  ? 342 VAL B N     1 
ATOM   12017 C  CA    A VAL B 2 342 ? 26.828  -7.421  23.897  0.20 32.80  ? 342 VAL B CA    1 
ATOM   12018 C  CA    B VAL B 2 342 ? 27.186  -7.277  24.077  0.80 33.91  ? 342 VAL B CA    1 
ATOM   12019 C  C     A VAL B 2 342 ? 25.868  -7.098  25.035  0.20 33.19  ? 342 VAL B C     1 
ATOM   12020 C  C     B VAL B 2 342 ? 26.273  -6.970  25.245  0.80 31.90  ? 342 VAL B C     1 
ATOM   12021 O  O     A VAL B 2 342 ? 24.738  -7.600  25.081  0.20 29.13  ? 342 VAL B O     1 
ATOM   12022 O  O     B VAL B 2 342 ? 25.361  -7.743  25.554  0.80 34.87  ? 342 VAL B O     1 
ATOM   12023 C  CB    A VAL B 2 342 ? 26.334  -6.859  22.556  0.20 31.62  ? 342 VAL B CB    1 
ATOM   12024 C  CB    B VAL B 2 342 ? 26.711  -6.581  22.790  0.80 28.27  ? 342 VAL B CB    1 
ATOM   12025 C  CG1   A VAL B 2 342 ? 27.439  -6.942  21.507  0.20 35.38  ? 342 VAL B CG1   1 
ATOM   12026 C  CG1   B VAL B 2 342 ? 27.596  -6.987  21.614  0.80 36.00  ? 342 VAL B CG1   1 
ATOM   12027 C  CG2   A VAL B 2 342 ? 25.091  -7.594  22.075  0.20 32.63  ? 342 VAL B CG2   1 
ATOM   12028 C  CG2   B VAL B 2 342 ? 25.233  -6.859  22.525  0.80 34.52  ? 342 VAL B CG2   1 
ATOM   12029 N  N     A GLU B 2 343 ? 26.326  -6.267  25.974  0.20 34.92  ? 343 GLU B N     1 
ATOM   12030 N  N     B GLU B 2 343 ? 26.522  -5.847  25.916  0.80 31.56  ? 343 GLU B N     1 
ATOM   12031 C  CA    A GLU B 2 343 ? 25.525  -5.963  27.155  0.20 32.48  ? 343 GLU B CA    1 
ATOM   12032 C  CA    B GLU B 2 343 ? 25.754  -5.529  27.112  0.80 32.24  ? 343 GLU B CA    1 
ATOM   12033 C  C     A GLU B 2 343 ? 24.314  -5.101  26.831  0.20 33.34  ? 343 GLU B C     1 
ATOM   12034 C  C     B GLU B 2 343 ? 24.621  -4.549  26.857  0.80 32.69  ? 343 GLU B C     1 
ATOM   12035 O  O     A GLU B 2 343 ? 23.327  -5.143  27.574  0.20 24.93  ? 343 GLU B O     1 
ATOM   12036 O  O     B GLU B 2 343 ? 23.889  -4.222  27.795  0.80 36.25  ? 343 GLU B O     1 
ATOM   12037 C  CB    A GLU B 2 343 ? 26.384  -5.266  28.215  0.20 33.49  ? 343 GLU B CB    1 
ATOM   12038 C  CB    B GLU B 2 343 ? 26.662  -4.975  28.213  0.80 33.58  ? 343 GLU B CB    1 
ATOM   12039 C  CG    A GLU B 2 343 ? 26.814  -3.846  27.855  0.20 35.62  ? 343 GLU B CG    1 
ATOM   12040 C  CG    B GLU B 2 343 ? 27.201  -3.585  27.928  0.80 35.15  ? 343 GLU B CG    1 
ATOM   12041 C  CD    A GLU B 2 343 ? 27.877  -3.807  26.771  0.20 40.32  ? 343 GLU B CD    1 
ATOM   12042 C  CD    B GLU B 2 343 ? 28.574  -3.615  27.279  0.80 49.23  ? 343 GLU B CD    1 
ATOM   12043 O  OE1   A GLU B 2 343 ? 28.460  -4.871  26.469  0.20 40.52  ? 343 GLU B OE1   1 
ATOM   12044 O  OE1   B GLU B 2 343 ? 28.995  -4.704  26.829  0.80 46.15  ? 343 GLU B OE1   1 
ATOM   12045 O  OE2   A GLU B 2 343 ? 28.128  -2.715  26.218  0.20 40.29  ? 343 GLU B OE2   1 
ATOM   12046 O  OE2   B GLU B 2 343 ? 29.236  -2.554  27.231  0.80 57.35  ? 343 GLU B OE2   1 
ATOM   12047 N  N     A TRP B 2 344 ? 24.364  -4.335  25.743  0.20 31.56  ? 344 TRP B N     1 
ATOM   12048 N  N     B TRP B 2 344 ? 24.445  -4.083  25.624  0.80 31.52  ? 344 TRP B N     1 
ATOM   12049 C  CA    A TRP B 2 344 ? 23.299  -3.408  25.386  0.20 32.55  ? 344 TRP B CA    1 
ATOM   12050 C  CA    B TRP B 2 344 ? 23.386  -3.139  25.307  0.80 32.68  ? 344 TRP B CA    1 
ATOM   12051 C  C     A TRP B 2 344 ? 22.147  -4.075  24.640  0.20 29.68  ? 344 TRP B C     1 
ATOM   12052 C  C     B TRP B 2 344 ? 22.214  -3.785  24.566  0.80 29.37  ? 344 TRP B C     1 
ATOM   12053 O  O     A TRP B 2 344 ? 21.301  -3.369  24.082  0.20 30.41  ? 344 TRP B O     1 
ATOM   12054 O  O     B TRP B 2 344 ? 21.334  -3.069  24.082  0.80 30.70  ? 344 TRP B O     1 
ATOM   12055 C  CB    A TRP B 2 344 ? 23.868  -2.249  24.559  0.20 29.45  ? 344 TRP B CB    1 
ATOM   12056 C  CB    B TRP B 2 344 ? 23.951  -1.950  24.521  0.80 28.19  ? 344 TRP B CB    1 
ATOM   12057 C  CG    A TRP B 2 344 ? 24.898  -2.647  23.526  0.20 34.37  ? 344 TRP B CG    1 
ATOM   12058 C  CG    B TRP B 2 344 ? 25.026  -2.278  23.457  0.80 33.95  ? 344 TRP B CG    1 
ATOM   12059 C  CD1   A TRP B 2 344 ? 26.233  -2.840  23.735  0.20 35.72  ? 344 TRP B CD1   1 
ATOM   12060 C  CD1   B TRP B 2 344 ? 26.376  -2.359  23.656  0.80 36.53  ? 344 TRP B CD1   1 
ATOM   12061 C  CD2   A TRP B 2 344 ? 24.674  -2.875  22.128  0.20 32.76  ? 344 TRP B CD2   1 
ATOM   12062 C  CD2   B TRP B 2 344 ? 24.814  -2.532  22.061  0.80 32.98  ? 344 TRP B CD2   1 
ATOM   12063 N  NE1   A TRP B 2 344 ? 26.853  -3.184  22.557  0.20 34.47  ? 344 TRP B NE1   1 
ATOM   12064 N  NE1   B TRP B 2 344 ? 27.019  -2.656  22.472  0.80 30.78  ? 344 TRP B NE1   1 
ATOM   12065 C  CE2   A TRP B 2 344 ? 25.918  -3.213  21.556  0.20 34.94  ? 344 TRP B CE2   1 
ATOM   12066 C  CE2   B TRP B 2 344 ? 26.081  -2.769  21.478  0.80 37.28  ? 344 TRP B CE2   1 
ATOM   12067 C  CE3   A TRP B 2 344 ? 23.544  -2.831  21.306  0.20 34.21  ? 344 TRP B CE3   1 
ATOM   12068 C  CE3   B TRP B 2 344 ? 23.678  -2.582  21.245  0.80 34.93  ? 344 TRP B CE3   1 
ATOM   12069 C  CZ2   A TRP B 2 344 ? 26.063  -3.503  20.201  0.20 34.53  ? 344 TRP B CZ2   1 
ATOM   12070 C  CZ2   B TRP B 2 344 ? 26.239  -3.051  20.121  0.80 32.82  ? 344 TRP B CZ2   1 
ATOM   12071 C  CZ3   A TRP B 2 344 ? 23.690  -3.123  19.959  0.20 31.15  ? 344 TRP B CZ3   1 
ATOM   12072 C  CZ3   B TRP B 2 344 ? 23.837  -2.873  19.898  0.80 31.01  ? 344 TRP B CZ3   1 
ATOM   12073 C  CH2   A TRP B 2 344 ? 24.939  -3.453  19.421  0.20 34.68  ? 344 TRP B CH2   1 
ATOM   12074 C  CH2   B TRP B 2 344 ? 25.108  -3.096  19.348  0.80 35.04  ? 344 TRP B CH2   1 
ATOM   12075 N  N     A ILE B 2 345 ? 22.096  -5.403  24.608  0.20 29.23  ? 345 ILE B N     1 
ATOM   12076 N  N     B ILE B 2 345 ? 22.192  -5.112  24.453  0.80 28.65  ? 345 ILE B N     1 
ATOM   12077 C  CA    A ILE B 2 345 ? 20.926  -6.119  24.105  0.20 27.82  ? 345 ILE B CA    1 
ATOM   12078 C  CA    B ILE B 2 345 ? 20.997  -5.839  24.023  0.80 26.17  ? 345 ILE B CA    1 
ATOM   12079 C  C     A ILE B 2 345 ? 20.443  -7.043  25.217  0.20 30.83  ? 345 ILE B C     1 
ATOM   12080 C  C     B ILE B 2 345 ? 20.658  -6.816  25.141  0.80 31.50  ? 345 ILE B C     1 
ATOM   12081 O  O     A ILE B 2 345 ? 20.953  -8.164  25.359  0.20 30.54  ? 345 ILE B O     1 
ATOM   12082 O  O     B ILE B 2 345 ? 21.171  -7.944  25.163  0.80 32.27  ? 345 ILE B O     1 
ATOM   12083 C  CB    A ILE B 2 345 ? 21.236  -6.892  22.813  0.20 31.74  ? 345 ILE B CB    1 
ATOM   12084 C  CB    B ILE B 2 345 ? 21.186  -6.570  22.679  0.80 33.08  ? 345 ILE B CB    1 
ATOM   12085 C  CG1   A ILE B 2 345 ? 21.778  -5.942  21.737  0.20 33.30  ? 345 ILE B CG1   1 
ATOM   12086 C  CG1   B ILE B 2 345 ? 21.569  -5.597  21.551  0.80 34.62  ? 345 ILE B CG1   1 
ATOM   12087 C  CG2   A ILE B 2 345 ? 19.987  -7.598  22.309  0.20 30.90  ? 345 ILE B CG2   1 
ATOM   12088 C  CG2   B ILE B 2 345 ? 19.908  -7.295  22.308  0.80 31.07  ? 345 ILE B CG2   1 
ATOM   12089 C  CD1   A ILE B 2 345 ? 22.006  -6.596  20.382  0.20 31.09  ? 345 ILE B CD1   1 
ATOM   12090 C  CD1   B ILE B 2 345 ? 21.778  -6.275  20.178  0.80 30.79  ? 345 ILE B CD1   1 
ATOM   12091 N  N     A PRO B 2 346 ? 19.486  -6.610  26.037  0.20 30.49  ? 346 PRO B N     1 
ATOM   12092 N  N     B PRO B 2 346 ? 19.833  -6.419  26.102  0.80 30.41  ? 346 PRO B N     1 
ATOM   12093 C  CA    A PRO B 2 346 ? 19.044  -7.445  27.164  0.20 31.46  ? 346 PRO B CA    1 
ATOM   12094 C  CA    B PRO B 2 346 ? 19.508  -7.322  27.214  0.80 29.78  ? 346 PRO B CA    1 
ATOM   12095 C  C     A PRO B 2 346 ? 18.332  -8.699  26.679  0.20 29.72  ? 346 PRO B C     1 
ATOM   12096 C  C     B PRO B 2 346 ? 18.777  -8.557  26.707  0.80 29.39  ? 346 PRO B C     1 
ATOM   12097 O  O     A PRO B 2 346 ? 17.460  -8.639  25.808  0.20 34.10  ? 346 PRO B O     1 
ATOM   12098 O  O     B PRO B 2 346 ? 18.065  -8.509  25.702  0.80 37.04  ? 346 PRO B O     1 
ATOM   12099 C  CB    A PRO B 2 346 ? 18.090  -6.526  27.940  0.20 29.89  ? 346 PRO B CB    1 
ATOM   12100 C  CB    B PRO B 2 346 ? 18.596  -6.476  28.115  0.80 30.49  ? 346 PRO B CB    1 
ATOM   12101 C  CG    A PRO B 2 346 ? 18.395  -5.144  27.463  0.20 28.29  ? 346 PRO B CG    1 
ATOM   12102 C  CG    B PRO B 2 346 ? 18.693  -5.082  27.622  0.80 28.01  ? 346 PRO B CG    1 
ATOM   12103 C  CD    A PRO B 2 346 ? 18.839  -5.290  26.038  0.20 28.83  ? 346 PRO B CD    1 
ATOM   12104 C  CD    B PRO B 2 346 ? 19.117  -5.141  26.178  0.80 28.41  ? 346 PRO B CD    1 
ATOM   12105 N  N     A ASN B 2 347 ? 18.705  -9.837  27.266  0.20 28.71  ? 347 ASN B N     1 
ATOM   12106 N  N     B ASN B 2 347 ? 18.973  -9.673  27.404  0.80 27.52  ? 347 ASN B N     1 
ATOM   12107 C  CA    A ASN B 2 347 ? 18.146  -11.145 26.926  0.20 28.73  ? 347 ASN B CA    1 
ATOM   12108 C  CA    B ASN B 2 347 ? 18.223  -10.902 27.136  0.80 26.74  ? 347 ASN B CA    1 
ATOM   12109 C  C     A ASN B 2 347 ? 18.291  -11.416 25.425  0.20 29.20  ? 347 ASN B C     1 
ATOM   12110 C  C     B ASN B 2 347 ? 18.451  -11.393 25.705  0.80 28.69  ? 347 ASN B C     1 
ATOM   12111 O  O     A ASN B 2 347 ? 17.321  -11.485 24.671  0.20 27.89  ? 347 ASN B O     1 
ATOM   12112 O  O     B ASN B 2 347 ? 17.520  -11.806 25.018  0.80 26.12  ? 347 ASN B O     1 
ATOM   12113 C  CB    A ASN B 2 347 ? 16.680  -11.244 27.370  0.20 33.90  ? 347 ASN B CB    1 
ATOM   12114 C  CB    B ASN B 2 347 ? 16.730  -10.692 27.403  0.80 30.86  ? 347 ASN B CB    1 
ATOM   12115 C  CG    A ASN B 2 347 ? 16.195  -12.678 27.471  0.20 41.33  ? 347 ASN B CG    1 
ATOM   12116 C  CG    B ASN B 2 347 ? 15.996  -11.982 27.696  0.80 42.23  ? 347 ASN B CG    1 
ATOM   12117 O  OD1   A ASN B 2 347 ? 16.973  -13.589 27.760  0.20 41.61  ? 347 ASN B OD1   1 
ATOM   12118 O  OD1   B ASN B 2 347 ? 16.573  -12.939 28.222  0.80 46.12  ? 347 ASN B OD1   1 
ATOM   12119 N  ND2   A ASN B 2 347 ? 14.905  -12.884 27.235  0.20 45.41  ? 347 ASN B ND2   1 
ATOM   12120 N  ND2   B ASN B 2 347 ? 14.706  -12.012 27.367  0.80 50.09  ? 347 ASN B ND2   1 
ATOM   12121 N  N     A ASN B 2 348 ? 19.549  -11.553 25.012  0.20 30.88  ? 348 ASN B N     1 
ATOM   12122 N  N     B ASN B 2 348 ? 19.698  -11.345 25.238  0.80 30.22  ? 348 ASN B N     1 
ATOM   12123 C  CA    A ASN B 2 348 ? 19.884  -11.750 23.608  0.20 30.16  ? 348 ASN B CA    1 
ATOM   12124 C  CA    B ASN B 2 348 ? 19.957  -11.574 23.822  0.80 30.89  ? 348 ASN B CA    1 
ATOM   12125 C  C     A ASN B 2 348 ? 20.054  -13.219 23.238  0.20 32.29  ? 348 ASN B C     1 
ATOM   12126 C  C     B ASN B 2 348 ? 20.328  -13.020 23.494  0.80 33.93  ? 348 ASN B C     1 
ATOM   12127 O  O     A ASN B 2 348 ? 20.550  -13.519 22.146  0.20 30.41  ? 348 ASN B O     1 
ATOM   12128 O  O     B ASN B 2 348 ? 20.859  -13.285 22.404  0.80 33.08  ? 348 ASN B O     1 
ATOM   12129 C  CB    A ASN B 2 348 ? 21.149  -10.961 23.253  0.20 29.05  ? 348 ASN B CB    1 
ATOM   12130 C  CB    B ASN B 2 348 ? 21.031  -10.605 23.315  0.80 28.48  ? 348 ASN B CB    1 
ATOM   12131 C  CG    A ASN B 2 348 ? 22.389  -11.472 23.965  0.20 30.31  ? 348 ASN B CG    1 
ATOM   12132 C  CG    B ASN B 2 348 ? 22.347  -10.705 24.069  0.80 29.54  ? 348 ASN B CG    1 
ATOM   12133 O  OD1   A ASN B 2 348 ? 22.304  -12.165 24.977  0.20 29.93  ? 348 ASN B OD1   1 
ATOM   12134 O  OD1   B ASN B 2 348 ? 22.442  -11.295 25.145  0.80 29.33  ? 348 ASN B OD1   1 
ATOM   12135 N  ND2   A ASN B 2 348 ? 23.557  -11.121 23.434  0.20 30.04  ? 348 ASN B ND2   1 
ATOM   12136 N  ND2   B ASN B 2 348 ? 23.381  -10.106 23.493  0.80 28.21  ? 348 ASN B ND2   1 
ATOM   12137 N  N     A VAL B 2 349 ? 19.640  -14.135 24.110  0.20 27.93  ? 349 VAL B N     1 
ATOM   12138 N  N     B VAL B 2 349 ? 20.034  -13.964 24.384  0.80 26.13  ? 349 VAL B N     1 
ATOM   12139 C  CA    A VAL B 2 349 ? 19.726  -15.570 23.864  0.20 31.03  ? 349 VAL B CA    1 
ATOM   12140 C  CA    B VAL B 2 349 ? 20.278  -15.390 24.148  0.80 29.76  ? 349 VAL B CA    1 
ATOM   12141 C  C     A VAL B 2 349 ? 18.332  -16.164 24.018  0.20 32.67  ? 349 VAL B C     1 
ATOM   12142 C  C     B VAL B 2 349 ? 18.961  -16.127 24.346  0.80 34.71  ? 349 VAL B C     1 
ATOM   12143 O  O     A VAL B 2 349 ? 17.644  -15.891 25.008  0.20 31.08  ? 349 VAL B O     1 
ATOM   12144 O  O     B VAL B 2 349 ? 18.338  -16.014 25.410  0.80 33.87  ? 349 VAL B O     1 
ATOM   12145 C  CB    A VAL B 2 349 ? 20.721  -16.253 24.821  0.20 32.55  ? 349 VAL B CB    1 
ATOM   12146 C  CB    B VAL B 2 349 ? 21.357  -15.959 25.083  0.80 29.33  ? 349 VAL B CB    1 
ATOM   12147 C  CG1   A VAL B 2 349 ? 20.842  -17.739 24.501  0.20 33.92  ? 349 VAL B CG1   1 
ATOM   12148 C  CG1   B VAL B 2 349 ? 21.459  -17.483 24.926  0.80 35.68  ? 349 VAL B CG1   1 
ATOM   12149 C  CG2   A VAL B 2 349 ? 22.080  -15.576 24.749  0.20 31.33  ? 349 VAL B CG2   1 
ATOM   12150 C  CG2   B VAL B 2 349 ? 22.692  -15.308 24.822  0.80 30.95  ? 349 VAL B CG2   1 
ATOM   12151 N  N     A LYS B 2 350 ? 17.917  -16.966 23.040  0.20 32.05  ? 350 LYS B N     1 
ATOM   12152 N  N     B LYS B 2 350 ? 18.543  -16.888 23.335  0.80 27.80  ? 350 LYS B N     1 
ATOM   12153 C  CA    A LYS B 2 350 ? 16.636  -17.659 23.082  0.20 31.73  ? 350 LYS B CA    1 
ATOM   12154 C  CA    B LYS B 2 350 ? 17.242  -17.551 23.332  0.80 31.76  ? 350 LYS B CA    1 
ATOM   12155 C  C     A LYS B 2 350 ? 16.875  -19.145 22.867  0.20 32.37  ? 350 LYS B C     1 
ATOM   12156 C  C     B LYS B 2 350 ? 17.428  -19.052 23.176  0.80 33.98  ? 350 LYS B C     1 
ATOM   12157 O  O     A LYS B 2 350 ? 17.567  -19.534 21.921  0.20 32.52  ? 350 LYS B O     1 
ATOM   12158 O  O     B LYS B 2 350 ? 18.195  -19.504 22.319  0.80 33.63  ? 350 LYS B O     1 
ATOM   12159 C  CB    A LYS B 2 350 ? 15.668  -17.120 22.025  0.20 33.25  ? 350 LYS B CB    1 
ATOM   12160 C  CB    B LYS B 2 350 ? 16.345  -17.019 22.215  0.80 31.95  ? 350 LYS B CB    1 
ATOM   12161 C  CG    A LYS B 2 350 ? 14.225  -17.577 22.210  0.20 36.13  ? 350 LYS B CG    1 
ATOM   12162 C  CG    B LYS B 2 350 ? 14.959  -17.650 22.177  0.80 34.79  ? 350 LYS B CG    1 
ATOM   12163 C  CD    A LYS B 2 350 ? 13.580  -16.886 23.405  0.20 32.43  ? 350 LYS B CD    1 
ATOM   12164 C  CD    B LYS B 2 350 ? 14.125  -17.211 23.382  0.80 30.10  ? 350 LYS B CD    1 
ATOM   12165 C  CE    A LYS B 2 350 ? 12.089  -17.193 23.497  0.20 38.17  ? 350 LYS B CE    1 
ATOM   12166 C  CE    B LYS B 2 350 ? 12.646  -17.451 23.161  0.80 40.60  ? 350 LYS B CE    1 
ATOM   12167 N  NZ    A LYS B 2 350 ? 11.811  -18.605 23.887  0.20 37.80  ? 350 LYS B NZ    1 
ATOM   12168 N  NZ    B LYS B 2 350 ? 11.858  -16.765 24.216  0.80 41.67  ? 350 LYS B NZ    1 
ATOM   12169 N  N     A THR B 2 351 ? 16.301  -19.968 23.740  0.20 36.22  ? 351 THR B N     1 
ATOM   12170 N  N     B THR B 2 351 ? 16.742  -19.814 24.022  0.80 36.00  ? 351 THR B N     1 
ATOM   12171 C  CA    A THR B 2 351 ? 16.510  -21.410 23.725  0.20 38.19  ? 351 THR B CA    1 
ATOM   12172 C  CA    B THR B 2 351 ? 16.811  -21.268 24.045  0.80 37.47  ? 351 THR B CA    1 
ATOM   12173 C  C     A THR B 2 351 ? 15.175  -22.119 23.553  0.20 40.66  ? 351 THR B C     1 
ATOM   12174 C  C     B THR B 2 351 ? 15.493  -21.833 23.534  0.80 41.83  ? 351 THR B C     1 
ATOM   12175 O  O     A THR B 2 351 ? 14.209  -21.812 24.260  0.20 37.64  ? 351 THR B O     1 
ATOM   12176 O  O     B THR B 2 351 ? 14.418  -21.360 23.920  0.80 35.74  ? 351 THR B O     1 
ATOM   12177 C  CB    A THR B 2 351 ? 17.191  -21.881 25.015  0.20 41.69  ? 351 THR B CB    1 
ATOM   12178 C  CB    B THR B 2 351 ? 17.091  -21.784 25.466  0.80 43.42  ? 351 THR B CB    1 
ATOM   12179 O  OG1   A THR B 2 351 ? 18.458  -21.226 25.156  0.20 42.65  ? 351 THR B OG1   1 
ATOM   12180 O  OG1   B THR B 2 351 ? 18.473  -21.585 25.795  0.80 49.35  ? 351 THR B OG1   1 
ATOM   12181 C  CG2   A THR B 2 351 ? 17.403  -23.387 24.987  0.20 40.84  ? 351 THR B CG2   1 
ATOM   12182 C  CG2   B THR B 2 351 ? 16.755  -23.260 25.591  0.80 43.58  ? 351 THR B CG2   1 
ATOM   12183 N  N     A ALA B 2 352 ? 15.126  -23.065 22.618  0.20 38.95  ? 352 ALA B N     1 
ATOM   12184 N  N     B ALA B 2 352 ? 15.581  -22.829 22.659  0.80 35.67  ? 352 ALA B N     1 
ATOM   12185 C  CA    A ALA B 2 352 ? 13.945  -23.883 22.384  0.20 39.56  ? 352 ALA B CA    1 
ATOM   12186 C  CA    B ALA B 2 352 ? 14.441  -23.626 22.235  0.80 39.80  ? 352 ALA B CA    1 
ATOM   12187 C  C     A ALA B 2 352 ? 14.353  -25.347 22.324  0.20 42.24  ? 352 ALA B C     1 
ATOM   12188 C  C     B ALA B 2 352 ? 14.746  -25.092 22.498  0.80 43.52  ? 352 ALA B C     1 
ATOM   12189 O  O     A ALA B 2 352 ? 15.428  -25.682 21.818  0.20 38.35  ? 352 ALA B O     1 
ATOM   12190 O  O     B ALA B 2 352 ? 15.908  -25.510 22.501  0.80 35.41  ? 352 ALA B O     1 
ATOM   12191 C  CB    A ALA B 2 352 ? 13.227  -23.483 21.092  0.20 40.15  ? 352 ALA B CB    1 
ATOM   12192 C  CB    B ALA B 2 352 ? 14.119  -23.421 20.752  0.80 49.80  ? 352 ALA B CB    1 
ATOM   12193 N  N     A VAL B 2 353 ? 13.492  -26.214 22.843  0.20 39.64  ? 353 VAL B N     1 
ATOM   12194 N  N     B VAL B 2 353 ? 13.696  -25.871 22.730  0.80 38.54  ? 353 VAL B N     1 
ATOM   12195 C  CA    A VAL B 2 353 ? 13.758  -27.643 22.891  0.20 40.36  ? 353 VAL B CA    1 
ATOM   12196 C  CA    B VAL B 2 353 ? 13.831  -27.298 22.975  0.80 38.71  ? 353 VAL B CA    1 
ATOM   12197 C  C     A VAL B 2 353 ? 12.808  -28.356 21.937  0.20 43.24  ? 353 VAL B C     1 
ATOM   12198 C  C     B VAL B 2 353 ? 12.784  -28.031 22.151  0.80 42.92  ? 353 VAL B C     1 
ATOM   12199 O  O     A VAL B 2 353 ? 11.754  -27.838 21.555  0.20 46.46  ? 353 VAL B O     1 
ATOM   12200 O  O     B VAL B 2 353 ? 11.630  -27.594 22.058  0.80 50.18  ? 353 VAL B O     1 
ATOM   12201 C  CB    A VAL B 2 353 ? 13.624  -28.206 24.320  0.20 44.62  ? 353 VAL B CB    1 
ATOM   12202 C  CB    B VAL B 2 353 ? 13.697  -27.628 24.477  0.80 44.37  ? 353 VAL B CB    1 
ATOM   12203 C  CG1   A VAL B 2 353 ? 14.540  -27.454 25.275  0.20 44.71  ? 353 VAL B CG1   1 
ATOM   12204 C  CG1   B VAL B 2 353 ? 12.410  -27.046 25.037  0.80 57.63  ? 353 VAL B CG1   1 
ATOM   12205 C  CG2   A VAL B 2 353 ? 12.181  -28.122 24.786  0.20 50.32  ? 353 VAL B CG2   1 
ATOM   12206 C  CG2   B VAL B 2 353 ? 13.767  -29.132 24.702  0.80 45.63  ? 353 VAL B CG2   1 
ATOM   12207 N  N     A CYS B 2 354 ? 13.194  -29.569 21.549  0.20 43.40  ? 354 CYS B N     1 
ATOM   12208 N  N     B CYS B 2 354 ? 13.190  -29.140 21.542  0.80 42.96  ? 354 CYS B N     1 
ATOM   12209 C  CA    A CYS B 2 354 ? 12.372  -30.390 20.675  0.20 46.46  ? 354 CYS B CA    1 
ATOM   12210 C  CA    B CYS B 2 354 ? 12.301  -29.913 20.689  0.80 47.65  ? 354 CYS B CA    1 
ATOM   12211 C  C     A CYS B 2 354 ? 12.443  -31.841 21.123  0.20 47.91  ? 354 CYS B C     1 
ATOM   12212 C  C     B CYS B 2 354 ? 12.464  -31.385 21.026  0.80 48.30  ? 354 CYS B C     1 
ATOM   12213 O  O     A CYS B 2 354 ? 13.462  -32.297 21.649  0.20 47.33  ? 354 CYS B O     1 
ATOM   12214 O  O     B CYS B 2 354 ? 13.586  -31.898 21.027  0.80 43.42  ? 354 CYS B O     1 
ATOM   12215 C  CB    A CYS B 2 354 ? 12.804  -30.275 19.210  0.20 43.61  ? 354 CYS B CB    1 
ATOM   12216 C  CB    B CYS B 2 354 ? 12.596  -29.651 19.209  0.80 38.27  ? 354 CYS B CB    1 
ATOM   12217 S  SG    A CYS B 2 354 ? 11.885  -31.368 18.111  0.20 43.32  ? 354 CYS B SG    1 
ATOM   12218 S  SG    B CYS B 2 354 ? 11.558  -30.568 18.053  0.80 45.72  ? 354 CYS B SG    1 
ATOM   12219 N  N     A ASP B 2 355 ? 11.344  -32.566 20.903  0.20 46.11  ? 355 ASP B N     1 
ATOM   12220 N  N     B ASP B 2 355 ? 11.342  -32.058 21.307  0.80 46.87  ? 355 ASP B N     1 
ATOM   12221 C  CA    A ASP B 2 355 ? 11.265  -33.955 21.341  0.20 47.71  ? 355 ASP B CA    1 
ATOM   12222 C  CA    B ASP B 2 355 ? 11.395  -33.425 21.817  0.80 46.00  ? 355 ASP B CA    1 
ATOM   12223 C  C     A ASP B 2 355 ? 12.022  -34.884 20.399  0.20 48.01  ? 355 ASP B C     1 
ATOM   12224 C  C     B ASP B 2 355 ? 11.961  -34.396 20.797  0.80 46.94  ? 355 ASP B C     1 
ATOM   12225 O  O     A ASP B 2 355 ? 12.901  -35.637 20.832  0.20 49.86  ? 355 ASP B O     1 
ATOM   12226 O  O     B ASP B 2 355 ? 12.523  -35.430 21.173  0.80 51.64  ? 355 ASP B O     1 
ATOM   12227 C  CB    A ASP B 2 355 ? 9.801   -34.388 21.450  0.20 48.92  ? 355 ASP B CB    1 
ATOM   12228 C  CB    B ASP B 2 355 ? 9.997   -33.887 22.238  0.80 44.99  ? 355 ASP B CB    1 
ATOM   12229 C  CG    A ASP B 2 355 ? 8.952   -33.391 22.211  0.20 49.40  ? 355 ASP B CG    1 
ATOM   12230 C  CG    B ASP B 2 355 ? 9.442   -33.091 23.391  0.80 52.62  ? 355 ASP B CG    1 
ATOM   12231 O  OD1   A ASP B 2 355 ? 9.480   -32.325 22.589  0.20 49.68  ? 355 ASP B OD1   1 
ATOM   12232 O  OD1   B ASP B 2 355 ? 9.864   -33.333 24.541  0.80 58.31  ? 355 ASP B OD1   1 
ATOM   12233 O  OD2   A ASP B 2 355 ? 7.755   -33.674 22.430  0.20 55.12  ? 355 ASP B OD2   1 
ATOM   12234 O  OD2   B ASP B 2 355 ? 8.590   -32.212 23.145  0.80 63.60  ? 355 ASP B OD2   1 
ATOM   12235 N  N     A ILE B 2 356 ? 11.697  -34.842 19.111  0.20 48.09  ? 356 ILE B N     1 
ATOM   12236 N  N     B ILE B 2 356 ? 11.819  -34.093 19.510  0.80 47.97  ? 356 ILE B N     1 
ATOM   12237 C  CA    A ILE B 2 356 ? 12.249  -35.783 18.139  0.20 48.81  ? 356 ILE B CA    1 
ATOM   12238 C  CA    B ILE B 2 356 ? 12.105  -35.043 18.442  0.80 48.91  ? 356 ILE B CA    1 
ATOM   12239 C  C     A ILE B 2 356 ? 13.694  -35.419 17.815  0.20 48.41  ? 356 ILE B C     1 
ATOM   12240 C  C     B ILE B 2 356 ? 13.561  -34.855 18.020  0.80 49.58  ? 356 ILE B C     1 
ATOM   12241 O  O     A ILE B 2 356 ? 13.965  -34.310 17.330  0.20 46.33  ? 356 ILE B O     1 
ATOM   12242 O  O     B ILE B 2 356 ? 13.899  -33.791 17.476  0.80 44.13  ? 356 ILE B O     1 
ATOM   12243 C  CB    A ILE B 2 356 ? 11.387  -35.832 16.866  0.20 48.94  ? 356 ILE B CB    1 
ATOM   12244 C  CB    B ILE B 2 356 ? 11.151  -34.850 17.258  0.80 46.99  ? 356 ILE B CB    1 
ATOM   12245 C  CG1   A ILE B 2 356 ? 12.111  -36.603 15.759  0.20 47.54  ? 356 ILE B CG1   1 
ATOM   12246 C  CG1   B ILE B 2 356 ? 9.708   -34.747 17.764  0.80 42.09  ? 356 ILE B CG1   1 
ATOM   12247 C  CG2   A ILE B 2 356 ? 10.995  -34.428 16.415  0.20 47.01  ? 356 ILE B CG2   1 
ATOM   12248 C  CG2   B ILE B 2 356 ? 11.293  -35.994 16.275  0.80 52.16  ? 356 ILE B CG2   1 
ATOM   12249 C  CD1   A ILE B 2 356 ? 12.294  -38.075 16.063  0.20 49.32  ? 356 ILE B CD1   1 
ATOM   12250 C  CD1   B ILE B 2 356 ? 8.687   -34.773 16.650  0.80 50.42  ? 356 ILE B CD1   1 
ATOM   12251 N  N     A PRO B 2 357 ? 14.649  -36.308 18.074  0.20 49.33  ? 357 PRO B N     1 
ATOM   12252 N  N     B PRO B 2 357 ? 14.437  -35.827 18.257  0.80 50.24  ? 357 PRO B N     1 
ATOM   12253 C  CA    A PRO B 2 357 ? 16.042  -36.039 17.708  0.20 49.43  ? 357 PRO B CA    1 
ATOM   12254 C  CA    B PRO B 2 357 ? 15.840  -35.693 17.847  0.80 49.10  ? 357 PRO B CA    1 
ATOM   12255 C  C     A PRO B 2 357 ? 16.287  -36.363 16.246  0.20 48.50  ? 357 PRO B C     1 
ATOM   12256 C  C     B PRO B 2 357 ? 16.037  -36.167 16.418  0.80 46.74  ? 357 PRO B C     1 
ATOM   12257 O  O     A PRO B 2 357 ? 15.445  -37.001 15.596  0.20 50.00  ? 357 PRO B O     1 
ATOM   12258 O  O     B PRO B 2 357 ? 15.153  -36.827 15.851  0.80 50.26  ? 357 PRO B O     1 
ATOM   12259 C  CB    A PRO B 2 357 ? 16.827  -36.984 18.628  0.20 51.25  ? 357 PRO B CB    1 
ATOM   12260 C  CB    B PRO B 2 357 ? 16.576  -36.598 18.844  0.80 52.74  ? 357 PRO B CB    1 
ATOM   12261 C  CG    A PRO B 2 357 ? 15.906  -38.138 18.816  0.20 50.60  ? 357 PRO B CG    1 
ATOM   12262 C  CG    B PRO B 2 357 ? 15.571  -37.651 19.188  0.80 48.71  ? 357 PRO B CG    1 
ATOM   12263 C  CD    A PRO B 2 357 ? 14.513  -37.557 18.846  0.20 48.41  ? 357 PRO B CD    1 
ATOM   12264 C  CD    B PRO B 2 357 ? 14.214  -37.013 19.104  0.80 44.92  ? 357 PRO B CD    1 
ATOM   12265 N  N     A PRO B 2 358 ? 17.430  -35.941 15.683  0.20 52.32  ? 358 PRO B N     1 
ATOM   12266 N  N     B PRO B 2 358 ? 17.184  -35.848 15.786  0.80 53.87  ? 358 PRO B N     1 
ATOM   12267 C  CA    A PRO B 2 358 ? 17.746  -36.321 14.299  0.20 49.30  ? 358 PRO B CA    1 
ATOM   12268 C  CA    B PRO B 2 358 ? 17.442  -36.361 14.432  0.80 47.23  ? 358 PRO B CA    1 
ATOM   12269 C  C     A PRO B 2 358 ? 18.083  -37.798 14.175  0.20 55.25  ? 358 PRO B C     1 
ATOM   12270 C  C     B PRO B 2 358 ? 17.699  -37.858 14.445  0.80 55.95  ? 358 PRO B C     1 
ATOM   12271 O  O     A PRO B 2 358 ? 18.034  -38.537 15.165  0.20 55.40  ? 358 PRO B O     1 
ATOM   12272 O  O     B PRO B 2 358 ? 17.718  -38.477 15.515  0.80 55.22  ? 358 PRO B O     1 
ATOM   12273 C  CB    A PRO B 2 358 ? 18.951  -35.436 13.959  0.20 51.34  ? 358 PRO B CB    1 
ATOM   12274 C  CB    B PRO B 2 358 ? 18.692  -35.590 13.982  0.80 52.21  ? 358 PRO B CB    1 
ATOM   12275 C  CG    A PRO B 2 358 ? 19.590  -35.167 15.275  0.20 45.94  ? 358 PRO B CG    1 
ATOM   12276 C  CG    B PRO B 2 358 ? 18.923  -34.538 15.008  0.80 44.66  ? 358 PRO B CG    1 
ATOM   12277 C  CD    A PRO B 2 358 ? 18.456  -35.049 16.253  0.20 51.55  ? 358 PRO B CD    1 
ATOM   12278 C  CD    B PRO B 2 358 ? 18.290  -35.006 16.270  0.80 52.20  ? 358 PRO B CD    1 
ATOM   12279 N  N     A ARG B 2 359 ? 18.430  -38.239 12.969  0.20 56.65  ? 359 ARG B N     1 
ATOM   12280 N  N     B ARG B 2 359 ? 17.913  -38.446 13.269  0.80 61.06  ? 359 ARG B N     1 
ATOM   12281 C  CA    A ARG B 2 359 ? 18.726  -39.646 12.747  0.20 56.37  ? 359 ARG B CA    1 
ATOM   12282 C  CA    B ARG B 2 359 ? 18.217  -39.869 13.193  0.80 56.95  ? 359 ARG B CA    1 
ATOM   12283 C  C     A ARG B 2 359 ? 20.006  -40.048 13.473  0.20 57.13  ? 359 ARG B C     1 
ATOM   12284 C  C     B ARG B 2 359 ? 19.649  -40.126 13.643  0.80 56.55  ? 359 ARG B C     1 
ATOM   12285 O  O     A ARG B 2 359 ? 20.916  -39.240 13.674  0.20 56.73  ? 359 ARG B O     1 
ATOM   12286 O  O     B ARG B 2 359 ? 20.546  -39.309 13.417  0.80 58.49  ? 359 ARG B O     1 
ATOM   12287 C  CB    A ARG B 2 359 ? 18.853  -39.944 11.250  0.20 57.64  ? 359 ARG B CB    1 
ATOM   12288 C  CB    B ARG B 2 359 ? 18.000  -40.391 11.768  0.80 59.43  ? 359 ARG B CB    1 
ATOM   12289 C  CG    A ARG B 2 359 ? 20.226  -39.658 10.649  0.20 56.82  ? 359 ARG B CG    1 
ATOM   12290 C  CG    B ARG B 2 359 ? 18.286  -41.887 11.595  0.80 65.97  ? 359 ARG B CG    1 
ATOM   12291 C  CD    A ARG B 2 359 ? 20.491  -38.167 10.517  0.20 53.13  ? 359 ARG B CD    1 
ATOM   12292 C  CD    B ARG B 2 359 ? 17.395  -42.524 10.534  0.80 71.45  ? 359 ARG B CD    1 
ATOM   12293 N  NE    A ARG B 2 359 ? 21.911  -37.873 10.359  0.20 52.72  ? 359 ARG B NE    1 
ATOM   12294 N  NE    B ARG B 2 359 ? 17.471  -43.984 10.531  0.80 72.13  ? 359 ARG B NE    1 
ATOM   12295 C  CZ    A ARG B 2 359 ? 22.742  -37.646 11.367  0.20 49.88  ? 359 ARG B CZ    1 
ATOM   12296 C  CZ    B ARG B 2 359 ? 16.813  -44.774 11.370  0.80 64.60  ? 359 ARG B CZ    1 
ATOM   12297 N  NH1   A ARG B 2 359 ? 22.329  -37.682 12.624  0.20 52.53  ? 359 ARG B NH1   1 
ATOM   12298 N  NH1   B ARG B 2 359 ? 16.054  -44.280 12.334  0.80 68.56  ? 359 ARG B NH1   1 
ATOM   12299 N  NH2   A ARG B 2 359 ? 24.018  -37.376 11.109  0.20 49.67  ? 359 ARG B NH2   1 
ATOM   12300 N  NH2   B ARG B 2 359 ? 16.920  -46.095 11.240  0.80 56.37  ? 359 ARG B NH2   1 
ATOM   12301 N  N     A GLY B 2 360 ? 20.058  -41.312 13.886  0.20 56.98  ? 360 GLY B N     1 
ATOM   12302 N  N     B GLY B 2 360 ? 19.855  -41.269 14.294  0.80 55.27  ? 360 GLY B N     1 
ATOM   12303 C  CA    A GLY B 2 360 ? 21.228  -41.848 14.555  0.20 56.67  ? 360 GLY B CA    1 
ATOM   12304 C  CA    B GLY B 2 360 ? 21.162  -41.651 14.773  0.80 56.72  ? 360 GLY B CA    1 
ATOM   12305 C  C     A GLY B 2 360 ? 21.470  -41.274 15.936  0.20 56.45  ? 360 GLY B C     1 
ATOM   12306 C  C     B GLY B 2 360 ? 21.680  -40.843 15.937  0.80 57.61  ? 360 GLY B C     1 
ATOM   12307 O  O     A GLY B 2 360 ? 21.517  -42.013 16.924  0.20 53.78  ? 360 GLY B O     1 
ATOM   12308 O  O     B GLY B 2 360 ? 22.838  -41.032 16.332  0.80 61.37  ? 360 GLY B O     1 
ATOM   12309 N  N     A LEU B 2 361 ? 21.628  -39.956 16.017  0.20 57.06  ? 361 LEU B N     1 
ATOM   12310 N  N     B LEU B 2 361 ? 20.873  -39.945 16.495  0.80 57.58  ? 361 LEU B N     1 
ATOM   12311 C  CA    A LEU B 2 361 ? 21.915  -39.295 17.282  0.20 54.08  ? 361 LEU B CA    1 
ATOM   12312 C  CA    B LEU B 2 361 ? 21.264  -39.149 17.645  0.80 53.10  ? 361 LEU B CA    1 
ATOM   12313 C  C     A LEU B 2 361 ? 20.660  -39.233 18.143  0.20 53.18  ? 361 LEU B C     1 
ATOM   12314 C  C     B LEU B 2 361 ? 20.181  -39.235 18.704  0.80 53.45  ? 361 LEU B C     1 
ATOM   12315 O  O     A LEU B 2 361 ? 19.581  -38.879 17.659  0.20 53.43  ? 361 LEU B O     1 
ATOM   12316 O  O     B LEU B 2 361 ? 18.986  -39.218 18.390  0.80 55.33  ? 361 LEU B O     1 
ATOM   12317 C  CB    A LEU B 2 361 ? 22.454  -37.887 17.030  0.20 52.66  ? 361 LEU B CB    1 
ATOM   12318 C  CB    B LEU B 2 361 ? 21.497  -37.681 17.266  0.80 49.51  ? 361 LEU B CB    1 
ATOM   12319 C  CG    A LEU B 2 361 ? 23.627  -37.782 16.051  0.20 54.34  ? 361 LEU B CG    1 
ATOM   12320 C  CG    B LEU B 2 361 ? 22.779  -37.387 16.490  0.80 54.24  ? 361 LEU B CG    1 
ATOM   12321 C  CD1   A LEU B 2 361 ? 23.960  -36.327 15.754  0.20 48.82  ? 361 LEU B CD1   1 
ATOM   12322 C  CD1   B LEU B 2 361 ? 22.847  -35.919 16.109  0.80 46.14  ? 361 LEU B CD1   1 
ATOM   12323 C  CD2   A LEU B 2 361 ? 24.846  -38.511 16.594  0.20 53.31  ? 361 LEU B CD2   1 
ATOM   12324 C  CD2   B LEU B 2 361 ? 23.988  -37.788 17.318  0.80 57.03  ? 361 LEU B CD2   1 
ATOM   12325 N  N     A LYS B 2 362 ? 20.803  -39.584 19.421  0.20 54.30  ? 362 LYS B N     1 
ATOM   12326 N  N     B LYS B 2 362 ? 20.603  -39.337 19.960  0.80 56.66  ? 362 LYS B N     1 
ATOM   12327 C  CA    A LYS B 2 362 ? 19.708  -39.439 20.372  0.20 51.17  ? 362 LYS B CA    1 
ATOM   12328 C  CA    B LYS B 2 362 ? 19.652  -39.218 21.051  0.80 48.34  ? 362 LYS B CA    1 
ATOM   12329 C  C     A LYS B 2 362 ? 19.656  -38.044 20.976  0.20 51.05  ? 362 LYS B C     1 
ATOM   12330 C  C     B LYS B 2 362 ? 19.456  -37.766 21.457  0.80 51.30  ? 362 LYS B C     1 
ATOM   12331 O  O     A LYS B 2 362 ? 18.582  -37.595 21.393  0.20 51.09  ? 362 LYS B O     1 
ATOM   12332 O  O     B LYS B 2 362 ? 18.334  -37.359 21.774  0.80 51.32  ? 362 LYS B O     1 
ATOM   12333 C  CB    A LYS B 2 362 ? 19.830  -40.483 21.487  0.20 50.20  ? 362 LYS B CB    1 
ATOM   12334 C  CB    B LYS B 2 362 ? 20.103  -40.051 22.252  0.80 50.86  ? 362 LYS B CB    1 
ATOM   12335 C  CG    A LYS B 2 362 ? 18.527  -40.763 22.225  0.20 51.44  ? 362 LYS B CG    1 
ATOM   12336 C  CG    B LYS B 2 362 ? 19.849  -41.536 22.093  0.80 49.17  ? 362 LYS B CG    1 
ATOM   12337 C  CD    A LYS B 2 362 ? 18.703  -41.873 23.252  0.20 56.13  ? 362 LYS B CD    1 
ATOM   12338 C  CD    B LYS B 2 362 ? 19.963  -42.263 23.428  0.80 65.53  ? 362 LYS B CD    1 
ATOM   12339 C  CE    A LYS B 2 362 ? 17.364  -42.389 23.766  0.20 57.30  ? 362 LYS B CE    1 
ATOM   12340 C  CE    B LYS B 2 362 ? 18.741  -42.020 24.313  0.80 56.14  ? 362 LYS B CE    1 
ATOM   12341 N  NZ    A LYS B 2 362 ? 16.594  -41.357 24.516  0.20 43.32  ? 362 LYS B NZ    1 
ATOM   12342 N  NZ    B LYS B 2 362 ? 17.499  -42.614 23.730  0.80 58.33  ? 362 LYS B NZ    1 
ATOM   12343 N  N     A MET B 2 363 ? 20.792  -37.354 21.029  0.20 50.71  ? 363 MET B N     1 
ATOM   12344 N  N     B MET B 2 363 ? 20.525  -36.972 21.433  0.80 49.46  ? 363 MET B N     1 
ATOM   12345 C  CA    A MET B 2 363 ? 20.875  -35.974 21.478  0.20 48.88  ? 363 MET B CA    1 
ATOM   12346 C  CA    B MET B 2 363 ? 20.429  -35.547 21.701  0.80 50.11  ? 363 MET B CA    1 
ATOM   12347 C  C     A MET B 2 363 ? 21.389  -35.107 20.336  0.20 46.33  ? 363 MET B C     1 
ATOM   12348 C  C     B MET B 2 363 ? 21.448  -34.792 20.860  0.80 46.06  ? 363 MET B C     1 
ATOM   12349 O  O     A MET B 2 363 ? 21.996  -35.599 19.382  0.20 45.52  ? 363 MET B O     1 
ATOM   12350 O  O     B MET B 2 363 ? 22.584  -35.239 20.683  0.80 43.54  ? 363 MET B O     1 
ATOM   12351 C  CB    A MET B 2 363 ? 21.800  -35.835 22.696  0.20 49.66  ? 363 MET B CB    1 
ATOM   12352 C  CB    B MET B 2 363 ? 20.627  -35.238 23.186  0.80 53.03  ? 363 MET B CB    1 
ATOM   12353 C  CG    A MET B 2 363 ? 21.540  -36.834 23.818  0.20 54.79  ? 363 MET B CG    1 
ATOM   12354 C  CG    B MET B 2 363 ? 19.383  -35.507 24.012  0.80 54.94  ? 363 MET B CG    1 
ATOM   12355 S  SD    A MET B 2 363 ? 20.483  -36.201 25.137  0.20 54.95  ? 363 MET B SD    1 
ATOM   12356 S  SD    B MET B 2 363 ? 19.637  -35.274 25.768  0.80 57.18  ? 363 MET B SD    1 
ATOM   12357 C  CE    A MET B 2 363 ? 18.857  -36.387 24.413  0.20 51.72  ? 363 MET B CE    1 
ATOM   12358 C  CE    B MET B 2 363 ? 20.930  -36.473 26.069  0.80 64.06  ? 363 MET B CE    1 
ATOM   12359 N  N     A SER B 2 364 ? 21.139  -33.804 20.443  0.20 48.24  ? 364 SER B N     1 
ATOM   12360 N  N     B SER B 2 364 ? 21.019  -33.644 20.344  0.80 49.31  ? 364 SER B N     1 
ATOM   12361 C  CA    A SER B 2 364 ? 21.601  -32.852 19.440  0.20 42.45  ? 364 SER B CA    1 
ATOM   12362 C  CA    B SER B 2 364 ? 21.859  -32.770 19.544  0.80 40.69  ? 364 SER B CA    1 
ATOM   12363 C  C     A SER B 2 364 ? 21.470  -31.445 20.001  0.20 43.47  ? 364 SER B C     1 
ATOM   12364 C  C     B SER B 2 364 ? 21.569  -31.333 19.944  0.80 43.74  ? 364 SER B C     1 
ATOM   12365 O  O     A SER B 2 364 ? 20.758  -31.212 20.983  0.20 42.70  ? 364 SER B O     1 
ATOM   12366 O  O     B SER B 2 364 ? 20.586  -31.040 20.629  0.80 41.92  ? 364 SER B O     1 
ATOM   12367 C  CB    A SER B 2 364 ? 20.817  -32.976 18.129  0.20 44.91  ? 364 SER B CB    1 
ATOM   12368 C  CB    B SER B 2 364 ? 21.609  -32.964 18.045  0.80 44.84  ? 364 SER B CB    1 
ATOM   12369 O  OG    A SER B 2 364 ? 21.326  -32.089 17.147  0.20 44.01  ? 364 SER B OG    1 
ATOM   12370 O  OG    B SER B 2 364 ? 20.292  -32.564 17.696  0.80 46.91  ? 364 SER B OG    1 
ATOM   12371 N  N     A ALA B 2 365 ? 22.164  -30.508 19.357  0.20 41.08  ? 365 ALA B N     1 
ATOM   12372 N  N     B ALA B 2 365 ? 22.442  -30.429 19.519  0.80 39.66  ? 365 ALA B N     1 
ATOM   12373 C  CA    A ALA B 2 365 ? 22.119  -29.106 19.765  0.20 36.10  ? 365 ALA B CA    1 
ATOM   12374 C  CA    B ALA B 2 365 ? 22.209  -29.012 19.727  0.80 35.43  ? 365 ALA B CA    1 
ATOM   12375 C  C     A ALA B 2 365 ? 22.645  -28.268 18.609  0.20 36.98  ? 365 ALA B C     1 
ATOM   12376 C  C     B ALA B 2 365 ? 22.546  -28.283 18.440  0.80 35.98  ? 365 ALA B C     1 
ATOM   12377 O  O     A ALA B 2 365 ? 23.837  -28.334 18.292  0.20 40.44  ? 365 ALA B O     1 
ATOM   12378 O  O     B ALA B 2 365 ? 23.402  -28.725 17.668  0.80 40.45  ? 365 ALA B O     1 
ATOM   12379 C  CB    A ALA B 2 365 ? 22.939  -28.879 21.029  0.20 40.78  ? 365 ALA B CB    1 
ATOM   12380 C  CB    B ALA B 2 365 ? 23.036  -28.464 20.895  0.80 39.20  ? 365 ALA B CB    1 
ATOM   12381 N  N     A THR B 2 366 ? 21.768  -27.488 17.986  0.20 36.61  ? 366 THR B N     1 
ATOM   12382 N  N     B THR B 2 366 ? 21.857  -27.176 18.200  0.80 35.79  ? 366 THR B N     1 
ATOM   12383 C  CA    A THR B 2 366 ? 22.140  -26.633 16.868  0.20 37.23  ? 366 THR B CA    1 
ATOM   12384 C  CA    B THR B 2 366 ? 22.150  -26.337 17.045  0.80 37.17  ? 366 THR B CA    1 
ATOM   12385 C  C     A THR B 2 366 ? 22.240  -25.190 17.345  0.20 36.11  ? 366 THR B C     1 
ATOM   12386 C  C     B THR B 2 366 ? 22.247  -24.890 17.499  0.80 35.78  ? 366 THR B C     1 
ATOM   12387 O  O     A THR B 2 366 ? 21.373  -24.712 18.085  0.20 35.60  ? 366 THR B O     1 
ATOM   12388 O  O     B THR B 2 366 ? 21.402  -24.412 18.262  0.80 34.69  ? 366 THR B O     1 
ATOM   12389 C  CB    A THR B 2 366 ? 21.128  -26.753 15.726  0.20 38.05  ? 366 THR B CB    1 
ATOM   12390 C  CB    B THR B 2 366 ? 21.096  -26.507 15.953  0.80 37.51  ? 366 THR B CB    1 
ATOM   12391 O  OG1   A THR B 2 366 ? 21.019  -28.126 15.332  0.20 39.24  ? 366 THR B OG1   1 
ATOM   12392 O  OG1   B THR B 2 366 ? 21.036  -27.890 15.586  0.80 39.53  ? 366 THR B OG1   1 
ATOM   12393 C  CG2   A THR B 2 366 ? 21.571  -25.926 14.523  0.20 39.02  ? 366 THR B CG2   1 
ATOM   12394 C  CG2   B THR B 2 366 ? 21.466  -25.692 14.714  0.80 40.69  ? 366 THR B CG2   1 
ATOM   12395 N  N     A PHE B 2 367 ? 23.303  -24.508 16.931  0.20 34.79  ? 367 PHE B N     1 
ATOM   12396 N  N     B PHE B 2 367 ? 23.289  -24.211 17.037  0.80 33.84  ? 367 PHE B N     1 
ATOM   12397 C  CA    A PHE B 2 367 ? 23.574  -23.134 17.327  0.20 32.62  ? 367 PHE B CA    1 
ATOM   12398 C  CA    B PHE B 2 367 ? 23.618  -22.854 17.440  0.80 30.71  ? 367 PHE B CA    1 
ATOM   12399 C  C     A PHE B 2 367 ? 23.370  -22.200 16.142  0.20 34.94  ? 367 PHE B C     1 
ATOM   12400 C  C     B PHE B 2 367 ? 23.421  -21.925 16.251  0.80 36.10  ? 367 PHE B C     1 
ATOM   12401 O  O     A PHE B 2 367 ? 23.793  -22.502 15.022  0.20 32.69  ? 367 PHE B O     1 
ATOM   12402 O  O     B PHE B 2 367 ? 23.853  -22.245 15.138  0.80 32.66  ? 367 PHE B O     1 
ATOM   12403 C  CB    A PHE B 2 367 ? 25.002  -23.001 17.866  0.20 37.08  ? 367 PHE B CB    1 
ATOM   12404 C  CB    B PHE B 2 367 ? 25.065  -22.821 17.946  0.80 37.24  ? 367 PHE B CB    1 
ATOM   12405 C  CG    A PHE B 2 367 ? 25.442  -21.582 18.085  0.20 37.23  ? 367 PHE B CG    1 
ATOM   12406 C  CG    B PHE B 2 367 ? 25.639  -21.442 18.128  0.80 36.66  ? 367 PHE B CG    1 
ATOM   12407 C  CD1   A PHE B 2 367 ? 25.064  -20.894 19.226  0.20 38.67  ? 367 PHE B CD1   1 
ATOM   12408 C  CD1   B PHE B 2 367 ? 26.252  -20.786 17.073  0.80 36.28  ? 367 PHE B CD1   1 
ATOM   12409 C  CD2   A PHE B 2 367 ? 26.245  -20.940 17.157  0.20 36.59  ? 367 PHE B CD2   1 
ATOM   12410 C  CD2   B PHE B 2 367 ? 25.621  -20.830 19.371  0.80 40.04  ? 367 PHE B CD2   1 
ATOM   12411 C  CE1   A PHE B 2 367 ? 25.472  -19.593 19.432  0.20 38.25  ? 367 PHE B CE1   1 
ATOM   12412 C  CE1   B PHE B 2 367 ? 26.801  -19.532 17.246  0.80 40.43  ? 367 PHE B CE1   1 
ATOM   12413 C  CE2   A PHE B 2 367 ? 26.655  -19.638 17.358  0.20 40.00  ? 367 PHE B CE2   1 
ATOM   12414 C  CE2   B PHE B 2 367 ? 26.172  -19.581 19.549  0.80 40.34  ? 367 PHE B CE2   1 
ATOM   12415 C  CZ    A PHE B 2 367 ? 26.267  -18.964 18.499  0.20 39.94  ? 367 PHE B CZ    1 
ATOM   12416 C  CZ    B PHE B 2 367 ? 26.756  -18.931 18.486  0.80 44.13  ? 367 PHE B CZ    1 
ATOM   12417 N  N     A ILE B 2 368 ? 22.719  -21.066 16.395  0.20 32.01  ? 368 ILE B N     1 
ATOM   12418 N  N     B ILE B 2 368 ? 22.774  -20.782 16.478  0.80 31.68  ? 368 ILE B N     1 
ATOM   12419 C  CA    A ILE B 2 368 ? 22.516  -20.022 15.395  0.20 29.43  ? 368 ILE B CA    1 
ATOM   12420 C  CA    B ILE B 2 368 ? 22.680  -19.729 15.468  0.80 27.30  ? 368 ILE B CA    1 
ATOM   12421 C  C     A ILE B 2 368 ? 22.960  -18.709 16.023  0.20 31.29  ? 368 ILE B C     1 
ATOM   12422 C  C     B ILE B 2 368 ? 23.142  -18.432 16.111  0.80 32.05  ? 368 ILE B C     1 
ATOM   12423 O  O     A ILE B 2 368 ? 22.319  -18.215 16.959  0.20 31.37  ? 368 ILE B O     1 
ATOM   12424 O  O     B ILE B 2 368 ? 22.459  -17.890 16.992  0.80 29.71  ? 368 ILE B O     1 
ATOM   12425 C  CB    A ILE B 2 368 ? 21.059  -19.936 14.924  0.20 33.09  ? 368 ILE B CB    1 
ATOM   12426 C  CB    B ILE B 2 368 ? 21.267  -19.574 14.901  0.80 31.51  ? 368 ILE B CB    1 
ATOM   12427 C  CG1   A ILE B 2 368 ? 20.594  -21.285 14.370  0.20 35.82  ? 368 ILE B CG1   1 
ATOM   12428 C  CG1   B ILE B 2 368 ? 20.706  -20.938 14.495  0.80 37.42  ? 368 ILE B CG1   1 
ATOM   12429 C  CG2   A ILE B 2 368 ? 20.904  -18.838 13.887  0.20 30.91  ? 368 ILE B CG2   1 
ATOM   12430 C  CG2   B ILE B 2 368 ? 21.274  -18.617 13.733  0.80 30.70  ? 368 ILE B CG2   1 
ATOM   12431 C  CD1   A ILE B 2 368 ? 19.133  -21.311 13.971  0.20 37.23  ? 368 ILE B CD1   1 
ATOM   12432 C  CD1   B ILE B 2 368 ? 19.240  -20.899 14.128  0.80 39.50  ? 368 ILE B CD1   1 
ATOM   12433 N  N     A GLY B 2 369 ? 24.049  -18.141 15.514  0.20 31.73  ? 369 GLY B N     1 
ATOM   12434 N  N     B GLY B 2 369 ? 24.297  -17.933 15.680  0.80 31.75  ? 369 GLY B N     1 
ATOM   12435 C  CA    A GLY B 2 369 ? 24.649  -16.963 16.106  0.20 28.00  ? 369 GLY B CA    1 
ATOM   12436 C  CA    B GLY B 2 369 ? 24.805  -16.706 16.249  0.80 26.47  ? 369 GLY B CA    1 
ATOM   12437 C  C     A GLY B 2 369 ? 24.682  -15.781 15.157  0.20 27.97  ? 369 GLY B C     1 
ATOM   12438 C  C     B GLY B 2 369 ? 25.000  -15.572 15.269  0.80 28.67  ? 369 GLY B C     1 
ATOM   12439 O  O     A GLY B 2 369 ? 24.682  -15.941 13.935  0.20 25.51  ? 369 GLY B O     1 
ATOM   12440 O  O     B GLY B 2 369 ? 25.544  -15.762 14.178  0.80 26.97  ? 369 GLY B O     1 
ATOM   12441 N  N     A ASN B 2 370 ? 24.703  -14.588 15.738  0.20 27.83  ? 370 ASN B N     1 
ATOM   12442 N  N     B ASN B 2 370 ? 24.561  -14.379 15.654  0.80 27.40  ? 370 ASN B N     1 
ATOM   12443 C  CA    A ASN B 2 370 ? 24.924  -13.337 15.018  0.20 29.11  ? 370 ASN B CA    1 
ATOM   12444 C  CA    B ASN B 2 370 ? 24.932  -13.141 14.976  0.80 29.02  ? 370 ASN B CA    1 
ATOM   12445 C  C     A ASN B 2 370 ? 26.134  -12.651 15.651  0.20 30.36  ? 370 ASN B C     1 
ATOM   12446 C  C     B ASN B 2 370 ? 26.101  -12.553 15.771  0.80 30.56  ? 370 ASN B C     1 
ATOM   12447 O  O     A ASN B 2 370 ? 26.002  -11.639 16.345  0.20 29.29  ? 370 ASN B O     1 
ATOM   12448 O  O     B ASN B 2 370 ? 25.898  -11.932 16.816  0.80 29.06  ? 370 ASN B O     1 
ATOM   12449 C  CB    A ASN B 2 370 ? 23.661  -12.448 15.064  0.20 29.20  ? 370 ASN B CB    1 
ATOM   12450 C  CB    B ASN B 2 370 ? 23.737  -12.189 14.899  0.80 29.73  ? 370 ASN B CB    1 
ATOM   12451 C  CG    A ASN B 2 370 ? 23.733  -11.275 14.103  0.20 28.87  ? 370 ASN B CG    1 
ATOM   12452 C  CG    B ASN B 2 370 ? 23.933  -11.095 13.875  0.80 29.76  ? 370 ASN B CG    1 
ATOM   12453 O  OD1   A ASN B 2 370 ? 24.813  -10.871 13.673  0.20 31.34  ? 370 ASN B OD1   1 
ATOM   12454 O  OD1   B ASN B 2 370 ? 25.034  -10.912 13.356  0.80 32.32  ? 370 ASN B OD1   1 
ATOM   12455 N  ND2   A ASN B 2 370 ? 22.576  -10.721 13.761  0.20 28.13  ? 370 ASN B ND2   1 
ATOM   12456 N  ND2   B ASN B 2 370 ? 22.867  -10.373 13.560  0.80 27.11  ? 370 ASN B ND2   1 
ATOM   12457 N  N     A SER B 2 371 ? 27.317  -13.217 15.416  0.20 29.15  ? 371 SER B N     1 
ATOM   12458 N  N     B SER B 2 371 ? 27.332  -12.777 15.290  0.80 30.03  ? 371 SER B N     1 
ATOM   12459 C  CA    A SER B 2 371 ? 28.549  -12.792 16.069  0.20 29.39  ? 371 SER B CA    1 
ATOM   12460 C  CA    B SER B 2 371 ? 28.552  -12.398 16.001  0.80 30.49  ? 371 SER B CA    1 
ATOM   12461 C  C     A SER B 2 371 ? 29.331  -11.828 15.186  0.20 30.02  ? 371 SER B C     1 
ATOM   12462 C  C     B SER B 2 371 ? 29.413  -11.463 15.159  0.80 30.76  ? 371 SER B C     1 
ATOM   12463 O  O     A SER B 2 371 ? 29.416  -12.012 13.966  0.20 28.73  ? 371 SER B O     1 
ATOM   12464 O  O     B SER B 2 371 ? 29.555  -11.652 13.942  0.80 26.86  ? 371 SER B O     1 
ATOM   12465 C  CB    A SER B 2 371 ? 29.424  -14.002 16.405  0.20 30.67  ? 371 SER B CB    1 
ATOM   12466 C  CB    B SER B 2 371 ? 29.386  -13.624 16.377  0.80 30.70  ? 371 SER B CB    1 
ATOM   12467 O  OG    A SER B 2 371 ? 30.714  -13.608 16.847  0.20 26.92  ? 371 SER B OG    1 
ATOM   12468 O  OG    B SER B 2 371 ? 30.717  -13.259 16.738  0.80 25.49  ? 371 SER B OG    1 
ATOM   12469 N  N     A THR B 2 372 ? 29.913  -10.800 15.812  0.20 27.72  ? 372 THR B N     1 
ATOM   12470 N  N     B THR B 2 372 ? 30.006  -10.458 15.812  0.80 27.12  ? 372 THR B N     1 
ATOM   12471 C  CA    A THR B 2 372 ? 30.783  -9.890  15.075  0.20 30.45  ? 372 THR B CA    1 
ATOM   12472 C  CA    B THR B 2 372 ? 30.930  -9.591  15.084  0.80 30.84  ? 372 THR B CA    1 
ATOM   12473 C  C     A THR B 2 372 ? 32.053  -10.580 14.596  0.20 29.80  ? 372 THR B C     1 
ATOM   12474 C  C     B THR B 2 372 ? 32.160  -10.352 14.594  0.80 29.96  ? 372 THR B C     1 
ATOM   12475 O  O     A THR B 2 372 ? 32.748  -10.041 13.729  0.20 28.22  ? 372 THR B O     1 
ATOM   12476 O  O     B THR B 2 372 ? 32.873  -9.854  13.715  0.80 27.51  ? 372 THR B O     1 
ATOM   12477 C  CB    A THR B 2 372 ? 31.154  -8.680  15.936  0.20 30.66  ? 372 THR B CB    1 
ATOM   12478 C  CB    B THR B 2 372 ? 31.373  -8.409  15.954  0.80 30.23  ? 372 THR B CB    1 
ATOM   12479 O  OG1   A THR B 2 372 ? 31.968  -9.105  17.034  0.20 27.34  ? 372 THR B OG1   1 
ATOM   12480 O  OG1   B THR B 2 372 ? 32.135  -8.897  17.060  0.80 26.45  ? 372 THR B OG1   1 
ATOM   12481 C  CG2   A THR B 2 372 ? 29.900  -7.993  16.470  0.20 31.39  ? 372 THR B CG2   1 
ATOM   12482 C  CG2   B THR B 2 372 ? 30.160  -7.617  16.482  0.80 32.13  ? 372 THR B CG2   1 
ATOM   12483 N  N     A ALA B 2 373 ? 32.368  -11.760 15.138  0.20 30.82  ? 373 ALA B N     1 
ATOM   12484 N  N     B ALA B 2 373 ? 32.419  -11.549 15.134  0.80 31.42  ? 373 ALA B N     1 
ATOM   12485 C  CA    A ALA B 2 373 ? 33.530  -12.519 14.691  0.20 33.82  ? 373 ALA B CA    1 
ATOM   12486 C  CA    B ALA B 2 373 ? 33.594  -12.323 14.735  0.80 34.96  ? 373 ALA B CA    1 
ATOM   12487 C  C     A ALA B 2 373 ? 33.378  -13.049 13.271  0.20 31.34  ? 373 ALA B C     1 
ATOM   12488 C  C     B ALA B 2 373 ? 33.529  -12.788 13.283  0.80 32.17  ? 373 ALA B C     1 
ATOM   12489 O  O     A ALA B 2 373 ? 34.350  -13.581 12.722  0.20 29.71  ? 373 ALA B O     1 
ATOM   12490 O  O     B ALA B 2 373 ? 34.570  -13.149 12.713  0.80 27.96  ? 373 ALA B O     1 
ATOM   12491 C  CB    A ALA B 2 373 ? 33.797  -13.681 15.649  0.20 26.09  ? 373 ALA B CB    1 
ATOM   12492 C  CB    B ALA B 2 373 ? 33.763  -13.535 15.649  0.80 25.04  ? 373 ALA B CB    1 
ATOM   12493 N  N     A ILE B 2 374 ? 32.192  -12.918 12.669  0.20 31.90  ? 374 ILE B N     1 
ATOM   12494 N  N     B ILE B 2 374 ? 32.334  -12.795 12.680  0.80 32.59  ? 374 ILE B N     1 
ATOM   12495 C  CA    A ILE B 2 374 ? 31.988  -13.362 11.295  0.20 29.03  ? 374 ILE B CA    1 
ATOM   12496 C  CA    B ILE B 2 374 ? 32.174  -13.178 11.279  0.80 28.41  ? 374 ILE B CA    1 
ATOM   12497 C  C     A ILE B 2 374 ? 32.802  -12.531 10.312  0.20 31.41  ? 374 ILE B C     1 
ATOM   12498 C  C     B ILE B 2 374 ? 32.972  -12.267 10.356  0.80 33.66  ? 374 ILE B C     1 
ATOM   12499 O  O     A ILE B 2 374 ? 33.025  -12.966 9.175   0.20 27.02  ? 374 ILE B O     1 
ATOM   12500 O  O     B ILE B 2 374 ? 33.226  -12.626 9.197   0.80 23.64  ? 374 ILE B O     1 
ATOM   12501 C  CB    A ILE B 2 374 ? 30.487  -13.323 10.939  0.20 29.29  ? 374 ILE B CB    1 
ATOM   12502 C  CB    B ILE B 2 374 ? 30.678  -13.173 10.887  0.80 29.38  ? 374 ILE B CB    1 
ATOM   12503 C  CG1   A ILE B 2 374 ? 30.196  -14.170 9.696   0.20 30.52  ? 374 ILE B CG1   1 
ATOM   12504 C  CG1   B ILE B 2 374 ? 30.444  -13.883 9.546   0.80 31.56  ? 374 ILE B CG1   1 
ATOM   12505 C  CG2   A ILE B 2 374 ? 30.033  -11.895 10.708  0.20 24.19  ? 374 ILE B CG2   1 
ATOM   12506 C  CG2   B ILE B 2 374 ? 30.198  -11.770 10.751  0.80 22.67  ? 374 ILE B CG2   1 
ATOM   12507 C  CD1   A ILE B 2 374 ? 30.548  -15.632 9.846   0.20 32.67  ? 374 ILE B CD1   1 
ATOM   12508 C  CD1   B ILE B 2 374 ? 30.350  -15.383 9.619   0.80 32.83  ? 374 ILE B CD1   1 
ATOM   12509 N  N     A GLN B 2 375 ? 33.267  -11.344 10.716  0.20 30.45  ? 375 GLN B N     1 
ATOM   12510 N  N     B GLN B 2 375 ? 33.385  -11.088 10.837  0.80 29.83  ? 375 GLN B N     1 
ATOM   12511 C  CA    A GLN B 2 375 ? 34.119  -10.560 9.829   0.20 27.86  ? 375 GLN B CA    1 
ATOM   12512 C  CA    B GLN B 2 375 ? 34.219  -10.232 9.996   0.80 26.72  ? 375 GLN B CA    1 
ATOM   12513 C  C     A GLN B 2 375 ? 35.431  -11.272 9.524   0.20 30.44  ? 375 GLN B C     1 
ATOM   12514 C  C     B GLN B 2 375 ? 35.504  -10.926 9.555   0.80 32.31  ? 375 GLN B C     1 
ATOM   12515 O  O     A GLN B 2 375 ? 36.043  -10.998 8.485   0.20 28.07  ? 375 GLN B O     1 
ATOM   12516 O  O     B GLN B 2 375 ? 36.070  -10.552 8.520   0.80 26.54  ? 375 GLN B O     1 
ATOM   12517 C  CB    A GLN B 2 375 ? 34.391  -9.178  10.429  0.20 30.60  ? 375 GLN B CB    1 
ATOM   12518 C  CB    B GLN B 2 375 ? 34.556  -8.931  10.726  0.80 31.01  ? 375 GLN B CB    1 
ATOM   12519 C  CG    A GLN B 2 375 ? 35.105  -9.198  11.769  0.20 29.97  ? 375 GLN B CG    1 
ATOM   12520 C  CG    B GLN B 2 375 ? 35.399  -9.135  11.966  0.80 29.17  ? 375 GLN B CG    1 
ATOM   12521 C  CD    A GLN B 2 375 ? 35.244  -7.813  12.368  0.20 32.35  ? 375 GLN B CD    1 
ATOM   12522 C  CD    B GLN B 2 375 ? 35.925  -7.834  12.516  0.80 36.56  ? 375 GLN B CD    1 
ATOM   12523 O  OE1   A GLN B 2 375 ? 35.175  -6.809  11.659  0.20 33.90  ? 375 GLN B OE1   1 
ATOM   12524 O  OE1   B GLN B 2 375 ? 36.790  -7.196  11.907  0.80 39.93  ? 375 GLN B OE1   1 
ATOM   12525 N  NE2   A GLN B 2 375 ? 35.436  -7.751  13.681  0.20 33.90  ? 375 GLN B NE2   1 
ATOM   12526 N  NE2   B GLN B 2 375 ? 35.401  -7.421  13.669  0.80 34.12  ? 375 GLN B NE2   1 
ATOM   12527 N  N     A GLU B 2 376 ? 35.871  -12.185 10.396  0.20 26.81  ? 376 GLU B N     1 
ATOM   12528 N  N     B GLU B 2 376 ? 35.975  -11.930 10.302  0.80 25.18  ? 376 GLU B N     1 
ATOM   12529 C  CA    A GLU B 2 376 ? 37.040  -13.003 10.085  0.20 32.80  ? 376 GLU B CA    1 
ATOM   12530 C  CA    B GLU B 2 376 ? 37.196  -12.631 9.907   0.80 34.38  ? 376 GLU B CA    1 
ATOM   12531 C  C     A GLU B 2 376 ? 36.839  -13.806 8.806   0.20 29.51  ? 376 GLU B C     1 
ATOM   12532 C  C     B GLU B 2 376 ? 37.013  -13.400 8.599   0.80 32.64  ? 376 GLU B C     1 
ATOM   12533 O  O     A GLU B 2 376 ? 37.799  -14.048 8.063   0.20 30.46  ? 376 GLU B O     1 
ATOM   12534 O  O     B GLU B 2 376 ? 37.954  -13.510 7.790   0.80 28.43  ? 376 GLU B O     1 
ATOM   12535 C  CB    A GLU B 2 376 ? 37.349  -13.944 11.249  0.20 30.94  ? 376 GLU B CB    1 
ATOM   12536 C  CB    B GLU B 2 376 ? 37.633  -13.558 11.041  0.80 34.49  ? 376 GLU B CB    1 
