data_8QL9
# 
_entry.id   8QL9 
# 
_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   8QL9         pdb_00008ql9 10.2210/pdb8ql9/pdb 
WWPDB D_1292133181 ?            ?                   
# 
_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           8QL9 
_pdbx_database_PDB_obs_spr.replace_pdb_id   7YYV 
_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                        8QL9 
_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    294 ? ? ? ? 
# 
_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 ? ? ? ?     ? ? ? ? ? ? ? ?     ? ? ? ? ? 
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 430 430 430 ALA ALA B . n 
B 2 431 ASP 431 431 431 ASP ASP 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   601 127 HOH HOH A . 
I 9 HOH 2   602 316 HOH HOH A . 
I 9 HOH 3   603 313 HOH HOH A . 
I 9 HOH 4   604 137 HOH HOH A . 
I 9 HOH 5   605 81  HOH HOH A . 
I 9 HOH 6   606 296 HOH HOH A . 
I 9 HOH 7   607 154 HOH HOH A . 
I 9 HOH 8   608 124 HOH HOH A . 
I 9 HOH 9   609 238 HOH HOH A . 
I 9 HOH 10  610 176 HOH HOH A . 
I 9 HOH 11  611 189 HOH HOH A . 
I 9 HOH 12  612 146 HOH HOH A . 
I 9 HOH 13  613 76  HOH HOH A . 
I 9 HOH 14  614 77  HOH HOH A . 
I 9 HOH 15  615 48  HOH HOH A . 
I 9 HOH 16  616 226 HOH HOH A . 
I 9 HOH 17  617 43  HOH HOH A . 
I 9 HOH 18  618 210 HOH HOH A . 
I 9 HOH 19  619 329 HOH HOH A . 
I 9 HOH 20  620 78  HOH HOH A . 
I 9 HOH 21  621 121 HOH HOH A . 
I 9 HOH 22  622 126 HOH HOH A . 
I 9 HOH 23  623 178 HOH HOH A . 
I 9 HOH 24  624 7   HOH HOH A . 
I 9 HOH 25  625 102 HOH HOH A . 
I 9 HOH 26  626 47  HOH HOH A . 
I 9 HOH 27  627 207 HOH HOH A . 
I 9 HOH 28  628 40  HOH HOH A . 
I 9 HOH 29  629 144 HOH HOH A . 
I 9 HOH 30  630 116 HOH HOH A . 
I 9 HOH 31  631 22  HOH HOH A . 
I 9 HOH 32  632 261 HOH HOH A . 
I 9 HOH 33  633 114 HOH HOH A . 
I 9 HOH 34  634 322 HOH HOH A . 
I 9 HOH 35  635 16  HOH HOH A . 
I 9 HOH 36  636 79  HOH HOH A . 
I 9 HOH 37  637 164 HOH HOH A . 
I 9 HOH 38  638 103 HOH HOH A . 
I 9 HOH 39  639 182 HOH HOH A . 
I 9 HOH 40  640 165 HOH HOH A . 
I 9 HOH 41  641 19  HOH HOH A . 
I 9 HOH 42  642 199 HOH HOH A . 
I 9 HOH 43  643 3   HOH HOH A . 
I 9 HOH 44  644 83  HOH HOH A . 
I 9 HOH 45  645 283 HOH HOH A . 
I 9 HOH 46  646 45  HOH HOH A . 
I 9 HOH 47  647 168 HOH HOH A . 
I 9 HOH 48  648 28  HOH HOH A . 
I 9 HOH 49  649 222 HOH HOH A . 
I 9 HOH 50  650 8   HOH HOH A . 
I 9 HOH 51  651 51  HOH HOH A . 
I 9 HOH 52  652 34  HOH HOH A . 
I 9 HOH 53  653 13  HOH HOH A . 
I 9 HOH 54  654 148 HOH HOH A . 
I 9 HOH 55  655 258 HOH HOH A . 
I 9 HOH 56  656 298 HOH HOH A . 
I 9 HOH 57  657 183 HOH HOH A . 
I 9 HOH 58  658 104 HOH HOH A . 
I 9 HOH 59  659 270 HOH HOH A . 
I 9 HOH 60  660 65  HOH HOH A . 
I 9 HOH 61  661 172 HOH HOH A . 
I 9 HOH 62  662 62  HOH HOH A . 
I 9 HOH 63  663 111 HOH HOH A . 
I 9 HOH 64  664 14  HOH HOH A . 
I 9 HOH 65  665 57  HOH HOH A . 
I 9 HOH 66  666 17  HOH HOH A . 
I 9 HOH 67  667 9   HOH HOH A . 
I 9 HOH 68  668 75  HOH HOH A . 
I 9 HOH 69  669 306 HOH HOH A . 
I 9 HOH 70  670 1   HOH HOH A . 
I 9 HOH 71  671 60  HOH HOH A . 
I 9 HOH 72  672 10  HOH HOH A . 
I 9 HOH 73  673 335 HOH HOH A . 
I 9 HOH 74  674 6   HOH HOH A . 
I 9 HOH 75  675 131 HOH HOH A . 
I 9 HOH 76  676 156 HOH HOH A . 
I 9 HOH 77  677 120 HOH HOH A . 
I 9 HOH 78  678 123 HOH HOH A . 
I 9 HOH 79  679 223 HOH HOH A . 
I 9 HOH 80  680 100 HOH HOH A . 
I 9 HOH 81  681 67  HOH HOH A . 
I 9 HOH 82  682 12  HOH HOH A . 
I 9 HOH 83  683 42  HOH HOH A . 
I 9 HOH 84  684 310 HOH HOH A . 
I 9 HOH 85  685 66  HOH HOH A . 
I 9 HOH 86  686 206 HOH HOH A . 
I 9 HOH 87  687 333 HOH HOH A . 
I 9 HOH 88  688 286 HOH HOH A . 
I 9 HOH 89  689 213 HOH HOH A . 
I 9 HOH 90  690 140 HOH HOH A . 
I 9 HOH 91  691 141 HOH HOH A . 
I 9 HOH 92  692 289 HOH HOH A . 
I 9 HOH 93  693 276 HOH HOH A . 
I 9 HOH 94  694 161 HOH HOH A . 
I 9 HOH 95  695 130 HOH HOH A . 
I 9 HOH 96  696 128 HOH HOH A . 
I 9 HOH 97  697 201 HOH HOH A . 
I 9 HOH 98  698 221 HOH HOH A . 
I 9 HOH 99  699 117 HOH HOH A . 
I 9 HOH 100 700 241 HOH HOH A . 
I 9 HOH 101 701 87  HOH HOH A . 
I 9 HOH 102 702 97  HOH HOH A . 
I 9 HOH 103 703 197 HOH HOH A . 
I 9 HOH 104 704 193 HOH HOH A . 
I 9 HOH 105 705 163 HOH HOH A . 
I 9 HOH 106 706 80  HOH HOH A . 
I 9 HOH 107 707 91  HOH HOH A . 
I 9 HOH 108 708 50  HOH HOH A . 
I 9 HOH 109 709 228 HOH HOH A . 
I 9 HOH 110 710 328 HOH HOH A . 
I 9 HOH 111 711 216 HOH HOH A . 
I 9 HOH 112 712 56  HOH HOH A . 
I 9 HOH 113 713 119 HOH HOH A . 
I 9 HOH 114 714 143 HOH HOH A . 
I 9 HOH 115 715 37  HOH HOH A . 
I 9 HOH 116 716 25  HOH HOH A . 
I 9 HOH 117 717 292 HOH HOH A . 
I 9 HOH 118 718 232 HOH HOH A . 
I 9 HOH 119 719 142 HOH HOH A . 
I 9 HOH 120 720 252 HOH HOH A . 
I 9 HOH 121 721 239 HOH HOH A . 
I 9 HOH 122 722 112 HOH HOH A . 
I 9 HOH 123 723 55  HOH HOH A . 
I 9 HOH 124 724 308 HOH HOH A . 
I 9 HOH 125 725 314 HOH HOH A . 
I 9 HOH 126 726 323 HOH HOH A . 
I 9 HOH 127 727 208 HOH HOH A . 
I 9 HOH 128 728 187 HOH HOH A . 
I 9 HOH 129 729 174 HOH HOH A . 
I 9 HOH 130 730 259 HOH HOH A . 
I 9 HOH 131 731 203 HOH HOH A . 
I 9 HOH 132 732 274 HOH HOH A . 
I 9 HOH 133 733 158 HOH HOH A . 
I 9 HOH 134 734 153 HOH HOH A . 
I 9 HOH 135 735 235 HOH HOH A . 
I 9 HOH 136 736 229 HOH HOH A . 
I 9 HOH 137 737 237 HOH HOH A . 
I 9 HOH 138 738 186 HOH HOH A . 
I 9 HOH 139 739 256 HOH HOH A . 
I 9 HOH 140 740 318 HOH HOH A . 
I 9 HOH 141 741 254 HOH HOH A . 
I 9 HOH 142 742 198 HOH HOH A . 
I 9 HOH 143 743 264 HOH HOH A . 
I 9 HOH 144 744 288 HOH HOH A . 
I 9 HOH 145 745 319 HOH HOH A . 
J 9 HOH 1   601 115 HOH HOH B . 
J 9 HOH 2   602 152 HOH HOH B . 
J 9 HOH 3   603 312 HOH HOH B . 
J 9 HOH 4   604 74  HOH HOH B . 
J 9 HOH 5   605 118 HOH HOH B . 
J 9 HOH 6   606 110 HOH HOH B . 
J 9 HOH 7   607 96  HOH HOH B . 
J 9 HOH 8   608 220 HOH HOH B . 
J 9 HOH 9   609 15  HOH HOH B . 
J 9 HOH 10  610 299 HOH HOH B . 
J 9 HOH 11  611 70  HOH HOH B . 
J 9 HOH 12  612 36  HOH HOH B . 
J 9 HOH 13  613 41  HOH HOH B . 
J 9 HOH 14  614 64  HOH HOH B . 
J 9 HOH 15  615 304 HOH HOH B . 
J 9 HOH 16  616 250 HOH HOH B . 
J 9 HOH 17  617 251 HOH HOH B . 
J 9 HOH 18  618 93  HOH HOH B . 
J 9 HOH 19  619 69  HOH HOH B . 
J 9 HOH 20  620 38  HOH HOH B . 
J 9 HOH 21  621 46  HOH HOH B . 
J 9 HOH 22  622 211 HOH HOH B . 
J 9 HOH 23  623 279 HOH HOH B . 
J 9 HOH 24  624 181 HOH HOH B . 
J 9 HOH 25  625 217 HOH HOH B . 
J 9 HOH 26  626 257 HOH HOH B . 
J 9 HOH 27  627 71  HOH HOH B . 
J 9 HOH 28  628 249 HOH HOH B . 
J 9 HOH 29  629 24  HOH HOH B . 
J 9 HOH 30  630 86  HOH HOH B . 
J 9 HOH 31  631 85  HOH HOH B . 
J 9 HOH 32  632 63  HOH HOH B . 
J 9 HOH 33  633 133 HOH HOH B . 
J 9 HOH 34  634 138 HOH HOH B . 
J 9 HOH 35  635 240 HOH HOH B . 
J 9 HOH 36  636 155 HOH HOH B . 
J 9 HOH 37  637 95  HOH HOH B . 
J 9 HOH 38  638 162 HOH HOH B . 
J 9 HOH 39  639 321 HOH HOH B . 
J 9 HOH 40  640 90  HOH HOH B . 
J 9 HOH 41  641 159 HOH HOH B . 
J 9 HOH 42  642 266 HOH HOH B . 
J 9 HOH 43  643 185 HOH HOH B . 
J 9 HOH 44  644 151 HOH HOH B . 
J 9 HOH 45  645 265 HOH HOH B . 
J 9 HOH 46  646 134 HOH HOH B . 
J 9 HOH 47  647 244 HOH HOH B . 
J 9 HOH 48  648 33  HOH HOH B . 
J 9 HOH 49  649 293 HOH HOH B . 
J 9 HOH 50  650 169 HOH HOH B . 
J 9 HOH 51  651 92  HOH HOH B . 
J 9 HOH 52  652 107 HOH HOH B . 
J 9 HOH 53  653 184 HOH HOH B . 
J 9 HOH 54  654 21  HOH HOH B . 
J 9 HOH 55  655 307 HOH HOH B . 
J 9 HOH 56  656 99  HOH HOH B . 
J 9 HOH 57  657 280 HOH HOH B . 
J 9 HOH 58  658 139 HOH HOH B . 
J 9 HOH 59  659 101 HOH HOH B . 
J 9 HOH 60  660 227 HOH HOH B . 
J 9 HOH 61  661 53  HOH HOH B . 
J 9 HOH 62  662 287 HOH HOH B . 
J 9 HOH 63  663 209 HOH HOH B . 
J 9 HOH 64  664 331 HOH HOH B . 
J 9 HOH 65  665 145 HOH HOH B . 
J 9 HOH 66  666 271 HOH HOH B . 
J 9 HOH 67  667 195 HOH HOH B . 
J 9 HOH 68  668 190 HOH HOH B . 
J 9 HOH 69  669 191 HOH HOH B . 
J 9 HOH 70  670 325 HOH HOH B . 
J 9 HOH 71  671 269 HOH HOH B . 
J 9 HOH 72  672 303 HOH HOH B . 
J 9 HOH 73  673 247 HOH HOH B . 
J 9 HOH 74  674 301 HOH HOH B . 
K 9 HOH 1   201 132 HOH HOH F . 
K 9 HOH 2   202 82  HOH HOH F . 
K 9 HOH 3   203 291 HOH HOH F . 
K 9 HOH 4   204 253 HOH HOH F . 
K 9 HOH 5   205 106 HOH HOH F . 
K 9 HOH 6   206 109 HOH HOH F . 
K 9 HOH 7   207 54  HOH HOH F . 
K 9 HOH 8   208 297 HOH HOH F . 
K 9 HOH 9   209 305 HOH HOH F . 
K 9 HOH 10  210 225 HOH HOH F . 
K 9 HOH 11  211 89  HOH HOH F . 
K 9 HOH 12  212 39  HOH HOH F . 
K 9 HOH 13  213 171 HOH HOH F . 
K 9 HOH 14  214 49  HOH HOH F . 
K 9 HOH 15  215 205 HOH HOH F . 
K 9 HOH 16  216 129 HOH HOH F . 
K 9 HOH 17  217 231 HOH HOH F . 
K 9 HOH 18  218 125 HOH HOH F . 
K 9 HOH 19  219 59  HOH HOH F . 
K 9 HOH 20  220 149 HOH HOH F . 
K 9 HOH 21  221 29  HOH HOH F . 
K 9 HOH 22  222 105 HOH HOH F . 
K 9 HOH 23  223 72  HOH HOH F . 
K 9 HOH 24  224 18  HOH HOH F . 
K 9 HOH 25  225 167 HOH HOH F . 
K 9 HOH 26  226 309 HOH HOH F . 
K 9 HOH 27  227 73  HOH HOH F . 
K 9 HOH 28  228 218 HOH HOH F . 
K 9 HOH 29  229 88  HOH HOH F . 
K 9 HOH 30  230 44  HOH HOH F . 
K 9 HOH 31  231 157 HOH HOH F . 
K 9 HOH 32  232 2   HOH HOH F . 
K 9 HOH 33  233 27  HOH HOH F . 
K 9 HOH 34  234 243 HOH HOH F . 
K 9 HOH 35  235 26  HOH HOH F . 
K 9 HOH 36  236 212 HOH HOH F . 
K 9 HOH 37  237 30  HOH HOH F . 
K 9 HOH 38  238 179 HOH HOH F . 
K 9 HOH 39  239 61  HOH HOH F . 
K 9 HOH 40  240 166 HOH HOH F . 
K 9 HOH 41  241 242 HOH HOH F . 
K 9 HOH 42  242 262 HOH HOH F . 
K 9 HOH 43  243 11  HOH HOH F . 
K 9 HOH 44  244 35  HOH HOH F . 
K 9 HOH 45  245 32  HOH HOH F . 
K 9 HOH 46  246 20  HOH HOH F . 
K 9 HOH 47  247 334 HOH HOH F . 
K 9 HOH 48  248 290 HOH HOH F . 
K 9 HOH 49  249 68  HOH HOH F . 
K 9 HOH 50  250 31  HOH HOH F . 
K 9 HOH 51  251 136 HOH HOH F . 
K 9 HOH 52  252 23  HOH HOH F . 
K 9 HOH 53  253 230 HOH HOH F . 
K 9 HOH 54  254 147 HOH HOH F . 
K 9 HOH 55  255 214 HOH HOH F . 
K 9 HOH 56  256 135 HOH HOH F . 
K 9 HOH 57  257 215 HOH HOH F . 
K 9 HOH 58  258 196 HOH HOH F . 
K 9 HOH 59  259 200 HOH HOH F . 
K 9 HOH 60  260 285 HOH HOH F . 
K 9 HOH 61  261 224 HOH HOH F . 
K 9 HOH 62  262 52  HOH HOH F . 
K 9 HOH 63  263 113 HOH HOH F . 
K 9 HOH 64  264 284 HOH HOH F . 
K 9 HOH 65  265 267 HOH HOH F . 
K 9 HOH 66  266 255 HOH HOH F . 
K 9 HOH 67  267 202 HOH HOH F . 
K 9 HOH 68  268 272 HOH HOH F . 
K 9 HOH 69  269 327 HOH HOH F . 
K 9 HOH 70  270 315 HOH HOH F . 
K 9 HOH 71  271 300 HOH HOH F . 
K 9 HOH 72  272 326 HOH HOH F . 
K 9 HOH 73  273 245 HOH HOH F . 
K 9 HOH 74  274 192 HOH HOH F . 
K 9 HOH 75  275 160 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                     8QL9 
_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                         8QL9 
_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                   8QL9 
_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                                       8QL9 
_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                                     122155 
_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                                365.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.01 
_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                                   0.971 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   0.157 
_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                           0.50 
_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                                  0.265 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  2.178 
_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                                 8QL9 
_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                     102475 
_refine.ls_number_reflns_R_free                  1989 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.06 
_refine.ls_percent_reflns_R_free                 1.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2621 
_refine.ls_R_factor_R_free                       0.3061 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2612 
_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                 35.74 
_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                            0.30 
_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             294 
_refine_hist.number_atoms_total               8268 
_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        7889 
_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' ? 0.003  ? 16286 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.593  ? 22121 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.587 ? 5940  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 2457  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 2909  ? 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 7072 98.00  . . . . 0.3934 . . . . . . . . . . . 0.4092 
'X-RAY DIFFRACTION' 1.85 1.90 . . 140 7162 99.00  . . . . 0.3784 . . . . . . . . . . . 0.4021 
'X-RAY DIFFRACTION' 1.90 1.95 . . 145 7240 99.00  . . . . 0.3562 . . . . . . . . . . . 0.4044 
'X-RAY DIFFRACTION' 1.95 2.02 . . 141 7172 99.00  . . . . 0.3350 . . . . . . . . . . . 0.4162 
'X-RAY DIFFRACTION' 2.02 2.09 . . 142 7169 100.00 . . . . 0.3082 . . . . . . . . . . . 0.3238 
'X-RAY DIFFRACTION' 2.09 2.17 . . 142 7164 100.00 . . . . 0.2909 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 2.17 2.27 . . 141 7223 100.00 . . . . 0.2738 . . . . . . . . . . . 0.3153 
'X-RAY DIFFRACTION' 2.27 2.39 . . 142 7170 100.00 . . . . 0.2740 . . . . . . . . . . . 0.2956 
'X-RAY DIFFRACTION' 2.39 2.53 . . 142 7182 99.00  . . . . 0.2713 . . . . . . . . . . . 0.3061 
'X-RAY DIFFRACTION' 2.53 2.72 . . 143 7138 99.00  . . . . 0.2755 . . . . . . . . . . . 0.3312 
'X-RAY DIFFRACTION' 2.72 2.99 . . 142 7199 99.00  . . . . 0.2662 . . . . . . . . . . . 0.3321 
'X-RAY DIFFRACTION' 2.99 3.40 . . 142 7183 99.00  . . . . 0.2517 . . . . . . . . . . . 0.3074 
'X-RAY DIFFRACTION' 3.40 4.23 . . 143 7162 98.00  . . . . 0.2274 . . . . . . . . . . . 0.2537 
'X-RAY DIFFRACTION' 4.23 9.49 . . 144 7250 99.00  . . . . 0.2324 . . . . . . . . . . . 0.2873 
# 
_struct.entry_id                     8QL9 
_struct.title                        
'Ultrafast structural transitions in an azobenzene photoswitch at near-atomic resolution: 1 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        8QL9 
_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 8QL9        8QL9   ? 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 8QL9 A 1 ? 451 ? P81947 1 ? 451 ? 1 451 
2 2 8QL9 B 1 ? 445 ? Q6B856 1 ? 445 ? 1 445 
3 3 8QL9 F 1 ? 169 ? 8QL9   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)' 6330  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  36910 ? 
# 
_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 ASP A 47  ? THR A 51  ? ASP A 47  THR A 51  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 72  ? THR A 80  ? PRO A 72  THR A 80  1 ? 9  
HELX_P HELX_P4  AA4 GLY A 81  ? LEU A 86  ? GLY A 81  LEU A 86  5 ? 6  
HELX_P HELX_P5  AA5 HIS A 88  ? GLU A 90  ? HIS A 88  GLU A 90  5 ? 3  
HELX_P HELX_P6  AA6 ASN A 102 ? TYR A 108 ? ASN A 102 TYR A 108 1 ? 7  
HELX_P HELX_P7  AA7 TYR A 108 ? GLU A 113 ? TYR A 108 GLU A 113 1 ? 6  
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 ? GLU A 196 ? VAL A 182 GLU A 196 1 ? 15 
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 GLY A 416 ? GLY A 436 ? GLY A 416 GLY A 436 1 ? 21 
HELX_P HELX_P21 AC3 GLY B 10  ? HIS B 28  ? GLY B 10  HIS B 28  1 ? 19 
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 GLY B 71  ? SER B 78  ? GLY B 71  SER B 78  1 ? 8  
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 THR B 107 ? SER B 126 ? THR B 107 SER B 126 1 ? 20 
HELX_P HELX_P28 AD1 GLY B 142 ? TYR B 159 ? GLY B 142 TYR B 159 1 ? 18 
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 295 ? MET B 299 ? ASP B 295 MET B 299 5 ? 5  
HELX_P HELX_P36 AD9 ASP B 304 ? GLY B 308 ? ASP B 304 GLY B 308 5 ? 5  
HELX_P HELX_P37 AE1 SER B 322 ? ASN B 337 ? SER B 322 ASN B 337 1 ? 16 
HELX_P HELX_P38 AE2 SER B 338 ? PHE B 341 ? SER B 338 PHE B 341 5 ? 4  
HELX_P HELX_P39 AE3 ILE B 374 ? ARG B 391 ? ILE B 374 ARG B 391 1 ? 18 
HELX_P HELX_P40 AE4 LEU B 395 ? GLY B 400 ? LEU B 395 GLY B 400 1 ? 6  
HELX_P HELX_P41 AE5 ASP B 404 ? ALA B 428 ? ASP B 404 ALA B 428 1 ? 25 
HELX_P HELX_P42 AE6 LEU C 14  ? GLY C 25  ? LEU F 14  GLY F 25  1 ? 12 
HELX_P HELX_P43 AE7 GLN C 26  ? ASN C 36  ? GLN F 26  ASN F 36  1 ? 11 
HELX_P HELX_P44 AE8 THR C 49  ? TYR C 57  ? THR F 49  TYR F 57  1 ? 9  
HELX_P HELX_P45 AE9 HIS C 59  ? LYS C 68  ? HIS F 59  LYS F 68  1 ? 10 
HELX_P HELX_P46 AF1 THR C 82  ? GLY C 91  ? THR F 82  GLY F 91  1 ? 10 
HELX_P HELX_P47 AF2 HIS C 92  ? HIS C 102 ? HIS F 92  HIS F 102 1 ? 11 
HELX_P HELX_P48 AF3 THR C 115 ? MET C 123 ? THR F 115 MET F 123 1 ? 9  
HELX_P HELX_P49 AF4 HIS C 125 ? HIS C 135 ? HIS F 125 HIS F 135 1 ? 11 
HELX_P HELX_P50 AF5 THR C 148 ? ASN C 156 ? THR F 148 ASN F 156 1 ? 9  
HELX_P HELX_P51 AF6 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 ? ? ? ? ? ? ? 2.559 ? ? 
metalc2  metalc ? ? A ASP 39 OD1 B ? ? 1_555 F CA  . CA B ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.964 ? ? 
metalc3  metalc ? ? A ASP 39 OD2 A ? ? 1_555 F CA  . CA A ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc4  metalc ? ? A ASP 39 OD2 B ? ? 1_555 F CA  . CA B ? A ASP 39  A CA  503 1_555 ? ? ? ? ? ? ? 2.846 ? ? 
metalc5  metalc ? ? A THR 41 O   A ? ? 1_555 F CA  . CA A ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc6  metalc ? ? A THR 41 O   B ? ? 1_555 F CA  . CA B ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.624 ? ? 
metalc7  metalc ? ? A THR 41 OG1 A ? ? 1_555 F CA  . CA A ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.435 ? ? 
metalc8  metalc ? ? A THR 41 OG1 B ? ? 1_555 F CA  . CA B ? A THR 41  A CA  503 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc9  metalc ? ? A GLY 44 O   A ? ? 1_555 F CA  . CA A ? A GLY 44  A CA  503 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc10 metalc ? ? A GLY 44 O   B ? ? 1_555 F CA  . CA B ? A GLY 44  A CA  503 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc11 metalc ? ? A GLU 55 OE1 A ? ? 1_555 F CA  . CA A ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.775 ? ? 
metalc12 metalc ? ? A GLU 55 OE1 B ? ? 1_555 F CA  . CA B ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.866 ? ? 
metalc13 metalc ? ? A GLU 55 OE2 A ? ? 1_555 F CA  . CA A ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.674 ? ? 
metalc14 metalc ? ? A GLU 55 OE2 B ? ? 1_555 F CA  . CA B ? A GLU 55  A CA  503 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc15 metalc ? ? D GTP .  O1G A ? ? 1_555 E MG  . MG A ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc16 metalc ? ? D GTP .  O1G B ? ? 1_555 E MG  . MG B ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc17 metalc ? ? D GTP .  O2B A ? ? 1_555 E MG  . MG A ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc18 metalc ? ? D GTP .  O2B B ? ? 1_555 E MG  . MG B ? A GTP 501 A MG  502 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc19 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 624 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc20 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 624 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc21 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 643 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc22 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 643 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc23 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 664 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc24 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 664 1_555 ? ? ? ? ? ? ? 1.846 ? ? 
metalc25 metalc ? ? E MG  .  MG  A ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 673 1_555 ? ? ? ? ? ? ? 1.979 ? ? 
metalc26 metalc ? ? E MG  .  MG  B ? ? 1_555 I HOH . O  ? ? A MG  502 A HOH 673 1_555 ? ? ? ? ? ? ? 2.389 ? ? 
# 
_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 53.5  ? 
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_555 104.2 ? 
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 90.6  ? 
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 86.9  ? 
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_555 130.7 ? 
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 70.0  ? 
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_555 171.0 ? 
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_555 135.5 ? 
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 77.0  ? 
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 85.1  ? 
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_555 120.7 ? 
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 67.2  ? 
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 76.8  ? 
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_555 141.3 ? 
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 68.3  ? 
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_555 106.8 ? 
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 73.1  ? 
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_555 124.2 ? 
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_555 154.8 ? 
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 79.2  ? 
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 47.6  ? 
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 44.4  ? 
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 62.6  ? 
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 63.5  ? 
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 59.2  ? 
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_555 101.5 ? 
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 69.0  ? 
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_555 160.1 ? 
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_555 150.4 ? 
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_555 108.4 ? 
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_555 101.3 ? 
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_555 111.2 ? 
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 71.6  ? 
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 69.2  ? 
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_555 135.8 ? 
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 78.9  ? 
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_555 126.6 ? 
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 85.2  ? 
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_555 116.5 ? 
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_555 173.0 ? 
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 73.1  ? 
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 48.3  ? 
43 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 92.6  ? 
44 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 624 ? 1_555 80.4  ? 
45 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 624 ? 1_555 172.9 ? 
46 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 643 ? 1_555 169.7 ? 
47 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 643 ? 1_555 96.9  ? 
48 O   ? I HOH .  ? A HOH 624 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 643 ? 1_555 90.1  ? 
49 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 84.4  ? 
50 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 81.9  ? 
51 O   ? I HOH .  ? A HOH 624 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 96.0  ? 
52 O   ? I HOH .  ? A HOH 643 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 100.7 ? 
53 O1G A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 88.0  ? 
54 O2B A D GTP .  ? A GTP 501 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 91.8  ? 
55 O   ? I HOH .  ? A HOH 624 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 89.3  ? 
56 O   ? I HOH .  ? A HOH 643 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 87.9  ? 
57 O   ? I HOH .  ? A HOH 664 ? 1_555 MG A E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 169.9 ? 
58 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 85.8  ? 
59 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 624 ? 1_555 93.6  ? 
60 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 624 ? 1_555 146.1 ? 
61 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 643 ? 1_555 154.8 ? 
62 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 643 ? 1_555 90.0  ? 
63 O   ? I HOH .  ? A HOH 624 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 643 ? 1_555 76.3  ? 
64 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 108.2 ? 
65 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 106.7 ? 
66 O   ? I HOH .  ? A HOH 624 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 105.6 ? 
67 O   ? I HOH .  ? A HOH 643 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 664 ? 1_555 96.8  ? 
68 O1G B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 85.9  ? 
69 O2B B D GTP .  ? A GTP 501 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 69.1  ? 
70 O   ? I HOH .  ? A HOH 624 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 77.0  ? 
71 O   ? I HOH .  ? A HOH 643 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 69.4  ? 
72 O   ? I HOH .  ? A HOH 664 ? 1_555 MG B E MG . ? A MG 502 ? 1_555 O   ? I HOH .  ? A HOH 673 ? 1_555 165.2 ? 
# 
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 -0.59 
2 ALA 273 A . ? ALA 273 A PRO 274 A ? PRO 274 A 1 -2.19 
3 ALA 271 B . ? ALA 271 B PRO 272 B ? PRO 272 B 1 -1.85 
4 ALA 271 B . ? ALA 271 B PRO 272 B ? PRO 272 B 1 -2.47 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 2  ? 
AA3 ? 4  ? 
AA4 ? 10 ? 
AA5 ? 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      
AA4 6 7  ? parallel      
AA4 7 8  ? anti-parallel 
AA4 8 9  ? anti-parallel 
AA4 9 10 ? parallel      
AA5 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  LEU A 92  ? THR A 94  ? LEU A 92  THR A 94  
AA1 2  ALA A 65  ? ASP A 69  ? ALA A 65  ASP A 69  
AA1 3  CYS A 4   ? VAL A 9   ? CYS A 4   VAL A 9   
AA1 4  GLY A 134 ? SER A 140 ? GLY A 134 SER A 140 
AA1 5  SER A 165 ? TYR A 172 ? SER A 165 TYR A 172 
AA1 6  CYS A 200 ? ASP A 205 ? CYS A 200 ASP A 205 
AA2 1  PHE A 53  ? GLU A 55  ? PHE A 53  GLU A 55  
AA2 2  HIS A 61  ? PRO A 63  ? HIS A 61  PRO A 63  
AA3 1  LEU A 269 ? ALA A 273 ? LEU A 269 ALA A 273 
AA3 2  ARG A 373 ? 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   ? ALA B 9   ? GLU B 3   ALA B 9   
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  GLU B 198 ? ASP B 203 ? GLU B 198 ASP B 203 
AA4 7  PHE B 265 ? ALA B 271 ? PHE B 265 ALA B 271 
AA4 8  SER B 364 ? SER B 371 ? SER B 364 SER B 371 
AA4 9  TYR B 310 ? ARG B 318 ? TYR B 310 ARG B 318 
AA4 10 VAL B 349 ? CYS B 354 ? VAL B 349 CYS B 354 
AA5 1  TYR B 51  ? GLU B 53  ? TYR B 51  GLU B 53  
AA5 2  TYR B 59  ? PRO B 61  ? TYR B 59  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 HIS A 8   ? N HIS A 8   
AA1 3 4  N ILE A 7   ? N ILE A 7   O LEU A 136 ? O LEU A 136 
AA1 4 5  N VAL A 137 ? N VAL A 137 O PHE A 169 ? O PHE A 169 
AA1 5 6  N GLU A 168 ? N GLU A 168 O PHE A 202 ? O PHE A 202 
AA2 1 2  N SER A 54  ? N SER A 54  O VAL A 62  ? O VAL A 62  
AA3 1 2  N THR A 271 ? N THR A 271 O MET A 377 ? O MET A 377 
AA3 2 3  O CYS A 376 ? O CYS A 376 N LEU A 318 ? N LEU A 318 
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 LEU B 135 ? N LEU B 135 O PHE B 167 ? O PHE B 167 
AA4 5 6  N THR B 166 ? N THR B 166 O TYR B 200 ? O TYR B 200 
AA4 6 7  N THR B 199 ? N THR B 199 O PHE B 266 ? O PHE B 266 
AA4 7 8  N GLY B 269 ? N GLY B 269 O PHE B 367 ? O PHE B 367 
AA4 8 9  O ASN B 370 ? O ASN B 370 N LEU B 311 ? N LEU B 311 
AA4 9 10 N ALA B 315 ? N ALA B 315 O LYS B 350 ? O LYS B 350 
AA5 1 2  N ASN B 52  ? N ASN B 52  O VAL B 60  ? O VAL B 60  
# 
_pdbx_entry_details.entry_id                   8QL9 
_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 O   A HOH 612 ? ? O A HOH 732 ? ? 2.11 
2  1 O   A HOH 611 ? ? O A HOH 700 ? ? 2.12 
3  1 O   B HOH 655 ? ? O B HOH 672 ? ? 2.12 
4  1 OE1 A GLU 297 ? B O A HOH 601 ? ? 2.13 
5  1 O   A HOH 732 ? ? O A HOH 744 ? ? 2.13 
6  1 OD2 A ASP 47  ? A O A HOH 602 ? ? 2.14 
7  1 O   A ASP 98  ? A O A HOH 603 ? ? 2.14 
8  1 OD2 B ASP 249 ? B O B HOH 601 ? ? 2.14 
9  1 OH  B TYR 310 ? B O B HOH 602 ? ? 2.15 
10 1 OE1 B GLN 245 ? A O B HOH 603 ? ? 2.17 
11 1 OD2 F ASP 39  ? A O F HOH 201 ? ? 2.18 
12 1 O   A HOH 622 ? ? O A HOH 736 ? ? 2.18 
# 
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 -87.06  36.52   
2  1 TYR A 83  ? B -98.34  50.82   
3  1 ASN A 101 ? B 56.33   19.88   
4  1 TYR A 108 ? A -107.24 -72.48  
5  1 THR A 109 ? A -67.91  -73.24  
6  1 THR A 109 ? B -124.44 -73.33  
7  1 SER A 147 ? A -95.15  -63.76  
8  1 VAL A 177 ? A -110.22 74.70   
9  1 ARG A 215 ? A -70.49  -72.05  
10 1 HIS A 266 ? A -109.86 41.60   
11 1 HIS A 266 ? B -108.65 42.79   
12 1 LYS A 280 ? B -101.79 64.36   
13 1 ILE A 335 ? B -99.40  55.67   
14 1 THR A 337 ? A -105.96 -63.64  
15 1 PRO A 348 ? A -57.40  108.39  
16 1 THR A 349 ? A -59.32  94.28   
17 1 GLU A 411 ? B -102.88 43.14   
18 1 ARG B 2   ? A -131.00 -55.19  
19 1 ARG B 2   ? B -145.45 -98.08  
20 1 ASP B 39  ? A -158.01 45.86   
21 1 ALA B 54  ? A -121.25 -169.51 
22 1 ASN B 89  ? B -88.42  34.24   
23 1 THR B 107 ? A -117.80 -81.85  
24 1 THR B 107 ? B -117.27 -87.09  
25 1 ASP B 177 ? B -101.63 79.47   
26 1 LYS B 216 ? A 59.25   73.32   
27 1 PRO B 243 ? A -54.17  -74.62  
28 1 ASN B 247 ? B -62.52  82.67   
29 1 SER B 275 ? B -103.37 -149.53 
30 1 ARG B 276 ? B -105.94 55.93   
31 1 ALA B 302 ? A -69.15  59.62   
32 1 PRO B 358 ? A -72.83  -154.33 
33 1 PHE B 394 ? B 59.92   17.48   
34 1 ALA B 430 ? B -82.16  -73.82  
35 1 LYS F 68  ? A -69.83  0.14    
36 1 GLN F 166 ? B -102.60 63.36   
# 
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 GLU 432 ? B GLU 432 
21 1 Y 1 B GLN 433 ? B GLN 433 
22 1 Y 1 B GLY 434 ? B GLY 434 
23 1 Y 1 B GLU 435 ? B GLU 435 
24 1 Y 1 B PHE 436 ? B PHE 436 
25 1 Y 1 B GLU 437 ? B GLU 437 
26 1 Y 1 B GLU 438 ? B GLU 438 
27 1 Y 1 B GLU 439 ? B GLU 439 
28 1 Y 1 B GLU 440 ? B GLU 440 
29 1 Y 1 B GLY 441 ? B GLY 441 
30 1 Y 1 B GLU 442 ? B GLU 442 
31 1 Y 1 B ASP 443 ? B ASP 443 
32 1 Y 1 B GLU 444 ? B GLU 444 
33 1 Y 1 B ALA 445 ? B ALA 445 
34 1 Y 1 F MET 1   ? C MET 1   
35 1 Y 1 F ARG 2   ? C ARG 2   
36 1 Y 1 F GLY 3   ? C GLY 3   
37 1 Y 1 F SER 4   ? C SER 4   
38 1 Y 1 F HIS 5   ? C HIS 5   
39 1 Y 1 F HIS 6   ? C HIS 6   
40 1 Y 1 F HIS 7   ? C HIS 7   
41 1 Y 1 F HIS 8   ? C HIS 8   
42 1 Y 1 F HIS 9   ? C HIS 9   
43 1 Y 1 F HIS 10  ? C HIS 10  
44 1 Y 1 F GLY 11  ? C GLY 11  
45 1 Y 1 F SER 12  ? C SER 12  
46 1 Y 1 F LEU 168 ? C LEU 168 
47 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                    8QL9 
_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   ? -28.948 -3.711  36.074  0.50 44.00 ? 1   MET A N     1 
ATOM   2     N  N     B MET A 1 1   ? -27.724 -3.626  37.459  0.50 42.63 ? 1   MET A N     1 
ATOM   3     C  CA    A MET A 1 1   ? -27.500 -3.617  36.220  0.50 40.12 ? 1   MET A CA    1 
ATOM   4     C  CA    B MET A 1 1   ? -27.088 -4.473  36.462  0.50 41.58 ? 1   MET A CA    1 
ATOM   5     C  C     A MET A 1 1   ? -26.874 -2.796  35.095  0.50 40.74 ? 1   MET A C     1 
ATOM   6     C  C     B MET A 1 1   ? -26.791 -3.672  35.200  0.50 39.79 ? 1   MET A C     1 
ATOM   7     O  O     A MET A 1 1   ? -27.560 -2.037  34.409  0.50 38.50 ? 1   MET A O     1 
ATOM   8     O  O     B MET A 1 1   ? -27.707 -3.256  34.488  0.50 41.92 ? 1   MET A O     1 
ATOM   9     C  CB    A MET A 1 1   ? -26.878 -5.016  36.273  0.50 40.29 ? 1   MET A CB    1 
ATOM   10    C  CB    B MET A 1 1   ? -27.978 -5.674  36.133  0.50 41.54 ? 1   MET A CB    1 
ATOM   11    C  CG    A MET A 1 1   ? -27.318 -5.928  35.144  0.50 33.44 ? 1   MET A CG    1 
ATOM   12    C  CG    B MET A 1 1   ? -27.243 -6.879  35.555  0.50 35.38 ? 1   MET A CG    1 
ATOM   13    S  SD    A MET A 1 1   ? -26.412 -5.651  33.611  0.50 35.51 ? 1   MET A SD    1 
ATOM   14    S  SD    B MET A 1 1   ? -26.568 -6.640  33.897  0.50 34.91 ? 1   MET A SD    1 
ATOM   15    C  CE    A MET A 1 1   ? -27.492 -6.488  32.453  0.50 29.87 ? 1   MET A CE    1 
ATOM   16    C  CE    B MET A 1 1   ? -28.056 -6.253  32.977  0.50 33.11 ? 1   MET A CE    1 
ATOM   17    N  N     A ARG A 1 2   ? -25.561 -2.945  34.920  0.50 34.02 ? 2   ARG A N     1 
ATOM   18    N  N     B ARG A 1 2   ? -25.505 -3.461  34.930  0.50 35.21 ? 2   ARG A N     1 
ATOM   19    C  CA    A ARG A 1 2   ? -24.824 -2.270  33.858  0.50 32.45 ? 2   ARG A CA    1 
ATOM   20    C  CA    B ARG A 1 2   ? -25.057 -2.755  33.738  0.50 32.88 ? 2   ARG A CA    1 
ATOM   21    C  C     A ARG A 1 2   ? -23.768 -3.227  33.317  0.50 31.10 ? 2   ARG A C     1 
ATOM   22    C  C     B ARG A 1 2   ? -23.881 -3.506  33.128  0.50 31.04 ? 2   ARG A C     1 
ATOM   23    O  O     A ARG A 1 2   ? -22.963 -3.757  34.087  0.50 29.40 ? 2   ARG A O     1 
ATOM   24    O  O     B ARG A 1 2   ? -22.958 -3.910  33.839  0.50 28.75 ? 2   ARG A O     1 
ATOM   25    C  CB    A ARG A 1 2   ? -24.175 -0.978  34.376  0.50 31.87 ? 2   ARG A CB    1 
ATOM   26    C  CB    B ARG A 1 2   ? -24.673 -1.308  34.068  0.50 32.59 ? 2   ARG A CB    1 
ATOM   27    C  CG    A ARG A 1 2   ? -25.139 0.063   34.941  0.50 36.26 ? 2   ARG A CG    1 
ATOM   28    C  CG    B ARG A 1 2   ? -25.864 -0.426  34.425  0.50 38.74 ? 2   ARG A CG    1 
ATOM   29    C  CD    A ARG A 1 2   ? -24.389 1.292   35.450  0.50 32.90 ? 2   ARG A CD    1 
ATOM   30    C  CD    B ARG A 1 2   ? -25.448 1.024   34.557  0.50 33.19 ? 2   ARG A CD    1 
ATOM   31    N  NE    A ARG A 1 2   ? -23.701 1.994   34.372  0.50 32.67 ? 2   ARG A NE    1 
ATOM   32    N  NE    B ARG A 1 2   ? -24.707 1.472   33.386  0.50 27.61 ? 2   ARG A NE    1 
ATOM   33    C  CZ    A ARG A 1 2   ? -22.724 2.874   34.551  0.50 31.92 ? 2   ARG A CZ    1 
ATOM   34    C  CZ    B ARG A 1 2   ? -24.102 2.646   33.283  0.50 32.87 ? 2   ARG A CZ    1 
ATOM   35    N  NH1   A ARG A 1 2   ? -22.285 3.182   35.760  0.50 39.60 ? 2   ARG A NH1   1 
ATOM   36    N  NH1   B ARG A 1 2   ? -24.141 3.531   34.264  0.50 30.19 ? 2   ARG A NH1   1 
ATOM   37    N  NH2   A ARG A 1 2   ? -22.169 3.453   33.490  0.50 36.60 ? 2   ARG A NH2   1 
ATOM   38    N  NH2   B ARG A 1 2   ? -23.433 2.935   32.169  0.50 34.73 ? 2   ARG A NH2   1 
ATOM   39    N  N     A GLU A 1 3   ? -23.753 -3.428  31.998  0.50 30.48 ? 3   GLU A N     1 
ATOM   40    N  N     B GLU A 1 3   ? -23.912 -3.671  31.807  0.50 29.85 ? 3   GLU A N     1 
ATOM   41    C  CA    A GLU A 1 3   ? -23.017 -4.535  31.397  0.50 28.89 ? 3   GLU A CA    1 
ATOM   42    C  CA    B GLU A 1 3   ? -23.047 -4.630  31.133  0.50 29.23 ? 3   GLU A CA    1 
ATOM   43    C  C     A GLU A 1 3   ? -21.537 -4.203  31.195  0.50 24.21 ? 3   GLU A C     1 
ATOM   44    C  C     B GLU A 1 3   ? -21.607 -4.135  31.014  0.50 24.40 ? 3   GLU A C     1 
ATOM   45    O  O     A GLU A 1 3   ? -21.137 -3.041  31.086  0.50 22.98 ? 3   GLU A O     1 
ATOM   46    O  O     B GLU A 1 3   ? -21.344 -2.941  30.840  0.50 24.14 ? 3   GLU A O     1 
ATOM   47    C  CB    A GLU A 1 3   ? -23.633 -4.921  30.050  0.50 27.30 ? 3   GLU A CB    1 
ATOM   48    C  CB    B GLU A 1 3   ? -23.594 -4.949  29.739  0.50 26.27 ? 3   GLU A CB    1 
ATOM   49    C  CG    A GLU A 1 3   ? -25.109 -5.294  30.102  0.50 28.67 ? 3   GLU A CG    1 
ATOM   50    C  CG    B GLU A 1 3   ? -24.925 -5.701  29.727  0.50 27.02 ? 3   GLU A CG    1 
ATOM   51    C  CD    A GLU A 1 3   ? -26.038 -4.101  29.956  0.50 28.24 ? 3   GLU A CD    1 
ATOM   52    C  CD    B GLU A 1 3   ? -26.141 -4.787  29.818  0.50 28.56 ? 3   GLU A CD    1 
ATOM   53    O  OE1   A GLU A 1 3   ? -25.592 -2.953  30.167  0.50 27.91 ? 3   GLU A OE1   1 
ATOM   54    O  OE1   B GLU A 1 3   ? -25.985 -3.603  30.181  0.50 28.01 ? 3   GLU A OE1   1 
ATOM   55    O  OE2   A GLU A 1 3   ? -27.218 -4.315  29.615  0.50 27.72 ? 3   GLU A OE2   1 
ATOM   56    O  OE2   B GLU A 1 3   ? -27.259 -5.256  29.514  0.50 27.32 ? 3   GLU A OE2   1 
ATOM   57    N  N     A CYS A 1 4   ? -20.723 -5.261  31.121  0.50 25.50 ? 4   CYS A N     1 
ATOM   58    N  N     B CYS A 1 4   ? -20.673 -5.082  31.110  0.50 25.95 ? 4   CYS A N     1 
ATOM   59    C  CA    A CYS A 1 4   ? -19.295 -5.161  30.828  0.50 26.31 ? 4   CYS A CA    1 
ATOM   60    C  CA    B CYS A 1 4   ? -19.263 -4.873  30.788  0.50 25.48 ? 4   CYS A CA    1 
ATOM   61    C  C     A CYS A 1 4   ? -18.929 -6.113  29.698  0.50 23.17 ? 4   CYS A C     1 
ATOM   62    C  C     B CYS A 1 4   ? -18.852 -5.885  29.728  0.50 23.05 ? 4   CYS A C     1 
ATOM   63    O  O     A CYS A 1 4   ? -19.343 -7.275  29.699  0.50 24.95 ? 4   CYS A O     1 
ATOM   64    O  O     B CYS A 1 4   ? -19.147 -7.077  29.861  0.50 24.86 ? 4   CYS A O     1 
ATOM   65    C  CB    A CYS A 1 4   ? -18.433 -5.500  32.054  0.50 26.80 ? 4   CYS A CB    1 
ATOM   66    C  CB    B CYS A 1 4   ? -18.364 -5.035  32.022  0.50 28.00 ? 4   CYS A CB    1 
ATOM   67    S  SG    A CYS A 1 4   ? -18.745 -4.519  33.530  0.50 31.48 ? 4   CYS A SG    1 
ATOM   68    S  SG    B CYS A 1 4   ? -18.559 -3.795  33.325  0.50 31.25 ? 4   CYS A SG    1 
ATOM   69    N  N     A ILE A 1 5   ? -18.132 -5.626  28.746  0.50 27.73 ? 5   ILE A N     1 
ATOM   70    N  N     B ILE A 1 5   ? -18.160 -5.419  28.687  0.50 27.13 ? 5   ILE A N     1 
ATOM   71    C  CA    A ILE A 1 5   ? -17.610 -6.440  27.651  0.50 24.37 ? 5   ILE A CA    1 
ATOM   72    C  CA    B ILE A 1 5   ? -17.718 -6.276  27.589  0.50 24.24 ? 5   ILE A CA    1 
ATOM   73    C  C     A ILE A 1 5   ? -16.106 -6.592  27.849  0.50 24.63 ? 5   ILE A C     1 
ATOM   74    C  C     B ILE A 1 5   ? -16.234 -6.576  27.762  0.50 24.75 ? 5   ILE A C     1 
ATOM   75    O  O     A ILE A 1 5   ? -15.405 -5.602  28.086  0.50 24.32 ? 5   ILE A O     1 
ATOM   76    O  O     B ILE A 1 5   ? -15.426 -5.659  27.945  0.50 24.47 ? 5   ILE A O     1 
ATOM   77    C  CB    A ILE A 1 5   ? -17.925 -5.816  26.279  0.50 24.42 ? 5   ILE A CB    1 
ATOM   78    C  CB    B ILE A 1 5   ? -17.987 -5.619  26.224  0.50 24.25 ? 5   ILE A CB    1 
ATOM   79    C  CG1   A ILE A 1 5   ? -19.436 -5.770  26.038  0.50 26.66 ? 5   ILE A CG1   1 
ATOM   80    C  CG1   B ILE A 1 5   ? -19.486 -5.603  25.915  0.50 26.95 ? 5   ILE A CG1   1 
ATOM   81    C  CG2   A ILE A 1 5   ? -17.227 -6.593  25.157  0.50 23.13 ? 5   ILE A CG2   1 
ATOM   82    C  CG2   B ILE A 1 5   ? -17.208 -6.337  25.113  0.50 23.55 ? 5   ILE A CG2   1 
ATOM   83    C  CD1   A ILE A 1 5   ? -19.836 -5.029  24.768  0.50 28.98 ? 5   ILE A CD1   1 
ATOM   84    C  CD1   B ILE A 1 5   ? -19.835 -4.894  24.613  0.50 28.58 ? 5   ILE A CD1   1 
ATOM   85    N  N     A SER A 1 6   ? -15.616 -7.828  27.763  0.50 22.23 ? 6   SER A N     1 
ATOM   86    N  N     B SER A 1 6   ? -15.874 -7.858  27.706  0.50 21.59 ? 6   SER A N     1 
ATOM   87    C  CA    A SER A 1 6   ? -14.196 -8.134  27.910  0.50 18.46 ? 6   SER A CA    1 
ATOM   88    C  CA    B SER A 1 6   ? -14.476 -8.266  27.769  0.50 20.31 ? 6   SER A CA    1 
ATOM   89    C  C     A SER A 1 6   ? -13.621 -8.501  26.547  0.50 19.94 ? 6   SER A C     1 
ATOM   90    C  C     B SER A 1 6   ? -13.907 -8.401  26.362  0.50 19.42 ? 6   SER A C     1 
ATOM   91    O  O     A SER A 1 6   ? -14.114 -9.422  25.888  0.50 21.28 ? 6   SER A O     1 
ATOM   92    O  O     B SER A 1 6   ? -14.605 -8.819  25.434  0.50 21.11 ? 6   SER A O     1 
ATOM   93    C  CB    A SER A 1 6   ? -13.976 -9.276  28.906  0.50 19.64 ? 6   SER A CB    1 
ATOM   94    C  CB    B SER A 1 6   ? -14.323 -9.591  28.518  0.50 19.73 ? 6   SER A CB    1 
ATOM   95    O  OG    A SER A 1 6   ? -14.414 -8.916  30.209  0.50 18.28 ? 6   SER A OG    1 
ATOM   96    O  OG    B SER A 1 6   ? -14.796 -9.487  29.850  0.50 20.21 ? 6   SER A OG    1 
ATOM   97    N  N     A ILE A 1 7   ? -12.571 -7.796  26.136  0.50 20.25 ? 7   ILE A N     1 
ATOM   98    N  N     B ILE A 1 7   ? -12.634 -8.035  26.216  0.50 20.04 ? 7   ILE A N     1 
ATOM   99    C  CA    A ILE A 1 7   ? -11.912 -8.027  24.854  0.50 20.61 ? 7   ILE A CA    1 
ATOM   100   C  CA    B ILE A 1 7   ? -11.902 -8.134  24.956  0.50 20.78 ? 7   ILE A CA    1 
ATOM   101   C  C     A ILE A 1 7   ? -10.568 -8.686  25.127  0.50 22.60 ? 7   ILE A C     1 
ATOM   102   C  C     B ILE A 1 7   ? -10.542 -8.745  25.259  0.50 22.68 ? 7   ILE A C     1 
ATOM   103   O  O     A ILE A 1 7   ? -9.787  -8.192  25.949  0.50 22.21 ? 7   ILE A O     1 
ATOM   104   O  O     B ILE A 1 7   ? -9.837  -8.275  26.159  0.50 21.99 ? 7   ILE A O     1 
ATOM   105   C  CB    A ILE A 1 7   ? -11.736 -6.713  24.073  0.50 20.75 ? 7   ILE A CB    1 
ATOM   106   C  CB    B ILE A 1 7   ? -11.736 -6.759  24.278  0.50 20.22 ? 7   ILE A CB    1 
ATOM   107   C  CG1   A ILE A 1 7   ? -13.042 -5.915  24.086  0.50 22.89 ? 7   ILE A CG1   1 
ATOM   108   C  CG1   B ILE A 1 7   ? -13.095 -6.084  24.071  0.50 22.81 ? 7   ILE A CG1   1 
ATOM   109   C  CG2   A ILE A 1 7   ? -11.292 -6.995  22.636  0.50 22.82 ? 7   ILE A CG2   1 
ATOM   110   C  CG2   B ILE A 1 7   ? -10.991 -6.900  22.950  0.50 23.96 ? 7   ILE A CG2   1 
ATOM   111   C  CD1   A ILE A 1 7   ? -12.856 -4.455  23.741  0.50 26.51 ? 7   ILE A CD1   1 
ATOM   112   C  CD1   B ILE A 1 7   ? -12.987 -4.665  23.557  0.50 27.34 ? 7   ILE A CD1   1 
ATOM   113   N  N     A HIS A 1 8   ? -10.298 -9.798  24.444  0.50 22.00 ? 8   HIS A N     1 
ATOM   114   N  N     B HIS A 1 8   ? -10.177 -9.791  24.522  0.50 22.16 ? 8   HIS A N     1 
ATOM   115   C  CA    A HIS A 1 8   ? -9.080  -10.576 24.649  0.50 23.83 ? 8   HIS A CA    1 
ATOM   116   C  CA    B HIS A 1 8   ? -8.917  -10.498 24.731  0.50 23.41 ? 8   HIS A CA    1 
ATOM   117   C  C     A HIS A 1 8   ? -8.263  -10.568 23.363  0.50 20.14 ? 8   HIS A C     1 
ATOM   118   C  C     B HIS A 1 8   ? -8.101  -10.431 23.446  0.50 20.23 ? 8   HIS A C     1 
ATOM   119   O  O     A HIS A 1 8   ? -8.748  -11.007 22.315  0.50 25.91 ? 8   HIS A O     1 
ATOM   120   O  O     B HIS A 1 8   ? -8.546  -10.921 22.403  0.50 25.50 ? 8   HIS A O     1 
ATOM   121   C  CB    A HIS A 1 8   ? -9.420  -12.004 25.078  0.50 21.56 ? 8   HIS A CB    1 
ATOM   122   C  CB    B HIS A 1 8   ? -9.178  -11.947 25.148  0.50 21.72 ? 8   HIS A CB    1 
ATOM   123   C  CG    A HIS A 1 8   ? -10.333 -12.073 26.262  0.50 21.10 ? 8   HIS A CG    1 
ATOM   124   C  CG    B HIS A 1 8   ? -10.162 -12.080 26.269  0.50 20.95 ? 8   HIS A CG    1 
ATOM   125   N  ND1   A HIS A 1 8   ? -9.869  -12.068 27.560  0.50 24.70 ? 8   HIS A ND1   1 
ATOM   126   N  ND1   B HIS A 1 8   ? -9.781  -12.085 27.594  0.50 24.63 ? 8   HIS A ND1   1 
ATOM   127   C  CD2   A HIS A 1 8   ? -11.684 -12.134 26.346  0.50 21.66 ? 8   HIS A CD2   1 
ATOM   128   C  CD2   B HIS A 1 8   ? -11.511 -12.200 26.265  0.50 22.28 ? 8   HIS A CD2   1 
ATOM   129   C  CE1   A HIS A 1 8   ? -10.894 -12.130 28.392  0.50 24.11 ? 8   HIS A CE1   1 
ATOM   130   C  CE1   B HIS A 1 8   ? -10.853 -12.209 28.357  0.50 24.17 ? 8   HIS A CE1   1 
ATOM   131   N  NE2   A HIS A 1 8   ? -12.006 -12.179 27.680  0.50 20.52 ? 8   HIS A NE2   1 
ATOM   132   N  NE2   B HIS A 1 8   ? -11.915 -12.286 27.575  0.50 20.41 ? 8   HIS A NE2   1 
ATOM   133   N  N     A VAL A 1 9   ? -7.023  -10.084 23.448  0.50 21.45 ? 9   VAL A N     1 
ATOM   134   N  N     B VAL A 1 9   ? -6.911  -9.835  23.523  0.50 21.55 ? 9   VAL A N     1 
ATOM   135   C  CA    A VAL A 1 9   ? -6.216  -9.751  22.277  0.50 18.83 ? 9   VAL A CA    1 
ATOM   136   C  CA    B VAL A 1 9   ? -6.130  -9.467  22.342  0.50 18.12 ? 9   VAL A CA    1 
ATOM   137   C  C     A VAL A 1 9   ? -4.940  -10.584 22.285  0.50 20.47 ? 9   VAL A C     1 
ATOM   138   C  C     B VAL A 1 9   ? -4.752  -10.111 22.419  0.50 20.94 ? 9   VAL A C     1 
ATOM   139   O  O     A VAL A 1 9   ? -4.250  -10.660 23.306  0.50 18.87 ? 9   VAL A O     1 
ATOM   140   O  O     B VAL A 1 9   ? -3.978  -9.831  23.342  0.50 14.25 ? 9   VAL A O     1 
ATOM   141   C  CB    A VAL A 1 9   ? -5.874  -8.250  22.241  0.50 20.49 ? 9   VAL A CB    1 
ATOM   142   C  CB    B VAL A 1 9   ? -5.995  -7.944  22.199  0.50 21.59 ? 9   VAL A CB    1 
ATOM   143   C  CG1   A VAL A 1 9   ? -5.009  -7.924  21.021  0.50 20.89 ? 9   VAL A CG1   1 
ATOM   144   C  CG1   B VAL A 1 9   ? -5.156  -7.607  20.965  0.50 21.13 ? 9   VAL A CG1   1 
ATOM   145   C  CG2   A VAL A 1 9   ? -7.141  -7.416  22.236  0.50 23.19 ? 9   VAL A CG2   1 
ATOM   146   C  CG2   B VAL A 1 9   ? -7.360  -7.289  22.113  0.50 23.50 ? 9   VAL A CG2   1 
ATOM   147   N  N     A GLY A 1 10  ? -4.615  -11.184 21.144  0.50 22.21 ? 10  GLY A N     1 
ATOM   148   N  N     B GLY A 1 10  ? -4.424  -10.928 21.422  0.50 22.53 ? 10  GLY A N     1 
ATOM   149   C  CA    A GLY A 1 10  ? -3.384  -11.945 21.013  0.50 21.78 ? 10  GLY A CA    1 
ATOM   150   C  CA    B GLY A 1 10  ? -3.122  -11.556 21.356  0.50 19.92 ? 10  GLY A CA    1 
ATOM   151   C  C     A GLY A 1 10  ? -3.375  -13.201 21.874  0.50 25.34 ? 10  GLY A C     1 
ATOM   152   C  C     B GLY A 1 10  ? -3.053  -12.836 22.170  0.50 24.34 ? 10  GLY A C     1 
ATOM   153   O  O     A GLY A 1 10  ? -4.312  -13.500 22.615  0.50 20.78 ? 10  GLY A O     1 
ATOM   154   O  O     B GLY A 1 10  ? -3.952  -13.179 22.942  0.50 20.11 ? 10  GLY A O     1 
ATOM   155   N  N     A GLN A 1 11  ? -2.267  -13.941 21.776  0.50 21.60 ? 11  GLN A N     1 
ATOM   156   N  N     B GLN A 1 11  ? -1.945  -13.559 21.987  0.50 21.39 ? 11  GLN A N     1 
ATOM   157   C  CA    A GLN A 1 11  ? -2.164  -15.220 22.475  0.50 20.68 ? 11  GLN A CA    1 
ATOM   158   C  CA    B GLN A 1 11  ? -1.785  -14.862 22.628  0.50 22.05 ? 11  GLN A CA    1 
ATOM   159   C  C     A GLN A 1 11  ? -2.365  -15.059 23.979  0.50 22.71 ? 11  GLN A C     1 
ATOM   160   C  C     B GLN A 1 11  ? -1.995  -14.784 24.137  0.50 22.53 ? 11  GLN A C     1 
ATOM   161   O  O     A GLN A 1 11  ? -3.211  -15.732 24.581  0.50 19.69 ? 11  GLN A O     1 
ATOM   162   O  O     B GLN A 1 11  ? -2.754  -15.574 24.713  0.50 21.52 ? 11  GLN A O     1 
ATOM   163   C  CB    A GLN A 1 11  ? -0.814  -15.874 22.189  0.50 23.80 ? 11  GLN A CB    1 
ATOM   164   C  CB    B GLN A 1 11  ? -0.403  -15.436 22.316  0.50 19.83 ? 11  GLN A CB    1 
ATOM   165   C  CG    A GLN A 1 11  ? -0.552  -17.092 23.064  0.50 19.52 ? 11  GLN A CG    1 
ATOM   166   C  CG    B GLN A 1 11  ? 0.002   -16.554 23.263  0.50 21.25 ? 11  GLN A CG    1 
ATOM   167   C  CD    A GLN A 1 11  ? 0.678   -17.878 22.629  0.50 23.88 ? 11  GLN A CD    1 
ATOM   168   C  CD    B GLN A 1 11  ? 1.300   -17.230 22.859  0.50 21.48 ? 11  GLN A CD    1 
ATOM   169   O  OE1   A GLN A 1 11  ? 0.829   -18.220 21.457  0.50 16.51 ? 11  GLN A OE1   1 
ATOM   170   O  OE1   B GLN A 1 11  ? 1.576   -17.401 21.676  0.50 21.97 ? 11  GLN A OE1   1 
ATOM   171   N  NE2   A GLN A 1 11  ? 1.566   -18.156 23.574  0.50 22.21 ? 11  GLN A NE2   1 
ATOM   172   N  NE2   B GLN A 1 11  ? 2.099   -17.616 23.844  0.50 22.06 ? 11  GLN A NE2   1 
ATOM   173   N  N     A ALA A 1 12  ? -1.584  -14.175 24.608  0.50 20.91 ? 12  ALA A N     1 
ATOM   174   N  N     B ALA A 1 12  ? -1.327  -13.834 24.796  0.50 19.59 ? 12  ALA A N     1 
ATOM   175   C  CA    A ALA A 1 12  ? -1.639  -14.052 26.063  0.50 21.02 ? 12  ALA A CA    1 
ATOM   176   C  CA    B ALA A 1 12  ? -1.431  -13.729 26.249  0.50 21.67 ? 12  ALA A CA    1 
ATOM   177   C  C     A ALA A 1 12  ? -3.011  -13.577 26.535  0.50 22.59 ? 12  ALA A C     1 
ATOM   178   C  C     B ALA A 1 12  ? -2.866  -13.442 26.686  0.50 22.50 ? 12  ALA A C     1 
ATOM   179   O  O     A ALA A 1 12  ? -3.513  -14.042 27.565  0.50 21.89 ? 12  ALA A O     1 
ATOM   180   O  O     B ALA A 1 12  ? -3.397  -14.110 27.580  0.50 21.96 ? 12  ALA A O     1 
ATOM   181   C  CB    A ALA A 1 12  ? -0.543  -13.109 26.555  0.50 19.47 ? 12  ALA A CB    1 
ATOM   182   C  CB    B ALA A 1 12  ? -0.482  -12.647 26.765  0.50 18.52 ? 12  ALA A CB    1 
ATOM   183   N  N     A GLY A 1 13  ? -3.635  -12.656 25.797  0.50 20.37 ? 13  GLY A N     1 
ATOM   184   N  N     B GLY A 1 13  ? -3.512  -12.456 26.060  0.50 20.60 ? 13  GLY A N     1 
ATOM   185   C  CA    A GLY A 1 13  ? -4.964  -12.202 26.171  0.50 23.57 ? 13  GLY A CA    1 
ATOM   186   C  CA    B GLY A 1 13  ? -4.868  -12.105 26.457  0.50 23.49 ? 13  GLY A CA    1 
ATOM   187   C  C     A GLY A 1 13  ? -6.024  -13.267 25.985  0.50 22.22 ? 13  GLY A C     1 
ATOM   188   C  C     B GLY A 1 13  ? -5.866  -13.216 26.193  0.50 22.79 ? 13  GLY A C     1 
ATOM   189   O  O     A GLY A 1 13  ? -6.992  -13.326 26.751  0.50 20.65 ? 13  GLY A O     1 
ATOM   190   O  O     B GLY A 1 13  ? -6.800  -13.423 26.973  0.50 19.93 ? 13  GLY A O     1 
ATOM   191   N  N     A VAL A 1 14  ? -5.851  -14.128 24.983  0.50 19.11 ? 14  VAL A N     1 
ATOM   192   N  N     B VAL A 1 14  ? -5.676  -13.952 25.097  0.50 19.18 ? 14  VAL A N     1 
ATOM   193   C  CA    A VAL A 1 14  ? -6.796  -15.209 24.730  0.50 22.85 ? 14  VAL A CA    1 
ATOM   194   C  CA    B VAL A 1 14  ? -6.585  -15.042 24.755  0.50 22.99 ? 14  VAL A CA    1 
ATOM   195   C  C     A VAL A 1 14  ? -6.616  -16.339 25.735  0.50 20.19 ? 14  VAL A C     1 
ATOM   196   C  C     B VAL A 1 14  ? -6.453  -16.186 25.753  0.50 19.96 ? 14  VAL A C     1 
ATOM   197   O  O     A VAL A 1 14  ? -7.598  -16.890 26.248  0.50 21.86 ? 14  VAL A O     1 
ATOM   198   O  O     B VAL A 1 14  ? -7.454  -16.706 26.263  0.50 22.47 ? 14  VAL A O     1 
ATOM   199   C  CB    A VAL A 1 14  ? -6.640  -15.709 23.281  0.50 21.00 ? 14  VAL A CB    1 
ATOM   200   C  CB    B VAL A 1 14  ? -6.328  -15.523 23.315  0.50 20.69 ? 14  VAL A CB    1 
ATOM   201   C  CG1   A VAL A 1 14  ? -7.285  -17.072 23.109  0.50 20.13 ? 14  VAL A CG1   1 
ATOM   202   C  CG1   B VAL A 1 14  ? -6.965  -16.884 23.092  0.50 18.77 ? 14  VAL A CG1   1 
ATOM   203   C  CG2   A VAL A 1 14  ? -7.233  -14.699 22.303  0.50 22.99 ? 14  VAL A CG2   1 
ATOM   204   C  CG2   B VAL A 1 14  ? -6.861  -14.506 22.309  0.50 22.06 ? 14  VAL A CG2   1 
ATOM   205   N  N     A GLN A 1 15  ? -5.366  -16.714 26.028  0.50 19.55 ? 15  GLN A N     1 
ATOM   206   N  N     B GLN A 1 15  ? -5.217  -16.604 26.040  0.50 19.44 ? 15  GLN A N     1 
ATOM   207   C  CA    A GLN A 1 15  ? -5.142  -17.833 26.939  0.50 24.13 ? 15  GLN A CA    1 
ATOM   208   C  CA    B GLN A 1 15  ? -5.014  -17.726 26.953  0.50 23.94 ? 15  GLN A CA    1 
ATOM   209   C  C     A GLN A 1 15  ? -5.526  -17.483 28.374  0.50 22.57 ? 15  GLN A C     1 
ATOM   210   C  C     B GLN A 1 15  ? -5.427  -17.362 28.376  0.50 22.47 ? 15  GLN A C     1 
ATOM   211   O  O     A GLN A 1 15  ? -5.969  -18.360 29.124  0.50 23.67 ? 15  GLN A O     1 
ATOM   212   O  O     B GLN A 1 15  ? -6.104  -18.143 29.055  0.50 23.42 ? 15  GLN A O     1 
ATOM   213   C  CB    A GLN A 1 15  ? -3.688  -18.301 26.854  0.50 20.47 ? 15  GLN A CB    1 
ATOM   214   C  CB    B GLN A 1 15  ? -3.557  -18.190 26.904  0.50 20.42 ? 15  GLN A CB    1 
ATOM   215   C  CG    A GLN A 1 15  ? -3.346  -18.914 25.492  0.50 21.73 ? 15  GLN A CG    1 
ATOM   216   C  CG    B GLN A 1 15  ? -3.114  -18.651 25.513  0.50 21.45 ? 15  GLN A CG    1 
ATOM   217   C  CD    A GLN A 1 15  ? -2.093  -19.781 25.498  0.50 32.75 ? 15  GLN A CD    1 
ATOM   218   C  CD    B GLN A 1 15  ? -1.877  -19.540 25.530  0.50 32.78 ? 15  GLN A CD    1 
ATOM   219   O  OE1   A GLN A 1 15  ? -2.048  -20.826 24.842  0.50 36.21 ? 15  GLN A OE1   1 
ATOM   220   O  OE1   B GLN A 1 15  ? -1.932  -20.702 25.122  0.50 36.60 ? 15  GLN A OE1   1 
ATOM   221   N  NE2   A GLN A 1 15  ? -1.067  -19.345 26.222  0.50 28.73 ? 15  GLN A NE2   1 
ATOM   222   N  NE2   B GLN A 1 15  ? -0.754  -18.995 25.990  0.50 26.16 ? 15  GLN A NE2   1 
ATOM   223   N  N     A ILE A 1 16  ? -5.373  -16.223 28.778  0.50 20.61 ? 16  ILE A N     1 
ATOM   224   N  N     B ILE A 1 16  ? -5.022  -16.183 28.848  0.50 19.83 ? 16  ILE A N     1 
ATOM   225   C  CA    A ILE A 1 16  ? -5.882  -15.820 30.087  0.50 21.01 ? 16  ILE A CA    1 
ATOM   226   C  CA    B ILE A 1 16  ? -5.452  -15.731 30.169  0.50 22.12 ? 16  ILE A CA    1 
ATOM   227   C  C     A ILE A 1 16  ? -7.402  -15.739 30.063  0.50 24.74 ? 16  ILE A C     1 
ATOM   228   C  C     B ILE A 1 16  ? -6.966  -15.570 30.207  0.50 22.94 ? 16  ILE A C     1 
ATOM   229   O  O     A ILE A 1 16  ? -8.074  -16.179 31.004  0.50 21.71 ? 16  ILE A O     1 
ATOM   230   O  O     B ILE A 1 16  ? -7.617  -15.922 31.199  0.50 22.72 ? 16  ILE A O     1 
ATOM   231   C  CB    A ILE A 1 16  ? -5.244  -14.493 30.529  0.50 22.37 ? 16  ILE A CB    1 
ATOM   232   C  CB    B ILE A 1 16  ? -4.724  -14.430 30.548  0.50 21.22 ? 16  ILE A CB    1 
ATOM   233   C  CG1   A ILE A 1 16  ? -3.802  -14.736 30.963  0.50 23.09 ? 16  ILE A CG1   1 
ATOM   234   C  CG1   B ILE A 1 16  ? -3.242  -14.723 30.777  0.50 26.67 ? 16  ILE A CG1   1 
ATOM   235   C  CG2   A ILE A 1 16  ? -6.039  -13.862 31.667  0.50 18.02 ? 16  ILE A CG2   1 
ATOM   236   C  CG2   B ILE A 1 16  ? -5.358  -13.790 31.783  0.50 22.17 ? 16  ILE A CG2   1 
ATOM   237   C  CD1   A ILE A 1 16  ? -3.036  -13.472 31.237  0.50 23.97 ? 16  ILE A CD1   1 
ATOM   238   C  CD1   B ILE A 1 16  ? -2.359  -13.513 30.652  0.50 18.48 ? 16  ILE A CD1   1 
ATOM   239   N  N     A GLY A 1 17  ? -7.967  -15.191 28.983  0.50 21.93 ? 17  GLY A N     1 
ATOM   240   N  N     B GLY A 1 17  ? -7.551  -15.053 29.122  0.50 21.48 ? 17  GLY A N     1 
ATOM   241   C  CA    A GLY A 1 17  ? -9.414  -15.099 28.876  0.50 22.49 ? 17  GLY A CA    1 
ATOM   242   C  CA    B GLY A 1 17  ? -9.000  -14.957 29.048  0.50 22.77 ? 17  GLY A CA    1 
ATOM   243   C  C     A GLY A 1 17  ? -10.102 -16.450 28.932  0.50 28.68 ? 17  GLY A C     1 
ATOM   244   C  C     B GLY A 1 17  ? -9.686  -16.308 29.130  0.50 27.18 ? 17  GLY A C     1 
ATOM   245   O  O     A GLY A 1 17  ? -11.157 -16.593 29.559  0.50 25.15 ? 17  GLY A O     1 
ATOM   246   O  O     B GLY A 1 17  ? -10.720 -16.449 29.792  0.50 27.36 ? 17  GLY A O     1 
ATOM   247   N  N     A ASN A 1 18  ? -9.516  -17.463 28.286  0.50 22.29 ? 18  ASN A N     1 
ATOM   248   N  N     B ASN A 1 18  ? -9.123  -17.321 28.460  0.50 23.31 ? 18  ASN A N     1 
ATOM   249   C  CA    A ASN A 1 18  ? -10.090 -18.802 28.356  0.50 25.09 ? 18  ASN A CA    1 
ATOM   250   C  CA    B ASN A 1 18  ? -9.688  -18.666 28.545  0.50 23.70 ? 18  ASN A CA    1 
ATOM   251   C  C     A ASN A 1 18  ? -10.142 -19.293 29.801  0.50 28.06 ? 18  ASN A C     1 
ATOM   252   C  C     B ASN A 1 18  ? -9.621  -19.211 29.968  0.50 24.19 ? 18  ASN A C     1 
ATOM   253   O  O     A ASN A 1 18  ? -11.185 -19.761 30.277  0.50 21.15 ? 18  ASN A O     1 
ATOM   254   O  O     B ASN A 1 18  ? -10.502 -19.972 30.388  0.50 26.25 ? 18  ASN A O     1 
ATOM   255   C  CB    A ASN A 1 18  ? -9.289  -19.762 27.476  0.50 30.86 ? 18  ASN A CB    1 
ATOM   256   C  CB    B ASN A 1 18  ? -8.969  -19.599 27.570  0.50 29.77 ? 18  ASN A CB    1 
ATOM   257   C  CG    A ASN A 1 18  ? -10.151 -20.858 26.873  0.50 37.23 ? 18  ASN A CG    1 
ATOM   258   C  CG    B ASN A 1 18  ? -9.403  -21.047 27.713  0.50 35.78 ? 18  ASN A CG    1 
ATOM   259   O  OD1   A ASN A 1 18  ? -11.380 -20.767 26.864  0.50 34.85 ? 18  ASN A OD1   1 
ATOM   260   O  OD1   B ASN A 1 18  ? -8.577  -21.934 27.938  0.50 28.13 ? 18  ASN A OD1   1 
ATOM   261   N  ND2   A ASN A 1 18  ? -9.508  -21.900 26.362  0.50 33.74 ? 18  ASN A ND2   1 
ATOM   262   N  ND2   B ASN A 1 18  ? -10.702 -21.293 27.593  0.50 33.87 ? 18  ASN A ND2   1 
ATOM   263   N  N     A ALA A 1 19  ? -9.034  -19.152 30.529  0.50 25.18 ? 19  ALA A N     1 
ATOM   264   N  N     B ALA A 1 19  ? -8.597  -18.826 30.730  0.50 26.09 ? 19  ALA A N     1 
ATOM   265   C  CA    A ALA A 1 19  ? -8.995  -19.611 31.913  0.50 24.60 ? 19  ALA A CA    1 
ATOM   266   C  CA    B ALA A 1 19  ? -8.531  -19.243 32.124  0.50 24.42 ? 19  ALA A CA    1 
ATOM   267   C  C     A ALA A 1 19  ? -9.897  -18.770 32.809  0.50 23.86 ? 19  ALA A C     1 
ATOM   268   C  C     B ALA A 1 19  ? -9.536  -18.485 32.985  0.50 25.06 ? 19  ALA A C     1 
ATOM   269   O  O     A ALA A 1 19  ? -10.496 -19.292 33.756  0.50 24.33 ? 19  ALA A O     1 
ATOM   270   O  O     B ALA A 1 19  ? -10.080 -19.050 33.941  0.50 23.27 ? 19  ALA A O     1 
ATOM   271   C  CB    A ALA A 1 19  ? -7.560  -19.589 32.433  0.50 23.32 ? 19  ALA A CB    1 
ATOM   272   C  CB    B ALA A 1 19  ? -7.115  -19.047 32.660  0.50 23.95 ? 19  ALA A CB    1 
ATOM   273   N  N     A CYS A 1 20  ? -9.996  -17.466 32.537  0.50 23.84 ? 20  CYS A N     1 
ATOM   274   N  N     B CYS A 1 20  ? -9.796  -17.214 32.664  0.50 22.87 ? 20  CYS A N     1 
ATOM   275   C  CA    A CYS A 1 20  ? -10.840 -16.603 33.360  0.50 26.11 ? 20  CYS A CA    1 
ATOM   276   C  CA    B CYS A 1 20  ? -10.722 -16.413 33.459  0.50 25.87 ? 20  CYS A CA    1 
ATOM   277   C  C     A CYS A 1 20  ? -12.316 -16.942 33.194  0.50 27.27 ? 20  CYS A C     1 
ATOM   278   C  C     B CYS A 1 20  ? -12.158 -16.907 33.313  0.50 26.86 ? 20  CYS A C     1 
ATOM   279   O  O     A CYS A 1 20  ? -13.066 -16.982 34.180  0.50 24.41 ? 20  CYS A O     1 
ATOM   280   O  O     B CYS A 1 20  ? -12.866 -17.095 34.312  0.50 25.30 ? 20  CYS A O     1 
ATOM   281   C  CB    A CYS A 1 20  ? -10.584 -15.137 33.016  0.50 25.01 ? 20  CYS A CB    1 
ATOM   282   C  CB    B CYS A 1 20  ? -10.622 -14.943 33.054  0.50 25.43 ? 20  CYS A CB    1 
ATOM   283   S  SG    A CYS A 1 20  ? -9.045  -14.455 33.698  0.50 28.66 ? 20  CYS A SG    1 
ATOM   284   S  SG    B CYS A 1 20  ? -9.145  -14.076 33.658  0.50 25.61 ? 20  CYS A SG    1 
ATOM   285   N  N     A TRP A 1 21  ? -12.759 -17.176 31.954  0.50 24.27 ? 21  TRP A N     1 
ATOM   286   N  N     B TRP A 1 21  ? -12.617 -17.102 32.073  0.50 24.46 ? 21  TRP A N     1 
ATOM   287   C  CA    A TRP A 1 21  ? -14.162 -17.516 31.742  0.50 26.78 ? 21  TRP A CA    1 
ATOM   288   C  CA    B TRP A 1 21  ? -14.023 -17.438 31.872  0.50 26.63 ? 21  TRP A CA    1 
ATOM   289   C  C     A TRP A 1 21  ? -14.494 -18.894 32.291  0.50 24.20 ? 21  TRP A C     1 
ATOM   290   C  C     B TRP A 1 21  ? -14.341 -18.853 32.330  0.50 24.17 ? 21  TRP A C     1 
ATOM   291   O  O     A TRP A 1 21  ? -15.623 -19.120 32.742  0.50 28.38 ? 21  TRP A O     1 
ATOM   292   O  O     B TRP A 1 21  ? -15.481 -19.130 32.718  0.50 28.38 ? 21  TRP A O     1 
ATOM   293   C  CB    A TRP A 1 21  ? -14.514 -17.422 30.258  0.50 23.90 ? 21  TRP A CB    1 
ATOM   294   C  CB    B TRP A 1 21  ? -14.410 -17.233 30.408  0.50 24.38 ? 21  TRP A CB    1 
ATOM   295   C  CG    A TRP A 1 21  ? -14.619 -16.011 29.799  0.50 26.41 ? 21  TRP A CG    1 
ATOM   296   C  CG    B TRP A 1 21  ? -14.490 -15.787 30.064  0.50 26.51 ? 21  TRP A CG    1 
ATOM   297   C  CD1   A TRP A 1 21  ? -13.741 -15.334 28.996  0.50 20.06 ? 21  TRP A CD1   1 
ATOM   298   C  CD1   B TRP A 1 21  ? -13.501 -15.012 29.520  0.50 22.85 ? 21  TRP A CD1   1 
ATOM   299   C  CD2   A TRP A 1 21  ? -15.651 -15.079 30.141  0.50 23.67 ? 21  TRP A CD2   1 
ATOM   300   C  CD2   B TRP A 1 21  ? -15.611 -14.921 30.269  0.50 23.48 ? 21  TRP A CD2   1 
ATOM   301   N  NE1   A TRP A 1 21  ? -14.171 -14.043 28.811  0.50 23.59 ? 21  TRP A NE1   1 
ATOM   302   N  NE1   B TRP A 1 21  ? -13.944 -13.721 29.369  0.50 20.89 ? 21  TRP A NE1   1 
ATOM   303   C  CE2   A TRP A 1 21  ? -15.343 -13.863 29.503  0.50 24.04 ? 21  TRP A CE2   1 
ATOM   304   C  CE2   B TRP A 1 21  ? -15.237 -13.639 29.819  0.50 23.55 ? 21  TRP A CE2   1 
ATOM   305   C  CE3   A TRP A 1 21  ? -16.812 -15.159 30.920  0.50 27.85 ? 21  TRP A CE3   1 
ATOM   306   C  CE3   B TRP A 1 21  ? -16.900 -15.105 30.785  0.50 27.89 ? 21  TRP A CE3   1 
ATOM   307   C  CZ2   A TRP A 1 21  ? -16.150 -12.734 29.621  0.50 24.03 ? 21  TRP A CZ2   1 
ATOM   308   C  CZ2   B TRP A 1 21  ? -16.102 -12.550 29.867  0.50 24.05 ? 21  TRP A CZ2   1 
ATOM   309   C  CZ3   A TRP A 1 21  ? -17.614 -14.034 31.036  0.50 22.52 ? 21  TRP A CZ3   1 
ATOM   310   C  CZ3   B TRP A 1 21  ? -17.760 -14.018 30.831  0.50 21.98 ? 21  TRP A CZ3   1 
ATOM   311   C  CH2   A TRP A 1 21  ? -17.279 -12.840 30.390  0.50 24.25 ? 21  TRP A CH2   1 
ATOM   312   C  CH2   B TRP A 1 21  ? -17.357 -12.760 30.376  0.50 24.25 ? 21  TRP A CH2   1 
ATOM   313   N  N     A GLU A 1 22  ? -13.535 -19.824 32.263  0.50 23.00 ? 22  GLU A N     1 
ATOM   314   N  N     B GLU A 1 22  ? -13.359 -19.758 32.299  0.50 22.85 ? 22  GLU A N     1 
ATOM   315   C  CA    A GLU A 1 22  ? -13.729 -21.106 32.931  0.50 31.39 ? 22  GLU A CA    1 
ATOM   316   C  CA    B GLU A 1 22  ? -13.558 -21.066 32.912  0.50 31.40 ? 22  GLU A CA    1 
ATOM   317   C  C     A GLU A 1 22  ? -14.030 -20.903 34.411  0.50 29.63 ? 22  GLU A C     1 
ATOM   318   C  C     B GLU A 1 22  ? -13.805 -20.929 34.410  0.50 29.72 ? 22  GLU A C     1 
ATOM   319   O  O     A GLU A 1 22  ? -15.036 -21.401 34.930  0.50 26.06 ? 22  GLU A O     1 
ATOM   320   O  O     B GLU A 1 22  ? -14.691 -21.588 34.968  0.50 27.01 ? 22  GLU A O     1 
ATOM   321   C  CB    A GLU A 1 22  ? -12.490 -21.983 32.748  0.50 29.61 ? 22  GLU A CB    1 
ATOM   322   C  CB    B GLU A 1 22  ? -12.347 -21.961 32.642  0.50 29.40 ? 22  GLU A CB    1 
ATOM   323   C  CG    A GLU A 1 22  ? -12.477 -23.224 33.621  0.50 35.61 ? 22  GLU A CG    1 
ATOM   324   C  CG    B GLU A 1 22  ? -12.439 -23.334 33.283  0.50 35.99 ? 22  GLU A CG    1 
ATOM   325   C  CD    A GLU A 1 22  ? -11.150 -23.957 33.572  0.50 37.61 ? 22  GLU A CD    1 
ATOM   326   C  CD    B GLU A 1 22  ? -11.300 -24.246 32.875  0.50 36.32 ? 22  GLU A CD    1 
ATOM   327   O  OE1   A GLU A 1 22  ? -10.133 -23.322 33.223  0.50 39.77 ? 22  GLU A OE1   1 
ATOM   328   O  OE1   B GLU A 1 22  ? -10.163 -23.752 32.730  0.50 42.09 ? 22  GLU A OE1   1 
ATOM   329   O  OE2   A GLU A 1 22  ? -11.124 -25.166 33.880  0.50 44.79 ? 22  GLU A OE2   1 
ATOM   330   O  OE2   B GLU A 1 22  ? -11.544 -25.457 32.691  0.50 41.57 ? 22  GLU A OE2   1 
ATOM   331   N  N     A LEU A 1 23  ? -13.171 -20.150 35.101  0.50 27.04 ? 23  LEU A N     1 
ATOM   332   N  N     B LEU A 1 23  ? -13.045 -20.055 35.073  0.50 26.99 ? 23  LEU A N     1 
ATOM   333   C  CA    A LEU A 1 23  ? -13.384 -19.879 36.518  0.50 24.58 ? 23  LEU A CA    1 
ATOM   334   C  CA    B LEU A 1 23  ? -13.225 -19.854 36.507  0.50 24.61 ? 23  LEU A CA    1 
ATOM   335   C  C     A LEU A 1 23  ? -14.701 -19.148 36.752  0.50 28.52 ? 23  LEU A C     1 
ATOM   336   C  C     B LEU A 1 23  ? -14.528 -19.122 36.806  0.50 28.47 ? 23  LEU A C     1 
ATOM   337   O  O     A LEU A 1 23  ? -15.421 -19.447 37.711  0.50 25.99 ? 23  LEU A O     1 
ATOM   338   O  O     B LEU A 1 23  ? -15.196 -19.421 37.803  0.50 26.17 ? 23  LEU A O     1 
ATOM   339   C  CB    A LEU A 1 23  ? -12.208 -19.074 37.068  0.50 24.25 ? 23  LEU A CB    1 
ATOM   340   C  CB    B LEU A 1 23  ? -12.029 -19.093 37.076  0.50 24.20 ? 23  LEU A CB    1 
ATOM   341   C  CG    A LEU A 1 23  ? -12.254 -18.623 38.527  0.50 22.33 ? 23  LEU A CG    1 
ATOM   342   C  CG    B LEU A 1 23  ? -12.030 -18.769 38.570  0.50 23.01 ? 23  LEU A CG    1 
ATOM   343   C  CD1   A LEU A 1 23  ? -12.430 -19.813 39.464  0.50 26.32 ? 23  LEU A CD1   1 
ATOM   344   C  CD1   B LEU A 1 23  ? -12.287 -20.021 39.398  0.50 26.69 ? 23  LEU A CD1   1 
ATOM   345   C  CD2   A LEU A 1 23  ? -10.990 -17.859 38.868  0.50 25.55 ? 23  LEU A CD2   1 
ATOM   346   C  CD2   B LEU A 1 23  ? -10.704 -18.146 38.957  0.50 26.40 ? 23  LEU A CD2   1 
ATOM   347   N  N     A TYR A 1 24  ? -15.036 -18.192 35.880  0.50 24.99 ? 24  TYR A N     1 
ATOM   348   N  N     B TYR A 1 24  ? -14.903 -18.159 35.958  0.50 25.10 ? 24  TYR A N     1 
ATOM   349   C  CA    A TYR A 1 24  ? -16.309 -17.486 36.002  0.50 26.35 ? 24  TYR A CA    1 
ATOM   350   C  CA    B TYR A 1 24  ? -16.174 -17.460 36.134  0.50 26.17 ? 24  TYR A CA    1 
ATOM   351   C  C     A TYR A 1 24  ? -17.484 -18.452 35.945  0.50 28.03 ? 24  TYR A C     1 
ATOM   352   C  C     B TYR A 1 24  ? -17.337 -18.441 36.153  0.50 28.06 ? 24  TYR A C     1 
ATOM   353   O  O     A TYR A 1 24  ? -18.485 -18.264 36.646  0.50 25.37 ? 24  TYR A O     1 
ATOM   354   O  O     B TYR A 1 24  ? -18.179 -18.408 37.058  0.50 28.11 ? 24  TYR A O     1 
ATOM   355   C  CB    A TYR A 1 24  ? -16.458 -16.444 34.893  0.50 25.95 ? 24  TYR A CB    1 
ATOM   356   C  CB    B TYR A 1 24  ? -16.388 -16.441 35.015  0.50 25.94 ? 24  TYR A CB    1 
ATOM   357   C  CG    A TYR A 1 24  ? -15.568 -15.231 34.995  0.50 25.34 ? 24  TYR A CG    1 
ATOM   358   C  CG    B TYR A 1 24  ? -15.463 -15.252 35.009  0.50 25.35 ? 24  TYR A CG    1 
ATOM   359   C  CD1   A TYR A 1 24  ? -14.776 -14.998 36.114  0.50 27.32 ? 24  TYR A CD1   1 
ATOM   360   C  CD1   B TYR A 1 24  ? -14.719 -14.904 36.130  0.50 27.35 ? 24  TYR A CD1   1 
ATOM   361   C  CD2   A TYR A 1 24  ? -15.536 -14.301 33.967  0.50 23.21 ? 24  TYR A CD2   1 
ATOM   362   C  CD2   B TYR A 1 24  ? -15.352 -14.461 33.876  0.50 23.56 ? 24  TYR A CD2   1 
ATOM   363   C  CE1   A TYR A 1 24  ? -13.963 -13.872 36.191  0.50 26.91 ? 24  TYR A CE1   1 
ATOM   364   C  CE1   B TYR A 1 24  ? -13.874 -13.801 36.109  0.50 26.78 ? 24  TYR A CE1   1 
ATOM   365   C  CE2   A TYR A 1 24  ? -14.737 -13.183 34.038  0.50 29.51 ? 24  TYR A CE2   1 
ATOM   366   C  CE2   B TYR A 1 24  ? -14.515 -13.366 33.847  0.50 29.96 ? 24  TYR A CE2   1 
ATOM   367   C  CZ    A TYR A 1 24  ? -13.953 -12.970 35.146  0.50 28.48 ? 24  TYR A CZ    1 
ATOM   368   C  CZ    B TYR A 1 24  ? -13.782 -13.038 34.962  0.50 28.33 ? 24  TYR A CZ    1 
ATOM   369   O  OH    A TYR A 1 24  ? -13.162 -11.845 35.194  0.50 27.50 ? 24  TYR A OH    1 
ATOM   370   O  OH    B TYR A 1 24  ? -12.954 -11.940 34.919  0.50 25.92 ? 24  TYR A OH    1 
ATOM   371   N  N     A CYS A 1 25  ? -17.393 -19.479 35.094  0.50 24.75 ? 25  CYS A N     1 
ATOM   372   N  N     B CYS A 1 25  ? -17.403 -19.319 35.146  0.50 25.03 ? 25  CYS A N     1 
ATOM   373   C  CA    A CYS A 1 25  ? -18.462 -20.467 35.019  0.50 28.12 ? 25  CYS A CA    1 
ATOM   374   C  CA    B CYS A 1 25  ? -18.528 -20.241 35.043  0.50 28.13 ? 25  CYS A CA    1 
ATOM   375   C  C     A CYS A 1 25  ? -18.627 -21.190 36.348  0.50 28.53 ? 25  CYS A C     1 
ATOM   376   C  C     B CYS A 1 25  ? -18.593 -21.170 36.248  0.50 28.51 ? 25  CYS A C     1 
ATOM   377   O  O     A CYS A 1 25  ? -19.745 -21.314 36.866  0.50 30.48 ? 25  CYS A O     1 
ATOM   378   O  O     B CYS A 1 25  ? -19.686 -21.478 36.741  0.50 31.26 ? 25  CYS A O     1 
ATOM   379   C  CB    A CYS A 1 25  ? -18.184 -21.463 33.891  0.50 26.68 ? 25  CYS A CB    1 
ATOM   380   C  CB    B CYS A 1 25  ? -18.438 -21.037 33.740  0.50 27.54 ? 25  CYS A CB    1 
ATOM   381   S  SG    A CYS A 1 25  ? -18.474 -20.800 32.238  0.50 28.82 ? 25  CYS A SG    1 
ATOM   382   S  SG    B CYS A 1 25  ? -18.707 -20.025 32.251  0.50 23.20 ? 25  CYS A SG    1 
ATOM   383   N  N     A LEU A 1 26  ? -17.516 -21.655 36.924  0.50 25.99 ? 26  LEU A N     1 
ATOM   384   N  N     B LEU A 1 26  ? -17.434 -21.611 36.747  0.50 25.74 ? 26  LEU A N     1 
ATOM   385   C  CA    A LEU A 1 26  ? -17.575 -22.398 38.180  0.50 26.89 ? 26  LEU A CA    1 
ATOM   386   C  CA    B LEU A 1 26  ? -17.417 -22.442 37.947  0.50 27.01 ? 26  LEU A CA    1 
ATOM   387   C  C     A LEU A 1 26  ? -18.128 -21.539 39.309  0.50 32.29 ? 26  LEU A C     1 
ATOM   388   C  C     B LEU A 1 26  ? -17.946 -21.691 39.159  0.50 31.13 ? 26  LEU A C     1 
ATOM   389   O  O     A LEU A 1 26  ? -19.017 -21.971 40.056  0.50 27.14 ? 26  LEU A O     1 
ATOM   390   O  O     B LEU A 1 26  ? -18.574 -22.296 40.037  0.50 29.82 ? 26  LEU A O     1 
ATOM   391   C  CB    A LEU A 1 26  ? -16.189 -22.924 38.543  0.50 26.66 ? 26  LEU A CB    1 
ATOM   392   C  CB    B LEU A 1 26  ? -16.003 -22.948 38.227  0.50 27.21 ? 26  LEU A CB    1 
ATOM   393   C  CG    A LEU A 1 26  ? -15.571 -23.935 37.579  0.50 27.39 ? 26  LEU A CG    1 
ATOM   394   C  CG    B LEU A 1 26  ? -15.429 -24.011 37.295  0.50 28.55 ? 26  LEU A CG    1 
ATOM   395   C  CD1   A LEU A 1 26  ? -14.198 -24.352 38.064  0.50 34.23 ? 26  LEU A CD1   1 
ATOM   396   C  CD1   B LEU A 1 26  ? -14.005 -24.327 37.703  0.50 35.16 ? 26  LEU A CD1   1 
ATOM   397   C  CD2   A LEU A 1 26  ? -16.476 -25.145 37.415  0.50 34.91 ? 26  LEU A CD2   1 
ATOM   398   C  CD2   B LEU A 1 26  ? -16.286 -25.267 37.301  0.50 34.72 ? 26  LEU A CD2   1 
ATOM   399   N  N     A GLU A 1 27  ? -17.611 -20.315 39.452  0.50 22.23 ? 27  GLU A N     1 
ATOM   400   N  N     B GLU A 1 27  ? -17.700 -20.379 39.230  0.50 21.78 ? 27  GLU A N     1 
ATOM   401   C  CA    A GLU A 1 27  ? -18.027 -19.468 40.567  0.50 28.91 ? 27  GLU A CA    1 
ATOM   402   C  CA    B GLU A 1 27  ? -18.215 -19.596 40.350  0.50 28.26 ? 27  GLU A CA    1 
ATOM   403   C  C     A GLU A 1 27  ? -19.503 -19.100 40.488  0.50 26.73 ? 27  GLU A C     1 
ATOM   404   C  C     B GLU A 1 27  ? -19.724 -19.419 40.259  0.50 25.98 ? 27  GLU A C     1 
ATOM   405   O  O     A GLU A 1 27  ? -20.148 -18.897 41.526  0.50 23.69 ? 27  GLU A O     1 
ATOM   406   O  O     B GLU A 1 27  ? -20.420 -19.441 41.283  0.50 27.91 ? 27  GLU A O     1 
ATOM   407   C  CB    A GLU A 1 27  ? -17.180 -18.198 40.614  0.50 27.32 ? 27  GLU A CB    1 
ATOM   408   C  CB    B GLU A 1 27  ? -17.528 -18.231 40.408  0.50 27.02 ? 27  GLU A CB    1 
ATOM   409   C  CG    A GLU A 1 27  ? -15.688 -18.442 40.755  0.50 28.12 ? 27  GLU A CG    1 
ATOM   410   C  CG    B GLU A 1 27  ? -16.075 -18.268 40.858  0.50 29.08 ? 27  GLU A CG    1 
ATOM   411   C  CD    A GLU A 1 27  ? -14.900 -17.149 40.827  0.50 29.99 ? 27  GLU A CD    1 
ATOM   412   C  CD    B GLU A 1 27  ? -15.448 -16.885 40.900  0.50 29.19 ? 27  GLU A CD    1 
ATOM   413   O  OE1   A GLU A 1 27  ? -15.517 -16.074 40.667  0.50 28.56 ? 27  GLU A OE1   1 
ATOM   414   O  OE1   B GLU A 1 27  ? -16.060 -15.945 40.351  0.50 28.44 ? 27  GLU A OE1   1 
ATOM   415   O  OE2   A GLU A 1 27  ? -13.669 -17.206 41.046  0.50 26.57 ? 27  GLU A OE2   1 
ATOM   416   O  OE2   B GLU A 1 27  ? -14.349 -16.738 41.481  0.50 26.91 ? 27  GLU A OE2   1 
ATOM   417   N  N     A HIS A 1 28  ? -20.055 -18.994 39.280  0.50 25.84 ? 28  HIS A N     1 
ATOM   418   N  N     B HIS A 1 28  ? -20.249 -19.233 39.050  0.50 26.05 ? 28  HIS A N     1 
ATOM   419   C  CA    A HIS A 1 28  ? -21.444 -18.593 39.107  0.50 27.78 ? 28  HIS A CA    1 
ATOM   420   C  CA    B HIS A 1 28  ? -21.667 -18.958 38.856  0.50 28.49 ? 28  HIS A CA    1 
ATOM   421   C  C     A HIS A 1 28  ? -22.401 -19.767 38.972  0.50 32.03 ? 28  HIS A C     1 
ATOM   422   C  C     B HIS A 1 28  ? -22.490 -20.209 38.580  0.50 32.12 ? 28  HIS A C     1 
ATOM   423   O  O     A HIS A 1 28  ? -23.618 -19.552 38.970  0.50 29.13 ? 28  HIS A O     1 
ATOM   424   O  O     B HIS A 1 28  ? -23.719 -20.115 38.496  0.50 34.73 ? 28  HIS A O     1 
ATOM   425   C  CB    A HIS A 1 28  ? -21.588 -17.684 37.882  0.50 28.42 ? 28  HIS A CB    1 
ATOM   426   C  CB    B HIS A 1 28  ? -21.858 -17.953 37.715  0.50 27.77 ? 28  HIS A CB    1 
ATOM   427   C  CG    A HIS A 1 28  ? -21.087 -16.293 38.106  0.50 28.59 ? 28  HIS A CG    1 
ATOM   428   C  CG    B HIS A 1 28  ? -21.249 -16.613 37.983  0.50 28.38 ? 28  HIS A CG    1 
ATOM   429   N  ND1   A HIS A 1 28  ? -21.638 -15.451 39.047  0.50 29.58 ? 28  HIS A ND1   1 
ATOM   430   N  ND1   B HIS A 1 28  ? -21.727 -15.761 38.956  0.50 28.94 ? 28  HIS A ND1   1 
ATOM   431   C  CD2   A HIS A 1 28  ? -20.084 -15.599 37.520  0.50 28.13 ? 28  HIS A CD2   1 
ATOM   432   C  CD2   B HIS A 1 28  ? -20.199 -15.980 37.410  0.50 26.80 ? 28  HIS A CD2   1 
ATOM   433   C  CE1   A HIS A 1 28  ? -21.000 -14.294 39.026  0.50 28.17 ? 28  HIS A CE1   1 
ATOM   434   C  CE1   B HIS A 1 28  ? -20.999 -14.658 38.965  0.50 28.48 ? 28  HIS A CE1   1 
ATOM   435   N  NE2   A HIS A 1 28  ? -20.050 -14.360 38.112  0.50 27.47 ? 28  HIS A NE2   1 
ATOM   436   N  NE2   B HIS A 1 28  ? -20.062 -14.767 38.041  0.50 28.30 ? 28  HIS A NE2   1 
ATOM   437   N  N     A GLY A 1 29  ? -21.893 -20.993 38.868  0.50 31.67 ? 29  GLY A N     1 
ATOM   438   N  N     B GLY A 1 29  ? -21.856 -21.372 38.445  0.50 27.96 ? 29  GLY A N     1 
ATOM   439   C  CA    A GLY A 1 29  ? -22.761 -22.133 38.654  0.50 32.68 ? 29  GLY A CA    1 
ATOM   440   C  CA    B GLY A 1 29  ? -22.591 -22.596 38.193  0.50 31.14 ? 29  GLY A CA    1 
ATOM   441   C  C     A GLY A 1 29  ? -23.254 -22.265 37.234  0.50 35.92 ? 29  GLY A C     1 
ATOM   442   C  C     B GLY A 1 29  ? -23.027 -22.789 36.762  0.50 34.95 ? 29  GLY A C     1 
ATOM   443   O  O     A GLY A 1 29  ? -24.378 -22.728 37.014  0.50 27.53 ? 29  GLY A O     1 
ATOM   444   O  O     B GLY A 1 29  ? -23.974 -23.543 36.509  0.50 30.38 ? 29  GLY A O     1 
ATOM   445   N  N     A ILE A 1 30  ? -22.446 -21.856 36.259  0.50 27.46 ? 30  ILE A N     1 
ATOM   446   N  N     B ILE A 1 30  ? -22.375 -22.123 35.819  0.50 28.60 ? 30  ILE A N     1 
ATOM   447   C  CA    A ILE A 1 30  ? -22.791 -21.936 34.846  0.50 32.08 ? 30  ILE A CA    1 
ATOM   448   C  CA    B ILE A 1 30  ? -22.711 -22.229 34.404  0.50 31.45 ? 30  ILE A CA    1 
ATOM   449   C  C     A ILE A 1 30  ? -22.071 -23.133 34.246  0.50 34.36 ? 30  ILE A C     1 
ATOM   450   C  C     B ILE A 1 30  ? -21.939 -23.395 33.804  0.50 36.22 ? 30  ILE A C     1 
ATOM   451   O  O     A ILE A 1 30  ? -20.852 -23.279 34.409  0.50 32.03 ? 30  ILE A O     1 
ATOM   452   O  O     B ILE A 1 30  ? -20.710 -23.465 33.924  0.50 36.38 ? 30  ILE A O     1 
ATOM   453   C  CB    A ILE A 1 30  ? -22.418 -20.640 34.106  0.50 25.85 ? 30  ILE A CB    1 
ATOM   454   C  CB    B ILE A 1 30  ? -22.394 -20.918 33.666  0.50 26.02 ? 30  ILE A CB    1 
ATOM   455   C  CG1   A ILE A 1 30  ? -23.241 -19.468 34.644  0.50 27.83 ? 30  ILE A CG1   1 
ATOM   456   C  CG1   B ILE A 1 30  ? -23.089 -19.742 34.356  0.50 28.09 ? 30  ILE A CG1   1 
ATOM   457   C  CG2   A ILE A 1 30  ? -22.611 -20.807 32.606  0.50 32.45 ? 30  ILE A CG2   1 
ATOM   458   C  CG2   B ILE A 1 30  ? -22.803 -21.017 32.205  0.50 32.67 ? 30  ILE A CG2   1 
ATOM   459   C  CD1   A ILE A 1 30  ? -22.941 -18.151 33.977  0.50 31.84 ? 30  ILE A CD1   1 
ATOM   460   C  CD1   B ILE A 1 30  ? -22.809 -18.407 33.722  0.50 31.17 ? 30  ILE A CD1   1 
ATOM   461   N  N     A GLN A 1 31  ? -22.818 -23.986 33.557  0.50 35.63 ? 31  GLN A N     1 
ATOM   462   N  N     B GLN A 1 31  ? -22.658 -24.308 33.153  0.50 37.70 ? 31  GLN A N     1 
ATOM   463   C  CA    A GLN A 1 31  ? -22.288 -25.199 32.955  0.50 37.52 ? 31  GLN A CA    1 
ATOM   464   C  CA    B GLN A 1 31  ? -22.057 -25.494 32.567  0.50 37.44 ? 31  GLN A CA    1 
ATOM   465   C  C     A GLN A 1 31  ? -21.694 -24.901 31.582  0.50 37.15 ? 31  GLN A C     1 
ATOM   466   C  C     B GLN A 1 31  ? -21.241 -25.120 31.330  0.50 36.07 ? 31  GLN A C     1 
ATOM   467   O  O     A GLN A 1 31  ? -22.041 -23.897 30.950  0.50 36.91 ? 31  GLN A O     1 
ATOM   468   O  O     B GLN A 1 31  ? -21.357 -24.008 30.808  0.50 36.27 ? 31  GLN A O     1 
ATOM   469   C  CB    A GLN A 1 31  ? -23.394 -26.251 32.861  0.50 41.32 ? 31  GLN A CB    1 
ATOM   470   C  CB    B GLN A 1 31  ? -23.143 -26.510 32.214  0.50 42.15 ? 31  GLN A CB    1 
ATOM   471   C  CG    A GLN A 1 31  ? -23.818 -26.791 34.226  0.50 35.63 ? 31  GLN A CG    1 
ATOM   472   C  CG    B GLN A 1 31  ? -23.876 -27.097 33.409  0.50 40.75 ? 31  GLN A CG    1 
ATOM   473   C  CD    A GLN A 1 31  ? -24.923 -27.828 34.142  0.50 44.73 ? 31  GLN A CD    1 
ATOM   474   C  CD    B GLN A 1 31  ? -24.847 -28.192 33.006  0.50 42.96 ? 31  GLN A CD    1 
ATOM   475   O  OE1   A GLN A 1 31  ? -25.620 -27.934 33.132  0.50 40.28 ? 31  GLN A OE1   1 
ATOM   476   O  OE1   B GLN A 1 31  ? -24.649 -28.873 31.999  0.50 41.51 ? 31  GLN A OE1   1 
ATOM   477   N  NE2   A GLN A 1 31  ? -25.087 -28.601 35.210  0.50 43.83 ? 31  GLN A NE2   1 
ATOM   478   N  NE2   B GLN A 1 31  ? -25.909 -28.359 33.785  0.50 43.73 ? 31  GLN A NE2   1 
ATOM   479   N  N     A PRO A 1 32  ? -20.781 -25.751 31.096  0.50 34.94 ? 32  PRO A N     1 
ATOM   480   N  N     B PRO A 1 32  ? -20.392 -26.031 30.841  0.50 36.69 ? 32  PRO A N     1 
ATOM   481   C  CA    A PRO A 1 32  ? -20.029 -25.407 29.873  0.50 37.25 ? 32  PRO A CA    1 
ATOM   482   C  CA    B PRO A 1 32  ? -19.615 -25.728 29.626  0.50 35.22 ? 32  PRO A CA    1 
ATOM   483   C  C     A PRO A 1 32  ? -20.891 -25.149 28.646  0.50 39.93 ? 32  PRO A C     1 
ATOM   484   C  C     B PRO A 1 32  ? -20.463 -25.482 28.389  0.50 38.49 ? 32  PRO A C     1 
ATOM   485   O  O     A PRO A 1 32  ? -20.412 -24.505 27.704  0.50 37.73 ? 32  PRO A O     1 
ATOM   486   O  O     B PRO A 1 32  ? -19.949 -24.929 27.409  0.50 40.45 ? 32  PRO A O     1 
ATOM   487   C  CB    A PRO A 1 32  ? -19.125 -26.629 29.664  0.50 39.16 ? 32  PRO A CB    1 
ATOM   488   C  CB    B PRO A 1 32  ? -18.732 -26.971 29.456  0.50 40.76 ? 32  PRO A CB    1 
ATOM   489   C  CG    A PRO A 1 32  ? -18.975 -27.221 31.018  0.50 39.79 ? 32  PRO A CG    1 
ATOM   490   C  CG    B PRO A 1 32  ? -18.611 -27.534 30.828  0.50 40.60 ? 32  PRO A CG    1 
ATOM   491   C  CD    A PRO A 1 32  ? -20.286 -26.999 31.706  0.50 34.41 ? 32  PRO A CD    1 
ATOM   492   C  CD    B PRO A 1 32  ? -19.932 -27.275 31.486  0.50 34.04 ? 32  PRO A CD    1 
ATOM   493   N  N     A ASP A 1 33  ? -22.134 -25.623 28.616  0.50 36.13 ? 33  ASP A N     1 
ATOM   494   N  N     B ASP A 1 33  ? -21.737 -25.873 28.389  0.50 39.03 ? 33  ASP A N     1 
ATOM   495   C  CA    A ASP A 1 33  ? -23.003 -25.393 27.471  0.50 35.28 ? 33  ASP A CA    1 
ATOM   496   C  CA    B ASP A 1 33  ? -22.622 -25.600 27.266  0.50 35.80 ? 33  ASP A CA    1 
ATOM   497   C  C     A ASP A 1 33  ? -23.882 -24.159 27.632  0.50 39.07 ? 33  ASP A C     1 
ATOM   498   C  C     B ASP A 1 33  ? -23.445 -24.335 27.460  0.50 36.98 ? 33  ASP A C     1 
ATOM   499   O  O     A ASP A 1 33  ? -24.713 -23.893 26.758  0.50 38.12 ? 33  ASP A O     1 
ATOM   500   O  O     B ASP A 1 33  ? -24.272 -24.013 26.602  0.50 37.64 ? 33  ASP A O     1 
ATOM   501   C  CB    A ASP A 1 33  ? -23.872 -26.629 27.205  0.50 42.16 ? 33  ASP A CB    1 
ATOM   502   C  CB    B ASP A 1 33  ? -23.554 -26.793 27.016  0.50 41.63 ? 33  ASP A CB    1 
ATOM   503   C  CG    A ASP A 1 33  ? -24.642 -27.088 28.433  0.50 44.14 ? 33  ASP A CG    1 
ATOM   504   C  CG    B ASP A 1 33  ? -24.517 -27.041 28.166  0.50 43.49 ? 33  ASP A CG    1 
ATOM   505   O  OD1   A ASP A 1 33  ? -24.809 -26.290 29.380  0.50 44.48 ? 33  ASP A OD1   1 
ATOM   506   O  OD1   B ASP A 1 33  ? -24.321 -26.464 29.256  0.50 44.86 ? 33  ASP A OD1   1 
ATOM   507   O  OD2   A ASP A 1 33  ? -25.075 -28.261 28.451  0.50 50.10 ? 33  ASP A OD2   1 
ATOM   508   O  OD2   B ASP A 1 33  ? -25.478 -27.818 27.976  0.50 49.80 ? 33  ASP A OD2   1 
ATOM   509   N  N     A GLY A 1 34  ? -23.725 -23.409 28.724  0.50 35.18 ? 34  GLY A N     1 
ATOM   510   N  N     B GLY A 1 34  ? -23.244 -23.616 28.564  0.50 37.00 ? 34  GLY A N     1 
ATOM   511   C  CA    A GLY A 1 34  ? -24.424 -22.157 28.916  0.50 35.34 ? 34  GLY A CA    1 
ATOM   512   C  CA    B GLY A 1 34  ? -23.990 -22.411 28.846  0.50 33.38 ? 34  GLY A CA    1 
ATOM   513   C  C     A GLY A 1 34  ? -25.565 -22.192 29.913  0.50 30.23 ? 34  GLY A C     1 
ATOM   514   C  C     B GLY A 1 34  ? -25.253 -22.609 29.656  0.50 33.05 ? 34  GLY A C     1 
ATOM   515   O  O     A GLY A 1 34  ? -26.037 -21.122 30.318  0.50 32.71 ? 34  GLY A O     1 
ATOM   516   O  O     B GLY A 1 34  ? -25.957 -21.626 29.920  0.50 30.55 ? 34  GLY A O     1 
ATOM   517   N  N     A GLN A 1 35  ? -26.023 -23.372 30.322  0.50 34.57 ? 35  GLN A N     1 
ATOM   518   N  N     B GLN A 1 35  ? -25.566 -23.839 30.056  0.50 32.21 ? 35  GLN A N     1 
ATOM   519   C  CA    A GLN A 1 35  ? -27.159 -23.455 31.230  0.50 35.72 ? 35  GLN A CA    1 
ATOM   520   C  CA    B GLN A 1 35  ? -26.765 -24.098 30.840  0.50 38.17 ? 35  GLN A CA    1 
ATOM   521   C  C     A GLN A 1 35  ? -26.751 -23.075 32.649  0.50 38.09 ? 35  GLN A C     1 
ATOM   522   C  C     B GLN A 1 35  ? -26.525 -23.770 32.307  0.50 39.48 ? 35  GLN A C     1 
ATOM   523   O  O     A GLN A 1 35  ? -25.606 -23.272 33.064  0.50 40.60 ? 35  GLN A O     1 
ATOM   524   O  O     B GLN A 1 35  ? -25.442 -24.018 32.844  0.50 38.75 ? 35  GLN A O     1 
ATOM   525   C  CB    A GLN A 1 35  ? -27.762 -24.861 31.215  0.50 37.24 ? 35  GLN A CB    1 
ATOM   526   C  CB    B GLN A 1 35  ? -27.196 -25.558 30.692  0.50 40.31 ? 35  GLN A CB    1 
ATOM   527   C  CG    A GLN A 1 35  ? -28.407 -25.235 29.891  0.50 42.24 ? 35  GLN A CG    1 
ATOM   528   C  CG    B GLN A 1 35  ? -27.884 -25.866 29.374  0.50 41.65 ? 35  GLN A CG    1 
ATOM   529   C  CD    A GLN A 1 35  ? -29.498 -24.261 29.476  0.50 42.64 ? 35  GLN A CD    1 
ATOM   530   C  CD    B GLN A 1 35  ? -29.215 -25.150 29.237  0.50 43.60 ? 35  GLN A CD    1 
ATOM   531   O  OE1   A GLN A 1 35  ? -30.432 -23.996 30.235  0.50 43.06 ? 35  GLN A OE1   1 
ATOM   532   O  OE1   B GLN A 1 35  ? -29.929 -24.951 30.221  0.50 42.96 ? 35  GLN A OE1   1 
ATOM   533   N  NE2   A GLN A 1 35  ? -29.378 -23.717 28.270  0.50 38.93 ? 35  GLN A NE2   1 
ATOM   534   N  NE2   B GLN A 1 35  ? -29.552 -24.755 28.014  0.50 41.57 ? 35  GLN A NE2   1 
ATOM   535   N  N     A MET A 1 36  ? -27.710 -22.526 33.396  0.50 32.80 ? 36  MET A N     1 
ATOM   536   N  N     B MET A 1 36  ? -27.550 -23.216 32.954  0.50 36.26 ? 36  MET A N     1 
ATOM   537   C  CA    A MET A 1 36  ? -27.461 -22.013 34.742  0.50 30.87 ? 36  MET A CA    1 
ATOM   538   C  CA    B MET A 1 36  ? -27.467 -22.795 34.352  0.50 31.50 ? 36  MET A CA    1 
ATOM   539   C  C     A MET A 1 36  ? -28.677 -22.314 35.606  0.50 38.19 ? 36  MET A C     1 
ATOM   540   C  C     B MET A 1 36  ? -28.783 -23.140 35.038  0.50 37.68 ? 36  MET A C     1 
ATOM   541   O  O     A MET A 1 36  ? -29.580 -21.480 35.743  0.50 36.80 ? 36  MET A O     1 
ATOM   542   O  O     B MET A 1 36  ? -29.751 -22.366 34.965  0.50 40.62 ? 36  MET A O     1 
ATOM   543   C  CB    A MET A 1 36  ? -27.161 -20.514 34.717  0.50 34.83 ? 36  MET A CB    1 
ATOM   544   C  CB    B MET A 1 36  ? -27.164 -21.303 34.463  0.50 31.27 ? 36  MET A CB    1 
ATOM   545   C  CG    A MET A 1 36  ? -26.847 -19.902 36.073  0.50 31.07 ? 36  MET A CG    1 
ATOM   546   C  CG    B MET A 1 36  ? -26.977 -20.793 35.885  0.50 31.29 ? 36  MET A CG    1 
ATOM   547   S  SD    A MET A 1 36  ? -26.607 -18.115 35.989  0.50 37.06 ? 36  MET A SD    1 
ATOM   548   S  SD    B MET A 1 36  ? -26.648 -19.020 35.930  0.50 38.14 ? 36  MET A SD    1 
ATOM   549   C  CE    A MET A 1 36  ? -26.256 -17.742 37.705  0.50 35.48 ? 36  MET A CE    1 
ATOM   550   C  CE    B MET A 1 36  ? -26.549 -18.726 37.694  0.50 39.78 ? 36  MET A CE    1 
ATOM   551   N  N     A PRO A 1 37  ? -28.724 -23.502 36.217  0.50 41.43 ? 37  PRO A N     1 
ATOM   552   N  N     B PRO A 1 37  ? -28.858 -24.290 35.713  0.50 40.12 ? 37  PRO A N     1 
ATOM   553   C  CA    A PRO A 1 37  ? -29.956 -23.946 36.899  0.50 39.53 ? 37  PRO A CA    1 
ATOM   554   C  CA    B PRO A 1 37  ? -30.134 -24.688 36.331  0.50 38.75 ? 37  PRO A CA    1 
ATOM   555   C  C     A PRO A 1 37  ? -30.499 -22.980 37.942  0.50 41.56 ? 37  PRO A C     1 
ATOM   556   C  C     B PRO A 1 37  ? -30.572 -23.786 37.472  0.50 41.71 ? 37  PRO A C     1 
ATOM   557   O  O     A PRO A 1 37  ? -31.723 -22.858 38.077  0.50 42.50 ? 37  PRO A O     1 
ATOM   558   O  O     B PRO A 1 37  ? -31.779 -23.673 37.721  0.50 38.07 ? 37  PRO A O     1 
ATOM   559   C  CB    A PRO A 1 37  ? -29.530 -25.275 37.539  0.50 37.66 ? 37  PRO A CB    1 
ATOM   560   C  CB    B PRO A 1 37  ? -29.857 -26.117 36.823  0.50 42.08 ? 37  PRO A CB    1 
ATOM   561   C  CG    A PRO A 1 37  ? -28.418 -25.771 36.670  0.50 39.13 ? 37  PRO A CG    1 
ATOM   562   C  CG    B PRO A 1 37  ? -28.641 -26.568 36.065  0.50 36.68 ? 37  PRO A CG    1 
ATOM   563   C  CD    A PRO A 1 37  ? -27.676 -24.538 36.230  0.50 36.59 ? 37  PRO A CD    1 
ATOM   564   C  CD    B PRO A 1 37  ? -27.828 -25.332 35.845  0.50 38.71 ? 37  PRO A CD    1 
ATOM   565   N  N     A SER A 1 38  ? -29.633 -22.289 38.685  0.50 36.63 ? 38  SER A N     1 
ATOM   566   N  N     B SER A 1 38  ? -29.636 -23.148 38.181  0.50 41.63 ? 38  SER A N     1 
ATOM   567   C  CA    A SER A 1 38  ? -30.087 -21.411 39.757  0.50 38.56 ? 38  SER A CA    1 
ATOM   568   C  CA    B SER A 1 38  ? -30.003 -22.289 39.302  0.50 38.04 ? 38  SER A CA    1 
ATOM   569   C  C     A SER A 1 38  ? -30.683 -20.099 39.258  0.50 41.74 ? 38  SER A C     1 
ATOM   570   C  C     B SER A 1 38  ? -30.645 -20.982 38.861  0.50 41.94 ? 38  SER A C     1 
ATOM   571   O  O     A SER A 1 38  ? -31.237 -19.347 40.067  0.50 37.70 ? 38  SER A O     1 
ATOM   572   O  O     B SER A 1 38  ? -31.172 -20.255 39.711  0.50 40.50 ? 38  SER A O     1 
ATOM   573   C  CB    A SER A 1 38  ? -28.931 -21.117 40.715  0.50 46.17 ? 38  SER A CB    1 
ATOM   574   C  CB    B SER A 1 38  ? -28.777 -21.981 40.160  0.50 43.12 ? 38  SER A CB    1 
ATOM   575   O  OG    A SER A 1 38  ? -27.797 -20.639 40.013  0.50 40.95 ? 38  SER A OG    1 
ATOM   576   O  OG    B SER A 1 38  ? -27.824 -21.232 39.427  0.50 40.52 ? 38  SER A OG    1 
ATOM   577   N  N     A ASP A 1 39  ? -30.592 -19.804 37.962  0.50 39.40 ? 39  ASP A N     1 
ATOM   578   N  N     B ASP A 1 39  ? -30.612 -20.665 37.570  0.50 37.78 ? 39  ASP A N     1 
ATOM   579   C  CA    A ASP A 1 39  ? -31.129 -18.559 37.413  0.50 42.82 ? 39  ASP A CA    1 
ATOM   580   C  CA    B ASP A 1 39  ? -31.219 -19.442 37.051  0.50 41.43 ? 39  ASP A CA    1 
ATOM   581   C  C     A ASP A 1 39  ? -32.629 -18.725 37.202  0.50 37.43 ? 39  ASP A C     1 
ATOM   582   C  C     B ASP A 1 39  ? -32.664 -19.759 36.682  0.50 39.08 ? 39  ASP A C     1 
ATOM   583   O  O     A ASP A 1 39  ? -33.072 -19.291 36.200  0.50 34.81 ? 39  ASP A O     1 
ATOM   584   O  O     B ASP A 1 39  ? -32.933 -20.396 35.660  0.50 42.41 ? 39  ASP A O     1 
ATOM   585   C  CB    A ASP A 1 39  ? -30.423 -18.197 36.112  0.50 38.94 ? 39  ASP A CB    1 
ATOM   586   C  CB    B ASP A 1 39  ? -30.423 -18.915 35.861  0.50 40.72 ? 39  ASP A CB    1 
ATOM   587   C  CG    A ASP A 1 39  ? -30.781 -16.807 35.626  0.50 41.86 ? 39  ASP A CG    1 
ATOM   588   C  CG    B ASP A 1 39  ? -31.011 -17.647 35.275  0.50 42.14 ? 39  ASP A CG    1 
ATOM   589   O  OD1   A ASP A 1 39  ? -31.193 -15.973 36.461  0.50 42.88 ? 39  ASP A OD1   1 
ATOM   590   O  OD1   B ASP A 1 39  ? -31.835 -16.994 35.953  0.50 45.74 ? 39  ASP A OD1   1 
ATOM   591   O  OD2   A ASP A 1 39  ? -30.665 -16.553 34.408  0.50 39.63 ? 39  ASP A OD2   1 
ATOM   592   O  OD2   B ASP A 1 39  ? -30.651 -17.305 34.127  0.50 39.79 ? 39  ASP A OD2   1 
ATOM   593   N  N     A LYS A 1 40  ? -33.421 -18.210 38.144  0.50 47.19 ? 40  LYS A N     1 
ATOM   594   N  N     B LYS A 1 40  ? -33.600 -19.329 37.532  0.50 45.46 ? 40  LYS A N     1 
ATOM   595   C  CA    A LYS A 1 40  ? -34.862 -18.434 38.132  0.50 45.30 ? 40  LYS A CA    1 
ATOM   596   C  CA    B LYS A 1 40  ? -35.018 -19.547 37.274  0.50 40.14 ? 40  LYS A CA    1 
ATOM   597   C  C     A LYS A 1 40  ? -35.585 -17.684 37.019  0.50 47.04 ? 40  LYS A C     1 
ATOM   598   C  C     B LYS A 1 40  ? -35.564 -18.628 36.190  0.50 44.70 ? 40  LYS A C     1 
ATOM   599   O  O     A LYS A 1 40  ? -36.777 -17.937 36.808  0.50 37.24 ? 40  LYS A O     1 
ATOM   600   O  O     B LYS A 1 40  ? -36.565 -18.969 35.551  0.50 45.50 ? 40  LYS A O     1 
ATOM   601   C  CB    A LYS A 1 40  ? -35.461 -18.041 39.483  0.50 40.96 ? 40  LYS A CB    1 
ATOM   602   C  CB    B LYS A 1 40  ? -35.822 -19.353 38.562  0.50 36.65 ? 40  LYS A CB    1 
ATOM   603   N  N     A THR A 1 41  ? -34.914 -16.780 36.309  0.50 36.23 ? 41  THR A N     1 
ATOM   604   N  N     B THR A 1 41  ? -34.938 -17.474 35.972  0.50 40.17 ? 41  THR A N     1 
ATOM   605   C  CA    A THR A 1 41  ? -35.543 -15.978 35.259  0.50 39.66 ? 41  THR A CA    1 
ATOM   606   C  CA    B THR A 1 41  ? -35.358 -16.552 34.926  0.50 39.69 ? 41  THR A CA    1 
ATOM   607   C  C     A THR A 1 41  ? -34.925 -16.353 33.914  0.50 46.08 ? 41  THR A C     1 
ATOM   608   C  C     B THR A 1 41  ? -34.667 -16.935 33.622  0.50 46.25 ? 41  THR A C     1 
ATOM   609   O  O     A THR A 1 41  ? -33.803 -15.944 33.600  0.50 42.40 ? 41  THR A O     1 
ATOM   610   O  O     B THR A 1 41  ? -33.437 -16.868 33.520  0.50 39.59 ? 41  THR A O     1 
ATOM   611   C  CB    A THR A 1 41  ? -35.392 -14.486 35.545  0.50 44.09 ? 41  THR A CB    1 
ATOM   612   C  CB    B THR A 1 41  ? -35.035 -15.109 35.312  0.50 41.66 ? 41  THR A CB    1 
ATOM   613   O  OG1   A THR A 1 41  ? -34.003 -14.157 35.673  0.50 38.00 ? 41  THR A OG1   1 
ATOM   614   O  OG1   B THR A 1 41  ? -33.656 -15.011 35.693  0.50 39.17 ? 41  THR A OG1   1 
ATOM   615   C  CG2   A THR A 1 41  ? -36.123 -14.114 36.831  0.50 37.80 ? 41  THR A CG2   1 
ATOM   616   C  CG2   B THR A 1 41  ? -35.911 -14.657 36.474  0.50 43.60 ? 41  THR A CG2   1 
ATOM   617   N  N     A ILE A 1 42  ? -35.669 -17.121 33.121  0.50 41.62 ? 42  ILE A N     1 
ATOM   618   N  N     B ILE A 1 42  ? -35.456 -17.333 32.630  0.50 42.48 ? 42  ILE A N     1 
ATOM   619   C  CA    A ILE A 1 42  ? -35.196 -17.578 31.819  0.50 44.01 ? 42  ILE A CA    1 
ATOM   620   C  CA    B ILE A 1 42  ? -34.941 -17.811 31.352  0.50 44.10 ? 42  ILE A CA    1 
ATOM   621   C  C     A ILE A 1 42  ? -35.314 -16.446 30.806  0.50 41.77 ? 42  ILE A C     1 
ATOM   622   C  C     B ILE A 1 42  ? -35.193 -16.738 30.303  0.50 42.71 ? 42  ILE A C     1 
ATOM   623   O  O     A ILE A 1 42  ? -36.239 -15.629 30.860  0.50 35.12 ? 42  ILE A O     1 
ATOM   624   O  O     B ILE A 1 42  ? -36.336 -16.309 30.103  0.50 42.78 ? 42  ILE A O     1 
ATOM   625   C  CB    A ILE A 1 42  ? -35.990 -18.823 31.372  0.50 44.97 ? 42  ILE A CB    1 
ATOM   626   C  CB    B ILE A 1 42  ? -35.588 -19.145 30.949  0.50 46.00 ? 42  ILE A CB    1 
ATOM   627   C  CG1   A ILE A 1 42  ? -35.906 -19.915 32.438  0.50 40.61 ? 42  ILE A CG1   1 
ATOM   628   C  CG1   B ILE A 1 42  ? -35.354 -20.197 32.038  0.50 42.89 ? 42  ILE A CG1   1 
ATOM   629   C  CG2   A ILE A 1 42  ? -35.478 -19.350 30.039  0.50 45.25 ? 42  ILE A CG2   1 
ATOM   630   C  CG2   B ILE A 1 42  ? -35.042 -19.624 29.611  0.50 46.87 ? 42  ILE A CG2   1 
ATOM   631   C  CD1   A ILE A 1 42  ? -36.685 -21.167 32.092  0.50 43.65 ? 42  ILE A CD1   1 
ATOM   632   C  CD1   B ILE A 1 42  ? -35.848 -21.582 31.671  0.50 45.60 ? 42  ILE A CD1   1 
ATOM   633   N  N     A GLY A 1 43  ? -34.356 -16.385 29.880  0.50 44.86 ? 43  GLY A N     1 
ATOM   634   N  N     B GLY A 1 43  ? -34.124 -16.297 29.637  0.50 44.07 ? 43  GLY A N     1 
ATOM   635   C  CA    A GLY A 1 43  ? -34.416 -15.429 28.790  0.50 39.99 ? 43  GLY A CA    1 
ATOM   636   C  CA    B GLY A 1 43  ? -34.212 -15.333 28.562  0.50 39.63 ? 43  GLY A CA    1 
ATOM   637   C  C     A GLY A 1 43  ? -34.159 -13.989 29.164  0.50 39.19 ? 43  GLY A C     1 
ATOM   638   C  C     B GLY A 1 43  ? -33.584 -13.986 28.858  0.50 39.99 ? 43  GLY A C     1 
ATOM   639   O  O     A GLY A 1 43  ? -34.323 -13.106 28.317  0.50 42.53 ? 43  GLY A O     1 
ATOM   640   O  O     B GLY A 1 43  ? -33.229 -13.266 27.915  0.50 44.46 ? 43  GLY A O     1 
ATOM   641   N  N     A GLY A 1 44  ? -33.763 -13.720 30.400  0.50 41.60 ? 44  GLY A N     1 
ATOM   642   N  N     B GLY A 1 44  ? -33.441 -13.619 30.129  0.50 41.77 ? 44  GLY A N     1 
ATOM   643   C  CA    A GLY A 1 44  ? -33.503 -12.356 30.820  0.50 40.94 ? 44  GLY A CA    1 
ATOM   644   C  CA    B GLY A 1 44  ? -32.866 -12.332 30.474  0.50 42.76 ? 44  GLY A CA    1 
ATOM   645   C  C     A GLY A 1 44  ? -32.957 -12.355 32.228  0.50 44.71 ? 44  GLY A C     1 
ATOM   646   C  C     B GLY A 1 44  ? -32.827 -12.061 31.964  0.50 44.79 ? 44  GLY A C     1 
ATOM   647   O  O     A GLY A 1 44  ? -32.848 -13.399 32.877  0.50 43.74 ? 44  GLY A O     1 
ATOM   648   O  O     B GLY A 1 44  ? -32.755 -12.994 32.770  0.50 42.57 ? 44  GLY A O     1 
ATOM   649   N  N     A GLY A 1 45  ? -32.605 -11.163 32.697  0.50 46.74 ? 45  GLY A N     1 
ATOM   650   N  N     B GLY A 1 45  ? -32.866 -10.791 32.344  0.50 45.27 ? 45  GLY A N     1 
ATOM   651   C  CA    A GLY A 1 45  ? -32.083 -11.056 34.043  0.50 40.02 ? 45  GLY A CA    1 
ATOM   652   C  CA    B GLY A 1 45  ? -32.867 -10.396 33.738  0.50 40.85 ? 45  GLY A CA    1 
ATOM   653   C  C     A GLY A 1 45  ? -31.460 -9.722  34.388  0.50 42.67 ? 45  GLY A C     1 
ATOM   654   C  C     B GLY A 1 45  ? -31.701 -9.484  34.078  0.50 42.66 ? 45  GLY A C     1 
ATOM   655   O  O     A GLY A 1 45  ? -30.690 -9.153  33.606  0.50 36.15 ? 45  GLY A O     1 
ATOM   656   O  O     B GLY A 1 45  ? -30.771 -9.284  33.297  0.50 35.60 ? 45  GLY A O     1 
ATOM   657   N  N     A ASP A 1 46  ? -31.788 -9.224  35.579  0.50 37.20 ? 46  ASP A N     1 
ATOM   658   N  N     B ASP A 1 46  ? -31.775 -8.935  35.289  0.50 37.68 ? 46  ASP A N     1 
ATOM   659   C  CA    A ASP A 1 46  ? -31.232 -7.988  36.108  0.50 38.29 ? 46  ASP A CA    1 
ATOM   660   C  CA    B ASP A 1 46  ? -30.781 -8.002  35.807  0.50 36.66 ? 46  ASP A CA    1 
ATOM   661   C  C     A ASP A 1 46  ? -30.244 -8.255  37.240  0.50 38.76 ? 46  ASP A C     1 
ATOM   662   C  C     B ASP A 1 46  ? -30.033 -8.584  37.003  0.50 37.46 ? 46  ASP A C     1 
ATOM   663   O  O     A ASP A 1 46  ? -29.929 -7.346  38.015  0.50 41.01 ? 46  ASP A O     1 
ATOM   664   O  O     B ASP A 1 46  ? -29.678 -7.868  37.942  0.50 40.42 ? 46  ASP A O     1 
ATOM   665   C  CB    A ASP A 1 46  ? -32.363 -7.069  36.578  0.50 46.20 ? 46  ASP A CB    1 
ATOM   666   C  CB    B ASP A 1 46  ? -31.433 -6.677  36.192  0.50 40.79 ? 46  ASP A CB    1 
ATOM   667   C  CG    A ASP A 1 46  ? -31.942 -5.614  36.663  0.50 47.60 ? 46  ASP A CG    1 
ATOM   668   C  CG    B ASP A 1 46  ? -32.422 -6.188  35.153  0.50 45.36 ? 46  ASP A CG    1 
ATOM   669   O  OD1   A ASP A 1 46  ? -31.309 -5.123  35.705  0.50 41.94 ? 46  ASP A OD1   1 
ATOM   670   O  OD1   B ASP A 1 46  ? -32.174 -6.390  33.947  0.50 48.98 ? 46  ASP A OD1   1 
ATOM   671   O  OD2   A ASP A 1 46  ? -32.258 -4.960  37.681  0.50 47.24 ? 46  ASP A OD2   1 
ATOM   672   O  OD2   B ASP A 1 46  ? -33.457 -5.607  35.548  0.50 54.77 ? 46  ASP A OD2   1 
ATOM   673   N  N     A ASP A 1 47  ? -29.755 -9.488  37.351  0.50 31.50 ? 47  ASP A N     1 
ATOM   674   N  N     B ASP A 1 47  ? -29.797 -9.892  36.990  0.50 29.84 ? 47  ASP A N     1 
ATOM   675   C  CA    A ASP A 1 47  ? -28.842 -9.859  38.418  0.50 34.30 ? 47  ASP A CA    1 
ATOM   676   C  CA    B ASP A 1 47  ? -29.065 -10.518 38.076  0.50 33.46 ? 47  ASP A CA    1 
ATOM   677   C  C     A ASP A 1 47  ? -27.443 -9.308  38.152  0.50 34.38 ? 47  ASP A C     1 
ATOM   678   C  C     B ASP A 1 47  ? -27.583 -10.168 37.987  0.50 32.75 ? 47  ASP A C     1 
ATOM   679   O  O     A ASP A 1 47  ? -27.116 -8.857  37.049  0.50 33.75 ? 47  ASP A O     1 
ATOM   680   O  O     B ASP A 1 47  ? -27.082 -9.738  36.944  0.50 27.62 ? 47  ASP A O     1 
ATOM   681   C  CB    A ASP A 1 47  ? -28.789 -11.377 38.576  0.50 33.05 ? 47  ASP A CB    1 
ATOM   682   C  CB    B ASP A 1 47  ? -29.264 -12.027 38.045  0.50 33.82 ? 47  ASP A CB    1 
ATOM   683   C  CG    A ASP A 1 47  ? -30.055 -11.943 39.177  0.50 37.62 ? 47  ASP A CG    1 
ATOM   684   C  CG    B ASP A 1 47  ? -30.720 -12.411 38.136  0.50 34.64 ? 47  ASP A CG    1 
ATOM   685   O  OD1   A ASP A 1 47  ? -30.600 -11.319 40.109  0.50 36.92 ? 47  ASP A OD1   1 
ATOM   686   O  OD1   B ASP A 1 47  ? -31.511 -11.606 38.669  0.50 40.17 ? 47  ASP A OD1   1 
ATOM   687   O  OD2   A ASP A 1 47  ? -30.506 -13.014 38.720  0.50 33.71 ? 47  ASP A OD2   1 
ATOM   688   O  OD2   B ASP A 1 47  ? -31.079 -13.520 37.695  0.50 35.35 ? 47  ASP A OD2   1 
ATOM   689   N  N     A SER A 1 48  ? -26.604 -9.363  39.189  0.50 32.39 ? 48  SER A N     1 
ATOM   690   N  N     B SER A 1 48  ? -26.885 -10.360 39.111  0.50 32.07 ? 48  SER A N     1 
ATOM   691   C  CA    A SER A 1 48  ? -25.270 -8.787  39.084  0.50 27.72 ? 48  SER A CA    1 
ATOM   692   C  CA    B SER A 1 48  ? -25.504 -9.904  39.232  0.50 33.15 ? 48  SER A CA    1 
ATOM   693   C  C     A SER A 1 48  ? -24.374 -9.591  38.148  0.50 32.61 ? 48  SER A C     1 
ATOM   694   C  C     B SER A 1 48  ? -24.627 -10.464 38.117  0.50 27.86 ? 48  SER A C     1 
ATOM   695   O  O     A SER A 1 48  ? -23.428 -9.035  37.579  0.50 22.95 ? 48  SER A O     1 
ATOM   696   O  O     B SER A 1 48  ? -23.911 -9.718  37.439  0.50 27.26 ? 48  SER A O     1 
ATOM   697   C  CB    A SER A 1 48  ? -24.633 -8.679  40.468  0.50 31.12 ? 48  SER A CB    1 
ATOM   698   C  CB    B SER A 1 48  ? -24.947 -10.293 40.604  0.50 34.03 ? 48  SER A CB    1 
ATOM   699   O  OG    A SER A 1 48  ? -24.337 -9.960  40.992  0.50 34.06 ? 48  SER A OG    1 
ATOM   700   O  OG    B SER A 1 48  ? -24.688 -11.687 40.692  0.50 28.31 ? 48  SER A OG    1 
ATOM   701   N  N     A PHE A 1 49  ? -24.639 -10.890 37.977  0.50 26.24 ? 49  PHE A N     1 
ATOM   702   N  N     B PHE A 1 49  ? -24.685 -11.780 37.903  0.50 27.38 ? 49  PHE A N     1 
ATOM   703   C  CA    A PHE A 1 49  ? -23.837 -11.655 37.028  0.50 30.98 ? 49  PHE A CA    1 
ATOM   704   C  CA    B PHE A 1 49  ? -23.847 -12.433 36.902  0.50 30.30 ? 49  PHE A CA    1 
ATOM   705   C  C     A PHE A 1 49  ? -24.163 -11.307 35.583  0.50 32.08 ? 49  PHE A C     1 
ATOM   706   C  C     B PHE A 1 49  ? -24.225 -12.073 35.471  0.50 29.87 ? 49  PHE A C     1 
ATOM   707   O  O     A PHE A 1 49  ? -23.386 -11.659 34.687  0.50 27.53 ? 49  PHE A O     1 
ATOM   708   O  O     B PHE A 1 49  ? -23.476 -12.416 34.550  0.50 26.99 ? 49  PHE A O     1 
ATOM   709   C  CB    A PHE A 1 49  ? -24.001 -13.165 37.259  0.50 27.13 ? 49  PHE A CB    1 
ATOM   710   C  CB    B PHE A 1 49  ? -23.914 -13.950 37.070  0.50 26.79 ? 49  PHE A CB    1 
ATOM   711   C  CG    A PHE A 1 49  ? -25.400 -13.686 37.028  0.50 32.49 ? 49  PHE A CG    1 
ATOM   712   C  CG    B PHE A 1 49  ? -25.270 -14.527 36.788  0.50 33.64 ? 49  PHE A CG    1 
ATOM   713   C  CD1   A PHE A 1 49  ? -25.859 -13.956 35.746  0.50 29.70 ? 49  PHE A CD1   1 
ATOM   714   C  CD1   B PHE A 1 49  ? -26.257 -14.512 37.758  0.50 32.71 ? 49  PHE A CD1   1 
ATOM   715   C  CD2   A PHE A 1 49  ? -26.238 -13.944 38.099  0.50 31.39 ? 49  PHE A CD2   1 
ATOM   716   C  CD2   B PHE A 1 49  ? -25.562 -15.075 35.549  0.50 33.91 ? 49  PHE A CD2   1 
ATOM   717   C  CE1   A PHE A 1 49  ? -27.134 -14.446 35.540  0.50 33.58 ? 49  PHE A CE1   1 
ATOM   718   C  CE1   B PHE A 1 49  ? -27.508 -15.039 37.502  0.50 36.30 ? 49  PHE A CE1   1 
ATOM   719   C  CE2   A PHE A 1 49  ? -27.514 -14.438 37.899  0.50 36.07 ? 49  PHE A CE2   1 
ATOM   720   C  CE2   B PHE A 1 49  ? -26.811 -15.601 35.287  0.50 34.80 ? 49  PHE A CE2   1 
ATOM   721   C  CZ    A PHE A 1 49  ? -27.963 -14.687 36.619  0.50 35.97 ? 49  PHE A CZ    1 
ATOM   722   C  CZ    B PHE A 1 49  ? -27.785 -15.584 36.266  0.50 37.67 ? 49  PHE A CZ    1 
ATOM   723   N  N     A ASN A 1 50  ? -25.283 -10.623 35.333  0.50 23.28 ? 50  ASN A N     1 
ATOM   724   N  N     B ASN A 1 50  ? -25.362 -11.411 35.250  0.50 28.43 ? 50  ASN A N     1 
ATOM   725   C  CA    A ASN A 1 50  ? -25.612 -10.193 33.980  0.50 26.14 ? 50  ASN A CA    1 
ATOM   726   C  CA    B ASN A 1 50  ? -25.707 -11.009 33.893  0.50 23.83 ? 50  ASN A CA    1 
ATOM   727   C  C     A ASN A 1 50  ? -24.712 -9.074  33.482  0.50 26.32 ? 50  ASN A C     1 
ATOM   728   C  C     B ASN A 1 50  ? -24.869 -9.837  33.402  0.50 28.70 ? 50  ASN A C     1 
ATOM   729   O  O     A ASN A 1 50  ? -24.844 -8.669  32.322  0.50 25.69 ? 50  ASN A O     1 
ATOM   730   O  O     B ASN A 1 50  ? -24.888 -9.548  32.200  0.50 23.19 ? 50  ASN A O     1 
ATOM   731   C  CB    A ASN A 1 50  ? -27.076 -9.754  33.901  0.50 25.74 ? 50  ASN A CB    1 
ATOM   732   C  CB    B ASN A 1 50  ? -27.195 -10.664 33.796  0.50 28.21 ? 50  ASN A CB    1 
ATOM   733   C  CG    A ASN A 1 50  ? -28.030 -10.927 33.887  0.50 28.99 ? 50  ASN A CG    1 
ATOM   734   C  CG    B ASN A 1 50  ? -28.079 -11.897 33.777  0.50 32.79 ? 50  ASN A CG    1 
ATOM   735   O  OD1   A ASN A 1 50  ? -28.814 -11.115 34.817  0.50 31.31 ? 50  ASN A OD1   1 
ATOM   736   O  OD1   B ASN A 1 50  ? -28.804 -12.167 34.734  0.50 38.46 ? 50  ASN A OD1   1 
ATOM   737   N  ND2   A ASN A 1 50  ? -27.966 -11.731 32.831  0.50 29.58 ? 50  ASN A ND2   1 
ATOM   738   N  ND2   B ASN A 1 50  ? -28.029 -12.649 32.682  0.50 25.64 ? 50  ASN A ND2   1 
ATOM   739   N  N     A THR A 1 51  ? -23.818 -8.555  34.324  0.50 24.42 ? 51  THR A N     1 
ATOM   740   N  N     B THR A 1 51  ? -24.138 -9.163  34.297  0.50 26.71 ? 51  THR A N     1 
ATOM   741   C  CA    A THR A 1 51  ? -22.790 -7.653  33.831  0.50 26.91 ? 51  THR A CA    1 
ATOM   742   C  CA    B THR A 1 51  ? -23.226 -8.108  33.869  0.50 26.94 ? 51  THR A CA    1 
ATOM   743   C  C     A THR A 1 51  ? -21.812 -8.370  32.910  0.50 24.86 ? 51  THR A C     1 
ATOM   744   C  C     B THR A 1 51  ? -22.178 -8.640  32.901  0.50 24.57 ? 51  THR A C     1 
ATOM   745   O  O     A THR A 1 51  ? -21.181 -7.718  32.071  0.50 30.05 ? 51  THR A O     1 
ATOM   746   O  O     B THR A 1 51  ? -21.746 -7.917  31.997  0.50 26.07 ? 51  THR A O     1 
ATOM   747   C  CB    A THR A 1 51  ? -22.047 -7.013  35.004  0.50 22.76 ? 51  THR A CB    1 
ATOM   748   C  CB    B THR A 1 51  ? -22.548 -7.470  35.082  0.50 25.76 ? 51  THR A CB    1 
ATOM   749   O  OG1   A THR A 1 51  ? -21.375 -8.027  35.757  0.50 29.44 ? 51  THR A OG1   1 
ATOM   750   O  OG1   B THR A 1 51  ? -21.885 -8.482  35.849  0.50 30.28 ? 51  THR A OG1   1 
ATOM   751   C  CG2   A THR A 1 51  ? -23.034 -6.309  35.922  0.50 25.53 ? 51  THR A CG2   1 
ATOM   752   C  CG2   B THR A 1 51  ? -23.573 -6.779  35.963  0.50 23.61 ? 51  THR A CG2   1 
ATOM   753   N  N     A PHE A 1 52  ? -21.693 -9.697  33.035  0.50 27.11 ? 52  PHE A N     1 
ATOM   754   N  N     B PHE A 1 52  ? -21.772 -9.900  33.065  0.50 27.15 ? 52  PHE A N     1 
ATOM   755   C  CA    A PHE A 1 52  ? -20.744 -10.492 32.266  0.50 27.45 ? 52  PHE A CA    1 
ATOM   756   C  CA    B PHE A 1 52  ? -20.783 -10.533 32.203  0.50 27.39 ? 52  PHE A CA    1 
ATOM   757   C  C     A PHE A 1 52  ? -21.383 -11.556 31.381  0.50 25.86 ? 52  PHE A C     1 
ATOM   758   C  C     B PHE A 1 52  ? -21.374 -11.564 31.252  0.50 26.01 ? 52  PHE A C     1 
ATOM   759   O  O     A PHE A 1 52  ? -20.724 -12.022 30.442  0.50 26.53 ? 52  PHE A O     1 
ATOM   760   O  O     B PHE A 1 52  ? -20.655 -12.047 30.368  0.50 26.40 ? 52  PHE A O     1 
ATOM   761   C  CB    A PHE A 1 52  ? -19.741 -11.192 33.204  0.50 23.23 ? 52  PHE A CB    1 
ATOM   762   C  CB    B PHE A 1 52  ? -19.692 -11.211 33.051  0.50 23.07 ? 52  PHE A CB    1 
ATOM   763   C  CG    A PHE A 1 52  ? -18.585 -10.326 33.633  0.50 29.03 ? 52  PHE A CG    1 
ATOM   764   C  CG    B PHE A 1 52  ? -18.617 -10.277 33.531  0.50 29.03 ? 52  PHE A CG    1 
ATOM   765   C  CD1   A PHE A 1 52  ? -18.787 -9.037  34.096  0.50 29.72 ? 52  PHE A CD1   1 
ATOM   766   C  CD1   B PHE A 1 52  ? -18.928 -9.160  34.286  0.50 29.48 ? 52  PHE A CD1   1 
ATOM   767   C  CD2   A PHE A 1 52  ? -17.289 -10.821 33.596  0.50 28.44 ? 52  PHE A CD2   1 
ATOM   768   C  CD2   B PHE A 1 52  ? -17.284 -10.535 33.244  0.50 29.23 ? 52  PHE A CD2   1 
ATOM   769   C  CE1   A PHE A 1 52  ? -17.717 -8.250  34.490  0.50 28.91 ? 52  PHE A CE1   1 
ATOM   770   C  CE1   B PHE A 1 52  ? -17.932 -8.306  34.729  0.50 29.49 ? 52  PHE A CE1   1 
ATOM   771   C  CE2   A PHE A 1 52  ? -16.216 -10.041 33.994  0.50 29.23 ? 52  PHE A CE2   1 
ATOM   772   C  CE2   B PHE A 1 52  ? -16.283 -9.687  33.685  0.50 29.33 ? 52  PHE A CE2   1 
ATOM   773   C  CZ    A PHE A 1 52  ? -16.429 -8.756  34.442  0.50 26.95 ? 52  PHE A CZ    1 
ATOM   774   C  CZ    B PHE A 1 52  ? -16.607 -8.572  34.429  0.50 27.59 ? 52  PHE A CZ    1 
ATOM   775   N  N     A PHE A 1 53  ? -22.627 -11.962 31.649  0.50 26.56 ? 53  PHE A N     1 
ATOM   776   N  N     B PHE A 1 53  ? -22.651 -11.919 31.405  0.50 26.35 ? 53  PHE A N     1 
ATOM   777   C  CA    A PHE A 1 53  ? -23.287 -13.042 30.915  0.50 24.40 ? 53  PHE A CA    1 
ATOM   778   C  CA    B PHE A 1 53  ? -23.264 -12.973 30.608  0.50 25.03 ? 53  PHE A CA    1 
ATOM   779   C  C     A PHE A 1 53  ? -24.657 -12.575 30.438  0.50 28.07 ? 53  PHE A C     1 
ATOM   780   C  C     B PHE A 1 53  ? -24.611 -12.516 30.065  0.50 27.71 ? 53  PHE A C     1 
ATOM   781   O  O     A PHE A 1 53  ? -25.565 -12.388 31.254  0.50 24.20 ? 53  PHE A O     1 
ATOM   782   O  O     B PHE A 1 53  ? -25.399 -11.883 30.776  0.50 24.77 ? 53  PHE A O     1 
ATOM   783   C  CB    A PHE A 1 53  ? -23.456 -14.290 31.784  0.50 29.06 ? 53  PHE A CB    1 
ATOM   784   C  CB    B PHE A 1 53  ? -23.469 -14.255 31.426  0.50 27.63 ? 53  PHE A CB    1 
ATOM   785   C  CG    A PHE A 1 53  ? -22.198 -15.078 32.008  0.50 25.94 ? 53  PHE A CG    1 
ATOM   786   C  CG    B PHE A 1 53  ? -22.202 -14.846 31.982  0.50 25.59 ? 53  PHE A CG    1 
ATOM   787   C  CD1   A PHE A 1 53  ? -21.397 -14.831 33.110  0.50 30.53 ? 53  PHE A CD1   1 
ATOM   788   C  CD1   B PHE A 1 53  ? -21.659 -14.373 33.165  0.50 27.55 ? 53  PHE A CD1   1 
ATOM   789   C  CD2   A PHE A 1 53  ? -21.842 -16.103 31.144  0.50 30.38 ? 53  PHE A CD2   1 
ATOM   790   C  CD2   B PHE A 1 53  ? -21.572 -15.898 31.336  0.50 30.80 ? 53  PHE A CD2   1 
ATOM   791   C  CE1   A PHE A 1 53  ? -20.247 -15.573 33.331  0.50 27.51 ? 53  PHE A CE1   1 
ATOM   792   C  CE1   B PHE A 1 53  ? -20.502 -14.927 33.686  0.50 29.37 ? 53  PHE A CE1   1 
ATOM   793   C  CE2   A PHE A 1 53  ? -20.696 -16.848 31.360  0.50 28.36 ? 53  PHE A CE2   1 
ATOM   794   C  CE2   B PHE A 1 53  ? -20.416 -16.455 31.852  0.50 28.27 ? 53  PHE A CE2   1 
ATOM   795   C  CZ    A PHE A 1 53  ? -19.897 -16.580 32.452  0.50 25.03 ? 53  PHE A CZ    1 
ATOM   796   C  CZ    B PHE A 1 53  ? -19.881 -15.968 33.025  0.50 26.82 ? 53  PHE A CZ    1 
ATOM   797   N  N     A SER A 1 54  ? -24.822 -12.419 29.126  0.50 26.71 ? 54  SER A N     1 
ATOM   798   N  N     B SER A 1 54  ? -24.877 -12.855 28.807  0.50 27.80 ? 54  SER A N     1 
ATOM   799   C  CA    A SER A 1 54  ? -26.164 -12.260 28.584  0.50 31.57 ? 54  SER A CA    1 
ATOM   800   C  CA    B SER A 1 54  ? -26.183 -12.650 28.197  0.50 31.41 ? 54  SER A CA    1 
ATOM   801   C  C     A SER A 1 54  ? -26.868 -13.616 28.540  0.50 29.16 ? 54  SER A C     1 
ATOM   802   C  C     B SER A 1 54  ? -26.988 -13.946 28.232  0.50 31.11 ? 54  SER A C     1 
ATOM   803   O  O     A SER A 1 54  ? -26.266 -14.665 28.782  0.50 29.81 ? 54  SER A O     1 
ATOM   804   O  O     B SER A 1 54  ? -26.483 -15.013 28.587  0.50 30.67 ? 54  SER A O     1 
ATOM   805   C  CB    A SER A 1 54  ? -26.119 -11.630 27.193  0.50 32.01 ? 54  SER A CB    1 
ATOM   806   C  CB    B SER A 1 54  ? -26.034 -12.164 26.755  0.50 33.09 ? 54  SER A CB    1 
ATOM   807   O  OG    A SER A 1 54  ? -25.463 -12.480 26.270  0.50 28.82 ? 54  SER A OG    1 
ATOM   808   O  OG    B SER A 1 54  ? -25.648 -13.238 25.917  0.50 27.29 ? 54  SER A OG    1 
ATOM   809   N  N     A GLU A 1 55  ? -28.165 -13.592 28.228  0.50 34.48 ? 55  GLU A N     1 
ATOM   810   N  N     B GLU A 1 55  ? -28.261 -13.842 27.846  0.50 34.04 ? 55  GLU A N     1 
ATOM   811   C  CA    A GLU A 1 55  ? -28.980 -14.802 28.215  0.50 33.65 ? 55  GLU A CA    1 
ATOM   812   C  CA    B GLU A 1 55  ? -29.147 -14.994 27.745  0.50 33.71 ? 55  GLU A CA    1 
ATOM   813   C  C     A GLU A 1 55  ? -29.832 -14.857 26.956  0.50 28.31 ? 55  GLU A C     1 
ATOM   814   C  C     B GLU A 1 55  ? -29.891 -14.951 26.419  0.50 30.02 ? 55  GLU A C     1 
ATOM   815   O  O     A GLU A 1 55  ? -30.332 -13.829 26.490  0.50 33.51 ? 55  GLU A O     1 
ATOM   816   O  O     B GLU A 1 55  ? -30.368 -13.894 25.996  0.50 37.17 ? 55  GLU A O     1 
ATOM   817   C  CB    A GLU A 1 55  ? -29.892 -14.881 29.447  0.50 32.04 ? 55  GLU A CB    1 
ATOM   818   C  CB    B GLU A 1 55  ? -30.145 -15.045 28.904  0.50 31.35 ? 55  GLU A CB    1 
ATOM   819   C  CG    A GLU A 1 55  ? -29.169 -14.760 30.774  0.50 37.60 ? 55  GLU A CG    1 
ATOM   820   C  CG    B GLU A 1 55  ? -29.498 -15.142 30.267  0.50 35.71 ? 55  GLU A CG    1 
ATOM   821   C  CD    A GLU A 1 55  ? -30.119 -14.762 31.951  0.50 35.87 ? 55  GLU A CD    1 
ATOM   822   C  CD    B GLU A 1 55  ? -30.503 -15.025 31.388  0.50 36.40 ? 55  GLU A CD    1 
ATOM   823   O  OE1   A GLU A 1 55  ? -31.173 -15.426 31.857  0.50 39.56 ? 55  GLU A OE1   1 
ATOM   824   O  OE1   B GLU A 1 55  ? -31.539 -15.719 31.323  0.50 35.52 ? 55  GLU A OE1   1 
ATOM   825   O  OE2   A GLU A 1 55  ? -29.817 -14.095 32.964  0.50 32.53 ? 55  GLU A OE2   1 
ATOM   826   O  OE2   B GLU A 1 55  ? -30.261 -14.234 32.325  0.50 33.86 ? 55  GLU A OE2   1 
ATOM   827   N  N     A THR A 1 56  ? -30.009 -16.063 26.420  0.50 32.93 ? 56  THR A N     1 
ATOM   828   N  N     B THR A 1 56  ? -29.998 -16.115 25.778  0.50 37.40 ? 56  THR A N     1 
ATOM   829   C  CA    A THR A 1 56  ? -30.816 -16.291 25.232  0.50 38.63 ? 56  THR A CA    1 
ATOM   830   C  CA    B THR A 1 56  ? -30.477 -16.248 24.406  0.50 37.48 ? 56  THR A CA    1 
ATOM   831   C  C     A THR A 1 56  ? -32.176 -16.858 25.632  0.50 38.24 ? 56  THR A C     1 
ATOM   832   C  C     B THR A 1 56  ? -31.992 -16.370 24.306  0.50 45.94 ? 56  THR A C     1 
ATOM   833   O  O     A THR A 1 56  ? -32.500 -16.981 26.815  0.50 40.68 ? 56  THR A O     1 
ATOM   834   O  O     B THR A 1 56  ? -32.599 -15.798 23.393  0.50 46.85 ? 56  THR A O     1 
ATOM   835   C  CB    A THR A 1 56  ? -30.101 -17.234 24.265  0.50 38.15 ? 56  THR A CB    1 
ATOM   836   C  CB    B THR A 1 56  ? -29.847 -17.479 23.755  0.50 40.52 ? 56  THR A CB    1 
ATOM   837   O  OG1   A THR A 1 56  ? -30.137 -18.565 24.791  0.50 35.10 ? 56  THR A OG1   1 
ATOM   838   O  OG1   B THR A 1 56  ? -30.151 -18.633 24.549  0.50 36.20 ? 56  THR A OG1   1 
ATOM   839   C  CG2   A THR A 1 56  ? -28.653 -16.803 24.062  0.50 37.32 ? 56  THR A CG2   1 
ATOM   840   C  CG2   B THR A 1 56  ? -28.339 -17.322 23.650  0.50 31.12 ? 56  THR A CG2   1 
ATOM   841   N  N     A GLY A 1 57  ? -32.977 -17.232 24.630  0.50 38.18 ? 57  GLY A N     1 
ATOM   842   N  N     B GLY A 1 57  ? -32.608 -17.125 25.210  0.50 40.01 ? 57  GLY A N     1 
ATOM   843   C  CA    A GLY A 1 57  ? -34.307 -17.747 24.901  0.50 44.05 ? 57  GLY A CA    1 
ATOM   844   C  CA    B GLY A 1 57  ? -34.017 -17.441 25.108  0.50 44.93 ? 57  GLY A CA    1 
ATOM   845   C  C     A GLY A 1 57  ? -34.333 -19.152 25.462  0.50 43.75 ? 57  GLY A C     1 
ATOM   846   C  C     B GLY A 1 57  ? -34.249 -18.935 25.202  0.50 43.40 ? 57  GLY A C     1 
ATOM   847   O  O     A GLY A 1 57  ? -35.280 -19.518 26.164  0.50 46.46 ? 57  GLY A O     1 
ATOM   848   O  O     B GLY A 1 57  ? -35.372 -19.384 25.446  0.50 45.47 ? 57  GLY A O     1 
ATOM   849   N  N     A ALA A 1 58  ? -33.308 -19.957 25.173  0.50 44.65 ? 58  ALA A N     1 
ATOM   850   N  N     B ALA A 1 58  ? -33.182 -19.714 25.017  0.50 44.21 ? 58  ALA A N     1 
ATOM   851   C  CA    A ALA A 1 58  ? -33.242 -21.336 25.640  0.50 42.01 ? 58  ALA A CA    1 
ATOM   852   C  CA    B ALA A 1 58  ? -33.236 -21.166 25.130  0.50 41.07 ? 58  ALA A CA    1 
ATOM   853   C  C     A ALA A 1 58  ? -32.464 -21.487 26.946  0.50 43.50 ? 58  ALA A C     1 
ATOM   854   C  C     B ALA A 1 58  ? -32.486 -21.691 26.350  0.50 42.99 ? 58  ALA A C     1 
ATOM   855   O  O     A ALA A 1 58  ? -32.046 -22.601 27.284  0.50 35.96 ? 58  ALA A O     1 
ATOM   856   O  O     B ALA A 1 58  ? -32.218 -22.894 26.428  0.50 35.65 ? 58  ALA A O     1 
ATOM   857   C  CB    A ALA A 1 58  ? -32.628 -22.229 24.559  0.50 41.92 ? 58  ALA A CB    1 
ATOM   858   C  CB    B ALA A 1 58  ? -32.683 -21.815 23.858  0.50 43.94 ? 58  ALA A CB    1 
ATOM   859   N  N     A GLY A 1 59  ? -32.261 -20.398 27.683  0.50 38.38 ? 59  GLY A N     1 
ATOM   860   N  N     B GLY A 1 59  ? -32.140 -20.827 27.302  0.50 41.93 ? 59  GLY A N     1 
ATOM   861   C  CA    A GLY A 1 59  ? -31.548 -20.470 28.942  0.50 40.54 ? 59  GLY A CA    1 
ATOM   862   C  CA    B GLY A 1 59  ? -31.446 -21.259 28.502  0.50 39.74 ? 59  GLY A CA    1 
ATOM   863   C  C     A GLY A 1 59  ? -30.039 -20.460 28.837  0.50 34.48 ? 59  GLY A C     1 
ATOM   864   C  C     B GLY A 1 59  ? -29.936 -21.216 28.434  0.50 38.64 ? 59  GLY A C     1 
ATOM   865   O  O     A GLY A 1 59  ? -29.365 -20.702 29.845  0.50 36.39 ? 59  GLY A O     1 
ATOM   866   O  O     B GLY A 1 59  ? -29.276 -21.800 29.303  0.50 41.97 ? 59  GLY A O     1 
ATOM   867   N  N     A LYS A 1 60  ? -29.490 -20.202 27.653  0.50 35.84 ? 60  LYS A N     1 
ATOM   868   N  N     B LYS A 1 60  ? -29.366 -20.535 27.446  0.50 36.80 ? 60  LYS A N     1 
ATOM   869   C  CA    A LYS A 1 60  ? -28.046 -20.109 27.486  0.50 33.44 ? 60  LYS A CA    1 
ATOM   870   C  CA    B LYS A 1 60  ? -27.926 -20.519 27.216  0.50 33.73 ? 60  LYS A CA    1 
ATOM   871   C  C     A LYS A 1 60  ? -27.527 -18.828 28.128  0.50 31.63 ? 60  LYS A C     1 
ATOM   872   C  C     B LYS A 1 60  ? -27.338 -19.232 27.785  0.50 32.78 ? 60  LYS A C     1 
ATOM   873   O  O     A LYS A 1 60  ? -28.197 -17.795 28.122  0.50 33.46 ? 60  LYS A O     1 
ATOM   874   O  O     B LYS A 1 60  ? -27.762 -18.133 27.410  0.50 32.72 ? 60  LYS A O     1 