ATOM   12537 C  CG    A GLU B 2 376 ? 37.926  -13.266 12.482  0.20 33.02  ? 376 GLU B CG    1 
ATOM   12538 C  CG    B GLU B 2 376 ? 38.064  -12.811 12.308  0.80 33.72  ? 376 GLU B CG    1 
ATOM   12539 C  CD    A GLU B 2 376 ? 38.325  -14.265 13.550  0.20 33.28  ? 376 GLU B CD    1 
ATOM   12540 C  CD    B GLU B 2 376 ? 38.763  -13.707 13.317  0.80 31.23  ? 376 GLU B CD    1 
ATOM   12541 O  OE1   A GLU B 2 376 ? 37.836  -15.414 13.502  0.20 32.91  ? 376 GLU B OE1   1 
ATOM   12542 O  OE1   B GLU B 2 376 ? 38.449  -14.914 13.376  0.80 34.46  ? 376 GLU B OE1   1 
ATOM   12543 O  OE2   A GLU B 2 376 ? 39.132  -13.907 14.433  0.20 33.20  ? 376 GLU B OE2   1 
ATOM   12544 O  OE2   B GLU B 2 376 ? 39.630  -13.200 14.054  0.80 37.11  ? 376 GLU B OE2   1 
ATOM   12545 N  N     A LEU B 2 377 ? 35.603  -14.228 8.533   0.20 30.69  ? 377 LEU B N     1 
ATOM   12546 N  N     B LEU B 2 377 ? 35.807  -13.914 8.358   0.80 30.70  ? 377 LEU B N     1 
ATOM   12547 C  CA    A LEU B 2 377 ? 35.322  -14.945 7.293   0.20 31.24  ? 377 LEU B CA    1 
ATOM   12548 C  CA    B LEU B 2 377 ? 35.504  -14.574 7.088   0.80 29.49  ? 377 LEU B CA    1 
ATOM   12549 C  C     A LEU B 2 377 ? 35.369  -14.011 6.092   0.20 28.99  ? 377 LEU B C     1 
ATOM   12550 C  C     B LEU B 2 377 ? 35.500  -13.568 5.945   0.80 32.12  ? 377 LEU B C     1 
ATOM   12551 O  O     A LEU B 2 377 ? 35.879  -14.383 5.028   0.20 28.79  ? 377 LEU B O     1 
ATOM   12552 O  O     B LEU B 2 377 ? 36.075  -13.812 4.867   0.80 25.14  ? 377 LEU B O     1 
ATOM   12553 C  CB    A LEU B 2 377 ? 33.961  -15.636 7.389   0.20 30.49  ? 377 LEU B CB    1 
ATOM   12554 C  CB    B LEU B 2 377 ? 34.151  -15.284 7.213   0.80 30.99  ? 377 LEU B CB    1 
ATOM   12555 C  CG    A LEU B 2 377 ? 33.334  -16.181 6.104   0.20 33.05  ? 377 LEU B CG    1 
ATOM   12556 C  CG    B LEU B 2 377 ? 33.547  -16.257 6.200   0.80 33.97  ? 377 LEU B CG    1 
ATOM   12557 C  CD1   A LEU B 2 377 ? 32.709  -17.543 6.364   0.20 32.03  ? 377 LEU B CD1   1 
ATOM   12558 C  CD1   B LEU B 2 377 ? 32.283  -16.874 6.814   0.80 31.32  ? 377 LEU B CD1   1 
ATOM   12559 C  CD2   A LEU B 2 377 ? 32.289  -15.214 5.562   0.20 28.54  ? 377 LEU B CD2   1 
ATOM   12560 C  CD2   B LEU B 2 377 ? 33.210  -15.575 4.898   0.80 36.11  ? 377 LEU B CD2   1 
ATOM   12561 N  N     A PHE B 2 378 ? 34.841  -12.793 6.243   0.20 27.61  ? 378 PHE B N     1 
ATOM   12562 N  N     B PHE B 2 378 ? 34.850  -12.426 6.162   0.80 26.37  ? 378 PHE B N     1 
ATOM   12563 C  CA    A PHE B 2 378 ? 34.809  -11.857 5.123   0.20 28.98  ? 378 PHE B CA    1 
ATOM   12564 C  CA    B PHE B 2 378 ? 34.830  -11.383 5.148   0.80 28.35  ? 378 PHE B CA    1 
ATOM   12565 C  C     A PHE B 2 378 ? 36.204  -11.338 4.789   0.20 29.58  ? 378 PHE B C     1 
ATOM   12566 C  C     B PHE B 2 378 ? 36.218  -10.786 4.926   0.80 30.45  ? 378 PHE B C     1 
ATOM   12567 O  O     A PHE B 2 378 ? 36.563  -11.234 3.610   0.20 27.12  ? 378 PHE B O     1 
ATOM   12568 O  O     B PHE B 2 378 ? 36.570  -10.457 3.790   0.80 30.12  ? 378 PHE B O     1 
ATOM   12569 C  CB    A PHE B 2 378 ? 33.858  -10.700 5.432   0.20 27.32  ? 378 PHE B CB    1 
ATOM   12570 C  CB    B PHE B 2 378 ? 33.799  -10.322 5.540   0.80 25.04  ? 378 PHE B CB    1 
ATOM   12571 C  CG    A PHE B 2 378 ? 32.405  -11.098 5.470   0.20 28.89  ? 378 PHE B CG    1 
ATOM   12572 C  CG    B PHE B 2 378 ? 32.369  -10.827 5.508   0.80 29.25  ? 378 PHE B CG    1 
ATOM   12573 C  CD1   A PHE B 2 378 ? 31.699  -11.308 4.297   0.20 28.04  ? 378 PHE B CD1   1 
ATOM   12574 C  CD1   B PHE B 2 378 ? 31.885  -11.505 4.398   0.80 27.19  ? 378 PHE B CD1   1 
ATOM   12575 C  CD2   A PHE B 2 378 ? 31.744  -11.249 6.680   0.20 28.65  ? 378 PHE B CD2   1 
ATOM   12576 C  CD2   B PHE B 2 378 ? 31.522  -10.640 6.601   0.80 31.18  ? 378 PHE B CD2   1 
ATOM   12577 C  CE1   A PHE B 2 378 ? 30.365  -11.669 4.326   0.20 27.48  ? 378 PHE B CE1   1 
ATOM   12578 C  CE1   B PHE B 2 378 ? 30.580  -11.972 4.356   0.80 25.41  ? 378 PHE B CE1   1 
ATOM   12579 C  CE2   A PHE B 2 378 ? 30.410  -11.608 6.718   0.20 30.16  ? 378 PHE B CE2   1 
ATOM   12580 C  CE2   B PHE B 2 378 ? 30.209  -11.104 6.571   0.80 30.08  ? 378 PHE B CE2   1 
ATOM   12581 C  CZ    A PHE B 2 378 ? 29.717  -11.817 5.542   0.20 30.19  ? 378 PHE B CZ    1 
ATOM   12582 C  CZ    B PHE B 2 378 ? 29.734  -11.766 5.458   0.80 30.26  ? 378 PHE B CZ    1 
ATOM   12583 N  N     A LYS B 2 379 ? 37.002  -11.008 5.810   0.20 29.40  ? 379 LYS B N     1 
ATOM   12584 N  N     B LYS B 2 379 ? 37.027  -10.670 5.980   0.80 29.06  ? 379 LYS B N     1 
ATOM   12585 C  CA    A LYS B 2 379 ? 38.361  -10.530 5.566   0.20 28.38  ? 379 LYS B CA    1 
ATOM   12586 C  CA    B LYS B 2 379 ? 38.400  -10.201 5.802   0.80 28.52  ? 379 LYS B CA    1 
ATOM   12587 C  C     A LYS B 2 379 ? 39.177  -11.557 4.792   0.20 30.62  ? 379 LYS B C     1 
ATOM   12588 C  C     B LYS B 2 379 ? 39.213  -11.168 4.956   0.80 31.95  ? 379 LYS B C     1 
ATOM   12589 O  O     A LYS B 2 379 ? 39.971  -11.197 3.916   0.20 28.35  ? 379 LYS B O     1 
ATOM   12590 O  O     B LYS B 2 379 ? 40.017  -10.743 4.115   0.80 26.00  ? 379 LYS B O     1 
ATOM   12591 C  CB    A LYS B 2 379 ? 39.055  -10.200 6.887   0.20 34.86  ? 379 LYS B CB    1 
ATOM   12592 C  CB    B LYS B 2 379 ? 39.084  -10.022 7.156   0.80 36.59  ? 379 LYS B CB    1 
ATOM   12593 C  CG    A LYS B 2 379 ? 38.428  -9.075  7.689   0.20 32.00  ? 379 LYS B CG    1 
ATOM   12594 C  CG    B LYS B 2 379 ? 38.691  -8.803  7.938   0.80 33.58  ? 379 LYS B CG    1 
ATOM   12595 C  CD    A LYS B 2 379 ? 39.189  -8.888  8.992   0.20 34.97  ? 379 LYS B CD    1 
ATOM   12596 C  CD    B LYS B 2 379 ? 39.691  -8.630  9.066   0.80 34.79  ? 379 LYS B CD    1 
ATOM   12597 C  CE    A LYS B 2 379 ? 38.532  -7.868  9.895   0.20 34.82  ? 379 LYS B CE    1 
ATOM   12598 C  CE    B LYS B 2 379 ? 39.359  -7.440  9.917   0.80 36.45  ? 379 LYS B CE    1 
ATOM   12599 N  NZ    A LYS B 2 379 ? 39.231  -7.782  11.209  0.20 37.65  ? 379 LYS B NZ    1 
ATOM   12600 N  NZ    B LYS B 2 379 ? 40.161  -7.472  11.179  0.80 37.65  ? 379 LYS B NZ    1 
ATOM   12601 N  N     A ARG B 2 380 ? 38.998  -12.843 5.109   0.20 27.95  ? 380 ARG B N     1 
ATOM   12602 N  N     B ARG B 2 380 ? 39.036  -12.473 5.182   0.80 26.38  ? 380 ARG B N     1 
ATOM   12603 C  CA    A ARG B 2 380 ? 39.697  -13.894 4.376   0.20 30.50  ? 380 ARG B CA    1 
ATOM   12604 C  CA    B ARG B 2 380 ? 39.754  -13.479 4.402   0.80 31.29  ? 380 ARG B CA    1 
ATOM   12605 C  C     A ARG B 2 380 ? 39.337  -13.864 2.897   0.20 29.43  ? 380 ARG B C     1 
ATOM   12606 C  C     B ARG B 2 380 ? 39.427  -13.357 2.918   0.80 30.92  ? 380 ARG B C     1 
ATOM   12607 O  O     A ARG B 2 380 ? 40.199  -14.066 2.033   0.20 28.66  ? 380 ARG B O     1 
ATOM   12608 O  O     B ARG B 2 380 ? 40.327  -13.288 2.068   0.80 27.01  ? 380 ARG B O     1 
ATOM   12609 C  CB    A ARG B 2 380 ? 39.360  -15.257 4.980   0.20 30.89  ? 380 ARG B CB    1 
ATOM   12610 C  CB    B ARG B 2 380 ? 39.400  -14.874 4.922   0.80 30.93  ? 380 ARG B CB    1 
ATOM   12611 C  CG    A ARG B 2 380 ? 40.179  -16.416 4.428   0.20 31.42  ? 380 ARG B CG    1 
ATOM   12612 C  CG    B ARG B 2 380 ? 40.276  -16.026 4.400   0.80 30.33  ? 380 ARG B CG    1 
ATOM   12613 C  CD    A ARG B 2 380 ? 39.535  -17.745 4.801   0.20 30.01  ? 380 ARG B CD    1 
ATOM   12614 C  CD    B ARG B 2 380 ? 39.708  -17.377 4.887   0.80 29.94  ? 380 ARG B CD    1 
ATOM   12615 N  NE    A ARG B 2 380 ? 38.347  -18.015 3.998   0.20 29.83  ? 380 ARG B NE    1 
ATOM   12616 N  NE    B ARG B 2 380 ? 38.650  -17.903 4.026   0.80 29.59  ? 380 ARG B NE    1 
ATOM   12617 C  CZ    A ARG B 2 380 ? 37.332  -18.776 4.387   0.20 30.97  ? 380 ARG B CZ    1 
ATOM   12618 C  CZ    B ARG B 2 380 ? 37.514  -18.436 4.464   0.80 32.13  ? 380 ARG B CZ    1 
ATOM   12619 N  NH1   A ARG B 2 380 ? 37.300  -19.326 5.590   0.20 29.64  ? 380 ARG B NH1   1 
ATOM   12620 N  NH1   B ARG B 2 380 ? 37.204  -18.444 5.753   0.80 26.04  ? 380 ARG B NH1   1 
ATOM   12621 N  NH2   A ARG B 2 380 ? 36.317  -18.981 3.550   0.20 29.21  ? 380 ARG B NH2   1 
ATOM   12622 N  NH2   B ARG B 2 380 ? 36.658  -18.960 3.586   0.80 30.11  ? 380 ARG B NH2   1 
ATOM   12623 N  N     A ILE B 2 381 ? 38.065  -13.609 2.586   0.20 27.55  ? 381 ILE B N     1 
ATOM   12624 N  N     B ILE B 2 381 ? 38.134  -13.327 2.585   0.80 26.35  ? 381 ILE B N     1 
ATOM   12625 C  CA    A ILE B 2 381 ? 37.641  -13.540 1.192   0.20 27.73  ? 381 ILE B CA    1 
ATOM   12626 C  CA    B ILE B 2 381 ? 37.727  -13.226 1.188   0.80 27.09  ? 381 ILE B CA    1 
ATOM   12627 C  C     A ILE B 2 381 ? 38.166  -12.270 0.538   0.20 26.49  ? 381 ILE B C     1 
ATOM   12628 C  C     B ILE B 2 381 ? 38.160  -11.889 0.614   0.80 24.45  ? 381 ILE B C     1 
ATOM   12629 O  O     A ILE B 2 381 ? 38.671  -12.301 -0.591  0.20 27.95  ? 381 ILE B O     1 
ATOM   12630 O  O     B ILE B 2 381 ? 38.560  -11.802 -0.555  0.80 30.25  ? 381 ILE B O     1 
ATOM   12631 C  CB    A ILE B 2 381 ? 36.107  -13.632 1.095   0.20 31.59  ? 381 ILE B CB    1 
ATOM   12632 C  CB    B ILE B 2 381 ? 36.204  -13.445 1.056   0.80 32.49  ? 381 ILE B CB    1 
ATOM   12633 C  CG1   A ILE B 2 381 ? 35.599  -14.898 1.788   0.20 30.13  ? 381 ILE B CG1   1 
ATOM   12634 C  CG1   B ILE B 2 381 ? 35.814  -14.859 1.500   0.80 30.11  ? 381 ILE B CG1   1 
ATOM   12635 C  CG2   A ILE B 2 381 ? 35.663  -13.602 -0.360  0.20 28.15  ? 381 ILE B CG2   1 
ATOM   12636 C  CG2   B ILE B 2 381 ? 35.748  -13.214 -0.373  0.80 28.24  ? 381 ILE B CG2   1 
ATOM   12637 C  CD1   A ILE B 2 381 ? 34.092  -15.065 1.722   0.20 30.91  ? 381 ILE B CD1   1 
ATOM   12638 C  CD1   B ILE B 2 381 ? 34.292  -15.094 1.512   0.80 32.23  ? 381 ILE B CD1   1 
ATOM   12639 N  N     A SER B 2 382 ? 38.071  -11.138 1.241   0.20 24.06  ? 382 SER B N     1 
ATOM   12640 N  N     B SER B 2 382 ? 38.142  -10.839 1.431   0.80 22.34  ? 382 SER B N     1 
ATOM   12641 C  CA    A SER B 2 382 ? 38.445  -9.854  0.654   0.20 26.92  ? 382 SER B CA    1 
ATOM   12642 C  CA    B SER B 2 382 ? 38.576  -9.523  0.973   0.80 26.43  ? 382 SER B CA    1 
ATOM   12643 C  C     A SER B 2 382 ? 39.939  -9.784  0.355   0.20 29.58  ? 382 SER B C     1 
ATOM   12644 C  C     B SER B 2 382 ? 40.058  -9.510  0.608   0.80 30.95  ? 382 SER B C     1 
ATOM   12645 O  O     A SER B 2 382 ? 40.346  -9.209  -0.662  0.20 28.39  ? 382 SER B O     1 
ATOM   12646 O  O     B SER B 2 382 ? 40.463  -8.872  -0.375  0.80 28.80  ? 382 SER B O     1 
ATOM   12647 C  CB    A SER B 2 382 ? 38.032  -8.715  1.587   0.20 29.26  ? 382 SER B CB    1 
ATOM   12648 C  CB    B SER B 2 382 ? 38.291  -8.481  2.053   0.80 26.95  ? 382 SER B CB    1 
ATOM   12649 O  OG    A SER B 2 382 ? 38.319  -7.452  1.012   0.20 30.66  ? 382 SER B OG    1 
ATOM   12650 O  OG    B SER B 2 382 ? 38.551  -7.185  1.540   0.80 35.09  ? 382 SER B OG    1 
ATOM   12651 N  N     A GLU B 2 383 ? 40.773  -10.354 1.229   0.20 26.30  ? 383 GLU B N     1 
ATOM   12652 N  N     B GLU B 2 383 ? 40.892  -10.183 1.400   0.80 25.46  ? 383 GLU B N     1 
ATOM   12653 C  CA    A GLU B 2 383 ? 42.213  -10.318 0.987   0.20 29.51  ? 383 GLU B CA    1 
ATOM   12654 C  CA    B GLU B 2 383 ? 42.320  -10.209 1.084   0.80 29.63  ? 383 GLU B CA    1 
ATOM   12655 C  C     A GLU B 2 383 ? 42.586  -11.110 -0.259  0.20 29.39  ? 383 GLU B C     1 
ATOM   12656 C  C     B GLU B 2 383 ? 42.566  -10.895 -0.255  0.80 29.34  ? 383 GLU B C     1 
ATOM   12657 O  O     A GLU B 2 383 ? 43.535  -10.747 -0.966  0.20 29.36  ? 383 GLU B O     1 
ATOM   12658 O  O     B GLU B 2 383 ? 43.333  -10.392 -1.090  0.80 30.03  ? 383 GLU B O     1 
ATOM   12659 C  CB    A GLU B 2 383 ? 42.967  -10.847 2.210   0.20 30.65  ? 383 GLU B CB    1 
ATOM   12660 C  CB    B GLU B 2 383 ? 43.095  -10.906 2.211   0.80 30.57  ? 383 GLU B CB    1 
ATOM   12661 C  CG    A GLU B 2 383 ? 44.458  -10.538 2.206   0.20 34.06  ? 383 GLU B CG    1 
ATOM   12662 C  CG    B GLU B 2 383 ? 44.620  -10.803 2.105   0.80 33.96  ? 383 GLU B CG    1 
ATOM   12663 C  CD    A GLU B 2 383 ? 45.140  -10.943 3.499   0.20 37.70  ? 383 GLU B CD    1 
ATOM   12664 C  CD    B GLU B 2 383 ? 45.337  -11.579 3.207   0.80 37.93  ? 383 GLU B CD    1 
ATOM   12665 O  OE1   A GLU B 2 383 ? 44.576  -11.783 4.232   0.20 40.27  ? 383 GLU B OE1   1 
ATOM   12666 O  OE1   B GLU B 2 383 ? 44.676  -12.378 3.906   0.80 42.88  ? 383 GLU B OE1   1 
ATOM   12667 O  OE2   A GLU B 2 383 ? 46.236  -10.418 3.787   0.20 31.33  ? 383 GLU B OE2   1 
ATOM   12668 O  OE2   B GLU B 2 383 ? 46.563  -11.389 3.372   0.80 43.92  ? 383 GLU B OE2   1 
ATOM   12669 N  N     A GLN B 2 384 ? 41.855  -12.192 -0.542  0.20 28.06  ? 384 GLN B N     1 
ATOM   12670 N  N     B GLN B 2 384 ? 41.901  -12.035 -0.484  0.80 27.95  ? 384 GLN B N     1 
ATOM   12671 C  CA    A GLN B 2 384 ? 42.047  -12.914 -1.794  0.20 27.39  ? 384 GLN B CA    1 
ATOM   12672 C  CA    B GLN B 2 384 ? 42.112  -12.818 -1.698  0.80 26.82  ? 384 GLN B CA    1 
ATOM   12673 C  C     A GLN B 2 384 ? 41.509  -12.121 -2.978  0.20 30.25  ? 384 GLN B C     1 
ATOM   12674 C  C     B GLN B 2 384 ? 41.560  -12.106 -2.924  0.80 30.55  ? 384 GLN B C     1 
ATOM   12675 O  O     A GLN B 2 384 ? 42.070  -12.190 -4.078  0.20 29.82  ? 384 GLN B O     1 
ATOM   12676 O  O     B GLN B 2 384 ? 42.194  -12.109 -3.989  0.80 30.01  ? 384 GLN B O     1 
ATOM   12677 C  CB    A GLN B 2 384 ? 41.369  -14.281 -1.715  0.20 29.30  ? 384 GLN B CB    1 
ATOM   12678 C  CB    B GLN B 2 384 ? 41.457  -14.189 -1.537  0.80 29.46  ? 384 GLN B CB    1 
ATOM   12679 C  CG    A GLN B 2 384 ? 41.899  -15.179 -0.606  0.20 29.51  ? 384 GLN B CG    1 
ATOM   12680 C  CG    B GLN B 2 384 ? 42.025  -14.998 -0.372  0.80 28.70  ? 384 GLN B CG    1 
ATOM   12681 C  CD    A GLN B 2 384 ? 41.158  -16.499 -0.523  0.20 31.36  ? 384 GLN B CD    1 
ATOM   12682 C  CD    B GLN B 2 384 ? 41.264  -16.279 -0.117  0.80 30.48  ? 384 GLN B CD    1 
ATOM   12683 O  OE1   A GLN B 2 384 ? 39.998  -16.600 -0.928  0.20 31.24  ? 384 GLN B OE1   1 
ATOM   12684 O  OE1   B GLN B 2 384 ? 40.167  -16.485 -0.642  0.80 32.91  ? 384 GLN B OE1   1 
ATOM   12685 N  NE2   A GLN B 2 384 ? 41.826  -17.519 -0.001  0.20 31.78  ? 384 GLN B NE2   1 
ATOM   12686 N  NE2   B GLN B 2 384 ? 41.835  -17.144 0.700   0.80 31.62  ? 384 GLN B NE2   1 
ATOM   12687 N  N     A PHE B 2 385 ? 40.421  -11.375 -2.772  0.20 26.38  ? 385 PHE B N     1 
ATOM   12688 N  N     B PHE B 2 385 ? 40.359  -11.536 -2.806  0.80 25.95  ? 385 PHE B N     1 
ATOM   12689 C  CA    A PHE B 2 385 ? 39.913  -10.483 -3.809  0.20 27.66  ? 385 PHE B CA    1 
ATOM   12690 C  CA    B PHE B 2 385 ? 39.821  -10.672 -3.853  0.80 27.33  ? 385 PHE B CA    1 
ATOM   12691 C  C     A PHE B 2 385 ? 40.873  -9.324  -4.048  0.20 30.87  ? 385 PHE B C     1 
ATOM   12692 C  C     B PHE B 2 385 ? 40.839  -9.610  -4.245  0.80 32.73  ? 385 PHE B C     1 
ATOM   12693 O  O     A PHE B 2 385 ? 41.048  -8.876  -5.188  0.20 29.23  ? 385 PHE B O     1 
ATOM   12694 O  O     B PHE B 2 385 ? 41.150  -9.434  -5.432  0.80 28.18  ? 385 PHE B O     1 
ATOM   12695 C  CB    A PHE B 2 385 ? 38.526  -9.970  -3.411  0.20 27.34  ? 385 PHE B CB    1 
ATOM   12696 C  CB    B PHE B 2 385 ? 38.517  -10.017 -3.367  0.80 27.16  ? 385 PHE B CB    1 
ATOM   12697 C  CG    A PHE B 2 385 ? 37.871  -9.097  -4.447  0.20 28.55  ? 385 PHE B CG    1 
ATOM   12698 C  CG    B PHE B 2 385 ? 37.943  -9.005  -4.328  0.80 28.35  ? 385 PHE B CG    1 
ATOM   12699 C  CD1   A PHE B 2 385 ? 38.076  -7.727  -4.453  0.20 30.20  ? 385 PHE B CD1   1 
ATOM   12700 C  CD1   B PHE B 2 385 ? 38.419  -7.705  -4.369  0.80 29.17  ? 385 PHE B CD1   1 
ATOM   12701 C  CD2   A PHE B 2 385 ? 37.034  -9.647  -5.404  0.20 28.84  ? 385 PHE B CD2   1 
ATOM   12702 C  CD2   B PHE B 2 385 ? 36.919  -9.358  -5.187  0.80 27.12  ? 385 PHE B CD2   1 
ATOM   12703 C  CE1   A PHE B 2 385 ? 37.470  -6.923  -5.401  0.20 32.40  ? 385 PHE B CE1   1 
ATOM   12704 C  CE1   B PHE B 2 385 ? 37.895  -6.782  -5.261  0.80 31.50  ? 385 PHE B CE1   1 
ATOM   12705 C  CE2   A PHE B 2 385 ? 36.424  -8.848  -6.355  0.20 29.91  ? 385 PHE B CE2   1 
ATOM   12706 C  CE2   B PHE B 2 385 ? 36.387  -8.441  -6.076  0.80 30.52  ? 385 PHE B CE2   1 
ATOM   12707 C  CZ    A PHE B 2 385 ? 36.641  -7.485  -6.353  0.20 31.38  ? 385 PHE B CZ    1 
ATOM   12708 C  CZ    B PHE B 2 385 ? 36.869  -7.151  -6.108  0.80 32.43  ? 385 PHE B CZ    1 
ATOM   12709 N  N     A THR B 2 386 ? 41.502  -8.824  -2.980  0.20 28.04  ? 386 THR B N     1 
ATOM   12710 N  N     B THR B 2 386 ? 41.358  -8.881  -3.249  0.80 27.90  ? 386 THR B N     1 
ATOM   12711 C  CA    A THR B 2 386 ? 42.461  -7.734  -3.127  0.20 27.96  ? 386 THR B CA    1 
ATOM   12712 C  CA    B THR B 2 386 ? 42.264  -7.771  -3.529  0.80 27.16  ? 386 THR B CA    1 
ATOM   12713 C  C     A THR B 2 386 ? 43.724  -8.200  -3.846  0.20 30.69  ? 386 THR B C     1 
ATOM   12714 C  C     B THR B 2 386 ? 43.567  -8.250  -4.172  0.80 32.55  ? 386 THR B C     1 
ATOM   12715 O  O     A THR B 2 386 ? 44.276  -7.468  -4.676  0.20 27.95  ? 386 THR B O     1 
ATOM   12716 O  O     B THR B 2 386 ? 44.088  -7.592  -5.082  0.80 27.43  ? 386 THR B O     1 
ATOM   12717 C  CB    A THR B 2 386 ? 42.807  -7.153  -1.755  0.20 29.17  ? 386 THR B CB    1 
ATOM   12718 C  CB    B THR B 2 386 ? 42.531  -6.992  -2.240  0.80 28.20  ? 386 THR B CB    1 
ATOM   12719 O  OG1   A THR B 2 386 ? 41.605  -6.751  -1.085  0.20 31.94  ? 386 THR B OG1   1 
ATOM   12720 O  OG1   B THR B 2 386 ? 41.384  -6.187  -1.927  0.80 37.16  ? 386 THR B OG1   1 
ATOM   12721 C  CG2   A THR B 2 386 ? 43.717  -5.946  -1.902  0.20 30.13  ? 386 THR B CG2   1 
ATOM   12722 C  CG2   B THR B 2 386 ? 43.742  -6.087  -2.373  0.80 30.26  ? 386 THR B CG2   1 
ATOM   12723 N  N     A ALA B 2 387 ? 44.195  -9.414  -3.549  0.20 25.65  ? 387 ALA B N     1 
ATOM   12724 N  N     B ALA B 2 387 ? 44.110  -9.392  -3.725  0.80 25.04  ? 387 ALA B N     1 
ATOM   12725 C  CA    A ALA B 2 387 ? 45.411  -9.908  -4.189  0.20 26.66  ? 387 ALA B CA    1 
ATOM   12726 C  CA    B ALA B 2 387 ? 45.336  -9.901  -4.342  0.80 26.21  ? 387 ALA B CA    1 
ATOM   12727 C  C     A ALA B 2 387 ? 45.209  -10.221 -5.664  0.20 31.99  ? 387 ALA B C     1 
ATOM   12728 C  C     B ALA B 2 387 ? 45.148  -10.116 -5.834  0.80 33.33  ? 387 ALA B C     1 
ATOM   12729 O  O     A ALA B 2 387 ? 46.196  -10.292 -6.409  0.20 28.09  ? 387 ALA B O     1 
ATOM   12730 O  O     B ALA B 2 387 ? 45.957  -9.652  -6.647  0.80 31.68  ? 387 ALA B O     1 
ATOM   12731 C  CB    A ALA B 2 387 ? 45.923  -11.154 -3.467  0.20 25.86  ? 387 ALA B CB    1 
ATOM   12732 C  CB    B ALA B 2 387 ? 45.780  -11.200 -3.678  0.80 25.05  ? 387 ALA B CB    1 
ATOM   12733 N  N     A MET B 2 388 ? 43.965  -10.410 -6.103  0.20 29.14  ? 388 MET B N     1 
ATOM   12734 N  N     B MET B 2 388 ? 44.089  -10.838 -6.211  0.80 29.20  ? 388 MET B N     1 
ATOM   12735 C  CA    A MET B 2 388 ? 43.666  -10.751 -7.489  0.20 29.13  ? 388 MET B CA    1 
ATOM   12736 C  CA    B MET B 2 388 ? 43.778  -11.028 -7.624  0.80 29.14  ? 388 MET B CA    1 
ATOM   12737 C  C     A MET B 2 388 ? 43.280  -9.537  -8.321  0.20 30.34  ? 388 MET B C     1 
ATOM   12738 C  C     B MET B 2 388 ? 43.460  -9.702  -8.301  0.80 30.34  ? 388 MET B C     1 
ATOM   12739 O  O     A MET B 2 388 ? 43.811  -9.342  -9.419  0.20 28.06  ? 388 MET B O     1 
ATOM   12740 O  O     B MET B 2 388 ? 43.906  -9.447  -9.427  0.80 27.38  ? 388 MET B O     1 
ATOM   12741 C  CB    A MET B 2 388 ? 42.543  -11.794 -7.538  0.20 27.66  ? 388 MET B CB    1 
ATOM   12742 C  CB    B MET B 2 388 ? 42.603  -12.002 -7.774  0.80 27.39  ? 388 MET B CB    1 
ATOM   12743 C  CG    A MET B 2 388 ? 42.996  -13.182 -7.137  0.20 28.26  ? 388 MET B CG    1 
ATOM   12744 C  CG    B MET B 2 388 ? 42.940  -13.457 -7.445  0.80 28.08  ? 388 MET B CG    1 
ATOM   12745 S  SD    A MET B 2 388 ? 44.233  -13.804 -8.287  0.20 26.50  ? 388 MET B SD    1 
ATOM   12746 S  SD    B MET B 2 388 ? 43.776  -14.341 -8.791  0.80 30.41  ? 388 MET B SD    1 
ATOM   12747 C  CE    A MET B 2 388 ? 43.211  -14.119 -9.724  0.20 28.26  ? 388 MET B CE    1 
ATOM   12748 C  CE    B MET B 2 388 ? 42.428  -14.541 -9.945  0.80 30.19  ? 388 MET B CE    1 
ATOM   12749 N  N     A PHE B 2 389 ? 42.361  -8.711  -7.814  0.20 30.65  ? 389 PHE B N     1 
ATOM   12750 N  N     B PHE B 2 389 ? 42.694  -8.839  -7.626  0.80 31.97  ? 389 PHE B N     1 
ATOM   12751 C  CA    A PHE B 2 389 ? 41.896  -7.559  -8.578  0.20 30.38  ? 389 PHE B CA    1 
ATOM   12752 C  CA    B PHE B 2 389 ? 42.204  -7.620  -8.266  0.80 30.22  ? 389 PHE B CA    1 
ATOM   12753 C  C     A PHE B 2 389 ? 42.994  -6.519  -8.760  0.20 30.96  ? 389 PHE B C     1 
ATOM   12754 C  C     B PHE B 2 389 ? 43.334  -6.637  -8.554  0.80 30.38  ? 389 PHE B C     1 
ATOM   12755 O  O     A PHE B 2 389 ? 42.952  -5.744  -9.722  0.20 34.11  ? 389 PHE B O     1 
ATOM   12756 O  O     B PHE B 2 389 ? 43.327  -5.979  -9.600  0.80 36.97  ? 389 PHE B O     1 
ATOM   12757 C  CB    A PHE B 2 389 ? 40.678  -6.936  -7.895  0.20 30.54  ? 389 PHE B CB    1 
ATOM   12758 C  CB    B PHE B 2 389 ? 41.129  -6.957  -7.396  0.80 27.88  ? 389 PHE B CB    1 
ATOM   12759 C  CG    A PHE B 2 389 ? 40.110  -5.756  -8.630  0.20 33.51  ? 389 PHE B CG    1 
ATOM   12760 C  CG    B PHE B 2 389 ? 40.406  -5.830  -8.081  0.80 33.60  ? 389 PHE B CG    1 
ATOM   12761 C  CD1   A PHE B 2 389 ? 39.303  -5.939  -9.742  0.20 34.88  ? 389 PHE B CD1   1 
ATOM   12762 C  CD1   B PHE B 2 389 ? 39.839  -6.016  -9.331  0.80 32.92  ? 389 PHE B CD1   1 
ATOM   12763 C  CD2   A PHE B 2 389 ? 40.382  -4.464  -8.212  0.20 36.12  ? 389 PHE B CD2   1 
ATOM   12764 C  CD2   B PHE B 2 389 ? 40.295  -4.585  -7.477  0.80 38.29  ? 389 PHE B CD2   1 
ATOM   12765 C  CE1   A PHE B 2 389 ? 38.779  -4.855  -10.423 0.20 36.88  ? 389 PHE B CE1   1 
ATOM   12766 C  CE1   B PHE B 2 389 ? 39.174  -4.978  -9.974  0.80 38.83  ? 389 PHE B CE1   1 
ATOM   12767 C  CE2   A PHE B 2 389 ? 39.860  -3.376  -8.887  0.20 38.22  ? 389 PHE B CE2   1 
ATOM   12768 C  CE2   B PHE B 2 389 ? 39.629  -3.542  -8.112  0.80 40.67  ? 389 PHE B CE2   1 
ATOM   12769 C  CZ    A PHE B 2 389 ? 39.056  -3.572  -9.993  0.20 37.06  ? 389 PHE B CZ    1 
ATOM   12770 C  CZ    B PHE B 2 389 ? 39.069  -3.740  -9.362  0.80 36.82  ? 389 PHE B CZ    1 
ATOM   12771 N  N     A ARG B 2 390 ? 43.973  -6.476  -7.850  0.20 27.90  ? 390 ARG B N     1 
ATOM   12772 N  N     B ARG B 2 390 ? 44.290  -6.489  -7.623  0.80 24.58  ? 390 ARG B N     1 
ATOM   12773 C  CA    A ARG B 2 390 ? 45.081  -5.538  -8.003  0.20 30.12  ? 390 ARG B CA    1 
ATOM   12774 C  CA    B ARG B 2 390 ? 45.417  -5.580  -7.846  0.80 31.13  ? 390 ARG B CA    1 
ATOM   12775 C  C     A ARG B 2 390 ? 45.848  -5.797  -9.293  0.20 30.87  ? 390 ARG B C     1 
ATOM   12776 C  C     B ARG B 2 390 ? 46.183  -5.918  -9.123  0.80 31.75  ? 390 ARG B C     1 
ATOM   12777 O  O     A ARG B 2 390 ? 46.189  -4.857  -10.021 0.20 32.40  ? 390 ARG B O     1 
ATOM   12778 O  O     B ARG B 2 390 ? 46.717  -5.017  -9.785  0.80 31.92  ? 390 ARG B O     1 
ATOM   12779 C  CB    A ARG B 2 390 ? 46.017  -5.624  -6.797  0.20 28.16  ? 390 ARG B CB    1 
ATOM   12780 C  CB    B ARG B 2 390 ? 46.376  -5.608  -6.650  0.80 25.33  ? 390 ARG B CB    1 
ATOM   12781 C  CG    A ARG B 2 390 ? 45.624  -4.723  -5.635  0.20 27.37  ? 390 ARG B CG    1 
ATOM   12782 C  CG    B ARG B 2 390 ? 45.878  -4.863  -5.399  0.80 25.91  ? 390 ARG B CG    1 
ATOM   12783 C  CD    A ARG B 2 390 ? 46.430  -5.050  -4.389  0.20 30.59  ? 390 ARG B CD    1 
ATOM   12784 C  CD    B ARG B 2 390 ? 46.733  -5.188  -4.178  0.80 31.21  ? 390 ARG B CD    1 
ATOM   12785 N  NE    A ARG B 2 390 ? 46.214  -4.071  -3.331  0.20 37.98  ? 390 ARG B NE    1 
ATOM   12786 N  NE    B ARG B 2 390 ? 46.473  -4.269  -3.070  0.80 40.98  ? 390 ARG B NE    1 
ATOM   12787 C  CZ    A ARG B 2 390 ? 46.669  -4.190  -2.091  0.20 36.40  ? 390 ARG B CZ    1 
ATOM   12788 C  CZ    B ARG B 2 390 ? 47.101  -4.280  -1.898  0.80 36.96  ? 390 ARG B CZ    1 
ATOM   12789 N  NH1   A ARG B 2 390 ? 47.353  -5.255  -1.704  0.20 33.42  ? 390 ARG B NH1   1 
ATOM   12790 N  NH1   B ARG B 2 390 ? 48.024  -5.185  -1.610  0.80 32.18  ? 390 ARG B NH1   1 
ATOM   12791 N  NH2   A ARG B 2 390 ? 46.426  -3.219  -1.214  0.20 39.92  ? 390 ARG B NH2   1 
ATOM   12792 N  NH2   B ARG B 2 390 ? 46.798  -3.354  -0.992  0.80 40.48  ? 390 ARG B NH2   1 
ATOM   12793 N  N     A ARG B 2 391 ? 46.131  -7.062  -9.592  0.20 29.03  ? 391 ARG B N     1 
ATOM   12794 N  N     B ARG B 2 391 ? 46.286  -7.196  -9.469  0.80 28.32  ? 391 ARG B N     1 
ATOM   12795 C  CA    A ARG B 2 391 ? 46.827  -7.427  -10.820 0.20 28.97  ? 391 ARG B CA    1 
ATOM   12796 C  CA    B ARG B 2 391 ? 46.943  -7.567  -10.719 0.80 28.49  ? 391 ARG B CA    1 
ATOM   12797 C  C     A ARG B 2 391 ? 45.883  -7.592  -12.004 0.20 31.95  ? 391 ARG B C     1 
ATOM   12798 C  C     B ARG B 2 391 ? 45.958  -7.669  -11.875 0.80 32.07  ? 391 ARG B C     1 
ATOM   12799 O  O     A ARG B 2 391 ? 46.351  -7.862  -13.115 0.20 30.88  ? 391 ARG B O     1 
ATOM   12800 O  O     B ARG B 2 391 ? 46.356  -8.063  -12.978 0.80 30.94  ? 391 ARG B O     1 
ATOM   12801 C  CB    A ARG B 2 391 ? 47.632  -8.719  -10.620 0.20 30.15  ? 391 ARG B CB    1 
ATOM   12802 C  CB    B ARG B 2 391 ? 47.709  -8.896  -10.573 0.80 30.00  ? 391 ARG B CB    1 
ATOM   12803 C  CG    A ARG B 2 391 ? 48.850  -8.581  -9.709  0.20 32.74  ? 391 ARG B CG    1 
ATOM   12804 C  CG    B ARG B 2 391 ? 48.987  -8.833  -9.726  0.80 33.99  ? 391 ARG B CG    1 
ATOM   12805 C  CD    A ARG B 2 391 ? 48.467  -8.680  -8.240  0.20 25.80  ? 391 ARG B CD    1 
ATOM   12806 C  CD    B ARG B 2 391 ? 48.644  -8.767  -8.249  0.80 24.97  ? 391 ARG B CD    1 
ATOM   12807 N  NE    A ARG B 2 391 ? 49.585  -8.422  -7.340  0.20 24.96  ? 391 ARG B NE    1 
ATOM   12808 N  NE    B ARG B 2 391 ? 49.775  -8.598  -7.343  0.80 22.87  ? 391 ARG B NE    1 
ATOM   12809 C  CZ    A ARG B 2 391 ? 49.491  -8.446  -6.017  0.20 29.02  ? 391 ARG B CZ    1 
ATOM   12810 C  CZ    B ARG B 2 391 ? 49.610  -8.319  -6.056  0.80 29.56  ? 391 ARG B CZ    1 
ATOM   12811 N  NH1   A ARG B 2 391 ? 48.352  -8.737  -5.412  0.20 25.99  ? 391 ARG B NH1   1 
ATOM   12812 N  NH1   B ARG B 2 391 ? 48.405  -8.183  -5.540  0.80 24.63  ? 391 ARG B NH1   1 
ATOM   12813 N  NH2   A ARG B 2 391 ? 50.566  -8.171  -5.283  0.20 27.63  ? 391 ARG B NH2   1 
ATOM   12814 N  NH2   B ARG B 2 391 ? 50.673  -8.156  -5.275  0.80 27.80  ? 391 ARG B NH2   1 
ATOM   12815 N  N     A LYS B 2 392 ? 44.572  -7.442  -11.790 0.20 31.37  ? 392 LYS B N     1 
ATOM   12816 N  N     B LYS B 2 392 ? 44.685  -7.332  -11.643 0.80 31.24  ? 392 LYS B N     1 
ATOM   12817 C  CA    A LYS B 2 392 ? 43.575  -7.532  -12.858 0.20 32.20  ? 392 LYS B CA    1 
ATOM   12818 C  CA    B LYS B 2 392 ? 43.645  -7.385  -12.671 0.80 32.07  ? 392 LYS B CA    1 
ATOM   12819 C  C     A LYS B 2 392 ? 43.629  -8.888  -13.560 0.20 32.83  ? 392 LYS B C     1 
ATOM   12820 C  C     B LYS B 2 392 ? 43.599  -8.747  -13.354 0.80 32.61  ? 392 LYS B C     1 
ATOM   12821 O  O     A LYS B 2 392 ? 43.426  -8.990  -14.771 0.20 33.00  ? 392 LYS B O     1 
ATOM   12822 O  O     B LYS B 2 392 ? 43.297  -8.851  -14.542 0.80 32.17  ? 392 LYS B O     1 
ATOM   12823 C  CB    A LYS B 2 392 ? 43.741  -6.390  -13.864 0.20 36.80  ? 392 LYS B CB    1 
ATOM   12824 C  CB    B LYS B 2 392 ? 43.838  -6.272  -13.704 0.80 37.32  ? 392 LYS B CB    1 
ATOM   12825 C  CG    A LYS B 2 392 ? 43.684  -5.001  -13.244 0.20 34.94  ? 392 LYS B CG    1 
ATOM   12826 C  CG    B LYS B 2 392 ? 44.095  -4.899  -13.103 0.80 33.01  ? 392 LYS B CG    1 
ATOM   12827 C  CD    A LYS B 2 392 ? 42.276  -4.662  -12.778 0.20 39.29  ? 392 LYS B CD    1 
ATOM   12828 C  CD    B LYS B 2 392 ? 43.124  -3.865  -13.662 0.80 41.09  ? 392 LYS B CD    1 
ATOM   12829 C  CE    A LYS B 2 392 ? 42.243  -3.363  -11.990 0.20 41.57  ? 392 LYS B CE    1 
ATOM   12830 C  CE    B LYS B 2 392 ? 43.275  -2.521  -12.967 0.80 48.86  ? 392 LYS B CE    1 
ATOM   12831 N  NZ    A LYS B 2 392 ? 42.917  -3.498  -10.667 0.20 40.17  ? 392 LYS B NZ    1 
ATOM   12832 N  NZ    B LYS B 2 392 ? 42.816  -2.589  -11.556 0.80 51.91  ? 392 LYS B NZ    1 
ATOM   12833 N  N     A ALA B 2 393 ? 43.898  -9.940  -12.793 0.20 32.03  ? 393 ALA B N     1 
ATOM   12834 N  N     B ALA B 2 393 ? 43.904  -9.806  -12.611 0.80 31.69  ? 393 ALA B N     1 
ATOM   12835 C  CA    A ALA B 2 393 ? 44.022  -11.271 -13.372 0.20 33.43  ? 393 ALA B CA    1 
ATOM   12836 C  CA    B ALA B 2 393 ? 43.969  -11.131 -13.207 0.80 33.11  ? 393 ALA B CA    1 
ATOM   12837 C  C     A ALA B 2 393 ? 42.650  -11.828 -13.731 0.20 38.59  ? 393 ALA B C     1 
ATOM   12838 C  C     B ALA B 2 393 ? 42.587  -11.577 -13.665 0.80 40.01  ? 393 ALA B C     1 
ATOM   12839 O  O     A ALA B 2 393 ? 41.707  -11.753 -12.935 0.20 36.30  ? 393 ALA B O     1 
ATOM   12840 O  O     B ALA B 2 393 ? 41.615  -11.548 -12.896 0.80 36.00  ? 393 ALA B O     1 
ATOM   12841 C  CB    A ALA B 2 393 ? 44.739  -12.208 -12.402 0.20 34.52  ? 393 ALA B CB    1 
ATOM   12842 C  CB    B ALA B 2 393 ? 44.562  -12.135 -12.219 0.80 35.52  ? 393 ALA B CB    1 
ATOM   12843 N  N     A PHE B 2 394 ? 42.543  -12.379 -14.941 0.20 37.68  ? 394 PHE B N     1 
ATOM   12844 N  N     B PHE B 2 394 ? 42.504  -11.960 -14.939 0.80 39.02  ? 394 PHE B N     1 
ATOM   12845 C  CA    A PHE B 2 394 ? 41.321  -12.996 -15.456 0.20 37.41  ? 394 PHE B CA    1 
ATOM   12846 C  CA    B PHE B 2 394 ? 41.314  -12.543 -15.552 0.80 35.27  ? 394 PHE B CA    1 
ATOM   12847 C  C     A PHE B 2 394 ? 40.136  -12.035 -15.466 0.20 36.22  ? 394 PHE B C     1 
ATOM   12848 C  C     B PHE B 2 394 ? 40.119  -11.592 -15.560 0.80 34.62  ? 394 PHE B C     1 
ATOM   12849 O  O     A PHE B 2 394 ? 38.983  -12.472 -15.489 0.20 37.37  ? 394 PHE B O     1 
ATOM   12850 O  O     B PHE B 2 394 ? 38.986  -12.031 -15.738 0.80 34.52  ? 394 PHE B O     1 
ATOM   12851 C  CB    A PHE B 2 394 ? 40.964  -14.262 -14.667 0.20 39.68  ? 394 PHE B CB    1 
ATOM   12852 C  CB    B PHE B 2 394 ? 40.940  -13.865 -14.868 0.80 40.60  ? 394 PHE B CB    1 
ATOM   12853 C  CG    A PHE B 2 394 ? 41.988  -15.354 -14.778 0.20 42.76  ? 394 PHE B CG    1 
ATOM   12854 C  CG    B PHE B 2 394 ? 42.062  -14.864 -14.830 0.80 45.86  ? 394 PHE B CG    1 
ATOM   12855 C  CD1   A PHE B 2 394 ? 42.734  -15.507 -15.937 0.20 40.67  ? 394 PHE B CD1   1 
ATOM   12856 C  CD1   B PHE B 2 394 ? 42.908  -15.023 -15.921 0.80 38.66  ? 394 PHE B CD1   1 
ATOM   12857 C  CD2   A PHE B 2 394 ? 42.212  -16.223 -13.723 0.20 41.59  ? 394 PHE B CD2   1 
ATOM   12858 C  CD2   B PHE B 2 394 ? 42.288  -15.630 -13.699 0.80 43.78  ? 394 PHE B CD2   1 
ATOM   12859 C  CE1   A PHE B 2 394 ? 43.679  -16.509 -16.041 0.20 41.11  ? 394 PHE B CE1   1 
ATOM   12860 C  CE1   B PHE B 2 394 ? 43.947  -15.937 -15.886 0.80 42.34  ? 394 PHE B CE1   1 
ATOM   12861 C  CE2   A PHE B 2 394 ? 43.157  -17.229 -13.822 0.20 34.18  ? 394 PHE B CE2   1 
ATOM   12862 C  CE2   B PHE B 2 394 ? 43.328  -16.551 -13.657 0.80 30.45  ? 394 PHE B CE2   1 
ATOM   12863 C  CZ    A PHE B 2 394 ? 43.892  -17.371 -14.982 0.20 39.17  ? 394 PHE B CZ    1 
ATOM   12864 C  CZ    B PHE B 2 394 ? 44.161  -16.701 -14.754 0.80 41.32  ? 394 PHE B CZ    1 
ATOM   12865 N  N     A LEU B 2 395 ? 40.394  -10.725 -15.464 0.20 34.46  ? 395 LEU B N     1 
ATOM   12866 N  N     B LEU B 2 395 ? 40.339  -10.283 -15.405 0.80 31.68  ? 395 LEU B N     1 
ATOM   12867 C  CA    A LEU B 2 395 ? 39.301  -9.760  -15.408 0.20 37.00  ? 395 LEU B CA    1 
ATOM   12868 C  CA    B LEU B 2 395 ? 39.206  -9.363  -15.318 0.80 37.23  ? 395 LEU B CA    1 
ATOM   12869 C  C     A LEU B 2 395 ? 38.506  -9.728  -16.707 0.20 40.64  ? 395 LEU B C     1 
ATOM   12870 C  C     B LEU B 2 395 ? 38.413  -9.306  -16.619 0.80 40.69  ? 395 LEU B C     1 
ATOM   12871 O  O     A LEU B 2 395 ? 37.303  -9.438  -16.687 0.20 38.71  ? 395 LEU B O     1 
ATOM   12872 O  O     B LEU B 2 395 ? 37.210  -9.018  -16.597 0.80 36.59  ? 395 LEU B O     1 
ATOM   12873 C  CB    A LEU B 2 395 ? 39.847  -8.369  -15.085 0.20 38.49  ? 395 LEU B CB    1 
ATOM   12874 C  CB    B LEU B 2 395 ? 39.680  -7.962  -14.923 0.80 38.38  ? 395 LEU B CB    1 
ATOM   12875 C  CG    A LEU B 2 395 ? 38.804  -7.277  -14.845 0.20 42.65  ? 395 LEU B CG    1 
ATOM   12876 C  CG    B LEU B 2 395 ? 38.642  -7.171  -14.123 0.80 48.57  ? 395 LEU B CG    1 
ATOM   12877 C  CD1   A LEU B 2 395 ? 37.978  -7.588  -13.602 0.20 37.81  ? 395 LEU B CD1   1 
ATOM   12878 C  CD1   B LEU B 2 395 ? 38.480  -7.772  -12.739 0.80 33.05  ? 395 LEU B CD1   1 
ATOM   12879 C  CD2   A LEU B 2 395 ? 39.462  -5.918  -14.730 0.20 45.06  ? 395 LEU B CD2   1 
ATOM   12880 C  CD2   B LEU B 2 395 ? 38.974  -5.684  -14.038 0.80 46.34  ? 395 LEU B CD2   1 
ATOM   12881 N  N     A HIS B 2 396 ? 39.150  -10.028 -17.839 0.20 39.23  ? 396 HIS B N     1 
ATOM   12882 N  N     B HIS B 2 396 ? 39.063  -9.590  -17.756 0.80 40.79  ? 396 HIS B N     1 
ATOM   12883 C  CA    A HIS B 2 396 ? 38.471  -9.969  -19.128 0.20 40.53  ? 396 HIS B CA    1 
ATOM   12884 C  CA    B HIS B 2 396 ? 38.390  -9.556  -19.051 0.80 39.49  ? 396 HIS B CA    1 
ATOM   12885 C  C     A HIS B 2 396 ? 37.375  -11.018 -19.262 0.20 40.76  ? 396 HIS B C     1 
ATOM   12886 C  C     B HIS B 2 396 ? 37.349  -10.658 -19.205 0.80 41.06  ? 396 HIS B C     1 
ATOM   12887 O  O     A HIS B 2 396 ? 36.489  -10.864 -20.110 0.20 36.97  ? 396 HIS B O     1 
ATOM   12888 O  O     B HIS B 2 396 ? 36.443  -10.519 -20.037 0.80 34.13  ? 396 HIS B O     1 
ATOM   12889 C  CB    A HIS B 2 396 ? 39.485  -10.124 -20.265 0.20 37.83  ? 396 HIS B CB    1 
ATOM   12890 C  CB    B HIS B 2 396 ? 39.426  -9.669  -20.175 0.80 35.73  ? 396 HIS B CB    1 
ATOM   12891 C  CG    A HIS B 2 396 ? 40.200  -11.439 -20.263 0.20 43.52  ? 396 HIS B CG    1 
ATOM   12892 C  CG    B HIS B 2 396 ? 40.366  -10.819 -20.003 0.80 42.04  ? 396 HIS B CG    1 
ATOM   12893 N  ND1   A HIS B 2 396 ? 40.005  -12.394 -21.238 0.20 44.45  ? 396 HIS B ND1   1 
ATOM   12894 N  ND1   B HIS B 2 396 ? 40.197  -12.025 -20.651 0.80 47.50  ? 396 HIS B ND1   1 
ATOM   12895 C  CD2   A HIS B 2 396 ? 41.109  -11.959 -19.404 0.20 43.12  ? 396 HIS B CD2   1 
ATOM   12896 C  CD2   B HIS B 2 396 ? 41.477  -10.954 -19.238 0.80 38.03  ? 396 HIS B CD2   1 
ATOM   12897 C  CE1   A HIS B 2 396 ? 40.764  -13.445 -20.980 0.20 46.40  ? 396 HIS B CE1   1 
ATOM   12898 C  CE1   B HIS B 2 396 ? 41.165  -12.852 -20.297 0.80 46.65  ? 396 HIS B CE1   1 
ATOM   12899 N  NE2   A HIS B 2 396 ? 41.441  -13.207 -19.871 0.20 45.50  ? 396 HIS B NE2   1 
ATOM   12900 N  NE2   B HIS B 2 396 ? 41.953  -12.227 -19.438 0.80 44.01  ? 396 HIS B NE2   1 
ATOM   12901 N  N     A TRP B 2 397 ? 37.413  -12.079 -18.452 0.20 38.67  ? 397 TRP B N     1 
ATOM   12902 N  N     B TRP B 2 397 ? 37.471  -11.757 -18.452 0.80 37.58  ? 397 TRP B N     1 
ATOM   12903 C  CA    A TRP B 2 397 ? 36.330  -13.054 -18.455 0.20 40.81  ? 397 TRP B CA    1 
ATOM   12904 C  CA    B TRP B 2 397 ? 36.417  -12.765 -18.449 0.80 40.04  ? 397 TRP B CA    1 
ATOM   12905 C  C     A TRP B 2 397 ? 35.018  -12.456 -17.969 0.20 39.60  ? 397 TRP B C     1 
ATOM   12906 C  C     B TRP B 2 397 ? 35.100  -12.180 -17.969 0.80 39.17  ? 397 TRP B C     1 
ATOM   12907 O  O     A TRP B 2 397 ? 33.951  -12.977 -18.308 0.20 43.74  ? 397 TRP B O     1 
ATOM   12908 O  O     B TRP B 2 397 ? 34.031  -12.644 -18.373 0.80 43.57  ? 397 TRP B O     1 
ATOM   12909 C  CB    A TRP B 2 397 ? 36.700  -14.261 -17.592 0.20 43.88  ? 397 TRP B CB    1 
ATOM   12910 C  CB    B TRP B 2 397 ? 36.801  -13.953 -17.566 0.80 44.31  ? 397 TRP B CB    1 
ATOM   12911 C  CG    A TRP B 2 397 ? 37.824  -15.077 -18.148 0.20 46.21  ? 397 TRP B CG    1 
ATOM   12912 C  CG    B TRP B 2 397 ? 37.935  -14.768 -18.099 0.80 46.22  ? 397 TRP B CG    1 
ATOM   12913 C  CD1   A TRP B 2 397 ? 38.360  -14.988 -19.398 0.20 47.51  ? 397 TRP B CD1   1 
ATOM   12914 C  CD1   B TRP B 2 397 ? 38.654  -14.523 -19.226 0.80 48.13  ? 397 TRP B CD1   1 
ATOM   12915 C  CD2   A TRP B 2 397 ? 38.556  -16.107 -17.470 0.20 48.99  ? 397 TRP B CD2   1 
ATOM   12916 C  CD2   B TRP B 2 397 ? 38.479  -15.968 -17.528 0.80 49.40  ? 397 TRP B CD2   1 
ATOM   12917 N  NE1   A TRP B 2 397 ? 39.378  -15.899 -19.544 0.20 49.94  ? 397 TRP B NE1   1 
ATOM   12918 N  NE1   B TRP B 2 397 ? 39.616  -15.488 -19.397 0.80 51.91  ? 397 TRP B NE1   1 
ATOM   12919 C  CE2   A TRP B 2 397 ? 39.520  -16.597 -18.374 0.20 49.09  ? 397 TRP B CE2   1 
ATOM   12920 C  CE2   B TRP B 2 397 ? 39.533  -16.387 -18.366 0.80 49.37  ? 397 TRP B CE2   1 
ATOM   12921 C  CE3   A TRP B 2 397 ? 38.489  -16.661 -16.188 0.20 46.80  ? 397 TRP B CE3   1 
ATOM   12922 C  CE3   B TRP B 2 397 ? 38.183  -16.723 -16.387 0.80 47.09  ? 397 TRP B CE3   1 
ATOM   12923 C  CZ2   A TRP B 2 397 ? 40.410  -17.616 -18.036 0.20 47.22  ? 397 TRP B CZ2   1 
ATOM   12924 C  CZ2   B TRP B 2 397 ? 40.292  -17.529 -18.103 0.80 47.15  ? 397 TRP B CZ2   1 
ATOM   12925 C  CZ3   A TRP B 2 397 ? 39.374  -17.672 -15.855 0.20 46.20  ? 397 TRP B CZ3   1 
ATOM   12926 C  CZ3   B TRP B 2 397 ? 38.938  -17.859 -16.128 0.80 46.13  ? 397 TRP B CZ3   1 
ATOM   12927 C  CH2   A TRP B 2 397 ? 40.321  -18.138 -16.776 0.20 49.67  ? 397 TRP B CH2   1 
ATOM   12928 C  CH2   B TRP B 2 397 ? 39.979  -18.250 -16.984 0.80 51.64  ? 397 TRP B CH2   1 
ATOM   12929 N  N     A TYR B 2 398 ? 35.072  -11.379 -17.189 0.20 39.25  ? 398 TYR B N     1 
ATOM   12930 N  N     B TYR B 2 398 ? 35.154  -11.159 -17.121 0.80 38.79  ? 398 TYR B N     1 
ATOM   12931 C  CA    A TYR B 2 398 ? 33.879  -10.713 -16.681 0.20 41.63  ? 398 TYR B CA    1 
ATOM   12932 C  CA    B TYR B 2 398 ? 33.941  -10.551 -16.596 0.80 41.88  ? 398 TYR B CA    1 
ATOM   12933 C  C     A TYR B 2 398 ? 33.489  -9.492  -17.499 0.20 43.11  ? 398 TYR B C     1 
ATOM   12934 C  C     B TYR B 2 398 ? 33.490  -9.367  -17.442 0.80 43.01  ? 398 TYR B C     1 
ATOM   12935 O  O     A TYR B 2 398 ? 32.303  -9.301  -17.787 0.20 45.44  ? 398 TYR B O     1 
ATOM   12936 O  O     B TYR B 2 398 ? 32.335  -9.321  -17.873 0.80 45.42  ? 398 TYR B O     1 
ATOM   12937 C  CB    A TYR B 2 398 ? 34.084  -10.300 -15.220 0.20 39.84  ? 398 TYR B CB    1 
ATOM   12938 C  CB    B TYR B 2 398 ? 34.156  -10.125 -15.139 0.80 39.60  ? 398 TYR B CB    1 
ATOM   12939 C  CG    A TYR B 2 398 ? 34.347  -11.460 -14.288 0.20 42.30  ? 398 TYR B CG    1 
ATOM   12940 C  CG    B TYR B 2 398 ? 34.380  -11.299 -14.226 0.80 43.07  ? 398 TYR B CG    1 
ATOM   12941 C  CD1   A TYR B 2 398 ? 35.634  -11.952 -14.106 0.20 38.51  ? 398 TYR B CD1   1 
ATOM   12942 C  CD1   B TYR B 2 398 ? 35.617  -11.931 -14.170 0.80 38.46  ? 398 TYR B CD1   1 
ATOM   12943 C  CD2   A TYR B 2 398 ? 33.309  -12.063 -13.588 0.20 37.62  ? 398 TYR B CD2   1 
ATOM   12944 C  CD2   B TYR B 2 398 ? 33.348  -11.796 -13.431 0.80 37.34  ? 398 TYR B CD2   1 
ATOM   12945 C  CE1   A TYR B 2 398 ? 35.879  -13.014 -13.256 0.20 39.69  ? 398 TYR B CE1   1 
ATOM   12946 C  CE1   B TYR B 2 398 ? 35.824  -13.020 -13.347 0.80 40.08  ? 398 TYR B CE1   1 
ATOM   12947 C  CE2   A TYR B 2 398 ? 33.544  -13.126 -12.735 0.20 34.30  ? 398 TYR B CE2   1 
ATOM   12948 C  CE2   B TYR B 2 398 ? 33.548  -12.886 -12.602 0.80 33.61  ? 398 TYR B CE2   1 
ATOM   12949 C  CZ    A TYR B 2 398 ? 34.831  -13.596 -12.573 0.20 34.87  ? 398 TYR B CZ    1 
ATOM   12950 C  CZ    B TYR B 2 398 ? 34.788  -13.491 -12.562 0.80 34.52  ? 398 TYR B CZ    1 
ATOM   12951 O  OH    A TYR B 2 398 ? 35.072  -14.653 -11.726 0.20 33.63  ? 398 TYR B OH    1 
ATOM   12952 O  OH    B TYR B 2 398 ? 35.006  -14.575 -11.745 0.80 33.57  ? 398 TYR B OH    1 
ATOM   12953 N  N     A THR B 2 399 ? 34.461  -8.659  -17.882 0.20 43.17  ? 399 THR B N     1 
ATOM   12954 N  N     B THR B 2 399 ? 34.393  -8.415  -17.701 0.80 42.71  ? 399 THR B N     1 
ATOM   12955 C  CA    A THR B 2 399 ? 34.150  -7.470  -18.669 0.20 44.30  ? 399 THR B CA    1 
ATOM   12956 C  CA    B THR B 2 399 ? 34.038  -7.252  -18.504 0.80 43.73  ? 399 THR B CA    1 
ATOM   12957 C  C     A THR B 2 399 ? 33.603  -7.833  -20.043 0.20 48.98  ? 399 THR B C     1 
ATOM   12958 C  C     B THR B 2 399 ? 33.596  -7.642  -19.907 0.80 50.07  ? 399 THR B C     1 
ATOM   12959 O  O     A THR B 2 399 ? 32.803  -7.081  -20.611 0.20 51.07  ? 399 THR B O     1 
ATOM   12960 O  O     B THR B 2 399 ? 32.837  -6.896  -20.536 0.80 51.92  ? 399 THR B O     1 
ATOM   12961 C  CB    A THR B 2 399 ? 35.395  -6.591  -18.810 0.20 44.57  ? 399 THR B CB    1 
ATOM   12962 C  CB    B THR B 2 399 ? 35.213  -6.272  -18.571 0.80 44.56  ? 399 THR B CB    1 
ATOM   12963 O  OG1   A THR B 2 399 ? 36.454  -7.350  -19.412 0.20 46.28  ? 399 THR B OG1   1 
ATOM   12964 O  OG1   B THR B 2 399 ? 36.389  -6.949  -19.027 0.80 47.83  ? 399 THR B OG1   1 
ATOM   12965 C  CG2   A THR B 2 399 ? 35.853  -6.091  -17.447 0.20 46.25  ? 399 THR B CG2   1 
ATOM   12966 C  CG2   B THR B 2 399 ? 35.490  -5.691  -17.195 0.80 49.08  ? 399 THR B CG2   1 
ATOM   12967 N  N     A GLY B 2 400 ? 34.015  -8.977  -20.588 0.20 44.64  ? 400 GLY B N     1 
ATOM   12968 N  N     B GLY B 2 400 ? 34.031  -8.803  -20.397 0.80 44.01  ? 400 GLY B N     1 
ATOM   12969 C  CA    A GLY B 2 400 ? 33.533  -9.415  -21.883 0.20 47.39  ? 400 GLY B CA    1 
ATOM   12970 C  CA    B GLY B 2 400 ? 33.601  -9.294  -21.692 0.80 47.56  ? 400 GLY B CA    1 
ATOM   12971 C  C     A GLY B 2 400 ? 32.120  -9.955  -21.898 0.20 49.33  ? 400 GLY B C     1 
ATOM   12972 C  C     B GLY B 2 400 ? 32.154  -9.725  -21.751 0.80 50.43  ? 400 GLY B C     1 
ATOM   12973 O  O     A GLY B 2 400 ? 31.586  -10.223 -22.979 0.20 46.56  ? 400 GLY B O     1 
ATOM   12974 O  O     B GLY B 2 400 ? 31.626  -9.913  -22.854 0.80 45.93  ? 400 GLY B O     1 
ATOM   12975 N  N     A GLU B 2 401 ? 31.500  -10.118 -20.729 0.20 48.89  ? 401 GLU B N     1 
ATOM   12976 N  N     B GLU B 2 401 ? 31.503  -9.893  -20.602 0.80 49.35  ? 401 GLU B N     1 
ATOM   12977 C  CA    A GLU B 2 401 ? 30.140  -10.627 -20.627 0.20 44.42  ? 401 GLU B CA    1 
ATOM   12978 C  CA    B GLU B 2 401 ? 30.077  -10.175 -20.552 0.80 42.81  ? 401 GLU B CA    1 
ATOM   12979 C  C     A GLU B 2 401 ? 29.136  -9.548  -20.243 0.20 51.03  ? 401 GLU B C     1 
ATOM   12980 C  C     B GLU B 2 401 ? 29.250  -8.919  -20.288 0.80 53.83  ? 401 GLU B C     1 
ATOM   12981 O  O     A GLU B 2 401 ? 27.997  -9.874  -19.894 0.20 50.97  ? 401 GLU B O     1 
ATOM   12982 O  O     B GLU B 2 401 ? 28.048  -9.022  -20.024 0.80 51.69  ? 401 GLU B O     1 
ATOM   12983 C  CB    A GLU B 2 401 ? 30.085  -11.779 -19.623 0.20 45.70  ? 401 GLU B CB    1 
ATOM   12984 C  CB    B GLU B 2 401 ? 29.787  -11.227 -19.485 0.80 43.83  ? 401 GLU B CB    1 
ATOM   12985 C  CG    A GLU B 2 401 ? 30.959  -12.969 -19.987 0.20 47.60  ? 401 GLU B CG    1 
ATOM   12986 C  CG    B GLU B 2 401 ? 30.674  -12.453 -19.565 0.80 46.33  ? 401 GLU B CG    1 
ATOM   12987 C  CD    A GLU B 2 401 ? 30.398  -13.782 -21.140 0.20 51.32  ? 401 GLU B CD    1 
ATOM   12988 C  CD    B GLU B 2 401 ? 30.307  -13.370 -20.712 0.80 54.98  ? 401 GLU B CD    1 
ATOM   12989 O  OE1   A GLU B 2 401 ? 29.209  -13.600 -21.479 0.20 54.51  ? 401 GLU B OE1   1 
ATOM   12990 O  OE1   B GLU B 2 401 ? 29.108  -13.427 -21.075 0.80 57.56  ? 401 GLU B OE1   1 
ATOM   12991 O  OE2   A GLU B 2 401 ? 31.146  -14.609 -21.703 0.20 49.97  ? 401 GLU B OE2   1 
ATOM   12992 O  OE2   B GLU B 2 401 ? 31.216  -14.039 -21.245 0.80 48.75  ? 401 GLU B OE2   1 
ATOM   12993 N  N     A GLY B 2 402 ? 29.525  -8.275  -20.299 0.20 51.19  ? 402 GLY B N     1 
ATOM   12994 N  N     B GLY B 2 402 ? 29.863  -7.738  -20.347 0.80 51.22  ? 402 GLY B N     1 
ATOM   12995 C  CA    A GLY B 2 402 ? 28.630  -7.175  -20.001 0.20 50.37  ? 402 GLY B CA    1 
ATOM   12996 C  CA    B GLY B 2 402 ? 29.153  -6.494  -20.137 0.80 55.03  ? 402 GLY B CA    1 
ATOM   12997 C  C     A GLY B 2 402 ? 28.963  -6.402  -18.743 0.20 50.52  ? 402 GLY B C     1 
ATOM   12998 C  C     B GLY B 2 402 ? 29.378  -5.837  -18.789 0.80 53.87  ? 402 GLY B C     1 
ATOM   12999 O  O     A GLY B 2 402 ? 28.365  -5.342  -18.515 0.20 47.56  ? 402 GLY B O     1 
ATOM   13000 O  O     B GLY B 2 402 ? 28.984  -4.674  -18.617 0.80 44.93  ? 402 GLY B O     1 
ATOM   13001 N  N     A MET B 2 403 ? 29.889  -6.887  -17.921 0.20 51.68  ? 403 MET B N     1 
ATOM   13002 N  N     B MET B 2 403 ? 29.995  -6.536  -17.834 0.80 53.58  ? 403 MET B N     1 
ATOM   13003 C  CA    A MET B 2 403 ? 30.249  -6.183  -16.700 0.20 48.42  ? 403 MET B CA    1 
ATOM   13004 C  CA    B MET B 2 403 ? 30.294  -5.933  -16.541 0.80 48.20  ? 403 MET B CA    1 
ATOM   13005 C  C     A MET B 2 403 ? 31.289  -5.103  -16.983 0.20 47.22  ? 403 MET B C     1 
ATOM   13006 C  C     B MET B 2 403 ? 31.176  -4.706  -16.718 0.80 45.12  ? 403 MET B C     1 
ATOM   13007 O  O     A MET B 2 403 ? 32.005  -5.135  -17.987 0.20 48.19  ? 403 MET B O     1 
ATOM   13008 O  O     B MET B 2 403 ? 32.109  -4.702  -17.524 0.80 48.46  ? 403 MET B O     1 
ATOM   13009 C  CB    A MET B 2 403 ? 30.792  -7.154  -15.650 0.20 46.56  ? 403 MET B CB    1 
ATOM   13010 C  CB    B MET B 2 403 ? 31.005  -6.930  -15.624 0.80 46.45  ? 403 MET B CB    1 
ATOM   13011 C  CG    A MET B 2 403 ? 29.770  -8.136  -15.108 0.20 47.47  ? 403 MET B CG    1 
ATOM   13012 C  CG    B MET B 2 403 ? 30.137  -8.008  -15.018 0.80 48.09  ? 403 MET B CG    1 
ATOM   13013 S  SD    A MET B 2 403 ? 30.395  -9.060  -13.688 0.20 41.78  ? 403 MET B SD    1 
ATOM   13014 S  SD    B MET B 2 403 ? 30.902  -8.758  -13.562 0.80 40.33  ? 403 MET B SD    1 
ATOM   13015 C  CE    A MET B 2 403 ? 30.726  -7.724  -12.543 0.20 40.18  ? 403 MET B CE    1 
ATOM   13016 C  CE    B MET B 2 403 ? 30.775  -7.407  -12.398 0.80 39.71  ? 403 MET B CE    1 
ATOM   13017 N  N     A ASP B 2 404 ? 31.361  -4.135  -16.074 0.20 47.47  ? 404 ASP B N     1 
ATOM   13018 N  N     B ASP B 2 404 ? 30.874  -3.659  -15.959 0.80 48.71  ? 404 ASP B N     1 
ATOM   13019 C  CA    A ASP B 2 404 ? 32.371  -3.090  -16.098 0.20 49.85  ? 404 ASP B CA    1 
ATOM   13020 C  CA    B ASP B 2 404 ? 31.774  -2.525  -15.822 0.80 50.42  ? 404 ASP B CA    1 
ATOM   13021 C  C     A ASP B 2 404 ? 33.228  -3.191  -14.842 0.20 49.49  ? 404 ASP B C     1 
ATOM   13022 C  C     B ASP B 2 404 ? 32.785  -2.831  -14.724 0.80 52.49  ? 404 ASP B C     1 
ATOM   13023 O  O     A ASP B 2 404 ? 32.844  -3.823  -13.853 0.20 50.10  ? 404 ASP B O     1 
ATOM   13024 O  O     B ASP B 2 404 ? 32.450  -3.453  -13.710 0.80 50.46  ? 404 ASP B O     1 
ATOM   13025 C  CB    A ASP B 2 404 ? 31.733  -1.695  -16.196 0.20 48.67  ? 404 ASP B CB    1 
ATOM   13026 C  CB    B ASP B 2 404 ? 30.996  -1.248  -15.495 0.80 43.08  ? 404 ASP B CB    1 
ATOM   13027 C  CG    A ASP B 2 404 ? 30.976  -1.488  -17.497 0.20 49.86  ? 404 ASP B CG    1 
ATOM   13028 C  CG    B ASP B 2 404 ? 31.843  0.011   -15.626 0.80 52.85  ? 404 ASP B CG    1 
ATOM   13029 O  OD1   A ASP B 2 404 ? 30.959  -2.413  -18.335 0.20 53.29  ? 404 ASP B OD1   1 
ATOM   13030 O  OD1   B ASP B 2 404 ? 33.076  -0.106  -15.779 0.80 64.36  ? 404 ASP B OD1   1 
ATOM   13031 O  OD2   A ASP B 2 404 ? 30.400  -0.396  -17.684 0.20 48.43  ? 404 ASP B OD2   1 
ATOM   13032 O  OD2   B ASP B 2 404 ? 31.273  1.126   -15.583 0.80 64.23  ? 404 ASP B OD2   1 
ATOM   13033 N  N     A GLU B 2 405 ? 34.402  -2.556  -14.887 0.20 49.74  ? 405 GLU B N     1 
ATOM   13034 N  N     B GLU B 2 405 ? 34.030  -2.397  -14.939 0.80 48.70  ? 405 GLU B N     1 
ATOM   13035 C  CA    A GLU B 2 405 ? 35.326  -2.629  -13.759 0.20 50.46  ? 405 GLU B CA    1 
ATOM   13036 C  CA    B GLU B 2 405 ? 35.083  -2.633  -13.954 0.80 51.39  ? 405 GLU B CA    1 
ATOM   13037 C  C     A GLU B 2 405 ? 34.792  -1.931  -12.516 0.20 48.72  ? 405 GLU B C     1 
ATOM   13038 C  C     B GLU B 2 405 ? 34.766  -1.968  -12.619 0.80 48.96  ? 405 GLU B C     1 
ATOM   13039 O  O     A GLU B 2 405 ? 35.242  -2.241  -11.406 0.20 44.66  ? 405 GLU B O     1 
ATOM   13040 O  O     B GLU B 2 405 ? 35.213  -2.442  -11.565 0.80 44.76  ? 405 GLU B O     1 
ATOM   13041 C  CB    A GLU B 2 405 ? 36.681  -2.033  -14.140 0.20 51.55  ? 405 GLU B CB    1 
ATOM   13042 C  CB    B GLU B 2 405 ? 36.421  -2.131  -14.501 0.80 51.62  ? 405 GLU B CB    1 
ATOM   13043 C  CG    A GLU B 2 405 ? 37.457  -2.851  -15.156 0.20 50.86  ? 405 GLU B CG    1 
ATOM   13044 C  CG    B GLU B 2 405 ? 37.610  -2.307  -13.567 0.80 49.89  ? 405 GLU B CG    1 
ATOM   13045 C  CD    A GLU B 2 405 ? 38.904  -2.414  -15.270 0.20 51.56  ? 405 GLU B CD    1 
ATOM   13046 C  CD    B GLU B 2 405 ? 38.870  -1.657  -14.111 0.80 57.77  ? 405 GLU B CD    1 
ATOM   13047 O  OE1   A GLU B 2 405 ? 39.324  -1.530  -14.493 0.20 55.47  ? 405 GLU B OE1   1 
ATOM   13048 O  OE1   B GLU B 2 405 ? 38.766  -0.912  -15.109 0.80 57.01  ? 405 GLU B OE1   1 
ATOM   13049 O  OE2   A GLU B 2 405 ? 39.624  -2.955  -16.134 0.20 50.26  ? 405 GLU B OE2   1 
ATOM   13050 O  OE2   B GLU B 2 405 ? 39.961  -1.891  -13.542 0.80 56.39  ? 405 GLU B OE2   1 
ATOM   13051 N  N     A MET B 2 406 ? 33.849  -0.999  -12.671 0.20 46.38  ? 406 MET B N     1 
ATOM   13052 N  N     B MET B 2 406 ? 33.986  -0.882  -12.643 0.80 45.91  ? 406 MET B N     1 
ATOM   13053 C  CA    A MET B 2 406 ? 33.293  -0.307  -11.515 0.20 46.24  ? 406 MET B CA    1 
ATOM   13054 C  CA    B MET B 2 406 ? 33.603  -0.189  -11.420 0.80 45.13  ? 406 MET B CA    1 
ATOM   13055 C  C     A MET B 2 406 ? 32.415  -1.217  -10.666 0.20 44.62  ? 406 MET B C     1 
ATOM   13056 C  C     B MET B 2 406 ? 32.755  -1.054  -10.498 0.80 44.78  ? 406 MET B C     1 
ATOM   13057 O  O     A MET B 2 406 ? 32.212  -0.934  -9.481  0.20 45.80  ? 406 MET B O     1 
ATOM   13058 O  O     B MET B 2 406 ? 32.638  -0.740  -9.310  0.80 49.33  ? 406 MET B O     1 
ATOM   13059 C  CB    A MET B 2 406 ? 32.500  0.919   -11.970 0.20 50.83  ? 406 MET B CB    1 
ATOM   13060 C  CB    B MET B 2 406 ? 32.841  1.092   -11.757 0.80 51.95  ? 406 MET B CB    1 
ATOM   13061 C  CG    A MET B 2 406 ? 32.265  1.953   -10.880 0.20 48.86  ? 406 MET B CG    1 
ATOM   13062 C  CG    B MET B 2 406 ? 33.701  2.338   -11.807 0.80 54.79  ? 406 MET B CG    1 
ATOM   13063 S  SD    A MET B 2 406 ? 32.879  3.587   -11.340 0.20 54.58  ? 406 MET B SD    1 
ATOM   13064 S  SD    B MET B 2 406 ? 34.359  2.748   -10.181 0.80 64.75  ? 406 MET B SD    1 
ATOM   13065 C  CE    A MET B 2 406 ? 34.634  3.259   -11.498 0.20 53.42  ? 406 MET B CE    1 
ATOM   13066 C  CE    B MET B 2 406 ? 32.881  2.578   -9.179  0.80 50.95  ? 406 MET B CE    1 
ATOM   13067 N  N     A GLU B 2 407 ? 31.894  -2.305  -11.239 0.20 42.09  ? 407 GLU B N     1 
ATOM   13068 N  N     B GLU B 2 407 ? 32.147  -2.123  -11.012 0.80 40.44  ? 407 GLU B N     1 
ATOM   13069 C  CA    A GLU B 2 407 ? 31.096  -3.235  -10.449 0.20 43.36  ? 407 GLU B CA    1 
ATOM   13070 C  CA    B GLU B 2 407 ? 31.363  -2.990  -10.145 0.80 43.35  ? 407 GLU B CA    1 
ATOM   13071 C  C     A GLU B 2 407 ? 31.959  -4.022  -9.472  0.20 41.16  ? 407 GLU B C     1 
ATOM   13072 C  C     B GLU B 2 407 ? 32.243  -3.821  -9.220  0.80 42.37  ? 407 GLU B C     1 
ATOM   13073 O  O     A GLU B 2 407 ? 31.490  -4.385  -8.387  0.20 35.82  ? 407 GLU B O     1 
ATOM   13074 O  O     B GLU B 2 407 ? 31.757  -4.301  -8.189  0.80 34.26  ? 407 GLU B O     1 
ATOM   13075 C  CB    A GLU B 2 407 ? 30.327  -4.184  -11.367 0.20 43.27  ? 407 GLU B CB    1 
ATOM   13076 C  CB    B GLU B 2 407 ? 30.458  -3.899  -10.978 0.80 43.26  ? 407 GLU B CB    1 
ATOM   13077 C  CG    A GLU B 2 407 ? 29.372  -3.482  -12.319 0.20 45.46  ? 407 GLU B CG    1 
ATOM   13078 C  CG    B GLU B 2 407 ? 29.299  -4.468  -10.169 0.80 49.42  ? 407 GLU B CG    1 
ATOM   13079 C  CD    A GLU B 2 407 ? 28.488  -4.451  -13.077 0.20 45.72  ? 407 GLU B CD    1 
ATOM   13080 C  CD    B GLU B 2 407 ? 28.356  -5.333  -10.983 0.80 54.66  ? 407 GLU B CD    1 
ATOM   13081 O  OE1   A GLU B 2 407 ? 28.139  -5.509  -12.509 0.20 47.77  ? 407 GLU B OE1   1 
ATOM   13082 O  OE1   B GLU B 2 407 ? 28.233  -5.111  -12.208 0.80 49.42  ? 407 GLU B OE1   1 
ATOM   13083 O  OE2   A GLU B 2 407 ? 28.145  -4.159  -14.241 0.20 42.73  ? 407 GLU B OE2   1 
ATOM   13084 O  OE2   B GLU B 2 407 ? 27.733  -6.236  -10.383 0.80 52.15  ? 407 GLU B OE2   1 
ATOM   13085 N  N     A PHE B 2 408 ? 33.215  -4.297  -9.834  0.20 36.67  ? 408 PHE B N     1 
ATOM   13086 N  N     B PHE B 2 408 ? 33.523  -3.995  -9.562  0.80 33.43  ? 408 PHE B N     1 
ATOM   13087 C  CA    A PHE B 2 408 ? 34.127  -4.949  -8.900  0.20 38.24  ? 408 PHE B CA    1 
ATOM   13088 C  CA    B PHE B 2 408 ? 34.454  -4.674  -8.666  0.80 38.46  ? 408 PHE B CA    1 
ATOM   13089 C  C     A PHE B 2 408 ? 34.512  -4.014  -7.761  0.20 37.97  ? 408 PHE B C     1 
ATOM   13090 C  C     B PHE B 2 408 ? 34.846  -3.778  -7.497  0.80 37.85  ? 408 PHE B C     1 
ATOM   13091 O  O     A PHE B 2 408 ? 34.573  -4.434  -6.600  0.20 37.79  ? 408 PHE B O     1 
ATOM   13092 O  O     B PHE B 2 408 ? 34.810  -4.203  -6.337  0.80 37.58  ? 408 PHE B O     1 
ATOM   13093 C  CB    A PHE B 2 408 ? 35.376  -5.438  -9.635  0.20 36.61  ? 408 PHE B CB    1 
ATOM   13094 C  CB    B PHE B 2 408 ? 35.698  -5.130  -9.440  0.80 35.28  ? 408 PHE B CB    1 
ATOM   13095 C  CG    A PHE B 2 408 ? 35.155  -6.681  -10.447 0.20 37.66  ? 408 PHE B CG    1 
ATOM   13096 C  CG    B PHE B 2 408 ? 35.497  -6.398  -10.220 0.80 37.33  ? 408 PHE B CG    1 
ATOM   13097 C  CD1   A PHE B 2 408 ? 34.653  -6.604  -11.735 0.20 39.61  ? 408 PHE B CD1   1 
ATOM   13098 C  CD1   B PHE B 2 408 ? 34.855  -6.380  -11.450 0.80 39.77  ? 408 PHE B CD1   1 
ATOM   13099 C  CD2   A PHE B 2 408 ? 35.452  -7.927  -9.921  0.20 34.11  ? 408 PHE B CD2   1 
ATOM   13100 C  CD2   B PHE B 2 408 ? 35.951  -7.608  -9.727  0.80 35.00  ? 408 PHE B CD2   1 
ATOM   13101 C  CE1   A PHE B 2 408 ? 34.449  -7.749  -12.484 0.20 39.02  ? 408 PHE B CE1   1 
ATOM   13102 C  CE1   B PHE B 2 408 ? 34.667  -7.552  -12.170 0.80 39.73  ? 408 PHE B CE1   1 
ATOM   13103 C  CE2   A PHE B 2 408 ? 35.254  -9.074  -10.664 0.20 37.01  ? 408 PHE B CE2   1 
ATOM   13104 C  CE2   B PHE B 2 408 ? 35.776  -8.782  -10.441 0.80 37.54  ? 408 PHE B CE2   1 
ATOM   13105 C  CZ    A PHE B 2 408 ? 34.750  -8.986  -11.947 0.20 37.89  ? 408 PHE B CZ    1 
ATOM   13106 C  CZ    B PHE B 2 408 ? 35.131  -8.756  -11.664 0.80 39.73  ? 408 PHE B CZ    1 
ATOM   13107 N  N     A THR B 2 409 ? 34.774  -2.743  -8.073  0.20 37.55  ? 409 THR B N     1 
ATOM   13108 N  N     B THR B 2 409 ? 35.223  -2.529  -7.779  0.80 34.72  ? 409 THR B N     1 
ATOM   13109 C  CA    A THR B 2 409 ? 35.154  -1.794  -7.033  0.20 40.29  ? 409 THR B CA    1 
ATOM   13110 C  CA    B THR B 2 409 ? 35.637  -1.642  -6.699  0.80 41.87  ? 409 THR B CA    1 
ATOM   13111 C  C     A THR B 2 409 ? 33.994  -1.521  -6.083  0.20 38.21  ? 409 THR B C     1 
ATOM   13112 C  C     B THR B 2 409 ? 34.484  -1.383  -5.734  0.80 36.87  ? 409 THR B C     1 
ATOM   13113 O  O     A THR B 2 409 ? 34.199  -1.359  -4.875  0.20 41.54  ? 409 THR B O     1 
ATOM   13114 O  O     B THR B 2 409 ? 34.693  -1.289  -4.520  0.80 45.88  ? 409 THR B O     1 
ATOM   13115 C  CB    A THR B 2 409 ? 35.651  -0.492  -7.663  0.20 41.46  ? 409 THR B CB    1 
ATOM   13116 C  CB    B THR B 2 409 ? 36.177  -0.322  -7.260  0.80 38.83  ? 409 THR B CB    1 
ATOM   13117 O  OG1   A THR B 2 409 ? 34.632  0.051   -8.512  0.20 45.10  ? 409 THR B OG1   1 
ATOM   13118 O  OG1   B THR B 2 409 ? 35.118  0.405   -7.898  0.80 46.91  ? 409 THR B OG1   1 
ATOM   13119 C  CG2   A THR B 2 409 ? 36.907  -0.743  -8.481  0.20 43.36  ? 409 THR B CG2   1 
ATOM   13120 C  CG2   B THR B 2 409 ? 37.288  -0.582  -8.260  0.80 45.06  ? 409 THR B CG2   1 
ATOM   13121 N  N     A GLU B 2 410 ? 32.768  -1.468  -6.608  0.20 40.45  ? 410 GLU B N     1 
ATOM   13122 N  N     B GLU B 2 410 ? 33.260  -1.285  -6.255  0.80 38.66  ? 410 GLU B N     1 
ATOM   13123 C  CA    A GLU B 2 410 ? 31.612  -1.226  -5.751  0.20 39.53  ? 410 GLU B CA    1 
ATOM   13124 C  CA    B GLU B 2 410 ? 32.112  -1.020  -5.396  0.80 35.63  ? 410 GLU B CA    1 
ATOM   13125 C  C     A GLU B 2 410 ? 31.352  -2.407  -4.824  0.20 38.05  ? 410 GLU B C     1 
ATOM   13126 C  C     B GLU B 2 410 ? 31.786  -2.220  -4.516  0.80 39.73  ? 410 GLU B C     1 
ATOM   13127 O  O     A GLU B 2 410 ? 30.953  -2.219  -3.669  0.20 37.47  ? 410 GLU B O     1 
ATOM   13128 O  O     B GLU B 2 410 ? 31.474  -2.055  -3.331  0.80 33.29  ? 410 GLU B O     1 
ATOM   13129 C  CB    A GLU B 2 410 ? 30.377  -0.924  -6.600  0.20 40.52  ? 410 GLU B CB    1 
ATOM   13130 C  CB    B GLU B 2 410 ? 30.895  -0.620  -6.231  0.80 39.69  ? 410 GLU B CB    1 
ATOM   13131 C  CG    A GLU B 2 410 ? 30.386  0.463   -7.225  0.20 50.60  ? 410 GLU B CG    1 
ATOM   13132 C  CG    B GLU B 2 410 ? 30.956  0.818   -6.726  0.80 51.90  ? 410 GLU B CG    1 
ATOM   13133 C  CD    A GLU B 2 410 ? 29.156  0.735   -8.070  0.20 58.00  ? 410 GLU B CD    1 
ATOM   13134 C  CD    B GLU B 2 410 ? 29.688  1.259   -7.430  0.80 62.35  ? 410 GLU B CD    1 
ATOM   13135 O  OE1   A GLU B 2 410 ? 28.485  -0.236  -8.480  0.20 50.33  ? 410 GLU B OE1   1 
ATOM   13136 O  OE1   B GLU B 2 410 ? 28.619  0.660   -7.173  0.80 67.15  ? 410 GLU B OE1   1 
ATOM   13137 O  OE2   A GLU B 2 410 ? 28.858  1.922   -8.322  0.20 64.23  ? 410 GLU B OE2   1 
ATOM   13138 O  OE2   B GLU B 2 410 ? 29.763  2.209   -8.241  0.80 62.20  ? 410 GLU B OE2   1 
ATOM   13139 N  N     A ALA B 2 411 ? 31.578  -3.632  -5.306  0.20 36.88  ? 411 ALA B N     1 
ATOM   13140 N  N     B ALA B 2 411 ? 31.849  -3.433  -5.067  0.80 34.34  ? 411 ALA B N     1 
ATOM   13141 C  CA    A ALA B 2 411 ? 31.376  -4.803  -4.459  0.20 40.28  ? 411 ALA B CA    1 
ATOM   13142 C  CA    B ALA B 2 411 ? 31.678  -4.610  -4.223  0.80 42.52  ? 411 ALA B CA    1 
ATOM   13143 C  C     A ALA B 2 411 ? 32.409  -4.861  -3.341  0.20 39.31  ? 411 ALA B C     1 
ATOM   13144 C  C     B ALA B 2 411 ? 32.776  -4.682  -3.167  0.80 41.18  ? 411 ALA B C     1 
ATOM   13145 O  O     A ALA B 2 411 ? 32.079  -5.206  -2.201  0.20 36.78  ? 411 ALA B O     1 
ATOM   13146 O  O     B ALA B 2 411 ? 32.500  -4.967  -1.997  0.80 37.60  ? 411 ALA B O     1 
ATOM   13147 C  CB    A ALA B 2 411 ? 31.421  -6.077  -5.301  0.20 37.61  ? 411 ALA B CB    1 
ATOM   13148 C  CB    B ALA B 2 411 ? 31.653  -5.879  -5.075  0.80 38.98  ? 411 ALA B CB    1 
ATOM   13149 N  N     A GLU B 2 412 ? 33.666  -4.529  -3.649  0.20 35.54  ? 412 GLU B N     1 
ATOM   13150 N  N     B GLU B 2 412 ? 34.024  -4.396  -3.561  0.80 33.82  ? 412 GLU B N     1 
ATOM   13151 C  CA    A GLU B 2 412 ? 34.700  -4.509  -2.619  0.20 38.45  ? 412 GLU B CA    1 
ATOM   13152 C  CA    B GLU B 2 412 ? 35.145  -4.399  -2.619  0.80 38.79  ? 412 GLU B CA    1 
ATOM   13153 C  C     A GLU B 2 412 ? 34.460  -3.386  -1.618  0.20 36.62  ? 412 GLU B C     1 
ATOM   13154 C  C     B GLU B 2 412 ? 34.964  -3.332  -1.544  0.80 35.53  ? 412 GLU B C     1 
ATOM   13155 O  O     A GLU B 2 412 ? 34.684  -3.560  -0.414  0.20 36.21  ? 412 GLU B O     1 
ATOM   13156 O  O     B GLU B 2 412 ? 35.239  -3.573  -0.362  0.80 31.84  ? 412 GLU B O     1 
ATOM   13157 C  CB    A GLU B 2 412 ? 36.080  -4.366  -3.262  0.20 39.15  ? 412 GLU B CB    1 
ATOM   13158 C  CB    B GLU B 2 412 ? 36.464  -4.191  -3.378  0.80 41.24  ? 412 GLU B CB    1 
ATOM   13159 C  CG    A GLU B 2 412 ? 37.202  -4.081  -2.274  0.20 39.13  ? 412 GLU B CG    1 
ATOM   13160 C  CG    B GLU B 2 412 ? 37.738  -4.100  -2.518  0.80 37.94  ? 412 GLU B CG    1 
ATOM   13161 C  CD    A GLU B 2 412 ? 38.456  -3.559  -2.949  0.20 44.17  ? 412 GLU B CD    1 
ATOM   13162 C  CD    B GLU B 2 412 ? 38.978  -3.639  -3.311  0.80 49.89  ? 412 GLU B CD    1 
ATOM   13163 O  OE1   A GLU B 2 412 ? 38.522  -3.596  -4.197  0.20 46.13  ? 412 GLU B OE1   1 
ATOM   13164 O  OE1   B GLU B 2 412 ? 38.835  -2.832  -4.257  0.80 50.69  ? 412 GLU B OE1   1 
ATOM   13165 O  OE2   A GLU B 2 412 ? 39.374  -3.105  -2.233  0.20 46.26  ? 412 GLU B OE2   1 
ATOM   13166 O  OE2   B GLU B 2 412 ? 40.106  -4.086  -2.988  0.80 49.22  ? 412 GLU B OE2   1 
ATOM   13167 N  N     A SER B 2 413 ? 34.005  -2.227  -2.099  0.20 37.70  ? 413 SER B N     1 
ATOM   13168 N  N     B SER B 2 413 ? 34.502  -2.145  -1.933  0.80 35.75  ? 413 SER B N     1 
ATOM   13169 C  CA    A SER B 2 413 ? 33.748  -1.101  -1.206  0.20 37.49  ? 413 SER B CA    1 
ATOM   13170 C  CA    B SER B 2 413 ? 34.260  -1.094  -0.950  0.80 36.09  ? 413 SER B CA    1 
ATOM   13171 C  C     A SER B 2 413 ? 32.599  -1.402  -0.253  0.20 39.05  ? 413 SER B C     1 
ATOM   13172 C  C     B SER B 2 413 ? 33.118  -1.457  -0.010  0.80 39.48  ? 413 SER B C     1 
ATOM   13173 O  O     A SER B 2 413 ? 32.650  -1.032  0.926   0.20 37.56  ? 413 SER B O     1 
ATOM   13174 O  O     B SER B 2 413 ? 33.159  -1.107  1.178   0.80 38.75  ? 413 SER B O     1 
ATOM   13175 C  CB    A SER B 2 413 ? 33.456  0.156   -2.025  0.20 39.14  ? 413 SER B CB    1 
ATOM   13176 C  CB    B SER B 2 413 ? 33.968  0.226   -1.658  0.80 39.55  ? 413 SER B CB    1 
ATOM   13177 O  OG    A SER B 2 413 ? 33.227  1.276   -1.192  0.20 37.19  ? 413 SER B OG    1 
ATOM   13178 O  OG    B SER B 2 413 ? 34.086  1.314   -0.767  0.80 47.69  ? 413 SER B OG    1 
ATOM   13179 N  N     A ASN B 2 414 ? 31.554  -2.074  -0.740  0.20 39.41  ? 414 ASN B N     1 
ATOM   13180 N  N     B ASN B 2 414 ? 32.095  -2.155  -0.507  0.80 39.45  ? 414 ASN B N     1 
ATOM   13181 C  CA    A ASN B 2 414 ? 30.424  -2.392  0.128   0.20 39.91  ? 414 ASN B CA    1 
ATOM   13182 C  CA    B ASN B 2 414 ? 30.985  -2.515  0.373   0.80 39.30  ? 414 ASN B CA    1 
ATOM   13183 C  C     A ASN B 2 414 ? 30.771  -3.517  1.096   0.20 39.26  ? 414 ASN B C     1 
ATOM   13184 C  C     B ASN B 2 414 ? 31.417  -3.550  1.404   0.80 37.34  ? 414 ASN B C     1 
ATOM   13185 O  O     A ASN B 2 414 ? 30.385  -3.471  2.270   0.20 38.37  ? 414 ASN B O     1 
ATOM   13186 O  O     B ASN B 2 414 ? 30.994  -3.489  2.564   0.80 37.02  ? 414 ASN B O     1 
ATOM   13187 C  CB    A ASN B 2 414 ? 29.200  -2.761  -0.712  0.20 43.51  ? 414 ASN B CB    1 
ATOM   13188 C  CB    B ASN B 2 414 ? 29.795  -3.030  -0.441  0.80 46.01  ? 414 ASN B CB    1 
ATOM   13189 C  CG    A ASN B 2 414 ? 27.930  -2.850  0.116   0.20 45.62  ? 414 ASN B CG    1 
ATOM   13190 C  CG    B ASN B 2 414 ? 28.523  -3.134  0.389   0.80 46.10  ? 414 ASN B CG    1 
ATOM   13191 O  OD1   A ASN B 2 414 ? 27.784  -2.163  1.125   0.20 46.62  ? 414 ASN B OD1   1 
ATOM   13192 O  OD1   B ASN B 2 414 ? 28.429  -2.558  1.471   0.80 52.27  ? 414 ASN B OD1   1 
ATOM   13193 N  ND2   A ASN B 2 414 ? 27.003  -3.702  -0.309  0.20 45.29  ? 414 ASN B ND2   1 
ATOM   13194 N  ND2   B ASN B 2 414 ? 27.535  -3.863  -0.120  0.80 49.22  ? 414 ASN B ND2   1 
ATOM   13195 N  N     A MET B 2 415 ? 31.502  -4.533  0.626   0.20 38.58  ? 415 MET B N     1 
ATOM   13196 N  N     B MET B 2 415 ? 32.273  -4.497  1.007   0.80 38.34  ? 415 MET B N     1 
ATOM   13197 C  CA    A MET B 2 415 ? 31.848  -5.654  1.495   0.20 39.55  ? 415 MET B CA    1 
ATOM   13198 C  CA    B MET B 2 415 ? 32.704  -5.530  1.944   0.80 38.85  ? 415 MET B CA    1 
ATOM   13199 C  C     A MET B 2 415 ? 32.794  -5.220  2.608   0.20 37.85  ? 415 MET B C     1 
ATOM   13200 C  C     B MET B 2 415 ? 33.602  -4.956  3.030   0.80 40.45  ? 415 MET B C     1 
ATOM   13201 O  O     A MET B 2 415 ? 32.643  -5.647  3.759   0.20 34.05  ? 415 MET B O     1 
ATOM   13202 O  O     B MET B 2 415 ? 33.521  -5.368  4.195   0.80 34.24  ? 415 MET B O     1 
ATOM   13203 C  CB    A MET B 2 415 ? 32.463  -6.790  0.676   0.20 37.27  ? 415 MET B CB    1 
ATOM   13204 C  CB    B MET B 2 415 ? 33.411  -6.661  1.207   0.80 40.31  ? 415 MET B CB    1 
ATOM   13205 C  CG    A MET B 2 415 ? 32.899  -7.999  1.502   0.20 38.64  ? 415 MET B CG    1 
ATOM   13206 C  CG    B MET B 2 415 ? 32.496  -7.813  0.860   0.80 47.24  ? 415 MET B CG    1 
ATOM   13207 S  SD    A MET B 2 415 ? 33.227  -9.454  0.479   0.20 35.45  ? 415 MET B SD    1 
ATOM   13208 S  SD    B MET B 2 415 ? 33.245  -9.399  1.273   0.80 41.86  ? 415 MET B SD    1 
ATOM   13209 C  CE    A MET B 2 415 ? 33.978  -10.557 1.673   0.20 31.26  ? 415 MET B CE    1 
ATOM   13210 C  CE    B MET B 2 415 ? 34.862  -9.179  0.545   0.80 37.23  ? 415 MET B CE    1 
ATOM   13211 N  N     A ASN B 2 416 ? 33.773  -4.371  2.290   0.20 34.34  ? 416 ASN B N     1 
ATOM   13212 N  N     B ASN B 2 416 ? 34.466  -4.008  2.675   0.80 32.62  ? 416 ASN B N     1 
ATOM   13213 C  CA    A ASN B 2 416 ? 34.664  -3.879  3.334   0.20 34.87  ? 416 ASN B CA    1 
ATOM   13214 C  CA    B ASN B 2 416 ? 35.253  -3.357  3.713   0.80 34.74  ? 416 ASN B CA    1 
ATOM   13215 C  C     A ASN B 2 416 ? 33.968  -2.858  4.226   0.20 34.61  ? 416 ASN B C     1 
ATOM   13216 C  C     B ASN B 2 416 ? 34.373  -2.493  4.611   0.80 31.21  ? 416 ASN B C     1 
ATOM   13217 O  O     A ASN B 2 416 ? 34.350  -2.694  5.390   0.20 30.49  ? 416 ASN B O     1 
ATOM   13218 O  O     B ASN B 2 416 ? 34.640  -2.383  5.808   0.80 32.03  ? 416 ASN B O     1 
ATOM   13219 C  CB    A ASN B 2 416 ? 35.931  -3.295  2.713   0.20 34.43  ? 416 ASN B CB    1 
ATOM   13220 C  CB    B ASN B 2 416 ? 36.386  -2.546  3.084   0.80 31.48  ? 416 ASN B CB    1 
ATOM   13221 C  CG    A ASN B 2 416 ? 36.816  -4.362  2.097   0.20 35.06  ? 416 ASN B CG    1 
ATOM   13222 C  CG    B ASN B 2 416 ? 37.395  -3.429  2.382   0.80 38.30  ? 416 ASN B CG    1 
ATOM   13223 O  OD1   A ASN B 2 416 ? 36.791  -5.523  2.512   0.20 24.48  ? 416 ASN B OD1   1 
ATOM   13224 O  OD1   B ASN B 2 416 ? 37.611  -4.576  2.780   0.80 39.64  ? 416 ASN B OD1   1 
ATOM   13225 N  ND2   A ASN B 2 416 ? 37.606  -3.974  1.103   0.20 33.25  ? 416 ASN B ND2   1 
ATOM   13226 N  ND2   B ASN B 2 416 ? 38.007  -2.911  1.325   0.80 41.37  ? 416 ASN B ND2   1 
ATOM   13227 N  N     A ASP B 2 417 ? 32.946  -2.170  3.708   0.20 36.61  ? 417 ASP B N     1 
ATOM   13228 N  N     B ASP B 2 417 ? 33.305  -1.909  4.061   0.80 39.58  ? 417 ASP B N     1 
ATOM   13229 C  CA    A ASP B 2 417 ? 32.101  -1.355  4.576   0.20 32.02  ? 417 ASP B CA    1 
ATOM   13230 C  CA    B ASP B 2 417 ? 32.338  -1.186  4.888   0.80 28.17  ? 417 ASP B CA    1 
ATOM   13231 C  C     A ASP B 2 417 ? 31.354  -2.223  5.580   0.20 31.78  ? 417 ASP B C     1 
ATOM   13232 C  C     B ASP B 2 417 ? 31.646  -2.111  5.885   0.80 31.99  ? 417 ASP B C     1 
ATOM   13233 O  O     A ASP B 2 417 ? 31.155  -1.822  6.731   0.20 30.45  ? 417 ASP B O     1 
ATOM   13234 O  O     B ASP B 2 417 ? 31.341  -1.699  7.008   0.80 29.27  ? 417 ASP B O     1 
ATOM   13235 C  CB    A ASP B 2 417 ? 31.118  -0.531  3.744   0.20 35.25  ? 417 ASP B CB    1 
ATOM   13236 C  CB    B ASP B 2 417 ? 31.298  -0.497  4.001   0.80 34.35  ? 417 ASP B CB    1 
ATOM   13237 C  CG    A ASP B 2 417 ? 31.740  0.739   3.191   0.20 40.86  ? 417 ASP B CG    1 
ATOM   13238 C  CG    B ASP B 2 417 ? 31.834  0.758   3.327   0.80 41.49  ? 417 ASP B CG    1 
ATOM   13239 O  OD1   A ASP B 2 417 ? 32.937  0.986   3.456   0.20 40.58  ? 417 ASP B OD1   1 
ATOM   13240 O  OD1   B ASP B 2 417 ? 32.983  1.161   3.619   0.80 41.52  ? 417 ASP B OD1   1 
ATOM   13241 O  OD2   A ASP B 2 417 ? 31.031  1.490   2.491   0.20 40.94  ? 417 ASP B OD2   1 
ATOM   13242 O  OD2   B ASP B 2 417 ? 31.102  1.337   2.498   0.80 41.09  ? 417 ASP B OD2   1 
ATOM   13243 N  N     A LEU B 2 418 ? 30.940  -3.422  5.161   0.20 34.70  ? 418 LEU B N     1 
ATOM   13244 N  N     B LEU B 2 418 ? 31.393  -3.361  5.489   0.80 36.41  ? 418 LEU B N     1 
ATOM   13245 C  CA    A LEU B 2 418 ? 30.285  -4.351  6.077   0.20 31.21  ? 418 LEU B CA    1 
ATOM   13246 C  CA    B LEU B 2 418 ? 30.717  -4.327  6.354   0.80 30.10  ? 418 LEU B CA    1 
ATOM   13247 C  C     A LEU B 2 418 ? 31.227  -4.786  7.192   0.20 32.48  ? 418 LEU B C     1 
ATOM   13248 C  C     B LEU B 2 418 ? 31.613  -4.776  7.504   0.80 33.80  ? 418 LEU B C     1 
ATOM   13249 O  O     A LEU B 2 418 ? 30.802  -4.971  8.339   0.20 32.08  ? 418 LEU B O     1 
ATOM   13250 O  O     B LEU B 2 418 ? 31.163  -4.861  8.656   0.80 32.04  ? 418 LEU B O     1 
ATOM   13251 C  CB    A LEU B 2 418 ? 29.775  -5.569  5.307   0.20 32.84  ? 418 LEU B CB    1 
ATOM   13252 C  CB    B LEU B 2 418 ? 30.275  -5.529  5.522   0.80 31.50  ? 418 LEU B CB    1 
ATOM   13253 C  CG    A LEU B 2 418 ? 28.952  -6.586  6.099   0.20 31.99  ? 418 LEU B CG    1 
ATOM   13254 C  CG    B LEU B 2 418 ? 29.492  -6.662  6.183   0.80 33.18  ? 418 LEU B CG    1 
ATOM   13255 C  CD1   A LEU B 2 418 ? 27.610  -5.989  6.483   0.20 33.68  ? 418 LEU B CD1   1 
ATOM   13256 C  CD1   B LEU B 2 418 ? 28.042  -6.271  6.357   0.80 34.38  ? 418 LEU B CD1   1 
ATOM   13257 C  CD2   A LEU B 2 418 ? 28.769  -7.868  5.302   0.20 31.97  ? 418 LEU B CD2   1 
ATOM   13258 C  CD2   B LEU B 2 418 ? 29.616  -7.912  5.335   0.80 32.25  ? 418 LEU B CD2   1 
ATOM   13259 N  N     A VAL B 2 419 ? 32.511  -4.958  6.874   0.20 32.57  ? 419 VAL B N     1 
ATOM   13260 N  N     B VAL B 2 419 ? 32.879  -5.086  7.204   0.80 30.81  ? 419 VAL B N     1 
ATOM   13261 C  CA    A VAL B 2 419 ? 33.486  -5.373  7.878   0.20 31.44  ? 419 VAL B CA    1 
ATOM   13262 C  CA    B VAL B 2 419 ? 33.863  -5.407  8.236   0.80 32.49  ? 419 VAL B CA    1 
ATOM   13263 C  C     A VAL B 2 419 ? 33.676  -4.275  8.919   0.20 30.91  ? 419 VAL B C     1 
ATOM   13264 C  C     B VAL B 2 419 ? 33.994  -4.252  9.224   0.80 30.28  ? 419 VAL B C     1 
ATOM   13265 O  O     A VAL B 2 419 ? 33.669  -4.532  10.128  0.20 33.79  ? 419 VAL B O     1 
ATOM   13266 O  O     B VAL B 2 419 ? 34.153  -4.457  10.433  0.80 34.45  ? 419 VAL B O     1 
ATOM   13267 C  CB    A VAL B 2 419 ? 34.816  -5.753  7.202   0.20 30.38  ? 419 VAL B CB    1 
ATOM   13268 C  CB    B VAL B 2 419 ? 35.214  -5.756  7.570   0.80 28.38  ? 419 VAL B CB    1 
ATOM   13269 C  CG1   A VAL B 2 419 ? 35.866  -6.107  8.241   0.20 29.89  ? 419 VAL B CG1   1 
ATOM   13270 C  CG1   B VAL B 2 419 ? 36.376  -5.662  8.553   0.80 30.37  ? 419 VAL B CG1   1 
ATOM   13271 C  CG2   A VAL B 2 419 ? 34.604  -6.910  6.236   0.20 30.73  ? 419 VAL B CG2   1 
ATOM   13272 C  CG2   B VAL B 2 419 ? 35.144  -7.149  6.957   0.80 31.91  ? 419 VAL B CG2   1 
ATOM   13273 N  N     A SER B 2 420 ? 33.838  -3.031  8.462   0.20 30.88  ? 420 SER B N     1 
ATOM   13274 N  N     B SER B 2 420 ? 33.929  -3.020  8.723   0.80 30.81  ? 420 SER B N     1 
ATOM   13275 C  CA    A SER B 2 420 ? 33.976  -1.910  9.384   0.20 32.04  ? 420 SER B CA    1 
ATOM   13276 C  CA    B SER B 2 420 ? 34.023  -1.860  9.600   0.80 31.97  ? 420 SER B CA    1 
ATOM   13277 C  C     A SER B 2 420 ? 32.717  -1.692  10.211  0.20 32.22  ? 420 SER B C     1 
ATOM   13278 C  C     B SER B 2 420 ? 32.814  -1.785  10.519  0.80 31.79  ? 420 SER B C     1 
ATOM   13279 O  O     A SER B 2 420 ? 32.785  -1.060  11.270  0.20 31.96  ? 420 SER B O     1 
ATOM   13280 O  O     B SER B 2 420 ? 32.955  -1.574  11.727  0.80 33.26  ? 420 SER B O     1 
ATOM   13281 C  CB    A SER B 2 420 ? 34.318  -0.638  8.609   0.20 30.43  ? 420 SER B CB    1 
ATOM   13282 C  CB    B SER B 2 420 ? 34.133  -0.587  8.767   0.80 29.42  ? 420 SER B CB    1 
ATOM   13283 O  OG    A SER B 2 420 ? 35.454  -0.835  7.785   0.20 20.57  ? 420 SER B OG    1 
ATOM   13284 O  OG    B SER B 2 420 ? 34.540  0.506   9.572   0.80 45.46  ? 420 SER B OG    1 
ATOM   13285 N  N     A GLU B 2 421 ? 31.571  -2.194  9.745   0.20 31.05  ? 421 GLU B N     1 
ATOM   13286 N  N     B GLU B 2 421 ? 31.613  -1.952  9.951   0.80 29.83  ? 421 GLU B N     1 
ATOM   13287 C  CA    A GLU B 2 421 ? 30.335  -2.087  10.510  0.20 32.04  ? 421 GLU B CA    1 
ATOM   13288 C  CA    B GLU B 2 421 ? 30.382  -1.889  10.732  0.80 33.13  ? 421 GLU B CA    1 
ATOM   13289 C  C     A GLU B 2 421 ? 30.267  -3.121  11.625  0.20 34.17  ? 421 GLU B C     1 
ATOM   13290 C  C     B GLU B 2 421 ? 30.371  -2.945  11.828  0.80 35.16  ? 421 GLU B C     1 
ATOM   13291 O  O     A GLU B 2 421 ? 29.692  -2.844  12.683  0.20 34.36  ? 421 GLU B O     1 
ATOM   13292 O  O     B GLU B 2 421 ? 29.949  -2.673  12.956  0.80 36.34  ? 421 GLU B O     1 
ATOM   13293 C  CB    A GLU B 2 421 ? 29.132  -2.217  9.573   0.20 31.71  ? 421 GLU B CB    1 
ATOM   13294 C  CB    B GLU B 2 421 ? 29.179  -2.045  9.803   0.80 31.91  ? 421 GLU B CB    1 
ATOM   13295 C  CG    A GLU B 2 421 ? 28.886  -0.971  8.734   0.20 31.06  ? 421 GLU B CG    1 
ATOM   13296 C  CG    B GLU B 2 421 ? 27.827  -1.769  10.453  0.80 31.43  ? 421 GLU B CG    1 
ATOM   13297 C  CD    A GLU B 2 421 ? 28.233  -1.271  7.398   0.20 32.72  ? 421 GLU B CD    1 
ATOM   13298 C  CD    B GLU B 2 421 ? 26.708  -1.772  9.435   0.80 30.89  ? 421 GLU B CD    1 
ATOM   13299 O  OE1   A GLU B 2 421 ? 27.725  -2.397  7.219   0.20 36.97  ? 421 GLU B OE1   1 
ATOM   13300 O  OE1   B GLU B 2 421 ? 27.013  -1.855  8.226   0.80 38.30  ? 421 GLU B OE1   1 
ATOM   13301 O  OE2   A GLU B 2 421 ? 28.236  -0.381  6.522   0.20 29.12  ? 421 GLU B OE2   1 
ATOM   13302 O  OE2   B GLU B 2 421 ? 25.531  -1.704  9.835   0.80 34.94  ? 421 GLU B OE2   1 
ATOM   13303 N  N     A TYR B 2 422 ? 30.846  -4.306  11.416  0.20 33.02  ? 422 TYR B N     1 
ATOM   13304 N  N     B TYR B 2 422 ? 30.837  -4.154  11.514  0.80 33.16  ? 422 TYR B N     1 
ATOM   13305 C  CA    A TYR B 2 422 ? 30.932  -5.285  12.494  0.20 31.01  ? 422 TYR B CA    1 
ATOM   13306 C  CA    B TYR B 2 422 ? 31.002  -5.181  12.535  0.80 30.83  ? 422 TYR B CA    1 
ATOM   13307 C  C     A TYR B 2 422 ? 31.880  -4.818  13.591  0.20 36.00  ? 422 TYR B C     1 
ATOM   13308 C  C     B TYR B 2 422 ? 31.955  -4.734  13.634  0.80 36.60  ? 422 TYR B C     1 
ATOM   13309 O  O     A TYR B 2 422 ? 31.582  -4.969  14.781  0.20 28.89  ? 422 TYR B O     1 
ATOM   13310 O  O     B TYR B 2 422 ? 31.704  -4.979  14.818  0.80 28.48  ? 422 TYR B O     1 
ATOM   13311 C  CB    A TYR B 2 422 ? 31.381  -6.641  11.949  0.20 30.89  ? 422 TYR B CB    1 
ATOM   13312 C  CB    B TYR B 2 422 ? 31.520  -6.474  11.911  0.80 30.62  ? 422 TYR B CB    1 
ATOM   13313 C  CG    A TYR B 2 422 ? 30.283  -7.433  11.280  0.20 31.78  ? 422 TYR B CG    1 
ATOM   13314 C  CG    B TYR B 2 422 ? 30.459  -7.333  11.280  0.80 32.28  ? 422 TYR B CG    1 
ATOM   13315 C  CD1   A TYR B 2 422 ? 29.295  -8.056  12.031  0.20 29.04  ? 422 TYR B CD1   1 
ATOM   13316 C  CD1   B TYR B 2 422 ? 29.368  -7.768  12.017  0.80 27.94  ? 422 TYR B CD1   1 
ATOM   13317 C  CD2   A TYR B 2 422 ? 30.242  -7.569  9.900   0.20 33.93  ? 422 TYR B CD2   1 
ATOM   13318 C  CD2   B TYR B 2 422 ? 30.565  -7.735  9.957   0.80 35.50  ? 422 TYR B CD2   1 
ATOM   13319 C  CE1   A TYR B 2 422 ? 28.290  -8.784  11.424  0.20 30.22  ? 422 TYR B CE1   1 
ATOM   13320 C  CE1   B TYR B 2 422 ? 28.395  -8.563  11.447  0.80 30.68  ? 422 TYR B CE1   1 
ATOM   13321 C  CE2   A TYR B 2 422 ? 29.243  -8.293  9.285   0.20 30.39  ? 422 TYR B CE2   1 
ATOM   13322 C  CE2   B TYR B 2 422 ? 29.601  -8.530  9.383   0.80 28.78  ? 422 TYR B CE2   1 
ATOM   13323 C  CZ    A TYR B 2 422 ? 28.270  -8.899  10.051  0.20 27.89  ? 422 TYR B CZ    1 
ATOM   13324 C  CZ    B TYR B 2 422 ? 28.517  -8.937  10.133  0.80 27.17  ? 422 TYR B CZ    1 
ATOM   13325 O  OH    A TYR B 2 422 ? 27.274  -9.621  9.437   0.20 29.50  ? 422 TYR B OH    1 
ATOM   13326 O  OH    B TYR B 2 422 ? 27.560  -9.728  9.551   0.80 29.76  ? 422 TYR B OH    1 
ATOM   13327 N  N     A GLN B 2 423 ? 33.032  -4.260  13.211  0.20 29.60  ? 423 GLN B N     1 
ATOM   13328 N  N     B GLN B 2 423 ? 33.077  -4.119  13.261  0.80 28.84  ? 423 GLN B N     1 
ATOM   13329 C  CA    A GLN B 2 423 ? 33.973  -3.756  14.205  0.20 34.25  ? 423 GLN B CA    1 
ATOM   13330 C  CA    B GLN B 2 423 ? 34.053  -3.708  14.263  0.80 34.41  ? 423 GLN B CA    1 
ATOM   13331 C  C     A GLN B 2 423 ? 33.402  -2.563  14.963  0.20 32.83  ? 423 GLN B C     1 
ATOM   13332 C  C     B GLN B 2 423 ? 33.494  -2.614  15.167  0.80 32.74  ? 423 GLN B C     1 
ATOM   13333 O  O     A GLN B 2 423 ? 33.764  -2.336  16.124  0.20 34.38  ? 423 GLN B O     1 
ATOM   13334 O  O     B GLN B 2 423 ? 33.761  -2.604  16.377  0.80 33.77  ? 423 GLN B O     1 
ATOM   13335 C  CB    A GLN B 2 423 ? 35.295  -3.384  13.529  0.20 31.32  ? 423 GLN B CB    1 
ATOM   13336 C  CB    B GLN B 2 423 ? 35.341  -3.245  13.573  0.80 30.77  ? 423 GLN B CB    1 
ATOM   13337 C  CG    A GLN B 2 423 ? 36.416  -3.021  14.490  0.20 39.46  ? 423 GLN B CG    1 
ATOM   13338 C  CG    B GLN B 2 423 ? 36.482  -2.970  14.528  0.80 39.66  ? 423 GLN B CG    1 
ATOM   13339 C  CD    A GLN B 2 423 ? 36.898  -4.207  15.304  0.20 34.64  ? 423 GLN B CD    1 
ATOM   13340 C  CD    B GLN B 2 423 ? 37.092  -4.239  15.079  0.80 32.89  ? 423 GLN B CD    1 
ATOM   13341 O  OE1   A GLN B 2 423 ? 36.756  -5.359  14.891  0.20 38.92  ? 423 GLN B OE1   1 
ATOM   13342 O  OE1   B GLN B 2 423 ? 37.298  -5.208  14.348  0.80 43.87  ? 423 GLN B OE1   1 
ATOM   13343 N  NE2   A GLN B 2 423 ? 37.470  -3.929  16.470  0.20 40.25  ? 423 GLN B NE2   1 
ATOM   13344 N  NE2   B GLN B 2 423 ? 37.380  -4.245  16.376  0.80 41.71  ? 423 GLN B NE2   1 
ATOM   13345 N  N     A GLN B 2 424 ? 32.508  -1.799  14.329  0.20 29.58  ? 424 GLN B N     1 
ATOM   13346 N  N     B GLN B 2 424 ? 32.706  -1.691  14.603  0.80 29.08  ? 424 GLN B N     1 
ATOM   13347 C  CA    A GLN B 2 424 ? 31.873  -0.672  15.008  0.20 33.22  ? 424 GLN B CA    1 
ATOM   13348 C  CA    B GLN B 2 424 ? 32.122  -0.617  15.407  0.80 30.71  ? 424 GLN B CA    1 
ATOM   13349 C  C     A GLN B 2 424 ? 31.069  -1.140  16.216  0.20 32.69  ? 424 GLN B C     1 
ATOM   13350 C  C     B GLN B 2 424 ? 31.284  -1.159  16.562  0.80 33.58  ? 424 GLN B C     1 
ATOM   13351 O  O     A GLN B 2 424 ? 31.180  -0.572  17.310  0.20 34.45  ? 424 GLN B O     1 
ATOM   13352 O  O     B GLN B 2 424 ? 31.367  -0.653  17.694  0.80 30.65  ? 424 GLN B O     1 
ATOM   13353 C  CB    A GLN B 2 424 ? 30.981  0.087   14.027  0.20 35.23  ? 424 GLN B CB    1 
ATOM   13354 C  CB    B GLN B 2 424 ? 31.274  0.289   14.517  0.80 33.50  ? 424 GLN B CB    1 
ATOM   13355 C  CG    A GLN B 2 424 ? 29.972  1.016   14.681  0.20 39.02  ? 424 GLN B CG    1 
ATOM   13356 C  CG    B GLN B 2 424 ? 30.355  1.230   15.277  0.80 42.17  ? 424 GLN B CG    1 
ATOM   13357 C  CD    A GLN B 2 424 ? 29.004  1.615   13.678  0.20 44.12  ? 424 GLN B CD    1 
ATOM   13358 C  CD    B GLN B 2 424 ? 29.387  1.946   14.364  0.80 47.80  ? 424 GLN B CD    1 
ATOM   13359 O  OE1   A GLN B 2 424 ? 29.243  1.576   12.470  0.20 45.59  ? 424 GLN B OE1   1 
ATOM   13360 O  OE1   B GLN B 2 424 ? 29.468  1.825   13.138  0.80 51.85  ? 424 GLN B OE1   1 
ATOM   13361 N  NE2   A GLN B 2 424 ? 27.902  2.167   14.174  0.20 41.14  ? 424 GLN B NE2   1 
ATOM   13362 N  NE2   B GLN B 2 424 ? 28.460  2.697   14.953  0.80 46.75  ? 424 GLN B NE2   1 
ATOM   13363 N  N     A TYR B 2 425 ? 30.248  -2.177  16.036  0.20 33.08  ? 425 TYR B N     1 
ATOM   13364 N  N     B TYR B 2 425 ? 30.459  -2.181  16.306  0.80 33.57  ? 425 TYR B N     1 
ATOM   13365 C  CA    A TYR B 2 425 ? 29.445  -2.696  17.138  0.20 34.12  ? 425 TYR B CA    1 
ATOM   13366 C  CA    B TYR B 2 425 ? 29.622  -2.700  17.390  0.80 33.09  ? 425 TYR B CA    1 
ATOM   13367 C  C     A TYR B 2 425 ? 30.226  -3.646  18.034  0.20 30.06  ? 425 TYR B C     1 
ATOM   13368 C  C     B TYR B 2 425 ? 30.351  -3.709  18.255  0.80 28.75  ? 425 TYR B C     1 
ATOM   13369 O  O     A TYR B 2 425 ? 29.836  -3.850  19.188  0.20 37.62  ? 425 TYR B O     1 
ATOM   13370 O  O     B TYR B 2 425 ? 29.873  -4.037  19.347  0.80 38.54  ? 425 TYR B O     1 
ATOM   13371 C  CB    A TYR B 2 425 ? 28.198  -3.403  16.599  0.20 34.54  ? 425 TYR B CB    1 
ATOM   13372 C  CB    B TYR B 2 425 ? 28.320  -3.300  16.837  0.80 35.57  ? 425 TYR B CB    1 
ATOM   13373 C  CG    A TYR B 2 425 ? 27.319  -2.518  15.742  0.20 32.87  ? 425 TYR B CG    1 
ATOM   13374 C  CG    B TYR B 2 425 ? 27.477  -2.252  16.141  0.80 34.75  ? 425 TYR B CG    1 
ATOM   13375 C  CD1   A TYR B 2 425 ? 26.695  -1.400  16.278  0.20 33.73  ? 425 TYR B CD1   1 
ATOM   13376 C  CD1   B TYR B 2 425 ? 26.873  -1.223  16.857  0.80 34.74  ? 425 TYR B CD1   1 
ATOM   13377 C  CD2   A TYR B 2 425 ? 27.108  -2.807  14.402  0.20 31.64  ? 425 TYR B CD2   1 
ATOM   13378 C  CD2   B TYR B 2 425 ? 27.310  -2.275  14.769  0.80 31.04  ? 425 TYR B CD2   1 
ATOM   13379 C  CE1   A TYR B 2 425 ? 25.892  -0.587  15.498  0.20 33.74  ? 425 TYR B CE1   1 
ATOM   13380 C  CE1   B TYR B 2 425 ? 26.116  -0.242  16.209  0.80 31.71  ? 425 TYR B CE1   1 
ATOM   13381 C  CE2   A TYR B 2 425 ? 26.307  -2.002  13.613  0.20 30.96  ? 425 TYR B CE2   1 
ATOM   13382 C  CE2   B TYR B 2 425 ? 26.574  -1.313  14.119  0.80 31.37  ? 425 TYR B CE2   1 
ATOM   13383 C  CZ    A TYR B 2 425 ? 25.702  -0.893  14.165  0.20 33.00  ? 425 TYR B CZ    1 
ATOM   13384 C  CZ    B TYR B 2 425 ? 25.982  -0.298  14.831  0.80 32.59  ? 425 TYR B CZ    1 
ATOM   13385 O  OH    A TYR B 2 425 ? 24.903  -0.093  13.382  0.20 29.05  ? 425 TYR B OH    1 
ATOM   13386 O  OH    B TYR B 2 425 ? 25.245  0.646   14.151  0.80 35.62  ? 425 TYR B OH    1 
ATOM   13387 N  N     A GLN B 2 426 ? 31.315  -4.228  17.529  0.20 33.34  ? 426 GLN B N     1 
ATOM   13388 N  N     B GLN B 2 426 ? 31.507  -4.193  17.807  0.80 33.22  ? 426 GLN B N     1 
ATOM   13389 C  CA    A GLN B 2 426 ? 32.156  -5.082  18.359  0.20 32.78  ? 426 GLN B CA    1 
ATOM   13390 C  CA    B GLN B 2 426 ? 32.407  -4.881  18.719  0.80 30.12  ? 426 GLN B CA    1 
ATOM   13391 C  C     A GLN B 2 426 ? 32.824  -4.292  19.477  0.20 35.03  ? 426 GLN B C     1 
ATOM   13392 C  C     B GLN B 2 426 ? 33.006  -3.899  19.715  0.80 35.97  ? 426 GLN B C     1 
ATOM   13393 O  O     A GLN B 2 426 ? 33.033  -4.825  20.573  0.20 37.57  ? 426 GLN B O     1 
ATOM   13394 O  O     B GLN B 2 426 ? 33.085  -4.191  20.915  0.80 40.30  ? 426 GLN B O     1 
ATOM   13395 C  CB    A GLN B 2 426 ? 33.202  -5.778  17.485  0.20 32.31  ? 426 GLN B CB    1 
ATOM   13396 C  CB    B GLN B 2 426 ? 33.505  -5.595  17.920  0.80 31.58  ? 426 GLN B CB    1 
ATOM   13397 C  CG    A GLN B 2 426 ? 34.214  -6.627  18.232  0.20 35.60  ? 426 GLN B CG    1 
ATOM   13398 C  CG    B GLN B 2 426 ? 34.344  -6.574  18.718  0.80 36.34  ? 426 GLN B CG    1 
ATOM   13399 C  CD    A GLN B 2 426 ? 35.142  -7.368  17.289  0.20 36.25  ? 426 GLN B CD    1 
ATOM   13400 C  CD    B GLN B 2 426 ? 35.199  -7.438  17.825  0.80 36.54  ? 426 GLN B CD    1 
ATOM   13401 O  OE1   A GLN B 2 426 ? 34.708  -7.905  16.268  0.20 32.93  ? 426 GLN B OE1   1 
ATOM   13402 O  OE1   B GLN B 2 426 ? 34.697  -8.088  16.900  0.80 38.00  ? 426 GLN B OE1   1 
ATOM   13403 N  NE2   A GLN B 2 426 ? 36.429  -7.393  17.621  0.20 39.77  ? 426 GLN B NE2   1 
ATOM   13404 N  NE2   B GLN B 2 426 ? 36.508  -7.438  18.077  0.80 43.51  ? 426 GLN B NE2   1 
ATOM   13405 N  N     A ASP B 2 427 ? 33.150  -3.023  19.227  0.20 37.34  ? 427 ASP B N     1 
ATOM   13406 N  N     B ASP B 2 427 ? 33.406  -2.716  19.240  0.80 39.56  ? 427 ASP B N     1 
ATOM   13407 C  CA    A ASP B 2 427 ? 33.795  -2.158  20.206  0.20 38.43  ? 427 ASP B CA    1 
ATOM   13408 C  CA    B ASP B 2 427 ? 34.012  -1.719  20.119  0.80 38.10  ? 427 ASP B CA    1 
ATOM   13409 C  C     A ASP B 2 427 ? 32.818  -1.183  20.859  0.20 39.24  ? 427 ASP B C     1 
ATOM   13410 C  C     B ASP B 2 427 ? 32.986  -1.060  21.039  0.80 39.93  ? 427 ASP B C     1 
ATOM   13411 O  O     A ASP B 2 427 ? 33.240  -0.135  21.359  0.20 37.99  ? 427 ASP B O     1 
ATOM   13412 O  O     B ASP B 2 427 ? 33.343  -0.623  22.137  0.80 44.03  ? 427 ASP B O     1 
ATOM   13413 C  CB    A ASP B 2 427 ? 34.942  -1.385  19.552  0.20 36.51  ? 427 ASP B CB    1 
ATOM   13414 C  CB    B ASP B 2 427 ? 34.728  -0.648  19.292  0.80 32.04  ? 427 ASP B CB    1 
ATOM   13415 C  CG    A ASP B 2 427 ? 36.005  -2.296  18.962  0.20 39.55  ? 427 ASP B CG    1 
ATOM   13416 C  CG    B ASP B 2 427 ? 35.911  -1.204  18.507  0.80 46.49  ? 427 ASP B CG    1 
ATOM   13417 O  OD1   A ASP B 2 427 ? 36.463  -3.222  19.664  0.20 34.45  ? 427 ASP B OD1   1 
ATOM   13418 O  OD1   B ASP B 2 427 ? 36.459  -2.253  18.920  0.80 41.39  ? 427 ASP B OD1   1 
ATOM   13419 O  OD2   A ASP B 2 427 ? 36.384  -2.081  17.790  0.20 39.90  ? 427 ASP B OD2   1 
ATOM   13420 O  OD2   B ASP B 2 427 ? 36.300  -0.583  17.489  0.80 41.90  ? 427 ASP B OD2   1 
ATOM   13421 N  N     A ALA B 2 428 ? 31.527  -1.502  20.856  0.20 36.14  ? 428 ALA B N     1 
ATOM   13422 N  N     B ALA B 2 428 ? 31.721  -0.987  20.618  0.80 32.77  ? 428 ALA B N     1 
ATOM   13423 C  CA    A ALA B 2 428 ? 30.514  -0.632  21.436  0.20 39.92  ? 428 ALA B CA    1 
ATOM   13424 C  CA    B ALA B 2 428 ? 30.719  -0.221  21.348  0.80 37.54  ? 428 ALA B CA    1 
ATOM   13425 C  C     A ALA B 2 428 ? 30.333  -0.932  22.919  0.20 44.09  ? 428 ALA B C     1 
ATOM   13426 C  C     B ALA B 2 428 ? 30.536  -0.755  22.767  0.80 44.70  ? 428 ALA B C     1 
ATOM   13427 O  O     A ALA B 2 428 ? 30.400  -2.088  23.346  0.20 45.39  ? 428 ALA B O     1 
ATOM   13428 O  O     B ALA B 2 428 ? 30.738  -1.939  23.045  0.80 47.27  ? 428 ALA B O     1 
ATOM   13429 C  CB    A ALA B 2 428 ? 29.180  -0.796  20.704  0.20 38.31  ? 428 ALA B CB    1 
ATOM   13430 C  CB    B ALA B 2 428 ? 29.384  -0.253  20.599  0.80 41.08  ? 428 ALA B CB    1 
ATOM   13431 N  N     A THR B 2 429 ? 30.104  0.117   23.701  0.20 44.35  ? 429 THR B N     1 
ATOM   13432 N  N     B THR B 2 429 ? 30.152  0.140   23.673  0.80 44.45  ? 429 THR B N     1 
ATOM   13433 C  CA    A THR B 2 429 ? 29.874  -0.032  25.134  0.20 49.06  ? 429 THR B CA    1 
ATOM   13434 C  CA    B THR B 2 429 ? 29.932  -0.215  25.074  0.80 49.89  ? 429 THR B CA    1 
ATOM   13435 C  C     A THR B 2 429 ? 28.607  0.701   25.561  0.20 45.59  ? 429 THR B C     1 
ATOM   13436 C  C     B THR B 2 429 ? 28.539  0.205   25.543  0.80 45.07  ? 429 THR B C     1 
ATOM   13437 O  O     A THR B 2 429 ? 28.359  1.827   25.130  0.20 46.74  ? 429 THR B O     1 
ATOM   13438 O  O     B THR B 2 429 ? 27.921  1.090   24.953  0.80 49.14  ? 429 THR B O     1 
ATOM   13439 C  CB    A THR B 2 429 ? 31.063  0.495   25.961  0.20 48.22  ? 429 THR B CB    1 
ATOM   13440 C  CB    B THR B 2 429 ? 30.978  0.437   25.995  0.80 48.18  ? 429 THR B CB    1 
ATOM   13441 O  OG1   A THR B 2 429 ? 31.301  1.870   25.638  0.20 48.20  ? 429 THR B OG1   1 
ATOM   13442 O  OG1   B THR B 2 429 ? 30.951  1.857   25.810  0.80 48.67  ? 429 THR B OG1   1 
ATOM   13443 C  CG2   A THR B 2 429 ? 32.318  -0.316  25.675  0.20 51.20  ? 429 THR B CG2   1 
ATOM   13444 C  CG2   B THR B 2 429 ? 32.373  -0.087  25.679  0.80 52.00  ? 429 THR B CG2   1 
ATOM   13445 N  N     A ASP C 3 13  ? 54.169  -5.492  -37.280 0.20 55.51  ? 13  ASP F N     1 
ATOM   13446 N  N     B ASP C 3 13  ? 53.906  -5.434  -37.191 0.80 56.20  ? 13  ASP F N     1 
ATOM   13447 C  CA    A ASP C 3 13  ? 54.484  -5.496  -35.857 0.20 51.31  ? 13  ASP F CA    1 
ATOM   13448 C  CA    B ASP C 3 13  ? 54.570  -5.574  -35.899 0.80 51.09  ? 13  ASP F CA    1 
ATOM   13449 C  C     A ASP C 3 13  ? 54.119  -6.839  -35.236 0.20 48.01  ? 13  ASP F C     1 
ATOM   13450 C  C     B ASP C 3 13  ? 54.170  -6.880  -35.239 0.80 47.92  ? 13  ASP F C     1 
ATOM   13451 O  O     A ASP C 3 13  ? 53.015  -7.017  -34.723 0.20 52.14  ? 13  ASP F O     1 
ATOM   13452 O  O     B ASP C 3 13  ? 53.047  -7.026  -34.762 0.80 52.42  ? 13  ASP F O     1 
ATOM   13453 C  CB    A ASP C 3 13  ? 53.750  -4.363  -35.138 0.20 58.64  ? 13  ASP F CB    1 
ATOM   13454 C  CB    B ASP C 3 13  ? 54.233  -4.401  -34.981 0.80 60.92  ? 13  ASP F CB    1 
ATOM   13455 C  CG    A ASP C 3 13  ? 54.258  -4.141  -33.727 0.20 56.93  ? 13  ASP F CG    1 
ATOM   13456 C  CG    B ASP C 3 13  ? 54.769  -4.593  -33.580 0.80 57.31  ? 13  ASP F CG    1 
ATOM   13457 O  OD1   A ASP C 3 13  ? 55.276  -4.763  -33.354 0.20 55.70  ? 13  ASP F OD1   1 
ATOM   13458 O  OD1   B ASP C 3 13  ? 56.012  -4.597  -33.411 0.80 51.76  ? 13  ASP F OD1   1 
ATOM   13459 O  OD2   A ASP C 3 13  ? 53.639  -3.344  -32.990 0.20 57.22  ? 13  ASP F OD2   1 
ATOM   13460 O  OD2   B ASP C 3 13  ? 53.947  -4.749  -32.650 0.80 58.56  ? 13  ASP F OD2   1 
ATOM   13461 N  N     A LEU C 3 14  ? 55.058  -7.783  -35.282 0.20 44.66  ? 14  LEU F N     1 
ATOM   13462 N  N     B LEU C 3 14  ? 55.099  -7.831  -35.202 0.80 44.48  ? 14  LEU F N     1 
ATOM   13463 C  CA    A LEU C 3 14  ? 54.809  -9.123  -34.771 0.20 44.62  ? 14  LEU F CA    1 
ATOM   13464 C  CA    B LEU C 3 14  ? 54.766  -9.167  -34.739 0.80 44.78  ? 14  LEU F CA    1 
ATOM   13465 C  C     A LEU C 3 14  ? 54.873  -9.204  -33.252 0.20 44.59  ? 14  LEU F C     1 
ATOM   13466 C  C     B LEU C 3 14  ? 54.729  -9.283  -33.220 0.80 44.75  ? 14  LEU F C     1 
ATOM   13467 O  O     A LEU C 3 14  ? 54.457  -10.221 -32.686 0.20 43.79  ? 14  LEU F O     1 
ATOM   13468 O  O     B LEU C 3 14  ? 54.303  -10.325 -32.711 0.80 44.29  ? 14  LEU F O     1 
ATOM   13469 C  CB    A LEU C 3 14  ? 55.804  -10.108 -35.386 0.20 36.53  ? 14  LEU F CB    1 
ATOM   13470 C  CB    B LEU C 3 14  ? 55.757  -10.170 -35.326 0.80 36.21  ? 14  LEU F CB    1 
ATOM   13471 C  CG    A LEU C 3 14  ? 55.756  -10.213 -36.912 0.20 38.81  ? 14  LEU F CG    1 
ATOM   13472 C  CG    B LEU C 3 14  ? 55.727  -10.202 -36.858 0.80 38.88  ? 14  LEU F CG    1 
ATOM   13473 C  CD1   A LEU C 3 14  ? 56.822  -11.170 -37.418 0.20 33.52  ? 14  LEU F CD1   1 
ATOM   13474 C  CD1   B LEU C 3 14  ? 56.865  -11.053 -37.410 0.80 33.24  ? 14  LEU F CD1   1 
ATOM   13475 C  CD2   A LEU C 3 14  ? 54.375  -10.649 -37.377 0.20 33.92  ? 14  LEU F CD2   1 
ATOM   13476 C  CD2   B LEU C 3 14  ? 54.384  -10.710 -37.355 0.80 33.55  ? 14  LEU F CD2   1 
ATOM   13477 N  N     A GLY C 3 15  ? 55.381  -8.168  -32.582 0.20 44.31  ? 15  GLY F N     1 
ATOM   13478 N  N     B GLY C 3 15  ? 55.148  -8.245  -32.493 0.80 44.14  ? 15  GLY F N     1 
ATOM   13479 C  CA    A GLY C 3 15  ? 55.408  -8.183  -31.129 0.20 46.95  ? 15  GLY F CA    1 
ATOM   13480 C  CA    B GLY C 3 15  ? 55.124  -8.314  -31.040 0.80 48.25  ? 15  GLY F CA    1 
ATOM   13481 C  C     A GLY C 3 15  ? 54.019  -8.121  -30.521 0.20 46.61  ? 15  GLY F C     1 
ATOM   13482 C  C     B GLY C 3 15  ? 53.719  -8.423  -30.477 0.80 49.37  ? 15  GLY F C     1 
ATOM   13483 O  O     A GLY C 3 15  ? 53.744  -8.775  -29.511 0.20 45.60  ? 15  GLY F O     1 
ATOM   13484 O  O     B GLY C 3 15  ? 53.468  -9.202  -29.551 0.80 44.85  ? 15  GLY F O     1 
ATOM   13485 N  N     A LYS C 3 16  ? 53.125  -7.337  -31.128 0.20 48.00  ? 16  LYS F N     1 
ATOM   13486 N  N     B LYS C 3 16  ? 52.782  -7.649  -31.030 0.80 47.52  ? 16  LYS F N     1 
ATOM   13487 C  CA    A LYS C 3 16  ? 51.746  -7.281  -30.653 0.20 45.93  ? 16  LYS F CA    1 
ATOM   13488 C  CA    B LYS C 3 16  ? 51.396  -7.741  -30.587 0.80 44.64  ? 16  LYS F CA    1 
ATOM   13489 C  C     A LYS C 3 16  ? 51.019  -8.597  -30.898 0.20 45.59  ? 16  LYS F C     1 
ATOM   13490 C  C     B LYS C 3 16  ? 50.820  -9.124  -30.844 0.80 47.86  ? 16  LYS F C     1 
ATOM   13491 O  O     A LYS C 3 16  ? 50.107  -8.950  -30.141 0.20 43.31  ? 16  LYS F O     1 
ATOM   13492 O  O     B LYS C 3 16  ? 49.968  -9.594  -30.078 0.80 39.64  ? 16  LYS F O     1 
ATOM   13493 C  CB    A LYS C 3 16  ? 51.007  -6.122  -31.325 0.20 50.85  ? 16  LYS F CB    1 
ATOM   13494 C  CB    B LYS C 3 16  ? 50.551  -6.675  -31.285 0.80 52.07  ? 16  LYS F CB    1 
ATOM   13495 C  CG    A LYS C 3 16  ? 49.601  -5.859  -30.790 0.20 49.22  ? 16  LYS F CG    1 
ATOM   13496 C  CG    B LYS C 3 16  ? 51.065  -5.263  -31.077 0.80 49.16  ? 16  LYS F CG    1 
ATOM   13497 C  CD    A LYS C 3 16  ? 48.531  -6.441  -31.702 0.20 51.58  ? 16  LYS F CD    1 
ATOM   13498 C  CD    B LYS C 3 16  ? 51.090  -4.916  -29.597 0.80 66.52  ? 16  LYS F CD    1 
ATOM   13499 C  CE    A LYS C 3 16  ? 47.134  -6.145  -31.180 0.20 52.78  ? 16  LYS F CE    1 
ATOM   13500 C  CE    B LYS C 3 16  ? 52.432  -4.335  -29.175 0.80 61.16  ? 16  LYS F CE    1 
ATOM   13501 N  NZ    A LYS C 3 16  ? 46.887  -6.774  -29.852 0.20 53.34  ? 16  LYS F NZ    1 
ATOM   13502 N  NZ    B LYS C 3 16  ? 52.504  -4.224  -27.694 0.80 42.92  ? 16  LYS F NZ    1 
ATOM   13503 N  N     A LYS C 3 17  ? 51.405  -9.334  -31.941 0.20 42.40  ? 17  LYS F N     1 
ATOM   13504 N  N     B LYS C 3 17  ? 51.279  -9.797  -31.902 0.80 42.38  ? 17  LYS F N     1 
ATOM   13505 C  CA    A LYS C 3 17  ? 50.784  -10.627 -32.206 0.20 42.91  ? 17  LYS F CA    1 
ATOM   13506 C  CA    B LYS C 3 17  ? 50.773  -11.131 -32.211 0.80 41.68  ? 17  LYS F CA    1 
ATOM   13507 C  C     A LYS C 3 17  ? 51.387  -11.729 -31.346 0.20 39.08  ? 17  LYS F C     1 
ATOM   13508 C  C     B LYS C 3 17  ? 51.406  -12.191 -31.321 0.80 38.51  ? 17  LYS F C     1 
ATOM   13509 O  O     A LYS C 3 17  ? 50.703  -12.712 -31.036 0.20 39.77  ? 17  LYS F O     1 
ATOM   13510 O  O     B LYS C 3 17  ? 50.747  -13.173 -30.954 0.80 37.72  ? 17  LYS F O     1 
ATOM   13511 C  CB    A LYS C 3 17  ? 50.915  -10.980 -33.689 0.20 41.43  ? 17  LYS F CB    1 
ATOM   13512 C  CB    B LYS C 3 17  ? 51.024  -11.469 -33.679 0.80 39.83  ? 17  LYS F CB    1 
ATOM   13513 C  CG    A LYS C 3 17  ? 50.066  -12.164 -34.124 0.20 41.72  ? 17  LYS F CG    1 
ATOM   13514 C  CG    B LYS C 3 17  ? 50.237  -10.640 -34.667 0.80 45.99  ? 17  LYS F CG    1 
ATOM   13515 C  CD    A LYS C 3 17  ? 50.285  -12.492 -35.592 0.20 42.52  ? 17  LYS F CD    1 
ATOM   13516 C  CD    B LYS C 3 17  ? 50.616  -11.046 -36.089 0.80 50.66  ? 17  LYS F CD    1 
ATOM   13517 C  CE    A LYS C 3 17  ? 49.323  -13.567 -36.068 0.20 38.84  ? 17  LYS F CE    1 
ATOM   13518 C  CE    B LYS C 3 17  ? 49.724  -10.392 -37.132 0.80 62.86  ? 17  LYS F CE    1 
ATOM   13519 N  NZ    A LYS C 3 17  ? 49.469  -14.827 -35.296 0.20 39.06  ? 17  LYS F NZ    1 
ATOM   13520 N  NZ    B LYS C 3 17  ? 50.037  -10.901 -38.497 0.80 57.71  ? 17  LYS F NZ    1 
ATOM   13521 N  N     A LEU C 3 18  ? 52.654  -11.585 -30.951 0.20 36.88  ? 18  LEU F N     1 
ATOM   13522 N  N     B LEU C 3 18  ? 52.687  -12.029 -30.982 0.80 34.34  ? 18  LEU F N     1 
ATOM   13523 C  CA    A LEU C 3 18  ? 53.261  -12.563 -30.055 0.20 39.76  ? 18  LEU F CA    1 
ATOM   13524 C  CA    B LEU C 3 18  ? 53.280  -12.928 -30.001 0.80 40.19  ? 18  LEU F CA    1 
ATOM   13525 C  C     A LEU C 3 18  ? 52.610  -12.535 -28.676 0.20 37.34  ? 18  LEU F C     1 
ATOM   13526 C  C     B LEU C 3 18  ? 52.576  -12.784 -28.652 0.80 36.97  ? 18  LEU F C     1 
ATOM   13527 O  O     A LEU C 3 18  ? 52.533  -13.572 -28.007 0.20 36.23  ? 18  LEU F O     1 
ATOM   13528 O  O     B LEU C 3 18  ? 52.267  -13.786 -27.992 0.80 33.79  ? 18  LEU F O     1 
ATOM   13529 C  CB    A LEU C 3 18  ? 54.767  -12.311 -29.949 0.20 37.95  ? 18  LEU F CB    1 
ATOM   13530 C  CB    B LEU C 3 18  ? 54.787  -12.663 -29.881 0.80 37.91  ? 18  LEU F CB    1 
ATOM   13531 C  CG    A LEU C 3 18  ? 55.601  -13.340 -29.182 0.20 35.17  ? 18  LEU F CG    1 
ATOM   13532 C  CG    B LEU C 3 18  ? 55.516  -13.533 -28.852 0.80 36.38  ? 18  LEU F CG    1 
ATOM   13533 C  CD1   A LEU C 3 18  ? 55.453  -14.721 -29.796 0.20 35.42  ? 18  LEU F CD1   1 
ATOM   13534 C  CD1   B LEU C 3 18  ? 55.316  -15.007 -29.150 0.80 30.89  ? 18  LEU F CD1   1 
ATOM   13535 C  CD2   A LEU C 3 18  ? 57.065  -12.927 -29.141 0.20 33.12  ? 18  LEU F CD2   1 
ATOM   13536 C  CD2   B LEU C 3 18  ? 56.999  -13.201 -28.751 0.80 32.12  ? 18  LEU F CD2   1 
ATOM   13537 N  N     A LEU C 3 19  ? 52.128  -11.367 -28.243 0.20 40.96  ? 19  LEU F N     1 
ATOM   13538 N  N     B LEU C 3 19  ? 52.273  -11.544 -28.251 0.80 42.25  ? 19  LEU F N     1 
ATOM   13539 C  CA    A LEU C 3 19  ? 51.466  -11.274 -26.945 0.20 37.13  ? 19  LEU F CA    1 
ATOM   13540 C  CA    B LEU C 3 19  ? 51.583  -11.306 -26.984 0.80 37.00  ? 19  LEU F CA    1 
ATOM   13541 C  C     A LEU C 3 19  ? 50.170  -12.074 -26.926 0.20 38.01  ? 19  LEU F C     1 
ATOM   13542 C  C     B LEU C 3 19  ? 50.250  -12.042 -26.927 0.80 38.01  ? 19  LEU F C     1 
ATOM   13543 O  O     A LEU C 3 19  ? 49.880  -12.780 -25.952 0.20 35.23  ? 19  LEU F O     1 
ATOM   13544 O  O     B LEU C 3 19  ? 49.935  -12.706 -25.930 0.80 34.93  ? 19  LEU F O     1 
ATOM   13545 C  CB    A LEU C 3 19  ? 51.191  -9.810  -26.604 0.20 39.71  ? 19  LEU F CB    1 
ATOM   13546 C  CB    B LEU C 3 19  ? 51.364  -9.811  -26.788 0.80 39.88  ? 19  LEU F CB    1 
ATOM   13547 C  CG    A LEU C 3 19  ? 52.403  -8.928  -26.315 0.20 34.49  ? 19  LEU F CG    1 
ATOM   13548 C  CG    B LEU C 3 19  ? 52.523  -8.958  -26.300 0.80 34.14  ? 19  LEU F CG    1 
ATOM   13549 C  CD1   A LEU C 3 19  ? 52.028  -7.460  -26.443 0.20 36.09  ? 19  LEU F CD1   1 
ATOM   13550 C  CD1   B LEU C 3 19  ? 52.158  -7.491  -26.483 0.80 35.90  ? 19  LEU F CD1   1 
ATOM   13551 C  CD2   A LEU C 3 19  ? 52.945  -9.221  -24.926 0.20 35.49  ? 19  LEU F CD2   1 
ATOM   13552 C  CD2   B LEU C 3 19  ? 52.828  -9.261  -24.837 0.80 35.78  ? 19  LEU F CD2   1 
ATOM   13553 N  N     A GLU C 3 20  ? 49.374  -11.975 -27.994 0.20 38.95  ? 20  GLU F N     1 
ATOM   13554 N  N     B GLU C 3 20  ? 49.440  -11.918 -27.984 0.80 38.70  ? 20  GLU F N     1 
ATOM   13555 C  CA    A GLU C 3 20  ? 48.110  -12.702 -28.047 0.20 39.57  ? 20  GLU F CA    1 
ATOM   13556 C  CA    B GLU C 3 20  ? 48.163  -12.628 -28.027 0.80 39.56  ? 20  GLU F CA    1 
ATOM   13557 C  C     A GLU C 3 20  ? 48.326  -14.200 -28.209 0.20 38.15  ? 20  GLU F C     1 
ATOM   13558 C  C     B GLU C 3 20  ? 48.368  -14.134 -28.096 0.80 38.04  ? 20  GLU F C     1 
ATOM   13559 O  O     A GLU C 3 20  ? 47.503  -14.996 -27.746 0.20 36.17  ? 20  GLU F O     1 
ATOM   13560 O  O     B GLU C 3 20  ? 47.638  -14.893 -27.455 0.80 35.98  ? 20  GLU F O     1 
ATOM   13561 C  CB    A GLU C 3 20  ? 47.244  -12.166 -29.188 0.20 44.17  ? 20  GLU F CB    1 
ATOM   13562 C  CB    B GLU C 3 20  ? 47.329  -12.165 -29.223 0.80 43.83  ? 20  GLU F CB    1 
ATOM   13563 C  CG    A GLU C 3 20  ? 46.876  -10.700 -29.054 0.20 46.42  ? 20  GLU F CG    1 
ATOM   13564 C  CG    B GLU C 3 20  ? 46.710  -10.796 -29.078 0.80 45.65  ? 20  GLU F CG    1 
ATOM   13565 C  CD    A GLU C 3 20  ? 46.145  -10.169 -30.271 0.20 66.27  ? 20  GLU F CD    1 
ATOM   13566 C  CD    B GLU C 3 20  ? 45.787  -10.453 -30.233 0.80 68.92  ? 20  GLU F CD    1 
ATOM   13567 O  OE1   A GLU C 3 20  ? 46.216  -10.816 -31.337 0.20 66.55  ? 20  GLU F OE1   1 
ATOM   13568 O  OE1   B GLU C 3 20  ? 46.294  -10.179 -31.345 0.80 70.08  ? 20  GLU F OE1   1 
ATOM   13569 O  OE2   A GLU C 3 20  ? 45.498  -9.106  -30.161 0.20 68.68  ? 20  GLU F OE2   1 
ATOM   13570 O  OE2   B GLU C 3 20  ? 44.552  -10.470 -30.030 0.80 86.12  ? 20  GLU F OE2   1 
ATOM   13571 N  N     A ALA C 3 21  ? 49.415  -14.605 -28.867 0.20 37.67  ? 21  ALA F N     1 
ATOM   13572 N  N     B ALA C 3 21  ? 49.338  -14.590 -28.890 0.80 37.68  ? 21  ALA F N     1 
ATOM   13573 C  CA    A ALA C 3 21  ? 49.684  -16.029 -29.030 0.20 39.91  ? 21  ALA F CA    1 
ATOM   13574 C  CA    B ALA C 3 21  ? 49.571  -16.027 -28.994 0.80 40.17  ? 21  ALA F CA    1 
ATOM   13575 C  C     A ALA C 3 21  ? 50.030  -16.683 -27.698 0.20 37.39  ? 21  ALA F C     1 