ATOM   875   C  CB    A LYS A 1 60  ? -27.693 -20.135 25.999  0.50 35.40 ? 60  LYS A CB    1 
ATOM   876   C  CB    B LYS A 1 60  ? -27.635 -20.640 25.719  0.50 36.01 ? 60  LYS A CB    1 
ATOM   877   C  CG    A LYS A 1 60  ? -26.321 -20.678 25.648  0.50 39.55 ? 60  LYS A CG    1 
ATOM   878   C  CG    B LYS A 1 60  ? -26.173 -20.796 25.329  0.50 41.11 ? 60  LYS A CG    1 
ATOM   879   C  CD    A LYS A 1 60  ? -26.211 -20.859 24.134  0.50 44.43 ? 60  LYS A CD    1 
ATOM   880   C  CD    B LYS A 1 60  ? -26.058 -20.969 23.812  0.50 42.70 ? 60  LYS A CD    1 
ATOM   881   C  CE    A LYS A 1 60  ? -24.856 -21.389 23.712  0.50 42.51 ? 60  LYS A CE    1 
ATOM   882   C  CE    B LYS A 1 60  ? -24.622 -20.924 23.322  0.50 41.10 ? 60  LYS A CE    1 
ATOM   883   N  NZ    A LYS A 1 60  ? -24.513 -22.658 24.409  0.50 38.29 ? 60  LYS A NZ    1 
ATOM   884   N  NZ    B LYS A 1 60  ? -23.815 -22.071 23.818  0.50 41.38 ? 60  LYS A NZ    1 
ATOM   885   N  N     A HIS A 1 61  ? -26.321 -18.901 28.691  0.50 27.66 ? 61  HIS A N     1 
ATOM   886   N  N     B HIS A 1 61  ? -26.368 -19.370 28.686  0.50 28.33 ? 61  HIS A N     1 
ATOM   887   C  CA    A HIS A 1 61  ? -25.680 -17.754 29.331  0.50 26.78 ? 61  HIS A CA    1 
ATOM   888   C  CA    B HIS A 1 61  ? -25.654 -18.234 29.256  0.50 27.11 ? 61  HIS A CA    1 
ATOM   889   C  C     A HIS A 1 61  ? -24.332 -17.527 28.661  0.50 28.02 ? 61  HIS A C     1 
ATOM   890   C  C     B HIS A 1 61  ? -24.341 -18.062 28.504  0.50 29.40 ? 61  HIS A C     1 
ATOM   891   O  O     A HIS A 1 61  ? -23.392 -18.301 28.870  0.50 23.20 ? 61  HIS A O     1 
ATOM   892   O  O     B HIS A 1 61  ? -23.490 -18.958 28.522  0.50 27.73 ? 61  HIS A O     1 
ATOM   893   C  CB    A HIS A 1 61  ? -25.529 -17.978 30.833  0.50 27.21 ? 61  HIS A CB    1 
ATOM   894   C  CB    B HIS A 1 61  ? -25.407 -18.435 30.751  0.50 26.77 ? 61  HIS A CB    1 
ATOM   895   C  CG    A HIS A 1 61  ? -26.835 -18.039 31.559  0.50 32.48 ? 61  HIS A CG    1 
ATOM   896   C  CG    B HIS A 1 61  ? -26.661 -18.471 31.568  0.50 32.45 ? 61  HIS A CG    1 
ATOM   897   N  ND1   A HIS A 1 61  ? -27.738 -19.066 31.382  0.50 33.52 ? 61  HIS A ND1   1 
ATOM   898   N  ND1   B HIS A 1 61  ? -27.680 -19.367 31.327  0.50 32.44 ? 61  HIS A ND1   1 
ATOM   899   C  CD2   A HIS A 1 61  ? -27.402 -17.188 32.447  0.50 35.73 ? 61  HIS A CD2   1 
ATOM   900   C  CD2   B HIS A 1 61  ? -27.065 -17.716 32.618  0.50 34.53 ? 61  HIS A CD2   1 
ATOM   901   C  CE1   A HIS A 1 61  ? -28.799 -18.851 32.141  0.50 34.95 ? 61  HIS A CE1   1 
ATOM   902   C  CE1   B HIS A 1 61  ? -28.657 -19.164 32.194  0.50 35.45 ? 61  HIS A CE1   1 
ATOM   903   N  NE2   A HIS A 1 61  ? -28.623 -17.716 32.792  0.50 33.23 ? 61  HIS A NE2   1 
ATOM   904   N  NE2   B HIS A 1 61  ? -28.308 -18.169 32.989  0.50 35.54 ? 61  HIS A NE2   1 
ATOM   905   N  N     A VAL A 1 62  ? -24.243 -16.467 27.873  0.50 27.36 ? 62  VAL A N     1 
ATOM   906   N  N     B VAL A 1 62  ? -24.179 -16.915 27.852  0.50 28.57 ? 62  VAL A N     1 
ATOM   907   C  CA    A VAL A 1 62  ? -23.155 -16.258 26.919  0.50 27.70 ? 62  VAL A CA    1 
ATOM   908   C  CA    B VAL A 1 62  ? -23.117 -16.692 26.879  0.50 26.93 ? 62  VAL A CA    1 
ATOM   909   C  C     A VAL A 1 62  ? -22.284 -15.110 27.414  0.50 26.82 ? 62  VAL A C     1 
ATOM   910   C  C     B VAL A 1 62  ? -22.235 -15.557 27.379  0.50 26.97 ? 62  VAL A C     1 
ATOM   911   O  O     A VAL A 1 62  ? -22.807 -14.022 27.680  0.50 29.23 ? 62  VAL A O     1 
ATOM   912   O  O     B VAL A 1 62  ? -22.749 -14.481 27.690  0.50 29.66 ? 62  VAL A O     1 
ATOM   913   C  CB    A VAL A 1 62  ? -23.689 -15.960 25.506  0.50 32.55 ? 62  VAL A CB    1 
ATOM   914   C  CB    B VAL A 1 62  ? -23.665 -16.360 25.480  0.50 34.30 ? 62  VAL A CB    1 
ATOM   915   C  CG1   A VAL A 1 62  ? -22.549 -15.912 24.509  0.50 29.60 ? 62  VAL A CG1   1 
ATOM   916   C  CG1   B VAL A 1 62  ? -22.539 -16.339 24.465  0.50 29.41 ? 62  VAL A CG1   1 
ATOM   917   C  CG2   A VAL A 1 62  ? -24.719 -17.013 25.100  0.50 36.65 ? 62  VAL A CG2   1 
ATOM   918   C  CG2   B VAL A 1 62  ? -24.749 -17.358 25.078  0.50 35.47 ? 62  VAL A CG2   1 
ATOM   919   N  N     A PRO A 1 63  ? -20.969 -15.299 27.524  0.50 30.38 ? 63  PRO A N     1 
ATOM   920   N  N     B PRO A 1 63  ? -20.917 -15.741 27.451  0.50 31.18 ? 63  PRO A N     1 
ATOM   921   C  CA    A PRO A 1 63  ? -20.095 -14.211 27.980  0.50 21.88 ? 63  PRO A CA    1 
ATOM   922   C  CA    B PRO A 1 63  ? -20.033 -14.631 27.821  0.50 24.39 ? 63  PRO A CA    1 
ATOM   923   C  C     A PRO A 1 63  ? -20.182 -12.987 27.080  0.50 22.78 ? 63  PRO A C     1 
ATOM   924   C  C     B PRO A 1 63  ? -20.166 -13.455 26.865  0.50 25.06 ? 63  PRO A C     1 
ATOM   925   O  O     A PRO A 1 63  ? -20.269 -13.094 25.856  0.50 21.07 ? 63  PRO A O     1 
ATOM   926   O  O     B PRO A 1 63  ? -20.252 -13.623 25.647  0.50 23.61 ? 63  PRO A O     1 
ATOM   927   C  CB    A PRO A 1 63  ? -18.698 -14.841 27.922  0.50 27.37 ? 63  PRO A CB    1 
ATOM   928   C  CB    B PRO A 1 63  ? -18.636 -15.255 27.740  0.50 27.24 ? 63  PRO A CB    1 
ATOM   929   C  CG    A PRO A 1 63  ? -18.941 -16.306 28.064  0.50 29.19 ? 63  PRO A CG    1 
ATOM   930   C  CG    B PRO A 1 63  ? -18.868 -16.702 28.023  0.50 29.24 ? 63  PRO A CG    1 
ATOM   931   C  CD    A PRO A 1 63  ? -20.237 -16.565 27.349  0.50 29.39 ? 63  PRO A CD    1 
ATOM   932   C  CD    B PRO A 1 63  ? -20.198 -17.025 27.387  0.50 28.86 ? 63  PRO A CD    1 
ATOM   933   N  N     A ARG A 1 64  ? -20.161 -11.813 27.703  0.50 25.12 ? 64  ARG A N     1 
ATOM   934   N  N     B ARG A 1 64  ? -20.181 -12.252 27.438  0.50 23.40 ? 64  ARG A N     1 
ATOM   935   C  CA    A ARG A 1 64  ? -19.994 -10.560 26.972  0.50 21.08 ? 64  ARG A CA    1 
ATOM   936   C  CA    B ARG A 1 64  ? -20.149 -11.011 26.666  0.50 21.93 ? 64  ARG A CA    1 
ATOM   937   C  C     A ARG A 1 64  ? -18.499 -10.421 26.708  0.50 22.66 ? 64  ARG A C     1 
ATOM   938   C  C     B ARG A 1 64  ? -18.696 -10.666 26.326  0.50 23.14 ? 64  ARG A C     1 
ATOM   939   O  O     A ARG A 1 64  ? -17.757 -9.835  27.498  0.50 19.76 ? 64  ARG A O     1 
ATOM   940   O  O     B ARG A 1 64  ? -18.137 -9.662  26.768  0.50 23.15 ? 64  ARG A O     1 
ATOM   941   C  CB    A ARG A 1 64  ? -20.552 -9.383  27.764  0.50 21.91 ? 64  ARG A CB    1 
ATOM   942   C  CB    B ARG A 1 64  ? -20.813 -9.884  27.446  0.50 25.41 ? 64  ARG A CB    1 
ATOM   943   C  CG    A ARG A 1 64  ? -22.055 -9.468  28.038  0.50 23.82 ? 64  ARG A CG    1 
ATOM   944   C  CG    B ARG A 1 64  ? -22.194 -10.215 27.997  0.50 21.99 ? 64  ARG A CG    1 
ATOM   945   C  CD    A ARG A 1 64  ? -22.553 -8.259  28.821  0.50 24.76 ? 64  ARG A CD    1 
ATOM   946   C  CD    B ARG A 1 64  ? -22.667 -9.114  28.937  0.50 26.63 ? 64  ARG A CD    1 
ATOM   947   N  NE    A ARG A 1 64  ? -23.879 -8.484  29.385  0.50 25.79 ? 64  ARG A NE    1 
ATOM   948   N  NE    B ARG A 1 64  ? -23.976 -9.391  29.519  0.50 23.16 ? 64  ARG A NE    1 
ATOM   949   C  CZ    A ARG A 1 64  ? -25.013 -8.322  28.719  0.50 26.21 ? 64  ARG A CZ    1 
ATOM   950   C  CZ    B ARG A 1 64  ? -25.128 -9.211  28.889  0.50 26.66 ? 64  ARG A CZ    1 
ATOM   951   N  NH1   A ARG A 1 64  ? -25.021 -7.927  27.456  0.50 21.02 ? 64  ARG A NH1   1 
ATOM   952   N  NH1   B ARG A 1 64  ? -25.172 -8.806  27.631  0.50 22.74 ? 64  ARG A NH1   1 
ATOM   953   N  NH2   A ARG A 1 64  ? -26.168 -8.554  29.338  0.50 26.66 ? 64  ARG A NH2   1 
ATOM   954   N  NH2   B ARG A 1 64  ? -26.266 -9.439  29.541  0.50 24.88 ? 64  ARG A NH2   1 
ATOM   955   N  N     A ALA A 1 65  ? -18.041 -10.994 25.595  0.50 22.87 ? 65  ALA A N     1 
ATOM   956   N  N     B ALA A 1 65  ? -18.078 -11.540 25.535  0.50 21.75 ? 65  ALA A N     1 
ATOM   957   C  CA    A ALA A 1 65  ? -16.606 -11.096 25.366  0.50 18.19 ? 65  ALA A CA    1 
ATOM   958   C  CA    B ALA A 1 65  ? -16.643 -11.461 25.302  0.50 19.03 ? 65  ALA A CA    1 
ATOM   959   C  C     A ALA A 1 65  ? -16.302 -11.229 23.881  0.50 22.61 ? 65  ALA A C     1 
ATOM   960   C  C     B ALA A 1 65  ? -16.322 -11.717 23.838  0.50 22.65 ? 65  ALA A C     1 
ATOM   961   O  O     A ALA A 1 65  ? -17.100 -11.768 23.112  0.50 22.38 ? 65  ALA A O     1 
ATOM   962   O  O     B ALA A 1 65  ? -17.008 -12.482 23.155  0.50 21.43 ? 65  ALA A O     1 
ATOM   963   C  CB    A ALA A 1 65  ? -16.012 -12.286 26.129  0.50 22.90 ? 65  ALA A CB    1 
ATOM   964   C  CB    B ALA A 1 65  ? -15.881 -12.461 26.182  0.50 23.16 ? 65  ALA A CB    1 
ATOM   965   N  N     A VAL A 1 66  ? -15.123 -10.737 23.497  0.50 25.80 ? 66  VAL A N     1 
ATOM   966   N  N     B VAL A 1 66  ? -15.253 -11.070 23.376  0.50 26.89 ? 66  VAL A N     1 
ATOM   967   C  CA    A VAL A 1 66  ? -14.593 -10.867 22.145  0.50 26.70 ? 66  VAL A CA    1 
ATOM   968   C  CA    B VAL A 1 66  ? -14.717 -11.241 22.032  0.50 26.04 ? 66  VAL A CA    1 
ATOM   969   C  C     A VAL A 1 66  ? -13.151 -11.353 22.234  0.50 24.41 ? 66  VAL A C     1 
ATOM   970   C  C     B VAL A 1 66  ? -13.225 -11.539 22.140  0.50 24.61 ? 66  VAL A C     1 
ATOM   971   O  O     A VAL A 1 66  ? -12.380 -10.881 23.078  0.50 22.12 ? 66  VAL A O     1 
ATOM   972   O  O     B VAL A 1 66  ? -12.514 -10.914 22.936  0.50 22.23 ? 66  VAL A O     1 
ATOM   973   C  CB    A VAL A 1 66  ? -14.671 -9.532  21.373  0.50 27.22 ? 66  VAL A CB    1 
ATOM   974   C  CB    B VAL A 1 66  ? -14.969 -9.990  21.161  0.50 29.61 ? 66  VAL A CB    1 
ATOM   975   C  CG1   A VAL A 1 66  ? -14.231 -9.720  19.937  0.50 22.05 ? 66  VAL A CG1   1 
ATOM   976   C  CG1   B VAL A 1 66  ? -14.452 -8.738  21.858  0.50 27.12 ? 66  VAL A CG1   1 
ATOM   977   C  CG2   A VAL A 1 66  ? -16.085 -8.961  21.431  0.50 25.68 ? 66  VAL A CG2   1 
ATOM   978   C  CG2   B VAL A 1 66  ? -14.336 -10.146 19.790  0.50 22.17 ? 66  VAL A CG2   1 
ATOM   979   N  N     A PHE A 1 67  ? -12.792 -12.302 21.367  0.50 25.50 ? 67  PHE A N     1 
ATOM   980   N  N     B PHE A 1 67  ? -12.759 -12.506 21.352  0.50 25.55 ? 67  PHE A N     1 
ATOM   981   C  CA    A PHE A 1 67  ? -11.446 -12.865 21.290  0.50 26.68 ? 67  PHE A CA    1 
ATOM   982   C  CA    B PHE A 1 67  ? -11.352 -12.879 21.282  0.50 26.66 ? 67  PHE A CA    1 
ATOM   983   C  C     A PHE A 1 67  ? -10.880 -12.553 19.912  0.50 23.31 ? 67  PHE A C     1 
ATOM   984   C  C     B PHE A 1 67  ? -10.820 -12.522 19.902  0.50 23.29 ? 67  PHE A C     1 
ATOM   985   O  O     A PHE A 1 67  ? -11.490 -12.912 18.899  0.50 23.57 ? 67  PHE A O     1 
ATOM   986   O  O     B PHE A 1 67  ? -11.478 -12.788 18.892  0.50 23.61 ? 67  PHE A O     1 
ATOM   987   C  CB    A PHE A 1 67  ? -11.458 -14.381 21.512  0.50 26.45 ? 67  PHE A CB    1 
ATOM   988   C  CB    B PHE A 1 67  ? -11.150 -14.381 21.525  0.50 26.05 ? 67  PHE A CB    1 
ATOM   989   C  CG    A PHE A 1 67  ? -11.806 -14.801 22.912  0.50 25.48 ? 67  PHE A CG    1 
ATOM   990   C  CG    B PHE A 1 67  ? -11.562 -14.854 22.894  0.50 25.81 ? 67  PHE A CG    1 
ATOM   991   C  CD1   A PHE A 1 67  ? -13.092 -14.643 23.403  0.50 27.76 ? 67  PHE A CD1   1 
ATOM   992   C  CD1   B PHE A 1 67  ? -12.889 -14.825 23.292  0.50 27.74 ? 67  PHE A CD1   1 
ATOM   993   C  CD2   A PHE A 1 67  ? -10.849 -15.384 23.726  0.50 27.08 ? 67  PHE A CD2   1 
ATOM   994   C  CD2   B PHE A 1 67  ? -10.617 -15.363 23.770  0.50 26.82 ? 67  PHE A CD2   1 
ATOM   995   C  CE1   A PHE A 1 67  ? -13.411 -15.039 24.691  0.50 26.22 ? 67  PHE A CE1   1 
ATOM   996   C  CE1   B PHE A 1 67  ? -13.263 -15.269 24.551  0.50 27.24 ? 67  PHE A CE1   1 
ATOM   997   C  CE2   A PHE A 1 67  ? -11.160 -15.781 25.011  0.50 28.39 ? 67  PHE A CE2   1 
ATOM   998   C  CE2   B PHE A 1 67  ? -10.982 -15.808 25.025  0.50 28.22 ? 67  PHE A CE2   1 
ATOM   999   C  CZ    A PHE A 1 67  ? -12.443 -15.610 25.493  0.50 28.63 ? 67  PHE A CZ    1 
ATOM   1000  C  CZ    B PHE A 1 67  ? -12.308 -15.765 25.415  0.50 28.59 ? 67  PHE A CZ    1 
ATOM   1001  N  N     A VAL A 1 68  ? -9.717  -11.901 19.870  0.50 21.65 ? 68  VAL A N     1 
ATOM   1002  N  N     B VAL A 1 68  ? -9.630  -11.924 19.855  0.50 21.64 ? 68  VAL A N     1 
ATOM   1003  C  CA    A VAL A 1 68  ? -9.108  -11.482 18.612  0.50 22.05 ? 68  VAL A CA    1 
ATOM   1004  C  CA    B VAL A 1 68  ? -9.037  -11.516 18.586  0.50 22.01 ? 68  VAL A CA    1 
ATOM   1005  C  C     A VAL A 1 68  ? -7.628  -11.851 18.606  0.50 22.56 ? 68  VAL A C     1 
ATOM   1006  C  C     B VAL A 1 68  ? -7.541  -11.808 18.595  0.50 22.56 ? 68  VAL A C     1 
ATOM   1007  O  O     A VAL A 1 68  ? -6.895  -11.557 19.558  0.50 21.50 ? 68  VAL A O     1 
ATOM   1008  O  O     B VAL A 1 68  ? -6.846  -11.591 19.594  0.50 21.40 ? 68  VAL A O     1 
ATOM   1009  C  CB    A VAL A 1 68  ? -9.300  -9.974  18.353  0.50 26.43 ? 68  VAL A CB    1 
ATOM   1010  C  CB    B VAL A 1 68  ? -9.318  -10.030 18.271  0.50 26.44 ? 68  VAL A CB    1 
ATOM   1011  C  CG1   A VAL A 1 68  ? -8.856  -9.155  19.546  0.50 25.56 ? 68  VAL A CG1   1 
ATOM   1012  C  CG1   B VAL A 1 68  ? -8.719  -9.122  19.324  0.50 25.29 ? 68  VAL A CG1   1 
ATOM   1013  C  CG2   A VAL A 1 68  ? -8.549  -9.553  17.092  0.50 28.46 ? 68  VAL A CG2   1 
ATOM   1014  C  CG2   B VAL A 1 68  ? -8.798  -9.674  16.877  0.50 27.53 ? 68  VAL A CG2   1 
ATOM   1015  N  N     A ASP A 1 69  ? -7.198  -12.508 17.536  0.50 23.50 ? 69  ASP A N     1 
ATOM   1016  N  N     B ASP A 1 69  ? -7.052  -12.325 17.474  0.50 23.97 ? 69  ASP A N     1 
ATOM   1017  C  CA    A ASP A 1 69  ? -5.790  -12.783 17.312  0.50 23.54 ? 69  ASP A CA    1 
ATOM   1018  C  CA    B ASP A 1 69  ? -5.629  -12.536 17.279  0.50 23.10 ? 69  ASP A CA    1 
ATOM   1019  C  C     A ASP A 1 69  ? -5.532  -12.710 15.816  0.50 24.98 ? 69  ASP A C     1 
ATOM   1020  C  C     B ASP A 1 69  ? -5.344  -12.379 15.795  0.50 23.99 ? 69  ASP A C     1 
ATOM   1021  O  O     A ASP A 1 69  ? -6.415  -13.008 15.010  0.50 26.06 ? 69  ASP A O     1 
ATOM   1022  O  O     B ASP A 1 69  ? -6.222  -12.602 14.957  0.50 26.85 ? 69  ASP A O     1 
ATOM   1023  C  CB    A ASP A 1 69  ? -5.381  -14.154 17.866  0.50 24.04 ? 69  ASP A CB    1 
ATOM   1024  C  CB    B ASP A 1 69  ? -5.188  -13.916 17.783  0.50 23.77 ? 69  ASP A CB    1 
ATOM   1025  C  CG    A ASP A 1 69  ? -3.905  -14.230 18.202  0.50 23.99 ? 69  ASP A CG    1 
ATOM   1026  C  CG    B ASP A 1 69  ? -3.731  -13.946 18.203  0.50 23.79 ? 69  ASP A CG    1 
ATOM   1027  O  OD1   A ASP A 1 69  ? -3.181  -13.265 17.885  0.50 24.16 ? 69  ASP A OD1   1 
ATOM   1028  O  OD1   B ASP A 1 69  ? -3.030  -12.937 17.980  0.50 24.97 ? 69  ASP A OD1   1 
ATOM   1029  O  OD2   A ASP A 1 69  ? -3.474  -15.249 18.790  0.50 21.74 ? 69  ASP A OD2   1 
ATOM   1030  O  OD2   B ASP A 1 69  ? -3.291  -14.973 18.767  0.50 22.25 ? 69  ASP A OD2   1 
ATOM   1031  N  N     A LEU A 1 70  ? -4.320  -12.301 15.447  0.50 27.25 ? 70  LEU A N     1 
ATOM   1032  N  N     B LEU A 1 70  ? -4.117  -11.983 15.471  0.50 26.96 ? 70  LEU A N     1 
ATOM   1033  C  CA    A LEU A 1 70  ? -3.988  -12.214 14.030  0.50 25.08 ? 70  LEU A CA    1 
ATOM   1034  C  CA    B LEU A 1 70  ? -3.753  -11.774 14.077  0.50 24.61 ? 70  LEU A CA    1 
ATOM   1035  C  C     A LEU A 1 70  ? -3.603  -13.563 13.437  0.50 26.00 ? 70  LEU A C     1 
ATOM   1036  C  C     B LEU A 1 70  ? -3.309  -13.057 13.381  0.50 27.68 ? 70  LEU A C     1 
ATOM   1037  O  O     A LEU A 1 70  ? -3.671  -13.731 12.215  0.50 29.45 ? 70  LEU A O     1 
ATOM   1038  O  O     B LEU A 1 70  ? -2.965  -13.015 12.195  0.50 26.05 ? 70  LEU A O     1 
ATOM   1039  C  CB    A LEU A 1 70  ? -2.870  -11.192 13.818  0.50 22.12 ? 70  LEU A CB    1 
ATOM   1040  C  CB    B LEU A 1 70  ? -2.669  -10.695 13.980  0.50 21.87 ? 70  LEU A CB    1 
ATOM   1041  C  CG    A LEU A 1 70  ? -3.307  -9.742  14.036  0.50 26.67 ? 70  LEU A CG    1 
ATOM   1042  C  CG    B LEU A 1 70  ? -3.169  -9.324  14.454  0.50 27.13 ? 70  LEU A CG    1 
ATOM   1043  C  CD1   A LEU A 1 70  ? -2.146  -8.785  13.865  0.50 27.30 ? 70  LEU A CD1   1 
ATOM   1044  C  CD1   B LEU A 1 70  ? -2.131  -8.223  14.266  0.50 26.37 ? 70  LEU A CD1   1 
ATOM   1045  C  CD2   A LEU A 1 70  ? -4.455  -9.373  13.092  0.50 29.21 ? 70  LEU A CD2   1 
ATOM   1046  C  CD2   B LEU A 1 70  ? -4.476  -8.951  13.756  0.50 25.93 ? 70  LEU A CD2   1 
ATOM   1047  N  N     A GLU A 1 71  ? -3.200  -14.518 14.262  0.50 25.89 ? 71  GLU A N     1 
ATOM   1048  N  N     B GLU A 1 71  ? -3.310  -14.187 14.085  0.50 25.17 ? 71  GLU A N     1 
ATOM   1049  C  CA    A GLU A 1 71  ? -3.026  -15.899 13.848  0.50 28.81 ? 71  GLU A CA    1 
ATOM   1050  C  CA    B GLU A 1 71  ? -3.124  -15.506 13.495  0.50 27.38 ? 71  GLU A CA    1 
ATOM   1051  C  C     A GLU A 1 71  ? -4.101  -16.772 14.490  0.50 26.64 ? 71  GLU A C     1 
ATOM   1052  C  C     B GLU A 1 71  ? -3.884  -16.510 14.351  0.50 26.00 ? 71  GLU A C     1 
ATOM   1053  O  O     A GLU A 1 71  ? -4.682  -16.402 15.517  0.50 30.94 ? 71  GLU A O     1 
ATOM   1054  O  O     B GLU A 1 71  ? -3.987  -16.324 15.569  0.50 31.44 ? 71  GLU A O     1 
ATOM   1055  C  CB    A GLU A 1 71  ? -1.628  -16.406 14.226  0.50 26.43 ? 71  GLU A CB    1 
ATOM   1056  C  CB    B GLU A 1 71  ? -1.638  -15.881 13.390  0.50 24.06 ? 71  GLU A CB    1 
ATOM   1057  C  CG    A GLU A 1 71  ? -1.340  -16.386 15.710  0.50 27.91 ? 71  GLU A CG    1 
ATOM   1058  C  CG    B GLU A 1 71  ? -0.876  -15.830 14.701  0.50 25.78 ? 71  GLU A CG    1 
ATOM   1059  C  CD    A GLU A 1 71  ? -1.135  -17.776 16.272  0.50 27.09 ? 71  GLU A CD    1 
ATOM   1060  C  CD    B GLU A 1 71  ? -0.757  -17.187 15.353  0.50 27.12 ? 71  GLU A CD    1 
ATOM   1061  O  OE1   A GLU A 1 71  ? -1.179  -18.741 15.482  0.50 24.44 ? 71  GLU A OE1   1 
ATOM   1062  O  OE1   B GLU A 1 71  ? -1.352  -18.144 14.820  0.50 23.37 ? 71  GLU A OE1   1 
ATOM   1063  O  OE2   A GLU A 1 71  ? -0.943  -17.902 17.502  0.50 31.10 ? 71  GLU A OE2   1 
ATOM   1064  O  OE2   B GLU A 1 71  ? -0.063  -17.296 16.387  0.50 23.52 ? 71  GLU A OE2   1 
ATOM   1065  N  N     A PRO A 1 72  ? -4.413  -17.939 13.904  0.50 26.94 ? 72  PRO A N     1 
ATOM   1066  N  N     B PRO A 1 72  ? -4.427  -17.582 13.751  0.50 25.27 ? 72  PRO A N     1 
ATOM   1067  C  CA    A PRO A 1 72  ? -5.589  -18.692 14.369  0.50 28.84 ? 72  PRO A CA    1 
ATOM   1068  C  CA    B PRO A 1 72  ? -5.464  -18.363 14.443  0.50 29.29 ? 72  PRO A CA    1 
ATOM   1069  C  C     A PRO A 1 72  ? -5.312  -19.681 15.490  0.50 31.20 ? 72  PRO A C     1 
ATOM   1070  C  C     B PRO A 1 72  ? -4.976  -19.575 15.223  0.50 30.90 ? 72  PRO A C     1 
ATOM   1071  O  O     A PRO A 1 72  ? -6.229  -20.030 16.239  0.50 31.05 ? 72  PRO A O     1 
ATOM   1072  O  O     B PRO A 1 72  ? -5.774  -20.481 15.483  0.50 36.92 ? 72  PRO A O     1 
ATOM   1073  C  CB    A PRO A 1 72  ? -6.037  -19.429 13.105  0.50 28.02 ? 72  PRO A CB    1 
ATOM   1074  C  CB    B PRO A 1 72  ? -6.373  -18.802 13.291  0.50 27.69 ? 72  PRO A CB    1 
ATOM   1075  C  CG    A PRO A 1 72  ? -4.738  -19.725 12.410  0.50 30.79 ? 72  PRO A CG    1 
ATOM   1076  C  CG    B PRO A 1 72  ? -5.423  -18.982 12.145  0.50 34.30 ? 72  PRO A CG    1 
ATOM   1077  C  CD    A PRO A 1 72  ? -3.845  -18.527 12.675  0.50 27.93 ? 72  PRO A CD    1 
ATOM   1078  C  CD    B PRO A 1 72  ? -4.277  -18.005 12.347  0.50 28.21 ? 72  PRO A CD    1 
ATOM   1079  N  N     A THR A 1 73  ? -4.054  -20.123 15.614  0.50 29.18 ? 73  THR A N     1 
ATOM   1080  N  N     B THR A 1 73  ? -3.697  -19.622 15.605  0.50 29.23 ? 73  THR A N     1 
ATOM   1081  C  CA    A THR A 1 73  ? -3.736  -21.333 16.373  0.50 30.76 ? 73  THR A CA    1 
ATOM   1082  C  CA    B THR A 1 73  ? -3.192  -20.794 16.320  0.50 32.22 ? 73  THR A CA    1 
ATOM   1083  C  C     A THR A 1 73  ? -4.244  -21.273 17.812  0.50 32.56 ? 73  THR A C     1 
ATOM   1084  C  C     B THR A 1 73  ? -3.861  -20.954 17.682  0.50 31.29 ? 73  THR A C     1 
ATOM   1085  O  O     A THR A 1 73  ? -4.811  -22.250 18.317  0.50 32.61 ? 73  THR A O     1 
ATOM   1086  O  O     B THR A 1 73  ? -4.261  -22.061 18.060  0.50 35.57 ? 73  THR A O     1 
ATOM   1087  C  CB    A THR A 1 73  ? -2.225  -21.568 16.348  0.50 33.16 ? 73  THR A CB    1 
ATOM   1088  C  CB    B THR A 1 73  ? -1.673  -20.705 16.485  0.50 26.76 ? 73  THR A CB    1 
ATOM   1089  O  OG1   A THR A 1 73  ? -1.787  -21.692 14.989  0.50 38.08 ? 73  THR A OG1   1 
ATOM   1090  O  OG1   B THR A 1 73  ? -1.049  -20.792 15.198  0.50 39.93 ? 73  THR A OG1   1 
ATOM   1091  C  CG2   A THR A 1 73  ? -1.860  -22.827 17.113  0.50 36.46 ? 73  THR A CG2   1 
ATOM   1092  C  CG2   B THR A 1 73  ? -1.161  -21.826 17.374  0.50 34.01 ? 73  THR A CG2   1 
ATOM   1093  N  N     A VAL A 1 74  ? -4.055  -20.138 18.488  0.50 30.37 ? 74  VAL A N     1 
ATOM   1094  N  N     B VAL A 1 74  ? -4.001  -19.864 18.430  0.50 30.79 ? 74  VAL A N     1 
ATOM   1095  C  CA    A VAL A 1 74  ? -4.412  -20.057 19.900  0.50 27.68 ? 74  VAL A CA    1 
ATOM   1096  C  CA    B VAL A 1 74  ? -4.464  -19.954 19.810  0.50 27.64 ? 74  VAL A CA    1 
ATOM   1097  C  C     A VAL A 1 74  ? -5.926  -20.041 20.073  0.50 29.59 ? 74  VAL A C     1 
ATOM   1098  C  C     B VAL A 1 74  ? -5.984  -19.986 19.890  0.50 29.62 ? 74  VAL A C     1 
ATOM   1099  O  O     A VAL A 1 74  ? -6.474  -20.723 20.948  0.50 31.29 ? 74  VAL A O     1 
ATOM   1100  O  O     B VAL A 1 74  ? -6.553  -20.684 20.733  0.50 31.16 ? 74  VAL A O     1 
ATOM   1101  C  CB    A VAL A 1 74  ? -3.755  -18.824 20.543  0.50 29.68 ? 74  VAL A CB    1 
ATOM   1102  C  CB    B VAL A 1 74  ? -3.885  -18.786 20.628  0.50 29.43 ? 74  VAL A CB    1 
ATOM   1103  C  CG1   A VAL A 1 74  ? -4.060  -18.778 22.023  0.50 28.44 ? 74  VAL A CG1   1 
ATOM   1104  C  CG1   B VAL A 1 74  ? -4.060  -19.046 22.107  0.50 28.54 ? 74  VAL A CG1   1 
ATOM   1105  C  CG2   A VAL A 1 74  ? -2.251  -18.841 20.303  0.50 29.13 ? 74  VAL A CG2   1 
ATOM   1106  C  CG2   B VAL A 1 74  ? -2.416  -18.575 20.283  0.50 29.27 ? 74  VAL A CG2   1 
ATOM   1107  N  N     A ILE A 1 75  ? -6.624  -19.264 19.245  0.50 28.55 ? 75  ILE A N     1 
ATOM   1108  N  N     B ILE A 1 75  ? -6.661  -19.229 19.023  0.50 28.95 ? 75  ILE A N     1 
ATOM   1109  C  CA    A ILE A 1 75  ? -8.077  -19.195 19.344  0.50 33.38 ? 75  ILE A CA    1 
ATOM   1110  C  CA    B ILE A 1 75  ? -8.117  -19.219 19.018  0.50 33.82 ? 75  ILE A CA    1 
ATOM   1111  C  C     A ILE A 1 75  ? -8.719  -20.472 18.814  0.50 37.41 ? 75  ILE A C     1 
ATOM   1112  C  C     B ILE A 1 75  ? -8.677  -20.554 18.542  0.50 37.32 ? 75  ILE A C     1 
ATOM   1113  O  O     A ILE A 1 75  ? -9.785  -20.882 19.292  0.50 31.88 ? 75  ILE A O     1 
ATOM   1114  O  O     B ILE A 1 75  ? -9.803  -20.920 18.903  0.50 30.69 ? 75  ILE A O     1 
ATOM   1115  C  CB    A ILE A 1 75  ? -8.577  -17.929 18.623  0.50 29.67 ? 75  ILE A CB    1 
ATOM   1116  C  CB    B ILE A 1 75  ? -8.609  -18.028 18.174  0.50 26.84 ? 75  ILE A CB    1 
ATOM   1117  C  CG1   A ILE A 1 75  ? -8.301  -16.706 19.504  0.50 22.02 ? 75  ILE A CG1   1 
ATOM   1118  C  CG1   B ILE A 1 75  ? -8.233  -16.718 18.874  0.50 26.53 ? 75  ILE A CG1   1 
ATOM   1119  C  CG2   A ILE A 1 75  ? -10.050 -18.036 18.251  0.50 33.37 ? 75  ILE A CG2   1 
ATOM   1120  C  CG2   B ILE A 1 75  ? -10.107 -18.095 17.940  0.50 32.02 ? 75  ILE A CG2   1 
ATOM   1121  C  CD1   A ILE A 1 75  ? -8.866  -15.407 18.976  0.50 22.86 ? 75  ILE A CD1   1 
ATOM   1122  C  CD1   B ILE A 1 75  ? -8.833  -15.479 18.249  0.50 28.70 ? 75  ILE A CD1   1 
ATOM   1123  N  N     A ASP A 1 76  ? -8.074  -21.147 17.857  0.50 30.12 ? 76  ASP A N     1 
ATOM   1124  N  N     B ASP A 1 76  ? -7.904  -21.315 17.764  0.50 30.64 ? 76  ASP A N     1 
ATOM   1125  C  CA    A ASP A 1 76  ? -8.593  -22.432 17.391  0.50 34.67 ? 76  ASP A CA    1 
ATOM   1126  C  CA    B ASP A 1 76  ? -8.323  -22.668 17.415  0.50 35.04 ? 76  ASP A CA    1 
ATOM   1127  C  C     A ASP A 1 76  ? -8.672  -23.450 18.522  0.50 39.32 ? 76  ASP A C     1 
ATOM   1128  C  C     B ASP A 1 76  ? -8.364  -23.579 18.637  0.50 38.65 ? 76  ASP A C     1 
ATOM   1129  O  O     A ASP A 1 76  ? -9.517  -24.352 18.488  0.50 38.76 ? 76  ASP A O     1 
ATOM   1130  O  O     B ASP A 1 76  ? -9.165  -24.521 18.680  0.50 37.90 ? 76  ASP A O     1 
ATOM   1131  C  CB    A ASP A 1 76  ? -7.732  -22.973 16.250  0.50 38.38 ? 76  ASP A CB    1 
ATOM   1132  C  CB    B ASP A 1 76  ? -7.400  -23.249 16.342  0.50 37.39 ? 76  ASP A CB    1 
ATOM   1133  C  CG    A ASP A 1 76  ? -8.045  -22.314 14.920  0.50 36.54 ? 76  ASP A CG    1 
ATOM   1134  C  CG    B ASP A 1 76  ? -7.771  -22.790 14.944  0.50 35.94 ? 76  ASP A CG    1 
ATOM   1135  O  OD1   A ASP A 1 76  ? -9.166  -21.785 14.759  0.50 36.62 ? 76  ASP A OD1   1 
ATOM   1136  O  OD1   B ASP A 1 76  ? -8.651  -21.913 14.816  0.50 37.00 ? 76  ASP A OD1   1 
ATOM   1137  O  OD2   A ASP A 1 76  ? -7.171  -22.330 14.032  0.50 33.01 ? 76  ASP A OD2   1 
ATOM   1138  O  OD2   B ASP A 1 76  ? -7.190  -23.314 13.972  0.50 35.27 ? 76  ASP A OD2   1 
ATOM   1139  N  N     A GLU A 1 77  ? -7.805  -23.324 19.529  0.50 34.47 ? 77  GLU A N     1 
ATOM   1140  N  N     B GLU A 1 77  ? -7.520  -23.318 19.638  0.50 34.41 ? 77  GLU A N     1 
ATOM   1141  C  CA    A GLU A 1 77  ? -7.921  -24.167 20.712  0.50 38.07 ? 77  GLU A CA    1 
ATOM   1142  C  CA    B GLU A 1 77  ? -7.593  -24.068 20.886  0.50 38.27 ? 77  GLU A CA    1 
ATOM   1143  C  C     A GLU A 1 77  ? -9.162  -23.816 21.524  0.50 41.28 ? 77  GLU A C     1 
ATOM   1144  C  C     B GLU A 1 77  ? -8.845  -23.732 21.687  0.50 40.59 ? 77  GLU A C     1 
ATOM   1145  O  O     A GLU A 1 77  ? -9.778  -24.702 22.128  0.50 43.50 ? 77  GLU A O     1 
ATOM   1146  O  O     B GLU A 1 77  ? -9.293  -24.558 22.491  0.50 44.85 ? 77  GLU A O     1 
ATOM   1147  C  CB    A GLU A 1 77  ? -6.667  -24.031 21.575  0.50 39.61 ? 77  GLU A CB    1 
ATOM   1148  C  CB    B GLU A 1 77  ? -6.343  -23.807 21.730  0.50 39.10 ? 77  GLU A CB    1 
ATOM   1149  C  CG    A GLU A 1 77  ? -6.400  -25.211 22.492  0.50 41.12 ? 77  GLU A CG    1 
ATOM   1150  C  CG    B GLU A 1 77  ? -5.072  -24.428 21.168  0.50 38.36 ? 77  GLU A CG    1 
ATOM   1151  C  CD    A GLU A 1 77  ? -5.318  -26.130 21.955  0.50 45.81 ? 77  GLU A CD    1 
ATOM   1152  C  CD    B GLU A 1 77  ? -3.888  -24.286 22.104  0.50 44.72 ? 77  GLU A CD    1 
ATOM   1153  O  OE1   A GLU A 1 77  ? -4.882  -25.926 20.799  0.50 38.96 ? 77  GLU A OE1   1 
ATOM   1154  O  OE1   B GLU A 1 77  ? -3.679  -23.180 22.645  0.50 43.52 ? 77  GLU A OE1   1 
ATOM   1155  O  OE2   A GLU A 1 77  ? -4.896  -27.048 22.693  0.50 36.30 ? 77  GLU A OE2   1 
ATOM   1156  O  OE2   B GLU A 1 77  ? -3.167  -25.286 22.303  0.50 48.17 ? 77  GLU A OE2   1 
ATOM   1157  N  N     A VAL A 1 78  ? -9.543  -22.537 21.547  0.50 39.09 ? 78  VAL A N     1 
ATOM   1158  N  N     B VAL A 1 78  ? -9.414  -22.541 21.493  0.50 39.04 ? 78  VAL A N     1 
ATOM   1159  C  CA    A VAL A 1 78  ? -10.733 -22.119 22.283  0.50 39.13 ? 78  VAL A CA    1 
ATOM   1160  C  CA    B VAL A 1 78  ? -10.685 -22.212 22.130  0.50 39.25 ? 78  VAL A CA    1 
ATOM   1161  C  C     A VAL A 1 78  ? -12.005 -22.498 21.532  0.50 39.06 ? 78  VAL A C     1 
ATOM   1162  C  C     B VAL A 1 78  ? -11.850 -22.780 21.325  0.50 40.05 ? 78  VAL A C     1 
ATOM   1163  O  O     A VAL A 1 78  ? -13.014 -22.850 22.153  0.50 43.57 ? 78  VAL A O     1 
ATOM   1164  O  O     B VAL A 1 78  ? -12.870 -23.179 21.898  0.50 44.92 ? 78  VAL A O     1 
ATOM   1165  C  CB    A VAL A 1 78  ? -10.669 -20.607 22.563  0.50 32.67 ? 78  VAL A CB    1 
ATOM   1166  C  CB    B VAL A 1 78  ? -10.802 -20.688 22.318  0.50 33.40 ? 78  VAL A CB    1 
ATOM   1167  C  CG1   A VAL A 1 78  ? -11.900 -20.147 23.328  0.50 41.44 ? 78  VAL A CG1   1 
ATOM   1168  C  CG1   B VAL A 1 78  ? -12.170 -20.305 22.875  0.50 42.21 ? 78  VAL A CG1   1 
ATOM   1169  C  CG2   A VAL A 1 78  ? -9.402  -20.268 23.330  0.50 27.88 ? 78  VAL A CG2   1 
ATOM   1170  C  CG2   B VAL A 1 78  ? -9.699  -20.185 23.231  0.50 28.46 ? 78  VAL A CG2   1 
ATOM   1171  N  N     A ARG A 1 79  ? -11.976 -22.447 20.197  0.50 38.59 ? 79  ARG A N     1 
ATOM   1172  N  N     B ARG A 1 79  ? -11.715 -22.841 19.996  0.50 40.18 ? 79  ARG A N     1 
ATOM   1173  C  CA    A ARG A 1 79  ? -13.129 -22.834 19.392  0.50 39.58 ? 79  ARG A CA    1 
ATOM   1174  C  CA    B ARG A 1 79  ? -12.738 -23.463 19.161  0.50 39.85 ? 79  ARG A CA    1 
ATOM   1175  C  C     A ARG A 1 79  ? -13.461 -24.314 19.516  0.50 46.55 ? 79  ARG A C     1 
ATOM   1176  C  C     B ARG A 1 79  ? -12.877 -24.953 19.448  0.50 47.68 ? 79  ARG A C     1 
ATOM   1177  O  O     A ARG A 1 79  ? -14.583 -24.712 19.186  0.50 47.64 ? 79  ARG A O     1 
ATOM   1178  O  O     B ARG A 1 79  ? -13.961 -25.520 19.266  0.50 47.99 ? 79  ARG A O     1 
ATOM   1179  C  CB    A ARG A 1 79  ? -12.881 -22.497 17.919  0.50 37.25 ? 79  ARG A CB    1 
ATOM   1180  C  CB    B ARG A 1 79  ? -12.413 -23.250 17.681  0.50 40.22 ? 79  ARG A CB    1 
ATOM   1181  C  CG    A ARG A 1 79  ? -12.881 -21.012 17.592  0.50 36.74 ? 79  ARG A CG    1 
ATOM   1182  C  CG    B ARG A 1 79  ? -12.576 -21.824 17.185  0.50 37.47 ? 79  ARG A CG    1 
ATOM   1183  C  CD    A ARG A 1 79  ? -12.191 -20.751 16.261  0.50 32.63 ? 79  ARG A CD    1 
ATOM   1184  C  CD    B ARG A 1 79  ? -11.848 -21.619 15.863  0.50 36.24 ? 79  ARG A CD    1 
ATOM   1185  N  NE    A ARG A 1 79  ? -12.492 -19.426 15.730  0.50 35.99 ? 79  ARG A NE    1 
ATOM   1186  N  NE    B ARG A 1 79  ? -12.184 -20.344 15.241  0.50 33.15 ? 79  ARG A NE    1 
ATOM   1187  C  CZ    A ARG A 1 79  ? -11.642 -18.693 15.022  0.50 33.56 ? 79  ARG A CZ    1 
ATOM   1188  C  CZ    B ARG A 1 79  ? -11.427 -19.720 14.347  0.50 37.33 ? 79  ARG A CZ    1 
ATOM   1189  N  NH1   A ARG A 1 79  ? -10.407 -19.106 14.783  0.50 28.28 ? 79  ARG A NH1   1 
ATOM   1190  N  NH1   B ARG A 1 79  ? -10.260 -20.214 13.962  0.50 31.88 ? 79  ARG A NH1   1 
ATOM   1191  N  NH2   A ARG A 1 79  ? -12.038 -17.513 14.551  0.50 28.56 ? 79  ARG A NH2   1 
ATOM   1192  N  NH2   B ARG A 1 79  ? -11.847 -18.566 13.834  0.50 35.40 ? 79  ARG A NH2   1 
ATOM   1193  N  N     A THR A 1 80  ? -12.513 -25.139 19.968  0.50 47.39 ? 80  THR A N     1 
ATOM   1194  N  N     B THR A 1 80  ? -11.797 -25.607 19.881  0.50 46.46 ? 80  THR A N     1 
ATOM   1195  C  CA    A THR A 1 80  ? -12.703 -26.584 20.013  0.50 47.05 ? 80  THR A CA    1 
ATOM   1196  C  CA    B THR A 1 80  ? -11.797 -27.048 20.112  0.50 44.70 ? 80  THR A CA    1 
ATOM   1197  C  C     A THR A 1 80  ? -12.402 -27.180 21.383  0.50 44.49 ? 80  THR A C     1 
ATOM   1198  C  C     B THR A 1 80  ? -11.552 -27.403 21.576  0.50 44.70 ? 80  THR A C     1 
ATOM   1199  O  O     A THR A 1 80  ? -12.315 -28.407 21.503  0.50 46.79 ? 80  THR A O     1 
ATOM   1200  O  O     B THR A 1 80  ? -11.170 -28.538 21.876  0.50 51.26 ? 80  THR A O     1 
ATOM   1201  C  CB    A THR A 1 80  ? -11.833 -27.273 18.954  0.50 43.81 ? 80  THR A CB    1 
ATOM   1202  C  CB    B THR A 1 80  ? -10.750 -27.733 19.230  0.50 50.55 ? 80  THR A CB    1 
ATOM   1203  O  OG1   A THR A 1 80  ? -10.458 -26.922 19.160  0.50 49.92 ? 80  THR A OG1   1 
ATOM   1204  O  OG1   B THR A 1 80  ? -9.437  -27.453 19.736  0.50 41.54 ? 80  THR A OG1   1 
ATOM   1205  C  CG2   A THR A 1 80  ? -12.254 -26.851 17.555  0.50 51.01 ? 80  THR A CG2   1 
ATOM   1206  C  CG2   B THR A 1 80  ? -10.849 -27.236 17.794  0.50 46.40 ? 80  THR A CG2   1 
ATOM   1207  N  N     A GLY A 1 81  ? -12.239 -26.356 22.415  0.50 43.83 ? 81  GLY A N     1 
ATOM   1208  N  N     B GLY A 1 81  ? -11.763 -26.462 22.494  0.50 42.18 ? 81  GLY A N     1 
ATOM   1209  C  CA    A GLY A 1 81  ? -11.942 -26.841 23.750  0.50 48.25 ? 81  GLY A CA    1 
ATOM   1210  C  CA    B GLY A 1 81  ? -11.488 -26.680 23.898  0.50 47.74 ? 81  GLY A CA    1 
ATOM   1211  C  C     A GLY A 1 81  ? -13.176 -27.289 24.504  0.50 47.13 ? 81  GLY A C     1 
ATOM   1212  C  C     B GLY A 1 81  ? -12.681 -27.236 24.655  0.50 46.87 ? 81  GLY A C     1 
ATOM   1213  O  O     A GLY A 1 81  ? -14.185 -27.697 23.916  0.50 47.56 ? 81  GLY A O     1 
ATOM   1214  O  O     B GLY A 1 81  ? -13.682 -27.668 24.081  0.50 48.42 ? 81  GLY A O     1 
ATOM   1215  N  N     A THR A 1 82  ? -13.095 -27.211 25.835  0.50 47.34 ? 82  THR A N     1 
ATOM   1216  N  N     B THR A 1 82  ? -12.555 -27.222 25.985  0.50 47.04 ? 82  THR A N     1 
ATOM   1217  C  CA    A THR A 1 82  ? -14.219 -27.613 26.675  0.50 47.82 ? 82  THR A CA    1 
ATOM   1218  C  CA    B THR A 1 82  ? -13.648 -27.677 26.839  0.50 47.97 ? 82  THR A CA    1 
ATOM   1219  C  C     A THR A 1 82  ? -15.368 -26.617 26.572  0.50 51.34 ? 82  THR A C     1 
ATOM   1220  C  C     B THR A 1 82  ? -14.879 -26.796 26.673  0.50 50.77 ? 82  THR A C     1 
ATOM   1221  O  O     A THR A 1 82  ? -16.513 -26.999 26.303  0.50 50.82 ? 82  THR A O     1 
ATOM   1222  O  O     B THR A 1 82  ? -16.005 -27.299 26.572  0.50 50.32 ? 82  THR A O     1 
ATOM   1223  C  CB    A THR A 1 82  ? -13.767 -27.755 28.129  0.50 47.68 ? 82  THR A CB    1 
ATOM   1224  C  CB    B THR A 1 82  ? -13.199 -27.703 28.303  0.50 47.17 ? 82  THR A CB    1 
ATOM   1225  O  OG1   A THR A 1 82  ? -12.828 -28.832 28.239  0.50 45.78 ? 82  THR A OG1   1 
ATOM   1226  O  OG1   B THR A 1 82  ? -12.320 -28.813 28.520  0.50 46.46 ? 82  THR A OG1   1 
ATOM   1227  C  CG2   A THR A 1 82  ? -14.960 -28.029 29.035  0.50 47.94 ? 82  THR A CG2   1 
ATOM   1228  C  CG2   B THR A 1 82  ? -14.396 -27.824 29.237  0.50 48.63 ? 82  THR A CG2   1 
ATOM   1229  N  N     A TYR A 1 83  ? -15.081 -25.335 26.787  0.50 45.67 ? 83  TYR A N     1 
ATOM   1230  N  N     B TYR A 1 83  ? -14.686 -25.482 26.633  0.50 46.32 ? 83  TYR A N     1 
ATOM   1231  C  CA    A TYR A 1 83  ? -16.099 -24.286 26.753  0.50 43.63 ? 83  TYR A CA    1 
ATOM   1232  C  CA    B TYR A 1 83  ? -15.783 -24.523 26.497  0.50 41.85 ? 83  TYR A CA    1 
ATOM   1233  C  C     A TYR A 1 83  ? -16.324 -23.740 25.353  0.50 45.00 ? 83  TYR A C     1 
ATOM   1234  C  C     B TYR A 1 83  ? -15.941 -24.066 25.051  0.50 44.70 ? 83  TYR A C     1 
ATOM   1235  O  O     A TYR A 1 83  ? -16.569 -22.543 25.174  0.50 46.22 ? 83  TYR A O     1 
ATOM   1236  O  O     B TYR A 1 83  ? -16.003 -22.875 24.748  0.50 45.26 ? 83  TYR A O     1 
ATOM   1237  C  CB    A TYR A 1 83  ? -15.714 -23.172 27.721  0.50 45.15 ? 83  TYR A CB    1 
ATOM   1238  C  CB    B TYR A 1 83  ? -15.558 -23.339 27.431  0.50 45.85 ? 83  TYR A CB    1 
ATOM   1239  C  CG    A TYR A 1 83  ? -15.835 -23.582 29.169  0.50 41.05 ? 83  TYR A CG    1 
ATOM   1240  C  CG    B TYR A 1 83  ? -15.628 -23.713 28.896  0.50 40.64 ? 83  TYR A CG    1 
ATOM   1241  C  CD1   A TYR A 1 83  ? -14.773 -24.177 29.835  0.50 42.90 ? 83  TYR A CD1   1 
ATOM   1242  C  CD1   B TYR A 1 83  ? -14.540 -24.286 29.540  0.50 43.85 ? 83  TYR A CD1   1 
ATOM   1243  C  CD2   A TYR A 1 83  ? -17.021 -23.391 29.865  0.50 42.51 ? 83  TYR A CD2   1 
ATOM   1244  C  CD2   B TYR A 1 83  ? -16.786 -23.502 29.631  0.50 43.70 ? 83  TYR A CD2   1 
ATOM   1245  C  CE1   A TYR A 1 83  ? -14.886 -24.562 31.158  0.50 40.09 ? 83  TYR A CE1   1 
ATOM   1246  C  CE1   B TYR A 1 83  ? -14.603 -24.637 30.873  0.50 41.09 ? 83  TYR A CE1   1 
ATOM   1247  C  CE2   A TYR A 1 83  ? -17.144 -23.771 31.185  0.50 37.83 ? 83  TYR A CE2   1 
ATOM   1248  C  CE2   B TYR A 1 83  ? -16.857 -23.847 30.967  0.50 37.99 ? 83  TYR A CE2   1 
ATOM   1249  C  CZ    A TYR A 1 83  ? -16.074 -24.354 31.829  0.50 42.99 ? 83  TYR A CZ    1 
ATOM   1250  C  CZ    B TYR A 1 83  ? -15.760 -24.413 31.583  0.50 41.82 ? 83  TYR A CZ    1 
ATOM   1251  O  OH    A TYR A 1 83  ? -16.197 -24.732 33.149  0.50 43.86 ? 83  TYR A OH    1 
ATOM   1252  O  OH    B TYR A 1 83  ? -15.824 -24.759 32.916  0.50 46.48 ? 83  TYR A OH    1 
ATOM   1253  N  N     A ARG A 1 84  ? -16.253 -24.607 24.341  0.50 45.44 ? 84  ARG A N     1 
ATOM   1254  N  N     B ARG A 1 84  ? -16.015 -25.034 24.135  0.50 43.95 ? 84  ARG A N     1 
ATOM   1255  C  CA    A ARG A 1 84  ? -16.468 -24.169 22.967  0.50 39.71 ? 84  ARG A CA    1 
ATOM   1256  C  CA    B ARG A 1 84  ? -16.147 -24.716 22.718  0.50 40.64 ? 84  ARG A CA    1 
ATOM   1257  C  C     A ARG A 1 84  ? -17.903 -23.698 22.751  0.50 40.55 ? 84  ARG A C     1 
ATOM   1258  C  C     B ARG A 1 84  ? -17.550 -24.234 22.361  0.50 41.83 ? 84  ARG A C     1 
ATOM   1259  O  O     A ARG A 1 84  ? -18.135 -22.684 22.083  0.50 39.12 ? 84  ARG A O     1 
ATOM   1260  O  O     B ARG A 1 84  ? -17.709 -23.446 21.422  0.50 38.79 ? 84  ARG A O     1 
ATOM   1261  C  CB    A ARG A 1 84  ? -16.096 -25.302 22.006  0.50 45.22 ? 84  ARG A CB    1 
ATOM   1262  C  CB    B ARG A 1 84  ? -15.784 -25.939 21.879  0.50 46.45 ? 84  ARG A CB    1 
ATOM   1263  C  CG    A ARG A 1 84  ? -17.212 -25.811 21.105  0.50 44.19 ? 84  ARG A CG    1 
ATOM   1264  C  CG    B ARG A 1 84  ? -16.670 -27.141 22.138  0.50 46.02 ? 84  ARG A CG    1 
ATOM   1265  C  CD    A ARG A 1 84  ? -16.924 -27.236 20.661  0.50 45.84 ? 84  ARG A CD    1 
ATOM   1266  C  CD    B ARG A 1 84  ? -16.135 -28.385 21.464  0.50 50.02 ? 84  ARG A CD    1 
ATOM   1267  N  NE    A ARG A 1 84  ? -16.761 -28.123 21.807  0.50 49.27 ? 84  ARG A NE    1 
ATOM   1268  N  NE    B ARG A 1 84  ? -17.027 -29.523 21.652  0.50 51.59 ? 84  ARG A NE    1 
ATOM   1269  C  CZ    A ARG A 1 84  ? -16.367 -29.387 21.731  0.50 54.10 ? 84  ARG A CZ    1 
ATOM   1270  C  CZ    B ARG A 1 84  ? -16.714 -30.776 21.354  0.50 60.45 ? 84  ARG A CZ    1 
ATOM   1271  N  NH1   A ARG A 1 84  ? -16.073 -29.951 20.570  0.50 55.66 ? 84  ARG A NH1   1 
ATOM   1272  N  NH1   B ARG A 1 84  ? -15.527 -31.094 20.863  0.50 55.35 ? 84  ARG A NH1   1 
ATOM   1273  N  NH2   A ARG A 1 84  ? -16.259 -30.101 22.848  0.50 49.79 ? 84  ARG A NH2   1 
ATOM   1274  N  NH2   B ARG A 1 84  ? -17.613 -31.735 21.557  0.50 61.04 ? 84  ARG A NH2   1 
ATOM   1275  N  N     A GLN A 1 85  ? -18.881 -24.399 23.330  0.50 42.02 ? 85  GLN A N     1 
ATOM   1276  N  N     B GLN A 1 85  ? -18.574 -24.700 23.074  0.50 43.40 ? 85  GLN A N     1 
ATOM   1277  C  CA    A GLN A 1 85  ? -20.275 -24.013 23.130  0.50 36.79 ? 85  GLN A CA    1 
ATOM   1278  C  CA    B GLN A 1 85  ? -19.946 -24.289 22.804  0.50 38.72 ? 85  GLN A CA    1 
ATOM   1279  C  C     A GLN A 1 85  ? -20.671 -22.781 23.930  0.50 34.52 ? 85  GLN A C     1 
ATOM   1280  C  C     B GLN A 1 85  ? -20.394 -23.128 23.676  0.50 35.42 ? 85  GLN A C     1 
ATOM   1281  O  O     A GLN A 1 85  ? -21.846 -22.408 23.909  0.50 37.75 ? 85  GLN A O     1 
ATOM   1282  O  O     B GLN A 1 85  ? -21.533 -22.672 23.539  0.50 36.20 ? 85  GLN A O     1 
ATOM   1283  C  CB    A GLN A 1 85  ? -21.209 -25.173 23.494  0.50 45.54 ? 85  GLN A CB    1 
ATOM   1284  C  CB    B GLN A 1 85  ? -20.908 -25.469 22.992  0.50 44.39 ? 85  GLN A CB    1 
ATOM   1285  C  CG    A GLN A 1 85  ? -20.851 -26.505 22.851  0.50 44.02 ? 85  GLN A CG    1 
ATOM   1286  C  CG    B GLN A 1 85  ? -20.667 -26.635 22.048  0.50 47.20 ? 85  GLN A CG    1 
ATOM   1287  C  CD    A GLN A 1 85  ? -21.352 -27.693 23.659  0.50 50.58 ? 85  GLN A CD    1 
ATOM   1288  C  CD    B GLN A 1 85  ? -21.639 -27.776 22.277  0.50 47.65 ? 85  GLN A CD    1 
ATOM   1289  O  OE1   A GLN A 1 85  ? -20.699 -28.137 24.606  0.50 46.49 ? 85  GLN A OE1   1 
ATOM   1290  O  OE1   B GLN A 1 85  ? -22.593 -27.649 23.044  0.50 51.40 ? 85  GLN A OE1   1 
ATOM   1291  N  NE2   A GLN A 1 85  ? -22.515 -28.213 23.285  0.50 51.30 ? 85  GLN A NE2   1 
ATOM   1292  N  NE2   B GLN A 1 85  ? -21.398 -28.901 21.614  0.50 52.89 ? 85  GLN A NE2   1 
ATOM   1293  N  N     A LEU A 1 86  ? -19.728 -22.134 24.614  0.50 37.97 ? 86  LEU A N     1 
ATOM   1294  N  N     B LEU A 1 86  ? -19.529 -22.638 24.563  0.50 39.06 ? 86  LEU A N     1 
ATOM   1295  C  CA    A LEU A 1 86  ? -20.038 -21.039 25.525  0.50 32.57 ? 86  LEU A CA    1 
ATOM   1296  C  CA    B LEU A 1 86  ? -19.902 -21.513 25.412  0.50 33.70 ? 86  LEU A CA    1 
ATOM   1297  C  C     A LEU A 1 86  ? -20.076 -19.684 24.823  0.50 30.46 ? 86  LEU A C     1 
ATOM   1298  C  C     B LEU A 1 86  ? -19.952 -20.214 24.617  0.50 30.10 ? 86  LEU A C     1 
ATOM   1299  O  O     A LEU A 1 86  ? -21.010 -18.904 25.033  0.50 27.09 ? 86  LEU A O     1 
ATOM   1300  O  O     B LEU A 1 86  ? -20.865 -19.401 24.806  0.50 27.67 ? 86  LEU A O     1 
ATOM   1301  C  CB    A LEU A 1 86  ? -19.014 -21.016 26.664  0.50 29.64 ? 86  LEU A CB    1 
ATOM   1302  C  CB    B LEU A 1 86  ? -18.917 -21.395 26.575  0.50 30.73 ? 86  LEU A CB    1 
ATOM   1303  C  CG    A LEU A 1 86  ? -19.257 -20.089 27.854  0.50 30.78 ? 86  LEU A CG    1 
ATOM   1304  C  CG    B LEU A 1 86  ? -19.334 -20.580 27.797  0.50 30.60 ? 86  LEU A CG    1 
ATOM   1305  C  CD1   A LEU A 1 86  ? -20.311 -20.671 28.789  0.50 35.54 ? 86  LEU A CD1   1 
ATOM   1306  C  CD1   B LEU A 1 86  ? -20.362 -21.343 28.626  0.50 33.92 ? 86  LEU A CD1   1 
ATOM   1307  C  CD2   A LEU A 1 86  ? -17.956 -19.832 28.594  0.50 27.68 ? 86  LEU A CD2   1 
ATOM   1308  C  CD2   B LEU A 1 86  ? -18.118 -20.226 28.633  0.50 28.03 ? 86  LEU A CD2   1 
ATOM   1309  N  N     A PHE A 1 87  ? -19.078 -19.391 23.991  0.50 28.70 ? 87  PHE A N     1 
ATOM   1310  N  N     B PHE A 1 87  ? -18.991 -20.007 23.718  0.50 29.20 ? 87  PHE A N     1 
ATOM   1311  C  CA    A PHE A 1 87  ? -18.885 -18.058 23.438  0.50 27.31 ? 87  PHE A CA    1 
ATOM   1312  C  CA    B PHE A 1 87  ? -18.833 -18.736 23.020  0.50 33.46 ? 87  PHE A CA    1 
ATOM   1313  C  C     A PHE A 1 87  ? -19.673 -17.852 22.148  0.50 31.86 ? 87  PHE A C     1 
ATOM   1314  C  C     B PHE A 1 87  ? -19.582 -18.721 21.694  0.50 32.26 ? 87  PHE A C     1 
ATOM   1315  O  O     A PHE A 1 87  ? -20.056 -18.803 21.462  0.50 31.96 ? 87  PHE A O     1 
ATOM   1316  O  O     B PHE A 1 87  ? -19.628 -19.727 20.979  0.50 34.14 ? 87  PHE A O     1 
ATOM   1317  C  CB    A PHE A 1 87  ? -17.400 -17.803 23.163  0.50 33.33 ? 87  PHE A CB    1 
ATOM   1318  C  CB    B PHE A 1 87  ? -17.351 -18.446 22.765  0.50 28.07 ? 87  PHE A CB    1 
ATOM   1319  C  CG    A PHE A 1 87  ? -16.531 -17.933 24.374  0.50 30.51 ? 87  PHE A CG    1 
ATOM   1320  C  CG    B PHE A 1 87  ? -16.529 -18.370 24.014  0.50 30.83 ? 87  PHE A CG    1 
ATOM   1321  C  CD1   A PHE A 1 87  ? -16.437 -16.897 25.287  0.50 29.80 ? 87  PHE A CD1   1 
ATOM   1322  C  CD1   B PHE A 1 87  ? -16.522 -17.219 24.784  0.50 29.65 ? 87  PHE A CD1   1 
ATOM   1323  C  CD2   A PHE A 1 87  ? -15.806 -19.092 24.603  0.50 31.89 ? 87  PHE A CD2   1 
ATOM   1324  C  CD2   B PHE A 1 87  ? -15.766 -19.452 24.425  0.50 31.98 ? 87  PHE A CD2   1 
ATOM   1325  C  CE1   A PHE A 1 87  ? -15.639 -17.017 26.411  0.50 29.67 ? 87  PHE A CE1   1 
ATOM   1326  C  CE1   B PHE A 1 87  ? -15.767 -17.149 25.941  0.50 30.64 ? 87  PHE A CE1   1 
ATOM   1327  C  CE2   A PHE A 1 87  ? -15.003 -19.216 25.722  0.50 33.31 ? 87  PHE A CE2   1 
ATOM   1328  C  CE2   B PHE A 1 87  ? -15.007 -19.387 25.579  0.50 33.52 ? 87  PHE A CE2   1 
ATOM   1329  C  CZ    A PHE A 1 87  ? -14.922 -18.179 26.628  0.50 27.80 ? 87  PHE A CZ    1 
ATOM   1330  C  CZ    B PHE A 1 87  ? -15.011 -18.236 26.340  0.50 28.29 ? 87  PHE A CZ    1 
ATOM   1331  N  N     A HIS A 1 88  ? -19.908 -16.574 21.822  0.50 27.55 ? 88  HIS A N     1 
ATOM   1332  N  N     B HIS A 1 88  ? -20.166 -17.570 21.374  0.50 30.52 ? 88  HIS A N     1 
ATOM   1333  C  CA    A HIS A 1 88  ? -20.399 -16.185 20.506  0.50 34.31 ? 88  HIS A CA    1 
ATOM   1334  C  CA    B HIS A 1 88  ? -20.646 -17.326 20.023  0.50 32.18 ? 88  HIS A CA    1 
ATOM   1335  C  C     A HIS A 1 88  ? -19.351 -16.553 19.461  0.50 31.00 ? 88  HIS A C     1 
ATOM   1336  C  C     B HIS A 1 88  ? -19.492 -17.512 19.042  0.50 32.33 ? 88  HIS A C     1 
ATOM   1337  O  O     A HIS A 1 88  ? -18.303 -15.898 19.391  0.50 32.72 ? 88  HIS A O     1 
ATOM   1338  O  O     B HIS A 1 88  ? -18.391 -17.000 19.287  0.50 30.89 ? 88  HIS A O     1 
ATOM   1339  C  CB    A HIS A 1 88  ? -20.673 -14.680 20.428  0.50 37.35 ? 88  HIS A CB    1 
ATOM   1340  C  CB    B HIS A 1 88  ? -21.205 -15.908 19.891  0.50 33.74 ? 88  HIS A CB    1 
ATOM   1341  C  CG    A HIS A 1 88  ? -21.865 -14.217 21.206  0.50 36.39 ? 88  HIS A CG    1 
ATOM   1342  C  CG    B HIS A 1 88  ? -22.456 -15.660 20.675  0.50 42.94 ? 88  HIS A CG    1 
ATOM   1343  N  ND1   A HIS A 1 88  ? -23.149 -14.636 20.928  0.50 40.26 ? 88  HIS A ND1   1 
ATOM   1344  N  ND1   B HIS A 1 88  ? -22.738 -14.440 21.252  0.50 40.35 ? 88  HIS A ND1   1 
ATOM   1345  C  CD2   A HIS A 1 88  ? -21.971 -13.333 22.226  0.50 36.28 ? 88  HIS A CD2   1 
ATOM   1346  C  CD2   B HIS A 1 88  ? -23.511 -16.462 20.957  0.50 38.48 ? 88  HIS A CD2   1 
ATOM   1347  C  CE1   A HIS A 1 88  ? -23.990 -14.049 21.761  0.50 44.12 ? 88  HIS A CE1   1 
ATOM   1348  C  CE1   B HIS A 1 88  ? -23.905 -14.505 21.867  0.50 44.35 ? 88  HIS A CE1   1 
ATOM   1349  N  NE2   A HIS A 1 88  ? -23.302 -13.251 22.556  0.50 27.59 ? 88  HIS A NE2   1 
ATOM   1350  N  NE2   B HIS A 1 88  ? -24.396 -15.720 21.702  0.50 48.46 ? 88  HIS A NE2   1 
ATOM   1351  N  N     A PRO A 1 89  ? -19.586 -17.572 18.629  0.50 32.71 ? 89  PRO A N     1 
ATOM   1352  N  N     B PRO A 1 89  ? -19.690 -18.233 17.936  0.50 34.88 ? 89  PRO A N     1 
ATOM   1353  C  CA    A PRO A 1 89  ? -18.555 -17.958 17.648  0.50 35.30 ? 89  PRO A CA    1 
ATOM   1354  C  CA    B PRO A 1 89  ? -18.581 -18.400 16.980  0.50 31.54 ? 89  PRO A CA    1 
ATOM   1355  C  C     A PRO A 1 89  ? -18.184 -16.840 16.689  0.50 32.17 ? 89  PRO A C     1 
ATOM   1356  C  C     B PRO A 1 89  ? -18.088 -17.087 16.395  0.50 32.37 ? 89  PRO A C     1 
ATOM   1357  O  O     A PRO A 1 89  ? -17.050 -16.809 16.195  0.50 31.83 ? 89  PRO A O     1 
ATOM   1358  O  O     B PRO A 1 89  ? -16.876 -16.918 16.208  0.50 31.84 ? 89  PRO A O     1 
ATOM   1359  C  CB    A PRO A 1 89  ? -19.191 -19.149 16.917  0.50 33.26 ? 89  PRO A CB    1 
ATOM   1360  C  CB    B PRO A 1 89  ? -19.183 -19.320 15.910  0.50 33.93 ? 89  PRO A CB    1 
ATOM   1361  C  CG    A PRO A 1 89  ? -20.661 -18.996 17.133  0.50 35.05 ? 89  PRO A CG    1 
ATOM   1362  C  CG    B PRO A 1 89  ? -20.304 -20.030 16.604  0.50 35.29 ? 89  PRO A CG    1 
ATOM   1363  C  CD    A PRO A 1 89  ? -20.815 -18.373 18.491  0.50 37.03 ? 89  PRO A CD    1 
ATOM   1364  C  CD    B PRO A 1 89  ? -20.865 -19.041 17.574  0.50 36.29 ? 89  PRO A CD    1 
ATOM   1365  N  N     A GLU A 1 90  ? -19.104 -15.913 16.417  0.50 32.83 ? 90  GLU A N     1 
ATOM   1366  N  N     B GLU A 1 90  ? -18.987 -16.142 16.112  0.50 30.92 ? 90  GLU A N     1 
ATOM   1367  C  CA    A GLU A 1 90  ? -18.777 -14.748 15.606  0.50 32.97 ? 90  GLU A CA    1 
ATOM   1368  C  CA    B GLU A 1 90  ? -18.564 -14.854 15.576  0.50 32.77 ? 90  GLU A CA    1 
ATOM   1369  C  C     A GLU A 1 90  ? -17.869 -13.768 16.339  0.50 29.33 ? 90  GLU A C     1 
ATOM   1370  C  C     B GLU A 1 90  ? -17.866 -13.976 16.610  0.50 29.80 ? 90  GLU A C     1 
ATOM   1371  O  O     A GLU A 1 90  ? -17.208 -12.953 15.688  0.50 34.26 ? 90  GLU A O     1 
ATOM   1372  O  O     B GLU A 1 90  ? -17.479 -12.851 16.273  0.50 30.96 ? 90  GLU A O     1 
ATOM   1373  C  CB    A GLU A 1 90  ? -20.059 -14.040 15.162  0.50 35.50 ? 90  GLU A CB    1 
ATOM   1374  C  CB    B GLU A 1 90  ? -19.760 -14.103 14.982  0.50 36.08 ? 90  GLU A CB    1 
ATOM   1375  C  CG    A GLU A 1 90  ? -20.949 -13.560 16.300  0.50 36.95 ? 90  GLU A CG    1 
ATOM   1376  C  CG    B GLU A 1 90  ? -20.585 -13.302 15.981  0.50 35.90 ? 90  GLU A CG    1 
ATOM   1377  C  CD    A GLU A 1 90  ? -21.828 -14.659 16.872  0.50 35.12 ? 90  GLU A CD    1 
ATOM   1378  C  CD    B GLU A 1 90  ? -21.714 -14.103 16.602  0.50 36.70 ? 90  GLU A CD    1 
ATOM   1379  O  OE1   A GLU A 1 90  ? -21.645 -15.834 16.495  0.50 35.73 ? 90  GLU A OE1   1 
ATOM   1380  O  OE1   B GLU A 1 90  ? -21.578 -15.339 16.719  0.50 33.73 ? 90  GLU A OE1   1 
ATOM   1381  O  OE2   A GLU A 1 90  ? -22.709 -14.347 17.702  0.50 44.03 ? 90  GLU A OE2   1 
ATOM   1382  O  OE2   B GLU A 1 90  ? -22.743 -13.492 16.971  0.50 42.07 ? 90  GLU A OE2   1 
ATOM   1383  N  N     A GLN A 1 91  ? -17.818 -13.823 17.669  0.50 26.74 ? 91  GLN A N     1 
ATOM   1384  N  N     B GLN A 1 91  ? -17.690 -14.447 17.845  0.50 27.54 ? 91  GLN A N     1 
ATOM   1385  C  CA    A GLN A 1 91  ? -16.918 -12.979 18.443  0.50 28.42 ? 91  GLN A CA    1 
ATOM   1386  C  CA    B GLN A 1 91  ? -16.946 -13.710 18.855  0.50 26.31 ? 91  GLN A CA    1 
ATOM   1387  C  C     A GLN A 1 91  ? -15.573 -13.646 18.699  0.50 27.51 ? 91  GLN A C     1 
ATOM   1388  C  C     B GLN A 1 91  ? -15.511 -14.191 18.982  0.50 26.60 ? 91  GLN A C     1 
ATOM   1389  O  O     A GLN A 1 91  ? -14.817 -13.176 19.555  0.50 24.89 ? 91  GLN A O     1 
ATOM   1390  O  O     B GLN A 1 91  ? -14.821 -13.805 19.929  0.50 24.10 ? 91  GLN A O     1 
ATOM   1391  C  CB    A GLN A 1 91  ? -17.570 -12.576 19.771  0.50 30.94 ? 91  GLN A CB    1 
ATOM   1392  C  CB    B GLN A 1 91  ? -17.656 -13.784 20.210  0.50 27.69 ? 91  GLN A CB    1 
ATOM   1393  C  CG    A GLN A 1 91  ? -18.898 -11.830 19.621  0.50 34.34 ? 91  GLN A CG    1 
ATOM   1394  C  CG    B GLN A 1 91  ? -18.964 -12.998 20.257  0.50 27.79 ? 91  GLN A CG    1 
ATOM   1395  C  CD    A GLN A 1 91  ? -18.769 -10.514 18.870  0.50 30.05 ? 91  GLN A CD    1 
ATOM   1396  C  CD    B GLN A 1 91  ? -18.830 -11.578 19.715  0.50 34.46 ? 91  GLN A CD    1 
ATOM   1397  O  OE1   A GLN A 1 91  ? -17.722 -9.871  18.899  0.50 22.23 ? 91  GLN A OE1   1 
ATOM   1398  O  OE1   B GLN A 1 91  ? -17.773 -10.948 19.819  0.50 39.15 ? 91  GLN A OE1   1 
ATOM   1399  N  NE2   A GLN A 1 91  ? -19.843 -10.107 18.195  0.50 28.24 ? 91  GLN A NE2   1 
ATOM   1400  N  NE2   B GLN A 1 91  ? -19.906 -11.074 19.120  0.50 39.66 ? 91  GLN A NE2   1 
ATOM   1401  N  N     A LEU A 1 92  ? -15.265 -14.728 17.982  0.50 25.93 ? 92  LEU A N     1 
ATOM   1402  N  N     B LEU A 1 92  ? -15.053 -15.026 18.053  0.50 25.94 ? 92  LEU A N     1 
ATOM   1403  C  CA    A LEU A 1 92  ? -13.948 -15.366 17.991  0.50 27.53 ? 92  LEU A CA    1 
ATOM   1404  C  CA    B LEU A 1 92  ? -13.654 -15.427 17.941  0.50 27.70 ? 92  LEU A CA    1 
ATOM   1405  C  C     A LEU A 1 92  ? -13.324 -15.100 16.623  0.50 25.90 ? 92  LEU A C     1 
ATOM   1406  C  C     B LEU A 1 92  ? -13.168 -14.961 16.573  0.50 26.12 ? 92  LEU A C     1 
ATOM   1407  O  O     A LEU A 1 92  ? -13.654 -15.772 15.643  0.50 26.22 ? 92  LEU A O     1 
ATOM   1408  O  O     B LEU A 1 92  ? -13.625 -15.472 15.546  0.50 26.41 ? 92  LEU A O     1 
ATOM   1409  C  CB    A LEU A 1 92  ? -14.062 -16.862 18.272  0.50 27.43 ? 92  LEU A CB    1 
ATOM   1410  C  CB    B LEU A 1 92  ? -13.501 -16.939 18.106  0.50 26.50 ? 92  LEU A CB    1 
ATOM   1411  C  CG    A LEU A 1 92  ? -14.679 -17.290 19.607  0.50 32.24 ? 92  LEU A CG    1 
ATOM   1412  C  CG    B LEU A 1 92  ? -14.040 -17.537 19.411  0.50 28.81 ? 92  LEU A CG    1 
ATOM   1413  C  CD1   A LEU A 1 92  ? -15.140 -18.732 19.543  0.50 29.21 ? 92  LEU A CD1   1 
ATOM   1414  C  CD1   B LEU A 1 92  ? -14.091 -19.050 19.355  0.50 32.83 ? 92  LEU A CD1   1 
ATOM   1415  C  CD2   A LEU A 1 92  ? -13.677 -17.104 20.735  0.50 33.23 ? 92  LEU A CD2   1 
ATOM   1416  C  CD2   B LEU A 1 92  ? -13.204 -17.084 20.589  0.50 31.60 ? 92  LEU A CD2   1 
ATOM   1417  N  N     A ILE A 1 93  ? -12.423 -14.120 16.558  0.50 26.49 ? 93  ILE A N     1 
ATOM   1418  N  N     B ILE A 1 93  ? -12.262 -13.983 16.555  0.50 25.83 ? 93  ILE A N     1 
ATOM   1419  C  CA    A ILE A 1 93  ? -11.971 -13.546 15.294  0.50 24.55 ? 93  ILE A CA    1 
ATOM   1420  C  CA    B ILE A 1 93  ? -11.864 -13.293 15.329  0.50 24.03 ? 93  ILE A CA    1 
ATOM   1421  C  C     A ILE A 1 93  ? -10.478 -13.796 15.133  0.50 27.57 ? 93  ILE A C     1 
ATOM   1422  C  C     B ILE A 1 93  ? -10.383 -13.547 15.084  0.50 27.62 ? 93  ILE A C     1 
ATOM   1423  O  O     A ILE A 1 93  ? -9.691  -13.505 16.042  0.50 23.73 ? 93  ILE A O     1 
ATOM   1424  O  O     B ILE A 1 93  ? -9.540  -13.197 15.922  0.50 22.01 ? 93  ILE A O     1 
ATOM   1425  C  CB    A ILE A 1 93  ? -12.286 -12.041 15.221  0.50 26.57 ? 93  ILE A CB    1 
ATOM   1426  C  CB    B ILE A 1 93  ? -12.154 -11.786 15.401  0.50 26.52 ? 93  ILE A CB    1 
ATOM   1427  C  CG1   A ILE A 1 93  ? -13.756 -11.797 15.577  0.50 27.53 ? 93  ILE A CG1   1 
ATOM   1428  C  CG1   B ILE A 1 93  ? -13.634 -11.544 15.712  0.50 27.83 ? 93  ILE A CG1   1 
ATOM   1429  C  CG2   A ILE A 1 93  ? -11.976 -11.495 13.829  0.50 26.55 ? 93  ILE A CG2   1 
ATOM   1430  C  CG2   B ILE A 1 93  ? -11.763 -11.107 14.091  0.50 27.51 ? 93  ILE A CG2   1 
ATOM   1431  C  CD1   A ILE A 1 93  ? -14.058 -10.379 16.006  0.50 31.47 ? 93  ILE A CD1   1 
ATOM   1432  C  CD1   B ILE A 1 93  ? -13.970 -10.093 15.992  0.50 31.70 ? 93  ILE A CD1   1 
ATOM   1433  N  N     A THR A 1 94  ? -10.091 -14.323 13.970  0.50 27.89 ? 94  THR A N     1 
ATOM   1434  N  N     B THR A 1 94  ? -10.064 -14.134 13.930  0.50 27.96 ? 94  THR A N     1 
ATOM   1435  C  CA    A THR A 1 94  ? -8.692  -14.608 13.678  0.50 25.90 ? 94  THR A CA    1 
ATOM   1436  C  CA    B THR A 1 94  ? -8.701  -14.542 13.614  0.50 25.88 ? 94  THR A CA    1 
ATOM   1437  C  C     A THR A 1 94  ? -8.358  -14.231 12.244  0.50 26.37 ? 94  THR A C     1 
ATOM   1438  C  C     B THR A 1 94  ? -8.257  -13.973 12.276  0.50 26.75 ? 94  THR A C     1 
ATOM   1439  O  O     A THR A 1 94  ? -9.165  -14.437 11.331  0.50 28.03 ? 94  THR A O     1 
ATOM   1440  O  O     B THR A 1 94  ? -9.032  -13.939 11.314  0.50 29.81 ? 94  THR A O     1 
ATOM   1441  C  CB    A THR A 1 94  ? -8.347  -16.089 13.886  0.50 29.06 ? 94  THR A CB    1 
ATOM   1442  C  CB    B THR A 1 94  ? -8.570  -16.069 13.563  0.50 29.29 ? 94  THR A CB    1 
ATOM   1443  O  OG1   A THR A 1 94  ? -9.256  -16.908 13.139  0.50 27.88 ? 94  THR A OG1   1 
ATOM   1444  O  OG1   B THR A 1 94  ? -9.331  -16.582 12.462  0.50 27.15 ? 94  THR A OG1   1 
ATOM   1445  C  CG2   A THR A 1 94  ? -8.413  -16.458 15.350  0.50 28.03 ? 94  THR A CG2   1 
ATOM   1446  C  CG2   B THR A 1 94  ? -9.076  -16.691 14.835  0.50 26.46 ? 94  THR A CG2   1 
ATOM   1447  N  N     A GLY A 1 95  ? -7.161  -13.683 12.055  0.50 31.16 ? 95  GLY A N     1 
ATOM   1448  N  N     B GLY A 1 95  ? -6.996  -13.537 12.223  0.50 30.17 ? 95  GLY A N     1 
ATOM   1449  C  CA    A GLY A 1 95  ? -6.573  -13.501 10.741  0.50 27.56 ? 95  GLY A CA    1 
ATOM   1450  C  CA    B GLY A 1 95  ? -6.335  -13.211 10.979  0.50 28.21 ? 95  GLY A CA    1 
ATOM   1451  C  C     A GLY A 1 95  ? -5.790  -14.722 10.311  0.50 27.98 ? 95  GLY A C     1 
ATOM   1452  C  C     B GLY A 1 95  ? -5.491  -14.366 10.464  0.50 28.01 ? 95  GLY A C     1 
ATOM   1453  O  O     A GLY A 1 95  ? -6.133  -15.858 10.651  0.50 31.55 ? 95  GLY A O     1 
ATOM   1454  O  O     B GLY A 1 95  ? -5.541  -15.490 10.966  0.50 24.64 ? 95  GLY A O     1 
ATOM   1455  N  N     A LYS A 1 96  ? -4.710  -14.492 9.564   0.50 27.82 ? 96  LYS A N     1 
ATOM   1456  N  N     B LYS A 1 96  ? -4.687  -14.069 9.440   0.50 26.05 ? 96  LYS A N     1 
ATOM   1457  C  CA    A LYS A 1 96  ? -3.892  -15.602 9.086   0.50 31.73 ? 96  LYS A CA    1 
ATOM   1458  C  CA    B LYS A 1 96  ? -3.896  -15.090 8.764   0.50 33.25 ? 96  LYS A CA    1 
ATOM   1459  C  C     A LYS A 1 96  ? -2.422  -15.415 9.442   0.50 30.30 ? 96  LYS A C     1 
ATOM   1460  C  C     B LYS A 1 96  ? -2.402  -15.010 9.048   0.50 31.59 ? 96  LYS A C     1 
ATOM   1461  O  O     A LYS A 1 96  ? -1.693  -16.393 9.630   0.50 36.66 ? 96  LYS A O     1 
ATOM   1462  O  O     B LYS A 1 96  ? -1.674  -15.941 8.687   0.50 38.73 ? 96  LYS A O     1 
ATOM   1463  C  CB    A LYS A 1 96  ? -4.041  -15.769 7.570   0.50 34.00 ? 96  LYS A CB    1 
ATOM   1464  C  CB    B LYS A 1 96  ? -4.113  -15.011 7.244   0.50 31.80 ? 96  LYS A CB    1 
ATOM   1465  C  CG    A LYS A 1 96  ? -5.454  -16.106 7.117   0.50 41.68 ? 96  LYS A CG    1 
ATOM   1466  C  CG    B LYS A 1 96  ? -5.562  -15.187 6.818   0.50 46.88 ? 96  LYS A CG    1 
ATOM   1467  C  CD    A LYS A 1 96  ? -5.526  -16.312 5.611   0.50 45.13 ? 96  LYS A CD    1 
ATOM   1468  C  CD    B LYS A 1 96  ? -6.051  -16.608 7.066   0.50 40.55 ? 96  LYS A CD    1 
ATOM   1469  C  CE    A LYS A 1 96  ? -5.117  -17.726 5.221   0.50 49.01 ? 96  LYS A CE    1 
ATOM   1470  C  CE    B LYS A 1 96  ? -5.731  -17.516 5.891   0.50 48.52 ? 96  LYS A CE    1 
ATOM   1471  N  NZ    A LYS A 1 96  ? -6.086  -18.744 5.726   0.50 42.63 ? 96  LYS A NZ    1 
ATOM   1472  N  NZ    B LYS A 1 96  ? -6.419  -17.065 4.648   0.50 51.01 ? 96  LYS A NZ    1 
ATOM   1473  N  N     A GLU A 1 97  ? -1.980  -14.165 9.543   0.50 27.51 ? 97  GLU A N     1 
ATOM   1474  N  N     B GLU A 1 97  ? -1.930  -13.942 9.688   0.50 27.48 ? 97  GLU A N     1 
ATOM   1475  C  CA    A GLU A 1 97  ? -0.567  -13.837 9.692   0.50 28.54 ? 97  GLU A CA    1 
ATOM   1476  C  CA    B GLU A 1 97  ? -0.501  -13.668 9.794   0.50 28.44 ? 97  GLU A CA    1 
ATOM   1477  C  C     A GLU A 1 97  ? -0.411  -12.947 10.914  0.50 27.19 ? 97  GLU A C     1 
ATOM   1478  C  C     B GLU A 1 97  ? -0.299  -12.675 10.928  0.50 27.16 ? 97  GLU A C     1 
ATOM   1479  O  O     A GLU A 1 97  ? -1.002  -11.864 10.967  0.50 26.16 ? 97  GLU A O     1 
ATOM   1480  O  O     B GLU A 1 97  ? -0.945  -11.623 10.937  0.50 27.10 ? 97  GLU A O     1 
ATOM   1481  C  CB    A GLU A 1 97  ? -0.051  -13.137 8.431   0.50 29.21 ? 97  GLU A CB    1 
ATOM   1482  C  CB    B GLU A 1 97  ? 0.024   -13.108 8.465   0.50 29.20 ? 97  GLU A CB    1 
ATOM   1483  C  CG    A GLU A 1 97  ? 1.453   -13.031 8.303   0.50 35.23 ? 97  GLU A CG    1 
ATOM   1484  C  CG    B GLU A 1 97  ? 1.491   -12.730 8.423   0.50 35.64 ? 97  GLU A CG    1 
ATOM   1485  C  CD    A GLU A 1 97  ? 1.874   -12.572 6.914   0.50 38.45 ? 97  GLU A CD    1 
ATOM   1486  C  CD    B GLU A 1 97  ? 1.902   -12.202 7.051   0.50 38.08 ? 97  GLU A CD    1 
ATOM   1487  O  OE1   A GLU A 1 97  ? 1.757   -13.373 5.964   0.50 41.94 ? 97  GLU A OE1   1 
ATOM   1488  O  OE1   B GLU A 1 97  ? 1.004   -11.918 6.229   0.50 37.42 ? 97  GLU A OE1   1 
ATOM   1489  O  OE2   A GLU A 1 97  ? 2.304   -11.407 6.769   0.50 34.92 ? 97  GLU A OE2   1 
ATOM   1490  O  OE2   B GLU A 1 97  ? 3.119   -12.074 6.792   0.50 45.20 ? 97  GLU A OE2   1 
ATOM   1491  N  N     A ASP A 1 98  ? 0.367   -13.400 11.897  0.50 28.17 ? 98  ASP A N     1 
ATOM   1492  N  N     B ASP A 1 98  ? 0.573   -13.001 11.884  0.50 28.56 ? 98  ASP A N     1 
ATOM   1493  C  CA    A ASP A 1 98  ? 0.488   -12.642 13.135  0.50 28.84 ? 98  ASP A CA    1 
ATOM   1494  C  CA    B ASP A 1 98  ? 0.648   -12.209 13.108  0.50 29.16 ? 98  ASP A CA    1 
ATOM   1495  C  C     A ASP A 1 98  ? 1.447   -11.467 12.942  0.50 25.58 ? 98  ASP A C     1 
ATOM   1496  C  C     B ASP A 1 98  ? 1.509   -10.963 12.890  0.50 23.99 ? 98  ASP A C     1 
ATOM   1497  O  O     A ASP A 1 98  ? 1.999   -11.249 11.860  0.50 26.20 ? 98  ASP A O     1 
ATOM   1498  O  O     B ASP A 1 98  ? 1.821   -10.574 11.761  0.50 24.24 ? 98  ASP A O     1 
ATOM   1499  C  CB    A ASP A 1 98  ? 0.911   -13.552 14.291  0.50 22.38 ? 98  ASP A CB    1 
ATOM   1500  C  CB    B ASP A 1 98  ? 1.142   -13.053 14.288  0.50 23.16 ? 98  ASP A CB    1 
ATOM   1501  C  CG    A ASP A 1 98  ? 2.270   -14.208 14.080  0.50 28.34 ? 98  ASP A CG    1 
ATOM   1502  C  CG    B ASP A 1 98  ? 2.541   -13.636 14.084  0.50 26.67 ? 98  ASP A CG    1 
ATOM   1503  O  OD1   A ASP A 1 98  ? 3.020   -13.809 13.161  0.50 28.16 ? 98  ASP A OD1   1 
ATOM   1504  O  OD1   B ASP A 1 98  ? 3.447   -12.934 13.580  0.50 23.99 ? 98  ASP A OD1   1 
ATOM   1505  O  OD2   A ASP A 1 98  ? 2.584   -15.148 14.844  0.50 27.59 ? 98  ASP A OD2   1 
ATOM   1506  O  OD2   B ASP A 1 98  ? 2.742   -14.807 14.473  0.50 29.02 ? 98  ASP A OD2   1 
ATOM   1507  N  N     A ALA A 1 99  ? 1.644   -10.696 14.008  0.50 24.27 ? 99  ALA A N     1 
ATOM   1508  N  N     B ALA A 1 99  ? 1.892   -10.321 13.991  0.50 22.55 ? 99  ALA A N     1 
ATOM   1509  C  CA    A ALA A 1 99  ? 2.406   -9.458  13.949  0.50 23.48 ? 99  ALA A CA    1 
ATOM   1510  C  CA    B ALA A 1 99  ? 2.607   -9.054  13.974  0.50 25.07 ? 99  ALA A CA    1 
ATOM   1511  C  C     A ALA A 1 99  ? 3.912   -9.669  14.077  0.50 22.19 ? 99  ALA A C     1 
ATOM   1512  C  C     B ALA A 1 99  ? 4.110   -9.210  14.179  0.50 21.39 ? 99  ALA A C     1 
ATOM   1513  O  O     A ALA A 1 99  ? 4.642   -8.680  14.185  0.50 23.48 ? 99  ALA A O     1 
ATOM   1514  O  O     B ALA A 1 99  ? 4.814   -8.198  14.257  0.50 23.34 ? 99  ALA A O     1 
ATOM   1515  C  CB    A ALA A 1 99  ? 1.923   -8.493  15.037  0.50 21.31 ? 99  ALA A CB    1 
ATOM   1516  C  CB    B ALA A 1 99  ? 2.032   -8.115  15.042  0.50 20.89 ? 99  ALA A CB    1 
ATOM   1517  N  N     A ALA A 1 100 ? 4.384   -10.920 14.076  0.50 19.98 ? 100 ALA A N     1 
ATOM   1518  N  N     B ALA A 1 100 ? 4.606   -10.445 14.289  0.50 19.10 ? 100 ALA A N     1 
ATOM   1519  C  CA    A ALA A 1 100 ? 5.817   -11.230 14.109  0.50 23.68 ? 100 ALA A CA    1 
ATOM   1520  C  CA    B ALA A 1 100 ? 6.042   -10.738 14.313  0.50 24.09 ? 100 ALA A CA    1 
ATOM   1521  C  C     A ALA A 1 100 ? 6.523   -10.530 15.268  0.50 23.55 ? 100 ALA A C     1 
ATOM   1522  C  C     B ALA A 1 100 ? 6.767   -9.986  15.431  0.50 24.19 ? 100 ALA A C     1 
ATOM   1523  O  O     A ALA A 1 100 ? 7.689   -10.136 15.158  0.50 21.26 ? 100 ALA A O     1 
ATOM   1524  O  O     B ALA A 1 100 ? 7.833   -9.397  15.228  0.50 18.09 ? 100 ALA A O     1 
ATOM   1525  C  CB    A ALA A 1 100 ? 6.483   -10.875 12.777  0.50 21.29 ? 100 ALA A CB    1 
ATOM   1526  C  CB    B ALA A 1 100 ? 6.675   -10.442 12.952  0.50 21.88 ? 100 ALA A CB    1 
ATOM   1527  N  N     A ASN A 1 101 ? 5.809   -10.372 16.387  0.50 23.60 ? 101 ASN A N     1 
ATOM   1528  N  N     B ASN A 1 101 ? 6.180   -10.015 16.630  0.50 22.64 ? 101 ASN A N     1 
ATOM   1529  C  CA    A ASN A 1 101 ? 6.315   -9.662  17.562  0.50 18.76 ? 101 ASN A CA    1 
ATOM   1530  C  CA    B ASN A 1 101 ? 6.737   -9.368  17.818  0.50 18.70 ? 101 ASN A CA    1 
ATOM   1531  C  C     A ASN A 1 101 ? 6.739   -8.238  17.208  0.50 19.99 ? 101 ASN A C     1 
ATOM   1532  C  C     B ASN A 1 101 ? 6.986   -7.877  17.612  0.50 21.17 ? 101 ASN A C     1 
ATOM   1533  O  O     A ASN A 1 101 ? 7.722   -7.713  17.733  0.50 24.09 ? 101 ASN A O     1 
ATOM   1534  O  O     B ASN A 1 101 ? 7.752   -7.265  18.363  0.50 24.83 ? 101 ASN A O     1 
ATOM   1535  C  CB    A ASN A 1 101 ? 7.466   -10.428 18.218  0.50 25.71 ? 101 ASN A CB    1 
ATOM   1536  C  CB    B ASN A 1 101 ? 8.035   -10.050 18.272  0.50 24.68 ? 101 ASN A CB    1 
ATOM   1537  C  CG    A ASN A 1 101 ? 7.197   -11.920 18.316  0.50 25.21 ? 101 ASN A CG    1 
ATOM   1538  C  CG    B ASN A 1 101 ? 7.832   -11.504 18.662  0.50 29.52 ? 101 ASN A CG    1 
ATOM   1539  O  OD1   A ASN A 1 101 ? 8.080   -12.735 18.063  0.50 28.98 ? 101 ASN A OD1   1 
ATOM   1540  O  OD1   B ASN A 1 101 ? 8.727   -12.333 18.496  0.50 26.81 ? 101 ASN A OD1   1 
ATOM   1541  N  ND2   A ASN A 1 101 ? 5.979   -12.282 18.687  0.50 29.35 ? 101 ASN A ND2   1 
ATOM   1542  N  ND2   B ASN A 1 101 ? 6.657   -11.818 19.193  0.50 25.30 ? 101 ASN A ND2   1 
ATOM   1543  N  N     A ASN A 1 102 ? 5.991   -7.606  16.306  0.50 21.66 ? 102 ASN A N     1 
ATOM   1544  N  N     B ASN A 1 102 ? 6.336   -7.270  16.622  0.50 20.83 ? 102 ASN A N     1 
ATOM   1545  C  CA    A ASN A 1 102 ? 6.299   -6.263  15.827  0.50 21.39 ? 102 ASN A CA    1 
ATOM   1546  C  CA    B ASN A 1 102 ? 6.634   -5.905  16.201  0.50 21.60 ? 102 ASN A CA    1 
ATOM   1547  C  C     A ASN A 1 102 ? 5.095   -5.365  16.069  0.50 19.20 ? 102 ASN A C     1 
ATOM   1548  C  C     B ASN A 1 102 ? 5.400   -5.038  16.413  0.50 20.61 ? 102 ASN A C     1 
ATOM   1549  O  O     A ASN A 1 102 ? 4.026   -5.587  15.491  0.50 21.09 ? 102 ASN A O     1 
ATOM   1550  O  O     B ASN A 1 102 ? 4.388   -5.212  15.725  0.50 21.09 ? 102 ASN A O     1 
ATOM   1551  C  CB    A ASN A 1 102 ? 6.674   -6.285  14.341  0.50 21.97 ? 102 ASN A CB    1 
ATOM   1552  C  CB    B ASN A 1 102 ? 7.089   -5.876  14.740  0.50 21.29 ? 102 ASN A CB    1 
ATOM   1553  C  CG    A ASN A 1 102 ? 7.270   -4.972  13.861  0.50 23.25 ? 102 ASN A CG    1 
ATOM   1554  C  CG    B ASN A 1 102 ? 7.579   -4.505  14.303  0.50 23.20 ? 102 ASN A CG    1 
ATOM   1555  O  OD1   A ASN A 1 102 ? 7.051   -3.919  14.458  0.50 21.16 ? 102 ASN A OD1   1 
ATOM   1556  O  OD1   B ASN A 1 102 ? 6.858   -3.516  14.395  0.50 23.17 ? 102 ASN A OD1   1 
ATOM   1557  N  ND2   A ASN A 1 102 ? 8.033   -5.032  12.770  0.50 19.16 ? 102 ASN A ND2   1 
ATOM   1558  N  ND2   B ASN A 1 102 ? 8.820   -4.444  13.832  0.50 24.28 ? 102 ASN A ND2   1 
ATOM   1559  N  N     A TYR A 1 103 ? 5.280   -4.344  16.911  0.50 20.56 ? 103 TYR A N     1 
ATOM   1560  N  N     B TYR A 1 103 ? 5.506   -4.097  17.356  0.50 21.32 ? 103 TYR A N     1 
ATOM   1561  C  CA    A TYR A 1 103 ? 4.201   -3.405  17.214  0.50 22.08 ? 103 TYR A CA    1 
ATOM   1562  C  CA    B TYR A 1 103 ? 4.431   -3.144  17.636  0.50 20.79 ? 103 TYR A CA    1 
ATOM   1563  C  C     A TYR A 1 103 ? 3.669   -2.735  15.954  0.50 22.39 ? 103 TYR A C     1 
ATOM   1564  C  C     B TYR A 1 103 ? 3.891   -2.502  16.363  0.50 23.53 ? 103 TYR A C     1 
ATOM   1565  O  O     A TYR A 1 103 ? 2.458   -2.522  15.816  0.50 20.82 ? 103 TYR A O     1 
ATOM   1566  O  O     B TYR A 1 103 ? 2.676   -2.361  16.188  0.50 19.44 ? 103 TYR A O     1 
ATOM   1567  C  CB    A TYR A 1 103 ? 4.702   -2.353  18.208  0.50 20.20 ? 103 TYR A CB    1 
ATOM   1568  C  CB    B TYR A 1 103 ? 4.943   -2.064  18.595  0.50 21.57 ? 103 TYR A CB    1 
ATOM   1569  C  CG    A TYR A 1 103 ? 3.730   -1.216  18.486  0.50 23.47 ? 103 TYR A CG    1 
ATOM   1570  C  CG    B TYR A 1 103 ? 4.028   -0.855  18.739  0.50 20.54 ? 103 TYR A CG    1 
ATOM   1571  C  CD1   A TYR A 1 103 ? 3.628   -0.127  17.622  0.50 20.26 ? 103 TYR A CD1   1 
ATOM   1572  C  CD1   B TYR A 1 103 ? 3.035   -0.824  19.708  0.50 23.15 ? 103 TYR A CD1   1 
ATOM   1573  C  CD2   A TYR A 1 103 ? 2.931   -1.224  19.621  0.50 22.93 ? 103 TYR A CD2   1 
ATOM   1574  C  CD2   B TYR A 1 103 ? 4.164   0.254   17.908  0.50 21.78 ? 103 TYR A CD2   1 
ATOM   1575  C  CE1   A TYR A 1 103 ? 2.746   0.903   17.872  0.50 23.19 ? 103 TYR A CE1   1 
ATOM   1576  C  CE1   B TYR A 1 103 ? 2.198   0.271   19.842  0.50 20.37 ? 103 TYR A CE1   1 
ATOM   1577  C  CE2   A TYR A 1 103 ? 2.048   -0.194  19.881  0.50 23.05 ? 103 TYR A CE2   1 
ATOM   1578  C  CE2   B TYR A 1 103 ? 3.329   1.349   18.034  0.50 22.30 ? 103 TYR A CE2   1 
ATOM   1579  C  CZ    A TYR A 1 103 ? 1.958   0.865   19.009  0.50 22.65 ? 103 TYR A CZ    1 
ATOM   1580  C  CZ    B TYR A 1 103 ? 2.351   1.351   19.010  0.50 25.45 ? 103 TYR A CZ    1 
ATOM   1581  O  OH    A TYR A 1 103 ? 1.085   1.890   19.263  0.50 25.64 ? 103 TYR A OH    1 
ATOM   1582  O  OH    B TYR A 1 103 ? 1.520   2.431   19.146  0.50 26.83 ? 103 TYR A OH    1 
ATOM   1583  N  N     A ALA A 1 104 ? 4.563   -2.361  15.037  0.50 21.87 ? 104 ALA A N     1 
ATOM   1584  N  N     B ALA A 1 104 ? 4.787   -2.071  15.473  0.50 19.80 ? 104 ALA A N     1 
ATOM   1585  C  CA    A ALA A 1 104 ? 4.141   -1.628  13.847  0.50 24.97 ? 104 ALA A CA    1 
ATOM   1586  C  CA    B ALA A 1 104 ? 4.342   -1.328  14.300  0.50 25.27 ? 104 ALA A CA    1 
ATOM   1587  C  C     A ALA A 1 104 ? 3.187   -2.453  12.994  0.50 23.19 ? 104 ALA A C     1 
ATOM   1588  C  C     B ALA A 1 104 ? 3.547   -2.209  13.344  0.50 21.02 ? 104 ALA A C     1 
ATOM   1589  O  O     A ALA A 1 104 ? 2.197   -1.924  12.475  0.50 27.99 ? 104 ALA A O     1 
ATOM   1590  O  O     B ALA A 1 104 ? 2.603   -1.729  12.706  0.50 25.27 ? 104 ALA A O     1 
ATOM   1591  C  CB    A ALA A 1 104 ? 5.363   -1.204  13.031  0.50 21.57 ? 104 ALA A CB    1 
ATOM   1592  C  CB    B ALA A 1 104 ? 5.540   -0.700  13.587  0.50 21.90 ? 104 ALA A CB    1 
ATOM   1593  N  N     A ARG A 1 105 ? 3.471   -3.748  12.831  0.50 21.75 ? 105 ARG A N     1 
ATOM   1594  N  N     B ARG A 1 105 ? 3.909   -3.492  13.229  0.50 20.92 ? 105 ARG A N     1 
ATOM   1595  C  CA    A ARG A 1 105 ? 2.557   -4.629  12.109  0.50 21.90 ? 105 ARG A CA    1 
ATOM   1596  C  CA    B ARG A 1 105 ? 3.123   -4.408  12.406  0.50 22.90 ? 105 ARG A CA    1 
ATOM   1597  C  C     A ARG A 1 105 ? 1.197   -4.685  12.789  0.50 27.80 ? 105 ARG A C     1 
ATOM   1598  C  C     B ARG A 1 105 ? 1.719   -4.586  12.962  0.50 27.82 ? 105 ARG A C     1 
ATOM   1599  O  O     A ARG A 1 105 ? 0.162   -4.423  12.164  0.50 28.29 ? 105 ARG A O     1 
ATOM   1600  O  O     B ARG A 1 105 ? 0.754   -4.712  12.201  0.50 27.42 ? 105 ARG A O     1 
ATOM   1601  C  CB    A ARG A 1 105 ? 3.155   -6.032  12.002  0.50 24.43 ? 105 ARG A CB    1 
ATOM   1602  C  CB    B ARG A 1 105 ? 3.821   -5.764  12.299  0.50 23.50 ? 105 ARG A CB    1 
ATOM   1603  C  CG    A ARG A 1 105 ? 3.934   -6.270  10.741  0.50 26.06 ? 105 ARG A CG    1 
ATOM   1604  C  CG    B ARG A 1 105 ? 4.710   -5.905  11.094  0.50 27.61 ? 105 ARG A CG    1 
ATOM   1605  C  CD    A ARG A 1 105 ? 4.721   -7.572  10.782  0.50 23.47 ? 105 ARG A CD    1 
ATOM   1606  C  CD    B ARG A 1 105 ? 5.367   -7.274  11.027  0.50 21.96 ? 105 ARG A CD    1 
ATOM   1607  N  NE    A ARG A 1 105 ? 3.910   -8.728  10.420  0.50 25.18 ? 105 ARG A NE    1 
ATOM   1608  N  NE    B ARG A 1 105 ? 4.491   -8.295  10.464  0.50 26.31 ? 105 ARG A NE    1 
ATOM   1609  C  CZ    A ARG A 1 105 ? 3.678   -9.122  9.174   0.50 36.17 ? 105 ARG A CZ    1 
ATOM   1610  C  CZ    B ARG A 1 105 ? 4.294   -8.481  9.165   0.50 35.70 ? 105 ARG A CZ    1 
ATOM   1611  N  NH1   A ARG A 1 105 ? 4.163   -8.460  8.135   0.50 32.68 ? 105 ARG A NH1   1 
ATOM   1612  N  NH1   B ARG A 1 105 ? 4.847   -7.688  8.259   0.50 30.12 ? 105 ARG A NH1   1 
ATOM   1613  N  NH2   A ARG A 1 105 ? 2.941   -10.209 8.966   0.50 34.35 ? 105 ARG A NH2   1 
ATOM   1614  N  NH2   B ARG A 1 105 ? 3.525   -9.489  8.763   0.50 37.66 ? 105 ARG A NH2   1 
ATOM   1615  N  N     A GLY A 1 106 ? 1.183   -5.029  14.080  0.50 30.95 ? 106 GLY A N     1 
ATOM   1616  N  N     B GLY A 1 106 ? 1.582   -4.604  14.290  0.50 26.73 ? 106 GLY A N     1 
ATOM   1617  C  CA    A GLY A 1 106 ? -0.079  -5.156  14.791  0.50 24.19 ? 106 GLY A CA    1 
ATOM   1618  C  CA    B GLY A 1 106 ? 0.265   -4.762  14.879  0.50 24.93 ? 106 GLY A CA    1 
ATOM   1619  C  C     A GLY A 1 106 ? -0.926  -3.902  14.718  0.50 26.69 ? 106 GLY A C     1 
ATOM   1620  C  C     B GLY A 1 106 ? -0.578  -3.509  14.777  0.50 26.19 ? 106 GLY A C     1 
ATOM   1621  O  O     A GLY A 1 106 ? -2.153  -3.973  14.624  0.50 27.80 ? 106 GLY A O     1 
ATOM   1622  O  O     B GLY A 1 106 ? -1.803  -3.588  14.649  0.50 27.78 ? 106 GLY A O     1 
ATOM   1623  N  N     A HIS A 1 107 ? -0.281  -2.736  14.718  0.50 24.60 ? 107 HIS A N     1 
ATOM   1624  N  N     B HIS A 1 107 ? 0.063   -2.343  14.794  0.50 24.64 ? 107 HIS A N     1 
ATOM   1625  C  CA    A HIS A 1 107 ? -0.998  -1.470  14.759  0.50 25.47 ? 107 HIS A CA    1 
ATOM   1626  C  CA    B HIS A 1 107 ? -0.622  -1.063  14.877  0.50 24.53 ? 107 HIS A CA    1 
ATOM   1627  C  C     A HIS A 1 107 ? -1.244  -0.868  13.378  0.50 27.60 ? 107 HIS A C     1 
ATOM   1628  C  C     B HIS A 1 107 ? -0.815  -0.384  13.527  0.50 29.78 ? 107 HIS A C     1 
ATOM   1629  O  O     A HIS A 1 107 ? -2.292  -0.252  13.157  0.50 28.42 ? 107 HIS A O     1 
ATOM   1630  O  O     B HIS A 1 107 ? -1.842  0.270   13.313  0.50 25.70 ? 107 HIS A O     1 
ATOM   1631  C  CB    A HIS A 1 107 ? -0.237  -0.465  15.622  0.50 23.27 ? 107 HIS A CB    1 
ATOM   1632  C  CB    B HIS A 1 107 ? 0.155   -0.124  15.800  0.50 24.32 ? 107 HIS A CB    1 
ATOM   1633  C  CG    A HIS A 1 107 ? -0.987  0.807   15.858  0.50 27.61 ? 107 HIS A CG    1 
ATOM   1634  C  CG    B HIS A 1 107 ? -0.556  1.157   16.091  0.50 29.83 ? 107 HIS A CG    1 
ATOM   1635  N  ND1   A HIS A 1 107 ? -1.641  1.075   17.041  0.50 23.94 ? 107 HIS A ND1   1 
ATOM   1636  N  ND1   B HIS A 1 107 ? -1.343  1.328   17.208  0.50 24.94 ? 107 HIS A ND1   1 
ATOM   1637  C  CD2   A HIS A 1 107 ? -1.198  1.881   15.060  0.50 27.13 ? 107 HIS A CD2   1 
ATOM   1638  C  CD2   B HIS A 1 107 ? -0.607  2.327   15.410  0.50 28.98 ? 107 HIS A CD2   1 
ATOM   1639  C  CE1   A HIS A 1 107 ? -2.217  2.262   16.965  0.50 30.99 ? 107 HIS A CE1   1 
ATOM   1640  C  CE1   B HIS A 1 107 ? -1.843  2.551   17.207  0.50 30.44 ? 107 HIS A CE1   1 
ATOM   1641  N  NE2   A HIS A 1 107 ? -1.966  2.770   15.772  0.50 28.99 ? 107 HIS A NE2   1 
ATOM   1642  N  NE2   B HIS A 1 107 ? -1.412  3.178   16.128  0.50 29.02 ? 107 HIS A NE2   1 
ATOM   1643  N  N     A TYR A 1 108 ? -0.303  -1.005  12.445  0.50 29.09 ? 108 TYR A N     1 
ATOM   1644  N  N     B TYR A 1 108 ? 0.145   -0.513  12.612  0.50 26.37 ? 108 TYR A N     1 
ATOM   1645  C  CA    A TYR A 1 108 ? -0.411  -0.343  11.149  0.50 27.54 ? 108 TYR A CA    1 
ATOM   1646  C  CA    B TYR A 1 108 ? 0.160   0.310   11.411  0.50 29.41 ? 108 TYR A CA    1 
ATOM   1647  C  C     A TYR A 1 108 ? -0.735  -1.335  10.037  0.50 30.02 ? 108 TYR A C     1 
ATOM   1648  C  C     B TYR A 1 108 ? -0.129  -0.438  10.118  0.50 28.13 ? 108 TYR A C     1 
ATOM   1649  O  O     A TYR A 1 108 ? -1.866  -1.353  9.548   0.50 36.25 ? 108 TYR A O     1 
ATOM   1650  O  O     B TYR A 1 108 ? -0.620  0.178   9.170   0.50 30.04 ? 108 TYR A O     1 
ATOM   1651  C  CB    A TYR A 1 108 ? 0.864   0.450   10.847  0.50 28.92 ? 108 TYR A CB    1 
ATOM   1652  C  CB    B TYR A 1 108 ? 1.511   1.028   11.282  0.50 24.16 ? 108 TYR A CB    1 
ATOM   1653  C  CG    A TYR A 1 108 ? 1.027   1.658   11.744  0.50 30.11 ? 108 TYR A CG    1 
ATOM   1654  C  CG    B TYR A 1 108 ? 1.703   2.132   12.301  0.50 28.53 ? 108 TYR A CG    1 
ATOM   1655  C  CD1   A TYR A 1 108 ? 0.185   2.758   11.617  0.50 29.98 ? 108 TYR A CD1   1 
ATOM   1656  C  CD1   B TYR A 1 108 ? 0.936   3.292   12.249  0.50 32.25 ? 108 TYR A CD1   1 
ATOM   1657  C  CD2   A TYR A 1 108 ? 2.011   1.697   12.723  0.50 28.34 ? 108 TYR A CD2   1 
ATOM   1658  C  CD2   B TYR A 1 108 ? 2.651   2.021   13.308  0.50 28.55 ? 108 TYR A CD2   1 
ATOM   1659  C  CE1   A TYR A 1 108 ? 0.322   3.865   12.435  0.50 31.70 ? 108 TYR A CE1   1 
ATOM   1660  C  CE1   B TYR A 1 108 ? 1.105   4.307   13.173  0.50 30.86 ? 108 TYR A CE1   1 
ATOM   1661  C  CE2   A TYR A 1 108 ? 2.157   2.802   13.547  0.50 26.15 ? 108 TYR A CE2   1 
ATOM   1662  C  CE2   B TYR A 1 108 ? 2.830   3.030   14.234  0.50 27.76 ? 108 TYR A CE2   1 
ATOM   1663  C  CZ    A TYR A 1 108 ? 1.309   3.882   13.398  0.50 32.16 ? 108 TYR A CZ    1 
ATOM   1664  C  CZ    B TYR A 1 108 ? 2.054   4.169   14.165  0.50 34.57 ? 108 TYR A CZ    1 
ATOM   1665  O  OH    A TYR A 1 108 ? 1.446   4.983   14.214  0.50 37.13 ? 108 TYR A OH    1 
ATOM   1666  O  OH    B TYR A 1 108 ? 2.228   5.178   15.088  0.50 32.32 ? 108 TYR A OH    1 
ATOM   1667  N  N     A THR A 1 109 ? 0.215   -2.175  9.631   0.50 29.30 ? 109 THR A N     1 
ATOM   1668  N  N     B THR A 1 109 ? 0.154   -1.737  10.033  0.50 29.97 ? 109 THR A N     1 
ATOM   1669  C  CA    A THR A 1 109 ? 0.039   -2.977  8.424   0.50 30.71 ? 109 THR A CA    1 
ATOM   1670  C  CA    B THR A 1 109 ? -0.118  -2.424  8.775   0.50 33.46 ? 109 THR A CA    1 
ATOM   1671  C  C     A THR A 1 109 ? -1.049  -4.034  8.583   0.50 31.26 ? 109 THR A C     1 
ATOM   1672  C  C     B THR A 1 109 ? -1.024  -3.633  8.967   0.50 32.20 ? 109 THR A C     1 
ATOM   1673  O  O     A THR A 1 109 ? -2.141  -3.891  8.024   0.50 36.47 ? 109 THR A O     1 
ATOM   1674  O  O     B THR A 1 109 ? -2.202  -3.574  8.602   0.50 32.83 ? 109 THR A O     1 
ATOM   1675  C  CB    A THR A 1 109 ? 1.357   -3.642  8.031   0.50 30.92 ? 109 THR A CB    1 
ATOM   1676  C  CB    B THR A 1 109 ? 1.185   -2.832  8.080   0.50 27.52 ? 109 THR A CB    1 
ATOM   1677  O  OG1   A THR A 1 109 ? 1.544   -4.830  8.809   0.50 38.73 ? 109 THR A OG1   1 
ATOM   1678  O  OG1   B THR A 1 109 ? 2.068   -3.451  9.018   0.50 33.03 ? 109 THR A OG1   1 
ATOM   1679  C  CG2   A THR A 1 109 ? 2.512   -2.691  8.288   0.50 26.71 ? 109 THR A CG2   1 
ATOM   1680  C  CG2   B THR A 1 109 ? 1.862   -1.609  7.476   0.50 32.91 ? 109 THR A CG2   1 
ATOM   1681  N  N     A ILE A 1 110 ? -0.767  -5.092  9.346   0.50 27.22 ? 110 ILE A N     1 
ATOM   1682  N  N     B ILE A 1 110 ? -0.500  -4.721  9.540   0.50 27.01 ? 110 ILE A N     1 
ATOM   1683  C  CA    A ILE A 1 110 ? -1.694  -6.218  9.423   0.50 31.52 ? 110 ILE A CA    1 
ATOM   1684  C  CA    B ILE A 1 110 ? -1.266  -5.967  9.617   0.50 31.32 ? 110 ILE A CA    1 
ATOM   1685  C  C     A ILE A 1 110 ? -2.958  -5.833  10.183  0.50 31.55 ? 110 ILE A C     1 
ATOM   1686  C  C     B ILE A 1 110 ? -2.549  -5.760  10.416  0.50 30.87 ? 110 ILE A C     1 
ATOM   1687  O  O     A ILE A 1 110 ? -4.072  -6.182  9.775   0.50 30.73 ? 110 ILE A O     1 
ATOM   1688  O  O     B ILE A 1 110 ? -3.634  -6.187  10.005  0.50 31.55 ? 110 ILE A O     1 
ATOM   1689  C  CB    A ILE A 1 110 ? -1.006  -7.438  10.061  0.50 32.63 ? 110 ILE A CB    1 
ATOM   1690  C  CB    B ILE A 1 110 ? -0.410  -7.095  10.222  0.50 33.20 ? 110 ILE A CB    1 
ATOM   1691  C  CG1   A ILE A 1 110 ? 0.250   -7.817  9.274   0.50 34.69 ? 110 ILE A CG1   1 
ATOM   1692  C  CG1   B ILE A 1 110 ? 0.933   -7.215  9.500   0.50 33.92 ? 110 ILE A CG1   1 
ATOM   1693  C  CG2   A ILE A 1 110 ? -1.970  -8.611  10.129  0.50 30.25 ? 110 ILE A CG2   1 
ATOM   1694  C  CG2   B ILE A 1 110 ? -1.164  -8.411  10.156  0.50 34.69 ? 110 ILE A CG2   1 
ATOM   1695  C  CD1   A ILE A 1 110 ? -0.019  -8.176  7.827   0.50 29.70 ? 110 ILE A CD1   1 
ATOM   1696  C  CD1   B ILE A 1 110 ? 0.810   -7.651  8.052   0.50 31.67 ? 110 ILE A CD1   1 
ATOM   1697  N  N     A GLY A 1 111 ? -2.810  -5.117  11.301  0.50 29.02 ? 111 GLY A N     1 
ATOM   1698  N  N     B GLY A 1 111 ? -2.441  -5.102  11.572  0.50 29.54 ? 111 GLY A N     1 
ATOM   1699  C  CA    A GLY A 1 111 ? -3.961  -4.741  12.107  0.50 32.97 ? 111 GLY A CA    1 
ATOM   1700  C  CA    B GLY A 1 111 ? -3.611  -4.891  12.406  0.50 31.43 ? 111 GLY A CA    1 
ATOM   1701  C  C     A GLY A 1 111 ? -5.003  -3.942  11.354  0.50 30.73 ? 111 GLY A C     1 
ATOM   1702  C  C     B GLY A 1 111 ? -4.651  -3.994  11.768  0.50 31.49 ? 111 GLY A C     1 
ATOM   1703  O  O     A GLY A 1 111 ? -6.176  -3.941  11.741  0.50 28.45 ? 111 GLY A O     1 
ATOM   1704  O  O     B GLY A 1 111 ? -5.842  -4.110  12.069  0.50 29.10 ? 111 GLY A O     1 
ATOM   1705  N  N     A LYS A 1 112 ? -4.601  -3.262  10.281  0.50 35.17 ? 112 LYS A N     1 
ATOM   1706  N  N     B LYS A 1 112 ? -4.226  -3.095  10.880  0.50 32.62 ? 112 LYS A N     1 
ATOM   1707  C  CA    A LYS A 1 112 ? -5.551  -2.526  9.457   0.50 32.19 ? 112 LYS A CA    1 
ATOM   1708  C  CA    B LYS A 1 112 ? -5.166  -2.221  10.190  0.50 32.36 ? 112 LYS A CA    1 
ATOM   1709  C  C     A LYS A 1 112 ? -6.534  -3.462  8.762   0.50 30.21 ? 112 LYS A C     1 
ATOM   1710  C  C     B LYS A 1 112 ? -6.038  -2.971  9.192   0.50 32.28 ? 112 LYS A C     1 
ATOM   1711  O  O     A LYS A 1 112 ? -7.691  -3.089  8.534   0.50 29.50 ? 112 LYS A O     1 
ATOM   1712  O  O     B LYS A 1 112 ? -7.052  -2.423  8.746   0.50 32.58 ? 112 LYS A O     1 
ATOM   1713  C  CB    A LYS A 1 112 ? -4.774  -1.676  8.448   0.50 38.99 ? 112 LYS A CB    1 
ATOM   1714  C  CB    B LYS A 1 112 ? -4.404  -1.095  9.488   0.50 31.72 ? 112 LYS A CB    1 
ATOM   1715  C  CG    A LYS A 1 112 ? -5.519  -1.253  7.200   0.50 42.24 ? 112 LYS A CG    1 
ATOM   1716  C  CG    B LYS A 1 112 ? -5.255  0.114   9.132   0.50 39.34 ? 112 LYS A CG    1 
ATOM   1717  C  CD    A LYS A 1 112 ? -4.605  -0.432  6.295   0.50 41.99 ? 112 LYS A CD    1 
ATOM   1718  C  CD    B LYS A 1 112 ? -4.426  1.192   8.452   0.50 33.54 ? 112 LYS A CD    1 
ATOM   1719  C  CE    A LYS A 1 112 ? -3.219  -1.062  6.179   0.50 42.73 ? 112 LYS A CE    1 
ATOM   1720  C  CE    B LYS A 1 112 ? -5.287  2.378   8.041   0.50 37.08 ? 112 LYS A CE    1 
ATOM   1721  N  NZ    A LYS A 1 112 ? -3.257  -2.430  5.581   0.50 44.64 ? 112 LYS A NZ    1 
ATOM   1722  N  NZ    B LYS A 1 112 ? -6.333  1.992   7.048   0.50 55.31 ? 112 LYS A NZ    1 
ATOM   1723  N  N     A GLU A 1 113 ? -6.106  -4.688  8.448   0.50 32.25 ? 113 GLU A N     1 
ATOM   1724  N  N     B GLU A 1 113 ? -5.680  -4.207  8.840   0.50 30.63 ? 113 GLU A N     1 
ATOM   1725  C  CA    A GLU A 1 113 ? -6.952  -5.617  7.704   0.50 30.49 ? 113 GLU A CA    1 
ATOM   1726  C  CA    B GLU A 1 113 ? -6.475  -5.007  7.917   0.50 30.04 ? 113 GLU A CA    1 
ATOM   1727  C  C     A GLU A 1 113 ? -8.204  -6.039  8.467   0.50 27.92 ? 113 GLU A C     1 
ATOM   1728  C  C     B GLU A 1 113 ? -7.672  -5.676  8.584   0.50 29.94 ? 113 GLU A C     1 
ATOM   1729  O  O     A GLU A 1 113 ? -9.173  -6.480  7.839   0.50 25.03 ? 113 GLU A O     1 
ATOM   1730  O  O     B GLU A 1 113 ? -8.553  -6.177  7.877   0.50 30.13 ? 113 GLU A O     1 
ATOM   1731  C  CB    A GLU A 1 113 ? -6.168  -6.877  7.335   0.50 32.14 ? 113 GLU A CB    1 
ATOM   1732  C  CB    B GLU A 1 113 ? -5.598  -6.079  7.262   0.50 35.06 ? 113 GLU A CB    1 
ATOM   1733  C  CG    A GLU A 1 113 ? -5.151  -6.713  6.228   0.50 36.58 ? 113 GLU A CG    1 
ATOM   1734  C  CG    B GLU A 1 113 ? -4.393  -5.534  6.506   0.50 32.38 ? 113 GLU A CG    1 
ATOM   1735  C  CD    A GLU A 1 113 ? -4.577  -8.048  5.792   0.50 42.63 ? 113 GLU A CD    1 
ATOM   1736  C  CD    B GLU A 1 113 ? -3.500  -6.630  5.947   0.50 40.20 ? 113 GLU A CD    1 
ATOM   1737  O  OE1   A GLU A 1 113 ? -4.791  -9.047  6.513   0.50 35.17 ? 113 GLU A OE1   1 
ATOM   1738  O  OE1   B GLU A 1 113 ? -3.591  -7.780  6.428   0.50 44.44 ? 113 GLU A OE1   1 
ATOM   1739  O  OE2   A GLU A 1 113 ? -3.921  -8.099  4.733   0.50 45.73 ? 113 GLU A OE2   1 
ATOM   1740  O  OE2   B GLU A 1 113 ? -2.705  -6.339  5.026   0.50 39.23 ? 113 GLU A OE2   1 
ATOM   1741  N  N     A ILE A 1 114 ? -8.215  -5.938  9.797   0.50 27.72 ? 114 ILE A N     1 
ATOM   1742  N  N     B ILE A 1 114 ? -7.739  -5.692  9.917   0.50 25.33 ? 114 ILE A N     1 
ATOM   1743  C  CA    A ILE A 1 114 ? -9.274  -6.547  10.592  0.50 26.85 ? 114 ILE A CA    1 
ATOM   1744  C  CA    B ILE A 1 114 ? -8.748  -6.463  10.630  0.50 28.18 ? 114 ILE A CA    1 
ATOM   1745  C  C     A ILE A 1 114 ? -9.841  -5.618  11.656  0.50 29.82 ? 114 ILE A C     1 
ATOM   1746  C  C     B ILE A 1 114 ? -9.537  -5.632  11.630  0.50 30.03 ? 114 ILE A C     1 
ATOM   1747  O  O     A ILE A 1 114 ? -10.752 -6.017  12.386  0.50 29.13 ? 114 ILE A O     1 
ATOM   1748  O  O     B ILE A 1 114 ? -10.487 -6.142  12.227  0.50 30.24 ? 114 ILE A O     1 
ATOM   1749  C  CB    A ILE A 1 114 ? -8.785  -7.868  11.229  0.50 28.33 ? 114 ILE A CB    1 
ATOM   1750  C  CB    B ILE A 1 114 ? -8.107  -7.680  11.334  0.50 32.18 ? 114 ILE A CB    1 
ATOM   1751  C  CG1   A ILE A 1 114 ? -9.938  -8.860  11.376  0.50 34.08 ? 114 ILE A CG1   1 
ATOM   1752  C  CG1   B ILE A 1 114 ? -9.106  -8.828  11.462  0.50 29.31 ? 114 ILE A CG1   1 
ATOM   1753  C  CG2   A ILE A 1 114 ? -8.082  -7.613  12.556  0.50 28.66 ? 114 ILE A CG2   1 
ATOM   1754  C  CG2   B ILE A 1 114 ? -7.553  -7.289  12.694  0.50 28.14 ? 114 ILE A CG2   1 
ATOM   1755  C  CD1   A ILE A 1 114 ? -9.501  -10.308 11.305  0.50 32.00 ? 114 ILE A CD1   1 
ATOM   1756  C  CD1   B ILE A 1 114 ? -8.574  -10.012 12.245  0.50 31.81 ? 114 ILE A CD1   1 
ATOM   1757  N  N     A ILE A 1 115 ? -9.364  -4.375  11.747  0.50 27.26 ? 115 ILE A N     1 
ATOM   1758  N  N     B ILE A 1 115 ? -9.196  -4.355  11.817  0.50 27.47 ? 115 ILE A N     1 
ATOM   1759  C  CA    A ILE A 1 115 ? -9.815  -3.497  12.822  0.50 27.31 ? 115 ILE A CA    1 
ATOM   1760  C  CA    B ILE A 1 115 ? -9.778  -3.590  12.916  0.50 27.24 ? 115 ILE A CA    1 
ATOM   1761  C  C     A ILE A 1 115 ? -11.288 -3.133  12.654  0.50 29.01 ? 115 ILE A C     1 
ATOM   1762  C  C     B ILE A 1 115 ? -11.269 -3.359  12.688  0.50 28.91 ? 115 ILE A C     1 
ATOM   1763  O  O     A ILE A 1 115 ? -11.992 -2.907  13.646  0.50 29.03 ? 115 ILE A O     1 
ATOM   1764  O  O     B ILE A 1 115 ? -12.089 -3.592  13.584  0.50 23.97 ? 115 ILE A O     1 
ATOM   1765  C  CB    A ILE A 1 115 ? -8.917  -2.245  12.904  0.50 28.25 ? 115 ILE A CB    1 
ATOM   1766  C  CB    B ILE A 1 115 ? -9.010  -2.268  13.123  0.50 27.98 ? 115 ILE A CB    1 
ATOM   1767  C  CG1   A ILE A 1 115 ? -9.270  -1.407  14.134  0.50 30.09 ? 115 ILE A CG1   1 
ATOM   1768  C  CG1   B ILE A 1 115 ? -9.632  -1.459  14.262  0.50 31.98 ? 115 ILE A CG1   1 
ATOM   1769  C  CG2   A ILE A 1 115 ? -9.021  -1.407  11.632  0.50 32.10 ? 115 ILE A CG2   1 
ATOM   1770  C  CG2   B ILE A 1 115 ? -8.925  -1.448  11.831  0.50 32.20 ? 115 ILE A CG2   1 
ATOM   1771  C  CD1   A ILE A 1 115 ? -9.271  -2.193  15.431  0.50 28.90 ? 115 ILE A CD1   1 
ATOM   1772  C  CD1   B ILE A 1 115 ? -9.615  -2.177  15.597  0.50 27.87 ? 115 ILE A CD1   1 
ATOM   1773  N  N     A ASP A 1 116 ? -11.791 -3.097  11.415  0.50 26.94 ? 116 ASP A N     1 
ATOM   1774  N  N     B ASP A 1 116 ? -11.650 -2.933  11.477  0.50 27.09 ? 116 ASP A N     1 
ATOM   1775  C  CA    A ASP A 1 116 ? -13.191 -2.741  11.199  0.50 28.10 ? 116 ASP A CA    1 
ATOM   1776  C  CA    B ASP A 1 116 ? -13.044 -2.579  11.222  0.50 28.03 ? 116 ASP A CA    1 
ATOM   1777  C  C     A ASP A 1 116 ? -14.134 -3.878  11.577  0.50 29.51 ? 116 ASP A C     1 
ATOM   1778  C  C     B ASP A 1 116 ? -13.975 -3.772  11.391  0.50 29.22 ? 116 ASP A C     1 
ATOM   1779  O  O     A ASP A 1 116 ? -15.178 -3.637  12.193  0.50 31.05 ? 116 ASP A O     1 
ATOM   1780  O  O     B ASP A 1 116 ? -15.142 -3.598  11.758  0.50 31.18 ? 116 ASP A O     1 
ATOM   1781  C  CB    A ASP A 1 116 ? -13.417 -2.328  9.745   0.50 31.20 ? 116 ASP A CB    1 
ATOM   1782  C  CB    B ASP A 1 116 ? -13.190 -1.984  9.822   0.50 30.96 ? 116 ASP A CB    1 
ATOM   1783  C  CG    A ASP A 1 116 ? -13.079 -0.877  9.496   0.50 34.18 ? 116 ASP A CG    1 
ATOM   1784  C  CG    B ASP A 1 116 ? -12.339 -0.748  9.627   0.50 35.39 ? 116 ASP A CG    1 
ATOM   1785  O  OD1   A ASP A 1 116 ? -13.237 -0.061  10.428  0.50 34.70 ? 116 ASP A OD1   1 
ATOM   1786  O  OD1   B ASP A 1 116 ? -12.428 0.174   10.467  0.50 32.49 ? 116 ASP A OD1   1 
ATOM   1787  O  OD2   A ASP A 1 116 ? -12.661 -0.552  8.366   0.50 34.66 ? 116 ASP A OD2   1 
ATOM   1788  O  OD2   B ASP A 1 116 ? -11.571 -0.708  8.641   0.50 34.95 ? 116 ASP A OD2   1 
ATOM   1789  N  N     A LEU A 1 117 ? -13.792 -5.119  11.220  0.50 27.46 ? 117 LEU A N     1 
ATOM   1790  N  N     B LEU A 1 117 ? -13.487 -4.987  11.131  0.50 26.86 ? 117 LEU A N     1 
ATOM   1791  C  CA    A LEU A 1 117 ? -14.641 -6.243  11.603  0.50 28.77 ? 117 LEU A CA    1 
ATOM   1792  C  CA    B LEU A 1 117 ? -14.278 -6.171  11.448  0.50 28.95 ? 117 LEU A CA    1 
ATOM   1793  C  C     A LEU A 1 117 ? -14.685 -6.407  13.115  0.50 28.88 ? 117 LEU A C     1 
ATOM   1794  C  C     B LEU A 1 117 ? -14.449 -6.326  12.954  0.50 28.10 ? 117 LEU A C     1 
ATOM   1795  O  O     A LEU A 1 117 ? -15.738 -6.725  13.683  0.50 27.81 ? 117 LEU A O     1 
ATOM   1796  O  O     B LEU A 1 117 ? -15.539 -6.668  13.432  0.50 29.14 ? 117 LEU A O     1 
ATOM   1797  C  CB    A LEU A 1 117 ? -14.152 -7.533  10.944  0.50 29.28 ? 117 LEU A CB    1 
ATOM   1798  C  CB    B LEU A 1 117 ? -13.621 -7.417  10.857  0.50 31.33 ? 117 LEU A CB    1 
ATOM   1799  C  CG    A LEU A 1 117 ? -14.910 -8.798  11.353  0.50 31.48 ? 117 LEU A CG    1 
ATOM   1800  C  CG    B LEU A 1 117 ? -14.263 -8.751  11.237  0.50 28.28 ? 117 LEU A CG    1 
ATOM   1801  C  CD1   A LEU A 1 117 ? -16.408 -8.638  11.099  0.50 26.71 ? 117 LEU A CD1   1 
ATOM   1802  C  CD1   B LEU A 1 117 ? -15.674 -8.856  10.667  0.50 32.57 ? 117 LEU A CD1   1 
ATOM   1803  C  CD2   A LEU A 1 117 ? -14.369 -10.016 10.626  0.50 28.37 ? 117 LEU A CD2   1 
ATOM   1804  C  CD2   B LEU A 1 117 ? -13.400 -9.912  10.780  0.50 31.45 ? 117 LEU A CD2   1 
ATOM   1805  N  N     A VAL A 1 118 ? -13.549 -6.194  13.782  0.50 23.53 ? 118 VAL A N     1 
ATOM   1806  N  N     B VAL A 1 118 ? -13.382 -6.074  13.713  0.50 23.78 ? 118 VAL A N     1 
ATOM   1807  C  CA    A VAL A 1 118 ? -13.500 -6.309  15.237  0.50 31.38 ? 118 VAL A CA    1 
ATOM   1808  C  CA    B VAL A 1 118 ? -13.440 -6.218  15.163  0.50 31.34 ? 118 VAL A CA    1 
ATOM   1809  C  C     A VAL A 1 118 ? -14.491 -5.350  15.883  0.50 29.65 ? 118 VAL A C     1 
ATOM   1810  C  C     B VAL A 1 118 ? -14.376 -5.180  15.767  0.50 29.67 ? 118 VAL A C     1 
ATOM   1811  O  O     A VAL A 1 118 ? -15.189 -5.706  16.840  0.50 29.61 ? 118 VAL A O     1 
ATOM   1812  O  O     B VAL A 1 118 ? -15.200 -5.498  16.634  0.50 28.86 ? 118 VAL A O     1 
ATOM   1813  C  CB    A VAL A 1 118 ? -12.062 -6.073  15.737  0.50 25.81 ? 118 VAL A CB    1 
ATOM   1814  C  CB    B VAL A 1 118 ? -12.021 -6.127  15.755  0.50 25.82 ? 118 VAL A CB    1 
ATOM   1815  C  CG1   A VAL A 1 118 ? -12.051 -5.742  17.224  0.50 27.84 ? 118 VAL A CG1   1 
ATOM   1816  C  CG1   B VAL A 1 118 ? -12.075 -5.875  17.254  0.50 27.86 ? 118 VAL A CG1   1 
ATOM   1817  C  CG2   A VAL A 1 118 ? -11.209 -7.300  15.465  0.50 25.03 ? 118 VAL A CG2   1 
ATOM   1818  C  CG2   B VAL A 1 118 ? -11.256 -7.403  15.462  0.50 24.97 ? 118 VAL A CG2   1 
ATOM   1819  N  N     A LEU A 1 119 ? -14.590 -4.127  15.357  0.50 28.04 ? 119 LEU A N     1 
ATOM   1820  N  N     B LEU A 1 119 ? -14.274 -3.927  15.317  0.50 26.46 ? 119 LEU A N     1 
ATOM   1821  C  CA    A LEU A 1 119 ? -15.503 -3.152  15.946  0.50 29.70 ? 119 LEU A CA    1 
ATOM   1822  C  CA    B LEU A 1 119 ? -15.162 -2.891  15.833  0.50 30.32 ? 119 LEU A CA    1 
ATOM   1823  C  C     A LEU A 1 119 ? -16.958 -3.527  15.696  0.50 30.51 ? 119 LEU A C     1 
ATOM   1824  C  C     B LEU A 1 119 ? -16.618 -3.174  15.489  0.50 29.94 ? 119 LEU A C     1 
ATOM   1825  O  O     A LEU A 1 119 ? -17.788 -3.445  16.609  0.50 27.33 ? 119 LEU A O     1 
ATOM   1826  O  O     B LEU A 1 119 ? -17.516 -2.837  16.269  0.50 30.68 ? 119 LEU A O     1 
ATOM   1827  C  CB    A LEU A 1 119 ? -15.210 -1.757  15.402  0.50 31.17 ? 119 LEU A CB    1 
ATOM   1828  C  CB    B LEU A 1 119 ? -14.747 -1.524  15.292  0.50 28.41 ? 119 LEU A CB    1 
ATOM   1829  C  CG    A LEU A 1 119 ? -13.859 -1.152  15.774  0.50 27.94 ? 119 LEU A CG    1 
ATOM   1830  C  CG    B LEU A 1 119 ? -13.433 -0.956  15.818  0.50 31.02 ? 119 LEU A CG    1 
ATOM   1831  C  CD1   A LEU A 1 119 ? -13.765 0.239   15.196  0.50 33.07 ? 119 LEU A CD1   1 
ATOM   1832  C  CD1   B LEU A 1 119 ? -13.116 0.338   15.093  0.50 32.94 ? 119 LEU A CD1   1 
ATOM   1833  C  CD2   A LEU A 1 119 ? -13.658 -1.118  17.283  0.50 25.94 ? 119 LEU A CD2   1 
ATOM   1834  C  CD2   B LEU A 1 119 ? -13.500 -0.736  17.326  0.50 25.46 ? 119 LEU A CD2   1 
ATOM   1835  N  N     A ASP A 1 120 ? -17.291 -3.929  14.464  0.50 33.25 ? 120 ASP A N     1 
ATOM   1836  N  N     B ASP A 1 120 ? -16.876 -3.789  14.331  0.50 33.61 ? 120 ASP A N     1 
ATOM   1837  C  CA    A ASP A 1 120 ? -18.664 -4.328  14.165  0.50 30.79 ? 120 ASP A CA    1 
ATOM   1838  C  CA    B ASP A 1 120 ? -18.253 -4.107  13.965  0.50 30.89 ? 120 ASP A CA    1 
ATOM   1839  C  C     A ASP A 1 120 ? -19.105 -5.488  15.046  0.50 32.45 ? 120 ASP A C     1 
ATOM   1840  C  C     B ASP A 1 120 ? -18.837 -5.177  14.880  0.50 31.75 ? 120 ASP A C     1 
ATOM   1841  O  O     A ASP A 1 120 ? -20.260 -5.538  15.485  0.50 27.72 ? 120 ASP A O     1 
ATOM   1842  O  O     B ASP A 1 120 ? -20.005 -5.087  15.278  0.50 26.78 ? 120 ASP A O     1 
ATOM   1843  C  CB    A ASP A 1 120 ? -18.803 -4.697  12.687  0.50 30.07 ? 120 ASP A CB    1 
ATOM   1844  C  CB    B ASP A 1 120 ? -18.324 -4.549  12.502  0.50 31.30 ? 120 ASP A CB    1 
ATOM   1845  C  CG    A ASP A 1 120 ? -18.905 -3.481  11.788  0.50 37.02 ? 120 ASP A CG    1 
ATOM   1846  C  CG    B ASP A 1 120 ? -18.106 -3.399  11.526  0.50 37.28 ? 120 ASP A CG    1 
ATOM   1847  O  OD1   A ASP A 1 120 ? -18.895 -2.349  12.313  0.50 35.74 ? 120 ASP A OD1   1 
ATOM   1848  O  OD1   B ASP A 1 120 ? -17.879 -2.258  11.978  0.50 37.13 ? 120 ASP A OD1   1 
ATOM   1849  O  OD2   A ASP A 1 120 ? -18.994 -3.656  10.553  0.50 35.72 ? 120 ASP A OD2   1 
ATOM   1850  O  OD2   B ASP A 1 120 ? -18.162 -3.639  10.302  0.50 33.61 ? 120 ASP A OD2   1 
ATOM   1851  N  N     A ARG A 1 121 ? -18.200 -6.429  15.321  0.50 27.58 ? 121 ARG A N     1 
ATOM   1852  N  N     B ARG A 1 121 ? -18.039 -6.191  15.235  0.50 26.95 ? 121 ARG A N     1 
ATOM   1853  C  CA    A ARG A 1 121 ? -18.542 -7.523  16.224  0.50 31.60 ? 121 ARG A CA    1 
ATOM   1854  C  CA    B ARG A 1 121 ? -18.544 -7.261  16.093  0.50 31.44 ? 121 ARG A CA    1 
ATOM   1855  C  C     A ARG A 1 121 ? -18.690 -7.023  17.658  0.50 30.13 ? 121 ARG A C     1 
ATOM   1856  C  C     B ARG A 1 121 ? -18.722 -6.783  17.532  0.50 29.89 ? 121 ARG A C     1 
ATOM   1857  O  O     A ARG A 1 121 ? -19.554 -7.504  18.403  0.50 31.77 ? 121 ARG A O     1 
ATOM   1858  O  O     B ARG A 1 121 ? -19.658 -7.206  18.221  0.50 31.23 ? 121 ARG A O     1 
ATOM   1859  C  CB    A ARG A 1 121 ? -17.490 -8.628  16.123  0.50 27.66 ? 121 ARG A CB    1 
ATOM   1860  C  CB    B ARG A 1 121 ? -17.609 -8.471  16.034  0.50 28.04 ? 121 ARG A CB    1 
ATOM   1861  C  CG    A ARG A 1 121 ? -17.469 -9.346  14.777  0.50 32.08 ? 121 ARG A CG    1 
ATOM   1862  C  CG    B ARG A 1 121 ? -17.516 -9.136  14.659  0.50 32.02 ? 121 ARG A CG    1 
ATOM   1863  C  CD    A ARG A 1 121 ? -18.643 -10.314 14.631  0.50 30.77 ? 121 ARG A CD    1 
ATOM   1864  C  CD    B ARG A 1 121 ? -18.575 -10.223 14.471  0.50 31.17 ? 121 ARG A CD    1 
ATOM   1865  N  NE    A ARG A 1 121 ? -18.766 -10.830 13.271  0.50 32.73 ? 121 ARG A NE    1 
ATOM   1866  N  NE    B ARG A 1 121 ? -18.620 -10.713 13.096  0.50 33.54 ? 121 ARG A NE    1 
ATOM   1867  C  CZ    A ARG A 1 121 ? -18.004 -11.786 12.752  0.50 36.74 ? 121 ARG A CZ    1 
ATOM   1868  C  CZ    B ARG A 1 121 ? -17.824 -11.654 12.603  0.50 36.58 ? 121 ARG A CZ    1 
ATOM   1869  N  NH1   A ARG A 1 121 ? -17.041 -12.362 13.454  0.50 31.01 ? 121 ARG A NH1   1 
ATOM   1870  N  NH1   B ARG A 1 121 ? -16.902 -12.243 13.347  0.50 31.08 ? 121 ARG A NH1   1 
ATOM   1871  N  NH2   A ARG A 1 121 ? -18.211 -12.171 11.495  0.50 33.83 ? 121 ARG A NH2   1 
ATOM   1872  N  NH2   B ARG A 1 121 ? -17.959 -12.015 11.329  0.50 32.42 ? 121 ARG A NH2   1 
ATOM   1873  N  N     A ILE A 1 122 ? -17.862 -6.054  18.060  0.50 27.42 ? 122 ILE A N     1 
ATOM   1874  N  N     B ILE A 1 122 ? -17.828 -5.912  18.006  0.50 27.42 ? 122 ILE A N     1 
ATOM   1875  C  CA    A ILE A 1 122 ? -18.063 -5.383  19.342  0.50 31.30 ? 122 ILE A CA    1 
ATOM   1876  C  CA    B ILE A 1 122 ? -18.014 -5.295  19.318  0.50 31.30 ? 122 ILE A CA    1 
ATOM   1877  C  C     A ILE A 1 122 ? -19.409 -4.670  19.360  0.50 32.02 ? 122 ILE A C     1 
ATOM   1878  C  C     B ILE A 1 122 ? -19.279 -4.446  19.327  0.50 32.17 ? 122 ILE A C     1 
ATOM   1879  O  O     A ILE A 1 122 ? -20.121 -4.672  20.374  0.50 28.68 ? 122 ILE A O     1 
ATOM   1880  O  O     B ILE A 1 122 ? -20.002 -4.385  20.331  0.50 28.97 ? 122 ILE A O     1 
ATOM   1881  C  CB    A ILE A 1 122 ? -16.902 -4.408  19.619  0.50 27.89 ? 122 ILE A CB    1 
ATOM   1882  C  CB    B ILE A 1 122 ? -16.766 -4.475  19.695  0.50 28.01 ? 122 ILE A CB    1 
ATOM   1883  C  CG1   A ILE A 1 122 ? -15.634 -5.172  19.994  0.50 26.50 ? 122 ILE A CG1   1 
ATOM   1884  C  CG1   B ILE A 1 122 ? -15.609 -5.414  20.038  0.50 26.49 ? 122 ILE A CG1   1 
ATOM   1885  C  CG2   A ILE A 1 122 ? -17.267 -3.403  20.716  0.50 23.57 ? 122 ILE A CG2   1 
ATOM   1886  C  CG2   B ILE A 1 122 ? -17.057 -3.515  20.854  0.50 23.30 ? 122 ILE A CG2   1 
ATOM   1887  C  CD1   A ILE A 1 122 ? -14.411 -4.281  20.125  0.50 29.84 ? 122 ILE A CD1   1 
ATOM   1888  C  CD1   B ILE A 1 122 ? -14.244 -4.759  19.943  0.50 30.61 ? 122 ILE A CD1   1 
ATOM   1889  N  N     A ARG A 1 123 ? -19.783 -4.057  18.232  0.50 29.80 ? 123 ARG A N     1 
ATOM   1890  N  N     B ARG A 1 123 ? -19.572 -3.788  18.201  0.50 30.01 ? 123 ARG A N     1 
ATOM   1891  C  CA    A ARG A 1 123 ? -21.033 -3.307  18.163  0.50 28.48 ? 123 ARG A CA    1 
ATOM   1892  C  CA    B ARG A 1 123 ? -20.791 -2.994  18.089  0.50 29.64 ? 123 ARG A CA    1 
ATOM   1893  C  C     A ARG A 1 123 ? -22.241 -4.216  18.348  0.50 32.58 ? 123 ARG A C     1 
ATOM   1894  C  C     B ARG A 1 123 ? -22.033 -3.863  18.232  0.50 32.28 ? 123 ARG A C     1 
ATOM   1895  O  O     A ARG A 1 123 ? -23.246 -3.805  18.939  0.50 29.24 ? 123 ARG A O     1 
ATOM   1896  O  O     B ARG A 1 123 ? -23.010 -3.460  18.876  0.50 26.68 ? 123 ARG A O     1 
ATOM   1897  C  CB    A ARG A 1 123 ? -21.123 -2.565  16.831  0.50 32.00 ? 123 ARG A CB    1 
ATOM   1898  C  CB    B ARG A 1 123 ? -20.805 -2.251  16.753  0.50 33.45 ? 123 ARG A CB    1 
ATOM   1899  C  CG    A ARG A 1 123 ? -22.258 -1.554  16.754  0.50 35.68 ? 123 ARG A CG    1 
ATOM   1900  C  CG    B ARG A 1 123 ? -22.129 -1.576  16.423  0.50 36.55 ? 123 ARG A CG    1 
ATOM   1901  C  CD    A ARG A 1 123 ? -22.111 -0.634  15.547  0.50 34.68 ? 123 ARG A CD    1 
ATOM   1902  C  CD    B ARG A 1 123 ? -22.458 -0.490  17.430  0.50 35.66 ? 123 ARG A CD    1 
ATOM   1903  N  NE    A ARG A 1 123 ? -20.745 -0.150  15.382  0.50 40.67 ? 123 ARG A NE    1 
ATOM   1904  N  NE    B ARG A 1 123 ? -21.507 0.614   17.372  0.50 32.46 ? 123 ARG A NE    1 
ATOM   1905  C  CZ    A ARG A 1 123 ? -20.003 -0.367  14.304  0.50 35.19 ? 123 ARG A CZ    1 
ATOM   1906  C  CZ    B ARG A 1 123 ? -21.453 1.599   18.257  0.50 39.62 ? 123 ARG A CZ    1 
ATOM   1907  N  NH1   A ARG A 1 123 ? -20.481 -1.018  13.256  0.50 39.12 ? 123 ARG A NH1   1 
ATOM   1908  N  NH1   B ARG A 1 123 ? -22.267 1.636   19.300  0.50 41.63 ? 123 ARG A NH1   1 
ATOM   1909  N  NH2   A ARG A 1 123 ? -18.751 0.083   14.276  0.50 39.67 ? 123 ARG A NH2   1 
ATOM   1910  N  NH2   B ARG A 1 123 ? -20.560 2.571   18.093  0.50 32.23 ? 123 ARG A NH2   1 
ATOM   1911  N  N     A LYS A 1 124 ? -22.162 -5.454  17.850  0.50 30.87 ? 124 LYS A N     1 
ATOM   1912  N  N     B LYS A 1 124 ? -22.013 -5.056  17.633  0.50 29.70 ? 124 LYS A N     1 
ATOM   1913  C  CA    A LYS A 1 124 ? -23.268 -6.391  18.020  0.50 33.00 ? 124 LYS A CA    1 
ATOM   1914  C  CA    B LYS A 1 124 ? -23.143 -5.973  17.758  0.50 33.08 ? 124 LYS A CA    1 
ATOM   1915  C  C     A LYS A 1 124 ? -23.445 -6.797  19.478  0.50 33.17 ? 124 LYS A C     1 
ATOM   1916  C  C     B LYS A 1 124 ? -23.410 -6.318  19.218  0.50 32.33 ? 124 LYS A C     1 
ATOM   1917  O  O     A LYS A 1 124 ? -24.571 -7.064  19.914  0.50 26.36 ? 124 LYS A O     1 
ATOM   1918  O  O     B LYS A 1 124 ? -24.564 -6.326  19.665  0.50 28.48 ? 124 LYS A O     1 
ATOM   1919  C  CB    A LYS A 1 124 ? -23.047 -7.624  17.146  0.50 31.82 ? 124 LYS A CB    1 
ATOM   1920  C  CB    B LYS A 1 124 ? -22.878 -7.241  16.948  0.50 30.78 ? 124 LYS A CB    1 
ATOM   1921  C  CG    A LYS A 1 124 ? -24.148 -8.670  17.259  0.50 34.90 ? 124 LYS A CG    1 
ATOM   1922  C  CG    B LYS A 1 124 ? -23.898 -8.348  17.172  0.50 36.34 ? 124 LYS A CG    1 
ATOM   1923  C  CD    A LYS A 1 124 ? -23.983 -9.768  16.221  0.50 39.10 ? 124 LYS A CD    1 
ATOM   1924  C  CD    B LYS A 1 124 ? -23.509 -9.620  16.431  0.50 39.14 ? 124 LYS A CD    1 
ATOM   1925  C  CE    A LYS A 1 124 ? -25.079 -10.807 16.356  0.50 39.36 ? 124 LYS A CE    1 
ATOM   1926  C  CE    B LYS A 1 124 ? -24.539 -10.715 16.648  0.50 38.72 ? 124 LYS A CE    1 
ATOM   1927  N  NZ    A LYS A 1 124 ? -25.046 -11.802 15.255  0.50 29.17 ? 124 LYS A NZ    1 
ATOM   1928  N  NZ    B LYS A 1 124 ? -24.180 -11.967 15.933  0.50 38.66 ? 124 LYS A NZ    1 
ATOM   1929  N  N     A LEU A 1 125 ? -22.351 -6.861  20.240  0.50 31.53 ? 125 LEU A N     1 
ATOM   1930  N  N     B LEU A 1 125 ? -22.350 -6.616  19.974  0.50 31.92 ? 125 LEU A N     1 
ATOM   1931  C  CA    A LEU A 1 125 ? -22.468 -7.099  21.674  0.50 28.94 ? 125 LEU A CA    1 
ATOM   1932  C  CA    B LEU A 1 125 ? -22.500 -6.891  21.400  0.50 28.07 ? 125 LEU A CA    1 
ATOM   1933  C  C     A LEU A 1 125 ? -22.968 -5.856  22.397  0.50 32.91 ? 125 LEU A C     1 
ATOM   1934  C  C     B LEU A 1 125 ? -23.007 -5.663  22.143  0.50 32.04 ? 125 LEU A C     1 
ATOM   1935  O  O     A LEU A 1 125 ? -23.707 -5.959  23.383  0.50 33.38 ? 125 LEU A O     1 
ATOM   1936  O  O     B LEU A 1 125 ? -23.926 -5.756  22.964  0.50 34.52 ? 125 LEU A O     1 
ATOM   1937  C  CB    A LEU A 1 125 ? -21.125 -7.549  22.250  0.50 29.24 ? 125 LEU A CB    1 
ATOM   1938  C  CB    B LEU A 1 125 ? -21.166 -7.354  21.992  0.50 29.70 ? 125 LEU A CB    1 
ATOM   1939  C  CG    A LEU A 1 125 ? -20.820 -9.044  22.177  0.50 28.13 ? 125 LEU A CG    1 
ATOM   1940  C  CG    B LEU A 1 125 ? -20.537 -8.648  21.476  0.50 31.78 ? 125 LEU A CG    1 
ATOM   1941  C  CD1   A LEU A 1 125 ? -19.509 -9.356  22.870  0.50 28.43 ? 125 LEU A CD1   1 
ATOM   1942  C  CD1   B LEU A 1 125 ? -19.091 -8.738  21.929  0.50 29.33 ? 125 LEU A CD1   1 
ATOM   1943  C  CD2   A LEU A 1 125 ? -21.958 -9.847  22.790  0.50 32.39 ? 125 LEU A CD2   1 
ATOM   1944  C  CD2   B LEU A 1 125 ? -21.315 -9.860  21.951  0.50 32.02 ? 125 LEU A CD2   1 
ATOM   1945  N  N     A ALA A 1 126 ? -22.565 -4.672  21.928  0.50 30.85 ? 126 ALA A N     1 
ATOM   1946  N  N     B ALA A 1 126 ? -22.411 -4.500  21.868  0.50 30.65 ? 126 ALA A N     1 
ATOM   1947  C  CA    A ALA A 1 126 ? -23.060 -3.437  22.525  0.50 30.99 ? 126 ALA A CA    1 
ATOM   1948  C  CA    B ALA A 1 126 ? -22.767 -3.283  22.593  0.50 30.79 ? 126 ALA A CA    1 
ATOM   1949  C  C     A ALA A 1 126 ? -24.554 -3.270  22.282  0.50 35.18 ? 126 ALA A C     1 
ATOM   1950  C  C     B ALA A 1 126 ? -24.240 -2.937  22.406  0.50 35.48 ? 126 ALA A C     1 
ATOM   1951  O  O     A ALA A 1 126 ? -25.289 -2.841  23.181  0.50 30.26 ? 126 ALA A O     1 
ATOM   1952  O  O     B ALA A 1 126 ? -24.938 -2.603  23.372  0.50 28.79 ? 126 ALA A O     1 
ATOM   1953  C  CB    A ALA A 1 126 ? -22.286 -2.238  21.976  0.50 30.98 ? 126 ALA A CB    1 
ATOM   1954  C  CB    B ALA A 1 126 ? -21.877 -2.126  22.139  0.50 30.77 ? 126 ALA A CB    1 
ATOM   1955  N  N     A ASP A 1 127 ? -25.024 -3.622  21.078  0.50 31.65 ? 127 ASP A N     1 
ATOM   1956  N  N     B ASP A 1 127 ? -24.731 -3.017  21.163  0.50 28.98 ? 127 ASP A N     1 
ATOM   1957  C  CA    A ASP A 1 127 ? -26.448 -3.555  20.754  0.50 31.98 ? 127 ASP A CA    1 
ATOM   1958  C  CA    B ASP A 1 127 ? -26.138 -2.746  20.884  0.50 29.98 ? 127 ASP A CA    1 
ATOM   1959  C  C     A ASP A 1 127 ? -27.318 -4.309  21.753  0.50 31.33 ? 127 ASP A C     1 
ATOM   1960  C  C     B ASP A 1 127 ? -27.074 -3.716  21.596  0.50 31.71 ? 127 ASP A C     1 
ATOM   1961  O  O     A ASP A 1 127 ? -28.529 -4.069  21.811  0.50 34.44 ? 127 ASP A O     1 
ATOM   1962  O  O     B ASP A 1 127 ? -28.243 -3.384  21.813  0.50 35.97 ? 127 ASP A O     1 
ATOM   1963  C  CB    A ASP A 1 127 ? -26.696 -4.119  19.350  0.50 30.08 ? 127 ASP A CB    1 
ATOM   1964  C  CB    B ASP A 1 127 ? -26.396 -2.801  19.378  0.50 31.22 ? 127 ASP A CB    1 
ATOM   1965  C  CG    A ASP A 1 127 ? -26.279 -3.164  18.250  0.50 27.50 ? 127 ASP A CG    1 
ATOM   1966  C  CG    B ASP A 1 127 ? -25.878 -1.577  18.653  0.50 28.24 ? 127 ASP A CG    1 
ATOM   1967  O  OD1   A ASP A 1 127 ? -25.919 -2.013  18.565  0.50 27.17 ? 127 ASP A OD1   1 
ATOM   1968  O  OD1   B ASP A 1 127 ? -25.427 -0.625  19.328  0.50 24.73 ? 127 ASP A OD1   1 
ATOM   1969  O  OD2   A ASP A 1 127 ? -26.322 -3.564  17.066  0.50 34.40 ? 127 ASP A OD2   1 
ATOM   1970  O  OD2   B ASP A 1 127 ? -25.920 -1.571  17.403  0.50 35.06 ? 127 ASP A OD2   1 
ATOM   1971  N  N     A GLN A 1 128 ? -26.737 -5.213  22.535  0.50 33.40 ? 128 GLN A N     1 
ATOM   1972  N  N     B GLN A 1 128 ? -26.590 -4.903  21.955  0.50 33.33 ? 128 GLN A N     1 
ATOM   1973  C  CA    A GLN A 1 128 ? -27.483 -6.036  23.475  0.50 33.12 ? 128 GLN A CA    1 
ATOM   1974  C  CA    B GLN A 1 128 ? -27.381 -5.921  22.634  0.50 33.70 ? 128 GLN A CA    1 
ATOM   1975  C  C     A GLN A 1 128 ? -27.376 -5.544  24.913  0.50 32.94 ? 128 GLN A C     1 
ATOM   1976  C  C     B GLN A 1 128 ? -27.599 -5.611  24.110  0.50 35.88 ? 128 GLN A C     1 
ATOM   1977  O  O     A GLN A 1 128 ? -27.961 -6.161  25.809  0.50 26.36 ? 128 GLN A O     1 
ATOM   1978  O  O     B GLN A 1 128 ? -28.309 -6.361  24.789  0.50 35.10 ? 128 GLN A O     1 
ATOM   1979  C  CB    A GLN A 1 128 ? -27.010 -7.489  23.373  0.50 28.92 ? 128 GLN A CB    1 
ATOM   1980  C  CB    B GLN A 1 128 ? -26.693 -7.282  22.480  0.50 37.83 ? 128 GLN A CB    1 
ATOM   1981  C  CG    A GLN A 1 128 ? -27.149 -8.053  21.960  0.50 38.07 ? 128 GLN A CG    1 
ATOM   1982  C  CG    B GLN A 1 128 ? -27.590 -8.499  22.613  0.50 40.87 ? 128 GLN A CG    1 
ATOM   1983  C  CD    A GLN A 1 128 ? -26.427 -9.374  21.764  0.50 41.64 ? 128 GLN A CD    1 
ATOM   1984  C  CD    B GLN A 1 128 ? -26.814 -9.796  22.449  0.50 46.44 ? 128 GLN A CD    1 
ATOM   1985  O  OE1   A GLN A 1 128 ? -25.908 -9.654  20.682  0.50 43.36 ? 128 GLN A OE1   1 
ATOM   1986  O  OE1   B GLN A 1 128 ? -25.595 -9.782  22.267  0.50 41.52 ? 128 GLN A OE1   1 
ATOM   1987  N  NE2   A GLN A 1 128 ? -26.394 -10.196 22.808  0.50 48.02 ? 128 GLN A NE2   1 
ATOM   1988  N  NE2   B GLN A 1 128 ? -27.515 -10.922 22.516  0.50 46.85 ? 128 GLN A NE2   1 
ATOM   1989  N  N     A CYS A 1 129 ? -26.660 -4.448  25.151  0.50 33.04 ? 129 CYS A N     1 
ATOM   1990  N  N     B CYS A 1 129 ? -27.020 -4.528  24.618  0.50 31.87 ? 129 CYS A N     1 
ATOM   1991  C  CA    A CYS A 1 129 ? -26.506 -3.877  26.482  0.50 31.26 ? 129 CYS A CA    1 
ATOM   1992  C  CA    B CYS A 1 129 ? -27.088 -4.188  26.029  0.50 34.45 ? 129 CYS A CA    1 
ATOM   1993  C  C     A CYS A 1 129 ? -27.540 -2.778  26.702  0.50 29.60 ? 129 CYS A C     1 
ATOM   1994  C  C     B CYS A 1 129 ? -27.994 -2.980  26.238  0.50 30.99 ? 129 CYS A C     1 
ATOM   1995  O  O     A CYS A 1 129 ? -27.839 -2.002  25.790  0.50 35.57 ? 129 CYS A O     1 
ATOM   1996  O  O     B CYS A 1 129 ? -28.138 -2.129  25.356  0.50 35.54 ? 129 CYS A O     1 
ATOM   1997  C  CB    A CYS A 1 129 ? -25.093 -3.314  26.672  0.50 30.68 ? 129 CYS A CB    1 
ATOM   1998  C  CB    B CYS A 1 129 ? -25.688 -3.895  26.579  0.50 33.40 ? 129 CYS A CB    1 
ATOM   1999  S  SG    A CYS A 1 129 ? -23.757 -4.548  26.564  0.50 25.20 ? 129 CYS A SG    1 
ATOM   2000  S  SG    B CYS A 1 129 ? -24.404 -5.075  26.036  0.50 28.78 ? 129 CYS A SG    1 
ATOM   2001  N  N     A THR A 1 130 ? -28.085 -2.715  27.919  0.50 32.11 ? 130 THR A N     1 
ATOM   2002  N  N     B THR A 1 130 ? -28.607 -2.912  27.418  0.50 32.64 ? 130 THR A N     1 
ATOM   2003  C  CA    A THR A 1 130 ? -29.010 -1.635  28.255  0.50 31.77 ? 130 THR A CA    1 
ATOM   2004  C  CA    B THR A 1 130 ? -29.415 -1.762  27.804  0.50 31.38 ? 130 THR A CA    1 
ATOM   2005  C  C     A THR A 1 130 ? -28.264 -0.388  28.714  0.50 35.79 ? 130 THR A C     1 
ATOM   2006  C  C     B THR A 1 130 ? -28.653 -0.766  28.665  0.50 34.85 ? 130 THR A C     1 
ATOM   2007  O  O     A THR A 1 130 ? -28.627 0.732   28.335  0.50 36.58 ? 130 THR A O     1 
ATOM   2008  O  O     B THR A 1 130 ? -29.133 0.356   28.861  0.50 36.73 ? 130 THR A O     1 
ATOM   2009  C  CB    A THR A 1 130 ? -29.995 -2.088  29.338  0.50 29.08 ? 130 THR A CB    1 
ATOM   2010  C  CB    B THR A 1 130 ? -30.675 -2.215  28.558  0.50 32.17 ? 130 THR A CB    1 
ATOM   2011  O  OG1   A THR A 1 130 ? -29.272 -2.491  30.508  0.50 32.59 ? 130 THR A OG1   1 
ATOM   2012  O  OG1   B THR A 1 130 ? -30.306 -3.084  29.637  0.50 30.11 ? 130 THR A OG1   1 
ATOM   2013  C  CG2   A THR A 1 130 ? -30.842 -3.255  28.840  0.50 30.37 ? 130 THR A CG2   1 
ATOM   2014  C  CG2   B THR A 1 130 ? -31.627 -2.946  27.624  0.50 32.14 ? 130 THR A CG2   1 
ATOM   2015  N  N     A GLY A 1 131 ? -27.230 -0.562  29.534  0.50 29.99 ? 131 GLY A N     1 
ATOM   2016  N  N     B GLY A 1 131 ? -27.489 -1.149  29.187  0.50 28.12 ? 131 GLY A N     1 
ATOM   2017  C  CA    A GLY A 1 131 ? -26.433 0.555   30.000  0.50 29.21 ? 131 GLY A CA    1 
ATOM   2018  C  CA    B GLY A 1 131 ? -26.702 -0.264  30.020  0.50 28.30 ? 131 GLY A CA    1 
ATOM   2019  C  C     A GLY A 1 131 ? -24.970 0.188   30.144  0.50 28.58 ? 131 GLY A C     1 
ATOM   2020  C  C     B GLY A 1 131 ? -25.226 -0.602  29.993  0.50 32.31 ? 131 GLY A C     1 
ATOM   2021  O  O     A GLY A 1 131 ? -24.463 0.059   31.263  0.50 25.24 ? 131 GLY A O     1 
ATOM   2022  O  O     B GLY A 1 131 ? -24.656 -1.002  31.012  0.50 32.75 ? 131 GLY A O     1 
ATOM   2023  N  N     A LEU A 1 132 ? -24.290 0.009   29.011  0.50 25.41 ? 132 LEU A N     1 
ATOM   2024  N  N     B LEU A 1 132 ? -24.599 -0.454  28.828  0.50 26.17 ? 132 LEU A N     1 
ATOM   2025  C  CA    A LEU A 1 132 ? -22.897 -0.424  29.010  0.50 24.76 ? 132 LEU A CA    1 
ATOM   2026  C  CA    B LEU A 1 132 ? -23.178 -0.742  28.695  0.50 25.29 ? 132 LEU A CA    1 
ATOM   2027  C  C     A LEU A 1 132 ? -22.040 0.492   29.874  0.50 26.16 ? 132 LEU A C     1 
ATOM   2028  C  C     B LEU A 1 132 ? -22.363 0.292   29.460  0.50 25.62 ? 132 LEU A C     1 
ATOM   2029  O  O     A LEU A 1 132 ? -22.110 1.717   29.760  0.50 26.61 ? 132 LEU A O     1 
ATOM   2030  O  O     B LEU A 1 132 ? -22.541 1.499   29.272  0.50 27.88 ? 132 LEU A O     1 
ATOM   2031  C  CB    A LEU A 1 132 ? -22.365 -0.444  27.575  0.50 29.21 ? 132 LEU A CB    1 
ATOM   2032  C  CB    B LEU A 1 132 ? -22.783 -0.750  27.219  0.50 27.00 ? 132 LEU A CB    1 
ATOM   2033  C  CG    A LEU A 1 132 ? -20.862 -0.666  27.367  0.50 23.31 ? 132 LEU A CG    1 
ATOM   2034  C  CG    B LEU A 1 132 ? -21.308 -0.935  26.847  0.50 27.49 ? 132 LEU A CG    1 
ATOM   2035  C  CD1   A LEU A 1 132 ? -20.444 -2.054  27.833  0.50 25.18 ? 132 LEU A CD1   1 
ATOM   2036  C  CD1   B LEU A 1 132 ? -20.843 -2.358  27.122  0.50 25.39 ? 132 LEU A CD1   1 
ATOM   2037  C  CD2   A LEU A 1 132 ? -20.489 -0.454  25.906  0.50 28.84 ? 132 LEU A CD2   1 
ATOM   2038  C  CD2   B LEU A 1 132 ? -21.085 -0.564  25.390  0.50 28.46 ? 132 LEU A CD2   1 
ATOM   2039  N  N     A GLN A 1 133 ? -21.242 -0.112  30.758  0.50 25.42 ? 133 GLN A N     1 
ATOM   2040  N  N     B GLN A 1 133 ? -21.470 -0.176  30.332  0.50 24.16 ? 133 GLN A N     1 
ATOM   2041  C  CA    A GLN A 1 133 ? -20.306 0.677   31.553  0.50 27.28 ? 133 GLN A CA    1 
ATOM   2042  C  CA    B GLN A 1 133 ? -20.673 0.738   31.135  0.50 26.85 ? 133 GLN A CA    1 
ATOM   2043  C  C     A GLN A 1 133 ? -19.029 0.958   30.777  0.50 24.34 ? 133 GLN A C     1 
ATOM   2044  C  C     B GLN A 1 133 ? -19.187 0.713   30.810  0.50 24.23 ? 133 GLN A C     1 
ATOM   2045  O  O     A GLN A 1 133 ? -18.514 2.083   30.802  0.50 25.53 ? 133 GLN A O     1 
ATOM   2046  O  O     B GLN A 1 133 ? -18.473 1.634   31.224  0.50 26.04 ? 133 GLN A O     1 
ATOM   2047  C  CB    A GLN A 1 133 ? -19.946 -0.043  32.851  0.50 27.39 ? 133 GLN A CB    1 
ATOM   2048  C  CB    B GLN A 1 133 ? -20.873 0.466   32.635  0.50 27.61 ? 133 GLN A CB    1 
ATOM   2049  C  CG    A GLN A 1 133 ? -20.971 -1.015  33.368  0.50 28.98 ? 133 GLN A CG    1 
ATOM   2050  C  CG    B GLN A 1 133 ? -20.491 -0.919  33.115  0.50 28.87 ? 133 GLN A CG    1 
ATOM   2051  C  CD    A GLN A 1 133 ? -20.656 -1.480  34.778  0.50 30.53 ? 133 GLN A CD    1 
ATOM   2052  C  CD    B GLN A 1 133 ? -20.323 -0.967  34.628  0.50 30.15 ? 133 GLN A CD    1 
ATOM   2053  O  OE1   A GLN A 1 133 ? -19.865 -0.855  35.483  0.50 31.05 ? 133 GLN A OE1   1 
ATOM   2054  O  OE1   B GLN A 1 133 ? -20.018 0.045   35.255  0.50 28.92 ? 133 GLN A OE1   1 
ATOM   2055  N  NE2   A GLN A 1 133 ? -21.267 -2.584  35.193  0.50 27.58 ? 133 GLN A NE2   1 
ATOM   2056  N  NE2   B GLN A 1 133 ? -20.525 -2.142  35.219  0.50 27.61 ? 133 GLN A NE2   1 
ATOM   2057  N  N     A GLY A 1 134 ? -18.502 -0.056  30.109  0.50 26.77 ? 134 GLY A N     1 
ATOM   2058  N  N     B GLY A 1 134 ? -18.695 -0.291  30.096  0.50 26.91 ? 134 GLY A N     1 
ATOM   2059  C  CA    A GLY A 1 134 ? -17.246 0.069   29.396  0.50 27.71 ? 134 GLY A CA    1 
ATOM   2060  C  CA    B GLY A 1 134 ? -17.333 -0.224  29.611  0.50 27.08 ? 134 GLY A CA    1 
ATOM   2061  C  C     A GLY A 1 134 ? -16.653 -1.302  29.112  0.50 22.54 ? 134 GLY A C     1 
ATOM   2062  C  C     B GLY A 1 134 ? -16.736 -1.584  29.296  0.50 22.23 ? 134 GLY A C     1 
ATOM   2063  O  O     A GLY A 1 134 ? -17.373 -2.297  29.024  0.50 22.53 ? 134 GLY A O     1 
ATOM   2064  O  O     B GLY A 1 134 ? -17.423 -2.606  29.273  0.50 20.66 ? 134 GLY A O     1 
ATOM   2065  N  N     A PHE A 1 135 ? -15.329 -1.328  28.992  0.50 27.79 ? 135 PHE A N     1 
ATOM   2066  N  N     B PHE A 1 135 ? -15.426 -1.560  29.055  0.50 27.49 ? 135 PHE A N     1 
ATOM   2067  C  CA    A PHE A 1 135 ? -14.633 -2.483  28.447  0.50 24.98 ? 135 PHE A CA    1 
ATOM   2068  C  CA    B PHE A 1 135 ? -14.679 -2.707  28.563  0.50 24.53 ? 135 PHE A CA    1 
ATOM   2069  C  C     A PHE A 1 135 ? -13.540 -2.963  29.387  0.50 22.76 ? 135 PHE A C     1 
ATOM   2070  C  C     B PHE A 1 135 ? -13.520 -3.035  29.496  0.50 22.75 ? 135 PHE A C     1 
ATOM   2071  O  O     A PHE A 1 135 ? -12.891 -2.161  30.065  0.50 24.46 ? 135 PHE A O     1 
ATOM   2072  O  O     B PHE A 1 135 ? -12.997 -2.162  30.195  0.50 24.13 ? 135 PHE A O     1 