ATOM   13576 C  C     B ALA C 3 21  ? 50.000  -16.616 -27.655 0.80 37.31  ? 21  ALA F C     1 
ATOM   13577 O  O     A ALA C 3 21  ? 49.541  -17.776 -27.391 0.20 36.37  ? 21  ALA F O     1 
ATOM   13578 O  O     B ALA C 3 21  ? 49.594  -17.729 -27.298 0.80 35.98  ? 21  ALA F O     1 
ATOM   13579 C  CB    A ALA C 3 21  ? 50.811  -16.239 -30.040 0.20 38.68  ? 21  ALA F CB    1 
ATOM   13580 C  CB    B ALA C 3 21  ? 50.621  -16.317 -30.064 0.80 38.73  ? 21  ALA F CB    1 
ATOM   13581 N  N     A ALA C 3 22  ? 50.875  -16.030 -26.896 0.20 34.89  ? 22  ALA F N     1 
ATOM   13582 N  N     B ALA C 3 22  ? 50.833  -15.889 -26.907 0.80 34.55  ? 22  ALA F N     1 
ATOM   13583 C  CA    A ALA C 3 22  ? 51.249  -16.593 -25.604 0.20 36.10  ? 22  ALA F CA    1 
ATOM   13584 C  CA    B ALA C 3 22  ? 51.327  -16.406 -25.636 0.80 36.08  ? 22  ALA F CA    1 
ATOM   13585 C  C     A ALA C 3 22  ? 50.100  -16.522 -24.606 0.20 34.39  ? 22  ALA F C     1 
ATOM   13586 C  C     B ALA C 3 22  ? 50.205  -16.490 -24.609 0.80 34.32  ? 22  ALA F C     1 
ATOM   13587 O  O     A ALA C 3 22  ? 50.037  -17.337 -23.679 0.20 35.71  ? 22  ALA F O     1 
ATOM   13588 O  O     B ALA C 3 22  ? 50.165  -17.423 -23.798 0.80 35.66  ? 22  ALA F O     1 
ATOM   13589 C  CB    A ALA C 3 22  ? 52.480  -15.873 -25.055 0.20 32.88  ? 22  ALA F CB    1 
ATOM   13590 C  CB    B ALA C 3 22  ? 52.472  -15.532 -25.129 0.80 32.37  ? 22  ALA F CB    1 
ATOM   13591 N  N     A ARG C 3 23  ? 49.189  -15.563 -24.778 0.20 36.47  ? 23  ARG F N     1 
ATOM   13592 N  N     B ARG C 3 23  ? 49.278  -15.532 -24.640 0.80 36.43  ? 23  ARG F N     1 
ATOM   13593 C  CA    A ARG C 3 23  ? 48.039  -15.464 -23.883 0.20 37.01  ? 23  ARG F CA    1 
ATOM   13594 C  CA    B ARG C 3 23  ? 48.137  -15.570 -23.728 0.80 36.71  ? 23  ARG F CA    1 
ATOM   13595 C  C     A ARG C 3 23  ? 47.021  -16.560 -24.172 0.20 40.02  ? 23  ARG F C     1 
ATOM   13596 C  C     B ARG C 3 23  ? 47.201  -16.727 -24.054 0.80 40.62  ? 23  ARG F C     1 
ATOM   13597 O  O     A ARG C 3 23  ? 46.509  -17.207 -23.251 0.20 40.02  ? 23  ARG F O     1 
ATOM   13598 O  O     B ARG C 3 23  ? 46.666  -17.380 -23.147 0.80 40.48  ? 23  ARG F O     1 
ATOM   13599 C  CB    A ARG C 3 23  ? 47.392  -14.085 -24.009 0.20 38.73  ? 23  ARG F CB    1 
ATOM   13600 C  CB    B ARG C 3 23  ? 47.380  -14.245 -23.787 0.80 38.24  ? 23  ARG F CB    1 
ATOM   13601 C  CG    A ARG C 3 23  ? 46.100  -13.937 -23.218 0.20 44.09  ? 23  ARG F CG    1 
ATOM   13602 C  CG    B ARG C 3 23  ? 46.059  -14.250 -23.025 0.80 45.31  ? 23  ARG F CG    1 
ATOM   13603 C  CD    A ARG C 3 23  ? 45.320  -12.694 -23.623 0.20 46.60  ? 23  ARG F CD    1 
ATOM   13604 C  CD    B ARG C 3 23  ? 45.165  -13.098 -23.443 0.80 47.77  ? 23  ARG F CD    1 
ATOM   13605 N  NE    A ARG C 3 23  ? 46.036  -11.458 -23.330 0.20 47.45  ? 23  ARG F NE    1 
ATOM   13606 N  NE    B ARG C 3 23  ? 45.864  -11.819 -23.432 0.80 47.71  ? 23  ARG F NE    1 
ATOM   13607 C  CZ    A ARG C 3 23  ? 46.650  -10.712 -24.238 0.20 44.30  ? 23  ARG F CZ    1 
ATOM   13608 C  CZ    B ARG C 3 23  ? 45.929  -11.007 -22.385 0.80 57.68  ? 23  ARG F CZ    1 
ATOM   13609 N  NH1   A ARG C 3 23  ? 46.661  -11.048 -25.518 0.20 40.80  ? 23  ARG F NH1   1 
ATOM   13610 N  NH1   B ARG C 3 23  ? 45.353  -11.317 -21.232 0.80 59.16  ? 23  ARG F NH1   1 
ATOM   13611 N  NH2   A ARG C 3 23  ? 47.267  -9.598  -23.853 0.20 44.37  ? 23  ARG F NH2   1 
ATOM   13612 N  NH2   B ARG C 3 23  ? 46.583  -9.854  -22.499 0.80 48.97  ? 23  ARG F NH2   1 
ATOM   13613 N  N     A ALA C 3 24  ? 46.711  -16.780 -25.452 0.20 39.42  ? 24  ALA F N     1 
ATOM   13614 N  N     B ALA C 3 24  ? 46.981  -16.993 -25.337 0.80 40.26  ? 24  ALA F N     1 
ATOM   13615 C  CA    A ALA C 3 24  ? 45.712  -17.782 -25.805 0.20 37.18  ? 24  ALA F CA    1 
ATOM   13616 C  CA    B ALA C 3 24  ? 45.997  -17.976 -25.760 0.80 36.11  ? 24  ALA F CA    1 
ATOM   13617 C  C     A ALA C 3 24  ? 46.250  -19.199 -25.649 0.20 38.55  ? 24  ALA F C     1 
ATOM   13618 C  C     B ALA C 3 24  ? 46.578  -19.380 -25.903 0.80 37.68  ? 24  ALA F C     1 
ATOM   13619 O  O     A ALA C 3 24  ? 45.485  -20.118 -25.332 0.20 40.04  ? 24  ALA F O     1 
ATOM   13620 O  O     B ALA C 3 24  ? 45.877  -20.281 -26.375 0.80 49.35  ? 24  ALA F O     1 
ATOM   13621 C  CB    A ALA C 3 24  ? 45.222  -17.551 -27.234 0.20 41.58  ? 24  ALA F CB    1 
ATOM   13622 C  CB    B ALA C 3 24  ? 45.352  -17.525 -27.072 0.80 41.69  ? 24  ALA F CB    1 
ATOM   13623 N  N     A GLY C 3 25  ? 47.545  -19.396 -25.858 0.20 37.91  ? 25  GLY F N     1 
ATOM   13624 N  N     B GLY C 3 25  ? 47.825  -19.594 -25.494 0.80 36.57  ? 25  GLY F N     1 
ATOM   13625 C  CA    A GLY C 3 25  ? 48.148  -20.707 -25.756 0.20 39.15  ? 25  GLY F CA    1 
ATOM   13626 C  CA    B GLY C 3 25  ? 48.405  -20.926 -25.549 0.80 39.73  ? 25  GLY F CA    1 
ATOM   13627 C  C     A GLY C 3 25  ? 48.481  -21.379 -27.069 0.20 42.50  ? 25  GLY F C     1 
ATOM   13628 C  C     B GLY C 3 25  ? 48.574  -21.479 -26.945 0.80 43.19  ? 25  GLY F C     1 
ATOM   13629 O  O     A GLY C 3 25  ? 48.640  -22.605 -27.090 0.20 41.08  ? 25  GLY F O     1 
ATOM   13630 O  O     B GLY C 3 25  ? 48.424  -22.689 -27.151 0.80 40.60  ? 25  GLY F O     1 
ATOM   13631 N  N     A GLN C 3 26  ? 48.592  -20.624 -28.159 0.20 39.77  ? 26  GLN F N     1 
ATOM   13632 N  N     B GLN C 3 26  ? 48.883  -20.625 -27.918 0.80 39.42  ? 26  GLN F N     1 
ATOM   13633 C  CA    A GLN C 3 26  ? 48.885  -21.191 -29.472 0.20 34.00  ? 26  GLN F CA    1 
ATOM   13634 C  CA    B GLN C 3 26  ? 49.022  -21.059 -29.303 0.80 30.85  ? 26  GLN F CA    1 
ATOM   13635 C  C     A GLN C 3 26  ? 50.389  -21.392 -29.583 0.20 40.28  ? 26  GLN F C     1 
ATOM   13636 C  C     B GLN C 3 26  ? 50.497  -21.336 -29.554 0.80 40.25  ? 26  GLN F C     1 
ATOM   13637 O  O     A GLN C 3 26  ? 51.135  -20.454 -29.873 0.20 40.09  ? 26  GLN F O     1 
ATOM   13638 O  O     B GLN C 3 26  ? 51.239  -20.476 -30.030 0.80 39.77  ? 26  GLN F O     1 
ATOM   13639 C  CB    A GLN C 3 26  ? 48.358  -20.281 -30.575 0.20 43.01  ? 26  GLN F CB    1 
ATOM   13640 C  CB    B GLN C 3 26  ? 48.473  -20.009 -30.257 0.80 43.59  ? 26  GLN F CB    1 
ATOM   13641 C  CG    A GLN C 3 26  ? 46.865  -20.013 -30.489 0.20 43.00  ? 26  GLN F CG    1 
ATOM   13642 C  CG    B GLN C 3 26  ? 46.976  -19.782 -30.159 0.80 41.52  ? 26  GLN F CG    1 
ATOM   13643 C  CD    A GLN C 3 26  ? 46.398  -19.002 -31.514 0.20 49.86  ? 26  GLN F CD    1 
ATOM   13644 C  CD    B GLN C 3 26  ? 46.519  -18.692 -31.101 0.80 51.82  ? 26  GLN F CD    1 
ATOM   13645 O  OE1   A GLN C 3 26  ? 47.209  -18.345 -32.168 0.20 47.99  ? 26  GLN F OE1   1 
ATOM   13646 O  OE1   B GLN C 3 26  ? 47.018  -17.564 -31.049 0.80 50.57  ? 26  GLN F OE1   1 
ATOM   13647 N  NE2   A GLN C 3 26  ? 45.084  -18.870 -31.660 0.20 51.31  ? 26  GLN F NE2   1 
ATOM   13648 N  NE2   B GLN C 3 26  ? 45.580  -19.024 -31.985 0.80 52.06  ? 26  GLN F NE2   1 
ATOM   13649 N  N     A ASP C 3 27  ? 50.839  -22.628 -29.356 0.20 39.10  ? 27  ASP F N     1 
ATOM   13650 N  N     B ASP C 3 27  ? 50.919  -22.564 -29.239 0.80 38.58  ? 27  ASP F N     1 
ATOM   13651 C  CA    A ASP C 3 27  ? 52.271  -22.909 -29.346 0.20 41.87  ? 27  ASP F CA    1 
ATOM   13652 C  CA    B ASP C 3 27  ? 52.331  -22.926 -29.343 0.80 41.76  ? 27  ASP F CA    1 
ATOM   13653 C  C     A ASP C 3 27  ? 52.885  -22.726 -30.729 0.20 45.93  ? 27  ASP F C     1 
ATOM   13654 C  C     B ASP C 3 27  ? 52.862  -22.695 -30.752 0.80 46.02  ? 27  ASP F C     1 
ATOM   13655 O  O     A ASP C 3 27  ? 53.893  -22.026 -30.882 0.20 43.37  ? 27  ASP F O     1 
ATOM   13656 O  O     B ASP C 3 27  ? 53.905  -22.053 -30.939 0.80 43.36  ? 27  ASP F O     1 
ATOM   13657 C  CB    A ASP C 3 27  ? 52.526  -24.327 -28.835 0.20 44.51  ? 27  ASP F CB    1 
ATOM   13658 C  CB    B ASP C 3 27  ? 52.533  -24.388 -28.944 0.80 44.45  ? 27  ASP F CB    1 
ATOM   13659 C  CG    A ASP C 3 27  ? 52.069  -24.523 -27.404 0.20 46.14  ? 27  ASP F CG    1 
ATOM   13660 C  CG    B ASP C 3 27  ? 51.997  -24.702 -27.565 0.80 45.84  ? 27  ASP F CG    1 
ATOM   13661 O  OD1   A ASP C 3 27  ? 51.428  -23.606 -26.849 0.20 50.71  ? 27  ASP F OD1   1 
ATOM   13662 O  OD1   B ASP C 3 27  ? 51.105  -23.973 -27.077 0.80 57.13  ? 27  ASP F OD1   1 
ATOM   13663 O  OD2   A ASP C 3 27  ? 52.353  -25.597 -26.833 0.20 53.18  ? 27  ASP F OD2   1 
ATOM   13664 O  OD2   B ASP C 3 27  ? 52.477  -25.688 -26.965 0.80 54.37  ? 27  ASP F OD2   1 
ATOM   13665 N  N     A ASP C 3 28  ? 52.299  -23.366 -31.747 0.20 46.48  ? 28  ASP F N     1 
ATOM   13666 N  N     B ASP C 3 28  ? 52.161  -23.234 -31.755 0.80 46.27  ? 28  ASP F N     1 
ATOM   13667 C  CA    A ASP C 3 28  ? 52.898  -23.363 -33.080 0.20 47.91  ? 28  ASP F CA    1 
ATOM   13668 C  CA    B ASP C 3 28  ? 52.619  -23.149 -33.140 0.80 48.20  ? 28  ASP F CA    1 
ATOM   13669 C  C     A ASP C 3 28  ? 53.083  -21.953 -33.619 0.20 43.25  ? 28  ASP F C     1 
ATOM   13670 C  C     B ASP C 3 28  ? 52.868  -21.707 -33.545 0.80 41.46  ? 28  ASP F C     1 
ATOM   13671 O  O     A ASP C 3 28  ? 54.050  -21.688 -34.343 0.20 44.85  ? 28  ASP F O     1 
ATOM   13672 O  O     B ASP C 3 28  ? 53.917  -21.381 -34.114 0.80 47.37  ? 28  ASP F O     1 
ATOM   13673 C  CB    A ASP C 3 28  ? 52.044  -24.186 -34.046 0.20 55.12  ? 28  ASP F CB    1 
ATOM   13674 C  CB    B ASP C 3 28  ? 51.588  -23.780 -34.078 0.80 54.48  ? 28  ASP F CB    1 
ATOM   13675 C  CG    A ASP C 3 28  ? 52.195  -25.680 -33.833 0.20 66.10  ? 28  ASP F CG    1 
ATOM   13676 C  CG    B ASP C 3 28  ? 51.303  -25.228 -33.748 0.80 66.72  ? 28  ASP F CG    1 
ATOM   13677 O  OD1   A ASP C 3 28  ? 53.275  -26.112 -33.376 0.20 61.77  ? 28  ASP F OD1   1 
ATOM   13678 O  OD1   B ASP C 3 28  ? 52.209  -25.911 -33.220 0.80 73.24  ? 28  ASP F OD1   1 
ATOM   13679 O  OD2   A ASP C 3 28  ? 51.234  -26.422 -34.129 0.20 67.93  ? 28  ASP F OD2   1 
ATOM   13680 O  OD2   B ASP C 3 28  ? 50.172  -25.685 -34.025 0.80 69.51  ? 28  ASP F OD2   1 
ATOM   13681 N  N     A GLU C 3 29  ? 52.177  -21.035 -33.277 0.20 41.98  ? 29  GLU F N     1 
ATOM   13682 N  N     B GLU C 3 29  ? 51.909  -20.826 -33.248 0.80 39.83  ? 29  GLU F N     1 
ATOM   13683 C  CA    A GLU C 3 29  ? 52.318  -19.663 -33.747 0.20 41.63  ? 29  GLU F CA    1 
ATOM   13684 C  CA    B GLU C 3 29  ? 52.036  -19.430 -33.638 0.80 40.04  ? 29  GLU F CA    1 
ATOM   13685 C  C     A GLU C 3 29  ? 53.457  -18.941 -33.036 0.20 43.81  ? 29  GLU F C     1 
ATOM   13686 C  C     B GLU C 3 29  ? 53.230  -18.771 -32.951 0.80 46.07  ? 29  GLU F C     1 
ATOM   13687 O  O     A GLU C 3 29  ? 54.061  -18.027 -33.609 0.20 39.97  ? 29  GLU F O     1 
ATOM   13688 O  O     B GLU C 3 29  ? 53.926  -17.951 -33.560 0.80 39.93  ? 29  GLU F O     1 
ATOM   13689 C  CB    A GLU C 3 29  ? 51.002  -18.909 -33.562 0.20 43.12  ? 29  GLU F CB    1 
ATOM   13690 C  CB    B GLU C 3 29  ? 50.735  -18.690 -33.324 0.80 41.24  ? 29  GLU F CB    1 
ATOM   13691 C  CG    A GLU C 3 29  ? 50.941  -17.586 -34.307 0.20 47.90  ? 29  GLU F CG    1 
ATOM   13692 C  CG    B GLU C 3 29  ? 50.504  -17.418 -34.135 0.80 49.22  ? 29  GLU F CG    1 
ATOM   13693 C  CD    A GLU C 3 29  ? 51.067  -17.753 -35.812 0.20 50.34  ? 29  GLU F CD    1 
ATOM   13694 C  CD    B GLU C 3 29  ? 50.059  -17.687 -35.568 0.80 56.19  ? 29  GLU F CD    1 
ATOM   13695 O  OE1   A GLU C 3 29  ? 50.570  -18.767 -36.347 0.20 55.28  ? 29  GLU F OE1   1 
ATOM   13696 O  OE1   B GLU C 3 29  ? 50.024  -18.866 -35.979 0.80 63.89  ? 29  GLU F OE1   1 
ATOM   13697 O  OE2   A GLU C 3 29  ? 51.666  -16.871 -36.461 0.20 44.53  ? 29  GLU F OE2   1 
ATOM   13698 O  OE2   B GLU C 3 29  ? 49.742  -16.713 -36.288 0.80 60.79  ? 29  GLU F OE2   1 
ATOM   13699 N  N     A VAL C 3 30  ? 53.772  -19.337 -31.799 0.20 40.93  ? 30  VAL F N     1 
ATOM   13700 N  N     B VAL C 3 30  ? 53.501  -19.136 -31.691 0.80 39.55  ? 30  VAL F N     1 
ATOM   13701 C  CA    A VAL C 3 30  ? 54.870  -18.703 -31.074 0.20 39.88  ? 30  VAL F CA    1 
ATOM   13702 C  CA    B VAL C 3 30  ? 54.649  -18.570 -30.980 0.80 39.49  ? 30  VAL F CA    1 
ATOM   13703 C  C     A VAL C 3 30  ? 56.205  -18.999 -31.751 0.20 39.78  ? 30  VAL F C     1 
ATOM   13704 C  C     B VAL C 3 30  ? 55.952  -18.903 -31.706 0.80 40.42  ? 30  VAL F C     1 
ATOM   13705 O  O     A VAL C 3 30  ? 57.062  -18.114 -31.880 0.20 35.86  ? 30  VAL F O     1 
ATOM   13706 O  O     B VAL C 3 30  ? 56.777  -18.019 -31.981 0.80 34.95  ? 30  VAL F O     1 
ATOM   13707 C  CB    A VAL C 3 30  ? 54.866  -19.148 -29.599 0.20 38.23  ? 30  VAL F CB    1 
ATOM   13708 C  CB    B VAL C 3 30  ? 54.673  -19.060 -29.521 0.80 37.75  ? 30  VAL F CB    1 
ATOM   13709 C  CG1   A VAL C 3 30  ? 56.127  -18.668 -28.892 0.20 38.19  ? 30  VAL F CG1   1 
ATOM   13710 C  CG1   B VAL C 3 30  ? 56.024  -18.745 -28.877 0.80 38.23  ? 30  VAL F CG1   1 
ATOM   13711 C  CG2   A VAL C 3 30  ? 53.624  -18.620 -28.891 0.20 37.98  ? 30  VAL F CG2   1 
ATOM   13712 C  CG2   B VAL C 3 30  ? 53.523  -18.430 -28.730 0.80 37.53  ? 30  VAL F CG2   1 
ATOM   13713 N  N     A ARG C 3 31  ? 56.404  -20.242 -32.199 0.20 41.45  ? 31  ARG F N     1 
ATOM   13714 N  N     B ARG C 3 31  ? 56.160  -20.188 -32.017 0.80 40.70  ? 31  ARG F N     1 
ATOM   13715 C  CA    A ARG C 3 31  ? 57.626  -20.579 -32.923 0.20 40.88  ? 31  ARG F CA    1 
ATOM   13716 C  CA    B ARG C 3 31  ? 57.348  -20.601 -32.762 0.80 41.45  ? 31  ARG F CA    1 
ATOM   13717 C  C     A ARG C 3 31  ? 57.712  -19.851 -34.259 0.20 41.58  ? 31  ARG F C     1 
ATOM   13718 C  C     B ARG C 3 31  ? 57.466  -19.867 -34.094 0.80 42.70  ? 31  ARG F C     1 
ATOM   13719 O  O     A ARG C 3 31  ? 58.811  -19.487 -34.694 0.20 38.66  ? 31  ARG F O     1 
ATOM   13720 O  O     B ARG C 3 31  ? 58.559  -19.418 -34.464 0.80 40.15  ? 31  ARG F O     1 
ATOM   13721 C  CB    A ARG C 3 31  ? 57.713  -22.087 -33.157 0.20 44.62  ? 31  ARG F CB    1 
ATOM   13722 C  CB    B ARG C 3 31  ? 57.324  -22.112 -33.004 0.80 45.47  ? 31  ARG F CB    1 
ATOM   13723 C  CG    A ARG C 3 31  ? 57.743  -22.936 -31.895 0.20 49.99  ? 31  ARG F CG    1 
ATOM   13724 C  CG    B ARG C 3 31  ? 58.247  -22.930 -32.111 0.80 52.86  ? 31  ARG F CG    1 
ATOM   13725 C  CD    A ARG C 3 31  ? 57.966  -24.402 -32.244 0.20 51.41  ? 31  ARG F CD    1 
ATOM   13726 C  CD    B ARG C 3 31  ? 57.746  -22.999 -30.676 0.80 50.62  ? 31  ARG F CD    1 
ATOM   13727 N  NE    A ARG C 3 31  ? 57.697  -25.284 -31.116 0.20 52.63  ? 31  ARG F NE    1 
ATOM   13728 N  NE    B ARG C 3 31  ? 58.440  -24.032 -29.913 0.80 59.94  ? 31  ARG F NE    1 
ATOM   13729 C  CZ    A ARG C 3 31  ? 58.614  -25.709 -30.258 0.20 56.00  ? 31  ARG F CZ    1 
ATOM   13730 C  CZ    B ARG C 3 31  ? 57.955  -25.242 -29.658 0.80 59.92  ? 31  ARG F CZ    1 
ATOM   13731 N  NH1   A ARG C 3 31  ? 59.882  -25.348 -30.365 0.20 51.02  ? 31  ARG F NH1   1 
ATOM   13732 N  NH1   B ARG C 3 31  ? 56.755  -25.610 -30.074 0.80 50.20  ? 31  ARG F NH1   1 
ATOM   13733 N  NH2   A ARG C 3 31  ? 58.249  -26.518 -29.267 0.20 56.94  ? 31  ARG F NH2   1 
ATOM   13734 N  NH2   B ARG C 3 31  ? 58.695  -26.106 -28.967 0.80 60.19  ? 31  ARG F NH2   1 
ATOM   13735 N  N     A ILE C 3 32  ? 56.575  -19.634 -34.922 0.20 38.38  ? 32  ILE F N     1 
ATOM   13736 N  N     B ILE C 3 32  ? 56.361  -19.748 -34.839 0.80 37.54  ? 32  ILE F N     1 
ATOM   13737 C  CA    A ILE C 3 32  ? 56.595  -18.977 -36.226 0.20 37.80  ? 32  ILE F CA    1 
ATOM   13738 C  CA    B ILE C 3 32  ? 56.433  -19.127 -36.162 0.80 38.04  ? 32  ILE F CA    1 
ATOM   13739 C  C     A ILE C 3 32  ? 56.943  -17.502 -36.077 0.20 38.11  ? 32  ILE F C     1 
ATOM   13740 C  C     B ILE C 3 32  ? 56.822  -17.662 -36.038 0.80 38.84  ? 32  ILE F C     1 
ATOM   13741 O  O     A ILE C 3 32  ? 57.738  -16.956 -36.852 0.20 34.73  ? 32  ILE F O     1 
ATOM   13742 O  O     B ILE C 3 32  ? 57.668  -17.161 -36.791 0.80 34.41  ? 32  ILE F O     1 
ATOM   13743 C  CB    A ILE C 3 32  ? 55.248  -19.172 -36.947 0.20 37.11  ? 32  ILE F CB    1 
ATOM   13744 C  CB    B ILE C 3 32  ? 55.102  -19.290 -36.922 0.80 36.40  ? 32  ILE F CB    1 
ATOM   13745 C  CG1   A ILE C 3 32  ? 55.037  -20.649 -37.291 0.20 39.20  ? 32  ILE F CG1   1 
ATOM   13746 C  CG1   B ILE C 3 32  ? 54.720  -20.764 -37.041 0.80 39.70  ? 32  ILE F CG1   1 
ATOM   13747 C  CG2   A ILE C 3 32  ? 55.178  -18.313 -38.207 0.20 41.86  ? 32  ILE F CG2   1 
ATOM   13748 C  CG2   B ILE C 3 32  ? 55.208  -18.675 -38.322 0.80 43.58  ? 32  ILE F CG2   1 
ATOM   13749 C  CD1   A ILE C 3 32  ? 53.747  -20.924 -38.037 0.20 38.93  ? 32  ILE F CD1   1 
ATOM   13750 C  CD1   B ILE C 3 32  ? 55.671  -21.579 -37.863 0.80 38.01  ? 32  ILE F CD1   1 
ATOM   13751 N  N     A LEU C 3 33  ? 56.363  -16.837 -35.075 0.20 35.25  ? 33  LEU F N     1 
ATOM   13752 N  N     B LEU C 3 33  ? 56.218  -16.954 -35.078 0.80 35.23  ? 33  LEU F N     1 
ATOM   13753 C  CA    A LEU C 3 33  ? 56.619  -15.413 -34.889 0.20 30.24  ? 33  LEU F CA    1 
ATOM   13754 C  CA    B LEU C 3 33  ? 56.510  -15.536 -34.909 0.80 29.30  ? 33  LEU F CA    1 
ATOM   13755 C  C     A LEU C 3 33  ? 58.070  -15.157 -34.495 0.20 35.33  ? 33  LEU F C     1 
ATOM   13756 C  C     B LEU C 3 33  ? 57.961  -15.321 -34.487 0.80 35.88  ? 33  LEU F C     1 
ATOM   13757 O  O     A LEU C 3 33  ? 58.714  -14.252 -35.039 0.20 33.92  ? 33  LEU F O     1 
ATOM   13758 O  O     B LEU C 3 33  ? 58.647  -14.452 -35.038 0.80 34.10  ? 33  LEU F O     1 
ATOM   13759 C  CB    A LEU C 3 33  ? 55.654  -14.840 -33.847 0.20 33.30  ? 33  LEU F CB    1 
ATOM   13760 C  CB    B LEU C 3 33  ? 55.526  -14.913 -33.900 0.80 32.85  ? 33  LEU F CB    1 
ATOM   13761 C  CG    A LEU C 3 33  ? 54.182  -14.854 -34.266 0.20 33.01  ? 33  LEU F CG    1 
ATOM   13762 C  CG    B LEU C 3 33  ? 54.052  -14.942 -34.314 0.80 32.59  ? 33  LEU F CG    1 
ATOM   13763 C  CD1   A LEU C 3 33  ? 53.272  -14.448 -33.116 0.20 38.58  ? 33  LEU F CD1   1 
ATOM   13764 C  CD1   B LEU C 3 33  ? 53.127  -14.591 -33.149 0.80 38.81  ? 33  LEU F CD1   1 
ATOM   13765 C  CD2   A LEU C 3 33  ? 53.958  -13.947 -35.463 0.20 36.57  ? 33  LEU F CD2   1 
ATOM   13766 C  CD2   B LEU C 3 33  ? 53.786  -14.005 -35.467 0.80 36.46  ? 33  LEU F CD2   1 
ATOM   13767 N  N     A MET C 3 34  ? 58.609  -15.951 -33.565 0.20 34.33  ? 34  MET F N     1 
ATOM   13768 N  N     B MET C 3 34  ? 58.462  -16.119 -33.538 0.80 34.73  ? 34  MET F N     1 
ATOM   13769 C  CA    A MET C 3 34  ? 60.006  -15.785 -33.181 0.20 33.95  ? 34  MET F CA    1 
ATOM   13770 C  CA    B MET C 3 34  ? 59.855  -15.962 -33.134 0.80 33.63  ? 34  MET F CA    1 
ATOM   13771 C  C     A MET C 3 34  ? 60.958  -16.062 -34.338 0.20 31.60  ? 34  MET F C     1 
ATOM   13772 C  C     B MET C 3 34  ? 60.790  -16.186 -34.317 0.80 31.45  ? 34  MET F C     1 
ATOM   13773 O  O     A MET C 3 34  ? 62.097  -15.585 -34.317 0.20 32.95  ? 34  MET F O     1 
ATOM   13774 O  O     B MET C 3 34  ? 61.765  -15.449 -34.493 0.80 32.48  ? 34  MET F O     1 
ATOM   13775 C  CB    A MET C 3 34  ? 60.348  -16.694 -31.998 0.20 31.76  ? 34  MET F CB    1 
ATOM   13776 C  CB    B MET C 3 34  ? 60.198  -16.911 -31.985 0.80 30.87  ? 34  MET F CB    1 
ATOM   13777 C  CG    A MET C 3 34  ? 59.635  -16.328 -30.702 0.20 36.33  ? 34  MET F CG    1 
ATOM   13778 C  CG    B MET C 3 34  ? 59.490  -16.599 -30.656 0.80 37.00  ? 34  MET F CG    1 
ATOM   13779 S  SD    A MET C 3 34  ? 60.305  -17.209 -29.276 0.20 40.20  ? 34  MET F SD    1 
ATOM   13780 S  SD    B MET C 3 34  ? 60.149  -17.606 -29.304 0.80 43.10  ? 34  MET F SD    1 
ATOM   13781 C  CE    A MET C 3 34  ? 60.037  -18.911 -29.768 0.20 39.53  ? 34  MET F CE    1 
ATOM   13782 C  CE    B MET C 3 34  ? 60.198  -19.209 -30.099 0.80 40.92  ? 34  MET F CE    1 
ATOM   13783 N  N     A ALA C 3 35  ? 60.516  -16.816 -35.347 0.20 31.57  ? 35  ALA F N     1 
ATOM   13784 N  N     B ALA C 3 35  ? 60.478  -17.171 -35.166 0.80 27.83  ? 35  ALA F N     1 
ATOM   13785 C  CA    A ALA C 3 35  ? 61.353  -17.080 -36.511 0.20 32.06  ? 35  ALA F CA    1 
ATOM   13786 C  CA    B ALA C 3 35  ? 61.335  -17.450 -36.320 0.80 32.60  ? 35  ALA F CA    1 
ATOM   13787 C  C     A ALA C 3 35  ? 61.387  -15.912 -37.488 0.20 34.75  ? 35  ALA F C     1 
ATOM   13788 C  C     B ALA C 3 35  ? 61.369  -16.287 -37.306 0.80 33.67  ? 35  ALA F C     1 
ATOM   13789 O  O     A ALA C 3 35  ? 62.268  -15.872 -38.355 0.20 34.44  ? 35  ALA F O     1 
ATOM   13790 O  O     B ALA C 3 35  ? 62.348  -16.136 -38.052 0.80 38.00  ? 35  ALA F O     1 
ATOM   13791 C  CB    A ALA C 3 35  ? 60.870  -18.340 -37.234 0.20 32.79  ? 35  ALA F CB    1 
ATOM   13792 C  CB    B ALA C 3 35  ? 60.869  -18.724 -37.026 0.80 31.35  ? 35  ALA F CB    1 
ATOM   13793 N  N     A ASN C 3 36  ? 60.454  -14.968 -37.372 0.20 33.66  ? 36  ASN F N     1 
ATOM   13794 N  N     B ASN C 3 36  ? 60.319  -15.472 -37.341 0.80 34.44  ? 36  ASN F N     1 
ATOM   13795 C  CA    A ASN C 3 36  ? 60.393  -13.809 -38.254 0.20 33.76  ? 36  ASN F CA    1 
ATOM   13796 C  CA    B ASN C 3 36  ? 60.206  -14.346 -38.259 0.80 34.43  ? 36  ASN F CA    1 
ATOM   13797 C  C     A ASN C 3 36  ? 60.773  -12.518 -37.537 0.20 34.16  ? 36  ASN F C     1 
ATOM   13798 C  C     B ASN C 3 36  ? 60.585  -13.022 -37.616 0.80 32.05  ? 36  ASN F C     1 
ATOM   13799 O  O     A ASN C 3 36  ? 60.467  -11.425 -38.027 0.20 33.23  ? 36  ASN F O     1 
ATOM   13800 O  O     B ASN C 3 36  ? 60.279  -11.962 -38.174 0.80 34.75  ? 36  ASN F O     1 
ATOM   13801 C  CB    A ASN C 3 36  ? 59.002  -13.689 -38.878 0.20 34.93  ? 36  ASN F CB    1 
ATOM   13802 C  CB    B ASN C 3 36  ? 58.786  -14.262 -38.825 0.80 33.97  ? 36  ASN F CB    1 
ATOM   13803 C  CG    A ASN C 3 36  ? 58.735  -14.765 -39.914 0.20 40.44  ? 36  ASN F CG    1 
ATOM   13804 C  CG    B ASN C 3 36  ? 58.540  -15.279 -39.921 0.80 43.76  ? 36  ASN F CG    1 
ATOM   13805 O  OD1   A ASN C 3 36  ? 59.655  -15.237 -40.586 0.20 35.46  ? 36  ASN F OD1   1 
ATOM   13806 O  OD1   B ASN C 3 36  ? 58.284  -16.453 -39.649 0.80 37.29  ? 36  ASN F OD1   1 
ATOM   13807 N  ND2   A ASN C 3 36  ? 57.472  -15.159 -40.050 0.20 36.86  ? 36  ASN F ND2   1 
ATOM   13808 N  ND2   B ASN C 3 36  ? 58.622  -14.831 -41.173 0.80 40.93  ? 36  ASN F ND2   1 
ATOM   13809 N  N     A GLY C 3 37  ? 61.439  -12.621 -36.390 0.20 32.25  ? 37  GLY F N     1 
ATOM   13810 N  N     B GLY C 3 37  ? 61.238  -13.056 -36.458 0.80 31.85  ? 37  GLY F N     1 
ATOM   13811 C  CA    A GLY C 3 37  ? 61.927  -11.453 -35.689 0.20 31.02  ? 37  GLY F CA    1 
ATOM   13812 C  CA    B GLY C 3 37  ? 61.811  -11.867 -35.865 0.80 28.46  ? 37  GLY F CA    1 
ATOM   13813 C  C     A GLY C 3 37  ? 60.958  -10.820 -34.720 0.20 33.66  ? 37  GLY F C     1 
ATOM   13814 C  C     B GLY C 3 37  ? 60.986  -11.203 -34.787 0.80 33.51  ? 37  GLY F C     1 
ATOM   13815 O  O     A GLY C 3 37  ? 61.119  -9.639  -34.389 0.20 33.78  ? 37  GLY F O     1 
ATOM   13816 O  O     B GLY C 3 37  ? 61.336  -10.093 -34.364 0.80 35.63  ? 37  GLY F O     1 
ATOM   13817 N  N     A ALA C 3 38  ? 59.953  -11.559 -34.255 0.20 35.87  ? 38  ALA F N     1 
ATOM   13818 N  N     B ALA C 3 38  ? 59.905  -11.836 -34.334 0.80 37.23  ? 38  ALA F N     1 
ATOM   13819 C  CA    A ALA C 3 38  ? 59.019  -11.007 -33.283 0.20 33.13  ? 38  ALA F CA    1 
ATOM   13820 C  CA    B ALA C 3 38  ? 59.080  -11.259 -33.279 0.80 33.30  ? 38  ALA F CA    1 
ATOM   13821 C  C     A ALA C 3 38  ? 59.742  -10.691 -31.981 0.20 30.79  ? 38  ALA F C     1 
ATOM   13822 C  C     B ALA C 3 38  ? 59.921  -10.949 -32.047 0.80 29.93  ? 38  ALA F C     1 
ATOM   13823 O  O     A ALA C 3 38  ? 60.420  -11.549 -31.409 0.20 30.08  ? 38  ALA F O     1 
ATOM   13824 O  O     B ALA C 3 38  ? 60.833  -11.697 -31.693 0.80 29.63  ? 38  ALA F O     1 
ATOM   13825 C  CB    A ALA C 3 38  ? 57.872  -11.984 -33.027 0.20 31.54  ? 38  ALA F CB    1 
ATOM   13826 C  CB    B ALA C 3 38  ? 57.941  -12.215 -32.917 0.80 30.37  ? 38  ALA F CB    1 
ATOM   13827 N  N     A ASP C 3 39  ? 59.605  -9.444  -31.530 0.20 31.31  ? 39  ASP F N     1 
ATOM   13828 N  N     B ASP C 3 39  ? 59.619  -9.818  -31.410 0.80 32.37  ? 39  ASP F N     1 
ATOM   13829 C  CA    A ASP C 3 39  ? 60.163  -8.990  -30.263 0.20 30.74  ? 39  ASP F CA    1 
ATOM   13830 C  CA    B ASP C 3 39  ? 60.281  -9.388  -30.180 0.80 30.79  ? 39  ASP F CA    1 
ATOM   13831 C  C     A ASP C 3 39  ? 59.648  -9.852  -29.117 0.20 29.43  ? 39  ASP F C     1 
ATOM   13832 C  C     B ASP C 3 39  ? 59.738  -10.216 -29.019 0.80 28.66  ? 39  ASP F C     1 
ATOM   13833 O  O     A ASP C 3 39  ? 58.477  -9.753  -28.736 0.20 29.06  ? 39  ASP F O     1 
ATOM   13834 O  O     B ASP C 3 39  ? 58.630  -9.969  -28.532 0.80 30.04  ? 39  ASP F O     1 
ATOM   13835 C  CB    A ASP C 3 39  ? 59.811  -7.516  -30.035 0.20 27.13  ? 39  ASP F CB    1 
ATOM   13836 C  CB    B ASP C 3 39  ? 60.044  -7.898  -29.951 0.80 27.47  ? 39  ASP F CB    1 
ATOM   13837 C  CG    A ASP C 3 39  ? 60.397  -6.956  -28.750 0.20 26.69  ? 39  ASP F CG    1 
ATOM   13838 C  CG    B ASP C 3 39  ? 60.880  -7.333  -28.819 0.80 25.18  ? 39  ASP F CG    1 
ATOM   13839 O  OD1   A ASP C 3 39  ? 61.343  -7.559  -28.197 0.20 29.89  ? 39  ASP F OD1   1 
ATOM   13840 O  OD1   B ASP C 3 39  ? 61.495  -8.100  -28.034 0.80 31.19  ? 39  ASP F OD1   1 
ATOM   13841 O  OD2   A ASP C 3 39  ? 59.904  -5.901  -28.289 0.20 22.28  ? 39  ASP F OD2   1 
ATOM   13842 O  OD2   B ASP C 3 39  ? 60.947  -6.093  -28.721 0.80 35.58  ? 39  ASP F OD2   1 
ATOM   13843 N  N     A VAL C 3 40  ? 60.513  -10.706 -28.568 0.20 28.93  ? 40  VAL F N     1 
ATOM   13844 N  N     B VAL C 3 40  ? 60.536  -11.188 -28.562 0.80 29.25  ? 40  VAL F N     1 
ATOM   13845 C  CA    A VAL C 3 40  ? 60.103  -11.570 -27.465 0.20 27.86  ? 40  VAL F CA    1 
ATOM   13846 C  CA    B VAL C 3 40  ? 60.181  -12.037 -27.422 0.80 27.06  ? 40  VAL F CA    1 
ATOM   13847 C  C     A VAL C 3 40  ? 59.863  -10.751 -26.201 0.20 28.03  ? 40  VAL F C     1 
ATOM   13848 C  C     B VAL C 3 40  ? 59.935  -11.208 -26.163 0.80 28.87  ? 40  VAL F C     1 
ATOM   13849 O  O     A VAL C 3 40  ? 58.905  -10.998 -25.458 0.20 30.09  ? 40  VAL F O     1 
ATOM   13850 O  O     B VAL C 3 40  ? 59.166  -11.614 -25.277 0.80 33.01  ? 40  VAL F O     1 
ATOM   13851 C  CB    A VAL C 3 40  ? 61.150  -12.676 -27.240 0.20 26.32  ? 40  VAL F CB    1 
ATOM   13852 C  CB    B VAL C 3 40  ? 61.289  -13.100 -27.219 0.80 25.31  ? 40  VAL F CB    1 
ATOM   13853 C  CG1   A VAL C 3 40  ? 60.786  -13.527 -26.036 0.20 28.81  ? 40  VAL F CG1   1 
ATOM   13854 C  CG1   B VAL C 3 40  ? 61.313  -13.660 -25.817 0.80 27.54  ? 40  VAL F CG1   1 
ATOM   13855 C  CG2   A VAL C 3 40  ? 61.265  -13.548 -28.480 0.20 28.84  ? 40  VAL F CG2   1 
ATOM   13856 C  CG2   B VAL C 3 40  ? 61.128  -14.241 -28.216 0.80 26.25  ? 40  VAL F CG2   1 
ATOM   13857 N  N     A ASN C 3 41  ? 60.714  -9.759  -25.936 0.20 27.73  ? 41  ASN F N     1 
ATOM   13858 N  N     B ASN C 3 41  ? 60.563  -10.043 -26.058 0.80 26.35  ? 41  ASN F N     1 
ATOM   13859 C  CA    A ASN C 3 41  ? 60.537  -8.925  -24.752 0.20 28.62  ? 41  ASN F CA    1 
ATOM   13860 C  CA    B ASN C 3 41  ? 60.400  -9.178  -24.898 0.80 29.44  ? 41  ASN F CA    1 
ATOM   13861 C  C     A ASN C 3 41  ? 59.572  -7.778  -25.021 0.20 25.65  ? 41  ASN F C     1 
ATOM   13862 C  C     B ASN C 3 41  ? 59.542  -7.950  -25.191 0.80 23.92  ? 41  ASN F C     1 
ATOM   13863 O  O     A ASN C 3 41  ? 59.688  -6.711  -24.412 0.20 29.64  ? 41  ASN F O     1 
ATOM   13864 O  O     B ASN C 3 41  ? 59.691  -6.917  -24.537 0.80 29.38  ? 41  ASN F O     1 
ATOM   13865 C  CB    A ASN C 3 41  ? 61.875  -8.361  -24.268 0.20 28.97  ? 41  ASN F CB    1 
ATOM   13866 C  CB    B ASN C 3 41  ? 61.758  -8.758  -24.350 0.80 28.67  ? 41  ASN F CB    1 
ATOM   13867 C  CG    A ASN C 3 41  ? 62.792  -9.428  -23.707 0.20 32.54  ? 41  ASN F CG    1 
ATOM   13868 C  CG    B ASN C 3 41  ? 62.487  -9.906  -23.681 0.80 34.79  ? 41  ASN F CG    1 
ATOM   13869 O  OD1   A ASN C 3 41  ? 62.795  -9.695  -22.506 0.20 27.76  ? 41  ASN F OD1   1 
ATOM   13870 O  OD1   B ASN C 3 41  ? 62.050  -10.399 -22.660 0.80 27.29  ? 41  ASN F OD1   1 
ATOM   13871 N  ND2   A ASN C 3 41  ? 63.581  -10.043 -24.580 0.20 28.55  ? 41  ASN F ND2   1 
ATOM   13872 N  ND2   B ASN C 3 41  ? 63.601  -10.343 -24.266 0.80 28.15  ? 41  ASN F ND2   1 
ATOM   13873 N  N     A ALA C 3 42  ? 58.619  -7.984  -25.926 0.20 28.60  ? 42  ALA F N     1 
ATOM   13874 N  N     B ALA C 3 42  ? 58.636  -8.042  -26.161 0.80 28.84  ? 42  ALA F N     1 
ATOM   13875 C  CA    A ALA C 3 42  ? 57.675  -6.927  -26.257 0.20 30.02  ? 42  ALA F CA    1 
ATOM   13876 C  CA    B ALA C 3 42  ? 57.672  -6.970  -26.361 0.80 30.02  ? 42  ALA F CA    1 
ATOM   13877 C  C     A ALA C 3 42  ? 56.627  -6.779  -25.161 0.20 27.43  ? 42  ALA F C     1 
ATOM   13878 C  C     B ALA C 3 42  ? 56.822  -6.792  -25.106 0.80 26.72  ? 42  ALA F C     1 
ATOM   13879 O  O     A ALA C 3 42  ? 56.082  -7.767  -24.660 0.20 29.07  ? 42  ALA F O     1 
ATOM   13880 O  O     B ALA C 3 42  ? 56.721  -7.687  -24.265 0.80 28.99  ? 42  ALA F O     1 
ATOM   13881 C  CB    A ALA C 3 42  ? 56.994  -7.217  -27.595 0.20 33.43  ? 42  ALA F CB    1 
ATOM   13882 C  CB    B ALA C 3 42  ? 56.765  -7.270  -27.555 0.80 33.92  ? 42  ALA F CB    1 
ATOM   13883 N  N     A THR C 3 43  ? 56.340  -5.534  -24.797 0.20 29.05  ? 43  THR F N     1 
ATOM   13884 N  N     B THR C 3 43  ? 56.209  -5.621  -24.982 0.80 27.97  ? 43  THR F N     1 
ATOM   13885 C  CA    A THR C 3 43  ? 55.404  -5.221  -23.725 0.20 32.00  ? 43  THR F CA    1 
ATOM   13886 C  CA    B THR C 3 43  ? 55.327  -5.343  -23.849 0.80 31.77  ? 43  THR F CA    1 
ATOM   13887 C  C     A THR C 3 43  ? 54.108  -4.654  -24.291 0.20 34.19  ? 43  THR F C     1 
ATOM   13888 C  C     B THR C 3 43  ? 54.000  -4.768  -24.328 0.80 34.34  ? 43  THR F C     1 
ATOM   13889 O  O     A THR C 3 43  ? 54.083  -4.079  -25.383 0.20 35.76  ? 43  THR F O     1 
ATOM   13890 O  O     B THR C 3 43  ? 53.942  -4.040  -25.323 0.80 35.77  ? 43  THR F O     1 
ATOM   13891 C  CB    A THR C 3 43  ? 56.011  -4.219  -22.736 0.20 33.46  ? 43  THR F CB    1 
ATOM   13892 C  CB    B THR C 3 43  ? 55.967  -4.350  -22.843 0.80 33.47  ? 43  THR F CB    1 
ATOM   13893 O  OG1   A THR C 3 43  ? 56.552  -3.104  -23.454 0.20 36.88  ? 43  THR F OG1   1 
ATOM   13894 O  OG1   B THR C 3 43  ? 55.857  -3.018  -23.356 0.80 43.59  ? 43  THR F OG1   1 
ATOM   13895 C  CG2   A THR C 3 43  ? 57.115  -4.874  -21.920 0.20 33.86  ? 43  THR F CG2   1 
ATOM   13896 C  CG2   B THR C 3 43  ? 57.447  -4.671  -22.594 0.80 35.01  ? 43  THR F CG2   1 
ATOM   13897 N  N     A ASP C 3 44  ? 53.028  -4.815  -23.527 0.20 35.93  ? 44  ASP F N     1 
ATOM   13898 N  N     B ASP C 3 44  ? 52.925  -5.099  -23.608 0.80 36.54  ? 44  ASP F N     1 
ATOM   13899 C  CA    A ASP C 3 44  ? 51.716  -4.315  -23.912 0.20 37.93  ? 44  ASP F CA    1 
ATOM   13900 C  CA    B ASP C 3 44  ? 51.668  -4.392  -23.802 0.80 38.24  ? 44  ASP F CA    1 
ATOM   13901 C  C     A ASP C 3 44  ? 51.507  -2.930  -23.294 0.20 37.14  ? 44  ASP F C     1 
ATOM   13902 C  C     B ASP C 3 44  ? 51.712  -3.065  -23.047 0.80 37.13  ? 44  ASP F C     1 
ATOM   13903 O  O     A ASP C 3 44  ? 52.469  -2.245  -22.940 0.20 37.47  ? 44  ASP F O     1 
ATOM   13904 O  O     B ASP C 3 44  ? 52.724  -2.703  -22.438 0.80 33.93  ? 44  ASP F O     1 
ATOM   13905 C  CB    A ASP C 3 44  ? 50.633  -5.319  -23.500 0.20 34.02  ? 44  ASP F CB    1 
ATOM   13906 C  CB    B ASP C 3 44  ? 50.477  -5.261  -23.386 0.80 33.62  ? 44  ASP F CB    1 
ATOM   13907 C  CG    A ASP C 3 44  ? 50.497  -5.454  -21.991 0.20 35.61  ? 44  ASP F CG    1 
ATOM   13908 C  CG    B ASP C 3 44  ? 50.401  -5.525  -21.873 0.80 35.51  ? 44  ASP F CG    1 
ATOM   13909 O  OD1   A ASP C 3 44  ? 51.440  -5.081  -21.261 0.20 35.15  ? 44  ASP F OD1   1 
ATOM   13910 O  OD1   B ASP C 3 44  ? 51.089  -4.865  -21.069 0.80 35.58  ? 44  ASP F OD1   1 
ATOM   13911 O  OD2   A ASP C 3 44  ? 49.439  -5.933  -21.535 0.20 35.72  ? 44  ASP F OD2   1 
ATOM   13912 O  OD2   B ASP C 3 44  ? 49.625  -6.420  -21.492 0.80 37.85  ? 44  ASP F OD2   1 
ATOM   13913 N  N     A ALA C 3 45  ? 50.249  -2.506  -23.151 0.20 36.51  ? 45  ALA F N     1 
ATOM   13914 N  N     B ALA C 3 45  ? 50.588  -2.342  -23.060 0.80 37.01  ? 45  ALA F N     1 
ATOM   13915 C  CA    A ALA C 3 45  ? 49.966  -1.203  -22.561 0.20 37.96  ? 45  ALA F CA    1 
ATOM   13916 C  CA    B ALA C 3 45  ? 50.563  -0.992  -22.504 0.80 39.29  ? 45  ALA F CA    1 
ATOM   13917 C  C     A ALA C 3 45  ? 50.246  -1.169  -21.065 0.20 39.42  ? 45  ALA F C     1 
ATOM   13918 C  C     B ALA C 3 45  ? 50.818  -0.970  -21.002 0.80 43.86  ? 45  ALA F C     1 
ATOM   13919 O  O     A ALA C 3 45  ? 50.454  -0.084  -20.510 0.20 38.57  ? 45  ALA F O     1 
ATOM   13920 O  O     B ALA C 3 45  ? 51.251  0.060   -20.475 0.80 41.18  ? 45  ALA F O     1 
ATOM   13921 C  CB    A ALA C 3 45  ? 48.512  -0.809  -22.822 0.20 35.60  ? 45  ALA F CB    1 
ATOM   13922 C  CB    B ALA C 3 45  ? 49.227  -0.321  -22.805 0.80 32.19  ? 45  ALA F CB    1 
ATOM   13923 N  N     A SER C 3 46  ? 50.259  -2.324  -20.403 0.20 37.01  ? 46  SER F N     1 
ATOM   13924 N  N     B SER C 3 46  ? 50.572  -2.075  -20.306 0.80 36.83  ? 46  SER F N     1 
ATOM   13925 C  CA    A SER C 3 46  ? 50.499  -2.404  -18.969 0.20 37.37  ? 46  SER F CA    1 
ATOM   13926 C  CA    B SER C 3 46  ? 50.843  -2.158  -18.878 0.80 38.03  ? 46  SER F CA    1 
ATOM   13927 C  C     A SER C 3 46  ? 51.809  -3.118  -18.650 0.20 37.00  ? 46  SER F C     1 
ATOM   13928 C  C     B SER C 3 46  ? 52.232  -2.698  -18.564 0.80 40.04  ? 46  SER F C     1 
ATOM   13929 O  O     A SER C 3 46  ? 51.953  -3.712  -17.579 0.20 30.91  ? 46  SER F O     1 
ATOM   13930 O  O     B SER C 3 46  ? 52.594  -2.772  -17.385 0.80 37.72  ? 46  SER F O     1 
ATOM   13931 C  CB    A SER C 3 46  ? 49.330  -3.096  -18.271 0.20 37.64  ? 46  SER F CB    1 
ATOM   13932 C  CB    B SER C 3 46  ? 49.787  -3.030  -18.188 0.80 36.57  ? 46  SER F CB    1 
ATOM   13933 O  OG    A SER C 3 46  ? 49.225  -4.454  -18.663 0.20 38.70  ? 46  SER F OG    1 
ATOM   13934 O  OG    B SER C 3 46  ? 49.862  -4.378  -18.612 0.80 38.93  ? 46  SER F OG    1 
ATOM   13935 N  N     A GLY C 3 47  ? 52.767  -3.069  -19.577 0.20 32.93  ? 47  GLY F N     1 
ATOM   13936 N  N     B GLY C 3 47  ? 53.008  -3.082  -19.577 0.80 32.47  ? 47  GLY F N     1 
ATOM   13937 C  CA    A GLY C 3 47  ? 54.090  -3.629  -19.368 0.20 31.24  ? 47  GLY F CA    1 
ATOM   13938 C  CA    B GLY C 3 47  ? 54.341  -3.617  -19.366 0.80 30.19  ? 47  GLY F CA    1 
ATOM   13939 C  C     A GLY C 3 47  ? 54.169  -5.137  -19.305 0.20 30.48  ? 47  GLY F C     1 
ATOM   13940 C  C     B GLY C 3 47  ? 54.444  -5.122  -19.214 0.80 30.53  ? 47  GLY F C     1 
ATOM   13941 O  O     A GLY C 3 47  ? 55.192  -5.666  -18.858 0.20 28.83  ? 47  GLY F O     1 
ATOM   13942 O  O     B GLY C 3 47  ? 55.512  -5.613  -18.821 0.80 27.19  ? 47  GLY F O     1 
ATOM   13943 N  N     A LEU C 3 48  ? 53.134  -5.852  -19.739 0.20 27.91  ? 48  LEU F N     1 
ATOM   13944 N  N     B LEU C 3 48  ? 53.379  -5.874  -19.503 0.80 25.14  ? 48  LEU F N     1 
ATOM   13945 C  CA    A LEU C 3 48  ? 53.146  -7.307  -19.678 0.20 28.47  ? 48  LEU F CA    1 
ATOM   13946 C  CA    B LEU C 3 48  ? 53.460  -7.329  -19.490 0.80 27.33  ? 48  LEU F CA    1 
ATOM   13947 C  C     A LEU C 3 48  ? 53.866  -7.888  -20.888 0.20 32.94  ? 48  LEU F C     1 
ATOM   13948 C  C     B LEU C 3 48  ? 54.144  -7.836  -20.751 0.80 34.41  ? 48  LEU F C     1 
ATOM   13949 O  O     A LEU C 3 48  ? 53.595  -7.502  -22.029 0.20 31.64  ? 48  LEU F O     1 
ATOM   13950 O  O     B LEU C 3 48  ? 53.877  -7.345  -21.850 0.80 31.85  ? 48  LEU F O     1 
ATOM   13951 C  CB    A LEU C 3 48  ? 51.720  -7.848  -19.601 0.20 30.10  ? 48  LEU F CB    1 
ATOM   13952 C  CB    B LEU C 3 48  ? 52.070  -7.953  -19.393 0.80 28.06  ? 48  LEU F CB    1 
ATOM   13953 C  CG    A LEU C 3 48  ? 50.961  -7.482  -18.325 0.20 31.12  ? 48  LEU F CG    1 
ATOM   13954 C  CG    B LEU C 3 48  ? 51.281  -7.777  -18.094 0.80 29.00  ? 48  LEU F CG    1 
ATOM   13955 C  CD1   A LEU C 3 48  ? 49.506  -7.906  -18.424 0.20 35.42  ? 48  LEU F CD1   1 
ATOM   13956 C  CD1   B LEU C 3 48  ? 49.893  -8.377  -18.246 0.80 37.93  ? 48  LEU F CD1   1 
ATOM   13957 C  CD2   A LEU C 3 48  ? 51.628  -8.116  -17.115 0.20 32.19  ? 48  LEU F CD2   1 
ATOM   13958 C  CD2   B LEU C 3 48  ? 52.004  -8.410  -16.910 0.80 31.84  ? 48  LEU F CD2   1 
ATOM   13959 N  N     A THR C 3 49  ? 54.775  -8.825  -20.633 0.20 28.82  ? 49  THR F N     1 
ATOM   13960 N  N     B THR C 3 49  ? 54.997  -8.840  -20.591 0.80 28.07  ? 49  THR F N     1 
ATOM   13961 C  CA    A THR C 3 49  ? 55.547  -9.529  -21.644 0.20 32.52  ? 49  THR F CA    1 
ATOM   13962 C  CA    B THR C 3 49  ? 55.657  -9.513  -21.705 0.80 32.92  ? 49  THR F CA    1 
ATOM   13963 C  C     A THR C 3 49  ? 54.920  -10.881 -21.949 0.20 31.90  ? 49  THR F C     1 
ATOM   13964 C  C     B THR C 3 49  ? 54.889  -10.763 -22.109 0.80 32.93  ? 49  THR F C     1 
ATOM   13965 O  O     A THR C 3 49  ? 54.098  -11.385 -21.177 0.20 29.28  ? 49  THR F O     1 
ATOM   13966 O  O     B THR C 3 49  ? 53.963  -11.195 -21.415 0.80 29.05  ? 49  THR F O     1 
ATOM   13967 C  CB    A THR C 3 49  ? 56.989  -9.727  -21.164 0.20 28.31  ? 49  THR F CB    1 
ATOM   13968 C  CB    B THR C 3 49  ? 57.085  -9.892  -21.318 0.80 27.89  ? 49  THR F CB    1 
ATOM   13969 O  OG1   A THR C 3 49  ? 56.985  -10.472 -19.938 0.20 29.32  ? 49  THR F OG1   1 
ATOM   13970 O  OG1   B THR C 3 49  ? 57.050  -10.900 -20.293 0.80 26.27  ? 49  THR F OG1   1 
ATOM   13971 C  CG2   A THR C 3 49  ? 57.666  -8.386  -20.944 0.20 32.03  ? 49  THR F CG2   1 
ATOM   13972 C  CG2   B THR C 3 49  ? 57.861  -8.674  -20.851 0.80 33.46  ? 49  THR F CG2   1 
ATOM   13973 N  N     A PRO C 3 50  ? 55.276  -11.499 -23.082 0.20 27.45  ? 50  PRO F N     1 
ATOM   13974 N  N     B PRO C 3 50  ? 55.240  -11.378 -23.247 0.80 27.45  ? 50  PRO F N     1 
ATOM   13975 C  CA    A PRO C 3 50  ? 54.771  -12.854 -23.358 0.20 24.90  ? 50  PRO F CA    1 
ATOM   13976 C  CA    B PRO C 3 50  ? 54.672  -12.698 -23.556 0.80 22.98  ? 50  PRO F CA    1 
ATOM   13977 C  C     A PRO C 3 50  ? 55.126  -13.860 -22.279 0.20 28.98  ? 50  PRO F C     1 
ATOM   13978 C  C     B PRO C 3 50  ? 54.902  -13.704 -22.446 0.80 29.65  ? 50  PRO F C     1 
ATOM   13979 O  O     A PRO C 3 50  ? 54.411  -14.857 -22.115 0.20 29.14  ? 50  PRO F O     1 
ATOM   13980 O  O     B PRO C 3 50  ? 54.008  -14.508 -22.150 0.80 29.09  ? 50  PRO F O     1 
ATOM   13981 C  CB    A PRO C 3 50  ? 55.430  -13.204 -24.699 0.20 30.34  ? 50  PRO F CB    1 
ATOM   13982 C  CB    B PRO C 3 50  ? 55.398  -13.090 -24.849 0.80 30.57  ? 50  PRO F CB    1 
ATOM   13983 C  CG    A PRO C 3 50  ? 55.662  -11.881 -25.351 0.20 30.54  ? 50  PRO F CG    1 
ATOM   13984 C  CG    B PRO C 3 50  ? 55.690  -11.765 -25.512 0.80 30.42  ? 50  PRO F CG    1 
ATOM   13985 C  CD    A PRO C 3 50  ? 56.011  -10.943 -24.233 0.20 29.78  ? 50  PRO F CD    1 
ATOM   13986 C  CD    B PRO C 3 50  ? 56.020  -10.836 -24.382 0.80 29.88  ? 50  PRO F CD    1 
ATOM   13987 N  N     A LEU C 3 51  ? 56.208  -13.629 -21.532 0.20 26.60  ? 51  LEU F N     1 
ATOM   13988 N  N     B LEU C 3 51  ? 56.067  -13.655 -21.795 0.80 25.24  ? 51  LEU F N     1 
ATOM   13989 C  CA    A LEU C 3 51  ? 56.521  -14.507 -20.411 0.20 28.45  ? 51  LEU F CA    1 
ATOM   13990 C  CA    B LEU C 3 51  ? 56.311  -14.542 -20.663 0.80 29.65  ? 51  LEU F CA    1 
ATOM   13991 C  C     A LEU C 3 51  ? 55.552  -14.304 -19.250 0.20 27.68  ? 51  LEU F C     1 
ATOM   13992 C  C     B LEU C 3 51  ? 55.337  -14.281 -19.517 0.80 27.16  ? 51  LEU F C     1 
ATOM   13993 O  O     A LEU C 3 51  ? 55.354  -15.220 -18.444 0.20 26.35  ? 51  LEU F O     1 
ATOM   13994 O  O     B LEU C 3 51  ? 54.842  -15.224 -18.894 0.80 26.57  ? 51  LEU F O     1 
ATOM   13995 C  CB    A LEU C 3 51  ? 57.959  -14.278 -19.953 0.20 24.78  ? 51  LEU F CB    1 
ATOM   13996 C  CB    B LEU C 3 51  ? 57.747  -14.389 -20.184 0.80 23.09  ? 51  LEU F CB    1 
ATOM   13997 C  CG    A LEU C 3 51  ? 58.542  -15.337 -19.020 0.20 26.32  ? 51  LEU F CG    1 
ATOM   13998 C  CG    B LEU C 3 51  ? 58.129  -15.402 -19.123 0.80 26.86  ? 51  LEU F CG    1 
ATOM   13999 C  CD1   A LEU C 3 51  ? 58.597  -16.687 -19.719 0.20 29.46  ? 51  LEU F CD1   1 
ATOM   14000 C  CD1   B LEU C 3 51  ? 57.788  -16.809 -19.616 0.80 28.42  ? 51  LEU F CD1   1 
ATOM   14001 C  CD2   A LEU C 3 51  ? 59.918  -14.925 -18.527 0.20 24.20  ? 51  LEU F CD2   1 
ATOM   14002 C  CD2   B LEU C 3 51  ? 59.602  -15.260 -18.737 0.80 23.04  ? 51  LEU F CD2   1 
ATOM   14003 N  N     A HIS C 3 52  ? 54.943  -13.121 -19.146 0.20 30.27  ? 52  HIS F N     1 
ATOM   14004 N  N     B HIS C 3 52  ? 55.080  -13.011 -19.203 0.80 30.50  ? 52  HIS F N     1 
ATOM   14005 C  CA    A HIS C 3 52  ? 53.950  -12.876 -18.102 0.20 29.41  ? 52  HIS F CA    1 
ATOM   14006 C  CA    B HIS C 3 52  ? 54.074  -12.660 -18.195 0.80 29.92  ? 52  HIS F CA    1 
ATOM   14007 C  C     A HIS C 3 52  ? 52.609  -13.513 -18.448 0.20 32.49  ? 52  HIS F C     1 
ATOM   14008 C  C     B HIS C 3 52  ? 52.738  -13.355 -18.460 0.80 33.60  ? 52  HIS F C     1 
ATOM   14009 O  O     A HIS C 3 52  ? 51.977  -14.151 -17.598 0.20 29.66  ? 52  HIS F O     1 
ATOM   14010 O  O     B HIS C 3 52  ? 52.120  -13.926 -17.551 0.80 29.71  ? 52  HIS F O     1 
ATOM   14011 C  CB    A HIS C 3 52  ? 53.767  -11.372 -17.880 0.20 31.10  ? 52  HIS F CB    1 
ATOM   14012 C  CB    B HIS C 3 52  ? 53.858  -11.143 -18.180 0.80 32.73  ? 52  HIS F CB    1 
ATOM   14013 C  CG    A HIS C 3 52  ? 54.913  -10.713 -17.181 0.20 30.69  ? 52  HIS F CG    1 
ATOM   14014 C  CG    B HIS C 3 52  ? 54.800  -10.384 -17.298 0.80 33.18  ? 52  HIS F CG    1 
ATOM   14015 N  ND1   A HIS C 3 52  ? 55.947  -10.102 -17.858 0.20 27.65  ? 52  HIS F ND1   1 
ATOM   14016 N  ND1   B HIS C 3 52  ? 55.804  -9.578  -17.799 0.80 26.23  ? 52  HIS F ND1   1 
ATOM   14017 C  CD2   A HIS C 3 52  ? 55.179  -10.554 -15.863 0.20 26.71  ? 52  HIS F CD2   1 
ATOM   14018 C  CD2   B HIS C 3 52  ? 54.862  -10.268 -15.951 0.80 25.95  ? 52  HIS F CD2   1 
ATOM   14019 C  CE1   A HIS C 3 52  ? 56.803  -9.600  -16.986 0.20 26.42  ? 52  HIS F CE1   1 
ATOM   14020 C  CE1   B HIS C 3 52  ? 56.452  -9.013  -16.796 0.80 24.26  ? 52  HIS F CE1   1 
ATOM   14021 N  NE2   A HIS C 3 52  ? 56.363  -9.864  -15.769 0.20 26.44  ? 52  HIS F NE2   1 
ATOM   14022 N  NE2   B HIS C 3 52  ? 55.903  -9.421  -15.663 0.80 24.82  ? 52  HIS F NE2   1 
ATOM   14023 N  N     A LEU C 3 53  ? 52.150  -13.329 -19.687 0.20 30.47  ? 53  LEU F N     1 
ATOM   14024 N  N     B LEU C 3 53  ? 52.254  -13.271 -19.697 0.80 30.40  ? 53  LEU F N     1 
ATOM   14025 C  CA    A LEU C 3 53  ? 50.847  -13.855 -20.081 0.20 29.67  ? 53  LEU F CA    1 
ATOM   14026 C  CA    B LEU C 3 53  ? 50.945  -13.825 -20.027 0.80 29.56  ? 53  LEU F CA    1 
ATOM   14027 C  C     A LEU C 3 53  ? 50.848  -15.379 -20.116 0.20 32.47  ? 53  LEU F C     1 
ATOM   14028 C  C     B LEU C 3 53  ? 50.963  -15.352 -20.039 0.80 32.51  ? 53  LEU F C     1 
ATOM   14029 O  O     A LEU C 3 53  ? 49.854  -16.015 -19.746 0.20 31.04  ? 53  LEU F O     1 
ATOM   14030 O  O     B LEU C 3 53  ? 50.017  -15.992 -19.566 0.80 30.41  ? 53  LEU F O     1 
ATOM   14031 C  CB    A LEU C 3 53  ? 50.448  -13.283 -21.440 0.20 30.42  ? 53  LEU F CB    1 
ATOM   14032 C  CB    B LEU C 3 53  ? 50.490  -13.265 -21.370 0.80 30.20  ? 53  LEU F CB    1 
ATOM   14033 C  CG    A LEU C 3 53  ? 50.357  -11.758 -21.533 0.20 31.90  ? 53  LEU F CG    1 
ATOM   14034 C  CG    B LEU C 3 53  ? 50.390  -11.737 -21.403 0.80 31.59  ? 53  LEU F CG    1 
ATOM   14035 C  CD1   A LEU C 3 53  ? 50.054  -11.325 -22.956 0.20 38.97  ? 53  LEU F CD1   1 
ATOM   14036 C  CD1   B LEU C 3 53  ? 50.155  -11.226 -22.798 0.80 39.53  ? 53  LEU F CD1   1 
ATOM   14037 C  CD2   A LEU C 3 53  ? 49.297  -11.227 -20.580 0.20 37.13  ? 53  LEU F CD2   1 
ATOM   14038 C  CD2   B LEU C 3 53  ? 49.248  -11.292 -20.500 0.80 37.23  ? 53  LEU F CD2   1 
ATOM   14039 N  N     A ALA C 3 54  ? 51.954  -15.984 -20.555 0.20 30.62  ? 54  ALA F N     1 
ATOM   14040 N  N     B ALA C 3 54  ? 52.022  -15.957 -20.585 0.80 30.63  ? 54  ALA F N     1 
ATOM   14041 C  CA    A ALA C 3 54  ? 52.027  -17.441 -20.612 0.20 30.45  ? 54  ALA F CA    1 
ATOM   14042 C  CA    B ALA C 3 54  ? 52.124  -17.415 -20.557 0.80 30.47  ? 54  ALA F CA    1 
ATOM   14043 C  C     A ALA C 3 54  ? 52.037  -18.046 -19.213 0.20 30.25  ? 54  ALA F C     1 
ATOM   14044 C  C     B ALA C 3 54  ? 52.113  -17.935 -19.123 0.80 29.96  ? 54  ALA F C     1 
ATOM   14045 O  O     A ALA C 3 54  ? 51.310  -19.008 -18.935 0.20 28.47  ? 54  ALA F O     1 
ATOM   14046 O  O     B ALA C 3 54  ? 51.440  -18.929 -18.813 0.80 27.88  ? 54  ALA F O     1 
ATOM   14047 C  CB    A ALA C 3 54  ? 53.265  -17.874 -21.398 0.20 31.62  ? 54  ALA F CB    1 
ATOM   14048 C  CB    B ALA C 3 54  ? 53.393  -17.867 -21.283 0.80 31.56  ? 54  ALA F CB    1 
ATOM   14049 N  N     A ALA C 3 55  ? 52.861  -17.496 -18.318 0.20 26.47  ? 55  ALA F N     1 
ATOM   14050 N  N     B ALA C 3 55  ? 52.854  -17.273 -18.236 0.80 25.80  ? 55  ALA F N     1 
ATOM   14051 C  CA    A ALA C 3 55  ? 52.924  -18.004 -16.952 0.20 30.23  ? 55  ALA F CA    1 
ATOM   14052 C  CA    B ALA C 3 55  ? 52.831  -17.627 -16.820 0.80 30.27  ? 55  ALA F CA    1 
ATOM   14053 C  C     A ALA C 3 55  ? 51.615  -17.786 -16.203 0.20 30.22  ? 55  ALA F C     1 
ATOM   14054 C  C     B ALA C 3 55  ? 51.472  -17.337 -16.183 0.80 29.21  ? 55  ALA F C     1 
ATOM   14055 O  O     A ALA C 3 55  ? 51.306  -18.532 -15.267 0.20 32.98  ? 55  ALA F O     1 
ATOM   14056 O  O     B ALA C 3 55  ? 51.015  -18.089 -15.315 0.80 34.93  ? 55  ALA F O     1 
ATOM   14057 C  CB    A ALA C 3 55  ? 54.079  -17.345 -16.200 0.20 27.65  ? 55  ALA F CB    1 
ATOM   14058 C  CB    B ALA C 3 55  ? 53.938  -16.875 -16.084 0.80 25.83  ? 55  ALA F CB    1 
ATOM   14059 N  N     A THR C 3 56  ? 50.838  -16.776 -16.594 0.20 29.41  ? 56  THR F N     1 
ATOM   14060 N  N     B THR C 3 56  ? 50.816  -16.249 -16.589 0.80 28.82  ? 56  THR F N     1 
ATOM   14061 C  CA    A THR C 3 56  ? 49.563  -16.521 -15.934 0.20 28.77  ? 56  THR F CA    1 
ATOM   14062 C  CA    B THR C 3 56  ? 49.509  -15.924 -16.020 0.80 26.78  ? 56  THR F CA    1 
ATOM   14063 C  C     A THR C 3 56  ? 48.499  -17.518 -16.380 0.20 34.42  ? 56  THR F C     1 
ATOM   14064 C  C     B THR C 3 56  ? 48.463  -16.970 -16.395 0.80 38.17  ? 56  THR F C     1 
ATOM   14065 O  O     A THR C 3 56  ? 47.824  -18.134 -15.547 0.20 29.68  ? 56  THR F O     1 
ATOM   14066 O  O     B THR C 3 56  ? 47.654  -17.390 -15.552 0.80 30.59  ? 56  THR F O     1 
ATOM   14067 C  CB    A THR C 3 56  ? 49.107  -15.090 -16.215 0.20 30.40  ? 56  THR F CB    1 
ATOM   14068 C  CB    B THR C 3 56  ? 49.063  -14.542 -16.498 0.80 29.45  ? 56  THR F CB    1 
ATOM   14069 O  OG1   A THR C 3 56  ? 50.099  -14.173 -15.743 0.20 28.54  ? 56  THR F OG1   1 
ATOM   14070 O  OG1   B THR C 3 56  ? 49.942  -13.547 -15.972 0.80 30.58  ? 56  THR F OG1   1 
ATOM   14071 C  CG2   A THR C 3 56  ? 47.783  -14.802 -15.521 0.20 31.48  ? 56  THR F CG2   1 
ATOM   14072 C  CG2   B THR C 3 56  ? 47.630  -14.243 -16.044 0.80 30.74  ? 56  THR F CG2   1 
ATOM   14073 N  N     A TYR C 3 57  ? 48.342  -17.692 -17.691 0.20 31.08  ? 57  TYR F N     1 
ATOM   14074 N  N     B TYR C 3 57  ? 48.462  -17.404 -17.653 0.80 30.25  ? 57  TYR F N     1 
ATOM   14075 C  CA    A TYR C 3 57  ? 47.309  -18.556 -18.247 0.20 32.58  ? 57  TYR F CA    1 
ATOM   14076 C  CA    B TYR C 3 57  ? 47.413  -18.266 -18.174 0.80 31.61  ? 57  TYR F CA    1 
ATOM   14077 C  C     A TYR C 3 57  ? 47.701  -20.029 -18.257 0.20 34.31  ? 57  TYR F C     1 
ATOM   14078 C  C     B TYR C 3 57  ? 47.825  -19.730 -18.238 0.80 33.96  ? 57  TYR F C     1 
ATOM   14079 O  O     A TYR C 3 57  ? 46.991  -20.837 -18.865 0.20 36.71  ? 57  TYR F O     1 
ATOM   14080 O  O     B TYR C 3 57  ? 47.097  -20.539 -18.818 0.80 36.94  ? 57  TYR F O     1 
ATOM   14081 C  CB    A TYR C 3 57  ? 46.951  -18.098 -19.665 0.20 35.95  ? 57  TYR F CB    1 
ATOM   14082 C  CB    B TYR C 3 57  ? 46.964  -17.772 -19.554 0.80 35.99  ? 57  TYR F CB    1 
ATOM   14083 C  CG    A TYR C 3 57  ? 46.122  -16.830 -19.709 0.20 39.91  ? 57  TYR F CG    1 
ATOM   14084 C  CG    B TYR C 3 57  ? 46.199  -16.455 -19.535 0.80 40.44  ? 57  TYR F CG    1 
ATOM   14085 C  CD1   A TYR C 3 57  ? 46.717  -15.582 -19.575 0.20 40.89  ? 57  TYR F CD1   1 
ATOM   14086 C  CD1   B TYR C 3 57  ? 46.870  -15.241 -19.449 0.80 42.52  ? 57  TYR F CD1   1 
ATOM   14087 C  CD2   A TYR C 3 57  ? 44.744  -16.883 -19.887 0.20 43.47  ? 57  TYR F CD2   1 
ATOM   14088 C  CD2   B TYR C 3 57  ? 44.809  -16.426 -19.632 0.80 45.33  ? 57  TYR F CD2   1 
ATOM   14089 C  CE1   A TYR C 3 57  ? 45.965  -14.424 -19.616 0.20 39.42  ? 57  TYR F CE1   1 
ATOM   14090 C  CE1   B TYR C 3 57  ? 46.188  -14.040 -19.444 0.80 37.35  ? 57  TYR F CE1   1 
ATOM   14091 C  CE2   A TYR C 3 57  ? 43.984  -15.729 -19.929 0.20 41.21  ? 57  TYR F CE2   1 
ATOM   14092 C  CE2   B TYR C 3 57  ? 44.113  -15.224 -19.624 0.80 38.56  ? 57  TYR F CE2   1 
ATOM   14093 C  CZ    A TYR C 3 57  ? 44.600  -14.502 -19.792 0.20 44.74  ? 57  TYR F CZ    1 
ATOM   14094 C  CZ    B TYR C 3 57  ? 44.810  -14.034 -19.532 0.80 49.06  ? 57  TYR F CZ    1 
ATOM   14095 O  OH    A TYR C 3 57  ? 43.849  -13.349 -19.833 0.20 46.73  ? 57  TYR F OH    1 
ATOM   14096 O  OH    B TYR C 3 57  ? 44.138  -12.825 -19.528 0.80 48.72  ? 57  TYR F OH    1 
ATOM   14097 N  N     A GLY C 3 58  ? 48.802  -20.394 -17.610 0.20 32.77  ? 58  GLY F N     1 
ATOM   14098 N  N     B GLY C 3 58  ? 48.972  -20.090 -17.667 0.80 32.62  ? 58  GLY F N     1 
ATOM   14099 C  CA    A GLY C 3 58  ? 49.157  -21.795 -17.453 0.20 32.49  ? 58  GLY F CA    1 
ATOM   14100 C  CA    B GLY C 3 58  ? 49.278  -21.487 -17.422 0.80 31.93  ? 58  GLY F CA    1 
ATOM   14101 C  C     A GLY C 3 58  ? 49.612  -22.495 -18.715 0.20 37.04  ? 58  GLY F C     1 
ATOM   14102 C  C     B GLY C 3 58  ? 49.810  -22.278 -18.595 0.80 38.58  ? 58  GLY F C     1 
ATOM   14103 O  O     A GLY C 3 58  ? 49.275  -23.668 -18.923 0.20 36.55  ? 58  GLY F O     1 
ATOM   14104 O  O     B GLY C 3 58  ? 49.659  -23.503 -18.622 0.80 37.34  ? 58  GLY F O     1 
ATOM   14105 N  N     A HIS C 3 59  ? 50.374  -21.811 -19.564 0.20 33.28  ? 59  HIS F N     1 
ATOM   14106 N  N     B HIS C 3 59  ? 50.447  -21.623 -19.563 0.80 32.56  ? 59  HIS F N     1 
ATOM   14107 C  CA    A HIS C 3 59  ? 50.910  -22.407 -20.787 0.20 34.31  ? 59  HIS F CA    1 
ATOM   14108 C  CA    B HIS C 3 59  ? 50.951  -22.322 -20.747 0.80 34.37  ? 59  HIS F CA    1 
ATOM   14109 C  C     A HIS C 3 59  ? 52.373  -22.748 -20.525 0.20 35.62  ? 59  HIS F C     1 
ATOM   14110 C  C     B HIS C 3 59  ? 52.408  -22.695 -20.516 0.80 35.90  ? 59  HIS F C     1 
ATOM   14111 O  O     A HIS C 3 59  ? 53.275  -21.951 -20.786 0.20 33.14  ? 59  HIS F O     1 
ATOM   14112 O  O     B HIS C 3 59  ? 53.327  -21.959 -20.883 0.80 32.93  ? 59  HIS F O     1 
ATOM   14113 C  CB    A HIS C 3 59  ? 50.736  -21.464 -21.971 0.20 33.79  ? 59  HIS F CB    1 
ATOM   14114 C  CB    B HIS C 3 59  ? 50.764  -21.463 -21.986 0.80 33.62  ? 59  HIS F CB    1 
ATOM   14115 C  CG    A HIS C 3 59  ? 49.315  -21.058 -22.209 0.20 35.46  ? 59  HIS F CG    1 
ATOM   14116 C  CG    B HIS C 3 59  ? 49.350  -21.022 -22.191 0.80 35.62  ? 59  HIS F CG    1 
ATOM   14117 N  ND1   A HIS C 3 59  ? 48.295  -21.974 -22.357 0.20 34.76  ? 59  HIS F ND1   1 
ATOM   14118 N  ND1   B HIS C 3 59  ? 48.298  -21.912 -22.262 0.80 35.16  ? 59  HIS F ND1   1 
ATOM   14119 C  CD2   A HIS C 3 59  ? 48.743  -19.836 -22.319 0.20 34.20  ? 59  HIS F CD2   1 
ATOM   14120 C  CD2   B HIS C 3 59  ? 48.810  -19.788 -22.330 0.80 34.02  ? 59  HIS F CD2   1 
ATOM   14121 C  CE1   A HIS C 3 59  ? 47.156  -21.333 -22.550 0.20 37.77  ? 59  HIS F CE1   1 
ATOM   14122 C  CE1   B HIS C 3 59  ? 47.172  -21.243 -22.441 0.80 37.83  ? 59  HIS F CE1   1 
ATOM   14123 N  NE2   A HIS C 3 59  ? 47.400  -20.035 -22.532 0.20 38.91  ? 59  HIS F NE2   1 
ATOM   14124 N  NE2   B HIS C 3 59  ? 47.456  -19.954 -22.487 0.80 38.96  ? 59  HIS F NE2   1 
ATOM   14125 N  N     A LEU C 3 60  ? 52.602  -23.960 -20.012 0.20 28.99  ? 60  LEU F N     1 
ATOM   14126 N  N     B LEU C 3 60  ? 52.615  -23.882 -19.935 0.80 28.47  ? 60  LEU F N     1 
ATOM   14127 C  CA    A LEU C 3 60  ? 53.935  -24.350 -19.563 0.20 31.55  ? 60  LEU F CA    1 
ATOM   14128 C  CA    B LEU C 3 60  ? 53.953  -24.302 -19.529 0.80 31.21  ? 60  LEU F CA    1 
ATOM   14129 C  C     A LEU C 3 60  ? 54.922  -24.418 -20.724 0.20 36.07  ? 60  LEU F C     1 
ATOM   14130 C  C     B LEU C 3 60  ? 54.899  -24.409 -20.721 0.80 35.95  ? 60  LEU F C     1 
ATOM   14131 O  O     A LEU C 3 60  ? 56.036  -23.888 -20.635 0.20 33.64  ? 60  LEU F O     1 
ATOM   14132 O  O     B LEU C 3 60  ? 56.051  -23.964 -20.651 0.80 33.33  ? 60  LEU F O     1 
ATOM   14133 C  CB    A LEU C 3 60  ? 53.868  -25.696 -18.841 0.20 37.54  ? 60  LEU F CB    1 
ATOM   14134 C  CB    B LEU C 3 60  ? 53.878  -25.642 -18.797 0.80 37.51  ? 60  LEU F CB    1 
ATOM   14135 C  CG    A LEU C 3 60  ? 55.208  -26.299 -18.415 0.20 36.34  ? 60  LEU F CG    1 
ATOM   14136 C  CG    B LEU C 3 60  ? 55.212  -26.362 -18.587 0.80 36.18  ? 60  LEU F CG    1 
ATOM   14137 C  CD1   A LEU C 3 60  ? 55.882  -25.430 -17.363 0.20 38.68  ? 60  LEU F CD1   1 
ATOM   14138 C  CD1   B LEU C 3 60  ? 56.149  -25.539 -17.714 0.80 40.89  ? 60  LEU F CD1   1 
ATOM   14139 C  CD2   A LEU C 3 60  ? 55.029  -27.720 -17.907 0.20 32.20  ? 60  LEU F CD2   1 
ATOM   14140 C  CD2   B LEU C 3 60  ? 55.014  -27.748 -17.999 0.80 31.95  ? 60  LEU F CD2   1 
ATOM   14141 N  N     A GLU C 3 61  ? 54.536  -25.076 -21.819 0.20 37.97  ? 61  GLU F N     1 
ATOM   14142 N  N     B GLU C 3 61  ? 54.439  -25.005 -21.818 0.80 38.07  ? 61  GLU F N     1 
ATOM   14143 C  CA    A GLU C 3 61  ? 55.470  -25.265 -22.925 0.20 37.21  ? 61  GLU F CA    1 
ATOM   14144 C  CA    B GLU C 3 61  ? 55.338  -25.194 -22.950 0.80 37.08  ? 61  GLU F CA    1 
ATOM   14145 C  C     A GLU C 3 61  ? 55.858  -23.940 -23.569 0.20 35.69  ? 61  GLU F C     1 
ATOM   14146 C  C     B GLU C 3 61  ? 55.723  -23.861 -23.584 0.80 35.49  ? 61  GLU F C     1 
ATOM   14147 O  O     A GLU C 3 61  ? 56.961  -23.816 -24.114 0.20 38.64  ? 61  GLU F O     1 
ATOM   14148 O  O     B GLU C 3 61  ? 56.829  -23.728 -24.121 0.80 39.28  ? 61  GLU F O     1 
ATOM   14149 C  CB    A GLU C 3 61  ? 54.874  -26.216 -23.968 0.20 42.06  ? 61  GLU F CB    1 
ATOM   14150 C  CB    B GLU C 3 61  ? 54.701  -26.136 -23.982 0.80 41.81  ? 61  GLU F CB    1 
ATOM   14151 C  CG    A GLU C 3 61  ? 54.630  -27.640 -23.471 0.20 46.09  ? 61  GLU F CG    1 
ATOM   14152 C  CG    B GLU C 3 61  ? 54.395  -27.559 -23.479 0.80 46.16  ? 61  GLU F CG    1 
ATOM   14153 C  CD    A GLU C 3 61  ? 53.378  -27.772 -22.616 0.20 51.75  ? 61  GLU F CD    1 
ATOM   14154 C  CD    B GLU C 3 61  ? 53.174  -27.658 -22.550 0.80 52.69  ? 61  GLU F CD    1 
ATOM   14155 O  OE1   A GLU C 3 61  ? 52.521  -26.862 -22.657 0.20 46.87  ? 61  GLU F OE1   1 
ATOM   14156 O  OE1   B GLU C 3 61  ? 52.301  -26.757 -22.562 0.80 46.43  ? 61  GLU F OE1   1 
ATOM   14157 O  OE2   A GLU C 3 61  ? 53.253  -28.788 -21.900 0.20 58.78  ? 61  GLU F OE2   1 
ATOM   14158 O  OE2   B GLU C 3 61  ? 53.090  -28.657 -21.800 0.80 59.82  ? 61  GLU F OE2   1 
ATOM   14159 N  N     A ILE C 3 62  ? 54.977  -22.940 -23.516 0.20 32.74  ? 62  ILE F N     1 
ATOM   14160 N  N     B ILE C 3 62  ? 54.841  -22.862 -23.532 0.80 32.11  ? 62  ILE F N     1 
ATOM   14161 C  CA    A ILE C 3 62  ? 55.326  -21.627 -24.050 0.20 34.65  ? 62  ILE F CA    1 
ATOM   14162 C  CA    B ILE C 3 62  ? 55.184  -21.567 -24.111 0.80 34.67  ? 62  ILE F CA    1 
ATOM   14163 C  C     A ILE C 3 62  ? 56.361  -20.950 -23.159 0.20 35.78  ? 62  ILE F C     1 
ATOM   14164 C  C     B ILE C 3 62  ? 56.206  -20.848 -23.237 0.80 37.12  ? 62  ILE F C     1 
ATOM   14165 O  O     A ILE C 3 62  ? 57.298  -20.308 -23.650 0.20 31.40  ? 62  ILE F O     1 
ATOM   14166 O  O     B ILE C 3 62  ? 57.161  -20.245 -23.746 0.80 31.00  ? 62  ILE F O     1 
ATOM   14167 C  CB    A ILE C 3 62  ? 54.062  -20.766 -24.219 0.20 33.36  ? 62  ILE F CB    1 
ATOM   14168 C  CB    B ILE C 3 62  ? 53.914  -20.730 -24.335 0.80 33.26  ? 62  ILE F CB    1 
ATOM   14169 C  CG1   A ILE C 3 62  ? 53.171  -21.342 -25.323 0.20 37.89  ? 62  ILE F CG1   1 
ATOM   14170 C  CG1   B ILE C 3 62  ? 53.186  -21.206 -25.600 0.80 37.60  ? 62  ILE F CG1   1 
ATOM   14171 C  CG2   A ILE C 3 62  ? 54.428  -19.327 -24.538 0.20 32.53  ? 62  ILE F CG2   1 
ATOM   14172 C  CG2   B ILE C 3 62  ? 54.254  -19.259 -24.455 0.80 32.15  ? 62  ILE F CG2   1 
ATOM   14173 C  CD1   A ILE C 3 62  ? 51.905  -20.541 -25.575 0.20 37.33  ? 62  ILE F CD1   1 
ATOM   14174 C  CD1   B ILE C 3 62  ? 51.903  -20.421 -25.914 0.80 37.31  ? 62  ILE F CD1   1 
ATOM   14175 N  N     A VAL C 3 63  ? 56.218  -21.093 -21.839 0.20 31.32  ? 63  VAL F N     1 
ATOM   14176 N  N     B VAL C 3 63  ? 56.022  -20.905 -21.913 0.80 29.66  ? 63  VAL F N     1 
ATOM   14177 C  CA    A VAL C 3 63  ? 57.198  -20.533 -20.912 0.20 29.66  ? 63  VAL F CA    1 
ATOM   14178 C  CA    B VAL C 3 63  ? 57.042  -20.440 -20.970 0.80 29.11  ? 63  VAL F CA    1 
ATOM   14179 C  C     A VAL C 3 63  ? 58.569  -21.161 -21.136 0.20 28.99  ? 63  VAL F C     1 
ATOM   14180 C  C     B VAL C 3 63  ? 58.414  -21.003 -21.329 0.80 27.23  ? 63  VAL F C     1 
ATOM   14181 O  O     A VAL C 3 63  ? 59.601  -20.487 -21.036 0.20 30.40  ? 63  VAL F O     1 
ATOM   14182 O  O     B VAL C 3 63  ? 59.406  -20.271 -21.391 0.80 30.52  ? 63  VAL F O     1 
ATOM   14183 C  CB    A VAL C 3 63  ? 56.720  -20.718 -19.458 0.20 32.25  ? 63  VAL F CB    1 
ATOM   14184 C  CB    B VAL C 3 63  ? 56.644  -20.816 -19.529 0.80 32.40  ? 63  VAL F CB    1 
ATOM   14185 C  CG1   A VAL C 3 63  ? 57.746  -20.174 -18.476 0.20 31.46  ? 63  VAL F CG1   1 
ATOM   14186 C  CG1   B VAL C 3 63  ? 57.836  -20.743 -18.591 0.80 32.35  ? 63  VAL F CG1   1 
ATOM   14187 C  CG2   A VAL C 3 63  ? 55.376  -20.036 -19.253 0.20 32.91  ? 63  VAL F CG2   1 
ATOM   14188 C  CG2   B VAL C 3 63  ? 55.537  -19.903 -19.034 0.80 33.91  ? 63  VAL F CG2   1 
ATOM   14189 N  N     A GLU C 3 64  ? 58.603  -22.459 -21.449 0.20 29.48  ? 64  GLU F N     1 
ATOM   14190 N  N     B GLU C 3 64  ? 58.495  -22.316 -21.555 0.80 28.47  ? 64  GLU F N     1 
ATOM   14191 C  CA    A GLU C 3 64  ? 59.882  -23.142 -21.615 0.20 32.14  ? 64  GLU F CA    1 
ATOM   14192 C  CA    B GLU C 3 64  ? 59.798  -22.942 -21.749 0.80 31.69  ? 64  GLU F CA    1 
ATOM   14193 C  C     A GLU C 3 64  ? 60.586  -22.706 -22.894 0.20 33.23  ? 64  GLU F C     1 
ATOM   14194 C  C     B GLU C 3 64  ? 60.414  -22.540 -23.083 0.80 33.47  ? 64  GLU F C     1 
ATOM   14195 O  O     A GLU C 3 64  ? 61.817  -22.586 -22.921 0.20 32.09  ? 64  GLU F O     1 
ATOM   14196 O  O     B GLU C 3 64  ? 61.635  -22.364 -23.179 0.80 31.73  ? 64  GLU F O     1 
ATOM   14197 C  CB    A GLU C 3 64  ? 59.676  -24.657 -21.602 0.20 33.32  ? 64  GLU F CB    1 
ATOM   14198 C  CB    B GLU C 3 64  ? 59.679  -24.465 -21.631 0.80 32.56  ? 64  GLU F CB    1 
ATOM   14199 C  CG    A GLU C 3 64  ? 59.214  -25.212 -20.258 0.20 39.38  ? 64  GLU F CG    1 
ATOM   14200 C  CG    B GLU C 3 64  ? 59.285  -24.935 -20.219 0.80 40.55  ? 64  GLU F CG    1 
ATOM   14201 C  CD    A GLU C 3 64  ? 58.988  -26.715 -20.283 0.20 43.22  ? 64  GLU F CD    1 
ATOM   14202 C  CD    B GLU C 3 64  ? 59.211  -26.453 -20.048 0.80 43.33  ? 64  GLU F CD    1 
ATOM   14203 O  OE1   A GLU C 3 64  ? 58.924  -27.292 -21.390 0.20 47.00  ? 64  GLU F OE1   1 
ATOM   14204 O  OE1   B GLU C 3 64  ? 58.554  -27.135 -20.868 0.80 48.83  ? 64  GLU F OE1   1 
ATOM   14205 O  OE2   A GLU C 3 64  ? 58.877  -27.319 -19.194 0.20 40.80  ? 64  GLU F OE2   1 
ATOM   14206 O  OE2   B GLU C 3 64  ? 59.806  -26.965 -19.074 0.80 50.11  ? 64  GLU F OE2   1 
ATOM   14207 N  N     A VAL C 3 65  ? 59.828  -22.466 -23.964 0.20 32.53  ? 65  VAL F N     1 
ATOM   14208 N  N     B VAL C 3 65  ? 59.596  -22.377 -24.123 0.80 32.25  ? 65  VAL F N     1 
ATOM   14209 C  CA    A VAL C 3 65  ? 60.457  -22.058 -25.216 0.20 32.46  ? 65  VAL F CA    1 
ATOM   14210 C  CA    B VAL C 3 65  ? 60.154  -21.972 -25.410 0.80 32.61  ? 65  VAL F CA    1 
ATOM   14211 C  C     A VAL C 3 65  ? 60.869  -20.591 -25.167 0.20 32.41  ? 65  VAL F C     1 
ATOM   14212 C  C     B VAL C 3 65  ? 60.585  -20.515 -25.365 0.80 33.38  ? 65  VAL F C     1 
ATOM   14213 O  O     A VAL C 3 65  ? 61.897  -20.214 -25.743 0.20 29.87  ? 65  VAL F O     1 
ATOM   14214 O  O     B VAL C 3 65  ? 61.620  -20.143 -25.932 0.80 29.04  ? 65  VAL F O     1 
ATOM   14215 C  CB    A VAL C 3 65  ? 59.521  -22.344 -26.404 0.20 38.50  ? 65  VAL F CB    1 
ATOM   14216 C  CB    B VAL C 3 65  ? 59.157  -22.226 -26.555 0.80 39.04  ? 65  VAL F CB    1 
ATOM   14217 C  CG1   A VAL C 3 65  ? 60.187  -21.953 -27.717 0.20 40.25  ? 65  VAL F CG1   1 
ATOM   14218 C  CG1   B VAL C 3 65  ? 59.826  -21.912 -27.892 0.80 42.42  ? 65  VAL F CG1   1 
ATOM   14219 C  CG2   A VAL C 3 65  ? 59.136  -23.814 -26.429 0.20 40.28  ? 65  VAL F CG2   1 
ATOM   14220 C  CG2   B VAL C 3 65  ? 58.692  -23.667 -26.543 0.80 41.99  ? 65  VAL F CG2   1 
ATOM   14221 N  N     A LEU C 3 66  ? 60.098  -19.747 -24.475 0.20 31.72  ? 66  LEU F N     1 
ATOM   14222 N  N     B LEU C 3 66  ? 59.802  -19.663 -24.694 0.80 31.61  ? 66  LEU F N     1 
ATOM   14223 C  CA    A LEU C 3 66  ? 60.445  -18.331 -24.395 0.20 28.66  ? 66  LEU F CA    1 
ATOM   14224 C  CA    B LEU C 3 66  ? 60.213  -18.274 -24.539 0.80 28.82  ? 66  LEU F CA    1 
ATOM   14225 C  C     A LEU C 3 66  ? 61.769  -18.125 -23.670 0.20 32.23  ? 66  LEU F C     1 
ATOM   14226 C  C     B LEU C 3 66  ? 61.532  -18.178 -23.788 0.80 32.40  ? 66  LEU F C     1 
ATOM   14227 O  O     A LEU C 3 66  ? 62.609  -17.333 -24.113 0.20 31.42  ? 66  LEU F O     1 
ATOM   14228 O  O     B LEU C 3 66  ? 62.391  -17.353 -24.129 0.80 32.52  ? 66  LEU F O     1 
ATOM   14229 C  CB    A LEU C 3 66  ? 59.326  -17.550 -23.703 0.20 31.30  ? 66  LEU F CB    1 
ATOM   14230 C  CB    B LEU C 3 66  ? 59.121  -17.468 -23.827 0.80 30.89  ? 66  LEU F CB    1 
ATOM   14231 C  CG    A LEU C 3 66  ? 58.044  -17.295 -24.498 0.20 30.16  ? 66  LEU F CG    1 
ATOM   14232 C  CG    B LEU C 3 66  ? 57.790  -17.258 -24.543 0.80 30.21  ? 66  LEU F CG    1 
ATOM   14233 C  CD1   A LEU C 3 66  ? 57.010  -16.592 -23.627 0.20 29.51  ? 66  LEU F CD1   1 
ATOM   14234 C  CD1   B LEU C 3 66  ? 56.774  -16.656 -23.569 0.80 28.97  ? 66  LEU F CD1   1 
ATOM   14235 C  CD2   A LEU C 3 66  ? 58.335  -16.485 -25.750 0.20 33.49  ? 66  LEU F CD2   1 
ATOM   14236 C  CD2   B LEU C 3 66  ? 57.939  -16.381 -25.776 0.80 33.71  ? 66  LEU F CD2   1 
ATOM   14237 N  N     A LEU C 3 67  ? 61.978  -18.836 -22.559 0.20 28.63  ? 67  LEU F N     1 
ATOM   14238 N  N     B LEU C 3 67  ? 61.738  -19.033 -22.784 0.80 26.13  ? 67  LEU F N     1 
ATOM   14239 C  CA    A LEU C 3 67  ? 63.207  -18.660 -21.792 0.20 27.34  ? 67  LEU F CA    1 
ATOM   14240 C  CA    B LEU C 3 67  ? 62.967  -18.936 -22.002 0.80 26.36  ? 67  LEU F CA    1 
ATOM   14241 C  C     A LEU C 3 67  ? 64.430  -19.062 -22.608 0.20 29.96  ? 67  LEU F C     1 
ATOM   14242 C  C     B LEU C 3 67  ? 64.184  -19.487 -22.741 0.80 28.61  ? 67  LEU F C     1 
ATOM   14243 O  O     A LEU C 3 67  ? 65.464  -18.386 -22.564 0.20 29.78  ? 67  LEU F O     1 
ATOM   14244 O  O     B LEU C 3 67  ? 65.310  -19.219 -22.323 0.80 30.97  ? 67  LEU F O     1 
ATOM   14245 C  CB    A LEU C 3 67  ? 63.131  -19.465 -20.495 0.20 31.85  ? 67  LEU F CB    1 
ATOM   14246 C  CB    B LEU C 3 67  ? 62.813  -19.665 -20.667 0.80 31.28  ? 67  LEU F CB    1 
ATOM   14247 C  CG    A LEU C 3 67  ? 62.057  -18.999 -19.509 0.20 34.02  ? 67  LEU F CG    1 
ATOM   14248 C  CG    B LEU C 3 67  ? 61.903  -18.975 -19.649 0.80 34.50  ? 67  LEU F CG    1 
ATOM   14249 C  CD1   A LEU C 3 67  ? 61.899  -19.988 -18.365 0.20 35.65  ? 67  LEU F CD1   1 
ATOM   14250 C  CD1   B LEU C 3 67  ? 61.777  -19.817 -18.378 0.80 36.12  ? 67  LEU F CD1   1 
ATOM   14251 C  CD2   A LEU C 3 67  ? 62.379  -17.610 -18.978 0.20 31.58  ? 67  LEU F CD2   1 
ATOM   14252 C  CD2   B LEU C 3 67  ? 62.414  -17.584 -19.320 0.80 32.68  ? 67  LEU F CD2   1 
ATOM   14253 N  N     A LYS C 3 68  ? 64.326  -20.148 -23.372 0.20 26.67  ? 68  LYS F N     1 
ATOM   14254 N  N     B LYS C 3 68  ? 63.980  -20.262 -23.797 0.80 27.29  ? 68  LYS F N     1 
ATOM   14255 C  CA    A LYS C 3 68  ? 65.416  -20.577 -24.243 0.20 29.56  ? 68  LYS F CA    1 
ATOM   14256 C  CA    B LYS C 3 68  ? 65.063  -20.694 -24.679 0.80 25.94  ? 68  LYS F CA    1 
ATOM   14257 C  C     A LYS C 3 68  ? 65.669  -19.618 -25.399 0.20 30.80  ? 68  LYS F C     1 
ATOM   14258 C  C     B LYS C 3 68  ? 65.338  -19.688 -25.791 0.80 32.93  ? 68  LYS F C     1 
ATOM   14259 O  O     A LYS C 3 68  ? 66.615  -19.839 -26.165 0.20 29.67  ? 68  LYS F O     1 
ATOM   14260 O  O     B LYS C 3 68  ? 66.219  -19.927 -26.633 0.80 31.15  ? 68  LYS F O     1 
ATOM   14261 C  CB    A LYS C 3 68  ? 65.128  -21.980 -24.779 0.20 31.01  ? 68  LYS F CB    1 
ATOM   14262 C  CB    B LYS C 3 68  ? 64.729  -22.061 -25.282 0.80 32.05  ? 68  LYS F CB    1 
ATOM   14263 C  CG    A LYS C 3 68  ? 64.947  -23.029 -23.691 0.20 33.38  ? 68  LYS F CG    1 
ATOM   14264 C  CG    B LYS C 3 68  ? 64.706  -23.210 -24.273 0.80 35.13  ? 68  LYS F CG    1 
ATOM   14265 C  CD    A LYS C 3 68  ? 64.623  -24.391 -24.282 0.20 44.97  ? 68  LYS F CD    1 
ATOM   14266 C  CD    B LYS C 3 68  ? 64.442  -24.541 -24.983 0.80 49.98  ? 68  LYS F CD    1 
ATOM   14267 C  CE    A LYS C 3 68  ? 64.358  -25.417 -23.191 0.20 50.79  ? 68  LYS F CE    1 
ATOM   14268 C  CE    B LYS C 3 68  ? 64.413  -25.716 -24.007 0.80 56.22  ? 68  LYS F CE    1 
ATOM   14269 N  NZ    A LYS C 3 68  ? 63.992  -26.748 -23.752 0.20 54.38  ? 68  LYS F NZ    1 
ATOM   14270 N  NZ    B LYS C 3 68  ? 63.795  -26.937 -24.610 0.80 54.99  ? 68  LYS F NZ    1 
ATOM   14271 N  N     A HIS C 3 69  ? 64.864  -18.566 -25.545 0.20 30.02  ? 69  HIS F N     1 
ATOM   14272 N  N     B HIS C 3 69  ? 64.619  -18.566 -25.803 0.80 29.40  ? 69  HIS F N     1 
ATOM   14273 C  CA    A HIS C 3 69  ? 65.036  -17.566 -26.590 0.20 30.85  ? 69  HIS F CA    1 
ATOM   14274 C  CA    B HIS C 3 69  ? 64.723  -17.583 -26.874 0.80 30.87  ? 69  HIS F CA    1 
ATOM   14275 C  C     A HIS C 3 69  ? 65.208  -16.170 -25.997 0.20 27.53  ? 69  HIS F C     1 
ATOM   14276 C  C     B HIS C 3 69  ? 64.788  -16.167 -26.325 0.80 28.05  ? 69  HIS F C     1 
ATOM   14277 O  O     A HIS C 3 69  ? 64.646  -15.189 -26.486 0.20 27.41  ? 69  HIS F O     1 
ATOM   14278 O  O     B HIS C 3 69  ? 64.199  -15.242 -26.888 0.80 30.84  ? 69  HIS F O     1 
ATOM   14279 C  CB    A HIS C 3 69  ? 63.868  -17.602 -27.572 0.20 30.50  ? 69  HIS F CB    1 
ATOM   14280 C  CB    B HIS C 3 69  ? 63.563  -17.722 -27.849 0.80 30.98  ? 69  HIS F CB    1 
ATOM   14281 C  CG    A HIS C 3 69  ? 63.833  -18.838 -28.416 0.20 35.94  ? 69  HIS F CG    1 
ATOM   14282 C  CG    B HIS C 3 69  ? 63.692  -18.903 -28.755 0.80 38.73  ? 69  HIS F CG    1 
ATOM   14283 N  ND1   A HIS C 3 69  ? 63.483  -20.073 -27.913 0.20 32.86  ? 69  HIS F ND1   1 
ATOM   14284 N  ND1   B HIS C 3 69  ? 62.972  -20.063 -28.573 0.80 36.06  ? 69  HIS F ND1   1 
ATOM   14285 C  CD2   A HIS C 3 69  ? 64.118  -19.031 -29.726 0.20 35.71  ? 69  HIS F CD2   1 
ATOM   14286 C  CD2   B HIS C 3 69  ? 64.477  -19.110 -29.840 0.80 36.14  ? 69  HIS F CD2   1 
ATOM   14287 C  CE1   A HIS C 3 69  ? 63.547  -20.973 -28.879 0.20 37.07  ? 69  HIS F CE1   1 
ATOM   14288 C  CE1   B HIS C 3 69  ? 63.296  -20.929 -29.518 0.80 39.52  ? 69  HIS F CE1   1 
ATOM   14289 N  NE2   A HIS C 3 69  ? 63.929  -20.366 -29.989 0.20 34.61  ? 69  HIS F NE2   1 
ATOM   14290 N  NE2   B HIS C 3 69  ? 64.210  -20.377 -30.297 0.80 32.33  ? 69  HIS F NE2   1 
ATOM   14291 N  N     A GLY C 3 70  ? 65.997  -16.067 -24.931 0.20 26.65  ? 70  GLY F N     1 
ATOM   14292 N  N     B GLY C 3 70  ? 65.512  -15.970 -25.234 0.80 24.20  ? 70  GLY F N     1 
ATOM   14293 C  CA    A GLY C 3 70  ? 66.388  -14.774 -24.405 0.20 24.42  ? 70  GLY F CA    1 
ATOM   14294 C  CA    B GLY C 3 70  ? 65.869  -14.633 -24.801 0.80 23.47  ? 70  GLY F CA    1 
ATOM   14295 C  C     A GLY C 3 70  ? 65.333  -14.005 -23.643 0.20 27.44  ? 70  GLY F C     1 
ATOM   14296 C  C     B GLY C 3 70  ? 64.855  -13.887 -23.956 0.80 28.12  ? 70  GLY F C     1 
ATOM   14297 O  O     A GLY C 3 70  ? 65.564  -12.834 -23.322 0.20 25.25  ? 70  GLY F O     1 
ATOM   14298 O  O     B GLY C 3 70  ? 65.036  -12.682 -23.732 0.80 26.70  ? 70  GLY F O     1 
ATOM   14299 N  N     A ALA C 3 71  ? 64.184  -14.610 -23.344 0.20 26.80  ? 71  ALA F N     1 
ATOM   14300 N  N     B ALA C 3 71  ? 63.799  -14.546 -23.483 0.80 25.26  ? 71  ALA F N     1 
ATOM   14301 C  CA    A ALA C 3 71  ? 63.177  -13.918 -22.548 0.20 26.31  ? 71  ALA F CA    1 
ATOM   14302 C  CA    B ALA C 3 71  ? 62.916  -13.898 -22.518 0.80 25.94  ? 71  ALA F CA    1 
ATOM   14303 C  C     A ALA C 3 71  ? 63.740  -13.549 -21.182 0.20 25.73  ? 71  ALA F C     1 
ATOM   14304 C  C     B ALA C 3 71  ? 63.675  -13.541 -21.244 0.80 25.58  ? 71  ALA F C     1 
ATOM   14305 O  O     A ALA C 3 71  ? 64.456  -14.333 -20.552 0.20 25.91  ? 71  ALA F O     1 
ATOM   14306 O  O     B ALA C 3 71  ? 64.478  -14.333 -20.733 0.80 25.51  ? 71  ALA F O     1 
ATOM   14307 C  CB    A ALA C 3 71  ? 61.929  -14.785 -22.381 0.20 27.21  ? 71  ALA F CB    1 
ATOM   14308 C  CB    B ALA C 3 71  ? 61.729  -14.801 -22.182 0.80 26.65  ? 71  ALA F CB    1 
ATOM   14309 N  N     A ASP C 3 72  ? 63.420  -12.337 -20.730 0.20 27.42  ? 72  ASP F N     1 
ATOM   14310 N  N     B ASP C 3 72  ? 63.413  -12.331 -20.733 0.80 27.41  ? 72  ASP F N     1 
ATOM   14311 C  CA    A ASP C 3 72  ? 63.862  -11.853 -19.426 0.20 28.25  ? 72  ASP F CA    1 
ATOM   14312 C  CA    B ASP C 3 72  ? 63.919  -11.879 -19.436 0.80 28.41  ? 72  ASP F CA    1 
ATOM   14313 C  C     A ASP C 3 72  ? 62.989  -12.489 -18.353 0.20 26.97  ? 72  ASP F C     1 
ATOM   14314 C  C     B ASP C 3 72  ? 63.010  -12.467 -18.372 0.80 26.94  ? 72  ASP F C     1 
ATOM   14315 O  O     A ASP C 3 72  ? 61.784  -12.232 -18.291 0.20 26.71  ? 72  ASP F O     1 
ATOM   14316 O  O     B ASP C 3 72  ? 61.883  -12.013 -18.189 0.80 26.44  ? 72  ASP F O     1 
ATOM   14317 C  CB    A ASP C 3 72  ? 63.787  -10.331 -19.367 0.20 24.39  ? 72  ASP F CB    1 
ATOM   14318 C  CB    B ASP C 3 72  ? 63.935  -10.359 -19.357 0.80 23.98  ? 72  ASP F CB    1 
ATOM   14319 C  CG    A ASP C 3 72  ? 64.410  -9.761  -18.105 0.20 28.77  ? 72  ASP F CG    1 
ATOM   14320 C  CG    B ASP C 3 72  ? 64.640  -9.830  -18.108 0.80 28.59  ? 72  ASP F CG    1 
ATOM   14321 O  OD1   A ASP C 3 72  ? 64.993  -10.532 -17.312 0.20 29.48  ? 72  ASP F OD1   1 
ATOM   14322 O  OD1   B ASP C 3 72  ? 64.944  -10.607 -17.171 0.80 29.20  ? 72  ASP F OD1   1 
ATOM   14323 O  OD2   A ASP C 3 72  ? 64.318  -8.532  -17.911 0.20 32.80  ? 72  ASP F OD2   1 
ATOM   14324 O  OD2   B ASP C 3 72  ? 64.910  -8.612  -18.088 0.80 34.38  ? 72  ASP F OD2   1 
ATOM   14325 N  N     A VAL C 3 73  ? 63.597  -13.324 -17.508 0.20 26.27  ? 73  VAL F N     1 
ATOM   14326 N  N     B VAL C 3 73  ? 63.495  -13.497 -17.680 0.80 25.72  ? 73  VAL F N     1 
ATOM   14327 C  CA    A VAL C 3 73  ? 62.836  -14.024 -16.481 0.20 27.76  ? 73  VAL F CA    1 
ATOM   14328 C  CA    B VAL C 3 73  ? 62.684  -14.205 -16.699 0.80 27.61  ? 73  VAL F CA    1 
ATOM   14329 C  C     A VAL C 3 73  ? 62.406  -13.086 -15.359 0.20 29.01  ? 73  VAL F C     1 
ATOM   14330 C  C     B VAL C 3 73  ? 62.302  -13.320 -15.517 0.80 30.04  ? 73  VAL F C     1 
ATOM   14331 O  O     A VAL C 3 73  ? 61.482  -13.411 -14.601 0.20 28.57  ? 73  VAL F O     1 
ATOM   14332 O  O     B VAL C 3 73  ? 61.379  -13.660 -14.756 0.80 28.24  ? 73  VAL F O     1 
ATOM   14333 C  CB    A VAL C 3 73  ? 63.662  -15.206 -15.936 0.20 28.96  ? 73  VAL F CB    1 
ATOM   14334 C  CB    B VAL C 3 73  ? 63.462  -15.470 -16.266 0.80 27.48  ? 73  VAL F CB    1 
ATOM   14335 C  CG1   A VAL C 3 73  ? 64.722  -14.714 -14.958 0.20 26.65  ? 73  VAL F CG1   1 
ATOM   14336 C  CG1   B VAL C 3 73  ? 64.758  -15.087 -15.562 0.80 29.12  ? 73  VAL F CG1   1 
ATOM   14337 C  CG2   A VAL C 3 73  ? 62.757  -16.252 -15.293 0.20 28.12  ? 73  VAL F CG2   1 
ATOM   14338 C  CG2   B VAL C 3 73  ? 62.609  -16.396 -15.398 0.80 27.99  ? 73  VAL F CG2   1 
ATOM   14339 N  N     A ASN C 3 74  ? 63.043  -11.919 -15.239 0.20 27.07  ? 74  ASN F N     1 
ATOM   14340 N  N     B ASN C 3 74  ? 62.969  -12.171 -15.364 0.80 26.08  ? 74  ASN F N     1 
ATOM   14341 C  CA    A ASN C 3 74  ? 62.737  -10.954 -14.190 0.20 30.94  ? 74  ASN F CA    1 
ATOM   14342 C  CA    B ASN C 3 74  ? 62.737  -11.244 -14.262 0.80 32.92  ? 74  ASN F CA    1 
ATOM   14343 C  C     A ASN C 3 74  ? 62.076  -9.692  -14.735 0.20 30.48  ? 74  ASN F C     1 
ATOM   14344 C  C     B ASN C 3 74  ? 62.193  -9.895  -14.724 0.80 31.15  ? 74  ASN F C     1 
ATOM   14345 O  O     A ASN C 3 74  ? 62.145  -8.636  -14.097 0.20 29.30  ? 74  ASN F O     1 
ATOM   14346 O  O     B ASN C 3 74  ? 62.315  -8.903  -13.997 0.80 29.20  ? 74  ASN F O     1 
ATOM   14347 C  CB    A ASN C 3 74  ? 64.006  -10.596 -13.415 0.20 27.48  ? 74  ASN F CB    1 
ATOM   14348 C  CB    B ASN C 3 74  ? 64.024  -11.055 -13.456 0.80 27.71  ? 74  ASN F CB    1 
ATOM   14349 C  CG    A ASN C 3 74  ? 64.652  -11.805 -12.771 0.20 28.08  ? 74  ASN F CG    1 
ATOM   14350 C  CG    B ASN C 3 74  ? 64.294  -12.222 -12.554 0.80 29.29  ? 74  ASN F CG    1 
ATOM   14351 O  OD1   A ASN C 3 74  ? 63.971  -12.764 -12.407 0.20 29.73  ? 74  ASN F OD1   1 
ATOM   14352 O  OD1   B ASN C 3 74  ? 63.381  -12.707 -11.877 0.80 25.99  ? 74  ASN F OD1   1 
ATOM   14353 N  ND2   A ASN C 3 74  ? 65.970  -11.767 -12.625 0.20 27.17  ? 74  ASN F ND2   1 
ATOM   14354 N  ND2   B ASN C 3 74  ? 65.533  -12.708 -12.551 0.80 29.43  ? 74  ASN F ND2   1 
ATOM   14355 N  N     A ALA C 3 75  ? 61.440  -9.779  -15.902 0.20 28.90  ? 75  ALA F N     1 
ATOM   14356 N  N     B ALA C 3 75  ? 61.588  -9.835  -15.909 0.80 28.89  ? 75  ALA F N     1 
ATOM   14357 C  CA    A ALA C 3 75  ? 60.743  -8.630  -16.462 0.20 26.43  ? 75  ALA F CA    1 
ATOM   14358 C  CA    B ALA C 3 75  ? 60.939  -8.606  -16.347 0.80 25.35  ? 75  ALA F CA    1 
ATOM   14359 C  C     A ALA C 3 75  ? 59.621  -8.179  -15.533 0.20 27.60  ? 75  ALA F C     1 
ATOM   14360 C  C     B ALA C 3 75  ? 59.829  -8.206  -15.378 0.80 27.92  ? 75  ALA F C     1 
ATOM   14361 O  O     A ALA C 3 75  ? 58.907  -8.999  -14.952 0.20 26.66  ? 75  ALA F O     1 
ATOM   14362 O  O     B ALA C 3 75  ? 59.152  -9.056  -14.800 0.80 26.52  ? 75  ALA F O     1 
ATOM   14363 C  CB    A ALA C 3 75  ? 60.177  -8.972  -17.840 0.20 25.91  ? 75  ALA F CB    1 
ATOM   14364 C  CB    B ALA C 3 75  ? 60.346  -8.783  -17.745 0.80 25.38  ? 75  ALA F CB    1 
ATOM   14365 N  N     A ILE C 3 76  ? 59.467  -6.865  -15.399 0.20 27.60  ? 76  ILE F N     1 
ATOM   14366 N  N     B ILE C 3 76  ? 59.627  -6.899  -15.221 0.80 27.26  ? 76  ILE F N     1 
ATOM   14367 C  CA    A ILE C 3 76  ? 58.482  -6.272  -14.503 0.20 28.37  ? 76  ILE F CA    1 
ATOM   14368 C  CA    B ILE C 3 76  ? 58.547  -6.376  -14.389 0.80 28.13  ? 76  ILE F CA    1 
ATOM   14369 C  C     A ILE C 3 76  ? 57.544  -5.386  -15.310 0.20 31.93  ? 76  ILE F C     1 
ATOM   14370 C  C     B ILE C 3 76  ? 57.657  -5.468  -15.227 0.80 32.57  ? 76  ILE F C     1 
ATOM   14371 O  O     A ILE C 3 76  ? 57.975  -4.684  -16.231 0.20 29.11  ? 76  ILE F O     1 
ATOM   14372 O  O     B ILE C 3 76  ? 58.141  -4.757  -16.117 0.80 29.01  ? 76  ILE F O     1 
ATOM   14373 C  CB    A ILE C 3 76  ? 59.158  -5.470  -13.371 0.20 30.75  ? 76  ILE F CB    1 
ATOM   14374 C  CB    B ILE C 3 76  ? 59.077  -5.624  -13.151 0.80 31.91  ? 76  ILE F CB    1 
ATOM   14375 C  CG1   A ILE C 3 76  ? 60.249  -4.559  -13.936 0.20 33.68  ? 76  ILE F CG1   1 
ATOM   14376 C  CG1   B ILE C 3 76  ? 59.868  -4.381  -13.546 0.80 37.54  ? 76  ILE F CG1   1 
ATOM   14377 C  CG2   A ILE C 3 76  ? 59.739  -6.413  -12.329 0.20 31.51  ? 76  ILE F CG2   1 
ATOM   14378 C  CG2   B ILE C 3 76  ? 59.935  -6.547  -12.299 0.80 32.06  ? 76  ILE F CG2   1 
ATOM   14379 C  CD1   A ILE C 3 76  ? 60.984  -3.770  -12.879 0.20 31.90  ? 76  ILE F CD1   1 
ATOM   14380 C  CD1   B ILE C 3 76  ? 59.767  -3.269  -12.523 0.80 28.11  ? 76  ILE F CD1   1 
ATOM   14381 N  N     A ASP C 3 77  ? 56.260  -5.424  -14.961 0.20 27.24  ? 77  ASP F N     1 
ATOM   14382 N  N     B ASP C 3 77  ? 56.352  -5.503  -14.945 0.80 27.01  ? 77  ASP F N     1 
ATOM   14383 C  CA    A ASP C 3 77  ? 55.254  -4.595  -15.605 0.20 28.22  ? 77  ASP F CA    1 
ATOM   14384 C  CA    B ASP C 3 77  ? 55.409  -4.569  -15.550 0.80 27.83  ? 77  ASP F CA    1 
ATOM   14385 C  C     A ASP C 3 77  ? 55.190  -3.238  -14.905 0.20 30.79  ? 77  ASP F C     1 
ATOM   14386 C  C     B ASP C 3 77  ? 55.399  -3.275  -14.734 0.80 31.23  ? 77  ASP F C     1 
ATOM   14387 O  O     A ASP C 3 77  ? 56.060  -2.885  -14.102 0.20 30.80  ? 77  ASP F O     1 
ATOM   14388 O  O     B ASP C 3 77  ? 56.235  -3.061  -13.848 0.80 30.21  ? 77  ASP F O     1 
ATOM   14389 C  CB    A ASP C 3 77  ? 53.899  -5.300  -15.594 0.20 31.18  ? 77  ASP F CB    1 
ATOM   14390 C  CB    B ASP C 3 77  ? 54.023  -5.203  -15.673 0.80 31.28  ? 77  ASP F CB    1 
ATOM   14391 C  CG    A ASP C 3 77  ? 53.287  -5.364  -14.205 0.20 29.41  ? 77  ASP F CG    1 
ATOM   14392 C  CG    B ASP C 3 77  ? 53.347  -5.459  -14.312 0.80 29.16  ? 77  ASP F CG    1 
ATOM   14393 O  OD1   A ASP C 3 77  ? 54.048  -5.496  -13.223 0.20 30.60  ? 77  ASP F OD1   1 
ATOM   14394 O  OD1   B ASP C 3 77  ? 53.855  -5.023  -13.251 0.80 31.33  ? 77  ASP F OD1   1 
ATOM   14395 O  OD2   A ASP C 3 77  ? 52.047  -5.271  -14.094 0.20 28.30  ? 77  ASP F OD2   1 
ATOM   14396 O  OD2   B ASP C 3 77  ? 52.280  -6.099  -14.315 0.80 31.19  ? 77  ASP F OD2   1 
ATOM   14397 N  N     A ILE C 3 78  ? 54.145  -2.459  -15.194 0.20 29.01  ? 78  ILE F N     1 
ATOM   14398 N  N     B ILE C 3 78  ? 54.437  -2.390  -15.005 0.80 27.86  ? 78  ILE F N     1 
ATOM   14399 C  CA    A ILE C 3 78  ? 54.001  -1.148  -14.571 0.20 33.06  ? 78  ILE F CA    1 
ATOM   14400 C  CA    B ILE C 3 78  ? 54.502  -1.084  -14.366 0.80 30.75  ? 78  ILE F CA    1 
ATOM   14401 C  C     A ILE C 3 78  ? 53.738  -1.235  -13.077 0.20 31.86  ? 78  ILE F C     1 
ATOM   14402 C  C     B ILE C 3 78  ? 54.187  -1.192  -12.884 0.80 31.67  ? 78  ILE F C     1 
ATOM   14403 O  O     A ILE C 3 78  ? 53.818  -0.214  -12.385 0.20 35.85  ? 78  ILE F O     1 
ATOM   14404 O  O     B ILE C 3 78  ? 54.510  -0.276  -12.119 0.80 38.15  ? 78  ILE F O     1 
ATOM   14405 C  CB    A ILE C 3 78  ? 52.870  -0.336  -15.233 0.20 35.17  ? 78  ILE F CB    1 
ATOM   14406 C  CB    B ILE C 3 78  ? 53.562  -0.071  -15.048 0.80 38.31  ? 78  ILE F CB    1 
ATOM   14407 C  CG1   A ILE C 3 78  ? 51.541  -1.084  -15.116 0.20 34.36  ? 78  ILE F CG1   1 
ATOM   14408 C  CG1   B ILE C 3 78  ? 52.100  -0.458  -14.845 0.80 31.71  ? 78  ILE F CG1   1 
ATOM   14409 C  CG2   A ILE C 3 78  ? 53.205  -0.039  -16.687 0.20 34.06  ? 78  ILE F CG2   1 
ATOM   14410 C  CG2   B ILE C 3 78  ? 53.874  0.033   -16.528 0.80 35.61  ? 78  ILE F CG2   1 
ATOM   14411 C  CD1   A ILE C 3 78  ? 50.362  -0.315  -15.673 0.20 42.85  ? 78  ILE F CD1   1 
ATOM   14412 C  CD1   B ILE C 3 78  ? 51.135  0.527   -15.500 0.80 41.63  ? 78  ILE F CD1   1 
ATOM   14413 N  N     A MET C 3 79  ? 53.425  -2.424  -12.563 0.20 31.14  ? 79  MET F N     1 
ATOM   14414 N  N     B MET C 3 79  ? 53.597  -2.305  -12.458 0.80 30.88  ? 79  MET F N     1 
ATOM   14415 C  CA    A MET C 3 79  ? 53.199  -2.631  -11.137 0.20 31.86  ? 79  MET F CA    1 
ATOM   14416 C  CA    B MET C 3 79  ? 53.241  -2.522  -11.057 0.80 31.57  ? 79  MET F CA    1 
ATOM   14417 C  C     A MET C 3 79  ? 54.243  -3.546  -10.510 0.20 31.80  ? 79  MET F C     1 
ATOM   14418 C  C     B MET C 3 79  ? 54.330  -3.247  -10.280 0.80 32.72  ? 79  MET F C     1 
ATOM   14419 O  O     A MET C 3 79  ? 54.039  -4.032  -9.393  0.20 31.84  ? 79  MET F O     1 
ATOM   14420 O  O     B MET C 3 79  ? 54.137  -3.544  -9.096  0.80 33.02  ? 79  MET F O     1 
ATOM   14421 C  CB    A MET C 3 79  ? 51.795  -3.190  -10.902 0.20 36.33  ? 79  MET F CB    1 
ATOM   14422 C  CB    B MET C 3 79  ? 51.935  -3.309  -10.976 0.80 36.73  ? 79  MET F CB    1 
ATOM   14423 C  CG    A MET C 3 79  ? 50.684  -2.301  -11.435 0.20 40.21  ? 79  MET F CG    1 
ATOM   14424 C  CG    B MET C 3 79  ? 50.844  -2.750  -11.870 0.80 38.47  ? 79  MET F CG    1 
ATOM   14425 S  SD    A MET C 3 79  ? 50.732  -0.619  -10.777 0.20 38.31  ? 79  MET F SD    1 
ATOM   14426 S  SD    B MET C 3 79  ? 50.490  -1.001  -11.555 0.80 57.03  ? 79  MET F SD    1 
ATOM   14427 C  CE    A MET C 3 79  ? 49.367  0.120   -11.674 0.20 46.83  ? 79  MET F CE    1 
ATOM   14428 C  CE    B MET C 3 79  ? 50.148  -1.005  -9.796  0.80 47.87  ? 79  MET F CE    1 
ATOM   14429 N  N     A GLY C 3 80  ? 55.352  -3.796  -11.203 0.20 29.02  ? 80  GLY F N     1 
ATOM   14430 N  N     B GLY C 3 80  ? 55.464  -3.537  -10.913 0.80 26.37  ? 80  GLY F N     1 
ATOM   14431 C  CA    A GLY C 3 80  ? 56.419  -4.602  -10.648 0.20 28.32  ? 80  GLY F CA    1 
ATOM   14432 C  CA    B GLY C 3 80  ? 56.521  -4.297  -10.283 0.80 28.67  ? 80  GLY F CA    1 
ATOM   14433 C  C     A GLY C 3 80  ? 56.134  -6.083  -10.544 0.20 24.25  ? 80  GLY F C     1 
ATOM   14434 C  C     B GLY C 3 80  ? 56.363  -5.800  -10.325 0.80 20.25  ? 80  GLY F C     1 
ATOM   14435 O  O     A GLY C 3 80  ? 56.856  -6.789  -9.841  0.20 27.18  ? 80  GLY F O     1 
ATOM   14436 O  O     B GLY C 3 80  ? 57.176  -6.496  -9.717  0.80 29.04  ? 80  GLY F O     1 
ATOM   14437 N  N     A SER C 3 81  ? 55.108  -6.582  -11.229 0.20 25.47  ? 81  SER F N     1 
ATOM   14438 N  N     B SER C 3 81  ? 55.358  -6.329  -11.032 0.80 24.07  ? 81  SER F N     1 
ATOM   14439 C  CA    A SER C 3 81  ? 54.781  -8.002  -11.163 0.20 26.53  ? 81  SER F CA    1 
ATOM   14440 C  CA    B SER C 3 81  ? 55.118  -7.768  -11.060 0.80 25.21  ? 81  SER F CA    1 
ATOM   14441 C  C     A SER C 3 81  ? 55.695  -8.785  -12.097 0.20 26.49  ? 81  SER F C     1 
ATOM   14442 C  C     B SER C 3 81  ? 56.090  -8.464  -12.003 0.80 26.56  ? 81  SER F C     1 
ATOM   14443 O  O     A SER C 3 81  ? 55.737  -8.516  -13.303 0.20 25.25  ? 81  SER F O     1 
ATOM   14444 O  O     B SER C 3 81  ? 56.239  -8.051  -13.156 0.80 25.55  ? 81  SER F O     1 
ATOM   14445 C  CB    A SER C 3 81  ? 53.319  -8.240  -11.529 0.20 29.79  ? 81  SER F CB    1 
ATOM   14446 C  CB    B SER C 3 81  ? 53.686  -8.075  -11.513 0.80 30.29  ? 81  SER F CB    1 
ATOM   14447 O  OG    A SER C 3 81  ? 52.446  -7.491  -10.701 0.20 33.78  ? 81  SER F OG    1 
ATOM   14448 O  OG    B SER C 3 81  ? 52.699  -7.584  -10.622 0.80 36.19  ? 81  SER F OG    1 
ATOM   14449 N  N     A THR C 3 82  ? 56.414  -9.752  -11.542 0.20 25.37  ? 82  THR F N     1 
ATOM   14450 N  N     B THR C 3 82  ? 56.728  -9.537  -11.521 0.80 26.96  ? 82  THR F N     1 
ATOM   14451 C  CA    A THR C 3 82  ? 57.323  -10.624 -12.267 0.20 25.37  ? 82  THR F CA    1 
ATOM   14452 C  CA    B THR C 3 82  ? 57.485  -10.457 -12.361 0.80 25.00  ? 82  THR F CA    1 
ATOM   14453 C  C     A THR C 3 82  ? 56.594  -11.878 -12.729 0.20 26.46  ? 82  THR F C     1 
ATOM   14454 C  C     B THR C 3 82  ? 56.588  -11.592 -12.820 0.80 25.55  ? 82  THR F C     1 
ATOM   14455 O  O     A THR C 3 82  ? 55.515  -12.206 -12.219 0.20 26.95  ? 82  THR F O     1 
ATOM   14456 O  O     B THR C 3 82  ? 55.511  -11.825 -12.242 0.80 29.45  ? 82  THR F O     1 
ATOM   14457 C  CB    A THR C 3 82  ? 58.508  -11.003 -11.376 0.20 27.26  ? 82  THR F CB    1 
ATOM   14458 C  CB    B THR C 3 82  ? 58.680  -11.041 -11.595 0.80 26.95  ? 82  THR F CB    1 
ATOM   14459 O  OG1   A THR C 3 82  ? 58.047  -11.782 -10.264 0.20 28.75  ? 82  THR F OG1   1 
ATOM   14460 O  OG1   B THR C 3 82  ? 58.219  -11.767 -10.441 0.80 30.37  ? 82  THR F OG1   1 
ATOM   14461 C  CG2   A THR C 3 82  ? 59.208  -9.756  -10.856 0.20 25.82  ? 82  THR F CG2   1 
ATOM   14462 C  CG2   B THR C 3 82  ? 59.659  -9.960  -11.165 0.80 23.38  ? 82  THR F CG2   1 
ATOM   14463 N  N     A PRO C 3 83  ? 57.150  -12.603 -13.707 0.20 26.04  ? 83  PRO F N     1 
ATOM   14464 N  N     B PRO C 3 83  ? 56.998  -12.331 -13.858 0.80 26.20  ? 83  PRO F N     1 
ATOM   14465 C  CA    A PRO C 3 83  ? 56.533  -13.879 -14.105 0.20 23.60  ? 83  PRO F CA    1 
ATOM   14466 C  CA    B PRO C 3 83  ? 56.313  -13.596 -14.152 0.80 21.28  ? 83  PRO F CA    1 
ATOM   14467 C  C     A PRO C 3 83  ? 56.384  -14.866 -12.961 0.20 25.54  ? 83  PRO F C     1 
ATOM   14468 C  C     B PRO C 3 83  ? 56.159  -14.493 -12.930 0.80 25.23  ? 83  PRO F C     1 
ATOM   14469 O  O     A PRO C 3 83  ? 55.515  -15.744 -13.029 0.20 27.88  ? 83  PRO F O     1 
ATOM   14470 O  O     B PRO C 3 83  ? 55.096  -15.101 -12.749 0.80 27.91  ? 83  PRO F O     1 
ATOM   14471 C  CB    A PRO C 3 83  ? 57.491  -14.412 -15.180 0.20 24.58  ? 83  PRO F CB    1 
ATOM   14472 C  CB    B PRO C 3 83  ? 57.210  -14.229 -15.227 0.80 25.03  ? 83  PRO F CB    1 
ATOM   14473 C  CG    A PRO C 3 83  ? 58.151  -13.196 -15.727 0.20 25.29  ? 83  PRO F CG    1 
ATOM   14474 C  CG    B PRO C 3 83  ? 57.807  -13.051 -15.931 0.80 25.11  ? 83  PRO F CG    1 
ATOM   14475 C  CD    A PRO C 3 83  ? 58.300  -12.259 -14.564 0.20 23.62  ? 83  PRO F CD    1 
ATOM   14476 C  CD    B PRO C 3 83  ? 58.057  -12.032 -14.844 0.80 22.74  ? 83  PRO F CD    1 
ATOM   14477 N  N     A LEU C 3 84  ? 57.200  -14.753 -11.910 0.20 25.94  ? 84  LEU F N     1 
ATOM   14478 N  N     B LEU C 3 84  ? 57.177  -14.572 -12.064 0.80 25.10  ? 84  LEU F N     1 
ATOM   14479 C  CA    A LEU C 3 84  ? 57.048  -15.630 -10.754 0.20 25.62  ? 84  LEU F CA    1 
ATOM   14480 C  CA    B LEU C 3 84  ? 57.068  -15.438 -10.886 0.80 25.42  ? 84  LEU F CA    1 
ATOM   14481 C  C     A LEU C 3 84  ? 55.914  -15.179 -9.838  0.20 27.46  ? 84  LEU F C     1 
ATOM   14482 C  C     B LEU C 3 84  ? 55.955  -14.972 -9.939  0.80 28.00  ? 84  LEU F C     1 
ATOM   14483 O  O     A LEU C 3 84  ? 55.262  -16.020 -9.208  0.20 25.00  ? 84  LEU F O     1 
ATOM   14484 O  O     B LEU C 3 84  ? 55.223  -15.798 -9.384  0.80 23.68  ? 84  LEU F O     1 
ATOM   14485 C  CB    A LEU C 3 84  ? 58.365  -15.702 -9.978  0.20 30.29  ? 84  LEU F CB    1 
ATOM   14486 C  CB    B LEU C 3 84  ? 58.411  -15.508 -10.156 0.80 30.94  ? 84  LEU F CB    1 
ATOM   14487 C  CG    A LEU C 3 84  ? 58.404  -16.608 -8.746  0.20 31.11  ? 84  LEU F CG    1 
ATOM   14488 C  CG    B LEU C 3 84  ? 58.427  -16.374 -8.891  0.80 31.98  ? 84  LEU F CG    1 
ATOM   14489 C  CD1   A LEU C 3 84  ? 57.982  -18.026 -9.102  0.20 29.59  ? 84  LEU F CD1   1 
ATOM   14490 C  CD1   B LEU C 3 84  ? 57.898  -17.781 -9.181  0.80 29.74  ? 84  LEU F CD1   1 
ATOM   14491 C  CD2   A LEU C 3 84  ? 59.792  -16.598 -8.121  0.20 29.29  ? 84  LEU F CD2   1 
ATOM   14492 C  CD2   B LEU C 3 84  ? 59.826  -16.423 -8.266  0.80 29.11  ? 84  LEU F CD2   1 
ATOM   14493 N  N     A HIS C 3 85  ? 55.661  -13.871 -9.754  0.20 24.07  ? 85  HIS F N     1 
ATOM   14494 N  N     B HIS C 3 85  ? 55.827  -13.660 -9.729  0.80 23.26  ? 85  HIS F N     1 
ATOM   14495 C  CA    A HIS C 3 85  ? 54.548  -13.383 -8.943  0.20 27.98  ? 85  HIS F CA    1 
ATOM   14496 C  CA    B HIS C 3 85  ? 54.666  -13.122 -9.019  0.80 29.01  ? 85  HIS F CA    1 
ATOM   14497 C  C     A HIS C 3 85  ? 53.208  -13.823 -9.519  0.20 29.88  ? 85  HIS F C     1 
ATOM   14498 C  C     B HIS C 3 85  ? 53.371  -13.732 -9.537  0.80 31.00  ? 85  HIS F C     1 
ATOM   14499 O  O     A HIS C 3 85  ? 52.308  -14.225 -8.772  0.20 27.52  ? 85  HIS F O     1 
ATOM   14500 O  O     B HIS C 3 85  ? 52.578  -14.285 -8.767  0.80 27.62  ? 85  HIS F O     1 
ATOM   14501 C  CB    A HIS C 3 85  ? 54.599  -11.859 -8.832  0.20 26.01  ? 85  HIS F CB    1 
ATOM   14502 C  CB    B HIS C 3 85  ? 54.602  -11.601 -9.171  0.80 25.04  ? 85  HIS F CB    1 
ATOM   14503 C  CG    A HIS C 3 85  ? 55.660  -11.349 -7.907  0.20 25.89  ? 85  HIS F CG    1 
ATOM   14504 C  CG    B HIS C 3 85  ? 55.454  -10.850 -8.197  0.80 28.21  ? 85  HIS F CG    1 
ATOM   14505 N  ND1   A HIS C 3 85  ? 56.977  -11.211 -8.287  0.20 24.92  ? 85  HIS F ND1   1 
ATOM   14506 N  ND1   B HIS C 3 85  ? 56.639  -10.247 -8.556  0.80 23.35  ? 85  HIS F ND1   1 
ATOM   14507 C  CD2   A HIS C 3 85  ? 55.593  -10.929 -6.621  0.20 24.79  ? 85  HIS F CD2   1 
ATOM   14508 C  CD2   B HIS C 3 85  ? 55.270  -10.571 -6.884  0.80 23.18  ? 85  HIS F CD2   1 
ATOM   14509 C  CE1   A HIS C 3 85  ? 57.678  -10.733 -7.274  0.20 25.77  ? 85  HIS F CE1   1 
ATOM   14510 C  CE1   B HIS C 3 85  ? 57.164  -9.650  -7.498  0.80 26.47  ? 85  HIS F CE1   1 
ATOM   14511 N  NE2   A HIS C 3 85  ? 56.862  -10.554 -6.250  0.20 25.71  ? 85  HIS F NE2   1 
ATOM   14512 N  NE2   B HIS C 3 85  ? 56.348  -9.829  -6.471  0.80 24.15  ? 85  HIS F NE2   1 
ATOM   14513 N  N     A LEU C 3 86  ? 53.052  -13.752 -10.843 0.20 23.91  ? 86  LEU F N     1 
ATOM   14514 N  N     B LEU C 3 86  ? 53.153  -13.654 -10.852 0.80 23.29  ? 86  LEU F N     1 
ATOM   14515 C  CA    A LEU C 3 86  ? 51.781  -14.130 -11.452 0.20 25.51  ? 86  LEU F CA    1 
ATOM   14516 C  CA    B LEU C 3 86  ? 51.858  -14.026 -11.413 0.80 25.23  ? 86  LEU F CA    1 
ATOM   14517 C  C     A LEU C 3 86  ? 51.589  -15.641 -11.432 0.20 27.57  ? 86  LEU F C     1 
ATOM   14518 C  C     B LEU C 3 86  ? 51.643  -15.532 -11.344 0.80 28.01  ? 86  LEU F C     1 
ATOM   14519 O  O     A LEU C 3 86  ? 50.467  -16.128 -11.238 0.20 27.90  ? 86  LEU F O     1 
ATOM   14520 O  O     B LEU C 3 86  ? 50.537  -15.994 -11.027 0.80 27.87  ? 86  LEU F O     1 
ATOM   14521 C  CB    A LEU C 3 86  ? 51.705  -13.592 -12.882 0.20 27.58  ? 86  LEU F CB    1 
ATOM   14522 C  CB    B LEU C 3 86  ? 51.755  -13.522 -12.856 0.80 27.68  ? 86  LEU F CB    1 
ATOM   14523 C  CG    A LEU C 3 86  ? 51.769  -12.070 -13.015 0.20 28.96  ? 86  LEU F CG    1 
ATOM   14524 C  CG    B LEU C 3 86  ? 51.956  -12.012 -12.977 0.80 29.20  ? 86  LEU F CG    1 
ATOM   14525 C  CD1   A LEU C 3 86  ? 51.770  -11.643 -14.474 0.20 26.37  ? 86  LEU F CD1   1 
ATOM   14526 C  CD1   B LEU C 3 86  ? 51.939  -11.530 -14.414 0.80 25.62  ? 86  LEU F CD1   1 
ATOM   14527 C  CD2   A LEU C 3 86  ? 50.615  -11.420 -12.261 0.20 32.94  ? 86  LEU F CD2   1 
ATOM   14528 C  CD2   B LEU C 3 86  ? 50.896  -11.285 -12.141 0.80 34.53  ? 86  LEU F CD2   1 
ATOM   14529 N  N     A ALA C 3 87  ? 52.672  -16.399 -11.625 0.20 24.53  ? 87  ALA F N     1 
ATOM   14530 N  N     B ALA C 3 87  ? 52.692  -16.313 -11.625 0.80 24.32  ? 87  ALA F N     1 
ATOM   14531 C  CA    A ALA C 3 87  ? 52.578  -17.855 -11.566 0.20 23.61  ? 87  ALA F CA    1 
ATOM   14532 C  CA    B ALA C 3 87  ? 52.597  -17.768 -11.519 0.80 23.32  ? 87  ALA F CA    1 
ATOM   14533 C  C     A ALA C 3 87  ? 52.202  -18.326 -10.166 0.20 27.56  ? 87  ALA F C     1 
ATOM   14534 C  C     B ALA C 3 87  ? 52.267  -18.198 -10.088 0.80 27.24  ? 87  ALA F C     1 
ATOM   14535 O  O     A ALA C 3 87  ? 51.398  -19.253 -10.009 0.20 28.43  ? 87  ALA F O     1 
ATOM   14536 O  O     B ALA C 3 87  ? 51.502  -19.147 -9.876  0.80 28.49  ? 87  ALA F O     1 
ATOM   14537 C  CB    A ALA C 3 87  ? 53.899  -18.485 -12.007 0.20 30.03  ? 87  ALA F CB    1 
ATOM   14538 C  CB    B ALA C 3 87  ? 53.900  -18.415 -11.979 0.80 30.16  ? 87  ALA F CB    1 
ATOM   14539 N  N     A ALA C 3 88  ? 52.775  -17.702 -9.135  0.20 25.05  ? 88  ALA F N     1 
ATOM   14540 N  N     B ALA C 3 88  ? 52.842  -17.518 -9.094  0.80 24.45  ? 88  ALA F N     1 
ATOM   14541 C  CA    A ALA C 3 88  ? 52.442  -18.070 -7.764  0.20 25.97  ? 88  ALA F CA    1 
ATOM   14542 C  CA    B ALA C 3 88  ? 52.586  -17.897 -7.707  0.80 25.79  ? 88  ALA F CA    1 
ATOM   14543 C  C     A ALA C 3 88  ? 51.070  -17.558 -7.344  0.20 26.25  ? 88  ALA F C     1 
ATOM   14544 C  C     B ALA C 3 88  ? 51.188  -17.474 -7.270  0.80 26.11  ? 88  ALA F C     1 
ATOM   14545 O  O     A ALA C 3 88  ? 50.471  -18.115 -6.417  0.20 29.85  ? 88  ALA F O     1 
ATOM   14546 O  O     B ALA C 3 88  ? 50.534  -18.177 -6.486  0.80 29.80  ? 88  ALA F O     1 
ATOM   14547 C  CB    A ALA C 3 88  ? 53.513  -17.548 -6.805  0.20 26.73  ? 88  ALA F CB    1 
ATOM   14548 C  CB    B ALA C 3 88  ? 53.656  -17.293 -6.798  0.80 26.64  ? 88  ALA F CB    1 
ATOM   14549 N  N     A LEU C 3 89  ? 50.560  -16.516 -8.003  0.20 25.08  ? 89  LEU F N     1 
ATOM   14550 N  N     B LEU C 3 89  ? 50.715  -16.326 -7.759  0.80 23.93  ? 89  LEU F N     1 
ATOM   14551 C  CA    A LEU C 3 89  ? 49.243  -15.988 -7.663  0.20 25.22  ? 89  LEU F CA    1 
ATOM   14552 C  CA    B LEU C 3 89  ? 49.357  -15.893 -7.449  0.80 23.75  ? 89  LEU F CA    1 
ATOM   14553 C  C     A LEU C 3 89  ? 48.127  -16.842 -8.254  0.20 32.82  ? 89  LEU F C     1 
ATOM   14554 C  C     B LEU C 3 89  ? 48.330  -16.853 -8.042  0.80 35.01  ? 89  LEU F C     1 
ATOM   14555 O  O     A LEU C 3 89  ? 47.123  -17.109 -7.582  0.20 30.28  ? 89  LEU F O     1 
ATOM   14556 O  O     B LEU C 3 89  ? 47.429  -17.334 -7.337  0.80 32.24  ? 89  LEU F O     1 
ATOM   14557 C  CB    A LEU C 3 89  ? 49.118  -14.543 -8.144  0.20 23.96  ? 89  LEU F CB    1 
ATOM   14558 C  CB    B LEU C 3 89  ? 49.127  -14.475 -7.966  0.80 23.11  ? 89  LEU F CB    1 
ATOM   14559 C  CG    A LEU C 3 89  ? 47.773  -13.853 -7.906  0.20 30.02  ? 89  LEU F CG    1 
ATOM   14560 C  CG    B LEU C 3 89  ? 47.715  -13.919 -7.750  0.80 30.62  ? 89  LEU F CG    1 
ATOM   14561 C  CD1   A LEU C 3 89  ? 47.506  -13.697 -6.414  0.20 26.46  ? 89  LEU F CD1   1 
ATOM   14562 C  CD1   B LEU C 3 89  ? 47.625  -13.168 -6.420  0.80 25.54  ? 89  LEU F CD1   1 
ATOM   14563 C  CD2   A LEU C 3 89  ? 47.716  -12.506 -8.617  0.20 29.42  ? 89  LEU F CD2   1 
ATOM   14564 C  CD2   B LEU C 3 89  ? 47.276  -13.045 -8.916  0.80 29.84  ? 89  LEU F CD2   1 
ATOM   14565 N  N     A ILE C 3 90  ? 48.281  -17.278 -9.505  0.20 26.79  ? 90  ILE F N     1 
ATOM   14566 N  N     B ILE C 3 90  ? 48.450  -17.146 -9.343  0.80 25.60  ? 90  ILE F N     1 
ATOM   14567 C  CA    A ILE C 3 90  ? 47.250  -18.093 -10.139 0.20 29.19  ? 90  ILE F CA    1 
ATOM   14568 C  CA    B ILE C 3 90  ? 47.454  -17.982 -10.007 0.80 28.47  ? 90  ILE F CA    1 
ATOM   14569 C  C     A ILE C 3 90  ? 47.308  -19.530 -9.630  0.20 31.25  ? 90  ILE F C     1 
ATOM   14570 C  C     B ILE C 3 90  ? 47.600  -19.452 -9.616  0.80 30.73  ? 90  ILE F C     1 
ATOM   14571 O  O     A ILE C 3 90  ? 46.273  -20.184 -9.461  0.20 34.37  ? 90  ILE F O     1 
ATOM   14572 O  O     B ILE C 3 90  ? 46.634  -20.219 -9.706  0.80 36.38  ? 90  ILE F O     1 
ATOM   14573 C  CB    A ILE C 3 90  ? 47.389  -18.025 -11.670 0.20 33.21  ? 90  ILE F CB    1 
ATOM   14574 C  CB    B ILE C 3 90  ? 47.540  -17.809 -11.536 0.80 34.29  ? 90  ILE F CB    1 
ATOM   14575 C  CG1   A ILE C 3 90  ? 47.364  -16.571 -12.147 0.20 32.86  ? 90  ILE F CG1   1 
ATOM   14576 C  CG1   B ILE C 3 90  ? 47.551  -16.327 -11.907 0.80 33.93  ? 90  ILE F CG1   1 
ATOM   14577 C  CG2   A ILE C 3 90  ? 46.284  -18.825 -12.345 0.20 30.26  ? 90  ILE F CG2   1 
ATOM   14578 C  CG2   B ILE C 3 90  ? 46.367  -18.496 -12.225 0.80 29.70  ? 90  ILE F CG2   1 
ATOM   14579 C  CD1   A ILE C 3 90  ? 46.058  -15.859 -11.883 0.20 30.77  ? 90  ILE F CD1   1 
ATOM   14580 C  CD1   B ILE C 3 90  ? 46.303  -15.598 -11.526 0.80 28.98  ? 90  ILE F CD1   1 
ATOM   14581 N  N     A GLY C 3 91  ? 48.508  -20.042 -9.373  0.20 29.21  ? 91  GLY F N     1 
ATOM   14582 N  N     B GLY C 3 91  ? 48.773  -19.866 -9.164  0.80 28.46  ? 91  GLY F N     1 
ATOM   14583 C  CA    A GLY C 3 91  ? 48.655  -21.384 -8.844  0.20 30.67  ? 91  GLY F CA    1 
ATOM   14584 C  CA    B GLY C 3 91  ? 48.961  -21.203 -8.650  0.80 30.42  ? 91  GLY F CA    1 
ATOM   14585 C  C     A GLY C 3 91  ? 49.122  -22.390 -9.874  0.20 32.41  ? 91  GLY F C     1 
ATOM   14586 C  C     B GLY C 3 91  ? 49.501  -22.220 -9.628  0.80 31.74  ? 91  GLY F C     1 
ATOM   14587 O  O     A GLY C 3 91  ? 48.405  -23.347 -10.187 0.20 29.97  ? 91  GLY F O     1 
ATOM   14588 O  O     B GLY C 3 91  ? 49.227  -23.414 -9.463  0.80 29.28  ? 91  GLY F O     1 
ATOM   14589 N  N     A HIS C 3 92  ? 50.323  -22.180 -10.410 0.20 31.66  ? 92  HIS F N     1 
ATOM   14590 N  N     B HIS C 3 92  ? 50.260  -21.792 -10.637 0.80 31.49  ? 92  HIS F N     1 
ATOM   14591 C  CA    A HIS C 3 92  ? 50.928  -23.069 -11.402 0.20 34.53  ? 92  HIS F CA    1 
ATOM   14592 C  CA    B HIS C 3 92  ? 50.799  -22.697 -11.654 0.80 35.77  ? 92  HIS F CA    1 
ATOM   14593 C  C     A HIS C 3 92  ? 52.238  -23.596 -10.824 0.20 33.32  ? 92  HIS F C     1 
ATOM   14594 C  C     B HIS C 3 92  ? 52.118  -23.270 -11.146 0.80 33.25  ? 92  HIS F C     1 
ATOM   14595 O  O     A HIS C 3 92  ? 53.265  -22.910 -10.863 0.20 32.43  ? 92  HIS F O     1 
ATOM   14596 O  O     B HIS C 3 92  ? 53.200  -22.731 -11.394 0.80 30.72  ? 92  HIS F O     1 
ATOM   14597 C  CB    A HIS C 3 92  ? 51.149  -22.346 -12.726 0.20 33.17  ? 92  HIS F CB    1 
ATOM   14598 C  CB    B HIS C 3 92  ? 50.970  -21.971 -12.979 0.80 34.49  ? 92  HIS F CB    1 
ATOM   14599 C  CG    A HIS C 3 92  ? 49.888  -21.847 -13.361 0.20 32.57  ? 92  HIS F CG    1 
ATOM   14600 C  CG    B HIS C 3 92  ? 49.686  -21.501 -13.589 0.80 32.31  ? 92  HIS F CG    1 
ATOM   14601 N  ND1   A HIS C 3 92  ? 48.810  -22.666 -13.618 0.20 33.63  ? 92  HIS F ND1   1 
ATOM   14602 N  ND1   B HIS C 3 92  ? 48.646  -22.355 -13.888 0.80 35.24  ? 92  HIS F ND1   1 
ATOM   14603 C  CD2   A HIS C 3 92  ? 49.538  -20.615 -13.801 0.20 30.88  ? 92  HIS F CD2   1 
ATOM   14604 C  CD2   B HIS C 3 92  ? 49.281  -20.266 -13.970 0.80 29.10  ? 92  HIS F CD2   1 
ATOM   14605 C  CE1   A HIS C 3 92  ? 47.847  -21.959 -14.183 0.20 32.75  ? 92  HIS F CE1   1 
ATOM   14606 C  CE1   B HIS C 3 92  ? 47.653  -21.665 -14.422 0.80 31.47  ? 92  HIS F CE1   1 
ATOM   14607 N  NE2   A HIS C 3 92  ? 48.264  -20.711 -14.305 0.20 31.66  ? 92  HIS F NE2   1 
ATOM   14608 N  NE2   B HIS C 3 92  ? 48.012  -20.394 -14.479 0.80 31.47  ? 92  HIS F NE2   1 
ATOM   14609 N  N     A LEU C 3 93  ? 52.200  -24.825 -10.305 0.20 34.58  ? 93  LEU F N     1 
ATOM   14610 N  N     B LEU C 3 93  ? 52.023  -24.403 -10.446 0.80 32.52  ? 93  LEU F N     1 
ATOM   14611 C  CA    A LEU C 3 93  ? 53.354  -25.385 -9.608  0.20 34.75  ? 93  LEU F CA    1 
ATOM   14612 C  CA    B LEU C 3 93  ? 53.187  -24.986 -9.778  0.80 33.59  ? 93  LEU F CA    1 
ATOM   14613 C  C     A LEU C 3 93  ? 54.528  -25.610 -10.556 0.20 36.18  ? 93  LEU F C     1 
ATOM   14614 C  C     B LEU C 3 93  ? 54.296  -25.338 -10.764 0.80 36.69  ? 93  LEU F C     1 
ATOM   14615 O  O     A LEU C 3 93  ? 55.671  -25.258 -10.240 0.20 33.40  ? 93  LEU F O     1 