ATOM   2073  C  CB    A PHE A 1 135 ? -14.023 -2.146  27.076  0.50 25.93 ? 135 PHE A CB    1 
ATOM   2074  C  CB    B PHE A 1 135 ? -14.131 -2.448  27.143  0.50 26.58 ? 135 PHE A CB    1 
ATOM   2075  C  CG    A PHE A 1 135 ? -14.960 -1.403  26.169  0.50 23.14 ? 135 PHE A CG    1 
ATOM   2076  C  CG    B PHE A 1 135 ? -15.176 -2.008  26.152  0.50 22.72 ? 135 PHE A CG    1 
ATOM   2077  C  CD1   A PHE A 1 135 ? -15.926 -2.080  25.446  0.50 22.68 ? 135 PHE A CD1   1 
ATOM   2078  C  CD1   B PHE A 1 135 ? -15.450 -0.663  25.963  0.50 23.31 ? 135 PHE A CD1   1 
ATOM   2079  C  CD2   A PHE A 1 135 ? -14.879 -0.026  26.047  0.50 24.52 ? 135 PHE A CD2   1 
ATOM   2080  C  CD2   B PHE A 1 135 ? -15.876 -2.940  25.404  0.50 24.02 ? 135 PHE A CD2   1 
ATOM   2081  C  CE1   A PHE A 1 135 ? -16.798 -1.398  24.616  0.50 25.95 ? 135 PHE A CE1   1 
ATOM   2082  C  CE1   B PHE A 1 135 ? -16.412 -0.256  25.050  0.50 25.74 ? 135 PHE A CE1   1 
ATOM   2083  C  CE2   A PHE A 1 135 ? -15.741 0.663   25.214  0.50 26.52 ? 135 PHE A CE2   1 
ATOM   2084  C  CE2   B PHE A 1 135 ? -16.838 -2.542  24.491  0.50 22.67 ? 135 PHE A CE2   1 
ATOM   2085  C  CZ    A PHE A 1 135 ? -16.706 -0.024  24.502  0.50 25.45 ? 135 PHE A CZ    1 
ATOM   2086  C  CZ    B PHE A 1 135 ? -17.107 -1.198  24.314  0.50 25.27 ? 135 PHE A CZ    1 
ATOM   2087  N  N     A LEU A 1 136 ? -13.359 -4.280  29.425  0.50 20.15 ? 136 LEU A N     1 
ATOM   2088  N  N     B LEU A 1 136 ? -13.131 -4.311  29.500  0.50 20.15 ? 136 LEU A N     1 
ATOM   2089  C  CA    A LEU A 1 136 ? -12.175 -4.918  29.980  0.50 20.22 ? 136 LEU A CA    1 
ATOM   2090  C  CA    B LEU A 1 136 ? -11.919 -4.796  30.159  0.50 18.58 ? 136 LEU A CA    1 
ATOM   2091  C  C     A LEU A 1 136 ? -11.310 -5.381  28.814  0.50 17.59 ? 136 LEU A C     1 
ATOM   2092  C  C     B LEU A 1 136 ? -11.097 -5.522  29.100  0.50 17.67 ? 136 LEU A C     1 
ATOM   2093  O  O     A LEU A 1 136 ? -11.828 -5.922  27.833  0.50 21.10 ? 136 LEU A O     1 
ATOM   2094  O  O     B LEU A 1 136 ? -11.513 -6.576  28.604  0.50 16.87 ? 136 LEU A O     1 
ATOM   2095  C  CB    A LEU A 1 136 ? -12.550 -6.108  30.868  0.50 16.01 ? 136 LEU A CB    1 
ATOM   2096  C  CB    B LEU A 1 136 ? -12.235 -5.736  31.322  0.50 22.26 ? 136 LEU A CB    1 
ATOM   2097  C  CG    A LEU A 1 136 ? -13.577 -5.807  31.969  0.50 23.42 ? 136 LEU A CG    1 
ATOM   2098  C  CG    B LEU A 1 136 ? -13.143 -5.291  32.474  0.50 16.33 ? 136 LEU A CG    1 
ATOM   2099  C  CD1   A LEU A 1 136 ? -13.686 -6.958  32.963  0.50 22.47 ? 136 LEU A CD1   1 
ATOM   2100  C  CD1   B LEU A 1 136 ? -14.604 -5.441  32.102  0.50 19.99 ? 136 LEU A CD1   1 
ATOM   2101  C  CD2   A LEU A 1 136 ? -13.236 -4.515  32.678  0.50 18.90 ? 136 LEU A CD2   1 
ATOM   2102  C  CD2   B LEU A 1 136 ? -12.820 -6.097  33.726  0.50 24.66 ? 136 LEU A CD2   1 
ATOM   2103  N  N     A VAL A 1 137 ? -10.000 -5.151  28.912  0.50 21.62 ? 137 VAL A N     1 
ATOM   2104  N  N     B VAL A 1 137 ? -9.934  -4.972  28.759  0.50 21.94 ? 137 VAL A N     1 
ATOM   2105  C  CA    A VAL A 1 137 ? -9.080  -5.374  27.795  0.50 21.30 ? 137 VAL A CA    1 
ATOM   2106  C  CA    B VAL A 1 137 ? -9.129  -5.469  27.644  0.50 20.95 ? 137 VAL A CA    1 
ATOM   2107  C  C     A VAL A 1 137 ? -7.894  -6.203  28.279  0.50 18.31 ? 137 VAL A C     1 
ATOM   2108  C  C     B VAL A 1 137 ? -7.855  -6.101  28.194  0.50 18.23 ? 137 VAL A C     1 
ATOM   2109  O  O     A VAL A 1 137 ? -7.106  -5.735  29.108  0.50 20.84 ? 137 VAL A O     1 
ATOM   2110  O  O     B VAL A 1 137 ? -7.085  -5.446  28.907  0.50 19.05 ? 137 VAL A O     1 
ATOM   2111  C  CB    A VAL A 1 137 ? -8.595  -4.048  27.183  0.50 18.74 ? 137 VAL A CB    1 
ATOM   2112  C  CB    B VAL A 1 137 ? -8.803  -4.351  26.644  0.50 21.95 ? 137 VAL A CB    1 
ATOM   2113  C  CG1   A VAL A 1 137 ? -7.614  -4.314  26.051  0.50 21.35 ? 137 VAL A CG1   1 
ATOM   2114  C  CG1   B VAL A 1 137 ? -8.080  -4.921  25.442  0.50 20.99 ? 137 VAL A CG1   1 
ATOM   2115  C  CG2   A VAL A 1 137 ? -9.778  -3.227  26.687  0.50 23.58 ? 137 VAL A CG2   1 
ATOM   2116  C  CG2   B VAL A 1 137 ? -10.079 -3.635  26.222  0.50 23.95 ? 137 VAL A CG2   1 
ATOM   2117  N  N     A PHE A 1 138 ? -7.754  -7.416  27.739  0.50 18.47 ? 138 PHE A N     1 
ATOM   2118  N  N     B PHE A 1 138 ? -7.625  -7.364  27.834  0.50 18.41 ? 138 PHE A N     1 
ATOM   2119  C  CA    A PHE A 1 138 ? -6.709  -8.366  28.117  0.50 19.89 ? 138 PHE A CA    1 
ATOM   2120  C  CA    B PHE A 1 138 ? -6.517  -8.170  28.333  0.50 19.19 ? 138 PHE A CA    1 
ATOM   2121  C  C     A PHE A 1 138 ? -5.701  -8.471  26.979  0.50 18.27 ? 138 PHE A C     1 
ATOM   2122  C  C     B PHE A 1 138 ? -5.476  -8.315  27.232  0.50 18.21 ? 138 PHE A C     1 
ATOM   2123  O  O     A PHE A 1 138 ? -6.077  -8.823  25.855  0.50 19.11 ? 138 PHE A O     1 
ATOM   2124  O  O     B PHE A 1 138 ? -5.827  -8.647  26.094  0.50 20.39 ? 138 PHE A O     1 
ATOM   2125  C  CB    A PHE A 1 138 ? -7.296  -9.750  28.398  0.50 20.30 ? 138 PHE A CB    1 
ATOM   2126  C  CB    B PHE A 1 138 ? -6.992  -9.565  28.751  0.50 20.64 ? 138 PHE A CB    1 
ATOM   2127  C  CG    A PHE A 1 138 ? -8.069  -9.853  29.685  0.50 18.47 ? 138 PHE A CG    1 
ATOM   2128  C  CG    B PHE A 1 138 ? -8.107  -9.569  29.761  0.50 18.32 ? 138 PHE A CG    1 
ATOM   2129  C  CD1   A PHE A 1 138 ? -9.342  -9.319  29.795  0.50 20.52 ? 138 PHE A CD1   1 
ATOM   2130  C  CD1   B PHE A 1 138 ? -9.403  -9.223  29.400  0.50 19.60 ? 138 PHE A CD1   1 
ATOM   2131  C  CD2   A PHE A 1 138 ? -7.535  -10.525 30.772  0.50 16.69 ? 138 PHE A CD2   1 
ATOM   2132  C  CD2   B PHE A 1 138 ? -7.869  -9.966  31.065  0.50 23.33 ? 138 PHE A CD2   1 
ATOM   2133  C  CE1   A PHE A 1 138 ? -10.058 -9.427  30.982  0.50 23.15 ? 138 PHE A CE1   1 
ATOM   2134  C  CE1   B PHE A 1 138 ? -10.430 -9.241  30.327  0.50 26.35 ? 138 PHE A CE1   1 
ATOM   2135  C  CE2   A PHE A 1 138 ? -8.246  -10.642 31.954  0.50 28.05 ? 138 PHE A CE2   1 
ATOM   2136  C  CE2   B PHE A 1 138 ? -8.894  -9.986  31.995  0.50 23.09 ? 138 PHE A CE2   1 
ATOM   2137  C  CZ    A PHE A 1 138 ? -9.507  -10.093 32.056  0.50 24.11 ? 138 PHE A CZ    1 
ATOM   2138  C  CZ    B PHE A 1 138 ? -10.176 -9.622  31.623  0.50 20.36 ? 138 PHE A CZ    1 
ATOM   2139  N  N     A HIS A 1 139 ? -4.425  -8.212  27.274  0.50 18.43 ? 139 HIS A N     1 
ATOM   2140  N  N     B HIS A 1 139 ? -4.202  -8.111  27.571  0.50 17.19 ? 139 HIS A N     1 
ATOM   2141  C  CA    A HIS A 1 139 ? -3.437  -8.191  26.200  0.50 19.70 ? 139 HIS A CA    1 
ATOM   2142  C  CA    B HIS A 1 139 ? -3.168  -8.146  26.542  0.50 18.62 ? 139 HIS A CA    1 
ATOM   2143  C  C     A HIS A 1 139 ? -2.023  -8.205  26.771  0.50 18.21 ? 139 HIS A C     1 
ATOM   2144  C  C     B HIS A 1 139 ? -1.787  -8.194  27.182  0.50 17.90 ? 139 HIS A C     1 
ATOM   2145  O  O     A HIS A 1 139 ? -1.765  -7.649  27.841  0.50 20.02 ? 139 HIS A O     1 
ATOM   2146  O  O     B HIS A 1 139 ? -1.614  -7.885  28.364  0.50 20.24 ? 139 HIS A O     1 
ATOM   2147  C  CB    A HIS A 1 139 ? -3.628  -6.957  25.308  0.50 17.55 ? 139 HIS A CB    1 
ATOM   2148  C  CB    B HIS A 1 139 ? -3.279  -6.934  25.608  0.50 19.25 ? 139 HIS A CB    1 
ATOM   2149  C  CG    A HIS A 1 139 ? -3.336  -5.662  26.000  0.50 19.18 ? 139 HIS A CG    1 
ATOM   2150  C  CG    B HIS A 1 139 ? -2.925  -5.633  26.260  0.50 20.89 ? 139 HIS A CG    1 
ATOM   2151  N  ND1   A HIS A 1 139 ? -2.235  -4.888  25.698  0.50 18.70 ? 139 HIS A ND1   1 
ATOM   2152  N  ND1   B HIS A 1 139 ? -1.649  -5.108  26.233  0.50 19.31 ? 139 HIS A ND1   1 
ATOM   2153  C  CD2   A HIS A 1 139 ? -3.996  -5.007  26.985  0.50 18.45 ? 139 HIS A CD2   1 
ATOM   2154  C  CD2   B HIS A 1 139 ? -3.679  -4.750  26.957  0.50 20.17 ? 139 HIS A CD2   1 
ATOM   2155  C  CE1   A HIS A 1 139 ? -2.231  -3.812  26.465  0.50 20.87 ? 139 HIS A CE1   1 
ATOM   2156  C  CE1   B HIS A 1 139 ? -1.635  -3.957  26.881  0.50 20.90 ? 139 HIS A CE1   1 
ATOM   2157  N  NE2   A HIS A 1 139 ? -3.291  -3.857  27.250  0.50 20.15 ? 139 HIS A NE2   1 
ATOM   2158  N  NE2   B HIS A 1 139 ? -2.854  -3.715  27.328  0.50 17.76 ? 139 HIS A NE2   1 
ATOM   2159  N  N     A SER A 1 140 ? -1.104  -8.821  26.031  0.50 19.08 ? 140 SER A N     1 
ATOM   2160  N  N     B SER A 1 140 ? -0.803  -8.592  26.383  0.50 20.23 ? 140 SER A N     1 
ATOM   2161  C  CA    A SER A 1 140 ? 0.296   -8.768  26.425  0.50 19.50 ? 140 SER A CA    1 
ATOM   2162  C  CA    B SER A 1 140 ? 0.586   -8.488  26.800  0.50 18.93 ? 140 SER A CA    1 
ATOM   2163  C  C     A SER A 1 140 ? 0.885   -7.394  26.128  0.50 16.22 ? 140 SER A C     1 
ATOM   2164  C  C     B SER A 1 140 ? 1.159   -7.135  26.392  0.50 14.82 ? 140 SER A C     1 
ATOM   2165  O  O     A SER A 1 140 ? 0.411   -6.666  25.252  0.50 20.20 ? 140 SER A O     1 
ATOM   2166  O  O     B SER A 1 140 ? 0.637   -6.452  25.507  0.50 22.24 ? 140 SER A O     1 
ATOM   2167  C  CB    A SER A 1 140 ? 1.116   -9.838  25.697  0.50 20.90 ? 140 SER A CB    1 
ATOM   2168  C  CB    B SER A 1 140 ? 1.430   -9.612  26.190  0.50 20.57 ? 140 SER A CB    1 
ATOM   2169  O  OG    A SER A 1 140 ? 1.226   -9.564  24.306  0.50 19.15 ? 140 SER A OG    1 
ATOM   2170  O  OG    B SER A 1 140 ? 1.559   -9.460  24.787  0.50 17.70 ? 140 SER A OG    1 
ATOM   2171  N  N     A PHE A 1 141 ? 1.935   -7.047  26.878  0.50 17.12 ? 141 PHE A N     1 
ATOM   2172  N  N     B PHE A 1 141 ? 2.255   -6.753  27.052  0.50 19.40 ? 141 PHE A N     1 
ATOM   2173  C  CA    A PHE A 1 141 ? 2.786   -5.909  26.534  0.50 21.17 ? 141 PHE A CA    1 
ATOM   2174  C  CA    B PHE A 1 141 ? 3.083   -5.645  26.587  0.50 20.19 ? 141 PHE A CA    1 
ATOM   2175  C  C     A PHE A 1 141 ? 3.763   -6.265  25.416  0.50 21.59 ? 141 PHE A C     1 
ATOM   2176  C  C     B PHE A 1 141 ? 4.006   -6.046  25.442  0.50 21.97 ? 141 PHE A C     1 
ATOM   2177  O  O     A PHE A 1 141 ? 3.889   -5.537  24.425  0.50 22.66 ? 141 PHE A O     1 
ATOM   2178  O  O     B PHE A 1 141 ? 4.455   -5.178  24.683  0.50 19.06 ? 141 PHE A O     1 
ATOM   2179  C  CB    A PHE A 1 141 ? 3.586   -5.458  27.757  0.50 21.23 ? 141 PHE A CB    1 
ATOM   2180  C  CB    B PHE A 1 141 ? 3.955   -5.109  27.723  0.50 19.62 ? 141 PHE A CB    1 
ATOM   2181  C  CG    A PHE A 1 141 ? 2.918   -4.395  28.583  0.50 25.53 ? 141 PHE A CG    1 
ATOM   2182  C  CG    B PHE A 1 141 ? 3.272   -4.113  28.617  0.50 25.53 ? 141 PHE A CG    1 
ATOM   2183  C  CD1   A PHE A 1 141 ? 1.753   -3.780  28.157  0.50 24.09 ? 141 PHE A CD1   1 
ATOM   2184  C  CD1   B PHE A 1 141 ? 1.944   -3.772  28.429  0.50 24.20 ? 141 PHE A CD1   1 
ATOM   2185  C  CD2   A PHE A 1 141 ? 3.482   -3.997  29.785  0.50 22.73 ? 141 PHE A CD2   1 
ATOM   2186  C  CD2   B PHE A 1 141 ? 3.976   -3.508  29.646  0.50 22.30 ? 141 PHE A CD2   1 
ATOM   2187  C  CE1   A PHE A 1 141 ? 1.158   -2.795  28.922  0.50 27.65 ? 141 PHE A CE1   1 
ATOM   2188  C  CE1   B PHE A 1 141 ? 1.333   -2.849  29.253  0.50 28.92 ? 141 PHE A CE1   1 
ATOM   2189  C  CE2   A PHE A 1 141 ? 2.891   -3.015  30.557  0.50 32.51 ? 141 PHE A CE2   1 
ATOM   2190  C  CE2   B PHE A 1 141 ? 3.371   -2.584  30.473  0.50 29.63 ? 141 PHE A CE2   1 
ATOM   2191  C  CZ    A PHE A 1 141 ? 1.728   -2.416  30.128  0.50 27.58 ? 141 PHE A CZ    1 
ATOM   2192  C  CZ    B PHE A 1 141 ? 2.047   -2.258  30.281  0.50 26.44 ? 141 PHE A CZ    1 
ATOM   2193  N  N     A GLY A 1 142 ? 4.478   -7.379  25.581  0.50 20.63 ? 142 GLY A N     1 
ATOM   2194  N  N     B GLY A 1 142 ? 4.307   -7.334  25.311  0.50 20.38 ? 142 GLY A N     1 
ATOM   2195  C  CA    A GLY A 1 142 ? 5.641   -7.660  24.760  0.50 21.14 ? 142 GLY A CA    1 
ATOM   2196  C  CA    B GLY A 1 142 ? 5.408   -7.776  24.477  0.50 21.63 ? 142 GLY A CA    1 
ATOM   2197  C  C     A GLY A 1 142 ? 5.346   -8.235  23.393  0.50 21.67 ? 142 GLY A C     1 
ATOM   2198  C  C     B GLY A 1 142 ? 5.063   -8.138  23.049  0.50 20.71 ? 142 GLY A C     1 
ATOM   2199  O  O     A GLY A 1 142 ? 6.235   -8.233  22.537  0.50 18.07 ? 142 GLY A O     1 
ATOM   2200  O  O     B GLY A 1 142 ? 5.797   -7.771  22.128  0.50 24.51 ? 142 GLY A O     1 
ATOM   2201  N  N     A GLY A 1 143 ? 4.138   -8.739  23.171  0.50 22.56 ? 143 GLY A N     1 
ATOM   2202  N  N     B GLY A 1 143 ? 3.969   -8.868  22.851  0.50 23.45 ? 143 GLY A N     1 
ATOM   2203  C  CA    A GLY A 1 143 ? 3.788   -9.261  21.869  0.50 21.71 ? 143 GLY A CA    1 
ATOM   2204  C  CA    B GLY A 1 143 ? 3.597   -9.273  21.508  0.50 20.38 ? 143 GLY A CA    1 
ATOM   2205  C  C     A GLY A 1 143 ? 3.522   -8.166  20.860  0.50 20.42 ? 143 GLY A C     1 
ATOM   2206  C  C     B GLY A 1 143 ? 3.291   -8.081  20.623  0.50 21.36 ? 143 GLY A C     1 
ATOM   2207  O  O     A GLY A 1 143 ? 3.390   -6.987  21.193  0.50 20.99 ? 143 GLY A O     1 
ATOM   2208  O  O     B GLY A 1 143 ? 2.862   -7.019  21.086  0.50 22.31 ? 143 GLY A O     1 
ATOM   2209  N  N     A GLY A 1 144 ? 3.452   -8.574  19.596  0.50 22.95 ? 144 GLY A N     1 
ATOM   2210  N  N     B GLY A 1 144 ? 3.532   -8.254  19.323  0.50 24.43 ? 144 GLY A N     1 
ATOM   2211  C  CA    A GLY A 1 144 ? 3.154   -7.648  18.519  0.50 21.84 ? 144 GLY A CA    1 
ATOM   2212  C  CA    B GLY A 1 144 ? 3.216   -7.190  18.385  0.50 21.01 ? 144 GLY A CA    1 
ATOM   2213  C  C     A GLY A 1 144 ? 1.674   -7.362  18.383  0.50 22.06 ? 144 GLY A C     1 
ATOM   2214  C  C     B GLY A 1 144 ? 1.726   -6.939  18.279  0.50 21.95 ? 144 GLY A C     1 
ATOM   2215  O  O     A GLY A 1 144 ? 1.273   -6.220  18.144  0.50 24.28 ? 144 GLY A O     1 
ATOM   2216  O  O     B GLY A 1 144 ? 1.289   -5.799  18.103  0.50 24.80 ? 144 GLY A O     1 
ATOM   2217  N  N     A THR A 1 145 ? 0.846   -8.399  18.529  0.50 23.61 ? 145 THR A N     1 
ATOM   2218  N  N     B THR A 1 145 ? 0.925   -7.998  18.379  0.50 24.76 ? 145 THR A N     1 
ATOM   2219  C  CA    A THR A 1 145 ? -0.597  -8.188  18.534  0.50 21.55 ? 145 THR A CA    1 
ATOM   2220  C  CA    B THR A 1 145 ? -0.522  -7.824  18.421  0.50 22.84 ? 145 THR A CA    1 
ATOM   2221  C  C     A THR A 1 145 ? -1.057  -7.626  19.873  0.50 24.23 ? 145 THR A C     1 
ATOM   2222  C  C     B THR A 1 145 ? -0.953  -7.208  19.747  0.50 23.12 ? 145 THR A C     1 
ATOM   2223  O  O     A THR A 1 145 ? -1.891  -6.714  19.916  0.50 24.61 ? 145 THR A O     1 
ATOM   2224  O  O     B THR A 1 145 ? -1.642  -6.182  19.772  0.50 22.94 ? 145 THR A O     1 
ATOM   2225  C  CB    A THR A 1 145 ? -1.320  -9.501  18.215  0.50 21.68 ? 145 THR A CB    1 
ATOM   2226  C  CB    B THR A 1 145 ? -1.216  -9.166  18.188  0.50 21.16 ? 145 THR A CB    1 
ATOM   2227  O  OG1   A THR A 1 145 ? -0.940  -9.959  16.908  0.50 22.68 ? 145 THR A OG1   1 
ATOM   2228  O  OG1   B THR A 1 145 ? -0.860  -9.674  16.895  0.50 22.63 ? 145 THR A OG1   1 
ATOM   2229  C  CG2   A THR A 1 145 ? -2.830  -9.318  18.267  0.50 20.47 ? 145 THR A CG2   1 
ATOM   2230  C  CG2   B THR A 1 145 ? -2.725  -9.011  18.270  0.50 21.61 ? 145 THR A CG2   1 
ATOM   2231  N  N     A GLY A 1 146 ? -0.506  -8.143  20.973  0.50 21.39 ? 146 GLY A N     1 
ATOM   2232  N  N     B GLY A 1 146 ? -0.533  -7.811  20.860  0.50 20.99 ? 146 GLY A N     1 
ATOM   2233  C  CA    A GLY A 1 146 ? -0.889  -7.654  22.286  0.50 21.01 ? 146 GLY A CA    1 
ATOM   2234  C  CA    B GLY A 1 146 ? -0.934  -7.308  22.163  0.50 22.29 ? 146 GLY A CA    1 
ATOM   2235  C  C     A GLY A 1 146 ? -0.576  -6.185  22.488  0.50 21.78 ? 146 GLY A C     1 
ATOM   2236  C  C     B GLY A 1 146 ? -0.535  -5.861  22.385  0.50 21.40 ? 146 GLY A C     1 
ATOM   2237  O  O     A GLY A 1 146 ? -1.242  -5.510  23.276  0.50 23.61 ? 146 GLY A O     1 
ATOM   2238  O  O     B GLY A 1 146 ? -1.308  -5.072  22.927  0.50 19.67 ? 146 GLY A O     1 
ATOM   2239  N  N     A SER A 1 147 ? 0.440   -5.668  21.792  0.50 21.61 ? 147 SER A N     1 
ATOM   2240  N  N     B SER A 1 147 ? 0.671   -5.488  21.961  0.50 21.34 ? 147 SER A N     1 
ATOM   2241  C  CA    A SER A 1 147 ? 0.791   -4.253  21.875  0.50 22.23 ? 147 SER A CA    1 
ATOM   2242  C  CA    B SER A 1 147 ? 1.096   -4.103  22.128  0.50 22.91 ? 147 SER A CA    1 
ATOM   2243  C  C     A SER A 1 147 ? 0.147   -3.442  20.755  0.50 22.17 ? 147 SER A C     1 
ATOM   2244  C  C     B SER A 1 147 ? 0.459   -3.208  21.071  0.50 22.43 ? 147 SER A C     1 
ATOM   2245  O  O     A SER A 1 147 ? -0.697  -2.581  21.021  0.50 22.74 ? 147 SER A O     1 
ATOM   2246  O  O     B SER A 1 147 ? -0.235  -2.238  21.398  0.50 23.28 ? 147 SER A O     1 
ATOM   2247  C  CB    A SER A 1 147 ? 2.317   -4.073  21.857  0.50 21.61 ? 147 SER A CB    1 
ATOM   2248  C  CB    B SER A 1 147 ? 2.623   -4.005  22.076  0.50 20.42 ? 147 SER A CB    1 
ATOM   2249  O  OG    A SER A 1 147 ? 2.864   -4.360  20.580  0.50 21.92 ? 147 SER A OG    1 
ATOM   2250  O  OG    B SER A 1 147 ? 3.115   -4.487  20.840  0.50 21.66 ? 147 SER A OG    1 
ATOM   2251  N  N     A GLY A 1 148 ? 0.515   -3.728  19.503  0.50 23.00 ? 148 GLY A N     1 
ATOM   2252  N  N     B GLY A 1 148 ? 0.658   -3.545  19.798  0.50 22.74 ? 148 GLY A N     1 
ATOM   2253  C  CA    A GLY A 1 148 ? 0.118   -2.868  18.397  0.50 23.70 ? 148 GLY A CA    1 
ATOM   2254  C  CA    B GLY A 1 148 ? 0.274   -2.689  18.693  0.50 23.85 ? 148 GLY A CA    1 
ATOM   2255  C  C     A GLY A 1 148 ? -1.370  -2.894  18.105  0.50 28.11 ? 148 GLY A C     1 
ATOM   2256  C  C     B GLY A 1 148 ? -1.196  -2.667  18.335  0.50 28.13 ? 148 GLY A C     1 
ATOM   2257  O  O     A GLY A 1 148 ? -1.984  -1.846  17.884  0.50 20.47 ? 148 GLY A O     1 
ATOM   2258  O  O     B GLY A 1 148 ? -1.755  -1.588  18.108  0.50 20.30 ? 148 GLY A O     1 
ATOM   2259  N  N     A PHE A 1 149 ? -1.972  -4.086  18.081  0.50 25.83 ? 149 PHE A N     1 
ATOM   2260  N  N     B PHE A 1 149 ? -1.837  -3.838  18.263  0.50 26.71 ? 149 PHE A N     1 
ATOM   2261  C  CA    A PHE A 1 149 ? -3.405  -4.145  17.817  0.50 25.98 ? 149 PHE A CA    1 
ATOM   2262  C  CA    B PHE A 1 149 ? -3.242  -3.863  17.872  0.50 26.21 ? 149 PHE A CA    1 
ATOM   2263  C  C     A PHE A 1 149 ? -4.209  -3.622  18.996  0.50 21.86 ? 149 PHE A C     1 
ATOM   2264  C  C     B PHE A 1 149 ? -4.131  -3.313  18.977  0.50 22.91 ? 149 PHE A C     1 
ATOM   2265  O  O     A PHE A 1 149 ? -5.284  -3.049  18.798  0.50 24.97 ? 149 PHE A O     1 
ATOM   2266  O  O     B PHE A 1 149 ? -5.043  -2.523  18.708  0.50 23.21 ? 149 PHE A O     1 
ATOM   2267  C  CB    A PHE A 1 149 ? -3.843  -5.565  17.474  0.50 22.19 ? 149 PHE A CB    1 
ATOM   2268  C  CB    B PHE A 1 149 ? -3.685  -5.274  17.494  0.50 22.13 ? 149 PHE A CB    1 
ATOM   2269  C  CG    A PHE A 1 149 ? -5.217  -5.632  16.873  0.50 24.64 ? 149 PHE A CG    1 
ATOM   2270  C  CG    B PHE A 1 149 ? -5.091  -5.332  16.975  0.50 24.33 ? 149 PHE A CG    1 
ATOM   2271  C  CD1   A PHE A 1 149 ? -5.405  -5.383  15.522  0.50 28.93 ? 149 PHE A CD1   1 
ATOM   2272  C  CD1   B PHE A 1 149 ? -5.370  -4.970  15.667  0.50 28.29 ? 149 PHE A CD1   1 
ATOM   2273  C  CD2   A PHE A 1 149 ? -6.321  -5.920  17.657  0.50 26.38 ? 149 PHE A CD2   1 
ATOM   2274  C  CD2   B PHE A 1 149 ? -6.136  -5.722  17.796  0.50 26.24 ? 149 PHE A CD2   1 
ATOM   2275  C  CE1   A PHE A 1 149 ? -6.664  -5.433  14.962  0.50 27.06 ? 149 PHE A CE1   1 
ATOM   2276  C  CE1   B PHE A 1 149 ? -6.658  -5.010  15.182  0.50 27.28 ? 149 PHE A CE1   1 
ATOM   2277  C  CE2   A PHE A 1 149 ? -7.584  -5.972  17.103  0.50 28.27 ? 149 PHE A CE2   1 
ATOM   2278  C  CE2   B PHE A 1 149 ? -7.430  -5.766  17.315  0.50 27.71 ? 149 PHE A CE2   1 
ATOM   2279  C  CZ    A PHE A 1 149 ? -7.756  -5.729  15.753  0.50 28.35 ? 149 PHE A CZ    1 
ATOM   2280  C  CZ    B PHE A 1 149 ? -7.692  -5.409  16.005  0.50 27.57 ? 149 PHE A CZ    1 
ATOM   2281  N  N     A THR A 1 150 ? -3.701  -3.790  20.220  0.50 23.28 ? 150 THR A N     1 
ATOM   2282  N  N     B THR A 1 150 ? -3.880  -3.717  20.228  0.50 23.80 ? 150 THR A N     1 
ATOM   2283  C  CA    A THR A 1 150 ? -4.397  -3.260  21.390  0.50 21.47 ? 150 THR A CA    1 
ATOM   2284  C  CA    B THR A 1 150 ? -4.645  -3.180  21.354  0.50 20.86 ? 150 THR A CA    1 
ATOM   2285  C  C     A THR A 1 150 ? -4.524  -1.746  21.317  0.50 22.69 ? 150 THR A C     1 
ATOM   2286  C  C     B THR A 1 150 ? -4.576  -1.661  21.391  0.50 22.72 ? 150 THR A C     1 
ATOM   2287  O  O     A THR A 1 150 ? -5.611  -1.192  21.519  0.50 25.97 ? 150 THR A O     1 
ATOM   2288  O  O     B THR A 1 150 ? -5.565  -0.991  21.714  0.50 24.98 ? 150 THR A O     1 
ATOM   2289  C  CB    A THR A 1 150 ? -3.663  -3.656  22.669  0.50 18.18 ? 150 THR A CB    1 
ATOM   2290  C  CB    B THR A 1 150 ? -4.124  -3.748  22.674  0.50 20.41 ? 150 THR A CB    1 
ATOM   2291  O  OG1   A THR A 1 150 ? -3.684  -5.080  22.811  0.50 19.48 ? 150 THR A OG1   1 
ATOM   2292  O  OG1   B THR A 1 150 ? -4.155  -5.178  22.634  0.50 17.98 ? 150 THR A OG1   1 
ATOM   2293  C  CG2   A THR A 1 150 ? -4.329  -3.011  23.880  0.50 22.06 ? 150 THR A CG2   1 
ATOM   2294  C  CG2   B THR A 1 150 ? -4.985  -3.257  23.841  0.50 21.36 ? 150 THR A CG2   1 
ATOM   2295  N  N     A SER A 1 151 ? -3.415  -1.056  21.039  0.50 23.64 ? 151 SER A N     1 
ATOM   2296  N  N     B SER A 1 151 ? -3.409  -1.100  21.068  0.50 23.66 ? 151 SER A N     1 
ATOM   2297  C  CA    A SER A 1 151 ? -3.446  0.401   21.075  0.50 23.20 ? 151 SER A CA    1 
ATOM   2298  C  CA    B SER A 1 151 ? -3.277  0.351   21.046  0.50 23.28 ? 151 SER A CA    1 
ATOM   2299  C  C     A SER A 1 151 ? -4.300  0.958   19.946  0.50 25.59 ? 151 SER A C     1 
ATOM   2300  C  C     B SER A 1 151 ? -4.171  0.959   19.977  0.50 25.56 ? 151 SER A C     1 
ATOM   2301  O  O     A SER A 1 151 ? -5.013  1.950   20.133  0.50 25.97 ? 151 SER A O     1 
ATOM   2302  O  O     B SER A 1 151 ? -4.837  1.973   20.217  0.50 25.91 ? 151 SER A O     1 
ATOM   2303  C  CB    A SER A 1 151 ? -2.027  0.966   21.017  0.50 26.51 ? 151 SER A CB    1 
ATOM   2304  C  CB    B SER A 1 151 ? -1.817  0.739   20.825  0.50 26.37 ? 151 SER A CB    1 
ATOM   2305  O  OG    A SER A 1 151 ? -1.472  0.856   19.720  0.50 31.99 ? 151 SER A OG    1 
ATOM   2306  O  OG    B SER A 1 151 ? -1.241  -0.043  19.794  0.50 30.83 ? 151 SER A OG    1 
ATOM   2307  N  N     A LEU A 1 152 ? -4.244  0.330   18.768  0.50 28.58 ? 152 LEU A N     1 
ATOM   2308  N  N     B LEU A 1 152 ? -4.205  0.347   18.791  0.50 28.57 ? 152 LEU A N     1 
ATOM   2309  C  CA    A LEU A 1 152 ? -5.151  0.701   17.685  0.50 27.93 ? 152 LEU A CA    1 
ATOM   2310  C  CA    B LEU A 1 152 ? -5.130  0.791   17.753  0.50 27.92 ? 152 LEU A CA    1 
ATOM   2311  C  C     A LEU A 1 152 ? -6.603  0.518   18.103  0.50 26.86 ? 152 LEU A C     1 
ATOM   2312  C  C     B LEU A 1 152 ? -6.576  0.576   18.181  0.50 26.90 ? 152 LEU A C     1 
ATOM   2313  O  O     A LEU A 1 152 ? -7.449  1.381   17.842  0.50 29.00 ? 152 LEU A O     1 
ATOM   2314  O  O     B LEU A 1 152 ? -7.439  1.429   17.938  0.50 28.93 ? 152 LEU A O     1 
ATOM   2315  C  CB    A LEU A 1 152 ? -4.841  -0.130  16.439  0.50 26.78 ? 152 LEU A CB    1 
ATOM   2316  C  CB    B LEU A 1 152 ? -4.842  0.053   16.445  0.50 26.83 ? 152 LEU A CB    1 
ATOM   2317  C  CG    A LEU A 1 152 ? -5.875  -0.144  15.311  0.50 27.84 ? 152 LEU A CG    1 
ATOM   2318  C  CG    B LEU A 1 152 ? -5.811  0.303   15.287  0.50 29.90 ? 152 LEU A CG    1 
ATOM   2319  C  CD1   A LEU A 1 152 ? -6.051  1.248   14.716  0.50 30.34 ? 152 LEU A CD1   1 
ATOM   2320  C  CD1   B LEU A 1 152 ? -5.745  1.756   14.840  0.50 28.70 ? 152 LEU A CD1   1 
ATOM   2321  C  CD2   A LEU A 1 152 ? -5.479  -1.148  14.236  0.50 26.24 ? 152 LEU A CD2   1 
ATOM   2322  C  CD2   B LEU A 1 152 ? -5.517  -0.638  14.125  0.50 26.84 ? 152 LEU A CD2   1 
ATOM   2323  N  N     A LEU A 1 153 ? -6.905  -0.599  18.765  0.50 22.51 ? 153 LEU A N     1 
ATOM   2324  N  N     B LEU A 1 153 ? -6.857  -0.560  18.823  0.50 22.47 ? 153 LEU A N     1 
ATOM   2325  C  CA    A LEU A 1 153 ? -8.271  -0.855  19.210  0.50 25.39 ? 153 LEU A CA    1 
ATOM   2326  C  CA    B LEU A 1 153 ? -8.209  -0.824  19.305  0.50 25.50 ? 153 LEU A CA    1 
ATOM   2327  C  C     A LEU A 1 153 ? -8.699  0.143   20.282  0.50 24.48 ? 153 LEU A C     1 
ATOM   2328  C  C     B LEU A 1 153 ? -8.643  0.221   20.327  0.50 24.47 ? 153 LEU A C     1 
ATOM   2329  O  O     A LEU A 1 153 ? -9.825  0.658   20.245  0.50 26.24 ? 153 LEU A O     1 
ATOM   2330  O  O     B LEU A 1 153 ? -9.773  0.723   20.273  0.50 26.22 ? 153 LEU A O     1 
ATOM   2331  C  CB    A LEU A 1 153 ? -8.376  -2.294  19.716  0.50 20.62 ? 153 LEU A CB    1 
ATOM   2332  C  CB    B LEU A 1 153 ? -8.282  -2.230  19.903  0.50 20.87 ? 153 LEU A CB    1 
ATOM   2333  C  CG    A LEU A 1 153 ? -9.681  -2.806  20.330  0.50 20.92 ? 153 LEU A CG    1 
ATOM   2334  C  CG    B LEU A 1 153 ? -9.635  -2.705  20.444  0.50 20.83 ? 153 LEU A CG    1 
ATOM   2335  C  CD1   A LEU A 1 153 ? -10.890 -2.354  19.533  0.50 24.25 ? 153 LEU A CD1   1 
ATOM   2336  C  CD1   B LEU A 1 153 ? -10.578 -3.075  19.305  0.50 23.65 ? 153 LEU A CD1   1 
ATOM   2337  C  CD2   A LEU A 1 153 ? -9.625  -4.319  20.386  0.50 24.06 ? 153 LEU A CD2   1 
ATOM   2338  C  CD2   B LEU A 1 153 ? -9.446  -3.876  21.397  0.50 26.15 ? 153 LEU A CD2   1 
ATOM   2339  N  N     A MET A 1 154 ? -7.818  0.433   21.244  0.50 26.57 ? 154 MET A N     1 
ATOM   2340  N  N     B MET A 1 154 ? -7.753  0.572   21.262  0.50 26.45 ? 154 MET A N     1 
ATOM   2341  C  CA    A MET A 1 154 ? -8.165  1.394   22.287  0.50 26.31 ? 154 MET A CA    1 
ATOM   2342  C  CA    B MET A 1 154 ? -8.114  1.531   22.303  0.50 26.44 ? 154 MET A CA    1 
ATOM   2343  C  C     A MET A 1 154 ? -8.354  2.791   21.712  0.50 31.93 ? 154 MET A C     1 
ATOM   2344  C  C     B MET A 1 154 ? -8.424  2.899   21.708  0.50 31.89 ? 154 MET A C     1 
ATOM   2345  O  O     A MET A 1 154 ? -9.205  3.546   22.194  0.50 26.80 ? 154 MET A O     1 
ATOM   2346  O  O     B MET A 1 154 ? -9.367  3.570   22.141  0.50 26.89 ? 154 MET A O     1 
ATOM   2347  C  CB    A MET A 1 154 ? -7.096  1.400   23.381  0.50 25.36 ? 154 MET A CB    1 
ATOM   2348  C  CB    B MET A 1 154 ? -6.993  1.640   23.338  0.50 25.74 ? 154 MET A CB    1 
ATOM   2349  C  CG    A MET A 1 154 ? -6.942  0.071   24.093  0.50 25.09 ? 154 MET A CG    1 
ATOM   2350  C  CG    B MET A 1 154 ? -6.842  0.429   24.243  0.50 25.65 ? 154 MET A CG    1 
ATOM   2351  S  SD    A MET A 1 154 ? -8.301  -0.269  25.223  0.50 32.31 ? 154 MET A SD    1 
ATOM   2352  S  SD    B MET A 1 154 ? -8.178  0.267   25.441  0.50 34.68 ? 154 MET A SD    1 
ATOM   2353  C  CE    A MET A 1 154 ? -7.843  0.773   26.607  0.50 28.15 ? 154 MET A CE    1 
ATOM   2354  C  CE    B MET A 1 154 ? -7.495  -0.982  26.525  0.50 25.49 ? 154 MET A CE    1 
ATOM   2355  N  N     A GLU A 1 155 ? -7.579  3.148   20.685  0.50 29.22 ? 155 GLU A N     1 
ATOM   2356  N  N     B GLU A 1 155 ? -7.641  3.328   20.714  0.50 29.47 ? 155 GLU A N     1 
ATOM   2357  C  CA    A GLU A 1 155 ? -7.808  4.409   19.985  0.50 32.80 ? 155 GLU A CA    1 
ATOM   2358  C  CA    B GLU A 1 155 ? -7.913  4.599   20.046  0.50 32.59 ? 155 GLU A CA    1 
ATOM   2359  C  C     A GLU A 1 155 ? -9.205  4.451   19.376  0.50 32.93 ? 155 GLU A C     1 
ATOM   2360  C  C     B GLU A 1 155 ? -9.315  4.619   19.451  0.50 33.19 ? 155 GLU A C     1 
ATOM   2361  O  O     A GLU A 1 155 ? -9.921  5.452   19.504  0.50 31.68 ? 155 GLU A O     1 
ATOM   2362  O  O     B GLU A 1 155 ? -10.097 5.545   19.701  0.50 30.63 ? 155 GLU A O     1 
ATOM   2363  C  CB    A GLU A 1 155 ? -6.745  4.612   18.901  0.50 29.81 ? 155 GLU A CB    1 
ATOM   2364  C  CB    B GLU A 1 155 ? -6.874  4.858   18.954  0.50 30.09 ? 155 GLU A CB    1 
ATOM   2365  C  CG    A GLU A 1 155 ? -5.361  4.992   19.417  0.50 34.50 ? 155 GLU A CG    1 
ATOM   2366  C  CG    B GLU A 1 155 ? -5.462  5.070   19.458  0.50 34.46 ? 155 GLU A CG    1 
ATOM   2367  C  CD    A GLU A 1 155 ? -4.324  5.055   18.304  0.50 34.67 ? 155 GLU A CD    1 
ATOM   2368  C  CD    B GLU A 1 155 ? -4.464  5.206   18.323  0.50 35.09 ? 155 GLU A CD    1 
ATOM   2369  O  OE1   A GLU A 1 155 ? -4.631  4.603   17.181  0.50 31.84 ? 155 GLU A OE1   1 
ATOM   2370  O  OE1   B GLU A 1 155 ? -4.813  5.808   17.284  0.50 40.05 ? 155 GLU A OE1   1 
ATOM   2371  O  OE2   A GLU A 1 155 ? -3.208  5.563   18.547  0.50 32.15 ? 155 GLU A OE2   1 
ATOM   2372  O  OE2   B GLU A 1 155 ? -3.334  4.699   18.466  0.50 29.69 ? 155 GLU A OE2   1 
ATOM   2373  N  N     A ARG A 1 156 ? -9.613  3.364   18.711  0.50 28.12 ? 156 ARG A N     1 
ATOM   2374  N  N     B ARG A 1 156 ? -9.651  3.597   18.657  0.50 28.54 ? 156 ARG A N     1 
ATOM   2375  C  CA    A ARG A 1 156 ? -10.916 3.339   18.053  0.50 27.67 ? 156 ARG A CA    1 
ATOM   2376  C  CA    B ARG A 1 156 ? -10.969 3.525   18.042  0.50 27.83 ? 156 ARG A CA    1 
ATOM   2377  C  C     A ARG A 1 156 ? -12.051 3.439   19.065  0.50 29.00 ? 156 ARG A C     1 
ATOM   2378  C  C     B ARG A 1 156 ? -12.079 3.320   19.064  0.50 28.94 ? 156 ARG A C     1 
ATOM   2379  O  O     A ARG A 1 156 ? -12.952 4.272   18.921  0.50 30.76 ? 156 ARG A O     1 
ATOM   2380  O  O     B ARG A 1 156 ? -13.232 3.663   18.782  0.50 32.02 ? 156 ARG A O     1 
ATOM   2381  C  CB    A ARG A 1 156 ? -11.064 2.069   17.213  0.50 27.60 ? 156 ARG A CB    1 
ATOM   2382  C  CB    B ARG A 1 156 ? -10.995 2.398   17.013  0.50 30.06 ? 156 ARG A CB    1 
ATOM   2383  C  CG    A ARG A 1 156 ? -10.218 2.055   15.947  0.50 34.34 ? 156 ARG A CG    1 
ATOM   2384  C  CG    B ARG A 1 156 ? -9.942  2.535   15.916  0.50 34.05 ? 156 ARG A CG    1 
ATOM   2385  C  CD    A ARG A 1 156 ? -10.551 3.230   15.036  0.50 40.97 ? 156 ARG A CD    1 
ATOM   2386  C  CD    B ARG A 1 156 ? -10.226 3.721   15.006  0.50 41.14 ? 156 ARG A CD    1 
ATOM   2387  N  NE    A ARG A 1 156 ? -11.883 3.127   14.451  0.50 36.63 ? 156 ARG A NE    1 
ATOM   2388  N  NE    B ARG A 1 156 ? -11.401 3.499   14.172  0.50 38.58 ? 156 ARG A NE    1 
ATOM   2389  C  CZ    A ARG A 1 156 ? -12.159 2.492   13.319  0.50 37.74 ? 156 ARG A CZ    1 
ATOM   2390  C  CZ    B ARG A 1 156 ? -11.398 2.800   13.045  0.50 42.64 ? 156 ARG A CZ    1 
ATOM   2391  N  NH1   A ARG A 1 156 ? -11.219 1.862   12.632  0.50 42.54 ? 156 ARG A NH1   1 
ATOM   2392  N  NH1   B ARG A 1 156 ? -10.292 2.237   12.582  0.50 38.84 ? 156 ARG A NH1   1 
ATOM   2393  N  NH2   A ARG A 1 156 ? -13.411 2.484   12.868  0.50 40.16 ? 156 ARG A NH2   1 
ATOM   2394  N  NH2   B ARG A 1 156 ? -12.532 2.662   12.363  0.50 47.73 ? 156 ARG A NH2   1 
ATOM   2395  N  N     A LEU A 1 157 ? -12.027 2.587   20.094  0.50 23.71 ? 157 LEU A N     1 
ATOM   2396  N  N     B LEU A 1 157 ? -11.764 2.765   20.237  0.50 25.07 ? 157 LEU A N     1 
ATOM   2397  C  CA    A LEU A 1 157 ? -13.110 2.581   21.073  0.50 30.40 ? 157 LEU A CA    1 
ATOM   2398  C  CA    B LEU A 1 157 ? -12.765 2.669   21.293  0.50 30.10 ? 157 LEU A CA    1 
ATOM   2399  C  C     A LEU A 1 157 ? -13.244 3.926   21.779  0.50 29.66 ? 157 LEU A C     1 
ATOM   2400  C  C     B LEU A 1 157 ? -13.079 4.042   21.873  0.50 29.52 ? 157 LEU A C     1 
ATOM   2401  O  O     A LEU A 1 157 ? -14.359 4.337   22.115  0.50 29.95 ? 157 LEU A O     1 
ATOM   2402  O  O     B LEU A 1 157 ? -14.221 4.308   22.258  0.50 29.81 ? 157 LEU A O     1 
ATOM   2403  C  CB    A LEU A 1 157 ? -12.895 1.460   22.091  0.50 30.02 ? 157 LEU A CB    1 
ATOM   2404  C  CB    B LEU A 1 157 ? -12.292 1.716   22.389  0.50 28.22 ? 157 LEU A CB    1 
ATOM   2405  C  CG    A LEU A 1 157 ? -12.949 0.017   21.581  0.50 26.33 ? 157 LEU A CG    1 
ATOM   2406  C  CG    B LEU A 1 157 ? -12.321 0.226   22.043  0.50 22.63 ? 157 LEU A CG    1 
ATOM   2407  C  CD1   A LEU A 1 157 ? -12.764 -0.963  22.729  0.50 25.35 ? 157 LEU A CD1   1 
ATOM   2408  C  CD1   B LEU A 1 157 ? -11.889 -0.639  23.222  0.50 28.78 ? 157 LEU A CD1   1 
ATOM   2409  C  CD2   A LEU A 1 157 ? -14.253 -0.261  20.843  0.50 27.46 ? 157 LEU A CD2   1 
ATOM   2410  C  CD2   B LEU A 1 157 ? -13.702 -0.177  21.555  0.50 28.55 ? 157 LEU A CD2   1 
ATOM   2411  N  N     A SER A 1 158 ? -12.132 4.634   21.998  0.50 31.53 ? 158 SER A N     1 
ATOM   2412  N  N     B SER A 1 158 ? -12.081 4.926   21.938  0.50 31.36 ? 158 SER A N     1 
ATOM   2413  C  CA    A SER A 1 158 ? -12.212 5.951   22.620  0.50 30.45 ? 158 SER A CA    1 
ATOM   2414  C  CA    B SER A 1 158 ? -12.313 6.264   22.474  0.50 30.18 ? 158 SER A CA    1 
ATOM   2415  C  C     A SER A 1 158 ? -12.867 6.984   21.714  0.50 34.06 ? 158 SER A C     1 
ATOM   2416  C  C     B SER A 1 158 ? -13.319 7.031   21.624  0.50 35.58 ? 158 SER A C     1 
ATOM   2417  O  O     A SER A 1 158 ? -13.295 8.035   22.203  0.50 38.33 ? 158 SER A O     1 
ATOM   2418  O  O     B SER A 1 158 ? -14.243 7.663   22.151  0.50 32.92 ? 158 SER A O     1 
ATOM   2419  C  CB    A SER A 1 158 ? -10.823 6.433   23.036  0.50 31.26 ? 158 SER A CB    1 
ATOM   2420  C  CB    B SER A 1 158 ? -10.994 7.032   22.565  0.50 32.63 ? 158 SER A CB    1 
ATOM   2421  O  OG    A SER A 1 158 ? -10.525 6.026   24.362  0.50 30.63 ? 158 SER A OG    1 
ATOM   2422  O  OG    B SER A 1 158 ? -10.104 6.421   23.479  0.50 36.13 ? 158 SER A OG    1 
ATOM   2423  N  N     A VAL A 1 159 ? -12.948 6.714   20.414  0.50 33.07 ? 159 VAL A N     1 
ATOM   2424  N  N     B VAL A 1 159 ? -13.160 6.978   20.300  0.50 34.28 ? 159 VAL A N     1 
ATOM   2425  C  CA    A VAL A 1 159 ? -13.702 7.569   19.503  0.50 35.68 ? 159 VAL A CA    1 
ATOM   2426  C  CA    B VAL A 1 159 ? -14.022 7.759   19.417  0.50 34.82 ? 159 VAL A CA    1 
ATOM   2427  C  C     A VAL A 1 159 ? -15.172 7.171   19.466  0.50 36.51 ? 159 VAL A C     1 
ATOM   2428  C  C     B VAL A 1 159 ? -15.429 7.173   19.373  0.50 36.92 ? 159 VAL A C     1 
ATOM   2429  O  O     A VAL A 1 159 ? -16.054 8.034   19.464  0.50 34.21 ? 159 VAL A O     1 
ATOM   2430  O  O     B VAL A 1 159 ? -16.423 7.907   19.439  0.50 35.87 ? 159 VAL A O     1 
ATOM   2431  C  CB    A VAL A 1 159 ? -13.076 7.525   18.093  0.50 36.49 ? 159 VAL A CB    1 
ATOM   2432  C  CB    B VAL A 1 159 ? -13.405 7.846   18.009  0.50 36.59 ? 159 VAL A CB    1 
ATOM   2433  C  CG1   A VAL A 1 159 ? -13.927 8.310   17.104  0.50 39.75 ? 159 VAL A CG1   1 
ATOM   2434  C  CG1   B VAL A 1 159 ? -14.207 8.804   17.142  0.50 38.32 ? 159 VAL A CG1   1 
ATOM   2435  C  CG2   A VAL A 1 159 ? -11.650 8.066   18.121  0.50 38.59 ? 159 VAL A CG2   1 
ATOM   2436  C  CG2   B VAL A 1 159 ? -11.946 8.278   18.087  0.50 39.33 ? 159 VAL A CG2   1 
ATOM   2437  N  N     A ASP A 1 160 ? -15.451 5.865   19.447  0.50 31.23 ? 160 ASP A N     1 
ATOM   2438  N  N     B ASP A 1 160 ? -15.539 5.847   19.255  0.50 31.22 ? 160 ASP A N     1 
ATOM   2439  C  CA    A ASP A 1 160 ? -16.811 5.374   19.266  0.50 32.74 ? 160 ASP A CA    1 
ATOM   2440  C  CA    B ASP A 1 160 ? -16.839 5.212   19.075  0.50 32.48 ? 160 ASP A CA    1 
ATOM   2441  C  C     A ASP A 1 160 ? -17.603 5.296   20.565  0.50 33.42 ? 160 ASP A C     1 
ATOM   2442  C  C     B ASP A 1 160 ? -17.580 4.987   20.385  0.50 34.14 ? 160 ASP A C     1 
ATOM   2443  O  O     A ASP A 1 160 ? -18.839 5.313   20.517  0.50 37.19 ? 160 ASP A O     1 
ATOM   2444  O  O     B ASP A 1 160 ? -18.806 4.836   20.368  0.50 35.60 ? 160 ASP A O     1 
ATOM   2445  C  CB    A ASP A 1 160 ? -16.794 3.990   18.612  0.50 34.02 ? 160 ASP A CB    1 
ATOM   2446  C  CB    B ASP A 1 160 ? -16.678 3.877   18.345  0.50 34.63 ? 160 ASP A CB    1 
ATOM   2447  C  CG    A ASP A 1 160 ? -16.426 4.036   17.137  0.50 38.35 ? 160 ASP A CG    1 
ATOM   2448  C  CG    B ASP A 1 160 ? -16.372 4.053   16.869  0.50 37.94 ? 160 ASP A CG    1 
ATOM   2449  O  OD1   A ASP A 1 160 ? -15.723 4.980   16.715  0.50 34.41 ? 160 ASP A OD1   1 
ATOM   2450  O  OD1   B ASP A 1 160 ? -16.827 5.060   16.288  0.50 39.90 ? 160 ASP A OD1   1 
ATOM   2451  O  OD2   A ASP A 1 160 ? -16.854 3.120   16.402  0.50 31.44 ? 160 ASP A OD2   1 
ATOM   2452  O  OD2   B ASP A 1 160 ? -15.678 3.188   16.293  0.50 33.72 ? 160 ASP A OD2   1 
ATOM   2453  N  N     A TYR A 1 161 ? -16.938 5.193   21.712  0.50 31.98 ? 161 TYR A N     1 
ATOM   2454  N  N     B TYR A 1 161 ? -16.865 4.950   21.517  0.50 32.10 ? 161 TYR A N     1 
ATOM   2455  C  CA    A TYR A 1 161 ? -17.601 5.011   23.003  0.50 34.56 ? 161 TYR A CA    1 
ATOM   2456  C  CA    B TYR A 1 161 ? -17.464 4.760   22.842  0.50 34.78 ? 161 TYR A CA    1 
ATOM   2457  C  C     A TYR A 1 161 ? -17.061 6.011   24.016  0.50 37.06 ? 161 TYR A C     1 
ATOM   2458  C  C     B TYR A 1 161 ? -16.751 5.744   23.773  0.50 36.67 ? 161 TYR A C     1 
ATOM   2459  O  O     A TYR A 1 161 ? -16.592 5.651   25.098  0.50 33.61 ? 161 TYR A O     1 
ATOM   2460  O  O     B TYR A 1 161 ? -15.832 5.382   24.511  0.50 37.70 ? 161 TYR A O     1 
ATOM   2461  C  CB    A TYR A 1 161 ? -17.419 3.584   23.520  0.50 31.59 ? 161 TYR A CB    1 
ATOM   2462  C  CB    B TYR A 1 161 ? -17.335 3.315   23.326  0.50 31.09 ? 161 TYR A CB    1 
ATOM   2463  C  CG    A TYR A 1 161 ? -17.937 2.511   22.588  0.50 31.83 ? 161 TYR A CG    1 
ATOM   2464  C  CG    B TYR A 1 161 ? -17.921 2.289   22.380  0.50 32.34 ? 161 TYR A CG    1 
ATOM   2465  C  CD1   A TYR A 1 161 ? -17.142 2.011   21.562  0.50 34.12 ? 161 TYR A CD1   1 
ATOM   2466  C  CD1   B TYR A 1 161 ? -17.153 1.739   21.358  0.50 34.23 ? 161 TYR A CD1   1 
ATOM   2467  C  CD2   A TYR A 1 161 ? -19.221 1.990   22.740  0.50 36.28 ? 161 TYR A CD2   1 
ATOM   2468  C  CD2   B TYR A 1 161 ? -19.243 1.868   22.508  0.50 36.18 ? 161 TYR A CD2   1 
ATOM   2469  C  CE1   A TYR A 1 161 ? -17.611 1.027   20.708  0.50 33.17 ? 161 TYR A CE1   1 
ATOM   2470  C  CE1   B TYR A 1 161 ? -17.684 0.800   20.489  0.50 32.68 ? 161 TYR A CE1   1 
ATOM   2471  C  CE2   A TYR A 1 161 ? -19.698 1.004   21.891  0.50 32.28 ? 161 TYR A CE2   1 
ATOM   2472  C  CE2   B TYR A 1 161 ? -19.783 0.928   21.645  0.50 32.64 ? 161 TYR A CE2   1 
ATOM   2473  C  CZ    A TYR A 1 161 ? -18.887 0.529   20.876  0.50 33.37 ? 161 TYR A CZ    1 
ATOM   2474  C  CZ    B TYR A 1 161 ? -18.998 0.400   20.635  0.50 32.77 ? 161 TYR A CZ    1 
ATOM   2475  O  OH    A TYR A 1 161 ? -19.350 -0.447  20.026  0.50 30.54 ? 161 TYR A OH    1 
ATOM   2476  O  OH    B TYR A 1 161 ? -19.529 -0.532  19.772  0.50 29.84 ? 161 TYR A OH    1 
ATOM   2477  N  N     A GLY A 1 162 ? -17.139 7.299   23.669  0.50 38.72 ? 162 GLY A N     1 
ATOM   2478  N  N     B GLY A 1 162 ? -17.182 7.003   23.726  0.50 38.74 ? 162 GLY A N     1 
ATOM   2479  C  CA    A GLY A 1 162 ? -16.516 8.346   24.461  0.50 38.74 ? 162 GLY A CA    1 
ATOM   2480  C  CA    B GLY A 1 162 ? -16.488 8.080   24.404  0.50 38.82 ? 162 GLY A CA    1 
ATOM   2481  C  C     A GLY A 1 162 ? -16.975 8.414   25.904  0.50 28.24 ? 162 GLY A C     1 
ATOM   2482  C  C     B GLY A 1 162 ? -16.475 8.001   25.917  0.50 34.58 ? 162 GLY A C     1 
ATOM   2483  O  O     A GLY A 1 162 ? -16.277 9.000   26.738  0.50 32.21 ? 162 GLY A O     1 
ATOM   2484  O  O     B GLY A 1 162 ? -15.416 7.819   26.524  0.50 44.64 ? 162 GLY A O     1 
ATOM   2485  N  N     A LYS A 1 163 ? -18.125 7.827   26.227  0.50 35.25 ? 163 LYS A N     1 
ATOM   2486  N  N     B LYS A 1 163 ? -17.643 8.132   26.538  0.50 34.01 ? 163 LYS A N     1 
ATOM   2487  C  CA    A LYS A 1 163 ? -18.674 7.898   27.575  0.50 35.76 ? 163 LYS A CA    1 
ATOM   2488  C  CA    B LYS A 1 163 ? -17.745 8.251   27.989  0.50 35.81 ? 163 LYS A CA    1 
ATOM   2489  C  C     A LYS A 1 163 ? -18.513 6.599   28.357  0.50 35.26 ? 163 LYS A C     1 
ATOM   2490  C  C     B LYS A 1 163 ? -17.730 6.907   28.714  0.50 34.66 ? 163 LYS A C     1 
ATOM   2491  O  O     A LYS A 1 163 ? -19.108 6.459   29.432  0.50 36.89 ? 163 LYS A O     1 
ATOM   2492  O  O     B LYS A 1 163 ? -17.943 6.881   29.933  0.50 37.89 ? 163 LYS A O     1 
ATOM   2493  C  CB    A LYS A 1 163 ? -20.152 8.294   27.519  0.50 38.92 ? 163 LYS A CB    1 
ATOM   2494  C  CB    B LYS A 1 163 ? -19.015 9.022   28.360  0.50 25.07 ? 163 LYS A CB    1 
ATOM   2495  N  N     A LYS A 1 164 ? -17.721 5.653   27.858  0.50 33.24 ? 164 LYS A N     1 
ATOM   2496  N  N     B LYS A 1 164 ? -17.493 5.800   28.015  0.50 33.36 ? 164 LYS A N     1 
ATOM   2497  C  CA    A LYS A 1 164 ? -17.554 4.356   28.498  0.50 29.08 ? 164 LYS A CA    1 
ATOM   2498  C  CA    B LYS A 1 164 ? -17.456 4.501   28.672  0.50 29.44 ? 164 LYS A CA    1 
ATOM   2499  C  C     A LYS A 1 164 ? -16.116 4.189   28.972  0.50 26.57 ? 164 LYS A C     1 
ATOM   2500  C  C     B LYS A 1 164 ? -16.086 4.262   29.300  0.50 26.52 ? 164 LYS A C     1 
ATOM   2501  O  O     A LYS A 1 164 ? -15.171 4.496   28.239  0.50 32.18 ? 164 LYS A O     1 
ATOM   2502  O  O     B LYS A 1 164 ? -15.075 4.819   28.866  0.50 31.30 ? 164 LYS A O     1 
ATOM   2503  C  CB    A LYS A 1 164 ? -17.934 3.221   27.544  0.50 29.04 ? 164 LYS A CB    1 
ATOM   2504  C  CB    B LYS A 1 164 ? -17.776 3.381   27.681  0.50 29.09 ? 164 LYS A CB    1 
ATOM   2505  C  CG    A LYS A 1 164 ? -19.298 3.388   26.896  0.50 31.31 ? 164 LYS A CG    1 
ATOM   2506  C  CG    B LYS A 1 164 ? -18.950 3.659   26.758  0.50 30.87 ? 164 LYS A CG    1 
ATOM   2507  C  CD    A LYS A 1 164 ? -20.395 3.571   27.937  0.50 34.57 ? 164 LYS A CD    1 
ATOM   2508  C  CD    B LYS A 1 164 ? -20.271 3.739   27.504  0.50 36.44 ? 164 LYS A CD    1 
ATOM   2509  C  CE    A LYS A 1 164 ? -21.765 3.702   27.285  0.50 31.37 ? 164 LYS A CE    1 
ATOM   2510  C  CE    B LYS A 1 164 ? -21.437 3.813   26.525  0.50 38.00 ? 164 LYS A CE    1 
ATOM   2511  N  NZ    A LYS A 1 164 ? -22.843 3.929   28.283  0.50 37.67 ? 164 LYS A NZ    1 
ATOM   2512  N  NZ    B LYS A 1 164 ? -22.730 4.112   27.200  0.50 31.22 ? 164 LYS A NZ    1 
ATOM   2513  N  N     A SER A 1 165 ? -15.958 3.698   30.200  0.50 26.84 ? 165 SER A N     1 
ATOM   2514  N  N     B SER A 1 165 ? -16.064 3.433   30.340  0.50 27.42 ? 165 SER A N     1 
ATOM   2515  C  CA    A SER A 1 165 ? -14.646 3.554   30.814  0.50 29.25 ? 165 SER A CA    1 
ATOM   2516  C  CA    B SER A 1 165 ? -14.819 3.097   31.014  0.50 29.34 ? 165 SER A CA    1 
ATOM   2517  C  C     A SER A 1 165 ? -13.911 2.339   30.259  0.50 25.92 ? 165 SER A C     1 
ATOM   2518  C  C     B SER A 1 165 ? -14.075 2.008   30.252  0.50 25.58 ? 165 SER A C     1 
ATOM   2519  O  O     A SER A 1 165 ? -14.522 1.366   29.812  0.50 28.95 ? 165 SER A O     1 
ATOM   2520  O  O     B SER A 1 165 ? -14.677 1.145   29.611  0.50 29.18 ? 165 SER A O     1 
ATOM   2521  C  CB    A SER A 1 165 ? -14.776 3.426   32.333  0.50 29.87 ? 165 SER A CB    1 
ATOM   2522  C  CB    B SER A 1 165 ? -15.081 2.629   32.447  0.50 24.36 ? 165 SER A CB    1 
ATOM   2523  O  OG    A SER A 1 165 ? -15.449 4.544   32.883  0.50 29.75 ? 165 SER A OG    1 
ATOM   2524  O  OG    B SER A 1 165 ? -15.588 3.682   33.245  0.50 29.93 ? 165 SER A OG    1 
ATOM   2525  N  N     A LYS A 1 166 ? -12.583 2.396   30.304  0.50 26.13 ? 166 LYS A N     1 
ATOM   2526  N  N     B LYS A 1 166 ? -12.748 2.056   30.322  0.50 27.38 ? 166 LYS A N     1 
ATOM   2527  C  CA    A LYS A 1 166 ? -11.738 1.312   29.821  0.50 24.86 ? 166 LYS A CA    1 
ATOM   2528  C  CA    B LYS A 1 166 ? -11.911 1.037   29.702  0.50 24.96 ? 166 LYS A CA    1 
ATOM   2529  C  C     A LYS A 1 166 ? -10.791 0.875   30.926  0.50 23.18 ? 166 LYS A C     1 
ATOM   2530  C  C     B LYS A 1 166 ? -10.820 0.642   30.681  0.50 22.12 ? 166 LYS A C     1 
ATOM   2531  O  O     A LYS A 1 166 ? -10.133 1.713   31.550  0.50 26.64 ? 166 LYS A O     1 
ATOM   2532  O  O     B LYS A 1 166 ? -9.995  1.479   31.062  0.50 28.62 ? 166 LYS A O     1 
ATOM   2533  C  CB    A LYS A 1 166 ? -10.948 1.738   28.579  0.50 27.70 ? 166 LYS A CB    1 
ATOM   2534  C  CB    B LYS A 1 166 ? -11.313 1.535   28.381  0.50 28.75 ? 166 LYS A CB    1 
ATOM   2535  C  CG    A LYS A 1 166 ? -11.822 2.234   27.445  0.50 29.39 ? 166 LYS A CG    1 
ATOM   2536  C  CG    B LYS A 1 166 ? -12.362 1.872   27.330  0.50 27.67 ? 166 LYS A CG    1 
ATOM   2537  C  CD    A LYS A 1 166 ? -11.110 2.112   26.109  0.50 30.47 ? 166 LYS A CD    1 
ATOM   2538  C  CD    B LYS A 1 166 ? -11.783 1.895   25.925  0.50 29.16 ? 166 LYS A CD    1 
ATOM   2539  C  CE    A LYS A 1 166 ? -11.687 3.075   25.094  0.50 29.15 ? 166 LYS A CE    1 
ATOM   2540  C  CE    B LYS A 1 166 ? -10.684 2.936   25.788  0.50 27.63 ? 166 LYS A CE    1 
ATOM   2541  N  NZ    A LYS A 1 166 ? -11.578 4.474   25.588  0.50 34.16 ? 166 LYS A NZ    1 
ATOM   2542  N  NZ    B LYS A 1 166 ? -11.156 4.302   26.139  0.50 31.18 ? 166 LYS A NZ    1 
ATOM   2543  N  N     A LEU A 1 167 ? -10.729 -0.435  31.167  0.50 23.79 ? 167 LEU A N     1 
ATOM   2544  N  N     B LEU A 1 167 ? -10.826 -0.622  31.095  0.50 23.66 ? 167 LEU A N     1 
ATOM   2545  C  CA    A LEU A 1 167 ? -9.838  -1.019  32.162  0.50 20.16 ? 167 LEU A CA    1 
ATOM   2546  C  CA    B LEU A 1 167 ? -9.839  -1.170  32.015  0.50 20.50 ? 167 LEU A CA    1 
ATOM   2547  C  C     A LEU A 1 167 ? -9.033  -2.132  31.512  0.50 23.72 ? 167 LEU A C     1 
ATOM   2548  C  C     B LEU A 1 167 ? -8.883  -2.091  31.268  0.50 24.65 ? 167 LEU A C     1 
ATOM   2549  O  O     A LEU A 1 167 ? -9.611  -3.044  30.911  0.50 21.27 ? 167 LEU A O     1 
ATOM   2550  O  O     B LEU A 1 167 ? -9.193  -2.605  30.188  0.50 25.80 ? 167 LEU A O     1 
ATOM   2551  C  CB    A LEU A 1 167 ? -10.612 -1.576  33.362  0.50 24.47 ? 167 LEU A CB    1 
ATOM   2552  C  CB    B LEU A 1 167 ? -10.513 -1.936  33.161  0.50 21.48 ? 167 LEU A CB    1 
ATOM   2553  C  CG    A LEU A 1 167 ? -11.341 -0.563  34.249  0.50 27.38 ? 167 LEU A CG    1 
ATOM   2554  C  CG    B LEU A 1 167 ? -10.612 -1.191  34.494  0.50 27.59 ? 167 LEU A CG    1 
ATOM   2555  C  CD1   A LEU A 1 167 ? -12.714 -0.244  33.690  0.50 31.82 ? 167 LEU A CD1   1 
ATOM   2556  C  CD1   B LEU A 1 167 ? -11.060 0.251   34.274  0.50 23.51 ? 167 LEU A CD1   1 
ATOM   2557  C  CD2   A LEU A 1 167 ? -11.433 -1.071  35.679  0.50 23.03 ? 167 LEU A CD2   1 
ATOM   2558  C  CD2   B LEU A 1 167 ? -11.559 -1.911  35.434  0.50 22.77 ? 167 LEU A CD2   1 
ATOM   2559  N  N     A GLU A 1 168 ? -7.709  -2.066  31.635  0.50 23.36 ? 168 GLU A N     1 
ATOM   2560  N  N     B GLU A 1 168 ? -7.705  -2.295  31.861  0.50 24.05 ? 168 GLU A N     1 
ATOM   2561  C  CA    A GLU A 1 168 ? -6.831  -3.045  31.008  0.50 22.38 ? 168 GLU A CA    1 
ATOM   2562  C  CA    B GLU A 1 168 ? -6.675  -3.151  31.288  0.50 22.55 ? 168 GLU A CA    1 
ATOM   2563  C  C     A GLU A 1 168 ? -6.276  -4.019  32.033  0.50 21.05 ? 168 GLU A C     1 
ATOM   2564  C  C     B GLU A 1 168 ? -6.207  -4.182  32.301  0.50 21.61 ? 168 GLU A C     1 
ATOM   2565  O  O     A GLU A 1 168 ? -5.933  -3.633  33.154  0.50 23.30 ? 168 GLU A O     1 
ATOM   2566  O  O     B GLU A 1 168 ? -6.125  -3.908  33.501  0.50 25.49 ? 168 GLU A O     1 
ATOM   2567  C  CB    A GLU A 1 168 ? -5.653  -2.377  30.300  0.50 20.05 ? 168 GLU A CB    1 
ATOM   2568  C  CB    B GLU A 1 168 ? -5.448  -2.353  30.840  0.50 21.76 ? 168 GLU A CB    1 
ATOM   2569  C  CG    A GLU A 1 168 ? -6.006  -1.367  29.239  0.50 21.58 ? 168 GLU A CG    1 
ATOM   2570  C  CG    B GLU A 1 168 ? -5.458  -1.846  29.423  0.50 22.88 ? 168 GLU A CG    1 
ATOM   2571  C  CD    A GLU A 1 168 ? -4.764  -0.811  28.578  0.50 25.51 ? 168 GLU A CD    1 
ATOM   2572  C  CD    B GLU A 1 168 ? -4.241  -0.993  29.143  0.50 27.13 ? 168 GLU A CD    1 
ATOM   2573  O  OE1   A GLU A 1 168 ? -4.057  -1.582  27.895  0.50 22.67 ? 168 GLU A OE1   1 
ATOM   2574  O  OE1   B GLU A 1 168 ? -4.191  0.139   29.675  0.50 19.80 ? 168 GLU A OE1   1 
ATOM   2575  O  OE2   A GLU A 1 168 ? -4.465  0.385   28.774  0.50 30.72 ? 168 GLU A OE2   1 
ATOM   2576  O  OE2   B GLU A 1 168 ? -3.323  -1.465  28.424  0.50 19.47 ? 168 GLU A OE2   1 
ATOM   2577  N  N     A PHE A 1 169 ? -6.174  -5.281  31.628  0.50 20.89 ? 169 PHE A N     1 
ATOM   2578  N  N     B PHE A 1 169 ? -5.875  -5.366  31.793  0.50 20.95 ? 169 PHE A N     1 
ATOM   2579  C  CA    A PHE A 1 169 ? -5.300  -6.262  32.258  0.50 18.45 ? 169 PHE A CA    1 
ATOM   2580  C  CA    B PHE A 1 169 ? -5.064  -6.349  32.504  0.50 18.02 ? 169 PHE A CA    1 
ATOM   2581  C  C     A PHE A 1 169 ? -4.192  -6.540  31.250  0.50 23.18 ? 169 PHE A C     1 
ATOM   2582  C  C     B PHE A 1 169 ? -3.842  -6.617  31.636  0.50 22.34 ? 169 PHE A C     1 
ATOM   2583  O  O     A PHE A 1 169 ? -4.452  -7.093  30.177  0.50 20.79 ? 169 PHE A O     1 
ATOM   2584  O  O     B PHE A 1 169 ? -3.944  -7.299  30.612  0.50 21.47 ? 169 PHE A O     1 
ATOM   2585  C  CB    A PHE A 1 169 ? -6.061  -7.534  32.622  0.50 20.84 ? 169 PHE A CB    1 
ATOM   2586  C  CB    B PHE A 1 169 ? -5.848  -7.630  32.776  0.50 20.99 ? 169 PHE A CB    1 
ATOM   2587  C  CG    A PHE A 1 169 ? -7.169  -7.315  33.618  0.50 21.47 ? 169 PHE A CG    1 
ATOM   2588  C  CG    B PHE A 1 169 ? -6.936  -7.467  33.803  0.50 21.70 ? 169 PHE A CG    1 
ATOM   2589  C  CD1   A PHE A 1 169 ? -8.443  -6.984  33.197  0.50 23.10 ? 169 PHE A CD1   1 
ATOM   2590  C  CD1   B PHE A 1 169 ? -6.699  -7.750  35.136  0.50 21.45 ? 169 PHE A CD1   1 
ATOM   2591  C  CD2   A PHE A 1 169 ? -6.932  -7.432  34.975  0.50 22.28 ? 169 PHE A CD2   1 
ATOM   2592  C  CD2   B PHE A 1 169 ? -8.192  -7.022  33.436  0.50 22.06 ? 169 PHE A CD2   1 
ATOM   2593  C  CE1   A PHE A 1 169 ? -9.467  -6.777  34.113  0.50 26.99 ? 169 PHE A CE1   1 
ATOM   2594  C  CE1   B PHE A 1 169 ? -7.706  -7.597  36.085  0.50 22.02 ? 169 PHE A CE1   1 
ATOM   2595  C  CE2   A PHE A 1 169 ? -7.954  -7.230  35.896  0.50 20.41 ? 169 PHE A CE2   1 
ATOM   2596  C  CE2   B PHE A 1 169 ? -9.197  -6.865  34.379  0.50 27.32 ? 169 PHE A CE2   1 
ATOM   2597  C  CZ    A PHE A 1 169 ? -9.216  -6.900  35.460  0.50 23.16 ? 169 PHE A CZ    1 
ATOM   2598  C  CZ    B PHE A 1 169 ? -8.949  -7.152  35.700  0.50 23.06 ? 169 PHE A CZ    1 
ATOM   2599  N  N     A SER A 1 170 ? -2.969  -6.129  31.579  0.50 20.26 ? 170 SER A N     1 
ATOM   2600  N  N     B SER A 1 170 ? -2.697  -6.077  32.039  0.50 21.69 ? 170 SER A N     1 
ATOM   2601  C  CA    A SER A 1 170 ? -1.847  -6.165  30.651  0.50 18.53 ? 170 SER A CA    1 
ATOM   2602  C  CA    B SER A 1 170 ? -1.502  -6.046  31.208  0.50 19.87 ? 170 SER A CA    1 
ATOM   2603  C  C     A SER A 1 170 ? -0.697  -6.958  31.255  0.50 22.86 ? 170 SER A C     1 
ATOM   2604  C  C     B SER A 1 170 ? -0.487  -7.087  31.662  0.50 22.63 ? 170 SER A C     1 
ATOM   2605  O  O     A SER A 1 170 ? -0.290  -6.705  32.394  0.50 19.46 ? 170 SER A O     1 
ATOM   2606  O  O     B SER A 1 170 ? -0.228  -7.235  32.858  0.50 22.26 ? 170 SER A O     1 
ATOM   2607  C  CB    A SER A 1 170 ? -1.381  -4.748  30.307  0.50 20.67 ? 170 SER A CB    1 
ATOM   2608  C  CB    B SER A 1 170 ? -0.853  -4.661  31.257  0.50 20.86 ? 170 SER A CB    1 
ATOM   2609  O  OG    A SER A 1 170 ? -2.482  -3.861  30.204  0.50 25.74 ? 170 SER A OG    1 
ATOM   2610  O  OG    B SER A 1 170 ? -1.774  -3.642  30.919  0.50 23.84 ? 170 SER A OG    1 
ATOM   2611  N  N     A ILE A 1 171 ? -0.150  -7.892  30.482  0.50 20.43 ? 171 ILE A N     1 
ATOM   2612  N  N     B ILE A 1 171 ? 0.111   -7.786  30.703  0.50 21.47 ? 171 ILE A N     1 
ATOM   2613  C  CA    A ILE A 1 171 ? 0.886   -8.789  30.981  0.50 23.14 ? 171 ILE A CA    1 
ATOM   2614  C  CA    B ILE A 1 171 ? 1.219   -8.692  30.983  0.50 23.22 ? 171 ILE A CA    1 
ATOM   2615  C  C     A ILE A 1 171 ? 2.246   -8.150  30.718  0.50 21.07 ? 171 ILE A C     1 
ATOM   2616  C  C     B ILE A 1 171 ? 2.517   -7.954  30.690  0.50 19.67 ? 171 ILE A C     1 
ATOM   2617  O  O     A ILE A 1 171 ? 2.657   -7.982  29.568  0.50 20.48 ? 171 ILE A O     1 
ATOM   2618  O  O     B ILE A 1 171 ? 2.778   -7.566  29.545  0.50 21.62 ? 171 ILE A O     1 
ATOM   2619  C  CB    A ILE A 1 171 ? 0.783   -10.180 30.346  0.50 21.43 ? 171 ILE A CB    1 
ATOM   2620  C  CB    B ILE A 1 171 ? 1.122   -9.989  30.166  0.50 22.16 ? 171 ILE A CB    1 
ATOM   2621  C  CG1   A ILE A 1 171 ? -0.639  -10.728 30.512  0.50 23.60 ? 171 ILE A CG1   1 
ATOM   2622  C  CG1   B ILE A 1 171 ? -0.124  -10.768 30.569  0.50 23.52 ? 171 ILE A CG1   1 
ATOM   2623  C  CG2   A ILE A 1 171 ? 1.803   -11.125 30.972  0.50 25.40 ? 171 ILE A CG2   1 
ATOM   2624  C  CG2   B ILE A 1 171 ? 2.358   -10.847 30.408  0.50 24.44 ? 171 ILE A CG2   1 
ATOM   2625  C  CD1   A ILE A 1 171 ? -1.204  -10.566 31.916  0.50 20.07 ? 171 ILE A CD1   1 
ATOM   2626  C  CD1   B ILE A 1 171 ? -0.149  -11.131 32.038  0.50 27.62 ? 171 ILE A CD1   1 
ATOM   2627  N  N     A TYR A 1 172 ? 2.930   -7.790  31.796  0.50 20.37 ? 172 TYR A N     1 
ATOM   2628  N  N     B TYR A 1 172 ? 3.313   -7.759  31.723  0.50 22.00 ? 172 TYR A N     1 
ATOM   2629  C  CA    A TYR A 1 172 ? 4.267   -7.204  31.777  0.50 24.69 ? 172 TYR A CA    1 
ATOM   2630  C  CA    B TYR A 1 172 ? 4.601   -7.076  31.805  0.50 23.33 ? 172 TYR A CA    1 
ATOM   2631  C  C     A TYR A 1 172 ? 5.302   -8.305  31.547  0.50 22.71 ? 172 TYR A C     1 
ATOM   2632  C  C     B TYR A 1 172 ? 5.728   -8.093  31.632  0.50 23.43 ? 172 TYR A C     1 
ATOM   2633  O  O     A TYR A 1 172 ? 5.253   -9.340  32.218  0.50 21.39 ? 172 TYR A O     1 
ATOM   2634  O  O     B TYR A 1 172 ? 5.717   -9.136  32.298  0.50 23.35 ? 172 TYR A O     1 
ATOM   2635  C  CB    A TYR A 1 172 ? 4.491   -6.484  33.111  0.50 24.78 ? 172 TYR A CB    1 
ATOM   2636  C  CB    B TYR A 1 172 ? 4.702   -6.362  33.151  0.50 25.23 ? 172 TYR A CB    1 
ATOM   2637  C  CG    A TYR A 1 172 ? 5.818   -5.796  33.352  0.50 23.91 ? 172 TYR A CG    1 
ATOM   2638  C  CG    B TYR A 1 172 ? 6.021   -5.716  33.521  0.50 23.40 ? 172 TYR A CG    1 
ATOM   2639  C  CD1   A TYR A 1 172 ? 6.965   -6.529  33.620  0.50 21.81 ? 172 TYR A CD1   1 
ATOM   2640  C  CD1   B TYR A 1 172 ? 7.079   -6.478  33.993  0.50 21.88 ? 172 TYR A CD1   1 
ATOM   2641  C  CD2   A TYR A 1 172 ? 5.902   -4.411  33.404  0.50 22.87 ? 172 TYR A CD2   1 
ATOM   2642  C  CD2   B TYR A 1 172 ? 6.177   -4.336  33.481  0.50 23.53 ? 172 TYR A CD2   1 
ATOM   2643  C  CE1   A TYR A 1 172 ? 8.166   -5.908  33.877  0.50 23.72 ? 172 TYR A CE1   1 
ATOM   2644  C  CE1   B TYR A 1 172 ? 8.267   -5.899  34.363  0.50 23.41 ? 172 TYR A CE1   1 
ATOM   2645  C  CE2   A TYR A 1 172 ? 7.105   -3.775  33.662  0.50 25.96 ? 172 TYR A CE2   1 
ATOM   2646  C  CE2   B TYR A 1 172 ? 7.373   -3.741  33.849  0.50 25.33 ? 172 TYR A CE2   1 
ATOM   2647  C  CZ    A TYR A 1 172 ? 8.234   -4.532  33.895  0.50 25.96 ? 172 TYR A CZ    1 
ATOM   2648  C  CZ    B TYR A 1 172 ? 8.415   -4.532  34.289  0.50 26.78 ? 172 TYR A CZ    1 
ATOM   2649  O  OH    A TYR A 1 172 ? 9.436   -3.916  34.156  0.50 26.65 ? 172 TYR A OH    1 
ATOM   2650  O  OH    B TYR A 1 172 ? 9.609   -3.965  34.668  0.50 23.07 ? 172 TYR A OH    1 
ATOM   2651  N  N     A PRO A 1 173 ? 6.234   -8.131  30.612  0.50 18.30 ? 173 PRO A N     1 
ATOM   2652  N  N     B PRO A 1 173 ? 6.704   -7.833  30.761  0.50 21.72 ? 173 PRO A N     1 
ATOM   2653  C  CA    A PRO A 1 173 ? 7.113   -9.241  30.229  0.50 21.37 ? 173 PRO A CA    1 
ATOM   2654  C  CA    B PRO A 1 173 ? 7.629   -8.896  30.346  0.50 21.54 ? 173 PRO A CA    1 
ATOM   2655  C  C     A PRO A 1 173 ? 8.259   -9.484  31.200  0.50 24.73 ? 173 PRO A C     1 
ATOM   2656  C  C     B PRO A 1 173 ? 8.587   -9.338  31.443  0.50 25.07 ? 173 PRO A C     1 
ATOM   2657  O  O     A PRO A 1 173 ? 8.715   -8.588  31.915  0.50 24.61 ? 173 PRO A O     1 
ATOM   2658  O  O     B PRO A 1 173 ? 8.998   -8.559  32.306  0.50 23.04 ? 173 PRO A O     1 
ATOM   2659  C  CB    A PRO A 1 173 ? 7.648   -8.803  28.860  0.50 25.37 ? 173 PRO A CB    1 
ATOM   2660  C  CB    B PRO A 1 173 ? 8.395   -8.261  29.179  0.50 22.67 ? 173 PRO A CB    1 
ATOM   2661  C  CG    A PRO A 1 173 ? 7.616   -7.310  28.906  0.50 21.20 ? 173 PRO A CG    1 
ATOM   2662  C  CG    B PRO A 1 173 ? 8.282   -6.787  29.405  0.50 24.71 ? 173 PRO A CG    1 
ATOM   2663  C  CD    A PRO A 1 173 ? 6.437   -6.938  29.765  0.50 21.86 ? 173 PRO A CD    1 
ATOM   2664  C  CD    B PRO A 1 173 ? 6.937   -6.573  30.030  0.50 20.91 ? 173 PRO A CD    1 
ATOM   2665  N  N     A ALA A 1 174 ? 8.733   -10.728 31.196  0.50 25.06 ? 174 ALA A N     1 
ATOM   2666  N  N     B ALA A 1 174 ? 8.956   -10.618 31.374  0.50 25.53 ? 174 ALA A N     1 
ATOM   2667  C  CA    A ALA A 1 174 ? 9.864   -11.181 31.993  0.50 28.34 ? 174 ALA A CA    1 
ATOM   2668  C  CA    B ALA A 1 174 ? 9.950   -11.225 32.246  0.50 28.47 ? 174 ALA A CA    1 
ATOM   2669  C  C     A ALA A 1 174 ? 10.724  -12.124 31.165  0.50 29.52 ? 174 ALA A C     1 
ATOM   2670  C  C     B ALA A 1 174 ? 10.922  -12.028 31.391  0.50 30.30 ? 174 ALA A C     1 
ATOM   2671  O  O     A ALA A 1 174 ? 10.197  -12.900 30.358  0.50 30.95 ? 174 ALA A O     1 
ATOM   2672  O  O     B ALA A 1 174 ? 10.485  -12.811 30.532  0.50 29.93 ? 174 ALA A O     1 
ATOM   2673  C  CB    A ALA A 1 174 ? 9.404   -11.899 33.269  0.50 29.10 ? 174 ALA A CB    1 
ATOM   2674  C  CB    B ALA A 1 174 ? 9.296   -12.133 33.285  0.50 29.36 ? 174 ALA A CB    1 
ATOM   2675  N  N     A PRO A 1 175 ? 12.047  -12.097 31.355  0.50 35.48 ? 175 PRO A N     1 
ATOM   2676  N  N     B PRO A 1 175 ? 12.234  -11.893 31.608  0.50 34.81 ? 175 PRO A N     1 
ATOM   2677  C  CA    A PRO A 1 175 ? 12.923  -12.932 30.511  0.50 34.03 ? 175 PRO A CA    1 
ATOM   2678  C  CA    B PRO A 1 175 ? 13.198  -12.577 30.726  0.50 34.31 ? 175 PRO A CA    1 
ATOM   2679  C  C     A PRO A 1 175 ? 12.788  -14.423 30.767  0.50 36.51 ? 175 PRO A C     1 
ATOM   2680  C  C     B PRO A 1 175 ? 13.149  -14.093 30.817  0.50 36.43 ? 175 PRO A C     1 
ATOM   2681  O  O     A PRO A 1 175 ? 13.173  -15.216 29.897  0.50 36.24 ? 175 PRO A O     1 
ATOM   2682  O  O     B PRO A 1 175 ? 13.610  -14.764 29.886  0.50 39.45 ? 175 PRO A O     1 
ATOM   2683  C  CB    A PRO A 1 175 ? 14.329  -12.435 30.865  0.50 38.06 ? 175 PRO A CB    1 
ATOM   2684  C  CB    B PRO A 1 175 ? 14.557  -12.038 31.199  0.50 40.30 ? 175 PRO A CB    1 
ATOM   2685  C  CG    A PRO A 1 175 ? 14.191  -11.900 32.253  0.50 37.87 ? 175 PRO A CG    1 
ATOM   2686  C  CG    B PRO A 1 175 ? 14.241  -10.806 31.999  0.50 34.67 ? 175 PRO A CG    1 
ATOM   2687  C  CD    A PRO A 1 175 ? 12.812  -11.304 32.332  0.50 37.20 ? 175 PRO A CD    1 
ATOM   2688  C  CD    B PRO A 1 175 ? 12.905  -11.067 32.623  0.50 37.96 ? 175 PRO A CD    1 
ATOM   2689  N  N     A GLN A 1 176 ? 12.267  -14.828 31.928  0.50 34.70 ? 176 GLN A N     1 
ATOM   2690  N  N     B GLN A 1 176 ? 12.602  -14.655 31.898  0.50 33.57 ? 176 GLN A N     1 
ATOM   2691  C  CA    A GLN A 1 176 ? 12.066  -16.246 32.213  0.50 39.20 ? 176 GLN A CA    1 
ATOM   2692  C  CA    B GLN A 1 176 ? 12.591  -16.104 32.059  0.50 39.27 ? 176 GLN A CA    1 
ATOM   2693  C  C     A GLN A 1 176 ? 11.192  -16.899 31.149  0.50 39.08 ? 176 GLN A C     1 
ATOM   2694  C  C     B GLN A 1 176 ? 11.600  -16.794 31.131  0.50 38.96 ? 176 GLN A C     1 
ATOM   2695  O  O     A GLN A 1 176 ? 11.638  -17.789 30.416  0.50 46.86 ? 176 GLN A O     1 
ATOM   2696  O  O     B GLN A 1 176 ? 11.789  -17.973 30.814  0.50 48.21 ? 176 GLN A O     1 
ATOM   2697  C  CB    A GLN A 1 176 ? 11.446  -16.413 33.602  0.50 34.86 ? 176 GLN A CB    1 
ATOM   2698  C  CB    B GLN A 1 176 ? 12.271  -16.472 33.506  0.50 37.63 ? 176 GLN A CB    1 
ATOM   2699  C  CG    A GLN A 1 176 ? 12.416  -16.226 34.766  0.50 36.92 ? 176 GLN A CG    1 
ATOM   2700  C  CG    B GLN A 1 176 ? 13.183  -15.828 34.525  0.50 36.54 ? 176 GLN A CG    1 
ATOM   2701  C  CD    A GLN A 1 176 ? 12.838  -14.783 34.980  0.50 36.87 ? 176 GLN A CD    1 
ATOM   2702  C  CD    B GLN A 1 176 ? 12.413  -15.026 35.549  0.50 37.24 ? 176 GLN A CD    1 
ATOM   2703  O  OE1   A GLN A 1 176 ? 12.595  -13.915 34.143  0.50 27.18 ? 176 GLN A OE1   1 
ATOM   2704  O  OE1   B GLN A 1 176 ? 11.700  -14.081 35.205  0.50 34.56 ? 176 GLN A OE1   1 
ATOM   2705  N  NE2   A GLN A 1 176 ? 13.475  -14.521 36.116  0.50 40.04 ? 176 GLN A NE2   1 
ATOM   2706  N  NE2   B GLN A 1 176 ? 12.539  -15.404 36.816  0.50 42.53 ? 176 GLN A NE2   1 
ATOM   2707  N  N     A VAL A 1 177 ? 9.940   -16.462 31.047  0.50 36.80 ? 177 VAL A N     1 
ATOM   2708  N  N     B VAL A 1 177 ? 10.558  -16.093 30.676  0.50 35.42 ? 177 VAL A N     1 
ATOM   2709  C  CA    A VAL A 1 177 ? 9.048   -16.934 29.995  0.50 34.86 ? 177 VAL A CA    1 
ATOM   2710  C  CA    B VAL A 1 177 ? 9.547   -16.677 29.803  0.50 33.08 ? 177 VAL A CA    1 
ATOM   2711  C  C     A VAL A 1 177 ? 8.804   -15.792 29.016  0.50 31.74 ? 177 VAL A C     1 
ATOM   2712  C  C     B VAL A 1 177 ? 9.286   -15.841 28.560  0.50 31.74 ? 177 VAL A C     1 
ATOM   2713  O  O     A VAL A 1 177 ? 7.736   -15.170 29.007  0.50 29.94 ? 177 VAL A O     1 
ATOM   2714  O  O     B VAL A 1 177 ? 8.445   -16.218 27.743  0.50 37.42 ? 177 VAL A O     1 
ATOM   2715  C  CB    A VAL A 1 177 ? 7.733   -17.483 30.580  0.50 31.66 ? 177 VAL A CB    1 
ATOM   2716  C  CB    B VAL A 1 177 ? 8.222   -16.920 30.562  0.50 36.01 ? 177 VAL A CB    1 
ATOM   2717  C  CG1   A VAL A 1 177 ? 7.955   -18.880 31.133  0.50 40.27 ? 177 VAL A CG1   1 
ATOM   2718  C  CG1   B VAL A 1 177 ? 8.446   -17.785 31.799  0.50 32.61 ? 177 VAL A CG1   1 
ATOM   2719  C  CG2   A VAL A 1 177 ? 7.214   -16.569 31.680  0.50 33.37 ? 177 VAL A CG2   1 
ATOM   2720  C  CG2   B VAL A 1 177 ? 7.577   -15.595 30.941  0.50 27.99 ? 177 VAL A CG2   1 
ATOM   2721  N  N     A SER A 1 178 ? 9.803   -15.504 28.194  0.50 33.75 ? 178 SER A N     1 
ATOM   2722  N  N     B SER A 1 178 ? 9.982   -14.719 28.385  0.50 38.01 ? 178 SER A N     1 
ATOM   2723  C  CA    A SER A 1 178 ? 9.731   -14.448 27.198  0.50 32.85 ? 178 SER A CA    1 
ATOM   2724  C  CA    B SER A 1 178 ? 9.685   -13.793 27.299  0.50 32.91 ? 178 SER A CA    1 
ATOM   2725  C  C     A SER A 1 178 ? 9.677   -15.052 25.803  0.50 31.23 ? 178 SER A C     1 
ATOM   2726  C  C     B SER A 1 178 ? 9.941   -14.435 25.937  0.50 29.45 ? 178 SER A C     1 
ATOM   2727  O  O     A SER A 1 178 ? 9.950   -16.238 25.599  0.50 33.95 ? 178 SER A O     1 
ATOM   2728  O  O     B SER A 1 178 ? 10.646  -15.441 25.813  0.50 35.98 ? 178 SER A O     1 
ATOM   2729  C  CB    A SER A 1 178 ? 10.929  -13.500 27.320  0.50 27.36 ? 178 SER A CB    1 
ATOM   2730  C  CB    B SER A 1 178 ? 10.518  -12.520 27.444  0.50 27.37 ? 178 SER A CB    1 
ATOM   2731  O  OG    A SER A 1 178 ? 11.188  -12.847 26.090  0.50 36.92 ? 178 SER A OG    1 
ATOM   2732  O  OG    B SER A 1 178 ? 11.886  -12.827 27.641  0.50 35.69 ? 178 SER A OG    1 
ATOM   2733  N  N     A THR A 1 179 ? 9.318   -14.213 24.836  0.50 27.56 ? 179 THR A N     1 
ATOM   2734  N  N     B THR A 1 179 ? 9.356   -13.830 24.902  0.50 26.51 ? 179 THR A N     1 
ATOM   2735  C  CA    A THR A 1 179 ? 9.283   -14.616 23.438  0.50 26.11 ? 179 THR A CA    1 
ATOM   2736  C  CA    B THR A 1 179 ? 9.402   -14.384 23.555  0.50 26.69 ? 179 THR A CA    1 
ATOM   2737  C  C     A THR A 1 179 ? 10.313  -13.863 22.606  0.50 29.69 ? 179 THR A C     1 
ATOM   2738  C  C     B THR A 1 179 ? 10.220  -13.561 22.570  0.50 29.89 ? 179 THR A C     1 
ATOM   2739  O  O     A THR A 1 179 ? 11.223  -14.477 22.040  0.50 29.41 ? 179 THR A O     1 
ATOM   2740  O  O     B THR A 1 179 ? 10.402  -14.007 21.430  0.50 29.32 ? 179 THR A O     1 
ATOM   2741  C  CB    A THR A 1 179 ? 7.878   -14.405 22.852  0.50 30.02 ? 179 THR A CB    1 
ATOM   2742  C  CB    B THR A 1 179 ? 7.982   -14.543 22.991  0.50 29.75 ? 179 THR A CB    1 
ATOM   2743  O  OG1   A THR A 1 179 ? 6.906   -15.062 23.671  0.50 30.06 ? 179 THR A OG1   1 
ATOM   2744  O  OG1   B THR A 1 179 ? 7.374   -13.252 22.848  0.50 31.84 ? 179 THR A OG1   1 
ATOM   2745  C  CG2   A THR A 1 179 ? 7.799   -14.971 21.441  0.50 30.02 ? 179 THR A CG2   1 
ATOM   2746  C  CG2   B THR A 1 179 ? 7.133   -15.406 23.909  0.50 31.78 ? 179 THR A CG2   1 
ATOM   2747  N  N     A ALA A 1 180 ? 10.197  -12.540 22.529  0.50 27.76 ? 180 ALA A N     1 
ATOM   2748  N  N     B ALA A 1 180 ? 10.700  -12.380 22.956  0.50 26.92 ? 180 ALA A N     1 
ATOM   2749  C  CA    A ALA A 1 180 ? 10.932  -11.734 21.567  0.50 24.09 ? 180 ALA A CA    1 
ATOM   2750  C  CA    B ALA A 1 180 ? 11.420  -11.536 22.011  0.50 20.75 ? 180 ALA A CA    1 
ATOM   2751  C  C     A ALA A 1 180 ? 11.935  -10.823 22.264  0.50 20.39 ? 180 ALA A C     1 
ATOM   2752  C  C     B ALA A 1 180 ? 12.341  -10.587 22.763  0.50 21.82 ? 180 ALA A C     1 
ATOM   2753  O  O     A ALA A 1 180 ? 11.681  -10.316 23.359  0.50 20.63 ? 180 ALA A O     1 
ATOM   2754  O  O     B ALA A 1 180 ? 12.138  -10.294 23.942  0.50 22.46 ? 180 ALA A O     1 
ATOM   2755  C  CB    A ALA A 1 180 ? 9.971   -10.895 20.721  0.50 23.20 ? 180 ALA A CB    1 
ATOM   2756  C  CB    B ALA A 1 180 ? 10.460  -10.747 21.113  0.50 21.49 ? 180 ALA A CB    1 
ATOM   2757  N  N     A VAL A 1 181 ? 13.080  -10.606 21.615  0.50 23.40 ? 181 VAL A N     1 
ATOM   2758  N  N     B VAL A 1 181 ? 13.365  -10.107 22.055  0.50 19.61 ? 181 VAL A N     1 
ATOM   2759  C  CA    A VAL A 1 181 ? 14.059  -9.679  22.159  0.50 19.59 ? 181 VAL A CA    1 
ATOM   2760  C  CA    B VAL A 1 181 ? 14.286  -9.153  22.657  0.50 16.45 ? 181 VAL A CA    1 
ATOM   2761  C  C     A VAL A 1 181 ? 13.538  -8.246  22.130  0.50 17.32 ? 181 VAL A C     1 
ATOM   2762  C  C     B VAL A 1 181 ? 13.740  -7.730  22.602  0.50 20.06 ? 181 VAL A C     1 
ATOM   2763  O  O     A VAL A 1 181 ? 14.025  -7.399  22.887  0.50 23.09 ? 181 VAL A O     1 
ATOM   2764  O  O     B VAL A 1 181 ? 14.171  -6.876  23.388  0.50 22.03 ? 181 VAL A O     1 
ATOM   2765  C  CB    A VAL A 1 181 ? 15.389  -9.816  21.388  0.50 20.24 ? 181 VAL A CB    1 
ATOM   2766  C  CB    B VAL A 1 181 ? 15.656  -9.251  21.963  0.50 25.36 ? 181 VAL A CB    1 
ATOM   2767  C  CG1   A VAL A 1 181 ? 15.259  -9.232  19.990  0.50 21.13 ? 181 VAL A CG1   1 
ATOM   2768  C  CG1   B VAL A 1 181 ? 15.603  -8.594  20.602  0.50 21.69 ? 181 VAL A CG1   1 
ATOM   2769  C  CG2   A VAL A 1 181 ? 16.535  -9.174  22.157  0.50 25.26 ? 181 VAL A CG2   1 
ATOM   2770  C  CG2   B VAL A 1 181 ? 16.745  -8.644  22.823  0.50 28.95 ? 181 VAL A CG2   1 
ATOM   2771  N  N     A VAL A 1 182 ? 12.529  -7.960  21.303  0.50 17.00 ? 182 VAL A N     1 
ATOM   2772  N  N     B VAL A 1 182 ? 12.783  -7.459  21.714  0.50 18.52 ? 182 VAL A N     1 
ATOM   2773  C  CA    A VAL A 1 182 ? 12.040  -6.600  21.088  0.50 18.25 ? 182 VAL A CA    1 
ATOM   2774  C  CA    B VAL A 1 182 ? 12.235  -6.120  21.532  0.50 19.13 ? 182 VAL A CA    1 
ATOM   2775  C  C     A VAL A 1 182 ? 10.897  -6.221  22.029  0.50 20.47 ? 182 VAL A C     1 
ATOM   2776  C  C     B VAL A 1 182 ? 11.001  -5.909  22.402  0.50 18.99 ? 182 VAL A C     1 
ATOM   2777  O  O     A VAL A 1 182 ? 10.286  -5.158  21.875  0.50 21.15 ? 182 VAL A O     1 
ATOM   2778  O  O     B VAL A 1 182 ? 10.300  -4.902  22.257  0.50 20.06 ? 182 VAL A O     1 
ATOM   2779  C  CB    A VAL A 1 182 ? 11.594  -6.422  19.626  0.50 23.72 ? 182 VAL A CB    1 
ATOM   2780  C  CB    B VAL A 1 182 ? 11.891  -5.865  20.055  0.50 22.24 ? 182 VAL A CB    1 
ATOM   2781  C  CG1   A VAL A 1 182 ? 12.803  -6.391  18.698  0.50 19.84 ? 182 VAL A CG1   1 
ATOM   2782  C  CG1   B VAL A 1 182 ? 13.159  -5.828  19.206  0.50 20.32 ? 182 VAL A CG1   1 
ATOM   2783  C  CG2   A VAL A 1 182 ? 10.642  -7.541  19.227  0.50 20.95 ? 182 VAL A CG2   1 
ATOM   2784  C  CG2   B VAL A 1 182 ? 10.932  -6.932  19.545  0.50 23.18 ? 182 VAL A CG2   1 
ATOM   2785  N  N     A GLU A 1 183 ? 10.598  -7.071  23.009  0.50 21.80 ? 183 GLU A N     1 
ATOM   2786  N  N     B GLU A 1 183 ? 10.715  -6.853  23.294  0.50 22.23 ? 183 GLU A N     1 
ATOM   2787  C  CA    A GLU A 1 183 ? 9.466   -6.786  23.887  0.50 21.28 ? 183 GLU A CA    1 
ATOM   2788  C  CA    B GLU A 1 183 ? 9.600   -6.667  24.221  0.50 21.50 ? 183 GLU A CA    1 
ATOM   2789  C  C     A GLU A 1 183 ? 9.590   -5.479  24.674  0.50 22.31 ? 183 GLU A C     1 
ATOM   2790  C  C     B GLU A 1 183 ? 9.670   -5.350  24.990  0.50 21.30 ? 183 GLU A C     1 
ATOM   2791  O  O     A GLU A 1 183 ? 8.542   -4.861  24.929  0.50 22.43 ? 183 GLU A O     1 
ATOM   2792  O  O     B GLU A 1 183 ? 8.612   -4.726  25.175  0.50 23.05 ? 183 GLU A O     1 
ATOM   2793  C  CB    A GLU A 1 183 ? 9.228   -7.977  24.829  0.50 22.60 ? 183 GLU A CB    1 
ATOM   2794  C  CB    B GLU A 1 183 ? 9.503   -7.865  25.180  0.50 21.58 ? 183 GLU A CB    1 
ATOM   2795  C  CG    A GLU A 1 183 ? 8.818   -9.229  24.065  0.50 23.69 ? 183 GLU A CG    1 
ATOM   2796  C  CG    B GLU A 1 183 ? 9.074   -9.154  24.488  0.50 23.64 ? 183 GLU A CG    1 
ATOM   2797  C  CD    A GLU A 1 183 ? 8.073   -10.248 24.899  0.50 20.85 ? 183 GLU A CD    1 
ATOM   2798  C  CD    B GLU A 1 183 ? 8.595   -10.225 25.448  0.50 23.09 ? 183 GLU A CD    1 
ATOM   2799  O  OE1   A GLU A 1 183 ? 7.505   -9.886  25.956  0.50 24.76 ? 183 GLU A OE1   1 
ATOM   2800  O  OE1   B GLU A 1 183 ? 8.057   -9.880  26.523  0.50 25.09 ? 183 GLU A OE1   1 
ATOM   2801  O  OE2   A GLU A 1 183 ? 8.044   -11.422 24.478  0.50 20.91 ? 183 GLU A OE2   1 
ATOM   2802  O  OE2   B GLU A 1 183 ? 8.743   -11.416 25.117  0.50 21.95 ? 183 GLU A OE2   1 
ATOM   2803  N  N     A PRO A 1 184 ? 10.779  -4.998  25.069  0.50 22.08 ? 184 PRO A N     1 
ATOM   2804  N  N     B PRO A 1 184 ? 10.836  -4.857  25.433  0.50 24.46 ? 184 PRO A N     1 
ATOM   2805  C  CA    A PRO A 1 184 ? 10.836  -3.642  25.653  0.50 23.07 ? 184 PRO A CA    1 
ATOM   2806  C  CA    B PRO A 1 184 ? 10.852  -3.515  26.049  0.50 22.68 ? 184 PRO A CA    1 
ATOM   2807  C  C     A PRO A 1 184 ? 10.290  -2.559  24.737  0.50 22.06 ? 184 PRO A C     1 
ATOM   2808  C  C     B PRO A 1 184 ? 10.455  -2.400  25.095  0.50 21.96 ? 184 PRO A C     1 
ATOM   2809  O  O     A PRO A 1 184 ? 9.552   -1.680  25.202  0.50 23.81 ? 184 PRO A O     1 
ATOM   2810  O  O     B PRO A 1 184 ? 9.818   -1.430  25.527  0.50 23.81 ? 184 PRO A O     1 
ATOM   2811  C  CB    A PRO A 1 184 ? 12.331  -3.450  25.936  0.50 25.38 ? 184 PRO A CB    1 
ATOM   2812  C  CB    B PRO A 1 184 ? 12.303  -3.368  26.529  0.50 24.49 ? 184 PRO A CB    1 
ATOM   2813  C  CG    A PRO A 1 184 ? 12.833  -4.821  26.174  0.50 23.31 ? 184 PRO A CG    1 
ATOM   2814  C  CG    B PRO A 1 184 ? 12.781  -4.763  26.712  0.50 19.88 ? 184 PRO A CG    1 
ATOM   2815  C  CD    A PRO A 1 184 ? 12.066  -5.704  25.228  0.50 21.75 ? 184 PRO A CD    1 
ATOM   2816  C  CD    B PRO A 1 184 ? 12.134  -5.540  25.604  0.50 23.09 ? 184 PRO A CD    1 
ATOM   2817  N  N     A TYR A 1 185 ? 10.636  -2.592  23.446  0.50 21.25 ? 185 TYR A N     1 
ATOM   2818  N  N     B TYR A 1 185 ? 10.824  -2.498  23.814  0.50 22.92 ? 185 TYR A N     1 
ATOM   2819  C  CA    A TYR A 1 185 ? 10.092  -1.621  22.500  0.50 22.36 ? 185 TYR A CA    1 
ATOM   2820  C  CA    B TYR A 1 185 ? 10.345  -1.537  22.823  0.50 21.32 ? 185 TYR A CA    1 
ATOM   2821  C  C     A TYR A 1 185 ? 8.570   -1.678  22.469  0.50 20.51 ? 185 TYR A C     1 
ATOM   2822  C  C     B TYR A 1 185 ? 8.823   -1.516  22.786  0.50 22.28 ? 185 TYR A C     1 
ATOM   2823  O  O     A TYR A 1 185 ? 7.893   -0.644  22.521  0.50 20.15 ? 185 TYR A O     1 
ATOM   2824  O  O     B TYR A 1 185 ? 8.191   -0.491  23.066  0.50 22.50 ? 185 TYR A O     1 
ATOM   2825  C  CB    A TYR A 1 185 ? 10.644  -1.880  21.096  0.50 17.48 ? 185 TYR A CB    1 
ATOM   2826  C  CB    B TYR A 1 185 ? 10.891  -1.883  21.435  0.50 19.93 ? 185 TYR A CB    1 
ATOM   2827  C  CG    A TYR A 1 185 ? 12.048  -1.374  20.852  0.50 23.88 ? 185 TYR A CG    1 
ATOM   2828  C  CG    B TYR A 1 185 ? 12.309  -1.445  21.169  0.50 23.88 ? 185 TYR A CG    1 
ATOM   2829  C  CD1   A TYR A 1 185 ? 12.785  -0.770  21.862  0.50 23.59 ? 185 TYR A CD1   1 
ATOM   2830  C  CD1   B TYR A 1 185 ? 12.952  -0.537  21.998  0.50 23.53 ? 185 TYR A CD1   1 
ATOM   2831  C  CD2   A TYR A 1 185 ? 12.631  -1.491  19.598  0.50 23.21 ? 185 TYR A CD2   1 
ATOM   2832  C  CD2   B TYR A 1 185 ? 13.001  -1.936  20.072  0.50 21.58 ? 185 TYR A CD2   1 
ATOM   2833  C  CE1   A TYR A 1 185 ? 14.069  -0.307  21.628  0.50 26.23 ? 185 TYR A CE1   1 
ATOM   2834  C  CE1   B TYR A 1 185 ? 14.252  -0.137  21.741  0.50 26.42 ? 185 TYR A CE1   1 
ATOM   2835  C  CE2   A TYR A 1 185 ? 13.907  -1.028  19.356  0.50 23.23 ? 185 TYR A CE2   1 
ATOM   2836  C  CE2   B TYR A 1 185 ? 14.293  -1.543  19.810  0.50 23.48 ? 185 TYR A CE2   1 
ATOM   2837  C  CZ    A TYR A 1 185 ? 14.621  -0.439  20.374  0.50 23.97 ? 185 TYR A CZ    1 
ATOM   2838  C  CZ    B TYR A 1 185 ? 14.915  -0.644  20.646  0.50 24.59 ? 185 TYR A CZ    1 
ATOM   2839  O  OH    A TYR A 1 185 ? 15.897  0.020   20.134  0.50 26.62 ? 185 TYR A OH    1 
ATOM   2840  O  OH    B TYR A 1 185 ? 16.210  -0.250  20.383  0.50 27.08 ? 185 TYR A OH    1 
ATOM   2841  N  N     A ASN A 1 186 ? 8.017   -2.888  22.377  0.50 18.93 ? 186 ASN A N     1 
ATOM   2842  N  N     B ASN A 1 186 ? 8.220   -2.659  22.444  0.50 18.34 ? 186 ASN A N     1 
ATOM   2843  C  CA    A ASN A 1 186 ? 6.576   -3.038  22.225  0.50 19.70 ? 186 ASN A CA    1 
ATOM   2844  C  CA    B ASN A 1 186 ? 6.769   -2.737  22.319  0.50 19.94 ? 186 ASN A CA    1 
ATOM   2845  C  C     A ASN A 1 186 ? 5.835   -2.487  23.434  0.50 18.47 ? 186 ASN A C     1 
ATOM   2846  C  C     B ASN A 1 186 ? 6.080   -2.308  23.608  0.50 18.84 ? 186 ASN A C     1 
ATOM   2847  O  O     A ASN A 1 186 ? 4.761   -1.893  23.290  0.50 21.75 ? 186 ASN A O     1 
ATOM   2848  O  O     B ASN A 1 186 ? 5.064   -1.610  23.565  0.50 22.24 ? 186 ASN A O     1 
ATOM   2849  C  CB    A ASN A 1 186 ? 6.225   -4.509  21.999  0.50 21.70 ? 186 ASN A CB    1 
ATOM   2850  C  CB    B ASN A 1 186 ? 6.347   -4.157  21.937  0.50 20.80 ? 186 ASN A CB    1 
ATOM   2851  C  CG    A ASN A 1 186 ? 6.873   -5.075  20.745  0.50 21.18 ? 186 ASN A CG    1 
ATOM   2852  C  CG    B ASN A 1 186 ? 6.914   -4.600  20.597  0.50 19.90 ? 186 ASN A CG    1 
ATOM   2853  O  OD1   A ASN A 1 186 ? 7.065   -4.364  19.758  0.50 20.87 ? 186 ASN A OD1   1 
ATOM   2854  O  OD1   B ASN A 1 186 ? 7.425   -3.790  19.822  0.50 21.21 ? 186 ASN A OD1   1 
ATOM   2855  N  ND2   A ASN A 1 186 ? 7.217   -6.358  20.783  0.50 19.97 ? 186 ASN A ND2   1 
ATOM   2856  N  ND2   B ASN A 1 186 ? 6.819   -5.897  20.318  0.50 20.46 ? 186 ASN A ND2   1 
ATOM   2857  N  N     A SER A 1 187 ? 6.411   -2.650  24.629  0.50 21.40 ? 187 SER A N     1 
ATOM   2858  N  N     B SER A 1 187 ? 6.636   -2.697  24.760  0.50 22.16 ? 187 SER A N     1 
ATOM   2859  C  CA    A SER A 1 187 ? 5.756   -2.230  25.863  0.50 21.95 ? 187 SER A CA    1 
ATOM   2860  C  CA    B SER A 1 187 ? 6.038   -2.346  26.046  0.50 20.94 ? 187 SER A CA    1 
ATOM   2861  C  C     A SER A 1 187 ? 5.774   -0.717  26.040  0.50 26.55 ? 187 SER A C     1 
ATOM   2862  C  C     B SER A 1 187 ? 5.933   -0.836  26.208  0.50 26.45 ? 187 SER A C     1 
ATOM   2863  O  O     A SER A 1 187 ? 4.854   -0.160  26.647  0.50 22.23 ? 187 SER A O     1 
ATOM   2864  O  O     B SER A 1 187 ? 4.860   -0.305  26.518  0.50 21.88 ? 187 SER A O     1 
ATOM   2865  C  CB    A SER A 1 187 ? 6.427   -2.897  27.064  0.50 23.29 ? 187 SER A CB    1 
ATOM   2866  C  CB    B SER A 1 187 ? 6.857   -2.945  27.191  0.50 24.43 ? 187 SER A CB    1 
ATOM   2867  O  OG    A SER A 1 187 ? 6.572   -4.290  26.861  0.50 23.88 ? 187 SER A OG    1 
ATOM   2868  O  OG    B SER A 1 187 ? 6.891   -4.358  27.130  0.50 22.38 ? 187 SER A OG    1 
ATOM   2869  N  N     A ILE A 1 188 ? 6.804   -0.044  25.530  0.50 21.17 ? 188 ILE A N     1 
ATOM   2870  N  N     B ILE A 1 188 ? 7.045   -0.128  26.000  0.50 23.43 ? 188 ILE A N     1 
ATOM   2871  C  CA    A ILE A 1 188 ? 6.892   1.407   25.659  0.50 23.89 ? 188 ILE A CA    1 
ATOM   2872  C  CA    B ILE A 1 188 ? 7.044   1.327   26.126  0.50 22.30 ? 188 ILE A CA    1 
ATOM   2873  C  C     A ILE A 1 188 ? 5.953   2.092   24.675  0.50 25.56 ? 188 ILE A C     1 
ATOM   2874  C  C     B ILE A 1 188 ? 6.165   1.958   25.054  0.50 24.94 ? 188 ILE A C     1 
ATOM   2875  O  O     A ILE A 1 188 ? 5.298   3.085   25.010  0.50 23.33 ? 188 ILE A O     1 
ATOM   2876  O  O     B ILE A 1 188 ? 5.467   2.947   25.306  0.50 23.26 ? 188 ILE A O     1 
ATOM   2877  C  CB    A ILE A 1 188 ? 8.350   1.865   25.462  0.50 26.75 ? 188 ILE A CB    1 
ATOM   2878  C  CB    B ILE A 1 188 ? 8.490   1.859   26.062  0.50 28.26 ? 188 ILE A CB    1 
ATOM   2879  C  CG1   A ILE A 1 188 ? 9.262   1.233   26.517  0.50 30.93 ? 188 ILE A CG1   1 
ATOM   2880  C  CG1   B ILE A 1 188 ? 9.266   1.469   27.325  0.50 27.46 ? 188 ILE A CG1   1 
ATOM   2881  C  CG2   A ILE A 1 188 ? 8.453   3.391   25.474  0.50 25.92 ? 188 ILE A CG2   1 
ATOM   2882  C  CG2   B ILE A 1 188 ? 8.517   3.370   25.825  0.50 27.87 ? 188 ILE A CG2   1 
ATOM   2883  C  CD1   A ILE A 1 188 ? 8.801   1.440   27.935  0.50 27.90 ? 188 ILE A CD1   1 
ATOM   2884  C  CD1   B ILE A 1 188 ? 8.526   1.752   28.605  0.50 29.64 ? 188 ILE A CD1   1 
ATOM   2885  N  N     A LEU A 1 189 ? 5.884   1.581   23.443  0.50 22.51 ? 189 LEU A N     1 
ATOM   2886  N  N     B LEU A 1 189 ? 6.177   1.391   23.845  0.50 22.94 ? 189 LEU A N     1 
ATOM   2887  C  CA    A LEU A 1 189 ? 4.986   2.155   22.448  0.50 21.47 ? 189 LEU A CA    1 
ATOM   2888  C  CA    B LEU A 1 189 ? 5.438   1.984   22.734  0.50 19.89 ? 189 LEU A CA    1 
ATOM   2889  C  C     A LEU A 1 189 ? 3.521   1.897   22.779  0.50 21.36 ? 189 LEU A C     1 
ATOM   2890  C  C     B LEU A 1 189 ? 3.933   1.969   22.983  0.50 22.57 ? 189 LEU A C     1 
ATOM   2891  O  O     A LEU A 1 189 ? 2.667   2.735   22.470  0.50 20.83 ? 189 LEU A O     1 
ATOM   2892  O  O     B LEU A 1 189 ? 3.261   2.997   22.837  0.50 22.26 ? 189 LEU A O     1 
ATOM   2893  C  CB    A LEU A 1 189 ? 5.307   1.594   21.067  0.50 19.07 ? 189 LEU A CB    1 
ATOM   2894  C  CB    B LEU A 1 189 ? 5.780   1.249   21.439  0.50 19.15 ? 189 LEU A CB    1 
ATOM   2895  C  CG    A LEU A 1 189 ? 6.671   1.963   20.490  0.50 19.63 ? 189 LEU A CG    1 
ATOM   2896  C  CG    B LEU A 1 189 ? 7.191   1.544   20.923  0.50 18.55 ? 189 LEU A CG    1 
ATOM   2897  C  CD1   A LEU A 1 189 ? 7.018   1.019   19.347  0.50 22.18 ? 189 LEU A CD1   1 
ATOM   2898  C  CD1   B LEU A 1 189 ? 7.531   0.664   19.722  0.50 22.63 ? 189 LEU A CD1   1 
ATOM   2899  C  CD2   A LEU A 1 189 ? 6.667   3.405   20.023  0.50 18.78 ? 189 LEU A CD2   1 
ATOM   2900  C  CD2   B LEU A 1 189 ? 7.325   3.019   20.582  0.50 20.37 ? 189 LEU A CD2   1 
ATOM   2901  N  N     A THR A 1 190 ? 3.199   0.749   23.381  0.50 21.23 ? 190 THR A N     1 
ATOM   2902  N  N     B THR A 1 190 ? 3.378   0.810   23.350  0.50 20.68 ? 190 THR A N     1 
ATOM   2903  C  CA    A THR A 1 190 ? 1.804   0.501   23.735  0.50 26.30 ? 190 THR A CA    1 
ATOM   2904  C  CA    B THR A 1 190 ? 1.933   0.757   23.559  0.50 27.14 ? 190 THR A CA    1 
ATOM   2905  C  C     A THR A 1 190 ? 1.382   1.354   24.924  0.50 24.51 ? 190 THR A C     1 
ATOM   2906  C  C     B THR A 1 190 ? 1.523   1.508   24.818  0.50 24.31 ? 190 THR A C     1 
ATOM   2907  O  O     A THR A 1 190 ? 0.234   1.810   24.989  0.50 24.14 ? 190 THR A O     1 
ATOM   2908  O  O     B THR A 1 190 ? 0.411   2.045   24.880  0.50 22.87 ? 190 THR A O     1 
ATOM   2909  C  CB    A THR A 1 190 ? 1.561   -0.990  24.011  0.50 23.72 ? 190 THR A CB    1 
ATOM   2910  C  CB    B THR A 1 190 ? 1.434   -0.693  23.609  0.50 24.04 ? 190 THR A CB    1 
ATOM   2911  O  OG1   A THR A 1 190 ? 0.156   -1.228  24.149  0.50 21.08 ? 190 THR A OG1   1 
ATOM   2912  O  OG1   B THR A 1 190 ? 0.020   -0.717  23.364  0.50 24.30 ? 190 THR A OG1   1 
ATOM   2913  C  CG2   A THR A 1 190 ? 2.251   -1.453  25.282  0.50 25.74 ? 190 THR A CG2   1 
ATOM   2914  C  CG2   B THR A 1 190 ? 1.701   -1.339  24.964  0.50 21.20 ? 190 THR A CG2   1 
ATOM   2915  N  N     A THR A 1 191 ? 2.300   1.602   25.863  0.50 24.54 ? 191 THR A N     1 
ATOM   2916  N  N     B THR A 1 191 ? 2.405   1.580   25.817  0.50 24.53 ? 191 THR A N     1 
ATOM   2917  C  CA    A THR A 1 191 ? 1.970   2.446   27.008  0.50 25.59 ? 191 THR A CA    1 
ATOM   2918  C  CA    B THR A 1 191 ? 2.090   2.340   27.022  0.50 25.70 ? 191 THR A CA    1 
ATOM   2919  C  C     A THR A 1 191 ? 1.683   3.876   26.570  0.50 24.49 ? 191 THR A C     1 
ATOM   2920  C  C     B THR A 1 191 ? 1.990   3.830   26.721  0.50 25.39 ? 191 THR A C     1 
ATOM   2921  O  O     A THR A 1 191 ? 0.714   4.488   27.028  0.50 24.05 ? 191 THR A O     1 
ATOM   2922  O  O     B THR A 1 191 ? 1.086   4.508   27.221  0.50 23.52 ? 191 THR A O     1 
ATOM   2923  C  CB    A THR A 1 191 ? 3.104   2.415   28.031  0.50 23.20 ? 191 THR A CB    1 
ATOM   2924  C  CB    B THR A 1 191 ? 3.140   2.068   28.098  0.50 23.85 ? 191 THR A CB    1 
ATOM   2925  O  OG1   A THR A 1 191 ? 3.348   1.062   28.430  0.50 26.81 ? 191 THR A OG1   1 
ATOM   2926  O  OG1   B THR A 1 191 ? 3.064   0.692   28.490  0.50 24.95 ? 191 THR A OG1   1 
ATOM   2927  C  CG2   A THR A 1 191 ? 2.741   3.241   29.259  0.50 30.20 ? 191 THR A CG2   1 
ATOM   2928  C  CG2   B THR A 1 191 ? 2.914   2.956   29.316  0.50 30.44 ? 191 THR A CG2   1 
ATOM   2929  N  N     A HIS A 1 192 ? 2.509   4.423   25.673  0.50 22.14 ? 192 HIS A N     1 
ATOM   2930  N  N     B HIS A 1 192 ? 2.896   4.351   25.887  0.50 20.48 ? 192 HIS A N     1 
ATOM   2931  C  CA    A HIS A 1 192 ? 2.299   5.789   25.203  0.50 22.06 ? 192 HIS A CA    1 
ATOM   2932  C  CA    B HIS A 1 192 ? 2.837   5.762   25.511  0.50 22.57 ? 192 HIS A CA    1 
ATOM   2933  C  C     A HIS A 1 192 ? 0.963   5.929   24.484  0.50 28.43 ? 192 HIS A C     1 
ATOM   2934  C  C     B HIS A 1 192 ? 1.535   6.099   24.798  0.50 27.60 ? 192 HIS A C     1 
ATOM   2935  O  O     A HIS A 1 192 ? 0.127   6.763   24.849  0.50 26.02 ? 192 HIS A O     1 
ATOM   2936  O  O     B HIS A 1 192 ? 0.920   7.137   25.073  0.50 27.84 ? 192 HIS A O     1 
ATOM   2937  C  CB    A HIS A 1 192 ? 3.443   6.211   24.279  0.50 21.06 ? 192 HIS A CB    1 
ATOM   2938  C  CB    B HIS A 1 192 ? 4.030   6.122   24.624  0.50 20.61 ? 192 HIS A CB    1 
ATOM   2939  C  CG    A HIS A 1 192 ? 3.209   7.519   23.590  0.50 23.20 ? 192 HIS A CG    1 
ATOM   2940  C  CG    B HIS A 1 192 ? 3.854   7.399   23.858  0.50 24.68 ? 192 HIS A CG    1 
ATOM   2941  N  ND1   A HIS A 1 192 ? 2.791   8.650   24.259  0.50 24.80 ? 192 HIS A ND1   1 
ATOM   2942  N  ND1   B HIS A 1 192 ? 3.709   8.624   24.472  0.50 27.73 ? 192 HIS A ND1   1 
ATOM   2943  C  CD2   A HIS A 1 192 ? 3.333   7.877   22.289  0.50 26.38 ? 192 HIS A CD2   1 
ATOM   2944  C  CD2   B HIS A 1 192 ? 3.806   7.640   22.526  0.50 26.99 ? 192 HIS A CD2   1 
ATOM   2945  C  CE1   A HIS A 1 192 ? 2.669   9.648   23.401  0.50 25.33 ? 192 HIS A CE1   1 
ATOM   2946  C  CE1   B HIS A 1 192 ? 3.581   9.565   23.553  0.50 24.81 ? 192 HIS A CE1   1 
ATOM   2947  N  NE2   A HIS A 1 192 ? 2.994   9.206   22.200  0.50 29.60 ? 192 HIS A NE2   1 
ATOM   2948  N  NE2   B HIS A 1 192 ? 3.634   8.994   22.363  0.50 28.41 ? 192 HIS A NE2   1 
ATOM   2949  N  N     A THR A 1 193 ? 0.746   5.119   23.449  0.50 24.64 ? 193 THR A N     1 
ATOM   2950  N  N     B THR A 1 193 ? 1.100   5.240   23.873  0.50 24.93 ? 193 THR A N     1 
ATOM   2951  C  CA    A THR A 1 193 ? -0.415  5.310   22.589  0.50 24.55 ? 193 THR A CA    1 
ATOM   2952  C  CA    B THR A 1 193 ? -0.068  5.545   23.055  0.50 25.62 ? 193 THR A CA    1 
ATOM   2953  C  C     A THR A 1 193 ? -1.734  4.982   23.284  0.50 25.43 ? 193 THR A C     1 
ATOM   2954  C  C     B THR A 1 193 ? -1.385  5.227   23.756  0.50 24.57 ? 193 THR A C     1 
ATOM   2955  O  O     A THR A 1 193 ? -2.785  5.440   22.829  0.50 28.37 ? 193 THR A O     1 
ATOM   2956  O  O     B THR A 1 193 ? -2.414  5.813   23.404  0.50 25.32 ? 193 THR A O     1 
ATOM   2957  C  CB    A THR A 1 193 ? -0.254  4.473   21.322  0.50 25.31 ? 193 THR A CB    1 
ATOM   2958  C  CB    B THR A 1 193 ? 0.001   4.780   21.734  0.50 25.27 ? 193 THR A CB    1 
ATOM   2959  O  OG1   A THR A 1 193 ? 0.133   3.141   21.673  0.50 31.58 ? 193 THR A OG1   1 
ATOM   2960  O  OG1   B THR A 1 193 ? -0.164  3.381   21.984  0.50 30.51 ? 193 THR A OG1   1 
ATOM   2961  C  CG2   A THR A 1 193 ? 0.829   5.074   20.444  0.50 24.30 ? 193 THR A CG2   1 
ATOM   2962  C  CG2   B THR A 1 193 ? 1.349   5.008   21.055  0.50 21.84 ? 193 THR A CG2   1 
ATOM   2963  N  N     A THR A 1 194 ? -1.708  4.218   24.375  0.50 25.67 ? 194 THR A N     1 
ATOM   2964  N  N     B THR A 1 194 ? -1.381  4.321   24.727  0.50 24.67 ? 194 THR A N     1 
ATOM   2965  C  CA    A THR A 1 194 ? -2.933  3.842   25.075  0.50 21.57 ? 194 THR A CA    1 
ATOM   2966  C  CA    B THR A 1 194 ? -2.601  3.937   25.430  0.50 20.71 ? 194 THR A CA    1 
ATOM   2967  C  C     A THR A 1 194 ? -3.171  4.648   26.348  0.50 24.82 ? 194 THR A C     1 
ATOM   2968  C  C     B THR A 1 194 ? -2.853  4.772   26.679  0.50 25.02 ? 194 THR A C     1 
ATOM   2969  O  O     A THR A 1 194 ? -4.308  4.684   26.835  0.50 25.55 ? 194 THR A O     1 
ATOM   2970  O  O     B THR A 1 194 ? -3.963  4.730   27.224  0.50 27.74 ? 194 THR A O     1 
ATOM   2971  C  CB    A THR A 1 194 ? -2.905  2.340   25.414  0.50 28.36 ? 194 THR A CB    1 
ATOM   2972  C  CB    B THR A 1 194 ? -2.539  2.446   25.806  0.50 27.98 ? 194 THR A CB    1 
ATOM   2973  O  OG1   A THR A 1 194 ? -2.550  1.593   24.245  0.50 26.29 ? 194 THR A OG1   1 
ATOM   2974  O  OG1   B THR A 1 194 ? -2.001  1.697   24.708  0.50 26.20 ? 194 THR A OG1   1 
ATOM   2975  C  CG2   A THR A 1 194 ? -4.261  1.852   25.902  0.50 28.17 ? 194 THR A CG2   1 
ATOM   2976  C  CG2   B THR A 1 194 ? -3.923  1.901   26.134  0.50 27.75 ? 194 THR A CG2   1 
ATOM   2977  N  N     A LEU A 1 195 ? -2.136  5.318   26.867  0.50 24.08 ? 195 LEU A N     1 
ATOM   2978  N  N     B LEU A 1 195 ? -1.863  5.551   27.123  0.50 24.57 ? 195 LEU A N     1 
ATOM   2979  C  CA    A LEU A 1 195 ? -2.212  5.988   28.166  0.50 26.31 ? 195 LEU A CA    1 
ATOM   2980  C  CA    B LEU A 1 195 ? -1.932  6.181   28.440  0.50 25.61 ? 195 LEU A CA    1 
ATOM   2981  C  C     A LEU A 1 195 ? -3.462  6.859   28.291  0.50 28.26 ? 195 LEU A C     1 
ATOM   2982  C  C     B LEU A 1 195 ? -3.081  7.184   28.546  0.50 29.14 ? 195 LEU A C     1 
ATOM   2983  O  O     A LEU A 1 195 ? -4.203  6.768   29.278  0.50 23.40 ? 195 LEU A O     1 
ATOM   2984  O  O     B LEU A 1 195 ? -3.663  7.342   29.626  0.50 27.57 ? 195 LEU A O     1 
ATOM   2985  C  CB    A LEU A 1 195 ? -0.945  6.823   28.370  0.50 26.84 ? 195 LEU A CB    1 
ATOM   2986  C  CB    B LEU A 1 195 ? -0.589  6.847   28.747  0.50 25.53 ? 195 LEU A CB    1 
ATOM   2987  C  CG    A LEU A 1 195 ? -0.198  6.846   29.705  0.50 27.29 ? 195 LEU A CG    1 
ATOM   2988  C  CG    B LEU A 1 195 ? -0.205  7.249   30.171  0.50 31.93 ? 195 LEU A CG    1 
ATOM   2989  C  CD1   A LEU A 1 195 ? -0.070  5.460   30.303  0.50 29.21 ? 195 LEU A CD1   1 
ATOM   2990  C  CD1   B LEU A 1 195 ? -0.613  6.196   31.184  0.50 22.94 ? 195 LEU A CD1   1 
ATOM   2991  C  CD2   A LEU A 1 195 ? 1.177   7.467   29.501  0.50 26.95 ? 195 LEU A CD2   1 
ATOM   2992  C  CD2   B LEU A 1 195 ? 1.296   7.477   30.227  0.50 30.15 ? 195 LEU A CD2   1 
ATOM   2993  N  N     A GLU A 1 196 ? -3.720  7.700   27.286  0.50 29.99 ? 196 GLU A N     1 
ATOM   2994  N  N     B GLU A 1 196 ? -3.427  7.863   27.446  0.50 30.47 ? 196 GLU A N     1 
ATOM   2995  C  CA    A GLU A 1 196 ? -4.863  8.608   27.313  0.50 28.26 ? 196 GLU A CA    1 
ATOM   2996  C  CA    B GLU A 1 196 ? -4.554  8.795   27.468  0.50 28.42 ? 196 GLU A CA    1 
ATOM   2997  C  C     A GLU A 1 196 ? -6.195  7.894   27.108  0.50 32.87 ? 196 GLU A C     1 
ATOM   2998  C  C     B GLU A 1 196 ? -5.889  8.061   27.469  0.50 34.13 ? 196 GLU A C     1 
ATOM   2999  O  O     A GLU A 1 196 ? -7.246  8.497   27.350  0.50 33.09 ? 196 GLU A O     1 
ATOM   3000  O  O     B GLU A 1 196 ? -6.841  8.501   28.125  0.50 29.16 ? 196 GLU A O     1 
ATOM   3001  C  CB    A GLU A 1 196 ? -4.686  9.697   26.247  0.50 35.28 ? 196 GLU A CB    1 
ATOM   3002  C  CB    B GLU A 1 196 ? -4.478  9.752   26.271  0.50 35.08 ? 196 GLU A CB    1 
ATOM   3003  C  CG    A GLU A 1 196 ? -5.732  10.809  26.279  0.50 40.37 ? 196 GLU A CG    1 
ATOM   3004  C  CG    B GLU A 1 196 ? -5.770  9.884   25.462  0.50 36.45 ? 196 GLU A CG    1 
ATOM   3005  C  CD    A GLU A 1 196 ? -5.538  11.844  25.182  0.50 41.87 ? 196 GLU A CD    1 
ATOM   3006  C  CD    B GLU A 1 196 ? -5.636  10.823  24.270  0.50 37.28 ? 196 GLU A CD    1 
ATOM   3007  O  OE1   A GLU A 1 196 ? -4.568  11.723  24.405  0.50 34.60 ? 196 GLU A OE1   1 
ATOM   3008  O  OE1   B GLU A 1 196 ? -4.529  10.922  23.699  0.50 40.83 ? 196 GLU A OE1   1 
ATOM   3009  O  OE2   A GLU A 1 196 ? -6.363  12.778  25.098  0.50 43.28 ? 196 GLU A OE2   1 
ATOM   3010  O  OE2   B GLU A 1 196 ? -6.644  11.468  23.905  0.50 40.71 ? 196 GLU A OE2   1 
ATOM   3011  N  N     A HIS A 1 197 ? -6.184  6.627   26.700  0.50 26.50 ? 197 HIS A N     1 
ATOM   3012  N  N     B HIS A 1 197 ? -5.968  6.932   26.762  0.50 26.08 ? 197 HIS A N     1 
ATOM   3013  C  CA    A HIS A 1 197 ? -7.405  5.924   26.330  0.50 30.02 ? 197 HIS A CA    1 
ATOM   3014  C  CA    B HIS A 1 197 ? -7.216  6.213   26.548  0.50 30.11 ? 197 HIS A CA    1 
ATOM   3015  C  C     A HIS A 1 197 ? -7.778  4.808   27.299  0.50 31.03 ? 197 HIS A C     1 
ATOM   3016  C  C     B HIS A 1 197 ? -7.548  5.214   27.649  0.50 30.41 ? 197 HIS A C     1 
ATOM   3017  O  O     A HIS A 1 197 ? -8.658  3.998   26.987  0.50 28.76 ? 197 HIS A O     1 
ATOM   3018  O  O     B HIS A 1 197 ? -8.655  4.664   27.649  0.50 31.68 ? 197 HIS A O     1 
ATOM   3019  C  CB    A HIS A 1 197 ? -7.264  5.377   24.912  0.50 30.11 ? 197 HIS A CB    1 
ATOM   3020  C  CB    B HIS A 1 197 ? -7.164  5.474   25.210  0.50 29.08 ? 197 HIS A CB    1 
ATOM   3021  C  CG    A HIS A 1 197 ? -6.867  6.418   23.912  0.50 31.35 ? 197 HIS A CG    1 
ATOM   3022  C  CG    B HIS A 1 197 ? -6.868  6.362   24.043  0.50 31.26 ? 197 HIS A CG    1 
ATOM   3023  N  ND1   A HIS A 1 197 ? -7.648  7.518   23.637  0.50 32.54 ? 197 HIS A ND1   1 
ATOM   3024  N  ND1   B HIS A 1 197 ? -7.816  7.185   23.474  0.50 32.84 ? 197 HIS A ND1   1 
ATOM   3025  C  CD2   A HIS A 1 197 ? -5.764  6.534   23.134  0.50 33.22 ? 197 HIS A CD2   1 
ATOM   3026  C  CD2   B HIS A 1 197 ? -5.728  6.557   23.337  0.50 33.23 ? 197 HIS A CD2   1 
ATOM   3027  C  CE1   A HIS A 1 197 ? -7.050  8.264   22.725  0.50 35.28 ? 197 HIS A CE1   1 
ATOM   3028  C  CE1   B HIS A 1 197 ? -7.275  7.845   22.466  0.50 33.51 ? 197 HIS A CE1   1 
ATOM   3029  N  NE2   A HIS A 1 197 ? -5.904  7.689   22.403  0.50 32.90 ? 197 HIS A NE2   1 
ATOM   3030  N  NE2   B HIS A 1 197 ? -6.008  7.484   22.363  0.50 33.00 ? 197 HIS A NE2   1 
ATOM   3031  N  N     A SER A 1 198 ? -7.150  4.754   28.468  0.50 24.84 ? 198 SER A N     1 
ATOM   3032  N  N     B SER A 1 198 ? -6.632  4.959   28.573  0.50 25.87 ? 198 SER A N     1 
ATOM   3033  C  CA    A SER A 1 198 ? -7.462  3.749   29.473  0.50 22.20 ? 198 SER A CA    1 
ATOM   3034  C  CA    B SER A 1 198 ? -6.833  3.966   29.618  0.50 25.54 ? 198 SER A CA    1 
ATOM   3035  C  C     A SER A 1 198 ? -7.605  4.419   30.831  0.50 24.31 ? 198 SER A C     1 
ATOM   3036  C  C     B SER A 1 198 ? -7.243  4.654   30.912  0.50 25.18 ? 198 SER A C     1 
ATOM   3037  O  O     A SER A 1 198 ? -6.798  5.279   31.198  0.50 25.24 ? 198 SER A O     1 
ATOM   3038  O  O     B SER A 1 198 ? -6.602  5.620   31.335  0.50 25.24 ? 198 SER A O     1 
ATOM   3039  C  CB    A SER A 1 198 ? -6.382  2.674   29.537  0.50 26.32 ? 198 SER A CB    1 
ATOM   3040  C  CB    B SER A 1 198 ? -5.559  3.151   29.834  0.50 23.72 ? 198 SER A CB    1 
ATOM   3041  O  OG    A SER A 1 198 ? -6.770  1.611   30.385  0.50 25.27 ? 198 SER A OG    1 
ATOM   3042  O  OG    B SER A 1 198 ? -5.763  2.120   30.777  0.50 23.13 ? 198 SER A OG    1 
ATOM   3043  N  N     A ASP A 1 199 ? -8.626  4.005   31.580  0.50 24.11 ? 199 ASP A N     1 
ATOM   3044  N  N     B ASP A 1 199 ? -8.304  4.149   31.540  0.50 25.07 ? 199 ASP A N     1 
ATOM   3045  C  CA    A ASP A 1 199 ? -8.943  4.626   32.860  0.50 24.64 ? 199 ASP A CA    1 
ATOM   3046  C  CA    B ASP A 1 199 ? -8.768  4.705   32.805  0.50 24.42 ? 199 ASP A CA    1 
ATOM   3047  C  C     A ASP A 1 199 ? -8.174  4.016   34.023  0.50 27.65 ? 199 ASP A C     1 
ATOM   3048  C  C     B ASP A 1 199 ? -8.116  4.037   34.008  0.50 27.64 ? 199 ASP A C     1 
ATOM   3049  O  O     A ASP A 1 199 ? -7.873  4.720   34.993  0.50 26.17 ? 199 ASP A O     1 
ATOM   3050  O  O     B ASP A 1 199 ? -7.919  4.690   35.039  0.50 26.14 ? 199 ASP A O     1 
ATOM   3051  C  CB    A ASP A 1 199 ? -10.447 4.516   33.128  0.50 26.96 ? 199 ASP A CB    1 
ATOM   3052  C  CB    B ASP A 1 199 ? -10.291 4.578   32.909  0.50 27.45 ? 199 ASP A CB    1 
ATOM   3053  C  CG    A ASP A 1 199 ? -11.274 5.246   32.091  0.50 30.33 ? 199 ASP A CG    1 
ATOM   3054  C  CG    B ASP A 1 199 ? -11.017 5.367   31.832  0.50 31.08 ? 199 ASP A CG    1 
ATOM   3055  O  OD1   A ASP A 1 199 ? -11.532 6.450   32.285  0.50 29.52 ? 199 ASP A OD1   1 
ATOM   3056  O  OD1   B ASP A 1 199 ? -10.461 6.381   31.358  0.50 27.26 ? 199 ASP A OD1   1 
ATOM   3057  O  OD2   A ASP A 1 199 ? -11.635 4.628   31.065  0.50 26.16 ? 199 ASP A OD2   1 
ATOM   3058  O  OD2   B ASP A 1 199 ? -12.142 4.972   31.458  0.50 31.17 ? 199 ASP A OD2   1 
ATOM   3059  N  N     A CYS A 1 200 ? -7.853  2.727   33.944  0.50 23.96 ? 200 CYS A N     1 
ATOM   3060  N  N     B CYS A 1 200 ? -7.776  2.755   33.893  0.50 24.03 ? 200 CYS A N     1 
ATOM   3061  C  CA    A CYS A 1 200 ? -7.193  2.022   35.039  0.50 22.99 ? 200 CYS A CA    1 
ATOM   3062  C  CA    B CYS A 1 200 ? -7.130  2.002   34.958  0.50 22.98 ? 200 CYS A CA    1 
ATOM   3063  C  C     A CYS A 1 200 ? -6.638  0.720   34.486  0.50 24.59 ? 200 CYS A C     1 
ATOM   3064  C  C     B CYS A 1 200 ? -6.508  0.761   34.333  0.50 24.40 ? 200 CYS A C     1 
ATOM   3065  O  O     A CYS A 1 200 ? -7.389  -0.071  33.911  0.50 24.95 ? 200 CYS A O     1 
ATOM   3066  O  O     B CYS A 1 200 ? -7.045  0.208   33.372  0.50 25.20 ? 200 CYS A O     1 
ATOM   3067  C  CB    A CYS A 1 200 ? -8.179  1.760   36.181  0.50 25.14 ? 200 CYS A CB    1 
ATOM   3068  C  CB    B CYS A 1 200 ? -8.131  1.625   36.058  0.50 25.37 ? 200 CYS A CB    1 
ATOM   3069  S  SG    A CYS A 1 200 ? -7.589  0.629   37.448  0.50 27.29 ? 200 CYS A SG    1 
ATOM   3070  S  SG    B CYS A 1 200 ? -7.394  1.029   37.593  0.50 27.39 ? 200 CYS A SG    1 
ATOM   3071  N  N     A ALA A 1 201 ? -5.339  0.493   34.654  0.50 24.45 ? 201 ALA A N     1 
ATOM   3072  N  N     B ALA A 1 201 ? -5.372  0.329   34.876  0.50 24.45 ? 201 ALA A N     1 
ATOM   3073  C  CA    A ALA A 1 201 ? -4.670  -0.668  34.085  0.50 26.82 ? 201 ALA A CA    1 
ATOM   3074  C  CA    B ALA A 1 201 ? -4.649  -0.795  34.286  0.50 26.41 ? 201 ALA A CA    1 
ATOM   3075  C  C     A ALA A 1 201 ? -4.018  -1.485  35.189  0.50 25.73 ? 201 ALA A C     1 
ATOM   3076  C  C     B ALA A 1 201 ? -3.926  -1.577  35.370  0.50 25.66 ? 201 ALA A C     1 
ATOM   3077  O  O     A ALA A 1 201 ? -3.231  -0.952  35.978  0.50 25.67 ? 201 ALA A O     1 
ATOM   3078  O  O     B ALA A 1 201 ? -3.059  -1.027  36.055  0.50 26.00 ? 201 ALA A O     1 
ATOM   3079  C  CB    A ALA A 1 201 ? -3.620  -0.249  33.050  0.50 22.25 ? 201 ALA A CB    1 
ATOM   3080  C  CB    B ALA A 1 201 ? -3.653  -0.310  33.228  0.50 22.38 ? 201 ALA A CB    1 
ATOM   3081  N  N     A PHE A 1 202 ? -4.342  -2.776  35.232  0.50 22.17 ? 202 PHE A N     1 
ATOM   3082  N  N     B PHE A 1 202 ? -4.274  -2.856  35.508  0.50 21.16 ? 202 PHE A N     1 
ATOM   3083  C  CA    A PHE A 1 202 ? -3.799  -3.704  36.214  0.50 20.00 ? 202 PHE A CA    1 
ATOM   3084  C  CA    B PHE A 1 202 ? -3.584  -3.767  36.412  0.50 20.47 ? 202 PHE A CA    1 
ATOM   3085  C  C     A PHE A 1 202 ? -2.684  -4.510  35.551  0.50 24.82 ? 202 PHE A C     1 
ATOM   3086  C  C     B PHE A 1 202 ? -2.487  -4.484  35.631  0.50 24.89 ? 202 PHE A C     1 
ATOM   3087  O  O     A PHE A 1 202 ? -2.955  -5.391  34.729  0.50 23.36 ? 202 PHE A O     1 
ATOM   3088  O  O     B PHE A 1 202 ? -2.776  -5.325  34.775  0.50 23.50 ? 202 PHE A O     1 
ATOM   3089  C  CB    A PHE A 1 202 ? -4.897  -4.622  36.748  0.50 18.01 ? 202 PHE A CB    1 
ATOM   3090  C  CB    B PHE A 1 202 ? -4.558  -4.773  37.021  0.50 18.85 ? 202 PHE A CB    1 
ATOM   3091  C  CG    A PHE A 1 202 ? -6.077  -3.887  37.334  0.50 20.73 ? 202 PHE A CG    1 
ATOM   3092  C  CG    B PHE A 1 202 ? -5.620  -4.148  37.884  0.50 22.17 ? 202 PHE A CG    1 
ATOM   3093  C  CD1   A PHE A 1 202 ? -6.014  -3.353  38.610  0.50 23.16 ? 202 PHE A CD1   1 
ATOM   3094  C  CD1   B PHE A 1 202 ? -5.369  -3.865  39.218  0.50 22.12 ? 202 PHE A CD1   1 
ATOM   3095  C  CD2   A PHE A 1 202 ? -7.247  -3.730  36.606  0.50 18.89 ? 202 PHE A CD2   1 
ATOM   3096  C  CD2   B PHE A 1 202 ? -6.865  -3.846  37.361  0.50 17.92 ? 202 PHE A CD2   1 
ATOM   3097  C  CE1   A PHE A 1 202 ? -7.097  -2.668  39.152  0.50 20.49 ? 202 PHE A CE1   1 
ATOM   3098  C  CE1   B PHE A 1 202 ? -6.345  -3.289  40.018  0.50 20.79 ? 202 PHE A CE1   1 
ATOM   3099  C  CE2   A PHE A 1 202 ? -8.329  -3.050  37.133  0.50 19.90 ? 202 PHE A CE2   1 
ATOM   3100  C  CE2   B PHE A 1 202 ? -7.842  -3.265  38.151  0.50 30.25 ? 202 PHE A CE2   1 
ATOM   3101  C  CZ    A PHE A 1 202 ? -8.258  -2.523  38.411  0.50 23.64 ? 202 PHE A CZ    1 
ATOM   3102  C  CZ    B PHE A 1 202 ? -7.580  -2.986  39.481  0.50 22.57 ? 202 PHE A CZ    1 
ATOM   3103  N  N     A MET A 1 203 ? -1.437  -4.212  35.908  0.50 20.33 ? 203 MET A N     1 
ATOM   3104  N  N     B MET A 1 203 ? -1.232  -4.149  35.921  0.50 19.60 ? 203 MET A N     1 
ATOM   3105  C  CA    A MET A 1 203 ? -0.306  -4.929  35.346  0.50 26.39 ? 203 MET A CA    1 
ATOM   3106  C  CA    B MET A 1 203 ? -0.110  -4.834  35.300  0.50 26.72 ? 203 MET A CA    1 
ATOM   3107  C  C     A MET A 1 203 ? -0.085  -6.248  36.073  0.50 27.34 ? 203 MET A C     1 
ATOM   3108  C  C     B MET A 1 203 ? 0.174   -6.134  36.038  0.50 26.71 ? 203 MET A C     1 
ATOM   3109  O  O     A MET A 1 203 ? -0.311  -6.366  37.282  0.50 20.64 ? 203 MET A O     1 
ATOM   3110  O  O     B MET A 1 203 ? 0.233   -6.158  37.272  0.50 22.65 ? 203 MET A O     1 
ATOM   3111  C  CB    A MET A 1 203 ? 0.968   -4.085  35.417  0.50 27.87 ? 203 MET A CB    1 
ATOM   3112  C  CB    B MET A 1 203 ? 1.134   -3.947  35.296  0.50 27.82 ? 203 MET A CB    1 
ATOM   3113  C  CG    A MET A 1 203 ? 0.944   -2.843  34.549  0.50 32.88 ? 203 MET A CG    1 
ATOM   3114  C  CG    B MET A 1 203 ? 1.088   -2.824  34.279  0.50 32.85 ? 203 MET A CG    1 
ATOM   3115  S  SD    A MET A 1 203 ? 2.602   -2.332  34.059  0.50 36.68 ? 203 MET A SD    1 
ATOM   3116  S  SD    B MET A 1 203 ? 2.664   -1.959  34.158  0.50 38.71 ? 203 MET A SD    1 
ATOM   3117  C  CE    A MET A 1 203 ? 3.474   -2.430  35.621  0.50 27.48 ? 203 MET A CE    1 
ATOM   3118  C  CE    B MET A 1 203 ? 2.805   -1.259  35.801  0.50 24.46 ? 203 MET A CE    1 
ATOM   3119  N  N     A VAL A 1 204 ? 0.353   -7.248  35.313  0.50 21.90 ? 204 VAL A N     1 
ATOM   3120  N  N     B VAL A 1 204 ? 0.332   -7.212  35.279  0.50 21.86 ? 204 VAL A N     1 
ATOM   3121  C  CA    A VAL A 1 204 ? 0.705   -8.564  35.834  0.50 20.85 ? 204 VAL A CA    1 
ATOM   3122  C  CA    B VAL A 1 204 ? 0.690   -8.521  35.810  0.50 20.88 ? 204 VAL A CA    1 
ATOM   3123  C  C     A VAL A 1 204 ? 2.122   -8.862  35.358  0.50 22.83 ? 204 VAL A C     1 
ATOM   3124  C  C     B VAL A 1 204 ? 2.130   -8.788  35.392  0.50 22.83 ? 204 VAL A C     1 
ATOM   3125  O  O     A VAL A 1 204 ? 2.334   -9.144  34.174  0.50 21.63 ? 204 VAL A O     1 
ATOM   3126  O  O     B VAL A 1 204 ? 2.415   -8.960  34.201  0.50 21.87 ? 204 VAL A O     1 
ATOM   3127  C  CB    A VAL A 1 204 ? -0.268  -9.656  35.365  0.50 25.57 ? 204 VAL A CB    1 
ATOM   3128  C  CB    B VAL A 1 204 ? -0.251  -9.621  35.300  0.50 25.56 ? 204 VAL A CB    1 
ATOM   3129  C  CG1   A VAL A 1 204 ? 0.147   -11.009 35.911  0.50 28.59 ? 204 VAL A CG1   1 
ATOM   3130  C  CG1   B VAL A 1 204 ? -0.144  -10.865 36.166  0.50 29.57 ? 204 VAL A CG1   1 
ATOM   3131  C  CG2   A VAL A 1 204 ? -1.698  -9.315  35.773  0.50 28.52 ? 204 VAL A CG2   1 
ATOM   3132  C  CG2   B VAL A 1 204 ? -1.689  -9.114  35.241  0.50 29.55 ? 204 VAL A CG2   1 
ATOM   3133  N  N     A ASP A 1 205 ? 3.084   -8.800  36.276  0.50 20.07 ? 205 ASP A N     1 
ATOM   3134  N  N     B ASP A 1 205 ? 3.034   -8.818  36.368  0.50 20.11 ? 205 ASP A N     1 
ATOM   3135  C  CA    A ASP A 1 205 ? 4.497   -9.026  35.976  0.50 21.76 ? 205 ASP A CA    1 
ATOM   3136  C  CA    B ASP A 1 205 ? 4.463   -9.021  36.135  0.50 22.04 ? 205 ASP A CA    1 
ATOM   3137  C  C     A ASP A 1 205 ? 4.766   -10.526 35.968  0.50 24.39 ? 205 ASP A C     1 
ATOM   3138  C  C     B ASP A 1 205 ? 4.729   -10.512 35.975  0.50 24.39 ? 205 ASP A C     1 
ATOM   3139  O  O     A ASP A 1 205 ? 4.753   -11.168 37.024  0.50 21.82 ? 205 ASP A O     1 
ATOM   3140  O  O     B ASP A 1 205 ? 4.623   -11.273 36.942  0.50 22.22 ? 205 ASP A O     1 
ATOM   3141  C  CB    A ASP A 1 205 ? 5.355   -8.302  37.013  0.50 19.33 ? 205 ASP A CB    1 
ATOM   3142  C  CB    B ASP A 1 205 ? 5.255   -8.435  37.302  0.50 19.09 ? 205 ASP A CB    1 
ATOM   3143  C  CG    A ASP A 1 205 ? 6.837   -8.655  36.935  0.50 23.69 ? 205 ASP A CG    1 
ATOM   3144  C  CG    B ASP A 1 205 ? 6.752   -8.379  37.052  0.50 24.19 ? 205 ASP A CG    1 
ATOM   3145  O  OD1   A ASP A 1 205 ? 7.297   -9.231  35.926  0.50 22.80 ? 205 ASP A OD1   1 
ATOM   3146  O  OD1   B ASP A 1 205 ? 7.295   -9.240  36.326  0.50 21.91 ? 205 ASP A OD1   1 
ATOM   3147  O  OD2   A ASP A 1 205 ? 7.551   -8.340  37.913  0.50 22.38 ? 205 ASP A OD2   1 
ATOM   3148  O  OD2   B ASP A 1 205 ? 7.390   -7.467  37.621  0.50 21.81 ? 205 ASP A OD2   1 
ATOM   3149  N  N     A ASN A 1 206 ? 5.022   -11.083 34.777  0.50 21.63 ? 206 ASN A N     1 
ATOM   3150  N  N     B ASN A 1 206 ? 5.093   -10.931 34.759  0.50 21.56 ? 206 ASN A N     1 
ATOM   3151  C  CA    A ASN A 1 206 ? 5.260   -12.520 34.651  0.50 25.75 ? 206 ASN A CA    1 
ATOM   3152  C  CA    B ASN A 1 206 ? 5.296   -12.354 34.494  0.50 25.65 ? 206 ASN A CA    1 
ATOM   3153  C  C     A ASN A 1 206 ? 6.367   -13.004 35.581  0.50 24.88 ? 206 ASN A C     1 
ATOM   3154  C  C     B ASN A 1 206 ? 6.388   -12.953 35.378  0.50 24.95 ? 206 ASN A C     1 
ATOM   3155  O  O     A ASN A 1 206 ? 6.330   -14.148 36.049  0.50 21.84 ? 206 ASN A O     1 
ATOM   3156  O  O     B ASN A 1 206 ? 6.368   -14.158 35.651  0.50 23.80 ? 206 ASN A O     1 
ATOM   3157  C  CB    A ASN A 1 206 ? 5.603   -12.879 33.201  0.50 23.82 ? 206 ASN A CB    1 
ATOM   3158  C  CB    B ASN A 1 206 ? 5.622   -12.578 33.015  0.50 23.19 ? 206 ASN A CB    1 
ATOM   3159  C  CG    A ASN A 1 206 ? 4.382   -13.308 32.397  0.50 23.49 ? 206 ASN A CG    1 
ATOM   3160  C  CG    B ASN A 1 206 ? 4.441   -13.148 32.234  0.50 23.02 ? 206 ASN A CG    1 
ATOM   3161  O  OD1   A ASN A 1 206 ? 3.332   -13.623 32.959  0.50 24.98 ? 206 ASN A OD1   1 
ATOM   3162  O  OD1   B ASN A 1 206 ? 3.341   -13.297 32.771  0.50 24.70 ? 206 ASN A OD1   1 
ATOM   3163  N  ND2   A ASN A 1 206 ? 4.521   -13.330 31.077  0.50 23.61 ? 206 ASN A ND2   1 
ATOM   3164  N  ND2   B ASN A 1 206 ? 4.665   -13.461 30.963  0.50 23.89 ? 206 ASN A ND2   1 
ATOM   3165  N  N     A GLU A 1 207 ? 7.353   -12.151 35.870  0.50 23.59 ? 207 GLU A N     1 
ATOM   3166  N  N     B GLU A 1 207 ? 7.341   -12.140 35.843  0.50 23.61 ? 207 GLU A N     1 
ATOM   3167  C  CA    A GLU A 1 207 ? 8.419   -12.555 36.778  0.50 24.88 ? 207 GLU A CA    1 
ATOM   3168  C  CA    B GLU A 1 207 ? 8.352   -12.684 36.745  0.50 24.76 ? 207 GLU A CA    1 
ATOM   3169  C  C     A GLU A 1 207 ? 7.881   -12.798 38.183  0.50 21.02 ? 207 GLU A C     1 
ATOM   3170  C  C     B GLU A 1 207 ? 7.789   -12.888 38.145  0.50 20.99 ? 207 GLU A C     1 
ATOM   3171  O  O     A GLU A 1 207 ? 8.330   -13.715 38.877  0.50 23.18 ? 207 GLU A O     1 
ATOM   3172  O  O     B GLU A 1 207 ? 8.150   -13.854 38.824  0.50 23.53 ? 207 GLU A O     1 
ATOM   3173  C  CB    A GLU A 1 207 ? 9.525   -11.500 36.811  0.50 22.07 ? 207 GLU A CB    1 
ATOM   3174  C  CB    B GLU A 1 207 ? 9.584   -11.779 36.806  0.50 23.30 ? 207 GLU A CB    1 
ATOM   3175  C  CG    A GLU A 1 207 ? 10.708  -11.914 37.671  0.50 29.08 ? 207 GLU A CG    1 
ATOM   3176  C  CG    B GLU A 1 207 ? 10.693  -12.371 37.681  0.50 28.02 ? 207 GLU A CG    1 
ATOM   3177  C  CD    A GLU A 1 207 ? 11.834  -10.901 37.666  0.50 31.36 ? 207 GLU A CD    1 
ATOM   3178  C  CD    B GLU A 1 207 ? 11.938  -11.507 37.765  0.50 33.13 ? 207 GLU A CD    1 
ATOM   3179  O  OE1   A GLU A 1 207 ? 11.865  -10.041 36.759  0.50 25.23 ? 207 GLU A OE1   1 
ATOM   3180  O  OE1   B GLU A 1 207 ? 12.547  -11.222 36.710  0.50 27.52 ? 207 GLU A OE1   1 
ATOM   3181  O  OE2   A GLU A 1 207 ? 12.692  -10.974 38.572  0.50 37.22 ? 207 GLU A OE2   1 
ATOM   3182  O  OE2   B GLU A 1 207 ? 12.308  -11.119 38.895  0.50 31.98 ? 207 GLU A OE2   1 
ATOM   3183  N  N     A ALA A 1 208 ? 6.920   -11.983 38.618  0.50 27.17 ? 208 ALA A N     1 
ATOM   3184  N  N     B ALA A 1 208 ? 6.913   -11.988 38.591  0.50 27.17 ? 208 ALA A N     1 
ATOM   3185  C  CA    A ALA A 1 208 ? 6.343   -12.157 39.947  0.50 26.51 ? 208 ALA A CA    1 
ATOM   3186  C  CA    B ALA A 1 208 ? 6.288   -12.144 39.900  0.50 26.50 ? 208 ALA A CA    1 
ATOM   3187  C  C     A ALA A 1 208 ? 5.537   -13.447 40.030  0.50 24.46 ? 208 ALA A C     1 
ATOM   3188  C  C     B ALA A 1 208 ? 5.439   -13.408 39.948  0.50 24.46 ? 208 ALA A C     1 
ATOM   3189  O  O     A ALA A 1 208 ? 5.656   -14.205 40.999  0.50 26.39 ? 208 ALA A O     1 
ATOM   3190  O  O     B ALA A 1 208 ? 5.539   -14.203 40.890  0.50 26.53 ? 208 ALA A O     1 
ATOM   3191  C  CB    A ALA A 1 208 ? 5.471   -10.951 40.298  0.50 26.77 ? 208 ALA A CB    1 
ATOM   3192  C  CB    B ALA A 1 208 ? 5.446   -10.910 40.228  0.50 26.74 ? 208 ALA A CB    1 
ATOM   3193  N  N     A ILE A 1 209 ? 4.713   -13.714 39.014  0.50 19.93 ? 209 ILE A N     1 
ATOM   3194  N  N     B ILE A 1 209 ? 4.596   -13.609 38.931  0.50 20.00 ? 209 ILE A N     1 
ATOM   3195  C  CA    A ILE A 1 209 ? 3.865   -14.901 39.028  0.50 26.28 ? 209 ILE A CA    1 
ATOM   3196  C  CA    B ILE A 1 209 ? 3.783   -14.819 38.851  0.50 26.48 ? 209 ILE A CA    1 
ATOM   3197  C  C     A ILE A 1 209 ? 4.708   -16.163 38.896  0.50 25.99 ? 209 ILE A C     1 
ATOM   3198  C  C     B ILE A 1 209 ? 4.671   -16.051 38.766  0.50 26.09 ? 209 ILE A C     1 
ATOM   3199  O  O     A ILE A 1 209 ? 4.444   -17.176 39.554  0.50 23.68 ? 209 ILE A O     1 
ATOM   3200  O  O     B ILE A 1 209 ? 4.325   -17.118 39.286  0.50 23.34 ? 209 ILE A O     1 
ATOM   3201  C  CB    A ILE A 1 209 ? 2.806   -14.807 37.914  0.50 24.34 ? 209 ILE A CB    1 
ATOM   3202  C  CB    B ILE A 1 209 ? 2.825   -14.729 37.646  0.50 24.16 ? 209 ILE A CB    1 
ATOM   3203  C  CG1   A ILE A 1 209 ? 2.017   -13.501 38.029  0.50 25.55 ? 209 ILE A CG1   1 
ATOM   3204  C  CG1   B ILE A 1 209 ? 2.109   -13.376 37.624  0.50 27.13 ? 209 ILE A CG1   1 
ATOM   3205  C  CG2   A ILE A 1 209 ? 1.870   -16.008 37.964  0.50 31.57 ? 209 ILE A CG2   1 
ATOM   3206  C  CG2   B ILE A 1 209 ? 1.823   -15.875 37.661  0.50 31.73 ? 209 ILE A CG2   1 
ATOM   3207  C  CD1   A ILE A 1 209 ? 1.109   -13.427 39.240  0.50 29.94 ? 209 ILE A CD1   1 
ATOM   3208  C  CD1   B ILE A 1 209 ? 1.369   -13.032 38.899  0.50 26.37 ? 209 ILE A CD1   1 
ATOM   3209  N  N     A TYR A 1 210 ? 5.736   -16.122 38.042  0.50 23.47 ? 210 TYR A N     1 
ATOM   3210  N  N     B TYR A 1 210 ? 5.827   -15.922 38.110  0.50 23.48 ? 210 TYR A N     1 
ATOM   3211  C  CA    A TYR A 1 210 ? 6.623   -17.268 37.879  0.50 23.10 ? 210 TYR A CA    1 
ATOM   3212  C  CA    B TYR A 1 210 ? 6.797   -17.009 38.057  0.50 22.86 ? 210 TYR A CA    1 
ATOM   3213  C  C     A TYR A 1 210 ? 7.256   -17.668 39.209  0.50 26.78 ? 210 TYR A C     1 
ATOM   3214  C  C     B TYR A 1 210 ? 7.346   -17.316 39.447  0.50 25.84 ? 210 TYR A C     1 
ATOM   3215  O  O     A TYR A 1 210 ? 7.299   -18.856 39.552  0.50 23.81 ? 210 TYR A O     1 
ATOM   3216  O  O     B TYR A 1 210 ? 7.376   -18.476 39.876  0.50 24.30 ? 210 TYR A O     1 
ATOM   3217  C  CB    A TYR A 1 210 ? 7.694   -16.933 36.837  0.50 23.21 ? 210 TYR A CB    1 
ATOM   3218  C  CB    B TYR A 1 210 ? 7.918   -16.622 37.088  0.50 24.82 ? 210 TYR A CB    1 
ATOM   3219  C  CG    A TYR A 1 210 ? 8.555   -18.085 36.372  0.50 30.20 ? 210 TYR A CG    1 
ATOM   3220  C  CG    B TYR A 1 210 ? 8.846   -17.729 36.645  0.50 30.36 ? 210 TYR A CG    1 
ATOM   3221  C  CD1   A TYR A 1 210 ? 9.718   -18.432 37.054  0.50 28.71 ? 210 TYR A CD1   1 
ATOM   3222  C  CD1   B TYR A 1 210 ? 8.527   -18.539 35.560  0.50 32.00 ? 210 TYR A CD1   1 
ATOM   3223  C  CD2   A TYR A 1 210 ? 8.230   -18.802 35.225  0.50 29.29 ? 210 TYR A CD2   1 
ATOM   3224  C  CD2   B TYR A 1 210 ? 10.064  -17.936 37.282  0.50 27.33 ? 210 TYR A CD2   1 
ATOM   3225  C  CE1   A TYR A 1 210 ? 10.520  -19.474 36.618  0.50 33.71 ? 210 TYR A CE1   1 
ATOM   3226  C  CE1   B TYR A 1 210 ? 9.388   -19.538 35.136  0.50 30.71 ? 210 TYR A CE1   1 
ATOM   3227  C  CE2   A TYR A 1 210 ? 9.026   -19.846 34.781  0.50 31.57 ? 210 TYR A CE2   1 
ATOM   3228  C  CE2   B TYR A 1 210 ? 10.930  -18.929 36.862  0.50 30.26 ? 210 TYR A CE2   1 
ATOM   3229  C  CZ    A TYR A 1 210 ? 10.167  -20.180 35.483  0.50 35.75 ? 210 TYR A CZ    1 
ATOM   3230  C  CZ    B TYR A 1 210 ? 10.586  -19.730 35.795  0.50 35.56 ? 210 TYR A CZ    1 
ATOM   3231  O  OH    A TYR A 1 210 ? 10.962  -21.219 35.046  0.50 37.47 ? 210 TYR A OH    1 
ATOM   3232  O  OH    B TYR A 1 210 ? 11.447  -20.723 35.384  0.50 38.99 ? 210 TYR A OH    1 
ATOM   3233  N  N     A ASP A 1 211 ? 7.723   -16.687 39.983  0.50 22.91 ? 211 ASP A N     1 
ATOM   3234  N  N     B ASP A 1 211 ? 7.772   -16.279 40.172  0.50 23.58 ? 211 ASP A N     1 
ATOM   3235  C  CA    A ASP A 1 211 ? 8.403   -16.989 41.238  0.50 27.16 ? 211 ASP A CA    1 
ATOM   3236  C  CA    B ASP A 1 211 ? 8.339   -16.469 41.504  0.50 29.85 ? 211 ASP A CA    1 
ATOM   3237  C  C     A ASP A 1 211 ? 7.430   -17.516 42.290  0.50 29.27 ? 211 ASP A C     1 
ATOM   3238  C  C     B ASP A 1 211 ? 7.343   -17.136 42.449  0.50 29.36 ? 211 ASP A C     1 
ATOM   3239  O  O     A ASP A 1 211 ? 7.771   -18.421 43.060  0.50 27.00 ? 211 ASP A O     1 
ATOM   3240  O  O     B ASP A 1 211 ? 7.730   -17.954 43.292  0.50 26.32 ? 211 ASP A O     1 
ATOM   3241  C  CB    A ASP A 1 211 ? 9.132   -15.744 41.750  0.50 27.13 ? 211 ASP A CB    1 
ATOM   3242  C  CB    B ASP A 1 211 ? 8.795   -15.123 42.075  0.50 23.67 ? 211 ASP A CB    1 
ATOM   3243  C  CG    A ASP A 1 211 ? 10.310  -15.347 40.871  0.50 33.80 ? 211 ASP A CG    1 
ATOM   3244  C  CG    B ASP A 1 211 ? 10.163  -14.701 41.574  0.50 32.82 ? 211 ASP A CG    1 
ATOM   3245  O  OD1   A ASP A 1 211 ? 10.861  -16.225 40.171  0.50 26.45 ? 211 ASP A OD1   1 
ATOM   3246  O  OD1   B ASP A 1 211 ? 10.860  -15.529 40.943  0.50 32.00 ? 211 ASP A OD1   1 
ATOM   3247  O  OD2   A ASP A 1 211 ? 10.693  -14.155 40.887  0.50 34.95 ? 211 ASP A OD2   1 
ATOM   3248  O  OD2   B ASP A 1 211 ? 10.548  -13.535 41.813  0.50 33.21 ? 211 ASP A OD2   1 
ATOM   3249  N  N     A ILE A 1 212 ? 6.218   -16.958 42.349  0.50 25.06 ? 212 ILE A N     1 
ATOM   3250  N  N     B ILE A 1 212 ? 6.058   -16.796 42.326  0.50 24.56 ? 212 ILE A N     1 
ATOM   3251  C  CA    A ILE A 1 212 ? 5.222   -17.462 43.290  0.50 28.03 ? 212 ILE A CA    1 
ATOM   3252  C  CA    B ILE A 1 212 ? 5.052   -17.354 43.224  0.50 27.87 ? 212 ILE A CA    1 
ATOM   3253  C  C     A ILE A 1 212 ? 4.848   -18.898 42.944  0.50 25.06 ? 212 ILE A C     1 
ATOM   3254  C  C     B ILE A 1 212 ? 4.909   -18.856 43.004  0.50 25.11 ? 212 ILE A C     1 
ATOM   3255  O  O     A ILE A 1 212 ? 4.659   -19.738 43.832  0.50 29.27 ? 212 ILE A O     1 
ATOM   3256  O  O     B ILE A 1 212 ? 4.870   -19.637 43.961  0.50 29.32 ? 212 ILE A O     1 
ATOM   3257  C  CB    A ILE A 1 212 ? 3.993   -16.534 43.317  0.50 25.01 ? 212 ILE A CB    1 
ATOM   3258  C  CB    B ILE A 1 212 ? 3.711   -16.621 43.043  0.50 24.83 ? 212 ILE A CB    1 
ATOM   3259  C  CG1   A ILE A 1 212 ? 4.386   -15.150 43.836  0.50 25.43 ? 212 ILE A CG1   1 
ATOM   3260  C  CG1   B ILE A 1 212 ? 3.856   -15.154 43.449  0.50 28.90 ? 212 ILE A CG1   1 
ATOM   3261  C  CG2   A ILE A 1 212 ? 2.880   -17.127 44.180  0.50 30.30 ? 212 ILE A CG2   1 
ATOM   3262  C  CG2   B ILE A 1 212 ? 2.616   -17.296 43.864  0.50 29.66 ? 212 ILE A CG2   1 
ATOM   3263  C  CD1   A ILE A 1 212 ? 3.224   -14.167 43.918  0.50 25.58 ? 212 ILE A CD1   1 
ATOM   3264  C  CD1   B ILE A 1 212 ? 2.682   -14.287 43.051  0.50 24.49 ? 212 ILE A CD1   1 
ATOM   3265  N  N     A CYS A 1 213 ? 4.763   -19.210 41.649  0.50 25.94 ? 213 CYS A N     1 
ATOM   3266  N  N     B CYS A 1 213 ? 4.838   -19.284 41.741  0.50 25.91 ? 213 CYS A N     1 
ATOM   3267  C  CA    A CYS A 1 213 ? 4.458   -20.577 41.240  0.50 28.55 ? 213 CYS A CA    1 
ATOM   3268  C  CA    B CYS A 1 213 ? 4.701   -20.710 41.456  0.50 28.41 ? 213 CYS A CA    1 
ATOM   3269  C  C     A CYS A 1 213 ? 5.565   -21.540 41.651  0.50 29.09 ? 213 CYS A C     1 
ATOM   3270  C  C     B CYS A 1 213 ? 5.866   -21.507 42.031  0.50 30.28 ? 213 CYS A C     1 