ATOM   14616 O  O     B LEU C 3 93  ? 55.463  -24.984 -10.550 0.80 33.10  ? 93  LEU F O     1 
ATOM   14617 C  CB    A LEU C 3 93  ? 52.959  -26.695 -8.925  0.20 36.68  ? 93  LEU F CB    1 
ATOM   14618 C  CB    B LEU C 3 93  ? 52.772  -26.233 -8.992  0.80 37.55  ? 93  LEU F CB    1 
ATOM   14619 C  CG    A LEU C 3 93  ? 54.042  -27.387 -8.097  0.20 40.84  ? 93  LEU F CG    1 
ATOM   14620 C  CG    B LEU C 3 93  ? 53.944  -27.057 -8.450  0.80 40.86  ? 93  LEU F CG    1 
ATOM   14621 C  CD1   A LEU C 3 93  ? 54.382  -26.562 -6.869  0.20 35.78  ? 93  LEU F CD1   1 
ATOM   14622 C  CD1   B LEU C 3 93  ? 54.748  -26.271 -7.419  0.80 36.35  ? 93  LEU F CD1   1 
ATOM   14623 C  CD2   A LEU C 3 93  ? 53.605  -28.788 -7.701  0.20 43.38  ? 93  LEU F CD2   1 
ATOM   14624 C  CD2   B LEU C 3 93  ? 53.456  -28.371 -7.862  0.80 45.56  ? 93  LEU F CD2   1 
ATOM   14625 N  N     A GLU C 3 94  ? 54.267  -26.207 -11.720 0.20 33.67  ? 94  GLU F N     1 
ATOM   14626 N  N     B GLU C 3 94  ? 53.964  -26.073 -11.830 0.80 29.65  ? 94  GLU F N     1 
ATOM   14627 C  CA    A GLU C 3 94  ? 55.357  -26.537 -12.635 0.20 37.13  ? 94  GLU F CA    1 
ATOM   14628 C  CA    B GLU C 3 94  ? 55.021  -26.530 -12.735 0.80 39.65  ? 94  GLU F CA    1 
ATOM   14629 C  C     A GLU C 3 94  ? 55.983  -25.281 -13.227 0.20 34.05  ? 94  GLU F C     1 
ATOM   14630 C  C     B GLU C 3 94  ? 55.747  -25.350 -13.365 0.80 33.33  ? 94  GLU F C     1 
ATOM   14631 O  O     A GLU C 3 94  ? 57.203  -25.223 -13.423 0.20 35.38  ? 94  GLU F O     1 
ATOM   14632 O  O     B GLU C 3 94  ? 56.949  -25.429 -13.645 0.80 37.70  ? 94  GLU F O     1 
ATOM   14633 C  CB    A GLU C 3 94  ? 54.851  -27.464 -13.741 0.20 36.93  ? 94  GLU F CB    1 
ATOM   14634 C  CB    B GLU C 3 94  ? 54.445  -27.451 -13.815 0.80 36.35  ? 94  GLU F CB    1 
ATOM   14635 C  CG    A GLU C 3 94  ? 54.530  -28.882 -13.280 0.20 41.42  ? 94  GLU F CG    1 
ATOM   14636 C  CG    B GLU C 3 94  ? 53.663  -28.662 -13.284 0.80 47.32  ? 94  GLU F CG    1 
ATOM   14637 C  CD    A GLU C 3 94  ? 53.264  -28.972 -12.442 0.20 44.15  ? 94  GLU F CD    1 
ATOM   14638 C  CD    B GLU C 3 94  ? 52.143  -28.446 -13.219 0.80 50.08  ? 94  GLU F CD    1 
ATOM   14639 O  OE1   A GLU C 3 94  ? 52.497  -27.985 -12.399 0.20 42.61  ? 94  GLU F OE1   1 
ATOM   14640 O  OE1   B GLU C 3 94  ? 51.689  -27.301 -12.989 0.80 38.91  ? 94  GLU F OE1   1 
ATOM   14641 O  OE2   A GLU C 3 94  ? 53.037  -30.034 -11.824 0.20 45.84  ? 94  GLU F OE2   1 
ATOM   14642 O  OE2   B GLU C 3 94  ? 51.396  -29.436 -13.396 0.80 49.13  ? 94  GLU F OE2   1 
ATOM   14643 N  N     A ILE C 3 95  ? 55.168  -24.264 -13.511 0.20 32.56  ? 95  ILE F N     1 
ATOM   14644 N  N     B ILE C 3 95  ? 55.041  -24.239 -13.560 0.80 32.36  ? 95  ILE F N     1 
ATOM   14645 C  CA    A ILE C 3 95  ? 55.698  -23.020 -14.060 0.20 34.56  ? 95  ILE F CA    1 
ATOM   14646 C  CA    B ILE C 3 95  ? 55.645  -23.042 -14.125 0.80 34.42  ? 95  ILE F CA    1 
ATOM   14647 C  C     A ILE C 3 95  ? 56.596  -22.325 -13.044 0.20 34.47  ? 95  ILE F C     1 
ATOM   14648 C  C     B ILE C 3 95  ? 56.492  -22.311 -13.089 0.80 34.77  ? 95  ILE F C     1 
ATOM   14649 O  O     A ILE C 3 95  ? 57.618  -21.728 -13.405 0.20 28.80  ? 95  ILE F O     1 
ATOM   14650 O  O     B ILE C 3 95  ? 57.555  -21.773 -13.415 0.80 28.50  ? 95  ILE F O     1 
ATOM   14651 C  CB    A ILE C 3 95  ? 54.543  -22.115 -14.523 0.20 35.63  ? 95  ILE F CB    1 
ATOM   14652 C  CB    B ILE C 3 95  ? 54.539  -22.156 -14.717 0.80 36.21  ? 95  ILE F CB    1 
ATOM   14653 C  CG1   A ILE C 3 95  ? 53.758  -22.799 -15.645 0.20 31.78  ? 95  ILE F CG1   1 
ATOM   14654 C  CG1   B ILE C 3 95  ? 53.986  -22.835 -15.973 0.80 30.21  ? 95  ILE F CG1   1 
ATOM   14655 C  CG2   A ILE C 3 95  ? 55.064  -20.760 -14.978 0.20 34.62  ? 95  ILE F CG2   1 
ATOM   14656 C  CG2   B ILE C 3 95  ? 55.047  -20.745 -14.986 0.80 34.92  ? 95  ILE F CG2   1 
ATOM   14657 C  CD1   A ILE C 3 95  ? 52.624  -21.969 -16.194 0.20 33.88  ? 95  ILE F CD1   1 
ATOM   14658 C  CD1   B ILE C 3 95  ? 52.749  -22.194 -16.545 0.80 34.04  ? 95  ILE F CD1   1 
ATOM   14659 N  N     A VAL C 3 96  ? 56.241  -22.399 -11.758 0.20 28.89  ? 96  VAL F N     1 
ATOM   14660 N  N     B VAL C 3 96  ? 56.048  -22.278 -11.826 0.80 26.91  ? 96  VAL F N     1 
ATOM   14661 C  CA    A VAL C 3 96  ? 57.084  -21.807 -10.723 0.20 31.09  ? 96  VAL F CA    1 
ATOM   14662 C  CA    B VAL C 3 96  ? 56.904  -21.743 -10.770 0.80 30.68  ? 96  VAL F CA    1 
ATOM   14663 C  C     A VAL C 3 96  ? 58.455  -22.473 -10.705 0.20 34.09  ? 96  VAL F C     1 
ATOM   14664 C  C     B VAL C 3 96  ? 58.257  -22.441 -10.787 0.80 34.98  ? 96  VAL F C     1 
ATOM   14665 O  O     A VAL C 3 96  ? 59.487  -21.800 -10.592 0.20 31.70  ? 96  VAL F O     1 
ATOM   14666 O  O     B VAL C 3 96  ? 59.311  -21.797 -10.722 0.80 31.18  ? 96  VAL F O     1 
ATOM   14667 C  CB    A VAL C 3 96  ? 56.390  -21.894 -9.350  0.20 31.01  ? 96  VAL F CB    1 
ATOM   14668 C  CB    B VAL C 3 96  ? 56.223  -21.876 -9.397  0.80 31.05  ? 96  VAL F CB    1 
ATOM   14669 C  CG1   A VAL C 3 96  ? 57.374  -21.576 -8.232  0.20 30.25  ? 96  VAL F CG1   1 
ATOM   14670 C  CG1   B VAL C 3 96  ? 57.190  -21.444 -8.291  0.80 30.09  ? 96  VAL F CG1   1 
ATOM   14671 C  CG2   A VAL C 3 96  ? 55.206  -20.941 -9.304  0.20 28.90  ? 96  VAL F CG2   1 
ATOM   14672 C  CG2   B VAL C 3 96  ? 54.961  -21.037 -9.376  0.80 28.32  ? 96  VAL F CG2   1 
ATOM   14673 N  N     A GLU C 3 97  ? 58.490  -23.803 -10.827 0.20 32.84  ? 97  GLU F N     1 
ATOM   14674 N  N     B GLU C 3 97  ? 58.244  -23.772 -10.898 0.80 31.85  ? 97  GLU F N     1 
ATOM   14675 C  CA    A GLU C 3 97  ? 59.769  -24.507 -10.815 0.20 35.07  ? 97  GLU F CA    1 
ATOM   14676 C  CA    B GLU C 3 97  ? 59.495  -24.522 -10.840 0.80 35.48  ? 97  GLU F CA    1 
ATOM   14677 C  C     A GLU C 3 97  ? 60.606  -24.166 -12.042 0.20 32.76  ? 97  GLU F C     1 
ATOM   14678 C  C     B GLU C 3 97  ? 60.380  -24.226 -12.044 0.80 32.18  ? 97  GLU F C     1 
ATOM   14679 O  O     A GLU C 3 97  ? 61.832  -24.037 -11.946 0.20 34.88  ? 97  GLU F O     1 
ATOM   14680 O  O     B GLU C 3 97  ? 61.604  -24.108 -11.904 0.80 35.17  ? 97  GLU F O     1 
ATOM   14681 C  CB    A GLU C 3 97  ? 59.543  -26.016 -10.725 0.20 32.71  ? 97  GLU F CB    1 
ATOM   14682 C  CB    B GLU C 3 97  ? 59.203  -26.014 -10.727 0.80 31.33  ? 97  GLU F CB    1 
ATOM   14683 C  CG    A GLU C 3 97  ? 59.164  -26.506 -9.335  0.20 39.06  ? 97  GLU F CG    1 
ATOM   14684 C  CG    B GLU C 3 97  ? 58.724  -26.402 -9.324  0.80 37.82  ? 97  GLU F CG    1 
ATOM   14685 C  CD    A GLU C 3 97  ? 59.218  -28.016 -9.215  0.20 46.91  ? 97  GLU F CD    1 
ATOM   14686 C  CD    B GLU C 3 97  ? 58.485  -27.886 -9.155  0.80 49.38  ? 97  GLU F CD    1 
ATOM   14687 O  OE1   A GLU C 3 97  ? 59.130  -28.702 -10.255 0.20 41.42  ? 97  GLU F OE1   1 
ATOM   14688 O  OE1   B GLU C 3 97  ? 57.849  -28.495 -10.041 0.80 46.67  ? 97  GLU F OE1   1 
ATOM   14689 O  OE2   A GLU C 3 97  ? 59.354  -28.519 -8.078  0.20 53.40  ? 97  GLU F OE2   1 
ATOM   14690 O  OE2   B GLU C 3 97  ? 58.935  -28.443 -8.127  0.80 56.26  ? 97  GLU F OE2   1 
ATOM   14691 N  N     A VAL C 3 98  ? 59.964  -24.020 -13.204 0.20 32.89  ? 98  VAL F N     1 
ATOM   14692 N  N     B VAL C 3 98  ? 59.782  -24.096 -13.229 0.80 32.54  ? 98  VAL F N     1 
ATOM   14693 C  CA    A VAL C 3 98  ? 60.700  -23.685 -14.420 0.20 34.73  ? 98  VAL F CA    1 
ATOM   14694 C  CA    B VAL C 3 98  ? 60.555  -23.767 -14.422 0.80 34.99  ? 98  VAL F CA    1 
ATOM   14695 C  C     A VAL C 3 98  ? 61.289  -22.283 -14.320 0.20 33.07  ? 98  VAL F C     1 
ATOM   14696 C  C     B VAL C 3 98  ? 61.155  -22.371 -14.306 0.80 32.93  ? 98  VAL F C     1 
ATOM   14697 O  O     A VAL C 3 98  ? 62.422  -22.037 -14.754 0.20 34.08  ? 98  VAL F O     1 
ATOM   14698 O  O     B VAL C 3 98  ? 62.308  -22.139 -14.695 0.80 34.20  ? 98  VAL F O     1 
ATOM   14699 C  CB    A VAL C 3 98  ? 59.787  -23.833 -15.651 0.20 34.79  ? 98  VAL F CB    1 
ATOM   14700 C  CB    B VAL C 3 98  ? 59.670  -23.903 -15.674 0.80 34.62  ? 98  VAL F CB    1 
ATOM   14701 C  CG1   A VAL C 3 98  ? 60.492  -23.334 -16.904 0.20 37.45  ? 98  VAL F CG1   1 
ATOM   14702 C  CG1   B VAL C 3 98  ? 60.337  -23.248 -16.875 0.80 37.79  ? 98  VAL F CG1   1 
ATOM   14703 C  CG2   A VAL C 3 98  ? 59.361  -25.283 -15.821 0.20 39.01  ? 98  VAL F CG2   1 
ATOM   14704 C  CG2   B VAL C 3 98  ? 59.382  -25.369 -15.950 0.80 39.49  ? 98  VAL F CG2   1 
ATOM   14705 N  N     A LEU C 3 99  ? 60.536  -21.345 -13.741 0.20 32.34  ? 99  LEU F N     1 
ATOM   14706 N  N     B LEU C 3 99  ? 60.384  -21.418 -13.774 0.80 32.64  ? 99  LEU F N     1 
ATOM   14707 C  CA    A LEU C 3 99  ? 61.038  -19.984 -13.579 0.20 28.85  ? 99  LEU F CA    1 
ATOM   14708 C  CA    B LEU C 3 99  ? 60.884  -20.056 -13.625 0.80 28.11  ? 99  LEU F CA    1 
ATOM   14709 C  C     A LEU C 3 99  ? 62.239  -19.950 -12.643 0.20 32.91  ? 99  LEU F C     1 
ATOM   14710 C  C     B LEU C 3 99  ? 62.079  -20.011 -12.683 0.80 32.93  ? 99  LEU F C     1 
ATOM   14711 O  O     A LEU C 3 99  ? 63.255  -19.308 -12.938 0.20 34.19  ? 99  LEU F O     1 
ATOM   14712 O  O     B LEU C 3 99  ? 63.074  -19.325 -12.958 0.80 35.05  ? 99  LEU F O     1 
ATOM   14713 C  CB    A LEU C 3 99  ? 59.922  -19.075 -13.061 0.20 25.92  ? 99  LEU F CB    1 
ATOM   14714 C  CB    B LEU C 3 99  ? 59.769  -19.129 -13.125 0.80 25.07  ? 99  LEU F CB    1 
ATOM   14715 C  CG    A LEU C 3 99  ? 58.821  -18.749 -14.067 0.20 24.70  ? 99  LEU F CG    1 
ATOM   14716 C  CG    B LEU C 3 99  ? 58.654  -18.811 -14.116 0.80 24.10  ? 99  LEU F CG    1 
ATOM   14717 C  CD1   A LEU C 3 99  ? 57.622  -18.138 -13.365 0.20 29.19  ? 99  LEU F CD1   1 
ATOM   14718 C  CD1   B LEU C 3 99  ? 57.636  -17.830 -13.521 0.80 29.68  ? 99  LEU F CD1   1 
ATOM   14719 C  CD2   A LEU C 3 99  ? 59.354  -17.805 -15.128 0.20 25.46  ? 99  LEU F CD2   1 
ATOM   14720 C  CD2   B LEU C 3 99  ? 59.258  -18.243 -15.381 0.80 26.60  ? 99  LEU F CD2   1 
ATOM   14721 N  N     A LEU C 3 100 ? 62.143  -20.645 -11.507 0.20 34.21  ? 100 LEU F N     1 
ATOM   14722 N  N     B LEU C 3 100 ? 62.010  -20.754 -11.575 0.80 34.69  ? 100 LEU F N     1 
ATOM   14723 C  CA    A LEU C 3 100 ? 63.252  -20.678 -10.560 0.20 34.52  ? 100 LEU F CA    1 
ATOM   14724 C  CA    B LEU C 3 100 ? 63.128  -20.797 -10.638 0.80 34.72  ? 100 LEU F CA    1 
ATOM   14725 C  C     A LEU C 3 100 ? 64.477  -21.366 -11.148 0.20 33.84  ? 100 LEU F C     1 
ATOM   14726 C  C     B LEU C 3 100 ? 64.340  -21.483 -11.247 0.80 34.28  ? 100 LEU F C     1 
ATOM   14727 O  O     A LEU C 3 100 ? 65.609  -21.021 -10.791 0.20 32.02  ? 100 LEU F O     1 
ATOM   14728 O  O     B LEU C 3 100 ? 65.481  -21.065 -11.013 0.80 31.69  ? 100 LEU F O     1 
ATOM   14729 C  CB    A LEU C 3 100 ? 62.819  -21.374 -9.271  0.20 36.45  ? 100 LEU F CB    1 
ATOM   14730 C  CB    B LEU C 3 100 ? 62.714  -21.509 -9.357  0.80 36.93  ? 100 LEU F CB    1 
ATOM   14731 C  CG    A LEU C 3 100 ? 61.731  -20.655 -8.474  0.20 31.89  ? 100 LEU F CG    1 
ATOM   14732 C  CG    B LEU C 3 100 ? 61.751  -20.719 -8.476  0.80 31.81  ? 100 LEU F CG    1 
ATOM   14733 C  CD1   A LEU C 3 100 ? 61.212  -21.542 -7.357  0.20 38.05  ? 100 LEU F CD1   1 
ATOM   14734 C  CD1   B LEU C 3 100 ? 61.072  -21.665 -7.512  0.80 38.54  ? 100 LEU F CD1   1 
ATOM   14735 C  CD2   A LEU C 3 100 ? 62.259  -19.343 -7.917  0.20 33.51  ? 100 LEU F CD2   1 
ATOM   14736 C  CD2   B LEU C 3 100 ? 62.505  -19.629 -7.737  0.80 34.09  ? 100 LEU F CD2   1 
ATOM   14737 N  N     A LYS C 3 101 ? 64.276  -22.330 -12.049 0.20 32.16  ? 101 LYS F N     1 
ATOM   14738 N  N     B LYS C 3 101 ? 64.113  -22.541 -12.024 0.80 31.06  ? 101 LYS F N     1 
ATOM   14739 C  CA    A LYS C 3 101 ? 65.411  -23.003 -12.673 0.20 32.87  ? 101 LYS F CA    1 
ATOM   14740 C  CA    B LYS C 3 101 ? 65.221  -23.228 -12.674 0.80 32.48  ? 101 LYS F CA    1 
ATOM   14741 C  C     A LYS C 3 101 ? 66.243  -22.032 -13.502 0.20 34.15  ? 101 LYS F C     1 
ATOM   14742 C  C     B LYS C 3 101 ? 65.909  -22.359 -13.723 0.80 36.52  ? 101 LYS F C     1 
ATOM   14743 O  O     A LYS C 3 101 ? 67.479  -22.085 -13.478 0.20 29.13  ? 101 LYS F O     1 
ATOM   14744 O  O     B LYS C 3 101 ? 67.021  -22.692 -14.148 0.80 33.86  ? 101 LYS F O     1 
ATOM   14745 C  CB    A LYS C 3 101 ? 64.920  -24.169 -13.533 0.20 36.01  ? 101 LYS F CB    1 
ATOM   14746 C  CB    B LYS C 3 101 ? 64.728  -24.528 -13.317 0.80 34.43  ? 101 LYS F CB    1 
ATOM   14747 C  CG    A LYS C 3 101 ? 66.035  -25.003 -14.151 0.20 39.14  ? 101 LYS F CG    1 
ATOM   14748 C  CG    B LYS C 3 101 ? 65.781  -25.623 -13.401 0.80 47.00  ? 101 LYS F CG    1 
ATOM   14749 C  CD    A LYS C 3 101 ? 65.495  -26.297 -14.742 0.20 46.25  ? 101 LYS F CD    1 
ATOM   14750 C  CD    B LYS C 3 101 ? 65.397  -26.708 -14.403 0.80 46.78  ? 101 LYS F CD    1 
ATOM   14751 C  CE    A LYS C 3 101 ? 66.623  -27.194 -15.229 0.20 47.82  ? 101 LYS F CE    1 
ATOM   14752 C  CE    B LYS C 3 101 ? 65.761  -26.298 -15.826 0.80 55.46  ? 101 LYS F CE    1 
ATOM   14753 N  NZ    A LYS C 3 101 ? 66.120  -28.505 -15.726 0.20 47.44  ? 101 LYS F NZ    1 
ATOM   14754 N  NZ    B LYS C 3 101 ? 65.695  -27.440 -16.788 0.80 54.80  ? 101 LYS F NZ    1 
ATOM   14755 N  N     A HIS C 3 102 ? 65.586  -21.137 -14.242 0.20 32.51  ? 102 HIS F N     1 
ATOM   14756 N  N     B HIS C 3 102 ? 65.277  -21.262 -14.156 0.80 31.27  ? 102 HIS F N     1 
ATOM   14757 C  CA    A HIS C 3 102 ? 66.290  -20.150 -15.053 0.20 34.15  ? 102 HIS F CA    1 
ATOM   14758 C  CA    B HIS C 3 102 ? 65.847  -20.375 -15.162 0.80 35.17  ? 102 HIS F CA    1 
ATOM   14759 C  C     A HIS C 3 102 ? 66.758  -18.941 -14.255 0.20 30.68  ? 102 HIS F C     1 
ATOM   14760 C  C     B HIS C 3 102 ? 66.167  -18.982 -14.622 0.80 30.83  ? 102 HIS F C     1 
ATOM   14761 O  O     A HIS C 3 102 ? 67.331  -18.015 -14.839 0.20 23.43  ? 102 HIS F O     1 
ATOM   14762 O  O     B HIS C 3 102 ? 66.271  -18.031 -15.401 0.80 31.24  ? 102 HIS F O     1 
ATOM   14763 C  CB    A HIS C 3 102 ? 65.401  -19.691 -16.215 0.20 34.12  ? 102 HIS F CB    1 
ATOM   14764 C  CB    B HIS C 3 102 ? 64.919  -20.288 -16.373 0.80 35.23  ? 102 HIS F CB    1 
ATOM   14765 C  CG    A HIS C 3 102 ? 65.156  -20.750 -17.244 0.20 38.84  ? 102 HIS F CG    1 
ATOM   14766 C  CG    B HIS C 3 102 ? 64.985  -21.496 -17.253 0.80 42.37  ? 102 HIS F CG    1 
ATOM   14767 N  ND1   A HIS C 3 102 ? 64.290  -21.802 -17.037 0.20 39.07  ? 102 HIS F ND1   1 
ATOM   14768 N  ND1   B HIS C 3 102 ? 64.089  -22.540 -17.158 0.80 44.58  ? 102 HIS F ND1   1 
ATOM   14769 C  CD2   A HIS C 3 102 ? 65.672  -20.924 -18.484 0.20 37.32  ? 102 HIS F CD2   1 
ATOM   14770 C  CD2   B HIS C 3 102 ? 65.864  -21.842 -18.226 0.80 38.90  ? 102 HIS F CD2   1 
ATOM   14771 C  CE1   A HIS C 3 102 ? 64.277  -22.575 -18.109 0.20 43.29  ? 102 HIS F CE1   1 
ATOM   14772 C  CE1   B HIS C 3 102 ? 64.403  -23.470 -18.043 0.80 45.95  ? 102 HIS F CE1   1 
ATOM   14773 N  NE2   A HIS C 3 102 ? 65.109  -22.065 -19.000 0.20 43.00  ? 102 HIS F NE2   1 
ATOM   14774 N  NE2   B HIS C 3 102 ? 65.478  -23.072 -18.702 0.80 49.55  ? 102 HIS F NE2   1 
ATOM   14775 N  N     A GLY C 3 103 ? 66.531  -18.925 -12.952 0.20 28.50  ? 103 GLY F N     1 
ATOM   14776 N  N     B GLY C 3 103 ? 66.328  -18.842 -13.311 0.80 26.93  ? 103 GLY F N     1 
ATOM   14777 C  CA    A GLY C 3 103 ? 66.983  -17.849 -12.111 0.20 27.21  ? 103 GLY F CA    1 
ATOM   14778 C  CA    B GLY C 3 103 ? 66.951  -17.668 -12.741 0.80 24.34  ? 103 GLY F CA    1 
ATOM   14779 C  C     A GLY C 3 103 ? 66.004  -16.720 -11.883 0.20 27.52  ? 103 GLY F C     1 
ATOM   14780 C  C     B GLY C 3 103 ? 66.043  -16.641 -12.105 0.80 26.76  ? 103 GLY F C     1 
ATOM   14781 O  O     A GLY C 3 103 ? 66.442  -15.574 -11.728 0.20 28.92  ? 103 GLY F O     1 
ATOM   14782 O  O     B GLY C 3 103 ? 66.523  -15.546 -11.771 0.80 28.53  ? 103 GLY F O     1 
ATOM   14783 N  N     A ALA C 3 104 ? 64.702  -16.997 -11.862 0.20 31.42  ? 104 ALA F N     1 
ATOM   14784 N  N     B ALA C 3 104 ? 64.761  -16.946 -11.919 0.80 31.50  ? 104 ALA F N     1 
ATOM   14785 C  CA    A ALA C 3 104 ? 63.740  -15.966 -11.498 0.20 31.22  ? 104 ALA F CA    1 
ATOM   14786 C  CA    B ALA C 3 104 ? 63.852  -15.982 -11.307 0.80 31.64  ? 104 ALA F CA    1 
ATOM   14787 C  C     A ALA C 3 104 ? 63.962  -15.533 -10.055 0.20 32.23  ? 104 ALA F C     1 
ATOM   14788 C  C     B ALA C 3 104 ? 64.303  -15.628 -9.892  0.80 33.48  ? 104 ALA F C     1 
ATOM   14789 O  O     A ALA C 3 104 ? 64.227  -16.357 -9.176  0.20 30.36  ? 104 ALA F O     1 
ATOM   14790 O  O     B ALA C 3 104 ? 64.817  -16.472 -9.153  0.80 26.61  ? 104 ALA F O     1 
ATOM   14791 C  CB    A ALA C 3 104 ? 62.308  -16.474 -11.680 0.20 31.26  ? 104 ALA F CB    1 
ATOM   14792 C  CB    B ALA C 3 104 ? 62.423  -16.530 -11.287 0.80 32.43  ? 104 ALA F CB    1 
ATOM   14793 N  N     A ASP C 3 105 ? 63.868  -14.228 -9.818  0.20 30.51  ? 105 ASP F N     1 
ATOM   14794 N  N     B ASP C 3 105 ? 64.130  -14.359 -9.535  0.80 28.64  ? 105 ASP F N     1 
ATOM   14795 C  CA    A ASP C 3 105 ? 64.063  -13.688 -8.480  0.20 31.58  ? 105 ASP F CA    1 
ATOM   14796 C  CA    B ASP C 3 105 ? 64.460  -13.848 -8.212  0.80 32.42  ? 105 ASP F CA    1 
ATOM   14797 C  C     A ASP C 3 105 ? 62.956  -14.193 -7.561  0.20 29.78  ? 105 ASP F C     1 
ATOM   14798 C  C     B ASP C 3 105 ? 63.310  -14.198 -7.275  0.80 29.11  ? 105 ASP F C     1 
ATOM   14799 O  O     A ASP C 3 105 ? 61.777  -13.892 -7.775  0.20 30.34  ? 105 ASP F O     1 
ATOM   14800 O  O     B ASP C 3 105 ? 62.247  -13.578 -7.338  0.80 28.15  ? 105 ASP F O     1 
ATOM   14801 C  CB    A ASP C 3 105 ? 64.080  -12.162 -8.528  0.20 28.74  ? 105 ASP F CB    1 
ATOM   14802 C  CB    B ASP C 3 105 ? 64.682  -12.339 -8.277  0.80 28.01  ? 105 ASP F CB    1 
ATOM   14803 C  CG    A ASP C 3 105 ? 64.577  -11.539 -7.235  0.20 32.70  ? 105 ASP F CG    1 
ATOM   14804 C  CG    B ASP C 3 105 ? 64.969  -11.712 -6.913  0.80 34.25  ? 105 ASP F CG    1 
ATOM   14805 O  OD1   A ASP C 3 105 ? 64.914  -12.289 -6.292  0.20 34.26  ? 105 ASP F OD1   1 
ATOM   14806 O  OD1   B ASP C 3 105 ? 64.930  -12.417 -5.879  0.80 34.82  ? 105 ASP F OD1   1 
ATOM   14807 O  OD2   A ASP C 3 105 ? 64.633  -10.292 -7.164  0.20 36.79  ? 105 ASP F OD2   1 
ATOM   14808 O  OD2   B ASP C 3 105 ? 65.239  -10.491 -6.882  0.80 42.85  ? 105 ASP F OD2   1 
ATOM   14809 N  N     A VAL C 3 106 ? 63.337  -14.970 -6.544  0.20 29.20  ? 106 VAL F N     1 
ATOM   14810 N  N     B VAL C 3 106 ? 63.540  -15.174 -6.396  0.80 28.19  ? 106 VAL F N     1 
ATOM   14811 C  CA    A VAL C 3 106 ? 62.356  -15.541 -5.626  0.20 32.49  ? 106 VAL F CA    1 
ATOM   14812 C  CA    B VAL C 3 106 ? 62.493  -15.676 -5.506  0.80 33.15  ? 106 VAL F CA    1 
ATOM   14813 C  C     A VAL C 3 106 ? 61.877  -14.526 -4.595  0.20 32.16  ? 106 VAL F C     1 
ATOM   14814 C  C     B VAL C 3 106 ? 61.951  -14.571 -4.604  0.80 32.22  ? 106 VAL F C     1 
ATOM   14815 O  O     A VAL C 3 106 ? 60.760  -14.657 -4.076  0.20 31.97  ? 106 VAL F O     1 
ATOM   14816 O  O     B VAL C 3 106 ? 60.796  -14.631 -4.152  0.80 32.16  ? 106 VAL F O     1 
ATOM   14817 C  CB    A VAL C 3 106 ? 62.941  -16.788 -4.936  0.20 31.96  ? 106 VAL F CB    1 
ATOM   14818 C  CB    B VAL C 3 106 ? 63.052  -16.862 -4.691  0.80 32.36  ? 106 VAL F CB    1 
ATOM   14819 C  CG1   A VAL C 3 106 ? 64.081  -16.404 -4.000  0.20 31.20  ? 106 VAL F CG1   1 
ATOM   14820 C  CG1   B VAL C 3 106 ? 64.243  -16.411 -3.858  0.80 30.95  ? 106 VAL F CG1   1 
ATOM   14821 C  CG2   A VAL C 3 106 ? 61.859  -17.565 -4.192  0.20 34.18  ? 106 VAL F CG2   1 
ATOM   14822 C  CG2   B VAL C 3 106 ? 61.976  -17.479 -3.802  0.80 34.40  ? 106 VAL F CG2   1 
ATOM   14823 N  N     A ASN C 3 107 ? 62.679  -13.503 -4.296  0.20 28.01  ? 107 ASN F N     1 
ATOM   14824 N  N     B ASN C 3 107 ? 62.752  -13.537 -4.347  0.80 27.63  ? 107 ASN F N     1 
ATOM   14825 C  CA    A ASN C 3 107 ? 62.327  -12.490 -3.310  0.20 32.03  ? 107 ASN F CA    1 
ATOM   14826 C  CA    B ASN C 3 107 ? 62.392  -12.472 -3.423  0.80 32.15  ? 107 ASN F CA    1 
ATOM   14827 C  C     A ASN C 3 107 ? 62.062  -11.129 -3.945  0.20 33.96  ? 107 ASN F C     1 
ATOM   14828 C  C     B ASN C 3 107 ? 62.097  -11.152 -4.132  0.80 34.88  ? 107 ASN F C     1 
ATOM   14829 O  O     A ASN C 3 107 ? 62.185  -10.101 -3.271  0.20 33.95  ? 107 ASN F O     1 
ATOM   14830 O  O     B ASN C 3 107 ? 62.160  -10.091 -3.500  0.80 34.69  ? 107 ASN F O     1 
ATOM   14831 C  CB    A ASN C 3 107 ? 63.426  -12.380 -2.252  0.20 33.46  ? 107 ASN F CB    1 
ATOM   14832 C  CB    B ASN C 3 107 ? 63.503  -12.291 -2.387  0.80 33.68  ? 107 ASN F CB    1 
ATOM   14833 C  CG    A ASN C 3 107 ? 63.586  -13.653 -1.444  0.20 32.87  ? 107 ASN F CG    1 
ATOM   14834 C  CG    B ASN C 3 107 ? 63.545  -13.424 -1.382  0.80 33.70  ? 107 ASN F CG    1 
ATOM   14835 O  OD1   A ASN C 3 107 ? 62.620  -14.385 -1.221  0.20 30.20  ? 107 ASN F OD1   1 
ATOM   14836 O  OD1   B ASN C 3 107 ? 62.502  -13.872 -0.898  0.80 28.76  ? 107 ASN F OD1   1 
ATOM   14837 N  ND2   A ASN C 3 107 ? 64.807  -13.923 -0.998  0.20 27.81  ? 107 ASN F ND2   1 
ATOM   14838 N  ND2   B ASN C 3 107 ? 64.744  -13.898 -1.063  0.80 27.56  ? 107 ASN F ND2   1 
ATOM   14839 N  N     A ALA C 3 108 ? 61.703  -11.100 -5.227  0.20 30.57  ? 108 ALA F N     1 
ATOM   14840 N  N     B ALA C 3 108 ? 61.776  -11.193 -5.429  0.80 29.36  ? 108 ALA F N     1 
ATOM   14841 C  CA    A ALA C 3 108 ? 61.361  -9.842  -5.876  0.20 30.43  ? 108 ALA F CA    1 
ATOM   14842 C  CA    B ALA C 3 108 ? 61.370  -9.981  -6.134  0.80 29.52  ? 108 ALA F CA    1 
ATOM   14843 C  C     A ALA C 3 108 ? 60.112  -9.236  -5.241  0.20 29.84  ? 108 ALA F C     1 
ATOM   14844 C  C     B ALA C 3 108 ? 60.145  -9.359  -5.458  0.80 29.98  ? 108 ALA F C     1 
ATOM   14845 O  O     A ALA C 3 108 ? 59.221  -9.945  -4.766  0.20 31.16  ? 108 ALA F O     1 
ATOM   14846 O  O     B ALA C 3 108 ? 59.260  -10.066 -4.968  0.80 31.88  ? 108 ALA F O     1 
ATOM   14847 C  CB    A ALA C 3 108 ? 61.143  -10.058 -7.374  0.20 29.03  ? 108 ALA F CB    1 
ATOM   14848 C  CB    B ALA C 3 108 ? 61.068  -10.295 -7.599  0.80 28.00  ? 108 ALA F CB    1 
ATOM   14849 N  N     A VAL C 3 109 ? 60.055  -7.905  -5.234  0.20 27.22  ? 109 VAL F N     1 
ATOM   14850 N  N     B VAL C 3 109 ? 60.101  -8.026  -5.439  0.80 26.61  ? 109 VAL F N     1 
ATOM   14851 C  CA    A VAL C 3 109 ? 58.984  -7.155  -4.589  0.20 29.88  ? 109 VAL F CA    1 
ATOM   14852 C  CA    B VAL C 3 109 ? 59.121  -7.251  -4.689  0.80 29.76  ? 109 VAL F CA    1 
ATOM   14853 C  C     A VAL C 3 109 ? 58.277  -6.301  -5.634  0.20 28.72  ? 109 VAL F C     1 
ATOM   14854 C  C     B VAL C 3 109 ? 58.386  -6.316  -5.646  0.80 28.59  ? 109 VAL F C     1 
ATOM   14855 O  O     A VAL C 3 109 ? 58.927  -5.657  -6.464  0.20 31.79  ? 109 VAL F O     1 
ATOM   14856 O  O     B VAL C 3 109 ? 59.025  -5.540  -6.366  0.80 32.10  ? 109 VAL F O     1 
ATOM   14857 C  CB    A VAL C 3 109 ? 59.528  -6.274  -3.444  0.20 31.90  ? 109 VAL F CB    1 
ATOM   14858 C  CB    B VAL C 3 109 ? 59.800  -6.442  -3.567  0.80 33.25  ? 109 VAL F CB    1 
ATOM   14859 C  CG1   A VAL C 3 109 ? 58.386  -5.625  -2.681  0.20 30.89  ? 109 VAL F CG1   1 
ATOM   14860 C  CG1   B VAL C 3 109 ? 58.809  -5.481  -2.933  0.80 30.88  ? 109 VAL F CG1   1 
ATOM   14861 C  CG2   A VAL C 3 109 ? 60.408  -7.093  -2.512  0.20 31.94  ? 109 VAL F CG2   1 
ATOM   14862 C  CG2   B VAL C 3 109 ? 60.408  -7.369  -2.529  0.80 32.28  ? 109 VAL F CG2   1 
ATOM   14863 N  N     A ASP C 3 110 ? 56.946  -6.289  -5.582  0.20 27.81  ? 110 ASP F N     1 
ATOM   14864 N  N     B ASP C 3 110 ? 57.049  -6.358  -5.625  0.80 27.28  ? 110 ASP F N     1 
ATOM   14865 C  CA    A ASP C 3 110 ? 56.127  -5.508  -6.494  0.20 25.45  ? 110 ASP F CA    1 
ATOM   14866 C  CA    B ASP C 3 110 ? 56.230  -5.506  -6.482  0.80 25.14  ? 110 ASP F CA    1 
ATOM   14867 C  C     A ASP C 3 110 ? 55.746  -4.174  -5.845  0.20 27.10  ? 110 ASP F C     1 
ATOM   14868 C  C     B ASP C 3 110 ? 55.845  -4.218  -5.741  0.80 26.66  ? 110 ASP F C     1 
ATOM   14869 O  O     A ASP C 3 110 ? 56.256  -3.804  -4.784  0.20 28.91  ? 110 ASP F O     1 
ATOM   14870 O  O     B ASP C 3 110 ? 56.293  -3.961  -4.621  0.80 29.19  ? 110 ASP F O     1 
ATOM   14871 C  CB    A ASP C 3 110 ? 54.899  -6.321  -6.919  0.20 27.78  ? 110 ASP F CB    1 
ATOM   14872 C  CB    B ASP C 3 110 ? 55.017  -6.287  -7.005  0.80 27.62  ? 110 ASP F CB    1 
ATOM   14873 C  CG    A ASP C 3 110 ? 54.131  -6.890  -5.738  0.20 29.61  ? 110 ASP F CG    1 
ATOM   14874 C  CG    B ASP C 3 110 ? 54.031  -6.689  -5.909  0.80 30.22  ? 110 ASP F CG    1 
ATOM   14875 O  OD1   A ASP C 3 110 ? 54.431  -6.514  -4.582  0.20 28.49  ? 110 ASP F OD1   1 
ATOM   14876 O  OD1   B ASP C 3 110 ? 53.923  -5.985  -4.869  0.80 27.28  ? 110 ASP F OD1   1 
ATOM   14877 O  OD2   A ASP C 3 110 ? 53.226  -7.719  -5.970  0.20 26.36  ? 110 ASP F OD2   1 
ATOM   14878 O  OD2   B ASP C 3 110 ? 53.357  -7.725  -6.094  0.80 25.64  ? 110 ASP F OD2   1 
ATOM   14879 N  N     A THR C 3 111 ? 54.833  -3.440  -6.484  0.20 26.98  ? 111 THR F N     1 
ATOM   14880 N  N     B THR C 3 111 ? 54.980  -3.402  -6.350  0.80 26.22  ? 111 THR F N     1 
ATOM   14881 C  CA    A THR C 3 111 ? 54.466  -2.114  -5.997  0.20 28.11  ? 111 THR F CA    1 
ATOM   14882 C  CA    B THR C 3 111 ? 54.727  -2.067  -5.815  0.80 25.40  ? 111 THR F CA    1 
ATOM   14883 C  C     A THR C 3 111 ? 53.578  -2.157  -4.760  0.20 32.71  ? 111 THR F C     1 
ATOM   14884 C  C     B THR C 3 111 ? 53.873  -2.093  -4.551  0.80 34.92  ? 111 THR F C     1 
ATOM   14885 O  O     A THR C 3 111 ? 53.320  -1.102  -4.170  0.20 34.22  ? 111 THR F O     1 
ATOM   14886 O  O     B THR C 3 111 ? 53.865  -1.108  -3.799  0.80 34.09  ? 111 THR F O     1 
ATOM   14887 C  CB    A THR C 3 111 ? 53.762  -1.317  -7.097  0.20 31.93  ? 111 THR F CB    1 
ATOM   14888 C  CB    B THR C 3 111 ? 54.076  -1.181  -6.887  0.80 31.36  ? 111 THR F CB    1 
ATOM   14889 O  OG1   A THR C 3 111 ? 53.479  0.006   -6.624  0.20 37.37  ? 111 THR F OG1   1 
ATOM   14890 O  OG1   B THR C 3 111 ? 54.061  0.178   -6.440  0.80 44.40  ? 111 THR F OG1   1 
ATOM   14891 C  CG2   A THR C 3 111 ? 52.458  -1.986  -7.482  0.20 33.16  ? 111 THR F CG2   1 
ATOM   14892 C  CG2   B THR C 3 111 ? 52.646  -1.604  -7.136  0.80 31.94  ? 111 THR F CG2   1 
ATOM   14893 N  N     A TRP C 3 112 ? 53.107  -3.335  -4.353  0.20 29.93  ? 112 TRP F N     1 
ATOM   14894 N  N     B TRP C 3 112 ? 53.178  -3.194  -4.279  0.80 29.71  ? 112 TRP F N     1 
ATOM   14895 C  CA    A TRP C 3 112 ? 52.313  -3.475  -3.141  0.20 34.75  ? 112 TRP F CA    1 
ATOM   14896 C  CA    B TRP C 3 112 ? 52.519  -3.367  -2.994  0.80 36.09  ? 112 TRP F CA    1 
ATOM   14897 C  C     A TRP C 3 112 ? 53.084  -4.132  -2.006  0.20 34.98  ? 112 TRP F C     1 
ATOM   14898 C  C     B TRP C 3 112 ? 53.452  -3.976  -1.960  0.80 37.62  ? 112 TRP F C     1 
ATOM   14899 O  O     A TRP C 3 112 ? 52.510  -4.360  -0.936  0.20 31.97  ? 112 TRP F O     1 
ATOM   14900 O  O     B TRP C 3 112 ? 53.017  -4.299  -0.844  0.80 30.83  ? 112 TRP F O     1 
ATOM   14901 C  CB    A TRP C 3 112 ? 51.037  -4.272  -3.432  0.20 30.90  ? 112 TRP F CB    1 
ATOM   14902 C  CB    B TRP C 3 112 ? 51.257  -4.216  -3.168  0.80 29.64  ? 112 TRP F CB    1 
ATOM   14903 C  CG    A TRP C 3 112 ? 50.132  -3.595  -4.417  0.20 32.12  ? 112 TRP F CG    1 
ATOM   14904 C  CG    B TRP C 3 112 ? 50.324  -3.620  -4.197  0.80 31.85  ? 112 TRP F CG    1 
ATOM   14905 C  CD1   A TRP C 3 112 ? 49.293  -2.545  -4.174  0.20 32.98  ? 112 TRP F CD1   1 
ATOM   14906 C  CD1   B TRP C 3 112 ? 49.423  -2.606  -4.000  0.80 32.91  ? 112 TRP F CD1   1 
ATOM   14907 C  CD2   A TRP C 3 112 ? 49.974  -3.921  -5.803  0.20 33.44  ? 112 TRP F CD2   1 
ATOM   14908 C  CD2   B TRP C 3 112 ? 50.220  -3.982  -5.581  0.80 34.28  ? 112 TRP F CD2   1 
ATOM   14909 N  NE1   A TRP C 3 112 ? 48.623  -2.198  -5.323  0.20 34.08  ? 112 TRP F NE1   1 
ATOM   14910 N  NE1   B TRP C 3 112 ? 48.758  -2.328  -5.172  0.80 34.39  ? 112 TRP F NE1   1 
ATOM   14911 C  CE2   A TRP C 3 112 ? 49.024  -3.027  -6.337  0.20 33.93  ? 112 TRP F CE2   1 
ATOM   14912 C  CE2   B TRP C 3 112 ? 49.229  -3.157  -6.157  0.80 34.68  ? 112 TRP F CE2   1 
ATOM   14913 C  CE3   A TRP C 3 112 ? 50.545  -4.882  -6.645  0.20 32.30  ? 112 TRP F CE3   1 
ATOM   14914 C  CE3   B TRP C 3 112 ? 50.867  -4.928  -6.389  0.80 31.52  ? 112 TRP F CE3   1 
ATOM   14915 C  CZ2   A TRP C 3 112 ? 48.631  -3.065  -7.674  0.20 34.83  ? 112 TRP F CZ2   1 
ATOM   14916 C  CZ2   B TRP C 3 112 ? 48.870  -3.249  -7.500  0.80 35.11  ? 112 TRP F CZ2   1 
ATOM   14917 C  CZ3   A TRP C 3 112 ? 50.155  -4.917  -7.973  0.20 34.03  ? 112 TRP F CZ3   1 
ATOM   14918 C  CZ3   B TRP C 3 112 ? 50.509  -5.016  -7.727  0.80 35.10  ? 112 TRP F CZ3   1 
ATOM   14919 C  CH2   A TRP C 3 112 ? 49.206  -4.016  -8.473  0.20 35.37  ? 112 TRP F CH2   1 
ATOM   14920 C  CH2   B TRP C 3 112 ? 49.516  -4.184  -8.266  0.80 36.93  ? 112 TRP F CH2   1 
ATOM   14921 N  N     A GLY C 3 113 ? 54.365  -4.434  -2.207  0.20 31.29  ? 113 GLY F N     1 
ATOM   14922 N  N     B GLY C 3 113 ? 54.735  -4.099  -2.295  0.80 31.27  ? 113 GLY F N     1 
ATOM   14923 C  CA    A GLY C 3 113 ? 55.180  -5.052  -1.185  0.20 30.36  ? 113 GLY F CA    1 
ATOM   14924 C  CA    B GLY C 3 113 ? 55.691  -4.746  -1.426  0.80 26.90  ? 113 GLY F CA    1 
ATOM   14925 C  C     A GLY C 3 113 ? 55.141  -6.563  -1.152  0.20 30.60  ? 113 GLY F C     1 
ATOM   14926 C  C     B GLY C 3 113 ? 55.559  -6.249  -1.357  0.80 32.29  ? 113 GLY F C     1 
ATOM   14927 O  O     A GLY C 3 113 ? 55.862  -7.166  -0.347  0.20 30.61  ? 113 GLY F O     1 
ATOM   14928 O  O     B GLY C 3 113 ? 56.255  -6.874  -0.557  0.80 29.58  ? 113 GLY F O     1 
ATOM   14929 N  N     A ASP C 3 114 ? 54.334  -7.197  -1.998  0.20 28.84  ? 114 ASP F N     1 
ATOM   14930 N  N     B ASP C 3 114 ? 54.687  -6.849  -2.167  0.80 30.52  ? 114 ASP F N     1 
ATOM   14931 C  CA    A ASP C 3 114 ? 54.199  -8.645  -1.968  0.20 25.88  ? 114 ASP F CA    1 
ATOM   14932 C  CA    B ASP C 3 114 ? 54.486  -8.292  -2.132  0.80 27.63  ? 114 ASP F CA    1 
ATOM   14933 C  C     A ASP C 3 114 ? 55.375  -9.326  -2.656  0.20 28.40  ? 114 ASP F C     1 
ATOM   14934 C  C     B ASP C 3 114 ? 55.597  -9.018  -2.875  0.80 29.21  ? 114 ASP F C     1 
ATOM   14935 O  O     A ASP C 3 114 ? 56.001  -8.776  -3.566  0.20 29.41  ? 114 ASP F O     1 
ATOM   14936 O  O     B ASP C 3 114 ? 56.015  -8.610  -3.965  0.80 29.74  ? 114 ASP F O     1 
ATOM   14937 C  CB    A ASP C 3 114 ? 52.890  -9.077  -2.627  0.20 25.16  ? 114 ASP F CB    1 
ATOM   14938 C  CB    B ASP C 3 114 ? 53.135  -8.663  -2.740  0.80 24.86  ? 114 ASP F CB    1 
ATOM   14939 C  CG    A ASP C 3 114 ? 51.697  -8.909  -1.708  0.20 25.79  ? 114 ASP F CG    1 
ATOM   14940 C  CG    B ASP C 3 114 ? 51.983  -8.312  -1.827  0.80 24.03  ? 114 ASP F CG    1 
ATOM   14941 O  OD1   A ASP C 3 114 ? 51.858  -9.145  -0.491  0.20 26.57  ? 114 ASP F OD1   1 
ATOM   14942 O  OD1   B ASP C 3 114 ? 52.141  -8.514  -0.607  0.80 24.55  ? 114 ASP F OD1   1 
ATOM   14943 O  OD2   A ASP C 3 114 ? 50.606  -8.544  -2.196  0.20 26.44  ? 114 ASP F OD2   1 
ATOM   14944 O  OD2   B ASP C 3 114 ? 50.946  -7.823  -2.317  0.80 29.06  ? 114 ASP F OD2   1 
ATOM   14945 N  N     A THR C 3 115 ? 55.670  -10.536 -2.199  0.20 27.03  ? 115 THR F N     1 
ATOM   14946 N  N     B THR C 3 115 ? 56.071  -10.094 -2.267  0.80 29.04  ? 115 THR F N     1 
ATOM   14947 C  CA    A THR C 3 115 ? 56.666  -11.431 -2.758  0.20 28.14  ? 115 THR F CA    1 
ATOM   14948 C  CA    B THR C 3 115 ? 56.907  -11.095 -2.911  0.80 25.39  ? 115 THR F CA    1 
ATOM   14949 C  C     A THR C 3 115 ? 55.965  -12.684 -3.274  0.20 28.21  ? 115 THR F C     1 
ATOM   14950 C  C     B THR C 3 115 ? 56.020  -12.214 -3.433  0.80 31.49  ? 115 THR F C     1 
ATOM   14951 O  O     A THR C 3 115 ? 54.799  -12.929 -2.938  0.20 27.15  ? 115 THR F O     1 
ATOM   14952 O  O     B THR C 3 115 ? 54.825  -12.268 -3.114  0.80 25.66  ? 115 THR F O     1 
ATOM   14953 C  CB    A THR C 3 115 ? 57.711  -11.813 -1.697  0.20 28.51  ? 115 THR F CB    1 
ATOM   14954 C  CB    B THR C 3 115 ? 57.918  -11.638 -1.898  0.80 28.01  ? 115 THR F CB    1 
ATOM   14955 O  OG1   A THR C 3 115 ? 57.083  -12.592 -0.670  0.20 26.59  ? 115 THR F OG1   1 
ATOM   14956 O  OG1   B THR C 3 115 ? 57.220  -12.393 -0.894  0.80 27.10  ? 115 THR F OG1   1 
ATOM   14957 C  CG2   A THR C 3 115 ? 58.326  -10.566 -1.071  0.20 28.51  ? 115 THR F CG2   1 
ATOM   14958 C  CG2   B THR C 3 115 ? 58.665  -10.505 -1.224  0.80 29.08  ? 115 THR F CG2   1 
ATOM   14959 N  N     A PRO C 3 116 ? 56.641  -13.502 -4.106  0.20 26.35  ? 116 PRO F N     1 
ATOM   14960 N  N     B PRO C 3 116 ? 56.559  -13.122 -4.255  0.80 25.60  ? 116 PRO F N     1 
ATOM   14961 C  CA    A PRO C 3 116 ? 56.010  -14.745 -4.580  0.20 25.46  ? 116 PRO F CA    1 
ATOM   14962 C  CA    B PRO C 3 116 ? 55.768  -14.303 -4.645  0.80 21.39  ? 116 PRO F CA    1 
ATOM   14963 C  C     A PRO C 3 116 ? 55.499  -15.627 -3.449  0.20 25.28  ? 116 PRO F C     1 
ATOM   14964 C  C     B PRO C 3 116 ? 55.245  -15.095 -3.451  0.80 26.51  ? 116 PRO F C     1 
ATOM   14965 O  O     A PRO C 3 116 ? 54.599  -16.448 -3.648  0.20 27.08  ? 116 PRO F O     1 
ATOM   14966 O  O     B PRO C 3 116 ? 54.098  -15.562 -3.476  0.80 27.59  ? 116 PRO F O     1 
ATOM   14967 C  CB    A PRO C 3 116 ? 57.140  -15.434 -5.353  0.20 27.30  ? 116 PRO F CB    1 
ATOM   14968 C  CB    B PRO C 3 116 ? 56.763  -15.118 -5.484  0.80 30.45  ? 116 PRO F CB    1 
ATOM   14969 C  CG    A PRO C 3 116 ? 57.976  -14.310 -5.847  0.20 26.80  ? 116 PRO F CG    1 
ATOM   14970 C  CG    B PRO C 3 116 ? 57.636  -14.063 -6.117  0.80 25.71  ? 116 PRO F CG    1 
ATOM   14971 C  CD    A PRO C 3 116 ? 57.942  -13.266 -4.764  0.20 27.28  ? 116 PRO F CD    1 
ATOM   14972 C  CD    B PRO C 3 116 ? 57.823  -13.030 -5.025  0.80 27.06  ? 116 PRO F CD    1 
ATOM   14973 N  N     A LEU C 3 117 ? 56.068  -15.457 -2.256  0.20 27.16  ? 117 LEU F N     1 
ATOM   14974 N  N     B LEU C 3 117 ? 56.059  -15.233 -2.400  0.80 26.47  ? 117 LEU F N     1 
ATOM   14975 C  CA    A LEU C 3 117 ? 55.623  -16.220 -1.096  0.20 27.11  ? 117 LEU F CA    1 
ATOM   14976 C  CA    B LEU C 3 117 ? 55.648  -15.965 -1.200  0.80 27.81  ? 117 LEU F CA    1 
ATOM   14977 C  C     A LEU C 3 117 ? 54.301  -15.694 -0.547  0.20 27.31  ? 117 LEU F C     1 
ATOM   14978 C  C     B LEU C 3 117 ? 54.386  -15.363 -0.587  0.80 27.56  ? 117 LEU F C     1 
ATOM   14979 O  O     A LEU C 3 117 ? 53.469  -16.477 -0.074  0.20 26.17  ? 117 LEU F O     1 
ATOM   14980 O  O     B LEU C 3 117 ? 53.445  -16.090 -0.248  0.80 26.56  ? 117 LEU F O     1 
ATOM   14981 C  CB    A LEU C 3 117 ? 56.706  -16.196 -0.017  0.20 30.64  ? 117 LEU F CB    1 
ATOM   14982 C  CB    B LEU C 3 117 ? 56.796  -15.988 -0.182  0.80 30.65  ? 117 LEU F CB    1 
ATOM   14983 C  CG    A LEU C 3 117 ? 56.403  -16.956 1.276   0.20 26.92  ? 117 LEU F CG    1 
ATOM   14984 C  CG    B LEU C 3 117 ? 56.589  -16.721 1.161   0.80 27.63  ? 117 LEU F CG    1 
ATOM   14985 C  CD1   A LEU C 3 117 ? 56.039  -18.399 0.970   0.20 29.07  ? 117 LEU F CD1   1 
ATOM   14986 C  CD1   B LEU C 3 117 ? 56.301  -18.188 0.940   0.80 29.02  ? 117 LEU F CD1   1 
ATOM   14987 C  CD2   A LEU C 3 117 ? 57.584  -16.880 2.235   0.20 29.57  ? 117 LEU F CD2   1 
ATOM   14988 C  CD2   B LEU C 3 117 ? 57.791  -16.543 2.101   0.80 28.71  ? 117 LEU F CD2   1 
ATOM   14989 N  N     A HIS C 3 118 ? 54.085  -14.376 -0.602  0.20 27.85  ? 118 HIS F N     1 
ATOM   14990 N  N     B HIS C 3 118 ? 54.345  -14.031 -0.439  0.80 28.61  ? 118 HIS F N     1 
ATOM   14991 C  CA    A HIS C 3 118 ? 52.837  -13.808 -0.097  0.20 25.66  ? 118 HIS F CA    1 
ATOM   14992 C  CA    B HIS C 3 118 ? 53.136  -13.380 0.070   0.80 24.04  ? 118 HIS F CA    1 
ATOM   14993 C  C     A HIS C 3 118 ? 51.649  -14.234 -0.951  0.20 27.69  ? 118 HIS F C     1 
ATOM   14994 C  C     B HIS C 3 118 ? 51.906  -13.800 -0.722  0.80 29.67  ? 118 HIS F C     1 
ATOM   14995 O  O     A HIS C 3 118 ? 50.643  -14.731 -0.430  0.20 24.91  ? 118 HIS F O     1 
ATOM   14996 O  O     B HIS C 3 118 ? 50.850  -14.079 -0.146  0.80 24.55  ? 118 HIS F O     1 
ATOM   14997 C  CB    A HIS C 3 118 ? 52.929  -12.281 -0.045  0.20 23.54  ? 118 HIS F CB    1 
ATOM   14998 C  CB    B HIS C 3 118 ? 53.256  -11.857 0.011   0.80 22.92  ? 118 HIS F CB    1 
ATOM   14999 C  CG    A HIS C 3 118 ? 53.878  -11.760 0.988   0.20 27.50  ? 118 HIS F CG    1 
ATOM   15000 C  CG    B HIS C 3 118 ? 54.136  -11.248 1.059   0.80 30.32  ? 118 HIS F CG    1 
ATOM   15001 N  ND1   A HIS C 3 118 ? 55.204  -11.495 0.717   0.20 27.92  ? 118 HIS F ND1   1 
ATOM   15002 N  ND1   B HIS C 3 118 ? 55.450  -10.904 0.821   0.80 28.80  ? 118 HIS F ND1   1 
ATOM   15003 C  CD2   A HIS C 3 118 ? 53.691  -11.441 2.291   0.20 26.76  ? 118 HIS F CD2   1 
ATOM   15004 C  CD2   B HIS C 3 118 ? 53.870  -10.863 2.330   0.80 23.96  ? 118 HIS F CD2   1 
ATOM   15005 C  CE1   A HIS C 3 118 ? 55.793  -11.041 1.809   0.20 28.66  ? 118 HIS F CE1   1 
ATOM   15006 C  CE1   B HIS C 3 118 ? 55.964  -10.362 1.912   0.80 27.33  ? 118 HIS F CE1   1 
ATOM   15007 N  NE2   A HIS C 3 118 ? 54.895  -10.996 2.778   0.20 28.43  ? 118 HIS F NE2   1 
ATOM   15008 N  NE2   B HIS C 3 118 ? 55.020  -10.316 2.839   0.80 26.56  ? 118 HIS F NE2   1 
ATOM   15009 N  N     A LEU C 3 119 ? 51.743  -14.036 -2.270  0.20 24.48  ? 119 LEU F N     1 
ATOM   15010 N  N     B LEU C 3 119 ? 52.020  -13.834 -2.051  0.80 25.47  ? 119 LEU F N     1 
ATOM   15011 C  CA    A LEU C 3 119 ? 50.630  -14.373 -3.152  0.20 26.04  ? 119 LEU F CA    1 
ATOM   15012 C  CA    B LEU C 3 119 ? 50.852  -14.059 -2.894  0.80 24.63  ? 119 LEU F CA    1 
ATOM   15013 C  C     A LEU C 3 119 ? 50.314  -15.862 -3.109  0.20 27.05  ? 119 LEU F C     1 
ATOM   15014 C  C     B LEU C 3 119 ? 50.405  -15.513 -2.832  0.80 26.25  ? 119 LEU F C     1 
ATOM   15015 O  O     A LEU C 3 119 ? 49.152  -16.254 -3.270  0.20 28.39  ? 119 LEU F O     1 
ATOM   15016 O  O     B LEU C 3 119 ? 49.201  -15.794 -2.779  0.80 29.11  ? 119 LEU F O     1 
ATOM   15017 C  CB    A LEU C 3 119 ? 50.942  -13.932 -4.586  0.20 25.20  ? 119 LEU F CB    1 
ATOM   15018 C  CB    B LEU C 3 119 ? 51.158  -13.634 -4.341  0.80 25.78  ? 119 LEU F CB    1 
ATOM   15019 C  CG    A LEU C 3 119 ? 51.175  -12.435 -4.822  0.20 23.81  ? 119 LEU F CG    1 
ATOM   15020 C  CG    B LEU C 3 119 ? 51.429  -12.135 -4.529  0.80 22.90  ? 119 LEU F CG    1 
ATOM   15021 C  CD1   A LEU C 3 119 ? 51.555  -12.163 -6.271  0.20 27.11  ? 119 LEU F CD1   1 
ATOM   15022 C  CD1   B LEU C 3 119 ? 51.656  -11.741 -5.996  0.80 26.48  ? 119 LEU F CD1   1 
ATOM   15023 C  CD2   A LEU C 3 119 ? 49.953  -11.618 -4.438  0.20 23.96  ? 119 LEU F CD2   1 
ATOM   15024 C  CD2   B LEU C 3 119 ? 50.312  -11.292 -3.931  0.80 23.40  ? 119 LEU F CD2   1 
ATOM   15025 N  N     A ALA C 3 120 ? 51.327  -16.705 -2.889  0.20 26.49  ? 120 ALA F N     1 
ATOM   15026 N  N     B ALA C 3 120 ? 51.360  -16.451 -2.815  0.80 26.64  ? 120 ALA F N     1 
ATOM   15027 C  CA    A ALA C 3 120 ? 51.102  -18.136 -2.739  0.20 26.77  ? 120 ALA F CA    1 
ATOM   15028 C  CA    B ALA C 3 120 ? 51.008  -17.867 -2.755  0.80 26.88  ? 120 ALA F CA    1 
ATOM   15029 C  C     A ALA C 3 120 ? 50.586  -18.503 -1.354  0.20 26.95  ? 120 ALA F C     1 
ATOM   15030 C  C     B ALA C 3 120 ? 50.354  -18.216 -1.424  0.80 27.68  ? 120 ALA F C     1 
ATOM   15031 O  O     A ALA C 3 120 ? 50.072  -19.612 -1.172  0.20 25.71  ? 120 ALA F O     1 
ATOM   15032 O  O     B ALA C 3 120 ? 49.457  -19.068 -1.369  0.80 26.55  ? 120 ALA F O     1 
ATOM   15033 C  CB    A ALA C 3 120 ? 52.389  -18.910 -3.024  0.20 24.15  ? 120 ALA F CB    1 
ATOM   15034 C  CB    B ALA C 3 120 ? 52.244  -18.732 -2.968  0.80 22.85  ? 120 ALA F CB    1 
ATOM   15035 N  N     A ALA C 3 121 ? 50.723  -17.604 -0.379  0.20 24.73  ? 121 ALA F N     1 
ATOM   15036 N  N     B ALA C 3 121 ? 50.815  -17.577 -0.347  0.80 24.56  ? 121 ALA F N     1 
ATOM   15037 C  CA    A ALA C 3 121 ? 50.198  -17.830 0.960   0.20 25.98  ? 121 ALA F CA    1 
ATOM   15038 C  CA    B ALA C 3 121 ? 50.227  -17.761 0.974   0.80 25.90  ? 121 ALA F CA    1 
ATOM   15039 C  C     A ALA C 3 121 ? 48.779  -17.308 1.126   0.20 27.20  ? 121 ALA F C     1 
ATOM   15040 C  C     B ALA C 3 121 ? 48.802  -17.223 1.024   0.80 26.80  ? 121 ALA F C     1 
ATOM   15041 O  O     A ALA C 3 121 ? 48.003  -17.879 1.901   0.20 26.87  ? 121 ALA F O     1 
ATOM   15042 O  O     B ALA C 3 121 ? 47.886  -17.904 1.499   0.80 28.18  ? 121 ALA F O     1 
ATOM   15043 C  CB    A ALA C 3 121 ? 51.107  -17.171 1.999   0.20 25.24  ? 121 ALA F CB    1 
ATOM   15044 C  CB    B ALA C 3 121 ? 51.095  -17.062 2.013   0.80 25.42  ? 121 ALA F CB    1 
ATOM   15045 N  N     A ILE C 3 122 ? 48.428  -16.234 0.417   0.20 26.09  ? 122 ILE F N     1 
ATOM   15046 N  N     B ILE C 3 122 ? 48.608  -15.994 0.537   0.80 25.63  ? 122 ILE F N     1 
ATOM   15047 C  CA    A ILE C 3 122 ? 47.076  -15.692 0.494   0.20 29.99  ? 122 ILE F CA    1 
ATOM   15048 C  CA    B ILE C 3 122 ? 47.298  -15.346 0.561   0.80 31.65  ? 122 ILE F CA    1 
ATOM   15049 C  C     A ILE C 3 122 ? 46.093  -16.600 -0.233  0.20 29.57  ? 122 ILE F C     1 
ATOM   15050 C  C     B ILE C 3 122 ? 46.258  -16.200 -0.156  0.80 31.47  ? 122 ILE F C     1 
ATOM   15051 O  O     A ILE C 3 122 ? 44.982  -16.849 0.250   0.20 26.01  ? 122 ILE F O     1 
ATOM   15052 O  O     B ILE C 3 122 ? 45.111  -16.326 0.298   0.80 24.03  ? 122 ILE F O     1 
ATOM   15053 C  CB    A ILE C 3 122 ? 47.045  -14.259 -0.071  0.20 27.46  ? 122 ILE F CB    1 
ATOM   15054 C  CB    B ILE C 3 122 ? 47.401  -13.938 -0.063  0.80 25.10  ? 122 ILE F CB    1 
ATOM   15055 C  CG1   A ILE C 3 122 ? 47.972  -13.343 0.732   0.20 29.46  ? 122 ILE F CG1   1 
ATOM   15056 C  CG1   B ILE C 3 122 ? 48.202  -12.992 0.850   0.80 29.83  ? 122 ILE F CG1   1 
ATOM   15057 C  CG2   A ILE C 3 122 ? 45.619  -13.719 -0.086  0.20 29.19  ? 122 ILE F CG2   1 
ATOM   15058 C  CG2   B ILE C 3 122 ? 46.019  -13.398 -0.402  0.80 28.73  ? 122 ILE F CG2   1 
ATOM   15059 C  CD1   A ILE C 3 122 ? 48.068  -11.930 0.181   0.20 27.02  ? 122 ILE F CD1   1 
ATOM   15060 C  CD1   B ILE C 3 122 ? 48.459  -11.608 0.252   0.80 23.77  ? 122 ILE F CD1   1 
ATOM   15061 N  N     A MET C 3 123 ? 46.482  -17.109 -1.400  0.20 26.16  ? 123 MET F N     1 
ATOM   15062 N  N     B MET C 3 123 ? 46.642  -16.793 -1.285  0.80 25.06  ? 123 MET F N     1 
ATOM   15063 C  CA    A MET C 3 123 ? 45.608  -17.922 -2.234  0.20 29.73  ? 123 MET F CA    1 
ATOM   15064 C  CA    B MET C 3 123 ? 45.754  -17.578 -2.126  0.80 29.48  ? 123 MET F CA    1 
ATOM   15065 C  C     A MET C 3 123 ? 45.654  -19.403 -1.876  0.20 29.92  ? 123 MET F C     1 
ATOM   15066 C  C     B MET C 3 123 ? 45.719  -19.048 -1.730  0.80 29.83  ? 123 MET F C     1 
ATOM   15067 O  O     A MET C 3 123 ? 45.201  -20.233 -2.670  0.20 28.78  ? 123 MET F O     1 
ATOM   15068 O  O     B MET C 3 123 ? 44.908  -19.805 -2.277  0.80 29.34  ? 123 MET F O     1 
ATOM   15069 C  CB    A MET C 3 123 ? 45.965  -17.732 -3.712  0.20 29.99  ? 123 MET F CB    1 
ATOM   15070 C  CB    B MET C 3 123 ? 46.163  -17.450 -3.607  0.80 30.84  ? 123 MET F CB    1 
ATOM   15071 C  CG    A MET C 3 123 ? 45.857  -16.291 -4.193  0.20 30.93  ? 123 MET F CG    1 
ATOM   15072 C  CG    B MET C 3 123 ? 46.109  -16.017 -4.186  0.80 29.85  ? 123 MET F CG    1 
ATOM   15073 S  SD    A MET C 3 123 ? 44.191  -15.624 -3.990  0.20 30.92  ? 123 MET F SD    1 
ATOM   15074 S  SD    B MET C 3 123 ? 44.512  -15.178 -3.931  0.80 33.37  ? 123 MET F SD    1 
ATOM   15075 C  CE    A MET C 3 123 ? 43.288  -16.618 -5.173  0.20 32.85  ? 123 MET F CE    1 
ATOM   15076 C  CE    B MET C 3 123 ? 43.372  -16.400 -4.569  0.80 33.60  ? 123 MET F CE    1 
ATOM   15077 N  N     A GLY C 3 124 ? 46.190  -19.749 -0.709  0.20 29.38  ? 124 GLY F N     1 
ATOM   15078 N  N     B GLY C 3 124 ? 46.569  -19.471 -0.800  0.80 25.90  ? 124 GLY F N     1 
ATOM   15079 C  CA    A GLY C 3 124 ? 46.186  -21.133 -0.258  0.20 29.51  ? 124 GLY F CA    1 
ATOM   15080 C  CA    B GLY C 3 124 ? 46.460  -20.814 -0.256  0.80 29.68  ? 124 GLY F CA    1 
ATOM   15081 C  C     A GLY C 3 124 ? 46.936  -22.090 -1.157  0.20 32.27  ? 124 GLY F C     1 
ATOM   15082 C  C     B GLY C 3 124 ? 47.060  -21.914 -1.101  0.80 32.78  ? 124 GLY F C     1 
ATOM   15083 O  O     A GLY C 3 124 ? 46.492  -23.227 -1.359  0.20 28.45  ? 124 GLY F O     1 
ATOM   15084 O  O     B GLY C 3 124 ? 46.705  -23.085 -0.926  0.80 27.67  ? 124 GLY F O     1 
ATOM   15085 N  N     A HIS C 3 125 ? 48.070  -21.655 -1.708  0.20 32.44  ? 125 HIS F N     1 
ATOM   15086 N  N     B HIS C 3 125 ? 47.964  -21.584 -2.016  0.80 33.70  ? 125 HIS F N     1 
ATOM   15087 C  CA    A HIS C 3 125 ? 48.890  -22.502 -2.572  0.20 31.29  ? 125 HIS F CA    1 
ATOM   15088 C  CA    B HIS C 3 125 ? 48.630  -22.609 -2.817  0.80 30.65  ? 125 HIS F CA    1 
ATOM   15089 C  C     A HIS C 3 125 ? 49.981  -23.140 -1.717  0.20 33.38  ? 125 HIS F C     1 
ATOM   15090 C  C     B HIS C 3 125 ? 49.797  -23.156 -2.001  0.80 34.81  ? 125 HIS F C     1 
ATOM   15091 O  O     A HIS C 3 125 ? 51.148  -22.750 -1.749  0.20 32.65  ? 125 HIS F O     1 
ATOM   15092 O  O     B HIS C 3 125 ? 50.936  -22.710 -2.142  0.80 31.09  ? 125 HIS F O     1 
ATOM   15093 C  CB    A HIS C 3 125 ? 49.473  -21.692 -3.729  0.20 29.02  ? 125 HIS F CB    1 
ATOM   15094 C  CB    B HIS C 3 125 ? 49.119  -22.042 -4.149  0.80 26.70  ? 125 HIS F CB    1 
ATOM   15095 C  CG    A HIS C 3 125 ? 48.442  -21.129 -4.658  0.20 31.03  ? 125 HIS F CG    1 
ATOM   15096 C  CG    B HIS C 3 125 ? 48.095  -21.247 -4.898  0.80 32.11  ? 125 HIS F CG    1 
ATOM   15097 N  ND1   A HIS C 3 125 ? 47.419  -21.887 -5.185  0.20 30.19  ? 125 HIS F ND1   1 
ATOM   15098 N  ND1   B HIS C 3 125 ? 46.873  -21.763 -5.272  0.80 29.86  ? 125 HIS F ND1   1 
ATOM   15099 C  CD2   A HIS C 3 125 ? 48.284  -19.881 -5.161  0.20 28.23  ? 125 HIS F CD2   1 
ATOM   15100 C  CD2   B HIS C 3 125 ? 48.125  -19.976 -5.365  0.80 27.23  ? 125 HIS F CD2   1 
ATOM   15101 C  CE1   A HIS C 3 125 ? 46.671  -21.129 -5.968  0.20 31.33  ? 125 HIS F CE1   1 
ATOM   15102 C  CE1   B HIS C 3 125 ? 46.188  -20.838 -5.921  0.80 31.06  ? 125 HIS F CE1   1 
ATOM   15103 N  NE2   A HIS C 3 125 ? 47.175  -19.908 -5.971  0.20 29.88  ? 125 HIS F NE2   1 
ATOM   15104 N  NE2   B HIS C 3 125 ? 46.928  -19.745 -5.994  0.80 30.41  ? 125 HIS F NE2   1 
ATOM   15105 N  N     A LEU C 3 126 ? 49.583  -24.159 -0.949  0.20 30.76  ? 126 LEU F N     1 
ATOM   15106 N  N     B LEU C 3 126 ? 49.519  -24.165 -1.165  0.80 30.36  ? 126 LEU F N     1 
ATOM   15107 C  CA    A LEU C 3 126 ? 50.505  -24.777 -0.001  0.20 32.82  ? 126 LEU F CA    1 
ATOM   15108 C  CA    B LEU C 3 126 ? 50.489  -24.588 -0.157  0.80 32.66  ? 126 LEU F CA    1 
ATOM   15109 C  C     A LEU C 3 126 ? 51.667  -25.469 -0.700  0.20 31.96  ? 126 LEU F C     1 
ATOM   15110 C  C     B LEU C 3 126 ? 51.678  -25.327 -0.754  0.80 31.58  ? 126 LEU F C     1 
ATOM   15111 O  O     A LEU C 3 126 ? 52.783  -25.491 -0.167  0.20 30.67  ? 126 LEU F O     1 
ATOM   15112 O  O     B LEU C 3 126 ? 52.773  -25.281 -0.182  0.80 29.85  ? 126 LEU F O     1 
ATOM   15113 C  CB    A LEU C 3 126 ? 49.761  -25.774 0.887   0.20 32.74  ? 126 LEU F CB    1 
ATOM   15114 C  CB    B LEU C 3 126 ? 49.817  -25.468 0.892   0.80 32.74  ? 126 LEU F CB    1 
ATOM   15115 C  CG    A LEU C 3 126 ? 48.595  -25.203 1.697   0.20 33.72  ? 126 LEU F CG    1 
ATOM   15116 C  CG    B LEU C 3 126 ? 48.678  -24.740 1.609   0.80 32.40  ? 126 LEU F CG    1 
ATOM   15117 C  CD1   A LEU C 3 126 ? 47.992  -26.281 2.580   0.20 38.60  ? 126 LEU F CD1   1 
ATOM   15118 C  CD1   B LEU C 3 126 ? 48.237  -25.525 2.826   0.80 42.31  ? 126 LEU F CD1   1 
ATOM   15119 C  CD2   A LEU C 3 126 ? 49.047  -24.010 2.527   0.20 35.27  ? 126 LEU F CD2   1 
ATOM   15120 C  CD2   B LEU C 3 126 ? 49.134  -23.343 1.996   0.80 36.70  ? 126 LEU F CD2   1 
ATOM   15121 N  N     A GLU C 3 127 ? 51.429  -26.049 -1.878  0.20 35.70  ? 127 GLU F N     1 
ATOM   15122 N  N     B GLU C 3 127 ? 51.482  -26.052 -1.855  0.80 36.02  ? 127 GLU F N     1 
ATOM   15123 C  CA    A GLU C 3 127 ? 52.516  -26.689 -2.613  0.20 33.31  ? 127 GLU F CA    1 
ATOM   15124 C  CA    B GLU C 3 127 ? 52.619  -26.683 -2.519  0.80 32.82  ? 127 GLU F CA    1 
ATOM   15125 C  C     A GLU C 3 127 ? 53.539  -25.666 -3.090  0.20 36.85  ? 127 GLU F C     1 
ATOM   15126 C  C     B GLU C 3 127 ? 53.595  -25.638 -3.043  0.80 37.35  ? 127 GLU F C     1 
ATOM   15127 O  O     A GLU C 3 127 ? 54.750  -25.897 -2.990  0.20 37.68  ? 127 GLU F O     1 
ATOM   15128 O  O     B GLU C 3 127 ? 54.817  -25.832 -2.990  0.80 37.88  ? 127 GLU F O     1 
ATOM   15129 C  CB    A GLU C 3 127 ? 51.963  -27.478 -3.801  0.20 34.34  ? 127 GLU F CB    1 
ATOM   15130 C  CB    B GLU C 3 127 ? 52.141  -27.576 -3.665  0.80 33.43  ? 127 GLU F CB    1 
ATOM   15131 C  CG    A GLU C 3 127 ? 51.233  -28.757 -3.432  0.20 40.07  ? 127 GLU F CG    1 
ATOM   15132 C  CG    B GLU C 3 127 ? 51.967  -29.024 -3.290  0.80 37.17  ? 127 GLU F CG    1 
ATOM   15133 C  CD    A GLU C 3 127 ? 49.779  -28.527 -3.064  0.20 44.61  ? 127 GLU F CD    1 
ATOM   15134 C  CD    B GLU C 3 127 ? 50.763  -29.245 -2.407  0.80 52.62  ? 127 GLU F CD    1 
ATOM   15135 O  OE1   A GLU C 3 127 ? 49.371  -27.353 -2.925  0.20 36.52  ? 127 GLU F OE1   1 
ATOM   15136 O  OE1   B GLU C 3 127 ? 49.741  -28.551 -2.616  0.80 50.09  ? 127 GLU F OE1   1 
ATOM   15137 O  OE2   A GLU C 3 127 ? 49.043  -29.527 -2.918  0.20 40.95  ? 127 GLU F OE2   1 
ATOM   15138 O  OE2   B GLU C 3 127 ? 50.840  -30.106 -1.504  0.80 49.20  ? 127 GLU F OE2   1 
ATOM   15139 N  N     A ILE C 3 128 ? 53.073  -24.531 -3.615  0.20 34.42  ? 128 ILE F N     1 
ATOM   15140 N  N     B ILE C 3 128 ? 53.074  -24.528 -3.567  0.80 34.56  ? 128 ILE F N     1 
ATOM   15141 C  CA    A ILE C 3 128 ? 53.994  -23.510 -4.103  0.20 33.76  ? 128 ILE F CA    1 
ATOM   15142 C  CA    B ILE C 3 128 ? 53.947  -23.482 -4.089  0.80 33.85  ? 128 ILE F CA    1 
ATOM   15143 C  C     A ILE C 3 128 ? 54.749  -22.868 -2.945  0.20 33.64  ? 128 ILE F C     1 
ATOM   15144 C  C     B ILE C 3 128 ? 54.695  -22.801 -2.949  0.80 33.79  ? 128 ILE F C     1 
ATOM   15145 O  O     A ILE C 3 128 ? 55.928  -22.519 -3.082  0.20 31.33  ? 128 ILE F O     1 
ATOM   15146 O  O     B ILE C 3 128 ? 55.886  -22.487 -3.071  0.80 31.22  ? 128 ILE F O     1 
ATOM   15147 C  CB    A ILE C 3 128 ? 53.232  -22.466 -4.941  0.20 29.74  ? 128 ILE F CB    1 
ATOM   15148 C  CB    B ILE C 3 128 ? 53.127  -22.490 -4.932  0.80 29.77  ? 128 ILE F CB    1 
ATOM   15149 C  CG1   A ILE C 3 128 ? 52.514  -23.149 -6.106  0.20 32.07  ? 128 ILE F CG1   1 
ATOM   15150 C  CG1   B ILE C 3 128 ? 52.721  -23.153 -6.240  0.80 31.83  ? 128 ILE F CG1   1 
ATOM   15151 C  CG2   A ILE C 3 128 ? 54.178  -21.397 -5.467  0.20 30.48  ? 128 ILE F CG2   1 
ATOM   15152 C  CG2   B ILE C 3 128 ? 53.907  -21.226 -5.238  0.80 29.75  ? 128 ILE F CG2   1 
ATOM   15153 C  CD1   A ILE C 3 128 ? 51.692  -22.204 -6.953  0.20 33.50  ? 128 ILE F CD1   1 
ATOM   15154 C  CD1   B ILE C 3 128 ? 51.752  -22.340 -7.027  0.80 34.04  ? 128 ILE F CD1   1 
ATOM   15155 N  N     A VAL C 3 129 ? 54.096  -22.712 -1.789  0.20 27.96  ? 129 VAL F N     1 
ATOM   15156 N  N     B VAL C 3 129 ? 54.023  -22.601 -1.808  0.80 28.27  ? 129 VAL F N     1 
ATOM   15157 C  CA    A VAL C 3 129 ? 54.781  -22.176 -0.615  0.20 28.88  ? 129 VAL F CA    1 
ATOM   15158 C  CA    B VAL C 3 129 ? 54.706  -22.066 -0.633  0.80 28.72  ? 129 VAL F CA    1 
ATOM   15159 C  C     A VAL C 3 129 ? 55.965  -23.060 -0.236  0.20 28.19  ? 129 VAL F C     1 
ATOM   15160 C  C     B VAL C 3 129 ? 55.917  -22.926 -0.275  0.80 27.95  ? 129 VAL F C     1 
ATOM   15161 O  O     A VAL C 3 129 ? 57.059  -22.563 0.058   0.20 26.32  ? 129 VAL F O     1 
ATOM   15162 O  O     B VAL C 3 129 ? 57.024  -22.412 -0.068  0.80 25.03  ? 129 VAL F O     1 
ATOM   15163 C  CB    A VAL C 3 129 ? 53.792  -22.018 0.557   0.20 24.17  ? 129 VAL F CB    1 
ATOM   15164 C  CB    B VAL C 3 129 ? 53.728  -21.943 0.553   0.80 23.68  ? 129 VAL F CB    1 
ATOM   15165 C  CG1   A VAL C 3 129 ? 54.539  -21.741 1.843   0.20 29.68  ? 129 VAL F CG1   1 
ATOM   15166 C  CG1   B VAL C 3 129 ? 54.486  -21.635 1.795   0.80 29.79  ? 129 VAL F CG1   1 
ATOM   15167 C  CG2   A VAL C 3 129 ? 52.807  -20.896 0.269   0.20 25.62  ? 129 VAL F CG2   1 
ATOM   15168 C  CG2   B VAL C 3 129 ? 52.722  -20.838 0.277   0.80 25.49  ? 129 VAL F CG2   1 
ATOM   15169 N  N     A GLU C 3 130 ? 55.770  -24.381 -0.249  0.20 29.73  ? 130 GLU F N     1 
ATOM   15170 N  N     B GLU C 3 130 ? 55.730  -24.248 -0.197  0.80 29.03  ? 130 GLU F N     1 
ATOM   15171 C  CA    A GLU C 3 130 ? 56.867  -25.288 0.076   0.20 33.60  ? 130 GLU F CA    1 
ATOM   15172 C  CA    B GLU C 3 130 ? 56.858  -25.120 0.128   0.80 33.60  ? 130 GLU F CA    1 
ATOM   15173 C  C     A GLU C 3 130 ? 57.990  -25.210 -0.951  0.20 35.35  ? 130 GLU F C     1 
ATOM   15174 C  C     B GLU C 3 130 ? 57.967  -25.002 -0.912  0.80 36.15  ? 130 GLU F C     1 
ATOM   15175 O  O     A GLU C 3 130 ? 59.160  -25.401 -0.604  0.20 32.64  ? 130 GLU F O     1 
ATOM   15176 O  O     B GLU C 3 130 ? 59.150  -24.930 -0.557  0.80 29.26  ? 130 GLU F O     1 
ATOM   15177 C  CB    A GLU C 3 130 ? 56.355  -26.724 0.187   0.20 35.72  ? 130 GLU F CB    1 
ATOM   15178 C  CB    B GLU C 3 130 ? 56.408  -26.577 0.246   0.80 35.41  ? 130 GLU F CB    1 
ATOM   15179 C  CG    A GLU C 3 130 ? 55.447  -26.973 1.379   0.20 38.98  ? 130 GLU F CG    1 
ATOM   15180 C  CG    B GLU C 3 130 ? 55.485  -26.867 1.417   0.80 38.91  ? 130 GLU F CG    1 
ATOM   15181 C  CD    A GLU C 3 130 ? 55.072  -28.433 1.531   0.20 48.38  ? 130 GLU F CD    1 
ATOM   15182 C  CD    B GLU C 3 130 ? 55.426  -28.342 1.762   0.80 48.85  ? 130 GLU F CD    1 
ATOM   15183 O  OE1   A GLU C 3 130 ? 55.072  -29.157 0.512   0.20 47.16  ? 130 GLU F OE1   1 
ATOM   15184 O  OE1   B GLU C 3 130 ? 56.489  -28.941 2.029   0.80 49.98  ? 130 GLU F OE1   1 
ATOM   15185 O  OE2   A GLU C 3 130 ? 54.783  -28.857 2.671   0.20 46.20  ? 130 GLU F OE2   1 
ATOM   15186 O  OE2   B GLU C 3 130 ? 54.311  -28.904 1.760   0.80 60.33  ? 130 GLU F OE2   1 
ATOM   15187 N  N     A VAL C 3 131 ? 57.660  -24.932 -2.213  0.20 34.21  ? 131 VAL F N     1 
ATOM   15188 N  N     B VAL C 3 131 ? 57.605  -24.975 -2.197  0.80 34.29  ? 131 VAL F N     1 
ATOM   15189 C  CA    A VAL C 3 131 ? 58.696  -24.833 -3.236  0.20 33.22  ? 131 VAL F CA    1 
ATOM   15190 C  CA    B VAL C 3 131 ? 58.612  -24.890 -3.252  0.80 33.01  ? 131 VAL F CA    1 
ATOM   15191 C  C     A VAL C 3 131 ? 59.523  -23.569 -3.040  0.20 36.98  ? 131 VAL F C     1 
ATOM   15192 C  C     B VAL C 3 131 ? 59.450  -23.629 -3.086  0.80 37.00  ? 131 VAL F C     1 
ATOM   15193 O  O     A VAL C 3 131 ? 60.757  -23.597 -3.131  0.20 31.86  ? 131 VAL F O     1 
ATOM   15194 O  O     B VAL C 3 131 ? 60.685  -23.668 -3.184  0.80 32.19  ? 131 VAL F O     1 
ATOM   15195 C  CB    A VAL C 3 131 ? 58.067  -24.888 -4.641  0.20 34.65  ? 131 VAL F CB    1 
ATOM   15196 C  CB    B VAL C 3 131 ? 57.944  -24.947 -4.640  0.80 34.62  ? 131 VAL F CB    1 
ATOM   15197 C  CG1   A VAL C 3 131 ? 59.121  -24.628 -5.707  0.20 37.83  ? 131 VAL F CG1   1 
ATOM   15198 C  CG1   B VAL C 3 131 ? 58.956  -24.638 -5.736  0.80 38.13  ? 131 VAL F CG1   1 
ATOM   15199 C  CG2   A VAL C 3 131 ? 57.404  -26.236 -4.867  0.20 36.30  ? 131 VAL F CG2   1 
ATOM   15200 C  CG2   B VAL C 3 131 ? 57.325  -26.316 -4.870  0.80 36.40  ? 131 VAL F CG2   1 
ATOM   15201 N  N     A LEU C 3 132 ? 58.861  -22.444 -2.758  0.20 30.17  ? 132 LEU F N     1 
ATOM   15202 N  N     B LEU C 3 132 ? 58.793  -22.496 -2.813  0.80 30.05  ? 132 LEU F N     1 
ATOM   15203 C  CA    A LEU C 3 132 ? 59.571  -21.177 -2.615  0.20 31.03  ? 132 LEU F CA    1 
ATOM   15204 C  CA    B LEU C 3 132 ? 59.498  -21.223 -2.712  0.80 30.76  ? 132 LEU F CA    1 
ATOM   15205 C  C     A LEU C 3 132 ? 60.460  -21.172 -1.376  0.20 35.25  ? 132 LEU F C     1 
ATOM   15206 C  C     B LEU C 3 132 ? 60.423  -21.192 -1.501  0.80 35.62  ? 132 LEU F C     1 
ATOM   15207 O  O     A LEU C 3 132 ? 61.568  -20.622 -1.403  0.20 34.41  ? 132 LEU F O     1 
ATOM   15208 O  O     B LEU C 3 132 ? 61.573  -20.746 -1.603  0.80 34.62  ? 132 LEU F O     1 
ATOM   15209 C  CB    A LEU C 3 132 ? 58.569  -20.024 -2.565  0.20 31.81  ? 132 LEU F CB    1 
ATOM   15210 C  CB    B LEU C 3 132 ? 58.491  -20.069 -2.653  0.80 31.80  ? 132 LEU F CB    1 
ATOM   15211 C  CG    A LEU C 3 132 ? 57.746  -19.790 -3.835  0.20 30.40  ? 132 LEU F CG    1 
ATOM   15212 C  CG    B LEU C 3 132 ? 57.709  -19.749 -3.937  0.80 30.36  ? 132 LEU F CG    1 
ATOM   15213 C  CD1   A LEU C 3 132 ? 56.492  -18.996 -3.525  0.20 32.18  ? 132 LEU F CD1   1 
ATOM   15214 C  CD1   B LEU C 3 132 ? 56.742  -18.591 -3.726  0.80 34.04  ? 132 LEU F CD1   1 
ATOM   15215 C  CD2   A LEU C 3 132 ? 58.576  -19.080 -4.898  0.20 33.41  ? 132 LEU F CD2   1 
ATOM   15216 C  CD2   B LEU C 3 132 ? 58.647  -19.456 -5.120  0.80 34.85  ? 132 LEU F CD2   1 
ATOM   15217 N  N     A LEU C 3 133 ? 59.993  -21.780 -0.282  0.20 31.99  ? 133 LEU F N     1 
ATOM   15218 N  N     B LEU C 3 133 ? 59.939  -21.649 -0.340  0.80 31.83  ? 133 LEU F N     1 
ATOM   15219 C  CA    A LEU C 3 133 ? 60.794  -21.832 0.937   0.20 37.08  ? 133 LEU F CA    1 
ATOM   15220 C  CA    B LEU C 3 133 ? 60.820  -21.769 0.817   0.80 37.74  ? 133 LEU F CA    1 
ATOM   15221 C  C     A LEU C 3 133 ? 62.106  -22.570 0.705   0.20 35.25  ? 133 LEU F C     1 
ATOM   15222 C  C     B LEU C 3 133 ? 62.066  -22.576 0.483   0.80 35.21  ? 133 LEU F C     1 
ATOM   15223 O  O     A LEU C 3 133 ? 63.173  -22.116 1.136   0.20 34.02  ? 133 LEU F O     1 
ATOM   15224 O  O     B LEU C 3 133 ? 63.177  -22.207 0.874   0.80 33.60  ? 133 LEU F O     1 
ATOM   15225 C  CB    A LEU C 3 133 ? 59.997  -22.497 2.057   0.20 28.36  ? 133 LEU F CB    1 
ATOM   15226 C  CB    B LEU C 3 133 ? 60.080  -22.417 1.979   0.80 28.11  ? 133 LEU F CB    1 
ATOM   15227 C  CG    A LEU C 3 133 ? 59.382  -21.566 3.100   0.20 30.71  ? 133 LEU F CG    1 
ATOM   15228 C  CG    B LEU C 3 133 ? 58.983  -21.534 2.560   0.80 30.44  ? 133 LEU F CG    1 
ATOM   15229 C  CD1   A LEU C 3 133 ? 58.736  -20.361 2.436   0.20 28.47  ? 133 LEU F CD1   1 
ATOM   15230 C  CD1   B LEU C 3 133 ? 58.259  -22.269 3.687   0.80 31.33  ? 133 LEU F CD1   1 
ATOM   15231 C  CD2   A LEU C 3 133 ? 58.366  -22.332 3.929   0.20 31.84  ? 133 LEU F CD2   1 
ATOM   15232 C  CD2   B LEU C 3 133 ? 59.578  -20.223 3.026   0.80 30.23  ? 133 LEU F CD2   1 
ATOM   15233 N  N     A LYS C 3 134 ? 62.045  -23.719 0.028   0.20 38.56  ? 134 LYS F N     1 
ATOM   15234 N  N     B LYS C 3 134 ? 61.901  -23.685 -0.233  0.80 39.90  ? 134 LYS F N     1 
ATOM   15235 C  CA    A LYS C 3 134 ? 63.259  -24.483 -0.242  0.20 35.24  ? 134 LYS F CA    1 
ATOM   15236 C  CA    B LYS C 3 134 ? 63.054  -24.529 -0.535  0.80 34.58  ? 134 LYS F CA    1 
ATOM   15237 C  C     A LYS C 3 134 ? 64.223  -23.692 -1.116  0.20 37.65  ? 134 LYS F C     1 
ATOM   15238 C  C     B LYS C 3 134 ? 64.003  -23.889 -1.535  0.80 40.55  ? 134 LYS F C     1 
ATOM   15239 O  O     A LYS C 3 134 ? 65.440  -23.727 -0.900  0.20 30.91  ? 134 LYS F O     1 
ATOM   15240 O  O     B LYS C 3 134 ? 65.032  -24.494 -1.852  0.80 47.46  ? 134 LYS F O     1 
ATOM   15241 C  CB    A LYS C 3 134 ? 62.906  -25.815 -0.900  0.20 37.34  ? 134 LYS F CB    1 
ATOM   15242 C  CB    B LYS C 3 134 ? 62.575  -25.893 -1.033  0.80 36.88  ? 134 LYS F CB    1 
ATOM   15243 C  CG    A LYS C 3 134 ? 62.056  -26.728 -0.033  0.20 43.86  ? 134 LYS F CG    1 
ATOM   15244 C  CG    B LYS C 3 134 ? 61.745  -26.617 0.029   0.80 44.26  ? 134 LYS F CG    1 
ATOM   15245 C  CD    A LYS C 3 134 ? 61.725  -28.024 -0.754  0.20 45.61  ? 134 LYS F CD    1 
ATOM   15246 C  CD    B LYS C 3 134 ? 61.237  -27.991 -0.396  0.80 49.06  ? 134 LYS F CD    1 
ATOM   15247 C  CE    A LYS C 3 134 ? 60.860  -28.929 0.110   0.20 56.09  ? 134 LYS F CE    1 
ATOM   15248 C  CE    B LYS C 3 134 ? 60.347  -28.579 0.717   0.80 57.44  ? 134 LYS F CE    1 
ATOM   15249 N  NZ    A LYS C 3 134 ? 60.508  -30.194 -0.591  0.20 55.70  ? 134 LYS F NZ    1 
ATOM   15250 N  NZ    B LYS C 3 134 ? 59.776  -29.928 0.415   0.80 54.00  ? 134 LYS F NZ    1 
ATOM   15251 N  N     A HIS C 3 135 ? 63.696  -22.965 -2.101  0.20 34.48  ? 135 HIS F N     1 
ATOM   15252 N  N     B HIS C 3 135 ? 63.694  -22.681 -2.018  0.80 32.99  ? 135 HIS F N     1 
ATOM   15253 C  CA    A HIS C 3 135 ? 64.504  -22.144 -2.993  0.20 34.64  ? 135 HIS F CA    1 
ATOM   15254 C  CA    B HIS C 3 135 ? 64.556  -21.950 -2.938  0.80 34.15  ? 135 HIS F CA    1 
ATOM   15255 C  C     A HIS C 3 135 ? 64.951  -20.833 -2.356  0.20 33.16  ? 135 HIS F C     1 
ATOM   15256 C  C     B HIS C 3 135 ? 64.968  -20.595 -2.373  0.80 32.47  ? 135 HIS F C     1 
ATOM   15257 O  O     A HIS C 3 135 ? 65.486  -19.971 -3.061  0.20 35.04  ? 135 HIS F O     1 
ATOM   15258 O  O     B HIS C 3 135 ? 65.475  -19.738 -3.107  0.80 35.22  ? 135 HIS F O     1 
ATOM   15259 C  CB    A HIS C 3 135 ? 63.734  -21.858 -4.285  0.20 37.05  ? 135 HIS F CB    1 
ATOM   15260 C  CB    B HIS C 3 135 ? 63.865  -21.794 -4.289  0.80 37.14  ? 135 HIS F CB    1 
ATOM   15261 C  CG    A HIS C 3 135 ? 63.693  -23.016 -5.234  0.20 39.41  ? 135 HIS F CG    1 
ATOM   15262 C  CG    B HIS C 3 135 ? 63.940  -23.025 -5.135  0.80 40.03  ? 135 HIS F CG    1 
ATOM   15263 N  ND1   A HIS C 3 135 ? 64.720  -23.295 -6.110  0.20 42.77  ? 135 HIS F ND1   1 
ATOM   15264 N  ND1   B HIS C 3 135 ? 63.236  -24.174 -4.843  0.80 46.18  ? 135 HIS F ND1   1 
ATOM   15265 C  CD2   A HIS C 3 135 ? 62.750  -23.964 -5.445  0.20 40.61  ? 135 HIS F CD2   1 
ATOM   15266 C  CD2   B HIS C 3 135 ? 64.662  -23.299 -6.249  0.80 43.18  ? 135 HIS F CD2   1 
ATOM   15267 C  CE1   A HIS C 3 135 ? 64.411  -24.366 -6.820  0.20 40.16  ? 135 HIS F CE1   1 
ATOM   15268 C  CE1   B HIS C 3 135 ? 63.503  -25.095 -5.752  0.80 46.52  ? 135 HIS F CE1   1 
ATOM   15269 N  NE2   A HIS C 3 135 ? 63.221  -24.791 -6.436  0.20 41.79  ? 135 HIS F NE2   1 
ATOM   15270 N  NE2   B HIS C 3 135 ? 64.365  -24.589 -6.617  0.80 39.90  ? 135 HIS F NE2   1 
ATOM   15271 N  N     A GLY C 3 136 ? 64.744  -20.659 -1.054  0.20 33.89  ? 136 GLY F N     1 
ATOM   15272 N  N     B GLY C 3 136 ? 64.771  -20.383 -1.076  0.80 34.70  ? 136 GLY F N     1 
ATOM   15273 C  CA    A GLY C 3 136 ? 65.248  -19.485 -0.368  0.20 31.91  ? 136 GLY F CA    1 
ATOM   15274 C  CA    B GLY C 3 136 ? 65.324  -19.222 -0.409  0.80 30.82  ? 136 GLY F CA    1 
ATOM   15275 C  C     A GLY C 3 136 ? 64.322  -18.287 -0.385  0.20 31.43  ? 136 GLY F C     1 
ATOM   15276 C  C     B GLY C 3 136 ? 64.414  -18.028 -0.233  0.80 30.80  ? 136 GLY F C     1 
ATOM   15277 O  O     A GLY C 3 136 ? 64.748  -17.173 -0.704  0.20 33.22  ? 136 GLY F O     1 
ATOM   15278 O  O     B GLY C 3 136 ? 64.910  -16.951 0.107   0.80 32.21  ? 136 GLY F O     1 
ATOM   15279 N  N     A ALA C 3 137 ? 63.053  -18.496 -0.042  0.20 33.53  ? 137 ALA F N     1 
ATOM   15280 N  N     B ALA C 3 137 ? 63.106  -18.175 -0.439  0.80 31.59  ? 137 ALA F N     1 
ATOM   15281 C  CA    A ALA C 3 137 ? 62.120  -17.388 0.109   0.20 34.51  ? 137 ALA F CA    1 
ATOM   15282 C  CA    B ALA C 3 137 ? 62.187  -17.085 -0.123  0.80 35.60  ? 137 ALA F CA    1 
ATOM   15283 C  C     A ALA C 3 137 ? 62.304  -16.740 1.476   0.20 33.06  ? 137 ALA F C     1 
ATOM   15284 C  C     B ALA C 3 137 ? 62.424  -16.569 1.296   0.80 32.13  ? 137 ALA F C     1 
ATOM   15285 O  O     A ALA C 3 137 ? 62.399  -17.433 2.494   0.20 33.91  ? 137 ALA F O     1 
ATOM   15286 O  O     B ALA C 3 137 ? 62.712  -17.340 2.216   0.80 35.38  ? 137 ALA F O     1 
ATOM   15287 C  CB    A ALA C 3 137 ? 60.679  -17.866 -0.061  0.20 31.42  ? 137 ALA F CB    1 
ATOM   15288 C  CB    B ALA C 3 137 ? 60.740  -17.551 -0.285  0.80 30.59  ? 137 ALA F CB    1 
ATOM   15289 N  N     A ASP C 3 138 ? 62.350  -15.410 1.495   0.20 31.29  ? 138 ASP F N     1 
ATOM   15290 N  N     B ASP C 3 138 ? 62.287  -15.254 1.467   0.80 30.89  ? 138 ASP F N     1 
ATOM   15291 C  CA    A ASP C 3 138 ? 62.533  -14.663 2.735   0.20 33.08  ? 138 ASP F CA    1 
ATOM   15292 C  CA    B ASP C 3 138 ? 62.620  -14.564 2.714   0.80 32.94  ? 138 ASP F CA    1 
ATOM   15293 C  C     A ASP C 3 138 ? 61.239  -14.688 3.542   0.20 35.64  ? 138 ASP F C     1 
ATOM   15294 C  C     B ASP C 3 138 ? 61.386  -14.513 3.617   0.80 36.59  ? 138 ASP F C     1 
ATOM   15295 O  O     A ASP C 3 138 ? 60.223  -14.130 3.117   0.20 32.37  ? 138 ASP F O     1 
ATOM   15296 O  O     B ASP C 3 138 ? 60.438  -13.772 3.340   0.80 30.57  ? 138 ASP F O     1 
ATOM   15297 C  CB    A ASP C 3 138 ? 62.956  -13.231 2.419   0.20 35.92  ? 138 ASP F CB    1 
ATOM   15298 C  CB    B ASP C 3 138 ? 63.134  -13.162 2.392   0.80 36.18  ? 138 ASP F CB    1 
ATOM   15299 C  CG    A ASP C 3 138 ? 63.411  -12.466 3.649   0.20 39.73  ? 138 ASP F CG    1 
ATOM   15300 C  CG    B ASP C 3 138 ? 63.529  -12.361 3.629   0.80 40.55  ? 138 ASP F CG    1 
ATOM   15301 O  OD1   A ASP C 3 138 ? 63.540  -13.080 4.730   0.20 37.97  ? 138 ASP F OD1   1 
ATOM   15302 O  OD1   B ASP C 3 138 ? 63.615  -12.931 4.743   0.80 38.47  ? 138 ASP F OD1   1 
ATOM   15303 O  OD2   A ASP C 3 138 ? 63.641  -11.242 3.530   0.20 42.48  ? 138 ASP F OD2   1 
ATOM   15304 O  OD2   B ASP C 3 138 ? 63.762  -11.136 3.469   0.80 43.26  ? 138 ASP F OD2   1 
ATOM   15305 N  N     A VAL C 3 139 ? 61.270  -15.337 4.710   0.20 34.16  ? 139 VAL F N     1 
ATOM   15306 N  N     B VAL C 3 139 ? 61.406  -15.278 4.715   0.80 33.96  ? 139 VAL F N     1 
ATOM   15307 C  CA    A VAL C 3 139 ? 60.096  -15.370 5.580   0.20 34.35  ? 139 VAL F CA    1 
ATOM   15308 C  CA    B VAL C 3 139 ? 60.252  -15.312 5.610   0.80 34.56  ? 139 VAL F CA    1 
ATOM   15309 C  C     A VAL C 3 139 ? 59.950  -14.113 6.421   0.20 31.38  ? 139 VAL F C     1 
ATOM   15310 C  C     B VAL C 3 139 ? 60.089  -14.009 6.390   0.80 30.68  ? 139 VAL F C     1 
ATOM   15311 O  O     A VAL C 3 139 ? 58.944  -13.966 7.127   0.20 34.94  ? 139 VAL F O     1 
ATOM   15312 O  O     B VAL C 3 139 ? 59.027  -13.776 6.981   0.80 35.42  ? 139 VAL F O     1 
ATOM   15313 C  CB    A VAL C 3 139 ? 60.132  -16.594 6.515   0.20 35.96  ? 139 VAL F CB    1 
ATOM   15314 C  CB    B VAL C 3 139 ? 60.358  -16.508 6.575   0.80 36.27  ? 139 VAL F CB    1 
ATOM   15315 C  CG1   A VAL C 3 139 ? 60.080  -17.880 5.705   0.20 37.83  ? 139 VAL F CG1   1 
ATOM   15316 C  CG1   B VAL C 3 139 ? 60.556  -17.789 5.796   0.80 39.32  ? 139 VAL F CG1   1 
ATOM   15317 C  CG2   A VAL C 3 139 ? 61.376  -16.558 7.388   0.20 33.76  ? 139 VAL F CG2   1 
ATOM   15318 C  CG2   B VAL C 3 139 ? 61.494  -16.295 7.558   0.80 33.39  ? 139 VAL F CG2   1 
ATOM   15319 N  N     A ASN C 3 140 ? 60.923  -13.204 6.368   0.20 36.35  ? 140 ASN F N     1 
ATOM   15320 N  N     B ASN C 3 140 ? 61.116  -13.158 6.427   0.80 37.50  ? 140 ASN F N     1 
ATOM   15321 C  CA    A ASN C 3 140 ? 60.895  -11.971 7.144   0.20 32.70  ? 140 ASN F CA    1 
ATOM   15322 C  CA    B ASN C 3 140 ? 61.032  -11.861 7.092   0.80 32.33  ? 140 ASN F CA    1 
ATOM   15323 C  C     A ASN C 3 140 ? 60.633  -10.741 6.286   0.20 30.43  ? 140 ASN F C     1 
ATOM   15324 C  C     B ASN C 3 140 ? 60.530  -10.752 6.182   0.80 30.04  ? 140 ASN F C     1 
ATOM   15325 O  O     A ASN C 3 140 ? 60.846  -9.618  6.751   0.20 31.77  ? 140 ASN F O     1 
ATOM   15326 O  O     B ASN C 3 140 ? 60.361  -9.621  6.643   0.80 31.57  ? 140 ASN F O     1 
ATOM   15327 C  CB    A ASN C 3 140 ? 62.208  -11.798 7.909   0.20 30.78  ? 140 ASN F CB    1 
ATOM   15328 C  CB    B ASN C 3 140 ? 62.389  -11.449 7.646   0.80 30.44  ? 140 ASN F CB    1 
ATOM   15329 C  CG    A ASN C 3 140 ? 62.498  -12.957 8.840   0.20 32.67  ? 140 ASN F CG    1 
ATOM   15330 C  CG    B ASN C 3 140 ? 62.763  -12.199 8.894   0.80 30.09  ? 140 ASN F CG    1 
ATOM   15331 O  OD1   A ASN C 3 140 ? 61.591  -13.518 9.460   0.20 31.99  ? 140 ASN F OD1   1 
ATOM   15332 O  OD1   B ASN C 3 140 ? 61.942  -12.898 9.495   0.80 37.12  ? 140 ASN F OD1   1 
ATOM   15333 N  ND2   A ASN C 3 140 ? 63.770  -13.327 8.940   0.20 29.30  ? 140 ASN F ND2   1 
ATOM   15334 N  ND2   B ASN C 3 140 ? 64.020  -12.049 9.304   0.80 30.97  ? 140 ASN F ND2   1 
ATOM   15335 N  N     A ALA C 3 141 ? 60.180  -10.922 5.049   0.20 29.56  ? 141 ALA F N     1 
ATOM   15336 N  N     B ALA C 3 141 ? 60.294  -11.045 4.911   0.80 28.62  ? 141 ALA F N     1 
ATOM   15337 C  CA    A ALA C 3 141 ? 59.915  -9.796  4.165   0.20 32.85  ? 141 ALA F CA    1 
ATOM   15338 C  CA    B ALA C 3 141 ? 59.902  -10.019 3.957   0.80 34.00  ? 141 ALA F CA    1 
ATOM   15339 C  C     A ALA C 3 141 ? 58.515  -9.252  4.414   0.20 30.31  ? 141 ALA F C     1 
ATOM   15340 C  C     B ALA C 3 141 ? 58.539  -9.447  4.319   0.80 29.70  ? 141 ALA F C     1 
ATOM   15341 O  O     A ALA C 3 141 ? 57.541  -10.010 4.442   0.20 34.45  ? 141 ALA F O     1 
ATOM   15342 O  O     B ALA C 3 141 ? 57.569  -10.192 4.473   0.80 35.35  ? 141 ALA F O     1 
ATOM   15343 C  CB    A ALA C 3 141 ? 60.069  -10.219 2.705   0.20 31.10  ? 141 ALA F CB    1 
ATOM   15344 C  CB    B ALA C 3 141 ? 59.869  -10.606 2.548   0.80 29.10  ? 141 ALA F CB    1 
ATOM   15345 N  N     A GLN C 3 142 ? 58.417  -7.938  4.589   0.20 30.21  ? 142 GLN F N     1 
ATOM   15346 N  N     B GLN C 3 142 ? 58.466  -8.124  4.444   0.80 29.83  ? 142 GLN F N     1 
ATOM   15347 C  CA    A GLN C 3 142 ? 57.154  -7.275  4.872   0.20 32.32  ? 142 GLN F CA    1 
ATOM   15348 C  CA    B GLN C 3 142 ? 57.251  -7.422  4.825   0.80 32.23  ? 142 GLN F CA    1 
ATOM   15349 C  C     A GLN C 3 142 ? 56.632  -6.562  3.632   0.20 30.16  ? 142 GLN F C     1 
ATOM   15350 C  C     B GLN C 3 142 ? 56.630  -6.734  3.619   0.80 29.95  ? 142 GLN F C     1 
ATOM   15351 O  O     A GLN C 3 142 ? 57.402  -6.106  2.783   0.20 32.03  ? 142 GLN F O     1 
ATOM   15352 O  O     B GLN C 3 142 ? 57.344  -6.152  2.794   0.80 32.17  ? 142 GLN F O     1 
ATOM   15353 C  CB    A GLN C 3 142 ? 57.309  -6.271  6.017   0.20 35.06  ? 142 GLN F CB    1 
ATOM   15354 C  CB    B GLN C 3 142 ? 57.535  -6.369  5.898   0.80 36.20  ? 142 GLN F CB    1 
ATOM   15355 C  CG    A GLN C 3 142 ? 57.646  -6.896  7.361   0.20 32.77  ? 142 GLN F CG    1 
ATOM   15356 C  CG    B GLN C 3 142 ? 58.064  -6.897  7.216   0.80 31.68  ? 142 GLN F CG    1 
ATOM   15357 C  CD    A GLN C 3 142 ? 57.752  -5.860  8.461   0.20 35.09  ? 142 GLN F CD    1 
ATOM   15358 C  CD    B GLN C 3 142 ? 58.486  -5.763  8.122   0.80 31.39  ? 142 GLN F CD    1 
ATOM   15359 O  OE1   A GLN C 3 142 ? 58.729  -5.114  8.535   0.20 34.82  ? 142 GLN F OE1   1 
ATOM   15360 O  OE1   B GLN C 3 142 ? 59.567  -5.191  7.953   0.80 39.37  ? 142 GLN F OE1   1 
ATOM   15361 N  NE2   A GLN C 3 142 ? 56.739  -5.800  9.318   0.20 31.18  ? 142 GLN F NE2   1 
ATOM   15362 N  NE2   B GLN C 3 142 ? 57.623  -5.410  9.078   0.80 35.61  ? 142 GLN F NE2   1 
ATOM   15363 N  N     A ASP C 3 143 ? 55.308  -6.472  3.537   0.20 30.01  ? 143 ASP F N     1 
ATOM   15364 N  N     B ASP C 3 143 ? 55.299  -6.804  3.514   0.80 28.02  ? 143 ASP F N     1 
ATOM   15365 C  CA    A ASP C 3 143 ? 54.654  -5.804  2.421   0.20 30.11  ? 143 ASP F CA    1 
ATOM   15366 C  CA    B ASP C 3 143 ? 54.599  -6.006  2.517   0.80 29.18  ? 143 ASP F CA    1 
ATOM   15367 C  C     A ASP C 3 143 ? 54.489  -4.320  2.756   0.20 34.13  ? 143 ASP F C     1 
ATOM   15368 C  C     B ASP C 3 143 ? 54.514  -4.561  3.007   0.80 33.57  ? 143 ASP F C     1 
ATOM   15369 O  O     A ASP C 3 143 ? 55.214  -3.775  3.592   0.20 32.58  ? 143 ASP F O     1 
ATOM   15370 O  O     B ASP C 3 143 ? 55.045  -4.205  4.065   0.80 35.34  ? 143 ASP F O     1 
ATOM   15371 C  CB    A ASP C 3 143 ? 53.325  -6.500  2.103   0.20 30.45  ? 143 ASP F CB    1 
ATOM   15372 C  CB    B ASP C 3 143 ? 53.234  -6.626  2.168   0.80 30.10  ? 143 ASP F CB    1 
ATOM   15373 C  CG    A ASP C 3 143 ? 52.310  -6.373  3.226   0.20 32.66  ? 143 ASP F CG    1 
ATOM   15374 C  CG    B ASP C 3 143 ? 52.228  -6.637  3.329   0.80 31.68  ? 143 ASP F CG    1 
ATOM   15375 O  OD1   A ASP C 3 143 ? 52.722  -6.260  4.400   0.20 34.41  ? 143 ASP F OD1   1 
ATOM   15376 O  OD1   B ASP C 3 143 ? 52.391  -5.902  4.324   0.80 32.78  ? 143 ASP F OD1   1 
ATOM   15377 O  OD2   A ASP C 3 143 ? 51.097  -6.389  2.930   0.20 33.96  ? 143 ASP F OD2   1 
ATOM   15378 O  OD2   B ASP C 3 143 ? 51.246  -7.409  3.234   0.80 36.68  ? 143 ASP F OD2   1 
ATOM   15379 N  N     A LYS C 3 144 ? 53.544  -3.643  2.099   0.20 36.98  ? 144 LYS F N     1 
ATOM   15380 N  N     B LYS C 3 144 ? 53.873  -3.699  2.220   0.80 37.67  ? 144 LYS F N     1 
ATOM   15381 C  CA    A LYS C 3 144 ? 53.287  -2.246  2.432   0.20 39.74  ? 144 LYS F CA    1 
ATOM   15382 C  CA    B LYS C 3 144 ? 53.834  -2.291  2.592   0.80 39.70  ? 144 LYS F CA    1 
ATOM   15383 C  C     A LYS C 3 144 ? 52.701  -2.120  3.830   0.20 39.27  ? 144 LYS F C     1 
ATOM   15384 C  C     B LYS C 3 144 ? 53.060  -2.072  3.879   0.80 38.42  ? 144 LYS F C     1 
ATOM   15385 O  O     A LYS C 3 144 ? 52.995  -1.159  4.550   0.20 42.37  ? 144 LYS F O     1 
ATOM   15386 O  O     B LYS C 3 144 ? 53.211  -1.020  4.508   0.80 42.50  ? 144 LYS F O     1 
ATOM   15387 C  CB    A LYS C 3 144 ? 52.353  -1.619  1.398   0.20 40.07  ? 144 LYS F CB    1 
ATOM   15388 C  CB    B LYS C 3 144 ? 53.234  -1.460  1.459   0.80 40.74  ? 144 LYS F CB    1 
ATOM   15389 C  CG    A LYS C 3 144 ? 53.022  -1.301  0.074   0.20 42.68  ? 144 LYS F CG    1 
ATOM   15390 C  CG    B LYS C 3 144 ? 54.152  -1.299  0.253   0.80 49.33  ? 144 LYS F CG    1 
ATOM   15391 C  CD    A LYS C 3 144 ? 54.104  -0.246  0.243   0.20 46.46  ? 144 LYS F CD    1 
ATOM   15392 C  CD    B LYS C 3 144 ? 55.332  -0.368  0.549   0.80 53.78  ? 144 LYS F CD    1 
ATOM   15393 C  CE    A LYS C 3 144 ? 54.803  0.051   -1.074  0.20 39.97  ? 144 LYS F CE    1 
ATOM   15394 C  CE    B LYS C 3 144 ? 56.592  -1.134  0.938   0.80 53.55  ? 144 LYS F CE    1 
ATOM   15395 N  NZ    A LYS C 3 144 ? 55.848  1.100   -0.914  0.20 43.32  ? 144 LYS F NZ    1 
ATOM   15396 N  NZ    B LYS C 3 144 ? 57.637  -0.233  1.497   0.80 65.94  ? 144 LYS F NZ    1 
ATOM   15397 N  N     A PHE C 3 145 ? 51.872  -3.082  4.232   0.20 39.78  ? 145 PHE F N     1 
ATOM   15398 N  N     B PHE C 3 145 ? 52.252  -3.048  4.280   0.80 37.99  ? 145 PHE F N     1 
ATOM   15399 C  CA    A PHE C 3 145 ? 51.251  -3.083  5.550   0.20 39.13  ? 145 PHE F CA    1 
ATOM   15400 C  CA    B PHE C 3 145 ? 51.475  -3.003  5.510   0.80 38.14  ? 145 PHE F CA    1 
ATOM   15401 C  C     A PHE C 3 145 ? 52.156  -3.660  6.631   0.20 41.36  ? 145 PHE F C     1 
ATOM   15402 C  C     B PHE C 3 145 ? 52.238  -3.590  6.693   0.80 41.64  ? 145 PHE F C     1 
ATOM   15403 O  O     A PHE C 3 145 ? 51.783  -3.634  7.810   0.20 42.01  ? 145 PHE F O     1 
ATOM   15404 O  O     B PHE C 3 145 ? 51.670  -3.729  7.782   0.80 42.34  ? 145 PHE F O     1 
ATOM   15405 C  CB    A PHE C 3 145 ? 49.936  -3.868  5.505   0.20 45.60  ? 145 PHE F CB    1 
ATOM   15406 C  CB    B PHE C 3 145 ? 50.153  -3.751  5.313   0.80 45.33  ? 145 PHE F CB    1 
ATOM   15407 C  CG    A PHE C 3 145 ? 48.839  -3.178  4.742   0.20 51.63  ? 145 PHE F CG    1 
ATOM   15408 C  CG    B PHE C 3 145 ? 49.197  -3.072  4.369   0.80 49.64  ? 145 PHE F CG    1 
ATOM   15409 C  CD1   A PHE C 3 145 ? 48.878  -3.098  3.359   0.20 50.05  ? 145 PHE F CD1   1 
ATOM   15410 C  CD1   B PHE C 3 145 ? 49.517  -2.899  3.030   0.80 49.90  ? 145 PHE F CD1   1 
ATOM   15411 C  CD2   A PHE C 3 145 ? 47.761  -2.620  5.410   0.20 57.69  ? 145 PHE F CD2   1 
ATOM   15412 C  CD2   B PHE C 3 145 ? 47.962  -2.629  4.819   0.80 60.68  ? 145 PHE F CD2   1 
ATOM   15413 C  CE1   A PHE C 3 145 ? 47.869  -2.463  2.657   0.20 55.19  ? 145 PHE F CE1   1 
ATOM   15414 C  CE1   B PHE C 3 145 ? 48.638  -2.277  2.162   0.80 55.60  ? 145 PHE F CE1   1 
ATOM   15415 C  CE2   A PHE C 3 145 ? 46.748  -1.986  4.715   0.20 60.03  ? 145 PHE F CE2   1 
ATOM   15416 C  CE2   B PHE C 3 145 ? 47.078  -2.003  3.957   0.80 62.70  ? 145 PHE F CE2   1 
ATOM   15417 C  CZ    A PHE C 3 145 ? 46.801  -1.908  3.337   0.20 61.06  ? 145 PHE F CZ    1 
ATOM   15418 C  CZ    B PHE C 3 145 ? 47.417  -1.830  2.626   0.80 59.08  ? 145 PHE F CZ    1 
ATOM   15419 N  N     A GLY C 3 146 ? 53.329  -4.173  6.266   0.20 36.75  ? 146 GLY F N     1 
ATOM   15420 N  N     B GLY C 3 146 ? 53.508  -3.942  6.497   0.80 36.13  ? 146 GLY F N     1 
ATOM   15421 C  CA    A GLY C 3 146 ? 54.224  -4.764  7.238   0.20 37.80  ? 146 GLY F CA    1 
ATOM   15422 C  CA    B GLY C 3 146 ? 54.327  -4.529  7.532   0.80 39.63  ? 146 GLY F CA    1 
ATOM   15423 C  C     A GLY C 3 146 ? 53.886  -6.180  7.634   0.20 35.48  ? 146 GLY F C     1 
ATOM   15424 C  C     B GLY C 3 146 ? 54.181  -6.022  7.704   0.80 35.31  ? 146 GLY F C     1 
ATOM   15425 O  O     A GLY C 3 146 ? 54.328  -6.637  8.694   0.20 35.71  ? 146 GLY F O     1 
ATOM   15426 O  O     B GLY C 3 146 ? 54.868  -6.595  8.561   0.80 38.08  ? 146 GLY F O     1 
ATOM   15427 N  N     A LYS C 3 147 ? 53.118  -6.897  6.815   0.20 32.94  ? 147 LYS F N     1 
ATOM   15428 N  N     B LYS C 3 147 ? 53.324  -6.676  6.919   0.80 31.72  ? 147 LYS F N     1 
ATOM   15429 C  CA    A LYS C 3 147 ? 52.653  -8.241  7.140   0.20 32.24  ? 147 LYS F CA    1 
ATOM   15430 C  CA    B LYS C 3 147 ? 52.986  -8.078  7.142   0.80 31.07  ? 147 LYS F CA    1 
ATOM   15431 C  C     A LYS C 3 147 ? 53.498  -9.265  6.390   0.20 34.45  ? 147 LYS F C     1 
ATOM   15432 C  C     B LYS C 3 147 ? 53.973  -8.992  6.429   0.80 36.81  ? 147 LYS F C     1 
ATOM   15433 O  O     A LYS C 3 147 ? 53.434  -9.352  5.159   0.20 25.47  ? 147 LYS F O     1 
ATOM   15434 O  O     B LYS C 3 147 ? 54.343  -8.738  5.281   0.80 30.27  ? 147 LYS F O     1 
ATOM   15435 C  CB    A LYS C 3 147 ? 51.175  -8.402  6.792   0.20 36.61  ? 147 LYS F CB    1 
ATOM   15436 C  CB    B LYS C 3 147 ? 51.568  -8.380  6.649   0.80 34.42  ? 147 LYS F CB    1 
ATOM   15437 C  CG    A LYS C 3 147 ? 50.231  -7.693  7.746   0.20 37.07  ? 147 LYS F CG    1 
ATOM   15438 C  CG    B LYS C 3 147 ? 50.466  -7.544  7.305   0.80 37.94  ? 147 LYS F CG    1 
ATOM   15439 C  CD    A LYS C 3 147 ? 48.786  -8.037  7.438   0.20 42.23  ? 147 LYS F CD    1 
ATOM   15440 C  CD    B LYS C 3 147 ? 50.554  -7.602  8.812   0.80 42.95  ? 147 LYS F CD    1 
ATOM   15441 C  CE    A LYS C 3 147 ? 47.857  -7.522  8.526   0.20 53.83  ? 147 LYS F CE    1 
ATOM   15442 C  CE    B LYS C 3 147 ? 49.613  -6.589  9.448   0.80 51.32  ? 147 LYS F CE    1 
ATOM   15443 N  NZ    A LYS C 3 147 ? 48.206  -8.090  9.859   0.20 48.45  ? 147 LYS F NZ    1 
ATOM   15444 N  NZ    B LYS C 3 147 ? 48.190  -6.879  9.100   0.80 62.39  ? 147 LYS F NZ    1 
ATOM   15445 N  N     A THR C 3 148 ? 54.273  -10.049 7.135   0.20 31.54  ? 148 THR F N     1 
ATOM   15446 N  N     B THR C 3 148 ? 54.394  -10.058 7.112   0.80 31.38  ? 148 THR F N     1 
ATOM   15447 C  CA    A THR C 3 148 ? 55.040  -11.128 6.536   0.20 32.81  ? 148 THR F CA    1 
ATOM   15448 C  CA    B THR C 3 148 ? 55.137  -11.129 6.463   0.80 32.53  ? 148 THR F CA    1 
ATOM   15449 C  C     A THR C 3 148 ? 54.110  -12.264 6.114   0.20 35.78  ? 148 THR F C     1 
ATOM   15450 C  C     B THR C 3 148 ? 54.175  -12.252 6.095   0.80 36.14  ? 148 THR F C     1 
ATOM   15451 O  O     A THR C 3 148 ? 52.908  -12.266 6.401   0.20 33.08  ? 148 THR F O     1 
ATOM   15452 O  O     B THR C 3 148 ? 53.009  -12.270 6.509   0.80 33.07  ? 148 THR F O     1 
ATOM   15453 C  CB    A THR C 3 148 ? 56.097  -11.648 7.512   0.20 33.73  ? 148 THR F CB    1 
ATOM   15454 C  CB    B THR C 3 148 ? 56.265  -11.679 7.352   0.80 33.65  ? 148 THR F CB    1 
ATOM   15455 O  OG1   A THR C 3 148 ? 55.464  -12.051 8.732   0.20 34.90  ? 148 THR F OG1   1 
ATOM   15456 O  OG1   B THR C 3 148 ? 55.716  -12.513 8.378   0.80 37.68  ? 148 THR F OG1   1 
ATOM   15457 C  CG2   A THR C 3 148 ? 57.131  -10.570 7.814   0.20 33.31  ? 148 THR F CG2   1 
ATOM   15458 C  CG2   B THR C 3 148 ? 57.079  -10.556 7.996   0.80 33.02  ? 148 THR F CG2   1 
ATOM   15459 N  N     A ALA C 3 149 ? 54.685  -13.246 5.414   0.20 34.23  ? 149 ALA F N     1 
ATOM   15460 N  N     B ALA C 3 149 ? 54.677  -13.197 5.295   0.80 34.16  ? 149 ALA F N     1 
ATOM   15461 C  CA    A ALA C 3 149 ? 53.909  -14.416 5.019   0.20 29.20  ? 149 ALA F CA    1 
ATOM   15462 C  CA    B ALA C 3 149 ? 53.888  -14.386 4.989   0.80 28.85  ? 149 ALA F CA    1 
ATOM   15463 C  C     A ALA C 3 149 ? 53.379  -15.162 6.237   0.20 34.56  ? 149 ALA F C     1 
ATOM   15464 C  C     B ALA C 3 149 ? 53.363  -15.044 6.263   0.80 34.66  ? 149 ALA F C     1 
ATOM   15465 O  O     A ALA C 3 149 ? 52.256  -15.681 6.217   0.20 33.34  ? 149 ALA F O     1 
ATOM   15466 O  O     B ALA C 3 149 ? 52.185  -15.420 6.335   0.80 32.53  ? 149 ALA F O     1 
ATOM   15467 C  CB    A ALA C 3 149 ? 54.758  -15.342 4.148   0.20 32.59  ? 149 ALA F CB    1 
ATOM   15468 C  CB    B ALA C 3 149 ? 54.722  -15.377 4.172   0.80 32.54  ? 149 ALA F CB    1 
ATOM   15469 N  N     A PHE C 3 150 ? 54.168  -15.218 7.314   0.20 32.94  ? 150 PHE F N     1 
ATOM   15470 N  N     B PHE C 3 150 ? 54.207  -15.152 7.296   0.80 32.98  ? 150 PHE F N     1 
ATOM   15471 C  CA    A PHE C 3 150 ? 53.698  -15.873 8.530   0.20 33.45  ? 150 PHE F CA    1 
ATOM   15472 C  CA    B PHE C 3 150 ? 53.744  -15.742 8.550   0.80 33.26  ? 150 PHE F CA    1 
ATOM   15473 C  C     A PHE C 3 150 ? 52.649  -15.037 9.251   0.20 36.06  ? 150 PHE F C     1 
ATOM   15474 C  C     B PHE C 3 150 ? 52.637  -14.909 9.190   0.80 35.98  ? 150 PHE F C     1 
ATOM   15475 O  O     A PHE C 3 150 ? 51.732  -15.595 9.865   0.20 37.00  ? 150 PHE F O     1 
ATOM   15476 O  O     B PHE C 3 150 ? 51.674  -15.464 9.733   0.80 37.18  ? 150 PHE F O     1 
ATOM   15477 C  CB    A PHE C 3 150 ? 54.873  -16.171 9.462   0.20 38.68  ? 150 PHE F CB    1 
ATOM   15478 C  CB    B PHE C 3 150 ? 54.905  -15.925 9.530   0.80 39.53  ? 150 PHE F CB    1 
ATOM   15479 C  CG    A PHE C 3 150 ? 54.494  -16.979 10.671  0.20 35.42  ? 150 PHE F CG    1 
ATOM   15480 C  CG    B PHE C 3 150 ? 54.580  -16.860 10.676  0.80 35.08  ? 150 PHE F CG    1 
ATOM   15481 C  CD1   A PHE C 3 150 ? 54.115  -18.306 10.541  0.20 36.82  ? 150 PHE F CD1   1 
ATOM   15482 C  CD1   B PHE C 3 150 ? 53.917  -16.398 11.804  0.80 45.23  ? 150 PHE F CD1   1 
ATOM   15483 C  CD2   A PHE C 3 150 ? 54.519  -16.416 11.936  0.20 40.03  ? 150 PHE F CD2   1 
ATOM   15484 C  CD2   B PHE C 3 150 ? 54.923  -18.201 10.612  0.80 38.76  ? 150 PHE F CD2   1 
ATOM   15485 C  CE1   A PHE C 3 150 ? 53.764  -19.055 11.647  0.20 39.04  ? 150 PHE F CE1   1 
ATOM   15486 C  CE1   B PHE C 3 150 ? 53.606  -17.261 12.850  0.80 37.47  ? 150 PHE F CE1   1 
ATOM   15487 C  CE2   A PHE C 3 150 ? 54.168  -17.161 13.050  0.20 38.68  ? 150 PHE F CE2   1 
ATOM   15488 C  CE2   B PHE C 3 150 ? 54.621  -19.067 11.649  0.80 38.09  ? 150 PHE F CE2   1 
ATOM   15489 C  CZ    A PHE C 3 150 ? 53.791  -18.483 12.904  0.20 38.61  ? 150 PHE F CZ    1 
ATOM   15490 C  CZ    B PHE C 3 150 ? 53.964  -18.596 12.774  0.80 38.69  ? 150 PHE F CZ    1 
ATOM   15491 N  N     A ASP C 3 151 ? 52.762  -13.708 9.191   0.20 34.76  ? 151 ASP F N     1 
ATOM   15492 N  N     B ASP C 3 151 ? 52.759  -13.577 9.148   0.80 34.64  ? 151 ASP F N     1 
ATOM   15493 C  CA    A ASP C 3 151 ? 51.747  -12.852 9.794   0.20 35.55  ? 151 ASP F CA    1 
ATOM   15494 C  CA    B ASP C 3 151 ? 51.695  -12.715 9.659   0.80 35.60  ? 151 ASP F CA    1 
ATOM   15495 C  C     A ASP C 3 151 ? 50.405  -12.990 9.087   0.20 37.10  ? 151 ASP F C     1 
ATOM   15496 C  C     B ASP C 3 151 ? 50.361  -13.030 8.989   0.80 37.18  ? 151 ASP F C     1 
ATOM   15497 O  O     A ASP C 3 151 ? 49.354  -12.842 9.719   0.20 33.89  ? 151 ASP F O     1 
ATOM   15498 O  O     B ASP C 3 151 ? 49.323  -13.103 9.654   0.80 31.63  ? 151 ASP F O     1 
ATOM   15499 C  CB    A ASP C 3 151 ? 52.209  -11.394 9.780   0.20 34.76  ? 151 ASP F CB    1 
ATOM   15500 C  CB    B ASP C 3 151 ? 52.057  -11.239 9.449   0.80 33.90  ? 151 ASP F CB    1 
ATOM   15501 C  CG    A ASP C 3 151 ? 53.359  -11.137 10.734  0.20 37.52  ? 151 ASP F CG    1 
ATOM   15502 C  CG    B ASP C 3 151 ? 53.129  -10.739 10.413  0.80 39.16  ? 151 ASP F CG    1 
ATOM   15503 O  OD1   A ASP C 3 151 ? 53.343  -11.703 11.848  0.20 38.42  ? 151 ASP F OD1   1 
ATOM   15504 O  OD1   B ASP C 3 151 ? 52.979  -10.935 11.637  0.80 36.52  ? 151 ASP F OD1   1 
ATOM   15505 O  OD2   A ASP C 3 151 ? 54.282  -10.374 10.372  0.20 37.64  ? 151 ASP F OD2   1 
ATOM   15506 O  OD2   B ASP C 3 151 ? 54.125  -10.132 9.949   0.80 38.79  ? 151 ASP F OD2   1 
ATOM   15507 N  N     A ILE C 3 152 ? 50.420  -13.269 7.782   0.20 33.40  ? 152 ILE F N     1 
ATOM   15508 N  N     B ILE C 3 152 ? 50.368  -13.214 7.669   0.80 33.15  ? 152 ILE F N     1 
ATOM   15509 C  CA    A ILE C 3 152 ? 49.172  -13.499 7.063   0.20 36.26  ? 152 ILE F CA    1 
ATOM   15510 C  CA    B ILE C 3 152 ? 49.135  -13.542 6.961   0.80 36.25  ? 152 ILE F CA    1 
ATOM   15511 C  C     A ILE C 3 152 ? 48.498  -14.773 7.557   0.20 36.75  ? 152 ILE F C     1 
ATOM   15512 C  C     B ILE C 3 152 ? 48.533  -14.836 7.496   0.80 36.77  ? 152 ILE F C     1 
ATOM   15513 O  O     A ILE C 3 152 ? 47.282  -14.801 7.774   0.20 34.12  ? 152 ILE F O     1 
ATOM   15514 O  O     B ILE C 3 152 ? 47.319  -14.927 7.716   0.80 33.62  ? 152 ILE F O     1 
ATOM   15515 C  CB    A ILE C 3 152 ? 49.432  -13.548 5.545   0.20 33.65  ? 152 ILE F CB    1 
ATOM   15516 C  CB    B ILE C 3 152 ? 49.399  -13.624 5.446   0.80 33.62  ? 152 ILE F CB    1 
ATOM   15517 C  CG1   A ILE C 3 152 ? 49.838  -12.168 5.026   0.20 32.67  ? 152 ILE F CG1   1 
ATOM   15518 C  CG1   B ILE C 3 152 ? 49.658  -12.227 4.881   0.80 32.30  ? 152 ILE F CG1   1 
ATOM   15519 C  CG2   A ILE C 3 152 ? 48.205  -14.063 4.805   0.20 30.31  ? 152 ILE F CG2   1 
ATOM   15520 C  CG2   B ILE C 3 152 ? 48.241  -14.320 4.742   0.80 29.17  ? 152 ILE F CG2   1 
ATOM   15521 C  CD1   A ILE C 3 152 ? 50.139  -12.144 3.541   0.20 33.35  ? 152 ILE F CD1   1 
ATOM   15522 C  CD1   B ILE C 3 152 ? 50.804  -12.183 3.876   0.80 35.21  ? 152 ILE F CD1   1 
ATOM   15523 N  N     A SER C 3 153 ? 49.278  -15.840 7.753   0.20 33.91  ? 153 SER F N     1 
ATOM   15524 N  N     B SER C 3 153 ? 49.367  -15.856 7.709   0.80 33.48  ? 153 SER F N     1 
ATOM   15525 C  CA    A SER C 3 153 ? 48.704  -17.119 8.159   0.20 32.81  ? 153 SER F CA    1 
ATOM   15526 C  CA    B SER C 3 153 ? 48.860  -17.135 8.193   0.80 32.19  ? 153 SER F CA    1 
ATOM   15527 C  C     A SER C 3 153 ? 48.092  -17.043 9.552   0.20 38.00  ? 153 SER F C     1 
ATOM   15528 C  C     B SER C 3 153 ? 48.287  -17.022 9.599   0.80 38.14  ? 153 SER F C     1 
ATOM   15529 O  O     A SER C 3 153 ? 47.069  -17.683 9.822   0.20 38.27  ? 153 SER F O     1 
ATOM   15530 O  O     B SER C 3 153 ? 47.408  -17.811 9.967   0.80 38.69  ? 153 SER F O     1 
ATOM   15531 C  CB    A SER C 3 153 ? 49.770  -18.213 8.108   0.20 35.52  ? 153 SER F CB    1 
ATOM   15532 C  CB    B SER C 3 153 ? 49.967  -18.188 8.178   0.80 35.69  ? 153 SER F CB    1 
ATOM   15533 O  OG    A SER C 3 153 ? 50.813  -17.950 9.032   0.20 40.97  ? 153 SER F OG    1 
ATOM   15534 O  OG    B SER C 3 153 ? 50.919  -17.937 9.202   0.80 42.48  ? 153 SER F OG    1 
ATOM   15535 N  N     A ILE C 3 154 ? 48.704  -16.271 10.453  0.20 38.78  ? 154 ILE F N     1 
ATOM   15536 N  N     B ILE C 3 154 ? 48.768  -16.070 10.402  0.80 38.63  ? 154 ILE F N     1 
ATOM   15537 C  CA    A ILE C 3 154 ? 48.184  -16.181 11.815  0.20 37.97  ? 154 ILE F CA    1 
ATOM   15538 C  CA    B ILE C 3 154 ? 48.248  -15.929 11.761  0.80 37.51  ? 154 ILE F CA    1 
ATOM   15539 C  C     A ILE C 3 154 ? 46.900  -15.361 11.847  0.20 42.66  ? 154 ILE F C     1 
ATOM   15540 C  C     B ILE C 3 154 ? 46.972  -15.100 11.772  0.80 44.41  ? 154 ILE F C     1 
ATOM   15541 O  O     A ILE C 3 154 ? 45.976  -15.660 12.613  0.20 41.74  ? 154 ILE F O     1 
ATOM   15542 O  O     B ILE C 3 154 ? 45.981  -15.477 12.411  0.80 42.35  ? 154 ILE F O     1 
ATOM   15543 C  CB    A ILE C 3 154 ? 49.257  -15.603 12.756  0.20 38.86  ? 154 ILE F CB    1 
ATOM   15544 C  CB    B ILE C 3 154 ? 49.320  -15.337 12.691  0.80 38.12  ? 154 ILE F CB    1 
ATOM   15545 C  CG1   A ILE C 3 154 ? 50.487  -16.511 12.775  0.20 41.52  ? 154 ILE F CG1   1 
ATOM   15546 C  CG1   B ILE C 3 154 ? 50.319  -16.422 13.058  0.80 41.69  ? 154 ILE F CG1   1 
ATOM   15547 C  CG2   A ILE C 3 154 ? 48.709  -15.439 14.166  0.20 43.80  ? 154 ILE F CG2   1 
ATOM   15548 C  CG2   B ILE C 3 154 ? 48.685  -14.779 13.955  0.80 48.30  ? 154 ILE F CG2   1 
ATOM   15549 C  CD1   A ILE C 3 154 ? 50.182  -17.935 13.183  0.20 44.10  ? 154 ILE F CD1   1 
ATOM   15550 C  CD1   B ILE C 3 154 ? 49.661  -17.713 13.482  0.80 45.47  ? 154 ILE F CD1   1 
ATOM   15551 N  N     A ASP C 3 155 ? 46.809  -14.331 11.000  0.20 41.38  ? 155 ASP F N     1 
ATOM   15552 N  N     B ASP C 3 155 ? 46.965  -13.972 11.050  0.80 41.90  ? 155 ASP F N     1 
ATOM   15553 C  CA    A ASP C 3 155 ? 45.646  -13.447 11.033  0.20 39.76  ? 155 ASP F CA    1 
ATOM   15554 C  CA    B ASP C 3 155 ? 45.770  -13.135 10.977  0.80 38.85  ? 155 ASP F CA    1 
ATOM   15555 C  C     A ASP C 3 155 ? 44.397  -14.134 10.493  0.20 42.87  ? 155 ASP F C     1 
ATOM   15556 C  C     B ASP C 3 155 ? 44.609  -13.828 10.270  0.80 43.85  ? 155 ASP F C     1 
ATOM   15557 O  O     A ASP C 3 155 ? 43.308  -13.984 11.060  0.20 39.96  ? 155 ASP F O     1 
ATOM   15558 O  O     B ASP C 3 155 ? 43.458  -13.395 10.415  0.80 42.51  ? 155 ASP F O     1 
ATOM   15559 C  CB    A ASP C 3 155 ? 45.933  -12.170 10.242  0.20 41.92  ? 155 ASP F CB    1 
ATOM   15560 C  CB    B ASP C 3 155 ? 46.088  -11.815 10.268  0.80 41.99  ? 155 ASP F CB    1 
ATOM   15561 C  CG    A ASP C 3 155 ? 46.947  -11.275 10.925  0.20 43.66  ? 155 ASP F CG    1 
ATOM   15562 C  CG    B ASP C 3 155 ? 47.134  -10.990 10.997  0.80 44.62  ? 155 ASP F CG    1 
ATOM   15563 O  OD1   A ASP C 3 155 ? 47.435  -11.645 12.013  0.20 44.58  ? 155 ASP F OD1   1 
ATOM   15564 O  OD1   B ASP C 3 155 ? 47.598  -11.410 12.080  0.80 45.04  ? 155 ASP F OD1   1 
ATOM   15565 O  OD2   A ASP C 3 155 ? 47.255  -10.200 10.371  0.20 44.93  ? 155 ASP F OD2   1 
ATOM   15566 O  OD2   B ASP C 3 155 ? 47.505  -9.919  10.477  0.80 46.50  ? 155 ASP F OD2   1 
ATOM   15567 N  N     A ASN C 3 156 ? 44.527  -14.885 9.400   0.20 38.70  ? 156 ASN F N     1 
ATOM   15568 N  N     B ASN C 3 156 ? 44.876  -14.891 9.515   0.80 37.79  ? 156 ASN F N     1 
ATOM   15569 C  CA    A ASN C 3 156 ? 43.384  -15.486 8.726   0.20 39.25  ? 156 ASN F CA    1 
ATOM   15570 C  CA    B ASN C 3 156 ? 43.834  -15.664 8.855   0.80 40.64  ? 156 ASN F CA    1 
ATOM   15571 C  C     A ASN C 3 156 ? 43.101  -16.914 9.180   0.20 39.33  ? 156 ASN F C     1 
ATOM   15572 C  C     B ASN C 3 156 ? 43.542  -16.982 9.558   0.80 39.92  ? 156 ASN F C     1 
ATOM   15573 O  O     A ASN C 3 156 ? 42.359  -17.630 8.499   0.20 39.01  ? 156 ASN F O     1 
ATOM   15574 O  O     B ASN C 3 156 ? 42.632  -17.700 9.138   0.80 40.90  ? 156 ASN F O     1 
ATOM   15575 C  CB    A ASN C 3 156 ? 43.591  -15.454 7.206   0.20 38.35  ? 156 ASN F CB    1 
ATOM   15576 C  CB    B ASN C 3 156 ? 44.222  -15.946 7.393   0.80 34.64  ? 156 ASN F CB    1 
ATOM   15577 C  CG    A ASN C 3 156 ? 44.729  -16.348 6.748   0.20 35.91  ? 156 ASN F CG    1 
ATOM   15578 C  CG    B ASN C 3 156 ? 44.067  -14.737 6.505   0.80 43.21  ? 156 ASN F CG    1 
ATOM   15579 O  OD1   A ASN C 3 156 ? 45.520  -16.834 7.553   0.20 33.95  ? 156 ASN F OD1   1 
ATOM   15580 O  OD1   B ASN C 3 156 ? 43.307  -13.818 6.818   0.80 51.61  ? 156 ASN F OD1   1 
ATOM   15581 N  ND2   A ASN C 3 156 ? 44.820  -16.562 5.442   0.20 36.52  ? 156 ASN F ND2   1 
ATOM   15582 N  ND2   B ASN C 3 156 ? 44.784  -14.729 5.384   0.80 40.67  ? 156 ASN F ND2   1 
ATOM   15583 N  N     A GLY C 3 157 ? 43.683  -17.344 10.298  0.20 38.90  ? 157 GLY F N     1 
ATOM   15584 N  N     B GLY C 3 157 ? 44.302  -17.324 10.597  0.80 39.53  ? 157 GLY F N     1 
ATOM   15585 C  CA    A GLY C 3 157 ? 43.420  -18.660 10.849  0.20 37.51  ? 157 GLY F CA    1 
ATOM   15586 C  CA    B GLY C 3 157 ? 44.128  -18.602 11.266  0.80 39.20  ? 157 GLY F CA    1 
ATOM   15587 C  C     A GLY C 3 157 ? 43.740  -19.818 9.926   0.20 37.33  ? 157 GLY F C     1 
ATOM   15588 C  C     B GLY C 3 157 ? 44.325  -19.810 10.377  0.80 41.29  ? 157 GLY F C     1 
ATOM   15589 O  O     A GLY C 3 157 ? 42.913  -20.714 9.738   0.20 35.28  ? 157 GLY F O     1 
ATOM   15590 O  O     B GLY C 3 157 ? 43.738  -20.867 10.639  0.80 33.58  ? 157 GLY F O     1 
ATOM   15591 N  N     A ASN C 3 158 ? 44.934  -19.823 9.345   0.20 35.77  ? 158 ASN F N     1 
ATOM   15592 N  N     B ASN C 3 158 ? 45.139  -19.694 9.328   0.80 34.23  ? 158 ASN F N     1 
ATOM   15593 C  CA    A ASN C 3 158 ? 45.365  -20.905 8.464   0.20 37.37  ? 158 ASN F CA    1 
ATOM   15594 C  CA    B ASN C 3 158 ? 45.372  -20.833 8.441   0.80 37.44  ? 158 ASN F CA    1 
ATOM   15595 C  C     A ASN C 3 158 ? 46.482  -21.661 9.179   0.20 36.76  ? 158 ASN F C     1 
ATOM   15596 C  C     B ASN C 3 158 ? 46.425  -21.719 9.085   0.80 36.70  ? 158 ASN F C     1 
ATOM   15597 O  O     A ASN C 3 158 ? 47.665  -21.358 9.011   0.20 34.98  ? 158 ASN F O     1 
ATOM   15598 O  O     B ASN C 3 158 ? 47.628  -21.490 8.936   0.80 34.68  ? 158 ASN F O     1 
ATOM   15599 C  CB    A ASN C 3 158 ? 45.820  -20.369 7.110   0.20 35.02  ? 158 ASN F CB    1 
ATOM   15600 C  CB    B ASN C 3 158 ? 45.809  -20.377 7.054   0.80 35.03  ? 158 ASN F CB    1 
ATOM   15601 C  CG    A ASN C 3 158 ? 45.872  -21.447 6.049   0.20 34.61  ? 158 ASN F CG    1 
ATOM   15602 C  CG    B ASN C 3 158 ? 45.831  -21.515 6.060   0.80 34.59  ? 158 ASN F CG    1 
ATOM   15603 O  OD1   A ASN C 3 158 ? 46.033  -22.627 6.355   0.20 37.34  ? 158 ASN F OD1   1 
ATOM   15604 O  OD1   B ASN C 3 158 ? 45.807  -22.685 6.440   0.80 37.71  ? 158 ASN F OD1   1 
ATOM   15605 N  ND2   A ASN C 3 158 ? 45.731  -21.047 4.792   0.20 36.81  ? 158 ASN F ND2   1 
ATOM   15606 N  ND2   B ASN C 3 158 ? 45.873  -21.183 4.780   0.80 37.11  ? 158 ASN F ND2   1 
ATOM   15607 N  N     A GLU C 3 159 ? 46.095  -22.651 9.988   0.20 39.44  ? 159 GLU F N     1 
ATOM   15608 N  N     B GLU C 3 159 ? 45.976  -22.746 9.805   0.80 40.26  ? 159 GLU F N     1 
ATOM   15609 C  CA    A GLU C 3 159 ? 47.090  -23.438 10.707  0.20 38.52  ? 159 GLU F CA    1 
ATOM   15610 C  CA    B GLU C 3 159 ? 46.915  -23.567 10.559  0.80 38.53  ? 159 GLU F CA    1 
ATOM   15611 C  C     A GLU C 3 159 ? 47.925  -24.291 9.761   0.20 37.46  ? 159 GLU F C     1 
ATOM   15612 C  C     B GLU C 3 159 ? 47.799  -24.418 9.651   0.80 37.45  ? 159 GLU F C     1 
ATOM   15613 O  O     A GLU C 3 159 ? 49.115  -24.507 10.014  0.20 36.65  ? 159 GLU F O     1 
ATOM   15614 O  O     B GLU C 3 159 ? 48.944  -24.711 10.010  0.80 35.39  ? 159 GLU F O     1 
ATOM   15615 C  CB    A GLU C 3 159 ? 46.412  -24.319 11.756  0.20 41.38  ? 159 GLU F CB    1 
ATOM   15616 C  CB    B GLU C 3 159 ? 46.154  -24.437 11.556  0.80 40.91  ? 159 GLU F CB    1 
ATOM   15617 C  CG    A GLU C 3 159 ? 45.620  -23.550 12.797  0.20 43.90  ? 159 GLU F CG    1 
ATOM   15618 C  CG    B GLU C 3 159 ? 45.580  -23.645 12.712  0.80 43.78  ? 159 GLU F CG    1 
ATOM   15619 C  CD    A GLU C 3 159 ? 45.160  -24.429 13.947  0.20 53.80  ? 159 GLU F CD    1 
ATOM   15620 C  CD    B GLU C 3 159 ? 44.865  -24.524 13.728  0.80 54.17  ? 159 GLU F CD    1 
ATOM   15621 O  OE1   A GLU C 3 159 ? 45.920  -25.341 14.343  0.20 48.10  ? 159 GLU F OE1   1 
ATOM   15622 O  OE1   B GLU C 3 159 ? 44.157  -25.464 13.307  0.80 60.35  ? 159 GLU F OE1   1 
ATOM   15623 O  OE2   A GLU C 3 159 ? 44.038  -24.211 14.452  0.20 55.02  ? 159 GLU F OE2   1 
ATOM   15624 O  OE2   B GLU C 3 159 ? 45.021  -24.278 14.945  0.80 61.66  ? 159 GLU F OE2   1 
ATOM   15625 N  N     A ASP C 3 160 ? 47.326  -24.783 8.673   0.20 38.98  ? 160 ASP F N     1 
ATOM   15626 N  N     B ASP C 3 160 ? 47.302  -24.826 8.480   0.80 39.04  ? 160 ASP F N     1 
ATOM   15627 C  CA    A ASP C 3 160 ? 48.078  -25.589 7.717   0.20 35.08  ? 160 ASP F CA    1 
ATOM   15628 C  CA    B ASP C 3 160 ? 48.149  -25.591 7.569   0.80 34.39  ? 160 ASP F CA    1 
ATOM   15629 C  C     A ASP C 3 160 ? 49.189  -24.775 7.065   0.20 36.13  ? 160 ASP F C     1 
ATOM   15630 C  C     B ASP C 3 160 ? 49.308  -24.746 7.054   0.80 36.01  ? 160 ASP F C     1 
ATOM   15631 O  O     A ASP C 3 160 ? 50.295  -25.283 6.845   0.20 35.99  ? 160 ASP F O     1 
ATOM   15632 O  O     B ASP C 3 160 ? 50.450  -25.216 7.001   0.80 35.58  ? 160 ASP F O     1 
ATOM   15633 C  CB    A ASP C 3 160 ? 47.134  -26.158 6.659   0.20 38.52  ? 160 ASP F CB    1 
ATOM   15634 C  CB    B ASP C 3 160 ? 47.325  -26.128 6.403   0.80 38.54  ? 160 ASP F CB    1 
ATOM   15635 C  CG    A ASP C 3 160 ? 46.104  -27.095 7.249   0.20 43.31  ? 160 ASP F CG    1 
ATOM   15636 C  CG    B ASP C 3 160 ? 46.347  -27.184 6.826   0.80 43.87  ? 160 ASP F CG    1 
ATOM   15637 O  OD1   A ASP C 3 160 ? 46.503  -28.135 7.814   0.20 44.93  ? 160 ASP F OD1   1 
ATOM   15638 O  OD1   B ASP C 3 160 ? 46.731  -28.053 7.635   0.80 45.35  ? 160 ASP F OD1   1 
ATOM   15639 O  OD2   A ASP C 3 160 ? 44.898  -26.784 7.163   0.20 41.96  ? 160 ASP F OD2   1 
ATOM   15640 O  OD2   B ASP C 3 160 ? 45.191  -27.140 6.356   0.80 51.14  ? 160 ASP F OD2   1 
ATOM   15641 N  N     A LEU C 3 161 ? 48.913  -23.509 6.748   0.20 33.24  ? 161 LEU F N     1 
ATOM   15642 N  N     B LEU C 3 161 ? 49.028  -23.499 6.671   0.80 32.83  ? 161 LEU F N     1 
ATOM   15643 C  CA    A LEU C 3 161 ? 49.953  -22.633 6.223   0.20 32.23  ? 161 LEU F CA    1 
ATOM   15644 C  CA    B LEU C 3 161 ? 50.076  -22.608 6.186   0.80 31.74  ? 161 LEU F CA    1 
ATOM   15645 C  C     A LEU C 3 161 ? 50.961  -22.259 7.301   0.20 37.88  ? 161 LEU F C     1 
ATOM   15646 C  C     B LEU C 3 161 ? 51.100  -22.319 7.273   0.80 38.67  ? 161 LEU F C     1 
ATOM   15647 O  O     A LEU C 3 161 ? 52.155  -22.115 7.010   0.20 32.11  ? 161 LEU F O     1 
ATOM   15648 O  O     B LEU C 3 161 ? 52.312  -22.343 7.020   0.80 29.78  ? 161 LEU F O     1 
ATOM   15649 C  CB    A LEU C 3 161 ? 49.321  -21.377 5.625   0.20 30.37  ? 161 LEU F CB    1 
ATOM   15650 C  CB    B LEU C 3 161 ? 49.452  -21.309 5.687   0.80 29.83  ? 161 LEU F CB    1 
ATOM   15651 C  CG    A LEU C 3 161 ? 50.253  -20.281 5.110   0.20 30.93  ? 161 LEU F CG    1 
ATOM   15652 C  CG    B LEU C 3 161 ? 50.379  -20.187 5.218   0.80 30.16  ? 161 LEU F CG    1 
ATOM   15653 C  CD1   A LEU C 3 161 ? 51.179  -20.825 4.031   0.20 31.84  ? 161 LEU F CD1   1 
ATOM   15654 C  CD1   B LEU C 3 161 ? 51.334  -20.709 4.147   0.80 32.11  ? 161 LEU F CD1   1 
ATOM   15655 C  CD2   A LEU C 3 161 ? 49.432  -19.116 4.583   0.20 32.49  ? 161 LEU F CD2   1 