ATOM   3271  O  O     A CYS A 1 213 ? 5.293   -22.692 42.015  0.50 29.84 ? 213 CYS A O     1 
ATOM   3272  O  O     B CYS A 1 213 ? 5.666   -22.582 42.610  0.50 26.92 ? 213 CYS A O     1 
ATOM   3273  C  CB    A CYS A 1 213 ? 4.224   -20.637 39.730  0.50 26.88 ? 213 CYS A CB    1 
ATOM   3274  C  CB    B CYS A 1 213 ? 4.584   -20.939 39.948  0.50 25.76 ? 213 CYS A CB    1 
ATOM   3275  S  SG    A CYS A 1 213 ? 2.623   -19.973 39.212  0.50 25.18 ? 213 CYS A SG    1 
ATOM   3276  S  SG    B CYS A 1 213 ? 3.006   -20.405 39.236  0.50 29.11 ? 213 CYS A SG    1 
ATOM   3277  N  N     A ARG A 1 214 ? 6.820   -21.088 41.605  0.50 28.25 ? 214 ARG A N     1 
ATOM   3278  N  N     B ARG A 1 214 ? 7.089   -20.987 41.894  0.50 28.34 ? 214 ARG A N     1 
ATOM   3279  C  CA    A ARG A 1 214 ? 7.926   -21.943 42.024  0.50 29.43 ? 214 ARG A CA    1 
ATOM   3280  C  CA    B ARG A 1 214 ? 8.262   -21.694 42.400  0.50 31.43 ? 214 ARG A CA    1 
ATOM   3281  C  C     A ARG A 1 214 ? 7.998   -22.062 43.543  0.50 31.47 ? 214 ARG A C     1 
ATOM   3282  C  C     B ARG A 1 214 ? 8.267   -21.751 43.923  0.50 32.06 ? 214 ARG A C     1 
ATOM   3283  O  O     A ARG A 1 214 ? 8.122   -23.168 44.079  0.50 33.83 ? 214 ARG A O     1 
ATOM   3284  O  O     B ARG A 1 214 ? 8.434   -22.824 44.513  0.50 33.56 ? 214 ARG A O     1 
ATOM   3285  C  CB    A ARG A 1 214 ? 9.245   -21.407 41.472  0.50 30.30 ? 214 ARG A CB    1 
ATOM   3286  C  CB    B ARG A 1 214 ? 9.537   -21.021 41.895  0.50 27.90 ? 214 ARG A CB    1 
ATOM   3287  C  CG    A ARG A 1 214 ? 9.415   -21.603 39.978  0.50 30.23 ? 214 ARG A CG    1 
ATOM   3288  C  CG    B ARG A 1 214 ? 9.822   -21.244 40.424  0.50 33.16 ? 214 ARG A CG    1 
ATOM   3289  C  CD    A ARG A 1 214 ? 10.849  -21.305 39.567  0.50 36.64 ? 214 ARG A CD    1 
ATOM   3290  C  CD    B ARG A 1 214 ? 10.904  -20.292 39.933  0.50 36.42 ? 214 ARG A CD    1 
ATOM   3291  N  NE    A ARG A 1 214 ? 11.788  -21.658 40.626  0.50 35.65 ? 214 ARG A NE    1 
ATOM   3292  N  NE    B ARG A 1 214 ? 11.984  -20.126 40.899  0.50 39.73 ? 214 ARG A NE    1 
ATOM   3293  C  CZ    A ARG A 1 214 ? 12.367  -22.844 40.756  0.50 39.31 ? 214 ARG A CZ    1 
ATOM   3294  C  CZ    B ARG A 1 214 ? 13.099  -20.844 40.914  0.50 44.56 ? 214 ARG A CZ    1 
ATOM   3295  N  NH1   A ARG A 1 214 ? 12.148  -23.818 39.889  0.50 41.19 ? 214 ARG A NH1   1 
ATOM   3296  N  NH1   B ARG A 1 214 ? 13.316  -21.802 40.027  0.50 40.50 ? 214 ARG A NH1   1 
ATOM   3297  N  NH2   A ARG A 1 214 ? 13.185  -23.057 41.783  0.50 40.19 ? 214 ARG A NH2   1 
ATOM   3298  N  NH2   B ARG A 1 214 ? 14.020  -20.594 41.840  0.50 46.51 ? 214 ARG A NH2   1 
ATOM   3299  N  N     A ARG A 1 215 ? 7.926   -20.935 44.254  0.50 29.03 ? 215 ARG A N     1 
ATOM   3300  N  N     B ARG A 1 215 ? 8.100   -20.600 44.577  0.50 29.11 ? 215 ARG A N     1 
ATOM   3301  C  CA    A ARG A 1 215 ? 8.041   -20.947 45.708  0.50 32.71 ? 215 ARG A CA    1 
ATOM   3302  C  CA    B ARG A 1 215 ? 8.274   -20.537 46.025  0.50 31.98 ? 215 ARG A CA    1 
ATOM   3303  C  C     A ARG A 1 215 ? 6.816   -21.571 46.363  0.50 33.02 ? 215 ARG A C     1 
ATOM   3304  C  C     B ARG A 1 215 ? 7.054   -21.043 46.786  0.50 33.97 ? 215 ARG A C     1 
ATOM   3305  O  O     A ARG A 1 215 ? 6.881   -22.690 46.885  0.50 29.38 ? 215 ARG A O     1 
ATOM   3306  O  O     B ARG A 1 215 ? 7.201   -21.558 47.901  0.50 36.40 ? 215 ARG A O     1 
ATOM   3307  C  CB    A ARG A 1 215 ? 8.238   -19.529 46.248  0.50 34.86 ? 215 ARG A CB    1 
ATOM   3308  C  CB    B ARG A 1 215 ? 8.598   -19.103 46.451  0.50 33.91 ? 215 ARG A CB    1 
ATOM   3309  C  CG    A ARG A 1 215 ? 9.618   -18.953 46.024  0.50 43.72 ? 215 ARG A CG    1 
ATOM   3310  C  CG    B ARG A 1 215 ? 9.936   -18.588 45.941  0.50 45.97 ? 215 ARG A CG    1 
ATOM   3311  C  CD    A ARG A 1 215 ? 9.769   -17.609 46.717  0.50 39.48 ? 215 ARG A CD    1 
ATOM   3312  C  CD    B ARG A 1 215 ? 10.112  -17.101 46.216  0.50 39.25 ? 215 ARG A CD    1 
ATOM   3313  N  NE    A ARG A 1 215 ? 8.926   -16.580 46.121  0.50 43.98 ? 215 ARG A NE    1 
ATOM   3314  N  NE    B ARG A 1 215 ? 9.113   -16.296 45.521  0.50 44.76 ? 215 ARG A NE    1 
ATOM   3315  C  CZ    A ARG A 1 215 ? 8.935   -15.304 46.485  0.50 37.84 ? 215 ARG A CZ    1 
ATOM   3316  C  CZ    B ARG A 1 215 ? 8.016   -15.807 46.084  0.50 39.55 ? 215 ARG A CZ    1 
ATOM   3317  N  NH1   A ARG A 1 215 ? 9.725   -14.868 47.452  0.50 41.60 ? 215 ARG A NH1   1 
ATOM   3318  N  NH1   B ARG A 1 215 ? 7.750   -16.001 47.365  0.50 35.97 ? 215 ARG A NH1   1 
ATOM   3319  N  NH2   A ARG A 1 215 ? 8.135   -14.444 45.860  0.50 35.47 ? 215 ARG A NH2   1 
ATOM   3320  N  NH2   B ARG A 1 215 ? 7.164   -15.106 45.340  0.50 32.55 ? 215 ARG A NH2   1 
ATOM   3321  N  N     A ASN A 1 216 ? 5.693   -20.848 46.334  0.50 32.76 ? 216 ASN A N     1 
ATOM   3322  N  N     B ASN A 1 216 ? 5.855   -20.913 46.219  0.50 32.55 ? 216 ASN A N     1 
ATOM   3323  C  CA    A ASN A 1 216 ? 4.528   -21.224 47.124  0.50 34.25 ? 216 ASN A CA    1 
ATOM   3324  C  CA    B ASN A 1 216 ? 4.626   -21.302 46.903  0.50 34.17 ? 216 ASN A CA    1 
ATOM   3325  C  C     A ASN A 1 216 ? 3.822   -22.462 46.589  0.50 34.59 ? 216 ASN A C     1 
ATOM   3326  C  C     B ASN A 1 216 ? 4.028   -22.595 46.374  0.50 34.58 ? 216 ASN A C     1 
ATOM   3327  O  O     A ASN A 1 216 ? 3.039   -23.074 47.324  0.50 30.58 ? 216 ASN A O     1 
ATOM   3328  O  O     B ASN A 1 216 ? 3.776   -23.523 47.150  0.50 34.81 ? 216 ASN A O     1 
ATOM   3329  C  CB    A ASN A 1 216 ? 3.542   -20.056 47.190  0.50 30.72 ? 216 ASN A CB    1 
ATOM   3330  C  CB    B ASN A 1 216 ? 3.581   -20.181 46.800  0.50 31.18 ? 216 ASN A CB    1 
ATOM   3331  C  CG    A ASN A 1 216 ? 4.189   -18.775 47.676  0.50 34.31 ? 216 ASN A CG    1 
ATOM   3332  C  CG    B ASN A 1 216 ? 3.831   -19.062 47.783  0.50 34.30 ? 216 ASN A CG    1 
ATOM   3333  O  OD1   A ASN A 1 216 ? 5.296   -18.430 47.264  0.50 39.58 ? 216 ASN A OD1   1 
ATOM   3334  O  OD1   B ASN A 1 216 ? 4.966   -18.817 48.188  0.50 40.34 ? 216 ASN A OD1   1 
ATOM   3335  N  ND2   A ASN A 1 216 ? 3.505   -18.067 48.569  0.50 44.08 ? 216 ASN A ND2   1 
ATOM   3336  N  ND2   B ASN A 1 216 ? 2.763   -18.381 48.186  0.50 40.17 ? 216 ASN A ND2   1 
ATOM   3337  N  N     A LEU A 1 217 ? 4.074   -22.849 45.338  0.50 29.61 ? 217 LEU A N     1 
ATOM   3338  N  N     B LEU A 1 217 ? 3.782   -22.681 45.068  0.50 27.46 ? 217 LEU A N     1 
ATOM   3339  C  CA    A LEU A 1 217 ? 3.435   -24.021 44.760  0.50 28.87 ? 217 LEU A CA    1 
ATOM   3340  C  CA    B LEU A 1 217 ? 3.091   -23.832 44.507  0.50 27.89 ? 217 LEU A CA    1 
ATOM   3341  C  C     A LEU A 1 217 ? 4.399   -25.162 44.473  0.50 30.73 ? 217 LEU A C     1 
ATOM   3342  C  C     B LEU A 1 217 ? 4.021   -24.996 44.203  0.50 29.79 ? 217 LEU A C     1 
ATOM   3343  O  O     A LEU A 1 217 ? 3.945   -26.248 44.097  0.50 38.21 ? 217 LEU A O     1 
ATOM   3344  O  O     B LEU A 1 217 ? 3.557   -26.009 43.668  0.50 36.73 ? 217 LEU A O     1 
ATOM   3345  C  CB    A LEU A 1 217 ? 2.693   -23.637 43.472  0.50 28.92 ? 217 LEU A CB    1 
ATOM   3346  C  CB    B LEU A 1 217 ? 2.325   -23.407 43.252  0.50 28.64 ? 217 LEU A CB    1 
ATOM   3347  C  CG    A LEU A 1 217 ? 1.653   -22.534 43.669  0.50 28.47 ? 217 LEU A CG    1 
ATOM   3348  C  CG    B LEU A 1 217 ? 1.256   -22.371 43.604  0.50 29.03 ? 217 LEU A CG    1 
ATOM   3349  C  CD1   A LEU A 1 217 ? 0.923   -22.237 42.372  0.50 31.78 ? 217 LEU A CD1   1 
ATOM   3350  C  CD1   B LEU A 1 217 ? 0.563   -21.827 42.369  0.50 30.94 ? 217 LEU A CD1   1 
ATOM   3351  C  CD2   A LEU A 1 217 ? 0.674   -22.928 44.769  0.50 30.23 ? 217 LEU A CD2   1 
ATOM   3352  C  CD2   B LEU A 1 217 ? 0.242   -22.985 44.572  0.50 29.72 ? 217 LEU A CD2   1 
ATOM   3353  N  N     A ASP A 1 218 ? 5.706   -24.949 44.647  0.50 31.73 ? 218 ASP A N     1 
ATOM   3354  N  N     B ASP A 1 218 ? 5.308   -24.875 44.537  0.50 30.49 ? 218 ASP A N     1 
ATOM   3355  C  CA    A ASP A 1 218 ? 6.726   -25.987 44.475  0.50 33.72 ? 218 ASP A CA    1 
ATOM   3356  C  CA    B ASP A 1 218 ? 6.284   -25.961 44.418  0.50 33.49 ? 218 ASP A CA    1 
ATOM   3357  C  C     A ASP A 1 218 ? 6.748   -26.546 43.056  0.50 37.09 ? 218 ASP A C     1 
ATOM   3358  C  C     B ASP A 1 218 ? 6.462   -26.418 42.974  0.50 37.02 ? 218 ASP A C     1 
ATOM   3359  O  O     A ASP A 1 218 ? 7.126   -27.699 42.840  0.50 39.58 ? 218 ASP A O     1 
ATOM   3360  O  O     B ASP A 1 218 ? 6.691   -27.600 42.707  0.50 40.26 ? 218 ASP A O     1 
ATOM   3361  C  CB    A ASP A 1 218 ? 6.554   -27.122 45.491  0.50 41.03 ? 218 ASP A CB    1 
ATOM   3362  C  CB    B ASP A 1 218 ? 5.911   -27.144 45.318  0.50 39.48 ? 218 ASP A CB    1 
ATOM   3363  C  CG    A ASP A 1 218 ? 7.187   -26.808 46.832  0.50 40.38 ? 218 ASP A CG    1 
ATOM   3364  C  CG    B ASP A 1 218 ? 6.089   -26.831 46.791  0.50 41.32 ? 218 ASP A CG    1 
ATOM   3365  O  OD1   A ASP A 1 218 ? 7.734   -25.696 46.988  0.50 45.38 ? 218 ASP A OD1   1 
ATOM   3366  O  OD1   B ASP A 1 218 ? 6.958   -25.993 47.116  0.50 41.16 ? 218 ASP A OD1   1 
ATOM   3367  O  OD2   A ASP A 1 218 ? 7.138   -27.675 47.734  0.50 50.67 ? 218 ASP A OD2   1 
ATOM   3368  O  OD2   B ASP A 1 218 ? 5.362   -27.417 47.622  0.50 43.03 ? 218 ASP A OD2   1 
ATOM   3369  N  N     A ILE A 1 219 ? 6.359   -25.737 42.076  0.50 34.62 ? 219 ILE A N     1 
ATOM   3370  N  N     B ILE A 1 219 ? 6.377   -25.483 42.036  0.50 34.49 ? 219 ILE A N     1 
ATOM   3371  C  CA    A ILE A 1 219 ? 6.377   -26.149 40.676  0.50 33.05 ? 219 ILE A CA    1 
ATOM   3372  C  CA    B ILE A 1 219 ? 6.560   -25.764 40.618  0.50 33.81 ? 219 ILE A CA    1 
ATOM   3373  C  C     A ILE A 1 219 ? 7.745   -25.808 40.096  0.50 36.52 ? 219 ILE A C     1 
ATOM   3374  C  C     B ILE A 1 219 ? 7.979   -25.353 40.253  0.50 36.20 ? 219 ILE A C     1 
ATOM   3375  O  O     A ILE A 1 219 ? 8.144   -24.638 40.070  0.50 37.36 ? 219 ILE A O     1 
ATOM   3376  O  O     B ILE A 1 219 ? 8.305   -24.161 40.230  0.50 38.14 ? 219 ILE A O     1 
ATOM   3377  C  CB    A ILE A 1 219 ? 5.246   -25.479 39.883  0.50 34.26 ? 219 ILE A CB    1 
ATOM   3378  C  CB    B ILE A 1 219 ? 5.526   -25.029 39.757  0.50 36.05 ? 219 ILE A CB    1 
ATOM   3379  C  CG1   A ILE A 1 219 ? 3.886   -25.965 40.392  0.50 33.31 ? 219 ILE A CG1   1 
ATOM   3380  C  CG1   B ILE A 1 219 ? 4.113   -25.286 40.286  0.50 34.11 ? 219 ILE A CG1   1 
ATOM   3381  C  CG2   A ILE A 1 219 ? 5.397   -25.762 38.398  0.50 37.57 ? 219 ILE A CG2   1 
ATOM   3382  C  CG2   B ILE A 1 219 ? 5.643   -25.461 38.304  0.50 37.15 ? 219 ILE A CG2   1 
ATOM   3383  C  CD1   A ILE A 1 219 ? 2.701   -25.373 39.660  0.50 31.69 ? 219 ILE A CD1   1 
ATOM   3384  C  CD1   B ILE A 1 219 ? 3.051   -24.424 39.633  0.50 30.76 ? 219 ILE A CD1   1 
ATOM   3385  N  N     A GLU A 1 220 ? 8.460   -26.833 39.628  0.50 34.14 ? 220 GLU A N     1 
ATOM   3386  N  N     B GLU A 1 220 ? 8.831   -26.339 39.967  0.50 33.86 ? 220 GLU A N     1 
ATOM   3387  C  CA    A GLU A 1 220 ? 9.862   -26.665 39.254  0.50 38.16 ? 220 GLU A CA    1 
ATOM   3388  C  CA    B GLU A 1 220 ? 10.228  -26.042 39.671  0.50 36.24 ? 220 GLU A CA    1 
ATOM   3389  C  C     A GLU A 1 220 ? 10.019  -25.705 38.080  0.50 35.13 ? 220 GLU A C     1 
ATOM   3390  C  C     B GLU A 1 220 ? 10.367  -25.232 38.388  0.50 35.54 ? 220 GLU A C     1 
ATOM   3391  O  O     A GLU A 1 220 ? 10.831  -24.774 38.131  0.50 35.90 ? 220 GLU A O     1 
ATOM   3392  O  O     B GLU A 1 220 ? 11.121  -24.253 38.343  0.50 33.48 ? 220 GLU A O     1 
ATOM   3393  C  CB    A GLU A 1 220 ? 10.480  -28.025 38.926  0.50 37.06 ? 220 GLU A CB    1 
ATOM   3394  C  CB    B GLU A 1 220 ? 11.032  -27.341 39.577  0.50 39.52 ? 220 GLU A CB    1 
ATOM   3395  N  N     A ARG A 1 221 ? 9.254   -25.918 37.011  0.50 35.91 ? 221 ARG A N     1 
ATOM   3396  N  N     B ARG A 1 221 ? 9.637   -25.615 37.340  0.50 34.44 ? 221 ARG A N     1 
ATOM   3397  C  CA    A ARG A 1 221 ? 9.333   -25.083 35.814  0.50 34.21 ? 221 ARG A CA    1 
ATOM   3398  C  CA    B ARG A 1 221 ? 9.745   -25.003 36.014  0.50 35.66 ? 221 ARG A CA    1 
ATOM   3399  C  C     A ARG A 1 221 ? 7.913   -24.803 35.346  0.50 35.08 ? 221 ARG A C     1 
ATOM   3400  C  C     B ARG A 1 221 ? 8.358   -24.577 35.546  0.50 32.81 ? 221 ARG A C     1 
ATOM   3401  O  O     A ARG A 1 221 ? 7.321   -25.589 34.593  0.50 31.88 ? 221 ARG A O     1 
ATOM   3402  O  O     B ARG A 1 221 ? 7.713   -25.277 34.752  0.50 34.58 ? 221 ARG A O     1 
ATOM   3403  C  CB    A ARG A 1 221 ? 10.162  -25.757 34.719  0.50 42.20 ? 221 ARG A CB    1 
ATOM   3404  C  CB    B ARG A 1 221 ? 10.399  -25.971 35.026  0.50 42.35 ? 221 ARG A CB    1 
ATOM   3405  C  CG    A ARG A 1 221 ? 10.649  -24.821 33.623  0.50 38.09 ? 221 ARG A CG    1 
ATOM   3406  C  CG    B ARG A 1 221 ? 9.854   -27.391 35.119  0.50 30.54 ? 221 ARG A CG    1 
ATOM   3407  C  CD    A ARG A 1 221 ? 11.626  -25.533 32.701  0.50 51.47 ? 221 ARG A CD    1 
ATOM   3408  C  CD    B ARG A 1 221 ? 10.552  -28.347 34.168  0.50 57.80 ? 221 ARG A CD    1 
ATOM   3409  N  NE    A ARG A 1 221 ? 11.852  -24.804 31.459  0.50 52.88 ? 221 ARG A NE    1 
ATOM   3410  N  NE    B ARG A 1 221 ? 9.751   -29.545 33.942  0.50 42.43 ? 221 ARG A NE    1 
ATOM   3411  C  CZ    A ARG A 1 221 ? 11.113  -24.943 30.367  0.50 55.92 ? 221 ARG A CZ    1 
ATOM   3412  C  CZ    B ARG A 1 221 ? 9.639   -30.546 34.804  0.50 56.77 ? 221 ARG A CZ    1 
ATOM   3413  N  NH1   A ARG A 1 221 ? 10.084  -25.775 30.329  0.50 56.55 ? 221 ARG A NH1   1 
ATOM   3414  N  NH1   B ARG A 1 221 ? 10.271  -30.532 35.966  0.50 58.29 ? 221 ARG A NH1   1 
ATOM   3415  N  NH2   A ARG A 1 221 ? 11.411  -24.228 29.286  0.50 56.93 ? 221 ARG A NH2   1 
ATOM   3416  N  NH2   B ARG A 1 221 ? 8.870   -31.587 34.492  0.50 45.61 ? 221 ARG A NH2   1 
ATOM   3417  N  N     A PRO A 1 222 ? 7.324   -23.692 35.792  0.50 32.82 ? 222 PRO A N     1 
ATOM   3418  N  N     B PRO A 1 222 ? 7.866   -23.431 36.017  0.50 32.80 ? 222 PRO A N     1 
ATOM   3419  C  CA    A PRO A 1 222 ? 5.918   -23.418 35.466  0.50 25.29 ? 222 PRO A CA    1 
ATOM   3420  C  CA    B PRO A 1 222 ? 6.501   -23.014 35.665  0.50 28.57 ? 222 PRO A CA    1 
ATOM   3421  C  C     A PRO A 1 222 ? 5.705   -23.216 33.972  0.50 26.30 ? 222 PRO A C     1 
ATOM   3422  C  C     B PRO A 1 222 ? 6.358   -22.749 34.172  0.50 30.41 ? 222 PRO A C     1 
ATOM   3423  O  O     A PRO A 1 222 ? 6.561   -22.679 33.265  0.50 31.75 ? 222 PRO A O     1 
ATOM   3424  O  O     B PRO A 1 222 ? 7.219   -22.126 33.548  0.50 33.70 ? 222 PRO A O     1 
ATOM   3425  C  CB    A PRO A 1 222 ? 5.615   -22.134 36.249  0.50 28.09 ? 222 PRO A CB    1 
ATOM   3426  C  CB    B PRO A 1 222 ? 6.300   -21.729 36.478  0.50 29.43 ? 222 PRO A CB    1 
ATOM   3427  C  CG    A PRO A 1 222 ? 6.679   -22.046 37.295  0.50 33.47 ? 222 PRO A CG    1 
ATOM   3428  C  CG    B PRO A 1 222 ? 7.356   -21.758 37.536  0.50 32.91 ? 222 PRO A CG    1 
ATOM   3429  C  CD    A PRO A 1 222 ? 7.894   -22.679 36.695  0.50 32.40 ? 222 PRO A CD    1 
ATOM   3430  C  CD    B PRO A 1 222 ? 8.516   -22.483 36.937  0.50 32.65 ? 222 PRO A CD    1 
ATOM   3431  N  N     A THR A 1 223 ? 4.550   -23.668 33.496  0.50 27.51 ? 223 THR A N     1 
ATOM   3432  N  N     B THR A 1 223 ? 5.254   -23.228 33.605  0.50 25.66 ? 223 THR A N     1 
ATOM   3433  C  CA    A THR A 1 223 ? 4.087   -23.391 32.144  0.50 27.08 ? 223 THR A CA    1 
ATOM   3434  C  CA    B THR A 1 223 ? 4.891   -22.982 32.216  0.50 24.79 ? 223 THR A CA    1 
ATOM   3435  C  C     A THR A 1 223 ? 3.071   -22.254 32.165  0.50 28.21 ? 223 THR A C     1 
ATOM   3436  C  C     B THR A 1 223 ? 3.736   -21.987 32.163  0.50 30.26 ? 223 THR A C     1 
ATOM   3437  O  O     A THR A 1 223 ? 2.622   -21.805 33.222  0.50 25.36 ? 223 THR A O     1 
ATOM   3438  O  O     B THR A 1 223 ? 3.263   -21.497 33.192  0.50 26.72 ? 223 THR A O     1 
ATOM   3439  C  CB    A THR A 1 223 ? 3.461   -24.638 31.512  0.50 28.71 ? 223 THR A CB    1 
ATOM   3440  C  CB    B THR A 1 223 ? 4.513   -24.287 31.509  0.50 31.27 ? 223 THR A CB    1 
ATOM   3441  O  OG1   A THR A 1 223 ? 2.436   -25.146 32.376  0.50 30.17 ? 223 THR A OG1   1 
ATOM   3442  O  OG1   B THR A 1 223 ? 3.153   -24.619 31.814  0.50 28.70 ? 223 THR A OG1   1 
ATOM   3443  C  CG2   A THR A 1 223 ? 4.515   -25.711 31.280  0.50 29.80 ? 223 THR A CG2   1 
ATOM   3444  C  CG2   B THR A 1 223 ? 5.418   -25.423 31.966  0.50 32.43 ? 223 THR A CG2   1 
ATOM   3445  N  N     A TYR A 1 224 ? 2.702   -21.795 30.965  0.50 30.01 ? 224 TYR A N     1 
ATOM   3446  N  N     B TYR A 1 224 ? 3.277   -21.693 30.941  0.50 26.67 ? 224 TYR A N     1 
ATOM   3447  C  CA    A TYR A 1 224 ? 1.706   -20.734 30.861  0.50 29.92 ? 224 TYR A CA    1 
ATOM   3448  C  CA    B TYR A 1 224 ? 2.123   -20.815 30.775  0.50 29.73 ? 224 TYR A CA    1 
ATOM   3449  C  C     A TYR A 1 224 ? 0.360   -21.155 31.436  0.50 28.10 ? 224 TYR A C     1 
ATOM   3450  C  C     B TYR A 1 224 ? 0.914   -21.331 31.546  0.50 27.90 ? 224 TYR A C     1 
ATOM   3451  O  O     A TYR A 1 224 ? -0.408  -20.302 31.892  0.50 23.29 ? 224 TYR A O     1 
ATOM   3452  O  O     B TYR A 1 224 ? 0.171   -20.546 32.147  0.50 23.68 ? 224 TYR A O     1 
ATOM   3453  C  CB    A TYR A 1 224 ? 1.546   -20.300 29.407  0.50 27.60 ? 224 TYR A CB    1 
ATOM   3454  C  CB    B TYR A 1 224 ? 1.771   -20.676 29.293  0.50 29.76 ? 224 TYR A CB    1 
ATOM   3455  C  CG    A TYR A 1 224 ? 2.680   -19.429 28.921  0.50 25.28 ? 224 TYR A CG    1 
ATOM   3456  C  CG    B TYR A 1 224 ? 2.670   -19.750 28.503  0.50 27.97 ? 224 TYR A CG    1 
ATOM   3457  C  CD1   A TYR A 1 224 ? 3.249   -18.473 29.751  0.50 22.34 ? 224 TYR A CD1   1 
ATOM   3458  C  CD1   B TYR A 1 224 ? 3.000   -18.488 28.980  0.50 23.93 ? 224 TYR A CD1   1 
ATOM   3459  C  CD2   A TYR A 1 224 ? 3.197   -19.575 27.642  0.50 32.01 ? 224 TYR A CD2   1 
ATOM   3460  C  CD2   B TYR A 1 224 ? 3.189   -20.144 27.273  0.50 32.26 ? 224 TYR A CD2   1 
ATOM   3461  C  CE1   A TYR A 1 224 ? 4.287   -17.674 29.315  0.50 24.30 ? 224 TYR A CE1   1 
ATOM   3462  C  CE1   B TYR A 1 224 ? 3.822   -17.642 28.251  0.50 24.56 ? 224 TYR A CE1   1 
ATOM   3463  C  CE2   A TYR A 1 224 ? 4.236   -18.784 27.199  0.50 28.19 ? 224 TYR A CE2   1 
ATOM   3464  C  CE2   B TYR A 1 224 ? 4.009   -19.307 26.538  0.50 30.77 ? 224 TYR A CE2   1 
ATOM   3465  C  CZ    A TYR A 1 224 ? 4.777   -17.838 28.041  0.50 24.76 ? 224 TYR A CZ    1 
ATOM   3466  C  CZ    B TYR A 1 224 ? 4.320   -18.059 27.028  0.50 26.79 ? 224 TYR A CZ    1 
ATOM   3467  O  OH    A TYR A 1 224 ? 5.814   -17.052 27.602  0.50 26.02 ? 224 TYR A OH    1 
ATOM   3468  O  OH    B TYR A 1 224 ? 5.139   -17.231 26.289  0.50 23.63 ? 224 TYR A OH    1 
ATOM   3469  N  N     A THR A 1 225 ? 0.043   -22.450 31.408  0.50 28.37 ? 225 THR A N     1 
ATOM   3470  N  N     B THR A 1 225 ? 0.699   -22.648 31.538  0.50 25.97 ? 225 THR A N     1 
ATOM   3471  C  CA    A THR A 1 225 ? -1.176  -22.904 32.070  0.50 23.55 ? 225 THR A CA    1 
ATOM   3472  C  CA    B THR A 1 225 ? -0.475  -23.218 32.195  0.50 26.81 ? 225 THR A CA    1 
ATOM   3473  C  C     A THR A 1 225 ? -1.082  -22.698 33.577  0.50 27.90 ? 225 THR A C     1 
ATOM   3474  C  C     B THR A 1 225 ? -0.498  -22.877 33.682  0.50 29.16 ? 225 THR A C     1 
ATOM   3475  O  O     A THR A 1 225 ? -2.070  -22.335 34.223  0.50 25.88 ? 225 THR A O     1 
ATOM   3476  O  O     B THR A 1 225 ? -1.535  -22.470 34.220  0.50 27.12 ? 225 THR A O     1 
ATOM   3477  C  CB    A THR A 1 225 ? -1.449  -24.369 31.726  0.50 27.42 ? 225 THR A CB    1 
ATOM   3478  C  CB    B THR A 1 225 ? -0.508  -24.734 31.986  0.50 26.22 ? 225 THR A CB    1 
ATOM   3479  O  OG1   A THR A 1 225 ? -1.845  -24.468 30.352  0.50 30.34 ? 225 THR A OG1   1 
ATOM   3480  O  OG1   B THR A 1 225 ? -0.648  -25.023 30.589  0.50 30.56 ? 225 THR A OG1   1 
ATOM   3481  C  CG2   A THR A 1 225 ? -2.558  -24.931 32.597  0.50 29.05 ? 225 THR A CG2   1 
ATOM   3482  C  CG2   B THR A 1 225 ? -1.674  -25.355 32.744  0.50 31.09 ? 225 THR A CG2   1 
ATOM   3483  N  N     A ASN A 1 226 ? 0.110   -22.892 34.146  0.50 29.13 ? 226 ASN A N     1 
ATOM   3484  N  N     B ASN A 1 226 ? 0.643   -23.024 34.360  0.50 28.06 ? 226 ASN A N     1 
ATOM   3485  C  CA    A ASN A 1 226 ? 0.301   -22.664 35.575  0.50 26.85 ? 226 ASN A CA    1 
ATOM   3486  C  CA    B ASN A 1 226 ? 0.697   -22.736 35.790  0.50 27.23 ? 226 ASN A CA    1 
ATOM   3487  C  C     A ASN A 1 226 ? 0.182   -21.183 35.916  0.50 26.45 ? 226 ASN A C     1 
ATOM   3488  C  C     B ASN A 1 226 ? 0.486   -21.250 36.064  0.50 25.80 ? 226 ASN A C     1 
ATOM   3489  O  O     A ASN A 1 226 ? -0.491  -20.810 36.886  0.50 23.12 ? 226 ASN A O     1 
ATOM   3490  O  O     B ASN A 1 226 ? -0.269  -20.877 36.972  0.50 23.86 ? 226 ASN A O     1 
ATOM   3491  C  CB    A ASN A 1 226 ? 1.660   -23.213 36.014  0.50 22.35 ? 226 ASN A CB    1 
ATOM   3492  C  CB    B ASN A 1 226 ? 2.030   -23.204 36.371  0.50 22.25 ? 226 ASN A CB    1 
ATOM   3493  C  CG    A ASN A 1 226 ? 1.821   -24.691 35.710  0.50 29.27 ? 226 ASN A CG    1 
ATOM   3494  C  CG    B ASN A 1 226 ? 2.284   -24.679 36.138  0.50 27.54 ? 226 ASN A CG    1 
ATOM   3495  O  OD1   A ASN A 1 226 ? 2.599   -25.077 34.836  0.50 31.24 ? 226 ASN A OD1   1 
ATOM   3496  O  OD1   B ASN A 1 226 ? 3.308   -25.058 35.571  0.50 28.92 ? 226 ASN A OD1   1 
ATOM   3497  N  ND2   A ASN A 1 226 ? 1.092   -25.527 36.437  0.50 30.00 ? 226 ASN A ND2   1 
ATOM   3498  N  ND2   B ASN A 1 226 ? 1.352   -25.520 36.572  0.50 30.03 ? 226 ASN A ND2   1 
ATOM   3499  N  N     A LEU A 1 227 ? 0.831   -20.322 35.128  0.50 23.84 ? 227 LEU A N     1 
ATOM   3500  N  N     B LEU A 1 227 ? 1.154   -20.386 35.295  0.50 22.92 ? 227 LEU A N     1 
ATOM   3501  C  CA    A LEU A 1 227 ? 0.752   -18.884 35.372  0.50 23.16 ? 227 LEU A CA    1 
ATOM   3502  C  CA    B LEU A 1 227 ? 0.978   -18.948 35.476  0.50 22.58 ? 227 LEU A CA    1 
ATOM   3503  C  C     A LEU A 1 227 ? -0.682  -18.380 35.246  0.50 24.37 ? 227 LEU A C     1 
ATOM   3504  C  C     B LEU A 1 227 ? -0.466  -18.533 35.227  0.50 24.87 ? 227 LEU A C     1 
ATOM   3505  O  O     A LEU A 1 227 ? -1.159  -17.611 36.088  0.50 24.34 ? 227 LEU A O     1 
ATOM   3506  O  O     B LEU A 1 227 ? -1.028  -17.727 35.977  0.50 24.23 ? 227 LEU A O     1 
ATOM   3507  C  CB    A LEU A 1 227 ? 1.660   -18.134 34.394  0.50 24.04 ? 227 LEU A CB    1 
ATOM   3508  C  CB    B LEU A 1 227 ? 1.911   -18.180 34.537  0.50 24.77 ? 227 LEU A CB    1 
ATOM   3509  C  CG    A LEU A 1 227 ? 3.121   -18.573 34.277  0.50 23.53 ? 227 LEU A CG    1 
ATOM   3510  C  CG    B LEU A 1 227 ? 3.390   -18.568 34.506  0.50 23.36 ? 227 LEU A CG    1 
ATOM   3511  C  CD1   A LEU A 1 227 ? 3.848   -17.727 33.230  0.50 28.57 ? 227 LEU A CD1   1 
ATOM   3512  C  CD1   B LEU A 1 227 ? 4.135   -17.742 33.456  0.50 29.08 ? 227 LEU A CD1   1 
ATOM   3513  C  CD2   A LEU A 1 227 ? 3.827   -18.486 35.614  0.50 26.92 ? 227 LEU A CD2   1 
ATOM   3514  C  CD2   B LEU A 1 227 ? 4.030   -18.402 35.869  0.50 27.56 ? 227 LEU A CD2   1 
ATOM   3515  N  N     A ASN A 1 228 ? -1.382  -18.802 34.189  0.50 23.86 ? 228 ASN A N     1 
ATOM   3516  N  N     B ASN A 1 228 ? -1.081  -19.075 34.171  0.50 25.68 ? 228 ASN A N     1 
ATOM   3517  C  CA    A ASN A 1 228 ? -2.696  -18.249 33.879  0.50 23.07 ? 228 ASN A CA    1 
ATOM   3518  C  CA    B ASN A 1 228 ? -2.413  -18.636 33.772  0.50 24.10 ? 228 ASN A CA    1 
ATOM   3519  C  C     A ASN A 1 228 ? -3.773  -18.716 34.848  0.50 24.86 ? 228 ASN A C     1 
ATOM   3520  C  C     B ASN A 1 228 ? -3.457  -19.031 34.807  0.50 25.46 ? 228 ASN A C     1 
ATOM   3521  O  O     A ASN A 1 228 ? -4.800  -18.044 34.974  0.50 26.08 ? 228 ASN A O     1 
ATOM   3522  O  O     B ASN A 1 228 ? -4.334  -18.232 35.150  0.50 22.38 ? 228 ASN A O     1 
ATOM   3523  C  CB    A ASN A 1 228 ? -3.097  -18.607 32.447  0.50 25.94 ? 228 ASN A CB    1 
ATOM   3524  C  CB    B ASN A 1 228 ? -2.766  -19.210 32.398  0.50 23.14 ? 228 ASN A CB    1 
ATOM   3525  C  CG    A ASN A 1 228 ? -2.152  -18.014 31.416  0.50 21.61 ? 228 ASN A CG    1 
ATOM   3526  C  CG    B ASN A 1 228 ? -1.999  -18.533 31.279  0.50 23.77 ? 228 ASN A CG    1 
ATOM   3527  O  OD1   A ASN A 1 228 ? -1.370  -17.114 31.726  0.50 20.91 ? 228 ASN A OD1   1 
ATOM   3528  O  OD1   B ASN A 1 228 ? -1.437  -17.456 31.470  0.50 21.81 ? 228 ASN A OD1   1 
ATOM   3529  N  ND2   A ASN A 1 228 ? -2.212  -18.522 30.188  0.50 23.90 ? 228 ASN A ND2   1 
ATOM   3530  N  ND2   B ASN A 1 228 ? -1.973  -19.159 30.105  0.50 23.13 ? 228 ASN A ND2   1 
ATOM   3531  N  N     A ARG A 1 229 ? -3.580  -19.854 35.516  0.50 25.59 ? 229 ARG A N     1 
ATOM   3532  N  N     B ARG A 1 229 ? -3.384  -20.265 35.306  0.50 21.44 ? 229 ARG A N     1 
ATOM   3533  C  CA    A ARG A 1 229 ? -4.525  -20.244 36.560  0.50 24.36 ? 229 ARG A CA    1 
ATOM   3534  C  CA    B ARG A 1 229 ? -4.306  -20.683 36.358  0.50 28.07 ? 229 ARG A CA    1 
ATOM   3535  C  C     A ARG A 1 229 ? -4.392  -19.340 37.780  0.50 29.10 ? 229 ARG A C     1 
ATOM   3536  C  C     B ARG A 1 229 ? -4.219  -19.755 37.563  0.50 28.02 ? 229 ARG A C     1 
ATOM   3537  O  O     A ARG A 1 229 ? -5.401  -18.915 38.357  0.50 27.80 ? 229 ARG A O     1 
ATOM   3538  O  O     B ARG A 1 229 ? -5.245  -19.379 38.143  0.50 31.35 ? 229 ARG A O     1 
ATOM   3539  C  CB    A ARG A 1 229 ? -4.325  -21.711 36.945  0.50 23.96 ? 229 ARG A CB    1 
ATOM   3540  C  CB    B ARG A 1 229 ? -4.017  -22.131 36.758  0.50 25.63 ? 229 ARG A CB    1 
ATOM   3541  C  CG    A ARG A 1 229 ? -4.761  -22.700 35.870  0.50 26.80 ? 229 ARG A CG    1 
ATOM   3542  C  CG    B ARG A 1 229 ? -5.211  -23.055 36.621  0.50 31.74 ? 229 ARG A CG    1 
ATOM   3543  C  CD    A ARG A 1 229 ? -4.817  -24.127 36.407  0.50 31.90 ? 229 ARG A CD    1 
ATOM   3544  C  CD    B ARG A 1 229 ? -4.811  -24.449 36.149  0.50 31.73 ? 229 ARG A CD    1 
ATOM   3545  N  NE    A ARG A 1 229 ? -3.496  -24.685 36.670  0.50 30.30 ? 229 ARG A NE    1 
ATOM   3546  N  NE    B ARG A 1 229 ? -4.793  -24.555 34.694  0.50 39.73 ? 229 ARG A NE    1 
ATOM   3547  C  CZ    A ARG A 1 229 ? -3.005  -25.770 36.084  0.50 28.00 ? 229 ARG A CZ    1 
ATOM   3548  C  CZ    B ARG A 1 229 ? -5.873  -24.726 33.942  0.50 35.81 ? 229 ARG A CZ    1 
ATOM   3549  N  NH1   A ARG A 1 229 ? -3.710  -26.461 35.202  0.50 29.51 ? 229 ARG A NH1   1 
ATOM   3550  N  NH1   B ARG A 1 229 ? -7.083  -24.799 34.475  0.50 39.61 ? 229 ARG A NH1   1 
ATOM   3551  N  NH2   A ARG A 1 229 ? -1.783  -26.182 36.403  0.50 27.73 ? 229 ARG A NH2   1 
ATOM   3552  N  NH2   B ARG A 1 229 ? -5.738  -24.820 32.622  0.50 38.18 ? 229 ARG A NH2   1 
ATOM   3553  N  N     A LEU A 1 230 ? -3.157  -19.030 38.185  0.50 24.60 ? 230 LEU A N     1 
ATOM   3554  N  N     B LEU A 1 230 ? -3.004  -19.344 37.934  0.50 20.52 ? 230 LEU A N     1 
ATOM   3555  C  CA    A LEU A 1 230 ? -2.962  -18.099 39.294  0.50 27.21 ? 230 LEU A CA    1 
ATOM   3556  C  CA    B LEU A 1 230 ? -2.851  -18.432 39.065  0.50 28.07 ? 230 LEU A CA    1 
ATOM   3557  C  C     A LEU A 1 230 ? -3.418  -16.692 38.921  0.50 28.23 ? 230 LEU A C     1 
ATOM   3558  C  C     B LEU A 1 230 ? -3.371  -17.036 38.731  0.50 27.84 ? 230 LEU A C     1 
ATOM   3559  O  O     A LEU A 1 230 ? -4.033  -15.995 39.739  0.50 24.44 ? 230 LEU A O     1 
ATOM   3560  O  O     B LEU A 1 230 ? -4.078  -16.418 39.537  0.50 26.61 ? 230 LEU A O     1 
ATOM   3561  C  CB    A LEU A 1 230 ? -1.495  -18.098 39.725  0.50 26.80 ? 230 LEU A CB    1 
ATOM   3562  C  CB    B LEU A 1 230 ? -1.387  -18.374 39.498  0.50 27.24 ? 230 LEU A CB    1 
ATOM   3563  C  CG    A LEU A 1 230 ? -1.127  -17.194 40.904  0.50 25.99 ? 230 LEU A CG    1 
ATOM   3564  C  CG    B LEU A 1 230 ? -1.082  -17.478 40.699  0.50 25.33 ? 230 LEU A CG    1 
ATOM   3565  C  CD1   A LEU A 1 230 ? -1.960  -17.544 42.135  0.50 28.82 ? 230 LEU A CD1   1 
ATOM   3566  C  CD1   B LEU A 1 230 ? -1.834  -17.960 41.939  0.50 29.58 ? 230 LEU A CD1   1 
ATOM   3567  C  CD2   A LEU A 1 230 ? 0.353   -17.295 41.218  0.50 33.42 ? 230 LEU A CD2   1 
ATOM   3568  C  CD2   B LEU A 1 230 ? 0.408   -17.429 40.964  0.50 33.53 ? 230 LEU A CD2   1 
ATOM   3569  N  N     A ILE A 1 231 ? -3.130  -16.259 37.690  0.50 25.87 ? 231 ILE A N     1 
ATOM   3570  N  N     B ILE A 1 231 ? -3.027  -16.518 37.547  0.50 26.60 ? 231 ILE A N     1 
ATOM   3571  C  CA    A ILE A 1 231 ? -3.575  -14.942 37.243  0.50 25.06 ? 231 ILE A CA    1 
ATOM   3572  C  CA    B ILE A 1 231 ? -3.447  -15.168 37.172  0.50 24.71 ? 231 ILE A CA    1 
ATOM   3573  C  C     A ILE A 1 231 ? -5.095  -14.849 37.282  0.50 24.06 ? 231 ILE A C     1 
ATOM   3574  C  C     B ILE A 1 231 ? -4.966  -15.067 37.136  0.50 24.93 ? 231 ILE A C     1 
ATOM   3575  O  O     A ILE A 1 231 ? -5.656  -13.852 37.749  0.50 25.61 ? 231 ILE A O     1 
ATOM   3576  O  O     B ILE A 1 231 ? -5.547  -14.065 37.569  0.50 24.12 ? 231 ILE A O     1 
ATOM   3577  C  CB    A ILE A 1 231 ? -3.031  -14.637 35.834  0.50 23.85 ? 231 ILE A CB    1 
ATOM   3578  C  CB    B ILE A 1 231 ? -2.822  -14.763 35.823  0.50 24.16 ? 231 ILE A CB    1 
ATOM   3579  C  CG1   A ILE A 1 231 ? -1.513  -14.455 35.875  0.50 24.64 ? 231 ILE A CG1   1 
ATOM   3580  C  CG1   B ILE A 1 231 ? -1.314  -14.563 35.974  0.50 25.30 ? 231 ILE A CG1   1 
ATOM   3581  C  CG2   A ILE A 1 231 ? -3.698  -13.391 35.261  0.50 22.16 ? 231 ILE A CG2   1 
ATOM   3582  C  CG2   B ILE A 1 231 ? -3.474  -13.493 35.288  0.50 22.86 ? 231 ILE A CG2   1 
ATOM   3583  C  CD1   A ILE A 1 231 ? -0.858  -14.452 34.506  0.50 27.53 ? 231 ILE A CD1   1 
ATOM   3584  C  CD1   B ILE A 1 231 ? -0.564  -14.494 34.660  0.50 26.99 ? 231 ILE A CD1   1 
ATOM   3585  N  N     A SER A 1 232 ? -5.784  -15.889 36.802  0.50 25.83 ? 232 SER A N     1 
ATOM   3586  N  N     B SER A 1 232 ? -5.636  -16.100 36.619  0.50 26.42 ? 232 SER A N     1 
ATOM   3587  C  CA    A SER A 1 232 ? -7.241  -15.836 36.720  0.50 24.37 ? 232 SER A CA    1 
ATOM   3588  C  CA    B SER A 1 232 ? -7.091  -16.075 36.556  0.50 24.39 ? 232 SER A CA    1 
ATOM   3589  C  C     A SER A 1 232 ? -7.872  -15.750 38.105  0.50 25.44 ? 232 SER A C     1 
ATOM   3590  C  C     B SER A 1 232 ? -7.729  -16.087 37.939  0.50 25.60 ? 232 SER A C     1 
ATOM   3591  O  O     A SER A 1 232 ? -8.860  -15.033 38.301  0.50 20.20 ? 232 SER A O     1 
ATOM   3592  O  O     B SER A 1 232 ? -8.869  -15.635 38.085  0.50 21.33 ? 232 SER A O     1 
ATOM   3593  C  CB    A SER A 1 232 ? -7.770  -17.053 35.962  0.50 26.92 ? 232 SER A CB    1 
ATOM   3594  C  CB    B SER A 1 232 ? -7.603  -17.252 35.726  0.50 26.25 ? 232 SER A CB    1 
ATOM   3595  O  OG    A SER A 1 232 ? -7.624  -18.233 36.730  0.50 32.93 ? 232 SER A OG    1 
ATOM   3596  O  OG    B SER A 1 232 ? -6.866  -18.427 36.006  0.50 29.12 ? 232 SER A OG    1 
ATOM   3597  N  N     A GLN A 1 233 ? -7.316  -16.469 39.082  0.50 24.39 ? 233 GLN A N     1 
ATOM   3598  N  N     B GLN A 1 233 ? -7.018  -16.581 38.956  0.50 23.53 ? 233 GLN A N     1 
ATOM   3599  C  CA    A GLN A 1 233 ? -7.820  -16.349 40.446  0.50 28.73 ? 233 GLN A CA    1 
ATOM   3600  C  CA    B GLN A 1 233 ? -7.541  -16.522 40.316  0.50 30.13 ? 233 GLN A CA    1 
ATOM   3601  C  C     A GLN A 1 233 ? -7.643  -14.930 40.964  0.50 25.92 ? 233 GLN A C     1 
ATOM   3602  C  C     B GLN A 1 233 ? -7.519  -15.093 40.846  0.50 25.60 ? 233 GLN A C     1 
ATOM   3603  O  O     A GLN A 1 233 ? -8.501  -14.412 41.692  0.50 25.09 ? 233 GLN A O     1 
ATOM   3604  O  O     B GLN A 1 233 ? -8.426  -14.683 41.583  0.50 25.45 ? 233 GLN A O     1 
ATOM   3605  C  CB    A GLN A 1 233 ? -7.113  -17.347 41.363  0.50 28.27 ? 233 GLN A CB    1 
ATOM   3606  C  CB    B GLN A 1 233 ? -6.738  -17.457 41.223  0.50 29.27 ? 233 GLN A CB    1 
ATOM   3607  C  CG    A GLN A 1 233 ? -7.527  -17.235 42.816  0.50 32.76 ? 233 GLN A CG    1 
ATOM   3608  C  CG    B GLN A 1 233 ? -7.510  -18.001 42.411  0.50 28.13 ? 233 GLN A CG    1 
ATOM   3609  C  CD    A GLN A 1 233 ? -9.026  -17.422 43.009  0.50 29.37 ? 233 GLN A CD    1 
ATOM   3610  C  CD    B GLN A 1 233 ? -8.827  -18.637 42.005  0.50 27.99 ? 233 GLN A CD    1 
ATOM   3611  O  OE1   A GLN A 1 233 ? -9.727  -16.519 43.477  0.50 26.74 ? 233 GLN A OE1   1 
ATOM   3612  O  OE1   B GLN A 1 233 ? -9.886  -18.021 42.122  0.50 28.71 ? 233 GLN A OE1   1 
ATOM   3613  N  NE2   A GLN A 1 233 ? -9.522  -18.599 42.645  0.50 28.62 ? 233 GLN A NE2   1 
ATOM   3614  N  NE2   B GLN A 1 233 ? -8.769  -19.872 41.523  0.50 32.92 ? 233 GLN A NE2   1 
ATOM   3615  N  N     A ILE A 1 234 ? -6.538  -14.280 40.589  0.50 18.71 ? 234 ILE A N     1 
ATOM   3616  N  N     B ILE A 1 234 ? -6.498  -14.317 40.469  0.50 18.72 ? 234 ILE A N     1 
ATOM   3617  C  CA    A ILE A 1 234 ? -6.330  -12.893 40.983  0.50 23.90 ? 234 ILE A CA    1 
ATOM   3618  C  CA    B ILE A 1 234 ? -6.405  -12.926 40.903  0.50 23.80 ? 234 ILE A CA    1 
ATOM   3619  C  C     A ILE A 1 234 ? -7.267  -11.973 40.211  0.50 23.03 ? 234 ILE A C     1 
ATOM   3620  C  C     B ILE A 1 234 ? -7.402  -12.061 40.142  0.50 23.27 ? 234 ILE A C     1 
ATOM   3621  O  O     A ILE A 1 234 ? -7.875  -11.064 40.790  0.50 28.67 ? 234 ILE A O     1 
ATOM   3622  O  O     B ILE A 1 234 ? -8.160  -11.286 40.741  0.50 28.07 ? 234 ILE A O     1 
ATOM   3623  C  CB    A ILE A 1 234 ? -4.854  -12.500 40.796  0.50 23.71 ? 234 ILE A CB    1 
ATOM   3624  C  CB    B ILE A 1 234 ? -4.967  -12.404 40.731  0.50 23.59 ? 234 ILE A CB    1 
ATOM   3625  C  CG1   A ILE A 1 234 ? -3.962  -13.369 41.692  0.50 26.31 ? 234 ILE A CG1   1 
ATOM   3626  C  CG1   B ILE A 1 234 ? -4.011  -13.144 41.672  0.50 26.45 ? 234 ILE A CG1   1 
ATOM   3627  C  CG2   A ILE A 1 234 ? -4.659  -11.029 41.110  0.50 26.87 ? 234 ILE A CG2   1 
ATOM   3628  C  CG2   B ILE A 1 234 ? -4.919  -10.905 40.967  0.50 26.52 ? 234 ILE A CG2   1 
ATOM   3629  C  CD1   A ILE A 1 234 ? -2.480  -13.148 41.490  0.50 34.01 ? 234 ILE A CD1   1 
ATOM   3630  C  CD1   B ILE A 1 234 ? -2.551  -12.831 41.423  0.50 34.30 ? 234 ILE A CD1   1 
ATOM   3631  N  N     A VAL A 1 235 ? -7.419  -12.207 38.903  0.50 24.12 ? 235 VAL A N     1 
ATOM   3632  N  N     B VAL A 1 235 ? -7.418  -12.183 38.810  0.50 24.08 ? 235 VAL A N     1 
ATOM   3633  C  CA    A VAL A 1 235 ? -8.381  -11.442 38.110  0.50 21.51 ? 235 VAL A CA    1 
ATOM   3634  C  CA    B VAL A 1 235 ? -8.354  -11.418 37.988  0.50 21.49 ? 235 VAL A CA    1 
ATOM   3635  C  C     A VAL A 1 235 ? -9.790  -11.613 38.667  0.50 25.55 ? 235 VAL A C     1 
ATOM   3636  C  C     B VAL A 1 235 ? -9.792  -11.679 38.426  0.50 25.63 ? 235 VAL A C     1 
ATOM   3637  O  O     A VAL A 1 235 ? -10.561 -10.648 38.756  0.50 28.71 ? 235 VAL A O     1 
ATOM   3638  O  O     B VAL A 1 235 ? -10.641 -10.780 38.396  0.50 28.53 ? 235 VAL A O     1 
ATOM   3639  C  CB    A VAL A 1 235 ? -8.306  -11.859 36.627  0.50 25.09 ? 235 VAL A CB    1 
ATOM   3640  C  CB    B VAL A 1 235 ? -8.140  -11.751 36.497  0.50 25.57 ? 235 VAL A CB    1 
ATOM   3641  C  CG1   A VAL A 1 235 ? -9.436  -11.218 35.831  0.50 23.84 ? 235 VAL A CG1   1 
ATOM   3642  C  CG1   B VAL A 1 235 ? -9.120  -10.984 35.625  0.50 24.71 ? 235 VAL A CG1   1 
ATOM   3643  C  CG2   A VAL A 1 235 ? -6.950  -11.481 36.033  0.50 25.20 ? 235 VAL A CG2   1 
ATOM   3644  C  CG2   B VAL A 1 235 ? -6.694  -11.447 36.084  0.50 24.14 ? 235 VAL A CG2   1 
ATOM   3645  N  N     A SER A 1 236 ? -10.146 -12.839 39.056  0.50 26.05 ? 236 SER A N     1 
ATOM   3646  N  N     B SER A 1 236 ? -10.083 -12.908 38.852  0.50 25.21 ? 236 SER A N     1 
ATOM   3647  C  CA    A SER A 1 236 ? -11.473 -13.093 39.613  0.50 26.43 ? 236 SER A CA    1 
ATOM   3648  C  CA    B SER A 1 236 ? -11.422 -13.221 39.343  0.50 26.61 ? 236 SER A CA    1 
ATOM   3649  C  C     A SER A 1 236 ? -11.728 -12.237 40.847  0.50 25.65 ? 236 SER A C     1 
ATOM   3650  C  C     B SER A 1 236 ? -11.760 -12.420 40.595  0.50 25.41 ? 236 SER A C     1 
ATOM   3651  O  O     A SER A 1 236 ? -12.791 -11.619 40.980  0.50 25.83 ? 236 SER A O     1 
ATOM   3652  O  O     B SER A 1 236 ? -12.884 -11.925 40.738  0.50 25.85 ? 236 SER A O     1 
ATOM   3653  C  CB    A SER A 1 236 ? -11.625 -14.574 39.954  0.50 27.34 ? 236 SER A CB    1 
ATOM   3654  C  CB    B SER A 1 236 ? -11.539 -14.718 39.619  0.50 25.93 ? 236 SER A CB    1 
ATOM   3655  O  OG    A SER A 1 236 ? -12.878 -14.835 40.571  0.50 18.83 ? 236 SER A OG    1 
ATOM   3656  O  OG    B SER A 1 236 ? -12.246 -15.366 38.580  0.50 31.14 ? 236 SER A OG    1 
ATOM   3657  N  N     A SER A 1 237 ? -10.758 -12.189 41.765  0.50 27.05 ? 237 SER A N     1 
ATOM   3658  N  N     B SER A 1 237 ? -10.801 -12.287 41.516  0.50 27.38 ? 237 SER A N     1 
ATOM   3659  C  CA    A SER A 1 237 ? -10.917 -11.405 42.983  0.50 26.86 ? 237 SER A CA    1 
ATOM   3660  C  CA    B SER A 1 237 ? -11.054 -11.526 42.735  0.50 26.50 ? 237 SER A CA    1 
ATOM   3661  C  C     A SER A 1 237 ? -10.977 -9.910  42.711  0.50 28.06 ? 237 SER A C     1 
ATOM   3662  C  C     B SER A 1 237 ? -11.287 -10.050 42.443  0.50 27.58 ? 237 SER A C     1 
ATOM   3663  O  O     A SER A 1 237 ? -11.530 -9.166  43.528  0.50 26.57 ? 237 SER A O     1 
ATOM   3664  O  O     B SER A 1 237 ? -12.071 -9.398  43.142  0.50 24.57 ? 237 SER A O     1 
ATOM   3665  C  CB    A SER A 1 237 ? -9.779  -11.706 43.957  0.50 28.11 ? 237 SER A CB    1 
ATOM   3666  C  CB    B SER A 1 237 ? -9.891  -11.692 43.713  0.50 28.05 ? 237 SER A CB    1 
ATOM   3667  O  OG    A SER A 1 237 ? -9.853  -13.038 44.430  0.50 29.00 ? 237 SER A OG    1 
ATOM   3668  O  OG    B SER A 1 237 ? -9.821  -13.020 44.199  0.50 29.02 ? 237 SER A OG    1 
ATOM   3669  N  N     A ILE A 1 238 ? -10.421 -9.454  41.589  0.50 24.73 ? 238 ILE A N     1 
ATOM   3670  N  N     B ILE A 1 238 ? -10.625 -9.512  41.417  0.50 25.49 ? 238 ILE A N     1 
ATOM   3671  C  CA    A ILE A 1 238 ? -10.454 -8.034  41.258  0.50 25.20 ? 238 ILE A CA    1 
ATOM   3672  C  CA    B ILE A 1 238 ? -10.781 -8.101  41.072  0.50 24.83 ? 238 ILE A CA    1 
ATOM   3673  C  C     A ILE A 1 238 ? -11.767 -7.660  40.575  0.50 25.86 ? 238 ILE A C     1 
ATOM   3674  C  C     B ILE A 1 238 ? -12.170 -7.836  40.505  0.50 27.07 ? 238 ILE A C     1 
ATOM   3675  O  O     A ILE A 1 238 ? -12.246 -6.527  40.719  0.50 26.60 ? 238 ILE A O     1 
ATOM   3676  O  O     B ILE A 1 238 ? -12.846 -6.877  40.897  0.50 27.61 ? 238 ILE A O     1 
ATOM   3677  C  CB    A ILE A 1 238 ? -9.235  -7.677  40.387  0.50 24.50 ? 238 ILE A CB    1 
ATOM   3678  C  CB    B ILE A 1 238 ? -9.679  -7.670  40.087  0.50 22.32 ? 238 ILE A CB    1 
ATOM   3679  C  CG1   A ILE A 1 238 ? -7.943  -8.001  41.137  0.50 26.16 ? 238 ILE A CG1   1 
ATOM   3680  C  CG1   B ILE A 1 238 ? -8.323  -7.634  40.796  0.50 25.79 ? 238 ILE A CG1   1 
ATOM   3681  C  CG2   A ILE A 1 238 ? -9.243  -6.212  40.002  0.50 26.67 ? 238 ILE A CG2   1 
ATOM   3682  C  CG2   B ILE A 1 238 ? -10.010 -6.319  39.476  0.50 26.76 ? 238 ILE A CG2   1 
ATOM   3683  C  CD1   A ILE A 1 238 ? -6.699  -7.851  40.300  0.50 22.38 ? 238 ILE A CD1   1 
ATOM   3684  C  CD1   B ILE A 1 238 ? -7.146  -7.516  39.853  0.50 25.36 ? 238 ILE A CD1   1 
ATOM   3685  N  N     A THR A 1 239 ? -12.381 -8.592  39.844  0.50 25.80 ? 239 THR A N     1 
ATOM   3686  N  N     B THR A 1 239 ? -12.620 -8.681  39.581  0.50 26.61 ? 239 THR A N     1 
ATOM   3687  C  CA    A THR A 1 239 ? -13.624 -8.326  39.132  0.50 26.18 ? 239 THR A CA    1 
ATOM   3688  C  CA    B THR A 1 239 ? -13.896 -8.479  38.907  0.50 26.75 ? 239 THR A CA    1 
ATOM   3689  C  C     A THR A 1 239 ? -14.864 -8.813  39.870  0.50 28.89 ? 239 THR A C     1 
ATOM   3690  C  C     B THR A 1 239 ? -15.075 -9.083  39.657  0.50 28.80 ? 239 THR A C     1 
ATOM   3691  O  O     A THR A 1 239 ? -15.978 -8.483  39.446  0.50 25.18 ? 239 THR A O     1 
ATOM   3692  O  O     B THR A 1 239 ? -16.211 -8.962  39.187  0.50 26.31 ? 239 THR A O     1 
ATOM   3693  C  CB    A THR A 1 239 ? -13.597 -8.973  37.742  0.50 26.48 ? 239 THR A CB    1 
ATOM   3694  C  CB    B THR A 1 239 ? -13.853 -9.066  37.490  0.50 26.36 ? 239 THR A CB    1 
ATOM   3695  O  OG1   A THR A 1 239 ? -13.634 -10.399 37.877  0.50 23.48 ? 239 THR A OG1   1 
ATOM   3696  O  OG1   B THR A 1 239 ? -13.808 -10.497 37.563  0.50 23.22 ? 239 THR A OG1   1 
ATOM   3697  C  CG2   A THR A 1 239 ? -12.338 -8.566  36.981  0.50 25.21 ? 239 THR A CG2   1 
ATOM   3698  C  CG2   B THR A 1 239 ? -12.628 -8.559  36.734  0.50 25.55 ? 239 THR A CG2   1 
ATOM   3699  N  N     A ALA A 1 240 ? -14.702 -9.590  40.948  0.50 27.92 ? 240 ALA A N     1 
ATOM   3700  N  N     B ALA A 1 240 ? -14.839 -9.721  40.808  0.50 27.99 ? 240 ALA A N     1 
ATOM   3701  C  CA    A ALA A 1 240 ? -15.860 -10.090 41.686  0.50 25.97 ? 240 ALA A CA    1 
ATOM   3702  C  CA    B ALA A 1 240 ? -15.925 -10.391 41.518  0.50 25.80 ? 240 ALA A CA    1 
ATOM   3703  C  C     A ALA A 1 240 ? -16.798 -8.964  42.098  0.50 24.58 ? 240 ALA A C     1 
ATOM   3704  C  C     B ALA A 1 240 ? -17.026 -9.420  41.927  0.50 25.36 ? 240 ALA A C     1 
ATOM   3705  O  O     A ALA A 1 240 ? -18.019 -9.155  42.136  0.50 25.74 ? 240 ALA A O     1 
ATOM   3706  O  O     B ALA A 1 240 ? -18.202 -9.801  41.954  0.50 22.61 ? 240 ALA A O     1 
ATOM   3707  C  CB    A ALA A 1 240 ? -15.405 -10.871 42.920  0.50 27.06 ? 240 ALA A CB    1 
ATOM   3708  C  CB    B ALA A 1 240 ? -15.383 -11.120 42.748  0.50 26.76 ? 240 ALA A CB    1 
ATOM   3709  N  N     A SER A 1 241 ? -16.248 -7.782  42.391  0.50 21.33 ? 241 SER A N     1 
ATOM   3710  N  N     B SER A 1 241 ? -16.677 -8.168  42.238  0.50 23.19 ? 241 SER A N     1 
ATOM   3711  C  CA    A SER A 1 241 ? -17.061 -6.635  42.779  0.50 25.84 ? 241 SER A CA    1 
ATOM   3712  C  CA    B SER A 1 241 ? -17.690 -7.218  42.687  0.50 26.34 ? 241 SER A CA    1 
ATOM   3713  C  C     A SER A 1 241 ? -18.042 -6.213  41.694  0.50 23.56 ? 241 SER A C     1 
ATOM   3714  C  C     B SER A 1 241 ? -18.617 -6.781  41.561  0.50 27.47 ? 241 SER A C     1 
ATOM   3715  O  O     A SER A 1 241 ? -19.046 -5.562  42.001  0.50 22.97 ? 241 SER A O     1 
ATOM   3716  O  O     B SER A 1 241 ? -19.735 -6.331  41.836  0.50 22.26 ? 241 SER A O     1 
ATOM   3717  C  CB    A SER A 1 241 ? -16.154 -5.460  43.135  0.50 25.92 ? 241 SER A CB    1 
ATOM   3718  C  CB    B SER A 1 241 ? -17.030 -5.996  43.330  0.50 28.90 ? 241 SER A CB    1 
ATOM   3719  O  OG    A SER A 1 241 ? -15.303 -5.139  42.047  0.50 27.78 ? 241 SER A OG    1 
ATOM   3720  O  OG    B SER A 1 241 ? -16.294 -5.240  42.386  0.50 27.78 ? 241 SER A OG    1 
ATOM   3721  N  N     A LEU A 1 242 ? -17.770 -6.551  40.436  0.50 24.98 ? 242 LEU A N     1 
ATOM   3722  N  N     B LEU A 1 242 ? -18.182 -6.909  40.305  0.50 21.92 ? 242 LEU A N     1 
ATOM   3723  C  CA    A LEU A 1 242 ? -18.660 -6.197  39.341  0.50 20.44 ? 242 LEU A CA    1 
ATOM   3724  C  CA    B LEU A 1 242 ? -19.037 -6.630  39.159  0.50 19.38 ? 242 LEU A CA    1 
ATOM   3725  C  C     A LEU A 1 242 ? -19.743 -7.237  39.100  0.50 26.62 ? 242 LEU A C     1 
ATOM   3726  C  C     B LEU A 1 242 ? -19.977 -7.785  38.840  0.50 28.96 ? 242 LEU A C     1 
ATOM   3727  O  O     A LEU A 1 242 ? -20.740 -6.929  38.434  0.50 28.31 ? 242 LEU A O     1 
ATOM   3728  O  O     B LEU A 1 242 ? -20.962 -7.585  38.120  0.50 29.73 ? 242 LEU A O     1 
ATOM   3729  C  CB    A LEU A 1 242 ? -17.855 -6.007  38.049  0.50 28.46 ? 242 LEU A CB    1 
ATOM   3730  C  CB    B LEU A 1 242 ? -18.180 -6.323  37.926  0.50 28.76 ? 242 LEU A CB    1 
ATOM   3731  C  CG    A LEU A 1 242 ? -16.654 -5.063  38.117  0.50 26.71 ? 242 LEU A CG    1 
ATOM   3732  C  CG    B LEU A 1 242 ? -17.075 -5.275  38.075  0.50 26.36 ? 242 LEU A CG    1 
ATOM   3733  C  CD1   A LEU A 1 242 ? -15.787 -5.203  36.873  0.50 25.21 ? 242 LEU A CD1   1 
ATOM   3734  C  CD1   B LEU A 1 242 ? -16.090 -5.365  36.914  0.50 25.71 ? 242 LEU A CD1   1 
ATOM   3735  C  CD2   A LEU A 1 242 ? -17.114 -3.628  38.289  0.50 24.65 ? 242 LEU A CD2   1 
ATOM   3736  C  CD2   B LEU A 1 242 ? -17.666 -3.881  38.166  0.50 25.74 ? 242 LEU A CD2   1 
ATOM   3737  N  N     A ARG A 1 243 ? -19.577 -8.451  39.637  0.50 25.47 ? 243 ARG A N     1 
ATOM   3738  N  N     B ARG A 1 243 ? -19.691 -8.985  39.350  0.50 27.66 ? 243 ARG A N     1 
ATOM   3739  C  CA    A ARG A 1 243 ? -20.412 -9.586  39.277  0.50 23.92 ? 243 ARG A CA    1 
ATOM   3740  C  CA    B ARG A 1 243 ? -20.473 -10.178 39.058  0.50 25.31 ? 243 ARG A CA    1 
ATOM   3741  C  C     A ARG A 1 243 ? -21.307 -10.077 40.402  0.50 24.34 ? 243 ARG A C     1 
ATOM   3742  C  C     B ARG A 1 243 ? -21.290 -10.650 40.248  0.50 25.20 ? 243 ARG A C     1 
ATOM   3743  O  O     A ARG A 1 243 ? -22.264 -10.808 40.127  0.50 25.31 ? 243 ARG A O     1 
ATOM   3744  O  O     B ARG A 1 243 ? -22.047 -11.616 40.116  0.50 23.68 ? 243 ARG A O     1 
ATOM   3745  C  CB    A ARG A 1 243 ? -19.534 -10.756 38.801  0.50 24.95 ? 243 ARG A CB    1 
ATOM   3746  C  CB    B ARG A 1 243 ? -19.557 -11.319 38.592  0.50 21.45 ? 243 ARG A CB    1 
ATOM   3747  C  CG    A ARG A 1 243 ? -18.305 -10.313 38.016  0.50 27.06 ? 243 ARG A CG    1 
ATOM   3748  C  CG    B ARG A 1 243 ? -18.700 -10.982 37.385  0.50 28.48 ? 243 ARG A CG    1 
ATOM   3749  C  CD    A ARG A 1 243 ? -17.517 -11.487 37.445  0.50 25.11 ? 243 ARG A CD    1 
ATOM   3750  C  CD    B ARG A 1 243 ? -17.752 -12.118 37.034  0.50 24.30 ? 243 ARG A CD    1 
ATOM   3751  N  NE    A ARG A 1 243 ? -16.374 -11.856 38.274  0.50 24.73 ? 243 ARG A NE    1 
ATOM   3752  N  NE    B ARG A 1 243 ? -16.616 -12.202 37.945  0.50 25.69 ? 243 ARG A NE    1 
ATOM   3753  C  CZ    A ARG A 1 243 ? -16.226 -13.032 38.867  0.50 25.09 ? 243 ARG A CZ    1 
ATOM   3754  C  CZ    B ARG A 1 243 ? -16.398 -13.207 38.782  0.50 25.12 ? 243 ARG A CZ    1 
ATOM   3755  N  NH1   A ARG A 1 243 ? -17.130 -13.990 38.739  0.50 23.32 ? 243 ARG A NH1   1 
ATOM   3756  N  NH1   B ARG A 1 243 ? -17.223 -14.237 38.855  0.50 23.75 ? 243 ARG A NH1   1 
ATOM   3757  N  NH2   A ARG A 1 243 ? -15.137 -13.259 39.596  0.50 26.00 ? 243 ARG A NH2   1 
ATOM   3758  N  NH2   B ARG A 1 243 ? -15.318 -13.182 39.557  0.50 25.86 ? 243 ARG A NH2   1 
ATOM   3759  N  N     A PHE A 1 244 ? -21.027 -9.697  41.642  0.50 24.77 ? 244 PHE A N     1 
ATOM   3760  N  N     B PHE A 1 244 ? -21.145 -10.004 41.401  0.50 24.59 ? 244 PHE A N     1 
ATOM   3761  C  CA    A PHE A 1 244 ? -21.765 -10.145 42.813  0.50 25.67 ? 244 PHE A CA    1 
ATOM   3762  C  CA    B PHE A 1 244 ? -21.849 -10.381 42.614  0.50 25.07 ? 244 PHE A CA    1 
ATOM   3763  C  C     A PHE A 1 244 ? -22.318 -8.934  43.561  0.50 31.42 ? 244 PHE A C     1 
ATOM   3764  C  C     B PHE A 1 244 ? -22.305 -9.117  43.324  0.50 31.80 ? 244 PHE A C     1 
ATOM   3765  O  O     A PHE A 1 244 ? -22.140 -7.784  43.152  0.50 31.09 ? 244 PHE A O     1 
ATOM   3766  O  O     B PHE A 1 244 ? -21.716 -8.045  43.157  0.50 30.19 ? 244 PHE A O     1 
ATOM   3767  C  CB    A PHE A 1 244 ? -20.872 -10.986 43.732  0.50 25.86 ? 244 PHE A CB    1 
ATOM   3768  C  CB    B PHE A 1 244 ? -20.963 -11.212 43.556  0.50 25.37 ? 244 PHE A CB    1 
ATOM   3769  C  CG    A PHE A 1 244 ? -20.385 -12.261 43.108  0.50 26.66 ? 244 PHE A CG    1 
ATOM   3770  C  CG    B PHE A 1 244 ? -20.511 -12.524 42.978  0.50 27.68 ? 244 PHE A CG    1 
ATOM   3771  C  CD1   A PHE A 1 244 ? -21.245 -13.330 42.922  0.50 30.05 ? 244 PHE A CD1   1 
ATOM   3772  C  CD1   B PHE A 1 244 ? -21.415 -13.549 42.757  0.50 30.02 ? 244 PHE A CD1   1 
ATOM   3773  C  CD2   A PHE A 1 244 ? -19.062 -12.395 42.719  0.50 28.79 ? 244 PHE A CD2   1 
ATOM   3774  C  CD2   B PHE A 1 244 ? -19.177 -12.737 42.671  0.50 28.39 ? 244 PHE A CD2   1 
ATOM   3775  C  CE1   A PHE A 1 244 ? -20.798 -14.506 42.348  0.50 29.59 ? 244 PHE A CE1   1 
ATOM   3776  C  CE1   B PHE A 1 244 ? -20.999 -14.758 42.230  0.50 28.55 ? 244 PHE A CE1   1 
ATOM   3777  C  CE2   A PHE A 1 244 ? -18.610 -13.567 42.147  0.50 30.73 ? 244 PHE A CE2   1 
ATOM   3778  C  CE2   B PHE A 1 244 ? -18.757 -13.942 42.146  0.50 31.08 ? 244 PHE A CE2   1 
ATOM   3779  C  CZ    A PHE A 1 244 ? -19.478 -14.624 41.963  0.50 28.49 ? 244 PHE A CZ    1 
ATOM   3780  C  CZ    B PHE A 1 244 ? -19.667 -14.954 41.927  0.50 28.90 ? 244 PHE A CZ    1 
ATOM   3781  N  N     A ASP A 1 245 ? -22.999 -9.206  44.669  0.50 23.88 ? 245 ASP A N     1 
ATOM   3782  N  N     B ASP A 1 245 ? -23.362 -9.250  44.119  0.50 27.78 ? 245 ASP A N     1 
ATOM   3783  C  CA    A ASP A 1 245 ? -23.408 -8.138  45.565  0.50 31.01 ? 245 ASP A CA    1 
ATOM   3784  C  CA    B ASP A 1 245 ? -23.782 -8.147  44.966  0.50 30.37 ? 245 ASP A CA    1 
ATOM   3785  C  C     A ASP A 1 245 ? -22.187 -7.591  46.296  0.50 34.21 ? 245 ASP A C     1 
ATOM   3786  C  C     B ASP A 1 245 ? -22.645 -7.764  45.906  0.50 34.18 ? 245 ASP A C     1 
ATOM   3787  O  O     A ASP A 1 245 ? -21.237 -8.319  46.593  0.50 31.30 ? 245 ASP A O     1 
ATOM   3788  O  O     B ASP A 1 245 ? -21.838 -8.605  46.315  0.50 32.80 ? 245 ASP A O     1 
ATOM   3789  C  CB    A ASP A 1 245 ? -24.449 -8.649  46.563  0.50 28.69 ? 245 ASP A CB    1 
ATOM   3790  C  CB    B ASP A 1 245 ? -25.028 -8.535  45.760  0.50 25.37 ? 245 ASP A CB    1 
ATOM   3791  C  CG    A ASP A 1 245 ? -25.297 -7.529  47.154  0.50 34.80 ? 245 ASP A CG    1 
ATOM   3792  C  CG    B ASP A 1 245 ? -25.678 -7.347  46.457  0.50 33.21 ? 245 ASP A CG    1 
ATOM   3793  O  OD1   A ASP A 1 245 ? -24.749 -6.442  47.440  0.50 40.31 ? 245 ASP A OD1   1 
ATOM   3794  O  OD1   B ASP A 1 245 ? -25.451 -6.197  46.031  0.50 34.35 ? 245 ASP A OD1   1 
ATOM   3795  O  OD2   A ASP A 1 245 ? -26.516 -7.736  47.322  0.50 35.97 ? 245 ASP A OD2   1 
ATOM   3796  O  OD2   B ASP A 1 245 ? -26.419 -7.566  47.436  0.50 36.27 ? 245 ASP A OD2   1 
ATOM   3797  N  N     A GLY A 1 246 ? -22.207 -6.295  46.574  0.50 35.82 ? 246 GLY A N     1 
ATOM   3798  N  N     B GLY A 1 246 ? -22.570 -6.481  46.230  0.50 34.47 ? 246 GLY A N     1 
ATOM   3799  C  CA    A GLY A 1 246 ? -21.075 -5.672  47.232  0.50 36.66 ? 246 GLY A CA    1 
ATOM   3800  C  CA    B GLY A 1 246 ? -21.492 -6.002  47.073  0.50 36.92 ? 246 GLY A CA    1 
ATOM   3801  C  C     A GLY A 1 246 ? -21.266 -4.178  47.335  0.50 34.79 ? 246 GLY A C     1 
ATOM   3802  C  C     B GLY A 1 246 ? -21.613 -4.512  47.289  0.50 34.78 ? 246 GLY A C     1 
ATOM   3803  O  O     A GLY A 1 246 ? -22.136 -3.587  46.691  0.50 39.50 ? 246 GLY A O     1 
ATOM   3804  O  O     B GLY A 1 246 ? -22.491 -3.846  46.733  0.50 39.75 ? 246 GLY A O     1 
ATOM   3805  N  N     A ALA A 1 247 ? -20.421 -3.570  48.168  0.50 32.96 ? 247 ALA A N     1 
ATOM   3806  N  N     B ALA A 1 247 ? -20.702 -3.994  48.114  0.50 36.73 ? 247 ALA A N     1 
ATOM   3807  C  CA    A ALA A 1 247 ? -20.491 -2.143  48.438  0.50 36.63 ? 247 ALA A CA    1 
ATOM   3808  C  CA    B ALA A 1 247 ? -20.709 -2.589  48.502  0.50 38.20 ? 247 ALA A CA    1 
ATOM   3809  C  C     A ALA A 1 247 ? -19.244 -1.379  48.028  0.50 35.95 ? 247 ALA A C     1 
ATOM   3810  C  C     B ALA A 1 247 ? -19.408 -1.881  48.155  0.50 33.94 ? 247 ALA A C     1 
ATOM   3811  O  O     A ALA A 1 247 ? -19.270 -0.143  48.046  0.50 33.05 ? 247 ALA A O     1 
ATOM   3812  O  O     B ALA A 1 247 ? -19.172 -0.768  48.641  0.50 32.94 ? 247 ALA A O     1 
ATOM   3813  C  CB    A ALA A 1 247 ? -20.759 -1.890  49.931  0.50 40.58 ? 247 ALA A CB    1 
ATOM   3814  C  CB    B ALA A 1 247 ? -20.990 -2.452  50.002  0.50 41.26 ? 247 ALA A CB    1 
ATOM   3815  N  N     A LEU A 1 248 ? -18.162 -2.065  47.662  0.50 31.67 ? 248 LEU A N     1 
ATOM   3816  N  N     B LEU A 1 248 ? -18.562 -2.491  47.327  0.50 31.84 ? 248 LEU A N     1 
ATOM   3817  C  CA    A LEU A 1 248 ? -16.910 -1.432  47.274  0.50 28.41 ? 248 LEU A CA    1 
ATOM   3818  C  CA    B LEU A 1 248 ? -17.278 -1.916  46.956  0.50 28.06 ? 248 LEU A CA    1 
ATOM   3819  C  C     A LEU A 1 248 ? -16.582 -1.817  45.838  0.50 28.31 ? 248 LEU A C     1 
ATOM   3820  C  C     B LEU A 1 248 ? -17.007 -2.235  45.493  0.50 27.10 ? 248 LEU A C     1 
ATOM   3821  O  O     A LEU A 1 248 ? -16.660 -2.997  45.479  0.50 26.33 ? 248 LEU A O     1 
ATOM   3822  O  O     B LEU A 1 248 ? -17.165 -3.383  45.069  0.50 23.29 ? 248 LEU A O     1 
ATOM   3823  C  CB    A LEU A 1 248 ? -15.775 -1.845  48.218  0.50 29.74 ? 248 LEU A CB    1 
ATOM   3824  C  CB    B LEU A 1 248 ? -16.155 -2.464  47.849  0.50 27.38 ? 248 LEU A CB    1 
ATOM   3825  C  CG    A LEU A 1 248 ? -14.407 -1.184  48.034  0.50 31.06 ? 248 LEU A CG    1 
ATOM   3826  C  CG    B LEU A 1 248 ? -14.815 -1.726  47.876  0.50 33.16 ? 248 LEU A CG    1 
ATOM   3827  C  CD1   A LEU A 1 248 ? -14.501 0.319   48.221  0.50 30.73 ? 248 LEU A CD1   1 
ATOM   3828  C  CD1   B LEU A 1 248 ? -15.019 -0.261  48.206  0.50 29.18 ? 248 LEU A CD1   1 
ATOM   3829  C  CD2   A LEU A 1 248 ? -13.386 -1.785  48.997  0.50 28.15 ? 248 LEU A CD2   1 
ATOM   3830  C  CD2   B LEU A 1 248 ? -13.872 -2.374  48.885  0.50 28.45 ? 248 LEU A CD2   1 
ATOM   3831  N  N     A ASN A 1 249 ? -16.227 -0.818  45.022  0.50 26.61 ? 249 ASN A N     1 
ATOM   3832  N  N     B ASN A 1 249 ? -16.626 -1.214  44.726  0.50 28.97 ? 249 ASN A N     1 
ATOM   3833  C  CA    A ASN A 1 249 ? -15.909 -1.018  43.603  0.50 28.76 ? 249 ASN A CA    1 
ATOM   3834  C  CA    B ASN A 1 249 ? -16.260 -1.374  43.317  0.50 27.85 ? 249 ASN A CA    1 
ATOM   3835  C  C     A ASN A 1 249 ? -17.089 -1.633  42.848  0.50 26.78 ? 249 ASN A C     1 
ATOM   3836  C  C     B ASN A 1 249 ? -17.363 -2.081  42.530  0.50 29.09 ? 249 ASN A C     1 
ATOM   3837  O  O     A ASN A 1 249 ? -16.938 -2.598  42.095  0.50 28.36 ? 249 ASN A O     1 
ATOM   3838  O  O     B ASN A 1 249 ? -17.133 -3.089  41.858  0.50 28.27 ? 249 ASN A O     1 
ATOM   3839  C  CB    A ASN A 1 249 ? -14.651 -1.875  43.434  0.50 27.17 ? 249 ASN A CB    1 
ATOM   3840  C  CB    B ASN A 1 249 ? -14.932 -2.122  43.185  0.50 27.04 ? 249 ASN A CB    1 
ATOM   3841  C  CG    A ASN A 1 249 ? -13.390 -1.146  43.837  0.50 28.59 ? 249 ASN A CG    1 
ATOM   3842  C  CG    B ASN A 1 249 ? -13.764 -1.333  43.732  0.50 28.26 ? 249 ASN A CG    1 
ATOM   3843  O  OD1   A ASN A 1 249 ? -13.371 0.081   43.930  0.50 28.78 ? 249 ASN A OD1   1 
ATOM   3844  O  OD1   B ASN A 1 249 ? -13.832 -0.111  43.856  0.50 27.06 ? 249 ASN A OD1   1 
ATOM   3845  N  ND2   A ASN A 1 249 ? -12.316 -1.899  44.051  0.50 28.18 ? 249 ASN A ND2   1 
ATOM   3846  N  ND2   B ASN A 1 249 ? -12.676 -2.027  44.048  0.50 27.69 ? 249 ASN A ND2   1 
ATOM   3847  N  N     A VAL A 1 250 ? -18.275 -1.051  43.038  0.50 30.09 ? 250 VAL A N     1 
ATOM   3848  N  N     B VAL A 1 250 ? -18.581 -1.536  42.617  0.50 25.82 ? 250 VAL A N     1 
ATOM   3849  C  CA    A VAL A 1 250 ? -19.491 -1.682  42.531  0.50 26.91 ? 250 VAL A CA    1 
ATOM   3850  C  CA    B VAL A 1 250 ? -19.735 -2.170  41.986  0.50 26.69 ? 250 VAL A CA    1 
ATOM   3851  C  C     A VAL A 1 250 ? -19.647 -1.539  41.023  0.50 26.95 ? 250 VAL A C     1 
ATOM   3852  C  C     B VAL A 1 250 ? -19.944 -1.722  40.548  0.50 28.46 ? 250 VAL A C     1 
ATOM   3853  O  O     A VAL A 1 250 ? -20.447 -2.272  40.426  0.50 26.31 ? 250 VAL A O     1 
ATOM   3854  O  O     B VAL A 1 250 ? -20.736 -2.351  39.827  0.50 29.95 ? 250 VAL A O     1 
ATOM   3855  C  CB    A VAL A 1 250 ? -20.743 -1.124  43.232  0.50 30.69 ? 250 VAL A CB    1 
ATOM   3856  C  CB    B VAL A 1 250 ? -21.024 -1.913  42.796  0.50 27.18 ? 250 VAL A CB    1 
ATOM   3857  C  CG1   A VAL A 1 250 ? -20.499 -0.993  44.725  0.50 30.36 ? 250 VAL A CG1   1 
ATOM   3858  C  CG1   B VAL A 1 250 ? -20.732 -1.984  44.285  0.50 28.72 ? 250 VAL A CG1   1 
ATOM   3859  C  CG2   A VAL A 1 250 ? -21.159 0.209   42.621  0.50 29.71 ? 250 VAL A CG2   1 
ATOM   3860  C  CG2   B VAL A 1 250 ? -21.639 -0.572  42.419  0.50 26.32 ? 250 VAL A CG2   1 
ATOM   3861  N  N     A ASP A 1 251 ? -18.922 -0.619  40.388  0.50 27.54 ? 251 ASP A N     1 
ATOM   3862  N  N     B ASP A 1 251 ? -19.271 -0.658  40.105  0.50 30.18 ? 251 ASP A N     1 
ATOM   3863  C  CA    A ASP A 1 251 ? -18.954 -0.494  38.935  0.50 28.55 ? 251 ASP A CA    1 
ATOM   3864  C  CA    B ASP A 1 251 ? -19.247 -0.289  38.696  0.50 27.85 ? 251 ASP A CA    1 
ATOM   3865  C  C     A ASP A 1 251 ? -17.606 0.034   38.459  0.50 26.07 ? 251 ASP A C     1 
ATOM   3866  C  C     B ASP A 1 251 ? -17.831 0.138   38.325  0.50 26.07 ? 251 ASP A C     1 
ATOM   3867  O  O     A ASP A 1 251 ? -16.714 0.330   39.260  0.50 25.98 ? 251 ASP A O     1 
ATOM   3868  O  O     B ASP A 1 251 ? -16.967 0.321   39.187  0.50 26.31 ? 251 ASP A O     1 
ATOM   3869  C  CB    A ASP A 1 251 ? -20.127 0.388   38.475  0.50 29.42 ? 251 ASP A CB    1 
ATOM   3870  C  CB    B ASP A 1 251 ? -20.282 0.806   38.361  0.50 28.42 ? 251 ASP A CB    1 
ATOM   3871  C  CG    A ASP A 1 251 ? -20.087 1.793   39.055  0.50 31.23 ? 251 ASP A CG    1 
ATOM   3872  C  CG    B ASP A 1 251 ? -19.995 2.138   39.037  0.50 32.18 ? 251 ASP A CG    1 
ATOM   3873  O  OD1   A ASP A 1 251 ? -18.989 2.318   39.326  0.50 32.05 ? 251 ASP A OD1   1 
ATOM   3874  O  OD1   B ASP A 1 251 ? -19.033 2.235   39.818  0.50 33.40 ? 251 ASP A OD1   1 
ATOM   3875  O  OD2   A ASP A 1 251 ? -21.176 2.382   39.239  0.50 33.74 ? 251 ASP A OD2   1 
ATOM   3876  O  OD2   B ASP A 1 251 ? -20.752 3.102   38.783  0.50 36.53 ? 251 ASP A OD2   1 
ATOM   3877  N  N     A LEU A 1 252 ? -17.463 0.159   37.137  0.50 30.18 ? 252 LEU A N     1 
ATOM   3878  N  N     B LEU A 1 252 ? -17.594 0.292   37.021  0.50 29.95 ? 252 LEU A N     1 
ATOM   3879  C  CA    A LEU A 1 252 ? -16.197 0.624   36.575  0.50 29.50 ? 252 LEU A CA    1 
ATOM   3880  C  CA    B LEU A 1 252 ? -16.239 0.574   36.550  0.50 29.51 ? 252 LEU A CA    1 
ATOM   3881  C  C     A LEU A 1 252 ? -15.902 2.069   36.962  0.50 30.63 ? 252 LEU A C     1 
ATOM   3882  C  C     B LEU A 1 252 ? -15.762 1.952   36.995  0.50 30.50 ? 252 LEU A C     1 
ATOM   3883  O  O     A LEU A 1 252 ? -14.732 2.459   37.040  0.50 30.03 ? 252 LEU A O     1 
ATOM   3884  O  O     B LEU A 1 252 ? -14.582 2.129   37.317  0.50 30.05 ? 252 LEU A O     1 
ATOM   3885  C  CB    A LEU A 1 252 ? -16.206 0.471   35.053  0.50 24.43 ? 252 LEU A CB    1 
ATOM   3886  C  CB    B LEU A 1 252 ? -16.175 0.450   35.028  0.50 24.41 ? 252 LEU A CB    1 
ATOM   3887  C  CG    A LEU A 1 252 ? -16.488 -0.938  34.523  0.50 27.63 ? 252 LEU A CG    1 
ATOM   3888  C  CG    B LEU A 1 252 ? -16.254 -0.975  34.479  0.50 27.82 ? 252 LEU A CG    1 
ATOM   3889  C  CD1   A LEU A 1 252 ? -16.388 -0.977  33.004  0.50 30.17 ? 252 LEU A CD1   1 
ATOM   3890  C  CD1   B LEU A 1 252 ? -16.223 -0.970  32.960  0.50 30.21 ? 252 LEU A CD1   1 
ATOM   3891  C  CD2   A LEU A 1 252 ? -15.543 -1.953  35.154  0.50 26.57 ? 252 LEU A CD2   1 
ATOM   3892  C  CD2   B LEU A 1 252 ? -15.115 -1.815  35.035  0.50 25.09 ? 252 LEU A CD2   1 
ATOM   3893  N  N     A THR A 1 253 ? -16.939 2.876   37.201  0.50 31.67 ? 253 THR A N     1 
ATOM   3894  N  N     B THR A 1 253 ? -16.660 2.941   37.016  0.50 31.88 ? 253 THR A N     1 
ATOM   3895  C  CA    A THR A 1 253 ? -16.720 4.246   37.656  0.50 31.59 ? 253 THR A CA    1 
ATOM   3896  C  CA    B THR A 1 253 ? -16.270 4.282   37.442  0.50 27.08 ? 253 THR A CA    1 
ATOM   3897  C  C     A THR A 1 253 ? -15.981 4.272   38.990  0.50 31.58 ? 253 THR A C     1 
ATOM   3898  C  C     B THR A 1 253 ? -15.802 4.295   38.894  0.50 31.18 ? 253 THR A C     1 
ATOM   3899  O  O     A THR A 1 253 ? -15.082 5.096   39.197  0.50 28.09 ? 253 THR A O     1 
ATOM   3900  O  O     B THR A 1 253 ? -14.916 5.079   39.257  0.50 28.13 ? 253 THR A O     1 
ATOM   3901  C  CB    A THR A 1 253 ? -18.058 4.983   37.777  0.50 24.87 ? 253 THR A CB    1 
ATOM   3902  C  CB    B THR A 1 253 ? -17.439 5.253   37.236  0.50 31.50 ? 253 THR A CB    1 
ATOM   3903  O  OG1   A THR A 1 253 ? -18.645 5.137   36.480  0.50 38.22 ? 253 THR A OG1   1 
ATOM   3904  O  OG1   B THR A 1 253 ? -17.712 5.386   35.834  0.50 34.32 ? 253 THR A OG1   1 
ATOM   3905  C  CG2   A THR A 1 253 ? -17.871 6.352   38.407  0.50 29.31 ? 253 THR A CG2   1 
ATOM   3906  C  CG2   B THR A 1 253 ? -17.126 6.628   37.812  0.50 35.45 ? 253 THR A CG2   1 
ATOM   3907  N  N     A GLU A 1 254 ? -16.340 3.369   39.905  0.50 30.86 ? 254 GLU A N     1 
ATOM   3908  N  N     B GLU A 1 254 ? -16.368 3.427   39.738  0.50 30.81 ? 254 GLU A N     1 
ATOM   3909  C  CA    A GLU A 1 254 ? -15.771 3.409   41.246  0.50 32.28 ? 254 GLU A CA    1 
ATOM   3910  C  CA    B GLU A 1 254 ? -15.931 3.372   41.127  0.50 32.44 ? 254 GLU A CA    1 
ATOM   3911  C  C     A GLU A 1 254 ? -14.336 2.897   41.293  0.50 30.53 ? 254 GLU A C     1 
ATOM   3912  C  C     B GLU A 1 254 ? -14.520 2.816   41.270  0.50 30.42 ? 254 GLU A C     1 
ATOM   3913  O  O     A GLU A 1 254 ? -13.556 3.361   42.133  0.50 32.31 ? 254 GLU A O     1 
ATOM   3914  O  O     B GLU A 1 254 ? -13.875 3.077   42.289  0.50 31.42 ? 254 GLU A O     1 
ATOM   3915  C  CB    A GLU A 1 254 ? -16.639 2.610   42.214  0.50 30.35 ? 254 GLU A CB    1 
ATOM   3916  C  CB    B GLU A 1 254 ? -16.899 2.540   41.967  0.50 30.73 ? 254 GLU A CB    1 
ATOM   3917  C  CG    A GLU A 1 254 ? -16.379 2.968   43.661  0.50 35.12 ? 254 GLU A CG    1 
ATOM   3918  C  CG    B GLU A 1 254 ? -16.944 2.958   43.423  0.50 34.82 ? 254 GLU A CG    1 
ATOM   3919  C  CD    A GLU A 1 254 ? -17.187 2.131   44.623  0.50 30.76 ? 254 GLU A CD    1 
ATOM   3920  C  CD    B GLU A 1 254 ? -17.526 1.888   44.322  0.50 30.51 ? 254 GLU A CD    1 
ATOM   3921  O  OE1   A GLU A 1 254 ? -18.278 1.666   44.227  0.50 30.47 ? 254 GLU A OE1   1 
ATOM   3922  O  OE1   B GLU A 1 254 ? -18.551 1.279   43.941  0.50 28.47 ? 254 GLU A OE1   1 
ATOM   3923  O  OE2   A GLU A 1 254 ? -16.722 1.932   45.769  0.50 25.61 ? 254 GLU A OE2   1 
ATOM   3924  O  OE2   B GLU A 1 254 ? -16.946 1.651   45.406  0.50 29.06 ? 254 GLU A OE2   1 
ATOM   3925  N  N     A PHE A 1 255 ? -13.970 1.944   40.424  0.50 31.70 ? 255 PHE A N     1 
ATOM   3926  N  N     B PHE A 1 255 ? -14.029 2.051   40.288  0.50 31.58 ? 255 PHE A N     1 
ATOM   3927  C  CA    A PHE A 1 255 ? -12.562 1.577   40.285  0.50 27.03 ? 255 PHE A CA    1 
ATOM   3928  C  CA    B PHE A 1 255 ? -12.624 1.650   40.302  0.50 27.05 ? 255 PHE A CA    1 
ATOM   3929  C  C     A PHE A 1 255 ? -11.708 2.821   40.098  0.50 28.68 ? 255 PHE A C     1 
ATOM   3930  C  C     B PHE A 1 255 ? -11.714 2.871   40.255  0.50 28.77 ? 255 PHE A C     1 
ATOM   3931  O  O     A PHE A 1 255 ? -10.678 2.994   40.758  0.50 31.42 ? 255 PHE A O     1 
ATOM   3932  O  O     B PHE A 1 255 ? -10.775 2.995   41.048  0.50 31.12 ? 255 PHE A O     1 
ATOM   3933  C  CB    A PHE A 1 255 ? -12.369 0.625   39.102  0.50 27.93 ? 255 PHE A CB    1 
ATOM   3934  C  CB    B PHE A 1 255 ? -12.319 0.720   39.124  0.50 27.91 ? 255 PHE A CB    1 
ATOM   3935  C  CG    A PHE A 1 255 ? -12.586 -0.824  39.436  0.50 26.60 ? 255 PHE A CG    1 
ATOM   3936  C  CG    B PHE A 1 255 ? -12.656 -0.724  39.374  0.50 26.66 ? 255 PHE A CG    1 
ATOM   3937  C  CD1   A PHE A 1 255 ? -13.862 -1.361  39.462  0.50 32.05 ? 255 PHE A CD1   1 
ATOM   3938  C  CD1   B PHE A 1 255 ? -13.966 -1.171  39.301  0.50 32.35 ? 255 PHE A CD1   1 
ATOM   3939  C  CD2   A PHE A 1 255 ? -11.512 -1.655  39.704  0.50 29.57 ? 255 PHE A CD2   1 
ATOM   3940  C  CD2   B PHE A 1 255 ? -11.659 -1.639  39.663  0.50 29.42 ? 255 PHE A CD2   1 
ATOM   3941  C  CE1   A PHE A 1 255 ? -14.062 -2.695  39.758  0.50 28.76 ? 255 PHE A CE1   1 
ATOM   3942  C  CE1   B PHE A 1 255 ? -14.273 -2.504  39.521  0.50 28.44 ? 255 PHE A CE1   1 
ATOM   3943  C  CE2   A PHE A 1 255 ? -11.705 -2.989  40.002  0.50 28.38 ? 255 PHE A CE2   1 
ATOM   3944  C  CE2   B PHE A 1 255 ? -11.959 -2.970  39.883  0.50 28.64 ? 255 PHE A CE2   1 
ATOM   3945  C  CZ    A PHE A 1 255 ? -12.984 -3.509  40.027  0.50 30.13 ? 255 PHE A CZ    1 
ATOM   3946  C  CZ    B PHE A 1 255 ? -13.267 -3.402  39.812  0.50 29.24 ? 255 PHE A CZ    1 
ATOM   3947  N  N     A GLN A 1 256 ? -12.141 3.710   39.203  0.50 29.69 ? 256 GLN A N     1 
ATOM   3948  N  N     B GLN A 1 256 ? -11.995 3.795   39.334  0.50 29.34 ? 256 GLN A N     1 
ATOM   3949  C  CA    A GLN A 1 256 ? -11.454 4.982   39.018  0.50 33.02 ? 256 GLN A CA    1 
ATOM   3950  C  CA    B GLN A 1 256 ? -11.136 4.962   39.153  0.50 32.00 ? 256 GLN A CA    1 
ATOM   3951  C  C     A GLN A 1 256 ? -11.574 5.852   40.262  0.50 28.04 ? 256 GLN A C     1 
ATOM   3952  C  C     B GLN A 1 256 ? -11.235 5.908   40.341  0.50 27.35 ? 256 GLN A C     1 
ATOM   3953  O  O     A GLN A 1 256 ? -10.591 6.464   40.695  0.50 28.67 ? 256 GLN A O     1 
ATOM   3954  O  O     B GLN A 1 256 ? -10.218 6.414   40.828  0.50 28.76 ? 256 GLN A O     1 
ATOM   3955  C  CB    A GLN A 1 256 ? -12.025 5.700   37.794  0.50 28.48 ? 256 GLN A CB    1 
ATOM   3956  C  CB    B GLN A 1 256 ? -11.508 5.684   37.858  0.50 29.69 ? 256 GLN A CB    1 
ATOM   3957  C  CG    A GLN A 1 256 ? -11.241 6.911   37.339  0.50 36.69 ? 256 GLN A CG    1 
ATOM   3958  C  CG    B GLN A 1 256 ? -11.548 4.778   36.641  0.50 26.39 ? 256 GLN A CG    1 
ATOM   3959  C  CD    A GLN A 1 256 ? -11.597 7.317   35.922  0.50 35.75 ? 256 GLN A CD    1 
ATOM   3960  C  CD    B GLN A 1 256 ? -12.301 5.398   35.484  0.50 30.34 ? 256 GLN A CD    1 
ATOM   3961  O  OE1   A GLN A 1 256 ? -12.498 6.744   35.308  0.50 35.42 ? 256 GLN A OE1   1 
ATOM   3962  O  OE1   B GLN A 1 256 ? -11.952 6.480   35.011  0.50 32.39 ? 256 GLN A OE1   1 
ATOM   3963  N  NE2   A GLN A 1 256 ? -10.884 8.304   35.391  0.50 45.79 ? 256 GLN A NE2   1 
ATOM   3964  N  NE2   B GLN A 1 256 ? -13.343 4.716   35.021  0.50 29.09 ? 256 GLN A NE2   1 
ATOM   3965  N  N     A THR A 1 257 ? -12.769 5.903   40.857  0.50 29.32 ? 257 THR A N     1 
ATOM   3966  N  N     B THR A 1 257 ? -12.458 6.170   40.811  0.50 29.84 ? 257 THR A N     1 
ATOM   3967  C  CA    A THR A 1 257 ? -12.992 6.730   42.041  0.50 31.08 ? 257 THR A CA    1 
ATOM   3968  C  CA    B THR A 1 257 ? -12.639 7.020   41.985  0.50 30.67 ? 257 THR A CA    1 
ATOM   3969  C  C     A THR A 1 257 ? -12.069 6.328   43.186  0.50 31.41 ? 257 THR A C     1 
ATOM   3970  C  C     B THR A 1 257 ? -11.911 6.453   43.200  0.50 31.55 ? 257 THR A C     1 
ATOM   3971  O  O     A THR A 1 257 ? -11.471 7.184   43.849  0.50 34.27 ? 257 THR A O     1 
ATOM   3972  O  O     B THR A 1 257 ? -11.322 7.205   43.987  0.50 34.17 ? 257 THR A O     1 
ATOM   3973  C  CB    A THR A 1 257 ? -14.454 6.629   42.483  0.50 27.92 ? 257 THR A CB    1 
ATOM   3974  C  CB    B THR A 1 257 ? -14.132 7.185   42.282  0.50 31.36 ? 257 THR A CB    1 
ATOM   3975  O  OG1   A THR A 1 257 ? -15.306 7.122   41.442  0.50 29.15 ? 257 THR A OG1   1 
ATOM   3976  O  OG1   B THR A 1 257 ? -14.754 7.928   41.226  0.50 27.35 ? 257 THR A OG1   1 
ATOM   3977  C  CG2   A THR A 1 257 ? -14.687 7.438   43.749  0.50 35.71 ? 257 THR A CG2   1 
ATOM   3978  C  CG2   B THR A 1 257 ? -14.348 7.910   43.607  0.50 35.85 ? 257 THR A CG2   1 
ATOM   3979  N  N     A ASN A 1 258 ? -11.937 5.025   43.432  0.50 29.27 ? 258 ASN A N     1 
ATOM   3980  N  N     B ASN A 1 258 ? -11.923 5.129   43.362  0.50 29.40 ? 258 ASN A N     1 
ATOM   3981  C  CA    A ASN A 1 258 ? -11.212 4.566   44.612  0.50 27.34 ? 258 ASN A CA    1 
ATOM   3982  C  CA    B ASN A 1 258 ? -11.318 4.511   44.535  0.50 27.39 ? 258 ASN A CA    1 
ATOM   3983  C  C     A ASN A 1 258 ? -9.702  4.522   44.399  0.50 31.01 ? 258 ASN A C     1 
ATOM   3984  C  C     B ASN A 1 258 ? -9.821  4.273   44.392  0.50 30.50 ? 258 ASN A C     1 
ATOM   3985  O  O     A ASN A 1 258 ? -8.940  4.809   45.328  0.50 26.83 ? 258 ASN A O     1 
ATOM   3986  O  O     B ASN A 1 258 ? -9.124  4.191   45.410  0.50 28.37 ? 258 ASN A O     1 
ATOM   3987  C  CB    A ASN A 1 258 ? -11.723 3.188   45.032  0.50 30.58 ? 258 ASN A CB    1 
ATOM   3988  C  CB    B ASN A 1 258 ? -12.010 3.182   44.842  0.50 29.83 ? 258 ASN A CB    1 
ATOM   3989  C  CG    A ASN A 1 258 ? -13.033 3.258   45.795  0.50 29.83 ? 258 ASN A CG    1 
ATOM   3990  C  CG    B ASN A 1 258 ? -13.433 3.368   45.331  0.50 31.28 ? 258 ASN A CG    1 
ATOM   3991  O  OD1   A ASN A 1 258 ? -13.286 4.212   46.532  0.50 31.34 ? 258 ASN A OD1   1 
ATOM   3992  O  OD1   B ASN A 1 258 ? -13.816 4.458   45.754  0.50 29.17 ? 258 ASN A OD1   1 
ATOM   3993  N  ND2   A ASN A 1 258 ? -13.874 2.248   45.618  0.50 32.33 ? 258 ASN A ND2   1 
ATOM   3994  N  ND2   B ASN A 1 258 ? -14.222 2.302   45.278  0.50 31.99 ? 258 ASN A ND2   1 
ATOM   3995  N  N     A LEU A 1 259 ? -9.243  4.169   43.194  0.50 29.95 ? 259 LEU A N     1 
ATOM   3996  N  N     B LEU A 1 259 ? -9.304  4.156   43.167  0.50 29.95 ? 259 LEU A N     1 
ATOM   3997  C  CA    A LEU A 1 259 ? -7.844  3.813   43.001  0.50 30.84 ? 259 LEU A CA    1 
ATOM   3998  C  CA    B LEU A 1 259 ? -7.917  3.755   42.973  0.50 30.82 ? 259 LEU A CA    1 
ATOM   3999  C  C     A LEU A 1 259 ? -7.012  4.841   42.245  0.50 31.49 ? 259 LEU A C     1 
ATOM   4000  C  C     B LEU A 1 259 ? -7.100  4.673   42.075  0.50 31.28 ? 259 LEU A C     1 
ATOM   4001  O  O     A LEU A 1 259 ? -5.781  4.775   42.317  0.50 28.89 ? 259 LEU A O     1 
ATOM   4002  O  O     B LEU A 1 259 ? -5.880  4.495   42.004  0.50 28.29 ? 259 LEU A O     1 
ATOM   4003  C  CB    A LEU A 1 259 ? -7.737  2.469   42.264  0.50 30.06 ? 259 LEU A CB    1 
ATOM   4004  C  CB    B LEU A 1 259 ? -7.852  2.332   42.399  0.50 30.25 ? 259 LEU A CB    1 
ATOM   4005  C  CG    A LEU A 1 259 ? -8.182  1.234   43.046  0.50 27.96 ? 259 LEU A CG    1 
ATOM   4006  C  CG    B LEU A 1 259 ? -8.527  1.242   43.232  0.50 26.94 ? 259 LEU A CG    1 
ATOM   4007  C  CD1   A LEU A 1 259 ? -8.035  -0.014  42.186  0.50 26.22 ? 259 LEU A CD1   1 
ATOM   4008  C  CD1   B LEU A 1 259 ? -8.662  -0.032  42.408  0.50 27.52 ? 259 LEU A CD1   1 
ATOM   4009  C  CD2   A LEU A 1 259 ? -7.384  1.102   44.333  0.50 31.37 ? 259 LEU A CD2   1 
ATOM   4010  C  CD2   B LEU A 1 259 ? -7.745  0.979   44.508  0.50 31.25 ? 259 LEU A CD2   1 
ATOM   4011  N  N     A VAL A 1 260 ? -7.629  5.777   41.532  0.50 31.98 ? 260 VAL A N     1 
ATOM   4012  N  N     B VAL A 1 260 ? -7.709  5.640   41.399  0.50 31.51 ? 260 VAL A N     1 
ATOM   4013  C  CA    A VAL A 1 260 ? -6.863  6.641   40.632  0.50 27.05 ? 260 VAL A CA    1 
ATOM   4014  C  CA    B VAL A 1 260 ? -6.962  6.481   40.467  0.50 27.12 ? 260 VAL A CA    1 
ATOM   4015  C  C     A VAL A 1 260 ? -7.069  8.113   40.976  0.50 29.26 ? 260 VAL A C     1 
ATOM   4016  C  C     B VAL A 1 260 ? -7.115  7.949   40.853  0.50 29.36 ? 260 VAL A C     1 
ATOM   4017  O  O     A VAL A 1 260 ? -7.943  8.767   40.391  0.50 27.14 ? 260 VAL A O     1 
ATOM   4018  O  O     B VAL A 1 260 ? -8.114  8.586   40.488  0.50 28.10 ? 260 VAL A O     1 
ATOM   4019  C  CB    A VAL A 1 260 ? -7.236  6.368   39.166  0.50 29.24 ? 260 VAL A CB    1 
ATOM   4020  C  CB    B VAL A 1 260 ? -7.423  6.241   39.020  0.50 29.10 ? 260 VAL A CB    1 
ATOM   4021  C  CG1   A VAL A 1 260 ? -6.257  7.063   38.233  0.50 28.30 ? 260 VAL A CG1   1 
ATOM   4022  C  CG1   B VAL A 1 260 ? -6.506  6.967   38.059  0.50 28.31 ? 260 VAL A CG1   1 
ATOM   4023  C  CG2   A VAL A 1 260 ? -7.270  4.865   38.887  0.50 29.81 ? 260 VAL A CG2   1 
ATOM   4024  C  CG2   B VAL A 1 260 ? -7.445  4.738   38.709  0.50 29.20 ? 260 VAL A CG2   1 
ATOM   4025  N  N     A PRO A 1 261 ? -6.283  8.683   41.896  0.50 33.98 ? 261 PRO A N     1 
ATOM   4026  N  N     B PRO A 1 261 ? -6.150  8.534   41.568  0.50 33.54 ? 261 PRO A N     1 
ATOM   4027  C  CA    A PRO A 1 261 ? -6.441  10.120  42.190  0.50 35.10 ? 261 PRO A CA    1 
ATOM   4028  C  CA    B PRO A 1 261 ? -6.319  9.928   42.006  0.50 35.08 ? 261 PRO A CA    1 
ATOM   4029  C  C     A PRO A 1 261 ? -6.045  11.029  41.037  0.50 37.41 ? 261 PRO A C     1 
ATOM   4030  C  C     B PRO A 1 261 ? -6.174  10.942  40.885  0.50 37.45 ? 261 PRO A C     1 
ATOM   4031  O  O     A PRO A 1 261 ? -6.698  12.058  40.820  0.50 35.17 ? 261 PRO A O     1 
ATOM   4032  O  O     B PRO A 1 261 ? -6.730  12.045  40.984  0.50 35.09 ? 261 PRO A O     1 
ATOM   4033  C  CB    A PRO A 1 261 ? -5.542  10.327  43.419  0.50 38.22 ? 261 PRO A CB    1 
ATOM   4034  C  CB    B PRO A 1 261 ? -5.218  10.097  43.059  0.50 36.10 ? 261 PRO A CB    1 
ATOM   4035  C  CG    A PRO A 1 261 ? -4.593  9.169   43.410  0.50 35.14 ? 261 PRO A CG    1 
ATOM   4036  C  CG    B PRO A 1 261 ? -4.145  9.165   42.607  0.50 36.69 ? 261 PRO A CG    1 
ATOM   4037  C  CD    A PRO A 1 261 ? -5.357  8.021   42.831  0.50 34.25 ? 261 PRO A CD    1 
ATOM   4038  C  CD    B PRO A 1 261 ? -4.861  7.970   42.007  0.50 36.29 ? 261 PRO A CD    1 
ATOM   4039  N  N     A TYR A 1 262 ? -4.983  10.696  40.301  0.50 33.18 ? 262 TYR A N     1 
ATOM   4040  N  N     B TYR A 1 262 ? -5.428  10.612  39.834  0.50 35.83 ? 262 TYR A N     1 
ATOM   4041  C  CA    A TYR A 1 262 ? -4.627  11.443  39.105  0.50 36.79 ? 262 TYR A CA    1 
ATOM   4042  C  CA    B TYR A 1 262 ? -5.180  11.498  38.708  0.50 34.78 ? 262 TYR A CA    1 
ATOM   4043  C  C     A TYR A 1 262 ? -4.596  10.517  37.895  0.50 35.25 ? 262 TYR A C     1 
ATOM   4044  C  C     B TYR A 1 262 ? -5.039  10.641  37.460  0.50 35.32 ? 262 TYR A C     1 
ATOM   4045  O  O     A TYR A 1 262 ? -4.067  9.404   37.983  0.50 30.18 ? 262 TYR A O     1 
ATOM   4046  O  O     B TYR A 1 262 ? -4.629  9.478   37.558  0.50 35.20 ? 262 TYR A O     1 
ATOM   4047  C  CB    A TYR A 1 262 ? -3.270  12.143  39.261  0.50 36.02 ? 262 TYR A CB    1 
ATOM   4048  C  CB    B TYR A 1 262 ? -3.924  12.352  38.940  0.50 36.62 ? 262 TYR A CB    1 
ATOM   4049  C  CG    A TYR A 1 262 ? -3.348  13.379  40.126  0.50 37.17 ? 262 TYR A CG    1 
ATOM   4050  C  CG    B TYR A 1 262 ? -4.083  13.307  40.102  0.50 36.94 ? 262 TYR A CG    1 
ATOM   4051  C  CD1   A TYR A 1 262 ? -3.900  14.556  39.634  0.50 35.81 ? 262 TYR A CD1   1 
ATOM   4052  C  CD1   B TYR A 1 262 ? -4.736  14.523  39.937  0.50 38.56 ? 262 TYR A CD1   1 
ATOM   4053  C  CD2   A TYR A 1 262 ? -2.886  13.369  41.436  0.50 37.73 ? 262 TYR A CD2   1 
ATOM   4054  C  CD2   B TYR A 1 262 ? -3.605  12.984  41.369  0.50 38.27 ? 262 TYR A CD2   1 
ATOM   4055  C  CE1   A TYR A 1 262 ? -3.986  15.690  40.418  0.50 40.35 ? 262 TYR A CE1   1 
ATOM   4056  C  CE1   B TYR A 1 262 ? -4.897  15.399  40.994  0.50 35.80 ? 262 TYR A CE1   1 
ATOM   4057  C  CE2   A TYR A 1 262 ? -2.965  14.501  42.228  0.50 39.19 ? 262 TYR A CE2   1 
ATOM   4058  C  CE2   B TYR A 1 262 ? -3.765  13.852  42.436  0.50 35.60 ? 262 TYR A CE2   1 
ATOM   4059  C  CZ    A TYR A 1 262 ? -3.519  15.657  41.712  0.50 38.80 ? 262 TYR A CZ    1 
ATOM   4060  C  CZ    B TYR A 1 262 ? -4.410  15.058  42.237  0.50 34.63 ? 262 TYR A CZ    1 
ATOM   4061  O  OH    A TYR A 1 262 ? -3.606  16.788  42.486  0.50 41.89 ? 262 TYR A OH    1 
ATOM   4062  O  OH    B TYR A 1 262 ? -4.571  15.930  43.283  0.50 41.81 ? 262 TYR A OH    1 
ATOM   4063  N  N     A PRO A 1 263 ? -5.139  10.954  36.753  0.50 33.25 ? 263 PRO A N     1 
ATOM   4064  N  N     B PRO A 1 263 ? -5.363  11.181  36.279  0.50 33.93 ? 263 PRO A N     1 
ATOM   4065  C  CA    A PRO A 1 263 ? -5.460  9.999   35.677  0.50 34.61 ? 263 PRO A CA    1 
ATOM   4066  C  CA    B PRO A 1 263 ? -5.570  10.306  35.108  0.50 35.02 ? 263 PRO A CA    1 
ATOM   4067  C  C     A PRO A 1 263 ? -4.263  9.272   35.092  0.50 31.23 ? 263 PRO A C     1 
ATOM   4068  C  C     B PRO A 1 263 ? -4.354  9.498   34.685  0.50 32.18 ? 263 PRO A C     1 
ATOM   4069  O  O     A PRO A 1 263 ? -4.413  8.116   34.674  0.50 30.52 ? 263 PRO A O     1 
ATOM   4070  O  O     B PRO A 1 263 ? -4.517  8.339   34.278  0.50 29.86 ? 263 PRO A O     1 
ATOM   4071  C  CB    A PRO A 1 263 ? -6.149  10.882  34.625  0.50 39.81 ? 263 PRO A CB    1 
ATOM   4072  C  CB    B PRO A 1 263 ? -5.997  11.295  34.012  0.50 38.95 ? 263 PRO A CB    1 
ATOM   4073  C  CG    A PRO A 1 263 ? -6.669  12.059  35.400  0.50 40.58 ? 263 PRO A CG    1 
ATOM   4074  C  CG    B PRO A 1 263 ? -6.576  12.455  34.756  0.50 41.21 ? 263 PRO A CG    1 
ATOM   4075  C  CD    A PRO A 1 263 ? -5.637  12.308  36.459  0.50 38.41 ? 263 PRO A CD    1 
ATOM   4076  C  CD    B PRO A 1 263 ? -5.742  12.576  35.998  0.50 39.44 ? 263 PRO A CD    1 
ATOM   4077  N  N     A ARG A 1 264 ? -3.083  9.900   35.039  0.50 29.51 ? 264 ARG A N     1 
ATOM   4078  N  N     B ARG A 1 264 ? -3.144  10.065  34.759  0.50 28.20 ? 264 ARG A N     1 
ATOM   4079  C  CA    A ARG A 1 264 ? -1.931  9.245   34.422  0.50 28.99 ? 264 ARG A CA    1 
ATOM   4080  C  CA    B ARG A 1 264 ? -1.970  9.388   34.210  0.50 29.28 ? 264 ARG A CA    1 
ATOM   4081  C  C     A ARG A 1 264 ? -1.291  8.206   35.335  0.50 29.76 ? 264 ARG A C     1 
ATOM   4082  C  C     B ARG A 1 264 ? -1.479  8.253   35.101  0.50 29.69 ? 264 ARG A C     1 
ATOM   4083  O  O     A ARG A 1 264 ? -0.670  7.256   34.844  0.50 27.92 ? 264 ARG A O     1 
ATOM   4084  O  O     B ARG A 1 264 ? -1.003  7.229   34.598  0.50 31.04 ? 264 ARG A O     1 
ATOM   4085  C  CB    A ARG A 1 264 ? -0.883  10.281  34.011  0.50 27.51 ? 264 ARG A CB    1 
ATOM   4086  C  CB    B ARG A 1 264 ? -0.836  10.388  33.981  0.50 27.55 ? 264 ARG A CB    1 
ATOM   4087  C  CG    A ARG A 1 264 ? -1.234  11.059  32.754  0.50 31.54 ? 264 ARG A CG    1 
ATOM   4088  C  CG    B ARG A 1 264 ? -0.869  11.076  32.629  0.50 31.76 ? 264 ARG A CG    1 
ATOM   4089  C  CD    A ARG A 1 264 ? -0.249  12.198  32.514  0.50 31.36 ? 264 ARG A CD    1 
ATOM   4090  C  CD    B ARG A 1 264 ? 0.151   12.209  32.553  0.50 30.84 ? 264 ARG A CD    1 
ATOM   4091  N  NE    A ARG A 1 264 ? 1.116   11.724  32.316  0.50 28.44 ? 264 ARG A NE    1 
ATOM   4092  N  NE    B ARG A 1 264 ? 1.531   11.735  32.580  0.50 27.05 ? 264 ARG A NE    1 
ATOM   4093  C  CZ    A ARG A 1 264 ? 1.619   11.365  31.142  0.50 27.34 ? 264 ARG A CZ    1 
ATOM   4094  C  CZ    B ARG A 1 264 ? 2.229   11.404  31.501  0.50 28.28 ? 264 ARG A CZ    1 
ATOM   4095  N  NH1   A ARG A 1 264 ? 0.890   11.393  30.040  0.50 26.89 ? 264 ARG A NH1   1 
ATOM   4096  N  NH1   B ARG A 1 264 ? 1.698   11.463  30.292  0.50 22.97 ? 264 ARG A NH1   1 
ATOM   4097  N  NH2   A ARG A 1 264 ? 2.884   10.961  31.075  0.50 28.01 ? 264 ARG A NH2   1 
ATOM   4098  N  NH2   B ARG A 1 264 ? 3.491   11.006  31.639  0.50 30.78 ? 264 ARG A NH2   1 
ATOM   4099  N  N     A ILE A 1 265 ? -1.403  8.371   36.649  0.50 30.83 ? 265 ILE A N     1 
ATOM   4100  N  N     B ILE A 1 265 ? -1.549  8.422   36.418  0.50 30.77 ? 265 ILE A N     1 
ATOM   4101  C  CA    A ILE A 1 265 ? -0.833  7.401   37.575  0.50 29.55 ? 265 ILE A CA    1 
ATOM   4102  C  CA    B ILE A 1 265 ? -1.014  7.420   37.331  0.50 30.34 ? 265 ILE A CA    1 
ATOM   4103  C  C     A ILE A 1 265 ? -1.902  6.363   37.897  0.50 28.14 ? 265 ILE A C     1 
ATOM   4104  C  C     B ILE A 1 265 ? -2.115  6.423   37.672  0.50 28.91 ? 265 ILE A C     1 
ATOM   4105  O  O     A ILE A 1 265 ? -2.332  6.224   39.048  0.50 31.65 ? 265 ILE A O     1 
ATOM   4106  O  O     B ILE A 1 265 ? -2.563  6.335   38.821  0.50 30.21 ? 265 ILE A O     1 
ATOM   4107  C  CB    A ILE A 1 265 ? -0.280  8.092   38.838  0.50 32.71 ? 265 ILE A CB    1 
ATOM   4108  C  CB    B ILE A 1 265 ? -0.414  8.084   38.586  0.50 32.36 ? 265 ILE A CB    1 
ATOM   4109  C  CG1   A ILE A 1 265 ? -1.312  9.039   39.453  0.50 30.79 ? 265 ILE A CG1   1 
ATOM   4110  C  CG1   B ILE A 1 265 ? -1.364  9.139   39.156  0.50 30.51 ? 265 ILE A CG1   1 
ATOM   4111  C  CG2   A ILE A 1 265 ? 0.976   8.889   38.492  0.50 34.18 ? 265 ILE A CG2   1 
ATOM   4112  C  CG2   B ILE A 1 265 ? 0.926   8.734   38.246  0.50 33.94 ? 265 ILE A CG2   1 
ATOM   4113  C  CD1   A ILE A 1 265 ? -0.842  9.703   40.732  0.50 38.85 ? 265 ILE A CD1   1 
ATOM   4114  C  CD1   B ILE A 1 265 ? -0.814  9.858   40.370  0.50 38.54 ? 265 ILE A CD1   1 
ATOM   4115  N  N     A HIS A 1 266 ? -2.339  5.621   36.878  0.50 28.15 ? 266 HIS A N     1 
ATOM   4116  N  N     B HIS A 1 266 ? -2.560  5.660   36.672  0.50 28.31 ? 266 HIS A N     1 
ATOM   4117  C  CA    A HIS A 1 266 ? -3.488  4.730   36.996  0.50 28.88 ? 266 HIS A CA    1 
ATOM   4118  C  CA    B HIS A 1 266 ? -3.695  4.756   36.827  0.50 29.02 ? 266 HIS A CA    1 
ATOM   4119  C  C     A HIS A 1 266 ? -3.090  3.256   36.959  0.50 22.88 ? 266 HIS A C     1 
ATOM   4120  C  C     B HIS A 1 266 ? -3.265  3.292   36.834  0.50 23.01 ? 266 HIS A C     1 
ATOM   4121  O  O     A HIS A 1 266 ? -3.773  2.431   36.354  0.50 26.20 ? 266 HIS A O     1 
ATOM   4122  O  O     B HIS A 1 266 ? -3.922  2.433   36.246  0.50 26.27 ? 266 HIS A O     1 
ATOM   4123  C  CB    A HIS A 1 266 ? -4.529  5.036   35.915  0.50 27.71 ? 266 HIS A CB    1 
ATOM   4124  C  CB    B HIS A 1 266 ? -4.752  5.011   35.748  0.50 27.55 ? 266 HIS A CB    1 
ATOM   4125  C  CG    A HIS A 1 266 ? -4.041  4.878   34.503  0.50 28.82 ? 266 HIS A CG    1 
ATOM   4126  C  CG    B HIS A 1 266 ? -4.276  4.814   34.337  0.50 28.68 ? 266 HIS A CG    1 
ATOM   4127  N  ND1   A HIS A 1 266 ? -4.202  5.862   33.550  0.50 25.82 ? 266 HIS A ND1   1 
ATOM   4128  N  ND1   B HIS A 1 266 ? -4.217  5.845   33.423  0.50 25.73 ? 266 HIS A ND1   1 
ATOM   4129  C  CD2   A HIS A 1 266 ? -3.437  3.842   33.872  0.50 26.45 ? 266 HIS A CD2   1 
ATOM   4130  C  CD2   B HIS A 1 266 ? -3.888  3.701   33.669  0.50 27.08 ? 266 HIS A CD2   1 
ATOM   4131  C  CE1   A HIS A 1 266 ? -3.704  5.446   32.399  0.50 29.01 ? 266 HIS A CE1   1 
ATOM   4132  C  CE1   B HIS A 1 266 ? -3.788  5.380   32.262  0.50 28.88 ? 266 HIS A CE1   1 
ATOM   4133  N  NE2   A HIS A 1 266 ? -3.235  4.222   32.566  0.50 29.09 ? 266 HIS A NE2   1 
ATOM   4134  N  NE2   B HIS A 1 266 ? -3.584  4.081   32.384  0.50 26.54 ? 266 HIS A NE2   1 
ATOM   4135  N  N     A PHE A 1 267 ? -2.001  2.898   37.640  0.50 23.30 ? 267 PHE A N     1 
ATOM   4136  N  N     B PHE A 1 267 ? -2.175  2.981   37.541  0.50 23.15 ? 267 PHE A N     1 
ATOM   4137  C  CA    A PHE A 1 267 ? -1.475  1.534   37.627  0.50 23.50 ? 267 PHE A CA    1 
ATOM   4138  C  CA    B PHE A 1 267 ? -1.592  1.641   37.565  0.50 23.47 ? 267 PHE A CA    1 
ATOM   4139  C  C     A PHE A 1 267 ? -1.474  0.963   39.038  0.50 24.25 ? 267 PHE A C     1 
ATOM   4140  C  C     B PHE A 1 267 ? -1.533  1.140   39.004  0.50 24.55 ? 267 PHE A C     1 
ATOM   4141  O  O     A PHE A 1 267 ? -0.464  1.040   39.757  0.50 25.03 ? 267 PHE A O     1 
ATOM   4142  O  O     B PHE A 1 267 ? -0.494  1.247   39.674  0.50 25.41 ? 267 PHE A O     1 
ATOM   4143  C  CB    A PHE A 1 267 ? -0.086  1.504   37.002  0.50 23.87 ? 267 PHE A CB    1 
ATOM   4144  C  CB    B PHE A 1 267 ? -0.214  1.642   36.913  0.50 24.09 ? 267 PHE A CB    1 
ATOM   4145  C  CG    A PHE A 1 267 ? -0.072  1.997   35.590  0.50 26.23 ? 267 PHE A CG    1 
ATOM   4146  C  CG    B PHE A 1 267 ? -0.228  2.174   35.515  0.50 25.95 ? 267 PHE A CG    1 
ATOM   4147  C  CD1   A PHE A 1 267 ? -0.398  1.146   34.546  0.50 27.71 ? 267 PHE A CD1   1 
ATOM   4148  C  CD1   B PHE A 1 267 ? -0.482  1.330   34.446  0.50 27.86 ? 267 PHE A CD1   1 
ATOM   4149  C  CD2   A PHE A 1 267 ? 0.226   3.321   35.305  0.50 26.34 ? 267 PHE A CD2   1 
ATOM   4150  C  CD2   B PHE A 1 267 ? -0.020  3.523   35.268  0.50 25.91 ? 267 PHE A CD2   1 
ATOM   4151  C  CE1   A PHE A 1 267 ? -0.402  1.600   33.241  0.50 21.95 ? 267 PHE A CE1   1 
ATOM   4152  C  CE1   B PHE A 1 267 ? -0.508  1.817   33.156  0.50 21.95 ? 267 PHE A CE1   1 
ATOM   4153  C  CE2   A PHE A 1 267 ? 0.225   3.782   33.997  0.50 25.31 ? 267 PHE A CE2   1 
ATOM   4154  C  CE2   B PHE A 1 267 ? -0.044  4.018   33.976  0.50 25.05 ? 267 PHE A CE2   1 
ATOM   4155  C  CZ    A PHE A 1 267 ? -0.091  2.920   32.968  0.50 23.56 ? 267 PHE A CZ    1 
ATOM   4156  C  CZ    B PHE A 1 267 ? -0.290  3.164   32.922  0.50 22.92 ? 267 PHE A CZ    1 
ATOM   4157  N  N     A PRO A 1 268 ? -2.588  0.383   39.474  0.50 23.74 ? 268 PRO A N     1 
ATOM   4158  N  N     B PRO A 1 268 ? -2.624  0.577   39.506  0.50 23.63 ? 268 PRO A N     1 
ATOM   4159  C  CA    A PRO A 1 268 ? -2.645  -0.187  40.822  0.50 26.29 ? 268 PRO A CA    1 
ATOM   4160  C  CA    B PRO A 1 268 ? -2.619  0.049   40.869  0.50 26.25 ? 268 PRO A CA    1 
ATOM   4161  C  C     A PRO A 1 268 ? -1.780  -1.431  40.946  0.50 27.36 ? 268 PRO A C     1 
ATOM   4162  C  C     B PRO A 1 268 ? -1.942  -1.312  40.938  0.50 27.39 ? 268 PRO A C     1 
ATOM   4163  O  O     A PRO A 1 268 ? -1.502  -2.133  39.970  0.50 24.55 ? 268 PRO A O     1 
ATOM   4164  O  O     B PRO A 1 268 ? -1.833  -2.046  39.953  0.50 25.40 ? 268 PRO A O     1 
ATOM   4165  C  CB    A PRO A 1 268 ? -4.131  -0.523  41.003  0.50 24.00 ? 268 PRO A CB    1 
ATOM   4166  C  CB    B PRO A 1 268 ? -4.108  -0.052  41.224  0.50 23.82 ? 268 PRO A CB    1 
ATOM   4167  C  CG    A PRO A 1 268 ? -4.848  0.306   39.980  0.50 24.62 ? 268 PRO A CG    1 
ATOM   4168  C  CG    B PRO A 1 268 ? -4.852  0.012   39.916  0.50 25.48 ? 268 PRO A CG    1 
ATOM   4169  C  CD    A PRO A 1 268 ? -3.903  0.362   38.814  0.50 22.38 ? 268 PRO A CD    1 
ATOM   4170  C  CD    B PRO A 1 268 ? -3.874  0.265   38.796  0.50 22.32 ? 268 PRO A CD    1 
ATOM   4171  N  N     A LEU A 1 269 ? -1.353  -1.695  42.176  0.50 24.63 ? 269 LEU A N     1 
ATOM   4172  N  N     B LEU A 1 269 ? -1.468  -1.625  42.137  0.50 24.51 ? 269 LEU A N     1 
ATOM   4173  C  CA    A LEU A 1 269 ? -0.562  -2.870  42.518  0.50 20.81 ? 269 LEU A CA    1 
ATOM   4174  C  CA    B LEU A 1 269 ? -0.819  -2.894  42.427  0.50 21.58 ? 269 LEU A CA    1 
ATOM   4175  C  C     A LEU A 1 269 ? -1.450  -3.846  43.276  0.50 26.11 ? 269 LEU A C     1 
ATOM   4176  C  C     B LEU A 1 269 ? -1.837  -3.867  43.009  0.50 26.24 ? 269 LEU A C     1 
ATOM   4177  O  O     A LEU A 1 269 ? -1.977  -3.511  44.342  0.50 23.72 ? 269 LEU A O     1 
ATOM   4178  O  O     B LEU A 1 269 ? -2.742  -3.471  43.752  0.50 20.72 ? 269 LEU A O     1 
ATOM   4179  C  CB    A LEU A 1 269 ? 0.649   -2.479  43.363  0.50 23.58 ? 269 LEU A CB    1 
ATOM   4180  C  CB    B LEU A 1 269 ? 0.337   -2.692  43.408  0.50 22.60 ? 269 LEU A CB    1 
ATOM   4181  C  CG    A LEU A 1 269 ? 1.428   -3.625  44.007  0.50 24.12 ? 269 LEU A CG    1 
ATOM   4182  C  CG    B LEU A 1 269 ? 1.065   -3.931  43.925  0.50 21.35 ? 269 LEU A CG    1 
ATOM   4183  C  CD1   A LEU A 1 269 ? 2.081   -4.503  42.947  0.50 23.75 ? 269 LEU A CD1   1 
ATOM   4184  C  CD1   B LEU A 1 269 ? 1.821   -4.620  42.798  0.50 23.44 ? 269 LEU A CD1   1 
ATOM   4185  C  CD2   A LEU A 1 269 ? 2.469   -3.075  44.977  0.50 28.96 ? 269 LEU A CD2   1 
ATOM   4186  C  CD2   B LEU A 1 269 ? 2.003   -3.554  45.066  0.50 30.67 ? 269 LEU A CD2   1 
ATOM   4187  N  N     A ALA A 1 270 ? -1.620  -5.042  42.731  0.50 23.11 ? 270 ALA A N     1 
ATOM   4188  N  N     B ALA A 1 270 ? -1.693  -5.139  42.659  0.50 23.26 ? 270 ALA A N     1 
ATOM   4189  C  CA    A ALA A 1 270 ? -2.442  -6.063  43.364  0.50 21.59 ? 270 ALA A CA    1 
ATOM   4190  C  CA    B ALA A 1 270 ? -2.547  -6.197  43.182  0.50 22.24 ? 270 ALA A CA    1 
ATOM   4191  C  C     A ALA A 1 270 ? -1.572  -7.013  44.175  0.50 22.84 ? 270 ALA A C     1 
ATOM   4192  C  C     B ALA A 1 270 ? -1.696  -7.181  43.968  0.50 23.43 ? 270 ALA A C     1 
ATOM   4193  O  O     A ALA A 1 270 ? -0.493  -7.426  43.731  0.50 24.64 ? 270 ALA A O     1 
ATOM   4194  O  O     B ALA A 1 270 ? -0.614  -7.577  43.515  0.50 24.20 ? 270 ALA A O     1 
ATOM   4195  C  CB    A ALA A 1 270 ? -3.246  -6.845  42.325  0.50 26.88 ? 270 ALA A CB    1 
ATOM   4196  C  CB    B ALA A 1 270 ? -3.292  -6.917  42.054  0.50 26.68 ? 270 ALA A CB    1 
ATOM   4197  N  N     A THR A 1 271 ? -2.049  -7.341  45.372  0.50 23.75 ? 271 THR A N     1 
ATOM   4198  N  N     B THR A 1 271 ? -2.182  -7.564  45.144  0.50 24.14 ? 271 THR A N     1 
ATOM   4199  C  CA    A THR A 1 271 ? -1.432  -8.307  46.268  0.50 27.17 ? 271 THR A CA    1 
ATOM   4200  C  CA    B THR A 1 271 ? -1.543  -8.569  45.978  0.50 26.62 ? 271 THR A CA    1 
ATOM   4201  C  C     A THR A 1 271 ? -2.513  -9.295  46.688  0.50 22.73 ? 271 THR A C     1 
ATOM   4202  C  C     B THR A 1 271 ? -2.596  -9.593  46.377  0.50 24.48 ? 271 THR A C     1 
ATOM   4203  O  O     A THR A 1 271 ? -3.658  -8.900  46.911  0.50 24.98 ? 271 THR A O     1 
ATOM   4204  O  O     B THR A 1 271 ? -3.782  -9.273  46.462  0.50 24.19 ? 271 THR A O     1 
ATOM   4205  C  CB    A THR A 1 271 ? -0.826  -7.609  47.496  0.50 27.73 ? 271 THR A CB    1 
ATOM   4206  C  CB    B THR A 1 271 ? -0.903  -7.933  47.221  0.50 27.29 ? 271 THR A CB    1 
ATOM   4207  O  OG1   A THR A 1 271 ? -0.165  -6.403  47.083  0.50 28.74 ? 271 THR A OG1   1 
ATOM   4208  O  OG1   B THR A 1 271 ? -0.206  -6.740  46.838  0.50 29.44 ? 271 THR A OG1   1 
ATOM   4209  C  CG2   A THR A 1 271 ? 0.171   -8.513  48.200  0.50 26.76 ? 271 THR A CG2   1 
ATOM   4210  C  CG2   B THR A 1 271 ? 0.079   -8.891  47.872  0.50 28.61 ? 271 THR A CG2   1 
ATOM   4211  N  N     A TYR A 1 272 ? -2.160  -10.578 46.778  0.50 28.15 ? 272 TYR A N     1 
ATOM   4212  N  N     B TYR A 1 272 ? -2.165  -10.835 46.600  0.50 28.38 ? 272 TYR A N     1 
ATOM   4213  C  CA    A TYR A 1 272 ? -3.160  -11.623 46.964  0.50 26.08 ? 272 TYR A CA    1 
ATOM   4214  C  CA    B TYR A 1 272 ? -3.104  -11.921 46.845  0.50 26.92 ? 272 TYR A CA    1 
ATOM   4215  C  C     A TYR A 1 272 ? -2.622  -12.723 47.869  0.50 30.22 ? 272 TYR A C     1 
ATOM   4216  C  C     B TYR A 1 272 ? -2.543  -12.887 47.879  0.50 30.16 ? 272 TYR A C     1 
ATOM   4217  O  O     A TYR A 1 272 ? -1.472  -13.147 47.727  0.50 26.28 ? 272 TYR A O     1 
ATOM   4218  O  O     B TYR A 1 272 ? -1.342  -13.174 47.885  0.50 26.13 ? 272 TYR A O     1 
ATOM   4219  C  CB    A TYR A 1 272 ? -3.585  -12.214 45.610  0.50 27.49 ? 272 TYR A CB    1 
ATOM   4220  C  CB    B TYR A 1 272 ? -3.423  -12.675 45.545  0.50 28.46 ? 272 TYR A CB    1 
ATOM   4221  C  CG    A TYR A 1 272 ? -4.565  -13.360 45.707  0.50 28.27 ? 272 TYR A CG    1 
ATOM   4222  C  CG    B TYR A 1 272 ? -4.571  -13.649 45.673  0.50 28.44 ? 272 TYR A CG    1 
ATOM   4223  C  CD1   A TYR A 1 272 ? -5.914  -13.130 45.949  0.50 30.05 ? 272 TYR A CD1   1 
ATOM   4224  C  CD1   B TYR A 1 272 ? -4.361  -14.942 46.130  0.50 31.37 ? 272 TYR A CD1   1 
ATOM   4225  C  CD2   A TYR A 1 272 ? -4.142  -14.673 45.543  0.50 31.58 ? 272 TYR A CD2   1 
ATOM   4226  C  CD2   B TYR A 1 272 ? -5.864  -13.274 45.338  0.50 27.98 ? 272 TYR A CD2   1 
ATOM   4227  C  CE1   A TYR A 1 272 ? -6.810  -14.174 46.037  0.50 29.61 ? 272 TYR A CE1   1 
ATOM   4228  C  CE1   B TYR A 1 272 ? -5.406  -15.832 46.254  0.50 31.37 ? 272 TYR A CE1   1 
ATOM   4229  C  CE2   A TYR A 1 272 ? -5.032  -15.724 45.626  0.50 30.38 ? 272 TYR A CE2   1 
ATOM   4230  C  CE2   B TYR A 1 272 ? -6.916  -14.157 45.457  0.50 30.51 ? 272 TYR A CE2   1 
ATOM   4231  C  CZ    A TYR A 1 272 ? -6.365  -15.469 45.873  0.50 28.77 ? 272 TYR A CZ    1 
ATOM   4232  C  CZ    B TYR A 1 272 ? -6.682  -15.436 45.916  0.50 29.32 ? 272 TYR A CZ    1 
ATOM   4233  O  OH    A TYR A 1 272 ? -7.256  -16.515 45.959  0.50 37.04 ? 272 TYR A OH    1 
ATOM   4234  O  OH    B TYR A 1 272 ? -7.729  -16.324 46.039  0.50 37.03 ? 272 TYR A OH    1 
ATOM   4235  N  N     A ALA A 1 273 ? -3.470  -13.199 48.783  0.50 29.29 ? 273 ALA A N     1 
ATOM   4236  N  N     B ALA A 1 273 ? -3.425  -13.403 48.736  0.50 29.29 ? 273 ALA A N     1 
ATOM   4237  C  CA    A ALA A 1 273 ? -3.062  -14.201 49.758  0.50 30.07 ? 273 ALA A CA    1 
ATOM   4238  C  CA    B ALA A 1 273 ? -3.036  -14.345 49.777  0.50 30.07 ? 273 ALA A CA    1 
ATOM   4239  C  C     A ALA A 1 273 ? -4.298  -14.931 50.261  0.50 23.54 ? 273 ALA A C     1 
ATOM   4240  C  C     B ALA A 1 273 ? -4.273  -15.098 50.240  0.50 23.47 ? 273 ALA A C     1 
ATOM   4241  O  O     A ALA A 1 273 ? -5.382  -14.337 50.316  0.50 26.60 ? 273 ALA A O     1 
ATOM   4242  O  O     B ALA A 1 273 ? -5.372  -14.532 50.240  0.50 26.41 ? 273 ALA A O     1 
ATOM   4243  C  CB    A ALA A 1 273 ? -2.307  -13.552 50.927  0.50 25.48 ? 273 ALA A CB    1 
ATOM   4244  C  CB    B ALA A 1 273 ? -2.375  -13.620 50.958  0.50 25.50 ? 273 ALA A CB    1 
ATOM   4245  N  N     A PRO A 1 274 ? -4.173  -16.210 50.645  0.50 25.82 ? 274 PRO A N     1 
ATOM   4246  N  N     B PRO A 1 274 ? -4.134  -16.370 50.640  0.50 25.90 ? 274 PRO A N     1 
ATOM   4247  C  CA    A PRO A 1 274 ? -2.960  -17.038 50.635  0.50 24.43 ? 274 PRO A CA    1 
ATOM   4248  C  CA    B PRO A 1 274 ? -2.911  -17.180 50.653  0.50 24.45 ? 274 PRO A CA    1 
ATOM   4249  C  C     A PRO A 1 274 ? -2.825  -17.866 49.364  0.50 31.33 ? 274 PRO A C     1 
ATOM   4250  C  C     B PRO A 1 274 ? -2.776  -18.059 49.413  0.50 31.45 ? 274 PRO A C     1 
ATOM   4251  O  O     A PRO A 1 274 ? -3.817  -18.186 48.720  0.50 29.46 ? 274 PRO A O     1 
ATOM   4252  O  O     B PRO A 1 274 ? -3.768  -18.554 48.893  0.50 27.88 ? 274 PRO A O     1 
ATOM   4253  C  CB    A PRO A 1 274 ? -3.162  -17.924 51.866  0.50 29.62 ? 274 PRO A CB    1 
ATOM   4254  C  CB    B PRO A 1 274 ? -3.087  -18.016 51.923  0.50 29.58 ? 274 PRO A CB    1 
ATOM   4255  C  CG    A PRO A 1 274 ? -4.652  -18.175 51.863  0.50 30.65 ? 274 PRO A CG    1 
ATOM   4256  C  CG    B PRO A 1 274 ? -4.576  -18.278 51.958  0.50 30.86 ? 274 PRO A CG    1 
ATOM   4257  C  CD    A PRO A 1 274 ? -5.282  -16.896 51.338  0.50 26.83 ? 274 PRO A CD    1 
ATOM   4258  C  CD    B PRO A 1 274 ? -5.229  -17.041 51.369  0.50 26.77 ? 274 PRO A CD    1 
ATOM   4259  N  N     A VAL A 1 275 ? -1.602  -18.229 48.984  0.50 22.42 ? 275 VAL A N     1 
ATOM   4260  N  N     B VAL A 1 275 ? -1.560  -18.277 48.922  0.50 22.37 ? 275 VAL A N     1 
ATOM   4261  C  CA    A VAL A 1 275 ? -1.349  -19.125 47.863  0.50 28.60 ? 275 VAL A CA    1 
ATOM   4262  C  CA    B VAL A 1 275 ? -1.312  -19.178 47.804  0.50 28.63 ? 275 VAL A CA    1 
ATOM   4263  C  C     A VAL A 1 275 ? -0.699  -20.377 48.436  0.50 29.38 ? 275 VAL A C     1 
ATOM   4264  C  C     B VAL A 1 275 ? -0.711  -20.453 48.382  0.50 29.37 ? 275 VAL A C     1 
ATOM   4265  O  O     A VAL A 1 275 ? 0.428   -20.321 48.946  0.50 29.21 ? 275 VAL A O     1 
ATOM   4266  O  O     B VAL A 1 275 ? 0.388   -20.432 48.947  0.50 29.20 ? 275 VAL A O     1 
ATOM   4267  C  CB    A VAL A 1 275 ? -0.465  -18.474 46.793  0.50 30.86 ? 275 VAL A CB    1 
ATOM   4268  C  CB    B VAL A 1 275 ? -0.394  -18.535 46.756  0.50 30.87 ? 275 VAL A CB    1 
ATOM   4269  C  CG1   A VAL A 1 275 ? -0.033  -19.500 45.770  0.50 33.48 ? 275 VAL A CG1   1 
ATOM   4270  C  CG1   B VAL A 1 275 ? -0.005  -19.550 45.704  0.50 33.53 ? 275 VAL A CG1   1 
ATOM   4271  C  CG2   A VAL A 1 275 ? -1.213  -17.332 46.123  0.50 32.91 ? 275 VAL A CG2   1 
ATOM   4272  C  CG2   B VAL A 1 275 ? -1.086  -17.343 46.118  0.50 32.97 ? 275 VAL A CG2   1 
ATOM   4273  N  N     A ILE A 1 276 ? -1.412  -21.501 48.377  0.50 30.29 ? 276 ILE A N     1 
ATOM   4274  N  N     B ILE A 1 276 ? -1.440  -21.564 48.267  0.50 30.26 ? 276 ILE A N     1 
ATOM   4275  C  CA    A ILE A 1 276 ? -0.998  -22.737 49.030  0.50 29.27 ? 276 ILE A CA    1 
ATOM   4276  C  CA    B ILE A 1 276 ? -1.076  -22.819 48.913  0.50 29.23 ? 276 ILE A CA    1 
ATOM   4277  C  C     A ILE A 1 276 ? -1.183  -23.892 48.055  0.50 29.30 ? 276 ILE A C     1 
ATOM   4278  C  C     B ILE A 1 276 ? -1.123  -23.943 47.888  0.50 29.34 ? 276 ILE A C     1 
ATOM   4279  O  O     A ILE A 1 276 ? -2.244  -24.020 47.433  0.50 33.15 ? 276 ILE A O     1 
ATOM   4280  O  O     B ILE A 1 276 ? -2.045  -24.011 47.067  0.50 32.64 ? 276 ILE A O     1 
ATOM   4281  C  CB    A ILE A 1 276 ? -1.794  -22.986 50.326  0.50 27.47 ? 276 ILE A CB    1 
ATOM   4282  C  CB    B ILE A 1 276 ? -2.011  -23.129 50.102  0.50 28.34 ? 276 ILE A CB    1 
ATOM   4283  C  CG1   A ILE A 1 276 ? -1.556  -21.850 51.324  0.50 29.15 ? 276 ILE A CG1   1 
ATOM   4284  C  CG1   B ILE A 1 276 ? -2.112  -21.923 51.037  0.50 29.43 ? 276 ILE A CG1   1 
ATOM   4285  C  CG2   A ILE A 1 276 ? -1.421  -24.327 50.935  0.50 32.42 ? 276 ILE A CG2   1 
ATOM   4286  C  CG2   B ILE A 1 276 ? -1.523  -24.355 50.860  0.50 32.38 ? 276 ILE A CG2   1 
ATOM   4287  C  CD1   A ILE A 1 276 ? -2.402  -21.944 52.578  0.50 37.65 ? 276 ILE A CD1   1 
ATOM   4288  C  CD1   B ILE A 1 276 ? -3.135  -22.093 52.147  0.50 35.24 ? 276 ILE A CD1   1 
ATOM   4289  N  N     A SER A 1 277 ? -0.158  -24.733 47.934  0.50 26.37 ? 277 SER A N     1 
ATOM   4290  N  N     B SER A 1 277 ? -0.130  -24.827 47.939  0.50 26.38 ? 277 SER A N     1 
ATOM   4291  C  CA    A SER A 1 277 ? -0.178  -25.827 46.973  0.50 28.87 ? 277 SER A CA    1 
ATOM   4292  C  CA    B SER A 1 277 ? -0.085  -25.956 47.020  0.50 28.94 ? 277 SER A CA    1 
ATOM   4293  C  C     A SER A 1 277 ? -1.309  -26.807 47.265  0.50 33.54 ? 277 SER A C     1 
ATOM   4294  C  C     B SER A 1 277 ? -1.257  -26.900 47.255  0.50 33.61 ? 277 SER A C     1 
ATOM   4295  O  O     A SER A 1 277 ? -1.660  -27.063 48.421  0.50 33.62 ? 277 SER A O     1 
ATOM   4296  O  O     B SER A 1 277 ? -1.656  -27.151 48.397  0.50 33.61 ? 277 SER A O     1 
ATOM   4297  C  CB    A SER A 1 277 ? 1.160   -26.570 46.984  0.50 32.12 ? 277 SER A CB    1 
ATOM   4298  C  CB    B SER A 1 277 ? 1.234   -26.717 47.177  0.50 31.74 ? 277 SER A CB    1 
ATOM   4299  O  OG    A SER A 1 277 ? 1.107   -27.732 46.171  0.50 32.11 ? 277 SER A OG    1 
ATOM   4300  O  OG    B SER A 1 277 ? 1.227   -27.912 46.414  0.50 32.77 ? 277 SER A OG    1 
ATOM   4301  N  N     A ALA A 1 278 ? -1.870  -27.373 46.191  0.50 35.37 ? 278 ALA A N     1 
ATOM   4302  N  N     B ALA A 1 278 ? -1.802  -27.438 46.159  0.50 35.36 ? 278 ALA A N     1 
ATOM   4303  C  CA    A ALA A 1 278 ? -2.933  -28.361 46.333  0.50 34.50 ? 278 ALA A CA    1 
ATOM   4304  C  CA    B ALA A 1 278 ? -2.886  -28.408 46.267  0.50 34.48 ? 278 ALA A CA    1 
ATOM   4305  C  C     A ALA A 1 278 ? -2.447  -29.648 46.985  0.50 39.78 ? 278 ALA A C     1 
ATOM   4306  C  C     B ALA A 1 278 ? -2.436  -29.706 46.923  0.50 39.77 ? 278 ALA A C     1 
ATOM   4307  O  O     A ALA A 1 278 ? -3.269  -30.414 47.499  0.50 38.36 ? 278 ALA A O     1 
ATOM   4308  O  O     B ALA A 1 278 ? -3.278  -30.444 47.446  0.50 38.36 ? 278 ALA A O     1 
ATOM   4309  C  CB    A ALA A 1 278 ? -3.557  -28.674 44.973  0.50 32.89 ? 278 ALA A CB    1 
ATOM   4310  C  CB    B ALA A 1 278 ? -3.483  -28.702 44.890  0.50 32.99 ? 278 ALA A CB    1 
ATOM   4311  N  N     A GLU A 1 279 ? -1.137  -29.908 46.979  0.50 35.25 ? 279 GLU A N     1 
ATOM   4312  N  N     B GLU A 1 279 ? -1.134  -30.002 46.909  0.50 35.26 ? 279 GLU A N     1 
ATOM   4313  C  CA    A GLU A 1 279 ? -0.619  -31.083 47.670  0.50 41.24 ? 279 GLU A CA    1 
ATOM   4314  C  CA    B GLU A 1 279 ? -0.634  -31.166 47.630  0.50 41.28 ? 279 GLU A CA    1 
ATOM   4315  C  C     A GLU A 1 279 ? -0.712  -30.947 49.183  0.50 41.89 ? 279 GLU A C     1 
ATOM   4316  C  C     B GLU A 1 279 ? -0.754  -31.001 49.138  0.50 41.91 ? 279 GLU A C     1 
ATOM   4317  O  O     A GLU A 1 279 ? -0.585  -31.950 49.892  0.50 41.74 ? 279 GLU A O     1 
ATOM   4318  O  O     B GLU A 1 279 ? -0.726  -32.000 49.864  0.50 41.78 ? 279 GLU A O     1 
ATOM   4319  C  CB    A GLU A 1 279 ? 0.827   -31.352 47.251  0.50 43.18 ? 279 GLU A CB    1 
ATOM   4320  C  CB    B GLU A 1 279 ? 0.823   -31.440 47.251  0.50 43.17 ? 279 GLU A CB    1 
ATOM   4321  C  CG    A GLU A 1 279 ? 0.966   -31.851 45.823  0.50 49.99 ? 279 GLU A CG    1 
ATOM   4322  C  CG    B GLU A 1 279 ? 1.043   -31.813 45.792  0.50 50.07 ? 279 GLU A CG    1 
ATOM   4323  C  CD    A GLU A 1 279 ? 0.287   -33.192 45.601  0.50 51.83 ? 279 GLU A CD    1 
ATOM   4324  C  CD    B GLU A 1 279 ? 0.566   -33.216 45.456  0.50 52.35 ? 279 GLU A CD    1 
ATOM   4325  O  OE1   A GLU A 1 279 ? 0.602   -34.152 46.337  0.50 52.64 ? 279 GLU A OE1   1 
ATOM   4326  O  OE1   B GLU A 1 279 ? -0.663  -33.437 45.392  0.50 52.39 ? 279 GLU A OE1   1 
ATOM   4327  O  OE2   A GLU A 1 279 ? -0.568  -33.283 44.692  0.50 51.56 ? 279 GLU A OE2   1 
ATOM   4328  O  OE2   B GLU A 1 279 ? 1.424   -34.101 45.257  0.50 54.96 ? 279 GLU A OE2   1 
ATOM   4329  N  N     A LYS A 1 280 ? -0.928  -29.737 49.690  0.50 39.74 ? 280 LYS A N     1 
ATOM   4330  N  N     B LYS A 1 280 ? -0.886  -29.770 49.621  0.50 39.67 ? 280 LYS A N     1 
ATOM   4331  C  CA    A LYS A 1 280 ? -1.179  -29.518 51.115  0.50 43.66 ? 280 LYS A CA    1 
ATOM   4332  C  CA    B LYS A 1 280 ? -1.074  -29.498 51.046  0.50 43.75 ? 280 LYS A CA    1 
ATOM   4333  C  C     A LYS A 1 280 ? -2.681  -29.390 51.372  0.50 41.07 ? 280 LYS A C     1 
ATOM   4334  C  C     B LYS A 1 280 ? -2.543  -29.196 51.337  0.50 41.03 ? 280 LYS A C     1 
ATOM   4335  O  O     A LYS A 1 280 ? -3.181  -28.357 51.812  0.50 42.81 ? 280 LYS A O     1 
ATOM   4336  O  O     B LYS A 1 280 ? -2.918  -28.096 51.740  0.50 43.78 ? 280 LYS A O     1 
ATOM   4337  C  CB    A LYS A 1 280 ? -0.425  -28.283 51.601  0.50 42.86 ? 280 LYS A CB    1 
ATOM   4338  C  CB    B LYS A 1 280 ? -0.170  -28.349 51.482  0.50 43.17 ? 280 LYS A CB    1 
ATOM   4339  C  CG    A LYS A 1 280 ? 1.081   -28.328 51.378  0.50 40.57 ? 280 LYS A CG    1 
ATOM   4340  C  CG    B LYS A 1 280 ? 1.309   -28.604 51.234  0.50 39.36 ? 280 LYS A CG    1 
ATOM   4341  C  CD    A LYS A 1 280 ? 1.746   -27.047 51.872  0.50 43.92 ? 280 LYS A CD    1 
ATOM   4342  C  CD    B LYS A 1 280 ? 1.976   -29.230 52.450  0.50 45.00 ? 280 LYS A CD    1 
ATOM   4343  C  CE    A LYS A 1 280 ? 3.255   -27.082 51.672  0.50 43.49 ? 280 LYS A CE    1 
ATOM   4344  C  CE    B LYS A 1 280 ? 2.060   -28.235 53.600  0.50 51.75 ? 280 LYS A CE    1 
ATOM   4345  N  NZ    A LYS A 1 280 ? 3.899   -25.770 51.989  0.50 35.08 ? 280 LYS A NZ    1 
ATOM   4346  N  NZ    B LYS A 1 280 ? 2.777   -28.794 54.780  0.50 48.69 ? 280 LYS A NZ    1 
ATOM   4347  N  N     A ALA A 1 281 ? -3.404  -30.475 51.083  0.50 44.02 ? 281 ALA A N     1 
ATOM   4348  N  N     B ALA A 1 281 ? -3.383  -30.211 51.116  0.50 43.98 ? 281 ALA A N     1 
ATOM   4349  C  CA    A ALA A 1 281 ? -4.859  -30.462 51.208  0.50 44.00 ? 281 ALA A CA    1 
ATOM   4350  C  CA    B ALA A 1 281 ? -4.823  -30.038 51.283  0.50 44.70 ? 281 ALA A CA    1 
ATOM   4351  C  C     A ALA A 1 281 ? -5.326  -30.310 52.649  0.50 48.85 ? 281 ALA A C     1 
ATOM   4352  C  C     B ALA A 1 281 ? -5.189  -29.791 52.741  0.50 48.57 ? 281 ALA A C     1 
ATOM   4353  O  O     A ALA A 1 281 ? -6.469  -29.896 52.876  0.50 42.08 ? 281 ALA A O     1 
ATOM   4354  O  O     B ALA A 1 281 ? -5.970  -28.884 53.053  0.50 44.92 ? 281 ALA A O     1 
ATOM   4355  C  CB    A ALA A 1 281 ? -5.454  -31.737 50.610  0.50 40.26 ? 281 ALA A CB    1 
ATOM   4356  C  CB    B ALA A 1 281 ? -5.564  -31.263 50.747  0.50 39.74 ? 281 ALA A CB    1 
ATOM   4357  N  N     A TYR A 1 282 ? -4.478  -30.632 53.624  0.50 47.18 ? 282 TYR A N     1 
ATOM   4358  N  N     B TYR A 1 282 ? -4.636  -30.591 53.651  0.50 47.26 ? 282 TYR A N     1 
ATOM   4359  C  CA    A TYR A 1 282 ? -4.842  -30.567 55.032  0.50 46.93 ? 282 TYR A CA    1 
ATOM   4360  C  CA    B TYR A 1 282 ? -4.963  -30.498 55.065  0.50 46.94 ? 282 TYR A CA    1 
ATOM   4361  C  C     A TYR A 1 282 ? -4.182  -29.389 55.738  0.50 48.72 ? 282 TYR A C     1 
ATOM   4362  C  C     B TYR A 1 282 ? -4.116  -29.467 55.793  0.50 48.73 ? 282 TYR A C     1 
ATOM   4363  O  O     A TYR A 1 282 ? -3.946  -29.432 56.949  0.50 45.69 ? 282 TYR A O     1 
ATOM   4364  O  O     B TYR A 1 282 ? -3.959  -29.554 57.018  0.50 45.66 ? 282 TYR A O     1 
ATOM   4365  C  CB    A TYR A 1 282 ? -4.496  -31.880 55.727  0.50 41.58 ? 282 TYR A CB    1 
ATOM   4366  C  CB    B TYR A 1 282 ? -4.843  -31.877 55.715  0.50 42.09 ? 282 TYR A CB    1 
ATOM   4367  C  CG    A TYR A 1 282 ? -5.478  -32.978 55.407  0.50 41.62 ? 282 TYR A CG    1 
ATOM   4368  C  CG    B TYR A 1 282 ? -5.958  -32.786 55.262  0.50 42.02 ? 282 TYR A CG    1 
ATOM   4369  C  CD1   A TYR A 1 282 ? -5.316  -33.779 54.284  0.50 40.11 ? 282 TYR A CD1   1 
ATOM   4370  C  CD1   B TYR A 1 282 ? -7.172  -32.813 55.942  0.50 42.66 ? 282 TYR A CD1   1 
ATOM   4371  C  CD2   A TYR A 1 282 ? -6.581  -33.202 56.225  0.50 42.65 ? 282 TYR A CD2   1 
ATOM   4372  C  CD2   B TYR A 1 282 ? -5.818  -33.582 54.132  0.50 40.11 ? 282 TYR A CD2   1 
ATOM   4373  C  CE1   A TYR A 1 282 ? -6.220  -34.781 53.992  0.50 36.80 ? 282 TYR A CE1   1 
ATOM   4374  C  CE1   B TYR A 1 282 ? -8.206  -33.622 55.526  0.50 37.89 ? 282 TYR A CE1   1 
ATOM   4375  C  CE2   A TYR A 1 282 ? -7.486  -34.198 55.944  0.50 40.00 ? 282 TYR A CE2   1 
ATOM   4376  C  CE2   B TYR A 1 282 ? -6.846  -34.398 53.708  0.50 37.82 ? 282 TYR A CE2   1 
ATOM   4377  C  CZ    A TYR A 1 282 ? -7.303  -34.985 54.827  0.50 39.86 ? 282 TYR A CZ    1 
ATOM   4378  C  CZ    B TYR A 1 282 ? -8.038  -34.414 54.410  0.50 37.10 ? 282 TYR A CZ    1 
ATOM   4379  O  OH    A TYR A 1 282 ? -8.211  -35.976 54.549  0.50 33.61 ? 282 TYR A OH    1 
ATOM   4380  O  OH    B TYR A 1 282 ? -9.067  -35.218 53.995  0.50 35.54 ? 282 TYR A OH    1 
ATOM   4381  N  N     A HIS A 1 283 ? -3.897  -28.330 54.987  0.50 45.21 ? 283 HIS A N     1 
ATOM   4382  N  N     B HIS A 1 283 ? -3.581  -28.490 55.063  0.50 45.75 ? 283 HIS A N     1 
ATOM   4383  C  CA    A HIS A 1 283 ? -3.280  -27.142 55.555  0.50 44.80 ? 283 HIS A CA    1 
ATOM   4384  C  CA    B HIS A 1 283 ? -2.889  -27.369 55.675  0.50 45.09 ? 283 HIS A CA    1 
ATOM   4385  C  C     A HIS A 1 283 ? -4.150  -26.556 56.658  0.50 46.95 ? 283 HIS A C     1 
ATOM   4386  C  C     B HIS A 1 283 ? -3.790  -26.676 56.688  0.50 46.05 ? 283 HIS A C     1 
ATOM   4387  O  O     A HIS A 1 283 ? -5.382  -26.571 56.578  0.50 49.53 ? 283 HIS A O     1 
ATOM   4388  O  O     B HIS A 1 283 ? -5.012  -26.608 56.523  0.50 49.76 ? 283 HIS A O     1 
ATOM   4389  C  CB    A HIS A 1 283 ? -3.056  -26.099 54.459  0.50 45.18 ? 283 HIS A CB    1 
ATOM   4390  C  CB    B HIS A 1 283 ? -2.456  -26.369 54.600  0.50 45.21 ? 283 HIS A CB    1 
ATOM   4391  C  CG    A HIS A 1 283 ? -4.323  -25.623 53.815  0.50 43.72 ? 283 HIS A CG    1 
ATOM   4392  C  CG    B HIS A 1 283 ? -3.601  -25.760 53.852  0.50 42.36 ? 283 HIS A CG    1 
ATOM   4393  N  ND1   A HIS A 1 283 ? -5.191  -24.749 54.434  0.50 43.60 ? 283 HIS A ND1   1 
ATOM   4394  N  ND1   B HIS A 1 283 ? -4.071  -26.273 52.662  0.50 45.56 ? 283 HIS A ND1   1 
ATOM   4395  C  CD2   A HIS A 1 283 ? -4.875  -25.910 52.611  0.50 43.73 ? 283 HIS A CD2   1 
ATOM   4396  C  CD2   B HIS A 1 283 ? -4.379  -24.686 54.130  0.50 43.26 ? 283 HIS A CD2   1 
ATOM   4397  C  CE1   A HIS A 1 283 ? -6.219  -24.514 53.638  0.50 39.39 ? 283 HIS A CE1   1 
ATOM   4398  C  CE1   B HIS A 1 283 ? -5.085  -25.541 52.237  0.50 41.96 ? 283 HIS A CE1   1 
ATOM   4399  N  NE2   A HIS A 1 283 ? -6.051  -25.206 52.526  0.50 40.59 ? 283 HIS A NE2   1 
ATOM   4400  N  NE2   B HIS A 1 283 ? -5.293  -24.572 53.111  0.50 44.02 ? 283 HIS A NE2   1 
ATOM   4401  N  N     A GLU A 1 284 ? -3.499  -26.046 57.700  0.50 50.52 ? 284 GLU A N     1 
ATOM   4402  N  N     B GLU A 1 284 ? -3.175  -26.168 57.750  0.50 50.38 ? 284 GLU A N     1 
ATOM   4403  C  CA    A GLU A 1 284 ? -4.196  -25.226 58.679  0.50 48.30 ? 284 GLU A CA    1 
ATOM   4404  C  CA    B GLU A 1 284 ? -3.899  -25.343 58.705  0.50 49.03 ? 284 GLU A CA    1 
ATOM   4405  C  C     A GLU A 1 284 ? -4.740  -23.974 58.002  0.50 47.32 ? 284 GLU A C     1 
ATOM   4406  C  C     B GLU A 1 284 ? -4.401  -24.079 58.019  0.50 47.46 ? 284 GLU A C     1 
ATOM   4407  O  O     A GLU A 1 284 ? -4.117  -23.421 57.091  0.50 50.92 ? 284 GLU A O     1 
ATOM   4408  O  O     B GLU A 1 284 ? -3.749  -23.531 57.126  0.50 51.66 ? 284 GLU A O     1 
ATOM   4409  C  CB    A GLU A 1 284 ? -3.251  -24.854 59.822  0.50 52.79 ? 284 GLU A CB    1 
ATOM   4410  C  CB    B GLU A 1 284 ? -2.998  -24.989 59.891  0.50 52.92 ? 284 GLU A CB    1 
ATOM   4411  C  CG    A GLU A 1 284 ? -1.774  -24.905 59.444  0.50 53.27 ? 284 GLU A CG    1 
ATOM   4412  C  CG    B GLU A 1 284 ? -1.776  -24.128 59.548  0.50 54.47 ? 284 GLU A CG    1 
ATOM   4413  C  CD    A GLU A 1 284 ? -1.402  -23.894 58.374  0.50 55.80 ? 284 GLU A CD    1 
ATOM   4414  C  CD    B GLU A 1 284 ? -0.692  -24.878 58.782  0.50 54.19 ? 284 GLU A CD    1 
ATOM   4415  O  OE1   A GLU A 1 284 ? -1.439  -22.679 58.661  0.50 57.26 ? 284 GLU A OE1   1 
ATOM   4416  O  OE1   B GLU A 1 284 ? -0.865  -26.085 58.508  0.50 52.35 ? 284 GLU A OE1   1 
ATOM   4417  O  OE2   A GLU A 1 284 ? -1.084  -24.316 57.241  0.50 49.94 ? 284 GLU A OE2   1 
ATOM   4418  O  OE2   B GLU A 1 284 ? 0.335   -24.253 58.447  0.50 57.53 ? 284 GLU A OE2   1 
ATOM   4419  N  N     A GLN A 1 285 ? -5.917  -23.533 58.437  0.50 49.05 ? 285 GLN A N     1 
ATOM   4420  N  N     B GLN A 1 285 ? -5.580  -23.622 58.431  0.50 48.44 ? 285 GLN A N     1 
ATOM   4421  C  CA    A GLN A 1 285 ? -6.592  -22.398 57.816  0.50 46.17 ? 285 GLN A CA    1 
ATOM   4422  C  CA    B GLN A 1 285 ? -6.180  -22.452 57.809  0.50 47.26 ? 285 GLN A CA    1 
ATOM   4423  C  C     A GLN A 1 285 ? -6.107  -21.113 58.479  0.50 46.65 ? 285 GLN A C     1 
ATOM   4424  C  C     B GLN A 1 285 ? -5.614  -21.176 58.419  0.50 46.71 ? 285 GLN A C     1 
ATOM   4425  O  O     A GLN A 1 285 ? -6.376  -20.874 59.661  0.50 40.92 ? 285 GLN A O     1 
ATOM   4426  O  O     B GLN A 1 285 ? -5.287  -21.121 59.608  0.50 49.19 ? 285 GLN A O     1 
ATOM   4427  C  CB    A GLN A 1 285 ? -8.108  -22.545 57.924  0.50 48.01 ? 285 GLN A CB    1 
ATOM   4428  C  CB    B GLN A 1 285 ? -7.702  -22.482 57.955  0.50 47.47 ? 285 GLN A CB    1 
ATOM   4429  C  CG    A GLN A 1 285 ? -8.669  -23.781 57.226  0.50 42.06 ? 285 GLN A CG    1 
ATOM   4430  C  CG    B GLN A 1 285 ? -8.363  -23.718 57.347  0.50 42.05 ? 285 GLN A CG    1 
ATOM   4431  C  CD    A GLN A 1 285 ? -8.675  -23.668 55.708  0.50 46.30 ? 285 GLN A CD    1 
ATOM   4432  C  CD    B GLN A 1 285 ? -8.383  -23.707 55.824  0.50 46.62 ? 285 GLN A CD    1 
ATOM   4433  O  OE1   A GLN A 1 285 ? -8.364  -22.618 55.142  0.50 38.74 ? 285 GLN A OE1   1 
ATOM   4434  O  OE1   B GLN A 1 285 ? -8.179  -22.670 55.189  0.50 39.09 ? 285 GLN A OE1   1 
ATOM   4435  N  NE2   A GLN A 1 285 ? -9.038  -24.759 55.041  0.50 45.72 ? 285 GLN A NE2   1 
ATOM   4436  N  NE2   B GLN A 1 285 ? -8.636  -24.870 55.231  0.50 46.56 ? 285 GLN A NE2   1 
ATOM   4437  N  N     A LEU A 1 286 ? -5.395  -20.288 57.712  0.50 43.06 ? 286 LEU A N     1 
ATOM   4438  N  N     B LEU A 1 286 ? -5.497  -20.147 57.584  0.50 43.07 ? 286 LEU A N     1 
ATOM   4439  C  CA    A LEU A 1 286 ? -4.837  -19.047 58.226  0.50 38.44 ? 286 LEU A CA    1 
ATOM   4440  C  CA    B LEU A 1 286 ? -4.904  -18.874 57.966  0.50 38.55 ? 286 LEU A CA    1 
ATOM   4441  C  C     A LEU A 1 286 ? -5.943  -18.106 58.699  0.50 39.70 ? 286 LEU A C     1 
ATOM   4442  C  C     B LEU A 1 286 ? -5.991  -17.884 58.363  0.50 39.85 ? 286 LEU A C     1 
ATOM   4443  O  O     A LEU A 1 286 ? -7.097  -18.186 58.269  0.50 35.73 ? 286 LEU A O     1 
ATOM   4444  O  O     B LEU A 1 286 ? -7.020  -17.773 57.691  0.50 36.37 ? 286 LEU A O     1 
ATOM   4445  C  CB    A LEU A 1 286 ? -3.991  -18.360 57.154  0.50 38.48 ? 286 LEU A CB    1 
ATOM   4446  C  CB    B LEU A 1 286 ? -4.066  -18.302 56.821  0.50 37.98 ? 286 LEU A CB    1 
ATOM   4447  C  CG    A LEU A 1 286 ? -2.864  -19.194 56.538  0.50 37.79 ? 286 LEU A CG    1 
ATOM   4448  C  CG    B LEU A 1 286 ? -2.613  -18.771 56.684  0.50 37.69 ? 286 LEU A CG    1 
ATOM   4449  C  CD1   A LEU A 1 286 ? -2.208  -18.449 55.390  0.50 36.75 ? 286 LEU A CD1   1 
ATOM   4450  C  CD1   B LEU A 1 286 ? -2.513  -20.284 56.538  0.50 41.52 ? 286 LEU A CD1   1 
ATOM   4451  C  CD2   A LEU A 1 286 ? -1.830  -19.570 57.590  0.50 40.15 ? 286 LEU A CD2   1 
ATOM   4452  C  CD2   B LEU A 1 286 ? -1.933  -18.080 55.515  0.50 39.33 ? 286 LEU A CD2   1 
ATOM   4453  N  N     A SER A 1 287 ? -5.571  -17.200 59.597  0.50 34.22 ? 287 SER A N     1 
ATOM   4454  N  N     B SER A 1 287 ? -5.750  -17.163 59.456  0.50 34.08 ? 287 SER A N     1 
ATOM   4455  C  CA    A SER A 1 287 ? -6.504  -16.242 60.166  0.50 36.47 ? 287 SER A CA    1 
ATOM   4456  C  CA    B SER A 1 287 ? -6.714  -16.213 59.984  0.50 36.77 ? 287 SER A CA    1 
ATOM   4457  C  C     A SER A 1 287 ? -6.579  -14.981 59.309  0.50 33.15 ? 287 SER A C     1 
ATOM   4458  C  C     B SER A 1 287 ? -6.746  -14.944 59.135  0.50 33.03 ? 287 SER A C     1 
ATOM   4459  O  O     A SER A 1 287 ? -5.769  -14.757 58.407  0.50 32.09 ? 287 SER A O     1 
ATOM   4460  O  O     B SER A 1 287 ? -5.903  -14.719 58.262  0.50 32.19 ? 287 SER A O     1 
ATOM   4461  C  CB    A SER A 1 287 ? -6.093  -15.884 61.592  0.50 35.85 ? 287 SER A CB    1 
ATOM   4462  C  CB    B SER A 1 287 ? -6.380  -15.859 61.430  0.50 35.53 ? 287 SER A CB    1 
ATOM   4463  O  OG    A SER A 1 287 ? -4.854  -15.197 61.597  0.50 36.52 ? 287 SER A OG    1 
ATOM   4464  O  OG    B SER A 1 287 ? -5.466  -14.778 61.485  0.50 33.96 ? 287 SER A OG    1 
ATOM   4465  N  N     A VAL A 1 288 ? -7.579  -14.148 59.609  0.50 32.02 ? 288 VAL A N     1 
ATOM   4466  N  N     B VAL A 1 288 ? -7.744  -14.102 59.415  0.50 31.77 ? 288 VAL A N     1 
ATOM   4467  C  CA    A VAL A 1 288 ? -7.721  -12.867 58.922  0.50 31.51 ? 288 VAL A CA    1 
ATOM   4468  C  CA    B VAL A 1 288 ? -7.884  -12.832 58.707  0.50 31.22 ? 288 VAL A CA    1 
ATOM   4469  C  C     A VAL A 1 288 ? -6.464  -12.025 59.097  0.50 33.43 ? 288 VAL A C     1 
ATOM   4470  C  C     B VAL A 1 288 ? -6.653  -11.958 58.920  0.50 33.62 ? 288 VAL A C     1 
ATOM   4471  O  O     A VAL A 1 288 ? -5.977  -11.403 58.144  0.50 28.80 ? 288 VAL A O     1 
ATOM   4472  O  O     B VAL A 1 288 ? -6.126  -11.360 57.973  0.50 28.74 ? 288 VAL A O     1 
ATOM   4473  C  CB    A VAL A 1 288 ? -8.972  -12.126 59.429  0.50 29.20 ? 288 VAL A CB    1 
ATOM   4474  C  CB    B VAL A 1 288 ? -9.175  -12.119 59.153  0.50 29.12 ? 288 VAL A CB    1 
ATOM   4475  C  CG1   A VAL A 1 288 ? -8.997  -10.698 58.912  0.50 30.82 ? 288 VAL A CG1   1 
ATOM   4476  C  CG1   B VAL A 1 288 ? -9.092  -10.629 58.876  0.50 30.78 ? 288 VAL A CG1   1 
ATOM   4477  C  CG2   A VAL A 1 288 ? -10.226 -12.858 59.008  0.50 29.24 ? 288 VAL A CG2   1 
ATOM   4478  C  CG2   B VAL A 1 288 ? -10.381 -12.721 58.448  0.50 28.59 ? 288 VAL A CG2   1 
ATOM   4479  N  N     A ALA A 1 289 ? -5.916  -11.998 60.314  0.50 31.24 ? 289 ALA A N     1 
ATOM   4480  N  N     B ALA A 1 289 ? -6.170  -11.877 60.163  0.50 32.12 ? 289 ALA A N     1 
ATOM   4481  C  CA    A ALA A 1 289 ? -4.703  -11.226 60.558  0.50 30.58 ? 289 ALA A CA    1 
ATOM   4482  C  CA    B ALA A 1 289 ? -5.010  -11.041 60.448  0.50 29.92 ? 289 ALA A CA    1 
ATOM   4483  C  C     A ALA A 1 289 ? -3.551  -11.723 59.695  0.50 33.02 ? 289 ALA A C     1 
ATOM   4484  C  C     B ALA A 1 289 ? -3.763  -11.545 59.735  0.50 32.76 ? 289 ALA A C     1 
ATOM   4485  O  O     A ALA A 1 289 ? -2.820  -10.920 59.103  0.50 32.85 ? 289 ALA A O     1 
ATOM   4486  O  O     B ALA A 1 289 ? -2.905  -10.743 59.347  0.50 31.77 ? 289 ALA A O     1 
ATOM   4487  C  CB    A ALA A 1 289 ? -4.329  -11.286 62.038  0.50 37.73 ? 289 ALA A CB    1 
ATOM   4488  C  CB    B ALA A 1 289 ? -4.768  -10.971 61.955  0.50 36.75 ? 289 ALA A CB    1 
ATOM   4489  N  N     A GLU A 1 290 ? -3.388  -13.045 59.592  0.50 29.32 ? 290 GLU A N     1 
ATOM   4490  N  N     B GLU A 1 290 ? -3.651  -12.862 59.540  0.50 28.46 ? 290 GLU A N     1 
ATOM   4491  C  CA    A GLU A 1 290 ? -2.266  -13.604 58.841  0.50 28.00 ? 290 GLU A CA    1 
ATOM   4492  C  CA    B GLU A 1 290 ? -2.452  -13.428 58.926  0.50 28.61 ? 290 GLU A CA    1 
ATOM   4493  C  C     A GLU A 1 290 ? -2.351  -13.248 57.360  0.50 31.69 ? 290 GLU A C     1 
ATOM   4494  C  C     B GLU A 1 290 ? -2.455  -13.267 57.408  0.50 31.59 ? 290 GLU A C     1 
ATOM   4495  O  O     A GLU A 1 290 ? -1.367  -12.793 56.762  0.50 30.24 ? 290 GLU A O     1 
ATOM   4496  O  O     B GLU A 1 290 ? -1.410  -12.979 56.813  0.50 30.64 ? 290 GLU A O     1 
ATOM   4497  C  CB    A GLU A 1 290 ? -2.219  -15.121 59.025  0.50 31.87 ? 290 GLU A CB    1 
ATOM   4498  C  CB    B GLU A 1 290 ? -2.319  -14.901 59.313  0.50 32.88 ? 290 GLU A CB    1 
ATOM   4499  C  CG    A GLU A 1 290 ? -1.743  -15.575 60.397  0.50 36.38 ? 290 GLU A CG    1 
ATOM   4500  C  CG    B GLU A 1 290 ? -2.016  -15.117 60.793  0.50 37.08 ? 290 GLU A CG    1 
ATOM   4501  C  CD    A GLU A 1 290 ? -1.770  -17.082 60.551  0.50 34.41 ? 290 GLU A CD    1 
ATOM   4502  C  CD    B GLU A 1 290 ? -2.160  -16.564 61.224  0.50 39.16 ? 290 GLU A CD    1 
ATOM   4503  O  OE1   A GLU A 1 290 ? -2.874  -17.649 60.706  0.50 41.37 ? 290 GLU A OE1   1 
ATOM   4504  O  OE1   B GLU A 1 290 ? -3.096  -17.240 60.744  0.50 40.69 ? 290 GLU A OE1   1 
ATOM   4505  O  OE2   A GLU A 1 290 ? -0.688  -17.702 60.505  0.50 39.05 ? 290 GLU A OE2   1 
ATOM   4506  O  OE2   B GLU A 1 290 ? -1.339  -17.023 62.048  0.50 41.07 ? 290 GLU A OE2   1 
ATOM   4507  N  N     A ILE A 1 291 ? -3.516  -13.461 56.743  0.50 27.13 ? 291 ILE A N     1 
ATOM   4508  N  N     B ILE A 1 291 ? -3.606  -13.459 56.759  0.50 27.15 ? 291 ILE A N     1 
ATOM   4509  C  CA    A ILE A 1 291 ? -3.635  -13.175 55.316  0.50 28.01 ? 291 ILE A CA    1 
ATOM   4510  C  CA    B ILE A 1 291 ? -3.657  -13.230 55.319  0.50 28.01 ? 291 ILE A CA    1 
ATOM   4511  C  C     A ILE A 1 291 ? -3.610  -11.672 55.060  0.50 30.72 ? 291 ILE A C     1 
ATOM   4512  C  C     B ILE A 1 291 ? -3.580  -11.740 55.012  0.50 30.68 ? 291 ILE A C     1 
ATOM   4513  O  O     A ILE A 1 291 ? -3.126  -11.225 54.014  0.50 30.87 ? 291 ILE A O     1 
ATOM   4514  O  O     B ILE A 1 291 ? -3.058  -11.344 53.965  0.50 30.97 ? 291 ILE A O     1 
ATOM   4515  C  CB    A ILE A 1 291 ? -4.900  -13.831 54.727  0.50 28.80 ? 291 ILE A CB    1 
ATOM   4516  C  CB    B ILE A 1 291 ? -4.913  -13.871 54.694  0.50 28.81 ? 291 ILE A CB    1 
ATOM   4517  C  CG1   A ILE A 1 291 ? -6.172  -13.172 55.263  0.50 26.56 ? 291 ILE A CG1   1 
ATOM   4518  C  CG1   B ILE A 1 291 ? -6.192  -13.291 55.298  0.50 26.55 ? 291 ILE A CG1   1 
ATOM   4519  C  CG2   A ILE A 1 291 ? -4.919  -15.321 55.024  0.50 30.88 ? 291 ILE A CG2   1 
ATOM   4520  C  CG2   B ILE A 1 291 ? -4.883  -15.381 54.855  0.50 30.89 ? 291 ILE A CG2   1 
ATOM   4521  C  CD1   A ILE A 1 291 ? -7.441  -13.694 54.620  0.50 26.94 ? 291 ILE A CD1   1 
ATOM   4522  C  CD1   B ILE A 1 291 ? -7.458  -13.845 54.674  0.50 26.95 ? 291 ILE A CD1   1 
ATOM   4523  N  N     A THR A 1 292 ? -4.113  -10.867 56.000  0.50 26.57 ? 292 THR A N     1 
ATOM   4524  N  N     B THR A 1 292 ? -4.087  -10.891 55.910  0.50 26.61 ? 292 THR A N     1 
ATOM   4525  C  CA    A THR A 1 292 ? -4.064  -9.417  55.831  0.50 26.78 ? 292 THR A CA    1 
ATOM   4526  C  CA    B THR A 1 292 ? -3.969  -9.450  55.706  0.50 26.63 ? 292 THR A CA    1 
ATOM   4527  C  C     A THR A 1 292 ? -2.635  -8.903  55.963  0.50 31.90 ? 292 THR A C     1 
ATOM   4528  C  C     B THR A 1 292 ? -2.518  -8.998  55.836  0.50 32.18 ? 292 THR A C     1 
ATOM   4529  O  O     A THR A 1 292 ? -2.175  -8.097  55.145  0.50 31.68 ? 292 THR A O     1 
ATOM   4530  O  O     B THR A 1 292 ? -2.059  -8.134  55.077  0.50 31.37 ? 292 THR A O     1 
ATOM   4531  C  CB    A THR A 1 292 ? -4.981  -8.730  56.845  0.50 28.09 ? 292 THR A CB    1 
ATOM   4532  C  CB    B THR A 1 292 ? -4.861  -8.700  56.698  0.50 28.21 ? 292 THR A CB    1 
ATOM   4533  O  OG1   A THR A 1 292 ? -6.345  -9.080  56.575  0.50 27.77 ? 292 THR A OG1   1 
ATOM   4534  O  OG1   B THR A 1 292 ? -6.190  -9.236  56.649  0.50 28.21 ? 292 THR A OG1   1 
ATOM   4535  C  CG2   A THR A 1 292 ? -4.829  -7.223  56.767  0.50 24.66 ? 292 THR A CG2   1 
ATOM   4536  C  CG2   B THR A 1 292 ? -4.915  -7.225  56.353  0.50 24.96 ? 292 THR A CG2   1 
ATOM   4537  N  N     A ASN A 1 293 ? -1.913  -9.366  56.987  0.50 29.82 ? 293 ASN A N     1 
ATOM   4538  N  N     B ASN A 1 293 ? -1.782  -9.577  56.789  0.50 29.92 ? 293 ASN A N     1 
ATOM   4539  C  CA    A ASN A 1 293 ? -0.505  -9.001  57.105  0.50 32.17 ? 293 ASN A CA    1 
ATOM   4540  C  CA    B ASN A 1 293 ? -0.350  -9.307  56.898  0.50 31.45 ? 293 ASN A CA    1 
ATOM   4541  C  C     A ASN A 1 293 ? 0.292   -9.481  55.900  0.50 32.63 ? 293 ASN A C     1 
ATOM   4542  C  C     B ASN A 1 293 ? 0.367   -9.608  55.590  0.50 33.26 ? 293 ASN A C     1 
ATOM   4543  O  O     A ASN A 1 293 ? 1.307   -8.871  55.544  0.50 34.62 ? 293 ASN A O     1 
ATOM   4544  O  O     B ASN A 1 293 ? 1.176   -8.806  55.108  0.50 33.90 ? 293 ASN A O     1 
ATOM   4545  C  CB    A ASN A 1 293 ? 0.086   -9.564  58.400  0.50 31.83 ? 293 ASN A CB    1 
ATOM   4546  C  CB    B ASN A 1 293 ? 0.258   -10.137 58.030  0.50 31.96 ? 293 ASN A CB    1 
ATOM   4547  C  CG    A ASN A 1 293 ? -0.626  -9.051  59.640  0.50 40.75 ? 293 ASN A CG    1 
ATOM   4548  C  CG    B ASN A 1 293 ? 0.273   -9.405  59.352  0.50 35.48 ? 293 ASN A CG    1 
ATOM   4549  O  OD1   A ASN A 1 293 ? -1.448  -8.139  59.564  0.50 39.44 ? 293 ASN A OD1   1 
ATOM   4550  O  OD1   B ASN A 1 293 ? 0.311   -8.175  59.395  0.50 41.92 ? 293 ASN A OD1   1 
ATOM   4551  N  ND2   A ASN A 1 293 ? -0.316  -9.642  60.790  0.50 42.48 ? 293 ASN A ND2   1 
ATOM   4552  N  ND2   B ASN A 1 293 ? 0.254   -10.161 60.445  0.50 40.22 ? 293 ASN A ND2   1 
ATOM   4553  N  N     A ALA A 1 294 ? -0.164  -10.556 55.248  0.50 30.83 ? 294 ALA A N     1 
ATOM   4554  N  N     B ALA A 1 294 ? 0.065   -10.766 54.996  0.50 32.01 ? 294 ALA A N     1 
ATOM   4555  C  CA    A ALA A 1 294 ? 0.493   -11.053 54.045  0.50 32.10 ? 294 ALA A CA    1 
ATOM   4556  C  CA    B ALA A 1 294 ? 0.788   -11.238 53.820  0.50 30.98 ? 294 ALA A CA    1 
ATOM   4557  C  C     A ALA A 1 294 ? 0.293   -10.134 52.847  0.50 32.12 ? 294 ALA A C     1 
ATOM   4558  C  C     B ALA A 1 294 ? 0.643   -10.313 52.619  0.50 32.91 ? 294 ALA A C     1 
ATOM   4559  O  O     A ALA A 1 294 ? 1.019   -10.267 51.855  0.50 30.31 ? 294 ALA A O     1 
ATOM   4560  O  O     B ALA A 1 294 ? 1.476   -10.372 51.708  0.50 27.27 ? 294 ALA A O     1 
ATOM   4561  C  CB    A ALA A 1 294 ? -0.011  -12.457 53.710  0.50 27.70 ? 294 ALA A CB    1 
ATOM   4562  C  CB    B ALA A 1 294 ? 0.314   -12.644 53.451  0.50 28.26 ? 294 ALA A CB    1 
ATOM   4563  N  N     A CYS A 1 295 ? -0.665  -9.206  52.912  0.50 30.36 ? 295 CYS A N     1 
ATOM   4564  N  N     B CYS A 1 295 ? -0.385  -9.462  52.591  0.50 30.37 ? 295 CYS A N     1 
ATOM   4565  C  CA    A CYS A 1 295 ? -0.822  -8.212  51.852  0.50 31.26 ? 295 CYS A CA    1 
ATOM   4566  C  CA    B CYS A 1 295 ? -0.577  -8.586  51.438  0.50 29.72 ? 295 CYS A CA    1 
ATOM   4567  C  C     A CYS A 1 295 ? 0.310   -7.199  51.818  0.50 31.44 ? 295 CYS A C     1 
ATOM   4568  C  C     B CYS A 1 295 ? 0.427   -7.441  51.410  0.50 32.97 ? 295 CYS A C     1 
ATOM   4569  O  O     A CYS A 1 295 ? 0.315   -6.334  50.936  0.50 29.55 ? 295 CYS A O     1 
ATOM   4570  O  O     B CYS A 1 295 ? 0.753   -6.933  50.332  0.50 30.53 ? 295 CYS A O     1 
ATOM   4571  C  CB    A CYS A 1 295 ? -2.148  -7.466  52.001  0.50 27.08 ? 295 CYS A CB    1 
ATOM   4572  C  CB    B CYS A 1 295 ? -1.999  -8.032  51.426  0.50 29.08 ? 295 CYS A CB    1 
ATOM   4573  S  SG    A CYS A 1 295 ? -3.618  -8.466  51.723  0.50 32.99 ? 295 CYS A SG    1 
ATOM   4574  S  SG    B CYS A 1 295 ? -3.214  -9.219  50.873  0.50 26.85 ? 295 CYS A SG    1 
ATOM   4575  N  N     A PHE A 1 296 ? 1.254   -7.270  52.754  0.50 34.33 ? 296 PHE A N     1 
ATOM   4576  N  N     B PHE A 1 296 ? 0.922   -7.019  52.568  0.50 33.07 ? 296 PHE A N     1 
ATOM   4577  C  CA    A PHE A 1 296 ? 2.383   -6.352  52.786  0.50 33.15 ? 296 PHE A CA    1 
ATOM   4578  C  CA    B PHE A 1 296 ? 1.888   -5.934  52.632  0.50 32.04 ? 296 PHE A CA    1 
ATOM   4579  C  C     A PHE A 1 296 ? 3.713   -7.078  52.643  0.50 36.66 ? 296 PHE A C     1 
ATOM   4580  C  C     B PHE A 1 296 ? 3.325   -6.426  52.515  0.50 34.41 ? 296 PHE A C     1 
ATOM   4581  O  O     A PHE A 1 296 ? 4.771   -6.463  52.830  0.50 36.28 ? 296 PHE A O     1 
ATOM   4582  O  O     B PHE A 1 296 ? 4.256   -5.657  52.779  0.50 34.31 ? 296 PHE A O     1 
ATOM   4583  C  CB    A PHE A 1 296 ? 2.340   -5.521  54.069  0.50 35.12 ? 296 PHE A CB    1 
ATOM   4584  C  CB    B PHE A 1 296 ? 1.689   -5.138  53.924  0.50 35.08 ? 296 PHE A CB    1 
ATOM   4585  C  CG    A PHE A 1 296 ? 1.055   -4.760  54.241  0.50 33.33 ? 296 PHE A CG    1 
ATOM   4586  C  CG    B PHE A 1 296 ? 0.325   -4.519  54.037  0.50 31.99 ? 296 PHE A CG    1 
ATOM   4587  C  CD1   A PHE A 1 296 ? 0.874   -3.534  53.623  0.50 28.17 ? 296 PHE A CD1   1 
ATOM   4588  C  CD1   B PHE A 1 296 ? -0.728  -5.226  54.595  0.50 32.79 ? 296 PHE A CD1   1 
ATOM   4589  C  CD2   A PHE A 1 296 ? 0.019   -5.281  55.000  0.50 29.80 ? 296 PHE A CD2   1 
ATOM   4590  C  CD2   B PHE A 1 296 ? 0.090   -3.238  53.567  0.50 31.26 ? 296 PHE A CD2   1 
ATOM   4591  C  CE1   A PHE A 1 296 ? -0.310  -2.834  53.768  0.50 33.71 ? 296 PHE A CE1   1 
ATOM   4592  C  CE1   B PHE A 1 296 ? -1.991  -4.662  54.688  0.50 34.46 ? 296 PHE A CE1   1 
ATOM   4593  C  CE2   A PHE A 1 296 ? -1.167  -4.585  55.151  0.50 35.85 ? 296 PHE A CE2   1 
ATOM   4594  C  CE2   B PHE A 1 296 ? -1.170  -2.668  53.659  0.50 32.04 ? 296 PHE A CE2   1 
ATOM   4595  C  CZ    A PHE A 1 296 ? -1.330  -3.358  54.535  0.50 34.37 ? 296 PHE A CZ    1 
ATOM   4596  C  CZ    B PHE A 1 296 ? -2.210  -3.381  54.221  0.50 31.69 ? 296 PHE A CZ    1 
ATOM   4597  N  N     A GLU A 1 297 ? 3.686   -8.366  52.311  0.50 34.72 ? 297 GLU A N     1 
ATOM   4598  N  N     B GLU A 1 297 ? 3.523   -7.684  52.110  0.50 35.18 ? 297 GLU A N     1 
ATOM   4599  C  CA    A GLU A 1 297 ? 4.897   -9.095  51.966  0.50 33.77 ? 297 GLU A CA    1 
ATOM   4600  C  CA    B GLU A 1 297 ? 4.786   -8.350  51.818  0.50 31.62 ? 297 GLU A CA    1 
ATOM   4601  C  C     A GLU A 1 297 ? 5.188   -8.897  50.485  0.50 32.96 ? 297 GLU A C     1 
ATOM   4602  C  C     B GLU A 1 297 ? 5.033   -8.395  50.317  0.50 32.74 ? 297 GLU A C     1 
ATOM   4603  O  O     A GLU A 1 297 ? 4.365   -9.295  49.649  0.50 33.57 ? 297 GLU A O     1 
ATOM   4604  O  O     B GLU A 1 297 ? 4.109   -8.673  49.544  0.50 35.67 ? 297 GLU A O     1 
ATOM   4605  C  CB    A GLU A 1 297 ? 4.740   -10.575 52.271  0.50 30.78 ? 297 GLU A CB    1 
ATOM   4606  C  CB    B GLU A 1 297 ? 4.796   -9.777  52.370  0.50 33.71 ? 297 GLU A CB    1 
ATOM   4607  C  CG    A GLU A 1 297 ? 4.357   -10.886 53.710  0.50 38.96 ? 297 GLU A CG    1 
ATOM   4608  C  CG    B GLU A 1 297 ? 4.920   -9.859  53.879  0.50 39.05 ? 297 GLU A CG    1 
ATOM   4609  C  CD    A GLU A 1 297 ? 5.507   -10.694 54.680  0.50 40.78 ? 297 GLU A CD    1 
ATOM   4610  C  CD    B GLU A 1 297 ? 6.274   -9.394  54.379  0.50 43.66 ? 297 GLU A CD    1 
ATOM   4611  O  OE1   A GLU A 1 297 ? 6.669   -10.904 54.277  0.50 39.73 ? 297 GLU A OE1   1 
ATOM   4612  O  OE1   B GLU A 1 297 ? 7.246   -9.421  53.589  0.50 45.30 ? 297 GLU A OE1   1 
ATOM   4613  O  OE2   A GLU A 1 297 ? 5.247   -10.328 55.846  0.50 48.19 ? 297 GLU A OE2   1 
ATOM   4614  O  OE2   B GLU A 1 297 ? 6.367   -8.998  55.560  0.50 50.42 ? 297 GLU A OE2   1 
ATOM   4615  N  N     A PRO A 1 298 ? 6.326   -8.292  50.113  0.50 32.01 ? 298 PRO A N     1 
ATOM   4616  N  N     B PRO A 1 298 ? 6.269   -8.127  49.887  0.50 32.80 ? 298 PRO A N     1 
ATOM   4617  C  CA    A PRO A 1 298 ? 6.623   -8.078  48.686  0.50 32.84 ? 298 PRO A CA    1 
ATOM   4618  C  CA    B PRO A 1 298 ? 6.560   -8.136  48.441  0.50 32.11 ? 298 PRO A CA    1 
ATOM   4619  C  C     A PRO A 1 298 ? 6.583   -9.356  47.858  0.50 29.73 ? 298 PRO A C     1 
ATOM   4620  C  C     B PRO A 1 298 ? 6.361   -9.491  47.784  0.50 30.27 ? 298 PRO A C     1 
ATOM   4621  O  O     A PRO A 1 298 ? 6.400   -9.300  46.638  0.50 37.23 ? 298 PRO A O     1 
ATOM   4622  O  O     B PRO A 1 298 ? 5.949   -9.547  46.617  0.50 35.86 ? 298 PRO A O     1 
ATOM   4623  C  CB    A PRO A 1 298 ? 8.034   -7.474  48.709  0.50 32.22 ? 298 PRO A CB    1 
ATOM   4624  C  CB    B PRO A 1 298 ? 8.031   -7.695  48.377  0.50 33.40 ? 298 PRO A CB    1 
ATOM   4625  C  CG    A PRO A 1 298 ? 8.162   -6.845  50.053  0.50 36.71 ? 298 PRO A CG    1 
ATOM   4626  C  CG    B PRO A 1 298 ? 8.288   -6.991  49.670  0.50 33.20 ? 298 PRO A CG    1 
ATOM   4627  C  CD    A PRO A 1 298 ? 7.350   -7.701  50.993  0.50 31.86 ? 298 PRO A CD    1 
ATOM   4628  C  CD    B PRO A 1 298 ? 7.426   -7.692  50.687  0.50 32.99 ? 298 PRO A CD    1 
ATOM   4629  N  N     A ALA A 1 299 ? 6.748   -10.511 48.511  0.50 31.58 ? 299 ALA A N     1 
ATOM   4630  N  N     B ALA A 1 299 ? 6.627   -10.583 48.506  0.50 31.81 ? 299 ALA A N     1 
ATOM   4631  C  CA    A ALA A 1 299 ? 6.706   -11.790 47.805  0.50 33.72 ? 299 ALA A CA    1 
ATOM   4632  C  CA    B ALA A 1 299 ? 6.602   -11.923 47.926  0.50 33.68 ? 299 ALA A CA    1 
ATOM   4633  C  C     A ALA A 1 299 ? 5.363   -12.019 47.125  0.50 31.85 ? 299 ALA A C     1 
ATOM   4634  C  C     B ALA A 1 299 ? 5.244   -12.311 47.355  0.50 31.90 ? 299 ALA A C     1 
ATOM   4635  O  O     A ALA A 1 299 ? 5.307   -12.565 46.016  0.50 30.80 ? 299 ALA A O     1 
ATOM   4636  O  O     B ALA A 1 299 ? 5.165   -13.282 46.592  0.50 26.43 ? 299 ALA A O     1 
ATOM   4637  C  CB    A ALA A 1 299 ? 6.993   -12.935 48.775  0.50 38.88 ? 299 ALA A CB    1 
ATOM   4638  C  CB    B ALA A 1 299 ? 7.013   -12.955 48.977  0.50 39.12 ? 299 ALA A CB    1 
ATOM   4639  N  N     A ASN A 1 300 ? 4.269   -11.628 47.779  0.50 29.65 ? 300 ASN A N     1 
ATOM   4640  N  N     B ASN A 1 300 ? 4.177   -11.597 47.710  0.50 29.59 ? 300 ASN A N     1 
ATOM   4641  C  CA    A ASN A 1 300 ? 2.926   -11.954 47.321  0.50 27.71 ? 300 ASN A CA    1 
ATOM   4642  C  CA    B ASN A 1 300 ? 2.837   -11.928 47.250  0.50 27.78 ? 300 ASN A CA    1 
ATOM   4643  C  C     A ASN A 1 300 ? 2.356   -10.917 46.358  0.50 30.11 ? 300 ASN A C     1 
ATOM   4644  C  C     B ASN A 1 300 ? 2.313   -10.974 46.181  0.50 30.11 ? 300 ASN A C     1 
ATOM   4645  O  O     A ASN A 1 300 ? 1.133   -10.839 46.201  0.50 26.27 ? 300 ASN A O     1 
ATOM   4646  O  O     B ASN A 1 300 ? 1.185   -11.155 45.713  0.50 26.80 ? 300 ASN A O     1 
ATOM   4647  C  CB    A ASN A 1 300 ? 1.992   -12.126 48.522  0.50 27.01 ? 300 ASN A CB    1 
ATOM   4648  C  CB    B ASN A 1 300 ? 1.866   -11.956 48.441  0.50 26.38 ? 300 ASN A CB    1 
ATOM   4649  C  CG    A ASN A 1 300 ? 2.519   -13.136 49.528  0.50 31.50 ? 300 ASN A CG    1 
ATOM   4650  C  CG    B ASN A 1 300 ? 2.250   -12.994 49.484  0.50 31.77 ? 300 ASN A CG    1 
ATOM   4651  O  OD1   A ASN A 1 300 ? 3.295   -14.026 49.181  0.50 34.24 ? 300 ASN A OD1   1 
ATOM   4652  O  OD1   B ASN A 1 300 ? 2.455   -14.165 49.167  0.50 30.23 ? 300 ASN A OD1   1 
ATOM   4653  N  ND2   A ASN A 1 300 ? 2.102   -13.000 50.781  0.50 34.19 ? 300 ASN A ND2   1 
ATOM   4654  N  ND2   B ASN A 1 300 ? 2.359   -12.563 50.736  0.50 33.99 ? 300 ASN A ND2   1 
ATOM   4655  N  N     A GLN A 1 301 ? 3.206   -10.132 45.703  0.50 26.18 ? 301 GLN A N     1 
ATOM   4656  N  N     B GLN A 1 301 ? 3.101   -9.982  45.771  0.50 25.95 ? 301 GLN A N     1 
ATOM   4657  C  CA    A GLN A 1 301 ? 2.755   -9.077  44.809  0.50 28.05 ? 301 GLN A CA    1 
ATOM   4658  C  CA    B GLN A 1 301 ? 2.617   -8.948  44.867  0.50 27.87 ? 301 GLN A CA    1 
ATOM   4659  C  C     A GLN A 1 301 ? 2.778   -9.546  43.361  0.50 27.42 ? 301 GLN A C     1 
ATOM   4660  C  C     B GLN A 1 301 ? 2.560   -9.440  43.425  0.50 27.36 ? 301 GLN A C     1 
ATOM   4661  O  O     A GLN A 1 301 ? 3.624   -10.349 42.962  0.50 24.23 ? 301 GLN A O     1 
ATOM   4662  O  O     B GLN A 1 301 ? 3.275   -10.361 43.022  0.50 24.62 ? 301 GLN A O     1 
ATOM   4663  C  CB    A GLN A 1 301 ? 3.628   -7.833  44.962  0.50 30.47 ? 301 GLN A CB    1 
ATOM   4664  C  CB    B GLN A 1 301 ? 3.504   -7.707  44.946  0.50 30.34 ? 301 GLN A CB    1 
ATOM   4665  C  CG    A GLN A 1 301 ? 3.826   -7.427  46.401  0.50 27.30 ? 301 GLN A CG    1 
ATOM   4666  C  CG    B GLN A 1 301 ? 3.288   -6.890  46.196  0.50 29.56 ? 301 GLN A CG    1 
ATOM   4667  C  CD    A GLN A 1 301 ? 4.503   -6.088  46.536  0.50 34.71 ? 301 GLN A CD    1 
ATOM   4668  C  CD    B GLN A 1 301 ? 4.409   -5.912  46.452  0.50 34.95 ? 301 GLN A CD    1 
ATOM   4669  O  OE1   A GLN A 1 301 ? 4.008   -5.208  47.238  0.50 30.79 ? 301 GLN A OE1   1 
ATOM   4670  O  OE1   B GLN A 1 301 ? 4.796   -5.690  47.597  0.50 26.66 ? 301 GLN A OE1   1 
ATOM   4671  N  NE2   A GLN A 1 301 ? 5.642   -5.921  45.864  0.50 30.39 ? 301 GLN A NE2   1 
ATOM   4672  N  NE2   B GLN A 1 301 ? 4.939   -5.319  45.385  0.50 29.34 ? 301 GLN A NE2   1 
ATOM   4673  N  N     A MET A 1 302 ? 1.836   -9.022  42.573  0.50 22.64 ? 302 MET A N     1 
ATOM   4674  N  N     B MET A 1 302 ? 1.693   -8.790  42.642  0.50 22.67 ? 302 MET A N     1 
ATOM   4675  C  CA    A MET A 1 302 ? 1.735   -9.366  41.161  0.50 26.71 ? 302 MET A CA    1 
ATOM   4676  C  CA    B MET A 1 302 ? 1.551   -9.082  41.221  0.50 26.32 ? 302 MET A CA    1 
ATOM   4677  C  C     A MET A 1 302 ? 2.684   -8.554  40.288  0.50 24.66 ? 302 MET A C     1 
ATOM   4678  C  C     B MET A 1 302 ? 2.615   -8.392  40.380  0.50 24.86 ? 302 MET A C     1 
ATOM   4679  O  O     A MET A 1 302 ? 2.847   -8.879  39.107  0.50 24.89 ? 302 MET A O     1 
ATOM   4680  O  O     B MET A 1 302 ? 2.812   -8.772  39.222  0.50 24.81 ? 302 MET A O     1 
ATOM   4681  C  CB    A MET A 1 302 ? 0.292   -9.179  40.685  0.50 29.65 ? 302 MET A CB    1 
ATOM   4682  C  CB    B MET A 1 302 ? 0.157   -8.665  40.737  0.50 26.66 ? 302 MET A CB    1 
ATOM   4683  C  CG    A MET A 1 302 ? -0.041  -9.922  39.402  0.50 33.94 ? 302 MET A CG    1 
ATOM   4684  C  CG    B MET A 1 302 ? -0.313  -9.356  39.469  0.50 34.16 ? 302 MET A CG    1 
ATOM   4685  S  SD    A MET A 1 302 ? -1.813  -10.120 39.157  0.50 40.01 ? 302 MET A SD    1 
ATOM   4686  S  SD    B MET A 1 302 ? -2.106  -9.297  39.256  0.50 39.89 ? 302 MET A SD    1 
ATOM   4687  C  CE    A MET A 1 302 ? -2.360  -8.419  39.269  0.50 35.01 ? 302 MET A CE    1 
ATOM   4688  C  CE    B MET A 1 302 ? -2.344  -7.640  38.614  0.50 32.14 ? 302 MET A CE    1 
ATOM   4689  N  N     A VAL A 1 303 ? 3.303   -7.512  40.835  0.50 26.61 ? 303 VAL A N     1 
ATOM   4690  N  N     B VAL A 1 303 ? 3.289   -7.385  40.932  0.50 26.73 ? 303 VAL A N     1 
ATOM   4691  C  CA    A VAL A 1 303 ? 4.344   -6.746  40.158  0.50 25.51 ? 303 VAL A CA    1 
ATOM   4692  C  CA    B VAL A 1 303 ? 4.392   -6.693  40.277  0.50 25.64 ? 303 VAL A CA    1 
ATOM   4693  C  C     A VAL A 1 303 ? 5.488   -6.574  41.146  0.50 25.68 ? 303 VAL A C     1 
ATOM   4694  C  C     B VAL A 1 303 ? 5.603   -6.767  41.193  0.50 25.33 ? 303 VAL A C     1 
ATOM   4695  O  O     A VAL A 1 303 ? 5.289   -6.027  42.238  0.50 28.29 ? 303 VAL A O     1 
ATOM   4696  O  O     B VAL A 1 303 ? 5.467   -6.706  42.420  0.50 27.49 ? 303 VAL A O     1 
ATOM   4697  C  CB    A VAL A 1 303 ? 3.840   -5.378  39.664  0.50 25.78 ? 303 VAL A CB    1 
ATOM   4698  C  CB    B VAL A 1 303 ? 4.047   -5.220  39.960  0.50 26.25 ? 303 VAL A CB    1 
ATOM   4699  C  CG1   A VAL A 1 303 ? 5.010   -4.518  39.192  0.50 27.13 ? 303 VAL A CG1   1 
ATOM   4700  C  CG1   B VAL A 1 303 ? 5.151   -4.566  39.127  0.50 27.10 ? 303 VAL A CG1   1 
ATOM   4701  C  CG2   A VAL A 1 303 ? 2.828   -5.554  38.541  0.50 24.40 ? 303 VAL A CG2   1 
ATOM   4702  C  CG2   B VAL A 1 303 ? 2.715   -5.114  39.249  0.50 20.31 ? 303 VAL A CG2   1 
ATOM   4703  N  N     A LYS A 1 304 ? 6.678   -7.037  40.772  0.50 24.47 ? 304 LYS A N     1 
ATOM   4704  N  N     B LYS A 1 304 ? 6.787   -6.896  40.602  0.50 24.27 ? 304 LYS A N     1 
ATOM   4705  C  CA    A LYS A 1 304 ? 7.808   -7.027  41.696  0.50 24.76 ? 304 LYS A CA    1 
ATOM   4706  C  CA    B LYS A 1 304 ? 8.023   -6.838  41.372  0.50 25.67 ? 304 LYS A CA    1 
ATOM   4707  C  C     A LYS A 1 304 ? 8.277   -5.596  41.927  0.50 27.79 ? 304 LYS A C     1 
ATOM   4708  C  C     B LYS A 1 304 ? 8.309   -5.386  41.736  0.50 28.04 ? 304 LYS A C     1 
ATOM   4709  O  O     A LYS A 1 304 ? 8.906   -4.987  41.056  0.50 26.54 ? 304 LYS A O     1 
ATOM   4710  O  O     B LYS A 1 304 ? 8.607   -4.568  40.859  0.50 27.28 ? 304 LYS A O     1 
ATOM   4711  C  CB    A LYS A 1 304 ? 8.941   -7.901  41.165  0.50 33.20 ? 304 LYS A CB    1 
ATOM   4712  C  CB    B LYS A 1 304 ? 9.181   -7.447  40.583  0.50 29.42 ? 304 LYS A CB    1 
ATOM   4713  C  CG    A LYS A 1 304 ? 8.635   -9.388  41.240  0.50 28.51 ? 304 LYS A CG    1 
ATOM   4714  C  CG    B LYS A 1 304 ? 9.118   -8.964  40.428  0.50 30.42 ? 304 LYS A CG    1 
ATOM   4715  C  CD    A LYS A 1 304 ? 9.783   -10.245 40.716  0.50 30.07 ? 304 LYS A CD    1 
ATOM   4716  C  CD    B LYS A 1 304 ? 9.884   -9.693  41.531  0.50 33.68 ? 304 LYS A CD    1 
ATOM   4717  C  CE    A LYS A 1 304 ? 10.863  -10.453 41.764  0.50 35.10 ? 304 LYS A CE    1 
ATOM   4718  C  CE    B LYS A 1 304 ? 9.081   -9.804  42.824  0.50 35.13 ? 304 LYS A CE    1 
ATOM   4719  N  NZ    A LYS A 1 304 ? 11.827  -11.513 41.355  0.50 36.71 ? 304 LYS A NZ    1 
ATOM   4720  N  NZ    B LYS A 1 304 ? 9.868   -10.451 43.916  0.50 44.01 ? 304 LYS A NZ    1 
ATOM   4721  N  N     A CYS A 1 305 ? 7.954   -5.058  43.100  0.50 28.63 ? 305 CYS A N     1 
ATOM   4722  N  N     B CYS A 1 305 ? 8.207   -5.066  43.025  0.50 28.47 ? 305 CYS A N     1 
ATOM   4723  C  CA    A CYS A 1 305 ? 8.471   -3.778  43.571  0.50 29.99 ? 305 CYS A CA    1 
ATOM   4724  C  CA    B CYS A 1 305 ? 8.535   -3.747  43.555  0.50 29.99 ? 305 CYS A CA    1 
ATOM   4725  C  C     A CYS A 1 305 ? 8.399   -3.790  45.094  0.50 34.28 ? 305 CYS A C     1 
ATOM   4726  C  C     B CYS A 1 305 ? 8.481   -3.816  45.076  0.50 34.29 ? 305 CYS A C     1 
ATOM   4727  O  O     A CYS A 1 305 ? 7.884   -4.733  45.702  0.50 30.70 ? 305 CYS A O     1 
ATOM   4728  O  O     B CYS A 1 305 ? 7.983   -4.783  45.659  0.50 30.74 ? 305 CYS A O     1 
ATOM   4729  C  CB    A CYS A 1 305 ? 7.697   -2.599  42.974  0.50 31.56 ? 305 CYS A CB    1 
ATOM   4730  C  CB    B CYS A 1 305 ? 7.595   -2.659  43.026  0.50 31.55 ? 305 CYS A CB    1 
ATOM   4731  S  SG    A CYS A 1 305 ? 5.997   -2.433  43.565  0.50 27.73 ? 305 CYS A SG    1 
ATOM   4732  S  SG    B CYS A 1 305 ? 5.838   -3.022  43.222  0.50 30.12 ? 305 CYS A SG    1 
ATOM   4733  N  N     A ASP A 1 306 ? 8.922   -2.731  45.714  0.50 33.19 ? 306 ASP A N     1 
ATOM   4734  N  N     B ASP A 1 306 ? 9.000   -2.768  45.711  0.50 33.17 ? 306 ASP A N     1 
ATOM   4735  C  CA    A ASP A 1 306 ? 9.032   -2.654  47.171  0.50 39.54 ? 306 ASP A CA    1 
ATOM   4736  C  CA    B ASP A 1 306 ? 9.107   -2.703  47.166  0.50 39.55 ? 306 ASP A CA    1 
ATOM   4737  C  C     A ASP A 1 306 ? 8.224   -1.475  47.698  0.50 35.70 ? 306 ASP A C     1 
ATOM   4738  C  C     B ASP A 1 306 ? 8.221   -1.585  47.702  0.50 35.71 ? 306 ASP A C     1 
ATOM   4739  O  O     A ASP A 1 306 ? 8.732   -0.346  47.772  0.50 34.77 ? 306 ASP A O     1 
ATOM   4740  O  O     B ASP A 1 306 ? 8.569   -0.403  47.551  0.50 35.06 ? 306 ASP A O     1 
ATOM   4741  C  CB    A ASP A 1 306 ? 10.494  -2.550  47.598  0.50 38.95 ? 306 ASP A CB    1 
ATOM   4742  C  CB    B ASP A 1 306 ? 10.564  -2.476  47.575  0.50 38.91 ? 306 ASP A CB    1 
ATOM   4743  C  CG    A ASP A 1 306 ? 10.704  -2.960  49.037  0.50 41.79 ? 306 ASP A CG    1 
ATOM   4744  C  CG    B ASP A 1 306 ? 10.767  -2.510  49.079  0.50 42.29 ? 306 ASP A CG    1 
ATOM   4745  O  OD1   A ASP A 1 306 ? 9.696   -3.203  49.733  0.50 40.81 ? 306 ASP A OD1   1 
ATOM   4746  O  OD1   B ASP A 1 306 ? 9.822   -2.881  49.811  0.50 41.12 ? 306 ASP A OD1   1 
ATOM   4747  O  OD2   A ASP A 1 306 ? 11.870  -3.047  49.470  0.50 41.05 ? 306 ASP A OD2   1 
ATOM   4748  O  OD2   B ASP A 1 306 ? 11.878  -2.159  49.528  0.50 40.89 ? 306 ASP A OD2   1 
ATOM   4749  N  N     A PRO A 1 307 ? 6.963   -1.693  48.088  0.50 32.63 ? 307 PRO A N     1 
ATOM   4750  N  N     B PRO A 1 307 ? 7.089   -1.895  48.343  0.50 33.38 ? 307 PRO A N     1 
ATOM   4751  C  CA    A PRO A 1 307 ? 6.149   -0.587  48.621  0.50 38.21 ? 307 PRO A CA    1 
ATOM   4752  C  CA    B PRO A 1 307 ? 6.189   -0.824  48.808  0.50 38.18 ? 307 PRO A CA    1 
ATOM   4753  C  C     A PRO A 1 307 ? 6.680   0.028   49.909  0.50 38.31 ? 307 PRO A C     1 
ATOM   4754  C  C     B PRO A 1 307 ? 6.807   0.089   49.850  0.50 38.57 ? 307 PRO A C     1 
ATOM   4755  O  O     A PRO A 1 307 ? 6.152   1.065   50.331  0.50 40.67 ? 307 PRO A O     1 
ATOM   4756  O  O     B PRO A 1 307 ? 6.294   1.195   50.061  0.50 40.40 ? 307 PRO A O     1 
ATOM   4757  C  CB    A PRO A 1 307 ? 4.776   -1.237  48.841  0.50 38.16 ? 307 PRO A CB    1 
ATOM   4758  C  CB    B PRO A 1 307 ? 4.991   -1.589  49.389  0.50 38.89 ? 307 PRO A CB    1 
ATOM   4759  C  CG    A PRO A 1 307 ? 4.746   -2.354  47.875  0.50 35.46 ? 307 PRO A CG    1 
ATOM   4760  C  CG    B PRO A 1 307 ? 5.093   -2.957  48.844  0.50 32.20 ? 307 PRO A CG    1 
ATOM   4761  C  CD    A PRO A 1 307 ? 6.152   -2.895  47.839  0.50 36.16 ? 307 PRO A CD    1 
ATOM   4762  C  CD    B PRO A 1 307 ? 6.555   -3.230  48.651  0.50 34.49 ? 307 PRO A CD    1 
ATOM   4763  N  N     A ARG A 1 308 ? 7.693   -0.564  50.547  0.50 40.50 ? 308 ARG A N     1 
ATOM   4764  N  N     B ARG A 1 308 ? 7.885   -0.330  50.513  0.50 40.27 ? 308 ARG A N     1 
ATOM   4765  C  CA    A ARG A 1 308 ? 8.317   0.096   51.689  0.50 42.94 ? 308 ARG A CA    1 
ATOM   4766  C  CA    B ARG A 1 308 ? 8.539   0.530   51.488  0.50 42.78 ? 308 ARG A CA    1 
ATOM   4767  C  C     A ARG A 1 308 ? 8.954   1.415   51.267  0.50 43.04 ? 308 ARG A C     1 
ATOM   4768  C  C     B ARG A 1 308 ? 9.360   1.635   50.837  0.50 43.79 ? 308 ARG A C     1 
ATOM   4769  O  O     A ARG A 1 308 ? 8.838   2.424   51.972  0.50 45.24 ? 308 ARG A O     1 
ATOM   4770  O  O     B ARG A 1 308 ? 9.848   2.523   51.545  0.50 42.65 ? 308 ARG A O     1 
ATOM   4771  C  CB    A ARG A 1 308 ? 9.353   -0.829  52.328  0.50 46.42 ? 308 ARG A CB    1 
ATOM   4772  C  CB    B ARG A 1 308 ? 9.432   -0.306  52.408  0.50 45.53 ? 308 ARG A CB    1 
ATOM   4773  C  CG    A ARG A 1 308 ? 8.816   -2.185  52.743  0.50 43.49 ? 308 ARG A CG    1 
ATOM   4774  C  CG    B ARG A 1 308 ? 8.811   -1.627  52.832  0.50 40.91 ? 308 ARG A CG    1 
ATOM   4775  C  CD    A ARG A 1 308 ? 9.951   -3.181  52.847  0.50 49.83 ? 308 ARG A CD    1 
ATOM   4776  C  CD    B ARG A 1 308 ? 9.789   -2.454  53.646  0.50 47.32 ? 308 ARG A CD    1 
ATOM   4777  N  NE    A ARG A 1 308 ? 9.473   -4.511  53.199  0.50 56.85 ? 308 ARG A NE    1 
ATOM   4778  N  NE    B ARG A 1 308 ? 9.622   -3.882  53.407  0.50 56.81 ? 308 ARG A NE    1 
ATOM   4779  C  CZ    A ARG A 1 308 ? 10.202  -5.615  53.116  0.50 51.79 ? 308 ARG A CZ    1 
ATOM   4780  C  CZ    B ARG A 1 308 ? 8.883   -4.692  54.153  0.50 52.16 ? 308 ARG A CZ    1 
ATOM   4781  N  NH1   A ARG A 1 308 ? 11.446  -5.589  52.666  0.50 44.38 ? 308 ARG A NH1   1 
ATOM   4782  N  NH1   B ARG A 1 308 ? 8.223   -4.248  55.211  0.50 54.53 ? 308 ARG A NH1   1 
ATOM   4783  N  NH2   A ARG A 1 308 ? 9.668   -6.773  53.491  0.50 43.79 ? 308 ARG A NH2   1 
ATOM   4784  N  NH2   B ARG A 1 308 ? 8.808   -5.981  53.831  0.50 41.68 ? 308 ARG A NH2   1 
ATOM   4785  N  N     A HIS A 1 309 ? 9.609   1.427   50.102  0.50 43.94 ? 309 HIS A N     1 
ATOM   4786  N  N     B HIS A 1 309 ? 9.521   1.605   49.514  0.50 43.74 ? 309 HIS A N     1 
ATOM   4787  C  CA    A HIS A 1 309 ? 10.243  2.614   49.539  0.50 44.08 ? 309 HIS A CA    1 
ATOM   4788  C  CA    B HIS A 1 309 ? 10.231  2.656   48.794  0.50 45.75 ? 309 HIS A CA    1 
ATOM   4789  C  C     A HIS A 1 309 ? 9.258   3.478   48.762  0.50 42.84 ? 309 HIS A C     1 
ATOM   4790  C  C     B HIS A 1 309 ? 9.328   3.838   48.466  0.50 42.19 ? 309 HIS A C     1 
ATOM   4791  O  O     A HIS A 1 309 ? 9.660   4.177   47.826  0.50 40.65 ? 309 HIS A O     1 
ATOM   4792  O  O     B HIS A 1 309 ? 9.749   4.991   48.599  0.50 48.34 ? 309 HIS A O     1 
ATOM   4793  C  CB    A HIS A 1 309 ? 11.411  2.212   48.634  0.50 43.33 ? 309 HIS A CB    1 
ATOM   4794  C  CB    B HIS A 1 309 ? 10.835  2.095   47.503  0.50 39.92 ? 309 HIS A CB    1 
ATOM   4795  C  CG    A HIS A 1 309 ? 12.312  1.176   49.231  0.50 47.11 ? 309 HIS A CG    1 
ATOM   4796  C  CG    B HIS A 1 309 ? 11.937  1.106   47.730  0.50 47.85 ? 309 HIS A CG    1 
ATOM   4797  N  ND1   A HIS A 1 309 ? 12.987  0.242   48.471  0.50 50.82 ? 309 HIS A ND1   1 
ATOM   4798  N  ND1   B HIS A 1 309 ? 12.552  0.423   46.702  0.50 40.11 ? 309 HIS A ND1   1 
ATOM   4799  C  CD2   A HIS A 1 309 ? 12.647  0.926   50.518  0.50 47.25 ? 309 HIS A CD2   1 
ATOM   4800  C  CD2   B HIS A 1 309 ? 12.535  0.686   48.870  0.50 47.29 ? 309 HIS A CD2   1 
ATOM   4801  C  CE1   A HIS A 1 309 ? 13.695  -0.540  49.267  0.50 49.44 ? 309 HIS A CE1   1 
ATOM   4802  C  CE1   B HIS A 1 309 ? 13.480  -0.375  47.199  0.50 40.14 ? 309 HIS A CE1   1 
ATOM   4803  N  NE2   A HIS A 1 309 ? 13.506  -0.146  50.513  0.50 45.72 ? 309 HIS A NE2   1 
ATOM   4804  N  NE2   B HIS A 1 309 ? 13.490  -0.235  48.512  0.50 49.58 ? 309 HIS A NE2   1 
ATOM   4805  N  N     A GLY A 1 310 ? 7.970   3.419   49.100  0.50 41.42 ? 310 GLY A N     1 
ATOM   4806  N  N     B GLY A 1 310 ? 8.094   3.575   48.035  0.50 40.95 ? 310 GLY A N     1 
ATOM   4807  C  CA    A GLY A 1 310 ? 6.975   4.190   48.387  0.50 38.44 ? 310 GLY A CA    1 
ATOM   4808  C  CA    B GLY A 1 310 ? 7.142   4.617   47.725  0.50 39.36 ? 310 GLY A CA    1 
ATOM   4809  C  C     A GLY A 1 310 ? 5.959   4.820   49.321  0.50 36.90 ? 310 GLY A C     1 
ATOM   4810  C  C     B GLY A 1 310 ? 6.118   4.810   48.830  0.50 36.92 ? 310 GLY A C     1 
ATOM   4811  O  O     A GLY A 1 310 ? 6.082   4.751   50.546  0.50 39.04 ? 310 GLY A O     1 
ATOM   4812  O  O     B GLY A 1 310 ? 6.267   4.332   49.955  0.50 40.22 ? 310 GLY A O     1 
ATOM   4813  N  N     A LYS A 1 311 ? 4.948   5.439   48.719  0.50 36.92 ? 311 LYS A N     1 
ATOM   4814  N  N     B LYS A 1 311 ? 5.054   5.535   48.487  0.50 36.26 ? 311 LYS A N     1 
ATOM   4815  C  CA    A LYS A 1 311 ? 3.856   6.049   49.465  0.50 34.50 ? 311 LYS A CA    1 
ATOM   4816  C  CA    B LYS A 1 311 ? 3.986   5.843   49.426  0.50 34.51 ? 311 LYS A CA    1 
ATOM   4817  C  C     A LYS A 1 311 ? 2.531   5.643   48.839  0.50 33.65 ? 311 LYS A C     1 
ATOM   4818  C  C     B LYS A 1 311 ? 2.640   5.488   48.810  0.50 33.58 ? 311 LYS A C     1 
ATOM   4819  O  O     A LYS A 1 311 ? 2.426   5.531   47.616  0.50 28.43 ? 311 LYS A O     1 
ATOM   4820  O  O     B LYS A 1 311 ? 2.493   5.411   47.588  0.50 28.27 ? 311 LYS A O     1 
ATOM   4821  C  CB    A LYS A 1 311 ? 3.964   7.584   49.510  0.50 37.23 ? 311 LYS A CB    1 
ATOM   4822  C  CB    B LYS A 1 311 ? 4.005   7.324   49.837  0.50 37.77 ? 311 LYS A CB    1 
ATOM   4823  C  CG    A LYS A 1 311 ? 5.139   8.082   50.329  0.50 38.62 ? 311 LYS A CG    1 
ATOM   4824  C  CG    B LYS A 1 311 ? 5.374   7.821   50.263  0.50 39.12 ? 311 LYS A CG    1 
ATOM   4825  C  CD    A LYS A 1 311 ? 5.069   9.581   50.543  0.50 44.11 ? 311 LYS A CD    1 
ATOM   4826  C  CD    B LYS A 1 311 ? 5.313   9.225   50.826  0.50 43.70 ? 311 LYS A CD    1 
ATOM   4827  C  CE    A LYS A 1 311 ? 6.309   10.090  51.262  0.50 46.03 ? 311 LYS A CE    1 
ATOM   4828  C  CE    B LYS A 1 311 ? 6.711   9.800   50.984  0.50 45.19 ? 311 LYS A CE    1 
ATOM   4829  N  NZ    A LYS A 1 311 ? 6.583   9.314   52.503  0.50 49.73 ? 311 LYS A NZ    1 
ATOM   4830  N  NZ    B LYS A 1 311 ? 7.643   8.805   51.585  0.50 41.95 ? 311 LYS A NZ    1 
ATOM   4831  N  N     A TYR A 1 312 ? 1.530   5.396   49.685  0.50 28.53 ? 312 TYR A N     1 
ATOM   4832  N  N     B TYR A 1 312 ? 1.653   5.270   49.680  0.50 28.31 ? 312 TYR A N     1 
ATOM   4833  C  CA    A TYR A 1 312 ? 0.219   4.952   49.232  0.50 31.38 ? 312 TYR A CA    1 
ATOM   4834  C  CA    B TYR A 1 312 ? 0.317   4.867   49.264  0.50 31.34 ? 312 TYR A CA    1 
ATOM   4835  C  C     A TYR A 1 312 ? -0.699  6.141   48.982  0.50 30.57 ? 312 TYR A C     1 
ATOM   4836  C  C     B TYR A 1 312 ? -0.562  6.077   48.972  0.50 30.63 ? 312 TYR A C     1 
ATOM   4837  O  O     A TYR A 1 312 ? -0.749  7.082   49.778  0.50 32.29 ? 312 TYR A O     1 
ATOM   4838  O  O     B TYR A 1 312 ? -0.468  7.109   49.643  0.50 32.45 ? 312 TYR A O     1 
ATOM   4839  C  CB    A TYR A 1 312 ? -0.421  4.027   50.266  0.50 31.61 ? 312 TYR A CB    1 
ATOM   4840  C  CB    B TYR A 1 312 ? -0.352  4.016   50.343  0.50 31.56 ? 312 TYR A CB    1 
ATOM   4841  C  CG    A TYR A 1 312 ? 0.234   2.675   50.407  0.50 28.89 ? 312 TYR A CG    1 
ATOM   4842  C  CG    B TYR A 1 312 ? 0.212   2.628   50.508  0.50 28.97 ? 312 TYR A CG    1 
ATOM   4843  C  CD1   A TYR A 1 312 ? -0.138  1.618   49.588  0.50 30.58 ? 312 TYR A CD1   1 
ATOM   4844  C  CD1   B TYR A 1 312 ? -0.114  1.616   49.616  0.50 30.60 ? 312 TYR A CD1   1 
ATOM   4845  C  CD2   A TYR A 1 312 ? 1.201   2.445   51.379  0.50 34.61 ? 312 TYR A CD2   1 
ATOM   4846  C  CD2   B TYR A 1 312 ? 1.045   2.319   51.578  0.50 34.58 ? 312 TYR A CD2   1 
ATOM   4847  C  CE1   A TYR A 1 312 ? 0.448   0.373   49.720  0.50 32.19 ? 312 TYR A CE1   1 
ATOM   4848  C  CE1   B TYR A 1 312 ? 0.391   0.340   49.772  0.50 32.20 ? 312 TYR A CE1   1 
ATOM   4849  C  CE2   A TYR A 1 312 ? 1.795   1.200   51.516  0.50 35.00 ? 312 TYR A CE2   1 
ATOM   4850  C  CE2   B TYR A 1 312 ? 1.556   1.043   51.742  0.50 35.19 ? 312 TYR A CE2   1 
ATOM   4851  C  CZ    A TYR A 1 312 ? 1.412   0.169   50.687  0.50 32.32 ? 312 TYR A CZ    1 
ATOM   4852  C  CZ    B TYR A 1 312 ? 1.223   0.058   50.837  0.50 32.21 ? 312 TYR A CZ    1 
ATOM   4853  O  OH    A TYR A 1 312 ? 1.995   -1.069  50.819  0.50 39.92 ? 312 TYR A OH    1 
ATOM   4854  O  OH    B TYR A 1 312 ? 1.724   -1.212  50.992  0.50 40.12 ? 312 TYR A OH    1 
ATOM   4855  N  N     A MET A 1 313 ? -1.424  6.091   47.867  0.50 27.42 ? 313 MET A N     1 
ATOM   4856  N  N     B MET A 1 313 ? -1.425  5.934   47.970  0.50 27.40 ? 313 MET A N     1 
ATOM   4857  C  CA    A MET A 1 313 ? -2.484  7.042   47.571  0.50 30.39 ? 313 MET A CA    1 
ATOM   4858  C  CA    B MET A 1 313 ? -2.468  6.903   47.654  0.50 30.31 ? 313 MET A CA    1 
ATOM   4859  C  C     A MET A 1 313 ? -3.866  6.411   47.626  0.50 33.77 ? 313 MET A C     1 
ATOM   4860  C  C     B MET A 1 313 ? -3.864  6.382   47.946  0.50 33.95 ? 313 MET A C     1 
ATOM   4861  O  O     A MET A 1 313 ? -4.867  7.132   47.532  0.50 34.78 ? 313 MET A O     1 
ATOM   4862  O  O     B MET A 1 313 ? -4.732  7.149   48.367  0.50 31.60 ? 313 MET A O     1 
ATOM   4863  C  CB    A MET A 1 313 ? -2.264  7.669   46.187  0.50 35.57 ? 313 MET A CB    1 
ATOM   4864  C  CB    B MET A 1 313 ? -2.381  7.320   46.179  0.50 35.98 ? 313 MET A CB    1 
ATOM   4865  C  CG    A MET A 1 313 ? -1.012  8.521   46.083  0.50 33.04 ? 313 MET A CG    1 
ATOM   4866  C  CG    B MET A 1 313 ? -1.260  8.301   45.867  0.50 33.47 ? 313 MET A CG    1 
ATOM   4867  S  SD    A MET A 1 313 ? -0.394  8.639   44.389  0.50 34.70 ? 313 MET A SD    1 
ATOM   4868  S  SD    B MET A 1 313 ? -0.943  8.498   44.095  0.50 31.33 ? 313 MET A SD    1 
ATOM   4869  C  CE    A MET A 1 313 ? 0.572   7.136   44.284  0.50 30.47 ? 313 MET A CE    1 
ATOM   4870  C  CE    B MET A 1 313 ? 0.110   7.084   43.787  0.50 33.46 ? 313 MET A CE    1 
ATOM   4871  N  N     A ALA A 1 314 ? -3.942  5.093   47.776  0.50 27.79 ? 314 ALA A N     1 
ATOM   4872  N  N     B ALA A 1 314 ? -4.100  5.089   47.738  0.50 27.85 ? 314 ALA A N     1 
ATOM   4873  C  CA    A ALA A 1 314 ? -5.182  4.341   47.876  0.50 30.65 ? 314 ALA A CA    1 
ATOM   4874  C  CA    B ALA A 1 314 ? -5.376  4.472   48.062  0.50 30.35 ? 314 ALA A CA    1 
ATOM   4875  C  C     A ALA A 1 314 ? -4.828  2.934   48.323  0.50 30.58 ? 314 ALA A C     1 
ATOM   4876  C  C     B ALA A 1 314 ? -5.148  2.989   48.301  0.50 29.74 ? 314 ALA A C     1 
ATOM   4877  O  O     A ALA A 1 314 ? -3.769  2.410   47.965  0.50 27.96 ? 314 ALA A O     1 
ATOM   4878  O  O     B ALA A 1 314 ? -4.131  2.424   47.889  0.50 29.18 ? 314 ALA A O     1 
ATOM   4879  C  CB    A ALA A 1 314 ? -5.936  4.303   46.543  0.50 30.61 ? 314 ALA A CB    1 
ATOM   4880  C  CB    B ALA A 1 314 ? -6.409  4.687   46.952  0.50 33.58 ? 314 ALA A CB    1 
ATOM   4881  N  N     A CYS A 1 315 ? -5.715  2.334   49.112  0.50 26.17 ? 315 CYS A N     1 
ATOM   4882  N  N     B CYS A 1 315 ? -6.110  2.362   48.976  0.50 26.49 ? 315 CYS A N     1 
ATOM   4883  C  CA    A CYS A 1 315 ? -5.495  0.970   49.586  0.50 29.13 ? 315 CYS A CA    1 
ATOM   4884  C  CA    B CYS A 1 315 ? -6.003  0.945   49.299  0.50 30.00 ? 315 CYS A CA    1 
ATOM   4885  C  C     A CYS A 1 315 ? -6.853  0.344   49.866  0.50 31.11 ? 315 CYS A C     1 
ATOM   4886  C  C     B CYS A 1 315 ? -7.395  0.346   49.440  0.50 28.15 ? 315 CYS A C     1 
ATOM   4887  O  O     A CYS A 1 315 ? -7.499  0.679   50.865  0.50 24.50 ? 315 CYS A O     1 
ATOM   4888  O  O     B CYS A 1 315 ? -8.252  0.922   50.117  0.50 29.32 ? 315 CYS A O     1 
ATOM   4889  C  CB    A CYS A 1 315 ? -4.610  0.952   50.829  0.50 30.10 ? 315 CYS A CB    1 
ATOM   4890  C  CB    B CYS A 1 315 ? -5.205  0.738   50.589  0.50 27.40 ? 315 CYS A CB    1 
ATOM   4891  S  SG    A CYS A 1 315 ? -3.874  -0.656  51.191  0.50 42.48 ? 315 CYS A SG    1 
ATOM   4892  S  SG    B CYS A 1 315 ? -4.774  -0.976  50.910  0.50 37.02 ? 315 CYS A SG    1 
ATOM   4893  N  N     A CYS A 1 316 ? -7.281  -0.554  48.986  0.50 20.52 ? 316 CYS A N     1 
ATOM   4894  N  N     B CYS A 1 316 ? -7.606  -0.811  48.810  0.50 22.59 ? 316 CYS A N     1 
ATOM   4895  C  CA    A CYS A 1 316 ? -8.548  -1.256  49.131  0.50 24.44 ? 316 CYS A CA    1 
ATOM   4896  C  CA    B CYS A 1 316 ? -8.862  -1.553  48.893  0.50 23.15 ? 316 CYS A CA    1 
ATOM   4897  C  C     A CYS A 1 316 ? -8.282  -2.721  49.441  0.50 28.23 ? 316 CYS A C     1 
ATOM   4898  C  C     B CYS A 1 316 ? -8.553  -3.010  49.200  0.50 26.97 ? 316 CYS A C     1 
ATOM   4899  O  O     A CYS A 1 316 ? -7.337  -3.317  48.911  0.50 22.08 ? 316 CYS A O     1 
ATOM   4900  O  O     B CYS A 1 316 ? -7.801  -3.657  48.462  0.50 22.55 ? 316 CYS A O     1 
ATOM   4901  C  CB    A CYS A 1 316 ? -9.396  -1.136  47.864  0.50 28.41 ? 316 CYS A CB    1 
ATOM   4902  C  CB    B CYS A 1 316 ? -9.664  -1.455  47.590  0.50 26.82 ? 316 CYS A CB    1 
ATOM   4903  S  SG    A CYS A 1 316 ? -9.578  0.549   47.277  0.50 33.11 ? 316 CYS A SG    1 
ATOM   4904  S  SG    B CYS A 1 316 ? -10.378 0.151   47.238  0.50 31.70 ? 316 CYS A SG    1 
ATOM   4905  N  N     A LEU A 1 317 ? -9.108  -3.287  50.315  0.50 21.25 ? 317 LEU A N     1 
ATOM   4906  N  N     B LEU A 1 317 ? -9.130  -3.526  50.280  0.50 21.93 ? 317 LEU A N     1 
ATOM   4907  C  CA    A LEU A 1 317 ? -9.022  -4.688  50.699  0.50 24.58 ? 317 LEU A CA    1 
ATOM   4908  C  CA    B LEU A 1 317 ? -8.984  -4.927  50.659  0.50 24.37 ? 317 LEU A CA    1 
ATOM   4909  C  C     A LEU A 1 317 ? -10.251 -5.434  50.201  0.50 25.08 ? 317 LEU A C     1 
ATOM   4910  C  C     B LEU A 1 317 ? -10.320 -5.633  50.452  0.50 25.37 ? 317 LEU A C     1 
ATOM   4911  O  O     A LEU A 1 317 ? -11.385 -4.994  50.422  0.50 25.97 ? 317 LEU A O     1 
ATOM   4912  O  O     B LEU A 1 317 ? -11.301 -5.327  51.142  0.50 23.00 ? 317 LEU A O     1 
ATOM   4913  C  CB    A LEU A 1 317 ? -8.894  -4.832  52.215  0.50 28.67 ? 317 LEU A CB    1 
ATOM   4914  C  CB    B LEU A 1 317 ? -8.510  -5.051  52.106  0.50 28.28 ? 317 LEU A CB    1 
ATOM   4915  C  CG    A LEU A 1 317 ? -7.474  -4.640  52.745  0.50 26.16 ? 317 LEU A CG    1 
ATOM   4916  C  CG    B LEU A 1 317 ? -7.221  -4.293  52.441  0.50 23.13 ? 317 LEU A CG    1 
ATOM   4917  C  CD1   A LEU A 1 317 ? -7.490  -4.473  54.250  0.50 30.21 ? 317 LEU A CD1   1 
ATOM   4918  C  CD1   B LEU A 1 317 ? -7.387  -3.517  53.736  0.50 33.67 ? 317 LEU A CD1   1 
ATOM   4919  C  CD2   A LEU A 1 317 ? -6.635  -5.833  52.358  0.50 30.23 ? 317 LEU A CD2   1 
ATOM   4920  C  CD2   B LEU A 1 317 ? -6.046  -5.248  52.547  0.50 26.60 ? 317 LEU A CD2   1 
ATOM   4921  N  N     A LEU A 1 318 ? -10.021 -6.562  49.533  0.50 20.49 ? 318 LEU A N     1 
ATOM   4922  N  N     B LEU A 1 318 ? -10.350 -6.582  49.512  0.50 20.53 ? 318 LEU A N     1 
ATOM   4923  C  CA    A LEU A 1 318 ? -11.083 -7.408  49.002  0.50 20.98 ? 318 LEU A CA    1 
ATOM   4924  C  CA    B LEU A 1 318 ? -11.575 -7.259  49.079  0.50 20.72 ? 318 LEU A CA    1 
ATOM   4925  C  C     A LEU A 1 318 ? -10.933 -8.787  49.633  0.50 21.44 ? 318 LEU A C     1 
ATOM   4926  C  C     B LEU A 1 318 ? -11.527 -8.713  49.539  0.50 22.71 ? 318 LEU A C     1 
ATOM   4927  O  O     A LEU A 1 318 ? -10.001 -9.528  49.299  0.50 19.55 ? 318 LEU A O     1 
ATOM   4928  O  O     B LEU A 1 318 ? -10.824 -9.535  48.945  0.50 20.16 ? 318 LEU A O     1 
ATOM   4929  C  CB    A LEU A 1 318 ? -11.013 -7.477  47.475  0.50 25.30 ? 318 LEU A CB    1 
ATOM   4930  C  CB    B LEU A 1 318 ? -11.729 -7.182  47.563  0.50 24.58 ? 318 LEU A CB    1 
ATOM   4931  C  CG    A LEU A 1 318 ? -10.815 -6.131  46.767  0.50 23.76 ? 318 LEU A CG    1 
ATOM   4932  C  CG    B LEU A 1 318 ? -11.974 -5.818  46.928  0.50 22.80 ? 318 LEU A CG    1 
ATOM   4933  C  CD1   A LEU A 1 318 ? -10.411 -6.323  45.300  0.50 18.93 ? 318 LEU A CD1   1 
ATOM   4934  C  CD1   B LEU A 1 318 ? -11.543 -5.847  45.479  0.50 32.26 ? 318 LEU A CD1   1 
ATOM   4935  C  CD2   A LEU A 1 318 ? -12.058 -5.274  46.865  0.50 25.14 ? 318 LEU A CD2   1 
ATOM   4936  C  CD2   B LEU A 1 318 ? -13.447 -5.453  47.046  0.50 22.07 ? 318 LEU A CD2   1 
ATOM   4937  N  N     A TYR A 1 319 ? -11.829 -9.120  50.561  0.50 20.90 ? 319 TYR A N     1 
ATOM   4938  N  N     B TYR A 1 319 ? -12.302 -9.040  50.568  0.50 20.21 ? 319 TYR A N     1 
ATOM   4939  C  CA    A TYR A 1 319 ? -11.827 -10.412 51.232  0.50 19.29 ? 319 TYR A CA    1 
ATOM   4940  C  CA    B TYR A 1 319 ? -12.262 -10.371 51.155  0.50 20.68 ? 319 TYR A CA    1 
ATOM   4941  C  C     A TYR A 1 319 ? -12.862 -11.341 50.607  0.50 21.64 ? 319 TYR A C     1 
ATOM   4942  C  C     B TYR A 1 319 ? -13.281 -11.303 50.508  0.50 21.49 ? 319 TYR A C     1 
ATOM   4943  O  O     A TYR A 1 319 ? -13.895 -10.897 50.100  0.50 21.04 ? 319 TYR A O     1 
ATOM   4944  O  O     B TYR A 1 319 ? -14.356 -10.880 50.079  0.50 21.71 ? 319 TYR A O     1 
ATOM   4945  C  CB    A TYR A 1 319 ? -12.128 -10.265 52.726  0.50 25.30 ? 319 TYR A CB    1 
ATOM   4946  C  CB    B TYR A 1 319 ? -12.514 -10.300 52.663  0.50 26.62 ? 319 TYR A CB    1 
ATOM   4947  C  CG    A TYR A 1 319 ? -11.118 -9.458  53.504  0.50 21.41 ? 319 TYR A CG    1 
ATOM   4948  C  CG    B TYR A 1 319 ? -11.348 -9.727  53.420  0.50 20.40 ? 319 TYR A CG    1 
ATOM   4949  C  CD1   A TYR A 1 319 ? -9.985  -10.060 54.040  0.50 19.80 ? 319 TYR A CD1   1 
ATOM   4950  C  CD1   B TYR A 1 319 ? -10.325 -10.550 53.875  0.50 20.09 ? 319 TYR A CD1   1 
ATOM   4951  C  CD2   A TYR A 1 319 ? -11.298 -8.097  53.707  0.50 18.73 ? 319 TYR A CD2   1 
ATOM   4952  C  CD2   B TYR A 1 319 ? -11.248 -8.364  53.649  0.50 18.72 ? 319 TYR A CD2   1 
ATOM   4953  C  CE1   A TYR A 1 319 ? -9.060  -9.328  54.754  0.50 24.58 ? 319 TYR A CE1   1 
ATOM   4954  C  CE1   B TYR A 1 319 ? -9.247  -10.034 54.557  0.50 19.88 ? 319 TYR A CE1   1 
ATOM   4955  C  CE2   A TYR A 1 319 ? -10.377 -7.356  54.420  0.50 23.44 ? 319 TYR A CE2   1 
ATOM   4956  C  CE2   B TYR A 1 319 ? -10.171 -7.836  54.325  0.50 23.50 ? 319 TYR A CE2   1 
ATOM   4957  C  CZ    A TYR A 1 319 ? -9.259  -7.975  54.939  0.50 24.51 ? 319 TYR A CZ    1 
ATOM   4958  C  CZ    B TYR A 1 319 ? -9.171  -8.673  54.776  0.50 25.49 ? 319 TYR A CZ    1 
ATOM   4959  O  OH    A TYR A 1 319 ? -8.344  -7.244  55.653  0.50 23.49 ? 319 TYR A OH    1 
ATOM   4960  O  OH    B TYR A 1 319 ? -8.095  -8.150  55.453  0.50 19.58 ? 319 TYR A OH    1 
ATOM   4961  N  N     A ARG A 1 320 ? -12.579 -12.643 50.665  0.50 20.05 ? 320 ARG A N     1 
ATOM   4962  N  N     B ARG A 1 320 ? -12.932 -12.588 50.457  0.50 19.98 ? 320 ARG A N     1 
ATOM   4963  C  CA    A ARG A 1 320 ? -13.497 -13.672 50.184  0.50 23.49 ? 320 ARG A CA    1 
ATOM   4964  C  CA    B ARG A 1 320 ? -13.822 -13.640 49.984  0.50 24.00 ? 320 ARG A CA    1 
ATOM   4965  C  C     A ARG A 1 320 ? -13.475 -14.837 51.159  0.50 25.37 ? 320 ARG A C     1 
ATOM   4966  C  C     B ARG A 1 320 ? -13.853 -14.745 51.028  0.50 25.88 ? 320 ARG A C     1 
ATOM   4967  O  O     A ARG A 1 320 ? -12.448 -15.506 51.300  0.50 25.24 ? 320 ARG A O     1 
ATOM   4968  O  O     B ARG A 1 320 ? -12.798 -15.265 51.403  0.50 25.95 ? 320 ARG A O     1 
ATOM   4969  C  CB    A ARG A 1 320 ? -13.124 -14.160 48.775  0.50 21.63 ? 320 ARG A CB    1 
ATOM   4970  C  CB    B ARG A 1 320 ? -13.357 -14.205 48.638  0.50 21.08 ? 320 ARG A CB    1 
ATOM   4971  C  CG    A ARG A 1 320 ? -13.283 -13.132 47.672  0.50 26.10 ? 320 ARG A CG    1 
ATOM   4972  C  CG    B ARG A 1 320 ? -13.233 -13.180 47.538  0.50 26.33 ? 320 ARG A CG    1 
ATOM   4973  C  CD    A ARG A 1 320 ? -12.864 -13.698 46.310  0.50 28.07 ? 320 ARG A CD    1 
ATOM   4974  C  CD    B ARG A 1 320 ? -12.774 -13.831 46.242  0.50 27.94 ? 320 ARG A CD    1 
ATOM   4975  N  NE    A ARG A 1 320 ? -13.994 -14.195 45.532  0.50 23.63 ? 320 ARG A NE    1 
ATOM   4976  N  NE    B ARG A 1 320 ? -13.836 -14.593 45.597  0.50 24.51 ? 320 ARG A NE    1 
ATOM   4977  C  CZ    A ARG A 1 320 ? -13.978 -14.372 44.216  0.50 32.92 ? 320 ARG A CZ    1 
ATOM   4978  C  CZ    B ARG A 1 320 ? -13.741 -15.124 44.384  0.50 30.21 ? 320 ARG A CZ    1 
ATOM   4979  N  NH1   A ARG A 1 320 ? -12.909 -14.077 43.490  0.50 22.28 ? 320 ARG A NH1   1 
ATOM   4980  N  NH1   B ARG A 1 320 ? -12.641 -14.998 43.658  0.50 27.06 ? 320 ARG A NH1   1 
ATOM   4981  N  NH2   A ARG A 1 320 ? -15.063 -14.848 43.611  0.50 28.57 ? 320 ARG A NH2   1 
ATOM   4982  N  NH2   B ARG A 1 320 ? -14.779 -15.788 43.882  0.50 31.05 ? 320 ARG A NH2   1 
ATOM   4983  N  N     A GLY A 1 321 ? -14.601 -15.080 51.834  0.50 25.84 ? 321 GLY A N     1 
ATOM   4984  N  N     B GLY A 1 321 ? -15.050 -15.096 51.507  0.50 24.22 ? 321 GLY A N     1 
ATOM   4985  C  CA    A GLY A 1 321 ? -14.782 -16.278 52.632  0.50 23.93 ? 321 GLY A CA    1 
ATOM   4986  C  CA    B GLY A 1 321 ? -15.177 -16.262 52.363  0.50 22.27 ? 321 GLY A CA    1 
ATOM   4987  C  C     A GLY A 1 321 ? -15.163 -15.950 54.072  0.50 19.70 ? 321 GLY A C     1 
ATOM   4988  C  C     B GLY A 1 321 ? -15.568 -16.016 53.810  0.50 20.02 ? 321 GLY A C     1 
ATOM   4989  O  O     A GLY A 1 321 ? -15.936 -15.021 54.331  0.50 24.54 ? 321 GLY A O     1 
ATOM   4990  O  O     B GLY A 1 321 ? -16.228 -15.024 54.132  0.50 25.04 ? 321 GLY A O     1 
ATOM   4991  N  N     A ASP A 1 322 ? -14.602 -16.722 55.003  0.50 20.96 ? 322 ASP A N     1 
ATOM   4992  N  N     B ASP A 1 322 ? -15.152 -16.934 54.684  0.50 20.69 ? 322 ASP A N     1 
ATOM   4993  C  CA    A ASP A 1 322 ? -14.975 -16.685 56.421  0.50 22.32 ? 322 ASP A CA    1 
ATOM   4994  C  CA    B ASP A 1 322 ? -15.572 -16.957 56.086  0.50 21.03 ? 322 ASP A CA    1 
ATOM   4995  C  C     A ASP A 1 322 ? -14.253 -15.520 57.096  0.50 22.55 ? 322 ASP A C     1 
ATOM   4996  C  C     B ASP A 1 322 ? -14.796 -15.889 56.850  0.50 22.17 ? 322 ASP A C     1 
ATOM   4997  O  O     A ASP A 1 322 ? -13.208 -15.672 57.735  0.50 25.90 ? 322 ASP A O     1 
ATOM   4998  O  O     B ASP A 1 322 ? -13.824 -16.162 57.558  0.50 21.74 ? 322 ASP A O     1 
ATOM   4999  C  CB    A ASP A 1 322 ? -14.637 -18.017 57.079  0.50 21.42 ? 322 ASP A CB    1 
ATOM   5000  C  CB    B ASP A 1 322 ? -15.348 -18.345 56.668  0.50 23.04 ? 322 ASP A CB    1 
ATOM   5001  C  CG    A ASP A 1 322 ? -15.052 -18.082 58.540  0.50 25.87 ? 322 ASP A CG    1 
ATOM   5002  C  CG    B ASP A 1 322 ? -15.759 -18.446 58.127  0.50 22.05 ? 322 ASP A CG    1 
ATOM   5003  O  OD1   A ASP A 1 322 ? -15.881 -17.258 58.977  0.50 20.51 ? 322 ASP A OD1   1 
ATOM   5004  O  OD1   B ASP A 1 322 ? -16.630 -17.664 58.565  0.50 24.80 ? 322 ASP A OD1   1 
ATOM   5005  O  OD2   A ASP A 1 322 ? -14.533 -18.961 59.257  0.50 24.82 ? 322 ASP A OD2   1 
ATOM   5006  O  OD2   B ASP A 1 322 ? -15.192 -19.300 58.837  0.50 28.44 ? 322 ASP A OD2   1 
ATOM   5007  N  N     A VAL A 1 323 ? -14.828 -14.328 56.950  0.50 21.34 ? 323 VAL A N     1 
ATOM   5008  N  N     B VAL A 1 323 ? -15.248 -14.644 56.708  0.50 21.68 ? 323 VAL A N     1 
ATOM   5009  C  CA    A VAL A 1 323 ? -14.185 -13.081 57.359  0.50 24.47 ? 323 VAL A CA    1 
ATOM   5010  C  CA    B VAL A 1 323 ? -14.508 -13.474 57.171  0.50 22.79 ? 323 VAL A CA    1 
ATOM   5011  C  C     A VAL A 1 323 ? -15.188 -12.249 58.153  0.50 26.61 ? 323 VAL A C     1 
ATOM   5012  C  C     B VAL A 1 323 ? -15.438 -12.612 58.018  0.50 25.60 ? 323 VAL A C     1 
ATOM   5013  O  O     A VAL A 1 323 ? -16.169 -11.749 57.587  0.50 25.07 ? 323 VAL A O     1 
ATOM   5014  O  O     B VAL A 1 323 ? -16.367 -11.990 57.488  0.50 25.56 ? 323 VAL A O     1 
ATOM   5015  C  CB    A VAL A 1 323 ? -13.655 -12.290 56.150  0.50 23.89 ? 323 VAL A CB    1 
ATOM   5016  C  CB    B VAL A 1 323 ? -13.929 -12.664 56.001  0.50 24.42 ? 323 VAL A CB    1 
ATOM   5017  C  CG1   A VAL A 1 323 ? -13.090 -10.963 56.589  0.50 25.65 ? 323 VAL A CG1   1 
ATOM   5018  C  CG1   B VAL A 1 323 ? -13.303 -11.378 56.494  0.50 25.55 ? 323 VAL A CG1   1 
ATOM   5019  C  CG2   A VAL A 1 323 ? -12.596 -13.095 55.408  0.50 25.11 ? 323 VAL A CG2   1 
ATOM   5020  C  CG2   B VAL A 1 323 ? -12.904 -13.494 55.243  0.50 25.11 ? 323 VAL A CG2   1 
ATOM   5021  N  N     A VAL A 1 324 ? -14.933 -12.084 59.451  0.50 25.77 ? 324 VAL A N     1 
ATOM   5022  N  N     B VAL A 1 324 ? -15.178 -12.558 59.320  0.50 25.40 ? 324 VAL A N     1 
ATOM   5023  C  CA    A VAL A 1 324 ? -15.763 -11.260 60.332  0.50 26.11 ? 324 VAL A CA    1 
ATOM   5024  C  CA    B VAL A 1 324 ? -15.980 -11.738 60.233  0.50 26.66 ? 324 VAL A CA    1 
ATOM   5025  C  C     A VAL A 1 324 ? -15.301 -9.811  60.240  0.50 23.40 ? 324 VAL A C     1 
ATOM   5026  C  C     B VAL A 1 324 ? -15.455 -10.305 60.202  0.50 24.49 ? 324 VAL A C     1 
ATOM   5027  O  O     A VAL A 1 324 ? -14.106 -9.534  60.414  0.50 26.51 ? 324 VAL A O     1 
ATOM   5028  O  O     B VAL A 1 324 ? -14.237 -10.098 60.324  0.50 24.28 ? 324 VAL A O     1 
ATOM   5029  C  CB    A VAL A 1 324 ? -15.714 -11.759 61.787  0.50 21.56 ? 324 VAL A CB    1 
ATOM   5030  C  CB    B VAL A 1 324 ? -15.934 -12.309 61.650  0.50 24.02 ? 324 VAL A CB    1 
ATOM   5031  C  CG1   A VAL A 1 324 ? -16.554 -10.865 62.688  0.50 26.84 ? 324 VAL A CG1   1 
ATOM   5032  C  CG1   B VAL A 1 324 ? -16.935 -11.601 62.544  0.50 24.75 ? 324 VAL A CG1   1 
ATOM   5033  C  CG2   A VAL A 1 324 ? -16.187 -13.201 61.880  0.50 23.06 ? 324 VAL A CG2   1 
ATOM   5034  C  CG2   B VAL A 1 324 ? -16.201 -13.807 61.628  0.50 22.95 ? 324 VAL A CG2   1 
ATOM   5035  N  N     A PRO A 1 325 ? -16.213 -8.864  59.991  0.50 22.93 ? 325 PRO A N     1 
ATOM   5036  N  N     B PRO A 1 325 ? -16.332 -9.304  60.066  0.50 24.14 ? 325 PRO A N     1 
ATOM   5037  C  CA    A PRO A 1 325 ? -15.799 -7.456  59.836  0.50 22.85 ? 325 PRO A CA    1 
ATOM   5038  C  CA    B PRO A 1 325 ? -15.848 -7.921  59.881  0.50 23.08 ? 325 PRO A CA    1 
ATOM   5039  C  C     A PRO A 1 325 ? -15.030 -6.903  61.021  0.50 28.38 ? 325 PRO A C     1 
ATOM   5040  C  C     B PRO A 1 325 ? -15.001 -7.380  61.023  0.50 29.26 ? 325 PRO A C     1 
ATOM   5041  O  O     A PRO A 1 325 ? -14.127 -6.082  60.829  0.50 24.10 ? 325 PRO A O     1 
ATOM   5042  O  O     B PRO A 1 325 ? -13.969 -6.750  60.767  0.50 23.80 ? 325 PRO A O     1 
ATOM   5043  C  CB    A PRO A 1 325 ? -17.136 -6.729  59.633  0.50 25.86 ? 325 PRO A CB    1 
ATOM   5044  C  CB    B PRO A 1 325 ? -17.151 -7.128  59.712  0.50 25.32 ? 325 PRO A CB    1 
ATOM   5045  C  CG    A PRO A 1 325 ? -18.041 -7.767  59.045  0.50 25.68 ? 325 PRO A CG    1 
ATOM   5046  C  CG    B PRO A 1 325 ? -18.134 -8.117  59.176  0.50 24.45 ? 325 PRO A CG    1 
ATOM   5047  C  CD    A PRO A 1 325 ? -17.640 -9.066  59.679  0.50 26.67 ? 325 PRO A CD    1 
ATOM   5048  C  CD    B PRO A 1 325 ? -17.780 -9.428  59.822  0.50 26.16 ? 325 PRO A CD    1 
ATOM   5049  N  N     A LYS A 1 326 ? -15.365 -7.324  62.245  0.50 28.20 ? 326 LYS A N     1 
ATOM   5050  N  N     B LYS A 1 326 ? -15.412 -7.583  62.281  0.50 28.43 ? 326 LYS A N     1 
ATOM   5051  C  CA    A LYS A 1 326 ? -14.582 -6.909  63.403  0.50 30.90 ? 326 LYS A CA    1 
ATOM   5052  C  CA    B LYS A 1 326 ? -14.643 -7.033  63.394  0.50 30.94 ? 326 LYS A CA    1 
ATOM   5053  C  C     A LYS A 1 326 ? -13.150 -7.425  63.313  0.50 29.37 ? 326 LYS A C     1 
ATOM   5054  C  C     B LYS A 1 326 ? -13.224 -7.585  63.442  0.50 29.71 ? 326 LYS A C     1 
ATOM   5055  O  O     A LYS A 1 326 ? -12.203 -6.716  63.674  0.50 32.92 ? 326 LYS A O     1 
ATOM   5056  O  O     B LYS A 1 326 ? -12.351 -6.967  64.061  0.50 32.29 ? 326 LYS A O     1 
ATOM   5057  C  CB    A LYS A 1 326 ? -15.246 -7.397  64.690  0.50 29.62 ? 326 LYS A CB    1 
ATOM   5058  C  CB    B LYS A 1 326 ? -15.354 -7.304  64.723  0.50 29.52 ? 326 LYS A CB    1 
ATOM   5059  C  CG    A LYS A 1 326 ? -14.388 -7.223  65.929  0.50 35.93 ? 326 LYS A CG    1 
ATOM   5060  C  CG    B LYS A 1 326 ? -15.386 -8.769  65.125  0.50 28.53 ? 326 LYS A CG    1 
ATOM   5061  C  CD    A LYS A 1 326 ? -14.937 -8.014  67.106  0.50 33.78 ? 326 LYS A CD    1 
ATOM   5062  C  CD    B LYS A 1 326 ? -16.113 -8.964  66.444  0.50 25.26 ? 326 LYS A CD    1 
ATOM   5063  C  CE    A LYS A 1 326 ? -14.929 -9.506  66.814  0.50 37.78 ? 326 LYS A CE    1 
ATOM   5064  C  CE    B LYS A 1 326 ? -16.378 -10.440 66.712  0.50 32.73 ? 326 LYS A CE    1 
ATOM   5065  N  NZ    A LYS A 1 326 ? -13.559 -10.009 66.490  0.50 27.23 ? 326 LYS A NZ    1 
ATOM   5066  N  NZ    B LYS A 1 326 ? -15.136 -11.265 66.700  0.50 34.15 ? 326 LYS A NZ    1 
ATOM   5067  N  N     A ASP A 1 327 ? -12.971 -8.659  62.835  0.50 28.86 ? 327 ASP A N     1 
ATOM   5068  N  N     B ASP A 1 327 ? -12.973 -8.730  62.808  0.50 28.87 ? 327 ASP A N     1 
ATOM   5069  C  CA    A ASP A 1 327 ? -11.621 -9.197  62.693  0.50 27.21 ? 327 ASP A CA    1 
ATOM   5070  C  CA    B ASP A 1 327 ? -11.607 -9.233  62.729  0.50 27.17 ? 327 ASP A CA    1 
ATOM   5071  C  C     A ASP A 1 327 ? -10.798 -8.385  61.700  0.50 28.72 ? 327 ASP A C     1 
ATOM   5072  C  C     B ASP A 1 327 ? -10.792 -8.490  61.676  0.50 28.72 ? 327 ASP A C     1 
ATOM   5073  O  O     A ASP A 1 327 ? -9.576  -8.271  61.854  0.50 33.26 ? 327 ASP A O     1 
ATOM   5074  O  O     B ASP A 1 327 ? -9.578  -8.325  61.842  0.50 33.28 ? 327 ASP A O     1 
ATOM   5075  C  CB    A ASP A 1 327 ? -11.676 -10.665 62.266  0.50 24.89 ? 327 ASP A CB    1 
ATOM   5076  C  CB    B ASP A 1 327 ? -11.610 -10.735 62.441  0.50 24.41 ? 327 ASP A CB    1 
ATOM   5077  C  CG    A ASP A 1 327 ? -12.114 -11.589 63.384  0.50 32.94 ? 327 ASP A CG    1 
ATOM   5078  C  CG    B ASP A 1 327 ? -12.177 -11.547 63.587  0.50 33.02 ? 327 ASP A CG    1 
ATOM   5079  O  OD1   A ASP A 1 327 ? -11.805 -11.298 64.561  0.50 28.92 ? 327 ASP A OD1   1 
ATOM   5080  O  OD1   B ASP A 1 327 ? -12.806 -10.946 64.484  0.50 30.66 ? 327 ASP A OD1   1 
ATOM   5081  O  OD2   A ASP A 1 327 ? -12.760 -12.614 63.079  0.50 26.02 ? 327 ASP A OD2   1 
ATOM   5082  O  OD2   B ASP A 1 327 ? -11.985 -12.782 63.592  0.50 29.12 ? 327 ASP A OD2   1 
ATOM   5083  N  N     A VAL A 1 328 ? -11.444 -7.811  60.682  0.50 28.04 ? 328 VAL A N     1 
ATOM   5084  N  N     B VAL A 1 328 ? -11.432 -8.031  60.599  0.50 27.73 ? 328 VAL A N     1 
ATOM   5085  C  CA    A VAL A 1 328 ? -10.726 -6.945  59.748  0.50 28.24 ? 328 VAL A CA    1 
ATOM   5086  C  CA    B VAL A 1 328 ? -10.724 -7.214  59.616  0.50 27.37 ? 328 VAL A CA    1 
ATOM   5087  C  C     A VAL A 1 328 ? -10.222 -5.697  60.460  0.50 31.51 ? 328 VAL A C     1 
ATOM   5088  C  C     B VAL A 1 328 ? -10.380 -5.854  60.208  0.50 30.53 ? 328 VAL A C     1 
ATOM   5089  O  O     A VAL A 1 328 ? -9.110  -5.221  60.199  0.50 31.66 ? 328 VAL A O     1 
ATOM   5090  O  O     B VAL A 1 328 ? -9.242  -5.383  60.098  0.50 31.33 ? 328 VAL A O     1 
ATOM   5091  C  CB    A VAL A 1 328 ? -11.625 -6.577  58.553  0.50 26.70 ? 328 VAL A CB    1 
ATOM   5092  C  CB    B VAL A 1 328 ? -11.554 -7.065  58.330  0.50 27.48 ? 328 VAL A CB    1 
ATOM   5093  C  CG1   A VAL A 1 328 ? -10.816 -5.812  57.504  0.50 24.83 ? 328 VAL A CG1   1 
ATOM   5094  C  CG1   B VAL A 1 328 ? -10.835 -6.137  57.350  0.50 24.95 ? 328 VAL A CG1   1 
ATOM   5095  C  CG2   A VAL A 1 328 ? -12.245 -7.820  57.958  0.50 24.74 ? 328 VAL A CG2   1 
ATOM   5096  C  CG2   B VAL A 1 328 ? -11.792 -8.416  57.700  0.50 23.66 ? 328 VAL A CG2   1 
ATOM   5097  N  N     A ASN A 1 329 ? -11.031 -5.149  61.371  0.50 26.99 ? 329 ASN A N     1 
ATOM   5098  N  N     B ASN A 1 329 ? -11.360 -5.205  60.848  0.50 27.72 ? 329 ASN A N     1 
ATOM   5099  C  CA    A ASN A 1 329 ? -10.647 -3.932  62.079  0.50 32.35 ? 329 ASN A CA    1 
ATOM   5100  C  CA    B ASN A 1 329 ? -11.114 -3.897  61.446  0.50 31.37 ? 329 ASN A CA    1 
ATOM   5101  C  C     A ASN A 1 329 ? -9.406  -4.159  62.932  0.50 34.61 ? 329 ASN A C     1 
ATOM   5102  C  C     B ASN A 1 329 ? -10.013 -3.968  62.495  0.50 30.80 ? 329 ASN A C     1 
ATOM   5103  O  O     A ASN A 1 329 ? -8.463  -3.359  62.903  0.50 31.99 ? 329 ASN A O     1 
ATOM   5104  O  O     B ASN A 1 329 ? -9.172  -3.064  62.584  0.50 33.17 ? 329 ASN A O     1 
ATOM   5105  C  CB    A ASN A 1 329 ? -11.808 -3.437  62.944  0.50 30.06 ? 329 ASN A CB    1 
ATOM   5106  C  CB    B ASN A 1 329 ? -12.402 -3.342  62.058  0.50 32.56 ? 329 ASN A CB    1 
ATOM   5107  C  CG    A ASN A 1 329 ? -13.012 -3.027  62.123  0.50 32.37 ? 329 ASN A CG    1 
ATOM   5108  C  CG    B ASN A 1 329 ? -13.415 -2.928  61.007  0.50 35.88 ? 329 ASN A CG    1 
ATOM   5109  O  OD1   A ASN A 1 329 ? -12.881 -2.587  60.978  0.50 37.58 ? 329 ASN A OD1   1 
ATOM   5110  O  OD1   B ASN A 1 329 ? -14.597 -3.265  61.096  0.50 35.87 ? 329 ASN A OD1   1 
ATOM   5111  N  ND2   A ASN A 1 329 ? -14.198 -3.169  62.704  0.50 32.52 ? 329 ASN A ND2   1 
ATOM   5112  N  ND2   B ASN A 1 329 ? -12.953 -2.199  59.999  0.50 33.64 ? 329 ASN A ND2   1 
ATOM   5113  N  N     A ALA A 1 330 ? -9.387  -5.251  63.701  0.50 34.32 ? 330 ALA A N     1 
ATOM   5114  N  N     B ALA A 1 330 ? -10.001 -5.033  63.299  0.50 29.76 ? 330 ALA A N     1 
ATOM   5115  C  CA    A ALA A 1 330 ? -8.241  -5.521  64.563  0.50 33.41 ? 330 ALA A CA    1 
ATOM   5116  C  CA    B ALA A 1 330 ? -8.902  -5.227  64.239  0.50 34.94 ? 330 ALA A CA    1 
ATOM   5117  C  C     A ALA A 1 330 ? -6.985  -5.800  63.746  0.50 36.59 ? 330 ALA A C     1 
ATOM   5118  C  C     B ALA A 1 330 ? -7.580  -5.408  63.505  0.50 33.52 ? 330 ALA A C     1 
ATOM   5119  O  O     A ALA A 1 330 ? -5.880  -5.406  64.139  0.50 33.69 ? 330 ALA A O     1 
ATOM   5120  O  O     B ALA A 1 330 ? -6.551  -4.856  63.915  0.50 36.80 ? 330 ALA A O     1 
ATOM   5121  C  CB    A ALA A 1 330 ? -8.549  -6.692  65.497  0.50 29.05 ? 330 ALA A CB    1 
ATOM   5122  C  CB    B ALA A 1 330 ? -9.188  -6.426  65.143  0.50 30.50 ? 330 ALA A CB    1 
ATOM   5123  N  N     A ALA A 1 331 ? -7.135  -6.473  62.604  0.50 34.98 ? 331 ALA A N     1 
ATOM   5124  N  N     B ALA A 1 331 ? -7.589  -6.170  62.409  0.50 33.96 ? 331 ALA A N     1 
ATOM   5125  C  CA    A ALA A 1 331 ? -5.982  -6.738  61.751  0.50 31.55 ? 331 ALA A CA    1 
ATOM   5126  C  CA    B ALA A 1 331 ? -6.362  -6.387  61.650  0.50 32.56 ? 331 ALA A CA    1 
ATOM   5127  C  C     A ALA A 1 331 ? -5.436  -5.450  61.145  0.50 36.50 ? 331 ALA A C     1 
ATOM   5128  C  C     B ALA A 1 331 ? -5.841  -5.084  61.056  0.50 36.23 ? 331 ALA A C     1 
ATOM   5129  O  O     A ALA A 1 331 ? -4.217  -5.255  61.080  0.50 36.61 ? 331 ALA A O     1 
ATOM   5130  O  O     B ALA A 1 331 ? -4.625  -4.861  61.000  0.50 36.05 ? 331 ALA A O     1 
ATOM   5131  C  CB    A ALA A 1 331 ? -6.364  -7.734  60.657  0.50 33.68 ? 331 ALA A CB    1 
ATOM   5132  C  CB    B ALA A 1 331 ? -6.603  -7.424  60.554  0.50 33.59 ? 331 ALA A CB    1 
ATOM   5133  N  N     A ILE A 1 332 ? -6.324  -4.555  60.708  0.50 34.18 ? 332 ILE A N     1 
ATOM   5134  N  N     B ILE A 1 332 ? -6.745  -4.206  60.613  0.50 34.09 ? 332 ILE A N     1 
ATOM   5135  C  CA    A ILE A 1 332 ? -5.883  -3.290  60.130  0.50 37.59 ? 332 ILE A CA    1 
ATOM   5136  C  CA    B ILE A 1 332 ? -6.320  -2.911  60.088  0.50 37.52 ? 332 ILE A CA    1 
ATOM   5137  C  C     A ILE A 1 332 ? -5.361  -2.355  61.212  0.50 43.09 ? 332 ILE A C     1 
ATOM   5138  C  C     B ILE A 1 332 ? -5.653  -2.088  61.179  0.50 42.94 ? 332 ILE A C     1 
ATOM   5139  O  O     A ILE A 1 332 ? -4.323  -1.705  61.038  0.50 46.50 ? 332 ILE A O     1 
ATOM   5140  O  O     B ILE A 1 332 ? -4.721  -1.320  60.910  0.50 45.98 ? 332 ILE A O     1 
ATOM   5141  C  CB    A ILE A 1 332 ? -7.027  -2.641  59.332  0.50 35.54 ? 332 ILE A CB    1 
ATOM   5142  C  CB    B ILE A 1 332 ? -7.517  -2.167  59.461  0.50 30.79 ? 332 ILE A CB    1 
ATOM   5143  C  CG1   A ILE A 1 332 ? -7.288  -3.419  58.040  0.50 33.34 ? 332 ILE A CG1   1 
ATOM   5144  C  CG1   B ILE A 1 332 ? -8.132  -3.007  58.339  0.50 37.37 ? 332 ILE A CG1   1 
ATOM   5145  C  CG2   A ILE A 1 332 ? -6.716  -1.181  59.030  0.50 34.74 ? 332 ILE A CG2   1 
ATOM   5146  C  CG2   B ILE A 1 332 ? -7.093  -0.807  58.928  0.50 34.97 ? 332 ILE A CG2   1 
ATOM   5147  C  CD1   A ILE A 1 332 ? -8.497  -2.910  57.276  0.50 29.17 ? 332 ILE A CD1   1 
ATOM   5148  C  CD1   B ILE A 1 332 ? -7.104  -3.632  57.412  0.50 31.26 ? 332 ILE A CD1   1 
ATOM   5149  N  N     A ALA A 1 333 ? -6.068  -2.270  62.345  0.50 36.60 ? 333 ALA A N     1 
ATOM   5150  N  N     B ALA A 1 333 ? -6.103  -2.239  62.426  0.50 36.60 ? 333 ALA A N     1 
ATOM   5151  C  CA    A ALA A 1 333 ? -5.672  -1.348  63.407  0.50 44.46 ? 333 ALA A CA    1 
ATOM   5152  C  CA    B ALA A 1 333 ? -5.431  -1.571  63.533  0.50 43.72 ? 333 ALA A CA    1 
ATOM   5153  C  C     A ALA A 1 333 ? -4.244  -1.599  63.868  0.50 40.27 ? 333 ALA A C     1 
ATOM   5154  C  C     B ALA A 1 333 ? -4.025  -2.121  63.733  0.50 39.20 ? 333 ALA A C     1 
ATOM   5155  O  O     A ALA A 1 333 ? -3.576  -0.677  64.350  0.50 46.96 ? 333 ALA A O     1 
ATOM   5156  O  O     B ALA A 1 333 ? -3.083  -1.359  63.975  0.50 46.57 ? 333 ALA A O     1 
ATOM   5157  C  CB    A ALA A 1 333 ? -6.637  -1.450  64.590  0.50 36.82 ? 333 ALA A CB    1 
ATOM   5158  C  CB    B ALA A 1 333 ? -6.255  -1.713  64.814  0.50 37.76 ? 333 ALA A CB    1 
ATOM   5159  N  N     A THR A 1 334 ? -3.759  -2.833  63.727  0.50 39.35 ? 334 THR A N     1 
ATOM   5160  N  N     B THR A 1 334 ? -3.863  -3.443  63.620  0.50 39.00 ? 334 THR A N     1 
ATOM   5161  C  CA    A THR A 1 334 ? -2.350  -3.103  63.985  0.50 43.49 ? 334 THR A CA    1 
ATOM   5162  C  CA    B THR A 1 334 ? -2.545  -4.044  63.801  0.50 41.85 ? 334 THR A CA    1 
ATOM   5163  C  C     A THR A 1 334 ? -1.469  -2.503  62.892  0.50 48.84 ? 334 THR A C     1 
ATOM   5164  C  C     B THR A 1 334 ? -1.588  -3.662  62.679  0.50 45.55 ? 334 THR A C     1 
ATOM   5165  O  O     A THR A 1 334 ? -0.385  -1.977  63.177  0.50 50.49 ? 334 THR A O     1 
ATOM   5166  O  O     B THR A 1 334 ? -0.379  -3.549  62.914  0.50 53.67 ? 334 THR A O     1 
ATOM   5167  C  CB    A THR A 1 334 ? -2.120  -4.612  64.098  0.50 42.58 ? 334 THR A CB    1 
ATOM   5168  C  CB    B THR A 1 334 ? -2.659  -5.565  63.891  0.50 43.08 ? 334 THR A CB    1 
ATOM   5169  O  OG1   A THR A 1 334 ? -2.876  -5.133  65.199  0.50 45.47 ? 334 THR A OG1   1 
ATOM   5170  O  OG1   B THR A 1 334 ? -3.328  -6.066  62.727  0.50 44.71 ? 334 THR A OG1   1 
ATOM   5171  C  CG2   A THR A 1 334 ? -0.644  -4.924  64.312  0.50 45.88 ? 334 THR A CG2   1 
ATOM   5172  C  CG2   B THR A 1 334 ? -3.429  -5.976  65.139  0.50 41.02 ? 334 THR A CG2   1 
ATOM   5173  N  N     A ILE A 1 335 ? -1.929  -2.555  61.639  0.50 47.86 ? 335 ILE A N     1 
ATOM   5174  N  N     B ILE A 1 335 ? -2.095  -3.462  61.464  0.50 44.93 ? 335 ILE A N     1 
ATOM   5175  C  CA    A ILE A 1 335 ? -1.110  -2.107  60.514  0.50 48.75 ? 335 ILE A CA    1 
ATOM   5176  C  CA    B ILE A 1 335 ? -1.244  -3.078  60.343  0.50 48.35 ? 335 ILE A CA    1 
ATOM   5177  C  C     A ILE A 1 335 ? -0.877  -0.602  60.567  0.50 52.02 ? 335 ILE A C     1 
ATOM   5178  C  C     B ILE A 1 335 ? -1.351  -1.573  60.134  0.50 50.49 ? 335 ILE A C     1 
ATOM   5179  O  O     A ILE A 1 335 ? 0.200   -0.121  60.191  0.50 54.84 ? 335 ILE A O     1 
ATOM   5180  O  O     B ILE A 1 335 ? -1.693  -1.102  59.043  0.50 53.97 ? 335 ILE A O     1 
ATOM   5181  C  CB    A ILE A 1 335 ? -1.762  -2.544  59.186  0.50 47.95 ? 335 ILE A CB    1 
ATOM   5182  C  CB    B ILE A 1 335 ? -1.611  -3.857  59.067  0.50 45.17 ? 335 ILE A CB    1 
ATOM   5183  C  CG1   A ILE A 1 335 ? -1.079  -3.798  58.641  0.50 45.15 ? 335 ILE A CG1   1 
ATOM   5184  C  CG1   B ILE A 1 335 ? -1.905  -5.317  59.408  0.50 42.96 ? 335 ILE A CG1   1 
ATOM   5185  C  CG2   A ILE A 1 335 ? -1.724  -1.427  58.152  0.50 48.59 ? 335 ILE A CG2   1 
ATOM   5186  C  CG2   B ILE A 1 335 ? -0.473  -3.803  58.064  0.50 47.35 ? 335 ILE A CG2   1 
ATOM   5187  C  CD1   A ILE A 1 335 ? -1.247  -5.006  59.516  0.50 45.62 ? 335 ILE A CD1   1 
ATOM   5188  C  CD1   B ILE A 1 335 ? -2.032  -6.212  58.201  0.50 36.16 ? 335 ILE A CD1   1 
ATOM   5189  N  N     A LYS A 1 336 ? -1.863  0.165   61.038  0.50 51.99 ? 336 LYS A N     1 
ATOM   5190  N  N     B LYS A 1 336 ? -1.070  -0.811  61.189  0.50 51.98 ? 336 LYS A N     1 
ATOM   5191  C  CA    A LYS A 1 336 ? -1.706  1.612   61.113  0.50 49.57 ? 336 LYS A CA    1 
ATOM   5192  C  CA    B LYS A 1 336 ? -1.016  0.643   61.113  0.50 53.09 ? 336 LYS A CA    1 
ATOM   5193  C  C     A LYS A 1 336 ? -0.688  2.035   62.165  0.50 53.26 ? 336 LYS A C     1 
ATOM   5194  C  C     B LYS A 1 336 ? 0.253   1.148   61.785  0.50 56.89 ? 336 LYS A C     1 
ATOM   5195  O  O     A LYS A 1 336 ? -0.138  3.137   62.069  0.50 59.03 ? 336 LYS A O     1 
ATOM   5196  O  O     B LYS A 1 336 ? 0.755   2.227   61.456  0.50 62.31 ? 336 LYS A O     1 
ATOM   5197  C  CB    A LYS A 1 336 ? -3.056  2.275   61.402  0.50 51.05 ? 336 LYS A CB    1 
ATOM   5198  C  CB    B LYS A 1 336 ? -2.247  1.271   61.770  0.50 51.78 ? 336 LYS A CB    1 
ATOM   5199  C  CG    A LYS A 1 336 ? -4.096  2.073   60.308  0.50 49.83 ? 336 LYS A CG    1 
ATOM   5200  C  CG    B LYS A 1 336 ? -3.381  1.604   60.815  0.50 52.17 ? 336 LYS A CG    1 
ATOM   5201  C  CD    A LYS A 1 336 ? -5.412  2.756   60.656  0.50 45.33 ? 336 LYS A CD    1 
ATOM   5202  C  CD    B LYS A 1 336 ? -4.564  2.190   61.570  0.50 48.57 ? 336 LYS A CD    1 
ATOM   5203  C  CE    A LYS A 1 336 ? -6.421  2.607   59.528  0.50 47.79 ? 336 LYS A CE    1 
ATOM   5204  C  CE    B LYS A 1 336 ? -4.178  3.453   62.328  0.50 43.96 ? 336 LYS A CE    1 
ATOM   5205  N  NZ    A LYS A 1 336 ? -7.755  3.175   59.875  0.50 53.10 ? 336 LYS A NZ    1 
ATOM   5206  N  NZ    B LYS A 1 336 ? -4.112  4.646   61.441  0.50 45.42 ? 336 LYS A NZ    1 
ATOM   5207  N  N     A THR A 1 337 ? -0.418  1.189   63.159  0.50 60.14 ? 337 THR A N     1 
ATOM   5208  N  N     B THR A 1 337 ? 0.779   0.367   62.728  0.50 59.77 ? 337 THR A N     1 
ATOM   5209  C  CA    A THR A 1 337 ? 0.478   1.541   64.255  0.50 57.42 ? 337 THR A CA    1 
ATOM   5210  C  CA    B THR A 1 337 ? 1.931   0.792   63.512  0.50 61.66 ? 337 THR A CA    1 
ATOM   5211  C  C     A THR A 1 337 ? 1.828   0.841   64.145  0.50 63.13 ? 337 THR A C     1 
ATOM   5212  C  C     B THR A 1 337 ? 3.028   -0.265  63.516  0.50 63.02 ? 337 THR A C     1 
ATOM   5213  O  O     A THR A 1 337 ? 2.861   1.498   63.979  0.50 63.26 ? 337 THR A O     1 
ATOM   5214  O  O     B THR A 1 337 ? 4.216   0.072   63.541  0.50 62.71 ? 337 THR A O     1 
ATOM   5215  C  CB    A THR A 1 337 ? -0.179  1.208   65.602  0.50 58.53 ? 337 THR A CB    1 
ATOM   5216  C  CB    B THR A 1 337 ? 1.507   1.115   64.947  0.50 60.88 ? 337 THR A CB    1 
ATOM   5217  O  OG1   A THR A 1 337 ? -0.520  -0.183  65.639  0.50 55.63 ? 337 THR A OG1   1 
ATOM   5218  O  OG1   B THR A 1 337 ? 0.743   0.025   65.478  0.50 58.54 ? 337 THR A OG1   1 
ATOM   5219  C  CG2   A THR A 1 337 ? -1.437  2.040   65.804  0.50 58.30 ? 337 THR A CG2   1 
ATOM   5220  C  CG2   B THR A 1 337 ? 0.669   2.385   64.983  0.50 58.97 ? 337 THR A CG2   1 
ATOM   5221  N  N     A LYS A 1 338 ? 1.835   -0.492  64.227  0.50 58.14 ? 338 LYS A N     1 
ATOM   5222  N  N     B LYS A 1 338 ? 2.647   -1.545  63.492  0.50 61.11 ? 338 LYS A N     1 
ATOM   5223  C  CA    A LYS A 1 338 ? 3.092   -1.226  64.337  0.50 61.49 ? 338 LYS A CA    1 
ATOM   5224  C  CA    B LYS A 1 338 ? 3.645   -2.609  63.529  0.50 62.16 ? 338 LYS A CA    1 
ATOM   5225  C  C     A LYS A 1 338 ? 3.956   -1.059  63.091  0.50 61.76 ? 338 LYS A C     1 
ATOM   5226  C  C     B LYS A 1 338 ? 4.451   -2.714  62.240  0.50 58.86 ? 338 LYS A C     1 
ATOM   5227  O  O     A LYS A 1 338 ? 5.173   -0.866  63.196  0.50 62.26 ? 338 LYS A O     1 
ATOM   5228  O  O     B LYS A 1 338 ? 5.457   -3.432  62.221  0.50 61.71 ? 338 LYS A O     1 
ATOM   5229  C  CB    A LYS A 1 338 ? 2.812   -2.706  64.599  0.50 61.10 ? 338 LYS A CB    1 
ATOM   5230  C  CB    B LYS A 1 338 ? 2.983   -3.956  63.839  0.50 61.59 ? 338 LYS A CB    1 
ATOM   5231  C  CG    A LYS A 1 338 ? 4.068   -3.549  64.765  0.50 61.91 ? 338 LYS A CG    1 
ATOM   5232  C  CG    B LYS A 1 338 ? 2.539   -4.740  62.616  0.50 55.79 ? 338 LYS A CG    1 
ATOM   5233  C  CD    A LYS A 1 338 ? 3.742   -5.008  65.042  0.50 61.99 ? 338 LYS A CD    1 
ATOM   5234  C  CD    B LYS A 1 338 ? 2.111   -6.151  62.989  0.50 53.31 ? 338 LYS A CD    1 
ATOM   5235  C  CE    A LYS A 1 338 ? 3.019   -5.175  66.370  0.50 55.91 ? 338 LYS A CE    1 
ATOM   5236  C  CE    B LYS A 1 338 ? 3.284   -6.968  63.513  0.50 59.19 ? 338 LYS A CE    1 
ATOM   5237  N  NZ    A LYS A 1 338 ? 2.729   -6.606  66.668  0.50 58.07 ? 338 LYS A NZ    1 
ATOM   5238  N  NZ    B LYS A 1 338 ? 4.303   -7.231  62.455  0.50 56.57 ? 338 LYS A NZ    1 
ATOM   5239  N  N     A ARG A 1 339 ? 3.353   -1.121  61.909  0.50 61.92 ? 339 ARG A N     1 
ATOM   5240  N  N     B ARG A 1 339 ? 4.044   -2.022  61.174  0.50 60.88 ? 339 ARG A N     1 
ATOM   5241  C  CA    A ARG A 1 339 ? 4.116   -1.148  60.670  0.50 58.84 ? 339 ARG A CA    1 
ATOM   5242  C  CA    B ARG A 1 339 ? 4.806   -2.009  59.930  0.50 61.12 ? 339 ARG A CA    1 
ATOM   5243  C  C     A ARG A 1 339 ? 4.283   0.251   60.090  0.50 60.39 ? 339 ARG A C     1 
ATOM   5244  C  C     B ARG A 1 339 ? 5.010   -0.574  59.457  0.50 61.75 ? 339 ARG A C     1 
ATOM   5245  O  O     A ARG A 1 339 ? 3.430   1.126   60.259  0.50 57.58 ? 339 ARG A O     1 
ATOM   5246  O  O     B ARG A 1 339 ? 4.664   0.377   60.166  0.50 61.15 ? 339 ARG A O     1 
ATOM   5247  C  CB    A ARG A 1 339 ? 3.438   -2.063  59.649  0.50 57.46 ? 339 ARG A CB    1 
ATOM   5248  C  CB    B ARG A 1 339 ? 4.103   -2.842  58.853  0.50 56.40 ? 339 ARG A CB    1 
ATOM   5249  C  CG    A ARG A 1 339 ? 2.955   -3.369  60.253  0.50 59.80 ? 339 ARG A CG    1 
ATOM   5250  C  CG    B ARG A 1 339 ? 3.846   -4.289  59.252  0.50 55.01 ? 339 ARG A CG    1 
ATOM   5251  C  CD    A ARG A 1 339 ? 2.968   -4.509  59.251  0.50 58.09 ? 339 ARG A CD    1 
ATOM   5252  C  CD    B ARG A 1 339 ? 3.140   -5.036  58.140  0.50 52.44 ? 339 ARG A CD    1 
ATOM   5253  N  NE    A ARG A 1 339 ? 2.648   -5.779  59.892  0.50 51.95 ? 339 ARG A NE    1 
ATOM   5254  N  NE    B ARG A 1 339 ? 4.025   -5.289  57.011  0.50 43.15 ? 339 ARG A NE    1 
ATOM   5255  C  CZ    A ARG A 1 339 ? 3.528   -6.536  60.534  0.50 56.71 ? 339 ARG A CZ    1 
ATOM   5256  C  CZ    B ARG A 1 339 ? 4.392   -6.495  56.602  0.50 47.18 ? 339 ARG A CZ    1 
ATOM   5257  N  NH1   A ARG A 1 339 ? 4.799   -6.183  60.637  0.50 59.13 ? 339 ARG A NH1   1 
ATOM   5258  N  NH1   B ARG A 1 339 ? 3.933   -7.591  57.182  0.50 49.02 ? 339 ARG A NH1   1 
ATOM   5259  N  NH2   A ARG A 1 339 ? 3.122   -7.675  61.088  0.50 50.45 ? 339 ARG A NH2   1 
ATOM   5260  N  NH2   B ARG A 1 339 ? 5.232   -6.605  55.577  0.50 43.85 ? 339 ARG A NH2   1 
ATOM   5261  N  N     A SER A 1 340 ? 5.408   0.454   59.405  0.50 59.83 ? 340 SER A N     1 
ATOM   5262  N  N     B SER A 1 340 ? 5.585   -0.407  58.270  0.50 58.12 ? 340 SER A N     1 
ATOM   5263  C  CA    A SER A 1 340 ? 5.698   1.714   58.725  0.50 57.23 ? 340 SER A CA    1 
ATOM   5264  C  CA    B SER A 1 340 ? 5.898   0.909   57.719  0.50 57.52 ? 340 SER A CA    1 
ATOM   5265  C  C     A SER A 1 340 ? 5.086   1.649   57.331  0.50 56.08 ? 340 SER A C     1 
ATOM   5266  C  C     B SER A 1 340 ? 4.895   1.227   56.610  0.50 51.53 ? 340 SER A C     1 
ATOM   5267  O  O     A SER A 1 340 ? 5.679   1.098   56.401  0.50 50.96 ? 340 SER A O     1 
ATOM   5268  O  O     B SER A 1 340 ? 5.100   0.879   55.446  0.50 54.00 ? 340 SER A O     1 
ATOM   5269  C  CB    A SER A 1 340 ? 7.200   1.968   58.665  0.50 62.66 ? 340 SER A CB    1 
ATOM   5270  C  CB    B SER A 1 340 ? 7.334   0.952   57.208  0.50 57.68 ? 340 SER A CB    1 
ATOM   5271  O  OG    A SER A 1 340 ? 7.730   2.199   59.959  0.50 66.69 ? 340 SER A OG    1 
ATOM   5272  O  OG    B SER A 1 340 ? 7.581   -0.090  56.281  0.50 58.20 ? 340 SER A OG    1 
ATOM   5273  N  N     A ILE A 1 341 ? 3.891   2.213   57.189  0.50 55.12 ? 341 ILE A N     1 
ATOM   5274  N  N     B ILE A 1 341 ? 3.820   1.920   56.977  0.50 55.10 ? 341 ILE A N     1 
ATOM   5275  C  CA    A ILE A 1 341 ? 3.148   2.211   55.934  0.50 49.21 ? 341 ILE A CA    1 
ATOM   5276  C  CA    B ILE A 1 341 ? 2.765   2.313   56.049  0.50 49.44 ? 341 ILE A CA    1 
ATOM   5277  C  C     A ILE A 1 341 ? 2.718   3.652   55.694  0.50 45.39 ? 341 ILE A C     1 
ATOM   5278  C  C     B ILE A 1 341 ? 2.619   3.826   56.115  0.50 45.61 ? 341 ILE A C     1 
ATOM   5279  O  O     A ILE A 1 341 ? 1.770   4.141   56.319  0.50 46.68 ? 341 ILE A O     1 
ATOM   5280  O  O     B ILE A 1 341 ? 2.263   4.375   57.165  0.50 47.92 ? 341 ILE A O     1 
ATOM   5281  C  CB    A ILE A 1 341 ? 1.951   1.254   55.971  0.50 53.35 ? 341 ILE A CB    1 
ATOM   5282  C  CB    B ILE A 1 341 ? 1.429   1.625   56.371  0.50 50.74 ? 341 ILE A CB    1 
ATOM   5283  C  CG1   A ILE A 1 341 ? 2.452   -0.191  55.895  0.50 51.21 ? 341 ILE A CG1   1 
ATOM   5284  C  CG1   B ILE A 1 341 ? 1.545   0.110   56.197  0.50 50.99 ? 341 ILE A CG1   1 
ATOM   5285  C  CG2   A ILE A 1 341 ? 0.974   1.546   54.846  0.50 44.15 ? 341 ILE A CG2   1 
ATOM   5286  C  CG2   B ILE A 1 341 ? 0.315   2.181   55.493  0.50 43.43 ? 341 ILE A CG2   1 
ATOM   5287  C  CD1   A ILE A 1 341 ? 1.435   -1.219  56.308  0.50 49.07 ? 341 ILE A CD1   1 
ATOM   5288  C  CD1   B ILE A 1 341 ? 0.253   -0.628  56.457  0.50 46.06 ? 341 ILE A CD1   1 
ATOM   5289  N  N     A GLN A 1 342 ? 3.425   4.343   54.806  0.50 46.92 ? 342 GLN A N     1 
ATOM   5290  N  N     B GLN A 1 342 ? 2.885   4.496   54.996  0.50 45.68 ? 342 GLN A N     1 
ATOM   5291  C  CA    A GLN A 1 342 ? 3.261   5.779   54.631  0.50 44.92 ? 342 GLN A CA    1 
ATOM   5292  C  CA    B GLN A 1 342 ? 2.771   5.946   54.901  0.50 41.04 ? 342 GLN A CA    1 
ATOM   5293  C  C     A GLN A 1 342 ? 2.279   6.067   53.504  0.50 37.90 ? 342 GLN A C     1 
ATOM   5294  C  C     B GLN A 1 342 ? 1.910   6.292   53.696  0.50 34.56 ? 342 GLN A C     1 
ATOM   5295  O  O     A GLN A 1 342 ? 2.425   5.546   52.392  0.50 37.50 ? 342 GLN A O     1 
ATOM   5296  O  O     B GLN A 1 342 ? 2.246   5.928   52.564  0.50 38.92 ? 342 GLN A O     1 
ATOM   5297  C  CB    A GLN A 1 342 ? 4.606   6.443   54.331  0.50 47.54 ? 342 GLN A CB    1 
ATOM   5298  C  CB    B GLN A 1 342 ? 4.148   6.608   54.784  0.50 47.45 ? 342 GLN A CB    1 
ATOM   5299  C  CG    A GLN A 1 342 ? 5.764   5.930   55.175  0.50 49.01 ? 342 GLN A CG    1 
ATOM   5300  C  CG    B GLN A 1 342 ? 5.028   6.456   56.017  0.50 50.03 ? 342 GLN A CG    1 
ATOM   5301  C  CD    A GLN A 1 342 ? 7.090   6.556   54.783  0.50 53.11 ? 342 GLN A CD    1 
ATOM   5302  C  CD    B GLN A 1 342 ? 6.431   7.001   55.805  0.50 54.76 ? 342 GLN A CD    1 
ATOM   5303  O  OE1   A GLN A 1 342 ? 7.153   7.732   54.421  0.50 52.76 ? 342 GLN A OE1   1 
ATOM   5304  O  OE1   B GLN A 1 342 ? 6.858   7.228   54.672  0.50 54.51 ? 342 GLN A OE1   1 
ATOM   5305  N  NE2   A GLN A 1 342 ? 8.156   5.768   54.844  0.50 55.24 ? 342 GLN A NE2   1 
ATOM   5306  N  NE2   B GLN A 1 342 ? 7.153   7.214   56.899  0.50 59.02 ? 342 GLN A NE2   1 
ATOM   5307  N  N     A PHE A 1 343 ? 1.280   6.885   53.799  0.50 33.12 ? 343 PHE A N     1 
ATOM   5308  N  N     B PHE A 1 343 ? 0.801   6.979   53.941  0.50 35.24 ? 343 PHE A N     1 
ATOM   5309  C  CA    A PHE A 1 343 ? 0.428   7.483   52.787  0.50 34.80 ? 343 PHE A CA    1 
ATOM   5310  C  CA    B PHE A 1 343 ? -0.030  7.517   52.878  0.50 33.91 ? 343 PHE A CA    1 
ATOM   5311  C  C     A PHE A 1 343 ? 0.954   8.870   52.444  0.50 37.19 ? 343 PHE A C     1 
ATOM   5312  C  C     B PHE A 1 343 ? 0.406   8.939   52.549  0.50 37.06 ? 343 PHE A C     1 
ATOM   5313  O  O     A PHE A 1 343 ? 1.688   9.488   53.219  0.50 38.22 ? 343 PHE A O     1 
ATOM   5314  O  O     B PHE A 1 343 ? 1.034   9.626   53.357  0.50 37.50 ? 343 PHE A O     1 
ATOM   5315  C  CB    A PHE A 1 343 ? -1.021  7.576   53.272  0.50 34.90 ? 343 PHE A CB    1 
ATOM   5316  C  CB    B PHE A 1 343 ? -1.506  7.502   53.281  0.50 35.37 ? 343 PHE A CB    1 
ATOM   5317  C  CG    A PHE A 1 343 ? -1.732  6.256   53.324  0.50 35.01 ? 343 PHE A CG    1 
ATOM   5318  C  CG    B PHE A 1 343 ? -2.193  6.190   53.037  0.50 35.62 ? 343 PHE A CG    1 
ATOM   5319  C  CD1   A PHE A 1 343 ? -1.489  5.362   54.352  0.50 41.54 ? 343 PHE A CD1   1 
ATOM   5320  C  CD1   B PHE A 1 343 ? -1.887  5.077   53.801  0.50 40.26 ? 343 PHE A CD1   1 
ATOM   5321  C  CD2   A PHE A 1 343 ? -2.651  5.911   52.346  0.50 37.40 ? 343 PHE A CD2   1 
ATOM   5322  C  CD2   B PHE A 1 343 ? -3.160  6.074   52.053  0.50 37.66 ? 343 PHE A CD2   1 
ATOM   5323  C  CE1   A PHE A 1 343 ? -2.145  4.144   54.400  0.50 40.68 ? 343 PHE A CE1   1 
ATOM   5324  C  CE1   B PHE A 1 343 ? -2.524  3.869   53.578  0.50 39.27 ? 343 PHE A CE1   1 
ATOM   5325  C  CE2   A PHE A 1 343 ? -3.311  4.696   52.389  0.50 33.61 ? 343 PHE A CE2   1 
ATOM   5326  C  CE2   B PHE A 1 343 ? -3.801  4.869   51.827  0.50 33.50 ? 343 PHE A CE2   1 
ATOM   5327  C  CZ    A PHE A 1 343 ? -3.059  3.813   53.417  0.50 39.69 ? 343 PHE A CZ    1 
ATOM   5328  C  CZ    B PHE A 1 343 ? -3.483  3.766   52.591  0.50 35.25 ? 343 PHE A CZ    1 
ATOM   5329  N  N     A VAL A 1 344 ? 0.582   9.356   51.259  0.50 33.68 ? 344 VAL A N     1 
ATOM   5330  N  N     B VAL A 1 344 ? 0.073   9.376   51.333  0.50 32.34 ? 344 VAL A N     1 
ATOM   5331  C  CA    A VAL A 1 344 ? 0.933   10.729  50.925  0.50 34.50 ? 344 VAL A CA    1 
ATOM   5332  C  CA    B VAL A 1 344 ? 0.299   10.769  50.977  0.50 36.79 ? 344 VAL A CA    1 
ATOM   5333  C  C     A VAL A 1 344 ? 0.176   11.682  51.844  0.50 40.99 ? 344 VAL A C     1 
ATOM   5334  C  C     B VAL A 1 344 ? -0.566  11.651  51.867  0.50 38.54 ? 344 VAL A C     1 
ATOM   5335  O  O     A VAL A 1 344 ? -0.872  11.349  52.412  0.50 33.54 ? 344 VAL A O     1 
ATOM   5336  O  O     B VAL A 1 344 ? -1.682  11.278  52.252  0.50 37.26 ? 344 VAL A O     1 
ATOM   5337  C  CB    A VAL A 1 344 ? 0.657   11.041  49.445  0.50 37.52 ? 344 VAL A CB    1 
ATOM   5338  C  CB    B VAL A 1 344 ? 0.008   11.006  49.485  0.50 36.40 ? 344 VAL A CB    1 
ATOM   5339  C  CG1   A VAL A 1 344 ? 1.371   10.041  48.550  0.50 34.11 ? 344 VAL A CG1   1 
ATOM   5340  C  CG1   B VAL A 1 344 ? 0.992   10.226  48.625  0.50 33.88 ? 344 VAL A CG1   1 
ATOM   5341  C  CG2   A VAL A 1 344 ? -0.827  11.038  49.170  0.50 37.65 ? 344 VAL A CG2   1 
ATOM   5342  C  CG2   B VAL A 1 344 ? -1.421  10.614  49.146  0.50 36.34 ? 344 VAL A CG2   1 
ATOM   5343  N  N     A ASP A 1 345 ? 0.731   12.884  52.007  0.50 39.95 ? 345 ASP A N     1 
ATOM   5344  N  N     B ASP A 1 345 ? -0.040  12.826  52.221  0.50 40.99 ? 345 ASP A N     1 
ATOM   5345  C  CA    A ASP A 1 345 ? 0.141   13.848  52.928  0.50 47.23 ? 345 ASP A CA    1 
ATOM   5346  C  CA    B ASP A 1 345 ? -0.752  13.704  53.141  0.50 40.33 ? 345 ASP A CA    1 
ATOM   5347  C  C     A ASP A 1 345 ? -1.262  14.266  52.513  0.50 45.09 ? 345 ASP A C     1 
ATOM   5348  C  C     B ASP A 1 345 ? -2.005  14.306  52.521  0.50 45.50 ? 345 ASP A C     1 
ATOM   5349  O  O     A ASP A 1 345 ? -2.053  14.668  53.373  0.50 46.45 ? 345 ASP A O     1 
ATOM   5350  O  O     B ASP A 1 345 ? -2.859  14.812  53.257  0.50 47.50 ? 345 ASP A O     1 
ATOM   5351  C  CB    A ASP A 1 345 ? 1.036   15.084  53.044  0.50 49.55 ? 345 ASP A CB    1 
ATOM   5352  C  CB    B ASP A 1 345 ? 0.168   14.827  53.623  0.50 49.51 ? 345 ASP A CB    1 
ATOM   5353  C  CG    A ASP A 1 345 ? 2.345   14.790  53.749  0.50 51.78 ? 345 ASP A CG    1 
ATOM   5354  C  CG    B ASP A 1 345 ? 1.432   14.307  54.279  0.50 49.86 ? 345 ASP A CG    1 
ATOM   5355  O  OD1   A ASP A 1 345 ? 2.353   13.930  54.657  0.50 47.49 ? 345 ASP A OD1   1 
ATOM   5356  O  OD1   B ASP A 1 345 ? 1.331   13.427  55.161  0.50 53.90 ? 345 ASP A OD1   1 
ATOM   5357  O  OD2   A ASP A 1 345 ? 3.367   15.415  53.393  0.50 51.17 ? 345 ASP A OD2   1 
ATOM   5358  O  OD2   B ASP A 1 345 ? 2.528   14.777  53.908  0.50 52.40 ? 345 ASP A OD2   1 
ATOM   5359  N  N     A TRP A 1 346 ? -1.595  14.169  51.226  0.50 39.60 ? 346 TRP A N     1 
ATOM   5360  N  N     B TRP A 1 346 ? -2.141  14.268  51.196  0.50 40.11 ? 346 TRP A N     1 
ATOM   5361  C  CA    A TRP A 1 346 ? -2.871  14.651  50.718  0.50 40.53 ? 346 TRP A CA    1 
ATOM   5362  C  CA    B TRP A 1 346 ? -3.276  14.902  50.537  0.50 40.59 ? 346 TRP A CA    1 
ATOM   5363  C  C     A TRP A 1 346 ? -3.909  13.547  50.554  0.50 43.55 ? 346 TRP A C     1 
ATOM   5364  C  C     B TRP A 1 346 ? -4.450  13.957  50.309  0.50 43.20 ? 346 TRP A C     1 
ATOM   5365  O  O     A TRP A 1 346 ? -5.005  13.814  50.049  0.50 42.89 ? 346 TRP A O     1 
ATOM   5366  O  O     B TRP A 1 346 ? -5.485  14.393  49.796  0.50 44.30 ? 346 TRP A O     1 
ATOM   5367  C  CB    A TRP A 1 346 ? -2.667  15.385  49.390  0.50 39.91 ? 346 TRP A CB    1 
ATOM   5368  C  CB    B TRP A 1 346 ? -2.841  15.529  49.207  0.50 40.47 ? 346 TRP A CB    1 
ATOM   5369  C  CG    A TRP A 1 346 ? -1.809  14.663  48.389  0.50 37.55 ? 346 TRP A CG    1 
ATOM   5370  C  CG    B TRP A 1 346 ? -1.936  14.682  48.354  0.50 37.60 ? 346 TRP A CG    1 
ATOM   5371  C  CD1   A TRP A 1 346 ? -0.454  14.755  48.253  0.50 39.24 ? 346 TRP A CD1   1 
ATOM   5372  C  CD1   B TRP A 1 346 ? -0.572  14.660  48.379  0.50 39.05 ? 346 TRP A CD1   1 
ATOM   5373  C  CD2   A TRP A 1 346 ? -2.253  13.754  47.373  0.50 36.12 ? 346 TRP A CD2   1 
ATOM   5374  C  CD2   B TRP A 1 346 ? -2.332  13.760  47.331  0.50 36.12 ? 346 TRP A CD2   1 
ATOM   5375  N  NE1   A TRP A 1 346 ? -0.026  13.956  47.219  0.50 39.17 ? 346 TRP A NE1   1 
ATOM   5376  N  NE1   B TRP A 1 346 ? -0.094  13.774  47.442  0.50 39.96 ? 346 TRP A NE1   1 
ATOM   5377  C  CE2   A TRP A 1 346 ? -1.111  13.335  46.659  0.50 39.98 ? 346 TRP A CE2   1 
ATOM   5378  C  CE2   B TRP A 1 346 ? -1.155  13.209  46.785  0.50 40.16 ? 346 TRP A CE2   1 
ATOM   5379  C  CE3   A TRP A 1 346 ? -3.505  13.260  46.994  0.50 39.22 ? 346 TRP A CE3   1 
ATOM   5380  C  CE3   B TRP A 1 346 ? -3.568  13.343  46.827  0.50 39.34 ? 346 TRP A CE3   1 
ATOM   5381  C  CZ2   A TRP A 1 346 ? -1.185  12.436  45.596  0.50 36.41 ? 346 TRP A CZ2   1 
ATOM   5382  C  CZ2   B TRP A 1 346 ? -1.179  12.262  45.762  0.50 36.65 ? 346 TRP A CZ2   1 
ATOM   5383  C  CZ3   A TRP A 1 346 ? -3.575  12.371  45.934  0.50 38.84 ? 346 TRP A CZ3   1 
ATOM   5384  C  CZ3   B TRP A 1 346 ? -3.588  12.403  45.809  0.50 38.78 ? 346 TRP A CZ3   1 
ATOM   5385  C  CH2   A TRP A 1 346 ? -2.423  11.966  45.251  0.50 36.60 ? 346 TRP A CH2   1 
ATOM   5386  C  CH2   B TRP A 1 346 ? -2.402  11.871  45.291  0.50 36.56 ? 346 TRP A CH2   1 
ATOM   5387  N  N     A CYS A 1 347 ? -3.603  12.318  50.978  0.50 38.37 ? 347 CYS A N     1 
ATOM   5388  N  N     B CYS A 1 347 ? -4.330  12.692  50.689  0.50 40.95 ? 347 CYS A N     1 
ATOM   5389  C  CA    A CYS A 1 347 ? -4.615  11.280  50.888  0.50 42.89 ? 347 CYS A CA    1 
ATOM   5390  C  CA    B CYS A 1 347 ? -5.417  11.734  50.596  0.50 41.24 ? 347 CYS A CA    1 
ATOM   5391  C  C     A CYS A 1 347 ? -5.129  10.908  52.272  0.50 48.79 ? 347 CYS A C     1 
ATOM   5392  C  C     B CYS A 1 347 ? -5.771  11.211  51.980  0.50 45.27 ? 347 CYS A C     1 
ATOM   5393  O  O     A CYS A 1 347 ? -4.336  10.759  53.210  0.50 42.70 ? 347 CYS A O     1 
ATOM   5394  O  O     B CYS A 1 347 ? -4.993  11.365  52.930  0.50 49.00 ? 347 CYS A O     1 
ATOM   5395  C  CB    A CYS A 1 347 ? -4.078  10.019  50.201  0.50 38.79 ? 347 CYS A CB    1 
ATOM   5396  C  CB    B CYS A 1 347 ? -5.045  10.559  49.679  0.50 40.61 ? 347 CYS A CB    1 
ATOM   5397  S  SG    A CYS A 1 347 ? -4.111  10.086  48.395  0.50 40.17 ? 347 CYS A SG    1 
ATOM   5398  S  SG    B CYS A 1 347 ? -5.629  10.730  47.974  0.50 56.29 ? 347 CYS A SG    1 
ATOM   5399  N  N     A PRO A 1 348 ? -6.445  10.762  52.431  0.50 45.88 ? 348 PRO A N     1 
ATOM   5400  N  N     B PRO A 1 348 ? -6.946  10.605  52.137  0.50 47.88 ? 348 PRO A N     1 
ATOM   5401  C  CA    A PRO A 1 348 ? -6.984  10.270  53.705  0.50 50.71 ? 348 PRO A CA    1 
ATOM   5402  C  CA    B PRO A 1 348 ? -7.246  9.909   53.391  0.50 50.86 ? 348 PRO A CA    1 
ATOM   5403  C  C     A PRO A 1 348 ? -6.408  8.912   54.071  0.50 48.98 ? 348 PRO A C     1 
ATOM   5404  C  C     B PRO A 1 348 ? -6.224  8.818   53.678  0.50 47.55 ? 348 PRO A C     1 
ATOM   5405  O  O     A PRO A 1 348 ? -6.732  7.903   53.435  0.50 51.41 ? 348 PRO A O     1 
ATOM   5406  O  O     B PRO A 1 348 ? -5.489  8.361   52.800  0.50 41.49 ? 348 PRO A O     1 
ATOM   5407  C  CB    A PRO A 1 348 ? -8.494  10.191  53.443  0.50 48.35 ? 348 PRO A CB    1 
ATOM   5408  C  CB    B PRO A 1 348 ? -8.638  9.317   53.147  0.50 46.44 ? 348 PRO A CB    1 
ATOM   5409  C  CG    A PRO A 1 348 ? -8.736  11.160  52.329  0.50 47.44 ? 348 PRO A CG    1 
ATOM   5410  C  CG    B PRO A 1 348 ? -9.257  10.233  52.152  0.50 50.61 ? 348 PRO A CG    1 
ATOM   5411  C  CD    A PRO A 1 348 ? -7.507  11.101  51.468  0.50 44.30 ? 348 PRO A CD    1 
ATOM   5412  C  CD    B PRO A 1 348 ? -8.129  10.696  51.261  0.50 43.58 ? 348 PRO A CD    1 
ATOM   5413  N  N     A THR A 1 349 ? -5.541  8.883   55.084  0.50 46.96 ? 349 THR A N     1 
ATOM   5414  N  N     B THR A 1 349 ? -6.178  8.410   54.943  0.50 49.13 ? 349 THR A N     1 
ATOM   5415  C  CA    A THR A 1 349 ? -4.923  7.641   55.533  0.50 45.99 ? 349 THR A CA    1 
ATOM   5416  C  CA    B THR A 1 349 ? -5.351  7.293   55.375  0.50 46.99 ? 349 THR A CA    1 
ATOM   5417  C  C     A THR A 1 349 ? -5.994  6.648   55.971  0.50 47.35 ? 349 THR A C     1 
ATOM   5418  C  C     B THR A 1 349 ? -6.191  6.061   55.687  0.50 47.60 ? 349 THR A C     1 
ATOM   5419  O  O     A THR A 1 349 ? -6.452  6.683   57.118  0.50 51.63 ? 349 THR A O     1 
ATOM   5420  O  O     B THR A 1 349 ? -5.664  5.067   56.198  0.50 47.58 ? 349 THR A O     1 
ATOM   5421  C  CB    A THR A 1 349 ? -3.936  7.912   56.674  0.50 46.20 ? 349 THR A CB    1 
ATOM   5422  C  CB    B THR A 1 349 ? -4.512  7.707   56.588  0.50 44.65 ? 349 THR A CB    1 
ATOM   5423  O  OG1   A THR A 1 349 ? -2.898  8.791   56.216  0.50 42.12 ? 349 THR A OG1   1 
ATOM   5424  O  OG1   B THR A 1 349 ? -4.121  9.077   56.439  0.50 45.32 ? 349 THR A OG1   1 
ATOM   5425  C  CG2   A THR A 1 349 ? -3.306  6.613   57.167  0.50 49.41 ? 349 THR A CG2   1 
ATOM   5426  C  CG2   B THR A 1 349 ? -3.250  6.855   56.699  0.50 49.70 ? 349 THR A CG2   1 
ATOM   5427  N  N     A GLY A 1 350 ? -6.409  5.771   55.061  0.50 48.97 ? 350 GLY A N     1 
ATOM   5428  N  N     B GLY A 1 350 ? -7.484  6.099   55.374  0.50 44.23 ? 350 GLY A N     1 
ATOM   5429  C  CA    A GLY A 1 350 ? -7.469  4.829   55.367  0.50 42.93 ? 350 GLY A CA    1 
ATOM   5430  C  CA    B GLY A 1 350 ? -8.366  4.990   55.660  0.50 44.26 ? 350 GLY A CA    1 
ATOM   5431  C  C     A GLY A 1 350 ? -7.476  3.657   54.414  0.50 39.98 ? 350 GLY A C     1 
ATOM   5432  C  C     B GLY A 1 350 ? -8.433  3.977   54.530  0.50 41.08 ? 350 GLY A C     1 
ATOM   5433  O  O     A GLY A 1 350 ? -7.025  3.751   53.267  0.50 39.61 ? 350 GLY A O     1 
ATOM   5434  O  O     B GLY A 1 350 ? -8.248  4.301   53.359  0.50 43.93 ? 350 GLY A O     1 
ATOM   5435  N  N     A PHE A 1 351 ? -8.006  2.542   54.909  0.50 36.39 ? 351 PHE A N     1 
ATOM   5436  N  N     B PHE A 1 351 ? -8.706  2.735   54.907  0.50 37.18 ? 351 PHE A N     1 
ATOM   5437  C  CA    A PHE A 1 351 ? -8.119  1.296   54.160  0.50 32.07 ? 351 PHE A CA    1 
ATOM   5438  C  CA    B PHE A 1 351 ? -8.797  1.621   53.979  0.50 33.85 ? 351 PHE A CA    1 
ATOM   5439  C  C     A PHE A 1 351 ? -9.593  1.041   53.880  0.50 36.03 ? 351 PHE A C     1 
ATOM   5440  C  C     B PHE A 1 351 ? -10.254 1.361   53.614  0.50 34.12 ? 351 PHE A C     1 
ATOM   5441  O  O     A PHE A 1 351 ? -10.372 0.809   54.810  0.50 31.27 ? 351 PHE A O     1 
ATOM   5442  O  O     B PHE A 1 351 ? -11.162 1.566   54.422  0.50 31.65 ? 351 PHE A O     1 
ATOM   5443  C  CB    A PHE A 1 351 ? -7.519  0.129   54.943  0.50 39.61 ? 351 PHE A CB    1 
ATOM   5444  C  CB    B PHE A 1 351 ? -8.185  0.357   54.589  0.50 35.50 ? 351 PHE A CB    1 
ATOM   5445  C  CG    A PHE A 1 351 ? -6.044  0.251   55.200  0.50 35.18 ? 351 PHE A CG    1 
ATOM   5446  C  CG    B PHE A 1 351 ? -6.699  0.443   54.822  0.50 38.67 ? 351 PHE A CG    1 
ATOM   5447  C  CD1   A PHE A 1 351 ? -5.566  1.088   56.196  0.50 41.80 ? 351 PHE A CD1   1 
ATOM   5448  C  CD1   B PHE A 1 351 ? -6.179  1.253   55.819  0.50 39.59 ? 351 PHE A CD1   1 
ATOM   5449  C  CD2   A PHE A 1 351 ? -5.138  -0.497  54.467  0.50 40.38 ? 351 PHE A CD2   1 
ATOM   5450  C  CD2   B PHE A 1 351 ? -5.824  -0.310  54.058  0.50 36.37 ? 351 PHE A CD2   1 
ATOM   5451  C  CE1   A PHE A 1 351 ? -4.210  1.194   56.441  0.50 36.44 ? 351 PHE A CE1   1 
ATOM   5452  C  CE1   B PHE A 1 351 ? -4.815  1.326   56.034  0.50 39.85 ? 351 PHE A CE1   1 
ATOM   5453  C  CE2   A PHE A 1 351 ? -3.778  -0.397  54.707  0.50 36.00 ? 351 PHE A CE2   1 
ATOM   5454  C  CE2   B PHE A 1 351 ? -4.458  -0.243  54.270  0.50 42.57 ? 351 PHE A CE2   1 
ATOM   5455  C  CZ    A PHE A 1 351 ? -3.315  0.452   55.692  0.50 43.22 ? 351 PHE A CZ    1 
ATOM   5456  C  CZ    B PHE A 1 351 ? -3.955  0.576   55.258  0.50 40.33 ? 351 PHE A CZ    1 
ATOM   5457  N  N     A LYS A 1 352 ? -9.975  1.077   52.606  0.50 31.68 ? 352 LYS A N     1 
ATOM   5458  N  N     B LYS A 1 352 ? -10.469 0.906   52.385  0.50 30.04 ? 352 LYS A N     1 
ATOM   5459  C  CA    A LYS A 1 352 ? -11.333 0.719   52.221  0.50 26.51 ? 352 LYS A CA    1 
ATOM   5460  C  CA    B LYS A 1 352 ? -11.779 0.463   51.932  0.50 28.26 ? 352 LYS A CA    1 
ATOM   5461  C  C     A LYS A 1 352 ? -11.472 -0.797  52.182  0.50 26.53 ? 352 LYS A C     1 
ATOM   5462  C  C     B LYS A 1 352 ? -11.828 -1.058  51.974  0.50 26.80 ? 352 LYS A C     1 
ATOM   5463  O  O     A LYS A 1 352 ? -10.557 -1.510  51.761  0.50 27.24 ? 352 LYS A O     1 
ATOM   5464  O  O     B LYS A 1 352 ? -10.912 -1.727  51.483  0.50 26.72 ? 352 LYS A O     1 
ATOM   5465  C  CB    A LYS A 1 352 ? -11.687 1.325   50.864  0.50 23.80 ? 352 LYS A CB    1 
ATOM   5466  C  CB    B LYS A 1 352 ? -12.074 0.966   50.519  0.50 29.40 ? 352 LYS A CB    1 
ATOM   5467  C  CG    A LYS A 1 352 ? -11.752 2.838   50.870  0.50 34.76 ? 352 LYS A CG    1 
ATOM   5468  C  CG    B LYS A 1 352 ? -12.522 2.414   50.430  0.50 29.79 ? 352 LYS A CG    1 
ATOM   5469  C  CD    A LYS A 1 352 ? -11.775 3.398   49.463  0.50 32.44 ? 352 LYS A CD    1 
ATOM   5470  C  CD    B LYS A 1 352 ? -12.925 2.740   49.000  0.50 32.93 ? 352 LYS A CD    1 
ATOM   5471  C  CE    A LYS A 1 352 ? -11.665 4.911   49.485  0.50 34.16 ? 352 LYS A CE    1 
ATOM   5472  C  CE    B LYS A 1 352 ? -13.618 4.087   48.893  0.50 39.46 ? 352 LYS A CE    1 
ATOM   5473  N  NZ    A LYS A 1 352 ? -10.623 5.360   50.447  0.50 43.47 ? 352 LYS A NZ    1 
ATOM   5474  N  NZ    B LYS A 1 352 ? -12.657 5.235   48.889  0.50 35.15 ? 352 LYS A NZ    1 
ATOM   5475  N  N     A VAL A 1 353 ? -12.622 -1.292  52.633  0.50 26.88 ? 353 VAL A N     1 
ATOM   5476  N  N     B VAL A 1 353 ? -12.892 -1.602  52.561  0.50 28.14 ? 353 VAL A N     1 
ATOM   5477  C  CA    A VAL A 1 353 ? -12.819 -2.716  52.878  0.50 27.99 ? 353 VAL A CA    1 
ATOM   5478  C  CA    B VAL A 1 353 ? -13.014 -3.037  52.789  0.50 28.32 ? 353 VAL A CA    1 
ATOM   5479  C  C     A VAL A 1 353 ? -14.044 -3.199  52.114  0.50 28.91 ? 353 VAL A C     1 
ATOM   5480  C  C     B VAL A 1 353 ? -14.315 -3.534  52.173  0.50 29.10 ? 353 VAL A C     1 
ATOM   5481  O  O     A VAL A 1 353 ? -15.104 -2.567  52.165  0.50 26.10 ? 353 VAL A O     1 
ATOM   5482  O  O     B VAL A 1 353 ? -15.377 -2.939  52.383  0.50 26.03 ? 353 VAL A O     1 
ATOM   5483  C  CB    A VAL A 1 353 ? -12.977 -3.015  54.383  0.50 29.04 ? 353 VAL A CB    1 
ATOM   5484  C  CB    B VAL A 1 353 ? -12.970 -3.383  54.291  0.50 29.55 ? 353 VAL A CB    1 
ATOM   5485  C  CG1   A VAL A 1 353 ? -13.452 -4.442  54.596  0.50 30.41 ? 353 VAL A CG1   1 
ATOM   5486  C  CG1   B VAL A 1 353 ? -13.092 -4.885  54.488  0.50 29.56 ? 353 VAL A CG1   1 
ATOM   5487  C  CG2   A VAL A 1 353 ? -11.661 -2.777  55.109  0.50 28.73 ? 353 VAL A CG2   1 
ATOM   5488  C  CG2   B VAL A 1 353 ? -11.685 -2.861  54.922  0.50 28.99 ? 353 VAL A CG2   1 
ATOM   5489  N  N     A GLY A 1 354 ? -13.891 -4.303  51.402  0.50 27.65 ? 354 GLY A N     1 
ATOM   5490  N  N     B GLY A 1 354 ? -14.229 -4.616  51.418  0.50 26.93 ? 354 GLY A N     1 
ATOM   5491  C  CA    A GLY A 1 354 ? -15.028 -5.029  50.859  0.50 25.11 ? 354 GLY A CA    1 
ATOM   5492  C  CA    B GLY A 1 354 ? -15.414 -5.321  50.953  0.50 24.25 ? 354 GLY A CA    1 
ATOM   5493  C  C     A GLY A 1 354 ? -14.966 -6.471  51.308  0.50 21.52 ? 354 GLY A C     1 
ATOM   5494  C  C     B GLY A 1 354 ? -15.259 -6.801  51.222  0.50 21.58 ? 354 GLY A C     1 
ATOM   5495  O  O     A GLY A 1 354 ? -13.887 -7.052  51.408  0.50 21.67 ? 354 GLY A O     1 
ATOM   5496  O  O     B GLY A 1 354 ? -14.160 -7.343  51.138  0.50 20.88 ? 354 GLY A O     1 
ATOM   5497  N  N     A ILE A 1 355 ? -16.132 -7.039  51.604  0.50 22.95 ? 355 ILE A N     1 
ATOM   5498  N  N     B ILE A 1 355 ? -16.371 -7.449  51.560  0.50 23.22 ? 355 ILE A N     1 
ATOM   5499  C  CA    A ILE A 1 355 ? -16.209 -8.404  52.113  0.50 22.13 ? 355 ILE A CA    1 
ATOM   5500  C  CA    B ILE A 1 355 ? -16.358 -8.855  51.948  0.50 20.58 ? 355 ILE A CA    1 
ATOM   5501  C  C     A ILE A 1 355 ? -17.287 -9.162  51.351  0.50 24.02 ? 355 ILE A C     1 
ATOM   5502  C  C     B ILE A 1 355 ? -17.380 -9.617  51.114  0.50 23.22 ? 355 ILE A C     1 
ATOM   5503  O  O     A ILE A 1 355 ? -18.466 -8.788  51.393  0.50 27.46 ? 355 ILE A O     1 
ATOM   5504  O  O     B ILE A 1 355 ? -18.551 -9.228  51.049  0.50 28.84 ? 355 ILE A O     1 
ATOM   5505  C  CB    A ILE A 1 355 ? -16.484 -8.442  53.625  0.50 21.65 ? 355 ILE A CB    1 
ATOM   5506  C  CB    B ILE A 1 355 ? -16.642 -9.032  53.452  0.50 25.22 ? 355 ILE A CB    1 
ATOM   5507  C  CG1   A ILE A 1 355 ? -15.360 -7.738  54.389  0.50 24.78 ? 355 ILE A CG1   1 
ATOM   5508  C  CG1   B ILE A 1 355 ? -15.618 -8.255  54.280  0.50 24.43 ? 355 ILE A CG1   1 
ATOM   5509  C  CG2   A ILE A 1 355 ? -16.607 -9.881  54.105  0.50 25.74 ? 355 ILE A CG2   1 
ATOM   5510  C  CG2   B ILE A 1 355 ? -16.602 -10.508 53.830  0.50 25.64 ? 355 ILE A CG2   1 
ATOM   5511  C  CD1   A ILE A 1 355 ? -15.525 -7.785  55.909  0.50 23.52 ? 355 ILE A CD1   1 
ATOM   5512  C  CD1   B ILE A 1 355 ? -15.911 -8.255  55.781  0.50 23.72 ? 355 ILE A CD1   1 
ATOM   5513  N  N     A ASN A 1 356 ? -16.875 -10.214 50.646  0.50 25.15 ? 356 ASN A N     1 
ATOM   5514  N  N     B ASN A 1 356 ? -16.929 -10.695 50.472  0.50 25.47 ? 356 ASN A N     1 
ATOM   5515  C  CA    A ASN A 1 356 ? -17.758 -11.218 50.066  0.50 26.16 ? 356 ASN A CA    1 
ATOM   5516  C  CA    B ASN A 1 356 ? -17.782 -11.645 49.762  0.50 26.16 ? 356 ASN A CA    1 
ATOM   5517  C  C     A ASN A 1 356 ? -17.580 -12.493 50.880  0.50 24.11 ? 356 ASN A C     1 
ATOM   5518  C  C     B ASN A 1 356 ? -17.788 -12.928 50.586  0.50 24.43 ? 356 ASN A C     1 
ATOM   5519  O  O     A ASN A 1 356 ? -16.452 -12.949 51.077  0.50 24.40 ? 356 ASN A O     1 
ATOM   5520  O  O     B ASN A 1 356 ? -16.768 -13.611 50.686  0.50 24.44 ? 356 ASN A O     1 
ATOM   5521  C  CB    A ASN A 1 356 ? -17.417 -11.452 48.588  0.50 26.01 ? 356 ASN A CB    1 
ATOM   5522  C  CB    B ASN A 1 356 ? -17.263 -11.883 48.342  0.50 24.94 ? 356 ASN A CB    1 
ATOM   5523  C  CG    A ASN A 1 356 ? -18.370 -12.416 47.897  0.50 28.16 ? 356 ASN A CG    1 
ATOM   5524  C  CG    B ASN A 1 356 ? -18.109 -12.871 47.551  0.50 24.66 ? 356 ASN A CG    1 
ATOM   5525  O  OD1   A ASN A 1 356 ? -18.791 -13.424 48.467  0.50 34.19 ? 356 ASN A OD1   1 
ATOM   5526  O  OD1   B ASN A 1 356 ? -18.461 -13.949 48.033  0.50 26.12 ? 356 ASN A OD1   1 
ATOM   5527  N  ND2   A ASN A 1 356 ? -18.712 -12.107 46.651  0.50 33.67 ? 356 ASN A ND2   1 
ATOM   5528  N  ND2   B ASN A 1 356 ? -18.431 -12.504 46.314  0.50 30.99 ? 356 ASN A ND2   1 
ATOM   5529  N  N     A TYR A 1 357 ? -18.681 -13.056 51.375  0.50 25.62 ? 357 TYR A N     1 
ATOM   5530  N  N     B TYR A 1 357 ? -18.928 -13.260 51.183  0.50 25.42 ? 357 TYR A N     1 
ATOM   5531  C  CA    A TYR A 1 357 ? -18.584 -14.127 52.359  0.50 23.35 ? 357 TYR A CA    1 
ATOM   5532  C  CA    B TYR A 1 357 ? -18.952 -14.382 52.111  0.50 24.97 ? 357 TYR A CA    1 
ATOM   5533  C  C     A TYR A 1 357 ? -18.488 -15.521 51.753  0.50 25.18 ? 357 TYR A C     1 
ATOM   5534  C  C     B TYR A 1 357 ? -18.996 -15.744 51.419  0.50 24.40 ? 357 TYR A C     1 
ATOM   5535  O  O     A TYR A 1 357 ? -18.446 -16.499 52.506  0.50 23.38 ? 357 TYR A O     1 
ATOM   5536  O  O     B TYR A 1 357 ? -19.349 -16.740 52.058  0.50 27.33 ? 357 TYR A O     1 
ATOM   5537  C  CB    A TYR A 1 357 ? -19.767 -14.051 53.320  0.50 25.92 ? 357 TYR A CB    1 
ATOM   5538  C  CB    B TYR A 1 357 ? -20.122 -14.225 53.078  0.50 24.93 ? 357 TYR A CB    1 
ATOM   5539  C  CG    A TYR A 1 357 ? -19.708 -12.819 54.178  0.50 21.64 ? 357 TYR A CG    1 
ATOM   5540  C  CG    B TYR A 1 357 ? -19.995 -12.980 53.921  0.50 21.15 ? 357 TYR A CG    1 
ATOM   5541  C  CD1   A TYR A 1 357 ? -18.975 -12.808 55.359  0.50 22.30 ? 357 TYR A CD1   1 
ATOM   5542  C  CD1   B TYR A 1 357 ? -19.196 -12.969 55.060  0.50 21.87 ? 357 TYR A CD1   1 
ATOM   5543  C  CD2   A TYR A 1 357 ? -20.363 -11.655 53.800  0.50 23.13 ? 357 TYR A CD2   1 
ATOM   5544  C  CD2   B TYR A 1 357 ? -20.653 -11.810 53.569  0.50 22.75 ? 357 TYR A CD2   1 
ATOM   5545  C  CE1   A TYR A 1 357 ? -18.914 -11.673 56.152  0.50 25.52 ? 357 TYR A CE1   1 
ATOM   5546  C  CE1   B TYR A 1 357 ? -19.079 -11.831 55.843  0.50 26.68 ? 357 TYR A CE1   1 
ATOM   5547  C  CE2   A TYR A 1 357 ? -20.307 -10.516 54.585  0.50 29.04 ? 357 TYR A CE2   1 
ATOM   5548  C  CE2   B TYR A 1 357 ? -20.536 -10.666 54.339  0.50 29.58 ? 357 TYR A CE2   1 
ATOM   5549  C  CZ    A TYR A 1 357 ? -19.586 -10.533 55.762  0.50 24.25 ? 357 TYR A CZ    1 
ATOM   5550  C  CZ    B TYR A 1 357 ? -19.751 -10.683 55.477  0.50 24.67 ? 357 TYR A CZ    1 
ATOM   5551  O  OH    A TYR A 1 357 ? -19.531 -9.401  56.544  0.50 24.91 ? 357 TYR A OH    1 
ATOM   5552  O  OH    B TYR A 1 357 ? -19.637 -9.548  56.246  0.50 25.74 ? 357 TYR A OH    1 
ATOM   5553  N  N     A GLN A 1 358 ? -18.432 -15.641 50.431  0.50 28.61 ? 358 GLN A N     1 
ATOM   5554  N  N     B GLN A 1 358 ? -18.637 -15.819 50.139  0.50 29.12 ? 358 GLN A N     1 
ATOM   5555  C  CA    A GLN A 1 358 ? -18.181 -17.005 49.982  0.50 27.94 ? 358 GLN A CA    1 
ATOM   5556  C  CA    B GLN A 1 358 ? -18.464 -17.107 49.479  0.50 26.58 ? 358 GLN A CA    1 
ATOM   5557  C  C     A GLN A 1 358 ? -16.691 -17.208 49.723  0.50 24.90 ? 358 GLN A C     1 
ATOM   5558  C  C     B GLN A 1 358 ? -16.980 -17.396 49.334  0.50 25.17 ? 358 GLN A C     1 
ATOM   5559  O  O     A GLN A 1 358 ? -16.030 -16.313 49.189  0.50 28.84 ? 358 GLN A O     1 
ATOM   5560  O  O     B GLN A 1 358 ? -16.233 -16.523 48.861  0.50 29.74 ? 358 GLN A O     1 
ATOM   5561  C  CB    A GLN A 1 358 ? -18.969 -17.312 48.707  0.50 27.69 ? 358 GLN A CB    1 
ATOM   5562  C  CB    B GLN A 1 358 ? -19.132 -17.109 48.105  0.50 30.75 ? 358 GLN A CB    1 
ATOM   5563  C  CG    A GLN A 1 358 ? -19.072 -18.793 48.366  0.50 33.62 ? 358 GLN A CG    1 
ATOM   5564  C  CG    B GLN A 1 358 ? -19.107 -18.457 47.387  0.50 26.35 ? 358 GLN A CG    1 
ATOM   5565  C  CD    A GLN A 1 358 ? -20.058 -19.530 49.257  0.50 30.37 ? 358 GLN A CD    1 
ATOM   5566  C  CD    B GLN A 1 358 ? -19.944 -19.514 48.094  0.50 34.95 ? 358 GLN A CD    1 
ATOM   5567  O  OE1   A GLN A 1 358 ? -20.908 -18.916 49.901  0.50 28.66 ? 358 GLN A OE1   1 
ATOM   5568  O  OE1   B GLN A 1 358 ? -20.928 -19.200 48.768  0.50 27.31 ? 358 GLN A OE1   1 
ATOM   5569  N  NE2   A GLN A 1 358 ? -19.952 -20.854 49.293  0.50 32.62 ? 358 GLN A NE2   1 
ATOM   5570  N  NE2   B GLN A 1 358 ? -19.549 -20.774 47.950  0.50 30.06 ? 358 GLN A NE2   1 
ATOM   5571  N  N     A PRO A 1 359 ? -16.119 -18.346 50.112  0.50 24.51 ? 359 PRO A N     1 
ATOM   5572  N  N     B PRO A 1 359 ? -16.498 -18.574 49.742  0.50 22.63 ? 359 PRO A N     1 
ATOM   5573  C  CA    A PRO A 1 359 ? -14.685 -18.584 49.873  0.50 27.16 ? 359 PRO A CA    1 
ATOM   5574  C  CA    B PRO A 1 359 ? -15.073 -18.860 49.598  0.50 29.70 ? 359 PRO A CA    1 
ATOM   5575  C  C     A PRO A 1 359 ? -14.395 -18.685 48.388  0.50 28.06 ? 359 PRO A C     1 
ATOM   5576  C  C     B PRO A 1 359 ? -14.709 -19.019 48.135  0.50 26.43 ? 359 PRO A C     1 
ATOM   5577  O  O     A PRO A 1 359 ? -15.320 -18.879 47.585  0.50 25.79 ? 359 PRO A O     1 
ATOM   5578  O  O     B PRO A 1 359 ? -15.567 -19.362 47.304  0.50 28.67 ? 359 PRO A O     1 
ATOM   5579  C  CB    A PRO A 1 359 ? -14.424 -19.921 50.584  0.50 30.37 ? 359 PRO A CB    1 
ATOM   5580  C  CB    B PRO A 1 359 ? -14.898 -20.179 50.370  0.50 31.41 ? 359 PRO A CB    1 
ATOM   5581  C  CG    A PRO A 1 359 ? -15.511 -20.022 51.607  0.50 30.34 ? 359 PRO A CG    1 
ATOM   5582  C  CG    B PRO A 1 359 ? -16.218 -20.840 50.241  0.50 28.18 ? 359 PRO A CG    1 
ATOM   5583  C  CD    A PRO A 1 359 ? -16.710 -19.385 50.971  0.50 26.16 ? 359 PRO A CD    1 
ATOM   5584  C  CD    B PRO A 1 359 ? -17.243 -19.737 50.258  0.50 31.32 ? 359 PRO A CD    1 
ATOM   5585  N  N     A PRO A 1 360 ? -13.129 -18.562 47.983  0.50 31.05 ? 360 PRO A N     1 
ATOM   5586  N  N     B PRO A 1 360 ? -13.451 -18.779 47.768  0.50 30.97 ? 360 PRO A N     1 
ATOM   5587  C  CA    A PRO A 1 360 ? -12.804 -18.648 46.558  0.50 30.62 ? 360 PRO A CA    1 
ATOM   5588  C  CA    B PRO A 1 360 ? -13.083 -18.823 46.353  0.50 29.72 ? 360 PRO A CA    1 
ATOM   5589  C  C     A PRO A 1 360 ? -13.067 -20.042 46.015  0.50 32.30 ? 360 PRO A C     1 
ATOM   5590  C  C     B PRO A 1 360 ? -13.209 -20.229 45.798  0.50 31.86 ? 360 PRO A C     1 
ATOM   5591  O  O     A PRO A 1 360 ? -13.092 -21.038 46.742  0.50 27.74 ? 360 PRO A O     1 
ATOM   5592  O  O     B PRO A 1 360 ? -13.120 -21.223 46.522  0.50 28.22 ? 360 PRO A O     1 
ATOM   5593  C  CB    A PRO A 1 360 ? -11.306 -18.312 46.501  0.50 29.75 ? 360 PRO A CB    1 
ATOM   5594  C  CB    B PRO A 1 360 ? -11.618 -18.358 46.340  0.50 30.45 ? 360 PRO A CB    1 
ATOM   5595  C  CG    A PRO A 1 360 ? -10.981 -17.681 47.818  0.50 32.52 ? 360 PRO A CG    1 
ATOM   5596  C  CG    B PRO A 1 360 ? -11.347 -17.830 47.723  0.50 34.17 ? 360 PRO A CG    1 
ATOM   5597  C  CD    A PRO A 1 360 ? -11.936 -18.293 48.804  0.50 25.31 ? 360 PRO A CD    1 
ATOM   5598  C  CD    B PRO A 1 360 ? -12.286 -18.537 48.634  0.50 26.03 ? 360 PRO A CD    1 
ATOM   5599  N  N     A THR A 1 361 ? -13.271 -20.091 44.706  0.50 28.71 ? 361 THR A N     1 
ATOM   5600  N  N     B THR A 1 361 ? -13.437 -20.297 44.493  0.50 27.88 ? 361 THR A N     1 
ATOM   5601  C  CA    A THR A 1 361 ? -13.440 -21.337 43.979  0.50 27.62 ? 361 THR A CA    1 
ATOM   5602  C  CA    B THR A 1 361 ? -13.499 -21.552 43.768  0.50 27.46 ? 361 THR A CA    1 
ATOM   5603  C  C     A THR A 1 361 ? -12.083 -21.814 43.472  0.50 33.02 ? 361 THR A C     1 
ATOM   5604  C  C     B THR A 1 361 ? -12.163 -21.790 43.077  0.50 33.97 ? 361 THR A C     1 
ATOM   5605  O  O     A THR A 1 361 ? -11.197 -21.010 43.173  0.50 30.12 ? 361 THR A O     1 
ATOM   5606  O  O     B THR A 1 361 ? -11.588 -20.870 42.493  0.50 32.11 ? 361 THR A O     1 
ATOM   5607  C  CB    A THR A 1 361 ? -14.416 -21.136 42.815  0.50 29.38 ? 361 THR A CB    1 
ATOM   5608  C  CB    B THR A 1 361 ? -14.633 -21.526 42.740  0.50 30.10 ? 361 THR A CB    1 
ATOM   5609  O  OG1   A THR A 1 361 ? -15.698 -20.741 43.327  0.50 29.35 ? 361 THR A OG1   1 
ATOM   5610  O  OG1   B THR A 1 361 ? -15.869 -21.206 43.395  0.50 29.51 ? 361 THR A OG1   1 
ATOM   5611  C  CG2   A THR A 1 361 ? -14.576 -22.404 41.986  0.50 37.01 ? 361 THR A CG2   1 
ATOM   5612  C  CG2   B THR A 1 361 ? -14.763 -22.872 42.048  0.50 39.75 ? 361 THR A CG2   1 
ATOM   5613  N  N     A VAL A 1 362 ? -11.911 -23.132 43.416  0.50 32.94 ? 362 VAL A N     1 
ATOM   5614  N  N     B VAL A 1 362 ? -11.658 -23.017 43.173  0.50 35.05 ? 362 VAL A N     1 
ATOM   5615  C  CA    A VAL A 1 362 ? -10.750 -23.746 42.783  0.50 38.47 ? 362 VAL A CA    1 
ATOM   5616  C  CA    B VAL A 1 362 ? -10.477 -23.428 42.423  0.50 36.52 ? 362 VAL A CA    1 
ATOM   5617  C  C     A VAL A 1 362 ? -11.224 -24.504 41.552  0.50 35.67 ? 362 VAL A C     1 
ATOM   5618  C  C     B VAL A 1 362 ? -10.929 -24.347 41.298  0.50 35.83 ? 362 VAL A C     1 
ATOM   5619  O  O     A VAL A 1 362 ? -12.307 -25.101 41.558  0.50 35.06 ? 362 VAL A O     1 
ATOM   5620  O  O     B VAL A 1 362 ? -11.960 -25.023 41.396  0.50 33.14 ? 362 VAL A O     1 
ATOM   5621  C  CB    A VAL A 1 362 ? -9.988  -24.683 43.740  0.50 39.68 ? 362 VAL A CB    1 
ATOM   5622  C  CB    B VAL A 1 362 ? -9.413  -24.119 43.303  0.50 37.35 ? 362 VAL A CB    1 
ATOM   5623  C  CG1   A VAL A 1 362 ? -9.167  -23.876 44.735  0.50 38.12 ? 362 VAL A CG1   1 
ATOM   5624  C  CG1   B VAL A 1 362 ? -8.809  -23.127 44.287  0.50 32.58 ? 362 VAL A CG1   1 
ATOM   5625  C  CG2   A VAL A 1 362 ? -10.955 -25.606 44.454  0.50 42.84 ? 362 VAL A CG2   1 
ATOM   5626  C  CG2   B VAL A 1 362 ? -10.009 -25.319 44.026  0.50 41.00 ? 362 VAL A CG2   1 
ATOM   5627  N  N     A VAL A 1 363 ? -10.420 -24.469 40.495  0.50 36.42 ? 363 VAL A N     1 
ATOM   5628  N  N     B VAL A 1 363 ? -10.154 -24.364 40.220  0.50 36.44 ? 363 VAL A N     1 
ATOM   5629  C  CA    A VAL A 1 363 ? -10.752 -25.191 39.271  0.50 35.65 ? 363 VAL A CA    1 
ATOM   5630  C  CA    B VAL A 1 363 ? -10.542 -25.088 39.012  0.50 35.73 ? 363 VAL A CA    1 
ATOM   5631  C  C     A VAL A 1 363 ? -10.237 -26.620 39.401  0.50 38.26 ? 363 VAL A C     1 
ATOM   5632  C  C     B VAL A 1 363 ? -10.061 -26.532 39.095  0.50 38.22 ? 363 VAL A C     1 
ATOM   5633  O  O     A VAL A 1 363 ? -9.154  -26.842 39.963  0.50 36.12 ? 363 VAL A O     1 
ATOM   5634  O  O     B VAL A 1 363 ? -9.060  -26.816 39.770  0.50 36.04 ? 363 VAL A O     1 
ATOM   5635  C  CB    A VAL A 1 363 ? -10.178 -24.494 38.026  0.50 39.22 ? 363 VAL A CB    1 
ATOM   5636  C  CB    B VAL A 1 363 ? -9.996  -24.399 37.751  0.50 38.65 ? 363 VAL A CB    1 
ATOM   5637  C  CG1   A VAL A 1 363 ? -10.765 -23.096 37.884  0.50 37.03 ? 363 VAL A CG1   1 
ATOM   5638  C  CG1   B VAL A 1 363 ? -10.512 -22.969 37.666  0.50 37.48 ? 363 VAL A CG1   1 
ATOM   5639  C  CG2   A VAL A 1 363 ? -8.664  -24.437 38.085  0.50 41.65 ? 363 VAL A CG2   1 
ATOM   5640  C  CG2   B VAL A 1 363 ? -8.479  -24.428 37.739  0.50 43.03 ? 363 VAL A CG2   1 
ATOM   5641  N  N     A PRO A 1 364 ? -10.987 -27.615 38.933  0.50 39.01 ? 364 PRO A N     1 
ATOM   5642  N  N     B PRO A 1 364 ? -10.748 -27.472 38.447  0.50 38.24 ? 364 PRO A N     1 
ATOM   5643  C  CA    A PRO A 1 364 ? -10.466 -28.986 38.932  0.50 39.62 ? 364 PRO A CA    1 
ATOM   5644  C  CA    B PRO A 1 364 ? -10.208 -28.832 38.341  0.50 40.07 ? 364 PRO A CA    1 
ATOM   5645  C  C     A PRO A 1 364 ? -9.234  -29.084 38.046  0.50 38.45 ? 364 PRO A C     1 
ATOM   5646  C  C     B PRO A 1 364 ? -8.908  -28.822 37.554  0.50 40.79 ? 364 PRO A C     1 
ATOM   5647  O  O     A PRO A 1 364 ? -9.209  -28.566 36.927  0.50 41.76 ? 364 PRO A O     1 
ATOM   5648  O  O     B PRO A 1 364 ? -8.833  -28.273 36.452  0.50 39.55 ? 364 PRO A O     1 
ATOM   5649  C  CB    A PRO A 1 364 ? -11.635 -29.811 38.382  0.50 42.36 ? 364 PRO A CB    1 
ATOM   5650  C  CB    B PRO A 1 364 ? -11.315 -29.598 37.606  0.50 39.93 ? 364 PRO A CB    1 
ATOM   5651  C  CG    A PRO A 1 364 ? -12.476 -28.828 37.624  0.50 45.00 ? 364 PRO A CG    1 
ATOM   5652  C  CG    B PRO A 1 364 ? -12.097 -28.545 36.889  0.50 46.48 ? 364 PRO A CG    1 
ATOM   5653  C  CD    A PRO A 1 364 ? -12.346 -27.535 38.372  0.50 40.57 ? 364 PRO A CD    1 
ATOM   5654  C  CD    B PRO A 1 364 ? -12.054 -27.342 37.781  0.50 40.51 ? 364 PRO A CD    1 
ATOM   5655  N  N     A GLY A 1 365 ? -8.202  -29.744 38.563  0.50 37.56 ? 365 GLY A N     1 
ATOM   5656  N  N     B GLY A 1 365 ? -7.878  -29.426 38.133  0.50 37.95 ? 365 GLY A N     1 
ATOM   5657  C  CA    A GLY A 1 365 ? -6.936  -29.832 37.870  0.50 38.92 ? 365 GLY A CA    1 
ATOM   5658  C  CA    B GLY A 1 365 ? -6.558  -29.385 37.546  0.50 38.43 ? 365 GLY A CA    1 
ATOM   5659  C  C     A GLY A 1 365 ? -5.987  -28.686 38.128  0.50 38.50 ? 365 GLY A C     1 
ATOM   5660  C  C     B GLY A 1 365 ? -5.688  -28.243 38.017  0.50 38.58 ? 365 GLY A C     1 
ATOM   5661  O  O     A GLY A 1 365 ? -4.873  -28.691 37.585  0.50 34.26 ? 365 GLY A O     1 
ATOM   5662  O  O     B GLY A 1 365 ? -4.628  -28.010 37.424  0.50 35.82 ? 365 GLY A O     1 
ATOM   5663  N  N     A GLY A 1 366 ? -6.381  -27.713 38.942  0.50 35.60 ? 366 GLY A N     1 
ATOM   5664  N  N     B GLY A 1 366 ? -6.096  -27.525 39.061  0.50 35.73 ? 366 GLY A N     1 
ATOM   5665  C  CA    A GLY A 1 366 ? -5.538  -26.580 39.236  0.50 31.48 ? 366 GLY A CA    1 
ATOM   5666  C  CA    B GLY A 1 366 ? -5.311  -26.411 39.537  0.50 30.03 ? 366 GLY A CA    1 
ATOM   5667  C  C     A GLY A 1 366 ? -4.383  -26.942 40.153  0.50 35.15 ? 366 GLY A C     1 