ATOM   15656 C  CD2   B LEU C 3 161 ? 49.530  -19.053 4.676   0.80 32.62  ? 161 LEU F CD2   1 
ATOM   15657 N  N     A ALA C 3 162 ? 50.505  -22.104 8.545   0.20 32.71  ? 162 ALA F N     1 
ATOM   15658 N  N     B ALA C 3 162 ? 50.632  -22.033 8.491   0.80 32.12  ? 162 ALA F N     1 
ATOM   15659 C  CA    A ALA C 3 162 ? 51.416  -21.738 9.623   0.20 35.26  ? 162 ALA F CA    1 
ATOM   15660 C  CA    B ALA C 3 162 ? 51.561  -21.699 9.562   0.80 34.96  ? 162 ALA F CA    1 
ATOM   15661 C  C     A ALA C 3 162 ? 52.388  -22.869 9.936   0.20 37.80  ? 162 ALA F C     1 
ATOM   15662 C  C     B ALA C 3 162 ? 52.493  -22.864 9.855   0.80 37.73  ? 162 ALA F C     1 
ATOM   15663 O  O     A ALA C 3 162 ? 53.555  -22.618 10.254  0.20 43.25  ? 162 ALA F O     1 
ATOM   15664 O  O     B ALA C 3 162 ? 53.688  -22.661 10.091  0.80 44.38  ? 162 ALA F O     1 
ATOM   15665 C  CB    A ALA C 3 162 ? 50.625  -21.347 10.870  0.20 36.12  ? 162 ALA F CB    1 
ATOM   15666 C  CB    B ALA C 3 162 ? 50.798  -21.281 10.817  0.80 35.97  ? 162 ALA F CB    1 
ATOM   15667 N  N     A GLU C 3 163 ? 51.927  -24.120 9.848   0.20 35.56  ? 163 GLU F N     1 
ATOM   15668 N  N     B GLU C 3 163 ? 51.974  -24.093 9.820   0.80 35.27  ? 163 GLU F N     1 
ATOM   15669 C  CA    A GLU C 3 163 ? 52.808  -25.251 10.125  0.20 40.41  ? 163 GLU F CA    1 
ATOM   15670 C  CA    B GLU C 3 163 ? 52.835  -25.261 9.981   0.80 40.37  ? 163 GLU F CA    1 
ATOM   15671 C  C     A GLU C 3 163 ? 53.941  -25.328 9.110   0.20 43.67  ? 163 GLU F C     1 
ATOM   15672 C  C     B GLU C 3 163 ? 53.905  -25.290 8.898   0.80 44.34  ? 163 GLU F C     1 
ATOM   15673 O  O     A GLU C 3 163 ? 55.077  -25.667 9.461   0.20 44.23  ? 163 GLU F O     1 
ATOM   15674 O  O     B GLU C 3 163 ? 55.098  -25.424 9.191   0.80 44.21  ? 163 GLU F O     1 
ATOM   15675 C  CB    A GLU C 3 163 ? 52.009  -26.555 10.133  0.20 41.33  ? 163 GLU F CB    1 
ATOM   15676 C  CB    B GLU C 3 163 ? 52.005  -26.549 9.944   0.80 40.86  ? 163 GLU F CB    1 
ATOM   15677 C  CG    A GLU C 3 163 ? 51.047  -26.695 11.304  0.20 49.11  ? 163 GLU F CG    1 
ATOM   15678 C  CG    B GLU C 3 163 ? 51.103  -26.769 11.151  0.80 49.85  ? 163 GLU F CG    1 
ATOM   15679 C  CD    A GLU C 3 163 ? 50.180  -27.936 11.201  0.20 53.46  ? 163 GLU F CD    1 
ATOM   15680 C  CD    B GLU C 3 163 ? 50.109  -27.904 10.942  0.80 54.52  ? 163 GLU F CD    1 
ATOM   15681 O  OE1   A GLU C 3 163 ? 50.316  -28.680 10.206  0.20 54.89  ? 163 GLU F OE1   1 
ATOM   15682 O  OE1   B GLU C 3 163 ? 50.292  -28.701 9.995   0.80 55.89  ? 163 GLU F OE1   1 
ATOM   15683 O  OE2   A GLU C 3 163 ? 49.361  -28.168 12.116  0.20 53.76  ? 163 GLU F OE2   1 
ATOM   15684 O  OE2   B GLU C 3 163 ? 49.138  -27.989 11.723  0.80 53.36  ? 163 GLU F OE2   1 
ATOM   15685 N  N     A ILE C 3 164 ? 53.649  -25.015 7.845   0.20 39.20  ? 164 ILE F N     1 
ATOM   15686 N  N     B ILE C 3 164 ? 53.484  -25.152 7.638   0.80 38.73  ? 164 ILE F N     1 
ATOM   15687 C  CA    A ILE C 3 164 ? 54.683  -25.038 6.814   0.20 40.86  ? 164 ILE F CA    1 
ATOM   15688 C  CA    B ILE C 3 164 ? 54.413  -25.140 6.508   0.80 41.31  ? 164 ILE F CA    1 
ATOM   15689 C  C     A ILE C 3 164 ? 55.744  -23.986 7.101   0.20 42.27  ? 164 ILE F C     1 
ATOM   15690 C  C     B ILE C 3 164 ? 55.529  -24.134 6.745   0.80 42.04  ? 164 ILE F C     1 
ATOM   15691 O  O     A ILE C 3 164 ? 56.949  -24.252 7.003   0.20 44.19  ? 164 ILE F O     1 
ATOM   15692 O  O     B ILE C 3 164 ? 56.719  -24.439 6.575   0.80 44.55  ? 164 ILE F O     1 
ATOM   15693 C  CB    A ILE C 3 164 ? 54.053  -24.835 5.423   0.20 39.94  ? 164 ILE F CB    1 
ATOM   15694 C  CB    B ILE C 3 164 ? 53.655  -24.828 5.203   0.80 40.36  ? 164 ILE F CB    1 
ATOM   15695 C  CG1   A ILE C 3 164 ? 52.981  -25.894 5.155   0.20 40.82  ? 164 ILE F CG1   1 
ATOM   15696 C  CG1   B ILE C 3 164 ? 52.733  -25.989 4.819   0.80 40.67  ? 164 ILE F CG1   1 
ATOM   15697 C  CG2   A ILE C 3 164 ? 55.125  -24.862 4.348   0.20 40.93  ? 164 ILE F CG2   1 
ATOM   15698 C  CG2   B ILE C 3 164 ? 54.626  -24.505 4.089   0.80 41.70  ? 164 ILE F CG2   1 
ATOM   15699 C  CD1   A ILE C 3 164 ? 52.148  -25.619 3.919   0.20 37.43  ? 164 ILE F CD1   1 
ATOM   15700 C  CD1   B ILE C 3 164 ? 53.469  -27.261 4.489   0.80 39.45  ? 164 ILE F CD1   1 
ATOM   15701 N  N     A LEU C 3 165 ? 55.316  -22.775 7.462   0.20 37.72  ? 165 LEU F N     1 
ATOM   15702 N  N     B LEU C 3 165 ? 55.160  -22.918 7.154   0.80 34.69  ? 165 LEU F N     1 
ATOM   15703 C  CA    A LEU C 3 165 ? 56.246  -21.679 7.691   0.20 39.71  ? 165 LEU F CA    1 
ATOM   15704 C  CA    B LEU C 3 165 ? 56.118  -21.826 7.292   0.80 38.60  ? 165 LEU F CA    1 
ATOM   15705 C  C     A LEU C 3 165 ? 56.986  -21.796 9.018   0.20 45.02  ? 165 LEU F C     1 
ATOM   15706 C  C     B LEU C 3 165 ? 57.081  -22.010 8.459   0.80 44.22  ? 165 LEU F C     1 
ATOM   15707 O  O     A LEU C 3 165 ? 57.993  -21.107 9.211   0.20 48.87  ? 165 LEU F O     1 
ATOM   15708 O  O     B LEU C 3 165 ? 57.978  -21.175 8.628   0.80 53.11  ? 165 LEU F O     1 
ATOM   15709 C  CB    A LEU C 3 165 ? 55.503  -20.343 7.625   0.20 38.49  ? 165 LEU F CB    1 
ATOM   15710 C  CB    B LEU C 3 165 ? 55.374  -20.495 7.429   0.80 37.96  ? 165 LEU F CB    1 
ATOM   15711 C  CG    A LEU C 3 165 ? 54.739  -20.082 6.324   0.20 35.26  ? 165 LEU F CG    1 
ATOM   15712 C  CG    B LEU C 3 165 ? 54.767  -19.897 6.153   0.80 35.00  ? 165 LEU F CG    1 
ATOM   15713 C  CD1   A LEU C 3 165 ? 54.002  -18.755 6.385   0.20 31.96  ? 165 LEU F CD1   1 
ATOM   15714 C  CD1   B LEU C 3 165 ? 53.945  -18.668 6.488   0.80 31.52  ? 165 LEU F CD1   1 
ATOM   15715 C  CD2   A LEU C 3 165 ? 55.679  -20.121 5.126   0.20 36.67  ? 165 LEU F CD2   1 
ATOM   15716 C  CD2   B LEU C 3 165 ? 55.854  -19.537 5.133   0.80 35.24  ? 165 LEU F CD2   1 
ATOM   15717 N  N     A GLN C 3 166 ? 56.516  -22.646 9.933   0.20 45.26  ? 166 GLN F N     1 
ATOM   15718 N  N     B GLN C 3 166 ? 56.940  -23.067 9.253   0.80 45.92  ? 166 GLN F N     1 
ATOM   15719 C  CA    A GLN C 3 166 ? 57.224  -22.849 11.190  0.20 47.79  ? 166 GLN F CA    1 
ATOM   15720 C  CA    B GLN C 3 166 ? 57.843  -23.344 10.369  0.80 54.10  ? 166 GLN F CA    1 
ATOM   15721 C  C     A GLN C 3 166 ? 58.363  -23.853 11.069  0.20 52.06  ? 166 GLN F C     1 
ATOM   15722 C  C     B GLN C 3 166 ? 58.669  -24.581 10.023  0.80 53.70  ? 166 GLN F C     1 
ATOM   15723 O  O     A GLN C 3 166 ? 59.227  -23.895 11.951  0.20 49.77  ? 166 GLN F O     1 
ATOM   15724 O  O     B GLN C 3 166 ? 58.368  -25.698 10.451  0.80 60.53  ? 166 GLN F O     1 
ATOM   15725 C  CB    A GLN C 3 166 ? 56.254  -23.304 12.284  0.20 46.02  ? 166 GLN F CB    1 
ATOM   15726 C  CB    B GLN C 3 166 ? 57.060  -23.538 11.668  0.80 47.77  ? 166 GLN F CB    1 
ATOM   15727 C  CG    A GLN C 3 166 ? 55.376  -22.194 12.842  0.20 44.62  ? 166 GLN F CG    1 
ATOM   15728 C  CG    B GLN C 3 166 ? 56.247  -22.339 12.101  0.80 44.09  ? 166 GLN F CG    1 
ATOM   15729 C  CD    A GLN C 3 166 ? 54.509  -22.660 13.998  0.20 44.97  ? 166 GLN F CD    1 
ATOM   15730 C  CD    B GLN C 3 166 ? 55.610  -22.549 13.455  0.80 45.50  ? 166 GLN F CD    1 
ATOM   15731 O  OE1   A GLN C 3 166 ? 55.005  -22.921 15.095  0.20 44.09  ? 166 GLN F OE1   1 
ATOM   15732 O  OE1   B GLN C 3 166 ? 54.402  -22.362 13.626  0.80 45.37  ? 166 GLN F OE1   1 
ATOM   15733 N  NE2   A GLN C 3 166 ? 53.208  -22.770 13.757  0.20 36.90  ? 166 GLN F NE2   1 
ATOM   15734 N  NE2   B GLN C 3 166 ? 56.421  -22.946 14.433  0.80 52.22  ? 166 GLN F NE2   1 
ATOM   15735 N  N     A LYS C 3 167 ? 58.388  -24.654 10.007  0.20 53.31  ? 167 LYS F N     1 
ATOM   15736 N  N     B LYS C 3 167 ? 59.732  -24.373 9.247   0.80 61.03  ? 167 LYS F N     1 
ATOM   15737 C  CA    A LYS C 3 167 ? 59.468  -25.616 9.807   0.20 57.58  ? 167 LYS F CA    1 
ATOM   15738 C  CA    B LYS C 3 167 ? 60.579  -25.479 8.801   0.80 61.50  ? 167 LYS F CA    1 
ATOM   15739 C  C     A LYS C 3 167 ? 60.783  -24.898 9.516   0.20 58.62  ? 167 LYS F C     1 
ATOM   15740 C  C     B LYS C 3 167 ? 62.040  -25.068 8.625   0.80 69.05  ? 167 LYS F C     1 
ATOM   15741 O  O     A LYS C 3 167 ? 60.866  -24.079 8.600   0.20 56.60  ? 167 LYS F O     1 
ATOM   15742 O  O     B LYS C 3 167 ? 62.940  -25.913 8.645   0.80 61.15  ? 167 LYS F O     1 
ATOM   15743 C  CB    A LYS C 3 167 ? 59.138  -26.583 8.665   0.20 59.50  ? 167 LYS F CB    1 
ATOM   15744 C  CB    B LYS C 3 167 ? 60.035  -26.061 7.490   0.80 64.26  ? 167 LYS F CB    1 
ATOM   15745 C  CG    A LYS C 3 167 ? 57.919  -27.459 8.902   0.20 54.03  ? 167 LYS F CG    1 
ATOM   15746 C  CG    B LYS C 3 167 ? 59.026  -27.189 7.691   0.80 65.94  ? 167 LYS F CG    1 
ATOM   15747 C  CD    A LYS C 3 167 ? 57.860  -28.631 7.923   0.20 56.31  ? 167 LYS F CD    1 
ATOM   15748 C  CD    B LYS C 3 167 ? 58.229  -27.489 6.430   0.80 64.31  ? 167 LYS F CD    1 
ATOM   15749 C  CE    A LYS C 3 167 ? 57.806  -28.174 6.469   0.20 60.44  ? 167 LYS F CE    1 
ATOM   15750 C  CE    B LYS C 3 167 ? 59.126  -27.697 5.219   0.80 62.56  ? 167 LYS F CE    1 
ATOM   15751 N  NZ    A LYS C 3 167 ? 59.155  -28.063 5.838   0.20 62.25  ? 167 LYS F NZ    1 
ATOM   15752 N  NZ    B LYS C 3 167 ? 59.210  -26.472 4.372   0.80 56.49  ? 167 LYS F NZ    1 
HETATM 15753 P  PG    A GTP D 4 .   ? 2.371   -12.007 18.220  0.20 26.11  ? 501 GTP A PG    1 
HETATM 15754 P  PG    B GTP D 4 .   ? 2.318   -11.345 17.989  0.80 21.47  ? 501 GTP A PG    1 
HETATM 15755 O  O1G   A GTP D 4 .   ? 2.278   -13.477 18.547  0.20 24.24  ? 501 GTP A O1G   1 
HETATM 15756 O  O1G   B GTP D 4 .   ? 2.430   -12.846 18.150  0.80 25.81  ? 501 GTP A O1G   1 
HETATM 15757 O  O2G   A GTP D 4 .   ? 1.459   -11.665 17.065  0.20 22.60  ? 501 GTP A O2G   1 
HETATM 15758 O  O2G   B GTP D 4 .   ? 1.468   -10.980 16.801  0.80 24.27  ? 501 GTP A O2G   1 
HETATM 15759 O  O3G   A GTP D 4 .   ? 3.781   -11.676 17.814  0.20 24.99  ? 501 GTP A O3G   1 
HETATM 15760 O  O3G   B GTP D 4 .   ? 3.649   -10.649 18.006  0.80 23.19  ? 501 GTP A O3G   1 
HETATM 15761 O  O3B   A GTP D 4 .   ? 1.959   -11.144 19.521  0.20 23.24  ? 501 GTP A O3B   1 
HETATM 15762 O  O3B   B GTP D 4 .   ? 1.488   -10.759 19.260  0.80 24.77  ? 501 GTP A O3B   1 
HETATM 15763 P  PB    A GTP D 4 .   ? 0.932   -11.747 20.610  0.20 22.27  ? 501 GTP A PB    1 
HETATM 15764 P  PB    B GTP D 4 .   ? 0.899   -11.587 20.523  0.80 24.23  ? 501 GTP A PB    1 
HETATM 15765 O  O1B   A GTP D 4 .   ? 0.593   -10.674 21.618  0.20 21.39  ? 501 GTP A O1B   1 
HETATM 15766 O  O1B   B GTP D 4 .   ? -0.070  -10.597 21.107  0.80 20.13  ? 501 GTP A O1B   1 
HETATM 15767 O  O2B   A GTP D 4 .   ? -0.316  -12.271 19.944  0.20 22.32  ? 501 GTP A O2B   1 
HETATM 15768 O  O2B   B GTP D 4 .   ? 0.222   -12.889 20.205  0.80 19.52  ? 501 GTP A O2B   1 
HETATM 15769 O  O3A   A GTP D 4 .   ? 1.718   -12.947 21.332  0.20 14.55  ? 501 GTP A O3A   1 
HETATM 15770 O  O3A   B GTP D 4 .   ? 2.184   -11.792 21.458  0.80 20.09  ? 501 GTP A O3A   1 
HETATM 15771 P  PA    A GTP D 4 .   ? 1.698   -13.116 22.932  0.20 24.45  ? 501 GTP A PA    1 
HETATM 15772 P  PA    B GTP D 4 .   ? 2.221   -12.448 22.918  0.80 23.91  ? 501 GTP A PA    1 
HETATM 15773 O  O1A   A GTP D 4 .   ? 0.287   -12.883 23.417  0.20 22.21  ? 501 GTP A O1A   1 
HETATM 15774 O  O1A   B GTP D 4 .   ? 0.917   -12.190 23.609  0.80 21.50  ? 501 GTP A O1A   1 
HETATM 15775 O  O2A   A GTP D 4 .   ? 2.181   -14.503 23.284  0.20 24.17  ? 501 GTP A O2A   1 
HETATM 15776 O  O2A   B GTP D 4 .   ? 2.655   -13.896 22.802  0.80 23.32  ? 501 GTP A O2A   1 
HETATM 15777 O  "O5'" A GTP D 4 .   ? 2.674   -11.975 23.521  0.20 23.71  ? 501 GTP A "O5'" 1 
HETATM 15778 O  "O5'" B GTP D 4 .   ? 3.387   -11.559 23.572  0.80 24.41  ? 501 GTP A "O5'" 1 
HETATM 15779 C  "C5'" A GTP D 4 .   ? 4.007   -12.266 23.881  0.20 23.61  ? 501 GTP A "C5'" 1 
HETATM 15780 C  "C5'" B GTP D 4 .   ? 4.507   -12.126 24.200  0.80 23.85  ? 501 GTP A "C5'" 1 
HETATM 15781 C  "C4'" A GTP D 4 .   ? 4.202   -12.000 25.373  0.20 25.12  ? 501 GTP A "C4'" 1 
HETATM 15782 C  "C4'" B GTP D 4 .   ? 4.512   -11.738 25.685  0.80 23.07  ? 501 GTP A "C4'" 1 
HETATM 15783 O  "O4'" A GTP D 4 .   ? 3.058   -12.425 26.083  0.20 23.71  ? 501 GTP A "O4'" 1 
HETATM 15784 O  "O4'" B GTP D 4 .   ? 3.356   -12.241 26.346  0.80 23.95  ? 501 GTP A "O4'" 1 
HETATM 15785 C  "C3'" A GTP D 4 .   ? 5.389   -12.769 25.917  0.20 24.70  ? 501 GTP A "C3'" 1 
HETATM 15786 C  "C3'" B GTP D 4 .   ? 5.699   -12.384 26.352  0.80 18.96  ? 501 GTP A "C3'" 1 
HETATM 15787 O  "O3'" A GTP D 4 .   ? 6.321   -11.866 26.461  0.20 25.85  ? 501 GTP A "O3'" 1 
HETATM 15788 O  "O3'" B GTP D 4 .   ? 6.137   -11.558 27.396  0.80 25.02  ? 501 GTP A "O3'" 1 
HETATM 15789 C  "C2'" A GTP D 4 .   ? 4.850   -13.652 27.018  0.20 28.25  ? 501 GTP A "C2'" 1 
HETATM 15790 C  "C2'" B GTP D 4 .   ? 5.158   -13.680 26.892  0.80 28.13  ? 501 GTP A "C2'" 1 
HETATM 15791 O  "O2'" A GTP D 4 .   ? 5.617   -13.459 28.183  0.20 28.39  ? 501 GTP A "O2'" 1 
HETATM 15792 O  "O2'" B GTP D 4 .   ? 5.905   -14.119 28.007  0.80 23.66  ? 501 GTP A "O2'" 1 
HETATM 15793 C  "C1'" A GTP D 4 .   ? 3.404   -13.214 27.207  0.20 27.30  ? 501 GTP A "C1'" 1 
HETATM 15794 C  "C1'" B GTP D 4 .   ? 3.734   -13.279 27.249  0.80 28.46  ? 501 GTP A "C1'" 1 
HETATM 15795 N  N9    A GTP D 4 .   ? 2.494   -14.374 27.231  0.20 29.23  ? 501 GTP A N9    1 
HETATM 15796 N  N9    B GTP D 4 .   ? 2.763   -14.376 27.095  0.80 29.64  ? 501 GTP A N9    1 
HETATM 15797 C  C8    A GTP D 4 .   ? 2.052   -15.078 26.141  0.20 25.48  ? 501 GTP A C8    1 
HETATM 15798 C  C8    B GTP D 4 .   ? 2.396   -15.063 25.963  0.80 24.64  ? 501 GTP A C8    1 
HETATM 15799 N  N7    A GTP D 4 .   ? 1.218   -16.055 26.564  0.20 26.30  ? 501 GTP A N7    1 
HETATM 15800 N  N7    B GTP D 4 .   ? 1.426   -15.951 26.313  0.80 26.12  ? 501 GTP A N7    1 
HETATM 15801 C  C5    A GTP D 4 .   ? 1.107   -15.976 27.908  0.20 26.81  ? 501 GTP A C5    1 
HETATM 15802 C  C5    B GTP D 4 .   ? 1.149   -15.821 27.637  0.80 27.20  ? 501 GTP A C5    1 
HETATM 15803 C  C6    A GTP D 4 .   ? 0.390   -16.726 28.830  0.20 26.55  ? 501 GTP A C6    1 
HETATM 15804 C  C6    B GTP D 4 .   ? 0.272   -16.459 28.509  0.80 25.79  ? 501 GTP A C6    1 
HETATM 15805 O  O6    A GTP D 4 .   ? -0.315  -17.665 28.452  0.20 26.95  ? 501 GTP A O6    1 
HETATM 15806 O  O6    B GTP D 4 .   ? -0.484  -17.355 28.104  0.80 25.30  ? 501 GTP A O6    1 
HETATM 15807 N  N1    A GTP D 4 .   ? 0.473   -16.408 30.171  0.20 26.63  ? 501 GTP A N1    1 
HETATM 15808 N  N1    B GTP D 4 .   ? 0.245   -16.067 29.838  0.80 24.16  ? 501 GTP A N1    1 
HETATM 15809 C  C2    A GTP D 4 .   ? 1.268   -15.354 30.584  0.20 25.10  ? 501 GTP A C2    1 
HETATM 15810 C  C2    B GTP D 4 .   ? 1.100   -15.068 30.291  0.80 26.21  ? 501 GTP A C2    1 
HETATM 15811 N  N2    A GTP D 4 .   ? 1.348   -15.049 31.874  0.20 27.52  ? 501 GTP A N2    1 
HETATM 15812 N  N2    B GTP D 4 .   ? 1.097   -14.676 31.555  0.80 27.57  ? 501 GTP A N2    1 
HETATM 15813 N  N3    A GTP D 4 .   ? 1.979   -14.617 29.658  0.20 25.46  ? 501 GTP A N3    1 
HETATM 15814 N  N3    B GTP D 4 .   ? 1.969   -14.458 29.411  0.80 24.08  ? 501 GTP A N3    1 
HETATM 15815 C  C4    A GTP D 4 .   ? 1.898   -14.920 28.342  0.20 24.29  ? 501 GTP A C4    1 
HETATM 15816 C  C4    B GTP D 4 .   ? 1.979   -14.823 28.127  0.80 24.22  ? 501 GTP A C4    1 
HETATM 15817 MG MG    A MG  E 5 .   ? 0.547   -14.215 18.298  0.20 23.89  2 502 MG  A MG    1 
HETATM 15818 MG MG    B MG  E 5 .   ? 0.986   -14.152 18.698  0.80 26.25  2 502 MG  A MG    1 
HETATM 15819 CA CA    A CA  F 6 .   ? -31.994 -14.683 34.401  0.20 139.67 2 503 CA  A CA    1 
HETATM 15820 CA CA    B CA  F 6 .   ? -31.936 -14.769 33.998  0.80 444.78 2 503 CA  A CA    1 
HETATM 15821 P  PB    A GDP G 7 .   ? 27.656  -23.028 -10.380 0.20 31.49  ? 501 GDP B PB    1 
HETATM 15822 P  PB    B GDP G 7 .   ? 27.707  -23.516 -9.870  0.80 37.96  ? 501 GDP B PB    1 
HETATM 15823 O  O1B   A GDP G 7 .   ? 28.041  -21.918 -11.324 0.20 29.76  ? 501 GDP B O1B   1 
HETATM 15824 O  O1B   B GDP G 7 .   ? 27.914  -22.521 -10.984 0.80 30.78  ? 501 GDP B O1B   1 
HETATM 15825 O  O2B   A GDP G 7 .   ? 26.797  -24.022 -11.120 0.20 30.34  ? 501 GDP B O2B   1 
HETATM 15826 O  O2B   B GDP G 7 .   ? 27.236  -24.853 -10.390 0.80 29.35  ? 501 GDP B O2B   1 
HETATM 15827 O  O3B   A GDP G 7 .   ? 26.893  -22.423 -9.225  0.20 32.25  ? 501 GDP B O3B   1 
HETATM 15828 O  O3B   B GDP G 7 .   ? 26.683  -22.920 -8.934  0.80 35.93  ? 501 GDP B O3B   1 
HETATM 15829 O  O3A   A GDP G 7 .   ? 29.008  -23.753 -9.892  0.20 35.51  ? 501 GDP B O3A   1 
HETATM 15830 O  O3A   B GDP G 7 .   ? 29.119  -23.737 -9.145  0.80 35.33  ? 501 GDP B O3A   1 
HETATM 15831 P  PA    A GDP G 7 .   ? 29.180  -24.416 -8.437  0.20 34.24  ? 501 GDP B PA    1 
HETATM 15832 P  PA    B GDP G 7 .   ? 29.361  -24.639 -7.844  0.80 37.91  ? 501 GDP B PA    1 
HETATM 15833 O  O1A   A GDP G 7 .   ? 29.673  -25.839 -8.558  0.20 36.43  ? 501 GDP B O1A   1 
HETATM 15834 O  O1A   B GDP G 7 .   ? 30.037  -25.955 -8.156  0.80 35.94  ? 501 GDP B O1A   1 
HETATM 15835 O  O2A   A GDP G 7 .   ? 27.895  -24.367 -7.647  0.20 33.98  ? 501 GDP B O2A   1 
HETATM 15836 O  O2A   B GDP G 7 .   ? 28.064  -24.839 -7.102  0.80 38.44  ? 501 GDP B O2A   1 
HETATM 15837 O  "O5'" A GDP G 7 .   ? 30.319  -23.511 -7.750  0.20 33.09  ? 501 GDP B "O5'" 1 
HETATM 15838 O  "O5'" B GDP G 7 .   ? 30.362  -23.659 -7.059  0.80 36.68  ? 501 GDP B "O5'" 1 
HETATM 15839 C  "C5'" A GDP G 7 .   ? 31.512  -24.117 -7.262  0.20 35.35  ? 501 GDP B "C5'" 1 
HETATM 15840 C  "C5'" B GDP G 7 .   ? 31.713  -24.016 -6.810  0.80 37.61  ? 501 GDP B "C5'" 1 
HETATM 15841 C  "C4'" A GDP G 7 .   ? 31.726  -23.742 -5.804  0.20 35.28  ? 501 GDP B "C4'" 1 
HETATM 15842 C  "C4'" B GDP G 7 .   ? 31.903  -23.798 -5.322  0.80 33.06  ? 501 GDP B "C4'" 1 
HETATM 15843 O  "O4'" A GDP G 7 .   ? 30.804  -24.485 -5.003  0.20 34.51  ? 501 GDP B "O4'" 1 
HETATM 15844 O  "O4'" B GDP G 7 .   ? 30.938  -24.607 -4.647  0.80 34.96  ? 501 GDP B "O4'" 1 
HETATM 15845 C  "C3'" A GDP G 7 .   ? 33.123  -24.132 -5.367  0.20 32.90  ? 501 GDP B "C3'" 1 
HETATM 15846 C  "C3'" B GDP G 7 .   ? 33.253  -24.298 -4.883  0.80 31.68  ? 501 GDP B "C3'" 1 
HETATM 15847 O  "O3'" A GDP G 7 .   ? 33.674  -23.090 -4.557  0.20 35.19  ? 501 GDP B "O3'" 1 
HETATM 15848 O  "O3'" B GDP G 7 .   ? 33.607  -23.527 -3.735  0.80 26.74  ? 501 GDP B "O3'" 1 
HETATM 15849 C  "C2'" A GDP G 7 .   ? 32.949  -25.384 -4.538  0.20 34.95  ? 501 GDP B "C2'" 1 
HETATM 15850 C  "C2'" B GDP G 7 .   ? 32.999  -25.718 -4.450  0.80 35.56  ? 501 GDP B "C2'" 1 
HETATM 15851 O  "O2'" A GDP G 7 .   ? 33.859  -25.362 -3.435  0.20 32.59  ? 501 GDP B "O2'" 1 
HETATM 15852 O  "O2'" B GDP G 7 .   ? 33.980  -26.121 -3.491  0.80 29.43  ? 501 GDP B "O2'" 1 
HETATM 15853 C  "C1'" A GDP G 7 .   ? 31.495  -25.340 -4.086  0.20 33.95  ? 501 GDP B "C1'" 1 
HETATM 15854 C  "C1'" B GDP G 7 .   ? 31.611  -25.581 -3.844  0.80 32.96  ? 501 GDP B "C1'" 1 
HETATM 15855 N  N9    A GDP G 7 .   ? 30.867  -26.682 -4.126  0.20 37.43  ? 501 GDP B N9    1 
HETATM 15856 N  N9    B GDP G 7 .   ? 30.783  -26.800 -3.861  0.80 39.24  ? 501 GDP B N9    1 
HETATM 15857 C  C8    A GDP G 7 .   ? 30.607  -27.399 -5.236  0.20 35.64  ? 501 GDP B C8    1 
HETATM 15858 C  C8    B GDP G 7 .   ? 30.248  -27.405 -4.942  0.80 36.00  ? 501 GDP B C8    1 
HETATM 15859 N  N7    A GDP G 7 .   ? 30.012  -28.582 -4.929  0.20 34.82  ? 501 GDP B N7    1 
HETATM 15860 N  N7    B GDP G 7 .   ? 29.506  -28.483 -4.574  0.80 37.07  ? 501 GDP B N7    1 
HETATM 15861 C  C5    A GDP G 7 .   ? 29.871  -28.626 -3.591  0.20 36.53  ? 501 GDP B C5    1 
HETATM 15862 C  C5    B GDP G 7 .   ? 29.539  -28.563 -3.228  0.80 35.19  ? 501 GDP B C5    1 
HETATM 15863 C  C6    A GDP G 7 .   ? 29.323  -29.585 -2.602  0.20 37.02  ? 501 GDP B C6    1 
HETATM 15864 C  C6    B GDP G 7 .   ? 28.984  -29.450 -2.178  0.80 36.61  ? 501 GDP B C6    1 
HETATM 15865 O  O6    A GDP G 7 .   ? 28.829  -30.675 -2.961  0.20 39.15  ? 501 GDP B O6    1 
HETATM 15866 O  O6    B GDP G 7 .   ? 28.257  -30.431 -2.462  0.80 39.53  ? 501 GDP B O6    1 
HETATM 15867 N  N1    A GDP G 7 .   ? 29.371  -29.248 -1.309  0.20 35.61  ? 501 GDP B N1    1 
HETATM 15868 N  N1    B GDP G 7 .   ? 29.274  -29.167 -0.907  0.80 36.97  ? 501 GDP B N1    1 
HETATM 15869 C  C2    A GDP G 7 .   ? 29.895  -28.084 -0.884  0.20 36.61  ? 501 GDP B C2    1 
HETATM 15870 C  C2    B GDP G 7 .   ? 30.045  -28.125 -0.543  0.80 37.37  ? 501 GDP B C2    1 
HETATM 15871 N  N2    A GDP G 7 .   ? 29.904  -27.826 0.445   0.20 35.13  ? 501 GDP B N2    1 
HETATM 15872 N  N2    B GDP G 7 .   ? 30.290  -27.923 0.776   0.80 35.56  ? 501 GDP B N2    1 
HETATM 15873 N  N3    A GDP G 7 .   ? 30.418  -27.160 -1.731  0.20 35.79  ? 501 GDP B N3    1 
HETATM 15874 N  N3    B GDP G 7 .   ? 30.598  -27.277 -1.446  0.80 35.61  ? 501 GDP B N3    1 
HETATM 15875 C  C4    A GDP G 7 .   ? 30.432  -27.370 -3.068  0.20 36.55  ? 501 GDP B C4    1 
HETATM 15876 C  C4    B GDP G 7 .   ? 30.379  -27.440 -2.768  0.80 36.54  ? 501 GDP B C4    1 
HETATM 15877 N  N1    A IBL H 8 .   ? 14.116  -17.444 16.861  0.20 41.67  ? 502 IBL B N1    1 
HETATM 15878 N  N1    B IBL H 8 .   ? 14.648  -17.301 17.768  0.80 38.17  ? 502 IBL B N1    1 
HETATM 15879 C  C7    A IBL H 8 .   ? 14.677  -21.103 16.882  0.20 45.49  ? 502 IBL B C7    1 
HETATM 15880 C  C7    B IBL H 8 .   ? 13.803  -19.861 15.288  0.80 47.99  ? 502 IBL B C7    1 
HETATM 15881 C  C8    A IBL H 8 .   ? 15.719  -21.819 18.865  0.20 41.46  ? 502 IBL B C8    1 
HETATM 15882 C  C8    B IBL H 8 .   ? 15.699  -20.814 14.305  0.80 53.03  ? 502 IBL B C8    1 
HETATM 15883 C  C9    A IBL H 8 .   ? 14.249  -21.440 15.593  0.20 46.01  ? 502 IBL B C9    1 
HETATM 15884 C  C9    B IBL H 8 .   ? 12.474  -19.567 14.967  0.80 52.24  ? 502 IBL B C9    1 
HETATM 15885 O  O1    A IBL H 8 .   ? 15.260  -22.120 17.570  0.20 47.11  ? 502 IBL B O1    1 
HETATM 15886 O  O1    B IBL H 8 .   ? 14.338  -20.938 14.643  0.80 54.41  ? 502 IBL B O1    1 
HETATM 15887 C  C1    A IBL H 8 .   ? 15.469  -13.979 20.148  0.20 29.65  ? 502 IBL B C1    1 
HETATM 15888 C  C1    B IBL H 8 .   ? 16.256  -13.623 20.644  0.80 29.93  ? 502 IBL B C1    1 
HETATM 15889 C  C5    A IBL H 8 .   ? 13.981  -18.842 16.499  0.20 42.64  ? 502 IBL B C5    1 
HETATM 15890 C  C5    B IBL H 8 .   ? 13.811  -18.068 16.870  0.80 41.98  ? 502 IBL B C5    1 
HETATM 15891 C  C6    A IBL H 8 .   ? 14.524  -19.804 17.354  0.20 43.15  ? 502 IBL B C6    1 
HETATM 15892 C  C6    B IBL H 8 .   ? 14.484  -19.124 16.254  0.80 42.10  ? 502 IBL B C6    1 
HETATM 15893 C  C4    A IBL H 8 .   ? 14.342  -15.949 18.593  0.20 37.84  ? 502 IBL B C4    1 
HETATM 15894 C  C4    B IBL H 8 .   ? 14.895  -15.494 19.147  0.80 39.78  ? 502 IBL B C4    1 
HETATM 15895 O  O4    A IBL H 8 .   ? 13.348  -13.838 21.332  0.20 22.50  ? 502 IBL B O4    1 
HETATM 15896 O  O4    B IBL H 8 .   ? 14.145  -13.195 21.806  0.80 33.04  ? 502 IBL B O4    1 
HETATM 15897 C  C3    A IBL H 8 .   ? 15.642  -15.510 18.317  0.20 29.44  ? 502 IBL B C3    1 
HETATM 15898 C  C3    B IBL H 8 .   ? 16.266  -15.320 18.948  0.80 31.44  ? 502 IBL B C3    1 
HETATM 15899 O  O3    A IBL H 8 .   ? 13.218  -20.954 13.589  0.20 46.59  ? 502 IBL B O3    1 
HETATM 15900 O  O3    B IBL H 8 .   ? 10.547  -18.269 15.193  0.80 60.36  ? 502 IBL B O3    1 
HETATM 15901 C  C2    A IBL H 8 .   ? 16.212  -14.526 19.108  0.20 34.89  ? 502 IBL B C2    1 
HETATM 15902 C  C2    B IBL H 8 .   ? 16.951  -14.383 19.707  0.80 40.76  ? 502 IBL B C2    1 
HETATM 15903 N  N     A IBL H 8 .   ? 13.869  -17.199 18.062  0.20 40.64  ? 502 IBL B N     1 
HETATM 15904 N  N     B IBL H 8 .   ? 14.068  -16.347 18.335  0.80 41.73  ? 502 IBL B N     1 
HETATM 15905 C  C     A IBL H 8 .   ? 17.207  -13.302 21.528  0.20 31.48  ? 502 IBL B C     1 
HETATM 15906 C  C     B IBL H 8 .   ? 17.915  -11.988 20.833  0.80 29.20  ? 502 IBL B C     1 
HETATM 15907 O  O     A IBL H 8 .   ? 15.958  -12.991 20.957  0.20 27.95  ? 502 IBL B O     1 
HETATM 15908 O  O     B IBL H 8 .   ? 16.849  -12.683 21.437  0.80 35.10  ? 502 IBL B O     1 
HETATM 15909 C  C10   A IBL H 8 .   ? 15.608  -22.982 14.572  0.20 41.67  ? 502 IBL B C10   1 
HETATM 15910 C  C10   B IBL H 8 .   ? 12.081  -19.960 12.745  0.80 48.15  ? 502 IBL B C10   1 
HETATM 15911 C  C11   A IBL H 8 .   ? 13.642  -20.468 14.786  0.20 47.21  ? 502 IBL B C11   1 
HETATM 15912 C  C11   B IBL H 8 .   ? 11.816  -18.517 15.623  0.80 49.21  ? 502 IBL B C11   1 
HETATM 15913 C  C12   A IBL H 8 .   ? 12.942  -20.010 12.585  0.20 46.54  ? 502 IBL B C12   1 
HETATM 15914 C  C12   B IBL H 8 .   ? 9.695   -17.647 16.125  0.80 51.58  ? 502 IBL B C12   1 
HETATM 15915 C  C13   A IBL H 8 .   ? 13.503  -19.150 15.227  0.20 46.24  ? 502 IBL B C13   1 
HETATM 15916 C  C13   B IBL H 8 .   ? 12.480  -17.759 16.581  0.80 42.17  ? 502 IBL B C13   1 
HETATM 15917 C  C14   A IBL H 8 .   ? 13.553  -15.354 19.578  0.20 30.60  ? 502 IBL B C14   1 
HETATM 15918 C  C14   B IBL H 8 .   ? 14.186  -14.762 20.102  0.80 33.90  ? 502 IBL B C14   1 
HETATM 15919 C  C15   A IBL H 8 .   ? 14.137  -14.361 20.366  0.20 33.15  ? 502 IBL B C15   1 
HETATM 15920 C  C15   B IBL H 8 .   ? 14.882  -13.824 20.861  0.80 35.95  ? 502 IBL B C15   1 
HETATM 15921 O  O2    A IBL H 8 .   ? 14.347  -22.726 15.148  0.20 43.24  ? 502 IBL B O2    1 
HETATM 15922 O  O2    B IBL H 8 .   ? 11.784  -20.332 14.072  0.80 52.38  ? 502 IBL B O2    1 
HETATM 15923 O  O     . HOH I 9 .   ? -14.166 5.227   26.633  1.00 49.26  ? 601 HOH A O     1 
HETATM 15924 O  O     . HOH I 9 .   ? -18.528 -26.245 25.521  1.00 44.40  ? 602 HOH A O     1 
HETATM 15925 O  O     . HOH I 9 .   ? -1.452  -3.812  46.634  1.00 34.63  ? 603 HOH A O     1 
HETATM 15926 O  O     . HOH I 9 .   ? -7.875  -17.004 10.280  1.00 41.54  ? 604 HOH A O     1 
HETATM 15927 O  O     . HOH I 9 .   ? -6.223  7.959   50.685  1.00 51.19  ? 605 HOH A O     1 
HETATM 15928 O  O     . HOH I 9 .   ? 2.566   -15.137 11.232  1.00 43.22  ? 606 HOH A O     1 
HETATM 15929 O  O     . HOH I 9 .   ? 1.414   4.314   17.547  1.00 34.73  ? 607 HOH A O     1 
HETATM 15930 O  O     . HOH I 9 .   ? 4.652   7.143   14.141  1.00 46.84  ? 608 HOH A O     1 
HETATM 15931 O  O     . HOH I 9 .   ? -31.371 -10.715 30.846  1.00 51.48  ? 609 HOH A O     1 
HETATM 15932 O  O     . HOH I 9 .   ? -18.452 1.968   48.202  1.00 45.61  ? 610 HOH A O     1 
HETATM 15933 O  O     . HOH I 9 .   ? -4.725  -17.163 17.917  1.00 30.62  ? 611 HOH A O     1 
HETATM 15934 O  O     . HOH I 9 .   ? -16.016 -15.254 46.328  1.00 42.07  ? 612 HOH A O     1 
HETATM 15935 O  O     . HOH I 9 .   ? -2.519  -30.123 54.380  1.00 45.04  ? 613 HOH A O     1 
HETATM 15936 O  O     . HOH I 9 .   ? -8.283  7.966   35.016  1.00 47.00  ? 614 HOH A O     1 
HETATM 15937 O  O     . HOH I 9 .   ? 2.089   -15.062 20.269  1.00 26.95  ? 615 HOH A O     1 
HETATM 15938 O  O     . HOH I 9 .   ? 10.639  -29.981 31.544  1.00 64.78  ? 616 HOH A O     1 
HETATM 15939 O  O     . HOH I 9 .   ? -16.552 -0.662  11.871  1.00 51.10  ? 617 HOH A O     1 
HETATM 15940 O  O     . HOH I 9 .   ? -11.527 -8.509  67.002  1.00 47.64  ? 618 HOH A O     1 
HETATM 15941 O  O     . HOH I 9 .   ? 16.593  6.454   25.427  1.00 37.26  ? 619 HOH A O     1 
HETATM 15942 O  O     . HOH I 9 .   ? 1.487   -15.544 17.100  1.00 25.57  ? 620 HOH A O     1 
HETATM 15943 O  O     . HOH I 9 .   ? -0.425  -13.128 17.237  1.00 25.80  ? 621 HOH A O     1 
HETATM 15944 O  O     . HOH I 9 .   ? 5.571   -15.938 49.566  1.00 56.46  ? 622 HOH A O     1 
HETATM 15945 O  O     . HOH I 9 .   ? 9.870   -7.692  37.136  1.00 43.78  ? 623 HOH A O     1 
HETATM 15946 O  O     . HOH I 9 .   ? -13.626 -7.455  43.766  1.00 38.39  ? 624 HOH A O     1 
HETATM 15947 O  O     . HOH I 9 .   ? -6.448  -24.589 30.060  1.00 57.60  ? 625 HOH A O     1 
HETATM 15948 O  O     . HOH I 9 .   ? -0.646  -15.654 18.733  1.00 26.44  ? 626 HOH A O     1 
HETATM 15949 O  O     . HOH I 9 .   ? -7.736  4.340   50.523  1.00 41.13  ? 627 HOH A O     1 
HETATM 15950 O  O     . HOH I 9 .   ? -17.433 -9.838  45.813  1.00 43.17  ? 628 HOH A O     1 
HETATM 15951 O  O     . HOH I 9 .   ? -16.338 -20.049 60.944  1.00 46.16  ? 629 HOH A O     1 
HETATM 15952 O  O     . HOH I 9 .   ? -7.079  -21.237 26.225  1.00 45.10  ? 630 HOH A O     1 
HETATM 15953 O  O     . HOH I 9 .   ? -17.357 -8.982  30.167  1.00 34.31  ? 631 HOH A O     1 
HETATM 15954 O  O     . HOH I 9 .   ? -22.900 -19.966 26.307  1.00 43.17  ? 632 HOH A O     1 
HETATM 15955 O  O     . HOH I 9 .   ? 2.249   -23.899 49.561  1.00 35.72  ? 633 HOH A O     1 
HETATM 15956 O  O     . HOH I 9 .   ? -15.030 -19.287 15.478  1.00 44.57  ? 634 HOH A O     1 
HETATM 15957 O  O     . HOH I 9 .   ? 0.266   -28.382 41.283  1.00 51.29  ? 635 HOH A O     1 
HETATM 15958 O  O     . HOH I 9 .   ? 15.795  -8.465  30.138  1.00 46.77  ? 636 HOH A O     1 
HETATM 15959 O  O     . HOH I 9 .   ? 8.900   -26.118 32.201  1.00 52.79  ? 637 HOH A O     1 
HETATM 15960 O  O     . HOH I 9 .   ? 1.753   -5.193  48.762  1.00 40.58  ? 638 HOH A O     1 
HETATM 15961 O  O     . HOH I 9 .   ? -20.296 5.401   31.448  1.00 52.34  ? 639 HOH A O     1 
HETATM 15962 O  O     . HOH I 9 .   ? 4.729   -8.946  27.771  1.00 24.00  ? 640 HOH A O     1 
HETATM 15963 O  O     . HOH I 9 .   ? -0.189  3.904   39.678  1.00 33.99  ? 641 HOH A O     1 
HETATM 15964 O  O     . HOH I 9 .   ? -12.469 -18.161 42.962  1.00 39.50  ? 642 HOH A O     1 
HETATM 15965 O  O     . HOH I 9 .   ? 4.006   2.605   49.246  1.00 39.97  ? 643 HOH A O     1 
HETATM 15966 O  O     . HOH I 9 .   ? -23.517 -7.640  25.215  1.00 36.09  ? 644 HOH A O     1 
HETATM 15967 O  O     . HOH I 9 .   ? -10.404 -3.150  8.742   1.00 34.91  ? 645 HOH A O     1 
HETATM 15968 O  O     . HOH I 9 .   ? -19.372 2.826   35.573  1.00 42.75  ? 646 HOH A O     1 
HETATM 15969 O  O     . HOH I 9 .   ? -10.789 -21.987 47.938  1.00 44.40  ? 647 HOH A O     1 
HETATM 15970 O  O     . HOH I 9 .   ? 7.324   -12.327 29.842  1.00 28.54  ? 648 HOH A O     1 
HETATM 15971 O  O     . HOH I 9 .   ? -5.978  -30.375 47.226  1.00 35.19  ? 649 HOH A O     1 
HETATM 15972 O  O     . HOH I 9 .   ? -23.034 -11.798 24.889  1.00 39.49  ? 650 HOH A O     1 
HETATM 15973 O  O     . HOH I 9 .   ? -18.224 -4.954  46.617  1.00 34.81  ? 651 HOH A O     1 
HETATM 15974 O  O     . HOH I 9 .   ? -13.268 -10.773 31.849  1.00 37.38  ? 652 HOH A O     1 
HETATM 15975 O  O     . HOH I 9 .   ? -1.634  -10.656 24.233  1.00 22.63  ? 653 HOH A O     1 
HETATM 15976 O  O     . HOH I 9 .   ? -14.298 -8.568  48.188  1.00 37.30  ? 654 HOH A O     1 
HETATM 15977 O  O     . HOH I 9 .   ? -6.785  -18.732 47.194  1.00 39.16  ? 655 HOH A O     1 
HETATM 15978 O  O     . HOH I 9 .   ? 5.209   -14.660 19.302  1.00 39.44  ? 656 HOH A O     1 
HETATM 15979 O  O     . HOH I 9 .   ? 9.651   -4.657  9.091   1.00 44.64  ? 657 HOH A O     1 
HETATM 15980 O  O     . HOH I 9 .   ? -17.589 6.862   41.712  1.00 46.11  ? 658 HOH A O     1 
HETATM 15981 O  O     . HOH I 9 .   ? 18.106  -0.636  13.169  1.00 32.76  ? 659 HOH A O     1 
HETATM 15982 O  O     . HOH I 9 .   ? -1.035  -1.719  37.403  1.00 28.74  ? 660 HOH A O     1 
HETATM 15983 O  O     . HOH I 9 .   ? -1.404  -1.057  30.746  1.00 30.13  ? 661 HOH A O     1 
HETATM 15984 O  O     . HOH I 9 .   ? 0.752   1.124   42.247  1.00 29.87  ? 662 HOH A O     1 
HETATM 15985 O  O     . HOH I 9 .   ? -1.530  8.878   25.380  1.00 34.14  ? 663 HOH A O     1 
HETATM 15986 O  O     . HOH I 9 .   ? -9.736  -14.892 61.106  1.00 43.95  ? 664 HOH A O     1 
HETATM 15987 O  O     . HOH I 9 .   ? 7.593   -27.601 37.023  1.00 54.15  ? 665 HOH A O     1 
HETATM 15988 O  O     . HOH I 9 .   ? 3.781   5.228   20.783  1.00 43.75  ? 666 HOH A O     1 
HETATM 15989 O  O     . HOH I 9 .   ? -0.848  -4.852  39.639  1.00 25.54  ? 667 HOH A O     1 
HETATM 15990 O  O     . HOH I 9 .   ? -2.525  2.401   30.339  1.00 28.30  ? 668 HOH A O     1 
HETATM 15991 O  O     . HOH I 9 .   ? 13.788  0.375   39.143  1.00 44.30  ? 669 HOH A O     1 
HETATM 15992 O  O     . HOH I 9 .   ? -16.483 -18.372 44.779  1.00 34.45  ? 670 HOH A O     1 
HETATM 15993 O  O     . HOH I 9 .   ? -18.050 -7.562  62.924  1.00 36.53  ? 671 HOH A O     1 
HETATM 15994 O  O     . HOH I 9 .   ? -8.766  -0.338  62.024  1.00 39.56  ? 672 HOH A O     1 
HETATM 15995 O  O     . HOH I 9 .   ? -1.155  -0.421  26.893  1.00 35.46  ? 673 HOH A O     1 
HETATM 15996 O  O     . HOH I 9 .   ? -10.011 -35.995 56.592  1.00 35.36  ? 674 HOH A O     1 
HETATM 15997 O  O     . HOH I 9 .   ? -23.000 -20.574 50.315  1.00 39.48  ? 675 HOH A O     1 
HETATM 15998 O  O     . HOH I 9 .   ? -28.615 -7.157  28.977  1.00 40.31  ? 676 HOH A O     1 
HETATM 15999 O  O     . HOH I 9 .   ? 10.032  -8.696  34.817  1.00 37.29  ? 677 HOH A O     1 
HETATM 16000 O  O     . HOH I 9 .   ? -4.342  -21.463 47.796  1.00 37.60  ? 678 HOH A O     1 
HETATM 16001 O  O     . HOH I 9 .   ? 11.766  -4.851  33.149  1.00 32.92  ? 679 HOH A O     1 
HETATM 16002 O  O     . HOH I 9 .   ? 23.160  7.614   21.203  1.00 52.61  ? 680 HOH A O     1 
HETATM 16003 O  O     . HOH I 9 .   ? 8.030   -11.011 50.942  1.00 46.48  ? 681 HOH A O     1 
HETATM 16004 O  O     . HOH I 9 .   ? 23.654  1.438   25.228  1.00 36.62  ? 682 HOH A O     1 
HETATM 16005 O  O     . HOH I 9 .   ? -9.656  8.337   29.148  1.00 46.42  ? 683 HOH A O     1 
HETATM 16006 O  O     . HOH I 9 .   ? -9.004  -19.370 11.287  1.00 51.14  ? 684 HOH A O     1 
HETATM 16007 O  O     . HOH I 9 .   ? 13.625  2.995   44.334  1.00 45.64  ? 685 HOH A O     1 
HETATM 16008 O  O     . HOH I 9 .   ? -14.798 0.316   54.055  1.00 43.87  ? 686 HOH A O     1 
HETATM 16009 O  O     . HOH I 9 .   ? -3.620  -21.332 29.862  1.00 33.32  ? 687 HOH A O     1 
HETATM 16010 O  O     . HOH I 9 .   ? -13.567 -14.704 64.866  1.00 51.93  ? 688 HOH A O     1 
HETATM 16011 O  O     . HOH I 9 .   ? -11.711 -5.201  8.794   1.00 38.38  ? 689 HOH A O     1 
HETATM 16012 O  O     . HOH I 9 .   ? -3.641  -10.678 10.042  1.00 47.84  ? 690 HOH A O     1 
HETATM 16013 O  O     . HOH I 9 .   ? -5.487  8.705   31.664  1.00 47.95  ? 691 HOH A O     1 
HETATM 16014 O  O     . HOH I 9 .   ? -12.760 -17.592 11.569  1.00 50.44  ? 692 HOH A O     1 
HETATM 16015 O  O     . HOH I 9 .   ? 9.688   -15.009 19.011  1.00 38.33  ? 693 HOH A O     1 
HETATM 16016 O  O     . HOH I 9 .   ? 4.547   2.786   52.701  1.00 49.94  ? 694 HOH A O     1 
HETATM 16017 O  O     . HOH I 9 .   ? -3.100  7.805   21.038  1.00 50.39  ? 695 HOH A O     1 
HETATM 16018 O  O     . HOH I 9 .   ? -29.281 -20.439 22.452  1.00 41.88  ? 696 HOH A O     1 
HETATM 16019 O  O     . HOH I 9 .   ? -20.051 -24.739 40.094  1.00 47.10  ? 697 HOH A O     1 
HETATM 16020 O  O     . HOH I 9 .   ? 0.294   0.657   29.501  1.00 33.75  ? 698 HOH A O     1 
HETATM 16021 O  O     . HOH I 9 .   ? -7.847  -20.835 46.867  1.00 35.71  ? 699 HOH A O     1 
HETATM 16022 O  O     . HOH I 9 .   ? -7.749  -9.928  63.609  1.00 35.66  ? 700 HOH A O     1 
HETATM 16023 O  O     . HOH I 9 .   ? -7.735  -12.748 62.693  1.00 35.98  ? 701 HOH A O     1 
HETATM 16024 O  O     . HOH I 9 .   ? -38.672 -16.505 33.377  1.00 54.06  ? 702 HOH A O     1 
HETATM 16025 O  O     . HOH I 9 .   ? -29.689 -9.397  30.569  1.00 48.20  ? 703 HOH A O     1 
HETATM 16026 O  O     . HOH I 9 .   ? 5.241   -31.166 54.978  1.00 63.94  ? 704 HOH A O     1 
HETATM 16027 O  O     . HOH I 9 .   ? 0.603   7.922   14.838  1.00 56.20  ? 705 HOH A O     1 
HETATM 16028 O  O     . HOH I 9 .   ? -7.772  -28.965 18.171  1.00 45.86  ? 706 HOH A O     1 
HETATM 16029 O  O     . HOH I 9 .   ? 17.109  -8.150  32.602  1.00 55.13  ? 707 HOH A O     1 
HETATM 16030 O  O     . HOH I 9 .   ? 4.889   -18.391 23.367  1.00 44.20  ? 708 HOH A O     1 
HETATM 16031 O  O     . HOH I 9 .   ? -7.515  -28.610 48.760  1.00 36.23  ? 709 HOH A O     1 
HETATM 16032 O  O     . HOH I 9 .   ? -2.663  -11.331 5.869   1.00 52.19  ? 710 HOH A O     1 
HETATM 16033 O  O     . HOH I 9 .   ? 4.022   14.019  28.592  1.00 47.37  ? 711 HOH A O     1 
HETATM 16034 O  O     . HOH I 9 .   ? 2.587   14.767  30.856  1.00 46.88  ? 712 HOH A O     1 
HETATM 16035 O  O     . HOH I 9 .   ? -9.078  -29.546 50.611  1.00 45.30  ? 713 HOH A O     1 
HETATM 16036 O  O     . HOH I 9 .   ? -29.366 -10.419 28.459  1.00 40.72  ? 714 HOH A O     1 
HETATM 16037 O  O     . HOH I 9 .   ? -18.111 -16.281 44.682  1.00 45.63  ? 715 HOH A O     1 
HETATM 16038 O  O     . HOH I 9 .   ? -2.380  13.430  35.453  1.00 40.04  ? 716 HOH A O     1 
HETATM 16039 O  O     . HOH I 9 .   ? -7.189  3.946   12.835  1.00 58.47  ? 717 HOH A O     1 
HETATM 16040 O  O     . HOH I 9 .   ? -15.344 -8.601  45.745  1.00 46.89  ? 718 HOH A O     1 
HETATM 16041 O  O     . HOH I 9 .   ? -7.473  -19.922 9.386   1.00 44.77  ? 719 HOH A O     1 
HETATM 16042 O  O     . HOH I 9 .   ? -10.824 -8.811  69.024  1.00 56.42  ? 720 HOH A O     1 
HETATM 16043 O  O     . HOH I 9 .   ? -36.685 -11.123 34.745  1.00 54.96  ? 721 HOH A O     1 
HETATM 16044 O  O     . HOH I 9 .   ? 19.310  1.167   11.237  1.00 44.86  ? 722 HOH A O     1 
HETATM 16045 O  O     . HOH I 9 .   ? -37.790 -9.877  36.706  1.00 59.34  ? 723 HOH A O     1 
HETATM 16046 O  O     . HOH J 9 .   ? 32.149  -19.413 22.151  1.00 54.24  ? 601 HOH B O     1 
HETATM 16047 O  O     . HOH J 9 .   ? 25.885  -24.543 -13.102 1.00 42.80  ? 602 HOH B O     1 
HETATM 16048 O  O     . HOH J 9 .   ? 11.302  -38.146 13.034  1.00 56.05  ? 603 HOH B O     1 
HETATM 16049 O  O     . HOH J 9 .   ? 25.720  -10.593 10.663  1.00 31.39  ? 604 HOH B O     1 
HETATM 16050 O  O     . HOH J 9 .   ? 29.896  -3.863  22.082  1.00 41.31  ? 605 HOH B O     1 
HETATM 16051 O  O     . HOH J 9 .   ? 0.672   -19.777 13.079  1.00 50.33  ? 606 HOH B O     1 
HETATM 16052 O  O     . HOH J 9 .   ? 23.104  -27.064 37.046  1.00 58.83  ? 607 HOH B O     1 
HETATM 16053 O  O     . HOH J 9 .   ? 16.634  -37.689 8.695   1.00 52.88  ? 608 HOH B O     1 
HETATM 16054 O  O     . HOH J 9 .   ? 0.803   -17.246 -12.516 1.00 54.97  ? 609 HOH B O     1 
HETATM 16055 O  O     . HOH J 9 .   ? 23.672  2.063   15.241  1.00 35.68  ? 610 HOH B O     1 
HETATM 16056 O  O     . HOH J 9 .   ? 19.195  -14.422 27.270  1.00 40.08  ? 611 HOH B O     1 
HETATM 16057 O  O     . HOH J 9 .   ? 5.010   -22.188 28.954  1.00 44.70  ? 612 HOH B O     1 
HETATM 16058 O  O     . HOH J 9 .   ? 45.940  -31.307 11.462  1.00 52.94  ? 613 HOH B O     1 
HETATM 16059 O  O     . HOH J 9 .   ? 15.490  -7.172  25.487  1.00 31.02  ? 614 HOH B O     1 
HETATM 16060 O  O     . HOH J 9 .   ? 26.152  -30.896 -13.071 1.00 52.66  ? 615 HOH B O     1 
HETATM 16061 O  O     . HOH J 9 .   ? 31.181  -14.002 19.274  1.00 30.83  ? 616 HOH B O     1 
HETATM 16062 O  O     . HOH J 9 .   ? 38.307  -5.215  11.693  1.00 45.86  ? 617 HOH B O     1 
HETATM 16063 O  O     . HOH J 9 .   ? 5.134   -13.666 11.422  1.00 45.02  ? 618 HOH B O     1 
HETATM 16064 O  O     . HOH J 9 .   ? 35.376  -23.846 -1.983  1.00 39.09  ? 619 HOH B O     1 
HETATM 16065 O  O     . HOH J 9 .   ? 36.248  -21.578 14.288  1.00 42.33  ? 620 HOH B O     1 
HETATM 16066 O  O     . HOH J 9 .   ? 19.889  -39.954 2.853   1.00 45.00  ? 621 HOH B O     1 
HETATM 16067 O  O     . HOH J 9 .   ? 13.604  -6.576  5.644   1.00 59.20  ? 622 HOH B O     1 
HETATM 16068 O  O     . HOH J 9 .   ? 7.146   -21.794 10.285  1.00 43.33  ? 623 HOH B O     1 
HETATM 16069 O  O     . HOH J 9 .   ? 27.757  -20.495 -7.637  1.00 32.82  ? 624 HOH B O     1 
HETATM 16070 O  O     . HOH J 9 .   ? 28.047  -18.514 -24.219 1.00 57.01  ? 625 HOH B O     1 
HETATM 16071 O  O     . HOH J 9 .   ? 40.317  -18.553 21.143  1.00 44.64  ? 626 HOH B O     1 
HETATM 16072 O  O     . HOH J 9 .   ? 46.116  -11.476 6.330   1.00 46.84  ? 627 HOH B O     1 
HETATM 16073 O  O     . HOH J 9 .   ? 15.275  -19.177 26.117  1.00 49.99  ? 628 HOH B O     1 
HETATM 16074 O  O     . HOH J 9 .   ? 38.388  -17.558 8.102   1.00 36.21  ? 629 HOH B O     1 
HETATM 16075 O  O     . HOH J 9 .   ? 20.383  -4.621  4.268   1.00 37.30  ? 630 HOH B O     1 
HETATM 16076 O  O     . HOH J 9 .   ? 15.831  -21.322 9.388   1.00 38.63  ? 631 HOH B O     1 
HETATM 16077 O  O     . HOH J 9 .   ? 42.469  -19.244 6.125   1.00 35.76  ? 632 HOH B O     1 
HETATM 16078 O  O     . HOH J 9 .   ? 19.461  -29.666 16.867  1.00 50.26  ? 633 HOH B O     1 
HETATM 16079 O  O     . HOH J 9 .   ? 17.809  -36.443 11.071  1.00 52.67  ? 634 HOH B O     1 
HETATM 16080 O  O     . HOH J 9 .   ? 25.517  -23.732 -6.054  1.00 35.87  ? 635 HOH B O     1 
HETATM 16081 O  O     . HOH J 9 .   ? 31.439  -21.295 -2.695  1.00 32.41  ? 636 HOH B O     1 
HETATM 16082 O  O     . HOH J 9 .   ? 1.896   -13.071 1.676   1.00 45.89  ? 637 HOH B O     1 
HETATM 16083 O  O     . HOH J 9 .   ? 27.850  -13.982 12.821  1.00 27.69  ? 638 HOH B O     1 
HETATM 16084 O  O     . HOH J 9 .   ? 42.020  -19.857 3.211   1.00 46.06  ? 639 HOH B O     1 
HETATM 16085 O  O     . HOH J 9 .   ? 22.888  -2.081  8.781   1.00 25.64  ? 640 HOH B O     1 
HETATM 16086 O  O     . HOH J 9 .   ? 40.182  -17.060 12.948  1.00 47.84  ? 641 HOH B O     1 
HETATM 16087 O  O     . HOH J 9 .   ? 42.897  -19.768 -4.414  1.00 39.93  ? 642 HOH B O     1 
HETATM 16088 O  O     . HOH J 9 .   ? 38.720  -18.123 1.110   1.00 32.96  ? 643 HOH B O     1 
HETATM 16089 O  O     . HOH J 9 .   ? 42.924  -14.374 2.618   1.00 41.87  ? 644 HOH B O     1 
HETATM 16090 O  O     . HOH J 9 .   ? 48.715  -8.752  -14.393 1.00 37.48  ? 645 HOH B O     1 
HETATM 16091 O  O     . HOH J 9 .   ? 15.363  -22.036 6.783   1.00 43.10  ? 646 HOH B O     1 
HETATM 16092 O  O     . HOH J 9 .   ? 27.341  -7.135  -7.373  1.00 39.68  ? 647 HOH B O     1 
HETATM 16093 O  O     . HOH J 9 .   ? 20.410  -7.911  -8.898  1.00 49.48  ? 648 HOH B O     1 
HETATM 16094 O  O     . HOH J 9 .   ? 20.679  -9.034  -15.205 1.00 40.01  ? 649 HOH B O     1 
HETATM 16095 O  O     . HOH J 9 .   ? 34.939  -19.346 30.634  1.00 54.18  ? 650 HOH B O     1 
HETATM 16096 O  O     . HOH J 9 .   ? 32.431  -39.680 14.015  1.00 50.96  ? 651 HOH B O     1 
HETATM 16097 O  O     . HOH J 9 .   ? 37.171  -0.325  -3.124  1.00 49.33  ? 652 HOH B O     1 
HETATM 16098 O  O     . HOH J 9 .   ? 35.105  0.313   12.703  1.00 38.93  ? 653 HOH B O     1 
HETATM 16099 O  O     . HOH J 9 .   ? 23.192  -8.492  27.566  1.00 45.80  ? 654 HOH B O     1 
HETATM 16100 O  O     . HOH J 9 .   ? 0.412   -16.651 -0.167  1.00 53.44  ? 655 HOH B O     1 
HETATM 16101 O  O     . HOH J 9 .   ? 47.367  -8.516  1.647   1.00 44.35  ? 656 HOH B O     1 
HETATM 16102 O  O     . HOH J 9 .   ? 21.241  -9.913  -21.537 1.00 59.94  ? 657 HOH B O     1 
HETATM 16103 O  O     . HOH J 9 .   ? 15.789  -23.905 -21.076 1.00 56.91  ? 658 HOH B O     1 
HETATM 16104 O  O     . HOH J 9 .   ? 46.150  -8.951  -0.997  1.00 36.03  ? 659 HOH B O     1 
HETATM 16105 O  O     . HOH J 9 .   ? 19.383  -31.217 14.795  1.00 40.81  ? 660 HOH B O     1 
HETATM 16106 O  O     . HOH J 9 .   ? 27.828  -2.986  -21.065 1.00 55.72  ? 661 HOH B O     1 
HETATM 16107 O  O     . HOH J 9 .   ? 5.125   -6.329  -5.827  1.00 48.74  ? 662 HOH B O     1 
HETATM 16108 O  O     . HOH J 9 .   ? 16.616  -44.751 7.357   1.00 54.18  ? 663 HOH B O     1 
HETATM 16109 O  O     . HOH J 9 .   ? 0.924   -15.641 -2.386  1.00 48.70  ? 664 HOH B O     1 
HETATM 16110 O  O     . HOH J 9 .   ? 25.159  -33.583 34.577  1.00 62.46  ? 665 HOH B O     1 
HETATM 16111 O  O     . HOH J 9 .   ? 29.034  4.289   5.882   1.00 53.13  ? 666 HOH B O     1 
HETATM 16112 O  O     . HOH J 9 .   ? 22.649  -12.937 -27.186 1.00 57.66  ? 667 HOH B O     1 
HETATM 16113 O  O     . HOH J 9 .   ? 27.097  5.030   3.540   1.00 50.21  ? 668 HOH B O     1 
HETATM 16114 O  O     . HOH J 9 .   ? 21.413  -7.380  -23.142 1.00 51.88  ? 669 HOH B O     1 
HETATM 16115 O  O     . HOH J 9 .   ? 5.618   -40.377 -11.470 1.00 54.89  ? 670 HOH B O     1 
HETATM 16116 O  O     . HOH J 9 .   ? 23.793  -14.994 -28.034 1.00 51.94  ? 671 HOH B O     1 
HETATM 16117 O  O     . HOH J 9 .   ? 27.290  -33.126 36.070  1.00 56.13  ? 672 HOH B O     1 
HETATM 16118 O  O     . HOH J 9 .   ? 40.291  -22.160 -18.427 1.00 58.10  ? 673 HOH B O     1 
HETATM 16119 O  O     . HOH K 9 .   ? 52.168  -25.460 -13.947 1.00 47.28  ? 201 HOH F O     1 
HETATM 16120 O  O     . HOH K 9 .   ? 55.111  -24.480 -30.933 1.00 53.62  ? 202 HOH F O     1 
HETATM 16121 O  O     . HOH K 9 .   ? 65.855  -16.596 -21.373 1.00 37.99  ? 203 HOH F O     1 
HETATM 16122 O  O     . HOH K 9 .   ? 60.006  -25.236 13.553  1.00 48.44  ? 204 HOH F O     1 
HETATM 16123 O  O     . HOH K 9 .   ? 51.562  -2.590  -32.618 1.00 60.89  ? 205 HOH F O     1 
HETATM 16124 O  O     . HOH K 9 .   ? 43.378  -27.458 8.739   1.00 41.34  ? 206 HOH F O     1 
HETATM 16125 O  O     . HOH K 9 .   ? 52.271  -24.691 -23.625 1.00 48.29  ? 207 HOH F O     1 
HETATM 16126 O  O     . HOH K 9 .   ? 47.385  -5.042  -19.981 1.00 49.24  ? 208 HOH F O     1 
HETATM 16127 O  O     . HOH K 9 .   ? 52.258  -24.809 14.573  1.00 48.79  ? 209 HOH F O     1 
HETATM 16128 O  O     . HOH K 9 .   ? 48.157  -24.343 -22.003 1.00 48.77  ? 210 HOH F O     1 
HETATM 16129 O  O     . HOH K 9 .   ? 40.589  -19.232 8.839   1.00 49.73  ? 211 HOH F O     1 
HETATM 16130 O  O     . HOH K 9 .   ? 59.750  -15.054 -43.318 1.00 43.41  ? 212 HOH F O     1 
HETATM 16131 O  O     . HOH K 9 .   ? 50.746  -6.807  -12.305 1.00 32.74  ? 213 HOH F O     1 
HETATM 16132 O  O     . HOH K 9 .   ? 48.190  -8.329  -2.436  1.00 30.48  ? 214 HOH F O     1 
HETATM 16133 O  O     . HOH K 9 .   ? 43.975  -16.427 2.454   1.00 37.39  ? 215 HOH F O     1 
HETATM 16134 O  O     . HOH K 9 .   ? 50.000  -8.296  0.843   1.00 34.89  ? 216 HOH F O     1 
HETATM 16135 O  O     . HOH K 9 .   ? 65.962  -18.655 -9.130  1.00 37.21  ? 217 HOH F O     1 
HETATM 16136 O  O     . HOH K 9 .   ? 51.310  0.553   3.858   1.00 43.66  ? 218 HOH F O     1 
HETATM 16137 O  O     . HOH K 9 .   ? 60.895  -13.237 -10.053 1.00 35.79  ? 219 HOH F O     1 
HETATM 16138 O  O     . HOH K 9 .   ? 49.383  -25.149 -4.212  1.00 48.31  ? 220 HOH F O     1 
HETATM 16139 O  O     . HOH K 9 .   ? 47.253  -26.126 -2.102  1.00 50.21  ? 221 HOH F O     1 
HETATM 16140 O  O     . HOH K 9 .   ? 62.754  -13.000 -32.830 1.00 31.15  ? 222 HOH F O     1 
HETATM 16141 O  O     . HOH K 9 .   ? 58.274  -2.123  -15.980 1.00 43.77  ? 223 HOH F O     1 
HETATM 16142 O  O     . HOH K 9 .   ? 54.899  -8.133  11.525  1.00 37.14  ? 224 HOH F O     1 
HETATM 16143 O  O     . HOH K 9 .   ? 59.025  -15.170 -2.134  1.00 24.91  ? 225 HOH F O     1 
HETATM 16144 O  O     . HOH K 9 .   ? 48.750  -7.115  4.122   1.00 41.57  ? 226 HOH F O     1 
HETATM 16145 O  O     . HOH K 9 .   ? 52.263  -8.924  -8.356  1.00 28.67  ? 227 HOH F O     1 
HETATM 16146 O  O     . HOH K 9 .   ? 59.630  -6.915  -8.750  1.00 36.48  ? 228 HOH F O     1 
HETATM 16147 O  O     . HOH K 9 .   ? 59.705  -11.356 -20.392 1.00 35.59  ? 229 HOH F O     1 
HETATM 16148 O  O     . HOH K 9 .   ? 57.057  -12.848 4.018   1.00 35.08  ? 230 HOH F O     1 
HETATM 16149 O  O     . HOH K 9 .   ? 64.729  -14.737 -38.071 1.00 40.49  ? 231 HOH F O     1 
HETATM 16150 O  O     . HOH K 9 .   ? 58.676  -12.468 -22.729 1.00 25.82  ? 232 HOH F O     1 
HETATM 16151 O  O     . HOH K 9 .   ? 58.340  -14.058 9.792   1.00 40.99  ? 233 HOH F O     1 
HETATM 16152 O  O     . HOH K 9 .   ? 60.075  -14.018 -12.336 1.00 27.41  ? 234 HOH F O     1 
HETATM 16153 O  O     . HOH K 9 .   ? 63.631  -19.945 2.746   1.00 41.19  ? 235 HOH F O     1 
HETATM 16154 O  O     . HOH K 9 .   ? 59.435  -13.543 0.415   1.00 38.09  ? 236 HOH F O     1 
HETATM 16155 O  O     . HOH K 9 .   ? 56.860  -15.822 6.935   1.00 42.45  ? 237 HOH F O     1 
HETATM 16156 O  O     . HOH K 9 .   ? 62.067  -14.538 11.987  1.00 30.18  ? 238 HOH F O     1 
HETATM 16157 O  O     . HOH K 9 .   ? 48.812  -11.017 -16.284 1.00 46.02  ? 239 HOH F O     1 
HETATM 16158 O  O     . HOH K 9 .   ? 44.809  -24.541 0.544   1.00 34.42  ? 240 HOH F O     1 
HETATM 16159 O  O     . HOH K 9 .   ? 49.304  -5.200  -15.940 1.00 49.78  ? 241 HOH F O     1 
HETATM 16160 O  O     . HOH K 9 .   ? 58.786  -7.711  0.840   1.00 31.26  ? 242 HOH F O     1 
HETATM 16161 O  O     . HOH K 9 .   ? 66.307  -14.660 -18.338 1.00 27.56  ? 243 HOH F O     1 
HETATM 16162 O  O     . HOH K 9 .   ? 40.840  -13.238 8.259   1.00 42.14  ? 244 HOH F O     1 
HETATM 16163 O  O     . HOH K 9 .   ? 61.338  -5.596  -22.258 1.00 46.52  ? 245 HOH F O     1 
HETATM 16164 O  O     . HOH K 9 .   ? 62.982  -5.996  -18.905 1.00 50.81  ? 246 HOH F O     1 
HETATM 16165 O  O     . HOH K 9 .   ? 62.654  -6.525  -6.323  1.00 43.16  ? 247 HOH F O     1 
HETATM 16166 O  O     . HOH K 9 .   ? 60.982  -6.274  3.926   1.00 35.52  ? 248 HOH F O     1 
HETATM 16167 O  O     . HOH K 9 .   ? 66.498  -16.300 -6.454  1.00 43.17  ? 249 HOH F O     1 
HETATM 16168 O  O     . HOH K 9 .   ? 40.841  -11.198 10.431  1.00 42.33  ? 250 HOH F O     1 
HETATM 16169 O  O     . HOH K 9 .   ? 49.505  -0.190  4.800   1.00 51.71  ? 251 HOH F O     1 
HETATM 16170 O  O     . HOH K 9 .   ? 62.990  -7.600  2.665   1.00 57.84  ? 252 HOH F O     1 
HETATM 16171 O  O     . HOH K 9 .   ? 47.047  -10.325 -17.898 1.00 46.61  ? 253 HOH F O     1 
HETATM 16172 O  O     . HOH K 9 .   ? 64.605  -4.433  -18.953 1.00 51.00  ? 254 HOH F O     1 
HETATM 16173 O  O     . HOH K 9 .   ? 60.504  -5.852  -20.119 1.00 38.49  ? 255 HOH F O     1 
HETATM 16174 O  O     . HOH K 9 .   ? 61.471  -7.107  0.892   1.00 37.04  ? 256 HOH F O     1 
HETATM 16175 O  O     . HOH K 9 .   ? 62.220  -6.658  -9.553  1.00 38.49  ? 257 HOH F O     1 
# 