ATOM   5668  C  C     B GLY A 1 366 ? -4.222  -26.828 40.507  0.50 34.02 ? 366 GLY A C     1 
ATOM   5669  O  O     A GLY A 1 366 ? -4.121  -28.102 40.478  0.50 33.66 ? 366 GLY A O     1 
ATOM   5670  O  O     B GLY A 1 366 ? -4.238  -27.912 41.093  0.50 30.84 ? 366 GLY A O     1 
ATOM   5671  N  N     A ASP A 1 367 ? -3.676  -25.897 40.577  0.50 28.15 ? 367 ASP A N     1 
ATOM   5672  N  N     B ASP A 1 367 ? -3.247  -25.940 40.662  0.50 29.30 ? 367 ASP A N     1 
ATOM   5673  C  CA    A ASP A 1 367 ? -2.522  -26.030 41.449  0.50 30.84 ? 367 ASP A CA    1 
ATOM   5674  C  CA    B ASP A 1 367 ? -2.157  -26.132 41.605  0.50 30.94 ? 367 ASP A CA    1 
ATOM   5675  C  C     A ASP A 1 367 ? -2.776  -25.514 42.857  0.50 29.61 ? 367 ASP A C     1 
ATOM   5676  C  C     B ASP A 1 367 ? -2.472  -25.565 42.982  0.50 29.88 ? 367 ASP A C     1 
ATOM   5677  O  O     A ASP A 1 367 ? -1.904  -25.666 43.719  0.50 31.27 ? 367 ASP A O     1 
ATOM   5678  O  O     B ASP A 1 367 ? -1.626  -25.648 43.878  0.50 31.88 ? 367 ASP A O     1 
ATOM   5679  C  CB    A ASP A 1 367 ? -1.320  -25.281 40.851  0.50 30.19 ? 367 ASP A CB    1 
ATOM   5680  C  CB    B ASP A 1 367 ? -0.875  -25.487 41.065  0.50 31.94 ? 367 ASP A CB    1 
ATOM   5681  C  CG    A ASP A 1 367 ? -0.956  -25.770 39.461  0.50 32.31 ? 367 ASP A CG    1 
ATOM   5682  C  CG    B ASP A 1 367 ? -0.511  -25.979 39.677  0.50 33.47 ? 367 ASP A CG    1 
ATOM   5683  O  OD1   A ASP A 1 367 ? -0.539  -26.940 39.333  0.50 38.80 ? 367 ASP A OD1   1 
ATOM   5684  O  OD1   B ASP A 1 367 ? -0.641  -27.192 39.420  0.50 39.55 ? 367 ASP A OD1   1 
ATOM   5685  O  OD2   A ASP A 1 367 ? -1.091  -24.985 38.495  0.50 24.54 ? 367 ASP A OD2   1 
ATOM   5686  O  OD2   B ASP A 1 367 ? -0.096  -25.150 38.839  0.50 30.40 ? 367 ASP A OD2   1 
ATOM   5687  N  N     A LEU A 1 368 ? -3.936  -24.918 43.113  0.50 31.20 ? 368 LEU A N     1 
ATOM   5688  N  N     B LEU A 1 368 ? -3.660  -24.996 43.165  0.50 30.48 ? 368 LEU A N     1 
ATOM   5689  C  CA    A LEU A 1 368 ? -4.215  -24.244 44.372  0.50 28.73 ? 368 LEU A CA    1 
ATOM   5690  C  CA    B LEU A 1 368 ? -4.043  -24.318 44.396  0.50 28.89 ? 368 LEU A CA    1 
ATOM   5691  C  C     A LEU A 1 368 ? -5.045  -25.121 45.298  0.50 31.57 ? 368 LEU A C     1 
ATOM   5692  C  C     B LEU A 1 368 ? -4.976  -25.191 45.224  0.50 31.52 ? 368 LEU A C     1 
ATOM   5693  O  O     A LEU A 1 368 ? -5.954  -25.830 44.855  0.50 30.33 ? 368 LEU A O     1 
ATOM   5694  O  O     B LEU A 1 368 ? -5.913  -25.795 44.693  0.50 30.45 ? 368 LEU A O     1 
ATOM   5695  C  CB    A LEU A 1 368 ? -4.953  -22.927 44.132  0.50 30.39 ? 368 LEU A CB    1 
ATOM   5696  C  CB    B LEU A 1 368 ? -4.734  -22.989 44.086  0.50 30.41 ? 368 LEU A CB    1 
ATOM   5697  C  CG    A LEU A 1 368 ? -4.077  -21.722 43.798  0.50 30.34 ? 368 LEU A CG    1 
ATOM   5698  C  CG    B LEU A 1 368 ? -3.911  -21.897 43.404  0.50 30.74 ? 368 LEU A CG    1 
ATOM   5699  C  CD1   A LEU A 1 368 ? -4.858  -20.432 43.996  0.50 32.07 ? 368 LEU A CD1   1 
ATOM   5700  C  CD1   B LEU A 1 368 ? -4.799  -21.061 42.499  0.50 30.38 ? 368 LEU A CD1   1 
ATOM   5701  C  CD2   A LEU A 1 368 ? -2.822  -21.734 44.652  0.50 33.30 ? 368 LEU A CD2   1 
ATOM   5702  C  CD2   B LEU A 1 368 ? -3.235  -21.024 44.444  0.50 38.31 ? 368 LEU A CD2   1 
ATOM   5703  N  N     A ALA A 1 369 ? -4.732  -25.054 46.588  0.50 33.70 ? 369 ALA A N     1 
ATOM   5704  N  N     B ALA A 1 369 ? -4.722  -25.242 46.528  0.50 33.89 ? 369 ALA A N     1 
ATOM   5705  C  CA    A ALA A 1 369 ? -5.539  -25.708 47.604  0.50 34.96 ? 369 ALA A CA    1 
ATOM   5706  C  CA    B ALA A 1 369 ? -5.605  -25.950 47.438  0.50 34.50 ? 369 ALA A CA    1 
ATOM   5707  C  C     A ALA A 1 369 ? -6.763  -24.865 47.930  0.50 31.74 ? 369 ALA A C     1 
ATOM   5708  C  C     B ALA A 1 369 ? -6.825  -25.097 47.769  0.50 31.24 ? 369 ALA A C     1 
ATOM   5709  O  O     A ALA A 1 369 ? -6.763  -23.641 47.764  0.50 30.12 ? 369 ALA A O     1 
ATOM   5710  O  O     B ALA A 1 369 ? -6.831  -23.876 47.590  0.50 30.65 ? 369 ALA A O     1 
ATOM   5711  C  CB    A ALA A 1 369 ? -4.723  -25.938 48.876  0.50 37.22 ? 369 ALA A CB    1 
ATOM   5712  C  CB    B ALA A 1 369 ? -4.869  -26.325 48.723  0.50 39.45 ? 369 ALA A CB    1 
ATOM   5713  N  N     A LYS A 1 370 ? -7.815  -25.533 48.391  0.50 32.13 ? 370 LYS A N     1 
ATOM   5714  N  N     B LYS A 1 370 ? -7.870  -25.760 48.258  0.50 32.12 ? 370 LYS A N     1 
ATOM   5715  C  CA    A LYS A 1 370 ? -8.970  -24.823 48.920  0.50 37.36 ? 370 LYS A CA    1 
ATOM   5716  C  CA    B LYS A 1 370 ? -9.045  -25.047 48.739  0.50 37.56 ? 370 LYS A CA    1 
ATOM   5717  C  C     A LYS A 1 370 ? -8.586  -24.096 50.201  0.50 31.27 ? 370 LYS A C     1 
ATOM   5718  C  C     B LYS A 1 370 ? -8.692  -24.229 49.974  0.50 31.34 ? 370 LYS A C     1 
ATOM   5719  O  O     A LYS A 1 370 ? -7.844  -24.624 51.032  0.50 35.57 ? 370 LYS A O     1 
ATOM   5720  O  O     B LYS A 1 370 ? -7.972  -24.695 50.861  0.50 35.09 ? 370 LYS A O     1 
ATOM   5721  C  CB    A LYS A 1 370 ? -10.119 -25.794 49.194  0.50 38.18 ? 370 LYS A CB    1 
ATOM   5722  C  CB    B LYS A 1 370 ? -10.173 -26.026 49.074  0.50 38.22 ? 370 LYS A CB    1 
ATOM   5723  C  CG    A LYS A 1 370 ? -10.719 -26.420 47.947  0.50 43.50 ? 370 LYS A CG    1 
ATOM   5724  C  CG    B LYS A 1 370 ? -10.821 -26.710 47.876  0.50 44.17 ? 370 LYS A CG    1 
ATOM   5725  C  CD    A LYS A 1 370 ? -11.871 -27.354 48.295  0.50 47.13 ? 370 LYS A CD    1 
ATOM   5726  C  CD    B LYS A 1 370 ? -12.086 -27.452 48.306  0.50 46.70 ? 370 LYS A CD    1 
ATOM   5727  C  CE    A LYS A 1 370 ? -12.609 -27.809 47.045  0.50 51.72 ? 370 LYS A CE    1 
ATOM   5728  C  CE    B LYS A 1 370 ? -12.832 -28.060 47.123  0.50 51.77 ? 370 LYS A CE    1 
ATOM   5729  N  NZ    A LYS A 1 370 ? -11.689 -28.414 46.042  0.50 50.69 ? 370 LYS A NZ    1 
ATOM   5730  N  NZ    B LYS A 1 370 ? -12.174 -29.289 46.591  0.50 47.57 ? 370 LYS A NZ    1 
ATOM   5731  N  N     A VAL A 1 371 ? -9.085  -22.869 50.355  0.50 30.26 ? 371 VAL A N     1 
ATOM   5732  N  N     B VAL A 1 371 ? -9.194  -22.997 50.027  0.50 29.85 ? 371 VAL A N     1 
ATOM   5733  C  CA    A VAL A 1 371 ? -8.862  -22.090 51.566  0.50 33.00 ? 371 VAL A CA    1 
ATOM   5734  C  CA    B VAL A 1 371 ? -9.030  -22.141 51.194  0.50 31.99 ? 371 VAL A CA    1 
ATOM   5735  C  C     A VAL A 1 371 ? -10.196 -21.551 52.065  0.50 29.30 ? 371 VAL A C     1 
ATOM   5736  C  C     B VAL A 1 371 ? -10.399 -21.647 51.638  0.50 29.60 ? 371 VAL A C     1 
ATOM   5737  O  O     A VAL A 1 371 ? -11.163 -21.416 51.314  0.50 27.59 ? 371 VAL A O     1 
ATOM   5738  O  O     B VAL A 1 371 ? -11.316 -21.474 50.828  0.50 27.40 ? 371 VAL A O     1 
ATOM   5739  C  CB    A VAL A 1 371 ? -7.860  -20.934 51.353  0.50 30.08 ? 371 VAL A CB    1 
ATOM   5740  C  CB    B VAL A 1 371 ? -8.082  -20.949 50.923  0.50 30.48 ? 371 VAL A CB    1 
ATOM   5741  C  CG1   A VAL A 1 371 ? -6.477  -21.478 51.010  0.50 29.17 ? 371 VAL A CG1   1 
ATOM   5742  C  CG1   B VAL A 1 371 ? -6.711  -21.441 50.471  0.50 29.47 ? 371 VAL A CG1   1 
ATOM   5743  C  CG2   A VAL A 1 371 ? -8.358  -19.988 50.271  0.50 27.99 ? 371 VAL A CG2   1 
ATOM   5744  C  CG2   B VAL A 1 371 ? -8.683  -20.003 49.898  0.50 28.53 ? 371 VAL A CG2   1 
ATOM   5745  N  N     A GLN A 1 372 ? -10.231 -21.237 53.359  0.50 33.63 ? 372 GLN A N     1 
ATOM   5746  N  N     B GLN A 1 372 ? -10.535 -21.419 52.943  0.50 31.63 ? 372 GLN A N     1 
ATOM   5747  C  CA    A GLN A 1 372 ? -11.442 -20.735 53.997  0.50 31.86 ? 372 GLN A CA    1 
ATOM   5748  C  CA    B GLN A 1 372 ? -11.791 -20.944 53.505  0.50 29.46 ? 372 GLN A CA    1 
ATOM   5749  C  C     A GLN A 1 372 ? -11.589 -19.225 53.884  0.50 28.76 ? 372 GLN A C     1 
ATOM   5750  C  C     B GLN A 1 372 ? -11.924 -19.430 53.472  0.50 28.64 ? 372 GLN A C     1 
ATOM   5751  O  O     A GLN A 1 372 ? -12.714 -18.712 53.922  0.50 25.34 ? 372 GLN A O     1 
ATOM   5752  O  O     B GLN A 1 372 ? -13.044 -18.916 53.591  0.50 27.16 ? 372 GLN A O     1 
ATOM   5753  C  CB    A GLN A 1 372 ? -11.465 -21.140 55.473  0.50 30.41 ? 372 GLN A CB    1 
ATOM   5754  C  CB    B GLN A 1 372 ? -11.944 -21.434 54.949  0.50 36.08 ? 372 GLN A CB    1 
ATOM   5755  C  CG    A GLN A 1 372 ? -11.941 -22.562 55.704  0.50 36.96 ? 372 GLN A CG    1 
ATOM   5756  C  CG    B GLN A 1 372 ? -12.267 -22.914 55.057  0.50 35.14 ? 372 GLN A CG    1 
ATOM   5757  C  CD    A GLN A 1 372 ? -13.318 -22.808 55.123  0.50 34.46 ? 372 GLN A CD    1 
ATOM   5758  C  CD    B GLN A 1 372 ? -13.485 -23.300 54.237  0.50 41.37 ? 372 GLN A CD    1 
ATOM   5759  O  OE1   A GLN A 1 372 ? -13.462 -23.451 54.082  0.50 41.90 ? 372 GLN A OE1   1 
ATOM   5760  O  OE1   B GLN A 1 372 ? -13.476 -24.304 53.523  0.50 38.27 ? 372 GLN A OE1   1 
ATOM   5761  N  NE2   A GLN A 1 372 ? -14.341 -22.291 55.791  0.50 34.20 ? 372 GLN A NE2   1 
ATOM   5762  N  NE2   B GLN A 1 372 ? -14.543 -22.498 54.333  0.50 34.00 ? 372 GLN A NE2   1 
ATOM   5763  N  N     A ARG A 1 373 ? -10.481 -18.501 53.766  0.50 23.04 ? 373 ARG A N     1 
ATOM   5764  N  N     B ARG A 1 373 ? -10.818 -18.707 53.324  0.50 24.01 ? 373 ARG A N     1 
ATOM   5765  C  CA    A ARG A 1 373 ? -10.536 -17.064 53.564  0.50 25.43 ? 373 ARG A CA    1 
ATOM   5766  C  CA    B ARG A 1 373 ? -10.864 -17.254 53.237  0.50 26.31 ? 373 ARG A CA    1 
ATOM   5767  C  C     A ARG A 1 373 ? -9.328  -16.638 52.748  0.50 21.12 ? 373 ARG A C     1 
ATOM   5768  C  C     B ARG A 1 373 ? -9.654  -16.768 52.456  0.50 22.32 ? 373 ARG A C     1 
ATOM   5769  O  O     A ARG A 1 373 ? -8.263  -17.257 52.810  0.50 22.92 ? 373 ARG A O     1 
ATOM   5770  O  O     B ARG A 1 373 ? -8.526  -17.201 52.713  0.50 22.86 ? 373 ARG A O     1 
ATOM   5771  C  CB    A ARG A 1 373 ? -10.581 -16.295 54.886  0.50 22.99 ? 373 ARG A CB    1 
ATOM   5772  C  CB    B ARG A 1 373 ? -10.903 -16.611 54.627  0.50 25.24 ? 373 ARG A CB    1 
ATOM   5773  C  CG    A ARG A 1 373 ? -9.433  -16.592 55.819  0.50 26.42 ? 373 ARG A CG    1 
ATOM   5774  C  CG    B ARG A 1 373 ? -9.815  -17.078 55.577  0.50 23.74 ? 373 ARG A CG    1 
ATOM   5775  C  CD    A ARG A 1 373 ? -9.676  -15.966 57.181  0.50 25.60 ? 373 ARG A CD    1 
ATOM   5776  C  CD    B ARG A 1 373 ? -10.166 -16.738 57.019  0.50 25.58 ? 373 ARG A CD    1 
ATOM   5777  N  NE    A ARG A 1 373 ? -10.855 -16.529 57.825  0.50 26.43 ? 373 ARG A NE    1 
ATOM   5778  N  NE    B ARG A 1 373 ? -11.087 -17.709 57.600  0.50 29.91 ? 373 ARG A NE    1 
ATOM   5779  C  CZ    A ARG A 1 373 ? -10.834 -17.591 58.618  0.50 27.07 ? 373 ARG A CZ    1 
ATOM   5780  C  CZ    B ARG A 1 373 ? -10.708 -18.830 58.201  0.50 29.00 ? 373 ARG A CZ    1 
ATOM   5781  N  NH1   A ARG A 1 373 ? -9.706  -18.228 58.890  0.50 34.70 ? 373 ARG A NH1   1 
ATOM   5782  N  NH1   B ARG A 1 373 ? -9.430  -19.155 58.315  0.50 30.96 ? 373 ARG A NH1   1 
ATOM   5783  N  NH2   A ARG A 1 373 ? -11.971 -18.027 59.148  0.50 24.48 ? 373 ARG A NH2   1 
ATOM   5784  N  NH2   B ARG A 1 373 ? -11.634 -19.648 58.695  0.50 31.89 ? 373 ARG A NH2   1 
ATOM   5785  N  N     A ALA A 1 374 ? -9.515  -15.578 51.973  0.50 18.20 ? 374 ALA A N     1 
ATOM   5786  N  N     B ALA A 1 374 ? -9.897  -15.879 51.501  0.50 18.78 ? 374 ALA A N     1 
ATOM   5787  C  CA    A ALA A 1 374 ? -8.456  -15.045 51.132  0.50 20.95 ? 374 ALA A CA    1 
ATOM   5788  C  CA    B ALA A 1 374 ? -8.841  -15.283 50.700  0.50 23.26 ? 374 ALA A CA    1 
ATOM   5789  C  C     A ALA A 1 374 ? -8.654  -13.543 51.038  0.50 23.95 ? 374 ALA A C     1 
ATOM   5790  C  C     B ALA A 1 374 ? -9.068  -13.782 50.628  0.50 23.73 ? 374 ALA A C     1 
ATOM   5791  O  O     A ALA A 1 374 ? -9.693  -13.006 51.437  0.50 20.36 ? 374 ALA A O     1 
ATOM   5792  O  O     B ALA A 1 374 ? -10.169 -13.283 50.883  0.50 22.77 ? 374 ALA A O     1 
ATOM   5793  C  CB    A ALA A 1 374 ? -8.449  -15.701 49.747  0.50 22.48 ? 374 ALA A CB    1 
ATOM   5794  C  CB    B ALA A 1 374 ? -8.785  -15.883 49.288  0.50 21.40 ? 374 ALA A CB    1 
ATOM   5795  N  N     A VAL A 1 375 ? -7.641  -12.861 50.518  0.50 20.92 ? 375 VAL A N     1 
ATOM   5796  N  N     B VAL A 1 375 ? -8.009  -13.059 50.284  0.50 21.90 ? 375 VAL A N     1 
ATOM   5797  C  CA    A VAL A 1 375 ? -7.684  -11.407 50.440  0.50 20.98 ? 375 VAL A CA    1 
ATOM   5798  C  CA    B VAL A 1 375 ? -8.062  -11.606 50.193  0.50 20.14 ? 375 VAL A CA    1 
ATOM   5799  C  C     A VAL A 1 375 ? -6.934  -10.952 49.194  0.50 19.19 ? 375 VAL A C     1 
ATOM   5800  C  C     B VAL A 1 375 ? -7.204  -11.155 49.018  0.50 18.57 ? 375 VAL A C     1 
ATOM   5801  O  O     A VAL A 1 375 ? -5.822  -11.412 48.919  0.50 23.69 ? 375 VAL A O     1 
ATOM   5802  O  O     B VAL A 1 375 ? -6.147  -11.734 48.744  0.50 25.57 ? 375 VAL A O     1 
ATOM   5803  C  CB    A VAL A 1 375 ? -7.104  -10.757 51.713  0.50 23.59 ? 375 VAL A CB    1 
ATOM   5804  C  CB    B VAL A 1 375 ? -7.596  -10.940 51.506  0.50 20.96 ? 375 VAL A CB    1 
ATOM   5805  C  CG1   A VAL A 1 375 ? -5.698  -11.272 51.997  0.50 25.48 ? 375 VAL A CG1   1 
ATOM   5806  C  CG1   B VAL A 1 375 ? -6.158  -11.323 51.831  0.50 24.60 ? 375 VAL A CG1   1 
ATOM   5807  C  CG2   A VAL A 1 375 ? -7.121  -9.245  51.595  0.50 19.60 ? 375 VAL A CG2   1 
ATOM   5808  C  CG2   B VAL A 1 375 ? -7.749  -9.421  51.435  0.50 22.04 ? 375 VAL A CG2   1 
ATOM   5809  N  N     A CYS A 1 376 ? -7.557  -10.054 48.439  0.50 21.17 ? 376 CYS A N     1 
ATOM   5810  N  N     B CYS A 1 376 ? -7.668  -10.123 48.324  0.50 21.23 ? 376 CYS A N     1 
ATOM   5811  C  CA    A CYS A 1 376 ? -6.920  -9.357  47.329  0.50 22.23 ? 376 CYS A CA    1 
ATOM   5812  C  CA    B CYS A 1 376 ? -6.883  -9.426  47.316  0.50 22.19 ? 376 CYS A CA    1 
ATOM   5813  C  C     A CYS A 1 376 ? -6.850  -7.884  47.696  0.50 24.07 ? 376 CYS A C     1 
ATOM   5814  C  C     B CYS A 1 376 ? -6.870  -7.949  47.673  0.50 24.07 ? 376 CYS A C     1 
ATOM   5815  O  O     A CYS A 1 376 ? -7.889  -7.250  47.909  0.50 24.89 ? 376 CYS A O     1 
ATOM   5816  O  O     B CYS A 1 376 ? -7.931  -7.356  47.894  0.50 24.71 ? 376 CYS A O     1 
ATOM   5817  C  CB    A CYS A 1 376 ? -7.702  -9.547  46.029  0.50 21.58 ? 376 CYS A CB    1 
ATOM   5818  C  CB    B CYS A 1 376 ? -7.460  -9.627  45.915  0.50 23.51 ? 376 CYS A CB    1 
ATOM   5819  S  SG    A CYS A 1 376 ? -7.064  -8.569  44.640  0.50 25.07 ? 376 CYS A SG    1 
ATOM   5820  S  SG    B CYS A 1 376 ? -6.415  -8.942  44.610  0.50 26.88 ? 376 CYS A SG    1 
ATOM   5821  N  N     A MET A 1 377 ? -5.635  -7.350  47.802  0.50 24.64 ? 377 MET A N     1 
ATOM   5822  N  N     B MET A 1 377 ? -5.675  -7.368  47.760  0.50 24.66 ? 377 MET A N     1 
ATOM   5823  C  CA    A MET A 1 377 ? -5.433  -5.941  48.112  0.50 24.26 ? 377 MET A CA    1 
ATOM   5824  C  CA    B MET A 1 377 ? -5.516  -5.955  48.075  0.50 24.23 ? 377 MET A CA    1 
ATOM   5825  C  C     A MET A 1 377 ? -5.082  -5.194  46.834  0.50 24.77 ? 377 MET A C     1 
ATOM   5826  C  C     B MET A 1 377 ? -5.096  -5.199  46.824  0.50 24.76 ? 377 MET A C     1 
ATOM   5827  O  O     A MET A 1 377 ? -4.076  -5.503  46.182  0.50 23.41 ? 377 MET A O     1 
ATOM   5828  O  O     B MET A 1 377 ? -4.169  -5.616  46.118  0.50 23.53 ? 377 MET A O     1 
ATOM   5829  C  CB    A MET A 1 377 ? -4.336  -5.745  49.158  0.50 21.57 ? 377 MET A CB    1 
ATOM   5830  C  CB    B MET A 1 377 ? -4.486  -5.733  49.186  0.50 21.64 ? 377 MET A CB    1 
ATOM   5831  C  CG    A MET A 1 377 ? -3.897  -4.290  49.289  0.50 26.98 ? 377 MET A CG    1 
ATOM   5832  C  CG    B MET A 1 377 ? -4.305  -4.260  49.537  0.50 27.38 ? 377 MET A CG    1 
ATOM   5833  S  SD    A MET A 1 377 ? -2.646  -3.986  50.552  0.50 43.47 ? 377 MET A SD    1 
ATOM   5834  S  SD    B MET A 1 377 ? -3.184  -3.936  50.912  0.50 26.34 ? 377 MET A SD    1 
ATOM   5835  C  CE    A MET A 1 377 ? -3.618  -4.136  52.044  0.50 39.83 ? 377 MET A CE    1 
ATOM   5836  C  CE    B MET A 1 377 ? -1.595  -3.919  50.077  0.50 28.83 ? 377 MET A CE    1 
ATOM   5837  N  N     A LEU A 1 378 ? -5.913  -4.219  46.478  0.50 22.25 ? 378 LEU A N     1 
ATOM   5838  N  N     B LEU A 1 378 ? -5.776  -4.089  46.560  0.50 22.55 ? 378 LEU A N     1 
ATOM   5839  C  CA    A LEU A 1 378 ? -5.626  -3.290  45.392  0.50 25.47 ? 378 LEU A CA    1 
ATOM   5840  C  CA    B LEU A 1 378 ? -5.436  -3.185  45.473  0.50 25.40 ? 378 LEU A CA    1 
ATOM   5841  C  C     A LEU A 1 378 ? -5.182  -1.974  46.017  0.50 26.84 ? 378 LEU A C     1 
ATOM   5842  C  C     B LEU A 1 378 ? -4.956  -1.871  46.071  0.50 27.05 ? 378 LEU A C     1 
ATOM   5843  O  O     A LEU A 1 378 ? -5.983  -1.281  46.654  0.50 27.84 ? 378 LEU A O     1 
ATOM   5844  O  O     B LEU A 1 378 ? -5.587  -1.336  46.990  0.50 23.74 ? 378 LEU A O     1 
ATOM   5845  C  CB    A LEU A 1 378 ? -6.848  -3.082  44.502  0.50 24.82 ? 378 LEU A CB    1 
ATOM   5846  C  CB    B LEU A 1 378 ? -6.641  -2.960  44.561  0.50 24.65 ? 378 LEU A CB    1 
ATOM   5847  C  CG    A LEU A 1 378 ? -7.561  -4.319  43.963  0.50 27.16 ? 378 LEU A CG    1 
ATOM   5848  C  CG    B LEU A 1 378 ? -7.362  -4.260  44.206  0.50 26.56 ? 378 LEU A CG    1 
ATOM   5849  C  CD1   A LEU A 1 378 ? -8.761  -3.900  43.140  0.50 28.53 ? 378 LEU A CD1   1 
ATOM   5850  C  CD1   B LEU A 1 378 ? -8.658  -3.984  43.473  0.50 27.19 ? 378 LEU A CD1   1 
ATOM   5851  C  CD2   A LEU A 1 378 ? -6.607  -5.171  43.130  0.50 26.61 ? 378 LEU A CD2   1 
ATOM   5852  C  CD2   B LEU A 1 378 ? -6.451  -5.163  43.376  0.50 26.97 ? 378 LEU A CD2   1 
ATOM   5853  N  N     A SER A 1 379 ? -3.909  -1.639  45.857  0.50 25.30 ? 379 SER A N     1 
ATOM   5854  N  N     B SER A 1 379 ? -3.834  -1.363  45.567  0.50 24.78 ? 379 SER A N     1 
ATOM   5855  C  CA    A SER A 1 379 ? -3.389  -0.365  46.320  0.50 23.75 ? 379 SER A CA    1 
ATOM   5856  C  CA    B SER A 1 379 ? -3.252  -0.151  46.123  0.50 23.34 ? 379 SER A CA    1 
ATOM   5857  C  C     A SER A 1 379 ? -2.829  0.409   45.136  0.50 28.36 ? 379 SER A C     1 
ATOM   5858  C  C     B SER A 1 379 ? -2.566  0.639   45.022  0.50 29.43 ? 379 SER A C     1 
ATOM   5859  O  O     A SER A 1 379 ? -2.716  -0.107  44.021  0.50 25.85 ? 379 SER A O     1 
ATOM   5860  O  O     B SER A 1 379 ? -1.808  0.075   44.226  0.50 28.75 ? 379 SER A O     1 
ATOM   5861  C  CB    A SER A 1 379 ? -2.320  -0.557  47.408  0.50 26.48 ? 379 SER A CB    1 
ATOM   5862  C  CB    B SER A 1 379 ? -2.255  -0.476  47.245  0.50 26.82 ? 379 SER A CB    1 
ATOM   5863  O  OG    A SER A 1 379 ? -1.281  -1.428  46.985  0.50 33.10 ? 379 SER A OG    1 
ATOM   5864  O  OG    B SER A 1 379 ? -1.122  -1.169  46.744  0.50 33.15 ? 379 SER A OG    1 
ATOM   5865  N  N     A ASN A 1 380 ? -2.504  1.674   45.386  0.50 27.55 ? 380 ASN A N     1 
ATOM   5866  N  N     B ASN A 1 380 ? -2.844  1.938   44.977  0.50 28.63 ? 380 ASN A N     1 
ATOM   5867  C  CA    A ASN A 1 380 ? -1.794  2.514   44.427  0.50 25.40 ? 380 ASN A CA    1 
ATOM   5868  C  CA    B ASN A 1 380 ? -2.109  2.861   44.116  0.50 26.71 ? 380 ASN A CA    1 
ATOM   5869  C  C     A ASN A 1 380 ? -0.606  3.110   45.165  0.50 28.24 ? 380 ASN A C     1 
ATOM   5870  C  C     B ASN A 1 380 ? -0.946  3.399   44.938  0.50 28.36 ? 380 ASN A C     1 
ATOM   5871  O  O     A ASN A 1 380 ? -0.775  3.981   46.025  0.50 26.57 ? 380 ASN A O     1 
ATOM   5872  O  O     B ASN A 1 380 ? -1.107  4.324   45.738  0.50 28.96 ? 380 ASN A O     1 
ATOM   5873  C  CB    A ASN A 1 380 ? -2.695  3.607   43.844  0.50 25.11 ? 380 ASN A CB    1 
ATOM   5874  C  CB    B ASN A 1 380 ? -3.014  3.978   43.607  0.50 24.67 ? 380 ASN A CB    1 
ATOM   5875  C  CG    A ASN A 1 380 ? -2.119  4.223   42.576  0.50 28.19 ? 380 ASN A CG    1 
ATOM   5876  C  CG    B ASN A 1 380 ? -2.490  4.617   42.325  0.50 27.13 ? 380 ASN A CG    1 
ATOM   5877  O  OD1   A ASN A 1 380 ? -0.910  4.208   42.363  0.50 24.33 ? 380 ASN A OD1   1 
ATOM   5878  O  OD1   B ASN A 1 380 ? -1.282  4.734   42.124  0.50 26.09 ? 380 ASN A OD1   1 
ATOM   5879  N  ND2   A ASN A 1 380 ? -2.987  4.768   41.730  0.50 25.40 ? 380 ASN A ND2   1 
ATOM   5880  N  ND2   B ASN A 1 380 ? -3.403  5.027   41.453  0.50 25.94 ? 380 ASN A ND2   1 
ATOM   5881  N  N     A THR A 1 381 ? 0.587   2.626   44.848  0.50 26.94 ? 381 THR A N     1 
ATOM   5882  N  N     B THR A 1 381 ? 0.224   2.795   44.765  0.50 25.77 ? 381 THR A N     1 
ATOM   5883  C  CA    A THR A 1 381 ? 1.803   3.044   45.521  0.50 30.27 ? 381 THR A CA    1 
ATOM   5884  C  CA    B THR A 1 381 ? 1.435   3.201   45.461  0.50 30.38 ? 381 THR A CA    1 
ATOM   5885  C  C     A THR A 1 381 ? 2.808   3.564   44.504  0.50 28.92 ? 381 THR A C     1 
ATOM   5886  C  C     B THR A 1 381 ? 2.464   3.677   44.447  0.50 28.47 ? 381 THR A C     1 
ATOM   5887  O  O     A THR A 1 381 ? 2.877   3.084   43.369  0.50 30.91 ? 381 THR A O     1 
ATOM   5888  O  O     B THR A 1 381 ? 2.566   3.124   43.346  0.50 32.09 ? 381 THR A O     1 
ATOM   5889  C  CB    A THR A 1 381 ? 2.418   1.891   46.318  0.50 32.19 ? 381 THR A CB    1 
ATOM   5890  C  CB    B THR A 1 381 ? 2.013   2.051   46.293  0.50 31.16 ? 381 THR A CB    1 
ATOM   5891  O  OG1   A THR A 1 381 ? 3.732   2.259   46.753  0.50 29.55 ? 381 THR A OG1   1 
ATOM   5892  O  OG1   B THR A 1 381 ? 3.355   2.369   46.681  0.50 28.75 ? 381 THR A OG1   1 
ATOM   5893  C  CG2   A THR A 1 381 ? 2.499   0.631   45.466  0.50 29.10 ? 381 THR A CG2   1 
ATOM   5894  C  CG2   B THR A 1 381 ? 2.009   0.755   45.489  0.50 30.10 ? 381 THR A CG2   1 
ATOM   5895  N  N     A THR A 1 382 ? 3.590   4.559   44.925  0.50 28.89 ? 382 THR A N     1 
ATOM   5896  N  N     B THR A 1 382 ? 3.228   4.705   44.814  0.50 27.23 ? 382 THR A N     1 
ATOM   5897  C  CA    A THR A 1 382 ? 4.629   5.097   44.054  0.50 30.97 ? 382 THR A CA    1 
ATOM   5898  C  CA    B THR A 1 382 ? 4.258   5.187   43.899  0.50 30.34 ? 382 THR A CA    1 
ATOM   5899  C  C     A THR A 1 382 ? 5.704   4.067   43.735  0.50 32.76 ? 382 THR A C     1 
ATOM   5900  C  C     B THR A 1 382 ? 5.422   4.214   43.751  0.50 32.45 ? 382 THR A C     1 
ATOM   5901  O  O     A THR A 1 382 ? 6.463   4.259   42.780  0.50 25.42 ? 382 THR A O     1 
ATOM   5902  O  O     B THR A 1 382 ? 6.319   4.475   42.941  0.50 25.80 ? 382 THR A O     1 
ATOM   5903  C  CB    A THR A 1 382 ? 5.280   6.324   44.693  0.50 33.59 ? 382 THR A CB    1 
ATOM   5904  C  CB    B THR A 1 382 ? 4.786   6.552   44.349  0.50 31.50 ? 382 THR A CB    1 
ATOM   5905  O  OG1   A THR A 1 382 ? 5.832   5.958   45.963  0.50 29.63 ? 382 THR A OG1   1 
ATOM   5906  O  OG1   B THR A 1 382 ? 5.143   6.499   45.735  0.50 32.23 ? 382 THR A OG1   1 
ATOM   5907  C  CG2   A THR A 1 382 ? 4.263   7.433   44.886  0.50 33.04 ? 382 THR A CG2   1 
ATOM   5908  C  CG2   B THR A 1 382 ? 3.739   7.629   44.132  0.50 31.01 ? 382 THR A CG2   1 
ATOM   5909  N  N     A ALA A 1 383 ? 5.776   2.975   44.502  0.50 28.61 ? 383 ALA A N     1 
ATOM   5910  N  N     B ALA A 1 383 ? 5.430   3.104   44.495  0.50 29.20 ? 383 ALA A N     1 
ATOM   5911  C  CA    A ALA A 1 383 ? 6.852   2.008   44.328  0.50 32.12 ? 383 ALA A CA    1 
ATOM   5912  C  CA    B ALA A 1 383 ? 6.485   2.112   44.337  0.50 29.87 ? 383 ALA A CA    1 
ATOM   5913  C  C     A ALA A 1 383 ? 6.757   1.246   43.013  0.50 29.83 ? 383 ALA A C     1 
ATOM   5914  C  C     B ALA A 1 383 ? 6.408   1.393   42.998  0.50 28.73 ? 383 ALA A C     1 
ATOM   5915  O  O     A ALA A 1 383 ? 7.761   0.674   42.576  0.50 29.86 ? 383 ALA A O     1 
ATOM   5916  O  O     B ALA A 1 383 ? 7.416   0.839   42.549  0.50 29.81 ? 383 ALA A O     1 
ATOM   5917  C  CB    A ALA A 1 383 ? 6.868   1.020   45.492  0.50 27.95 ? 383 ALA A CB    1 
ATOM   5918  C  CB    B ALA A 1 383 ? 6.436   1.092   45.474  0.50 29.66 ? 383 ALA A CB    1 
ATOM   5919  N  N     A ILE A 1 384 ? 5.584   1.218   42.376  0.50 27.18 ? 384 ILE A N     1 
ATOM   5920  N  N     B ILE A 1 384 ? 5.242   1.394   42.346  0.50 28.85 ? 384 ILE A N     1 
ATOM   5921  C  CA    A ILE A 1 384 ? 5.467   0.533   41.096  0.50 29.84 ? 384 ILE A CA    1 
ATOM   5922  C  CA    B ILE A 1 384 ? 5.112   0.764   41.038  0.50 29.09 ? 384 ILE A CA    1 
ATOM   5923  C  C     A ILE A 1 384 ? 6.263   1.257   40.016  0.50 30.73 ? 384 ILE A C     1 
ATOM   5924  C  C     B ILE A 1 384 ? 5.881   1.518   39.964  0.50 29.74 ? 384 ILE A C     1 
ATOM   5925  O  O     A ILE A 1 384 ? 6.606   0.653   38.991  0.50 25.55 ? 384 ILE A O     1 
ATOM   5926  O  O     B ILE A 1 384 ? 5.951   1.057   38.818  0.50 35.67 ? 384 ILE A O     1 
ATOM   5927  C  CB    A ILE A 1 384 ? 3.983   0.374   40.704  0.50 31.41 ? 384 ILE A CB    1 
ATOM   5928  C  CB    B ILE A 1 384 ? 3.619   0.617   40.676  0.50 31.30 ? 384 ILE A CB    1 
ATOM   5929  C  CG1   A ILE A 1 384 ? 3.827   -0.682  39.606  0.50 28.45 ? 384 ILE A CG1   1 
ATOM   5930  C  CG1   B ILE A 1 384 ? 3.403   -0.577  39.741  0.50 27.13 ? 384 ILE A CG1   1 
ATOM   5931  C  CG2   A ILE A 1 384 ? 3.387   1.706   40.273  0.50 29.89 ? 384 ILE A CG2   1 
ATOM   5932  C  CG2   B ILE A 1 384 ? 3.078   1.899   40.066  0.50 28.24 ? 384 ILE A CG2   1 
ATOM   5933  C  CD1   A ILE A 1 384 ? 2.400   -1.093  39.350  0.50 28.70 ? 384 ILE A CD1   1 
ATOM   5934  C  CD1   B ILE A 1 384 ? 1.967   -1.045  39.678  0.50 29.85 ? 384 ILE A CD1   1 
ATOM   5935  N  N     A ALA A 1 385 ? 6.592   2.536   40.235  0.50 27.55 ? 385 ALA A N     1 
ATOM   5936  N  N     B ALA A 1 385 ? 6.477   2.662   40.314  0.50 27.17 ? 385 ALA A N     1 
ATOM   5937  C  CA    A ALA A 1 385 ? 7.491   3.247   39.331  0.50 31.35 ? 385 ALA A CA    1 
ATOM   5938  C  CA    B ALA A 1 385 ? 7.426   3.316   39.420  0.50 31.37 ? 385 ALA A CA    1 
ATOM   5939  C  C     A ALA A 1 385 ? 8.792   2.484   39.111  0.50 29.13 ? 385 ALA A C     1 
ATOM   5940  C  C     B ALA A 1 385 ? 8.612   2.413   39.101  0.50 28.91 ? 385 ALA A C     1 
ATOM   5941  O  O     A ALA A 1 385 ? 9.397   2.590   38.038  0.50 29.30 ? 385 ALA A O     1 
ATOM   5942  O  O     B ALA A 1 385 ? 9.163   2.488   37.997  0.50 28.66 ? 385 ALA A O     1 
ATOM   5943  C  CB    A ALA A 1 385 ? 7.789   4.644   39.878  0.50 28.18 ? 385 ALA A CB    1 
ATOM   5944  C  CB    B ALA A 1 385 ? 7.916   4.625   40.040  0.50 27.89 ? 385 ALA A CB    1 
ATOM   5945  N  N     A GLU A 1 386 ? 9.238   1.718   40.114  0.50 25.96 ? 386 GLU A N     1 
ATOM   5946  N  N     B GLU A 1 386 ? 9.019   1.563   40.055  0.50 26.36 ? 386 GLU A N     1 
ATOM   5947  C  CA    A GLU A 1 386 ? 10.432  0.892   39.950  0.50 31.22 ? 386 GLU A CA    1 
ATOM   5948  C  CA    B GLU A 1 386 ? 10.157  0.670   39.844  0.50 31.53 ? 386 GLU A CA    1 
ATOM   5949  C  C     A GLU A 1 386 ? 10.281  -0.072  38.781  0.50 32.04 ? 386 GLU A C     1 
ATOM   5950  C  C     B GLU A 1 386 ? 9.995   -0.159  38.578  0.50 32.48 ? 386 GLU A C     1 
ATOM   5951  O  O     A GLU A 1 386 ? 11.247  -0.329  38.049  0.50 30.25 ? 386 GLU A O     1 
ATOM   5952  O  O     B GLU A 1 386 ? 10.954  -0.342  37.817  0.50 31.63 ? 386 GLU A O     1 
ATOM   5953  C  CB    A GLU A 1 386 ? 10.719  0.121   41.242  0.50 33.76 ? 386 GLU A CB    1 
ATOM   5954  C  CB    B GLU A 1 386 ? 10.335  -0.260  41.049  0.50 31.70 ? 386 GLU A CB    1 
ATOM   5955  C  CG    A GLU A 1 386 ? 11.132  0.991   42.419  0.50 31.17 ? 386 GLU A CG    1 
ATOM   5956  C  CG    B GLU A 1 386 ? 10.604  0.431   42.374  0.50 32.94 ? 386 GLU A CG    1 
ATOM   5957  C  CD    A GLU A 1 386 ? 11.289  0.198   43.708  0.50 38.57 ? 386 GLU A CD    1 
ATOM   5958  C  CD    B GLU A 1 386 ? 10.901  -0.562  43.491  0.50 39.02 ? 386 GLU A CD    1 
ATOM   5959  O  OE1   A GLU A 1 386 ? 10.582  -0.821  43.877  0.50 35.40 ? 386 GLU A OE1   1 
ATOM   5960  O  OE1   B GLU A 1 386 ? 11.613  -1.558  43.231  0.50 39.09 ? 386 GLU A OE1   1 
ATOM   5961  O  OE2   A GLU A 1 386 ? 12.126  0.589   44.550  0.50 40.85 ? 386 GLU A OE2   1 
ATOM   5962  O  OE2   B GLU A 1 386 ? 10.414  -0.352  44.623  0.50 38.26 ? 386 GLU A OE2   1 
ATOM   5963  N  N     A ALA A 1 387 ? 9.075   -0.618  38.591  0.50 27.43 ? 387 ALA A N     1 
ATOM   5964  N  N     B ALA A 1 387 ? 8.784   -0.674  38.339  0.50 26.94 ? 387 ALA A N     1 
ATOM   5965  C  CA    A ALA A 1 387 ? 8.828   -1.491  37.449  0.50 30.86 ? 387 ALA A CA    1 
ATOM   5966  C  CA    B ALA A 1 387 ? 8.534   -1.469  37.141  0.50 30.49 ? 387 ALA A CA    1 
ATOM   5967  C  C     A ALA A 1 387 ? 8.929   -0.725  36.135  0.50 30.61 ? 387 ALA A C     1 
ATOM   5968  C  C     B ALA A 1 387 ? 8.772   -0.654  35.876  0.50 30.34 ? 387 ALA A C     1 
ATOM   5969  O  O     A ALA A 1 387 ? 9.398   -1.269  35.128  0.50 27.02 ? 387 ALA A O     1 
ATOM   5970  O  O     B ALA A 1 387 ? 9.283   -1.178  34.878  0.50 27.12 ? 387 ALA A O     1 
ATOM   5971  C  CB    A ALA A 1 387 ? 7.460   -2.158  37.584  0.50 25.71 ? 387 ALA A CB    1 
ATOM   5972  C  CB    B ALA A 1 387 ? 7.110   -2.022  37.166  0.50 26.48 ? 387 ALA A CB    1 
ATOM   5973  N  N     A TRP A 1 388 ? 8.497   0.540   36.122  0.50 28.29 ? 388 TRP A N     1 
ATOM   5974  N  N     B TRP A 1 388 ? 8.415   0.633   35.897  0.50 28.23 ? 388 TRP A N     1 
ATOM   5975  C  CA    A TRP A 1 388 ? 8.641   1.350   34.915  0.50 25.84 ? 388 TRP A CA    1 
ATOM   5976  C  CA    B TRP A 1 388 ? 8.651   1.475   34.729  0.50 26.04 ? 388 TRP A CA    1 
ATOM   5977  C  C     A TRP A 1 388 ? 10.101  1.688   34.645  0.50 29.64 ? 388 TRP A C     1 
ATOM   5978  C  C     B TRP A 1 388 ? 10.134  1.767   34.544  0.50 29.69 ? 388 TRP A C     1 
ATOM   5979  O  O     A TRP A 1 388 ? 10.530  1.717   33.486  0.50 28.96 ? 388 TRP A O     1 
ATOM   5980  O  O     B TRP A 1 388 ? 10.618  1.843   33.409  0.50 28.78 ? 388 TRP A O     1 
ATOM   5981  C  CB    A TRP A 1 388 ? 7.822   2.637   35.026  0.50 28.88 ? 388 TRP A CB    1 
ATOM   5982  C  CB    B TRP A 1 388 ? 7.875   2.786   34.843  0.50 28.46 ? 388 TRP A CB    1 
ATOM   5983  C  CG    A TRP A 1 388 ? 6.337   2.449   34.952  0.50 27.31 ? 388 TRP A CG    1 
ATOM   5984  C  CG    B TRP A 1 388 ? 6.385   2.642   34.879  0.50 27.81 ? 388 TRP A CG    1 
ATOM   5985  C  CD1   A TRP A 1 388 ? 5.415   2.868   35.868  0.50 29.54 ? 388 TRP A CD1   1 
ATOM   5986  C  CD1   B TRP A 1 388 ? 5.542   3.121   35.840  0.50 29.18 ? 388 TRP A CD1   1 
ATOM   5987  C  CD2   A TRP A 1 388 ? 5.598   1.815   33.900  0.50 29.95 ? 388 TRP A CD2   1 
ATOM   5988  C  CD2   B TRP A 1 388 ? 5.554   1.998   33.903  0.50 29.96 ? 388 TRP A CD2   1 
ATOM   5989  N  NE1   A TRP A 1 388 ? 4.150   2.526   35.456  0.50 26.57 ? 388 TRP A NE1   1 
ATOM   5990  N  NE1   B TRP A 1 388 ? 4.243   2.809   35.529  0.50 26.57 ? 388 TRP A NE1   1 
ATOM   5991  C  CE2   A TRP A 1 388 ? 4.233   1.877   34.254  0.50 28.08 ? 388 TRP A CE2   1 
ATOM   5992  C  CE2   B TRP A 1 388 ? 4.221   2.117   34.347  0.50 27.59 ? 388 TRP A CE2   1 
ATOM   5993  C  CE3   A TRP A 1 388 ? 5.956   1.192   32.700  0.50 29.30 ? 388 TRP A CE3   1 
ATOM   5994  C  CE3   B TRP A 1 388 ? 5.807   1.323   32.705  0.50 29.23 ? 388 TRP A CE3   1 
ATOM   5995  C  CZ2   A TRP A 1 388 ? 3.228   1.347   33.449  0.50 25.16 ? 388 TRP A CZ2   1 
ATOM   5996  C  CZ2   B TRP A 1 388 ? 3.147   1.595   33.633  0.50 25.24 ? 388 TRP A CZ2   1 
ATOM   5997  C  CZ3   A TRP A 1 388 ? 4.954   0.665   31.901  0.50 33.33 ? 388 TRP A CZ3   1 
ATOM   5998  C  CZ3   B TRP A 1 388 ? 4.737   0.805   31.996  0.50 33.50 ? 388 TRP A CZ3   1 
ATOM   5999  C  CH2   A TRP A 1 388 ? 3.607   0.743   32.282  0.50 30.66 ? 388 TRP A CH2   1 
ATOM   6000  C  CH2   B TRP A 1 388 ? 3.424   0.941   32.464  0.50 29.79 ? 388 TRP A CH2   1 
ATOM   6001  N  N     A ALA A 1 389 ? 10.872  1.970   35.698  0.50 25.96 ? 389 ALA A N     1 
ATOM   6002  N  N     B ALA A 1 389 ? 10.866  1.958   35.645  0.50 25.99 ? 389 ALA A N     1 
ATOM   6003  C  CA    A ALA A 1 389 ? 12.287  2.268   35.511  0.50 31.27 ? 389 ALA A CA    1 
ATOM   6004  C  CA    B ALA A 1 389 ? 12.291  2.247   35.539  0.50 31.27 ? 389 ALA A CA    1 
ATOM   6005  C  C     A ALA A 1 389 ? 13.047  1.046   35.011  0.50 29.76 ? 389 ALA A C     1 
ATOM   6006  C  C     B ALA A 1 389 ? 13.050  1.073   34.933  0.50 29.78 ? 389 ALA A C     1 
ATOM   6007  O  O     A ALA A 1 389 ? 13.943  1.169   34.165  0.50 29.80 ? 389 ALA A O     1 
ATOM   6008  O  O     B ALA A 1 389 ? 13.921  1.264   34.075  0.50 29.72 ? 389 ALA A O     1 
ATOM   6009  C  CB    A ALA A 1 389 ? 12.890  2.788   36.817  0.50 29.78 ? 389 ALA A CB    1 
ATOM   6010  C  CB    B ALA A 1 389 ? 12.858  2.608   36.913  0.50 29.89 ? 389 ALA A CB    1 
ATOM   6011  N  N     A ARG A 1 390 ? 12.704  -0.141  35.520  0.50 26.70 ? 390 ARG A N     1 
ATOM   6012  N  N     B ARG A 1 390 ? 12.732  -0.151  35.364  0.50 26.54 ? 390 ARG A N     1 
ATOM   6013  C  CA    A ARG A 1 390 ? 13.355  -1.363  35.054  0.50 31.68 ? 390 ARG A CA    1 
ATOM   6014  C  CA    B ARG A 1 390 ? 13.400  -1.324  34.808  0.50 31.50 ? 390 ARG A CA    1 
ATOM   6015  C  C     A ARG A 1 390 ? 13.124  -1.573  33.565  0.50 33.68 ? 390 ARG A C     1 
ATOM   6016  C  C     B ARG A 1 390 ? 13.115  -1.462  33.320  0.50 33.58 ? 390 ARG A C     1 
ATOM   6017  O  O     A ARG A 1 390 ? 14.040  -1.966  32.834  0.50 29.75 ? 390 ARG A O     1 
ATOM   6018  O  O     B ARG A 1 390 ? 13.992  -1.857  32.543  0.50 30.19 ? 390 ARG A O     1 
ATOM   6019  C  CB    A ARG A 1 390 ? 12.846  -2.574  35.836  0.50 31.91 ? 390 ARG A CB    1 
ATOM   6020  C  CB    B ARG A 1 390 ? 12.962  -2.588  35.549  0.50 31.89 ? 390 ARG A CB    1 
ATOM   6021  C  CG    A ARG A 1 390 ? 13.439  -2.738  37.224  0.50 39.09 ? 390 ARG A CG    1 
ATOM   6022  C  CG    B ARG A 1 390 ? 13.404  -2.657  37.001  0.50 38.90 ? 390 ARG A CG    1 
ATOM   6023  C  CD    A ARG A 1 390 ? 13.328  -4.182  37.689  0.50 42.07 ? 390 ARG A CD    1 
ATOM   6024  C  CD    B ARG A 1 390 ? 13.263  -4.070  37.547  0.50 41.98 ? 390 ARG A CD    1 
ATOM   6025  N  NE    A ARG A 1 390 ? 11.977  -4.710  37.542  0.50 38.39 ? 390 ARG A NE    1 
ATOM   6026  N  NE    B ARG A 1 390 ? 11.924  -4.608  37.341  0.50 37.96 ? 390 ARG A NE    1 
ATOM   6027  C  CZ    A ARG A 1 390 ? 11.051  -4.686  38.493  0.50 37.63 ? 390 ARG A CZ    1 
ATOM   6028  C  CZ    B ARG A 1 390 ? 10.957  -4.590  38.249  0.50 37.81 ? 390 ARG A CZ    1 
ATOM   6029  N  NH1   A ARG A 1 390 ? 11.292  -4.156  39.680  0.50 37.78 ? 390 ARG A NH1   1 
ATOM   6030  N  NH1   B ARG A 1 390 ? 11.144  -4.067  39.449  0.50 37.20 ? 390 ARG A NH1   1 
ATOM   6031  N  NH2   A ARG A 1 390 ? 9.855   -5.214  38.247  0.50 34.96 ? 390 ARG A NH2   1 
ATOM   6032  N  NH2   B ARG A 1 390 ? 9.774   -5.119  37.947  0.50 34.89 ? 390 ARG A NH2   1 
ATOM   6033  N  N     A LEU A 1 391 ? 11.900  -1.319  33.101  0.50 30.09 ? 391 LEU A N     1 
ATOM   6034  N  N     B LEU A 1 391 ? 11.889  -1.143  32.908  0.50 29.85 ? 391 LEU A N     1 
ATOM   6035  C  CA    A LEU A 1 391 ? 11.590  -1.499  31.689  0.50 27.80 ? 391 LEU A CA    1 
ATOM   6036  C  CA    B LEU A 1 391 ? 11.527  -1.213  31.498  0.50 29.46 ? 391 LEU A CA    1 
ATOM   6037  C  C     A LEU A 1 391 ? 12.184  -0.374  30.849  0.50 31.36 ? 391 LEU A C     1 
ATOM   6038  C  C     B LEU A 1 391 ? 12.236  -0.126  30.697  0.50 31.00 ? 391 LEU A C     1 
ATOM   6039  O  O     A LEU A 1 391 ? 12.628  -0.606  29.718  0.50 29.92 ? 391 LEU A O     1 
ATOM   6040  O  O     B LEU A 1 391 ? 12.813  -0.399  29.638  0.50 30.39 ? 391 LEU A O     1 
ATOM   6041  C  CB    A LEU A 1 391 ? 10.074  -1.580  31.506  0.50 30.13 ? 391 LEU A CB    1 
ATOM   6042  C  CB    B LEU A 1 391 ? 10.009  -1.097  31.361  0.50 29.94 ? 391 LEU A CB    1 
ATOM   6043  C  CG    A LEU A 1 391 ? 9.514   -2.379  30.328  0.50 31.81 ? 391 LEU A CG    1 
ATOM   6044  C  CG    B LEU A 1 391 ? 9.317   -1.482  30.060  0.50 29.84 ? 391 LEU A CG    1 
ATOM   6045  C  CD1   A LEU A 1 391 ? 10.191  -3.732  30.227  0.50 26.88 ? 391 LEU A CD1   1 
ATOM   6046  C  CD1   B LEU A 1 391 ? 9.913   -2.754  29.482  0.50 28.01 ? 391 LEU A CD1   1 
ATOM   6047  C  CD2   A LEU A 1 391 ? 8.015   -2.550  30.482  0.50 25.56 ? 391 LEU A CD2   1 
ATOM   6048  C  CD2   B LEU A 1 391 ? 7.835   -1.672  30.353  0.50 31.31 ? 391 LEU A CD2   1 
ATOM   6049  N  N     A ASP A 1 392 ? 12.220  0.847   31.395  0.50 29.92 ? 392 ASP A N     1 
ATOM   6050  N  N     B ASP A 1 392 ? 12.208  1.115   31.197  0.50 29.86 ? 392 ASP A N     1 
ATOM   6051  C  CA    A ASP A 1 392 ? 12.688  1.998   30.629  0.50 28.07 ? 392 ASP A CA    1 
ATOM   6052  C  CA    B ASP A 1 392 ? 12.871  2.221   30.510  0.50 27.82 ? 392 ASP A CA    1 
ATOM   6053  C  C     A ASP A 1 392 ? 14.182  1.924   30.336  0.50 30.20 ? 392 ASP A C     1 
ATOM   6054  C  C     B ASP A 1 392 ? 14.364  1.963   30.351  0.50 30.36 ? 392 ASP A C     1 
ATOM   6055  O  O     A ASP A 1 392 ? 14.633  2.445   29.307  0.50 31.80 ? 392 ASP A O     1 
ATOM   6056  O  O     B ASP A 1 392 ? 14.964  2.337   29.335  0.50 31.16 ? 392 ASP A O     1 
ATOM   6057  C  CB    A ASP A 1 392 ? 12.354  3.297   31.368  0.50 25.61 ? 392 ASP A CB    1 
ATOM   6058  C  CB    B ASP A 1 392 ? 12.642  3.527   31.275  0.50 26.32 ? 392 ASP A CB    1 
ATOM   6059  C  CG    A ASP A 1 392 ? 10.943  3.787   31.083  0.50 31.91 ? 392 ASP A CG    1 
ATOM   6060  C  CG    B ASP A 1 392 ? 11.203  3.995   31.223  0.50 31.36 ? 392 ASP A CG    1 
ATOM   6061  O  OD1   A ASP A 1 392 ? 10.235  3.142   30.280  0.50 31.57 ? 392 ASP A OD1   1 
ATOM   6062  O  OD1   B ASP A 1 392 ? 10.495  3.661   30.250  0.50 32.62 ? 392 ASP A OD1   1 
ATOM   6063  O  OD2   A ASP A 1 392 ? 10.537  4.822   31.656  0.50 31.59 ? 392 ASP A OD2   1 
ATOM   6064  O  OD2   B ASP A 1 392 ? 10.779  4.711   32.155  0.50 30.62 ? 392 ASP A OD2   1 
ATOM   6065  N  N     A HIS A 1 393 ? 14.966  1.290   31.212  0.50 28.75 ? 393 HIS A N     1 
ATOM   6066  N  N     B HIS A 1 393 ? 14.980  1.327   31.351  0.50 28.74 ? 393 HIS A N     1 
ATOM   6067  C  CA    A HIS A 1 393 ? 16.397  1.181   30.946  0.50 27.79 ? 393 HIS A CA    1 
ATOM   6068  C  CA    B HIS A 1 393 ? 16.415  1.069   31.309  0.50 27.04 ? 393 HIS A CA    1 
ATOM   6069  C  C     A HIS A 1 393 ? 16.699  0.088   29.927  0.50 29.61 ? 393 HIS A C     1 
ATOM   6070  C  C     B HIS A 1 393 ? 16.780  0.170   30.133  0.50 29.45 ? 393 HIS A C     1 
ATOM   6071  O  O     A HIS A 1 393 ? 17.606  0.248   29.100  0.50 27.92 ? 393 HIS A O     1 
ATOM   6072  O  O     B HIS A 1 393 ? 17.723  0.460   29.383  0.50 27.30 ? 393 HIS A O     1 
ATOM   6073  C  CB    A HIS A 1 393 ? 17.176  0.923   32.234  0.50 27.75 ? 393 HIS A CB    1 
ATOM   6074  C  CB    B HIS A 1 393 ? 16.860  0.446   32.632  0.50 27.06 ? 393 HIS A CB    1 
ATOM   6075  C  CG    A HIS A 1 393 ? 18.657  0.841   32.025  0.50 31.51 ? 393 HIS A CG    1 
ATOM   6076  C  CG    B HIS A 1 393 ? 18.333  0.202   32.722  0.50 32.28 ? 393 HIS A CG    1 
ATOM   6077  N  ND1   A HIS A 1 393 ? 19.406  1.913   31.589  0.50 28.76 ? 393 HIS A ND1   1 
ATOM   6078  N  ND1   B HIS A 1 393 ? 19.238  1.204   33.000  0.50 33.97 ? 393 HIS A ND1   1 
ATOM   6079  C  CD2   A HIS A 1 393 ? 19.524  -0.189  32.170  0.50 29.27 ? 393 HIS A CD2   1 
ATOM   6080  C  CD2   B HIS A 1 393 ? 19.059  -0.931  32.574  0.50 32.72 ? 393 HIS A CD2   1 
ATOM   6081  C  CE1   A HIS A 1 393 ? 20.673  1.552   31.488  0.50 25.19 ? 393 HIS A CE1   1 
ATOM   6082  C  CE1   B HIS A 1 393 ? 20.458  0.698   33.020  0.50 28.12 ? 393 HIS A CE1   1 
ATOM   6083  N  NE2   A HIS A 1 393 ? 20.771  0.280   31.832  0.50 29.35 ? 393 HIS A NE2   1 
ATOM   6084  N  NE2   B HIS A 1 393 ? 20.377  -0.595  32.765  0.50 30.34 ? 393 HIS A NE2   1 
ATOM   6085  N  N     A LYS A 1 394 ? 15.972  -1.035  29.985  0.50 28.71 ? 394 LYS A N     1 
ATOM   6086  N  N     B LYS A 1 394 ? 16.042  -0.933  29.956  0.50 28.77 ? 394 LYS A N     1 
ATOM   6087  C  CA    A LYS A 1 394 ? 16.105  -2.051  28.945  0.50 29.51 ? 394 LYS A CA    1 
ATOM   6088  C  CA    B LYS A 1 394 ? 16.300  -1.820  28.826  0.50 29.75 ? 394 LYS A CA    1 
ATOM   6089  C  C     A LYS A 1 394 ? 15.814  -1.458  27.574  0.50 28.87 ? 394 LYS A C     1 
ATOM   6090  C  C     B LYS A 1 394 ? 16.015  -1.120  27.503  0.50 28.11 ? 394 LYS A C     1 
ATOM   6091  O  O     A LYS A 1 394 ? 16.455  -1.819  26.583  0.50 26.60 ? 394 LYS A O     1 
ATOM   6092  O  O     B LYS A 1 394 ? 16.756  -1.295  26.531  0.50 26.74 ? 394 LYS A O     1 
ATOM   6093  C  CB    A LYS A 1 394 ? 15.176  -3.235  29.224  0.50 25.10 ? 394 LYS A CB    1 
ATOM   6094  C  CB    B LYS A 1 394 ? 15.470  -3.099  28.950  0.50 26.90 ? 394 LYS A CB    1 
ATOM   6095  C  CG    A LYS A 1 394 ? 15.577  -4.090  30.418  0.50 30.90 ? 394 LYS A CG    1 
ATOM   6096  C  CG    B LYS A 1 394 ? 15.906  -4.016  30.082  0.50 29.36 ? 394 LYS A CG    1 
ATOM   6097  C  CD    A LYS A 1 394 ? 14.562  -5.204  30.667  0.50 32.96 ? 394 LYS A CD    1 
ATOM   6098  C  CD    B LYS A 1 394 ? 15.255  -5.386  29.978  0.50 31.55 ? 394 LYS A CD    1 
ATOM   6099  C  CE    A LYS A 1 394 ? 14.892  -5.990  31.928  0.50 36.05 ? 394 LYS A CE    1 
ATOM   6100  C  CE    B LYS A 1 394 ? 15.658  -6.280  31.142  0.50 36.36 ? 394 LYS A CE    1 
ATOM   6101  N  NZ    A LYS A 1 394 ? 13.935  -7.110  32.157  0.50 39.49 ? 394 LYS A NZ    1 
ATOM   6102  N  NZ    B LYS A 1 394 ? 15.060  -7.644  31.041  0.50 36.56 ? 394 LYS A NZ    1 
ATOM   6103  N  N     A PHE A 1 395 ? 14.845  -0.542  27.504  0.50 29.04 ? 395 PHE A N     1 
ATOM   6104  N  N     B PHE A 1 395 ? 14.946  -0.318  27.453  0.50 28.61 ? 395 PHE A N     1 
ATOM   6105  C  CA    A PHE A 1 395 ? 14.628  0.232   26.287  0.50 24.73 ? 395 PHE A CA    1 
ATOM   6106  C  CA    B PHE A 1 395 ? 14.637  0.459   26.255  0.50 24.89 ? 395 PHE A CA    1 
ATOM   6107  C  C     A PHE A 1 395 ? 15.866  1.052   25.942  0.50 30.74 ? 395 PHE A C     1 
ATOM   6108  C  C     B PHE A 1 395 ? 15.817  1.337   25.854  0.50 30.54 ? 395 PHE A C     1 
ATOM   6109  O  O     A PHE A 1 395 ? 16.307  1.080   24.786  0.50 28.28 ? 395 PHE A O     1 
ATOM   6110  O  O     B PHE A 1 395 ? 16.286  1.286   24.710  0.50 28.47 ? 395 PHE A O     1 
ATOM   6111  C  CB    A PHE A 1 395 ? 13.401  1.133   26.474  0.50 27.40 ? 395 PHE A CB    1 
ATOM   6112  C  CB    B PHE A 1 395 ? 13.383  1.307   26.510  0.50 27.59 ? 395 PHE A CB    1 
ATOM   6113  C  CG    A PHE A 1 395 ? 13.028  1.939   25.259  0.50 25.53 ? 395 PHE A CG    1 
ATOM   6114  C  CG    B PHE A 1 395 ? 12.962  2.175   25.345  0.50 25.32 ? 395 PHE A CG    1 
ATOM   6115  C  CD1   A PHE A 1 395 ? 13.621  3.165   25.011  0.50 24.89 ? 395 PHE A CD1   1 
ATOM   6116  C  CD1   B PHE A 1 395 ? 13.632  3.353   25.050  0.50 25.06 ? 395 PHE A CD1   1 
ATOM   6117  C  CD2   A PHE A 1 395 ? 12.057  1.485   24.385  0.50 27.36 ? 395 PHE A CD2   1 
ATOM   6118  C  CD2   B PHE A 1 395 ? 11.860  1.836   24.581  0.50 26.68 ? 395 PHE A CD2   1 
ATOM   6119  C  CE1   A PHE A 1 395 ? 13.272  3.912   23.903  0.50 28.41 ? 395 PHE A CE1   1 
ATOM   6120  C  CE1   B PHE A 1 395 ? 13.237  4.153   23.994  0.50 28.44 ? 395 PHE A CE1   1 
ATOM   6121  C  CE2   A PHE A 1 395 ? 11.701  2.229   23.270  0.50 29.95 ? 395 PHE A CE2   1 
ATOM   6122  C  CE2   B PHE A 1 395 ? 11.456  2.637   23.522  0.50 30.02 ? 395 PHE A CE2   1 
ATOM   6123  C  CZ    A PHE A 1 395 ? 12.308  3.446   23.033  0.50 30.48 ? 395 PHE A CZ    1 
ATOM   6124  C  CZ    B PHE A 1 395 ? 12.146  3.798   23.231  0.50 28.57 ? 395 PHE A CZ    1 
ATOM   6125  N  N     A ASP A 1 396 ? 16.458  1.706   26.949  0.50 26.12 ? 396 ASP A N     1 
ATOM   6126  N  N     B ASP A 1 396 ? 16.314  2.148   26.794  0.50 26.59 ? 396 ASP A N     1 
ATOM   6127  C  CA    A ASP A 1 396 ? 17.567  2.623   26.702  0.50 28.44 ? 396 ASP A CA    1 
ATOM   6128  C  CA    B ASP A 1 396 ? 17.348  3.125   26.474  0.50 26.43 ? 396 ASP A CA    1 
ATOM   6129  C  C     A ASP A 1 396 ? 18.804  1.893   26.196  0.50 25.98 ? 396 ASP A C     1 
ATOM   6130  C  C     B ASP A 1 396 ? 18.621  2.452   25.971  0.50 27.84 ? 396 ASP A C     1 
ATOM   6131  O  O     A ASP A 1 396 ? 19.548  2.433   25.368  0.50 26.15 ? 396 ASP A O     1 
ATOM   6132  O  O     B ASP A 1 396 ? 19.269  2.959   25.050  0.50 21.77 ? 396 ASP A O     1 
ATOM   6133  C  CB    A ASP A 1 396 ? 17.904  3.404   27.973  0.50 26.47 ? 396 ASP A CB    1 
ATOM   6134  C  CB    B ASP A 1 396 ? 17.650  3.992   27.696  0.50 25.18 ? 396 ASP A CB    1 
ATOM   6135  C  CG    A ASP A 1 396 ? 16.821  4.384   28.363  0.50 28.95 ? 396 ASP A CG    1 
ATOM   6136  C  CG    B ASP A 1 396 ? 16.528  4.965   28.017  0.50 27.33 ? 396 ASP A CG    1 
ATOM   6137  O  OD1   A ASP A 1 396 ? 16.022  4.772   27.488  0.50 25.84 ? 396 ASP A OD1   1 
ATOM   6138  O  OD1   B ASP A 1 396 ? 15.580  5.072   27.215  0.50 26.39 ? 396 ASP A OD1   1 
ATOM   6139  O  OD2   A ASP A 1 396 ? 16.774  4.772   29.547  0.50 24.31 ? 396 ASP A OD2   1 
ATOM   6140  O  OD2   B ASP A 1 396 ? 16.593  5.627   29.073  0.50 23.06 ? 396 ASP A OD2   1 
ATOM   6141  N  N     A LEU A 1 397 ? 19.048  0.674   26.686  0.50 24.32 ? 397 LEU A N     1 
ATOM   6142  N  N     B LEU A 1 397 ? 18.991  1.310   26.563  0.50 23.40 ? 397 LEU A N     1 
ATOM   6143  C  CA    A LEU A 1 397 ? 20.249  -0.056  26.280  0.50 30.19 ? 397 LEU A CA    1 
ATOM   6144  C  CA    B LEU A 1 397 ? 20.208  0.611   26.152  0.50 30.05 ? 397 LEU A CA    1 
ATOM   6145  C  C     A LEU A 1 397 ? 20.254  -0.332  24.781  0.50 27.61 ? 397 LEU A C     1 
ATOM   6146  C  C     B LEU A 1 397 ? 20.167  0.246   24.673  0.50 28.32 ? 397 LEU A C     1 
ATOM   6147  O  O     A LEU A 1 397 ? 21.305  -0.257  24.134  0.50 25.51 ? 397 LEU A O     1 
ATOM   6148  O  O     B LEU A 1 397 ? 21.080  0.589   23.911  0.50 26.24 ? 397 LEU A O     1 
ATOM   6149  C  CB    A LEU A 1 397 ? 20.369  -1.363  27.066  0.50 29.37 ? 397 LEU A CB    1 
ATOM   6150  C  CB    B LEU A 1 397 ? 20.408  -0.649  26.996  0.50 30.26 ? 397 LEU A CB    1 
ATOM   6151  C  CG    A LEU A 1 397 ? 20.791  -1.256  28.533  0.50 27.55 ? 397 LEU A CG    1 
ATOM   6152  C  CG    B LEU A 1 397 ? 21.036  -0.549  28.384  0.50 30.17 ? 397 LEU A CG    1 
ATOM   6153  C  CD1   A LEU A 1 397 ? 20.796  -2.623  29.196  0.50 27.73 ? 397 LEU A CD1   1 
ATOM   6154  C  CD1   B LEU A 1 397 ? 21.094  -1.930  29.014  0.50 26.72 ? 397 LEU A CD1   1 
ATOM   6155  C  CD2   A LEU A 1 397 ? 22.155  -0.595  28.656  0.50 32.09 ? 397 LEU A CD2   1 
ATOM   6156  C  CD2   B LEU A 1 397 ? 22.425  0.066   28.310  0.50 34.66 ? 397 LEU A CD2   1 
ATOM   6157  N  N     A MET A 1 398 ? 19.089  -0.646  24.209  0.50 28.48 ? 398 MET A N     1 
ATOM   6158  N  N     B MET A 1 398 ? 19.117  -0.465  24.251  0.50 28.62 ? 398 MET A N     1 
ATOM   6159  C  CA    A MET A 1 398 ? 18.995  -0.917  22.778  0.50 24.98 ? 398 MET A CA    1 
ATOM   6160  C  CA    B MET A 1 398 ? 19.005  -0.848  22.847  0.50 24.97 ? 398 MET A CA    1 
ATOM   6161  C  C     A MET A 1 398 ? 18.794  0.345   21.951  0.50 28.06 ? 398 MET A C     1 
ATOM   6162  C  C     B MET A 1 398 ? 18.802  0.370   21.958  0.50 28.06 ? 398 MET A C     1 
ATOM   6163  O  O     A MET A 1 398 ? 19.365  0.466   20.862  0.50 24.02 ? 398 MET A O     1 
ATOM   6164  O  O     B MET A 1 398 ? 19.329  0.424   20.840  0.50 24.00 ? 398 MET A O     1 
ATOM   6165  C  CB    A MET A 1 398 ? 17.845  -1.885  22.488  0.50 27.36 ? 398 MET A CB    1 
ATOM   6166  C  CB    B MET A 1 398 ? 17.862  -1.843  22.656  0.50 27.68 ? 398 MET A CB    1 
ATOM   6167  C  CG    A MET A 1 398 ? 18.009  -3.268  23.076  0.50 28.38 ? 398 MET A CG    1 
ATOM   6168  C  CG    B MET A 1 398 ? 18.028  -3.133  23.430  0.50 28.77 ? 398 MET A CG    1 
ATOM   6169  S  SD    A MET A 1 398 ? 16.839  -4.416  22.334  0.50 27.86 ? 398 MET A SD    1 
ATOM   6170  S  SD    B MET A 1 398 ? 16.686  -4.290  23.130  0.50 33.33 ? 398 MET A SD    1 
ATOM   6171  C  CE    A MET A 1 398 ? 15.283  -3.609  22.712  0.50 23.12 ? 398 MET A CE    1 
ATOM   6172  C  CE    B MET A 1 398 ? 15.283  -3.361  23.748  0.50 25.11 ? 398 MET A CE    1 
ATOM   6173  N  N     A TYR A 1 399 ? 17.987  1.285   22.445  0.50 25.83 ? 399 TYR A N     1 
ATOM   6174  N  N     B TYR A 1 399 ? 18.045  1.358   22.434  0.50 25.82 ? 399 TYR A N     1 
ATOM   6175  C  CA    A TYR A 1 399 ? 17.557  2.400   21.607  0.50 25.48 ? 399 TYR A CA    1 
ATOM   6176  C  CA    B TYR A 1 399 ? 17.794  2.530   21.607  0.50 25.21 ? 399 TYR A CA    1 
ATOM   6177  C  C     A TYR A 1 399 ? 18.699  3.356   21.291  0.50 27.02 ? 399 TYR A C     1 
ATOM   6178  C  C     B TYR A 1 399 ? 19.005  3.451   21.541  0.50 26.49 ? 399 TYR A C     1 
ATOM   6179  O  O     A TYR A 1 399 ? 18.702  3.978   20.222  0.50 27.47 ? 399 TYR A O     1 
ATOM   6180  O  O     B TYR A 1 399 ? 19.160  4.188   20.561  0.50 26.66 ? 399 TYR A O     1 
ATOM   6181  C  CB    A TYR A 1 399 ? 16.412  3.154   22.280  0.50 25.02 ? 399 TYR A CB    1 
ATOM   6182  C  CB    B TYR A 1 399 ? 16.574  3.298   22.115  0.50 25.60 ? 399 TYR A CB    1 
ATOM   6183  C  CG    A TYR A 1 399 ? 15.934  4.334   21.475  0.50 28.43 ? 399 TYR A CG    1 
ATOM   6184  C  CG    B TYR A 1 399 ? 16.071  4.286   21.094  0.50 29.87 ? 399 TYR A CG    1 
ATOM   6185  C  CD1   A TYR A 1 399 ? 15.259  4.149   20.276  0.50 27.75 ? 399 TYR A CD1   1 
ATOM   6186  C  CD1   B TYR A 1 399 ? 15.520  3.847   19.898  0.50 28.40 ? 399 TYR A CD1   1 
ATOM   6187  C  CD2   A TYR A 1 399 ? 16.169  5.633   21.904  0.50 28.22 ? 399 TYR A CD2   1 
ATOM   6188  C  CD2   B TYR A 1 399 ? 16.170  5.654   21.310  0.50 29.59 ? 399 TYR A CD2   1 
ATOM   6189  C  CE1   A TYR A 1 399 ? 14.827  5.226   19.530  0.50 29.42 ? 399 TYR A CE1   1 
ATOM   6190  C  CE1   B TYR A 1 399 ? 15.074  4.740   18.948  0.50 25.87 ? 399 TYR A CE1   1 
ATOM   6191  C  CE2   A TYR A 1 399 ? 15.735  6.717   21.167  0.50 29.10 ? 399 TYR A CE2   1 
ATOM   6192  C  CE2   B TYR A 1 399 ? 15.719  6.556   20.367  0.50 31.57 ? 399 TYR A CE2   1 
ATOM   6193  C  CZ    A TYR A 1 399 ? 15.064  6.507   19.981  0.50 31.30 ? 399 TYR A CZ    1 
ATOM   6194  C  CZ    B TYR A 1 399 ? 15.173  6.092   19.188  0.50 31.58 ? 399 TYR A CZ    1 
ATOM   6195  O  OH    A TYR A 1 399 ? 14.631  7.581   19.240  0.50 35.49 ? 399 TYR A OH    1 
ATOM   6196  O  OH    B TYR A 1 399 ? 14.725  6.984   18.243  0.50 33.72 ? 399 TYR A OH    1 
ATOM   6197  N  N     A ALA A 1 400 ? 19.666  3.492   22.200  0.50 25.71 ? 400 ALA A N     1 
ATOM   6198  N  N     B ALA A 1 400 ? 19.872  3.420   22.558  0.50 25.77 ? 400 ALA A N     1 
ATOM   6199  C  CA    A ALA A 1 400 ? 20.823  4.336   21.922  0.50 24.70 ? 400 ALA A CA    1 
ATOM   6200  C  CA    B ALA A 1 400 ? 21.111  4.190   22.491  0.50 21.53 ? 400 ALA A CA    1 
ATOM   6201  C  C     A ALA A 1 400 ? 21.542  3.901   20.650  0.50 26.41 ? 400 ALA A C     1 
ATOM   6202  C  C     B ALA A 1 400 ? 21.972  3.759   21.312  0.50 28.05 ? 400 ALA A C     1 
ATOM   6203  O  O     A ALA A 1 400 ? 22.072  4.745   19.919  0.50 23.40 ? 400 ALA A O     1 
ATOM   6204  O  O     B ALA A 1 400 ? 22.711  4.576   20.755  0.50 19.17 ? 400 ALA A O     1 
ATOM   6205  C  CB    A ALA A 1 400 ? 21.783  4.316   23.111  0.50 24.94 ? 400 ALA A CB    1 
ATOM   6206  C  CB    B ALA A 1 400 ? 21.897  4.055   23.795  0.50 24.94 ? 400 ALA A CB    1 
ATOM   6207  N  N     A LYS A 1 401 ? 21.559  2.599   20.362  0.50 24.08 ? 401 LYS A N     1 
ATOM   6208  N  N     B LYS A 1 401 ? 21.890  2.488   20.922  0.50 24.84 ? 401 LYS A N     1 
ATOM   6209  C  CA    A LYS A 1 401 ? 22.188  2.065   19.160  0.50 27.53 ? 401 LYS A CA    1 
ATOM   6210  C  CA    B LYS A 1 401 ? 22.575  1.965   19.748  0.50 26.67 ? 401 LYS A CA    1 
ATOM   6211  C  C     A LYS A 1 401 ? 21.246  1.995   17.963  0.50 28.94 ? 401 LYS A C     1 
ATOM   6212  C  C     B LYS A 1 401 ? 21.663  1.865   18.533  0.50 28.80 ? 401 LYS A C     1 
ATOM   6213  O  O     A LYS A 1 401 ? 21.697  1.647   16.863  0.50 27.40 ? 401 LYS A O     1 
ATOM   6214  O  O     B LYS A 1 401 ? 22.121  1.437   17.466  0.50 33.13 ? 401 LYS A O     1 
ATOM   6215  C  CB    A LYS A 1 401 ? 22.747  0.661   19.434  0.50 26.76 ? 401 LYS A CB    1 
ATOM   6216  C  CB    B LYS A 1 401 ? 23.168  0.584   20.052  0.50 27.88 ? 401 LYS A CB    1 
ATOM   6217  C  CG    A LYS A 1 401 ? 24.157  0.621   20.005  0.50 33.98 ? 401 LYS A CG    1 
ATOM   6218  C  CG    B LYS A 1 401 ? 24.615  0.591   20.521  0.50 33.76 ? 401 LYS A CG    1 
ATOM   6219  C  CD    A LYS A 1 401 ? 24.220  1.156   21.422  0.50 33.77 ? 401 LYS A CD    1 
ATOM   6220  C  CD    B LYS A 1 401 ? 24.778  1.384   21.800  0.50 37.91 ? 401 LYS A CD    1 
ATOM   6221  C  CE    A LYS A 1 401 ? 25.650  1.134   21.953  0.50 33.99 ? 401 LYS A CE    1 
ATOM   6222  C  CE    B LYS A 1 401 ? 26.125  1.126   22.449  0.50 33.16 ? 401 LYS A CE    1 
ATOM   6223  N  NZ    A LYS A 1 401 ? 25.777  1.857   23.255  0.50 28.32 ? 401 LYS A NZ    1 
ATOM   6224  N  NZ    B LYS A 1 401 ? 26.303  1.979   23.655  0.50 31.85 ? 401 LYS A NZ    1 
ATOM   6225  N  N     A ARG A 1 402 ? 19.962  2.310   18.152  0.50 24.86 ? 402 ARG A N     1 
ATOM   6226  N  N     B ARG A 1 402 ? 20.389  2.239   18.675  0.50 25.78 ? 402 ARG A N     1 
ATOM   6227  C  CA    A ARG A 1 402 ? 18.926  2.147   17.127  0.50 22.85 ? 402 ARG A CA    1 
ATOM   6228  C  CA    B ARG A 1 402 ? 19.381  2.107   17.621  0.50 22.88 ? 402 ARG A CA    1 
ATOM   6229  C  C     A ARG A 1 402 ? 18.764  0.686   16.712  0.50 24.62 ? 402 ARG A C     1 
ATOM   6230  C  C     B ARG A 1 402 ? 19.209  0.654   17.184  0.50 24.05 ? 402 ARG A C     1 
ATOM   6231  O  O     A ARG A 1 402 ? 18.431  0.388   15.561  0.50 29.43 ? 402 ARG A O     1 
ATOM   6232  O  O     B ARG A 1 402 ? 18.881  0.375   16.027  0.50 29.26 ? 402 ARG A O     1 
ATOM   6233  C  CB    A ARG A 1 402 ? 19.197  3.019   15.896  0.50 26.43 ? 402 ARG A CB    1 
ATOM   6234  C  CB    B ARG A 1 402 ? 19.709  2.996   16.418  0.50 27.41 ? 402 ARG A CB    1 
ATOM   6235  C  CG    A ARG A 1 402 ? 19.084  4.513   16.136  0.50 27.43 ? 402 ARG A CG    1 
ATOM   6236  C  CG    B ARG A 1 402 ? 19.891  4.466   16.758  0.50 27.47 ? 402 ARG A CG    1 
ATOM   6237  C  CD    A ARG A 1 402 ? 17.743  4.877   16.754  0.50 34.27 ? 402 ARG A CD    1 
ATOM   6238  C  CD    B ARG A 1 402 ? 18.619  5.073   17.335  0.50 32.84 ? 402 ARG A CD    1 
ATOM   6239  N  NE    A ARG A 1 402 ? 17.482  6.310   16.681  0.50 35.72 ? 402 ARG A NE    1 
ATOM   6240  N  NE    B ARG A 1 402 ? 18.640  6.529   17.255  0.50 35.65 ? 402 ARG A NE    1 
ATOM   6241  C  CZ    A ARG A 1 402 ? 17.941  7.201   17.548  0.50 34.22 ? 402 ARG A CZ    1 
ATOM   6242  C  CZ    B ARG A 1 402 ? 18.951  7.337   18.260  0.50 36.75 ? 402 ARG A CZ    1 
ATOM   6243  N  NH1   A ARG A 1 402 ? 18.702  6.844   18.569  0.50 38.74 ? 402 ARG A NH1   1 
ATOM   6244  N  NH1   B ARG A 1 402 ? 19.232  6.866   19.467  0.50 36.36 ? 402 ARG A NH1   1 
ATOM   6245  N  NH2   A ARG A 1 402 ? 17.629  8.484   17.386  0.50 39.69 ? 402 ARG A NH2   1 
ATOM   6246  N  NH2   B ARG A 1 402 ? 18.976  8.650   18.052  0.50 26.30 ? 402 ARG A NH2   1 
ATOM   6247  N  N     A ALA A 1 403 ? 18.991  -0.240  17.642  0.50 22.22 ? 403 ALA A N     1 
ATOM   6248  N  N     B ALA A 1 403 ? 19.421  -0.283  18.107  0.50 19.55 ? 403 ALA A N     1 
ATOM   6249  C  CA    A ALA A 1 403 ? 18.883  -1.656  17.322  0.50 24.45 ? 403 ALA A CA    1 
ATOM   6250  C  CA    B ALA A 1 403 ? 19.326  -1.697  17.777  0.50 23.34 ? 403 ALA A CA    1 
ATOM   6251  C  C     A ALA A 1 403 ? 17.428  -2.043  17.076  0.50 26.23 ? 403 ALA A C     1 
ATOM   6252  C  C     B ALA A 1 403 ? 17.875  -2.101  17.543  0.50 25.00 ? 403 ALA A C     1 
ATOM   6253  O  O     A ALA A 1 403 ? 16.537  -1.693  17.860  0.50 23.09 ? 403 ALA A O     1 
ATOM   6254  O  O     B ALA A 1 403 ? 16.993  -1.788  18.352  0.50 21.24 ? 403 ALA A O     1 
ATOM   6255  C  CB    A ALA A 1 403 ? 19.479  -2.503  18.446  0.50 25.77 ? 403 ALA A CB    1 
ATOM   6256  C  CB    B ALA A 1 403 ? 19.936  -2.545  18.892  0.50 25.01 ? 403 ALA A CB    1 
ATOM   6257  N  N     A PHE A 1 404 ? 17.194  -2.764  15.975  0.50 22.31 ? 404 PHE A N     1 
ATOM   6258  N  N     B PHE A 1 404 ? 17.636  -2.806  16.434  0.50 20.77 ? 404 PHE A N     1 
ATOM   6259  C  CA    A PHE A 1 404 ? 15.912  -3.330  15.556  0.50 25.16 ? 404 PHE A CA    1 
ATOM   6260  C  CA    B PHE A 1 404 ? 16.339  -3.328  16.001  0.50 23.79 ? 404 PHE A CA    1 
ATOM   6261  C  C     A PHE A 1 404 ? 14.916  -2.286  15.060  0.50 24.18 ? 404 PHE A C     1 
ATOM   6262  C  C     B PHE A 1 404 ? 15.359  -2.242  15.568  0.50 24.16 ? 404 PHE A C     1 
ATOM   6263  O  O     A PHE A 1 404 ? 13.790  -2.653  14.706  0.50 22.44 ? 404 PHE A O     1 
ATOM   6264  O  O     B PHE A 1 404 ? 14.225  -2.570  15.194  0.50 23.66 ? 404 PHE A O     1 
ATOM   6265  C  CB    A PHE A 1 404 ? 15.242  -4.154  16.671  0.50 18.68 ? 404 PHE A CB    1 
ATOM   6266  C  CB    B PHE A 1 404 ? 15.656  -4.188  17.079  0.50 19.53 ? 404 PHE A CB    1 
ATOM   6267  C  CG    A PHE A 1 404 ? 16.110  -5.251  17.218  0.50 18.55 ? 404 PHE A CG    1 
ATOM   6268  C  CG    B PHE A 1 404 ? 16.517  -5.306  17.601  0.50 18.81 ? 404 PHE A CG    1 
ATOM   6269  C  CD1   A PHE A 1 404 ? 16.235  -6.452  16.544  0.50 18.83 ? 404 PHE A CD1   1 
ATOM   6270  C  CD1   B PHE A 1 404 ? 16.598  -6.509  16.923  0.50 19.92 ? 404 PHE A CD1   1 
ATOM   6271  C  CD2   A PHE A 1 404 ? 16.807  -5.077  18.403  0.50 21.00 ? 404 PHE A CD2   1 
ATOM   6272  C  CD2   B PHE A 1 404 ? 17.236  -5.154  18.775  0.50 21.16 ? 404 PHE A CD2   1 
ATOM   6273  C  CE1   A PHE A 1 404 ? 17.041  -7.463  17.040  0.50 24.74 ? 404 PHE A CE1   1 
ATOM   6274  C  CE1   B PHE A 1 404 ? 17.392  -7.541  17.399  0.50 23.74 ? 404 PHE A CE1   1 
ATOM   6275  C  CE2   A PHE A 1 404 ? 17.604  -6.086  18.912  0.50 21.90 ? 404 PHE A CE2   1 
ATOM   6276  C  CE2   B PHE A 1 404 ? 18.024  -6.182  19.263  0.50 21.42 ? 404 PHE A CE2   1 
ATOM   6277  C  CZ    A PHE A 1 404 ? 17.721  -7.282  18.229  0.50 23.04 ? 404 PHE A CZ    1 
ATOM   6278  C  CZ    B PHE A 1 404 ? 18.103  -7.378  18.571  0.50 23.91 ? 404 PHE A CZ    1 
ATOM   6279  N  N     A VAL A 1 405 ? 15.294  -1.008  14.996  0.50 24.17 ? 405 VAL A N     1 
ATOM   6280  N  N     B VAL A 1 405 ? 15.746  -0.965  15.605  0.50 21.76 ? 405 VAL A N     1 
ATOM   6281  C  CA    A VAL A 1 405 ? 14.325  0.048   14.710  0.50 26.59 ? 405 VAL A CA    1 
ATOM   6282  C  CA    B VAL A 1 405 ? 14.820  0.110   15.255  0.50 27.50 ? 405 VAL A CA    1 
ATOM   6283  C  C     A VAL A 1 405 ? 13.817  -0.045  13.273  0.50 25.44 ? 405 VAL A C     1 
ATOM   6284  C  C     B VAL A 1 405 ? 14.343  -0.019  13.813  0.50 26.40 ? 405 VAL A C     1 
ATOM   6285  O  O     A VAL A 1 405 ? 12.648  0.250   12.995  0.50 21.24 ? 405 VAL A O     1 
ATOM   6286  O  O     B VAL A 1 405 ? 13.204  0.348   13.491  0.50 25.60 ? 405 VAL A O     1 
ATOM   6287  C  CB    A VAL A 1 405 ? 14.946  1.425   15.011  0.50 24.28 ? 405 VAL A CB    1 
ATOM   6288  C  CB    B VAL A 1 405 ? 15.481  1.479   15.524  0.50 24.63 ? 405 VAL A CB    1 
ATOM   6289  C  CG1   A VAL A 1 405 ? 14.026  2.548   14.550  0.50 31.23 ? 405 VAL A CG1   1 
ATOM   6290  C  CG1   B VAL A 1 405 ? 14.687  2.611   14.886  0.50 29.56 ? 405 VAL A CG1   1 
ATOM   6291  C  CG2   A VAL A 1 405 ? 15.225  1.557   16.503  0.50 27.86 ? 405 VAL A CG2   1 
ATOM   6292  C  CG2   B VAL A 1 405 ? 15.604  1.717   17.027  0.50 25.49 ? 405 VAL A CG2   1 
ATOM   6293  N  N     A HIS A 1 406 ? 14.678  -0.452  12.337  0.50 24.41 ? 406 HIS A N     1 
ATOM   6294  N  N     B HIS A 1 406 ? 15.179  -0.573  12.932  0.50 27.59 ? 406 HIS A N     1 
ATOM   6295  C  CA    A HIS A 1 406 ? 14.253  -0.533  10.944  0.50 21.44 ? 406 HIS A CA    1 
ATOM   6296  C  CA    B HIS A 1 406 ? 14.863  -0.564  11.507  0.50 24.91 ? 406 HIS A CA    1 
ATOM   6297  C  C     A HIS A 1 406 ? 13.087  -1.501  10.774  0.50 27.09 ? 406 HIS A C     1 
ATOM   6298  C  C     B HIS A 1 406 ? 13.639  -1.415  11.177  0.50 26.92 ? 406 HIS A C     1 
ATOM   6299  O  O     A HIS A 1 406 ? 12.301  -1.365  9.829   0.50 27.01 ? 406 HIS A O     1 
ATOM   6300  O  O     B HIS A 1 406 ? 12.926  -1.108  10.214  0.50 24.12 ? 406 HIS A O     1 
ATOM   6301  C  CB    A HIS A 1 406 ? 15.430  -0.935  10.051  0.50 27.02 ? 406 HIS A CB    1 
ATOM   6302  C  CB    B HIS A 1 406 ? 16.078  -1.026  10.696  0.50 23.17 ? 406 HIS A CB    1 
ATOM   6303  C  CG    A HIS A 1 406 ? 15.876  -2.351  10.240  0.50 26.56 ? 406 HIS A CG    1 
ATOM   6304  C  CG    B HIS A 1 406 ? 16.356  -2.493  10.800  0.50 28.06 ? 406 HIS A CG    1 
ATOM   6305  N  ND1   A HIS A 1 406 ? 16.499  -2.787  11.389  0.50 27.13 ? 406 HIS A ND1   1 
ATOM   6306  N  ND1   B HIS A 1 406 ? 17.030  -3.052  11.865  0.50 21.20 ? 406 HIS A ND1   1 
ATOM   6307  C  CD2   A HIS A 1 406 ? 15.779  -3.432  9.431   0.50 23.92 ? 406 HIS A CD2   1 
ATOM   6308  C  CD2   B HIS A 1 406 ? 16.052  -3.518  9.969   0.50 24.27 ? 406 HIS A CD2   1 
ATOM   6309  C  CE1   A HIS A 1 406 ? 16.769  -4.075  11.279  0.50 24.21 ? 406 HIS A CE1   1 
ATOM   6310  C  CE1   B HIS A 1 406 ? 17.121  -4.358  11.690  0.50 24.42 ? 406 HIS A CE1   1 
ATOM   6311  N  NE2   A HIS A 1 406 ? 16.346  -4.491  10.099  0.50 26.07 ? 406 HIS A NE2   1 
ATOM   6312  N  NE2   B HIS A 1 406 ? 16.541  -4.666  10.543  0.50 24.96 ? 406 HIS A NE2   1 
ATOM   6313  N  N     A TRP A 1 407 ? 12.947  -2.472  11.686  0.50 22.82 ? 407 TRP A N     1 
ATOM   6314  N  N     B TRP A 1 407 ? 13.369  -2.476  11.953  0.50 23.58 ? 407 TRP A N     1 
ATOM   6315  C  CA    A TRP A 1 407 ? 11.818  -3.398  11.627  0.50 26.04 ? 407 TRP A CA    1 
ATOM   6316  C  CA    B TRP A 1 407 ? 12.176  -3.281  11.692  0.50 25.09 ? 407 TRP A CA    1 
ATOM   6317  C  C     A TRP A 1 407 ? 10.487  -2.681  11.795  0.50 25.80 ? 407 TRP A C     1 
ATOM   6318  C  C     B TRP A 1 407 ? 10.898  -2.491  11.954  0.50 26.16 ? 407 TRP A C     1 
ATOM   6319  O  O     A TRP A 1 407 ? 9.468   -3.116  11.245  0.50 27.50 ? 407 TRP A O     1 
ATOM   6320  O  O     B TRP A 1 407 ? 9.872   -2.739  11.310  0.50 27.76 ? 407 TRP A O     1 
ATOM   6321  C  CB    A TRP A 1 407 ? 11.959  -4.472  12.701  0.50 25.61 ? 407 TRP A CB    1 
ATOM   6322  C  CB    B TRP A 1 407 ? 12.169  -4.553  12.546  0.50 25.33 ? 407 TRP A CB    1 
ATOM   6323  C  CG    A TRP A 1 407 ? 12.933  -5.517  12.344  0.50 26.75 ? 407 TRP A CG    1 
ATOM   6324  C  CG    B TRP A 1 407 ? 13.270  -5.537  12.281  0.50 27.64 ? 407 TRP A CG    1 
ATOM   6325  C  CD1   A TRP A 1 407 ? 14.077  -5.839  13.013  0.50 24.78 ? 407 TRP A CD1   1 
ATOM   6326  C  CD1   B TRP A 1 407 ? 14.155  -6.033  13.194  0.50 24.65 ? 407 TRP A CD1   1 
ATOM   6327  C  CD2   A TRP A 1 407 ? 12.869  -6.385  11.211  0.50 23.00 ? 407 TRP A CD2   1 
ATOM   6328  C  CD2   B TRP A 1 407 ? 13.593  -6.165  11.029  0.50 26.75 ? 407 TRP A CD2   1 
ATOM   6329  N  NE1   A TRP A 1 407 ? 14.726  -6.863  12.368  0.50 23.47 ? 407 TRP A NE1   1 
ATOM   6330  N  NE1   B TRP A 1 407 ? 15.010  -6.923  12.591  0.50 23.09 ? 407 TRP A NE1   1 
ATOM   6331  C  CE2   A TRP A 1 407 ? 14.005  -7.213  11.257  0.50 23.18 ? 407 TRP A CE2   1 
ATOM   6332  C  CE2   B TRP A 1 407 ? 14.691  -7.019  11.263  0.50 24.01 ? 407 TRP A CE2   1 
ATOM   6333  C  CE3   A TRP A 1 407 ? 11.962  -6.538  10.158  0.50 26.18 ? 407 TRP A CE3   1 
ATOM   6334  C  CE3   B TRP A 1 407 ? 13.069  -6.078  9.733   0.50 34.22 ? 407 TRP A CE3   1 
ATOM   6335  C  CZ2   A TRP A 1 407 ? 14.253  -8.187  10.298  0.50 29.47 ? 407 TRP A CZ2   1 
ATOM   6336  C  CZ2   B TRP A 1 407 ? 15.272  -7.784  10.253  0.50 25.62 ? 407 TRP A CZ2   1 
ATOM   6337  C  CZ3   A TRP A 1 407 ? 12.211  -7.507  9.207   0.50 29.38 ? 407 TRP A CZ3   1 
ATOM   6338  C  CZ3   B TRP A 1 407 ? 13.653  -6.838  8.725   0.50 23.58 ? 407 TRP A CZ3   1 
ATOM   6339  C  CH2   A TRP A 1 407 ? 13.346  -8.316  9.282   0.50 25.66 ? 407 TRP A CH2   1 
ATOM   6340  C  CH2   B TRP A 1 407 ? 14.741  -7.681  8.993   0.50 29.39 ? 407 TRP A CH2   1 
ATOM   6341  N  N     A TYR A 1 408 ? 10.478  -1.586  12.549  0.50 21.27 ? 408 TYR A N     1 
ATOM   6342  N  N     B TYR A 1 408 ? 10.936  -1.549  12.895  0.50 20.41 ? 408 TYR A N     1 
ATOM   6343  C  CA    A TYR A 1 408 ? 9.278   -0.800  12.799  0.50 25.34 ? 408 TYR A CA    1 
ATOM   6344  C  CA    B TYR A 1 408 ? 9.775   -0.711  13.175  0.50 27.49 ? 408 TYR A CA    1 
ATOM   6345  C  C     A TYR A 1 408 ? 9.025   0.207   11.682  0.50 27.46 ? 408 TYR A C     1 
ATOM   6346  C  C     B TYR A 1 408 ? 9.616   0.378   12.121  0.50 28.09 ? 408 TYR A C     1 
ATOM   6347  O  O     A TYR A 1 408 ? 7.906   0.304   11.172  0.50 26.59 ? 408 TYR A O     1 
ATOM   6348  O  O     B TYR A 1 408 ? 8.509   0.621   11.627  0.50 26.01 ? 408 TYR A O     1 
ATOM   6349  C  CB    A TYR A 1 408 ? 9.405   -0.096  14.154  0.50 21.45 ? 408 TYR A CB    1 
ATOM   6350  C  CB    B TYR A 1 408 ? 9.909   -0.100  14.571  0.50 22.22 ? 408 TYR A CB    1 
ATOM   6351  C  CG    A TYR A 1 408 ? 9.467   -1.057  15.324  0.50 21.92 ? 408 TYR A CG    1 
ATOM   6352  C  CG    B TYR A 1 408 ? 9.893   -1.127  15.680  0.50 21.50 ? 408 TYR A CG    1 
ATOM   6353  C  CD1   A TYR A 1 408 ? 10.612  -1.804  15.577  0.50 23.98 ? 408 TYR A CD1   1 
ATOM   6354  C  CD1   B TYR A 1 408 ? 11.027  -1.881  15.976  0.50 26.13 ? 408 TYR A CD1   1 
ATOM   6355  C  CD2   A TYR A 1 408 ? 8.377   -1.226  16.171  0.50 23.50 ? 408 TYR A CD2   1 
ATOM   6356  C  CD2   B TYR A 1 408 ? 8.746   -1.343  16.431  0.50 24.81 ? 408 TYR A CD2   1 
ATOM   6357  C  CE1   A TYR A 1 408 ? 10.676  -2.687  16.637  0.50 24.13 ? 408 TYR A CE1   1 
ATOM   6358  C  CE1   B TYR A 1 408 ? 11.016  -2.824  16.985  0.50 19.74 ? 408 TYR A CE1   1 
ATOM   6359  C  CE2   A TYR A 1 408 ? 8.429   -2.108  17.236  0.50 21.26 ? 408 TYR A CE2   1 
ATOM   6360  C  CE2   B TYR A 1 408 ? 8.724   -2.279  17.439  0.50 20.92 ? 408 TYR A CE2   1 
ATOM   6361  C  CZ    A TYR A 1 408 ? 9.578   -2.837  17.464  0.50 21.35 ? 408 TYR A CZ    1 
ATOM   6362  C  CZ    B TYR A 1 408 ? 9.855   -3.017  17.714  0.50 22.41 ? 408 TYR A CZ    1 
ATOM   6363  O  OH    A TYR A 1 408 ? 9.646   -3.719  18.518  0.50 22.40 ? 408 TYR A OH    1 
ATOM   6364  O  OH    B TYR A 1 408 ? 9.824   -3.950  18.721  0.50 22.64 ? 408 TYR A OH    1 
ATOM   6365  N  N     A VAL A 1 409 ? 10.060  0.946   11.274  0.50 26.54 ? 409 VAL A N     1 
ATOM   6366  N  N     B VAL A 1 409 ? 10.719  1.041   11.770  0.50 27.82 ? 409 VAL A N     1 
ATOM   6367  C  CA    A VAL A 1 409 ? 9.901   1.929   10.205  0.50 27.32 ? 409 VAL A CA    1 
ATOM   6368  C  CA    B VAL A 1 409 ? 10.697  2.042   10.706  0.50 29.02 ? 409 VAL A CA    1 
ATOM   6369  C  C     A VAL A 1 409 ? 9.530   1.252   8.891   0.50 28.09 ? 409 VAL A C     1 
ATOM   6370  C  C     B VAL A 1 409 ? 10.195  1.428   9.406   0.50 27.91 ? 409 VAL A C     1 
ATOM   6371  O  O     A VAL A 1 409 ? 8.780   1.813   8.084   0.50 30.88 ? 409 VAL A O     1 
ATOM   6372  O  O     B VAL A 1 409 ? 9.428   2.052   8.661   0.50 31.62 ? 409 VAL A O     1 
ATOM   6373  C  CB    A VAL A 1 409 ? 11.177  2.785   10.077  0.50 30.88 ? 409 VAL A CB    1 
ATOM   6374  C  CB    B VAL A 1 409 ? 12.097  2.665   10.540  0.50 28.66 ? 409 VAL A CB    1 
ATOM   6375  C  CG1   A VAL A 1 409 ? 11.029  3.817   8.964   0.50 29.82 ? 409 VAL A CG1   1 
ATOM   6376  C  CG1   B VAL A 1 409 ? 12.249  3.311   9.167   0.50 26.54 ? 409 VAL A CG1   1 
ATOM   6377  C  CG2   A VAL A 1 409 ? 11.473  3.480   11.399  0.50 26.72 ? 409 VAL A CG2   1 
ATOM   6378  C  CG2   B VAL A 1 409 ? 12.358  3.679   11.640  0.50 29.65 ? 409 VAL A CG2   1 
ATOM   6379  N  N     A GLY A 1 410 ? 10.025  0.038   8.660   0.50 24.79 ? 410 GLY A N     1 
ATOM   6380  N  N     B GLY A 1 410 ? 10.605  0.189   9.120   0.50 27.22 ? 410 GLY A N     1 
ATOM   6381  C  CA    A GLY A 1 410 ? 9.654   -0.696  7.465   0.50 30.64 ? 410 GLY A CA    1 
ATOM   6382  C  CA    B GLY A 1 410 ? 10.166  -0.480  7.909   0.50 29.89 ? 410 GLY A CA    1 
ATOM   6383  C  C     A GLY A 1 410 ? 8.236   -1.228  7.466   0.50 32.37 ? 410 GLY A C     1 
ATOM   6384  C  C     B GLY A 1 410 ? 8.673   -0.723  7.844   0.50 32.44 ? 410 GLY A C     1 
ATOM   6385  O  O     A GLY A 1 410 ? 7.797   -1.761  6.441   0.50 25.94 ? 410 GLY A O     1 
ATOM   6386  O  O     B GLY A 1 410 ? 8.142   -0.973  6.756   0.50 31.28 ? 410 GLY A O     1 
ATOM   6387  N  N     A GLU A 1 411 ? 7.515   -1.097  8.582   0.50 28.86 ? 411 GLU A N     1 
ATOM   6388  N  N     B GLU A 1 411 ? 7.982   -0.661  8.983   0.50 28.60 ? 411 GLU A N     1 
ATOM   6389  C  CA    A GLU A 1 411 ? 6.135   -1.554  8.706   0.50 29.84 ? 411 GLU A CA    1 
ATOM   6390  C  CA    B GLU A 1 411 ? 6.530   -0.810  9.033   0.50 27.69 ? 411 GLU A CA    1 
ATOM   6391  C  C     A GLU A 1 411 ? 5.192   -0.389  8.999   0.50 30.50 ? 411 GLU A C     1 
ATOM   6392  C  C     B GLU A 1 411 ? 5.828   0.531   9.203   0.50 29.10 ? 411 GLU A C     1 
ATOM   6393  O  O     A GLU A 1 411 ? 4.292   -0.489  9.838   0.50 34.19 ? 411 GLU A O     1 
ATOM   6394  O  O     B GLU A 1 411 ? 4.893   0.663   9.999   0.50 34.61 ? 411 GLU A O     1 
ATOM   6395  C  CB    A GLU A 1 411 ? 6.013   -2.634  9.781   0.50 28.91 ? 411 GLU A CB    1 
ATOM   6396  C  CB    B GLU A 1 411 ? 6.138   -1.774  10.146  0.50 27.67 ? 411 GLU A CB    1 
ATOM   6397  C  CG    A GLU A 1 411 ? 6.802   -3.911  9.496   0.50 27.59 ? 411 GLU A CG    1 
ATOM   6398  C  CG    B GLU A 1 411 ? 6.600   -3.198  9.911   0.50 29.66 ? 411 GLU A CG    1 
ATOM   6399  C  CD    A GLU A 1 411 ? 6.046   -4.904  8.633   0.50 29.61 ? 411 GLU A CD    1 
ATOM   6400  C  CD    B GLU A 1 411 ? 5.945   -3.840  8.697   0.50 28.67 ? 411 GLU A CD    1 
ATOM   6401  O  OE1   A GLU A 1 411 ? 4.891   -4.613  8.257   0.50 22.85 ? 411 GLU A OE1   1 
ATOM   6402  O  OE1   B GLU A 1 411 ? 4.888   -3.350  8.242   0.50 28.12 ? 411 GLU A OE1   1 
ATOM   6403  O  OE2   A GLU A 1 411 ? 6.597   -5.990  8.345   0.50 33.30 ? 411 GLU A OE2   1 
ATOM   6404  O  OE2   B GLU A 1 411 ? 6.489   -4.843  8.196   0.50 29.16 ? 411 GLU A OE2   1 
ATOM   6405  N  N     A GLY A 1 412 ? 5.401   0.739   8.322   0.50 28.10 ? 412 GLY A N     1 
ATOM   6406  N  N     B GLY A 1 412 ? 6.280   1.546   8.472   0.50 31.80 ? 412 GLY A N     1 
ATOM   6407  C  CA    A GLY A 1 412 ? 4.462   1.846   8.336   0.50 27.16 ? 412 GLY A CA    1 
ATOM   6408  C  CA    B GLY A 1 412 ? 5.598   2.824   8.439   0.50 33.33 ? 412 GLY A CA    1 
ATOM   6409  C  C     A GLY A 1 412 ? 4.600   2.835   9.473   0.50 29.99 ? 412 GLY A C     1 
ATOM   6410  C  C     B GLY A 1 412 ? 5.553   3.589   9.741   0.50 34.26 ? 412 GLY A C     1 
ATOM   6411  O  O     A GLY A 1 412 ? 3.713   3.679   9.644   0.50 33.57 ? 412 GLY A O     1 
ATOM   6412  O  O     B GLY A 1 412 ? 4.673   4.435   9.912   0.50 31.93 ? 412 GLY A O     1 
ATOM   6413  N  N     A MET A 1 413 ? 5.685   2.780   10.237  0.50 28.16 ? 413 MET A N     1 
ATOM   6414  N  N     B MET A 1 413 ? 6.468   3.326   10.668  0.50 33.58 ? 413 MET A N     1 
ATOM   6415  C  CA    A MET A 1 413 ? 5.828   3.561   11.457  0.50 30.17 ? 413 MET A CA    1 
ATOM   6416  C  CA    B MET A 1 413 ? 6.543   4.092   11.904  0.50 33.00 ? 413 MET A CA    1 
ATOM   6417  C  C     A MET A 1 413 ? 6.999   4.529   11.330  0.50 30.36 ? 413 MET A C     1 
ATOM   6418  C  C     B MET A 1 413 ? 7.686   5.093   11.824  0.50 29.30 ? 413 MET A C     1 
ATOM   6419  O  O     A MET A 1 413 ? 8.035   4.186   10.760  0.50 31.97 ? 413 MET A O     1 
ATOM   6420  O  O     B MET A 1 413 ? 8.772   4.776   11.330  0.50 29.01 ? 413 MET A O     1 
ATOM   6421  C  CB    A MET A 1 413 ? 6.017   2.617   12.650  0.50 28.22 ? 413 MET A CB    1 
ATOM   6422  C  CB    B MET A 1 413 ? 6.732   3.185   13.124  0.50 26.04 ? 413 MET A CB    1 
ATOM   6423  C  CG    A MET A 1 413 ? 6.440   3.270   13.935  0.50 31.48 ? 413 MET A CG    1 
ATOM   6424  C  CG    B MET A 1 413 ? 6.167   3.786   14.408  0.50 34.88 ? 413 MET A CG    1 
ATOM   6425  S  SD    A MET A 1 413 ? 6.368   2.118   15.320  0.50 31.77 ? 413 MET A SD    1 
ATOM   6426  S  SD    B MET A 1 413 ? 6.493   2.830   15.902  0.50 33.28 ? 413 MET A SD    1 
ATOM   6427  C  CE    A MET A 1 413 ? 7.341   3.052   16.489  0.50 22.81 ? 413 MET A CE    1 
ATOM   6428  C  CE    B MET A 1 413 ? 8.186   3.301   16.218  0.50 24.26 ? 413 MET A CE    1 
ATOM   6429  N  N     A GLU A 1 414 ? 6.833   5.743   11.854  0.50 28.36 ? 414 GLU A N     1 
ATOM   6430  N  N     B GLU A 1 414 ? 7.433   6.304   12.309  0.50 34.09 ? 414 GLU A N     1 
ATOM   6431  C  CA    A GLU A 1 414 ? 7.873   6.763   11.771  0.50 34.35 ? 414 GLU A CA    1 
ATOM   6432  C  CA    B GLU A 1 414 ? 8.464   7.330   12.359  0.50 29.13 ? 414 GLU A CA    1 
ATOM   6433  C  C     A GLU A 1 414 ? 8.870   6.619   12.914  0.50 31.96 ? 414 GLU A C     1 
ATOM   6434  C  C     B GLU A 1 414 ? 9.356   7.120   13.575  0.50 33.01 ? 414 GLU A C     1 
ATOM   6435  O  O     A GLU A 1 414 ? 8.487   6.412   14.068  0.50 33.36 ? 414 GLU A O     1 
ATOM   6436  O  O     B GLU A 1 414 ? 8.872   6.818   14.672  0.50 28.98 ? 414 GLU A O     1 
ATOM   6437  C  CB    A GLU A 1 414 ? 7.267   8.166   11.796  0.50 38.02 ? 414 GLU A CB    1 
ATOM   6438  C  CB    B GLU A 1 414 ? 7.830   8.718   12.410  0.50 38.40 ? 414 GLU A CB    1 
ATOM   6439  C  CG    A GLU A 1 414 ? 6.445   8.523   10.574  0.50 48.49 ? 414 GLU A CG    1 
ATOM   6440  C  CG    B GLU A 1 414 ? 6.942   9.042   11.222  0.50 43.78 ? 414 GLU A CG    1 
ATOM   6441  C  CD    A GLU A 1 414 ? 6.076   9.994   10.541  0.50 51.71 ? 414 GLU A CD    1 
ATOM   6442  C  CD    B GLU A 1 414 ? 6.021   10.216  11.488  0.50 50.57 ? 414 GLU A CD    1 
ATOM   6443  O  OE1   A GLU A 1 414 ? 6.835   10.809  11.109  0.50 47.33 ? 414 GLU A OE1   1 
ATOM   6444  O  OE1   B GLU A 1 414 ? 5.136   10.090  12.362  0.50 57.09 ? 414 GLU A OE1   1 
ATOM   6445  O  OE2   A GLU A 1 414 ? 5.026   10.334  9.956   0.50 60.93 ? 414 GLU A OE2   1 
ATOM   6446  O  OE2   B GLU A 1 414 ? 6.187   11.266  10.831  0.50 52.64 ? 414 GLU A OE2   1 
ATOM   6447  N  N     A GLU A 1 415 ? 10.158  6.751   12.579  0.50 29.53 ? 415 GLU A N     1 
ATOM   6448  N  N     B GLU A 1 415 ? 10.670  7.282   13.377  0.50 28.56 ? 415 GLU A N     1 
ATOM   6449  C  CA    A GLU A 1 415 ? 11.221  6.573   13.565  0.50 28.80 ? 415 GLU A CA    1 
ATOM   6450  C  CA    B GLU A 1 415 ? 11.596  7.195   14.502  0.50 30.24 ? 415 GLU A CA    1 
ATOM   6451  C  C     A GLU A 1 415 ? 11.066  7.512   14.755  0.50 29.37 ? 415 GLU A C     1 
ATOM   6452  C  C     B GLU A 1 415 ? 11.232  8.186   15.602  0.50 30.74 ? 415 GLU A C     1 
ATOM   6453  O  O     A GLU A 1 415 ? 11.427  7.148   15.880  0.50 34.65 ? 415 GLU A O     1 
ATOM   6454  O  O     B GLU A 1 415 ? 11.488  7.924   16.785  0.50 33.65 ? 415 GLU A O     1 
ATOM   6455  C  CB    A GLU A 1 415 ? 12.583  6.783   12.902  0.50 33.82 ? 415 GLU A CB    1 
ATOM   6456  C  CB    B GLU A 1 415 ? 13.032  7.421   14.025  0.50 33.60 ? 415 GLU A CB    1 
ATOM   6457  C  CG    A GLU A 1 415 ? 13.769  6.634   13.838  0.50 29.64 ? 415 GLU A CG    1 
ATOM   6458  C  CG    B GLU A 1 415 ? 14.036  7.631   15.153  0.50 33.15 ? 415 GLU A CG    1 
ATOM   6459  C  CD    A GLU A 1 415 ? 15.053  7.172   13.236  0.50 35.53 ? 415 GLU A CD    1 
ATOM   6460  C  CD    B GLU A 1 415 ? 15.312  6.837   14.971  0.50 39.76 ? 415 GLU A CD    1 
ATOM   6461  O  OE1   A GLU A 1 415 ? 15.407  6.748   12.114  0.50 40.57 ? 415 GLU A OE1   1 
ATOM   6462  O  OE1   B GLU A 1 415 ? 15.465  6.177   13.922  0.50 34.81 ? 415 GLU A OE1   1 
ATOM   6463  O  OE2   A GLU A 1 415 ? 15.698  8.029   13.880  0.50 33.95 ? 415 GLU A OE2   1 
ATOM   6464  O  OE2   B GLU A 1 415 ? 16.166  6.876   15.881  0.50 37.74 ? 415 GLU A OE2   1 
ATOM   6465  N  N     A GLY A 1 416 ? 10.531  8.714   14.534  0.50 27.89 ? 416 GLY A N     1 
ATOM   6466  N  N     B GLY A 1 416 ? 10.608  9.311   15.242  0.50 29.29 ? 416 GLY A N     1 
ATOM   6467  C  CA    A GLY A 1 416 ? 10.399  9.667   15.622  0.50 31.78 ? 416 GLY A CA    1 
ATOM   6468  C  CA    B GLY A 1 416 ? 10.142  10.258  16.240  0.50 33.39 ? 416 GLY A CA    1 
ATOM   6469  C  C     A GLY A 1 416 ? 9.482   9.190   16.731  0.50 32.09 ? 416 GLY A C     1 
ATOM   6470  C  C     B GLY A 1 416 ? 9.162   9.670   17.236  0.50 31.84 ? 416 GLY A C     1 
ATOM   6471  O  O     A GLY A 1 416 ? 9.705   9.508   17.901  0.50 28.51 ? 416 GLY A O     1 
ATOM   6472  O  O     B GLY A 1 416 ? 8.926   10.272  18.288  0.50 28.18 ? 416 GLY A O     1 
ATOM   6473  N  N     A GLU A 1 417 ? 8.451   8.412   16.381  0.50 33.57 ? 417 GLU A N     1 
ATOM   6474  N  N     B GLU A 1 417 ? 8.583   8.508   16.928  0.50 32.18 ? 417 GLU A N     1 
ATOM   6475  C  CA    A GLU A 1 417 ? 7.472   7.952   17.363  0.50 28.93 ? 417 GLU A CA    1 
ATOM   6476  C  CA    B GLU A 1 417 ? 7.693   7.849   17.879  0.50 27.88 ? 417 GLU A CA    1 
ATOM   6477  C  C     A GLU A 1 417 ? 8.134   7.266   18.552  0.50 28.36 ? 417 GLU A C     1 
ATOM   6478  C  C     B GLU A 1 417 ? 8.476   7.221   19.024  0.50 28.18 ? 417 GLU A C     1 
ATOM   6479  O  O     A GLU A 1 417 ? 7.607   7.315   19.672  0.50 30.42 ? 417 GLU A O     1 
ATOM   6480  O  O     B GLU A 1 417 ? 8.009   7.211   20.170  0.50 28.67 ? 417 GLU A O     1 
ATOM   6481  C  CB    A GLU A 1 417 ? 6.467   7.012   16.690  0.50 32.45 ? 417 GLU A CB    1 
ATOM   6482  C  CB    B GLU A 1 417 ? 6.847   6.796   17.162  0.50 31.12 ? 417 GLU A CB    1 
ATOM   6483  C  CG    A GLU A 1 417 ? 5.221   6.728   17.514  0.50 34.00 ? 417 GLU A CG    1 
ATOM   6484  C  CG    B GLU A 1 417 ? 5.935   5.995   18.081  0.50 29.73 ? 417 GLU A CG    1 
ATOM   6485  C  CD    A GLU A 1 417 ? 4.253   5.784   16.815  0.50 35.07 ? 417 GLU A CD    1 
ATOM   6486  C  CD    B GLU A 1 417 ? 4.585   5.704   17.452  0.50 33.38 ? 417 GLU A CD    1 
ATOM   6487  O  OE1   A GLU A 1 417 ? 4.305   5.678   15.571  0.50 33.63 ? 417 GLU A OE1   1 
ATOM   6488  O  OE1   B GLU A 1 417 ? 4.464   5.820   16.214  0.50 36.88 ? 417 GLU A OE1   1 
ATOM   6489  O  OE2   A GLU A 1 417 ? 3.440   5.144   17.512  0.50 32.18 ? 417 GLU A OE2   1 
ATOM   6490  O  OE2   B GLU A 1 417 ? 3.641   5.373   18.199  0.50 36.42 ? 417 GLU A OE2   1 
ATOM   6491  N  N     A PHE A 1 418 ? 9.286   6.627   18.333  0.50 25.55 ? 418 PHE A N     1 
ATOM   6492  N  N     B PHE A 1 418 ? 9.666   6.692   18.732  0.50 27.67 ? 418 PHE A N     1 
ATOM   6493  C  CA    A PHE A 1 418 ? 10.064  6.090   19.446  0.50 29.70 ? 418 PHE A CA    1 
ATOM   6494  C  CA    B PHE A 1 418 ? 10.491  6.073   19.767  0.50 27.93 ? 418 PHE A CA    1 
ATOM   6495  C  C     A PHE A 1 418 ? 10.404  7.177   20.459  0.50 32.30 ? 418 PHE A C     1 
ATOM   6496  C  C     B PHE A 1 418 ? 10.841  7.071   20.864  0.50 32.15 ? 418 PHE A C     1 
ATOM   6497  O  O     A PHE A 1 418 ? 10.324  6.953   21.672  0.50 29.84 ? 418 PHE A O     1 
ATOM   6498  O  O     B PHE A 1 418 ? 10.654  6.796   22.055  0.50 31.18 ? 418 PHE A O     1 
ATOM   6499  C  CB    A PHE A 1 418 ? 11.346  5.437   18.927  0.50 25.43 ? 418 PHE A CB    1 
ATOM   6500  C  CB    B PHE A 1 418 ? 11.769  5.509   19.146  0.50 26.49 ? 418 PHE A CB    1 
ATOM   6501  C  CG    A PHE A 1 418 ? 11.178  4.006   18.495  0.50 24.71 ? 418 PHE A CG    1 
ATOM   6502  C  CG    B PHE A 1 418 ? 11.667  4.074   18.713  0.50 25.71 ? 418 PHE A CG    1 
ATOM   6503  C  CD1   A PHE A 1 418 ? 11.312  2.974   19.411  0.50 24.52 ? 418 PHE A CD1   1 
ATOM   6504  C  CD1   B PHE A 1 418 ? 11.684  3.051   19.648  0.50 25.15 ? 418 PHE A CD1   1 
ATOM   6505  C  CD2   A PHE A 1 418 ? 10.910  3.691   17.172  0.50 27.07 ? 418 PHE A CD2   1 
ATOM   6506  C  CD2   B PHE A 1 418 ? 11.597  3.744   17.368  0.50 29.61 ? 418 PHE A CD2   1 
ATOM   6507  C  CE1   A PHE A 1 418 ? 11.169  1.654   19.020  0.50 26.44 ? 418 PHE A CE1   1 
ATOM   6508  C  CE1   B PHE A 1 418 ? 11.609  1.727   19.254  0.50 26.31 ? 418 PHE A CE1   1 
ATOM   6509  C  CE2   A PHE A 1 418 ? 10.768  2.372   16.773  0.50 27.39 ? 418 PHE A CE2   1 
ATOM   6510  C  CE2   B PHE A 1 418 ? 11.527  2.417   16.964  0.50 23.81 ? 418 PHE A CE2   1 
ATOM   6511  C  CZ    A PHE A 1 418 ? 10.897  1.352   17.699  0.50 27.69 ? 418 PHE A CZ    1 
ATOM   6512  C  CZ    B PHE A 1 418 ? 11.529  1.409   17.910  0.50 27.91 ? 418 PHE A CZ    1 
ATOM   6513  N  N     A SER A 1 419 ? 10.780  8.366   19.978  0.50 28.61 ? 419 SER A N     1 
ATOM   6514  N  N     B SER A 1 419 ? 11.352  8.242   20.477  0.50 28.41 ? 419 SER A N     1 
ATOM   6515  C  CA    A SER A 1 419 ? 11.207  9.430   20.881  0.50 30.94 ? 419 SER A CA    1 
ATOM   6516  C  CA    B SER A 1 419 ? 11.875  9.193   21.449  0.50 28.40 ? 419 SER A CA    1 
ATOM   6517  C  C     A SER A 1 419 ? 10.029  10.021  21.641  0.50 28.76 ? 419 SER A C     1 
ATOM   6518  C  C     B SER A 1 419 ? 10.770  9.935   22.189  0.50 31.45 ? 419 SER A C     1 
ATOM   6519  O  O     A SER A 1 419 ? 10.142  10.314  22.838  0.50 32.14 ? 419 SER A O     1 
ATOM   6520  O  O     B SER A 1 419 ? 10.951  10.302  23.356  0.50 30.21 ? 419 SER A O     1 
ATOM   6521  C  CB    A SER A 1 419 ? 11.939  10.524  20.102  0.50 32.02 ? 419 SER A CB    1 
ATOM   6522  C  CB    B SER A 1 419 ? 12.807  10.187  20.754  0.50 26.70 ? 419 SER A CB    1 
ATOM   6523  O  OG    A SER A 1 419 ? 13.045  9.994   19.405  0.50 29.48 ? 419 SER A OG    1 
ATOM   6524  O  OG    B SER A 1 419 ? 13.905  9.508   20.164  0.50 31.54 ? 419 SER A OG    1 
ATOM   6525  N  N     A GLU A 1 420 ? 8.892   10.207  20.966  0.50 28.95 ? 420 GLU A N     1 
ATOM   6526  N  N     B GLU A 1 420 ? 9.627   10.169  21.540  0.50 28.64 ? 420 GLU A N     1 
ATOM   6527  C  CA    A GLU A 1 420 ? 7.723   10.770  21.635  0.50 33.11 ? 420 GLU A CA    1 
ATOM   6528  C  CA    B GLU A 1 420 ? 8.516   10.789  22.253  0.50 30.90 ? 420 GLU A CA    1 
ATOM   6529  C  C     A GLU A 1 420 ? 7.213   9.844   22.733  0.50 28.84 ? 420 GLU A C     1 
ATOM   6530  C  C     B GLU A 1 420 ? 7.842   9.800   23.197  0.50 28.75 ? 420 GLU A C     1 
ATOM   6531  O  O     A GLU A 1 420 ? 6.748   10.307  23.782  0.50 30.05 ? 420 GLU A O     1 
ATOM   6532  O  O     B GLU A 1 420 ? 7.328   10.203  24.247  0.50 29.14 ? 420 GLU A O     1 
ATOM   6533  C  CB    A GLU A 1 420 ? 6.621   11.053  20.614  0.50 33.04 ? 420 GLU A CB    1 
ATOM   6534  C  CB    B GLU A 1 420 ? 7.506   11.373  21.266  0.50 33.65 ? 420 GLU A CB    1 
ATOM   6535  C  CG    A GLU A 1 420 ? 5.274   11.371  21.244  0.50 28.84 ? 420 GLU A CG    1 
ATOM   6536  C  CG    B GLU A 1 420 ? 6.694   10.343  20.502  0.50 28.93 ? 420 GLU A CG    1 
ATOM   6537  C  CD    A GLU A 1 420 ? 4.197   11.656  20.223  0.50 36.19 ? 420 GLU A CD    1 
ATOM   6538  C  CD    B GLU A 1 420 ? 5.541   10.964  19.741  0.50 39.82 ? 420 GLU A CD    1 
ATOM   6539  O  OE1   A GLU A 1 420 ? 4.347   12.631  19.457  0.50 36.50 ? 420 GLU A OE1   1 
ATOM   6540  O  OE1   B GLU A 1 420 ? 5.787   11.912  18.961  0.50 42.64 ? 420 GLU A OE1   1 
ATOM   6541  O  OE2   A GLU A 1 420 ? 3.201   10.899  20.179  0.50 37.28 ? 420 GLU A OE2   1 
ATOM   6542  O  OE2   B GLU A 1 420 ? 4.389   10.508  19.933  0.50 33.34 ? 420 GLU A OE2   1 
ATOM   6543  N  N     A ALA A 1 421 ? 7.301   8.530   22.516  0.50 22.77 ? 421 ALA A N     1 
ATOM   6544  N  N     B ALA A 1 421 ? 7.838   8.508   22.848  0.50 26.08 ? 421 ALA A N     1 
ATOM   6545  C  CA    A ALA A 1 421 ? 6.850   7.580   23.527  0.50 25.97 ? 421 ALA A CA    1 
ATOM   6546  C  CA    B ALA A 1 421 ? 7.335   7.496   23.773  0.50 25.44 ? 421 ALA A CA    1 
ATOM   6547  C  C     A ALA A 1 421 ? 7.798   7.543   24.720  0.50 26.93 ? 421 ALA A C     1 
ATOM   6548  C  C     B ALA A 1 421 ? 8.223   7.391   25.004  0.50 28.60 ? 421 ALA A C     1 
ATOM   6549  O  O     A ALA A 1 421 ? 7.350   7.480   25.872  0.50 25.29 ? 421 ALA A O     1 
ATOM   6550  O  O     B ALA A 1 421 ? 7.727   7.221   26.125  0.50 24.42 ? 421 ALA A O     1 
ATOM   6551  C  CB    A ALA A 1 421 ? 6.709   6.188   22.912  0.50 27.03 ? 421 ALA A CB    1 
ATOM   6552  C  CB    B ALA A 1 421 ? 7.232   6.142   23.071  0.50 27.73 ? 421 ALA A CB    1 
ATOM   6553  N  N     A ARG A 1 422 ? 9.109   7.581   24.470  0.50 24.57 ? 422 ARG A N     1 
ATOM   6554  N  N     B ARG A 1 422 ? 9.540   7.479   24.813  0.50 25.77 ? 422 ARG A N     1 
ATOM   6555  C  CA    A ARG A 1 422 ? 10.074  7.498   25.564  0.50 27.16 ? 422 ARG A CA    1 
ATOM   6556  C  CA    B ARG A 1 422 ? 10.452  7.507   25.950  0.50 27.70 ? 422 ARG A CA    1 
ATOM   6557  C  C     A ARG A 1 422 ? 10.034  8.740   26.449  0.50 27.32 ? 422 ARG A C     1 
ATOM   6558  C  C     B ARG A 1 422 ? 10.339  8.821   26.714  0.50 27.22 ? 422 ARG A C     1 
ATOM   6559  O  O     A ARG A 1 422 ? 10.249  8.639   27.663  0.50 27.37 ? 422 ARG A O     1 
ATOM   6560  O  O     B ARG A 1 422 ? 10.513  8.843   27.938  0.50 26.73 ? 422 ARG A O     1 
ATOM   6561  C  CB    A ARG A 1 422 ? 11.482  7.271   25.005  0.50 25.95 ? 422 ARG A CB    1 
ATOM   6562  C  CB    B ARG A 1 422 ? 11.886  7.277   25.468  0.50 28.02 ? 422 ARG A CB    1 
ATOM   6563  C  CG    A ARG A 1 422 ? 12.583  7.170   26.061  0.50 29.18 ? 422 ARG A CG    1 
ATOM   6564  C  CG    B ARG A 1 422 ? 12.923  7.208   26.578  0.50 29.00 ? 422 ARG A CG    1 
ATOM   6565  C  CD    A ARG A 1 422 ? 12.289  6.082   27.093  0.50 29.62 ? 422 ARG A CD    1 
ATOM   6566  C  CD    B ARG A 1 422 ? 12.603  6.100   27.570  0.50 28.62 ? 422 ARG A CD    1 
ATOM   6567  N  NE    A ARG A 1 422 ? 13.337  5.977   28.103  0.50 25.96 ? 422 ARG A NE    1 
ATOM   6568  N  NE    B ARG A 1 422 ? 13.579  6.041   28.651  0.50 27.42 ? 422 ARG A NE    1 
ATOM   6569  C  CZ    A ARG A 1 422 ? 13.322  6.602   29.275  0.50 31.93 ? 422 ARG A CZ    1 
ATOM   6570  C  CZ    B ARG A 1 422 ? 13.501  6.748   29.772  0.50 30.30 ? 422 ARG A CZ    1 
ATOM   6571  N  NH1   A ARG A 1 422 ? 12.315  7.384   29.632  0.50 26.60 ? 422 ARG A NH1   1 
ATOM   6572  N  NH1   B ARG A 1 422 ? 12.498  7.580   29.997  0.50 24.03 ? 422 ARG A NH1   1 
ATOM   6573  N  NH2   A ARG A 1 422 ? 14.343  6.437   30.111  0.50 30.50 ? 422 ARG A NH2   1 
ATOM   6574  N  NH2   B ARG A 1 422 ? 14.455  6.618   30.689  0.50 28.09 ? 422 ARG A NH2   1 
ATOM   6575  N  N     A GLU A 1 423 ? 9.770   9.914   25.870  0.50 27.24 ? 423 GLU A N     1 
ATOM   6576  N  N     B GLU A 1 423 ? 10.048  9.917   26.009  0.50 27.07 ? 423 GLU A N     1 
ATOM   6577  C  CA    A GLU A 1 423 ? 9.573   11.104  26.689  0.50 30.72 ? 423 GLU A CA    1 
ATOM   6578  C  CA    B GLU A 1 423 ? 9.822   11.200  26.666  0.50 30.60 ? 423 GLU A CA    1 
ATOM   6579  C  C     A GLU A 1 423 ? 8.300   10.999  27.515  0.50 28.82 ? 423 GLU A C     1 
ATOM   6580  C  C     B GLU A 1 423 ? 8.633   11.121  27.612  0.50 28.87 ? 423 GLU A C     1 
ATOM   6581  O  O     A GLU A 1 423 ? 8.243   11.514  28.637  0.50 28.04 ? 423 GLU A O     1 
ATOM   6582  O  O     B GLU A 1 423 ? 8.699   11.587  28.755  0.50 29.27 ? 423 GLU A O     1 
ATOM   6583  C  CB    A GLU A 1 423 ? 9.514   12.359  25.817  0.50 32.62 ? 423 GLU A CB    1 
ATOM   6584  C  CB    B GLU A 1 423 ? 9.602   12.290  25.615  0.50 33.11 ? 423 GLU A CB    1 
ATOM   6585  C  CG    A GLU A 1 423 ? 10.802  12.703  25.094  0.50 36.66 ? 423 GLU A CG    1 
ATOM   6586  C  CG    B GLU A 1 423 ? 9.175   13.637  26.175  0.50 41.53 ? 423 GLU A CG    1 
ATOM   6587  C  CD    A GLU A 1 423 ? 10.719  14.045  24.389  0.50 41.54 ? 423 GLU A CD    1 
ATOM   6588  C  CD    B GLU A 1 423 ? 8.636   14.568  25.100  0.50 40.12 ? 423 GLU A CD    1 
ATOM   6589  O  OE1   A GLU A 1 423 ? 10.158  14.996  24.978  0.50 36.33 ? 423 GLU A OE1   1 
ATOM   6590  O  OE1   B GLU A 1 423 ? 8.559   14.146  23.926  0.50 43.08 ? 423 GLU A OE1   1 
ATOM   6591  O  OE2   A GLU A 1 423 ? 11.201  14.146  23.242  0.50 36.62 ? 423 GLU A OE2   1 
ATOM   6592  O  OE2   B GLU A 1 423 ? 8.286   15.721  25.429  0.50 45.71 ? 423 GLU A OE2   1 
ATOM   6593  N  N     A ASP A 1 424 ? 7.271   10.347  26.971  0.50 30.94 ? 424 ASP A N     1 
ATOM   6594  N  N     B ASP A 1 424 ? 7.530   10.531  27.145  0.50 30.45 ? 424 ASP A N     1 
ATOM   6595  C  CA    A ASP A 1 424 ? 6.039   10.140  27.723  0.50 26.90 ? 424 ASP A CA    1 
ATOM   6596  C  CA    B ASP A 1 424 ? 6.373   10.319  28.006  0.50 26.98 ? 424 ASP A CA    1 
ATOM   6597  C  C     A ASP A 1 424 ? 6.290   9.279   28.954  0.50 27.53 ? 424 ASP A C     1 
ATOM   6598  C  C     B ASP A 1 424 ? 6.753   9.500   29.233  0.50 27.31 ? 424 ASP A C     1 
ATOM   6599  O  O     A ASP A 1 424 ? 5.676   9.494   30.006  0.50 22.17 ? 424 ASP A O     1 
ATOM   6600  O  O     B ASP A 1 424 ? 6.458   9.889   30.368  0.50 21.91 ? 424 ASP A O     1 
ATOM   6601  C  CB    A ASP A 1 424 ? 4.982   9.506   26.819  0.50 24.82 ? 424 ASP A CB    1 
ATOM   6602  C  CB    B ASP A 1 424 ? 5.257   9.633   27.215  0.50 25.59 ? 424 ASP A CB    1 
ATOM   6603  C  CG    A ASP A 1 424 ? 3.575   9.646   27.371  0.50 27.31 ? 424 ASP A CG    1 
ATOM   6604  C  CG    B ASP A 1 424 ? 3.881   9.893   27.795  0.50 26.78 ? 424 ASP A CG    1 
ATOM   6605  O  OD1   A ASP A 1 424 ? 3.385   10.430  28.327  0.50 27.06 ? 424 ASP A OD1   1 
ATOM   6606  O  OD1   B ASP A 1 424 ? 3.787   10.613  28.812  0.50 26.30 ? 424 ASP A OD1   1 
ATOM   6607  O  OD2   A ASP A 1 424 ? 2.660   8.978   26.837  0.50 25.53 ? 424 ASP A OD2   1 
ATOM   6608  O  OD2   B ASP A 1 424 ? 2.891   9.386   27.225  0.50 27.39 ? 424 ASP A OD2   1 
ATOM   6609  N  N     A MET A 1 425 ? 7.190   8.296   28.842  0.50 29.78 ? 425 MET A N     1 
ATOM   6610  N  N     B MET A 1 425 ? 7.441   8.374   29.023  0.50 30.06 ? 425 MET A N     1 
ATOM   6611  C  CA    A MET A 1 425 ? 7.545   7.487   30.004  0.50 29.77 ? 425 MET A CA    1 
ATOM   6612  C  CA    B MET A 1 425 ? 7.821   7.512   30.140  0.50 29.74 ? 425 MET A CA    1 
ATOM   6613  C  C     A MET A 1 425 ? 8.413   8.267   30.984  0.50 25.67 ? 425 MET A C     1 
ATOM   6614  C  C     B MET A 1 425 ? 8.695   8.251   31.147  0.50 25.80 ? 425 MET A C     1 
ATOM   6615  O  O     A MET A 1 425 ? 8.340   8.036   32.198  0.50 26.85 ? 425 MET A O     1 
ATOM   6616  O  O     B MET A 1 425 ? 8.564   8.047   32.361  0.50 26.07 ? 425 MET A O     1 
ATOM   6617  C  CB    A MET A 1 425 ? 8.263   6.213   29.562  0.50 25.68 ? 425 MET A CB    1 
ATOM   6618  C  CB    B MET A 1 425 ? 8.540   6.270   29.616  0.50 26.01 ? 425 MET A CB    1 
ATOM   6619  C  CG    A MET A 1 425 ? 7.490   5.379   28.550  0.50 28.15 ? 425 MET A CG    1 
ATOM   6620  C  CG    B MET A 1 425 ? 7.649   5.334   28.825  0.50 28.16 ? 425 MET A CG    1 
ATOM   6621  S  SD    A MET A 1 425 ? 5.860   4.882   29.144  0.50 27.14 ? 425 MET A SD    1 
ATOM   6622  S  SD    B MET A 1 425 ? 6.301   4.711   29.843  0.50 31.03 ? 425 MET A SD    1 
ATOM   6623  C  CE    A MET A 1 425 ? 6.305   3.983   30.627  0.50 30.77 ? 425 MET A CE    1 
ATOM   6624  C  CE    B MET A 1 425 ? 7.236   4.019   31.205  0.50 24.46 ? 425 MET A CE    1 
ATOM   6625  N  N     A ALA A 1 426 ? 9.252   9.173   30.481  0.50 28.37 ? 426 ALA A N     1 
ATOM   6626  N  N     B ALA A 1 426 ? 9.603   9.101   30.663  0.50 28.76 ? 426 ALA A N     1 
ATOM   6627  C  CA    A ALA A 1 426 ? 10.011  10.043  31.371  0.50 25.50 ? 426 ALA A CA    1 
ATOM   6628  C  CA    B ALA A 1 426 ? 10.403  9.919   31.567  0.50 24.20 ? 426 ALA A CA    1 
ATOM   6629  C  C     A ALA A 1 426 ? 9.079   10.966  32.143  0.50 28.05 ? 426 ALA A C     1 
ATOM   6630  C  C     B ALA A 1 426 ? 9.512   10.833  32.396  0.50 28.84 ? 426 ALA A C     1 
ATOM   6631  O  O     A ALA A 1 426 ? 9.287   11.216  33.335  0.50 32.27 ? 426 ALA A O     1 
ATOM   6632  O  O     B ALA A 1 426 ? 9.682   10.948  33.616  0.50 33.25 ? 426 ALA A O     1 
ATOM   6633  C  CB    A ALA A 1 426 ? 11.036  10.852  30.575  0.50 28.77 ? 426 ALA A CB    1 
ATOM   6634  C  CB    B ALA A 1 426 ? 11.428  10.733  30.774  0.50 29.47 ? 426 ALA A CB    1 
ATOM   6635  N  N     A ALA A 1 427 ? 8.036   11.472  31.479  0.50 27.30 ? 427 ALA A N     1 
ATOM   6636  N  N     B ALA A 1 427 ? 8.543   11.484  31.747  0.50 27.58 ? 427 ALA A N     1 
ATOM   6637  C  CA    A ALA A 1 427 ? 7.063   12.314  32.166  0.50 28.82 ? 427 ALA A CA    1 
ATOM   6638  C  CA    B ALA A 1 427 ? 7.579   12.296  32.480  0.50 29.79 ? 427 ALA A CA    1 
ATOM   6639  C  C     A ALA A 1 427 ? 6.324   11.534  33.246  0.50 31.42 ? 427 ALA A C     1 
ATOM   6640  C  C     B ALA A 1 427 ? 6.689   11.437  33.368  0.50 31.30 ? 427 ALA A C     1 
ATOM   6641  O  O     A ALA A 1 427 ? 6.008   12.081  34.309  0.50 30.30 ? 427 ALA A O     1 
ATOM   6642  O  O     B ALA A 1 427 ? 6.291   11.877  34.453  0.50 30.11 ? 427 ALA A O     1 
ATOM   6643  C  CB    A ALA A 1 427 ? 6.078   12.906  31.161  0.50 26.01 ? 427 ALA A CB    1 
ATOM   6644  C  CB    B ALA A 1 427 ? 6.732   13.115  31.507  0.50 24.00 ? 427 ALA A CB    1 
ATOM   6645  N  N     A LEU A 1 428 ? 6.039   10.253  32.995  0.50 25.69 ? 428 LEU A N     1 
ATOM   6646  N  N     B LEU A 1 428 ? 6.368   10.216  32.928  0.50 24.98 ? 428 LEU A N     1 
ATOM   6647  C  CA    A LEU A 1 428 ? 5.356   9.445   34.003  0.50 28.86 ? 428 LEU A CA    1 
ATOM   6648  C  CA    B LEU A 1 428 ? 5.581   9.310   33.762  0.50 30.91 ? 428 LEU A CA    1 
ATOM   6649  C  C     A LEU A 1 428 ? 6.268   9.151   35.187  0.50 30.63 ? 428 LEU A C     1 
ATOM   6650  C  C     B LEU A 1 428 ? 6.301   9.016   35.071  0.50 30.57 ? 428 LEU A C     1 
ATOM   6651  O  O     A LEU A 1 428 ? 5.819   9.173   36.339  0.50 32.91 ? 428 LEU A O     1 
ATOM   6652  O  O     B LEU A 1 428 ? 5.728   9.172   36.155  0.50 32.99 ? 428 LEU A O     1 
ATOM   6653  C  CB    A LEU A 1 428 ? 4.843   8.143   33.391  0.50 30.31 ? 428 LEU A CB    1 
ATOM   6654  C  CB    B LEU A 1 428 ? 5.289   8.014   33.004  0.50 27.75 ? 428 LEU A CB    1 
ATOM   6655  C  CG    A LEU A 1 428 ? 4.035   7.260   34.350  0.50 24.49 ? 428 LEU A CG    1 
ATOM   6656  C  CG    B LEU A 1 428 ? 4.262   7.087   33.662  0.50 30.35 ? 428 LEU A CG    1 
ATOM   6657  C  CD1   A LEU A 1 428 ? 2.736   7.952   34.746  0.50 31.10 ? 428 LEU A CD1   1 
ATOM   6658  C  CD1   B LEU A 1 428 ? 2.913   7.773   33.745  0.50 25.67 ? 428 LEU A CD1   1 
ATOM   6659  C  CD2   A LEU A 1 428 ? 3.755   5.899   33.741  0.50 20.64 ? 428 LEU A CD2   1 
ATOM   6660  C  CD2   B LEU A 1 428 ? 4.149   5.770   32.909  0.50 26.49 ? 428 LEU A CD2   1 
ATOM   6661  N  N     A GLU A 1 429 ? 7.546   8.853   34.929  0.50 26.40 ? 429 GLU A N     1 
ATOM   6662  N  N     B GLU A 1 429 ? 7.566   8.585   34.988  0.50 25.48 ? 429 GLU A N     1 
ATOM   6663  C  CA    A GLU A 1 429 ? 8.489   8.695   36.032  0.50 32.39 ? 429 GLU A CA    1 
ATOM   6664  C  CA    B GLU A 1 429 ? 8.358   8.370   36.195  0.50 31.84 ? 429 GLU A CA    1 
ATOM   6665  C  C     A GLU A 1 429 ? 8.568   9.970   36.864  0.50 33.98 ? 429 GLU A C     1 
ATOM   6666  C  C     B GLU A 1 429 ? 8.442   9.640   37.030  0.50 34.10 ? 429 GLU A C     1 
ATOM   6667  O  O     A GLU A 1 429 ? 8.665   9.912   38.095  0.50 34.50 ? 429 GLU A O     1 
ATOM   6668  O  O     B GLU A 1 429 ? 8.404   9.585   38.265  0.50 34.78 ? 429 GLU A O     1 
ATOM   6669  C  CB    A GLU A 1 429 ? 9.875   8.306   35.510  0.50 29.60 ? 429 GLU A CB    1 
ATOM   6670  C  CB    B GLU A 1 429 ? 9.767   7.889   35.836  0.50 30.39 ? 429 GLU A CB    1 
ATOM   6671  C  CG    A GLU A 1 429 ? 9.989   6.858   35.032  0.50 33.00 ? 429 GLU A CG    1 
ATOM   6672  C  CG    B GLU A 1 429 ? 9.840   6.522   35.166  0.50 31.63 ? 429 GLU A CG    1 
ATOM   6673  C  CD    A GLU A 1 429 ? 11.434  6.393   34.891  0.50 35.06 ? 429 GLU A CD    1 
ATOM   6674  C  CD    B GLU A 1 429 ? 11.168  5.834   35.428  0.50 34.79 ? 429 GLU A CD    1 
ATOM   6675  O  OE1   A GLU A 1 429 ? 12.284  6.805   35.710  0.50 28.90 ? 429 GLU A OE1   1 
ATOM   6676  O  OE1   B GLU A 1 429 ? 11.523  5.668   36.611  0.50 45.48 ? 429 GLU A OE1   1 
ATOM   6677  O  OE2   A GLU A 1 429 ? 11.720  5.611   33.958  0.50 34.37 ? 429 GLU A OE2   1 
ATOM   6678  O  OE2   B GLU A 1 429 ? 11.868  5.478   34.458  0.50 35.35 ? 429 GLU A OE2   1 
ATOM   6679  N  N     A LYS A 1 430 ? 8.513   11.132  36.210  0.50 34.10 ? 430 LYS A N     1 
ATOM   6680  N  N     B LYS A 1 430 ? 8.571   10.793  36.370  0.50 33.52 ? 430 LYS A N     1 
ATOM   6681  C  CA    A LYS A 1 430 ? 8.430   12.384  36.954  0.50 37.54 ? 430 LYS A CA    1 
ATOM   6682  C  CA    B LYS A 1 430 ? 8.624   12.064  37.084  0.50 37.82 ? 430 LYS A CA    1 
ATOM   6683  C  C     A LYS A 1 430 ? 7.080   12.539  37.643  0.50 36.66 ? 430 LYS A C     1 
ATOM   6684  C  C     B LYS A 1 430 ? 7.352   12.299  37.891  0.50 37.37 ? 430 LYS A C     1 
ATOM   6685  O  O     A LYS A 1 430 ? 6.997   13.181  38.697  0.50 34.36 ? 430 LYS A O     1 
ATOM   6686  O  O     B LYS A 1 430 ? 7.412   12.775  39.031  0.50 32.76 ? 430 LYS A O     1 
ATOM   6687  C  CB    A LYS A 1 430 ? 8.689   13.571  36.026  0.50 38.27 ? 430 LYS A CB    1 
ATOM   6688  C  CB    B LYS A 1 430 ? 8.855   13.203  36.091  0.50 38.15 ? 430 LYS A CB    1 
ATOM   6689  C  CG    A LYS A 1 430 ? 10.045  13.540  35.344  0.50 37.51 ? 430 LYS A CG    1 
ATOM   6690  C  CG    B LYS A 1 430 ? 8.856   14.596  36.696  0.50 37.40 ? 430 LYS A CG    1 
ATOM   6691  C  CD    A LYS A 1 430 ? 11.167  13.358  36.353  0.50 41.78 ? 430 LYS A CD    1 
ATOM   6692  C  CD    B LYS A 1 430 ? 9.152   15.633  35.626  0.50 34.21 ? 430 LYS A CD    1 
ATOM   6693  C  CE    A LYS A 1 430 ? 12.471  13.014  35.651  0.50 42.62 ? 430 LYS A CE    1 
ATOM   6694  C  CE    B LYS A 1 430 ? 8.128   15.570  34.499  0.50 42.15 ? 430 LYS A CE    1 
ATOM   6695  N  NZ    A LYS A 1 430 ? 12.307  11.812  34.782  0.50 36.15 ? 430 LYS A NZ    1 
ATOM   6696  N  NZ    B LYS A 1 430 ? 8.658   16.147  33.229  0.50 42.62 ? 430 LYS A NZ    1 
ATOM   6697  N  N     A ASP A 1 431 ? 6.016   11.966  37.070  0.50 32.51 ? 431 ASP A N     1 
ATOM   6698  N  N     B ASP A 1 431 ? 6.191   11.965  37.317  0.50 33.27 ? 431 ASP A N     1 
ATOM   6699  C  CA    A ASP A 1 431 ? 4.703   12.040  37.708  0.50 34.80 ? 431 ASP A CA    1 
ATOM   6700  C  CA    B ASP A 1 431 ? 4.933   12.125  38.044  0.50 33.61 ? 431 ASP A CA    1 
ATOM   6701  C  C     A ASP A 1 431 ? 4.723   11.414  39.095  0.50 32.56 ? 431 ASP A C     1 
ATOM   6702  C  C     B ASP A 1 431 ? 4.926   11.307  39.328  0.50 33.51 ? 431 ASP A C     1 
ATOM   6703  O  O     A ASP A 1 431 ? 4.142   11.961  40.040  0.50 37.57 ? 431 ASP A O     1 
ATOM   6704  O  O     B ASP A 1 431 ? 4.363   11.736  40.343  0.50 38.28 ? 431 ASP A O     1 
ATOM   6705  C  CB    A ASP A 1 431 ? 3.647   11.351  36.843  0.50 35.13 ? 431 ASP A CB    1 
ATOM   6706  C  CB    B ASP A 1 431 ? 3.754   11.728  37.157  0.50 34.84 ? 431 ASP A CB    1 
ATOM   6707  C  CG    A ASP A 1 431 ? 3.268   12.159  35.623  0.50 34.19 ? 431 ASP A CG    1 
ATOM   6708  C  CG    B ASP A 1 431 ? 3.538   12.693  36.010  0.50 35.34 ? 431 ASP A CG    1 
ATOM   6709  O  OD1   A ASP A 1 431 ? 3.370   13.401  35.679  0.50 39.92 ? 431 ASP A OD1   1 
ATOM   6710  O  OD1   B ASP A 1 431 ? 4.407   13.561  35.787  0.50 41.61 ? 431 ASP A OD1   1 
ATOM   6711  O  OD2   A ASP A 1 431 ? 2.857   11.554  34.609  0.50 32.08 ? 431 ASP A OD2   1 
ATOM   6712  O  OD2   B ASP A 1 431 ? 2.493   12.592  35.333  0.50 31.01 ? 431 ASP A OD2   1 
ATOM   6713  N  N     A TYR A 1 432 ? 5.375   10.257  39.235  0.50 33.80 ? 432 TYR A N     1 
ATOM   6714  N  N     B TYR A 1 432 ? 5.537   10.119  39.302  0.50 33.45 ? 432 TYR A N     1 
ATOM   6715  C  CA    A TYR A 1 432 ? 5.384   9.559   40.515  0.50 28.87 ? 432 TYR A CA    1 
ATOM   6716  C  CA    B TYR A 1 432 ? 5.651   9.326   40.521  0.50 29.67 ? 432 TYR A CA    1 
ATOM   6717  C  C     A TYR A 1 432 ? 6.348   10.193  41.510  0.50 34.43 ? 432 TYR A C     1 
ATOM   6718  C  C     B TYR A 1 432 ? 6.539   10.019  41.547  0.50 34.53 ? 432 TYR A C     1 
ATOM   6719  O  O     A TYR A 1 432 ? 6.075   10.188  42.717  0.50 35.65 ? 432 TYR A O     1 
ATOM   6720  O  O     B TYR A 1 432 ? 6.208   10.059  42.738  0.50 35.72 ? 432 TYR A O     1 
ATOM   6721  C  CB    A TYR A 1 432 ? 5.731   8.086   40.302  0.50 30.13 ? 432 TYR A CB    1 
ATOM   6722  C  CB    B TYR A 1 432 ? 6.194   7.934   40.199  0.50 28.11 ? 432 TYR A CB    1 
ATOM   6723  C  CG    A TYR A 1 432 ? 4.595   7.273   39.716  0.50 27.64 ? 432 TYR A CG    1 
ATOM   6724  C  CG    B TYR A 1 432 ? 5.158   6.976   39.656  0.50 26.85 ? 432 TYR A CG    1 
ATOM   6725  C  CD1   A TYR A 1 432 ? 4.436   7.154   38.340  0.50 27.00 ? 432 TYR A CD1   1 
ATOM   6726  C  CD1   B TYR A 1 432 ? 4.116   6.523   40.459  0.50 30.22 ? 432 TYR A CD1   1 
ATOM   6727  C  CD2   A TYR A 1 432 ? 3.679   6.629   40.540  0.50 30.12 ? 432 TYR A CD2   1 
ATOM   6728  C  CD2   B TYR A 1 432 ? 5.229   6.509   38.347  0.50 29.32 ? 432 TYR A CD2   1 
ATOM   6729  C  CE1   A TYR A 1 432 ? 3.400   6.410   37.800  0.50 29.49 ? 432 TYR A CE1   1 
ATOM   6730  C  CE1   B TYR A 1 432 ? 3.167   5.644   39.971  0.50 29.85 ? 432 TYR A CE1   1 
ATOM   6731  C  CE2   A TYR A 1 432 ? 2.637   5.885   40.009  0.50 29.44 ? 432 TYR A CE2   1 
ATOM   6732  C  CE2   B TYR A 1 432 ? 4.283   5.628   37.849  0.50 29.16 ? 432 TYR A CE2   1 
ATOM   6733  C  CZ    A TYR A 1 432 ? 2.503   5.779   38.639  0.50 27.87 ? 432 TYR A CZ    1 
ATOM   6734  C  CZ    B TYR A 1 432 ? 3.256   5.198   38.669  0.50 27.13 ? 432 TYR A CZ    1 
ATOM   6735  O  OH    A TYR A 1 432 ? 1.470   5.040   38.108  0.50 24.37 ? 432 TYR A OH    1 
ATOM   6736  O  OH    B TYR A 1 432 ? 2.310   4.325   38.183  0.50 27.17 ? 432 TYR A OH    1 
ATOM   6737  N  N     A GLU A 1 433 ? 7.470   10.738  41.032  0.50 36.93 ? 433 GLU A N     1 
ATOM   6738  N  N     B GLU A 1 433 ? 7.674   10.570  41.101  0.50 36.27 ? 433 GLU A N     1 
ATOM   6739  C  CA    A GLU A 1 433 ? 8.380   11.448  41.925  0.50 39.33 ? 433 GLU A CA    1 
ATOM   6740  C  CA    B GLU A 1 433 ? 8.567   11.274  42.016  0.50 39.55 ? 433 GLU A CA    1 
ATOM   6741  C  C     A GLU A 1 433 ? 7.730   12.708  42.484  0.50 37.96 ? 433 GLU A C     1 
ATOM   6742  C  C     B GLU A 1 433 ? 7.878   12.476  42.646  0.50 38.51 ? 433 GLU A C     1 
ATOM   6743  O  O     A GLU A 1 433 ? 7.884   13.020  43.670  0.50 43.96 ? 433 GLU A O     1 
ATOM   6744  O  O     B GLU A 1 433 ? 8.014   12.716  43.852  0.50 43.51 ? 433 GLU A O     1 
ATOM   6745  C  CB    A GLU A 1 433 ? 9.676   11.794  41.192  0.50 38.83 ? 433 GLU A CB    1 
ATOM   6746  C  CB    B GLU A 1 433 ? 9.833   11.719  41.286  0.50 38.75 ? 433 GLU A CB    1 
ATOM   6747  C  CG    A GLU A 1 433 ? 10.436  10.584  40.684  0.50 40.38 ? 433 GLU A CG    1 
ATOM   6748  C  CG    B GLU A 1 433 ? 10.569  10.603  40.580  0.50 40.50 ? 433 GLU A CG    1 
ATOM   6749  C  CD    A GLU A 1 433 ? 11.666  10.959  39.879  0.50 50.98 ? 433 GLU A CD    1 
ATOM   6750  C  CD    B GLU A 1 433 ? 11.951  11.022  40.115  0.50 50.82 ? 433 GLU A CD    1 
ATOM   6751  O  OE1   A GLU A 1 433 ? 11.958  12.170  39.765  0.50 47.03 ? 433 GLU A OE1   1 
ATOM   6752  O  OE1   B GLU A 1 433 ? 12.285  12.220  40.238  0.50 48.13 ? 433 GLU A OE1   1 
ATOM   6753  O  OE2   A GLU A 1 433 ? 12.336  10.041  39.358  0.50 47.64 ? 433 GLU A OE2   1 
ATOM   6754  O  OE2   B GLU A 1 433 ? 12.707  10.149  39.638  0.50 49.24 ? 433 GLU A OE2   1 
ATOM   6755  N  N     A GLU A 1 434 ? 6.993   13.441  41.644  0.50 38.85 ? 434 GLU A N     1 
ATOM   6756  N  N     B GLU A 1 434 ? 7.132   13.244  41.848  0.50 38.23 ? 434 GLU A N     1 
ATOM   6757  C  CA    A GLU A 1 434 ? 6.331   14.660  42.106  0.50 39.77 ? 434 GLU A CA    1 
ATOM   6758  C  CA    B GLU A 1 434 ? 6.463   14.427  42.380  0.50 39.64 ? 434 GLU A CA    1 
ATOM   6759  C  C     A GLU A 1 434 ? 5.302   14.358  43.188  0.50 40.27 ? 434 GLU A C     1 
ATOM   6760  C  C     B GLU A 1 434 ? 5.437   14.061  43.446  0.50 40.59 ? 434 GLU A C     1 
ATOM   6761  O  O     A GLU A 1 434 ? 5.198   15.092  44.178  0.50 40.99 ? 434 GLU A O     1 
ATOM   6762  O  O     B GLU A 1 434 ? 5.194   14.849  44.366  0.50 41.79 ? 434 GLU A O     1 
ATOM   6763  C  CB    A GLU A 1 434 ? 5.667   15.377  40.931  0.50 42.41 ? 434 GLU A CB    1 
ATOM   6764  C  CB    B GLU A 1 434 ? 5.810   15.219  41.246  0.50 42.19 ? 434 GLU A CB    1 
ATOM   6765  C  CG    A GLU A 1 434 ? 6.636   16.030  39.961  0.50 47.33 ? 434 GLU A CG    1 
ATOM   6766  C  CG    B GLU A 1 434 ? 6.806   15.747  40.219  0.50 46.26 ? 434 GLU A CG    1 
ATOM   6767  C  CD    A GLU A 1 434 ? 5.932   16.644  38.763  0.50 48.81 ? 434 GLU A CD    1 
ATOM   6768  C  CD    B GLU A 1 434 ? 6.198   16.770  39.276  0.50 50.32 ? 434 GLU A CD    1 
ATOM   6769  O  OE1   A GLU A 1 434 ? 4.692   16.514  38.667  0.50 44.45 ? 434 GLU A OE1   1 
ATOM   6770  O  OE1   B GLU A 1 434 ? 5.128   17.327  39.605  0.50 43.09 ? 434 GLU A OE1   1 
ATOM   6771  O  OE2   A GLU A 1 434 ? 6.619   17.255  37.917  0.50 51.82 ? 434 GLU A OE2   1 
ATOM   6772  O  OE2   B GLU A 1 434 ? 6.794   17.020  38.205  0.50 52.24 ? 434 GLU A OE2   1 
ATOM   6773  N  N     A VAL A 1 435 ? 4.531   13.282  43.014  0.50 39.23 ? 435 VAL A N     1 
ATOM   6774  N  N     B VAL A 1 435 ? 4.831   12.876  43.346  0.50 37.32 ? 435 VAL A N     1 
ATOM   6775  C  CA    A VAL A 1 435 ? 3.492   12.931  43.979  0.50 35.48 ? 435 VAL A CA    1 
ATOM   6776  C  CA    B VAL A 1 435 ? 3.978   12.390  44.425  0.50 36.29 ? 435 VAL A CA    1 
ATOM   6777  C  C     A VAL A 1 435 ? 4.101   12.589  45.332  0.50 41.59 ? 435 VAL A C     1 
ATOM   6778  C  C     B VAL A 1 435 ? 4.826   11.852  45.571  0.50 40.41 ? 435 VAL A C     1 
ATOM   6779  O  O     A VAL A 1 435 ? 3.489   12.836  46.381  0.50 38.41 ? 435 VAL A O     1 
ATOM   6780  O  O     B VAL A 1 435 ? 4.482   12.021  46.747  0.50 40.64 ? 435 VAL A O     1 
ATOM   6781  C  CB    A VAL A 1 435 ? 2.632   11.777  43.419  0.50 36.41 ? 435 VAL A CB    1 
ATOM   6782  C  CB    B VAL A 1 435 ? 2.993   11.330  43.896  0.50 34.56 ? 435 VAL A CB    1 
ATOM   6783  C  CG1   A VAL A 1 435 ? 2.470   10.664  44.440  0.50 38.05 ? 435 VAL A CG1   1 
ATOM   6784  C  CG1   B VAL A 1 435 ? 2.118   10.809  45.023  0.50 40.19 ? 435 VAL A CG1   1 
ATOM   6785  C  CG2   A VAL A 1 435 ? 1.276   12.297  42.963  0.50 34.51 ? 435 VAL A CG2   1 
ATOM   6786  C  CG2   B VAL A 1 435 ? 2.133   11.910  42.784  0.50 33.51 ? 435 VAL A CG2   1 
ATOM   6787  N  N     A GLY A 1 436 ? 5.311   12.041  45.338  0.50 42.64 ? 436 GLY A N     1 
ATOM   6788  N  N     B GLY A 1 436 ? 5.947   11.206  45.251  0.50 41.95 ? 436 GLY A N     1 
ATOM   6789  C  CA    A GLY A 1 436 ? 5.974   11.661  46.571  0.50 41.90 ? 436 GLY A CA    1 
ATOM   6790  C  CA    B GLY A 1 436 ? 6.867   10.743  46.269  0.50 38.52 ? 436 GLY A CA    1 
ATOM   6791  C  C     A GLY A 1 436 ? 6.297   10.182  46.626  0.50 41.62 ? 436 GLY A C     1 
ATOM   6792  C  C     B GLY A 1 436 ? 7.354   9.321   46.081  0.50 41.90 ? 436 GLY A C     1 
ATOM   6793  O  O     A GLY A 1 436 ? 5.621   9.415   47.314  0.50 47.77 ? 436 GLY A O     1 
ATOM   6794  O  O     B GLY A 1 436 ? 6.636   8.367   46.395  0.50 36.48 ? 436 GLY A O     1 
ATOM   6795  N  N     B VAL A 1 437 ? 8.576   9.170   45.575  0.50 41.56 ? 437 VAL A N     1 
ATOM   6796  C  CA    A VAL A 1 437 ? 8.575   7.665   45.817  0.50 46.40 ? 437 VAL A CA    1 
ATOM   6797  C  CA    B VAL A 1 437 ? 9.217   7.862   45.462  0.50 46.74 ? 437 VAL A CA    1 
ATOM   6798  C  C     A VAL A 1 437 ? 8.577   7.063   47.219  0.50 46.82 ? 437 VAL A C     1 
ATOM   6799  C  C     B VAL A 1 437 ? 10.696  8.038   45.139  0.50 51.24 ? 437 VAL A C     1 
ATOM   6800  O  O     A VAL A 1 437 ? 8.625   7.784   48.218  0.50 45.04 ? 437 VAL A O     1 
ATOM   6801  O  O     B VAL A 1 437 ? 11.409  8.768   45.829  0.50 53.97 ? 437 VAL A O     1 
ATOM   6802  C  CB    A VAL A 1 437 ? 9.883   7.351   45.065  0.50 45.70 ? 437 VAL A CB    1 
ATOM   6803  C  CB    B VAL A 1 437 ? 8.531   6.975   44.401  0.50 44.82 ? 437 VAL A CB    1 
ATOM   6804  C  CG1   A VAL A 1 437 ? 11.082  7.576   45.975  0.50 48.71 ? 437 VAL A CG1   1 
ATOM   6805  C  CG1   B VAL A 1 437 ? 8.604   7.622   43.033  0.50 37.51 ? 437 VAL A CG1   1 
ATOM   6806  C  CG2   A VAL A 1 437 ? 9.864   5.924   44.536  0.50 45.69 ? 437 VAL A CG2   1 
ATOM   6807  C  CG2   B VAL A 1 437 ? 9.161   5.588   44.381  0.50 43.59 ? 437 VAL A CG2   1 
ATOM   6808  N  N     A MET B 2 1   ? 1.711   -17.639 8.796   0.50 37.34 ? 1   MET B N     1 
ATOM   6809  N  N     B MET B 2 1   ? 3.551   -18.090 10.720  0.50 39.77 ? 1   MET B N     1 
ATOM   6810  C  CA    A MET B 2 1   ? 3.019   -18.068 8.303   0.50 46.53 ? 1   MET B CA    1 
ATOM   6811  C  CA    B MET B 2 1   ? 2.703   -18.488 9.603   0.50 37.69 ? 1   MET B CA    1 
ATOM   6812  C  C     A MET B 2 1   ? 3.109   -19.585 8.207   0.50 45.37 ? 1   MET B C     1 
ATOM   6813  C  C     B MET B 2 1   ? 3.008   -19.922 9.181   0.50 44.41 ? 1   MET B C     1 
ATOM   6814  O  O     A MET B 2 1   ? 3.339   -20.261 9.211   0.50 44.60 ? 1   MET B O     1 
ATOM   6815  O  O     B MET B 2 1   ? 3.060   -20.816 10.025  0.50 46.54 ? 1   MET B O     1 
ATOM   6816  C  CB    A MET B 2 1   ? 4.137   -17.550 9.211   0.50 45.37 ? 1   MET B CB    1 
ATOM   6817  C  CB    B MET B 2 1   ? 2.882   -17.524 8.428   0.50 46.56 ? 1   MET B CB    1 
ATOM   6818  C  CG    A MET B 2 1   ? 4.293   -16.048 9.212   0.50 42.67 ? 1   MET B CG    1 
ATOM   6819  C  CG    B MET B 2 1   ? 3.955   -16.475 8.666   0.50 42.31 ? 1   MET B CG    1 
ATOM   6820  S  SD    A MET B 2 1   ? 5.448   -15.399 8.002   0.50 47.30 ? 1   MET B SD    1 
ATOM   6821  S  SD    B MET B 2 1   ? 3.912   -15.100 7.503   0.50 52.52 ? 1   MET B SD    1 
ATOM   6822  C  CE    A MET B 2 1   ? 5.037   -13.664 8.106   0.50 39.48 ? 1   MET B CE    1 
ATOM   6823  C  CE    B MET B 2 1   ? 2.766   -15.713 6.278   0.50 31.81 ? 1   MET B CE    1 
ATOM   6824  N  N     A ARG B 2 2   ? 2.940   -20.123 6.999   0.50 38.45 ? 2   ARG B N     1 
ATOM   6825  N  N     B ARG B 2 2   ? 3.221   -20.149 7.882   0.50 42.28 ? 2   ARG B N     1 
ATOM   6826  C  CA    A ARG B 2 2   ? 2.998   -21.568 6.830   0.50 42.91 ? 2   ARG B CA    1 
ATOM   6827  C  CA    B ARG B 2 2   ? 3.327   -21.521 7.401   0.50 42.42 ? 2   ARG B CA    1 
ATOM   6828  C  C     A ARG B 2 2   ? 3.913   -21.985 5.681   0.50 39.14 ? 2   ARG B C     1 
ATOM   6829  C  C     B ARG B 2 2   ? 4.315   -21.715 6.250   0.50 38.60 ? 2   ARG B C     1 
ATOM   6830  O  O     A ARG B 2 2   ? 4.846   -22.767 5.887   0.50 45.61 ? 2   ARG B O     1 
ATOM   6831  O  O     B ARG B 2 2   ? 5.523   -21.828 6.482   0.50 37.56 ? 2   ARG B O     1 
ATOM   6832  C  CB    A ARG B 2 2   ? 1.591   -22.136 6.621   0.50 32.29 ? 2   ARG B CB    1 
ATOM   6833  C  CB    B ARG B 2 2   ? 1.935   -22.027 7.002   0.50 33.18 ? 2   ARG B CB    1 
ATOM   6834  C  CG    A ARG B 2 2   ? 0.684   -21.993 7.834   0.50 50.85 ? 2   ARG B CG    1 
ATOM   6835  C  CG    B ARG B 2 2   ? 0.986   -20.942 6.518   0.50 38.18 ? 2   ARG B CG    1 
ATOM   6836  C  CD    A ARG B 2 2   ? 1.263   -22.707 9.049   0.50 48.64 ? 2   ARG B CD    1 
ATOM   6837  C  CD    B ARG B 2 2   ? -0.410  -21.124 7.098   0.50 44.76 ? 2   ARG B CD    1 
ATOM   6838  N  NE    A ARG B 2 2   ? 0.581   -22.329 10.282  0.50 56.64 ? 2   ARG B NE    1 
ATOM   6839  N  NE    B ARG B 2 2   ? -0.488  -20.651 8.476   0.50 45.50 ? 2   ARG B NE    1 
ATOM   6840  C  CZ    A ARG B 2 2   ? 0.867   -22.821 11.480  0.50 51.59 ? 2   ARG B CZ    1 
ATOM   6841  C  CZ    B ARG B 2 2   ? -1.562  -20.750 9.248   0.50 47.42 ? 2   ARG B CZ    1 
ATOM   6842  N  NH1   A ARG B 2 2   ? 1.812   -23.734 11.646  0.50 56.00 ? 2   ARG B NH1   1 
ATOM   6843  N  NH1   B ARG B 2 2   ? -2.673  -21.327 8.819   0.50 55.70 ? 2   ARG B NH1   1 
ATOM   6844  N  NH2   A ARG B 2 2   ? 0.189   -22.387 12.539  0.50 48.80 ? 2   ARG B NH2   1 
ATOM   6845  N  NH2   B ARG B 2 2   ? -1.521  -20.258 10.483  0.50 40.20 ? 2   ARG B NH2   1 
ATOM   6846  N  N     A GLU B 2 3   ? 3.674   -21.467 4.479   0.50 36.00 ? 3   GLU B N     1 
ATOM   6847  N  N     B GLU B 2 3   ? 3.816   -21.751 5.015   0.50 37.88 ? 3   GLU B N     1 
ATOM   6848  C  CA    A GLU B 2 3   ? 4.298   -22.012 3.279   0.50 35.73 ? 3   GLU B CA    1 
ATOM   6849  C  CA    B GLU B 2 3   ? 4.535   -22.395 3.918   0.50 34.50 ? 3   GLU B CA    1 
ATOM   6850  C  C     A GLU B 2 3   ? 5.674   -21.405 3.026   0.50 33.29 ? 3   GLU B C     1 
ATOM   6851  C  C     B GLU B 2 3   ? 5.846   -21.694 3.577   0.50 31.68 ? 3   GLU B C     1 
ATOM   6852  O  O     A GLU B 2 3   ? 5.888   -20.205 3.224   0.50 32.45 ? 3   GLU B O     1 
ATOM   6853  O  O     B GLU B 2 3   ? 5.954   -20.466 3.628   0.50 32.95 ? 3   GLU B O     1 
ATOM   6854  C  CB    A GLU B 2 3   ? 3.403   -21.786 2.057   0.50 29.96 ? 3   GLU B CB    1 
ATOM   6855  C  CB    B GLU B 2 3   ? 3.658   -22.453 2.665   0.50 35.11 ? 3   GLU B CB    1 
ATOM   6856  C  CG    A GLU B 2 3   ? 1.898   -21.893 2.329   0.50 41.68 ? 3   GLU B CG    1 
ATOM   6857  C  CG    B GLU B 2 3   ? 2.388   -23.274 2.824   0.50 39.29 ? 3   GLU B CG    1 
ATOM   6858  C  CD    A GLU B 2 3   ? 1.423   -23.311 2.613   0.50 43.65 ? 3   GLU B CD    1 
ATOM   6859  C  CD    B GLU B 2 3   ? 1.267   -22.496 3.484   0.50 39.97 ? 3   GLU B CD    1 
ATOM   6860  O  OE1   A GLU B 2 3   ? 2.232   -24.258 2.496   0.50 44.01 ? 3   GLU B OE1   1 
ATOM   6861  O  OE1   B GLU B 2 3   ? 1.262   -21.252 3.373   0.50 34.98 ? 3   GLU B OE1   1 
ATOM   6862  O  OE2   A GLU B 2 3   ? 0.228   -23.475 2.951   0.50 37.21 ? 3   GLU B OE2   1 
ATOM   6863  O  OE2   B GLU B 2 3   ? 0.394   -23.128 4.114   0.50 42.52 ? 3   GLU B OE2   1 
ATOM   6864  N  N     A ILE B 2 4   ? 6.598   -22.251 2.566   0.50 36.18 ? 4   ILE B N     1 
ATOM   6865  N  N     B ILE B 2 4   ? 6.839   -22.496 3.197   0.50 35.17 ? 4   ILE B N     1 
ATOM   6866  C  CA    A ILE B 2 4   ? 7.957   -21.863 2.202   0.50 31.16 ? 4   ILE B CA    1 
ATOM   6867  C  CA    B ILE B 2 4   ? 8.130   -22.016 2.718   0.50 32.60 ? 4   ILE B CA    1 
ATOM   6868  C  C     A ILE B 2 4   ? 8.242   -22.411 0.810   0.50 31.32 ? 4   ILE B C     1 
ATOM   6869  C  C     B ILE B 2 4   ? 8.380   -22.629 1.347   0.50 33.09 ? 4   ILE B C     1 
ATOM   6870  O  O     A ILE B 2 4   ? 7.868   -23.546 0.499   0.50 34.62 ? 4   ILE B O     1 
ATOM   6871  O  O     B ILE B 2 4   ? 8.217   -23.841 1.167   0.50 34.53 ? 4   ILE B O     1 
ATOM   6872  C  CB    A ILE B 2 4   ? 8.989   -22.396 3.224   0.50 28.11 ? 4   ILE B CB    1 
ATOM   6873  C  CB    B ILE B 2 4   ? 9.271   -22.378 3.688   0.50 30.09 ? 4   ILE B CB    1 
ATOM   6874  C  CG1   A ILE B 2 4   ? 8.870   -21.649 4.556   0.50 33.46 ? 4   ILE B CG1   1 
ATOM   6875  C  CG1   B ILE B 2 4   ? 9.081   -21.665 5.030   0.50 31.81 ? 4   ILE B CG1   1 
ATOM   6876  C  CG2   A ILE B 2 4   ? 10.409  -22.308 2.673   0.50 31.58 ? 4   ILE B CG2   1 
ATOM   6877  C  CG2   B ILE B 2 4   ? 10.629  -22.030 3.079   0.50 31.38 ? 4   ILE B CG2   1 
ATOM   6878  C  CD1   A ILE B 2 4   ? 9.872   -22.098 5.598   0.50 36.05 ? 4   ILE B CD1   1 
ATOM   6879  C  CD1   B ILE B 2 4   ? 10.134  -22.014 6.059   0.50 36.31 ? 4   ILE B CD1   1 
ATOM   6880  N  N     A VAL B 2 5   ? 8.893   -21.610 -0.031  0.50 31.46 ? 5   VAL B N     1 
ATOM   6881  N  N     B VAL B 2 5   ? 8.770   -21.794 0.384   0.50 31.04 ? 5   VAL B N     1 
ATOM   6882  C  CA    A VAL B 2 5   ? 9.247   -22.025 -1.387  0.50 31.91 ? 5   VAL B CA    1 
ATOM   6883  C  CA    B VAL B 2 5   ? 9.155   -22.253 -0.947  0.50 34.64 ? 5   VAL B CA    1 
ATOM   6884  C  C     A VAL B 2 5   ? 10.754  -22.256 -1.417  0.50 34.51 ? 5   VAL B C     1 
ATOM   6885  C  C     B VAL B 2 5   ? 10.672  -22.337 -1.007  0.50 34.00 ? 5   VAL B C     1 
ATOM   6886  O  O     A VAL B 2 5   ? 11.544  -21.307 -1.496  0.50 35.58 ? 5   VAL B O     1 
ATOM   6887  O  O     B VAL B 2 5   ? 11.378  -21.481 -0.458  0.50 31.59 ? 5   VAL B O     1 
ATOM   6888  C  CB    A VAL B 2 5   ? 8.809   -21.002 -2.439  0.50 32.61 ? 5   VAL B CB    1 
ATOM   6889  C  CB    B VAL B 2 5   ? 8.598   -21.326 -2.044  0.50 29.96 ? 5   VAL B CB    1 
ATOM   6890  C  CG1   A VAL B 2 5   ? 9.313   -21.413 -3.810  0.50 32.52 ? 5   VAL B CG1   1 
ATOM   6891  C  CG1   B VAL B 2 5   ? 9.037   -21.799 -3.426  0.50 33.38 ? 5   VAL B CG1   1 
ATOM   6892  C  CG2   A VAL B 2 5   ? 7.300   -20.885 -2.456  0.50 38.72 ? 5   VAL B CG2   1 
ATOM   6893  C  CG2   B VAL B 2 5   ? 7.083   -21.272 -1.965  0.50 37.57 ? 5   VAL B CG2   1 
ATOM   6894  N  N     A HIS B 2 6   ? 11.150  -23.525 -1.368  0.50 34.60 ? 6   HIS B N     1 
ATOM   6895  N  N     B HIS B 2 6   ? 11.176  -23.377 -1.664  0.50 33.96 ? 6   HIS B N     1 
ATOM   6896  C  CA    A HIS B 2 6   ? 12.552  -23.923 -1.336  0.50 30.45 ? 6   HIS B CA    1 
ATOM   6897  C  CA    B HIS B 2 6   ? 12.603  -23.649 -1.751  0.50 30.84 ? 6   HIS B CA    1 
ATOM   6898  C  C     A HIS B 2 6   ? 13.094  -24.054 -2.755  0.50 29.65 ? 6   HIS B C     1 
ATOM   6899  C  C     B HIS B 2 6   ? 13.072  -23.497 -3.192  0.50 29.60 ? 6   HIS B C     1 
ATOM   6900  O  O     A HIS B 2 6   ? 12.482  -24.714 -3.599  0.50 32.44 ? 6   HIS B O     1 
ATOM   6901  O  O     B HIS B 2 6   ? 12.390  -23.924 -4.128  0.50 32.23 ? 6   HIS B O     1 
ATOM   6902  C  CB    A HIS B 2 6   ? 12.698  -25.244 -0.578  0.50 31.85 ? 6   HIS B CB    1 
ATOM   6903  C  CB    B HIS B 2 6   ? 12.914  -25.057 -1.234  0.50 30.83 ? 6   HIS B CB    1 
ATOM   6904  C  CG    A HIS B 2 6   ? 14.032  -25.900 -0.738  0.50 27.77 ? 6   HIS B CG    1 
ATOM   6905  C  CG    B HIS B 2 6   ? 14.320  -25.505 -1.487  0.50 31.40 ? 6   HIS B CG    1 
ATOM   6906  N  ND1   A HIS B 2 6   ? 15.076  -25.687 0.136   0.50 31.31 ? 6   HIS B ND1   1 
ATOM   6907  N  ND1   B HIS B 2 6   ? 15.351  -25.254 -0.608  0.50 30.16 ? 6   HIS B ND1   1 
ATOM   6908  C  CD2   A HIS B 2 6   ? 14.488  -26.776 -1.664  0.50 33.11 ? 6   HIS B CD2   1 
ATOM   6909  C  CD2   B HIS B 2 6   ? 14.862  -26.199 -2.515  0.50 32.42 ? 6   HIS B CD2   1 
ATOM   6910  C  CE1   A HIS B 2 6   ? 16.120  -26.400 -0.248  0.50 30.75 ? 6   HIS B CE1   1 
ATOM   6911  C  CE1   B HIS B 2 6   ? 16.469  -25.773 -1.084  0.50 32.99 ? 6   HIS B CE1   1 
ATOM   6912  N  NE2   A HIS B 2 6   ? 15.789  -27.070 -1.337  0.50 28.41 ? 6   HIS B NE2   1 
ATOM   6913  N  NE2   B HIS B 2 6   ? 16.200  -26.351 -2.242  0.50 30.02 ? 6   HIS B NE2   1 
ATOM   6914  N  N     A ILE B 2 7   ? 14.238  -23.420 -3.010  0.50 33.24 ? 7   ILE B N     1 
ATOM   6915  N  N     B ILE B 2 7   ? 14.227  -22.860 -3.364  0.50 29.67 ? 7   ILE B N     1 
ATOM   6916  C  CA    A ILE B 2 7   ? 14.906  -23.455 -4.305  0.50 28.75 ? 7   ILE B CA    1 
ATOM   6917  C  CA    B ILE B 2 7   ? 14.882  -22.735 -4.658  0.50 30.99 ? 7   ILE B CA    1 
ATOM   6918  C  C     A ILE B 2 7   ? 16.342  -23.922 -4.097  0.50 30.17 ? 7   ILE B C     1 
ATOM   6919  C  C     B ILE B 2 7   ? 16.332  -23.160 -4.484  0.50 31.24 ? 7   ILE B C     1 
ATOM   6920  O  O     A ILE B 2 7   ? 16.966  -23.611 -3.076  0.50 27.15 ? 7   ILE B O     1 
ATOM   6921  O  O     B ILE B 2 7   ? 17.004  -22.715 -3.548  0.50 26.67 ? 7   ILE B O     1 
ATOM   6922  C  CB    A ILE B 2 7   ? 14.877  -22.073 -4.995  0.50 30.42 ? 7   ILE B CB    1 
ATOM   6923  C  CB    B ILE B 2 7   ? 14.804  -21.298 -5.210  0.50 27.34 ? 7   ILE B CB    1 
ATOM   6924  C  CG1   A ILE B 2 7   ? 13.451  -21.523 -5.052  0.50 35.80 ? 7   ILE B CG1   1 
ATOM   6925  C  CG1   B ILE B 2 7   ? 13.358  -20.804 -5.233  0.50 37.91 ? 7   ILE B CG1   1 
ATOM   6926  C  CG2   A ILE B 2 7   ? 15.472  -22.151 -6.400  0.50 34.14 ? 7   ILE B CG2   1 
ATOM   6927  C  CG2   B ILE B 2 7   ? 15.411  -21.229 -6.605  0.50 33.72 ? 7   ILE B CG2   1 
ATOM   6928  C  CD1   A ILE B 2 7   ? 13.371  -20.107 -5.580  0.50 37.37 ? 7   ILE B CD1   1 
ATOM   6929  C  CD1   B ILE B 2 7   ? 13.222  -19.344 -5.591  0.50 37.66 ? 7   ILE B CD1   1 
ATOM   6930  N  N     A GLN B 2 8   ? 16.866  -24.679 -5.061  0.50 31.04 ? 8   GLN B N     1 
ATOM   6931  N  N     B GLN B 2 8   ? 16.816  -24.021 -5.376  0.50 33.01 ? 8   GLN B N     1 
ATOM   6932  C  CA    A GLN B 2 8   ? 18.264  -25.095 -5.051  0.50 26.93 ? 8   GLN B CA    1 
ATOM   6933  C  CA    B GLN B 2 8   ? 18.207  -24.448 -5.342  0.50 28.95 ? 8   GLN B CA    1 
ATOM   6934  C  C     A GLN B 2 8   ? 18.845  -24.886 -6.441  0.50 32.84 ? 8   GLN B C     1 
ATOM   6935  C  C     B GLN B 2 8   ? 18.822  -24.222 -6.713  0.50 30.86 ? 8   GLN B C     1 
ATOM   6936  O  O     A GLN B 2 8   ? 18.316  -25.415 -7.425  0.50 27.26 ? 8   GLN B O     1 
ATOM   6937  O  O     B GLN B 2 8   ? 18.273  -24.673 -7.723  0.50 30.47 ? 8   GLN B O     1 
ATOM   6938  C  CB    A GLN B 2 8   ? 18.411  -26.552 -4.600  0.50 30.85 ? 8   GLN B CB    1 
ATOM   6939  C  CB    B GLN B 2 8   ? 18.338  -25.914 -4.909  0.50 28.69 ? 8   GLN B CB    1 
ATOM   6940  C  CG    A GLN B 2 8   ? 17.460  -27.529 -5.272  0.50 35.51 ? 8   GLN B CG    1 
ATOM   6941  C  CG    B GLN B 2 8   ? 17.296  -26.866 -5.470  0.50 35.87 ? 8   GLN B CG    1 
ATOM   6942  C  CD    A GLN B 2 8   ? 17.391  -28.853 -4.542  0.50 33.00 ? 8   GLN B CD    1 
ATOM   6943  C  CD    B GLN B 2 8   ? 17.269  -28.184 -4.718  0.50 33.74 ? 8   GLN B CD    1 
ATOM   6944  O  OE1   A GLN B 2 8   ? 16.963  -28.917 -3.390  0.50 34.74 ? 8   GLN B OE1   1 
ATOM   6945  O  OE1   B GLN B 2 8   ? 17.097  -28.210 -3.500  0.50 35.74 ? 8   GLN B OE1   1 
ATOM   6946  N  NE2   A GLN B 2 8   ? 17.813  -29.918 -5.207  0.50 34.75 ? 8   GLN B NE2   1 
ATOM   6947  N  NE2   B GLN B 2 8   ? 17.450  -29.283 -5.438  0.50 32.17 ? 8   GLN B NE2   1 
ATOM   6948  N  N     A ALA B 2 9   ? 19.935  -24.123 -6.517  0.50 29.71 ? 9   ALA B N     1 
ATOM   6949  N  N     B ALA B 2 9   ? 19.954  -23.519 -6.742  0.50 28.95 ? 9   ALA B N     1 
ATOM   6950  C  CA    A ALA B 2 9   ? 20.490  -23.658 -7.780  0.50 33.10 ? 9   ALA B CA    1 
ATOM   6951  C  CA    B ALA B 2 9   ? 20.590  -23.085 -7.978  0.50 31.95 ? 9   ALA B CA    1 
ATOM   6952  C  C     A ALA B 2 9   ? 21.955  -24.046 -7.887  0.50 26.61 ? 9   ALA B C     1 
ATOM   6953  C  C     B ALA B 2 9   ? 22.039  -23.548 -8.010  0.50 29.13 ? 9   ALA B C     1 
ATOM   6954  O  O     A ALA B 2 9   ? 22.686  -24.041 -6.890  0.50 26.60 ? 9   ALA B O     1 
ATOM   6955  O  O     B ALA B 2 9   ? 22.780  -23.347 -7.043  0.50 24.15 ? 9   ALA B O     1 
ATOM   6956  C  CB    A ALA B 2 9   ? 20.345  -22.138 -7.915  0.50 26.80 ? 9   ALA B CB    1 
ATOM   6957  C  CB    B ALA B 2 9   ? 20.522  -21.563 -8.118  0.50 28.91 ? 9   ALA B CB    1 
ATOM   6958  N  N     A GLY B 2 10  ? 22.383  -24.365 -9.102  0.50 34.59 ? 10  GLY B N     1 
ATOM   6959  N  N     B GLY B 2 10  ? 22.444  -24.149 -9.127  0.50 34.57 ? 10  GLY B N     1 
ATOM   6960  C  CA    A GLY B 2 10  ? 23.761  -24.725 -9.355  0.50 32.13 ? 10  GLY B CA    1 
ATOM   6961  C  CA    B GLY B 2 10  ? 23.822  -24.558 -9.306  0.50 32.13 ? 10  GLY B CA    1 
ATOM   6962  C  C     A GLY B 2 10  ? 24.112  -26.102 -8.831  0.50 34.56 ? 10  GLY B C     1 
ATOM   6963  C  C     B GLY B 2 10  ? 24.120  -25.924 -8.726  0.50 34.37 ? 10  GLY B C     1 
ATOM   6964  O  O     A GLY B 2 10  ? 23.320  -26.782 -8.171  0.50 36.08 ? 10  GLY B O     1 
ATOM   6965  O  O     B GLY B 2 10  ? 23.252  -26.638 -8.216  0.50 36.12 ? 10  GLY B O     1 
ATOM   6966  N  N     A GLN B 2 11  ? 25.347  -26.510 -9.136  0.50 30.23 ? 11  GLN B N     1 
ATOM   6967  N  N     B GLN B 2 11  ? 25.402  -26.287 -8.799  0.50 30.33 ? 11  GLN B N     1 
ATOM   6968  C  CA    A GLN B 2 11  ? 25.830  -27.824 -8.726  0.50 32.72 ? 11  GLN B CA    1 
ATOM   6969  C  CA    B GLN B 2 11  ? 25.832  -27.616 -8.374  0.50 30.89 ? 11  GLN B CA    1 
ATOM   6970  C  C     A GLN B 2 11  ? 25.808  -27.977 -7.207  0.50 34.34 ? 11  GLN B C     1 
ATOM   6971  C  C     B GLN B 2 11  ? 25.739  -27.771 -6.862  0.50 35.14 ? 11  GLN B C     1 
ATOM   6972  O  O     A GLN B 2 11  ? 25.249  -28.947 -6.677  0.50 36.82 ? 11  GLN B O     1 
ATOM   6973  O  O     B GLN B 2 11  ? 25.073  -28.684 -6.359  0.50 35.05 ? 11  GLN B O     1 
ATOM   6974  C  CB    A GLN B 2 11  ? 27.236  -28.054 -9.282  0.50 32.43 ? 11  GLN B CB    1 
ATOM   6975  C  CB    B GLN B 2 11  ? 27.260  -27.882 -8.860  0.50 35.32 ? 11  GLN B CB    1 
ATOM   6976  C  CG    A GLN B 2 11  ? 27.265  -28.499 -10.743 0.50 37.55 ? 11  GLN B CG    1 
ATOM   6977  C  CG    B GLN B 2 11  ? 27.827  -29.218 -8.418  0.50 32.06 ? 11  GLN B CG    1 
ATOM   6978  C  CD    A GLN B 2 11  ? 27.495  -27.353 -11.717 0.50 37.67 ? 11  GLN B CD    1 
ATOM   6979  C  CD    B GLN B 2 11  ? 27.829  -30.254 -9.526  0.50 49.75 ? 11  GLN B CD    1 
ATOM   6980  O  OE1   A GLN B 2 11  ? 28.595  -26.794 -11.799 0.50 30.09 ? 11  GLN B OE1   1 
ATOM   6981  O  OE1   B GLN B 2 11  ? 26.783  -30.579 -10.096 0.50 51.20 ? 11  GLN B OE1   1 
ATOM   6982  N  NE2   A GLN B 2 11  ? 26.456  -26.997 -12.461 0.50 37.18 ? 11  GLN B NE2   1 
ATOM   6983  N  NE2   B GLN B 2 11  ? 29.010  -30.778 -9.841  0.50 34.78 ? 11  GLN B NE2   1 
ATOM   6984  N  N     A CYS B 2 12  ? 26.394  -27.018 -6.487  0.50 31.68 ? 12  CYS B N     1 
ATOM   6985  N  N     B CYS B 2 12  ? 26.414  -26.891 -6.115  0.50 31.46 ? 12  CYS B N     1 
ATOM   6986  C  CA    A CYS B 2 12  ? 26.469  -27.130 -5.032  0.50 30.14 ? 12  CYS B CA    1 
ATOM   6987  C  CA    B CYS B 2 12  ? 26.348  -26.963 -4.658  0.50 31.73 ? 12  CYS B CA    1 
ATOM   6988  C  C     A CYS B 2 12  ? 25.088  -27.061 -4.400  0.50 28.00 ? 12  CYS B C     1 
ATOM   6989  C  C     B CYS B 2 12  ? 24.912  -26.820 -4.175  0.50 26.41 ? 12  CYS B C     1 
ATOM   6990  O  O     A CYS B 2 12  ? 24.753  -27.874 -3.532  0.50 25.48 ? 12  CYS B O     1 
ATOM   6991  O  O     B CYS B 2 12  ? 24.451  -27.597 -3.332  0.50 29.37 ? 12  CYS B O     1 
ATOM   6992  C  CB    A CYS B 2 12  ? 27.364  -26.036 -4.456  0.50 28.03 ? 12  CYS B CB    1 
ATOM   6993  C  CB    B CYS B 2 12  ? 27.233  -25.888 -4.023  0.50 27.59 ? 12  CYS B CB    1 
ATOM   6994  S  SG    A CYS B 2 12  ? 27.180  -25.771 -2.670  0.50 34.76 ? 12  CYS B SG    1 
ATOM   6995  S  SG    B CYS B 2 12  ? 27.404  -26.052 -2.207  0.50 27.72 ? 12  CYS B SG    1 
ATOM   6996  N  N     A GLY B 2 13  ? 24.277  -26.087 -4.814  0.50 27.65 ? 13  GLY B N     1 
ATOM   6997  N  N     B GLY B 2 13  ? 24.186  -25.841 -4.719  0.50 27.67 ? 13  GLY B N     1 
ATOM   6998  C  CA    A GLY B 2 13  ? 22.951  -25.949 -4.236  0.50 28.62 ? 13  GLY B CA    1 
ATOM   6999  C  CA    B GLY B 2 13  ? 22.821  -25.602 -4.277  0.50 28.70 ? 13  GLY B CA    1 
ATOM   7000  C  C     A GLY B 2 13  ? 22.121  -27.209 -4.374  0.50 34.89 ? 13  GLY B C     1 
ATOM   7001  C  C     B GLY B 2 13  ? 21.915  -26.804 -4.468  0.50 34.88 ? 13  GLY B C     1 
ATOM   7002  O  O     A GLY B 2 13  ? 21.556  -27.706 -3.397  0.50 30.12 ? 13  GLY B O     1 
ATOM   7003  O  O     B GLY B 2 13  ? 21.033  -27.063 -3.647  0.50 32.75 ? 13  GLY B O     1 
ATOM   7004  N  N     A ASN B 2 14  ? 22.049  -27.751 -5.592  0.50 33.91 ? 14  ASN B N     1 
ATOM   7005  N  N     B ASN B 2 14  ? 22.122  -27.558 -5.547  0.50 33.82 ? 14  ASN B N     1 
ATOM   7006  C  CA    A ASN B 2 14  ? 21.300  -28.984 -5.805  0.50 37.45 ? 14  ASN B CA    1 
ATOM   7007  C  CA    B ASN B 2 14  ? 21.306  -28.745 -5.773  0.50 37.26 ? 14  ASN B CA    1 
ATOM   7008  C  C     A ASN B 2 14  ? 21.861  -30.138 -4.985  0.50 34.38 ? 14  ASN B C     1 
ATOM   7009  C  C     B ASN B 2 14  ? 21.788  -29.946 -4.971  0.50 34.34 ? 14  ASN B C     1 
ATOM   7010  O  O     A ASN B 2 14  ? 21.107  -31.027 -4.574  0.50 35.77 ? 14  ASN B O     1 
ATOM   7011  O  O     B ASN B 2 14  ? 20.972  -30.786 -4.577  0.50 35.32 ? 14  ASN B O     1 
ATOM   7012  C  CB    A ASN B 2 14  ? 21.293  -29.345 -7.288  0.50 33.44 ? 14  ASN B CB    1 
ATOM   7013  C  CB    B ASN B 2 14  ? 21.275  -29.088 -7.261  0.50 33.65 ? 14  ASN B CB    1 
ATOM   7014  C  CG    A ASN B 2 14  ? 20.304  -28.520 -8.075  0.50 35.73 ? 14  ASN B CG    1 
ATOM   7015  C  CG    B ASN B 2 14  ? 20.243  -28.286 -8.014  0.50 35.61 ? 14  ASN B CG    1 
ATOM   7016  O  OD1   A ASN B 2 14  ? 19.095  -28.728 -7.976  0.50 40.91 ? 14  ASN B OD1   1 
ATOM   7017  O  OD1   B ASN B 2 14  ? 19.044  -28.549 -7.908  0.50 40.92 ? 14  ASN B OD1   1 
ATOM   7018  N  ND2   A ASN B 2 14  ? 20.809  -27.575 -8.862  0.50 34.04 ? 14  ASN B ND2   1 
ATOM   7019  N  ND2   B ASN B 2 14  ? 20.698  -27.298 -8.778  0.50 33.95 ? 14  ASN B ND2   1 
ATOM   7020  N  N     A GLN B 2 15  ? 23.169  -30.142 -4.729  0.50 30.56 ? 15  GLN B N     1 
ATOM   7021  N  N     B GLN B 2 15  ? 23.094  -30.048 -4.718  0.50 30.50 ? 15  GLN B N     1 
ATOM   7022  C  CA    A GLN B 2 15  ? 23.763  -31.236 -3.967  0.50 34.05 ? 15  GLN B CA    1 
ATOM   7023  C  CA    B GLN B 2 15  ? 23.614  -31.206 -4.000  0.50 34.02 ? 15  GLN B CA    1 
ATOM   7024  C  C     A GLN B 2 15  ? 23.362  -31.159 -2.499  0.50 38.28 ? 15  GLN B C     1 
ATOM   7025  C  C     B GLN B 2 15  ? 23.228  -31.160 -2.526  0.50 38.25 ? 15  GLN B C     1 
ATOM   7026  O  O     A GLN B 2 15  ? 22.914  -32.152 -1.914  0.50 41.21 ? 15  GLN B O     1 
ATOM   7027  O  O     B GLN B 2 15  ? 22.673  -32.126 -1.990  0.50 41.36 ? 15  GLN B O     1 
ATOM   7028  C  CB    A GLN B 2 15  ? 25.284  -31.218 -4.119  0.50 37.40 ? 15  GLN B CB    1 
ATOM   7029  C  CB    B GLN B 2 15  ? 25.132  -31.287 -4.160  0.50 37.43 ? 15  GLN B CB    1 
ATOM   7030  C  CG    A GLN B 2 15  ? 25.941  -32.564 -3.868  0.50 41.69 ? 15  GLN B CG    1 
ATOM   7031  C  CG    B GLN B 2 15  ? 25.780  -32.438 -3.404  0.50 40.41 ? 15  GLN B CG    1 
ATOM   7032  C  CD    A GLN B 2 15  ? 25.612  -33.579 -4.947  0.50 47.96 ? 15  GLN B CD    1 
ATOM   7033  C  CD    B GLN B 2 15  ? 25.614  -33.781 -4.094  0.50 45.53 ? 15  GLN B CD    1 
ATOM   7034  O  OE1   A GLN B 2 15  ? 25.516  -34.779 -4.682  0.50 46.15 ? 15  GLN B OE1   1 
ATOM   7035  O  OE1   B GLN B 2 15  ? 25.059  -33.870 -5.190  0.50 50.04 ? 15  GLN B OE1   1 
ATOM   7036  N  NE2   A GLN B 2 15  ? 25.440  -33.100 -6.174  0.50 44.97 ? 15  GLN B NE2   1 
ATOM   7037  N  NE2   B GLN B 2 15  ? 26.103  -34.836 -3.452  0.50 43.59 ? 15  GLN B NE2   1 
ATOM   7038  N  N     A ILE B 2 16  ? 23.513  -29.986 -1.883  0.50 34.42 ? 16  ILE B N     1 
ATOM   7039  N  N     B ILE B 2 16  ? 23.512  -30.043 -1.850  0.50 34.43 ? 16  ILE B N     1 
ATOM   7040  C  CA    A ILE B 2 16  ? 23.052  -29.834 -0.509  0.50 35.38 ? 16  ILE B CA    1 
ATOM   7041  C  CA    B ILE B 2 16  ? 23.160  -29.950 -0.437  0.50 35.36 ? 16  ILE B CA    1 
ATOM   7042  C  C     A ILE B 2 16  ? 21.533  -29.721 -0.458  0.50 35.35 ? 16  ILE B C     1 
ATOM   7043  C  C     B ILE B 2 16  ? 21.648  -29.879 -0.268  0.50 35.99 ? 16  ILE B C     1 
ATOM   7044  O  O     A ILE B 2 16  ? 20.911  -30.134 0.527   0.50 34.91 ? 16  ILE B O     1 
ATOM   7045  O  O     B ILE B 2 16  ? 21.115  -30.285 0.773   0.50 34.46 ? 16  ILE B O     1 
ATOM   7046  C  CB    A ILE B 2 16  ? 23.732  -28.629 0.166   0.50 36.51 ? 16  ILE B CB    1 
ATOM   7047  C  CB    B ILE B 2 16  ? 23.864  -28.751 0.232   0.50 36.74 ? 16  ILE B CB    1 
ATOM   7048  C  CG1   A ILE B 2 16  ? 23.427  -27.334 -0.588  0.50 30.05 ? 16  ILE B CG1   1 
ATOM   7049  C  CG1   B ILE B 2 16  ? 23.108  -27.448 -0.029  0.50 33.46 ? 16  ILE B CG1   1 
ATOM   7050  C  CG2   A ILE B 2 16  ? 25.237  -28.847 0.254   0.50 34.40 ? 16  ILE B CG2   1 
ATOM   7051  C  CG2   B ILE B 2 16  ? 25.301  -28.631 -0.261  0.50 33.35 ? 16  ILE B CG2   1 
ATOM   7052  C  CD1   A ILE B 2 16  ? 24.046  -26.107 0.053   0.50 30.35 ? 16  ILE B CD1   1 
ATOM   7053  C  CD1   B ILE B 2 16  ? 23.482  -26.329 0.925   0.50 27.00 ? 16  ILE B CD1   1 
ATOM   7054  N  N     A GLY B 2 17  ? 20.911  -29.181 -1.508  0.50 35.18 ? 17  GLY B N     1 
ATOM   7055  N  N     B GLY B 2 17  ? 20.932  -29.384 -1.281  0.50 35.03 ? 17  GLY B N     1 
ATOM   7056  C  CA    A GLY B 2 17  ? 19.462  -29.110 -1.540  0.50 33.50 ? 17  GLY B CA    1 
ATOM   7057  C  CA    B GLY B 2 17  ? 19.480  -29.353 -1.202  0.50 35.25 ? 17  GLY B CA    1 
ATOM   7058  C  C     A GLY B 2 17  ? 18.799  -30.468 -1.628  0.50 35.43 ? 17  GLY B C     1 
ATOM   7059  C  C     B GLY B 2 17  ? 18.879  -30.742 -1.113  0.50 37.26 ? 17  GLY B C     1 
ATOM   7060  O  O     A GLY B 2 17  ? 17.697  -30.658 -1.107  0.50 34.96 ? 17  GLY B O     1 
ATOM   7061  O  O     B GLY B 2 17  ? 18.062  -31.024 -0.233  0.50 34.16 ? 17  GLY B O     1 
ATOM   7062  N  N     A ALA B 2 18  ? 19.449  -31.429 -2.286  0.50 37.29 ? 18  ALA B N     1 
ATOM   7063  N  N     B ALA B 2 18  ? 19.289  -31.634 -2.018  0.50 37.06 ? 18  ALA B N     1 
ATOM   7064  C  CA    A ALA B 2 18  ? 18.905  -32.782 -2.344  0.50 41.12 ? 18  ALA B CA    1 
ATOM   7065  C  CA    B ALA B 2 18  ? 18.793  -33.007 -1.988  0.50 39.94 ? 18  ALA B CA    1 
ATOM   7066  C  C     A ALA B 2 18  ? 19.135  -33.529 -1.036  0.50 42.20 ? 18  ALA B C     1 
ATOM   7067  C  C     B ALA B 2 18  ? 19.109  -33.679 -0.658  0.50 43.03 ? 18  ALA B C     1 
ATOM   7068  O  O     A ALA B 2 18  ? 18.276  -34.307 -0.602  0.50 43.37 ? 18  ALA B O     1 
ATOM   7069  O  O     B ALA B 2 18  ? 18.291  -34.444 -0.131  0.50 40.66 ? 18  ALA B O     1 
ATOM   7070  C  CB    A ALA B 2 18  ? 19.518  -33.548 -3.517  0.50 40.12 ? 18  ALA B CB    1 
ATOM   7071  C  CB    B ALA B 2 18  ? 19.385  -33.804 -3.151  0.50 43.47 ? 18  ALA B CB    1 
ATOM   7072  N  N     A LYS B 2 19  ? 20.288  -33.306 -0.398  0.50 40.13 ? 19  LYS B N     1 
ATOM   7073  N  N     B LYS B 2 19  ? 20.290  -33.403 -0.098  0.50 38.54 ? 19  LYS B N     1 
ATOM   7074  C  CA    A LYS B 2 19  ? 20.534  -33.893 0.915   0.50 36.36 ? 19  LYS B CA    1 
ATOM   7075  C  CA    B LYS B 2 19  ? 20.610  -33.898 1.236   0.50 38.05 ? 19  LYS B CA    1 
ATOM   7076  C  C     A LYS B 2 19  ? 19.565  -33.353 1.956   0.50 41.19 ? 19  LYS B C     1 
ATOM   7077  C  C     B LYS B 2 19  ? 19.619  -33.373 2.266   0.50 41.12 ? 19  LYS B C     1 
ATOM   7078  O  O     A LYS B 2 19  ? 19.184  -34.077 2.883   0.50 40.36 ? 19  LYS B O     1 
ATOM   7079  O  O     B LYS B 2 19  ? 19.197  -34.109 3.165   0.50 40.95 ? 19  LYS B O     1 
ATOM   7080  C  CB    A LYS B 2 19  ? 21.974  -33.626 1.355   0.50 38.34 ? 19  LYS B CB    1 
ATOM   7081  C  CB    B LYS B 2 19  ? 22.035  -33.500 1.622   0.50 38.41 ? 19  LYS B CB    1 
ATOM   7082  C  CG    A LYS B 2 19  ? 23.026  -34.477 0.660   0.50 45.68 ? 19  LYS B CG    1 
ATOM   7083  C  CG    B LYS B 2 19  ? 23.128  -34.242 0.872   0.50 44.81 ? 19  LYS B CG    1 
ATOM   7084  C  CD    A LYS B 2 19  ? 23.003  -35.921 1.147   0.50 44.60 ? 19  LYS B CD    1 
ATOM   7085  C  CD    B LYS B 2 19  ? 23.032  -35.745 1.087   0.50 44.68 ? 19  LYS B CD    1 
ATOM   7086  C  CE    A LYS B 2 19  ? 22.403  -36.850 0.103   0.50 44.04 ? 19  LYS B CE    1 
ATOM   7087  C  CE    B LYS B 2 19  ? 24.216  -36.466 0.460   0.50 48.52 ? 19  LYS B CE    1 
ATOM   7088  N  NZ    A LYS B 2 19  ? 22.670  -38.284 0.398   0.50 47.82 ? 19  LYS B NZ    1 
ATOM   7089  N  NZ    B LYS B 2 19  ? 23.949  -37.921 0.263   0.50 40.85 ? 19  LYS B NZ    1 
ATOM   7090  N  N     A PHE B 2 20  ? 19.165  -32.085 1.824   0.50 39.77 ? 20  PHE B N     1 
ATOM   7091  N  N     B PHE B 2 20  ? 19.235  -32.099 2.149   0.50 39.87 ? 20  PHE B N     1 
ATOM   7092  C  CA    A PHE B 2 20  ? 18.217  -31.497 2.764   0.50 37.83 ? 20  PHE B CA    1 
ATOM   7093  C  CA    B PHE B 2 20  ? 18.251  -31.530 3.065   0.50 37.40 ? 20  PHE B CA    1 
ATOM   7094  C  C     A PHE B 2 20  ? 16.897  -32.256 2.761   0.50 41.49 ? 20  PHE B C     1 
ATOM   7095  C  C     B PHE B 2 20  ? 16.899  -32.213 2.909   0.50 41.54 ? 20  PHE B C     1 
ATOM   7096  O  O     A PHE B 2 20  ? 16.347  -32.577 3.821   0.50 37.06 ? 20  PHE B O     1 
ATOM   7097  O  O     B PHE B 2 20  ? 16.265  -32.596 3.900   0.50 37.00 ? 20  PHE B O     1 
ATOM   7098  C  CB    A PHE B 2 20  ? 17.993  -30.025 2.421   0.50 37.79 ? 20  PHE B CB    1 
ATOM   7099  C  CB    B PHE B 2 20  ? 18.131  -30.024 2.824   0.50 39.45 ? 20  PHE B CB    1 
ATOM   7100  C  CG    A PHE B 2 20  ? 16.900  -29.375 3.222   0.50 39.37 ? 20  PHE B CG    1 
ATOM   7101  C  CG    B PHE B 2 20  ? 16.993  -29.378 3.564   0.50 39.15 ? 20  PHE B CG    1 
ATOM   7102  C  CD1   A PHE B 2 20  ? 16.970  -29.330 4.604   0.50 36.79 ? 20  PHE B CD1   1 
ATOM   7103  C  CD1   B PHE B 2 20  ? 17.020  -29.268 4.944   0.50 37.04 ? 20  PHE B CD1   1 
ATOM   7104  C  CD2   A PHE B 2 20  ? 15.809  -28.801 2.592   0.50 37.62 ? 20  PHE B CD2   1 
ATOM   7105  C  CD2   B PHE B 2 20  ? 15.903  -28.868 2.878   0.50 38.16 ? 20  PHE B CD2   1 
ATOM   7106  C  CE1   A PHE B 2 20  ? 15.969  -28.731 5.346   0.50 34.61 ? 20  PHE B CE1   1 
ATOM   7107  C  CE1   B PHE B 2 20  ? 15.979  -28.669 5.627   0.50 34.00 ? 20  PHE B CE1   1 
ATOM   7108  C  CE2   A PHE B 2 20  ? 14.802  -28.199 3.329   0.50 35.55 ? 20  PHE B CE2   1 
ATOM   7109  C  CE2   B PHE B 2 20  ? 14.856  -28.267 3.557   0.50 35.33 ? 20  PHE B CE2   1 
ATOM   7110  C  CZ    A PHE B 2 20  ? 14.884  -28.165 4.707   0.50 37.89 ? 20  PHE B CZ    1 
ATOM   7111  C  CZ    B PHE B 2 20  ? 14.896  -28.169 4.932   0.50 38.04 ? 20  PHE B CZ    1 
ATOM   7112  N  N     A TRP B 2 21  ? 16.373  -32.555 1.572   0.50 40.37 ? 21  TRP B N     1 
ATOM   7113  N  N     B TRP B 2 21  ? 16.442  -32.382 1.666   0.50 40.21 ? 21  TRP B N     1 
ATOM   7114  C  CA    A TRP B 2 21  ? 15.112  -33.283 1.494   0.50 38.38 ? 21  TRP B CA    1 
ATOM   7115  C  CA    B TRP B 2 21  ? 15.145  -33.003 1.431   0.50 38.59 ? 21  TRP B CA    1 
ATOM   7116  C  C     A TRP B 2 21  ? 15.268  -34.729 1.945   0.50 41.50 ? 21  TRP B C     1 
ATOM   7117  C  C     B TRP B 2 21  ? 15.138  -34.488 1.761   0.50 41.23 ? 21  TRP B C     1 
ATOM   7118  O  O     A TRP B 2 21  ? 14.335  -35.295 2.524   0.50 39.68 ? 21  TRP B O     1 
ATOM   7119  O  O     B TRP B 2 21  ? 14.061  -35.051 1.979   0.50 38.22 ? 21  TRP B O     1 
ATOM   7120  C  CB    A TRP B 2 21  ? 14.554  -33.215 0.074   0.50 37.34 ? 21  TRP B CB    1 
ATOM   7121  C  CB    B TRP B 2 21  ? 14.708  -32.782 -0.016  0.50 37.35 ? 21  TRP B CB    1 
ATOM   7122  C  CG    A TRP B 2 21  ? 14.142  -31.829 -0.333  0.50 38.63 ? 21  TRP B CG    1 
ATOM   7123  C  CG    B TRP B 2 21  ? 14.137  -31.416 -0.251  0.50 39.28 ? 21  TRP B CG    1 
ATOM   7124  C  CD1   A TRP B 2 21  ? 14.780  -31.010 -1.216  0.50 37.56 ? 21  TRP B CD1   1 
ATOM   7125  C  CD1   B TRP B 2 21  ? 14.646  -30.437 -1.053  0.50 35.86 ? 21  TRP B CD1   1 
ATOM   7126  C  CD2   A TRP B 2 21  ? 13.007  -31.096 0.147   0.50 38.82 ? 21  TRP B CD2   1 
ATOM   7127  C  CD2   B TRP B 2 21  ? 12.954  -30.870 0.347   0.50 37.84 ? 21  TRP B CD2   1 
ATOM   7128  N  NE1   A TRP B 2 21  ? 14.111  -29.815 -1.324  0.50 36.46 ? 21  TRP B NE1   1 
ATOM   7129  N  NE1   B TRP B 2 21  ? 13.847  -29.320 -1.003  0.50 34.45 ? 21  TRP B NE1   1 
ATOM   7130  C  CE2   A TRP B 2 21  ? 13.018  -29.842 -0.497  0.50 36.88 ? 21  TRP B CE2   1 
ATOM   7131  C  CE2   B TRP B 2 21  ? 12.802  -29.559 -0.150  0.50 35.86 ? 21  TRP B CE2   1 
ATOM   7132  C  CE3   A TRP B 2 21  ? 11.982  -31.380 1.053   0.50 38.84 ? 21  TRP B CE3   1 
ATOM   7133  C  CE3   B TRP B 2 21  ? 12.006  -31.364 1.248   0.50 38.79 ? 21  TRP B CE3   1 
ATOM   7134  C  CZ2   A TRP B 2 21  ? 12.045  -28.873 -0.264  0.50 37.39 ? 21  TRP B CZ2   1 
ATOM   7135  C  CZ2   B TRP B 2 21  ? 11.740  -28.737 0.223   0.50 35.82 ? 21  TRP B CZ2   1 
ATOM   7136  C  CZ3   A TRP B 2 21  ? 11.017  -30.417 1.285   0.50 38.22 ? 21  TRP B CZ3   1 
ATOM   7137  C  CZ3   B TRP B 2 21  ? 10.955  -30.546 1.621   0.50 37.27 ? 21  TRP B CZ3   1 
ATOM   7138  C  CH2   A TRP B 2 21  ? 11.053  -29.180 0.625   0.50 37.58 ? 21  TRP B CH2   1 
ATOM   7139  C  CH2   B TRP B 2 21  ? 10.828  -29.248 1.106   0.50 39.44 ? 21  TRP B CH2   1 
ATOM   7140  N  N     A GLU B 2 22  ? 16.433  -35.338 1.705   0.50 40.74 ? 22  GLU B N     1 
ATOM   7141  N  N     B GLU B 2 22  ? 16.305  -35.135 1.799   0.50 40.67 ? 22  GLU B N     1 
ATOM   7142  C  CA    A GLU B 2 22  ? 16.644  -36.717 2.135   0.50 43.34 ? 22  GLU B CA    1 
ATOM   7143  C  CA    B GLU B 2 22  ? 16.367  -36.517 2.266   0.50 43.71 ? 22  GLU B CA    1 
ATOM   7144  C  C     A GLU B 2 22  ? 16.653  -36.846 3.653   0.50 43.91 ? 22  GLU B C     1 
ATOM   7145  C  C     B GLU B 2 22  ? 16.213  -36.588 3.779   0.50 43.17 ? 22  GLU B C     1 
ATOM   7146  O  O     A GLU B 2 22  ? 16.236  -37.881 4.184   0.50 49.10 ? 22  GLU B O     1 
ATOM   7147  O  O     B GLU B 2 22  ? 15.431  -37.393 4.298   0.50 47.68 ? 22  GLU B O     1 
ATOM   7148  C  CB    A GLU B 2 22  ? 17.954  -37.263 1.566   0.50 41.81 ? 22  GLU B CB    1 
ATOM   7149  C  CB    B GLU B 2 22  ? 17.688  -37.166 1.848   0.50 40.53 ? 22  GLU B CB    1 
ATOM   7150  C  CG    A GLU B 2 22  ? 17.962  -37.457 0.060   0.50 47.01 ? 22  GLU B CG    1 
ATOM   7151  C  CG    B GLU B 2 22  ? 17.823  -37.487 0.372   0.50 46.98 ? 22  GLU B CG    1 
ATOM   7152  C  CD    A GLU B 2 22  ? 19.232  -38.131 -0.426  0.50 48.00 ? 22  GLU B CD    1 
ATOM   7153  C  CD    B GLU B 2 22  ? 19.194  -38.044 0.033   0.50 47.73 ? 22  GLU B CD    1 
ATOM   7154  O  OE1   A GLU B 2 22  ? 19.852  -38.872 0.366   0.50 50.43 ? 22  GLU B OE1   1 
ATOM   7155  O  OE1   B GLU B 2 22  ? 19.889  -38.512 0.961   0.50 49.90 ? 22  GLU B OE1   1 
ATOM   7156  O  OE2   A GLU B 2 22  ? 19.615  -37.916 -1.596  0.50 45.43 ? 22  GLU B OE2   1 
ATOM   7157  O  OE2   B GLU B 2 22  ? 19.581  -38.007 -1.155  0.50 45.59 ? 22  GLU B OE2   1 
ATOM   7158  N  N     A VAL B 2 23  ? 17.123  -35.824 4.365   0.50 43.01 ? 23  VAL B N     1 
ATOM   7159  N  N     B VAL B 2 23  ? 16.953  -35.744 4.501   0.50 42.88 ? 23  VAL B N     1 
ATOM   7160  C  CA    A VAL B 2 23  ? 17.216  -35.929 5.816   0.50 38.06 ? 23  VAL B CA    1 
ATOM   7161  C  CA    B VAL B 2 23  ? 17.069  -35.889 5.949   0.50 38.06 ? 23  VAL B CA    1 
ATOM   7162  C  C     A VAL B 2 23  ? 15.902  -35.556 6.502   0.50 44.31 ? 23  VAL B C     1 
ATOM   7163  C  C     B VAL B 2 23  ? 15.747  -35.562 6.636   0.50 44.40 ? 23  VAL B C     1 
ATOM   7164  O  O     A VAL B 2 23  ? 15.573  -36.127 7.546   0.50 42.82 ? 23  VAL B O     1 
ATOM   7165  O  O     B VAL B 2 23  ? 15.274  -36.319 7.492   0.50 42.90 ? 23  VAL B O     1 
ATOM   7166  C  CB    A VAL B 2 23  ? 18.387  -35.082 6.353   0.50 41.38 ? 23  VAL B CB    1 
ATOM   7167  C  CB    B VAL B 2 23  ? 18.219  -35.013 6.479   0.50 41.49 ? 23  VAL B CB    1 
ATOM   7168  C  CG1   A VAL B 2 23  ? 18.085  -33.593 6.265   0.50 40.71 ? 23  VAL B CG1   1 
ATOM   7169  C  CG1   B VAL B 2 23  ? 18.190  -34.954 7.996   0.50 40.43 ? 23  VAL B CG1   1 
ATOM   7170  C  CG2   A VAL B 2 23  ? 18.720  -35.476 7.785   0.50 40.07 ? 23  VAL B CG2   1 
ATOM   7171  C  CG2   B VAL B 2 23  ? 19.557  -35.553 5.993   0.50 37.58 ? 23  VAL B CG2   1 
ATOM   7172  N  N     A ILE B 2 24  ? 15.127  -34.632 5.935   0.50 43.80 ? 24  ILE B N     1 
ATOM   7173  N  N     B ILE B 2 24  ? 15.129  -34.434 6.276   0.50 44.55 ? 24  ILE B N     1 
ATOM   7174  C  CA    A ILE B 2 24  ? 13.890  -34.219 6.589   0.50 42.97 ? 24  ILE B CA    1 
ATOM   7175  C  CA    B ILE B 2 24  ? 13.897  -34.049 6.959   0.50 41.78 ? 24  ILE B CA    1 
ATOM   7176  C  C     A ILE B 2 24  ? 12.714  -35.116 6.207   0.50 42.94 ? 24  ILE B C     1 
ATOM   7177  C  C     B ILE B 2 24  ? 12.736  -34.938 6.529   0.50 43.33 ? 24  ILE B C     1 
ATOM   7178  O  O     A ILE B 2 24  ? 11.778  -35.271 6.998   0.50 44.62 ? 24  ILE B O     1 
ATOM   7179  O  O     B ILE B 2 24  ? 11.766  -35.103 7.280   0.50 44.47 ? 24  ILE B O     1 
ATOM   7180  C  CB    A ILE B 2 24  ? 13.575  -32.742 6.293   0.50 38.63 ? 24  ILE B CB    1 
ATOM   7181  C  CB    B ILE B 2 24  ? 13.578  -32.560 6.729   0.50 40.39 ? 24  ILE B CB    1 
ATOM   7182  C  CG1   A ILE B 2 24  ? 13.214  -32.542 4.821   0.50 39.70 ? 24  ILE B CG1   1 
ATOM   7183  C  CG1   B ILE B 2 24  ? 13.065  -32.327 5.307   0.50 36.36 ? 24  ILE B CG1   1 
ATOM   7184  C  CG2   A ILE B 2 24  ? 14.750  -31.860 6.689   0.50 38.55 ? 24  ILE B CG2   1 
ATOM   7185  C  CG2   B ILE B 2 24  ? 14.803  -31.705 7.017   0.50 37.92 ? 24  ILE B CG2   1 
ATOM   7186  C  CD1   A ILE B 2 24  ? 12.638  -31.174 4.518   0.50 41.53 ? 24  ILE B CD1   1 
ATOM   7187  C  CD1   B ILE B 2 24  ? 12.290  -31.033 5.142   0.50 40.28 ? 24  ILE B CD1   1 
ATOM   7188  N  N     A SER B 2 25  ? 12.732  -35.707 5.007   0.50 42.95 ? 25  SER B N     1 
ATOM   7189  N  N     B SER B 2 25  ? 12.803  -35.518 5.326   0.50 42.83 ? 25  SER B N     1 
ATOM   7190  C  CA    A SER B 2 25  ? 11.724  -36.708 4.674   0.50 41.83 ? 25  SER B CA    1 
ATOM   7191  C  CA    B SER B 2 25  ? 11.794  -36.495 4.930   0.50 42.32 ? 25  SER B CA    1 
ATOM   7192  C  C     A SER B 2 25  ? 11.829  -37.902 5.611   0.50 45.98 ? 25  SER B C     1 
ATOM   7193  C  C     B SER B 2 25  ? 11.799  -37.684 5.879   0.50 46.25 ? 25  SER B C     1 
ATOM   7194  O  O     A SER B 2 25  ? 10.812  -38.431 6.076   0.50 49.31 ? 25  SER B O     1 
ATOM   7195  O  O     B SER B 2 25  ? 10.739  -38.161 6.300   0.50 48.23 ? 25  SER B O     1 
ATOM   7196  C  CB    A SER B 2 25  ? 11.874  -37.155 3.220   0.50 44.08 ? 25  SER B CB    1 
ATOM   7197  C  CB    B SER B 2 25  ? 12.034  -36.959 3.494   0.50 43.85 ? 25  SER B CB    1 
ATOM   7198  O  OG    A SER B 2 25  ? 11.752  -36.062 2.327   0.50 42.85 ? 25  SER B OG    1 
ATOM   7199  O  OG    B SER B 2 25  ? 12.018  -35.869 2.588   0.50 43.36 ? 25  SER B OG    1 
ATOM   7200  N  N     A ASP B 2 26  ? 13.057  -38.333 5.905   0.50 46.63 ? 26  ASP B N     1 
ATOM   7201  N  N     B ASP B 2 26  ? 12.991  -38.166 6.234   0.50 47.09 ? 26  ASP B N     1 
ATOM   7202  C  CA    A ASP B 2 26  ? 13.261  -39.384 6.893   0.50 48.57 ? 26  ASP B CA    1 
ATOM   7203  C  CA    B ASP B 2 26  ? 13.099  -39.220 7.235   0.50 49.14 ? 26  ASP B CA    1 
ATOM   7204  C  C     A ASP B 2 26  ? 12.743  -38.957 8.261   0.50 49.23 ? 26  ASP B C     1 
ATOM   7205  C  C     B ASP B 2 26  ? 12.561  -38.754 8.582   0.50 49.08 ? 26  ASP B C     1 
ATOM   7206  O  O     A ASP B 2 26  ? 12.093  -39.743 8.960   0.50 46.20 ? 26  ASP B O     1 
ATOM   7207  O  O     B ASP B 2 26  ? 11.887  -39.515 9.286   0.50 45.79 ? 26  ASP B O     1 
ATOM   7208  C  CB    A ASP B 2 26  ? 14.745  -39.742 6.963   0.50 44.02 ? 26  ASP B CB    1 
ATOM   7209  C  CB    B ASP B 2 26  ? 14.554  -39.669 7.359   0.50 43.41 ? 26  ASP B CB    1 
ATOM   7210  C  CG    A ASP B 2 26  ? 15.018  -40.927 7.863   0.50 50.68 ? 26  ASP B CG    1 
ATOM   7211  C  CG    B ASP B 2 26  ? 14.740  -40.756 8.395   0.50 50.67 ? 26  ASP B CG    1 
ATOM   7212  O  OD1   A ASP B 2 26  ? 14.451  -42.009 7.605   0.50 53.69 ? 26  ASP B OD1   1 
ATOM   7213  O  OD1   B ASP B 2 26  ? 14.275  -41.890 8.155   0.50 56.11 ? 26  ASP B OD1   1 
ATOM   7214  O  OD2   A ASP B 2 26  ? 15.809  -40.780 8.819   0.50 51.17 ? 26  ASP B OD2   1 
ATOM   7215  O  OD2   B ASP B 2 26  ? 15.350  -40.476 9.448   0.50 56.08 ? 26  ASP B OD2   1 
ATOM   7216  N  N     A GLU B 2 27  ? 13.014  -37.709 8.653   0.50 49.46 ? 27  GLU B N     1 
ATOM   7217  N  N     B GLU B 2 27  ? 12.847  -37.504 8.958   0.50 50.41 ? 27  GLU B N     1 
ATOM   7218  C  CA    A GLU B 2 27  ? 12.555  -37.221 9.950   0.50 50.81 ? 27  GLU B CA    1 
ATOM   7219  C  CA    B GLU B 2 27  ? 12.329  -36.976 10.217  0.50 51.20 ? 27  GLU B CA    1 
ATOM   7220  C  C     A GLU B 2 27  ? 11.034  -37.229 10.035  0.50 45.58 ? 27  GLU B C     1 
ATOM   7221  C  C     B GLU B 2 27  ? 10.811  -36.857 10.195  0.50 46.31 ? 27  GLU B C     1 
ATOM   7222  O  O     A GLU B 2 27  ? 10.458  -37.664 11.039  0.50 51.80 ? 27  GLU B O     1 
ATOM   7223  O  O     B GLU B 2 27  ? 10.164  -37.005 11.239  0.50 52.51 ? 27  GLU B O     1 
ATOM   7224  C  CB    A GLU B 2 27  ? 13.100  -35.813 10.207  0.50 48.57 ? 27  GLU B CB    1 
ATOM   7225  C  CB    B GLU B 2 27  ? 12.956  -35.614 10.526  0.50 47.45 ? 27  GLU B CB    1 
ATOM   7226  C  CG    A GLU B 2 27  ? 14.597  -35.756 10.466  0.50 46.49 ? 27  GLU B CG    1 
ATOM   7227  C  CG    B GLU B 2 27  ? 14.447  -35.652 10.839  0.50 47.09 ? 27  GLU B CG    1 
ATOM   7228  C  CD    A GLU B 2 27  ? 15.100  -34.340 10.678  0.50 39.44 ? 27  GLU B CD    1 
ATOM   7229  C  CD    B GLU B 2 27  ? 14.945  -34.361 11.468  0.50 39.97 ? 27  GLU B CD    1 
ATOM   7230  O  OE1   A GLU B 2 27  ? 14.265  -33.414 10.744  0.50 42.94 ? 27  GLU B OE1   1 
ATOM   7231  O  OE1   B GLU B 2 27  ? 14.115  -33.468 11.737  0.50 40.24 ? 27  GLU B OE1   1 
ATOM   7232  O  OE2   A GLU B 2 27  ? 16.331  -34.152 10.780  0.50 45.71 ? 27  GLU B OE2   1 
ATOM   7233  O  OE2   B GLU B 2 27  ? 16.167  -34.238 11.697  0.50 42.02 ? 27  GLU B OE2   1 
ATOM   7234  N  N     A HIS B 2 28  ? 10.367  -36.748 8.987   0.50 45.40 ? 28  HIS B N     1 
ATOM   7235  N  N     B HIS B 2 28  ? 10.229  -36.593 9.029   0.50 45.49 ? 28  HIS B N     1 
ATOM   7236  C  CA    A HIS B 2 28  ? 8.912   -36.674 8.959   0.50 49.79 ? 28  HIS B CA    1 
ATOM   7237  C  CA    B HIS B 2 28  ? 8.793   -36.405 8.889   0.50 49.56 ? 28  HIS B CA    1 
ATOM   7238  C  C     A HIS B 2 28  ? 8.249   -37.987 8.558   0.50 49.42 ? 28  HIS B C     1 
ATOM   7239  C  C     B HIS B 2 28  ? 8.054   -37.693 8.549   0.50 49.68 ? 28  HIS B C     1 
ATOM   7240  O  O     A HIS B 2 28  ? 7.022   -38.021 8.415   0.50 46.93 ? 28  HIS B O     1 
ATOM   7241  O  O     B HIS B 2 28  ? 6.843   -37.653 8.309   0.50 46.46 ? 28  HIS B O     1 
ATOM   7242  C  CB    A HIS B 2 28  ? 8.464   -35.562 8.007   0.50 42.72 ? 28  HIS B CB    1 
ATOM   7243  C  CB    B HIS B 2 28  ? 8.507   -35.346 7.822   0.50 42.06 ? 28  HIS B CB    1 
ATOM   7244  C  CG    A HIS B 2 28  ? 8.665   -34.182 8.550   0.50 45.18 ? 28  HIS B CG    1 
ATOM   7245  C  CG    B HIS B 2 28  ? 8.983   -33.976 8.190   0.50 45.48 ? 28  HIS B CG    1 
ATOM   7246  N  ND1   A HIS B 2 28  ? 7.708   -33.533 9.301   0.50 39.89 ? 28  HIS B ND1   1 
ATOM   7247  N  ND1   B HIS B 2 28  ? 9.141   -32.968 7.263   0.50 39.51 ? 28  HIS B ND1   1 
ATOM   7248  C  CD2   A HIS B 2 28  ? 9.707   -33.324 8.446   0.50 40.26 ? 28  HIS B CD2   1 
ATOM   7249  C  CD2   B HIS B 2 28  ? 9.334   -33.446 9.385   0.50 44.64 ? 28  HIS B CD2   1 
ATOM   7250  C  CE1   A HIS B 2 28  ? 8.153   -32.336 9.638   0.50 39.56 ? 28  HIS B CE1   1 
ATOM   7251  C  CE1   B HIS B 2 28  ? 9.566   -31.875 7.872   0.50 38.50 ? 28  HIS B CE1   1 
ATOM   7252  N  NE2   A HIS B 2 28  ? 9.363   -32.184 9.132   0.50 42.57 ? 28  HIS B NE2   1 
ATOM   7253  N  NE2   B HIS B 2 28  ? 9.694   -32.139 9.159   0.50 41.50 ? 28  HIS B NE2   1 
ATOM   7254  N  N     A GLY B 2 29  ? 9.017   -39.056 8.371   0.50 50.43 ? 29  GLY B N     1 
ATOM   7255  N  N     B GLY B 2 29  ? 8.748   -38.826 8.527   0.50 49.83 ? 29  GLY B N     1 
ATOM   7256  C  CA    A GLY B 2 29  ? 8.442   -40.343 8.035   0.50 54.58 ? 29  GLY B CA    1 
ATOM   7257  C  CA    B GLY B 2 29  ? 8.105   -40.083 8.175   0.50 54.68 ? 29  GLY B CA    1 
ATOM   7258  C  C     A GLY B 2 29  ? 8.011   -40.507 6.596   0.50 53.41 ? 29  GLY B C     1 
ATOM   7259  C  C     B GLY B 2 29  ? 7.592   -40.121 6.752   0.50 53.61 ? 29  GLY B C     1 
ATOM   7260  O  O     A GLY B 2 29  ? 7.182   -41.376 6.306   0.50 55.58 ? 29  GLY B O     1 
ATOM   7261  O  O     B GLY B 2 29  ? 6.473   -40.590 6.510   0.50 55.97 ? 29  GLY B O     1 
ATOM   7262  N  N     A ILE B 2 30  ? 8.546   -39.706 5.681   0.50 49.92 ? 30  ILE B N     1 
ATOM   7263  N  N     B ILE B 2 30  ? 8.385   -39.634 5.802   0.50 49.82 ? 30  ILE B N     1 
ATOM   7264  C  CA    A ILE B 2 30  ? 8.203   -39.786 4.266   0.50 52.37 ? 30  ILE B CA    1 
ATOM   7265  C  CA    B ILE B 2 30  ? 8.003   -39.585 4.397   0.50 52.46 ? 30  ILE B CA    1 
ATOM   7266  C  C     A ILE B 2 30  ? 9.258   -40.616 3.550   0.50 54.37 ? 30  ILE B C     1 
ATOM   7267  C  C     B ILE B 2 30  ? 8.978   -40.447 3.608   0.50 53.94 ? 30  ILE B C     1 
ATOM   7268  O  O     A ILE B 2 30  ? 10.463  -40.449 3.781   0.50 52.85 ? 30  ILE B O     1 
ATOM   7269  O  O     B ILE B 2 30  ? 10.198  -40.275 3.720   0.50 53.17 ? 30  ILE B O     1 
ATOM   7270  C  CB    A ILE B 2 30  ? 8.078   -38.381 3.647   0.50 52.89 ? 30  ILE B CB    1 
ATOM   7271  C  CB    B ILE B 2 30  ? 7.987   -38.141 3.864   0.50 52.69 ? 30  ILE B CB    1 
ATOM   7272  C  CG1   A ILE B 2 30  ? 7.022   -37.569 4.401   0.50 49.81 ? 30  ILE B CG1   1 
ATOM   7273  C  CG1   B ILE B 2 30  ? 7.193   -37.234 4.808   0.50 48.42 ? 30  ILE B CG1   1 
ATOM   7274  C  CG2   A ILE B 2 30  ? 7.728   -38.472 2.168   0.50 54.52 ? 30  ILE B CG2   1 
ATOM   7275  C  CG2   B ILE B 2 30  ? 7.402   -38.094 2.462   0.50 53.65 ? 30  ILE B CG2   1 
ATOM   7276  C  CD1   A ILE B 2 30  ? 6.735   -36.214 3.793   0.50 48.99 ? 30  ILE B CD1   1 
ATOM   7277  C  CD1   B ILE B 2 30  ? 5.737   -37.620 4.955   0.50 52.83 ? 30  ILE B CD1   1 
ATOM   7278  N  N     A ASP B 2 31  ? 8.809   -41.513 2.688   0.50 57.87 ? 31  ASP B N     1 
ATOM   7279  N  N     B ASP B 2 31  ? 8.444   -41.371 2.821   0.50 57.56 ? 31  ASP B N     1 
ATOM   7280  C  CA    A ASP B 2 31  ? 9.669   -42.423 1.951   0.50 55.44 ? 31  ASP B CA    1 
ATOM   7281  C  CA    B ASP B 2 31  ? 9.253   -42.274 2.015   0.50 55.10 ? 31  ASP B CA    1 
ATOM   7282  C  C     A ASP B 2 31  ? 9.984   -41.859 0.571   0.50 56.63 ? 31  ASP B C     1 
ATOM   7283  C  C     B ASP B 2 31  ? 9.586   -41.626 0.680   0.50 57.22 ? 31  ASP B C     1 
ATOM   7284  O  O     A ASP B 2 31  ? 9.396   -40.862 0.144   0.50 60.58 ? 31  ASP B O     1 
ATOM   7285  O  O     B ASP B 2 31  ? 8.997   -40.610 0.301   0.50 61.10 ? 31  ASP B O     1 
ATOM   7286  C  CB    A ASP B 2 31  ? 9.004   -43.803 1.857   0.50 59.06 ? 31  ASP B CB    1 
ATOM   7287  C  CB    B ASP B 2 31  ? 8.512   -43.600 1.831   0.50 59.44 ? 31  ASP B CB    1 
ATOM   7288  C  CG    A ASP B 2 31  ? 7.627   -43.768 1.213   0.50 61.06 ? 31  ASP B CG    1 
ATOM   7289  C  CG    B ASP B 2 31  ? 7.166   -43.438 1.146   0.50 62.05 ? 31  ASP B CG    1 
ATOM   7290  O  OD1   A ASP B 2 31  ? 7.311   -42.810 0.476   0.50 62.77 ? 31  ASP B OD1   1 
ATOM   7291  O  OD1   B ASP B 2 31  ? 6.754   -42.291 0.880   0.50 64.94 ? 31  ASP B OD1   1 
ATOM   7292  O  OD2   A ASP B 2 31  ? 6.852   -44.719 1.450   0.50 57.93 ? 31  ASP B OD2   1 
ATOM   7293  O  OD2   B ASP B 2 31  ? 6.517   -44.470 0.873   0.50 59.63 ? 31  ASP B OD2   1 
ATOM   7294  N  N     A PRO B 2 32  ? 10.932  -42.463 -0.156  0.50 55.81 ? 32  PRO B N     1 
ATOM   7295  N  N     B PRO B 2 32  ? 10.554  -42.177 -0.062  0.50 55.29 ? 32  PRO B N     1 
ATOM   7296  C  CA    A PRO B 2 32  ? 11.260  -41.951 -1.499  0.50 57.58 ? 32  PRO B CA    1 
ATOM   7297  C  CA    B PRO B 2 32  ? 10.878  -41.605 -1.380  0.50 56.83 ? 32  PRO B CA    1 
ATOM   7298  C  C     A PRO B 2 32  ? 10.080  -41.886 -2.456  0.50 57.37 ? 32  PRO B C     1 
ATOM   7299  C  C     B PRO B 2 32  ? 9.700   -41.556 -2.337  0.50 57.98 ? 32  PRO B C     1 
ATOM   7300  O  O     A PRO B 2 32  ? 10.155  -41.157 -3.452  0.50 57.47 ? 32  PRO B O     1 
ATOM   7301  O  O     B PRO B 2 32  ? 9.699   -40.721 -3.251  0.50 57.82 ? 32  PRO B O     1 
ATOM   7302  C  CB    A PRO B 2 32  ? 12.320  -42.940 -1.996  0.50 56.64 ? 32  PRO B CB    1 
ATOM   7303  C  CB    B PRO B 2 32  ? 11.983  -42.533 -1.903  0.50 57.18 ? 32  PRO B CB    1 
ATOM   7304  C  CG    A PRO B 2 32  ? 12.988  -43.406 -0.757  0.50 53.21 ? 32  PRO B CG    1 
ATOM   7305  C  CG    B PRO B 2 32  ? 12.624  -43.072 -0.674  0.50 53.85 ? 32  PRO B CG    1 
ATOM   7306  C  CD    A PRO B 2 32  ? 11.910  -43.476 0.289   0.50 58.31 ? 32  PRO B CD    1 
ATOM   7307  C  CD    B PRO B 2 32  ? 11.517  -43.223 0.332   0.50 58.48 ? 32  PRO B CD    1 
ATOM   7308  N  N     A THR B 2 33  ? 8.999   -42.615 -2.195  0.50 58.73 ? 33  THR B N     1 
ATOM   7309  N  N     B THR B 2 33  ? 8.697   -42.417 -2.160  0.50 58.97 ? 33  THR B N     1 
ATOM   7310  C  CA    A THR B 2 33  ? 7.835   -42.620 -3.069  0.50 60.25 ? 33  THR B CA    1 
ATOM   7311  C  CA    B THR B 2 33  ? 7.533   -42.383 -3.039  0.50 60.08 ? 33  THR B CA    1 
ATOM   7312  C  C     A THR B 2 33  ? 6.797   -41.574 -2.680  0.50 61.19 ? 33  THR B C     1 
ATOM   7313  C  C     B THR B 2 33  ? 6.638   -41.192 -2.715  0.50 61.28 ? 33  THR B C     1 
ATOM   7314  O  O     A THR B 2 33  ? 5.691   -41.583 -3.228  0.50 63.62 ? 33  THR B O     1 
ATOM   7315  O  O     B THR B 2 33  ? 6.186   -40.480 -3.619  0.50 62.50 ? 33  THR B O     1 
ATOM   7316  C  CB    A THR B 2 33  ? 7.190   -44.008 -3.080  0.50 64.59 ? 33  THR B CB    1 
ATOM   7317  C  CB    B THR B 2 33  ? 6.752   -43.693 -2.929  0.50 64.08 ? 33  THR B CB    1 
ATOM   7318  O  OG1   A THR B 2 33  ? 6.775   -44.354 -1.752  0.50 63.99 ? 33  THR B OG1   1 
ATOM   7319  O  OG1   B THR B 2 33  ? 7.592   -44.786 -3.324  0.50 62.92 ? 33  THR B OG1   1 
ATOM   7320  C  CG2   A THR B 2 33  ? 8.179   -45.051 -3.585  0.50 58.55 ? 33  THR B CG2   1 
ATOM   7321  C  CG2   B THR B 2 33  ? 5.520   -43.656 -3.823  0.50 61.77 ? 33  THR B CG2   1 
ATOM   7322  N  N     A GLY B 2 34  ? 7.126   -40.676 -1.751  0.50 60.26 ? 34  GLY B N     1 
ATOM   7323  N  N     B GLY B 2 34  ? 6.371   -40.962 -1.431  0.50 60.20 ? 34  GLY B N     1 
ATOM   7324  C  CA    A GLY B 2 34  ? 6.193   -39.672 -1.291  0.50 59.09 ? 34  GLY B CA    1 
ATOM   7325  C  CA    B GLY B 2 34  ? 5.567   -39.829 -1.015  0.50 59.72 ? 34  GLY B CA    1 
ATOM   7326  C  C     A GLY B 2 34  ? 5.167   -40.155 -0.290  0.50 59.29 ? 34  GLY B C     1 
ATOM   7327  C  C     B GLY B 2 34  ? 4.613   -40.134 0.122   0.50 59.78 ? 34  GLY B C     1 
ATOM   7328  O  O     A GLY B 2 34  ? 4.391   -39.336 0.219   0.50 58.94 ? 34  GLY B O     1 
ATOM   7329  O  O     B GLY B 2 34  ? 3.952   -39.231 0.644   0.50 59.63 ? 34  GLY B O     1 
ATOM   7330  N  N     A SER B 2 35  ? 5.132   -41.449 0.010   0.50 61.82 ? 35  SER B N     1 
ATOM   7331  N  N     B SER B 2 35  ? 4.537   -41.401 0.520   0.50 63.51 ? 35  SER B N     1 
ATOM   7332  C  CA    A SER B 2 35  ? 4.180   -41.982 0.971   0.50 64.09 ? 35  SER B CA    1 
ATOM   7333  C  CA    B SER B 2 35  ? 3.590   -41.822 1.542   0.50 61.94 ? 35  SER B CA    1 
ATOM   7334  C  C     A SER B 2 35  ? 4.661   -41.734 2.395   0.50 60.97 ? 35  SER B C     1 
ATOM   7335  C  C     B SER B 2 35  ? 4.125   -41.538 2.943   0.50 59.78 ? 35  SER B C     1 
ATOM   7336  O  O     A SER B 2 35  ? 5.862   -41.744 2.681   0.50 60.19 ? 35  SER B O     1 
ATOM   7337  O  O     B SER B 2 35  ? 5.335   -41.460 3.171   0.50 58.65 ? 35  SER B O     1 
ATOM   7338  C  CB    A SER B 2 35  ? 3.975   -43.482 0.747   0.50 65.33 ? 35  SER B CB    1 
ATOM   7339  C  CB    B SER B 2 35  ? 3.279   -43.313 1.398   0.50 65.92 ? 35  SER B CB    1 
ATOM   7340  O  OG    A SER B 2 35  ? 3.640   -43.760 -0.601  0.50 60.94 ? 35  SER B OG    1 
ATOM   7341  O  OG    B SER B 2 35  ? 2.807   -43.612 0.096   0.50 67.98 ? 35  SER B OG    1 
ATOM   7342  N  N     A TYR B 2 36  ? 3.707   -41.506 3.292   0.50 59.72 ? 36  TYR B N     1 
ATOM   7343  N  N     B TYR B 2 36  ? 3.201   -41.392 3.886   0.50 59.81 ? 36  TYR B N     1 
ATOM   7344  C  CA    A TYR B 2 36  ? 4.000   -41.327 4.708   0.50 57.83 ? 36  TYR B CA    1 
ATOM   7345  C  CA    B TYR B 2 36  ? 3.536   -41.088 5.271   0.50 59.84 ? 36  TYR B CA    1 
ATOM   7346  C  C     A TYR B 2 36  ? 3.888   -42.674 5.411   0.50 60.05 ? 36  TYR B C     1 
ATOM   7347  C  C     B TYR B 2 36  ? 3.691   -42.388 6.054   0.50 60.76 ? 36  TYR B C     1 
ATOM   7348  O  O     A TYR B 2 36  ? 2.813   -43.284 5.427   0.50 60.40 ? 36  TYR B O     1 
ATOM   7349  O  O     B TYR B 2 36  ? 2.729   -43.151 6.199   0.50 62.92 ? 36  TYR B O     1 
ATOM   7350  C  CB    A TYR B 2 36  ? 3.050   -40.307 5.335   0.50 58.49 ? 36  TYR B CB    1 
ATOM   7351  C  CB    B TYR B 2 36  ? 2.462   -40.198 5.895   0.50 54.68 ? 36  TYR B CB    1 
ATOM   7352  C  CG    A TYR B 2 36  ? 3.107   -40.262 6.846   0.50 56.07 ? 36  TYR B CG    1 
ATOM   7353  C  CG    B TYR B 2 36  ? 2.635   -39.955 7.377   0.50 56.95 ? 36  TYR B CG    1 
ATOM   7354  C  CD1   A TYR B 2 36  ? 4.199   -39.713 7.504   0.50 55.11 ? 36  TYR B CD1   1 
ATOM   7355  C  CD1   B TYR B 2 36  ? 3.818   -39.433 7.883   0.50 56.08 ? 36  TYR B CD1   1 
ATOM   7356  C  CD2   A TYR B 2 36  ? 2.063   -40.761 7.615   0.50 58.51 ? 36  TYR B CD2   1 
ATOM   7357  C  CD2   B TYR B 2 36  ? 1.606   -40.234 8.269   0.50 56.14 ? 36  TYR B CD2   1 
ATOM   7358  C  CE1   A TYR B 2 36  ? 4.255   -39.669 8.884   0.50 56.44 ? 36  TYR B CE1   1 
ATOM   7359  C  CE1   B TYR B 2 36  ? 3.976   -39.206 9.238   0.50 58.35 ? 36  TYR B CE1   1 
ATOM   7360  C  CE2   A TYR B 2 36  ? 2.107   -40.721 8.996   0.50 56.77 ? 36  TYR B CE2   1 
ATOM   7361  C  CE2   B TYR B 2 36  ? 1.753   -40.009 9.626   0.50 57.65 ? 36  TYR B CE2   1 
ATOM   7362  C  CZ    A TYR B 2 36  ? 3.205   -40.173 9.626   0.50 60.48 ? 36  TYR B CZ    1 
ATOM   7363  C  CZ    B TYR B 2 36  ? 2.940   -39.494 10.104  0.50 59.28 ? 36  TYR B CZ    1 
ATOM   7364  O  OH    A TYR B 2 36  ? 3.254   -40.131 11.002  0.50 59.26 ? 36  TYR B OH    1 
ATOM   7365  O  OH    B TYR B 2 36  ? 3.094   -39.269 11.452  0.50 56.98 ? 36  TYR B OH    1 
ATOM   7366  N  N     A HIS B 2 37  ? 4.996   -43.137 5.982   0.50 61.63 ? 37  HIS B N     1 
ATOM   7367  N  N     B HIS B 2 37  ? 4.901   -42.633 6.561   0.50 61.06 ? 37  HIS B N     1 
ATOM   7368  C  CA    A HIS B 2 37  ? 5.053   -44.395 6.721   0.50 61.08 ? 37  HIS B CA    1 
ATOM   7369  C  CA    B HIS B 2 37  ? 5.221   -43.850 7.297   0.50 59.45 ? 37  HIS B CA    1 
ATOM   7370  C  C     A HIS B 2 37  ? 5.720   -44.184 8.073   0.50 60.44 ? 37  HIS B C     1 
ATOM   7371  C  C     B HIS B 2 37  ? 5.528   -43.589 8.765   0.50 58.62 ? 37  HIS B C     1 
ATOM   7372  O  O     A HIS B 2 37  ? 6.684   -44.862 8.437   0.50 62.59 ? 37  HIS B O     1 
ATOM   7373  O  O     B HIS B 2 37  ? 6.027   -44.485 9.453   0.50 60.41 ? 37  HIS B O     1 
ATOM   7374  C  CB    A HIS B 2 37  ? 5.783   -45.472 5.924   0.50 65.37 ? 37  HIS B CB    1 
ATOM   7375  C  CB    B HIS B 2 37  ? 6.407   -44.567 6.645   0.50 62.82 ? 37  HIS B CB    1 
ATOM   7376  C  CG    A HIS B 2 37  ? 4.947   -46.108 4.858   0.50 65.68 ? 37  HIS B CG    1 
ATOM   7377  C  CG    B HIS B 2 37  ? 6.067   -45.273 5.370   0.50 64.73 ? 37  HIS B CG    1 
ATOM   7378  N  ND1   A HIS B 2 37  ? 4.769   -45.542 3.613   0.50 69.86 ? 37  HIS B ND1   1 
ATOM   7379  N  ND1   B HIS B 2 37  ? 5.250   -44.722 4.407   0.50 66.61 ? 37  HIS B ND1   1 
ATOM   7380  C  CD2   A HIS B 2 37  ? 4.239   -47.262 4.851   0.50 65.84 ? 37  HIS B CD2   1 
ATOM   7381  C  CD2   B HIS B 2 37  ? 6.440   -46.486 4.897   0.50 66.79 ? 37  HIS B CD2   1 
ATOM   7382  C  CE1   A HIS B 2 37  ? 3.989   -46.322 2.886   0.50 68.38 ? 37  HIS B CE1   1 
ATOM   7383  C  CE1   B HIS B 2 37  ? 5.132   -45.566 3.397   0.50 69.25 ? 37  HIS B CE1   1 
ATOM   7384  N  NE2   A HIS B 2 37  ? 3.654   -47.372 3.613   0.50 68.77 ? 37  HIS B NE2   1 
ATOM   7385  N  NE2   B HIS B 2 37  ? 5.844   -46.644 3.669   0.50 68.77 ? 37  HIS B NE2   1 
ATOM   7386  N  N     A GLY B 2 38  ? 5.205   -43.228 8.840   0.50 57.68 ? 38  GLY B N     1 
ATOM   7387  N  N     B GLY B 2 38  ? 5.244   -42.389 9.264   0.50 56.81 ? 38  GLY B N     1 
ATOM   7388  C  CA    A GLY B 2 38  ? 5.700   -42.938 10.165  0.50 57.75 ? 38  GLY B CA    1 
ATOM   7389  C  CA    B GLY B 2 38  ? 5.621   -42.046 10.624  0.50 58.23 ? 38  GLY B CA    1 
ATOM   7390  C  C     A GLY B 2 38  ? 4.854   -43.572 11.249  0.50 62.70 ? 38  GLY B C     1 
ATOM   7391  C  C     B GLY B 2 38  ? 4.712   -42.695 11.657  0.50 63.36 ? 38  GLY B C     1 
ATOM   7392  O  O     A GLY B 2 38  ? 4.107   -44.531 11.018  0.50 63.86 ? 38  GLY B O     1 
ATOM   7393  O  O     B GLY B 2 38  ? 3.503   -42.820 11.466  0.50 59.38 ? 38  GLY B O     1 
ATOM   7394  N  N     A ASP B 2 39  ? 4.978   -43.027 12.458  0.50 65.68 ? 39  ASP B N     1 
ATOM   7395  N  N     B ASP B 2 39  ? 5.317   -43.106 12.770  0.50 66.00 ? 39  ASP B N     1 
ATOM   7396  C  CA    A ASP B 2 39  ? 4.188   -43.485 13.594  0.50 65.98 ? 39  ASP B CA    1 
ATOM   7397  C  CA    B ASP B 2 39  ? 4.588   -43.688 13.888  0.50 66.75 ? 39  ASP B CA    1 
ATOM   7398  C  C     A ASP B 2 39  ? 4.113   -42.398 14.658  0.50 67.19 ? 39  ASP B C     1 
ATOM   7399  C  C     B ASP B 2 39  ? 4.115   -42.644 14.891  0.50 67.69 ? 39  ASP B C     1 
ATOM   7400  O  O     A ASP B 2 39  ? 4.302   -42.669 15.849  0.50 70.80 ? 39  ASP B O     1 
ATOM   7401  O  O     B ASP B 2 39  ? 3.512   -43.009 15.906  0.50 71.53 ? 39  ASP B O     1 
ATOM   7402  C  CB    A ASP B 2 39  ? 4.771   -44.775 14.178  0.50 69.14 ? 39  ASP B CB    1 
ATOM   7403  C  CB    B ASP B 2 39  ? 5.457   -44.733 14.601  0.50 70.03 ? 39  ASP B CB    1 
ATOM   7404  C  CG    A ASP B 2 39  ? 6.242   -44.648 14.529  0.50 70.20 ? 39  ASP B CG    1 
ATOM   7405  C  CG    B ASP B 2 39  ? 6.756   -44.152 15.132  0.50 69.44 ? 39  ASP B CG    1 
ATOM   7406  O  OD1   A ASP B 2 39  ? 6.850   -43.608 14.202  0.50 72.66 ? 39  ASP B OD1   1 
ATOM   7407  O  OD1   B ASP B 2 39  ? 6.716   -43.417 16.141  0.50 66.42 ? 39  ASP B OD1   1 
ATOM   7408  O  OD2   A ASP B 2 39  ? 6.790   -45.592 15.136  0.50 69.86 ? 39  ASP B OD2   1 
ATOM   7409  O  OD2   B ASP B 2 39  ? 7.821   -44.435 14.541  0.50 69.42 ? 39  ASP B OD2   1 
ATOM   7410  N  N     A SER B 2 40  ? 3.841   -41.165 14.236  0.50 65.63 ? 40  SER B N     1 
ATOM   7411  N  N     B SER B 2 40  ? 4.377   -41.364 14.638  0.50 65.91 ? 40  SER B N     1 
ATOM   7412  C  CA    A SER B 2 40  ? 3.751   -40.039 15.153  0.50 63.19 ? 40  SER B CA    1 
ATOM   7413  C  CA    B SER B 2 40  ? 3.963   -40.289 15.526  0.50 63.64 ? 40  SER B CA    1 
ATOM   7414  C  C     A SER B 2 40  ? 2.976   -38.917 14.480  0.50 62.77 ? 40  SER B C     1 
ATOM   7415  C  C     B SER B 2 40  ? 3.358   -39.162 14.705  0.50 62.79 ? 40  SER B C     1 
ATOM   7416  O  O     A SER B 2 40  ? 3.190   -38.628 13.300  0.50 61.48 ? 40  SER B O     1 
ATOM   7417  O  O     B SER B 2 40  ? 3.862   -38.829 13.629  0.50 61.82 ? 40  SER B O     1 
ATOM   7418  C  CB    A SER B 2 40  ? 5.140   -39.546 15.575  0.50 63.64 ? 40  SER B CB    1 
ATOM   7419  C  CB    B SER B 2 40  ? 5.141   -39.758 16.354  0.50 64.79 ? 40  SER B CB    1 
ATOM   7420  O  OG    A SER B 2 40  ? 5.044   -38.372 16.364  0.50 64.09 ? 40  SER B OG    1 
ATOM   7421  O  OG    B SER B 2 40  ? 4.764   -38.614 17.101  0.50 66.58 ? 40  SER B OG    1 
ATOM   7422  N  N     A ASP B 2 41  ? 2.077   -38.288 15.238  0.50 59.70 ? 41  ASP B N     1 
ATOM   7423  N  N     B ASP B 2 41  ? 2.276   -38.577 15.219  0.50 60.37 ? 41  ASP B N     1 
ATOM   7424  C  CA    A ASP B 2 41  ? 1.305   -37.176 14.698  0.50 60.13 ? 41  ASP B CA    1 
ATOM   7425  C  CA    B ASP B 2 41  ? 1.623   -37.468 14.538  0.50 60.12 ? 41  ASP B CA    1 
ATOM   7426  C  C     A ASP B 2 41  ? 2.127   -35.898 14.597  0.50 59.51 ? 41  ASP B C     1 
ATOM   7427  C  C     B ASP B 2 41  ? 2.345   -36.141 14.736  0.50 59.77 ? 41  ASP B C     1 
ATOM   7428  O  O     A ASP B 2 41  ? 1.770   -35.009 13.818  0.50 57.22 ? 41  ASP B O     1 
ATOM   7429  O  O     B ASP B 2 41  ? 1.962   -35.148 14.108  0.50 57.27 ? 41  ASP B O     1 
ATOM   7430  C  CB    A ASP B 2 41  ? 0.061   -36.937 15.556  0.50 62.01 ? 41  ASP B CB    1 
ATOM   7431  C  CB    B ASP B 2 41  ? 0.171   -37.349 15.009  0.50 60.78 ? 41  ASP B CB    1 
ATOM   7432  C  CG    A ASP B 2 41  ? -0.838  -38.159 15.635  0.50 60.36 ? 41  ASP B CG    1 
ATOM   7433  C  CG    B ASP B 2 41  ? -0.693  -38.495 14.517  0.50 60.55 ? 41  ASP B CG    1 
ATOM   7434  O  OD1   A ASP B 2 41  ? -0.365  -39.220 16.096  0.50 55.67 ? 41  ASP B OD1   1 
ATOM   7435  O  OD1   B ASP B 2 41  ? -0.722  -38.732 13.291  0.50 63.47 ? 41  ASP B OD1   1 
ATOM   7436  O  OD2   A ASP B 2 41  ? -2.019  -38.057 15.240  0.50 54.45 ? 41  ASP B OD2   1 
ATOM   7437  O  OD2   B ASP B 2 41  ? -1.330  -39.167 15.355  0.50 53.20 ? 41  ASP B OD2   1 
ATOM   7438  N  N     A LEU B 2 42  ? 3.221   -35.792 15.356  0.50 60.06 ? 42  LEU B N     1 
ATOM   7439  N  N     B LEU B 2 42  ? 3.374   -36.100 15.585  0.50 60.48 ? 42  LEU B N     1 
ATOM   7440  C  CA    A LEU B 2 42  ? 4.053   -34.595 15.345  0.50 59.20 ? 42  LEU B CA    1 
ATOM   7441  C  CA    B LEU B 2 42  ? 4.202   -34.906 15.712  0.50 60.11 ? 42  LEU B CA    1 
ATOM   7442  C  C     A LEU B 2 42  ? 4.778   -34.382 14.022  0.50 55.08 ? 42  LEU B C     1 
ATOM   7443  C  C     B LEU B 2 42  ? 4.971   -34.591 14.436  0.50 54.89 ? 42  LEU B C     1 
ATOM   7444  O  O     A LEU B 2 42  ? 5.357   -33.309 13.821  0.50 51.37 ? 42  LEU B O     1 
ATOM   7445  O  O     B LEU B 2 42  ? 5.495   -33.479 14.307  0.50 52.18 ? 42  LEU B O     1 
ATOM   7446  C  CB    A LEU B 2 42  ? 5.080   -34.659 16.478  0.50 60.52 ? 42  LEU B CB    1 
ATOM   7447  C  CB    B LEU B 2 42  ? 5.185   -35.066 16.874  0.50 60.08 ? 42  LEU B CB    1 
ATOM   7448  C  CG    A LEU B 2 42  ? 4.561   -34.892 17.899  0.50 61.02 ? 42  LEU B CG    1 
ATOM   7449  C  CG    B LEU B 2 42  ? 4.620   -34.931 18.288  0.50 60.54 ? 42  LEU B CG    1 
ATOM   7450  C  CD1   A LEU B 2 42  ? 5.707   -34.842 18.895  0.50 57.74 ? 42  LEU B CD1   1 
ATOM   7451  C  CD1   B LEU B 2 42  ? 5.702   -35.199 19.322  0.50 57.95 ? 42  LEU B CD1   1 
ATOM   7452  C  CD2   A LEU B 2 42  ? 3.488   -33.881 18.263  0.50 58.96 ? 42  LEU B CD2   1 
ATOM   7453  C  CD2   B LEU B 2 42  ? 4.018   -33.551 18.484  0.50 58.16 ? 42  LEU B CD2   1 
ATOM   7454  N  N     A GLN B 2 43  ? 4.766   -35.367 13.125  0.50 54.47 ? 43  GLN B N     1 
ATOM   7455  N  N     B GLN B 2 43  ? 5.050   -35.533 13.501  0.50 54.71 ? 43  GLN B N     1 
ATOM   7456  C  CA    A GLN B 2 43  ? 5.455   -35.246 11.848  0.50 52.93 ? 43  GLN B CA    1 
ATOM   7457  C  CA    B GLN B 2 43  ? 5.763   -35.348 12.246  0.50 53.35 ? 43  GLN B CA    1 
ATOM   7458  C  C     A GLN B 2 43  ? 4.604   -34.593 10.769  0.50 54.17 ? 43  GLN B C     1 
ATOM   7459  C  C     B GLN B 2 43  ? 4.890   -34.754 11.150  0.50 53.66 ? 43  GLN B C     1 
ATOM   7460  O  O     A GLN B 2 43  ? 5.152   -34.121 9.766   0.50 51.62 ? 43  GLN B O     1 
ATOM   7461  O  O     B GLN B 2 43  ? 5.396   -34.479 10.057  0.50 52.40 ? 43  GLN B O     1 
ATOM   7462  C  CB    A GLN B 2 43  ? 5.910   -36.625 11.365  0.50 52.77 ? 43  GLN B CB    1 
ATOM   7463  C  CB    B GLN B 2 43  ? 6.334   -36.687 11.772  0.50 53.65 ? 43  GLN B CB    1 
ATOM   7464  C  CG    A GLN B 2 43  ? 6.804   -37.359 12.348  0.50 54.32 ? 43  GLN B CG    1 
ATOM   7465  C  CG    B GLN B 2 43  ? 7.108   -37.435 12.843  0.50 53.04 ? 43  GLN B CG    1 
ATOM   7466  C  CD    A GLN B 2 43  ? 7.058   -38.793 11.938  0.50 54.89 ? 43  GLN B CD    1 
ATOM   7467  C  CD    B GLN B 2 43  ? 7.318   -38.893 12.494  0.50 54.55 ? 43  GLN B CD    1 
ATOM   7468  O  OE1   A GLN B 2 43  ? 6.182   -39.454 11.381  0.50 54.81 ? 43  GLN B OE1   1 
ATOM   7469  O  OE1   B GLN B 2 43  ? 6.389   -39.695 12.566  0.50 57.98 ? 43  GLN B OE1   1 
ATOM   7470  N  NE2   A GLN B 2 43  ? 8.264   -39.282 12.206  0.50 53.52 ? 43  GLN B NE2   1 
ATOM   7471  N  NE2   B GLN B 2 43  ? 8.541   -39.243 12.112  0.50 53.20 ? 43  GLN B NE2   1 
ATOM   7472  N  N     A LEU B 2 44  ? 3.284   -34.552 10.951  0.50 53.49 ? 44  LEU B N     1 
ATOM   7473  N  N     B LEU B 2 44  ? 3.599   -34.546 11.414  0.50 53.80 ? 44  LEU B N     1 
ATOM   7474  C  CA    A LEU B 2 44  ? 2.378   -34.001 9.955   0.50 50.11 ? 44  LEU B CA    1 
ATOM   7475  C  CA    B LEU B 2 44  ? 2.664   -34.092 10.397  0.50 51.27 ? 44  LEU B CA    1 
ATOM   7476  C  C     A LEU B 2 44  ? 1.715   -32.700 10.385  0.50 51.15 ? 44  LEU B C     1 
ATOM   7477  C  C     B LEU B 2 44  ? 1.919   -32.817 10.765  0.50 50.93 ? 44  LEU B C     1 
ATOM   7478  O  O     A LEU B 2 44  ? 1.027   -32.080 9.566   0.50 49.65 ? 44  LEU B O     1 
ATOM   7479  O  O     B LEU B 2 44  ? 1.273   -32.231 9.888   0.50 50.45 ? 44  LEU B O     1 
ATOM   7480  C  CB    A LEU B 2 44  ? 1.291   -35.030 9.606   0.50 57.87 ? 44  LEU B CB    1 
ATOM   7481  C  CB    B LEU B 2 44  ? 1.638   -35.196 10.093  0.50 57.20 ? 44  LEU B CB    1 
ATOM   7482  C  CG    A LEU B 2 44  ? 1.775   -36.317 8.935   0.50 56.42 ? 44  LEU B CG    1 
ATOM   7483  C  CG    B LEU B 2 44  ? 1.383   -35.549 8.627   0.50 56.84 ? 44  LEU B CG    1 
ATOM   7484  C  CD1   A LEU B 2 44  ? 0.684   -37.375 8.950   0.50 58.66 ? 44  LEU B CD1   1 
ATOM   7485  C  CD1   B LEU B 2 44  ? 2.661   -36.017 7.955   0.50 56.95 ? 44  LEU B CD1   1 
ATOM   7486  C  CD2   A LEU B 2 44  ? 2.228   -36.036 7.511   0.50 55.83 ? 44  LEU B CD2   1 
ATOM   7487  C  CD2   B LEU B 2 44  ? 0.304   -36.616 8.532   0.50 59.65 ? 44  LEU B CD2   1 
ATOM   7488  N  N     A GLU B 2 45  ? 1.900   -32.272 11.637  0.50 49.46 ? 45  GLU B N     1 
ATOM   7489  N  N     B GLU B 2 45  ? 1.989   -32.369 12.023  0.50 49.08 ? 45  GLU B N     1 
ATOM   7490  C  CA    A GLU B 2 45  ? 1.262   -31.045 12.107  0.50 48.92 ? 45  GLU B CA    1 
ATOM   7491  C  CA    B GLU B 2 45  ? 1.223   -31.195 12.434  0.50 49.25 ? 45  GLU B CA    1 
ATOM   7492  C  C     A GLU B 2 45  ? 1.687   -29.847 11.269  0.50 47.40 ? 45  GLU B C     1 
ATOM   7493  C  C     B GLU B 2 45  ? 1.635   -29.947 11.666  0.50 46.50 ? 45  GLU B C     1 
ATOM   7494  O  O     A GLU B 2 45  ? 0.853   -29.027 10.867  0.50 48.09 ? 45  GLU B O     1 
ATOM   7495  O  O     B GLU B 2 45  ? 0.799   -29.073 11.412  0.50 47.79 ? 45  GLU B O     1 
ATOM   7496  C  CB    A GLU B 2 45  ? 1.591   -30.812 13.582  0.50 49.89 ? 45  GLU B CB    1 
ATOM   7497  C  CB    B GLU B 2 45  ? 1.375   -30.957 13.936  0.50 50.94 ? 45  GLU B CB    1 
ATOM   7498  C  CG    A GLU B 2 45  ? 1.159   -31.940 14.497  0.50 58.36 ? 45  GLU B CG    1 
ATOM   7499  C  CG    B GLU B 2 45  ? 0.624   -31.953 14.804  0.50 59.15 ? 45  GLU B CG    1 
ATOM   7500  C  CD    A GLU B 2 45  ? 1.244   -31.568 15.963  0.50 58.74 ? 45  GLU B CD    1 
ATOM   7501  C  CD    B GLU B 2 45  ? -0.045  -31.295 15.996  0.50 60.02 ? 45  GLU B CD    1 
ATOM   7502  O  OE1   A GLU B 2 45  ? 1.538   -30.391 16.265  0.50 58.89 ? 45  GLU B OE1   1 
ATOM   7503  O  OE1   B GLU B 2 45  ? -0.056  -30.046 16.058  0.50 62.09 ? 45  GLU B OE1   1 
ATOM   7504  O  OE2   A GLU B 2 45  ? 1.013   -32.453 16.814  0.50 58.50 ? 45  GLU B OE2   1 
ATOM   7505  O  OE2   B GLU B 2 45  ? -0.560  -32.025 16.870  0.50 60.20 ? 45  GLU B OE2   1 
ATOM   7506  N  N     A ARG B 2 46  ? 2.986   -29.731 10.990  0.50 52.27 ? 46  ARG B N     1 
ATOM   7507  N  N     B ARG B 2 46  ? 2.907   -29.839 11.292  0.50 53.51 ? 46  ARG B N     1 
ATOM   7508  C  CA    A ARG B 2 46  ? 3.518   -28.652 10.168  0.50 48.42 ? 46  ARG B CA    1 
ATOM   7509  C  CA    B ARG B 2 46  ? 3.406   -28.684 10.556  0.50 49.01 ? 46  ARG B CA    1 
ATOM   7510  C  C     A ARG B 2 46  ? 4.194   -29.197 8.914   0.50 49.61 ? 46  ARG B C     1 
ATOM   7511  C  C     B ARG B 2 46  ? 4.089   -29.124 9.270   0.50 50.30 ? 46  ARG B C     1 
ATOM   7512  O  O     A ARG B 2 46  ? 5.149   -28.606 8.408   0.50 43.90 ? 46  ARG B O     1 
ATOM   7513  O  O     B ARG B 2 46  ? 5.125   -28.581 8.874   0.50 44.02 ? 46  ARG B O     1 
ATOM   7514  C  CB    A ARG B 2 46  ? 4.491   -27.787 10.971  0.50 47.97 ? 46  ARG B CB    1 
ATOM   7515  C  CB    B ARG B 2 46  ? 4.349   -27.850 11.423  0.50 47.42 ? 46  ARG B CB    1 
ATOM   7516  C  CG    A ARG B 2 46  ? 3.947   -27.326 12.316  0.50 46.56 ? 46  ARG B CG    1 
ATOM   7517  C  CG    B ARG B 2 46  ? 3.826   -27.605 12.833  0.50 48.23 ? 46  ARG B CG    1 
ATOM   7518  C  CD    A ARG B 2 46  ? 4.849   -26.287 12.966  0.50 51.69 ? 46  ARG B CD    1 
ATOM   7519  C  CD    B ARG B 2 46  ? 4.479   -26.399 13.490  0.50 52.12 ? 46  ARG B CD    1 
ATOM   7520  N  NE    A ARG B 2 46  ? 4.630   -24.949 12.428  0.50 51.50 ? 46  ARG B NE    1 
ATOM   7521  N  NE    B ARG B 2 46  ? 3.727   -25.172 13.249  0.50 55.72 ? 46  ARG B NE    1 
ATOM   7522  C  CZ    A ARG B 2 46  ? 5.268   -23.861 12.837  0.50 44.55 ? 46  ARG B CZ    1 
ATOM   7523  C  CZ    B ARG B 2 46  ? 3.965   -24.325 12.257  0.50 52.47 ? 46  ARG B CZ    1 
ATOM   7524  N  NH1   A ARG B 2 46  ? 6.192   -23.914 13.782  0.50 40.02 ? 46  ARG B NH1   1 
ATOM   7525  N  NH1   B ARG B 2 46  ? 4.940   -24.534 11.388  0.50 53.02 ? 46  ARG B NH1   1 
ATOM   7526  N  NH2   A ARG B 2 46  ? 4.973   -22.688 12.282  0.50 43.54 ? 46  ARG B NH2   1 
ATOM   7527  N  NH2   B ARG B 2 46  ? 3.206   -23.240 12.134  0.50 56.51 ? 46  ARG B NH2   1 
ATOM   7528  N  N     A ILE B 2 47  ? 3.704   -30.330 8.404   0.50 50.18 ? 47  ILE B N     1 
ATOM   7529  N  N     B ILE B 2 47  ? 3.511   -30.120 8.593   0.50 50.41 ? 47  ILE B N     1 
ATOM   7530  C  CA    A ILE B 2 47  ? 4.325   -30.938 7.232   0.50 49.80 ? 47  ILE B CA    1 
ATOM   7531  C  CA    B ILE B 2 47  ? 4.092   -30.607 7.347   0.50 49.02 ? 47  ILE B CA    1 
ATOM   7532  C  C     A ILE B 2 47  ? 4.130   -30.064 6.001   0.50 47.99 ? 47  ILE B C     1 
ATOM   7533  C  C     B ILE B 2 47  ? 3.828   -29.658 6.186   0.50 48.04 ? 47  ILE B C     1 
ATOM   7534  O  O     A ILE B 2 47  ? 4.965   -30.072 5.087   0.50 43.46 ? 47  ILE B O     1 
ATOM   7535  O  O     B ILE B 2 47  ? 4.571   -29.682 5.196   0.50 47.96 ? 47  ILE B O     1 
ATOM   7536  C  CB    A ILE B 2 47  ? 3.774   -32.361 7.010   0.50 51.50 ? 47  ILE B CB    1 
ATOM   7537  C  CB    B ILE B 2 47  ? 3.569   -32.016 7.013   0.50 52.53 ? 47  ILE B CB    1 
ATOM   7538  C  CG1   A ILE B 2 47  ? 4.619   -33.107 5.977   0.50 49.20 ? 47  ILE B CG1   1 
ATOM   7539  C  CG1   B ILE B 2 47  ? 4.554   -32.748 6.102   0.50 48.45 ? 47  ILE B CG1   1 
ATOM   7540  C  CG2   A ILE B 2 47  ? 2.312   -32.322 6.580   0.50 53.35 ? 47  ILE B CG2   1 
ATOM   7541  C  CG2   B ILE B 2 47  ? 2.195   -31.951 6.354   0.50 52.22 ? 47  ILE B CG2   1 
ATOM   7542  C  CD1   A ILE B 2 47  ? 6.044   -33.325 6.413   0.50 47.21 ? 47  ILE B CD1   1 
ATOM   7543  C  CD1   B ILE B 2 47  ? 5.893   -32.991 6.746   0.50 46.10 ? 47  ILE B CD1   1 
ATOM   7544  N  N     A ASN B 2 48  ? 3.047   -29.283 5.961   0.50 44.58 ? 48  ASN B N     1 
ATOM   7545  N  N     B ASN B 2 48  ? 2.802   -28.808 6.288   0.50 43.43 ? 48  ASN B N     1 
ATOM   7546  C  CA    A ASN B 2 48  ? 2.759   -28.432 4.813   0.50 41.24 ? 48  ASN B CA    1 
ATOM   7547  C  CA    B ASN B 2 48  ? 2.469   -27.890 5.206   0.50 42.48 ? 48  ASN B CA    1 
ATOM   7548  C  C     A ASN B 2 48  ? 3.743   -27.280 4.663   0.50 42.26 ? 48  ASN B C     1 
ATOM   7549  C  C     B ASN B 2 48  ? 3.543   -26.833 4.979   0.50 41.50 ? 48  ASN B C     1 
ATOM   7550  O  O     A ASN B 2 48  ? 3.723   -26.611 3.623   0.50 38.70 ? 48  ASN B O     1 
ATOM   7551  O  O     B ASN B 2 48  ? 3.535   -26.182 3.927   0.50 39.96 ? 48  ASN B O     1 
ATOM   7552  C  CB    A ASN B 2 48  ? 1.336   -27.878 4.915   0.50 40.22 ? 48  ASN B CB    1 
ATOM   7553  C  CB    B ASN B 2 48  ? 1.130   -27.206 5.489   0.50 34.96 ? 48  ASN B CB    1 
ATOM   7554  N  N     A VAL B 2 49  ? 4.592   -27.031 5.665   0.50 41.23 ? 49  VAL B N     1 
ATOM   7555  N  N     B VAL B 2 49  ? 4.456   -26.643 5.937   0.50 38.13 ? 49  VAL B N     1 
ATOM   7556  C  CA    A VAL B 2 49  ? 5.553   -25.934 5.570   0.50 41.56 ? 49  VAL B CA    1 
ATOM   7557  C  CA    B VAL B 2 49  ? 5.517   -25.651 5.773   0.50 40.48 ? 49  VAL B CA    1 
ATOM   7558  C  C     A VAL B 2 49  ? 6.490   -26.143 4.387   0.50 38.75 ? 49  VAL B C     1 
ATOM   7559  C  C     B VAL B 2 49  ? 6.383   -25.992 4.567   0.50 38.93 ? 49  VAL B C     1 
ATOM   7560  O  O     A VAL B 2 49  ? 6.808   -25.198 3.654   0.50 41.31 ? 49  VAL B O     1 
ATOM   7561  O  O     B VAL B 2 49  ? 6.627   -25.148 3.697   0.50 41.12 ? 49  VAL B O     1 
ATOM   7562  C  CB    A VAL B 2 49  ? 6.329   -25.785 6.892   0.50 37.33 ? 49  VAL B CB    1 
ATOM   7563  C  CB    B VAL B 2 49  ? 6.360   -25.545 7.056   0.50 37.32 ? 49  VAL B CB    1 
ATOM   7564  C  CG1   A VAL B 2 49  ? 7.411   -24.725 6.759   0.50 36.74 ? 49  VAL B CG1   1 
ATOM   7565  C  CG1   B VAL B 2 49  ? 7.515   -24.576 6.851   0.50 36.64 ? 49  VAL B CG1   1 
ATOM   7566  C  CG2   A VAL B 2 49  ? 5.378   -25.433 8.028   0.50 40.95 ? 49  VAL B CG2   1 
ATOM   7567  C  CG2   B VAL B 2 49  ? 5.492   -25.111 8.223   0.50 40.63 ? 49  VAL B CG2   1 
ATOM   7568  N  N     A TYR B 2 50  ? 6.929   -27.381 4.166   0.50 40.31 ? 50  TYR B N     1 
ATOM   7569  N  N     B TYR B 2 50  ? 6.847   -27.238 4.489   0.50 37.53 ? 50  TYR B N     1 
ATOM   7570  C  CA    A TYR B 2 50  ? 7.853   -27.689 3.082   0.50 40.42 ? 50  TYR B CA    1 
ATOM   7571  C  CA    B TYR B 2 50  ? 7.755   -27.652 3.427   0.50 41.83 ? 50  TYR B CA    1 
ATOM   7572  C  C     A TYR B 2 50  ? 7.293   -28.648 2.039   0.50 40.49 ? 50  TYR B C     1 
ATOM   7573  C  C     B TYR B 2 50  ? 7.116   -28.528 2.359   0.50 41.46 ? 50  TYR B C     1 
ATOM   7574  O  O     A TYR B 2 50  ? 7.962   -28.890 1.028   0.50 42.20 ? 50  TYR B O     1 
ATOM   7575  O  O     B TYR B 2 50  ? 7.604   -28.543 1.228   0.50 40.01 ? 50  TYR B O     1 
ATOM   7576  C  CB    A TYR B 2 50  ? 9.161   -28.269 3.642   0.50 43.52 ? 50  TYR B CB    1 
ATOM   7577  C  CB    B TYR B 2 50  ? 8.961   -28.396 4.018   0.50 42.91 ? 50  TYR B CB    1 
ATOM   7578  C  CG    A TYR B 2 50  ? 10.112  -27.239 4.214   0.50 39.34 ? 50  TYR B CG    1 
ATOM   7579  C  CG    B TYR B 2 50  ? 9.980   -27.489 4.671   0.50 40.83 ? 50  TYR B CG    1 
ATOM   7580  C  CD1   A TYR B 2 50  ? 11.035  -26.592 3.401   0.50 43.68 ? 50  TYR B CD1   1 
ATOM   7581  C  CD1   B TYR B 2 50  ? 10.768  -26.638 3.907   0.50 41.59 ? 50  TYR B CD1   1 
ATOM   7582  C  CD2   A TYR B 2 50  ? 10.094  -26.921 5.567   0.50 42.61 ? 50  TYR B CD2   1 
ATOM   7583  C  CD2   B TYR B 2 50  ? 10.158  -27.486 6.049   0.50 40.47 ? 50  TYR B CD2   1 
ATOM   7584  C  CE1   A TYR B 2 50  ? 11.909  -25.652 3.917   0.50 37.58 ? 50  TYR B CE1   1 
ATOM   7585  C  CE1   B TYR B 2 50  ? 11.702  -25.805 4.495   0.50 37.18 ? 50  TYR B CE1   1 
ATOM   7586  C  CE2   A TYR B 2 50  ? 10.965  -25.982 6.092   0.50 37.21 ? 50  TYR B CE2   1 
ATOM   7587  C  CE2   B TYR B 2 50  ? 11.091  -26.656 6.645   0.50 38.50 ? 50  TYR B CE2   1 
ATOM   7588  C  CZ    A TYR B 2 50  ? 11.870  -25.353 5.263   0.50 37.08 ? 50  TYR B CZ    1 
ATOM   7589  C  CZ    B TYR B 2 50  ? 11.861  -25.820 5.864   0.50 37.47 ? 50  TYR B CZ    1 
ATOM   7590  O  OH    A TYR B 2 50  ? 12.739  -24.420 5.784   0.50 35.90 ? 50  TYR B OH    1 
ATOM   7591  O  OH    B TYR B 2 50  ? 12.791  -24.996 6.456   0.50 36.04 ? 50  TYR B OH    1 
ATOM   7592  N  N     A TYR B 2 51  ? 6.098   -29.200 2.242   0.50 41.79 ? 51  TYR B N     1 
ATOM   7593  N  N     B TYR B 2 51  ? 6.044   -29.250 2.677   0.50 40.97 ? 51  TYR B N     1 
ATOM   7594  C  CA    A TYR B 2 51  ? 5.538   -30.198 1.342   0.50 42.78 ? 51  TYR B CA    1 
ATOM   7595  C  CA    B TYR B 2 51  ? 5.421   -30.180 1.746   0.50 43.34 ? 51  TYR B CA    1 
ATOM   7596  C  C     A TYR B 2 51  ? 4.170   -29.762 0.836   0.50 41.98 ? 51  TYR B C     1 
ATOM   7597  C  C     B TYR B 2 51  ? 4.017   -29.720 1.379   0.50 42.45 ? 51  TYR B C     1 
ATOM   7598  O  O     A TYR B 2 51  ? 3.350   -29.242 1.598   0.50 41.24 ? 51  TYR B O     1 
ATOM   7599  O  O     B TYR B 2 51  ? 3.261   -29.255 2.237   0.50 40.70 ? 51  TYR B O     1 
ATOM   7600  C  CB    A TYR B 2 51  ? 5.412   -31.558 2.033   0.50 43.56 ? 51  TYR B CB    1 
ATOM   7601  C  CB    B TYR B 2 51  ? 5.346   -31.587 2.341   0.50 43.17 ? 51  TYR B CB    1 
ATOM   7602  C  CG    A TYR B 2 51  ? 6.730   -32.203 2.402   0.50 44.35 ? 51  TYR B CG    1 
ATOM   7603  C  CG    B TYR B 2 51  ? 6.684   -32.240 2.603   0.50 44.08 ? 51  TYR B CG    1 
ATOM   7604  C  CD1   A TYR B 2 51  ? 7.389   -31.857 3.573   0.50 36.96 ? 51  TYR B CD1   1 
ATOM   7605  C  CD1   B TYR B 2 51  ? 7.399   -31.961 3.758   0.50 37.00 ? 51  TYR B CD1   1 
ATOM   7606  C  CD2   A TYR B 2 51  ? 7.307   -33.170 1.586   0.50 41.38 ? 51  TYR B CD2   1 
ATOM   7607  C  CD2   B TYR B 2 51  ? 7.224   -33.149 1.700   0.50 41.50 ? 51  TYR B CD2   1 
ATOM   7608  C  CE1   A TYR B 2 51  ? 8.587   -32.449 3.921   0.50 40.46 ? 51  TYR B CE1   1 
ATOM   7609  C  CE1   B TYR B 2 51  ? 8.617   -32.561 4.007   0.50 40.49 ? 51  TYR B CE1   1 
ATOM   7610  C  CE2   A TYR B 2 51  ? 8.508   -33.769 1.926   0.50 42.86 ? 51  TYR B CE2   1 
ATOM   7611  C  CE2   B TYR B 2 51  ? 8.442   -33.756 1.940   0.50 42.84 ? 51  TYR B CE2   1 
ATOM   7612  C  CZ    A TYR B 2 51  ? 9.144   -33.403 3.094   0.50 43.15 ? 51  TYR B CZ    1 
ATOM   7613  C  CZ    B TYR B 2 51  ? 9.135   -33.456 3.094   0.50 43.16 ? 51  TYR B CZ    1 
ATOM   7614  O  OH    A TYR B 2 51  ? 10.338  -33.992 3.443   0.50 37.34 ? 51  TYR B OH    1 
ATOM   7615  O  OH    B TYR B 2 51  ? 10.349  -34.055 3.342   0.50 37.29 ? 51  TYR B OH    1 
ATOM   7616  N  N     A ASN B 2 52  ? 3.934   -29.983 -0.456  0.50 45.23 ? 52  ASN B N     1 
ATOM   7617  N  N     B ASN B 2 52  ? 3.675   -29.858 0.102   0.50 43.63 ? 52  ASN B N     1 
ATOM   7618  C  CA    A ASN B 2 52  ? 2.626   -29.791 -1.073  0.50 45.24 ? 52  ASN B CA    1 
ATOM   7619  C  CA    B ASN B 2 52  ? 2.309   -29.682 -0.362  0.50 44.99 ? 52  ASN B CA    1 
ATOM   7620  C  C     A ASN B 2 52  ? 1.929   -31.146 -1.128  0.50 49.21 ? 52  ASN B C     1 
ATOM   7621  C  C     B ASN B 2 52  ? 1.550   -31.003 -0.251  0.50 47.45 ? 52  ASN B C     1 
ATOM   7622  O  O     A ASN B 2 52  ? 2.363   -32.044 -1.857  0.50 50.25 ? 52  ASN B O     1 
ATOM   7623  O  O     B ASN B 2 52  ? 2.137   -32.075 -0.088  0.50 46.03 ? 52  ASN B O     1 
ATOM   7624  C  CB    A ASN B 2 52  ? 2.762   -29.189 -2.471  0.50 45.41 ? 52  ASN B CB    1 
ATOM   7625  C  CB    B ASN B 2 52  ? 2.289   -29.168 -1.804  0.50 48.31 ? 52  ASN B CB    1 
ATOM   7626  C  CG    A ASN B 2 52  ? 2.922   -27.683 -2.446  0.50 47.73 ? 52  ASN B CG    1 
ATOM   7627  C  CG    B ASN B 2 52  ? 2.428   -27.660 -1.889  0.50 48.90 ? 52  ASN B CG    1 
ATOM   7628  O  OD1   A ASN B 2 52  ? 2.216   -26.985 -1.719  0.50 52.04 ? 52  ASN B OD1   1 
ATOM   7629  O  OD1   B ASN B 2 52  ? 1.961   -26.934 -1.011  0.50 53.93 ? 52  ASN B OD1   1 
ATOM   7630  N  ND2   A ASN B 2 52  ? 3.854   -27.172 -3.244  0.50 49.57 ? 52  ASN B ND2   1 
ATOM   7631  N  ND2   B ASN B 2 52  ? 3.067   -27.180 -2.951  0.50 48.61 ? 52  ASN B ND2   1 
ATOM   7632  N  N     A GLU B 2 53  ? 0.855   -31.296 -0.359  0.50 50.02 ? 53  GLU B N     1 
ATOM   7633  N  N     B GLU B 2 53  ? 0.223   -30.918 -0.338  0.50 48.58 ? 53  GLU B N     1 
ATOM   7634  C  CA    A GLU B 2 53  ? 0.132   -32.559 -0.341  0.50 55.32 ? 53  GLU B CA    1 
ATOM   7635  C  CA    B GLU B 2 53  ? -0.652  -32.086 -0.269  0.50 55.60 ? 53  GLU B CA    1 
ATOM   7636  C  C     A GLU B 2 53  ? -0.648  -32.744 -1.637  0.50 57.68 ? 53  GLU B C     1 
ATOM   7637  C  C     B GLU B 2 53  ? -1.223  -32.353 -1.655  0.50 58.45 ? 53  GLU B C     1 
ATOM   7638  O  O     A GLU B 2 53  ? -1.254  -31.803 -2.156  0.50 60.01 ? 53  GLU B O     1 
ATOM   7639  O  O     B GLU B 2 53  ? -2.104  -31.622 -2.121  0.50 59.73 ? 53  GLU B O     1 
ATOM   7640  C  CB    A GLU B 2 53  ? -0.816  -32.621 0.857   0.50 55.58 ? 53  GLU B CB    1 
ATOM   7641  C  CB    B GLU B 2 53  ? -1.773  -31.885 0.748   0.50 55.81 ? 53  GLU B CB    1 
ATOM   7642  C  CG    A GLU B 2 53  ? -1.515  -33.963 1.010   0.50 58.26 ? 53  GLU B CG    1 
ATOM   7643  C  CG    B GLU B 2 53  ? -1.417  -32.293 2.164   0.50 53.88 ? 53  GLU B CG    1 
ATOM   7644  C  CD    A GLU B 2 53  ? -2.476  -33.997 2.180   0.50 52.32 ? 53  GLU B CD    1 
ATOM   7645  C  CD    B GLU B 2 53  ? -2.634  -32.378 3.066   0.50 57.07 ? 53  GLU B CD    1 
ATOM   7646  O  OE1   A GLU B 2 53  ? -2.698  -32.937 2.802   0.50 60.58 ? 53  GLU B OE1   1 
ATOM   7647  O  OE1   B GLU B 2 53  ? -3.757  -32.109 2.583   0.50 44.40 ? 53  GLU B OE1   1 
ATOM   7648  O  OE2   A GLU B 2 53  ? -3.011  -35.086 2.478   0.50 53.58 ? 53  GLU B OE2   1 
ATOM   7649  O  OE2   B GLU B 2 53  ? -2.468  -32.719 4.256   0.50 49.32 ? 53  GLU B OE2   1 
ATOM   7650  N  N     A ALA B 2 54  ? -0.626  -33.965 -2.158  0.50 59.32 ? 54  ALA B N     1 
ATOM   7651  N  N     B ALA B 2 54  ? -0.726  -33.402 -2.305  0.50 58.88 ? 54  ALA B N     1 
ATOM   7652  C  CA    A ALA B 2 54  ? -1.319  -34.316 -3.390  0.50 60.93 ? 54  ALA B CA    1 
ATOM   7653  C  CA    B ALA B 2 54  ? -1.245  -33.826 -3.595  0.50 60.05 ? 54  ALA B CA    1 
ATOM   7654  C  C     A ALA B 2 54  ? -2.321  -35.438 -3.112  0.50 64.03 ? 54  ALA B C     1 
ATOM   7655  C  C     B ALA B 2 54  ? -2.384  -34.826 -3.395  0.50 62.65 ? 54  ALA B C     1 
ATOM   7656  O  O     A ALA B 2 54  ? -2.600  -35.784 -1.960  0.50 62.01 ? 54  ALA B O     1 
ATOM   7657  O  O     B ALA B 2 54  ? -2.760  -35.166 -2.270  0.50 63.69 ? 54  ALA B O     1 
ATOM   7658  C  CB    A ALA B 2 54  ? -0.314  -34.709 -4.475  0.50 60.84 ? 54  ALA B CB    1 
ATOM   7659  C  CB    B ALA B 2 54  ? -0.129  -34.419 -4.453  0.50 60.39 ? 54  ALA B CB    1 
ATOM   7660  N  N     A THR B 2 55  ? -2.866  -36.004 -4.186  0.50 64.39 ? 55  THR B N     1 
ATOM   7661  N  N     B THR B 2 55  ? -2.942  -35.305 -4.504  0.50 65.01 ? 55  THR B N     1 
ATOM   7662  C  CA    A THR B 2 55  ? -3.837  -37.079 -4.071  0.50 65.17 ? 55  THR B CA    1 
ATOM   7663  C  CA    B THR B 2 55  ? -4.042  -36.258 -4.433  0.50 64.85 ? 55  THR B CA    1 
ATOM   7664  C  C     A THR B 2 55  ? -3.133  -38.420 -3.881  0.50 65.19 ? 55  THR B C     1 
ATOM   7665  C  C     B THR B 2 55  ? -3.538  -37.628 -3.995  0.50 65.82 ? 55  THR B C     1 
ATOM   7666  O  O     A THR B 2 55  ? -1.976  -38.608 -4.268  0.50 62.32 ? 55  THR B O     1 
ATOM   7667  O  O     B THR B 2 55  ? -2.471  -38.083 -4.419  0.50 63.32 ? 55  THR B O     1 
ATOM   7668  C  CB    A THR B 2 55  ? -4.737  -37.132 -5.306  0.50 61.43 ? 55  THR B CB    1 
ATOM   7669  C  CB    B THR B 2 55  ? -4.746  -36.367 -5.786  0.50 63.26 ? 55  THR B CB    1 
ATOM   7670  N  N     A GLY B 2 56  ? -3.855  -39.362 -3.279  0.50 61.03 ? 56  GLY B N     1 
ATOM   7671  N  N     B GLY B 2 56  ? -4.318  -38.287 -3.143  0.50 60.38 ? 56  GLY B N     1 
ATOM   7672  C  CA    A GLY B 2 56  ? -3.277  -40.653 -2.964  0.50 59.94 ? 56  GLY B CA    1 
ATOM   7673  C  CA    B GLY B 2 56  ? -3.955  -39.580 -2.606  0.50 63.02 ? 56  GLY B CA    1 
ATOM   7674  C  C     A GLY B 2 56  ? -2.344  -40.634 -1.777  0.50 66.96 ? 56  GLY B C     1 
ATOM   7675  C  C     B GLY B 2 56  ? -3.256  -39.555 -1.265  0.50 66.43 ? 56  GLY B C     1 
ATOM   7676  O  O     A GLY B 2 56  ? -1.438  -41.471 -1.698  0.50 65.58 ? 56  GLY B O     1 
ATOM   7677  O  O     B GLY B 2 56  ? -2.763  -40.602 -0.830  0.50 67.30 ? 56  GLY B O     1 
ATOM   7678  N  N     A ASN B 2 57  ? -2.543  -39.696 -0.847  0.50 66.60 ? 57  ASN B N     1 
ATOM   7679  N  N     B ASN B 2 57  ? -3.209  -38.399 -0.596  0.50 62.08 ? 57  ASN B N     1 
ATOM   7680  C  CA    A ASN B 2 57  ? -1.678  -39.532 0.323   0.50 65.66 ? 57  ASN B CA    1 
ATOM   7681  C  CA    B ASN B 2 57  ? -2.486  -38.228 0.667   0.50 63.53 ? 57  ASN B CA    1 
ATOM   7682  C  C     A ASN B 2 57  ? -0.229  -39.282 -0.091  0.50 61.67 ? 57  ASN B C     1 
ATOM   7683  C  C     B ASN B 2 57  ? -0.988  -38.466 0.475   0.50 66.46 ? 57  ASN B C     1 
ATOM   7684  O  O     A ASN B 2 57  ? 0.707   -39.815 0.507   0.50 60.92 ? 57  ASN B O     1 
ATOM   7685  O  O     B ASN B 2 57  ? -0.340  -39.182 1.243   0.50 62.99 ? 57  ASN B O     1 
ATOM   7686  C  CB    A ASN B 2 57  ? -1.778  -40.735 1.265   0.50 62.68 ? 57  ASN B CB    1 
ATOM   7687  C  CB    B ASN B 2 57  ? -3.055  -39.130 1.767   0.50 64.69 ? 57  ASN B CB    1 
ATOM   7688  N  N     A LYS B 2 58  ? -0.044  -38.462 -1.122  0.50 64.15 ? 58  LYS B N     1 
ATOM   7689  N  N     B LYS B 2 58  ? -0.438  -37.853 -0.570  0.50 63.33 ? 58  LYS B N     1 
ATOM   7690  C  CA    A LYS B 2 58  ? 1.279   -38.114 -1.618  0.50 64.24 ? 58  LYS B CA    1 
ATOM   7691  C  CA    B LYS B 2 58  ? 0.990   -37.892 -0.859  0.50 63.10 ? 58  LYS B CA    1 
ATOM   7692  C  C     A LYS B 2 58  ? 1.721   -36.764 -1.067  0.50 60.65 ? 58  LYS B C     1 
ATOM   7693  C  C     B LYS B 2 58  ? 1.547   -36.480 -0.768  0.50 59.47 ? 58  LYS B C     1 
ATOM   7694  O  O     A LYS B 2 58  ? 0.905   -35.870 -0.826  0.50 57.49 ? 58  LYS B O     1 
ATOM   7695  O  O     B LYS B 2 58  ? 0.956   -35.539 -1.311  0.50 56.96 ? 58  LYS B O     1 
ATOM   7696  C  CB    A LYS B 2 58  ? 1.307   -38.078 -3.149  0.50 61.55 ? 58  LYS B CB    1 
ATOM   7697  C  CB    B LYS B 2 58  ? 1.267   -38.493 -2.243  0.50 64.91 ? 58  LYS B CB    1 
ATOM   7698  C  CG    A LYS B 2 58  ? 1.169   -39.435 -3.818  0.50 67.99 ? 58  LYS B CG    1 
ATOM   7699  C  CG    B LYS B 2 58  ? 1.452   -40.009 -2.247  0.50 66.77 ? 58  LYS B CG    1 
ATOM   7700  C  CD    A LYS B 2 58  ? 1.503   -39.346 -5.299  0.50 73.00 ? 58  LYS B CD    1 
ATOM   7701  C  CD    B LYS B 2 58  ? 0.184   -40.729 -1.817  0.50 65.94 ? 58  LYS B CD    1 
ATOM   7702  C  CE    A LYS B 2 58  ? 1.216   -40.654 -6.019  0.50 75.24 ? 58  LYS B CE    1 
ATOM   7703  C  CE    B LYS B 2 58  ? 0.419   -42.212 -1.589  0.50 64.36 ? 58  LYS B CE    1 
ATOM   7704  N  NZ    A LYS B 2 58  ? -0.245  -40.932 -6.101  0.50 71.69 ? 58  LYS B NZ    1 
ATOM   7705  N  NZ    B LYS B 2 58  ? -0.770  -42.866 -0.981  0.50 61.73 ? 58  LYS B NZ    1 
ATOM   7706  N  N     A TYR B 2 59  ? 3.032   -36.625 -0.877  0.50 59.55 ? 59  TYR B N     1 
ATOM   7707  N  N     B TYR B 2 59  ? 2.680   -36.335 -0.087  0.50 59.99 ? 59  TYR B N     1 
ATOM   7708  C  CA    A TYR B 2 59  ? 3.642   -35.394 -0.377  0.50 51.48 ? 59  TYR B CA    1 
ATOM   7709  C  CA    B TYR B 2 59  ? 3.275   -35.033 0.185   0.50 52.17 ? 59  TYR B CA    1 
ATOM   7710  C  C     A TYR B 2 59  ? 4.775   -35.010 -1.324  0.50 52.54 ? 59  TYR B C     1 
ATOM   7711  C  C     B TYR B 2 59  ? 4.419   -34.780 -0.788  0.50 51.15 ? 59  TYR B C     1 
ATOM   7712  O  O     A TYR B 2 59  ? 5.848   -35.621 -1.297  0.50 52.20 ? 59  TYR B O     1 
ATOM   7713  O  O     B TYR B 2 59  ? 5.357   -35.581 -0.875  0.50 53.31 ? 59  TYR B O     1 
ATOM   7714  C  CB    A TYR B 2 59  ? 4.150   -35.567 1.050   0.50 50.53 ? 59  TYR B CB    1 
ATOM   7715  C  CB    B TYR B 2 59  ? 3.764   -34.957 1.631   0.50 52.95 ? 59  TYR B CB    1 
ATOM   7716  C  CG    A TYR B 2 59  ? 3.058   -35.654 2.092   0.50 53.92 ? 59  TYR B CG    1 
ATOM   7717  C  CG    B TYR B 2 59  ? 2.695   -35.299 2.643   0.50 51.67 ? 59  TYR B CG    1 
ATOM   7718  C  CD1   A TYR B 2 59  ? 2.477   -34.505 2.611   0.50 51.33 ? 59  TYR B CD1   1 
ATOM   7719  C  CD1   B TYR B 2 59  ? 1.793   -34.338 3.081   0.50 53.85 ? 59  TYR B CD1   1 
ATOM   7720  C  CD2   A TYR B 2 59  ? 2.617   -36.882 2.565   0.50 55.17 ? 59  TYR B CD2   1 
ATOM   7721  C  CD2   B TYR B 2 59  ? 2.583   -36.585 3.154   0.50 55.57 ? 59  TYR B CD2   1 
ATOM   7722  C  CE1   A TYR B 2 59  ? 1.482   -34.576 3.566   0.50 56.38 ? 59  TYR B CE1   1 
ATOM   7723  C  CE1   B TYR B 2 59  ? 0.811   -34.649 4.004   0.50 56.91 ? 59  TYR B CE1   1 
ATOM   7724  C  CE2   A TYR B 2 59  ? 1.622   -36.964 3.521   0.50 57.02 ? 59  TYR B CE2   1 
ATOM   7725  C  CE2   B TYR B 2 59  ? 1.606   -36.905 4.078   0.50 56.61 ? 59  TYR B CE2   1 
ATOM   7726  C  CZ    A TYR B 2 59  ? 1.058   -35.808 4.018   0.50 57.24 ? 59  TYR B CZ    1 
ATOM   7727  C  CZ    B TYR B 2 59  ? 0.723   -35.933 4.498   0.50 57.10 ? 59  TYR B CZ    1 
ATOM   7728  O  OH    A TYR B 2 59  ? 0.067   -35.882 4.970   0.50 58.32 ? 59  TYR B OH    1 
ATOM   7729  O  OH    B TYR B 2 59  ? -0.252  -36.248 5.415   0.50 59.30 ? 59  TYR B OH    1 
ATOM   7730  N  N     A VAL B 2 60  ? 4.538   -34.008 -2.156  0.50 43.65 ? 60  VAL B N     1 
ATOM   7731  N  N     B VAL B 2 60  ? 4.341   -33.671 -1.508  0.50 45.24 ? 60  VAL B N     1 
ATOM   7732  C  CA    A VAL B 2 60  ? 5.540   -33.494 -3.086  0.50 46.59 ? 60  VAL B CA    1 
ATOM   7733  C  CA    B VAL B 2 60  ? 5.338   -33.279 -2.502  0.50 46.38 ? 60  VAL B CA    1 
ATOM   7734  C  C     A VAL B 2 60  ? 6.224   -32.297 -2.436  0.50 43.34 ? 60  VAL B C     1 
ATOM   7735  C  C     B VAL B 2 60  ? 6.112   -32.089 -1.951  0.50 42.06 ? 60  VAL B C     1 
ATOM   7736  O  O     A VAL B 2 60  ? 5.530   -31.360 -2.015  0.50 44.70 ? 60  VAL B O     1 
ATOM   7737  O  O     B VAL B 2 60  ? 5.491   -31.114 -1.510  0.50 44.08 ? 60  VAL B O     1 
ATOM   7738  C  CB    A VAL B 2 60  ? 4.913   -33.097 -4.434  0.50 50.42 ? 60  VAL B CB    1 
ATOM   7739  C  CB    B VAL B 2 60  ? 4.687   -32.923 -3.852  0.50 49.09 ? 60  VAL B CB    1 
ATOM   7740  C  CG1   A VAL B 2 60  ? 5.961   -32.481 -5.345  0.50 49.69 ? 60  VAL B CG1   1 
ATOM   7741  C  CG1   B VAL B 2 60  ? 5.751   -32.642 -4.900  0.50 47.98 ? 60  VAL B CG1   1 
ATOM   7742  C  CG2   A VAL B 2 60  ? 4.272   -34.308 -5.095  0.50 52.52 ? 60  VAL B CG2   1 
ATOM   7743  C  CG2   B VAL B 2 60  ? 3.758   -34.042 -4.305  0.50 51.12 ? 60  VAL B CG2   1 
ATOM   7744  N  N     A PRO B 2 61  ? 7.551   -32.287 -2.328  0.50 47.74 ? 61  PRO B N     1 
ATOM   7745  N  N     B PRO B 2 61  ? 7.445   -32.123 -1.950  0.50 47.32 ? 61  PRO B N     1 
ATOM   7746  C  CA    A PRO B 2 61  ? 8.232   -31.121 -1.754  0.50 43.03 ? 61  PRO B CA    1 
ATOM   7747  C  CA    B PRO B 2 61  ? 8.210   -30.979 -1.439  0.50 42.37 ? 61  PRO B CA    1 
ATOM   7748  C  C     A PRO B 2 61  ? 7.984   -29.874 -2.588  0.50 40.29 ? 61  PRO B C     1 
ATOM   7749  C  C     B PRO B 2 61  ? 7.961   -29.726 -2.263  0.50 40.80 ? 61  PRO B C     1 
ATOM   7750  O  O     A PRO B 2 61  ? 8.017   -29.911 -3.819  0.50 42.24 ? 61  PRO B O     1 
ATOM   7751  O  O     B PRO B 2 61  ? 7.777   -29.783 -3.481  0.50 41.77 ? 61  PRO B O     1 
ATOM   7752  C  CB    A PRO B 2 61  ? 9.712   -31.525 -1.779  0.50 44.47 ? 61  PRO B CB    1 
ATOM   7753  C  CB    B PRO B 2 61  ? 9.667   -31.446 -1.555  0.50 44.62 ? 61  PRO B CB    1 
ATOM   7754  C  CG    A PRO B 2 61  ? 9.705   -33.014 -1.848  0.50 44.15 ? 61  PRO B CG    1 
ATOM   7755  C  CG    B PRO B 2 61  ? 9.591   -32.931 -1.592  0.50 44.08 ? 61  PRO B CG    1 
ATOM   7756  C  CD    A PRO B 2 61  ? 8.489   -33.377 -2.645  0.50 44.82 ? 61  PRO B CD    1 
ATOM   7757  C  CD    B PRO B 2 61  ? 8.318   -33.248 -2.317  0.50 44.70 ? 61  PRO B CD    1 
ATOM   7758  N  N     A ARG B 2 62  ? 7.719   -28.761 -1.903  0.50 41.84 ? 62  ARG B N     1 
ATOM   7759  N  N     B ARG B 2 62  ? 7.957   -28.585 -1.581  0.50 41.29 ? 62  ARG B N     1 
ATOM   7760  C  CA    A ARG B 2 62  ? 7.686   -27.458 -2.564  0.50 35.57 ? 62  ARG B CA    1 
ATOM   7761  C  CA    B ARG B 2 62  ? 7.742   -27.285 -2.215  0.50 36.72 ? 62  ARG B CA    1 
ATOM   7762  C  C     A ARG B 2 62  ? 9.137   -27.083 -2.850  0.50 42.01 ? 62  ARG B C     1 
ATOM   7763  C  C     B ARG B 2 62  ? 9.060   -26.688 -2.701  0.50 41.60 ? 62  ARG B C     1 
ATOM   7764  O  O     A ARG B 2 62  ? 9.798   -26.371 -2.092  0.50 37.18 ? 62  ARG B O     1 
ATOM   7765  O  O     B ARG B 2 62  ? 9.411   -25.550 -2.385  0.50 32.26 ? 62  ARG B O     1 
ATOM   7766  C  CB    A ARG B 2 62  ? 6.980   -26.409 -1.712  0.50 38.55 ? 62  ARG B CB    1 
ATOM   7767  C  CB    B ARG B 2 62  ? 7.036   -26.351 -1.240  0.50 36.74 ? 62  ARG B CB    1 
ATOM   7768  C  CG    A ARG B 2 62  ? 6.600   -25.153 -2.492  0.50 36.15 ? 62  ARG B CG    1 
ATOM   7769  C  CG    B ARG B 2 62  ? 6.286   -25.203 -1.890  0.50 37.08 ? 62  ARG B CG    1 
ATOM   7770  C  CD    A ARG B 2 62  ? 5.704   -24.209 -1.697  0.50 42.09 ? 62  ARG B CD    1 
ATOM   7771  C  CD    B ARG B 2 62  ? 5.518   -24.385 -0.856  0.50 45.27 ? 62  ARG B CD    1 
ATOM   7772  N  NE    A ARG B 2 62  ? 4.449   -24.830 -1.291  0.50 48.40 ? 62  ARG B NE    1 
ATOM   7773  N  NE    B ARG B 2 62  ? 4.398   -25.115 -0.271  0.50 44.39 ? 62  ARG B NE    1 
ATOM   7774  C  CZ    A ARG B 2 62  ? 4.220   -25.340 -0.088  0.50 44.52 ? 62  ARG B CZ    1 
ATOM   7775  C  CZ    B ARG B 2 62  ? 4.441   -25.753 0.891   0.50 43.14 ? 62  ARG B CZ    1 
ATOM   7776  N  NH1   A ARG B 2 62  ? 5.147   -25.326 0.856   0.50 41.50 ? 62  ARG B NH1   1 
ATOM   7777  N  NH1   B ARG B 2 62  ? 5.542   -25.781 1.622   0.50 42.12 ? 62  ARG B NH1   1 
ATOM   7778  N  NH2   A ARG B 2 62  ? 3.032   -25.878 0.174   0.50 42.94 ? 62  ARG B NH2   1 
ATOM   7779  N  NH2   B ARG B 2 62  ? 3.354   -26.380 1.329   0.50 40.71 ? 62  ARG B NH2   1 
ATOM   7780  N  N     A ALA B 2 63  ? 9.646   -27.606 -3.964  0.50 36.63 ? 63  ALA B N     1 
ATOM   7781  N  N     B ALA B 2 63  ? 9.800   -27.469 -3.484  0.50 37.17 ? 63  ALA B N     1 
ATOM   7782  C  CA    A ALA B 2 63  ? 11.052  -27.475 -4.310  0.50 39.43 ? 63  ALA B CA    1 
ATOM   7783  C  CA    B ALA B 2 63  ? 11.143  -27.115 -3.918  0.50 39.20 ? 63  ALA B CA    1 
ATOM   7784  C  C     A ALA B 2 63  ? 11.179  -27.156 -5.790  0.50 38.81 ? 63  ALA B C     1 
ATOM   7785  C  C     B ALA B 2 63  ? 11.177  -26.850 -5.417  0.50 37.43 ? 63  ALA B C     1 
ATOM   7786  O  O     A ALA B 2 63  ? 10.506  -27.770 -6.623  0.50 40.92 ? 63  ALA B O     1 
ATOM   7787  O  O     B ALA B 2 63  ? 10.484  -27.515 -6.194  0.50 41.45 ? 63  ALA B O     1 
ATOM   7788  C  CB    A ALA B 2 63  ? 11.826  -28.754 -3.972  0.50 36.37 ? 63  ALA B CB    1 
ATOM   7789  C  CB    B ALA B 2 63  ? 12.138  -28.227 -3.574  0.50 37.57 ? 63  ALA B CB    1 
ATOM   7790  N  N     A ILE B 2 64  ? 12.038  -26.193 -6.105  0.50 39.32 ? 64  ILE B N     1 
ATOM   7791  N  N     B ILE B 2 64  ? 11.999  -25.881 -5.811  0.50 38.92 ? 64  ILE B N     1 
ATOM   7792  C  CA    A ILE B 2 64  ? 12.329  -25.792 -7.474  0.50 36.51 ? 64  ILE B CA    1 
ATOM   7793  C  CA    B ILE B 2 64  ? 12.240  -25.539 -7.206  0.50 36.19 ? 64  ILE B CA    1 
ATOM   7794  C  C     A ILE B 2 64  ? 13.821  -26.011 -7.685  0.50 38.64 ? 64  ILE B C     1 
ATOM   7795  C  C     B ILE B 2 64  ? 13.720  -25.750 -7.489  0.50 37.76 ? 64  ILE B C     1 
ATOM   7796  O  O     A ILE B 2 64  ? 14.647  -25.343 -7.050  0.50 35.77 ? 64  ILE B O     1 
ATOM   7797  O  O     B ILE B 2 64  ? 14.572  -25.368 -6.679  0.50 34.98 ? 64  ILE B O     1 
ATOM   7798  C  CB    A ILE B 2 64  ? 11.932  -24.334 -7.739  0.50 37.94 ? 64  ILE B CB    1 
ATOM   7799  C  CB    B ILE B 2 64  ? 11.822  -24.085 -7.508  0.50 38.14 ? 64  ILE B CB    1 
ATOM   7800  C  CG1   A ILE B 2 64  ? 10.475  -24.111 -7.325  0.50 39.49 ? 64  ILE B CG1   1 
ATOM   7801  C  CG1   B ILE B 2 64  ? 10.334  -23.894 -7.205  0.50 39.53 ? 64  ILE B CG1   1 
ATOM   7802  C  CG2   A ILE B 2 64  ? 12.136  -23.976 -9.206  0.50 40.76 ? 64  ILE B CG2   1 
ATOM   7803  C  CG2   B ILE B 2 64  ? 12.140  -23.720 -8.949  0.50 40.67 ? 64  ILE B CG2   1 
ATOM   7804  C  CD1   A ILE B 2 64  ? 10.068  -22.662 -7.258  0.50 38.76 ? 64  ILE B CD1   1 
ATOM   7805  C  CD1   B ILE B 2 64  ? 9.929   -22.455 -7.008  0.50 37.85 ? 64  ILE B CD1   1 
ATOM   7806  N  N     A LEU B 2 65  ? 14.168  -26.954 -8.561  0.50 40.30 ? 65  LEU B N     1 
ATOM   7807  N  N     B LEU B 2 65  ? 14.024  -26.363 -8.632  0.50 40.18 ? 65  LEU B N     1 
ATOM   7808  C  CA    A LEU B 2 65  ? 15.554  -27.333 -8.815  0.50 36.76 ? 65  LEU B CA    1 
ATOM   7809  C  CA    B LEU B 2 65  ? 15.386  -26.740 -8.991  0.50 38.22 ? 65  LEU B CA    1 
ATOM   7810  C  C     A LEU B 2 65  ? 16.038  -26.633 -10.080 0.50 41.23 ? 65  LEU B C     1 
ATOM   7811  C  C     B LEU B 2 65  ? 15.792  -26.005 -10.261 0.50 40.93 ? 65  LEU B C     1 
ATOM   7812  O  O     A LEU B 2 65  ? 15.425  -26.776 -11.143 0.50 38.96 ? 65  LEU B O     1 
ATOM   7813  O  O     B LEU B 2 65  ? 15.034  -25.979 -11.235 0.50 40.76 ? 65  LEU B O     1 
ATOM   7814  C  CB    A LEU B 2 65  ? 15.692  -28.850 -8.953  0.50 37.49 ? 65  LEU B CB    1 
ATOM   7815  C  CB    B LEU B 2 65  ? 15.502  -28.258 -9.186  0.50 38.49 ? 65  LEU B CB    1 
ATOM   7816  C  CG    A LEU B 2 65  ? 15.467  -29.747 -7.730  0.50 44.67 ? 65  LEU B CG    1 
ATOM   7817  C  CG    B LEU B 2 65  ? 15.035  -29.180 -8.053  0.50 42.68 ? 65  LEU B CG    1 
ATOM   7818  C  CD1   A LEU B 2 65  ? 13.988  -29.926 -7.408  0.50 41.33 ? 65  LEU B CD1   1 
ATOM   7819  C  CD1   B LEU B 2 65  ? 13.535  -29.454 -8.106  0.50 43.69 ? 65  LEU B CD1   1 
ATOM   7820  C  CD2   A LEU B 2 65  ? 16.135  -31.101 -7.939  0.50 46.13 ? 65  LEU B CD2   1 
ATOM   7821  C  CD2   B LEU B 2 65  ? 15.810  -30.486 -8.076  0.50 46.49 ? 65  LEU B CD2   1 
ATOM   7822  N  N     A VAL B 2 66  ? 17.140  -25.889 -9.967  0.50 39.46 ? 66  VAL B N     1 
ATOM   7823  N  N     B VAL B 2 66  ? 16.985  -25.411 -10.252 0.50 37.53 ? 66  VAL B N     1 
ATOM   7824  C  CA    A VAL B 2 66  ? 17.627  -25.018 -11.031 0.50 39.69 ? 66  VAL B CA    1 
ATOM   7825  C  CA    B VAL B 2 66  ? 17.454  -24.615 -11.383 0.50 39.81 ? 66  VAL B CA    1 
ATOM   7826  C  C     A VAL B 2 66  ? 19.110  -25.282 -11.257 0.50 37.42 ? 66  VAL B C     1 
ATOM   7827  C  C     B VAL B 2 66  ? 18.966  -24.762 -11.502 0.50 37.67 ? 66  VAL B C     1 
ATOM   7828  O  O     A VAL B 2 66  ? 19.853  -25.543 -10.305 0.50 33.92 ? 66  VAL B O     1 
ATOM   7829  O  O     B VAL B 2 66  ? 19.680  -24.815 -10.497 0.50 38.49 ? 66  VAL B O     1 
ATOM   7830  C  CB    A VAL B 2 66  ? 17.394  -23.529 -10.688 0.50 38.95 ? 66  VAL B CB    1 
ATOM   7831  C  CB    B VAL B 2 66  ? 17.038  -23.132 -11.234 0.50 40.80 ? 66  VAL B CB    1 
ATOM   7832  C  CG1   A VAL B 2 66  ? 17.784  -22.632 -11.855 0.50 40.24 ? 66  VAL B CG1   1 
ATOM   7833  C  CG1   B VAL B 2 66  ? 17.496  -22.572 -9.898  0.50 40.02 ? 66  VAL B CG1   1 
ATOM   7834  C  CG2   A VAL B 2 66  ? 15.946  -23.288 -10.279 0.50 38.47 ? 66  VAL B CG2   1 
ATOM   7835  C  CG2   B VAL B 2 66  ? 17.588  -22.292 -12.380 0.50 41.31 ? 66  VAL B CG2   1 
ATOM   7836  N  N     A ASP B 2 67  ? 19.538  -25.213 -12.518 0.50 41.08 ? 67  ASP B N     1 
ATOM   7837  N  N     B ASP B 2 67  ? 19.446  -24.844 -12.743 0.50 41.41 ? 67  ASP B N     1 
ATOM   7838  C  CA    A ASP B 2 67  ? 20.953  -25.228 -12.874 0.50 40.10 ? 67  ASP B CA    1 
ATOM   7839  C  CA    B ASP B 2 67  ? 20.869  -24.774 -13.049 0.50 40.36 ? 67  ASP B CA    1 
ATOM   7840  C  C     A ASP B 2 67  ? 21.089  -24.939 -14.362 0.50 45.43 ? 67  ASP B C     1 
ATOM   7841  C  C     B ASP B 2 67  ? 21.029  -24.573 -14.548 0.50 45.58 ? 67  ASP B C     1 
ATOM   7842  O  O     A ASP B 2 67  ? 20.138  -25.097 -15.133 0.50 45.95 ? 67  ASP B O     1 
ATOM   7843  O  O     B ASP B 2 67  ? 20.306  -25.182 -15.340 0.50 45.58 ? 67  ASP B O     1 
ATOM   7844  C  CB    A ASP B 2 67  ? 21.622  -26.563 -12.531 0.50 41.55 ? 67  ASP B CB    1 
ATOM   7845  C  CB    B ASP B 2 67  ? 21.615  -26.039 -12.603 0.50 40.47 ? 67  ASP B CB    1 
ATOM   7846  C  CG    A ASP B 2 67  ? 23.138  -26.471 -12.531 0.50 40.96 ? 67  ASP B CG    1 
ATOM   7847  C  CG    B ASP B 2 67  ? 23.124  -25.857 -12.591 0.50 40.28 ? 67  ASP B CG    1 
ATOM   7848  O  OD1   A ASP B 2 67  ? 23.672  -25.402 -12.894 0.50 40.33 ? 67  ASP B OD1   1 
ATOM   7849  O  OD1   B ASP B 2 67  ? 23.629  -24.937 -13.270 0.50 38.91 ? 67  ASP B OD1   1 
ATOM   7850  O  OD2   A ASP B 2 67  ? 23.797  -27.462 -12.161 0.50 42.99 ? 67  ASP B OD2   1 
ATOM   7851  O  OD2   B ASP B 2 67  ? 23.808  -26.638 -11.899 0.50 41.63 ? 67  ASP B OD2   1 
ATOM   7852  N  N     A LEU B 2 68  ? 22.288  -24.507 -14.753 0.50 44.05 ? 68  LEU B N     1 
ATOM   7853  N  N     B LEU B 2 68  ? 21.982  -23.721 -14.926 0.50 41.76 ? 68  LEU B N     1 
ATOM   7854  C  CA    A LEU B 2 68  ? 22.611  -24.302 -16.159 0.50 45.32 ? 68  LEU B CA    1 
ATOM   7855  C  CA    B LEU B 2 68  ? 22.258  -23.457 -16.332 0.50 42.70 ? 68  LEU B CA    1 
ATOM   7856  C  C     A LEU B 2 68  ? 23.251  -25.525 -16.795 0.50 44.45 ? 68  LEU B C     1 
ATOM   7857  C  C     B LEU B 2 68  ? 22.802  -24.674 -17.073 0.50 43.58 ? 68  LEU B C     1 
ATOM   7858  O  O     A LEU B 2 68  ? 23.145  -25.708 -18.013 0.50 42.61 ? 68  LEU B O     1 
ATOM   7859  O  O     B LEU B 2 68  ? 22.910  -24.627 -18.303 0.50 39.15 ? 68  LEU B O     1 
ATOM   7860  C  CB    A LEU B 2 68  ? 23.552  -23.106 -16.325 0.50 40.21 ? 68  LEU B CB    1 
ATOM   7861  C  CB    B LEU B 2 68  ? 23.239  -22.289 -16.453 0.50 37.65 ? 68  LEU B CB    1 
ATOM   7862  C  CG    A LEU B 2 68  ? 23.010  -21.731 -15.945 0.50 38.44 ? 68  LEU B CG    1 
ATOM   7863  C  CG    B LEU B 2 68  ? 22.698  -20.929 -16.007 0.50 42.16 ? 68  LEU B CG    1 
ATOM   7864  C  CD1   A LEU B 2 68  ? 24.094  -20.682 -16.122 0.50 34.46 ? 68  LEU B CD1   1 
ATOM   7865  C  CD1   B LEU B 2 68  ? 23.828  -19.926 -15.811 0.50 34.88 ? 68  LEU B CD1   1 
ATOM   7866  C  CD2   A LEU B 2 68  ? 21.783  -21.388 -16.773 0.50 38.33 ? 68  LEU B CD2   1 
ATOM   7867  C  CD2   B LEU B 2 68  ? 21.679  -20.403 -17.008 0.50 35.47 ? 68  LEU B CD2   1 
ATOM   7868  N  N     A GLU B 2 69  ? 23.921  -26.360 -16.002 0.50 45.25 ? 69  GLU B N     1 
ATOM   7869  N  N     B GLU B 2 69  ? 23.139  -25.753 -16.367 0.50 41.66 ? 69  GLU B N     1 
ATOM   7870  C  CA    A GLU B 2 69  ? 24.553  -27.562 -16.528 0.50 48.37 ? 69  GLU B CA    1 
ATOM   7871  C  CA    B GLU B 2 69  ? 23.652  -26.970 -16.988 0.50 48.31 ? 69  GLU B CA    1 
ATOM   7872  C  C     A GLU B 2 69  ? 23.541  -28.697 -16.539 0.50 48.17 ? 69  GLU B C     1 
ATOM   7873  C  C     B GLU B 2 69  ? 22.704  -28.122 -16.681 0.50 47.13 ? 69  GLU B C     1 
ATOM   7874  O  O     A GLU B 2 69  ? 23.035  -29.069 -15.472 0.50 46.15 ? 69  GLU B O     1 
ATOM   7875  O  O     B GLU B 2 69  ? 22.422  -28.386 -15.499 0.50 43.07 ? 69  GLU B O     1 
ATOM   7876  C  CB    A GLU B 2 69  ? 25.762  -27.951 -15.692 0.50 45.47 ? 69  GLU B CB    1 
ATOM   7877  C  CB    B GLU B 2 69  ? 25.067  -27.278 -16.488 0.50 49.16 ? 69  GLU B CB    1 
ATOM   7878  C  CG    A GLU B 2 69  ? 26.951  -28.430 -16.517 0.50 46.89 ? 69  GLU B CG    1 
ATOM   7879  C  CG    B GLU B 2 69  ? 25.803  -28.351 -17.280 0.50 50.38 ? 69  GLU B CG    1 
ATOM   7880  C  CD    A GLU B 2 69  ? 26.588  -29.542 -17.484 0.50 46.91 ? 69  GLU B CD    1 
ATOM   7881  C  CD    B GLU B 2 69  ? 27.307  -28.324 -17.043 0.50 46.08 ? 69  GLU B CD    1 
ATOM   7882  O  OE1   A GLU B 2 69  ? 25.931  -30.516 -17.060 0.50 45.28 ? 69  GLU B OE1   1 
ATOM   7883  O  OE1   B GLU B 2 69  ? 27.832  -27.262 -16.644 0.50 38.73 ? 69  GLU B OE1   1 
ATOM   7884  O  OE2   A GLU B 2 69  ? 26.946  -29.434 -18.675 0.50 46.93 ? 69  GLU B OE2   1 
ATOM   7885  O  OE2   B GLU B 2 69  ? 27.966  -29.364 -17.256 0.50 42.42 ? 69  GLU B OE2   1 
ATOM   7886  N  N     A PRO B 2 70  ? 23.216  -29.270 -17.702 0.50 46.50 ? 70  PRO B N     1 
ATOM   7887  N  N     B PRO B 2 70  ? 22.185  -28.832 -17.689 0.50 44.05 ? 70  PRO B N     1 
ATOM   7888  C  CA    A PRO B 2 70  ? 22.194  -30.329 -17.746 0.50 44.83 ? 70  PRO B CA    1 
ATOM   7889  C  CA    B PRO B 2 70  ? 21.186  -29.880 -17.418 0.50 44.39 ? 70  PRO B CA    1 
ATOM   7890  C  C     A PRO B 2 70  ? 22.606  -31.628 -17.068 0.50 47.11 ? 70  PRO B C     1 
ATOM   7891  C  C     B PRO B 2 70  ? 21.759  -31.152 -16.810 0.50 45.80 ? 70  PRO B C     1 
ATOM   7892  O  O     A PRO B 2 70  ? 21.767  -32.528 -16.951 0.50 52.18 ? 70  PRO B O     1 
ATOM   7893  O  O     B PRO B 2 70  ? 20.976  -32.018 -16.398 0.50 49.30 ? 70  PRO B O     1 
ATOM   7894  C  CB    A PRO B 2 70  ? 21.972  -30.538 -19.250 0.50 44.95 ? 70  PRO B CB    1 
ATOM   7895  C  CB    B PRO B 2 70  ? 20.583  -30.151 -18.801 0.50 49.58 ? 70  PRO B CB    1 
ATOM   7896  C  CG    A PRO B 2 70  ? 23.232  -30.045 -19.892 0.50 49.20 ? 70  PRO B CG    1 
ATOM   7897  C  CG    B PRO B 2 70  ? 21.669  -29.797 -19.752 0.50 41.90 ? 70  PRO B CG    1 
ATOM   7898  C  CD    A PRO B 2 70  ? 23.686  -28.894 -19.047 0.50 44.06 ? 70  PRO B CD    1 
ATOM   7899  C  CD    B PRO B 2 70  ? 22.416  -28.645 -19.132 0.50 49.53 ? 70  PRO B CD    1 
ATOM   7900  N  N     A GLY B 2 71  ? 23.856  -31.766 -16.623 0.50 48.15 ? 71  GLY B N     1 
ATOM   7901  N  N     B GLY B 2 71  ? 23.084  -31.305 -16.749 0.50 46.57 ? 71  GLY B N     1 
ATOM   7902  C  CA    A GLY B 2 71  ? 24.254  -32.989 -15.946 0.50 46.72 ? 71  GLY B CA    1 
ATOM   7903  C  CA    B GLY B 2 71  ? 23.649  -32.469 -16.087 0.50 48.74 ? 71  GLY B CA    1 
ATOM   7904  C  C     A GLY B 2 71  ? 23.734  -33.095 -14.530 0.50 51.22 ? 71  GLY B C     1 
ATOM   7905  C  C     B GLY B 2 71  ? 23.260  -32.555 -14.625 0.50 50.50 ? 71  GLY B C     1 
ATOM   7906  O  O     A GLY B 2 71  ? 23.527  -34.204 -14.027 0.50 48.16 ? 71  GLY B O     1 
ATOM   7907  O  O     B GLY B 2 71  ? 23.070  -33.651 -14.090 0.50 47.61 ? 71  GLY B O     1 
ATOM   7908  N  N     A THR B 2 72  ? 23.502  -31.956 -13.873 0.50 47.41 ? 72  THR B N     1 
ATOM   7909  N  N     B THR B 2 72  ? 23.126  -31.403 -13.963 0.50 46.70 ? 72  THR B N     1 
ATOM   7910  C  CA    A THR B 2 72  ? 23.089  -31.970 -12.474 0.50 47.87 ? 72  THR B CA    1 
ATOM   7911  C  CA    B THR B 2 72  ? 22.659  -31.380 -12.582 0.50 50.35 ? 72  THR B CA    1 
ATOM   7912  C  C     A THR B 2 72  ? 21.716  -32.607 -12.291 0.50 53.32 ? 72  THR B C     1 
ATOM   7913  C  C     B THR B 2 72  ? 21.243  -31.930 -12.463 0.50 52.04 ? 72  THR B C     1 
ATOM   7914  O  O     A THR B 2 72  ? 21.457  -33.226 -11.252 0.50 48.06 ? 72  THR B O     1 
ATOM   7915  O  O     B THR B 2 72  ? 20.897  -32.544 -11.446 0.50 45.11 ? 72  THR B O     1 
ATOM   7916  C  CB    A THR B 2 72  ? 23.098  -30.545 -11.920 0.50 52.06 ? 72  THR B CB    1 
ATOM   7917  C  CB    B THR B 2 72  ? 22.724  -29.951 -12.041 0.50 49.05 ? 72  THR B CB    1 
ATOM   7918  O  OG1   A THR B 2 72  ? 24.330  -29.905 -12.279 0.50 47.61 ? 72  THR B OG1   1 
ATOM   7919  O  OG1   B THR B 2 72  ? 23.969  -29.354 -12.425 0.50 49.76 ? 72  THR B OG1   1 
ATOM   7920  C  CG2   A THR B 2 72  ? 22.964  -30.550 -10.403 0.50 45.37 ? 72  THR B CG2   1 
ATOM   7921  C  CG2   B THR B 2 72  ? 22.615  -29.945 -10.525 0.50 43.22 ? 72  THR B CG2   1 
ATOM   7922  N  N     A MET B 2 73  ? 20.827  -32.475 -13.279 0.50 51.97 ? 73  MET B N     1 
ATOM   7923  N  N     B MET B 2 73  ? 20.416  -31.726 -13.491 0.50 48.83 ? 73  MET B N     1 
ATOM   7924  C  CA    A MET B 2 73  ? 19.530  -33.135 -13.175 0.50 53.65 ? 73  MET B CA    1 
ATOM   7925  C  CA    B MET B 2 73  ? 19.061  -32.267 -13.476 0.50 53.34 ? 73  MET B CA    1 
ATOM   7926  C  C     A MET B 2 73  ? 19.674  -34.651 -13.205 0.50 50.56 ? 73  MET B C     1 
ATOM   7927  C  C     B MET B 2 73  ? 19.077  -33.791 -13.430 0.50 52.96 ? 73  MET B C     1 
ATOM   7928  O  O     A MET B 2 73  ? 18.825  -35.363 -12.660 0.50 47.99 ? 73  MET B O     1 
ATOM   7929  O  O     B MET B 2 73  ? 18.308  -34.406 -12.681 0.50 51.08 ? 73  MET B O     1 
ATOM   7930  C  CB    A MET B 2 73  ? 18.597  -32.665 -14.294 0.50 50.95 ? 73  MET B CB    1 
ATOM   7931  C  CB    B MET B 2 73  ? 18.295  -31.764 -14.701 0.50 51.23 ? 73  MET B CB    1 
ATOM   7932  C  CG    A MET B 2 73  ? 19.034  -33.076 -15.688 0.50 50.87 ? 73  MET B CG    1 
ATOM   7933  C  CG    B MET B 2 73  ? 16.842  -32.199 -14.779 0.50 52.30 ? 73  MET B CG    1 
ATOM   7934  S  SD    A MET B 2 73  ? 17.856  -32.636 -16.979 0.50 60.25 ? 73  MET B SD    1 
ATOM   7935  S  SD    B MET B 2 73  ? 15.939  -31.329 -16.082 0.50 58.86 ? 73  MET B SD    1 
ATOM   7936  C  CE    A MET B 2 73  ? 18.723  -33.212 -18.437 0.50 48.77 ? 73  MET B CE    1 
ATOM   7937  C  CE    B MET B 2 73  ? 16.791  -31.914 -17.546 0.50 49.61 ? 73  MET B CE    1 
ATOM   7938  N  N     A ASP B 2 74  ? 20.741  -35.161 -13.824 0.50 52.59 ? 74  ASP B N     1 
ATOM   7939  N  N     B ASP B 2 74  ? 19.961  -34.418 -14.211 0.50 51.40 ? 74  ASP B N     1 
ATOM   7940  C  CA    A ASP B 2 74  ? 20.945  -36.605 -13.870 0.50 51.35 ? 74  ASP B CA    1 
ATOM   7941  C  CA    B ASP B 2 74  ? 20.015  -35.876 -14.254 0.50 52.01 ? 74  ASP B CA    1 
ATOM   7942  C  C     A ASP B 2 74  ? 21.399  -37.145 -12.519 0.50 49.71 ? 74  ASP B C     1 
ATOM   7943  C  C     B ASP B 2 74  ? 20.525  -36.459 -12.942 0.50 49.97 ? 74  ASP B C     1 
ATOM   7944  O  O     A ASP B 2 74  ? 20.935  -38.204 -12.081 0.50 53.51 ? 74  ASP B O     1 
ATOM   7945  O  O     B ASP B 2 74  ? 19.966  -37.438 -12.435 0.50 49.40 ? 74  ASP B O     1 
ATOM   7946  C  CB    A ASP B 2 74  ? 21.961  -36.957 -14.957 0.50 48.22 ? 74  ASP B CB    1 
ATOM   7947  C  CB    B ASP B 2 74  ? 20.892  -36.333 -15.419 0.50 50.72 ? 74  ASP B CB    1 
ATOM   7948  C  CG    A ASP B 2 74  ? 21.546  -36.461 -16.329 0.50 49.79 ? 74  ASP B CG    1 
ATOM   7949  C  CG    B ASP B 2 74  ? 20.103  -36.536 -16.697 0.50 55.01 ? 74  ASP B CG    1 
ATOM   7950  O  OD1   A ASP B 2 74  ? 20.483  -35.816 -16.434 0.50 53.92 ? 74  ASP B OD1   1 
ATOM   7951  O  OD1   B ASP B 2 74  ? 19.105  -37.286 -16.664 0.50 49.42 ? 74  ASP B OD1   1 
ATOM   7952  O  OD2   A ASP B 2 74  ? 22.285  -36.717 -17.304 0.50 59.70 ? 74  ASP B OD2   1 
ATOM   7953  O  OD2   B ASP B 2 74  ? 20.475  -35.940 -17.731 0.50 49.60 ? 74  ASP B OD2   1 
ATOM   7954  N  N     A SER B 2 75  ? 22.307  -36.434 -11.844 0.50 49.66 ? 75  SER B N     1 
ATOM   7955  N  N     B SER B 2 75  ? 21.588  -35.877 -12.378 0.50 51.03 ? 75  SER B N     1 
ATOM   7956  C  CA    A SER B 2 75  ? 22.821  -36.923 -10.568 0.50 48.30 ? 75  SER B CA    1 
ATOM   7957  C  CA    B SER B 2 75  ? 22.170  -36.425 -11.157 0.50 51.30 ? 75  SER B CA    1 
ATOM   7958  C  C     A SER B 2 75  ? 21.769  -36.852 -9.469  0.50 53.09 ? 75  SER B C     1 
ATOM   7959  C  C     B SER B 2 75  ? 21.205  -36.320 -9.981  0.50 53.06 ? 75  SER B C     1 
ATOM   7960  O  O     A SER B 2 75  ? 21.796  -37.661 -8.535  0.50 53.61 ? 75  SER B O     1 
ATOM   7961  O  O     B SER B 2 75  ? 21.168  -37.208 -9.120  0.50 52.71 ? 75  SER B O     1 
ATOM   7962  C  CB    A SER B 2 75  ? 24.061  -36.129 -10.158 0.50 50.42 ? 75  SER B CB    1 
ATOM   7963  C  CB    B SER B 2 75  ? 23.484  -35.712 -10.839 0.50 49.06 ? 75  SER B CB    1 
ATOM   7964  O  OG    A SER B 2 75  ? 23.711  -34.839 -9.690  0.50 52.34 ? 75  SER B OG    1 
ATOM   7965  O  OG    B SER B 2 75  ? 23.287  -34.315 -10.714 0.50 51.86 ? 75  SER B OG    1 
ATOM   7966  N  N     A VAL B 2 76  ? 20.843  -35.896 -9.556  0.50 50.97 ? 76  VAL B N     1 
ATOM   7967  N  N     B VAL B 2 76  ? 20.418  -35.245 -9.924  0.50 48.35 ? 76  VAL B N     1 
ATOM   7968  C  CA    A VAL B 2 76  ? 19.783  -35.804 -8.558  0.50 52.45 ? 76  VAL B CA    1 
ATOM   7969  C  CA    B VAL B 2 76  ? 19.433  -35.106 -8.856  0.50 53.38 ? 76  VAL B CA    1 
ATOM   7970  C  C     A VAL B 2 76  ? 18.793  -36.952 -8.722  0.50 53.98 ? 76  VAL B C     1 
ATOM   7971  C  C     B VAL B 2 76  ? 18.311  -36.123 -9.031  0.50 51.85 ? 76  VAL B C     1 
ATOM   7972  O  O     A VAL B 2 76  ? 18.338  -37.541 -7.735  0.50 48.53 ? 76  VAL B O     1 
ATOM   7973  O  O     B VAL B 2 76  ? 17.898  -36.786 -8.071  0.50 51.09 ? 76  VAL B O     1 
ATOM   7974  C  CB    A VAL B 2 76  ? 19.086  -34.433 -8.644  0.50 52.31 ? 76  VAL B CB    1 
ATOM   7975  C  CB    B VAL B 2 76  ? 18.891  -33.667 -8.806  0.50 51.35 ? 76  VAL B CB    1 
ATOM   7976  C  CG1   A VAL B 2 76  ? 17.880  -34.387 -7.715  0.50 50.99 ? 76  VAL B CG1   1 
ATOM   7977  C  CG1   B VAL B 2 76  ? 17.704  -33.582 -7.860  0.50 50.78 ? 76  VAL B CG1   1 
ATOM   7978  C  CG2   A VAL B 2 76  ? 20.063  -33.319 -8.303  0.50 43.09 ? 76  VAL B CG2   1 
ATOM   7979  C  CG2   B VAL B 2 76  ? 19.987  -32.706 -8.372  0.50 42.81 ? 76  VAL B CG2   1 
ATOM   7980  N  N     A ARG B 2 77  ? 18.458  -37.299 -9.970  0.50 53.83 ? 77  ARG B N     1 
ATOM   7981  N  N     B ARG B 2 77  ? 17.802  -36.262 -10.261 0.50 51.20 ? 77  ARG B N     1 
ATOM   7982  C  CA    A ARG B 2 77  ? 17.447  -38.325 -10.214 0.50 53.25 ? 77  ARG B CA    1 
ATOM   7983  C  CA    B ARG B 2 77  ? 16.766  -37.255 -10.533 0.50 54.43 ? 77  ARG B CA    1 
ATOM   7984  C  C     A ARG B 2 77  ? 17.912  -39.707 -9.770  0.50 54.19 ? 77  ARG B C     1 
ATOM   7985  C  C     B ARG B 2 77  ? 17.222  -38.661 -10.166 0.50 53.17 ? 77  ARG B C     1 
ATOM   7986  O  O     A ARG B 2 77  ? 17.098  -40.508 -9.295  0.50 54.90 ? 77  ARG B O     1 
ATOM   7987  O  O     B ARG B 2 77  ? 16.410  -39.480 -9.718  0.50 54.07 ? 77  ARG B O     1 
ATOM   7988  C  CB    A ARG B 2 77  ? 17.066  -38.353 -11.695 0.50 51.93 ? 77  ARG B CB    1 
ATOM   7989  C  CB    B ARG B 2 77  ? 16.363  -37.215 -12.007 0.50 49.01 ? 77  ARG B CB    1 
ATOM   7990  C  CG    A ARG B 2 77  ? 16.305  -37.125 -12.171 0.50 49.00 ? 77  ARG B CG    1 
ATOM   7991  C  CG    B ARG B 2 77  ? 15.571  -35.991 -12.438 0.50 53.66 ? 77  ARG B CG    1 
ATOM   7992  C  CD    A ARG B 2 77  ? 15.768  -37.319 -13.582 0.50 50.41 ? 77  ARG B CD    1 
ATOM   7993  C  CD    B ARG B 2 77  ? 15.181  -36.119 -13.904 0.50 54.20 ? 77  ARG B CD    1 
ATOM   7994  N  NE    A ARG B 2 77  ? 15.176  -36.096 -14.113 0.50 54.28 ? 77  ARG B NE    1 
ATOM   7995  N  NE    B ARG B 2 77  ? 14.617  -34.893 -14.458 0.50 51.34 ? 77  ARG B NE    1 
ATOM   7996  C  CZ    A ARG B 2 77  ? 15.748  -35.322 -15.025 0.50 51.31 ? 77  ARG B CZ    1 
ATOM   7997  C  CZ    B ARG B 2 77  ? 13.325  -34.595 -14.459 0.50 54.74 ? 77  ARG B CZ    1 
ATOM   7998  N  NH1   A ARG B 2 77  ? 16.919  -35.630 -15.556 0.50 48.41 ? 77  ARG B NH1   1 
ATOM   7999  N  NH1   B ARG B 2 77  ? 12.429  -35.398 -13.906 0.50 55.08 ? 77  ARG B NH1   1 
ATOM   8000  N  NH2   A ARG B 2 77  ? 15.127  -34.212 -15.415 0.50 47.81 ? 77  ARG B NH2   1 
ATOM   8001  N  NH2   B ARG B 2 77  ? 12.920  -33.464 -15.031 0.50 49.21 ? 77  ARG B NH2   1 
ATOM   8002  N  N     A SER B 2 78  ? 19.201  -40.007 -9.912  0.50 54.81 ? 78  SER B N     1 
ATOM   8003  N  N     B SER B 2 78  ? 18.509  -38.960 -10.347 0.50 52.36 ? 78  SER B N     1 
ATOM   8004  C  CA    A SER B 2 78  ? 19.736  -41.303 -9.514  0.50 54.14 ? 78  SER B CA    1 
ATOM   8005  C  CA    B SER B 2 78  ? 19.046  -40.275 -10.020 0.50 54.63 ? 78  SER B CA    1 
ATOM   8006  C  C     A SER B 2 78  ? 19.901  -41.438 -8.002  0.50 54.96 ? 78  SER B C     1 
ATOM   8007  C  C     B SER B 2 78  ? 19.190  -40.504 -8.522  0.50 54.82 ? 78  SER B C     1 
ATOM   8008  O  O     A SER B 2 78  ? 20.440  -42.451 -7.542  0.50 54.48 ? 78  SER B O     1 
ATOM   8009  O  O     B SER B 2 78  ? 19.552  -41.616 -8.120  0.50 54.63 ? 78  SER B O     1 
ATOM   8010  C  CB    A SER B 2 78  ? 21.076  -41.556 -10.209 0.50 50.71 ? 78  SER B CB    1 
ATOM   8011  C  CB    B SER B 2 78  ? 20.400  -40.469 -10.707 0.50 54.65 ? 78  SER B CB    1 
ATOM   8012  O  OG    A SER B 2 78  ? 21.987  -40.497 -9.975  0.50 51.91 ? 78  SER B OG    1 
ATOM   8013  O  OG    B SER B 2 78  ? 20.269  -40.391 -12.116 0.50 53.08 ? 78  SER B OG    1 
ATOM   8014  N  N     A GLY B 2 79  ? 19.456  -40.448 -7.230  0.50 56.06 ? 79  GLY B N     1 
ATOM   8015  N  N     B GLY B 2 79  ? 18.921  -39.497 -7.693  0.50 56.74 ? 79  GLY B N     1 
ATOM   8016  C  CA    A GLY B 2 79  ? 19.497  -40.517 -5.790  0.50 56.38 ? 79  GLY B CA    1 
ATOM   8017  C  CA    B GLY B 2 79  ? 18.998  -39.643 -6.260  0.50 55.62 ? 79  GLY B CA    1 
ATOM   8018  C  C     A GLY B 2 79  ? 18.278  -41.220 -5.235  0.50 57.61 ? 79  GLY B C     1 
ATOM   8019  C  C     B GLY B 2 79  ? 17.842  -40.452 -5.710  0.50 55.26 ? 79  GLY B C     1 
ATOM   8020  O  O     A GLY B 2 79  ? 17.301  -41.470 -5.949  0.50 60.07 ? 79  GLY B O     1 
ATOM   8021  O  O     B GLY B 2 79  ? 16.844  -40.695 -6.395  0.50 52.73 ? 79  GLY B O     1 
ATOM   8022  N  N     A PRO B 2 80  ? 18.313  -41.560 -3.944  0.50 58.40 ? 80  PRO B N     1 
ATOM   8023  N  N     B PRO B 2 80  ? 17.954  -40.882 -4.449  0.50 57.21 ? 80  PRO B N     1 
ATOM   8024  C  CA    A PRO B 2 80  ? 17.184  -42.306 -3.360  0.50 59.08 ? 80  PRO B CA    1 
ATOM   8025  C  CA    B PRO B 2 80  ? 16.890  -41.728 -3.875  0.50 58.52 ? 80  PRO B CA    1 
ATOM   8026  C  C     A PRO B 2 80  ? 15.865  -41.555 -3.428  0.50 58.20 ? 80  PRO B C     1 
ATOM   8027  C  C     B PRO B 2 80  ? 15.543  -41.027 -3.802  0.50 59.44 ? 80  PRO B C     1 
ATOM   8028  O  O     A PRO B 2 80  ? 14.829  -42.164 -3.716  0.50 60.00 ? 80  PRO B O     1 
ATOM   8029  O  O     B PRO B 2 80  ? 14.531  -41.576 -4.259  0.50 57.87 ? 80  PRO B O     1 
ATOM   8030  C  CB    A PRO B 2 80  ? 17.632  -42.538 -1.909  0.50 59.94 ? 80  PRO B CB    1 
ATOM   8031  C  CB    B PRO B 2 80  ? 17.442  -42.079 -2.486  0.50 59.77 ? 80  PRO B CB    1 
ATOM   8032  C  CG    A PRO B 2 80  ? 19.124  -42.398 -1.930  0.50 55.41 ? 80  PRO B CG    1 
ATOM   8033  C  CG    B PRO B 2 80  ? 18.407  -40.976 -2.168  0.50 51.84 ? 80  PRO B CG    1 
ATOM   8034  C  CD    A PRO B 2 80  ? 19.402  -41.357 -2.975  0.50 59.36 ? 80  PRO B CD    1 
ATOM   8035  C  CD    B PRO B 2 80  ? 19.023  -40.589 -3.479  0.50 59.09 ? 80  PRO B CD    1 
ATOM   8036  N  N     A PHE B 2 81  ? 15.874  -40.247 -3.167  0.50 57.46 ? 81  PHE B N     1 
ATOM   8037  N  N     B PHE B 2 81  ? 15.503  -39.821 -3.240  0.50 56.15 ? 81  PHE B N     1 
ATOM   8038  C  CA    A PHE B 2 81  ? 14.677  -39.416 -3.220  0.50 54.08 ? 81  PHE B CA    1 
ATOM   8039  C  CA    B PHE B 2 81  ? 14.289  -39.020 -3.188  0.50 54.47 ? 81  PHE B CA    1 
ATOM   8040  C  C     A PHE B 2 81  ? 14.610  -38.583 -4.496  0.50 52.49 ? 81  PHE B C     1 
ATOM   8041  C  C     B PHE B 2 81  ? 14.113  -38.154 -4.430  0.50 53.58 ? 81  PHE B C     1 
ATOM   8042  O  O     A PHE B 2 81  ? 13.974  -37.524 -4.514  0.50 53.73 ? 81  PHE B O     1 
ATOM   8043  O  O     B PHE B 2 81  ? 13.409  -37.140 -4.374  0.50 50.47 ? 81  PHE B O     1 
ATOM   8044  C  CB    A PHE B 2 81  ? 14.613  -38.506 -1.992  0.50 53.18 ? 81  PHE B CB    1 
ATOM   8045  C  CB    B PHE B 2 81  ? 14.288  -38.148 -1.929  0.50 53.39 ? 81  PHE B CB    1 
ATOM   8046  C  CG    A PHE B 2 81  ? 14.372  -39.237 -0.700  0.50 50.38 ? 81  PHE B CG    1 
ATOM   8047  C  CG    B PHE B 2 81  ? 14.129  -38.923 -0.649  0.50 51.09 ? 81  PHE B CG    1 
ATOM   8048  C  CD1   A PHE B 2 81  ? 15.393  -39.941 -0.080  0.50 50.30 ? 81  PHE B CD1   1 
ATOM   8049  C  CD1   B PHE B 2 81  ? 15.161  -39.710 -0.163  0.50 49.95 ? 81  PHE B CD1   1 
ATOM   8050  C  CD2   A PHE B 2 81  ? 13.127  -39.205 -0.095  0.50 53.89 ? 81  PHE B CD2   1 
ATOM   8051  C  CD2   B PHE B 2 81  ? 12.951  -38.853 0.077   0.50 52.97 ? 81  PHE B CD2   1 
ATOM   8052  C  CE1   A PHE B 2 81  ? 15.173  -40.608 1.111   0.50 47.96 ? 81  PHE B CE1   1 
ATOM   8053  C  CE1   B PHE B 2 81  ? 15.021  -40.419 1.015   0.50 47.96 ? 81  PHE B CE1   1 
ATOM   8054  C  CE2   A PHE B 2 81  ? 12.901  -39.871 1.096   0.50 53.34 ? 81  PHE B CE2   1 
ATOM   8055  C  CE2   B PHE B 2 81  ? 12.804  -39.561 1.257   0.50 52.42 ? 81  PHE B CE2   1 
ATOM   8056  C  CZ    A PHE B 2 81  ? 13.927  -40.574 1.699   0.50 53.37 ? 81  PHE B CZ    1 
ATOM   8057  C  CZ    B PHE B 2 81  ? 13.842  -40.345 1.726   0.50 53.41 ? 81  PHE B CZ    1 
ATOM   8058  N  N     A GLY B 2 82  ? 15.250  -39.047 -5.570  0.50 53.47 ? 82  GLY B N     1 
ATOM   8059  N  N     B GLY B 2 82  ? 14.738  -38.533 -5.549  0.50 52.20 ? 82  GLY B N     1 
ATOM   8060  C  CA    A GLY B 2 82  ? 15.403  -38.255 -6.777  0.50 50.44 ? 82  GLY B CA    1 
ATOM   8061  C  CA    B GLY B 2 82  ? 14.671  -37.727 -6.755  0.50 51.14 ? 82  GLY B CA    1 
ATOM   8062  C  C     A GLY B 2 82  ? 14.176  -38.132 -7.652  0.50 53.80 ? 82  GLY B C     1 
ATOM   8063  C  C     B GLY B 2 82  ? 13.358  -37.807 -7.502  0.50 53.41 ? 82  GLY B C     1 
ATOM   8064  O  O     A GLY B 2 82  ? 14.168  -37.293 -8.558  0.50 56.67 ? 82  GLY B O     1 
ATOM   8065  O  O     B GLY B 2 82  ? 13.094  -36.957 -8.359  0.50 54.29 ? 82  GLY B O     1 
ATOM   8066  N  N     A GLN B 2 83  ? 13.144  -38.941 -7.417  0.50 53.98 ? 83  GLN B N     1 
ATOM   8067  N  N     B GLN B 2 83  ? 12.529  -38.805 -7.201  0.50 52.10 ? 83  GLN B N     1 
ATOM   8068  C  CA    A GLN B 2 83  ? 11.921  -38.876 -8.204  0.50 54.66 ? 83  GLN B CA    1 
ATOM   8069  C  CA    B GLN B 2 83  ? 11.256  -38.978 -7.887  0.50 55.70 ? 83  GLN B CA    1 
ATOM   8070  C  C     A GLN B 2 83  ? 10.731  -38.349 -7.415  0.50 53.18 ? 83  GLN B C     1 
ATOM   8071  C  C     B GLN B 2 83  ? 10.117  -38.204 -7.241  0.50 51.83 ? 83  GLN B C     1 
ATOM   8072  O  O     A GLN B 2 83  ? 9.615   -38.327 -7.946  0.50 53.89 ? 83  GLN B O     1 
ATOM   8073  O  O     B GLN B 2 83  ? 9.016   -38.176 -7.801  0.50 55.03 ? 83  GLN B O     1 
ATOM   8074  C  CB    A GLN B 2 83  ? 11.590  -40.256 -8.787  0.50 55.66 ? 83  GLN B CB    1 
ATOM   8075  C  CB    B GLN B 2 83  ? 10.880  -40.462 -7.945  0.50 52.48 ? 83  GLN B CB    1 
ATOM   8076  C  CG    A GLN B 2 83  ? 12.532  -40.704 -9.897  0.50 53.62 ? 83  GLN B CG    1 
ATOM   8077  C  CG    B GLN B 2 83  ? 11.956  -41.343 -8.538  0.50 56.62 ? 83  GLN B CG    1 
ATOM   8078  C  CD    A GLN B 2 83  ? 12.363  -39.897 -11.174 0.50 52.30 ? 83  GLN B CD    1 
ATOM   8079  C  CD    B GLN B 2 83  ? 12.317  -40.956 -9.958  0.50 53.93 ? 83  GLN B CD    1 
ATOM   8080  O  OE1   A GLN B 2 83  ? 11.330  -39.264 -11.391 0.50 54.20 ? 83  GLN B OE1   1 
ATOM   8081  O  OE1   B GLN B 2 83  ? 11.450  -40.590 -10.754 0.50 51.78 ? 83  GLN B OE1   1 
ATOM   8082  N  NE2   A GLN B 2 83  ? 13.380  -39.920 -12.027 0.50 50.43 ? 83  GLN B NE2   1 
ATOM   8083  N  NE2   B GLN B 2 83  ? 13.603  -41.033 -10.283 0.50 48.83 ? 83  GLN B NE2   1 
ATOM   8084  N  N     A ILE B 2 84  ? 10.935  -37.924 -6.167  0.50 54.80 ? 84  ILE B N     1 
ATOM   8085  N  N     B ILE B 2 84  ? 10.349  -37.579 -6.087  0.50 54.38 ? 84  ILE B N     1 
ATOM   8086  C  CA    A ILE B 2 84  ? 9.845   -37.323 -5.406  0.50 55.22 ? 84  ILE B CA    1 
ATOM   8087  C  CA    B ILE B 2 84  ? 9.276   -36.877 -5.394  0.50 55.29 ? 84  ILE B CA    1 
ATOM   8088  C  C     A ILE B 2 84  ? 9.597   -35.880 -5.825  0.50 52.26 ? 84  ILE B C     1 
ATOM   8089  C  C     B ILE B 2 84  ? 9.132   -35.429 -5.853  0.50 53.13 ? 84  ILE B C     1 
ATOM   8090  O  O     A ILE B 2 84  ? 8.488   -35.367 -5.628  0.50 54.20 ? 84  ILE B O     1 
ATOM   8091  O  O     B ILE B 2 84  ? 8.081   -34.816 -5.618  0.50 54.59 ? 84  ILE B O     1 
ATOM   8092  C  CB    A ILE B 2 84  ? 10.124  -37.404 -3.895  0.50 50.92 ? 84  ILE B CB    1 
ATOM   8093  C  CB    B ILE B 2 84  ? 9.491   -36.943 -3.870  0.50 51.37 ? 84  ILE B CB    1 
ATOM   8094  C  CG1   A ILE B 2 84  ? 8.843   -37.156 -3.096  0.50 56.29 ? 84  ILE B CG1   1 
ATOM   8095  C  CG1   B ILE B 2 84  ? 8.184   -36.654 -3.127  0.50 55.48 ? 84  ILE B CG1   1 
ATOM   8096  C  CG2   A ILE B 2 84  ? 11.197  -36.405 -3.485  0.50 54.76 ? 84  ILE B CG2   1 
ATOM   8097  C  CG2   B ILE B 2 84  ? 10.575  -35.969 -3.437  0.50 55.22 ? 84  ILE B CG2   1 
ATOM   8098  C  CD1   A ILE B 2 84  ? 9.051   -37.143 -1.597  0.50 55.43 ? 84  ILE B CD1   1 
ATOM   8099  C  CD1   B ILE B 2 84  ? 6.993   -37.409 -3.663  0.50 49.22 ? 84  ILE B CD1   1 
ATOM   8100  N  N     A PHE B 2 85  ? 10.589  -35.216 -6.411  0.50 49.09 ? 85  PHE B N     1 
ATOM   8101  N  N     B PHE B 2 85  ? 10.144  -34.871 -6.514  0.50 49.44 ? 85  PHE B N     1 
ATOM   8102  C  CA    A PHE B 2 85  ? 10.418  -33.833 -6.828  0.50 45.88 ? 85  PHE B CA    1 
ATOM   8103  C  CA    B PHE B 2 85  ? 10.051  -33.497 -6.987  0.50 46.18 ? 85  PHE B CA    1 
ATOM   8104  C  C     A PHE B 2 85  ? 9.510   -33.758 -8.048  0.50 52.22 ? 85  PHE B C     1 
ATOM   8105  C  C     B PHE B 2 85  ? 9.089   -33.402 -8.164  0.50 53.65 ? 85  PHE B C     1 
ATOM   8106  O  O     A PHE B 2 85  ? 9.562   -34.614 -8.935  0.50 56.11 ? 85  PHE B O     1 
ATOM   8107  O  O     B PHE B 2 85  ? 9.005   -34.311 -8.994  0.50 55.64 ? 85  PHE B O     1 
ATOM   8108  C  CB    A PHE B 2 85  ? 11.774  -33.199 -7.137  0.50 48.49 ? 85  PHE B CB    1 
ATOM   8109  C  CB    B PHE B 2 85  ? 11.429  -32.976 -7.392  0.50 49.01 ? 85  PHE B CB    1 
ATOM   8110  C  CG    A PHE B 2 85  ? 12.774  -33.343 -6.027  0.50 50.64 ? 85  PHE B CG    1 
ATOM   8111  C  CG    B PHE B 2 85  ? 12.392  -32.865 -6.248  0.50 50.61 ? 85  PHE B CG    1 
ATOM   8112  C  CD1   A PHE B 2 85  ? 12.704  -32.533 -4.904  0.50 49.56 ? 85  PHE B CD1   1 
ATOM   8113  C  CD1   B PHE B 2 85  ? 12.330  -31.788 -5.377  0.50 45.97 ? 85  PHE B CD1   1 
ATOM   8114  C  CD2   A PHE B 2 85  ? 13.783  -34.289 -6.103  0.50 49.01 ? 85  PHE B CD2   1 
ATOM   8115  C  CD2   B PHE B 2 85  ? 13.358  -33.837 -6.041  0.50 48.84 ? 85  PHE B CD2   1 
ATOM   8116  C  CE1   A PHE B 2 85  ? 13.620  -32.666 -3.880  0.50 45.66 ? 85  PHE B CE1   1 
ATOM   8117  C  CE1   B PHE B 2 85  ? 13.211  -31.683 -4.321  0.50 41.07 ? 85  PHE B CE1   1 
ATOM   8118  C  CE2   A PHE B 2 85  ? 14.702  -34.426 -5.082  0.50 50.28 ? 85  PHE B CE2   1 
ATOM   8119  C  CE2   B PHE B 2 85  ? 14.244  -33.738 -4.987  0.50 49.74 ? 85  PHE B CE2   1 
ATOM   8120  C  CZ    A PHE B 2 85  ? 14.621  -33.613 -3.969  0.50 49.45 ? 85  PHE B CZ    1 
ATOM   8121  C  CZ    B PHE B 2 85  ? 14.171  -32.659 -4.124  0.50 46.71 ? 85  PHE B CZ    1 
ATOM   8122  N  N     A ARG B 2 86  ? 8.671   -32.728 -8.084  0.50 53.94 ? 86  ARG B N     1 
ATOM   8123  N  N     B ARG B 2 86  ? 8.358   -32.298 -8.227  0.50 52.14 ? 86  ARG B N     1 
ATOM   8124  C  CA    A ARG B 2 86  ? 7.751   -32.554 -9.197  0.50 50.77 ? 86  ARG B CA    1 
ATOM   8125  C  CA    B ARG B 2 86  ? 7.463   -32.056 -9.350  0.50 50.14 ? 86  ARG B CA    1 
ATOM   8126  C  C     A ARG B 2 86  ? 8.534   -32.337 -10.488 0.50 51.71 ? 86  ARG B C     1 
ATOM   8127  C  C     B ARG B 2 86  ? 8.280   -31.894 -10.624 0.50 52.36 ? 86  ARG B C     1 
ATOM   8128  O  O     A ARG B 2 86  ? 9.400   -31.453 -10.541 0.50 53.55 ? 86  ARG B O     1 
ATOM   8129  O  O     B ARG B 2 86  ? 9.153   -31.017 -10.679 0.50 52.64 ? 86  ARG B O     1 
ATOM   8130  C  CB    A ARG B 2 86  ? 6.819   -31.373 -8.938  0.50 52.07 ? 86  ARG B CB    1 
ATOM   8131  C  CB    B ARG B 2 86  ? 6.612   -30.814 -9.101  0.50 50.97 ? 86  ARG B CB    1 
ATOM   8132  C  CG    A ARG B 2 86  ? 5.858   -31.074 -10.074 0.50 53.62 ? 86  ARG B CG    1 
ATOM   8133  C  CG    B ARG B 2 86  ? 5.148   -31.108 -8.813  0.50 51.29 ? 86  ARG B CG    1 
ATOM   8134  C  CD    A ARG B 2 86  ? 5.018   -29.845 -9.768  0.50 50.56 ? 86  ARG B CD    1 
ATOM   8135  C  CD    B ARG B 2 86  ? 4.377   -29.827 -8.531  0.50 55.84 ? 86  ARG B CD    1 
ATOM   8136  N  NE    A ARG B 2 86  ? 4.214   -30.023 -8.565  0.50 56.00 ? 86  ARG B NE    1 
ATOM   8137  N  NE    B ARG B 2 86  ? 2.963   -30.075 -8.270  0.50 50.56 ? 86  ARG B NE    1 
ATOM   8138  C  CZ    A ARG B 2 86  ? 3.445   -29.083 -8.034  0.50 53.20 ? 86  ARG B CZ    1 
ATOM   8139  C  CZ    B ARG B 2 86  ? 2.475   -30.469 -7.101  0.50 54.86 ? 86  ARG B CZ    1 
ATOM   8140  N  NH1   A ARG B 2 86  ? 3.352   -27.879 -8.573  0.50 54.57 ? 86  ARG B NH1   1 
ATOM   8141  N  NH1   B ARG B 2 86  ? 3.265   -30.706 -6.066  0.50 50.89 ? 86  ARG B NH1   1 
ATOM   8142  N  NH2   A ARG B 2 86  ? 2.753   -29.357 -6.931  0.50 52.81 ? 86  ARG B NH2   1 
ATOM   8143  N  NH2   B ARG B 2 86  ? 1.161   -30.630 -6.967  0.50 56.45 ? 86  ARG B NH2   1 
ATOM   8144  N  N     A PRO B 2 87  ? 8.274   -33.122 -11.537 0.50 52.49 ? 87  PRO B N     1 
ATOM   8145  N  N     B PRO B 2 87  ? 8.052   -32.714 -11.653 0.50 52.38 ? 87  PRO B N     1 
ATOM   8146  C  CA    A PRO B 2 87  ? 9.038   -32.952 -12.784 0.50 49.45 ? 87  PRO B CA    1 
ATOM   8147  C  CA    B PRO B 2 87  ? 8.803   -32.539 -12.908 0.50 49.55 ? 87  PRO B CA    1 
ATOM   8148  C  C     A PRO B 2 87  ? 8.853   -31.593 -13.435 0.50 52.85 ? 87  PRO B C     1 
ATOM   8149  C  C     B PRO B 2 87  ? 8.670   -31.147 -13.497 0.50 53.70 ? 87  PRO B C     1 
ATOM   8150  O  O     A PRO B 2 87  ? 9.763   -31.126 -14.132 0.50 50.49 ? 87  PRO B O     1 
ATOM   8151  O  O     B PRO B 2 87  ? 9.589   -30.681 -14.182 0.50 50.77 ? 87  PRO B O     1 
ATOM   8152  C  CB    A PRO B 2 87  ? 8.503   -34.082 -13.676 0.50 54.61 ? 87  PRO B CB    1 
ATOM   8153  C  CB    B PRO B 2 87  ? 8.195   -33.607 -13.827 0.50 54.09 ? 87  PRO B CB    1 
ATOM   8154  C  CG    A PRO B 2 87  ? 7.960   -35.097 -12.720 0.50 51.71 ? 87  PRO B CG    1 
ATOM   8155  C  CG    B PRO B 2 87  ? 7.674   -34.650 -12.891 0.50 53.63 ? 87  PRO B CG    1 
ATOM   8156  C  CD    A PRO B 2 87  ? 7.397   -34.303 -11.579 0.50 53.39 ? 87  PRO B CD    1 
ATOM   8157  C  CD    B PRO B 2 87  ? 7.177   -33.898 -11.688 0.50 53.56 ? 87  PRO B CD    1 
ATOM   8158  N  N     A ASP B 2 88  ? 7.707   -30.938 -13.228 0.50 52.87 ? 88  ASP B N     1 
ATOM   8159  N  N     B ASP B 2 88  ? 7.551   -30.465 -13.244 0.50 53.36 ? 88  ASP B N     1 
ATOM   8160  C  CA    A ASP B 2 88  ? 7.462   -29.644 -13.858 0.50 50.38 ? 88  ASP B CA    1 
ATOM   8161  C  CA    B ASP B 2 88  ? 7.400   -29.079 -13.671 0.50 50.61 ? 88  ASP B CA    1 
ATOM   8162  C  C     A ASP B 2 88  ? 8.391   -28.555 -13.337 0.50 50.71 ? 88  ASP B C     1 
ATOM   8163  C  C     B ASP B 2 88  ? 8.361   -28.146 -12.943 0.50 49.80 ? 88  ASP B C     1 
ATOM   8164  O  O     A ASP B 2 88  ? 8.622   -27.567 -14.043 0.50 55.02 ? 88  ASP B O     1 
ATOM   8165  O  O     B ASP B 2 88  ? 8.661   -27.062 -13.456 0.50 53.04 ? 88  ASP B O     1 
ATOM   8166  C  CB    A ASP B 2 88  ? 6.008   -29.216 -13.645 0.50 56.37 ? 88  ASP B CB    1 
ATOM   8167  C  CB    B ASP B 2 88  ? 5.953   -28.628 -13.453 0.50 57.10 ? 88  ASP B CB    1 
ATOM   8168  C  CG    A ASP B 2 88  ? 5.016   -30.251 -14.134 0.50 57.04 ? 88  ASP B CG    1 
ATOM   8169  C  CG    B ASP B 2 88  ? 5.703   -27.207 -13.920 0.50 55.67 ? 88  ASP B CG    1 
ATOM   8170  O  OD1   A ASP B 2 88  ? 4.877   -31.301 -13.469 0.50 55.60 ? 88  ASP B OD1   1 
ATOM   8171  O  OD1   B ASP B 2 88  ? 5.601   -26.992 -15.146 0.50 65.46 ? 88  ASP B OD1   1 
ATOM   8172  O  OD2   A ASP B 2 88  ? 4.373   -30.012 -15.180 0.50 60.43 ? 88  ASP B OD2   1 
ATOM   8173  O  OD2   B ASP B 2 88  ? 5.606   -26.306 -13.059 0.50 53.06 ? 88  ASP B OD2   1 
ATOM   8174  N  N     A ASN B 2 89  ? 8.923   -28.706 -12.123 0.50 47.20 ? 89  ASN B N     1 
ATOM   8175  N  N     B ASN B 2 89  ? 8.855   -28.543 -11.766 0.50 46.55 ? 89  ASN B N     1 
ATOM   8176  C  CA    A ASN B 2 89  ? 9.771   -27.670 -11.546 0.50 50.22 ? 89  ASN B CA    1 
ATOM   8177  C  CA    B ASN B 2 89  ? 9.767   -27.724 -10.975 0.50 47.74 ? 89  ASN B CA    1 
ATOM   8178  C  C     A ASN B 2 89  ? 11.226  -27.784 -11.981 0.50 49.38 ? 89  ASN B C     1 
ATOM   8179  C  C     B ASN B 2 89  ? 11.232  -27.947 -11.336 0.50 49.75 ? 89  ASN B C     1 
ATOM   8180  O  O     A ASN B 2 89  ? 11.964  -26.798 -11.873 0.50 47.42 ? 89  ASN B O     1 
ATOM   8181  O  O     B ASN B 2 89  ? 12.100  -27.884 -10.455 0.50 42.54 ? 89  ASN B O     1 
ATOM   8182  C  CB    A ASN B 2 89  ? 9.688   -27.709 -10.020 0.50 44.76 ? 89  ASN B CB    1 
ATOM   8183  C  CB    B ASN B 2 89  ? 9.545   -27.982 -9.485  0.50 46.79 ? 89  ASN B CB    1 
ATOM   8184  C  CG    A ASN B 2 89  ? 8.259   -27.738 -9.516  0.50 46.70 ? 89  ASN B CG    1 
ATOM   8185  C  CG    B ASN B 2 89  ? 8.225   -27.431 -8.990  0.50 47.77 ? 89  ASN B CG    1 
ATOM   8186  O  OD1   A ASN B 2 89  ? 7.941   -28.443 -8.560  0.50 46.24 ? 89  ASN B OD1   1 
ATOM   8187  O  OD1   B ASN B 2 89  ? 7.329   -27.133 -9.780  0.50 49.30 ? 89  ASN B OD1   1 
ATOM   8188  N  ND2   A ASN B 2 89  ? 7.387   -26.976 -10.165 0.50 47.55 ? 89  ASN B ND2   1 
ATOM   8189  N  ND2   B ASN B 2 89  ? 8.098   -27.288 -7.674  0.50 39.47 ? 89  ASN B ND2   1 
ATOM   8190  N  N     A PHE B 2 90  ? 11.654  -28.957 -12.453 0.50 47.48 ? 90  PHE B N     1 
ATOM   8191  N  N     B PHE B 2 90  ? 11.532  -28.211 -12.607 0.50 47.25 ? 90  PHE B N     1 
ATOM   8192  C  CA    A PHE B 2 90  ? 13.007  -29.144 -12.969 0.50 48.64 ? 90  PHE B CA    1 
ATOM   8193  C  CA    B PHE B 2 90  ? 12.902  -28.324 -13.100 0.50 46.61 ? 90  PHE B CA    1 
ATOM   8194  C  C     A PHE B 2 90  ? 13.287  -28.187 -14.120 0.50 45.34 ? 90  PHE B C     1 
ATOM   8195  C  C     B PHE B 2 90  ? 13.080  -27.282 -14.196 0.50 47.00 ? 90  PHE B C     1 
ATOM   8196  O  O     A PHE B 2 90  ? 12.707  -28.328 -15.200 0.50 49.49 ? 90  PHE B O     1 
ATOM   8197  O  O     B PHE B 2 90  ? 12.446  -27.376 -15.253 0.50 48.78 ? 90  PHE B O     1 
ATOM   8198  C  CB    A PHE B 2 90  ? 13.212  -30.585 -13.444 0.50 48.42 ? 90  PHE B CB    1 
ATOM   8199  C  CB    B PHE B 2 90  ? 13.193  -29.731 -13.626 0.50 47.70 ? 90  PHE B CB    1 
ATOM   8200  C  CG    A PHE B 2 90  ? 13.590  -31.547 -12.355 0.50 49.64 ? 90  PHE B CG    1 
ATOM   8201  C  CG    B PHE B 2 90  ? 13.264  -30.788 -12.555 0.50 49.67 ? 90  PHE B CG    1 
ATOM   8202  C  CD1   A PHE B 2 90  ? 12.642  -32.018 -11.464 0.50 50.30 ? 90  PHE B CD1   1 
ATOM   8203  C  CD1   B PHE B 2 90  ? 12.120  -31.207 -11.895 0.50 49.19 ? 90  PHE B CD1   1 
ATOM   8204  C  CD2   A PHE B 2 90  ? 14.894  -32.003 -12.241 0.50 49.53 ? 90  PHE B CD2   1 
ATOM   8205  C  CD2   B PHE B 2 90  ? 14.473  -31.380 -12.229 0.50 50.26 ? 90  PHE B CD2   1 
ATOM   8206  C  CE1   A PHE B 2 90  ? 12.989  -32.914 -10.469 0.50 50.53 ? 90  PHE B CE1   1 
ATOM   8207  C  CE1   B PHE B 2 90  ? 12.183  -32.183 -10.917 0.50 51.50 ? 90  PHE B CE1   1 
ATOM   8208  C  CE2   A PHE B 2 90  ? 15.248  -32.898 -11.250 0.50 52.09 ? 90  PHE B CE2   1 
ATOM   8209  C  CE2   B PHE B 2 90  ? 14.542  -32.359 -11.255 0.50 50.66 ? 90  PHE B CE2   1 
ATOM   8210  C  CZ    A PHE B 2 90  ? 14.294  -33.355 -10.363 0.50 49.79 ? 90  PHE B CZ    1 
ATOM   8211  C  CZ    B PHE B 2 90  ? 13.396  -32.760 -10.598 0.50 51.03 ? 90  PHE B CZ    1 
ATOM   8212  N  N     A VAL B 2 91  ? 14.170  -27.216 -13.906 0.50 43.37 ? 91  VAL B N     1 
ATOM   8213  N  N     B VAL B 2 91  ? 13.925  -26.285 -13.946 0.50 40.11 ? 91  VAL B N     1 
ATOM   8214  C  CA    A VAL B 2 91  ? 14.565  -26.269 -14.943 0.50 41.96 ? 91  VAL B CA    1 
ATOM   8215  C  CA    B VAL B 2 91  ? 14.153  -25.189 -14.886 0.50 37.24 ? 91  VAL B CA    1 
ATOM   8216  C  C     A VAL B 2 91  ? 16.081  -26.335 -15.074 0.50 43.91 ? 91  VAL B C     1 
ATOM   8217  C  C     B VAL B 2 91  ? 15.649  -25.147 -15.174 0.50 44.12 ? 91  VAL B C     1 
ATOM   8218  O  O     A VAL B 2 91  ? 16.813  -25.954 -14.151 0.50 38.49 ? 91  VAL B O     1 
ATOM   8219  O  O     B VAL B 2 91  ? 16.426  -24.569 -14.405 0.50 33.15 ? 91  VAL B O     1 
ATOM   8220  C  CB    A VAL B 2 91  ? 14.081  -24.843 -14.642 0.50 36.35 ? 91  VAL B CB    1 
ATOM   8221  C  CB    B VAL B 2 91  ? 13.650  -23.847 -14.347 0.50 39.40 ? 91  VAL B CB    1 
ATOM   8222  C  CG1   A VAL B 2 91  ? 14.201  -24.538 -13.159 0.50 45.77 ? 91  VAL B CG1   1 
ATOM   8223  C  CG1   B VAL B 2 91  ? 13.660  -22.803 -15.449 0.50 44.92 ? 91  VAL B CG1   1 
ATOM   8224  C  CG2   A VAL B 2 91  ? 14.846  -23.826 -15.479 0.50 37.60 ? 91  VAL B CG2   1 
ATOM   8225  C  CG2   B VAL B 2 91  ? 12.254  -23.998 -13.755 0.50 37.62 ? 91  VAL B CG2   1 
ATOM   8226  N  N     A PHE B 2 92  ? 16.553  -26.837 -16.214 0.50 44.31 ? 92  PHE B N     1 
ATOM   8227  N  N     B PHE B 2 92  ? 16.061  -25.753 -16.284 0.50 43.72 ? 92  PHE B N     1 
ATOM   8228  C  CA    A PHE B 2 92  ? 17.975  -27.035 -16.454 0.50 44.77 ? 92  PHE B CA    1 
ATOM   8229  C  CA    B PHE B 2 92  ? 17.471  -25.895 -16.613 0.50 39.97 ? 92  PHE B CA    1 
ATOM   8230  C  C     A PHE B 2 92  ? 18.318  -26.573 -17.861 0.50 42.07 ? 92  PHE B C     1 
ATOM   8231  C  C     B PHE B 2 92  ? 17.727  -25.416 -18.034 0.50 43.47 ? 92  PHE B C     1 
ATOM   8232  O  O     A PHE B 2 92  ? 17.702  -27.023 -18.831 0.50 41.58 ? 92  PHE B O     1 
ATOM   8233  O  O     B PHE B 2 92  ? 16.942  -25.698 -18.944 0.50 40.23 ? 92  PHE B O     1 
ATOM   8234  C  CB    A PHE B 2 92  ? 18.370  -28.508 -16.269 0.50 48.08 ? 92  PHE B CB    1 
ATOM   8235  C  CB    B PHE B 2 92  ? 17.932  -27.352 -16.456 0.50 45.64 ? 92  PHE B CB    1 
ATOM   8236  C  CG    A PHE B 2 92  ? 18.457  -28.940 -14.828 0.50 48.22 ? 92  PHE B CG    1 
ATOM   8237  C  CG    B PHE B 2 92  ? 18.034  -27.809 -15.024 0.50 45.26 ? 92  PHE B CG    1 
ATOM   8238  C  CD1   A PHE B 2 92  ? 17.313  -29.228 -14.102 0.50 49.43 ? 92  PHE B CD1   1 
ATOM   8239  C  CD1   B PHE B 2 92  ? 16.898  -27.994 -14.254 0.50 46.83 ? 92  PHE B CD1   1 
ATOM   8240  C  CD2   A PHE B 2 92  ? 19.687  -29.063 -14.202 0.50 46.96 ? 92  PHE B CD2   1 
ATOM   8241  C  CD2   B PHE B 2 92  ? 19.269  -28.068 -14.451 0.50 47.01 ? 92  PHE B CD2   1 
ATOM   8242  C  CE1   A PHE B 2 92  ? 17.393  -29.623 -12.779 0.50 46.75 ? 92  PHE B CE1   1 
ATOM   8243  C  CE1   B PHE B 2 92  ? 16.992  -28.414 -12.940 0.50 45.79 ? 92  PHE B CE1   1 
ATOM   8244  C  CE2   A PHE B 2 92  ? 19.771  -29.460 -12.879 0.50 50.78 ? 92  PHE B CE2   1 
ATOM   8245  C  CE2   B PHE B 2 92  ? 19.364  -28.495 -13.138 0.50 49.17 ? 92  PHE B CE2   1 
ATOM   8246  C  CZ    A PHE B 2 92  ? 18.623  -29.738 -12.166 0.50 42.14 ? 92  PHE B CZ    1 
ATOM   8247  C  CZ    B PHE B 2 92  ? 18.226  -28.664 -12.382 0.50 35.65 ? 92  PHE B CZ    1 
ATOM   8248  N  N     A GLY B 2 93  ? 19.299  -25.678 -17.965 0.50 44.87 ? 93  GLY B N     1 
ATOM   8249  N  N     B GLY B 2 93  ? 18.827  -24.687 -18.214 0.50 42.38 ? 93  GLY B N     1 
ATOM   8250  C  CA    A GLY B 2 93  ? 19.783  -25.205 -19.244 0.50 44.15 ? 93  GLY B CA    1 
ATOM   8251  C  CA    B GLY B 2 93  ? 19.252  -24.215 -19.515 0.50 41.01 ? 93  GLY B CA    1 
ATOM   8252  C  C     A GLY B 2 93  ? 20.713  -26.210 -19.894 0.50 45.16 ? 93  GLY B C     1 
ATOM   8253  C  C     B GLY B 2 93  ? 20.103  -25.235 -20.240 0.50 42.96 ? 93  GLY B C     1 
ATOM   8254  O  O     A GLY B 2 93  ? 20.780  -27.379 -19.508 0.50 46.79 ? 93  GLY B O     1 
ATOM   8255  O  O     B GLY B 2 93  ? 20.036  -26.439 -19.983 0.50 44.75 ? 93  GLY B O     1 
ATOM   8256  N  N     A GLN B 2 94  ? 21.453  -25.735 -20.900 0.50 44.12 ? 94  GLN B N     1 
ATOM   8257  N  N     B GLN B 2 94  ? 20.926  -24.736 -21.162 0.50 39.14 ? 94  GLN B N     1 
ATOM   8258  C  CA    A GLN B 2 94  ? 22.356  -26.591 -21.656 0.50 47.41 ? 94  GLN B CA    1 
ATOM   8259  C  CA    B GLN B 2 94  ? 21.782  -25.577 -21.991 0.50 48.02 ? 94  GLN B CA    1 
ATOM   8260  C  C     A GLN B 2 94  ? 23.826  -26.217 -21.541 0.50 53.87 ? 94  GLN B C     1 
ATOM   8261  C  C     B GLN B 2 94  ? 23.263  -25.384 -21.703 0.50 51.98 ? 94  GLN B C     1 
ATOM   8262  O  O     A GLN B 2 94  ? 24.678  -27.055 -21.855 0.50 47.02 ? 94  GLN B O     1 
ATOM   8263  O  O     B GLN B 2 94  ? 23.985  -26.364 -21.497 0.50 54.18 ? 94  GLN B O     1 
ATOM   8264  C  CB    A GLN B 2 94  ? 21.972  -26.596 -23.145 0.50 48.63 ? 94  GLN B CB    1 
ATOM   8265  C  CB    B GLN B 2 94  ? 21.504  -25.305 -23.477 0.50 47.13 ? 94  GLN B CB    1 
ATOM   8266  N  N     A SER B 2 95  ? 24.151  -25.003 -21.099 0.50 51.03 ? 95  SER B N     1 
ATOM   8267  N  N     B SER B 2 95  ? 23.740  -24.142 -21.690 0.50 49.83 ? 95  SER B N     1 
ATOM   8268  C  CA    A SER B 2 95  ? 25.527  -24.512 -21.085 0.50 56.23 ? 95  SER B CA    1 
ATOM   8269  C  CA    B SER B 2 95  ? 25.140  -23.842 -21.421 0.50 55.66 ? 95  SER B CA    1 
ATOM   8270  C  C     A SER B 2 95  ? 25.844  -23.950 -19.706 0.50 50.91 ? 95  SER B C     1 
ATOM   8271  C  C     B SER B 2 95  ? 25.291  -23.327 -19.996 0.50 52.56 ? 95  SER B C     1 
ATOM   8272  O  O     A SER B 2 95  ? 25.394  -22.852 -19.361 0.50 50.74 ? 95  SER B O     1 
ATOM   8273  O  O     B SER B 2 95  ? 24.583  -22.400 -19.587 0.50 49.58 ? 95  SER B O     1 
ATOM   8274  C  CB    A SER B 2 95  ? 25.736  -23.449 -22.164 0.50 54.73 ? 95  SER B CB    1 
ATOM   8275  C  CB    B SER B 2 95  ? 25.682  -22.810 -22.411 0.50 56.70 ? 95  SER B CB    1 
ATOM   8276  O  OG    A SER B 2 95  ? 24.821  -22.377 -22.002 0.50 52.34 ? 95  SER B OG    1 
ATOM   8277  O  OG    B SER B 2 95  ? 26.972  -22.367 -22.022 0.50 59.00 ? 95  SER B OG    1 
ATOM   8278  N  N     A GLY B 2 96  ? 26.629  -24.692 -18.928 0.50 45.36 ? 96  GLY B N     1 
ATOM   8279  N  N     B GLY B 2 96  ? 26.220  -23.923 -19.250 0.50 47.58 ? 96  GLY B N     1 
ATOM   8280  C  CA    A GLY B 2 96  ? 27.015  -24.225 -17.611 0.50 45.01 ? 96  GLY B CA    1 
ATOM   8281  C  CA    B GLY B 2 96  ? 26.461  -23.538 -17.873 0.50 47.07 ? 96  GLY B CA    1 
ATOM   8282  C  C     A GLY B 2 96  ? 27.837  -22.951 -17.665 0.50 41.63 ? 96  GLY B C     1 
ATOM   8283  C  C     B GLY B 2 96  ? 27.051  -22.151 -17.715 0.50 38.61 ? 96  GLY B C     1 
ATOM   8284  O  O     A GLY B 2 96  ? 28.406  -22.577 -18.691 0.50 38.78 ? 96  GLY B O     1 
ATOM   8285  O  O     B GLY B 2 96  ? 27.020  -21.343 -18.647 0.50 44.08 ? 96  GLY B O     1 
ATOM   8286  N  N     A ALA B 2 97  ? 27.897  -22.273 -16.518 0.50 36.15 ? 97  ALA B N     1 
ATOM   8287  N  N     B ALA B 2 97  ? 27.603  -21.866 -16.536 0.50 34.07 ? 97  ALA B N     1 
ATOM   8288  C  CA    A ALA B 2 97  ? 28.608  -21.004 -16.427 0.50 34.76 ? 97  ALA B CA    1 
ATOM   8289  C  CA    B ALA B 2 97  ? 28.132  -20.543 -16.235 0.50 35.62 ? 97  ALA B CA    1 
ATOM   8290  C  C     A ALA B 2 97  ? 30.121  -21.172 -16.395 0.50 33.36 ? 97  ALA B C     1 
ATOM   8291  C  C     B ALA B 2 97  ? 29.647  -20.449 -16.336 0.50 32.87 ? 97  ALA B C     1 
ATOM   8292  O  O     A ALA B 2 97  ? 30.842  -20.199 -16.646 0.50 39.70 ? 97  ALA B O     1 
ATOM   8293  O  O     B ALA B 2 97  ? 30.172  -19.334 -16.438 0.50 35.50 ? 97  ALA B O     1 
ATOM   8294  C  CB    A ALA B 2 97  ? 28.152  -20.232 -15.186 0.50 35.66 ? 97  ALA B CB    1 
ATOM   8295  C  CB    B ALA B 2 97  ? 27.704  -20.107 -14.829 0.50 36.01 ? 97  ALA B CB    1 
ATOM   8296  N  N     A GLY B 2 98  ? 30.618  -22.371 -16.101 0.50 37.76 ? 98  GLY B N     1 
ATOM   8297  N  N     B GLY B 2 98  ? 30.356  -21.574 -16.305 0.50 33.94 ? 98  GLY B N     1 
ATOM   8298  C  CA    A GLY B 2 98  ? 32.048  -22.610 -16.058 0.50 24.46 ? 98  GLY B CA    1 
ATOM   8299  C  CA    B GLY B 2 98  ? 31.809  -21.541 -16.408 0.50 33.15 ? 98  GLY B CA    1 
ATOM   8300  C  C     A GLY B 2 98  ? 32.763  -21.765 -15.020 0.50 28.66 ? 98  GLY B C     1 
ATOM   8301  C  C     B GLY B 2 98  ? 32.480  -20.712 -15.334 0.50 32.07 ? 98  GLY B C     1 
ATOM   8302  O  O     A GLY B 2 98  ? 33.801  -21.161 -15.309 0.50 31.99 ? 98  GLY B O     1 
ATOM   8303  O  O     B GLY B 2 98  ? 33.464  -20.015 -15.616 0.50 28.42 ? 98  GLY B O     1 
ATOM   8304  N  N     A ASN B 2 99  ? 32.207  -21.721 -13.809 0.50 32.07 ? 99  ASN B N     1 
ATOM   8305  N  N     B ASN B 2 99  ? 31.950  -20.752 -14.110 0.50 30.69 ? 99  ASN B N     1 
ATOM   8306  C  CA    A ASN B 2 99  ? 32.725  -20.940 -12.685 0.50 32.83 ? 99  ASN B CA    1 
ATOM   8307  C  CA    B ASN B 2 99  ? 32.510  -20.027 -12.964 0.50 30.01 ? 99  ASN B CA    1 
ATOM   8308  C  C     A ASN B 2 99  ? 32.797  -19.445 -12.984 0.50 27.09 ? 99  ASN B C     1 
ATOM   8309  C  C     B ASN B 2 99  ? 32.588  -18.524 -13.215 0.50 30.48 ? 99  ASN B C     1 
ATOM   8310  O  O     A ASN B 2 99  ? 33.592  -18.725 -12.372 0.50 28.14 ? 99  ASN B O     1 
ATOM   8311  O  O     B ASN B 2 99  ? 33.404  -17.826 -12.609 0.50 28.39 ? 99  ASN B O     1 
ATOM   8312  C  CB    A ASN B 2 99  ? 34.098  -21.450 -12.226 0.50 32.52 ? 99  ASN B CB    1 
ATOM   8313  C  CB    B ASN B 2 99  ? 33.888  -20.569 -12.576 0.50 29.75 ? 99  ASN B CB    1 
ATOM   8314  C  CG    A ASN B 2 99  ? 34.038  -22.856 -11.670 0.50 36.36 ? 99  ASN B CG    1 
ATOM   8315  C  CG    B ASN B 2 99  ? 33.844  -22.019 -12.146 0.50 35.13 ? 99  ASN B CG    1 
ATOM   8316  O  OD1   A ASN B 2 99  ? 33.614  -23.068 -10.536 0.50 35.73 ? 99  ASN B OD1   1 
ATOM   8317  O  OD1   B ASN B 2 99  ? 32.861  -22.477 -11.559 0.50 34.17 ? 99  ASN B OD1   1 
ATOM   8318  N  ND2   A ASN B 2 99  ? 34.466  -23.826 -12.467 0.50 35.49 ? 99  ASN B ND2   1 
ATOM   8319  N  ND2   B ASN B 2 99  ? 34.910  -22.755 -12.441 0.50 26.65 ? 99  ASN B ND2   1 
ATOM   8320  N  N     A ASN B 2 100 ? 31.969  -18.954 -13.902 0.50 28.41 ? 100 ASN B N     1 
ATOM   8321  N  N     B ASN B 2 100 ? 31.729  -18.008 -14.088 0.50 31.99 ? 100 ASN B N     1 
ATOM   8322  C  CA    A ASN B 2 100 ? 31.918  -17.536 -14.243 0.50 33.11 ? 100 ASN B CA    1 
ATOM   8323  C  CA    B ASN B 2 100 ? 31.721  -16.594 -14.446 0.50 34.23 ? 100 ASN B CA    1 
ATOM   8324  C  C     A ASN B 2 100 ? 30.626  -16.946 -13.692 0.50 30.88 ? 100 ASN B C     1 
ATOM   8325  C  C     B ASN B 2 100 ? 30.496  -15.945 -13.813 0.50 31.61 ? 100 ASN B C     1 
ATOM   8326  O  O     A ASN B 2 100 ? 29.532  -17.358 -14.092 0.50 30.47 ? 100 ASN B O     1 
ATOM   8327  O  O     B ASN B 2 100 ? 29.365  -16.197 -14.240 0.50 31.42 ? 100 ASN B O     1 
ATOM   8328  C  CB    A ASN B 2 100 ? 32.014  -17.332 -15.758 0.50 30.05 ? 100 ASN B CB    1 
ATOM   8329  C  CB    B ASN B 2 100 ? 31.725  -16.422 -15.965 0.50 30.42 ? 100 ASN B CB    1 
ATOM   8330  C  CG    A ASN B 2 100 ? 32.259  -15.878 -16.146 0.50 29.97 ? 100 ASN B CG    1 
ATOM   8331  C  CG    B ASN B 2 100 ? 31.969  -14.986 -16.393 0.50 32.50 ? 100 ASN B CG    1 
ATOM   8332  O  OD1   A ASN B 2 100 ? 31.707  -14.956 -15.546 0.50 29.25 ? 100 ASN B OD1   1 
ATOM   8333  O  OD1   B ASN B 2 100 ? 31.496  -14.047 -15.755 0.50 32.71 ? 100 ASN B OD1   1 
ATOM   8334  N  ND2   A ASN B 2 100 ? 33.088  -15.672 -17.166 0.50 35.42 ? 100 ASN B ND2   1 
ATOM   8335  N  ND2   B ASN B 2 100 ? 32.714  -14.810 -17.482 0.50 33.65 ? 100 ASN B ND2   1 
ATOM   8336  N  N     A TRP B 2 101 ? 30.760  -15.976 -12.781 0.50 34.80 ? 101 TRP B N     1 
ATOM   8337  N  N     B TRP B 2 101 ? 30.727  -15.110 -12.794 0.50 31.98 ? 101 TRP B N     1 
ATOM   8338  C  CA    A TRP B 2 101 ? 29.595  -15.346 -12.164 0.50 29.59 ? 101 TRP B CA    1 
ATOM   8339  C  CA    B TRP B 2 101 ? 29.629  -14.396 -12.148 0.50 31.00 ? 101 TRP B CA    1 
ATOM   8340  C  C     A TRP B 2 101 ? 28.800  -14.533 -13.178 0.50 31.49 ? 101 TRP B C     1 
ATOM   8341  C  C     B TRP B 2 101 ? 28.891  -13.511 -13.144 0.50 31.85 ? 101 TRP B C     1 
ATOM   8342  O  O     A TRP B 2 101 ? 27.564  -14.488 -13.114 0.50 26.39 ? 101 TRP B O     1 
ATOM   8343  O  O     B TRP B 2 101 ? 27.657  -13.404 -13.100 0.50 27.89 ? 101 TRP B O     1 
ATOM   8344  C  CB    A TRP B 2 101 ? 30.050  -14.453 -11.009 0.50 28.96 ? 101 TRP B CB    1 
ATOM   8345  C  CB    B TRP B 2 101 ? 30.165  -13.564 -10.979 0.50 26.55 ? 101 TRP B CB    1 
ATOM   8346  C  CG    A TRP B 2 101 ? 28.965  -13.965 -10.098 0.50 28.93 ? 101 TRP B CG    1 
ATOM   8347  C  CG    B TRP B 2 101 ? 29.106  -13.002 -10.060 0.50 29.03 ? 101 TRP B CG    1 
ATOM   8348  C  CD1   A TRP B 2 101 ? 28.468  -14.608 -9.005  0.50 31.03 ? 101 TRP B CD1   1 
ATOM   8349  C  CD1   B TRP B 2 101 ? 28.570  -13.607 -8.960  0.50 26.40 ? 101 TRP B CD1   1 
ATOM   8350  C  CD2   A TRP B 2 101 ? 28.273  -12.712 -10.174 0.50 24.59 ? 101 TRP B CD2   1 
ATOM   8351  C  CD2   B TRP B 2 101 ? 28.477  -11.717 -10.155 0.50 27.66 ? 101 TRP B CD2   1 
ATOM   8352  N  NE1   A TRP B 2 101 ? 27.498  -13.843 -8.405  0.50 24.31 ? 101 TRP B NE1   1 
ATOM   8353  N  NE1   B TRP B 2 101 ? 27.641  -12.785 -8.371  0.50 27.39 ? 101 TRP B NE1   1 
ATOM   8354  C  CE2   A TRP B 2 101 ? 27.360  -12.673 -9.103  0.50 27.83 ? 101 TRP B CE2   1 
ATOM   8355  C  CE2   B TRP B 2 101 ? 27.566  -11.617 -9.082  0.50 28.22 ? 101 TRP B CE2   1 
ATOM   8356  C  CE3   A TRP B 2 101 ? 28.336  -11.621 -11.046 0.50 29.14 ? 101 TRP B CE3   1 
ATOM   8357  C  CE3   B TRP B 2 101 ? 28.596  -10.641 -11.041 0.50 31.52 ? 101 TRP B CE3   1 
ATOM   8358  C  CZ2   A TRP B 2 101 ? 26.513  -11.588 -8.882  0.50 26.16 ? 101 TRP B CZ2   1 
ATOM   8359  C  CZ2   B TRP B 2 101 ? 26.775  -10.486 -8.875  0.50 24.08 ? 101 TRP B CZ2   1 
ATOM   8360  C  CZ3   A TRP B 2 101 ? 27.494  -10.545 -10.826 0.50 32.97 ? 101 TRP B CZ3   1 
ATOM   8361  C  CZ3   B TRP B 2 101 ? 27.811  -9.520  -10.834 0.50 32.06 ? 101 TRP B CZ3   1 
ATOM   8362  C  CH2   A TRP B 2 101 ? 26.594  -10.535 -9.751  0.50 30.84 ? 101 TRP B CH2   1 
ATOM   8363  C  CH2   B TRP B 2 101 ? 26.908  -9.453  -9.762  0.50 27.58 ? 101 TRP B CH2   1 
ATOM   8364  N  N     A ALA B 2 102 ? 29.495  -13.875 -14.112 0.50 27.55 ? 102 ALA B N     1 
ATOM   8365  N  N     B ALA B 2 102 ? 29.631  -12.875 -14.057 0.50 28.14 ? 102 ALA B N     1 
ATOM   8366  C  CA    A ALA B 2 102 ? 28.824  -13.014 -15.082 0.50 30.19 ? 102 ALA B CA    1 
ATOM   8367  C  CA    B ALA B 2 102 ? 29.002  -12.020 -15.059 0.50 32.88 ? 102 ALA B CA    1 
ATOM   8368  C  C     A ALA B 2 102 ? 27.921  -13.817 -16.008 0.50 31.23 ? 102 ALA B C     1 
ATOM   8369  C  C     B ALA B 2 102 ? 28.095  -12.824 -15.979 0.50 25.51 ? 102 ALA B C     1 
ATOM   8370  O  O     A ALA B 2 102 ? 26.841  -13.350 -16.387 0.50 32.70 ? 102 ALA B O     1 
ATOM   8371  O  O     B ALA B 2 102 ? 27.034  -12.343 -16.390 0.50 32.61 ? 102 ALA B O     1 
ATOM   8372  C  CB    A ALA B 2 102 ? 29.857  -12.227 -15.889 0.50 30.14 ? 102 ALA B CB    1 
ATOM   8373  C  CB    B ALA B 2 102 ? 30.069  -11.286 -15.871 0.50 27.03 ? 102 ALA B CB    1 
ATOM   8374  N  N     A LYS B 2 103 ? 28.346  -15.025 -16.388 0.50 33.05 ? 103 LYS B N     1 
ATOM   8375  N  N     B LYS B 2 103 ? 28.495  -14.053 -16.315 0.50 32.24 ? 103 LYS B N     1 
ATOM   8376  C  CA    A LYS B 2 103 ? 27.481  -15.888 -17.186 0.50 31.66 ? 103 LYS B CA    1 
ATOM   8377  C  CA    B LYS B 2 103 ? 27.659  -14.892 -17.170 0.50 34.12 ? 103 LYS B CA    1 
ATOM   8378  C  C     A LYS B 2 103 ? 26.245  -16.294 -16.399 0.50 33.80 ? 103 LYS B C     1 
ATOM   8379  C  C     B LYS B 2 103 ? 26.321  -15.185 -16.505 0.50 31.12 ? 103 LYS B C     1 
ATOM   8380  O  O     A LYS B 2 103 ? 25.139  -16.368 -16.950 0.50 31.80 ? 103 LYS B O     1 
ATOM   8381  O  O     B LYS B 2 103 ? 25.259  -15.014 -17.115 0.50 36.09 ? 103 LYS B O     1 
ATOM   8382  C  CB    A LYS B 2 103 ? 28.253  -17.122 -17.648 0.50 35.72 ? 103 LYS B CB    1 
ATOM   8383  C  CB    B LYS B 2 103 ? 28.385  -16.195 -17.508 0.50 35.76 ? 103 LYS B CB    1 
ATOM   8384  C  CG    A LYS B 2 103 ? 29.415  -16.814 -18.581 0.50 35.81 ? 103 LYS B CG    1 
ATOM   8385  C  CG    B LYS B 2 103 ? 28.769  -16.332 -18.977 0.50 38.83 ? 103 LYS B CG    1 
ATOM   8386  C  CD    A LYS B 2 103 ? 30.207  -18.068 -18.892 0.50 33.61 ? 103 LYS B CD    1 
ATOM   8387  C  CD    B LYS B 2 103 ? 29.119  -17.772 -19.330 0.50 28.15 ? 103 LYS B CD    1 
ATOM   8388  C  CE    A LYS B 2 103 ? 31.280  -17.810 -19.933 0.50 38.97 ? 103 LYS B CE    1 
ATOM   8389  C  CE    B LYS B 2 103 ? 29.526  -17.905 -20.789 0.50 42.50 ? 103 LYS B CE    1 
ATOM   8390  N  NZ    A LYS B 2 103 ? 30.681  -17.521 -21.267 0.50 48.91 ? 103 LYS B NZ    1 
ATOM   8391  N  NZ    B LYS B 2 103 ? 30.762  -17.125 -21.082 0.50 48.37 ? 103 LYS B NZ    1 
ATOM   8392  N  N     A GLY B 2 104 ? 26.411  -16.562 -15.104 0.50 33.35 ? 104 GLY B N     1 
ATOM   8393  N  N     B GLY B 2 104 ? 26.353  -15.626 -15.247 0.50 32.09 ? 104 GLY B N     1 
ATOM   8394  C  CA    A GLY B 2 104 ? 25.260  -16.882 -14.280 0.50 29.90 ? 104 GLY B CA    1 
ATOM   8395  C  CA    B GLY B 2 104 ? 25.117  -15.948 -14.554 0.50 26.96 ? 104 GLY B CA    1 
ATOM   8396  C  C     A GLY B 2 104 ? 24.311  -15.710 -14.127 0.50 27.83 ? 104 GLY B C     1 
ATOM   8397  C  C     B GLY B 2 104 ? 24.254  -14.740 -14.261 0.50 29.50 ? 104 GLY B C     1 
ATOM   8398  O  O     A GLY B 2 104 ? 23.091  -15.872 -14.212 0.50 32.26 ? 104 GLY B O     1 
ATOM   8399  O  O     B GLY B 2 104 ? 23.024  -14.833 -14.285 0.50 32.22 ? 104 GLY B O     1 
ATOM   8400  N  N     A HIS B 2 105 ? 24.854  -14.512 -13.914 0.50 26.49 ? 105 HIS B N     1 
ATOM   8401  N  N     B HIS B 2 105 ? 24.873  -13.593 -13.988 0.50 28.68 ? 105 HIS B N     1 
ATOM   8402  C  CA    A HIS B 2 105 ? 24.027  -13.370 -13.542 0.50 28.46 ? 105 HIS B CA    1 
ATOM   8403  C  CA    B HIS B 2 105 ? 24.114  -12.423 -13.566 0.50 29.44 ? 105 HIS B CA    1 
ATOM   8404  C  C     A HIS B 2 105 ? 23.485  -12.596 -14.737 0.50 31.91 ? 105 HIS B C     1 
ATOM   8405  C  C     B HIS B 2 105 ? 23.638  -11.553 -14.721 0.50 31.21 ? 105 HIS B C     1 
ATOM   8406  O  O     A HIS B 2 105 ? 22.383  -12.040 -14.648 0.50 25.69 ? 105 HIS B O     1 
ATOM   8407  O  O     B HIS B 2 105 ? 22.648  -10.832 -14.558 0.50 29.31 ? 105 HIS B O     1 
ATOM   8408  C  CB    A HIS B 2 105 ? 24.823  -12.415 -12.643 0.50 28.91 ? 105 HIS B CB    1 
ATOM   8409  C  CB    B HIS B 2 105 ? 24.947  -11.561 -12.609 0.50 25.28 ? 105 HIS B CB    1 
ATOM   8410  C  CG    A HIS B 2 105 ? 23.969  -11.535 -11.781 0.50 31.89 ? 105 HIS B CG    1 
ATOM   8411  C  CG    B HIS B 2 105 ? 24.126  -10.651 -11.748 0.50 32.57 ? 105 HIS B CG    1 
ATOM   8412  N  ND1   A HIS B 2 105 ? 23.469  -11.944 -10.564 0.50 22.75 ? 105 HIS B ND1   1 
ATOM   8413  N  ND1   B HIS B 2 105 ? 23.747  -9.387  -12.146 0.50 29.68 ? 105 HIS B ND1   1 
ATOM   8414  C  CD2   A HIS B 2 105 ? 23.531  -10.265 -11.959 0.50 32.65 ? 105 HIS B CD2   1 
ATOM   8415  C  CD2   B HIS B 2 105 ? 23.607  -10.826 -10.509 0.50 28.27 ? 105 HIS B CD2   1 
ATOM   8416  C  CE1   A HIS B 2 105 ? 22.759  -10.967 -10.029 0.50 26.27 ? 105 HIS B CE1   1 
ATOM   8417  C  CE1   B HIS B 2 105 ? 23.031  -8.823  -11.189 0.50 33.89 ? 105 HIS B CE1   1 
ATOM   8418  N  NE2   A HIS B 2 105 ? 22.780  -9.937  -10.855 0.50 30.00 ? 105 HIS B NE2   1 
ATOM   8419  N  NE2   B HIS B 2 105 ? 22.933  -9.674  -10.184 0.50 28.20 ? 105 HIS B NE2   1 
ATOM   8420  N  N     A TYR B 2 106 ? 24.218  -12.547 -15.856 0.50 31.22 ? 106 TYR B N     1 
ATOM   8421  N  N     B TYR B 2 106 ? 24.298  -11.603 -15.880 0.50 32.54 ? 106 TYR B N     1 
ATOM   8422  C  CA    A TYR B 2 106 ? 23.896  -11.619 -16.934 0.50 31.69 ? 106 TYR B CA    1 
ATOM   8423  C  CA    B TYR B 2 106 ? 24.035  -10.599 -16.905 0.50 34.93 ? 106 TYR B CA    1 
ATOM   8424  C  C     A TYR B 2 106 ? 23.491  -12.268 -18.251 0.50 35.63 ? 106 TYR B C     1 
ATOM   8425  C  C     B TYR B 2 106 ? 23.686  -11.171 -18.273 0.50 34.46 ? 106 TYR B C     1 
ATOM   8426  O  O     A TYR B 2 106 ? 22.651  -11.704 -18.956 0.50 37.00 ? 106 TYR B O     1 
ATOM   8427  O  O     B TYR B 2 106 ? 22.952  -10.533 -19.035 0.50 30.80 ? 106 TYR B O     1 
ATOM   8428  C  CB    A TYR B 2 106 ? 25.083  -10.680 -17.206 0.50 32.69 ? 106 TYR B CB    1 
ATOM   8429  C  CB    B TYR B 2 106 ? 25.239  -9.664  -17.032 0.50 31.74 ? 106 TYR B CB    1 
ATOM   8430  C  CG    A TYR B 2 106 ? 25.332  -9.675  -16.107 0.50 34.43 ? 106 TYR B CG    1 
ATOM   8431  C  CG    B TYR B 2 106 ? 25.265  -8.578  -15.982 0.50 32.40 ? 106 TYR B CG    1 
ATOM   8432  C  CD1   A TYR B 2 106 ? 24.380  -8.713  -15.795 0.50 36.73 ? 106 TYR B CD1   1 
ATOM   8433  C  CD1   B TYR B 2 106 ? 24.083  -8.067  -15.459 0.50 37.45 ? 106 TYR B CD1   1 
ATOM   8434  C  CD2   A TYR B 2 106 ? 26.519  -9.683  -15.385 0.50 31.18 ? 106 TYR B CD2   1 
ATOM   8435  C  CD2   B TYR B 2 106 ? 26.467  -8.069  -15.508 0.50 37.37 ? 106 TYR B CD2   1 
ATOM   8436  C  CE1   A TYR B 2 106 ? 24.600  -7.789  -14.792 0.50 34.99 ? 106 TYR B CE1   1 
ATOM   8437  C  CE1   B TYR B 2 106 ? 24.098  -7.073  -14.500 0.50 32.39 ? 106 TYR B CE1   1 
ATOM   8438  C  CE2   A TYR B 2 106 ? 26.746  -8.763  -14.379 0.50 33.82 ? 106 TYR B CE2   1 
ATOM   8439  C  CE2   B TYR B 2 106 ? 26.492  -7.076  -14.547 0.50 40.38 ? 106 TYR B CE2   1 
ATOM   8440  C  CZ    A TYR B 2 106 ? 25.785  -7.820  -14.088 0.50 35.04 ? 106 TYR B CZ    1 
ATOM   8441  C  CZ    B TYR B 2 106 ? 25.302  -6.582  -14.046 0.50 34.70 ? 106 TYR B CZ    1 
ATOM   8442  O  OH    A TYR B 2 106 ? 26.008  -6.899  -13.091 0.50 31.65 ? 106 TYR B OH    1 
ATOM   8443  O  OH    B TYR B 2 106 ? 25.319  -5.594  -13.092 0.50 40.66 ? 106 TYR B OH    1 
ATOM   8444  N  N     A THR B 2 107 ? 24.060  -13.415 -18.617 0.50 27.47 ? 107 THR B N     1 
ATOM   8445  N  N     B THR B 2 107 ? 24.194  -12.355 -18.610 0.50 31.00 ? 107 THR B N     1 
ATOM   8446  C  CA    A THR B 2 107 ? 23.814  -13.946 -19.955 0.50 37.28 ? 107 THR B CA    1 
ATOM   8447  C  CA    B THR B 2 107 ? 23.967  -12.869 -19.957 0.50 36.07 ? 107 THR B CA    1 
ATOM   8448  C  C     A THR B 2 107 ? 23.114  -15.300 -19.924 0.50 33.82 ? 107 THR B C     1 
ATOM   8449  C  C     B THR B 2 107 ? 23.165  -14.165 -19.945 0.50 38.65 ? 107 THR B C     1 
ATOM   8450  O  O     A THR B 2 107 ? 21.894  -15.376 -20.099 0.50 36.74 ? 107 THR B O     1 
ATOM   8451  O  O     B THR B 2 107 ? 21.936  -14.134 -20.066 0.50 40.04 ? 107 THR B O     1 
ATOM   8452  C  CB    A THR B 2 107 ? 25.125  -14.055 -20.738 0.50 37.13 ? 107 THR B CB    1 
ATOM   8453  C  CB    B THR B 2 107 ? 25.301  -13.061 -20.685 0.50 33.60 ? 107 THR B CB    1 
ATOM   8454  O  OG1   A THR B 2 107 ? 25.994  -14.998 -20.098 0.50 39.74 ? 107 THR B OG1   1 
ATOM   8455  O  OG1   B THR B 2 107 ? 26.150  -13.935 -19.931 0.50 33.56 ? 107 THR B OG1   1 
ATOM   8456  C  CG2   A THR B 2 107 ? 25.818  -12.704 -20.805 0.50 34.98 ? 107 THR B CG2   1 
ATOM   8457  C  CG2   B THR B 2 107 ? 25.994  -11.717 -20.854 0.50 36.14 ? 107 THR B CG2   1 
ATOM   8458  N  N     A GLU B 2 108 ? 23.882  -16.372 -19.721 0.50 36.25 ? 108 GLU B N     1 
ATOM   8459  N  N     B GLU B 2 108 ? 23.851  -15.304 -19.812 0.50 33.25 ? 108 GLU B N     1 
ATOM   8460  C  CA    A GLU B 2 108 ? 23.307  -17.714 -19.718 0.50 37.48 ? 108 GLU B CA    1 
ATOM   8461  C  CA    B GLU B 2 108 ? 23.174  -16.599 -19.805 0.50 33.23 ? 108 GLU B CA    1 
ATOM   8462  C  C     A GLU B 2 108 ? 22.214  -17.843 -18.663 0.50 38.01 ? 108 GLU B C     1 
ATOM   8463  C  C     B GLU B 2 108 ? 22.051  -16.636 -18.775 0.50 33.15 ? 108 GLU B C     1 
ATOM   8464  O  O     A GLU B 2 108 ? 21.116  -18.340 -18.942 0.50 37.84 ? 108 GLU B O     1 
ATOM   8465  O  O     B GLU B 2 108 ? 20.940  -17.098 -19.063 0.50 33.35 ? 108 GLU B O     1 
ATOM   8466  C  CB    A GLU B 2 108 ? 24.409  -18.747 -19.480 0.50 36.30 ? 108 GLU B CB    1 
ATOM   8467  C  CB    B GLU B 2 108 ? 24.188  -17.711 -19.525 0.50 35.05 ? 108 GLU B CB    1 
ATOM   8468  C  CG    A GLU B 2 108 ? 25.694  -18.466 -20.242 0.50 46.34 ? 108 GLU B CG    1 
ATOM   8469  C  CG    B GLU B 2 108 ? 25.224  -17.912 -20.615 0.50 45.11 ? 108 GLU B CG    1 
ATOM   8470  C  CD    A GLU B 2 108 ? 25.490  -18.456 -21.742 0.50 47.09 ? 108 GLU B CD    1 
ATOM   8471  C  CD    B GLU B 2 108 ? 24.828  -19.000 -21.594 0.50 50.07 ? 108 GLU B CD    1 
ATOM   8472  O  OE1   A GLU B 2 108 ? 24.802  -19.364 -22.257 0.50 53.76 ? 108 GLU B OE1   1 
ATOM   8473  O  OE1   B GLU B 2 108 ? 23.903  -19.780 -21.275 0.50 50.51 ? 108 GLU B OE1   1 
ATOM   8474  O  OE2   A GLU B 2 108 ? 26.009  -17.535 -22.408 0.50 52.93 ? 108 GLU B OE2   1 
ATOM   8475  O  OE2   B GLU B 2 108 ? 25.437  -19.073 -22.683 0.50 56.03 ? 108 GLU B OE2   1 
ATOM   8476  N  N     A GLY B 2 109 ? 22.498  -17.395 -17.440 0.50 36.43 ? 109 GLY B N     1 
ATOM   8477  N  N     B GLY B 2 109 ? 22.321  -16.140 -17.567 0.50 34.16 ? 109 GLY B N     1 
ATOM   8478  C  CA    A GLY B 2 109 ? 21.502  -17.487 -16.387 0.50 35.97 ? 109 GLY B CA    1 
ATOM   8479  C  CA    B GLY B 2 109 ? 21.349  -16.219 -16.490 0.50 30.38 ? 109 GLY B CA    1 
ATOM   8480  C  C     A GLY B 2 109 ? 20.291  -16.613 -16.646 0.50 34.82 ? 109 GLY B C     1 
ATOM   8481  C  C     B GLY B 2 109 ? 20.189  -15.255 -16.615 0.50 35.58 ? 109 GLY B C     1 
ATOM   8482  O  O     A GLY B 2 109 ? 19.152  -17.041 -16.444 0.50 37.68 ? 109 GLY B O     1 
ATOM   8483  O  O     B GLY B 2 109 ? 19.139  -15.488 -16.004 0.50 39.37 ? 109 GLY B O     1 
ATOM   8484  N  N     A ALA B 2 110 ? 20.519  -15.381 -17.111 0.50 30.69 ? 110 ALA B N     1 
ATOM   8485  N  N     B ALA B 2 110 ? 20.351  -14.175 -17.378 0.50 35.64 ? 110 ALA B N     1 
ATOM   8486  C  CA    A ALA B 2 110 ? 19.432  -14.422 -17.282 0.50 36.69 ? 110 ALA B CA    1 
ATOM   8487  C  CA    B ALA B 2 110 ? 19.274  -13.212 -17.577 0.50 38.10 ? 110 ALA B CA    1 
ATOM   8488  C  C     A ALA B 2 110 ? 18.446  -14.830 -18.369 0.50 39.77 ? 110 ALA B C     1 
ATOM   8489  C  C     B ALA B 2 110 ? 18.319  -13.615 -18.692 0.50 37.84 ? 110 ALA B C     1 
ATOM   8490  O  O     A ALA B 2 110 ? 17.292  -14.392 -18.334 0.50 44.23 ? 110 ALA B O     1 
ATOM   8491  O  O     B ALA B 2 110 ? 17.344  -12.898 -18.942 0.50 42.29 ? 110 ALA B O     1 
ATOM   8492  C  CB    A ALA B 2 110 ? 19.996  -13.035 -17.588 0.50 38.94 ? 110 ALA B CB    1 
ATOM   8493  C  CB    B ALA B 2 110 ? 19.850  -11.823 -17.866 0.50 32.70 ? 110 ALA B CB    1 
ATOM   8494  N  N     A GLU B 2 111 ? 18.869  -15.641 -19.339 0.50 39.50 ? 111 GLU B N     1 
ATOM   8495  N  N     B GLU B 2 111 ? 18.578  -14.732 -19.371 0.50 40.84 ? 111 GLU B N     1 
ATOM   8496  C  CA    A GLU B 2 111 ? 17.926  -16.144 -20.331 0.50 42.58 ? 111 GLU B CA    1 
ATOM   8497  C  CA    B GLU B 2 111 ? 17.678  -15.267 -20.381 0.50 41.12 ? 111 GLU B CA    1 
ATOM   8498  C  C     A GLU B 2 111 ? 17.032  -17.238 -19.765 0.50 46.29 ? 111 GLU B C     1 
ATOM   8499  C  C     B GLU B 2 111 ? 16.759  -16.345 -19.825 0.50 46.73 ? 111 GLU B C     1 
ATOM   8500  O  O     A GLU B 2 111 ? 15.976  -17.520 -20.341 0.50 48.16 ? 111 GLU B O     1 
ATOM   8501  O  O     B GLU B 2 111 ? 15.828  -16.768 -20.519 0.50 44.25 ? 111 GLU B O     1 
ATOM   8502  C  CB    A GLU B 2 111 ? 18.676  -16.664 -21.560 0.50 44.48 ? 111 GLU B CB    1 
ATOM   8503  C  CB    B GLU B 2 111 ? 18.491  -15.830 -21.558 0.50 44.94 ? 111 GLU B CB    1 
ATOM   8504  C  CG    A GLU B 2 111 ? 19.131  -15.574 -22.518 0.50 45.18 ? 111 GLU B CG    1 
ATOM   8505  C  CG    B GLU B 2 111 ? 17.786  -15.786 -22.905 0.50 54.93 ? 111 GLU B CG    1 
ATOM   8506  C  CD    A GLU B 2 111 ? 18.043  -15.163 -23.494 0.50 57.04 ? 111 GLU B CD    1 
ATOM   8507  C  CD    B GLU B 2 111 ? 18.745  -15.964 -24.072 0.50 56.15 ? 111 GLU B CD    1 
ATOM   8508  O  OE1   A GLU B 2 111 ? 17.177  -16.007 -23.812 0.50 56.59 ? 111 GLU B OE1   1 
ATOM   8509  O  OE1   B GLU B 2 111 ? 19.971  -16.041 -23.836 0.50 51.22 ? 111 GLU B OE1   1 
ATOM   8510  O  OE2   A GLU B 2 111 ? 18.052  -13.994 -23.939 0.50 56.67 ? 111 GLU B OE2   1 
ATOM   8511  O  OE2   B GLU B 2 111 ? 18.272  -16.023 -25.228 0.50 59.48 ? 111 GLU B OE2   1 
ATOM   8512  N  N     A LEU B 2 112 ? 17.425  -17.845 -18.646 0.50 38.75 ? 112 LEU B N     1 
ATOM   8513  N  N     B LEU B 2 112 ? 16.987  -16.775 -18.582 0.50 42.41 ? 112 LEU B N     1 
ATOM   8514  C  CA    A LEU B 2 112 ? 16.685  -18.944 -18.049 0.50 44.51 ? 112 LEU B CA    1 
ATOM   8515  C  CA    B LEU B 2 112 ? 16.257  -17.868 -17.961 0.50 44.41 ? 112 LEU B CA    1 
ATOM   8516  C  C     A LEU B 2 112 ? 15.916  -18.549 -16.794 0.50 43.13 ? 112 LEU B C     1 
ATOM   8517  C  C     B LEU B 2 112 ? 15.484  -17.458 -16.715 0.50 44.89 ? 112 LEU B C     1 
ATOM   8518  O  O     A LEU B 2 112 ? 15.161  -19.375 -16.270 0.50 45.97 ? 112 LEU B O     1 
ATOM   8519  O  O     B LEU B 2 112 ? 14.595  -18.206 -16.289 0.50 40.67 ? 112 LEU B O     1 
ATOM   8520  C  CB    A LEU B 2 112 ? 17.648  -20.095 -17.713 0.50 42.10 ? 112 LEU B CB    1 
ATOM   8521  C  CB    B LEU B 2 112 ? 17.232  -19.004 -17.598 0.50 44.03 ? 112 LEU B CB    1 
ATOM   8522  C  CG    A LEU B 2 112 ? 17.076  -21.511 -17.660 0.50 42.17 ? 112 LEU B CG    1 
ATOM   8523  C  CG    B LEU B 2 112 ? 16.762  -20.309 -16.949 0.50 40.85 ? 112 LEU B CG    1 
ATOM   8524  C  CD1   A LEU B 2 112 ? 16.435  -21.878 -18.988 0.50 39.79 ? 112 LEU B CD1   1 
ATOM   8525  C  CD1   B LEU B 2 112 ? 15.871  -21.103 -17.890 0.50 43.31 ? 112 LEU B CD1   1 
ATOM   8526  C  CD2   A LEU B 2 112 ? 18.164  -22.507 -17.298 0.50 45.92 ? 112 LEU B CD2   1 
ATOM   8527  C  CD2   B LEU B 2 112 ? 17.962  -21.135 -16.515 0.50 36.51 ? 112 LEU B CD2   1 
ATOM   8528  N  N     A VAL B 2 113 ? 16.073  -17.315 -16.308 0.50 44.78 ? 113 VAL B N     1 
ATOM   8529  N  N     B VAL B 2 113 ? 15.776  -16.289 -16.136 0.50 43.95 ? 113 VAL B N     1 
ATOM   8530  C  CA    A VAL B 2 113 ? 15.448  -16.933 -15.043 0.50 43.19 ? 113 VAL B CA    1 
ATOM   8531  C  CA    B VAL B 2 113 ? 15.177  -15.908 -14.859 0.50 43.59 ? 113 VAL B CA    1 
ATOM   8532  C  C     A VAL B 2 113 ? 13.929  -16.897 -15.177 0.50 45.07 ? 113 VAL B C     1 
ATOM   8533  C  C     B VAL B 2 113 ? 13.670  -15.721 -14.990 0.50 44.55 ? 113 VAL B C     1 
ATOM   8534  O  O     A VAL B 2 113 ? 13.205  -17.253 -14.239 0.50 39.70 ? 113 VAL B O     1 
ATOM   8535  O  O     B VAL B 2 113 ? 12.925  -15.941 -14.026 0.50 43.75 ? 113 VAL B O     1 
ATOM   8536  C  CB    A VAL B 2 113 ? 16.014  -15.587 -14.546 0.50 38.82 ? 113 VAL B CB    1 
ATOM   8537  C  CB    B VAL B 2 113 ? 15.868  -14.642 -14.307 0.50 39.34 ? 113 VAL B CB    1 
ATOM   8538  C  CG1   A VAL B 2 113 ? 15.751  -14.480 -15.555 0.50 43.84 ? 113 VAL B CG1   1 
ATOM   8539  C  CG1   B VAL B 2 113 ? 15.618  -13.441 -15.219 0.50 38.06 ? 113 VAL B CG1   1 
ATOM   8540  C  CG2   A VAL B 2 113 ? 15.425  -15.229 -13.186 0.50 40.23 ? 113 VAL B CG2   1 
ATOM   8541  C  CG2   B VAL B 2 113 ? 15.406  -14.350 -12.881 0.50 37.06 ? 113 VAL B CG2   1 
ATOM   8542  N  N     A ASP B 2 114 ? 13.418  -16.483 -16.340 0.50 44.73 ? 114 ASP B N     1 
ATOM   8543  N  N     B ASP B 2 114 ? 13.190  -15.328 -16.174 0.50 41.78 ? 114 ASP B N     1 
ATOM   8544  C  CA    A ASP B 2 114 ? 11.971  -16.454 -16.528 0.50 44.36 ? 114 ASP B CA    1 
ATOM   8545  C  CA    B ASP B 2 114 ? 11.748  -15.193 -16.371 0.50 41.51 ? 114 ASP B CA    1 
ATOM   8546  C  C     A ASP B 2 114 ? 11.370  -17.851 -16.454 0.50 42.14 ? 114 ASP B C     1 
ATOM   8547  C  C     B ASP B 2 114 ? 11.045  -16.542 -16.280 0.50 44.36 ? 114 ASP B C     1 
ATOM   8548  O  O     A ASP B 2 114 ? 10.241  -18.015 -15.982 0.50 44.54 ? 114 ASP B O     1 
ATOM   8549  O  O     B ASP B 2 114 ? 9.955   -16.643 -15.704 0.50 49.80 ? 114 ASP B O     1 
ATOM   8550  C  CB    A ASP B 2 114 ? 11.618  -15.791 -17.859 0.50 47.30 ? 114 ASP B CB    1 
ATOM   8551  C  CB    B ASP B 2 114 ? 11.456  -14.530 -17.717 0.50 48.61 ? 114 ASP B CB    1 
ATOM   8552  C  CG    A ASP B 2 114 ? 11.683  -14.276 -17.791 0.50 47.88 ? 114 ASP B CG    1 
ATOM   8553  C  CG    B ASP B 2 114 ? 11.631  -13.027 -17.676 0.50 45.93 ? 114 ASP B CG    1 
ATOM   8554  O  OD1   A ASP B 2 114 ? 11.409  -13.715 -16.709 0.50 47.71 ? 114 ASP B OD1   1 
ATOM   8555  O  OD1   B ASP B 2 114 ? 12.080  -12.506 -16.634 0.50 50.48 ? 114 ASP B OD1   1 
ATOM   8556  O  OD2   A ASP B 2 114 ? 12.005  -13.648 -18.820 0.50 44.39 ? 114 ASP B OD2   1 
ATOM   8557  O  OD2   B ASP B 2 114 ? 11.312  -12.365 -18.685 0.50 51.25 ? 114 ASP B OD2   1 
ATOM   8558  N  N     A SER B 2 115 ? 12.109  -18.868 -16.902 0.50 41.54 ? 115 SER B N     1 
ATOM   8559  N  N     B SER B 2 115 ? 11.651  -17.590 -16.842 0.50 42.92 ? 115 SER B N     1 
ATOM   8560  C  CA    A SER B 2 115 ? 11.627  -20.238 -16.770 0.50 45.67 ? 115 SER B CA    1 
ATOM   8561  C  CA    B SER B 2 115 ? 11.046  -18.915 -16.768 0.50 42.46 ? 115 SER B CA    1 
ATOM   8562  C  C     A SER B 2 115 ? 11.496  -20.646 -15.309 0.50 41.92 ? 115 SER B C     1 
ATOM   8563  C  C     B SER B 2 115 ? 11.114  -19.486 -15.357 0.50 43.58 ? 115 SER B C     1 
ATOM   8564  O  O     A SER B 2 115 ? 10.620  -21.447 -14.964 0.50 42.17 ? 115 SER B O     1 
ATOM   8565  O  O     B SER B 2 115 ? 10.241  -20.270 -14.966 0.50 43.22 ? 115 SER B O     1 
ATOM   8566  C  CB    A SER B 2 115 ? 12.560  -21.197 -17.508 0.50 39.76 ? 115 SER B CB    1 
ATOM   8567  C  CB    B SER B 2 115 ? 11.724  -19.858 -17.762 0.50 43.75 ? 115 SER B CB    1 
ATOM   8568  O  OG    A SER B 2 115 ? 12.626  -20.873 -18.887 0.50 41.86 ? 115 SER B OG    1 
ATOM   8569  O  OG    B SER B 2 115 ? 11.423  -19.493 -19.098 0.50 45.63 ? 115 SER B OG    1 
ATOM   8570  N  N     A VAL B 2 116 ? 12.351  -20.107 -14.439 0.50 41.78 ? 116 VAL B N     1 
ATOM   8571  N  N     B VAL B 2 116 ? 12.136  -19.113 -14.584 0.50 42.47 ? 116 VAL B N     1 
ATOM   8572  C  CA    A VAL B 2 116 ? 12.266  -20.423 -13.018 0.50 41.23 ? 116 VAL B CA    1 
ATOM   8573  C  CA    B VAL B 2 116 ? 12.202  -19.539 -13.189 0.50 43.77 ? 116 VAL B CA    1 
ATOM   8574  C  C     A VAL B 2 116 ? 11.166  -19.610 -12.348 0.50 41.41 ? 116 VAL B C     1 
ATOM   8575  C  C     B VAL B 2 116 ? 11.071  -18.909 -12.387 0.50 39.35 ? 116 VAL B C     1 
ATOM   8576  O  O     A VAL B 2 116 ? 10.385  -20.144 -11.551 0.50 42.16 ? 116 VAL B O     1 
ATOM   8577  O  O     B VAL B 2 116 ? 10.412  -19.579 -11.582 0.50 43.84 ? 116 VAL B O     1 
ATOM   8578  C  CB    A VAL B 2 116 ? 13.628  -20.194 -12.339 0.50 41.93 ? 116 VAL B CB    1 
ATOM   8579  C  CB    B VAL B 2 116 ? 13.580  -19.199 -12.590 0.50 41.29 ? 116 VAL B CB    1 
ATOM   8580  C  CG1   A VAL B 2 116 ? 13.566  -20.620 -10.880 0.50 42.92 ? 116 VAL B CG1   1 
ATOM   8581  C  CG1   B VAL B 2 116 ? 13.647  -19.626 -11.132 0.50 42.36 ? 116 VAL B CG1   1 
ATOM   8582  C  CG2   A VAL B 2 116 ? 14.725  -20.944 -13.080 0.50 39.40 ? 116 VAL B CG2   1 
ATOM   8583  C  CG2   B VAL B 2 116 ? 14.692  -19.861 -13.396 0.50 42.23 ? 116 VAL B CG2   1 
ATOM   8584  N  N     A LEU B 2 117 ? 11.089  -18.311 -12.656 0.50 35.25 ? 117 LEU B N     1 
ATOM   8585  N  N     B LEU B 2 117 ? 10.822  -17.614 -12.597 0.50 37.62 ? 117 LEU B N     1 
ATOM   8586  C  CA    A LEU B 2 117 ? 10.078  -17.458 -12.040 0.50 41.19 ? 117 LEU B CA    1 
ATOM   8587  C  CA    B LEU B 2 117 ? 9.771   -16.919 -11.863 0.50 42.52 ? 117 LEU B CA    1 
ATOM   8588  C  C     A LEU B 2 117 ? 8.672   -17.946 -12.362 0.50 48.36 ? 117 LEU B C     1 
ATOM   8589  C  C     B LEU B 2 117 ? 8.385   -17.476 -12.157 0.50 49.16 ? 117 LEU B C     1 
ATOM   8590  O  O     A LEU B 2 117 ? 7.783   -17.911 -11.501 0.50 47.80 ? 117 LEU B O     1 
ATOM   8591  O  O     B LEU B 2 117 ? 7.484   -17.327 -11.324 0.50 47.49 ? 117 LEU B O     1 
ATOM   8592  C  CB    A LEU B 2 117 ? 10.257  -16.011 -12.499 0.50 41.84 ? 117 LEU B CB    1 
ATOM   8593  C  CB    B LEU B 2 117 ? 9.798   -15.427 -12.192 0.50 42.14 ? 117 LEU B CB    1 
ATOM   8594  C  CG    A LEU B 2 117 ? 11.600  -15.338 -12.206 0.50 45.08 ? 117 LEU B CG    1 
ATOM   8595  C  CG    B LEU B 2 117 ? 11.004  -14.624 -11.710 0.50 43.57 ? 117 LEU B CG    1 
ATOM   8596  C  CD1   A LEU B 2 117 ? 11.664  -13.973 -12.869 0.50 43.55 ? 117 LEU B CD1   1 
ATOM   8597  C  CD1   B LEU B 2 117 ? 10.914  -13.191 -12.209 0.50 46.59 ? 117 LEU B CD1   1 
ATOM   8598  C  CD2   A LEU B 2 117 ? 11.836  -15.215 -10.708 0.50 38.44 ? 117 LEU B CD2   1 
ATOM   8599  C  CD2   B LEU B 2 117 ? 11.099  -14.659 -10.194 0.50 42.80 ? 117 LEU B CD2   1 
ATOM   8600  N  N     A ASP B 2 118 ? 8.449   -18.400 -13.600 0.50 46.41 ? 118 ASP B N     1 
ATOM   8601  N  N     B ASP B 2 118 ? 8.190   -18.104 -13.319 0.50 46.07 ? 118 ASP B N     1 
ATOM   8602  C  CA    A ASP B 2 118 ? 7.168   -19.010 -13.947 0.50 46.64 ? 118 ASP B CA    1 
ATOM   8603  C  CA    B ASP B 2 118 ? 6.880   -18.657 -13.646 0.50 46.52 ? 118 ASP B CA    1 
ATOM   8604  C  C     A ASP B 2 118 ? 6.840   -20.160 -13.005 0.50 47.22 ? 118 ASP B C     1 
ATOM   8605  C  C     B ASP B 2 118 ? 6.499   -19.778 -12.688 0.50 47.01 ? 118 ASP B C     1 
ATOM   8606  O  O     A ASP B 2 118 ? 5.692   -20.314 -12.572 0.50 46.87 ? 118 ASP B O     1 
ATOM   8607  O  O     B ASP B 2 118 ? 5.361   -19.839 -12.208 0.50 47.34 ? 118 ASP B O     1 
ATOM   8608  C  CB    A ASP B 2 118 ? 7.190   -19.505 -15.394 0.50 46.13 ? 118 ASP B CB    1 
ATOM   8609  C  CB    B ASP B 2 118 ? 6.864   -19.154 -15.092 0.50 45.73 ? 118 ASP B CB    1 
ATOM   8610  C  CG    A ASP B 2 118 ? 7.394   -18.384 -16.396 0.50 51.21 ? 118 ASP B CG    1 
ATOM   8611  C  CG    B ASP B 2 118 ? 6.410   -18.086 -16.068 0.50 47.16 ? 118 ASP B CG    1 
ATOM   8612  O  OD1   A ASP B 2 118 ? 7.456   -17.210 -15.974 0.50 50.42 ? 118 ASP B OD1   1 
ATOM   8613  O  OD1   B ASP B 2 118 ? 5.358   -17.461 -15.816 0.50 51.48 ? 118 ASP B OD1   1 
ATOM   8614  O  OD2   A ASP B 2 118 ? 7.506   -18.682 -17.606 0.50 49.84 ? 118 ASP B OD2   1 
ATOM   8615  O  OD2   B ASP B 2 118 ? 7.107   -17.864 -17.081 0.50 54.39 ? 118 ASP B OD2   1 
ATOM   8616  N  N     A VAL B 2 119 ? 7.842   -20.975 -12.671 0.50 43.85 ? 119 VAL B N     1 
ATOM   8617  N  N     B VAL B 2 119 ? 7.441   -20.678 -12.395 0.50 45.84 ? 119 VAL B N     1 
ATOM   8618  C  CA    A VAL B 2 119 ? 7.627   -22.081 -11.747 0.50 46.71 ? 119 VAL B CA    1 
ATOM   8619  C  CA    B VAL B 2 119 ? 7.131   -21.781 -11.494 0.50 46.91 ? 119 VAL B CA    1 
ATOM   8620  C  C     A VAL B 2 119 ? 7.359   -21.561 -10.339 0.50 46.49 ? 119 VAL B C     1 
ATOM   8621  C  C     B VAL B 2 119 ? 7.075   -21.295 -10.049 0.50 46.83 ? 119 VAL B C     1 
ATOM   8622  O  O     A VAL B 2 119 ? 6.512   -22.100 -9.616  0.50 47.45 ? 119 VAL B O     1 
ATOM   8623  O  O     B VAL B 2 119 ? 6.403   -21.906 -9.208  0.50 45.93 ? 119 VAL B O     1 
ATOM   8624  C  CB    A VAL B 2 119 ? 8.829   -23.041 -11.783 0.50 44.16 ? 119 VAL B CB    1 
ATOM   8625  C  CB    B VAL B 2 119 ? 8.146   -22.927 -11.679 0.50 45.06 ? 119 VAL B CB    1 
ATOM   8626  C  CG1   A VAL B 2 119 ? 8.712   -24.083 -10.689 0.50 43.96 ? 119 VAL B CG1   1 
ATOM   8627  C  CG1   B VAL B 2 119 ? 9.489   -22.561 -11.081 0.50 45.50 ? 119 VAL B CG1   1 
ATOM   8628  C  CG2   A VAL B 2 119 ? 8.932   -23.708 -13.147 0.50 44.24 ? 119 VAL B CG2   1 
ATOM   8629  C  CG2   B VAL B 2 119 ? 7.613   -24.214 -11.071 0.50 47.46 ? 119 VAL B CG2   1 
ATOM   8630  N  N     A VAL B 2 120 ? 8.067   -20.504 -9.928  0.50 46.74 ? 120 VAL B N     1 
ATOM   8631  N  N     B VAL B 2 120 ? 7.765   -20.196 -9.733  0.50 46.92 ? 120 VAL B N     1 
ATOM   8632  C  CA    A VAL B 2 120 ? 7.858   -19.943 -8.595  0.50 45.01 ? 120 VAL B CA    1 
ATOM   8633  C  CA    B VAL B 2 120 ? 7.695   -19.644 -8.384  0.50 45.35 ? 120 VAL B CA    1 
ATOM   8634  C  C     A VAL B 2 120 ? 6.422   -19.456 -8.446  0.50 47.27 ? 120 VAL B C     1 
ATOM   8635  C  C     B VAL B 2 120 ? 6.296   -19.110 -8.105  0.50 48.38 ? 120 VAL B C     1 
ATOM   8636  O  O     A VAL B 2 120 ? 5.755   -19.733 -7.440  0.50 43.84 ? 120 VAL B O     1 
ATOM   8637  O  O     B VAL B 2 120 ? 5.696   -19.410 -7.065  0.50 45.30 ? 120 VAL B O     1 
ATOM   8638  C  CB    A VAL B 2 120 ? 8.864   -18.811 -8.316  0.50 47.54 ? 120 VAL B CB    1 
ATOM   8639  C  CB    B VAL B 2 120 ? 8.762   -18.552 -8.189  0.50 47.90 ? 120 VAL B CB    1 
ATOM   8640  C  CG1   A VAL B 2 120 ? 8.660   -18.263 -6.912  0.50 42.03 ? 120 VAL B CG1   1 
ATOM   8641  C  CG1   B VAL B 2 120 ? 8.646   -17.955 -6.799  0.50 42.08 ? 120 VAL B CG1   1 
ATOM   8642  C  CG2   A VAL B 2 120 ? 10.291  -19.296 -8.494  0.50 46.61 ? 120 VAL B CG2   1 
ATOM   8643  C  CG2   B VAL B 2 120 ? 10.154  -19.116 -8.412  0.50 46.37 ? 120 VAL B CG2   1 
ATOM   8644  N  N     A ARG B 2 121 ? 5.924   -18.725 -9.449  0.50 47.68 ? 121 ARG B N     1 
ATOM   8645  N  N     B ARG B 2 121 ? 5.753   -18.317 -9.035  0.50 50.45 ? 121 ARG B N     1 
ATOM   8646  C  CA    A ARG B 2 121 ? 4.547   -18.238 -9.406  0.50 49.73 ? 121 ARG B CA    1 
ATOM   8647  C  CA    B ARG B 2 121 ? 4.403   -17.785 -8.868  0.50 48.67 ? 121 ARG B CA    1 
ATOM   8648  C  C     A ARG B 2 121 ? 3.560   -19.390 -9.276  0.50 49.73 ? 121 ARG B C     1 
ATOM   8649  C  C     B ARG B 2 121 ? 3.383   -18.903 -8.707  0.50 51.06 ? 121 ARG B C     1 
ATOM   8650  O  O     A ARG B 2 121 ? 2.579   -19.296 -8.528  0.50 53.21 ? 121 ARG B O     1 
ATOM   8651  O  O     B ARG B 2 121 ? 2.486   -18.817 -7.859  0.50 51.68 ? 121 ARG B O     1 
ATOM   8652  C  CB    A ARG B 2 121 ? 4.242   -17.412 -10.657 0.50 50.36 ? 121 ARG B CB    1 
ATOM   8653  C  CB    B ARG B 2 121 ? 4.028   -16.904 -10.059 0.50 49.36 ? 121 ARG B CB    1 
ATOM   8654  C  CG    A ARG B 2 121 ? 5.086   -16.156 -10.798 0.50 47.85 ? 121 ARG B CG    1 
ATOM   8655  C  CG    B ARG B 2 121 ? 4.832   -15.623 -10.204 0.50 43.93 ? 121 ARG B CG    1 
ATOM   8656  C  CD    A ARG B 2 121 ? 4.965   -15.556 -12.194 0.50 49.30 ? 121 ARG B CD    1 
ATOM   8657  C  CD    B ARG B 2 121 ? 4.291   -14.806 -11.367 0.50 48.85 ? 121 ARG B CD    1 
ATOM   8658  N  NE    A ARG B 2 121 ? 6.007   -14.567 -12.444 0.50 48.75 ? 121 ARG B NE    1 
ATOM   8659  N  NE    B ARG B 2 121 ? 4.928   -13.501 -11.492 0.50 49.45 ? 121 ARG B NE    1 
ATOM   8660  C  CZ    A ARG B 2 121 ? 6.210   -13.963 -13.608 0.50 55.89 ? 121 ARG B CZ    1 
ATOM   8661  C  CZ    B ARG B 2 121 ? 5.922   -13.229 -12.327 0.50 55.05 ? 121 ARG B CZ    1 
ATOM   8662  N  NH1   A ARG B 2 121 ? 5.452   -14.217 -14.662 0.50 58.21 ? 121 ARG B NH1   1 
ATOM   8663  N  NH1   B ARG B 2 121 ? 6.433   -14.158 -13.119 0.50 56.27 ? 121 ARG B NH1   1 
ATOM   8664  N  NH2   A ARG B 2 121 ? 7.202   -13.083 -13.717 0.50 46.44 ? 121 ARG B NH2   1 
ATOM   8665  N  NH2   B ARG B 2 121 ? 6.412   -11.993 -12.373 0.50 49.33 ? 121 ARG B NH2   1 
ATOM   8666  N  N     A LYS B 2 122 ? 3.807   -20.488 -9.992  0.50 49.08 ? 122 LYS B N     1 
ATOM   8667  N  N     B LYS B 2 122 ? 3.500   -19.959 -9.515  0.50 49.21 ? 122 LYS B N     1 
ATOM   8668  C  CA    A LYS B 2 122 ? 2.940   -21.658 -9.890  0.50 48.72 ? 122 LYS B CA    1 
ATOM   8669  C  CA    B LYS B 2 122 ? 2.571   -21.079 -9.410  0.50 48.76 ? 122 LYS B CA    1 
ATOM   8670  C  C     A LYS B 2 122 ? 2.890   -22.181 -8.459  0.50 50.92 ? 122 LYS B C     1 
ATOM   8671  C  C     B LYS B 2 122 ? 2.636   -21.713 -8.026  0.50 51.55 ? 122 LYS B C     1 
ATOM   8672  O  O     A LYS B 2 122 ? 1.808   -22.440 -7.918  0.50 54.34 ? 122 LYS B O     1 
ATOM   8673  O  O     B LYS B 2 122 ? 1.603   -21.950 -7.389  0.50 51.37 ? 122 LYS B O     1 
ATOM   8674  C  CB    A LYS B 2 122 ? 3.426   -22.745 -10.848 0.50 50.30 ? 122 LYS B CB    1 
ATOM   8675  C  CB    B LYS B 2 122 ? 2.875   -22.113 -10.495 0.50 48.80 ? 122 LYS B CB    1 
ATOM   8676  C  CG    A LYS B 2 122 ? 2.816   -24.113 -10.607 0.50 51.23 ? 122 LYS B CG    1 
ATOM   8677  C  CG    B LYS B 2 122 ? 2.057   -23.393 -10.391 0.50 51.57 ? 122 LYS B CG    1 
ATOM   8678  C  CD    A LYS B 2 122 ? 3.396   -25.137 -11.566 0.50 57.98 ? 122 LYS B CD    1 
ATOM   8679  C  CD    B LYS B 2 122 ? 0.561   -23.111 -10.441 0.50 51.90 ? 122 LYS B CD    1 
ATOM   8680  C  CE    A LYS B 2 122 ? 4.913   -25.152 -11.499 0.50 53.23 ? 122 LYS B CE    1 
ATOM   8681  C  CE    B LYS B 2 122 ? 0.150   -22.501 -11.773 0.50 57.26 ? 122 LYS B CE    1 
ATOM   8682  N  NZ    A LYS B 2 122 ? 5.503   -26.101 -12.482 0.50 52.20 ? 122 LYS B NZ    1 
ATOM   8683  N  NZ    B LYS B 2 122 ? -1.306  -22.192 -11.808 0.50 52.76 ? 122 LYS B NZ    1 
ATOM   8684  N  N     A GLU B 2 123 ? 4.056   -22.338 -7.827  0.50 47.97 ? 123 GLU B N     1 
ATOM   8685  N  N     B GLU B 2 123 ? 3.850   -21.990 -7.542  0.50 47.69 ? 123 GLU B N     1 
ATOM   8686  C  CA    A GLU B 2 123 ? 4.087   -22.821 -6.451  0.50 46.04 ? 123 GLU B CA    1 
ATOM   8687  C  CA    B GLU B 2 123 ? 3.998   -22.575 -6.214  0.50 45.54 ? 123 GLU B CA    1 
ATOM   8688  C  C     A GLU B 2 123 ? 3.552   -21.783 -5.474  0.50 44.19 ? 123 GLU B C     1 
ATOM   8689  C  C     B GLU B 2 123 ? 3.531   -21.612 -5.131  0.50 45.06 ? 123 GLU B C     1 
ATOM   8690  O  O     A GLU B 2 123 ? 2.915   -22.144 -4.479  0.50 50.16 ? 123 GLU B O     1 
ATOM   8691  O  O     B GLU B 2 123 ? 2.969   -22.035 -4.114  0.50 50.79 ? 123 GLU B O     1 
ATOM   8692  C  CB    A GLU B 2 123 ? 5.510   -23.222 -6.064  0.50 43.58 ? 123 GLU B CB    1 
ATOM   8693  C  CB    B GLU B 2 123 ? 5.452   -22.982 -5.975  0.50 43.61 ? 123 GLU B CB    1 
ATOM   8694  C  CG    A GLU B 2 123 ? 5.978   -24.540 -6.656  0.50 44.41 ? 123 GLU B CG    1 
ATOM   8695  C  CG    B GLU B 2 123 ? 5.850   -24.299 -6.613  0.50 44.14 ? 123 GLU B CG    1 
ATOM   8696  C  CD    A GLU B 2 123 ? 5.426   -25.748 -5.922  0.50 46.58 ? 123 GLU B CD    1 
ATOM   8697  C  CD    B GLU B 2 123 ? 5.457   -25.500 -5.775  0.50 46.96 ? 123 GLU B CD    1 
ATOM   8698  O  OE1   A GLU B 2 123 ? 4.644   -25.568 -4.962  0.50 51.40 ? 123 GLU B OE1   1 
ATOM   8699  O  OE1   B GLU B 2 123 ? 4.743   -25.321 -4.764  0.50 50.87 ? 123 GLU B OE1   1 
ATOM   8700  O  OE2   A GLU B 2 123 ? 5.779   -26.883 -6.302  0.50 43.82 ? 123 GLU B OE2   1 
ATOM   8701  O  OE2   B GLU B 2 123 ? 5.866   -26.628 -6.124  0.50 43.12 ? 123 GLU B OE2   1 
ATOM   8702  N  N     A SER B 2 124 ? 3.796   -20.496 -5.737  0.50 47.66 ? 124 SER B N     1 
ATOM   8703  N  N     B SER B 2 124 ? 3.756   -20.311 -5.330  0.50 48.59 ? 124 SER B N     1 
ATOM   8704  C  CA    A SER B 2 124 ? 3.340   -19.459 -4.817  0.50 47.62 ? 124 SER B CA    1 
ATOM   8705  C  CA    B SER B 2 124 ? 3.368   -19.333 -4.319  0.50 45.90 ? 124 SER B CA    1 
ATOM   8706  C  C     A SER B 2 124 ? 1.828   -19.276 -4.871  0.50 50.54 ? 124 SER B C     1 
ATOM   8707  C  C     B SER B 2 124 ? 1.853   -19.158 -4.264  0.50 51.89 ? 124 SER B C     1 
ATOM   8708  O  O     A SER B 2 124 ? 1.223   -18.851 -3.880  0.50 49.18 ? 124 SER B O     1 
ATOM   8709  O  O     B SER B 2 124 ? 1.274   -19.062 -3.175  0.50 48.07 ? 124 SER B O     1 
ATOM   8710  C  CB    A SER B 2 124 ? 4.048   -18.139 -5.121  0.50 46.63 ? 124 SER B CB    1 
ATOM   8711  C  CB    B SER B 2 124 ? 4.057   -17.997 -4.592  0.50 45.40 ? 124 SER B CB    1 
ATOM   8712  O  OG    A SER B 2 124 ? 5.449   -18.258 -4.933  0.50 44.14 ? 124 SER B OG    1 
ATOM   8713  O  OG    B SER B 2 124 ? 5.462   -18.106 -4.423  0.50 42.52 ? 124 SER B OG    1 
ATOM   8714  N  N     A GLU B 2 125 ? 1.202   -19.580 -6.010  0.50 53.21 ? 125 GLU B N     1 
ATOM   8715  N  N     B GLU B 2 125 ? 1.194   -19.116 -5.424  0.50 51.97 ? 125 GLU B N     1 
ATOM   8716  C  CA    A GLU B 2 125 ? -0.251  -19.480 -6.092  0.50 50.68 ? 125 GLU B CA    1 
ATOM   8717  C  CA    B GLU B 2 125 ? -0.252  -18.922 -5.450  0.50 50.86 ? 125 GLU B CA    1 
ATOM   8718  C  C     A GLU B 2 125 ? -0.934  -20.580 -5.292  0.50 52.73 ? 125 GLU B C     1 
ATOM   8719  C  C     B GLU B 2 125 ? -1.012  -20.090 -4.839  0.50 51.74 ? 125 GLU B C     1 
ATOM   8720  O  O     A GLU B 2 125 ? -2.068  -20.400 -4.835  0.50 53.74 ? 125 GLU B O     1 
ATOM   8721  O  O     B GLU B 2 125 ? -2.180  -19.925 -4.471  0.50 54.11 ? 125 GLU B O     1 
ATOM   8722  C  CB    A GLU B 2 125 ? -0.705  -19.525 -7.550  0.50 52.29 ? 125 GLU B CB    1 
ATOM   8723  C  CB    B GLU B 2 125 ? -0.736  -18.692 -6.883  0.50 54.17 ? 125 GLU B CB    1 
ATOM   8724  C  CG    A GLU B 2 125 ? -0.446  -18.241 -8.322  0.50 56.34 ? 125 GLU B CG    1 
ATOM   8725  C  CG    B GLU B 2 125 ? -0.504  -17.284 -7.404  0.50 50.83 ? 125 GLU B CG    1 
ATOM   8726  C  CD    A GLU B 2 125 ? -0.934  -18.319 -9.754  0.50 51.89 ? 125 GLU B CD    1 
ATOM   8727  C  CD    B GLU B 2 125 ? -1.284  -17.004 -8.674  0.50 53.46 ? 125 GLU B CD    1 
ATOM   8728  O  OE1   A GLU B 2 125 ? -1.481  -19.375 -10.135 0.50 49.04 ? 125 GLU B OE1   1 
ATOM   8729  O  OE1   B GLU B 2 125 ? -2.094  -17.866 -9.075  0.50 57.10 ? 125 GLU B OE1   1 
ATOM   8730  O  OE2   A GLU B 2 125 ? -0.771  -17.326 -10.494 0.50 53.61 ? 125 GLU B OE2   1 
ATOM   8731  O  OE2   B GLU B 2 125 ? -1.087  -15.923 -9.271  0.50 63.43 ? 125 GLU B OE2   1 
ATOM   8732  N  N     A SER B 2 126 ? -0.266  -21.719 -5.113  0.50 49.85 ? 126 SER B N     1 
ATOM   8733  N  N     B SER B 2 126 ? -0.386  -21.258 -4.724  0.50 51.53 ? 126 SER B N     1 
ATOM   8734  C  CA    A SER B 2 126 ? -0.780  -22.819 -4.308  0.50 51.34 ? 126 SER B CA    1 
ATOM   8735  C  CA    B SER B 2 126 ? -1.026  -22.432 -4.149  0.50 51.25 ? 126 SER B CA    1 
ATOM   8736  C  C     A SER B 2 126 ? -0.524  -22.631 -2.816  0.50 49.41 ? 126 SER B C     1 
ATOM   8737  C  C     B SER B 2 126 ? -0.770  -22.574 -2.652  0.50 48.87 ? 126 SER B C     1 
ATOM   8738  O  O     A SER B 2 126 ? -0.628  -23.600 -2.054  0.50 54.17 ? 126 SER B O     1 
ATOM   8739  O  O     B SER B 2 126 ? -1.127  -23.604 -2.070  0.50 55.20 ? 126 SER B O     1 
ATOM   8740  C  CB    A SER B 2 126 ? -0.170  -24.142 -4.778  0.50 49.68 ? 126 SER B CB    1 
ATOM   8741  C  CB    B SER B 2 126 ? -0.562  -23.692 -4.883  0.50 49.77 ? 126 SER B CB    1 
ATOM   8742  O  OG    A SER B 2 126 ? -0.436  -25.185 -3.855  0.50 54.10 ? 126 SER B OG    1 
ATOM   8743  O  OG    B SER B 2 126 ? -0.900  -23.631 -6.257  0.50 52.91 ? 126 SER B OG    1 
ATOM   8744  N  N     A CYS B 2 127 ? -0.191  -21.416 -2.386  0.50 49.22 ? 127 CYS B N     1 
ATOM   8745  N  N     B CYS B 2 127 ? -0.160  -21.575 -2.022  0.50 48.68 ? 127 CYS B N     1 
ATOM   8746  C  CA    A CYS B 2 127 ? 0.139   -21.132 -0.995  0.50 46.11 ? 127 CYS B CA    1 
ATOM   8747  C  CA    B CYS B 2 127 ? 0.066   -21.569 -0.585  0.50 46.80 ? 127 CYS B CA    1 
ATOM   8748  C  C     A CYS B 2 127 ? -1.034  -20.425 -0.329  0.50 47.53 ? 127 CYS B C     1 
ATOM   8749  C  C     B CYS B 2 127 ? -0.995  -20.725 0.111   0.50 46.14 ? 127 CYS B C     1 
ATOM   8750  O  O     A CYS B 2 127 ? -1.457  -19.355 -0.778  0.50 49.18 ? 127 CYS B O     1 
ATOM   8751  O  O     B CYS B 2 127 ? -1.506  -19.751 -0.447  0.50 47.52 ? 127 CYS B O     1 
ATOM   8752  C  CB    A CYS B 2 127 ? 1.400   -20.276 -0.899  0.50 42.98 ? 127 CYS B CB    1 
ATOM   8753  C  CB    B CYS B 2 127 ? 1.460   -21.031 -0.250  0.50 43.63 ? 127 CYS B CB    1 
ATOM   8754  S  SG    A CYS B 2 127 ? 2.909   -21.107 -1.435  0.50 38.65 ? 127 CYS B SG    1 
ATOM   8755  S  SG    B CYS B 2 127 ? 2.829   -22.103 -0.758  0.50 31.85 ? 127 CYS B SG    1 
ATOM   8756  N  N     A ASP B 2 128 ? -1.551  -21.022 0.747   0.50 44.77 ? 128 ASP B N     1 
ATOM   8757  N  N     B ASP B 2 128 ? -1.320  -21.109 1.346   0.50 44.93 ? 128 ASP B N     1 
ATOM   8758  C  CA    A ASP B 2 128 ? -2.622  -20.377 1.498   0.50 44.50 ? 128 ASP B CA    1 
ATOM   8759  C  CA    B ASP B 2 128 ? -2.341  -20.387 2.100   0.50 45.15 ? 128 ASP B CA    1 
ATOM   8760  C  C     A ASP B 2 128 ? -2.101  -19.169 2.267   0.50 43.48 ? 128 ASP B C     1 
ATOM   8761  C  C     B ASP B 2 128 ? -1.875  -18.977 2.438   0.50 44.20 ? 128 ASP B C     1 
ATOM   8762  O  O     A ASP B 2 128 ? -2.747  -18.115 2.289   0.50 42.59 ? 128 ASP B O     1 
ATOM   8763  O  O     B ASP B 2 128 ? -2.532  -17.990 2.087   0.50 42.62 ? 128 ASP B O     1 
ATOM   8764  C  CB    A ASP B 2 128 ? -3.280  -21.382 2.442   0.50 46.29 ? 128 ASP B CB    1 
ATOM   8765  C  CB    B ASP B 2 128 ? -2.704  -21.161 3.370   0.50 45.76 ? 128 ASP B CB    1 
ATOM   8766  C  CG    A ASP B 2 128 ? -4.397  -20.765 3.260   0.50 51.09 ? 128 ASP B CG    1 
ATOM   8767  C  CG    B ASP B 2 128 ? -3.660  -20.396 4.260   0.50 46.15 ? 128 ASP B CG    1 
ATOM   8768  O  OD1   A ASP B 2 128 ? -5.343  -20.215 2.655   0.50 45.38 ? 128 ASP B OD1   1 
ATOM   8769  O  OD1   B ASP B 2 128 ? -4.678  -19.890 3.741   0.50 49.45 ? 128 ASP B OD1   1 
ATOM   8770  O  OD2   A ASP B 2 128 ? -4.331  -20.836 4.506   0.50 49.72 ? 128 ASP B OD2   1 
ATOM   8771  O  OD2   B ASP B 2 128 ? -3.399  -20.307 5.479   0.50 46.46 ? 128 ASP B OD2   1 
ATOM   8772  N  N     A CYS B 2 129 ? -0.927  -19.300 2.903   0.50 44.39 ? 129 CYS B N     1 
ATOM   8773  N  N     B CYS B 2 129 ? -0.738  -18.862 3.125   0.50 42.66 ? 129 CYS B N     1 
ATOM   8774  C  CA    A CYS B 2 129 ? -0.285  -18.169 3.579   0.50 37.11 ? 129 CYS B CA    1 
ATOM   8775  C  CA    B CYS B 2 129 ? -0.149  -17.556 3.421   0.50 37.03 ? 129 CYS B CA    1 
ATOM   8776  C  C     A CYS B 2 129 ? 1.231   -18.388 3.500   0.50 37.68 ? 129 CYS B C     1 
ATOM   8777  C  C     B CYS B 2 129 ? 1.368   -17.732 3.425   0.50 33.69 ? 129 CYS B C     1 
ATOM   8778  O  O     A CYS B 2 129 ? 1.871   -18.880 4.433   0.50 33.89 ? 129 CYS B O     1 
ATOM   8779  O  O     B CYS B 2 129 ? 1.945   -18.146 4.434   0.50 30.69 ? 129 CYS B O     1 
ATOM   8780  C  CB    A CYS B 2 129 ? -0.757  -18.010 5.023   0.50 38.11 ? 129 CYS B CB    1 
ATOM   8781  C  CB    B CYS B 2 129 ? -0.662  -17.006 4.744   0.50 38.49 ? 129 CYS B CB    1 
ATOM   8782  S  SG    A CYS B 2 129 ? -0.353  -16.401 5.743   0.50 40.56 ? 129 CYS B SG    1 
ATOM   8783  S  SG    B CYS B 2 129 ? -0.448  -15.222 4.923   0.50 40.48 ? 129 CYS B SG    1 
ATOM   8784  N  N     A LEU B 2 130 ? 1.799   -18.011 2.356   0.50 37.50 ? 130 LEU B N     1 
ATOM   8785  N  N     B LEU B 2 130 ? 1.996   -17.425 2.293   0.50 41.14 ? 130 LEU B N     1 
ATOM   8786  C  CA    A LEU B 2 130 ? 3.228   -18.164 2.110   0.50 37.63 ? 130 LEU B CA    1 
ATOM   8787  C  CA    B LEU B 2 130 ? 3.430   -17.638 2.134   0.50 36.30 ? 130 LEU B CA    1 
ATOM   8788  C  C     A LEU B 2 130 ? 4.048   -17.308 3.072   0.50 33.80 ? 130 LEU B C     1 
ATOM   8789  C  C     B LEU B 2 130 ? 4.229   -16.741 3.074   0.50 35.83 ? 130 LEU B C     1 
ATOM   8790  O  O     A LEU B 2 130 ? 3.748   -16.128 3.280   0.50 38.74 ? 130 LEU B O     1 
ATOM   8791  O  O     B LEU B 2 130 ? 4.012   -15.527 3.127   0.50 37.85 ? 130 LEU B O     1 
ATOM   8792  C  CB    A LEU B 2 130 ? 3.529   -17.775 0.661   0.50 35.04 ? 130 LEU B CB    1 
ATOM   8793  C  CB    B LEU B 2 130 ? 3.829   -17.372 0.680   0.50 36.14 ? 130 LEU B CB    1 
ATOM   8794  C  CG    A LEU B 2 130 ? 4.973   -17.664 0.168   0.50 37.71 ? 130 LEU B CG    1 
ATOM   8795  C  CG    B LEU B 2 130 ? 5.314   -17.345 0.319   0.50 36.21 ? 130 LEU B CG    1 
ATOM   8796  C  CD1   A LEU B 2 130 ? 5.599   -19.034 0.045   0.50 38.27 ? 130 LEU B CD1   1 
ATOM   8797  C  CD1   B LEU B 2 130 ? 5.927   -18.728 0.442   0.50 38.75 ? 130 LEU B CD1   1 
ATOM   8798  C  CD2   A LEU B 2 130 ? 5.014   -16.926 -1.162  0.50 38.03 ? 130 LEU B CD2   1 
ATOM   8799  C  CD2   B LEU B 2 130 ? 5.490   -16.799 -1.086  0.50 37.58 ? 130 LEU B CD2   1 
ATOM   8800  N  N     A GLN B 2 131 ? 5.086   -17.906 3.663   0.50 33.26 ? 131 GLN B N     1 
ATOM   8801  N  N     B GLN B 2 131 ? 5.177   -17.341 3.803   0.50 32.64 ? 131 GLN B N     1 
ATOM   8802  C  CA    A GLN B 2 131 ? 6.015   -17.145 4.496   0.50 33.75 ? 131 GLN B CA    1 
ATOM   8803  C  CA    B GLN B 2 131 ? 5.995   -16.605 4.760   0.50 32.64 ? 131 GLN B CA    1 
ATOM   8804  C  C     A GLN B 2 131 ? 7.030   -16.394 3.643   0.50 31.90 ? 131 GLN B C     1 
ATOM   8805  C  C     B GLN B 2 131 ? 7.393   -16.268 4.251   0.50 29.89 ? 131 GLN B C     1 
ATOM   8806  O  O     A GLN B 2 131 ? 7.172   -15.170 3.743   0.50 26.98 ? 131 GLN B O     1 
ATOM   8807  O  O     B GLN B 2 131 ? 8.020   -15.346 4.786   0.50 23.15 ? 131 GLN B O     1 
ATOM   8808  C  CB    A GLN B 2 131 ? 6.766   -18.068 5.457   0.50 32.62 ? 131 GLN B CB    1 
ATOM   8809  C  CB    B GLN B 2 131 ? 6.130   -17.389 6.071   0.50 28.61 ? 131 GLN B CB    1 
ATOM   8810  C  CG    A GLN B 2 131 ? 5.936   -18.838 6.439   0.50 41.69 ? 131 GLN B CG    1 
ATOM   8811  C  CG    B GLN B 2 131 ? 6.938   -18.665 5.966   0.50 33.90 ? 131 GLN B CG    1 
ATOM   8812  C  CD    A GLN B 2 131 ? 6.795   -19.473 7.518   0.50 39.17 ? 131 GLN B CD    1 
ATOM   8813  C  CD    B GLN B 2 131 ? 7.413   -19.156 7.317   0.50 37.90 ? 131 GLN B CD    1 
ATOM   8814  O  OE1   A GLN B 2 131 ? 7.890   -18.991 7.816   0.50 38.98 ? 131 GLN B OE1   1 
ATOM   8815  O  OE1   B GLN B 2 131 ? 7.931   -18.381 8.120   0.50 34.76 ? 131 GLN B OE1   1 
ATOM   8816  N  NE2   A GLN B 2 131 ? 6.306   -20.558 8.105   0.50 34.15 ? 131 GLN B NE2   1 
ATOM   8817  N  NE2   B GLN B 2 131 ? 7.230   -20.448 7.580   0.50 34.32 ? 131 GLN B NE2   1 
ATOM   8818  N  N     A GLY B 2 132 ? 7.771   -17.124 2.820   0.50 31.69 ? 132 GLY B N     1 
ATOM   8819  N  N     B GLY B 2 132 ? 7.903   -16.979 3.257   0.50 32.00 ? 132 GLY B N     1 
ATOM   8820  C  CA    A GLY B 2 132 ? 8.832   -16.522 2.044   0.50 26.85 ? 132 GLY B CA    1 
ATOM   8821  C  CA    B GLY B 2 132 ? 9.205   -16.641 2.721   0.50 25.47 ? 132 GLY B CA    1 
ATOM   8822  C  C     A GLY B 2 132 ? 9.585   -17.538 1.215   0.50 30.66 ? 132 GLY B C     1 
ATOM   8823  C  C     B GLY B 2 132 ? 9.812   -17.788 1.937   0.50 30.78 ? 132 GLY B C     1 
ATOM   8824  O  O     A GLY B 2 132 ? 9.000   -18.523 0.754   0.50 31.56 ? 132 GLY B O     1 
ATOM   8825  O  O     B GLY B 2 132 ? 9.171   -18.808 1.680   0.50 28.33 ? 132 GLY B O     1 
ATOM   8826  N  N     A PHE B 2 133 ? 10.886  -17.323 1.034   0.50 27.62 ? 133 PHE B N     1 
ATOM   8827  N  N     B PHE B 2 133 ? 11.074  -17.584 1.563   0.50 27.96 ? 133 PHE B N     1 
ATOM   8828  C  CA    A PHE B 2 133 ? 11.667  -18.120 0.102   0.50 26.74 ? 133 PHE B CA    1 
ATOM   8829  C  CA    B PHE B 2 133 ? 11.817  -18.509 0.725   0.50 27.84 ? 133 PHE B CA    1 
ATOM   8830  C  C     A PHE B 2 133 ? 12.974  -18.560 0.741   0.50 30.45 ? 133 PHE B C     1 
ATOM   8831  C  C     B PHE B 2 133 ? 13.132  -18.869 1.406   0.50 29.31 ? 133 PHE B C     1 
ATOM   8832  O  O     A PHE B 2 133 ? 13.574  -17.835 1.540   0.50 29.47 ? 133 PHE B O     1 
ATOM   8833  O  O     B PHE B 2 133 ? 13.595  -18.177 2.315   0.50 25.75 ? 133 PHE B O     1 
ATOM   8834  C  CB    A PHE B 2 133 ? 11.938  -17.338 -1.187  0.50 31.75 ? 133 PHE B CB    1 
ATOM   8835  C  CB    B PHE B 2 133 ? 12.105  -17.906 -0.661  0.50 31.12 ? 133 PHE B CB    1 
ATOM   8836  C  CG    A PHE B 2 133 ? 10.689  -16.896 -1.889  0.50 27.87 ? 133 PHE B CG    1 
ATOM   8837  C  CG    B PHE B 2 133 ? 10.897  -17.309 -1.337  0.50 28.59 ? 133 PHE B CG    1 
ATOM   8838  C  CD1   A PHE B 2 133 ? 10.072  -15.701 -1.549  0.50 32.37 ? 133 PHE B CD1   1 
ATOM   8839  C  CD1   B PHE B 2 133 ? 10.506  -16.005 -1.068  0.50 31.05 ? 133 PHE B CD1   1 
ATOM   8840  C  CD2   A PHE B 2 133 ? 10.119  -17.684 -2.874  0.50 32.18 ? 133 PHE B CD2   1 
ATOM   8841  C  CD2   B PHE B 2 133 ? 10.167  -18.045 -2.254  0.50 31.66 ? 133 PHE B CD2   1 
ATOM   8842  C  CE1   A PHE B 2 133 ? 8.914   -15.297 -2.184  0.50 31.18 ? 133 PHE B CE1   1 
ATOM   8843  C  CE1   B PHE B 2 133 ? 9.398   -15.453 -1.688  0.50 31.89 ? 133 PHE B CE1   1 
ATOM   8844  C  CE2   A PHE B 2 133 ? 8.961   -17.286 -3.515  0.50 32.99 ? 133 PHE B CE2   1 
ATOM   8845  C  CE2   B PHE B 2 133 ? 9.061   -17.499 -2.882  0.50 33.97 ? 133 PHE B CE2   1 
ATOM   8846  C  CZ    A PHE B 2 133 ? 8.358   -16.091 -3.169  0.50 32.31 ? 133 PHE B CZ    1 
ATOM   8847  C  CZ    B PHE B 2 133 ? 8.676   -16.202 -2.598  0.50 31.69 ? 133 PHE B CZ    1 
ATOM   8848  N  N     A GLN B 2 134 ? 13.398  -19.768 0.374   0.50 27.55 ? 134 GLN B N     1 
ATOM   8849  N  N     B GLN B 2 134 ? 13.732  -19.968 0.952   0.50 26.08 ? 134 GLN B N     1 
ATOM   8850  C  CA    A GLN B 2 134 ? 14.606  -20.399 0.883   0.50 31.45 ? 134 GLN B CA    1 
ATOM   8851  C  CA    B GLN B 2 134 ? 15.097  -20.329 1.328   0.50 31.72 ? 134 GLN B CA    1 
ATOM   8852  C  C     A GLN B 2 134 ? 15.481  -20.807 -0.294  0.50 25.67 ? 134 GLN B C     1 
ATOM   8853  C  C     B GLN B 2 134 ? 15.820  -20.789 0.068   0.50 25.21 ? 134 GLN B C     1 
ATOM   8854  O  O     A GLN B 2 134 ? 14.966  -21.200 -1.344  0.50 26.48 ? 134 GLN B O     1 
ATOM   8855  O  O     B GLN B 2 134 ? 15.453  -21.809 -0.526  0.50 28.82 ? 134 GLN B O     1 
ATOM   8856  C  CB    A GLN B 2 134 ? 14.259  -21.620 1.744   0.50 31.82 ? 134 GLN B CB    1 
ATOM   8857  C  CB    B GLN B 2 134 ? 15.128  -21.404 2.422   0.50 28.53 ? 134 GLN B CB    1 
ATOM   8858  C  CG    A GLN B 2 134 ? 15.433  -22.276 2.448   0.50 32.59 ? 134 GLN B CG    1 
ATOM   8859  C  CG    B GLN B 2 134 ? 14.316  -22.664 2.139   0.50 34.48 ? 134 GLN B CG    1 
ATOM   8860  C  CD    A GLN B 2 134 ? 14.997  -23.423 3.347   0.50 34.68 ? 134 GLN B CD    1 
ATOM   8861  C  CD    B GLN B 2 134 ? 14.486  -23.722 3.215   0.50 34.17 ? 134 GLN B CD    1 
ATOM   8862  O  OE1   A GLN B 2 134 ? 14.360  -23.210 4.378   0.50 35.62 ? 134 GLN B OE1   1 
ATOM   8863  O  OE1   B GLN B 2 134 ? 14.524  -23.414 4.407   0.50 35.38 ? 134 GLN B OE1   1 
ATOM   8864  N  NE2   A GLN B 2 134 ? 15.332  -24.647 2.953   0.50 35.35 ? 134 GLN B NE2   1 
ATOM   8865  N  NE2   B GLN B 2 134 ? 14.598  -24.978 2.797   0.50 34.53 ? 134 GLN B NE2   1 
ATOM   8866  N  N     A LEU B 2 135 ? 16.802  -20.708 -0.128  0.50 22.40 ? 135 LEU B N     1 
ATOM   8867  N  N     B LEU B 2 135 ? 16.831  -20.030 -0.350  0.50 24.03 ? 135 LEU B N     1 
ATOM   8868  C  CA    A LEU B 2 135 ? 17.724  -21.085 -1.194  0.50 20.65 ? 135 LEU B CA    1 
ATOM   8869  C  CA    B LEU B 2 135 ? 17.601  -20.333 -1.550  0.50 22.29 ? 135 LEU B CA    1 
ATOM   8870  C  C     A LEU B 2 135 ? 18.989  -21.713 -0.626  0.50 21.66 ? 135 LEU B C     1 
ATOM   8871  C  C     B LEU B 2 135 ? 18.959  -20.897 -1.163  0.50 23.77 ? 135 LEU B C     1 
ATOM   8872  O  O     A LEU B 2 135 ? 19.558  -21.218 0.349   0.50 23.72 ? 135 LEU B O     1 
ATOM   8873  O  O     B LEU B 2 135 ? 19.700  -20.274 -0.395  0.50 24.28 ? 135 LEU B O     1 
ATOM   8874  C  CB    A LEU B 2 135 ? 18.122  -19.888 -2.067  0.50 25.23 ? 135 LEU B CB    1 
ATOM   8875  C  CB    B LEU B 2 135 ? 17.793  -19.093 -2.428  0.50 25.71 ? 135 LEU B CB    1 
ATOM   8876  C  CG    A LEU B 2 135 ? 19.117  -20.261 -3.181  0.50 22.35 ? 135 LEU B CG    1 
ATOM   8877  C  CG    B LEU B 2 135 ? 18.921  -19.225 -3.467  0.50 24.97 ? 135 LEU B CG    1 
ATOM   8878  C  CD1   A LEU B 2 135 ? 18.404  -20.937 -4.348  0.50 32.31 ? 135 LEU B CD1   1 
ATOM   8879  C  CD1   B LEU B 2 135 ? 18.517  -20.121 -4.628  0.50 34.16 ? 135 LEU B CD1   1 
ATOM   8880  C  CD2   A LEU B 2 135 ? 19.934  -19.063 -3.649  0.50 21.98 ? 135 LEU B CD2   1 
ATOM   8881  C  CD2   B LEU B 2 135 ? 19.403  -17.869 -3.969  0.50 29.85 ? 135 LEU B CD2   1 
ATOM   8882  N  N     A THR B 2 136 ? 19.430  -22.794 -1.261  0.50 23.91 ? 136 THR B N     1 
ATOM   8883  N  N     B THR B 2 136 ? 19.290  -22.060 -1.713  0.50 30.27 ? 136 THR B N     1 
ATOM   8884  C  CA    A THR B 2 136 ? 20.711  -23.426 -0.984  0.50 22.30 ? 136 THR B CA    1 
ATOM   8885  C  CA    B THR B 2 136 ? 20.585  -22.686 -1.497  0.50 24.35 ? 136 THR B CA    1 
ATOM   8886  C  C     A THR B 2 136 ? 21.582  -23.305 -2.228  0.50 24.81 ? 136 THR B C     1 
ATOM   8887  C  C     B THR B 2 136 ? 21.480  -22.461 -2.711  0.50 25.83 ? 136 THR B C     1 
ATOM   8888  O  O     A THR B 2 136 ? 21.124  -23.617 -3.331  0.50 29.21 ? 136 THR B O     1 
ATOM   8889  O  O     B THR B 2 136 ? 21.040  -22.594 -3.857  0.50 20.44 ? 136 THR B O     1 
ATOM   8890  C  CB    A THR B 2 136 ? 20.510  -24.894 -0.610  0.50 23.31 ? 136 THR B CB    1 
ATOM   8891  C  CB    B THR B 2 136 ? 20.426  -24.183 -1.228  0.50 26.67 ? 136 THR B CB    1 
ATOM   8892  O  OG1   A THR B 2 136 ? 20.123  -25.638 -1.776  0.50 26.77 ? 136 THR B OG1   1 
ATOM   8893  O  OG1   B THR B 2 136 ? 19.792  -24.808 -2.353  0.50 27.62 ? 136 THR B OG1   1 
ATOM   8894  C  CG2   A THR B 2 136 ? 19.405  -25.010 0.419   0.50 26.91 ? 136 THR B CG2   1 
ATOM   8895  C  CG2   B THR B 2 136 ? 19.584  -24.411 0.013   0.50 26.55 ? 136 THR B CG2   1 
ATOM   8896  N  N     A HIS B 2 137 ? 22.823  -22.847 -2.057  0.50 22.17 ? 137 HIS B N     1 
ATOM   8897  N  N     B HIS B 2 137 ? 22.734  -22.100 -2.452  0.50 22.11 ? 137 HIS B N     1 
ATOM   8898  C  CA    A HIS B 2 137 ? 23.696  -22.586 -3.198  0.50 27.40 ? 137 HIS B CA    1 
ATOM   8899  C  CA    B HIS B 2 137 ? 23.698  -21.847 -3.513  0.50 27.06 ? 137 HIS B CA    1 
ATOM   8900  C  C     A HIS B 2 137 ? 25.137  -22.428 -2.722  0.50 27.24 ? 137 HIS B C     1 
ATOM   8901  C  C     B HIS B 2 137 ? 25.078  -21.665 -2.904  0.50 27.16 ? 137 HIS B C     1 
ATOM   8902  O  O     A HIS B 2 137 ? 25.434  -22.473 -1.525  0.50 19.52 ? 137 HIS B O     1 
ATOM   8903  O  O     B HIS B 2 137 ? 25.210  -21.306 -1.731  0.50 24.21 ? 137 HIS B O     1 
ATOM   8904  C  CB    A HIS B 2 137 ? 23.242  -21.341 -3.968  0.50 26.72 ? 137 HIS B CB    1 
ATOM   8905  C  CB    B HIS B 2 137 ? 23.329  -20.605 -4.344  0.50 26.19 ? 137 HIS B CB    1 
ATOM   8906  C  CG    A HIS B 2 137 ? 23.360  -20.066 -3.190  0.50 26.06 ? 137 HIS B CG    1 
ATOM   8907  C  CG    B HIS B 2 137 ? 23.303  -19.327 -3.560  0.50 24.65 ? 137 HIS B CG    1 
ATOM   8908  N  ND1   A HIS B 2 137 ? 23.645  -18.856 -3.785  0.50 24.55 ? 137 HIS B ND1   1 
ATOM   8909  N  ND1   B HIS B 2 137 ? 23.388  -18.089 -4.160  0.50 23.54 ? 137 HIS B ND1   1 
ATOM   8910  C  CD2   A HIS B 2 137 ? 23.215  -19.809 -1.867  0.50 25.14 ? 137 HIS B CD2   1 
ATOM   8911  C  CD2   B HIS B 2 137 ? 23.181  -19.092 -2.232  0.50 25.79 ? 137 HIS B CD2   1 
ATOM   8912  C  CE1   A HIS B 2 137 ? 23.679  -17.911 -2.862  0.50 26.55 ? 137 HIS B CE1   1 
ATOM   8913  C  CE1   B HIS B 2 137 ? 23.332  -17.148 -3.235  0.50 24.19 ? 137 HIS B CE1   1 
ATOM   8914  N  NE2   A HIS B 2 137 ? 23.421  -18.463 -1.690  0.50 26.29 ? 137 HIS B NE2   1 
ATOM   8915  N  NE2   B HIS B 2 137 ? 23.205  -17.730 -2.056  0.50 27.32 ? 137 HIS B NE2   1 
ATOM   8916  N  N     A SER B 2 138 ? 26.038  -22.247 -3.687  0.50 26.13 ? 138 SER B N     1 
ATOM   8917  N  N     B SER B 2 138 ? 26.100  -21.938 -3.709  0.50 26.59 ? 138 SER B N     1 
ATOM   8918  C  CA    A SER B 2 138 ? 27.420  -21.876 -3.432  0.50 26.58 ? 138 SER B CA    1 
ATOM   8919  C  CA    B SER B 2 138 ? 27.445  -21.489 -3.399  0.50 25.97 ? 138 SER B CA    1 
ATOM   8920  C  C     A SER B 2 138 ? 27.657  -20.438 -3.866  0.50 23.04 ? 138 SER B C     1 
ATOM   8921  C  C     B SER B 2 138 ? 27.654  -20.101 -3.990  0.50 23.51 ? 138 SER B C     1 
ATOM   8922  O  O     A SER B 2 138 ? 26.916  -19.879 -4.680  0.50 28.20 ? 138 SER B O     1 
ATOM   8923  O  O     B SER B 2 138 ? 26.972  -19.694 -4.934  0.50 28.68 ? 138 SER B O     1 
ATOM   8924  C  CB    A SER B 2 138 ? 28.395  -22.794 -4.173  0.50 30.37 ? 138 SER B CB    1 
ATOM   8925  C  CB    B SER B 2 138 ? 28.492  -22.461 -3.948  0.50 30.11 ? 138 SER B CB    1 
ATOM   8926  O  OG    A SER B 2 138 ? 28.184  -22.736 -5.575  0.50 28.72 ? 138 SER B OG    1 
ATOM   8927  O  OG    B SER B 2 138 ? 28.400  -22.552 -5.358  0.50 28.85 ? 138 SER B OG    1 
ATOM   8928  N  N     A LEU B 2 139 ? 28.714  -19.844 -3.314  0.50 26.19 ? 139 LEU B N     1 
ATOM   8929  N  N     B LEU B 2 139 ? 28.589  -19.359 -3.404  0.50 24.35 ? 139 LEU B N     1 
ATOM   8930  C  CA    A LEU B 2 139 ? 29.110  -18.494 -3.682  0.50 24.34 ? 139 LEU B CA    1 
ATOM   8931  C  CA    B LEU B 2 139 ? 28.957  -18.054 -3.930  0.50 23.78 ? 139 LEU B CA    1 
ATOM   8932  C  C     A LEU B 2 139 ? 30.309  -18.457 -4.623  0.50 26.18 ? 139 LEU B C     1 
ATOM   8933  C  C     B LEU B 2 139 ? 30.207  -18.105 -4.801  0.50 26.36 ? 139 LEU B C     1 
ATOM   8934  O  O     A LEU B 2 139 ? 30.491  -17.459 -5.328  0.50 25.61 ? 139 LEU B O     1 
ATOM   8935  O  O     B LEU B 2 139 ? 30.581  -17.084 -5.385  0.50 26.21 ? 139 LEU B O     1 
ATOM   8936  C  CB    A LEU B 2 139 ? 29.435  -17.676 -2.428  0.50 23.36 ? 139 LEU B CB    1 
ATOM   8937  C  CB    B LEU B 2 139 ? 29.168  -17.058 -2.785  0.50 22.84 ? 139 LEU B CB    1 
ATOM   8938  C  CG    A LEU B 2 139 ? 28.353  -17.655 -1.342  0.50 22.02 ? 139 LEU B CG    1 
ATOM   8939  C  CG    B LEU B 2 139 ? 28.010  -16.820 -1.806  0.50 22.86 ? 139 LEU B CG    1 
ATOM   8940  C  CD1   A LEU B 2 139 ? 28.676  -16.608 -0.295  0.50 23.57 ? 139 LEU B CD1   1 
ATOM   8941  C  CD1   B LEU B 2 139 ? 28.361  -15.678 -0.870  0.50 26.91 ? 139 LEU B CD1   1 
ATOM   8942  C  CD2   A LEU B 2 139 ? 26.987  -17.408 -1.943  0.50 23.24 ? 139 LEU B CD2   1 
ATOM   8943  C  CD2   B LEU B 2 139 ? 26.713  -16.531 -2.546  0.50 22.20 ? 139 LEU B CD2   1 
ATOM   8944  N  N     A GLY B 2 140 ? 31.121  -19.508 -4.654  0.50 28.76 ? 140 GLY B N     1 
ATOM   8945  N  N     B GLY B 2 140 ? 30.855  -19.262 -4.907  0.50 27.06 ? 140 GLY B N     1 
ATOM   8946  C  CA    A GLY B 2 140 ? 32.330  -19.510 -5.451  0.50 29.85 ? 140 GLY B CA    1 
ATOM   8947  C  CA    B GLY B 2 140 ? 32.113  -19.360 -5.628  0.50 30.44 ? 140 GLY B CA    1 
ATOM   8948  C  C     A GLY B 2 140 ? 32.186  -19.979 -6.878  0.50 32.04 ? 140 GLY B C     1 
ATOM   8949  C  C     B GLY B 2 140 ? 31.963  -19.593 -7.117  0.50 33.28 ? 140 GLY B C     1 
ATOM   8950  O  O     A GLY B 2 140 ? 33.184  -20.026 -7.605  0.50 30.08 ? 140 GLY B O     1 
ATOM   8951  O  O     B GLY B 2 140 ? 32.801  -19.151 -7.910  0.50 31.72 ? 140 GLY B O     1 
ATOM   8952  N  N     A GLY B 2 141 ? 30.978  -20.318 -7.315  0.50 31.66 ? 141 GLY B N     1 
ATOM   8953  N  N     B GLY B 2 141 ? 30.902  -20.289 -7.510  0.50 32.01 ? 141 GLY B N     1 
ATOM   8954  C  CA    A GLY B 2 141 ? 30.781  -20.808 -8.665  0.50 30.60 ? 141 GLY B CA    1 
ATOM   8955  C  CA    B GLY B 2 141 ? 30.643  -20.570 -8.906  0.50 29.72 ? 141 GLY B CA    1 
ATOM   8956  C  C     A GLY B 2 141 ? 30.146  -19.799 -9.598  0.50 31.86 ? 141 GLY B C     1 
ATOM   8957  C  C     B GLY B 2 141 ? 30.038  -19.385 -9.630  0.50 32.50 ? 141 GLY B C     1 
ATOM   8958  O  O     A GLY B 2 141 ? 30.302  -18.587 -9.419  0.50 33.47 ? 141 GLY B O     1 
ATOM   8959  O  O     B GLY B 2 141 ? 30.081  -18.244 -9.164  0.50 33.55 ? 141 GLY B O     1 
ATOM   8960  N  N     A GLY B 2 142 ? 29.422  -20.292 -10.600 0.50 33.69 ? 142 GLY B N     1 
ATOM   8961  N  N     B GLY B 2 142 ? 29.454  -19.670 -10.791 0.50 32.25 ? 142 GLY B N     1 
ATOM   8962  C  CA    A GLY B 2 142 ? 28.763  -19.423 -11.552 0.50 32.04 ? 142 GLY B CA    1 
ATOM   8963  C  CA    B GLY B 2 142 ? 28.871  -18.630 -11.616 0.50 29.45 ? 142 GLY B CA    1 
ATOM   8964  C  C     A GLY B 2 142 ? 27.250  -19.461 -11.471 0.50 29.27 ? 142 GLY B C     1 
ATOM   8965  C  C     B GLY B 2 142 ? 27.356  -18.611 -11.635 0.50 30.21 ? 142 GLY B C     1 
ATOM   8966  O  O     A GLY B 2 142 ? 26.598  -18.415 -11.529 0.50 26.92 ? 142 GLY B O     1 
ATOM   8967  O  O     B GLY B 2 142 ? 26.753  -17.539 -11.728 0.50 26.37 ? 142 GLY B O     1 
ATOM   8968  N  N     A THR B 2 143 ? 26.678  -20.658 -11.333 0.50 28.77 ? 143 THR B N     1 
ATOM   8969  N  N     B THR B 2 143 ? 26.726  -19.785 -11.549 0.50 28.77 ? 143 THR B N     1 
ATOM   8970  C  CA    A THR B 2 143 ? 25.223  -20.792 -11.377 0.50 31.47 ? 143 THR B CA    1 
ATOM   8971  C  CA    B THR B 2 143 ? 25.268  -19.854 -11.616 0.50 28.78 ? 143 THR B CA    1 
ATOM   8972  C  C     A THR B 2 143 ? 24.586  -20.477 -10.028 0.50 22.85 ? 143 THR B C     1 
ATOM   8973  C  C     B THR B 2 143 ? 24.633  -19.477 -10.283 0.50 26.10 ? 143 THR B C     1 
ATOM   8974  O  O     A THR B 2 143 ? 23.760  -19.564 -9.920  0.50 25.61 ? 143 THR B O     1 
ATOM   8975  O  O     B THR B 2 143 ? 23.913  -18.477 -10.188 0.50 27.13 ? 143 THR B O     1 
ATOM   8976  C  CB    A THR B 2 143 ? 24.835  -22.200 -11.834 0.50 31.60 ? 143 THR B CB    1 
ATOM   8977  C  CB    B THR B 2 143 ? 24.816  -21.256 -12.039 0.50 31.74 ? 143 THR B CB    1 
ATOM   8978  O  OG1   A THR B 2 143 ? 25.493  -22.499 -13.071 0.50 33.42 ? 143 THR B OG1   1 
ATOM   8979  O  OG1   B THR B 2 143 ? 25.382  -21.582 -13.313 0.50 29.04 ? 143 THR B OG1   1 
ATOM   8980  C  CG2   A THR B 2 143 ? 23.334  -22.288 -12.038 0.50 34.33 ? 143 THR B CG2   1 
ATOM   8981  C  CG2   B THR B 2 143 ? 23.306  -21.314 -12.141 0.50 33.64 ? 143 THR B CG2   1 
ATOM   8982  N  N     A GLY B 2 144 ? 24.935  -21.245 -8.992  0.50 30.01 ? 144 GLY B N     1 
ATOM   8983  N  N     B GLY B 2 144 ? 24.887  -20.274 -9.243  0.50 25.80 ? 144 GLY B N     1 
ATOM   8984  C  CA    A GLY B 2 144 ? 24.398  -20.968 -7.670  0.50 23.56 ? 144 GLY B CA    1 
ATOM   8985  C  CA    B GLY B 2 144 ? 24.280  -20.000 -7.948  0.50 28.45 ? 144 GLY B CA    1 
ATOM   8986  C  C     A GLY B 2 144 ? 24.717  -19.564 -7.199  0.50 27.52 ? 144 GLY B C     1 
ATOM   8987  C  C     B GLY B 2 144 ? 24.621  -18.620 -7.422  0.50 26.99 ? 144 GLY B C     1 
ATOM   8988  O  O     A GLY B 2 144 ? 23.903  -18.931 -6.522  0.50 24.29 ? 144 GLY B O     1 
ATOM   8989  O  O     B GLY B 2 144 ? 23.773  -17.940 -6.837  0.50 26.90 ? 144 GLY B O     1 
ATOM   8990  N  N     A SER B 2 145 ? 25.888  -19.051 -7.574  0.50 27.25 ? 145 SER B N     1 
ATOM   8991  N  N     B SER B 2 145 ? 25.864  -18.182 -7.636  0.50 28.19 ? 145 SER B N     1 
ATOM   8992  C  CA    A SER B 2 145 ? 26.271  -17.685 -7.220  0.50 29.46 ? 145 SER B CA    1 
ATOM   8993  C  CA    B SER B 2 145 ? 26.280  -16.853 -7.199  0.50 28.01 ? 145 SER B CA    1 
ATOM   8994  C  C     A SER B 2 145 ? 25.615  -16.675 -8.155  0.50 29.00 ? 145 SER B C     1 
ATOM   8995  C  C     B SER B 2 145 ? 25.703  -15.773 -8.103  0.50 30.69 ? 145 SER B C     1 
ATOM   8996  O  O     A SER B 2 145 ? 24.762  -15.886 -7.737  0.50 24.75 ? 145 SER B O     1 
ATOM   8997  O  O     B SER B 2 145 ? 24.985  -14.877 -7.640  0.50 23.46 ? 145 SER B O     1 
ATOM   8998  C  CB    A SER B 2 145 ? 27.796  -17.544 -7.259  0.50 27.26 ? 145 SER B CB    1 
ATOM   8999  C  CB    B SER B 2 145 ? 27.806  -16.764 -7.178  0.50 26.85 ? 145 SER B CB    1 
ATOM   9000  O  OG    A SER B 2 145 ? 28.271  -17.611 -8.598  0.50 30.04 ? 145 SER B OG    1 
ATOM   9001  O  OG    B SER B 2 145 ? 28.323  -16.824 -8.502  0.50 29.94 ? 145 SER B OG    1 
ATOM   9002  N  N     A GLY B 2 146 ? 26.007  -16.694 -9.432  0.50 26.65 ? 146 GLY B N     1 
ATOM   9003  N  N     B GLY B 2 146 ? 26.017  -15.840 -9.399  0.50 22.42 ? 146 GLY B N     1 
ATOM   9004  C  CA    A GLY B 2 146 ? 25.527  -15.685 -10.363 0.50 26.12 ? 146 GLY B CA    1 
ATOM   9005  C  CA    B GLY B 2 146 ? 25.597  -14.836 -10.356 0.50 27.80 ? 146 GLY B CA    1 
ATOM   9006  C  C     A GLY B 2 146 ? 24.031  -15.766 -10.609 0.50 27.38 ? 146 GLY B C     1 
ATOM   9007  C  C     B GLY B 2 146 ? 24.110  -14.825 -10.654 0.50 29.53 ? 146 GLY B C     1 
ATOM   9008  O  O     A GLY B 2 146 ? 23.311  -14.775 -10.464 0.50 23.63 ? 146 GLY B O     1 
ATOM   9009  O  O     B GLY B 2 146 ? 23.442  -13.812 -10.434 0.50 25.87 ? 146 GLY B O     1 
ATOM   9010  N  N     A MET B 2 147 ? 23.542  -16.945 -11.003 0.50 26.58 ? 147 MET B N     1 
ATOM   9011  N  N     B MET B 2 147 ? 23.579  -15.935 -11.173 0.50 26.13 ? 147 MET B N     1 
ATOM   9012  C  CA    A MET B 2 147 ? 22.107  -17.080 -11.238 0.50 24.93 ? 147 MET B CA    1 
ATOM   9013  C  CA    B MET B 2 147 ? 22.146  -15.991 -11.451 0.50 25.35 ? 147 MET B CA    1 
ATOM   9014  C  C     A MET B 2 147 ? 21.319  -17.072 -9.934  0.50 23.30 ? 147 MET B C     1 
ATOM   9015  C  C     B MET B 2 147 ? 21.334  -15.960 -10.163 0.50 28.40 ? 147 MET B C     1 
ATOM   9016  O  O     A MET B 2 147 ? 20.195  -16.559 -9.895  0.50 25.47 ? 147 MET B O     1 
ATOM   9017  O  O     B MET B 2 147 ? 20.252  -15.363 -10.122 0.50 31.40 ? 147 MET B O     1 
ATOM   9018  C  CB    A MET B 2 147 ? 21.810  -18.357 -12.021 0.50 24.91 ? 147 MET B CB    1 
ATOM   9019  C  CB    B MET B 2 147 ? 21.807  -17.243 -12.259 0.50 27.41 ? 147 MET B CB    1 
ATOM   9020  C  CG    A MET B 2 147 ? 20.354  -18.498 -12.435 0.50 31.55 ? 147 MET B CG    1 
ATOM   9021  C  CG    B MET B 2 147 ? 20.391  -17.252 -12.810 0.50 28.19 ? 147 MET B CG    1 
ATOM   9022  S  SD    A MET B 2 147 ? 20.042  -20.005 -13.370 0.50 39.00 ? 147 MET B SD    1 
ATOM   9023  S  SD    B MET B 2 147 ? 19.921  -18.821 -13.564 0.50 33.25 ? 147 MET B SD    1 
ATOM   9024  C  CE    A MET B 2 147 ? 18.429  -19.650 -14.064 0.50 37.74 ? 147 MET B CE    1 
ATOM   9025  C  CE    B MET B 2 147 ? 18.198  -18.500 -13.936 0.50 40.88 ? 147 MET B CE    1 
ATOM   9026  N  N     A GLY B 2 148 ? 21.885  -17.634 -8.866  0.50 24.21 ? 148 GLY B N     1 
ATOM   9027  N  N     B GLY B 2 148 ? 21.841  -16.596 -9.104  0.50 24.55 ? 148 GLY B N     1 
ATOM   9028  C  CA    A GLY B 2 148 ? 21.173  -17.670 -7.599  0.50 28.37 ? 148 GLY B CA    1 
ATOM   9029  C  CA    B GLY B 2 148 ? 21.099  -16.645 -7.852  0.50 26.49 ? 148 GLY B CA    1 
ATOM   9030  C  C     A GLY B 2 148 ? 20.827  -16.289 -7.079  0.50 25.98 ? 148 GLY B C     1 
ATOM   9031  C  C     B GLY B 2 148 ? 20.818  -15.274 -7.269  0.50 26.55 ? 148 GLY B C     1 
ATOM   9032  O  O     A GLY B 2 148 ? 19.719  -16.061 -6.588  0.50 30.81 ? 148 GLY B O     1 
ATOM   9033  O  O     B GLY B 2 148 ? 19.717  -15.014 -6.779  0.50 32.19 ? 148 GLY B O     1 
ATOM   9034  N  N     A THR B 2 149 ? 21.769  -15.347 -7.181  0.50 25.74 ? 149 THR B N     1 
ATOM   9035  N  N     B THR B 2 149 ? 21.810  -14.381 -7.302  0.50 28.12 ? 149 THR B N     1 
ATOM   9036  C  CA    A THR B 2 149 ? 21.532  -14.000 -6.676  0.50 27.60 ? 149 THR B CA    1 
ATOM   9037  C  CA    B THR B 2 149 ? 21.586  -13.026 -6.809  0.50 30.61 ? 149 THR B CA    1 
ATOM   9038  C  C     A THR B 2 149 ? 20.611  -13.199 -7.587  0.50 27.60 ? 149 THR B C     1 
ATOM   9039  C  C     B THR B 2 149 ? 20.655  -12.246 -7.726  0.50 29.51 ? 149 THR B C     1 
ATOM   9040  O  O     A THR B 2 149 ? 19.863  -12.344 -7.101  0.50 33.92 ? 149 THR B O     1 
ATOM   9041  O  O     B THR B 2 149 ? 19.995  -11.303 -7.276  0.50 30.81 ? 149 THR B O     1 
ATOM   9042  C  CB    A THR B 2 149 ? 22.856  -13.255 -6.495  0.50 29.22 ? 149 THR B CB    1 
ATOM   9043  C  CB    B THR B 2 149 ? 22.911  -12.277 -6.648  0.50 27.70 ? 149 THR B CB    1 
ATOM   9044  O  OG1   A THR B 2 149 ? 23.570  -13.237 -7.737  0.50 26.68 ? 149 THR B OG1   1 
ATOM   9045  O  OG1   B THR B 2 149 ? 23.666  -12.358 -7.866  0.50 26.68 ? 149 THR B OG1   1 
ATOM   9046  C  CG2   A THR B 2 149 ? 23.709  -13.929 -5.430  0.50 25.74 ? 149 THR B CG2   1 
ATOM   9047  C  CG2   B THR B 2 149 ? 23.724  -12.859 -5.503  0.50 24.44 ? 149 THR B CG2   1 
ATOM   9048  N  N     A LEU B 2 150 ? 20.658  -13.442 -8.899  0.50 29.38 ? 150 LEU B N     1 
ATOM   9049  N  N     B LEU B 2 150 ? 20.594  -12.609 -9.009  0.50 29.62 ? 150 LEU B N     1 
ATOM   9050  C  CA    A LEU B 2 150 ? 19.673  -12.834 -9.788  0.50 29.29 ? 150 LEU B CA    1 
ATOM   9051  C  CA    B LEU B 2 150 ? 19.604  -11.996 -9.888  0.50 31.04 ? 150 LEU B CA    1 
ATOM   9052  C  C     A LEU B 2 150 ? 18.265  -13.281 -9.415  0.50 31.34 ? 150 LEU B C     1 
ATOM   9053  C  C     B LEU B 2 150 ? 18.205  -12.499 -9.557  0.50 33.08 ? 150 LEU B C     1 
ATOM   9054  O  O     A LEU B 2 150 ? 17.343  -12.462 -9.315  0.50 31.27 ? 150 LEU B O     1 
ATOM   9055  O  O     B LEU B 2 150 ? 17.251  -11.714 -9.503  0.50 31.83 ? 150 LEU B O     1 
ATOM   9056  C  CB    A LEU B 2 150 ? 19.980  -13.190 -11.242 0.50 33.14 ? 150 LEU B CB    1 
ATOM   9057  C  CB    B LEU B 2 150 ? 19.951  -12.277 -11.351 0.50 33.03 ? 150 LEU B CB    1 
ATOM   9058  C  CG    A LEU B 2 150 ? 18.998  -12.632 -12.279 0.50 34.79 ? 150 LEU B CG    1 
ATOM   9059  C  CG    B LEU B 2 150 ? 19.086  -11.576 -12.402 0.50 35.35 ? 150 LEU B CG    1 
ATOM   9060  C  CD1   A LEU B 2 150 ? 19.140  -11.120 -12.400 0.50 35.35 ? 150 LEU B CD1   1 
ATOM   9061  C  CD1   B LEU B 2 150 ? 19.223  -10.063 -12.296 0.50 35.98 ? 150 LEU B CD1   1 
ATOM   9062  C  CD2   A LEU B 2 150 ? 19.189  -13.306 -13.634 0.50 34.94 ? 150 LEU B CD2   1 
ATOM   9063  C  CD2   B LEU B 2 150 ? 19.451  -12.050 -13.800 0.50 29.62 ? 150 LEU B CD2   1 
ATOM   9064  N  N     A LEU B 2 151 ? 18.088  -14.585 -9.190  0.50 26.79 ? 151 LEU B N     1 
ATOM   9065  N  N     B LEU B 2 151 ? 18.071  -13.805 -9.316  0.50 29.22 ? 151 LEU B N     1 
ATOM   9066  C  CA    A LEU B 2 151 ? 16.780  -15.111 -8.817  0.50 33.05 ? 151 LEU B CA    1 
ATOM   9067  C  CA    B LEU B 2 151 ? 16.780  -14.368 -8.936  0.50 30.77 ? 151 LEU B CA    1 
ATOM   9068  C  C     A LEU B 2 151 ? 16.302  -14.527 -7.493  0.50 33.45 ? 151 LEU B C     1 
ATOM   9069  C  C     B LEU B 2 151 ? 16.295  -13.789 -7.611  0.50 34.85 ? 151 LEU B C     1 
ATOM   9070  O  O     A LEU B 2 151 ? 15.121  -14.197 -7.345  0.50 34.91 ? 151 LEU B O     1 
ATOM   9071  O  O     B LEU B 2 151 ? 15.099  -13.523 -7.444  0.50 34.36 ? 151 LEU B O     1 
ATOM   9072  C  CB    A LEU B 2 151 ? 16.834  -16.636 -8.745  0.50 34.36 ? 151 LEU B CB    1 
ATOM   9073  C  CB    B LEU B 2 151 ? 16.888  -15.891 -8.858  0.50 32.85 ? 151 LEU B CB    1 
ATOM   9074  C  CG    A LEU B 2 151 ? 16.411  -17.344 -10.031 0.50 40.66 ? 151 LEU B CG    1 
ATOM   9075  C  CG    B LEU B 2 151 ? 15.652  -16.712 -8.493  0.50 33.88 ? 151 LEU B CG    1 
ATOM   9076  C  CD1   A LEU B 2 151 ? 16.967  -18.756 -10.095 0.50 36.21 ? 151 LEU B CD1   1 
ATOM   9077  C  CD1   B LEU B 2 151 ? 14.499  -16.405 -9.427  0.50 34.80 ? 151 LEU B CD1   1 
ATOM   9078  C  CD2   A LEU B 2 151 ? 14.894  -17.358 -10.114 0.50 37.52 ? 151 LEU B CD2   1 
ATOM   9079  C  CD2   B LEU B 2 151 ? 15.995  -18.192 -8.532  0.50 33.61 ? 151 LEU B CD2   1 
ATOM   9080  N  N     A ILE B 2 152 ? 17.209  -14.394 -6.520  0.50 28.90 ? 152 ILE B N     1 
ATOM   9081  N  N     B ILE B 2 152 ? 17.215  -13.579 -6.663  0.50 26.22 ? 152 ILE B N     1 
ATOM   9082  C  CA    A ILE B 2 152 ? 16.864  -13.779 -5.241  0.50 33.07 ? 152 ILE B CA    1 
ATOM   9083  C  CA    B ILE B 2 152 ? 16.853  -12.994 -5.373  0.50 34.09 ? 152 ILE B CA    1 
ATOM   9084  C  C     A ILE B 2 152 ? 16.343  -12.365 -5.455  0.50 35.25 ? 152 ILE B C     1 
ATOM   9085  C  C     B ILE B 2 152 ? 16.210  -11.626 -5.568  0.50 35.32 ? 152 ILE B C     1 
ATOM   9086  O  O     A ILE B 2 152 ? 15.384  -11.932 -4.805  0.50 38.95 ? 152 ILE B O     1 
ATOM   9087  O  O     B ILE B 2 152 ? 15.148  -11.333 -5.007  0.50 39.96 ? 152 ILE B O     1 
ATOM   9088  C  CB    A ILE B 2 152 ? 18.085  -13.794 -4.303  0.50 30.89 ? 152 ILE B CB    1 
ATOM   9089  C  CB    B ILE B 2 152 ? 18.088  -12.904 -4.458  0.50 29.98 ? 152 ILE B CB    1 
ATOM   9090  C  CG1   A ILE B 2 152 ? 18.367  -15.214 -3.814  0.50 32.02 ? 152 ILE B CG1   1 
ATOM   9091  C  CG1   B ILE B 2 152 ? 18.466  -14.288 -3.927  0.50 32.11 ? 152 ILE B CG1   1 
ATOM   9092  C  CG2   A ILE B 2 152 ? 17.885  -12.834 -3.136  0.50 35.46 ? 152 ILE B CG2   1 
ATOM   9093  C  CG2   B ILE B 2 152 ? 17.838  -11.928 -3.316  0.50 30.81 ? 152 ILE B CG2   1 
ATOM   9094  C  CD1   A ILE B 2 152 ? 19.670  -15.340 -3.057  0.50 28.73 ? 152 ILE B CD1   1 
ATOM   9095  C  CD1   B ILE B 2 152 ? 19.620  -14.265 -2.938  0.50 30.68 ? 152 ILE B CD1   1 
ATOM   9096  N  N     A SER B 2 153 ? 16.951  -11.633 -6.389  0.50 33.38 ? 153 SER B N     1 
ATOM   9097  N  N     B SER B 2 153 ? 16.838  -10.772 -6.375  0.50 36.19 ? 153 SER B N     1 
ATOM   9098  C  CA    A SER B 2 153 ? 16.570  -10.244 -6.611  0.50 37.98 ? 153 SER B CA    1 
ATOM   9099  C  CA    B SER B 2 153 ? 16.343  -9.411  -6.530  0.50 40.20 ? 153 SER B CA    1 
ATOM   9100  C  C     A SER B 2 153 ? 15.229  -10.137 -7.329  0.50 34.56 ? 153 SER B C     1 
ATOM   9101  C  C     B SER B 2 153 ? 15.071  -9.338  -7.361  0.50 39.02 ? 153 SER B C     1 
ATOM   9102  O  O     A SER B 2 153 ? 14.400  -9.288  -6.982  0.50 40.92 ? 153 SER B O     1 
ATOM   9103  O  O     B SER B 2 153 ? 14.326  -8.358  -7.242  0.50 40.16 ? 153 SER B O     1 
ATOM   9104  C  CB    A SER B 2 153 ? 17.666  -9.533  -7.402  0.50 34.14 ? 153 SER B CB    1 
ATOM   9105  C  CB    B SER B 2 153 ? 17.415  -8.533  -7.161  0.50 37.67 ? 153 SER B CB    1 
ATOM   9106  O  OG    A SER B 2 153 ? 17.313  -8.195  -7.701  0.50 39.99 ? 153 SER B OG    1 
ATOM   9107  O  OG    B SER B 2 153 ? 18.633  -8.598  -6.443  0.50 34.93 ? 153 SER B OG    1 
ATOM   9108  N  N     A LYS B 2 154 ? 14.997  -10.983 -8.335  0.50 33.38 ? 154 LYS B N     1 
ATOM   9109  N  N     B LYS B 2 154 ? 14.815  -10.331 -8.214  0.50 33.25 ? 154 LYS B N     1 
ATOM   9110  C  CA    A LYS B 2 154 ? 13.754  -10.902 -9.098  0.50 36.63 ? 154 LYS B CA    1 
ATOM   9111  C  CA    B LYS B 2 154 ? 13.557  -10.349 -8.951  0.50 37.44 ? 154 LYS B CA    1 
ATOM   9112  C  C     A LYS B 2 154 ? 12.559  -11.356 -8.268  0.50 38.55 ? 154 LYS B C     1 
ATOM   9113  C  C     B LYS B 2 154 ? 12.393  -10.740 -8.047  0.50 38.58 ? 154 LYS B C     1 
ATOM   9114  O  O     A LYS B 2 154 ? 11.470  -10.778 -8.370  0.50 38.88 ? 154 LYS B O     1 
ATOM   9115  O  O     B LYS B 2 154 ? 11.291  -10.198 -8.180  0.50 40.30 ? 154 LYS B O     1 
ATOM   9116  C  CB    A LYS B 2 154 ? 13.866  -11.733 -10.376 0.50 38.58 ? 154 LYS B CB    1 
ATOM   9117  C  CB    B LYS B 2 154 ? 13.653  -11.303 -10.140 0.50 38.92 ? 154 LYS B CB    1 
ATOM   9118  C  CG    A LYS B 2 154 ? 14.824  -11.156 -11.407 0.50 40.46 ? 154 LYS B CG    1 
ATOM   9119  C  CG    B LYS B 2 154 ? 14.648  -10.869 -11.202 0.50 41.23 ? 154 LYS B CG    1 
ATOM   9120  C  CD    A LYS B 2 154 ? 14.399  -9.761  -11.831 0.50 44.03 ? 154 LYS B CD    1 
ATOM   9121  C  CD    B LYS B 2 154 ? 14.359  -9.460  -11.687 0.50 43.79 ? 154 LYS B CD    1 
ATOM   9122  C  CE    A LYS B 2 154 ? 15.326  -9.201  -12.894 0.50 49.73 ? 154 LYS B CE    1 
ATOM   9123  C  CE    B LYS B 2 154 ? 15.288  -9.083  -12.824 0.50 49.78 ? 154 LYS B CE    1 
ATOM   9124  N  NZ    A LYS B 2 154 ? 14.906  -7.836  -13.321 0.50 53.35 ? 154 LYS B NZ    1 
ATOM   9125  N  NZ    B LYS B 2 154 ? 15.197  -10.068 -13.935 0.50 46.95 ? 154 LYS B NZ    1 
ATOM   9126  N  N     A ILE B 2 155 ? 12.737  -12.399 -7.454  0.50 37.43 ? 155 ILE B N     1 
ATOM   9127  N  N     B ILE B 2 155 ? 12.626  -11.674 -7.123  0.50 38.58 ? 155 ILE B N     1 
ATOM   9128  C  CA    A ILE B 2 155 ? 11.674  -12.837 -6.558  0.50 31.83 ? 155 ILE B CA    1 
ATOM   9129  C  CA    B ILE B 2 155 ? 11.610  -12.036 -6.141  0.50 36.08 ? 155 ILE B CA    1 
ATOM   9130  C  C     A ILE B 2 155 ? 11.384  -11.765 -5.515  0.50 37.29 ? 155 ILE B C     1 
ATOM   9131  C  C     B ILE B 2 155 ? 11.346  -10.872 -5.193  0.50 35.84 ? 155 ILE B C     1 
ATOM   9132  O  O     A ILE B 2 155 ? 10.226  -11.531 -5.148  0.50 39.71 ? 155 ILE B O     1 
ATOM   9133  O  O     B ILE B 2 155 ? 10.192  -10.533 -4.906  0.50 40.52 ? 155 ILE B O     1 
ATOM   9134  C  CB    A ILE B 2 155 ? 12.055  -14.180 -5.910  0.50 38.16 ? 155 ILE B CB    1 
ATOM   9135  C  CB    B ILE B 2 155 ? 12.043  -13.300 -5.378  0.50 35.36 ? 155 ILE B CB    1 
ATOM   9136  C  CG1   A ILE B 2 155 ? 12.140  -15.275 -6.974  0.50 40.16 ? 155 ILE B CG1   1 
ATOM   9137  C  CG1   B ILE B 2 155 ? 12.057  -14.507 -6.318  0.50 39.93 ? 155 ILE B CG1   1 
ATOM   9138  C  CG2   A ILE B 2 155 ? 11.063  -14.559 -4.827  0.50 39.38 ? 155 ILE B CG2   1 
ATOM   9139  C  CG2   B ILE B 2 155 ? 11.138  -13.546 -4.183  0.50 35.99 ? 155 ILE B CG2   1 
ATOM   9140  C  CD1   A ILE B 2 155 ? 12.657  -16.590 -6.451  0.50 36.92 ? 155 ILE B CD1   1 
ATOM   9141  C  CD1   B ILE B 2 155 ? 12.863  -15.674 -5.799  0.50 34.58 ? 155 ILE B CD1   1 
ATOM   9142  N  N     A ARG B 2 156 ? 12.433  -11.099 -5.025  0.50 39.08 ? 156 ARG B N     1 
ATOM   9143  N  N     B ARG B 2 156 ? 12.417  -10.241 -4.697  0.50 36.76 ? 156 ARG B N     1 
ATOM   9144  C  CA    A ARG B 2 156 ? 12.265  -9.959  -4.131  0.50 36.93 ? 156 ARG B CA    1 
ATOM   9145  C  CA    B ARG B 2 156 ? 12.282  -9.113  -3.779  0.50 39.69 ? 156 ARG B CA    1 
ATOM   9146  C  C     A ARG B 2 156 ? 11.324  -8.920  -4.730  0.50 39.05 ? 156 ARG B C     1 
ATOM   9147  C  C     B ARG B 2 156 ? 11.476  -7.972  -4.392  0.50 41.47 ? 156 ARG B C     1 
ATOM   9148  O  O     A ARG B 2 156 ? 10.498  -8.332  -4.022  0.50 39.67 ? 156 ARG B O     1 
ATOM   9149  O  O     B ARG B 2 156 ? 10.864  -7.181  -3.664  0.50 41.29 ? 156 ARG B O     1 
ATOM   9150  C  CB    A ARG B 2 156 ? 13.633  -9.335  -3.842  0.50 37.59 ? 156 ARG B CB    1 
ATOM   9151  C  CB    B ARG B 2 156 ? 13.672  -8.627  -3.354  0.50 39.54 ? 156 ARG B CB    1 
ATOM   9152  C  CG    A ARG B 2 156 ? 13.649  -8.273  -2.758  0.50 42.20 ? 156 ARG B CG    1 
ATOM   9153  C  CG    B ARG B 2 156 ? 13.688  -7.394  -2.455  0.50 41.85 ? 156 ARG B CG    1 
ATOM   9154  C  CD    A ARG B 2 156 ? 13.748  -8.906  -1.385  0.50 41.65 ? 156 ARG B CD    1 
ATOM   9155  C  CD    B ARG B 2 156 ? 14.255  -7.714  -1.080  0.50 38.27 ? 156 ARG B CD    1 
ATOM   9156  N  NE    A ARG B 2 156 ? 14.000  -7.924  -0.337  0.50 38.74 ? 156 ARG B NE    1 
ATOM   9157  N  NE    B ARG B 2 156 ? 13.372  -8.590  -0.320  0.50 44.53 ? 156 ARG B NE    1 
ATOM   9158  C  CZ    A ARG B 2 156 ? 14.052  -8.216  0.955   0.50 38.57 ? 156 ARG B CZ    1 
ATOM   9159  C  CZ    B ARG B 2 156 ? 13.714  -9.211  0.800   0.50 37.22 ? 156 ARG B CZ    1 
ATOM   9160  N  NH1   A ARG B 2 156 ? 13.872  -9.453  1.390   0.50 39.08 ? 156 ARG B NH1   1 
ATOM   9161  N  NH1   B ARG B 2 156 ? 14.928  -9.089  1.315   0.50 34.19 ? 156 ARG B NH1   1 
ATOM   9162  N  NH2   A ARG B 2 156 ? 14.284  -7.244  1.834   0.50 42.58 ? 156 ARG B NH2   1 
ATOM   9163  N  NH2   B ARG B 2 156 ? 12.817  -9.973  1.419   0.50 30.41 ? 156 ARG B NH2   1 
ATOM   9164  N  N     A GLU B 2 157 ? 11.427  -8.694  -6.041  0.50 39.29 ? 157 GLU B N     1 
ATOM   9165  N  N     B GLU B 2 157 ? 11.458  -7.868  -5.722  0.50 37.92 ? 157 GLU B N     1 
ATOM   9166  C  CA    A GLU B 2 157 ? 10.620  -7.665  -6.685  0.50 42.09 ? 157 GLU B CA    1 
ATOM   9167  C  CA    B GLU B 2 157 ? 10.602  -6.878  -6.365  0.50 43.13 ? 157 GLU B CA    1 
ATOM   9168  C  C     A GLU B 2 157 ? 9.147   -8.050  -6.754  0.50 39.57 ? 157 GLU B C     1 
ATOM   9169  C  C     B GLU B 2 157 ? 9.142   -7.317  -6.363  0.50 39.28 ? 157 GLU B C     1 
ATOM   9170  O  O     A GLU B 2 157 ? 8.279   -7.177  -6.659  0.50 35.61 ? 157 GLU B O     1 
ATOM   9171  O  O     B GLU B 2 157 ? 8.250   -6.506  -6.097  0.50 39.63 ? 157 GLU B O     1 
ATOM   9172  C  CB    A GLU B 2 157 ? 11.166  -7.376  -8.085  0.50 39.90 ? 157 GLU B CB    1 
ATOM   9173  C  CB    B GLU B 2 157 ? 11.072  -6.618  -7.798  0.50 41.73 ? 157 GLU B CB    1 
ATOM   9174  C  CG    A GLU B 2 157 ? 12.582  -6.813  -8.089  0.50 46.90 ? 157 GLU B CG    1 
ATOM   9175  C  CG    B GLU B 2 157 ? 12.365  -5.826  -7.905  0.50 49.52 ? 157 GLU B CG    1 
ATOM   9176  C  CD    A GLU B 2 157 ? 13.129  -6.606  -9.489  0.50 46.98 ? 157 GLU B CD    1 
ATOM   9177  C  CD    B GLU B 2 157 ? 12.711  -5.480  -9.342  0.50 50.02 ? 157 GLU B CD    1 
ATOM   9178  O  OE1   A GLU B 2 157 ? 12.466  -7.037  -10.458 0.50 54.28 ? 157 GLU B OE1   1 
ATOM   9179  O  OE1   B GLU B 2 157 ? 11.952  -5.888  -10.249 0.50 58.31 ? 157 GLU B OE1   1 
ATOM   9180  O  OE2   A GLU B 2 157 ? 14.219  -6.010  -9.618  0.50 49.09 ? 157 GLU B OE2   1 
ATOM   9181  O  OE2   B GLU B 2 157 ? 13.736  -4.802  -9.564  0.50 52.57 ? 157 GLU B OE2   1 
ATOM   9182  N  N     A GLU B 2 158 ? 8.840   -9.336  -6.909  0.50 40.63 ? 158 GLU B N     1 
ATOM   9183  N  N     B GLU B 2 158 ? 8.882   -8.595  -6.648  0.50 40.68 ? 158 GLU B N     1 
ATOM   9184  C  CA    A GLU B 2 158 ? 7.455   -9.769  -7.055  0.50 39.22 ? 158 GLU B CA    1 
ATOM   9185  C  CA    B GLU B 2 158 ? 7.509   -9.073  -6.771  0.50 39.23 ? 158 GLU B CA    1 
ATOM   9186  C  C     A GLU B 2 158 ? 6.820   -10.211 -5.738  0.50 37.35 ? 158 GLU B C     1 
ATOM   9187  C  C     B GLU B 2 158 ? 6.876   -9.389  -5.419  0.50 37.07 ? 158 GLU B C     1 
ATOM   9188  O  O     A GLU B 2 158 ? 5.618   -10.494 -5.712  0.50 38.31 ? 158 GLU B O     1 
ATOM   9189  O  O     B GLU B 2 158 ? 5.661   -9.228  -5.260  0.50 38.90 ? 158 GLU B O     1 
ATOM   9190  C  CB    A GLU B 2 158 ? 7.368   -10.906 -8.079  0.50 37.80 ? 158 GLU B CB    1 
ATOM   9191  C  CB    B GLU B 2 158 ? 7.466   -10.307 -7.676  0.50 37.74 ? 158 GLU B CB    1 
ATOM   9192  C  CG    A GLU B 2 158 ? 7.785   -10.506 -9.494  0.50 42.04 ? 158 GLU B CG    1 
ATOM   9193  C  CG    B GLU B 2 158 ? 6.061   -10.813 -7.970  0.50 40.41 ? 158 GLU B CG    1 
ATOM   9194  C  CD    A GLU B 2 158 ? 7.452   -11.569 -10.528 0.50 37.87 ? 158 GLU B CD    1 
ATOM   9195  C  CD    B GLU B 2 158 ? 6.049   -11.962 -8.958  0.50 41.34 ? 158 GLU B CD    1 
ATOM   9196  O  OE1   A GLU B 2 158 ? 6.399   -12.222 -10.391 0.50 46.73 ? 158 GLU B OE1   1 
ATOM   9197  O  OE1   B GLU B 2 158 ? 7.136   -12.368 -9.416  0.50 48.59 ? 158 GLU B OE1   1 
ATOM   9198  O  OE2   A GLU B 2 158 ? 8.246   -11.754 -11.472 0.50 49.11 ? 158 GLU B OE2   1 
ATOM   9199  O  OE2   B GLU B 2 158 ? 4.951   -12.459 -9.279  0.50 42.38 ? 158 GLU B OE2   1 
ATOM   9200  N  N     A TYR B 2 159 ? 7.594   -10.287 -4.658  0.50 37.05 ? 159 TYR B N     1 
ATOM   9201  N  N     B TYR B 2 159 ? 7.666   -9.831  -4.439  0.50 35.99 ? 159 TYR B N     1 
ATOM   9202  C  CA    A TYR B 2 159 ? 7.077   -10.657 -3.340  0.50 34.77 ? 159 TYR B CA    1 
ATOM   9203  C  CA    B TYR B 2 159 ? 7.174   -10.159 -3.101  0.50 34.24 ? 159 TYR B CA    1 
ATOM   9204  C  C     A TYR B 2 159 ? 7.870   -9.926  -2.267  0.50 35.93 ? 159 TYR B C     1 
ATOM   9205  C  C     B TYR B 2 159 ? 7.905   -9.298  -2.075  0.50 38.10 ? 159 TYR B C     1 
ATOM   9206  O  O     A TYR B 2 159 ? 8.523   -10.550 -1.431  0.50 36.24 ? 159 TYR B O     1 
ATOM   9207  O  O     B TYR B 2 159 ? 8.711   -9.808  -1.286  0.50 37.14 ? 159 TYR B O     1 
ATOM   9208  C  CB    A TYR B 2 159 ? 7.145   -12.170 -3.115  0.50 36.23 ? 159 TYR B CB    1 
ATOM   9209  C  CB    B TYR B 2 159 ? 7.369   -11.640 -2.778  0.50 35.98 ? 159 TYR B CB    1 
ATOM   9210  C  CG    A TYR B 2 159 ? 6.571   -13.031 -4.212  0.50 37.60 ? 159 TYR B CG    1 
ATOM   9211  C  CG    B TYR B 2 159 ? 6.793   -12.608 -3.789  0.50 36.81 ? 159 TYR B CG    1 
ATOM   9212  C  CD1   A TYR B 2 159 ? 7.373   -13.484 -5.250  0.50 38.26 ? 159 TYR B CD1   1 
ATOM   9213  C  CD1   B TYR B 2 159 ? 7.494   -12.939 -4.939  0.50 38.35 ? 159 TYR B CD1   1 
ATOM   9214  C  CD2   A TYR B 2 159 ? 5.232   -13.400 -4.207  0.50 37.24 ? 159 TYR B CD2   1 
ATOM   9215  C  CD2   B TYR B 2 159 ? 5.559   -13.213 -3.577  0.50 38.13 ? 159 TYR B CD2   1 
ATOM   9216  C  CE1   A TYR B 2 159 ? 6.858   -14.276 -6.257  0.50 42.49 ? 159 TYR B CE1   1 
ATOM   9217  C  CE1   B TYR B 2 159 ? 6.976   -13.829 -5.859  0.50 40.08 ? 159 TYR B CE1   1 
ATOM   9218  C  CE2   A TYR B 2 159 ? 4.705   -14.196 -5.217  0.50 36.18 ? 159 TYR B CE2   1 
ATOM   9219  C  CE2   B TYR B 2 159 ? 5.033   -14.107 -4.492  0.50 34.42 ? 159 TYR B CE2   1 
ATOM   9220  C  CZ    A TYR B 2 159 ? 5.525   -14.626 -6.238  0.50 43.37 ? 159 TYR B CZ    1 
ATOM   9221  C  CZ    B TYR B 2 159 ? 5.746   -14.410 -5.631  0.50 43.85 ? 159 TYR B CZ    1 
ATOM   9222  O  OH    A TYR B 2 159 ? 5.018   -15.414 -7.243  0.50 51.16 ? 159 TYR B OH    1 
ATOM   9223  O  OH    B TYR B 2 159 ? 5.234   -15.298 -6.548  0.50 48.36 ? 159 TYR B OH    1 
ATOM   9224  N  N     A PRO B 2 160 ? 7.828   -8.590  -2.259  0.50 40.68 ? 160 PRO B N     1 
ATOM   9225  N  N     B PRO B 2 160 ? 7.637   -7.989  -2.046  0.50 40.03 ? 160 PRO B N     1 
ATOM   9226  C  CA    A PRO B 2 160 ? 8.675   -7.836  -1.317  0.50 39.93 ? 160 PRO B CA    1 
ATOM   9227  C  CA    B PRO B 2 160 ? 8.428   -7.095  -1.185  0.50 42.22 ? 160 PRO B CA    1 
ATOM   9228  C  C     A PRO B 2 160 ? 8.284   -8.019  0.140   0.50 41.28 ? 160 PRO B C     1 
ATOM   9229  C  C     B PRO B 2 160 ? 8.153   -7.247  0.305   0.50 42.13 ? 160 PRO B C     1 
ATOM   9230  O  O     A PRO B 2 160 ? 9.128   -7.812  1.022   0.50 39.32 ? 160 PRO B O     1 
ATOM   9231  O  O     B PRO B 2 160 ? 8.841   -6.603  1.107   0.50 40.34 ? 160 PRO B O     1 
ATOM   9232  C  CB    A PRO B 2 160 ? 8.475   -6.382  -1.767  0.50 41.99 ? 160 PRO B CB    1 
ATOM   9233  C  CB    B PRO B 2 160 ? 8.027   -5.699  -1.681  0.50 41.37 ? 160 PRO B CB    1 
ATOM   9234  C  CG    A PRO B 2 160 ? 7.088   -6.385  -2.347  0.50 37.76 ? 160 PRO B CG    1 
ATOM   9235  C  CG    B PRO B 2 160 ? 6.638   -5.878  -2.184  0.50 40.99 ? 160 PRO B CG    1 
ATOM   9236  C  CD    A PRO B 2 160 ? 6.872   -7.723  -2.973  0.50 38.61 ? 160 PRO B CD    1 
ATOM   9237  C  CD    B PRO B 2 160 ? 6.572   -7.267  -2.764  0.50 37.72 ? 160 PRO B CD    1 
ATOM   9238  N  N     A ASP B 2 161 ? 7.041   -8.408  0.421   0.50 39.94 ? 161 ASP B N     1 
ATOM   9239  N  N     B ASP B 2 161 ? 7.186   -8.068  0.715   0.50 39.81 ? 161 ASP B N     1 
ATOM   9240  C  CA    A ASP B 2 161 ? 6.568   -8.590  1.786   0.50 43.15 ? 161 ASP B CA    1 
ATOM   9241  C  CA    B ASP B 2 161 ? 6.882   -8.246  2.128   0.50 42.73 ? 161 ASP B CA    1 
ATOM   9242  C  C     A ASP B 2 161 ? 6.734   -10.022 2.287   0.50 40.65 ? 161 ASP B C     1 
ATOM   9243  C  C     B ASP B 2 161 ? 7.173   -9.654  2.630   0.50 39.87 ? 161 ASP B C     1 
ATOM   9244  O  O     A ASP B 2 161 ? 6.104   -10.395 3.282   0.50 41.89 ? 161 ASP B O     1 
ATOM   9245  O  O     B ASP B 2 161 ? 6.903   -9.946  3.798   0.50 40.83 ? 161 ASP B O     1 
ATOM   9246  C  CB    A ASP B 2 161 ? 5.106   -8.147  1.905   0.50 43.09 ? 161 ASP B CB    1 
ATOM   9247  C  CB    B ASP B 2 161 ? 5.416   -7.883  2.412   0.50 42.42 ? 161 ASP B CB    1 
ATOM   9248  C  CG    A ASP B 2 161 ? 4.279   -8.520  0.691   0.50 43.43 ? 161 ASP B CG    1 
ATOM   9249  C  CG    B ASP B 2 161 ? 4.436   -8.898  1.852   0.50 43.57 ? 161 ASP B CG    1 
ATOM   9250  O  OD1   A ASP B 2 161 ? 4.869   -8.744  -0.388  0.50 37.29 ? 161 ASP B OD1   1 
ATOM   9251  O  OD1   B ASP B 2 161 ? 4.775   -9.597  0.874   0.50 44.01 ? 161 ASP B OD1   1 
ATOM   9252  O  OD2   A ASP B 2 161 ? 3.035   -8.580  0.820   0.50 46.13 ? 161 ASP B OD2   1 
ATOM   9253  O  OD2   B ASP B 2 161 ? 3.314   -8.996  2.395   0.50 50.73 ? 161 ASP B OD2   1 
ATOM   9254  N  N     A ARG B 2 162 ? 7.561   -10.828 1.626   0.50 36.88 ? 162 ARG B N     1 
ATOM   9255  N  N     B ARG B 2 162 ? 7.718   -10.530 1.790   0.50 38.06 ? 162 ARG B N     1 
ATOM   9256  C  CA    A ARG B 2 162 ? 7.943   -12.137 2.129   0.50 31.16 ? 162 ARG B CA    1 
ATOM   9257  C  CA    B ARG B 2 162 ? 8.041   -11.888 2.196   0.50 31.17 ? 162 ARG B CA    1 
ATOM   9258  C  C     A ARG B 2 162 ? 9.425   -12.130 2.480   0.50 31.02 ? 162 ARG B C     1 
ATOM   9259  C  C     B ARG B 2 162 ? 9.523   -11.999 2.532   0.50 30.89 ? 162 ARG B C     1 
ATOM   9260  O  O     A ARG B 2 162 ? 10.175  -11.240 2.074   0.50 32.27 ? 162 ARG B O     1 
ATOM   9261  O  O     B ARG B 2 162 ? 10.355  -11.255 2.007   0.50 32.66 ? 162 ARG B O     1 
ATOM   9262  C  CB    A ARG B 2 162 ? 7.638   -13.241 1.108   0.50 30.39 ? 162 ARG B CB    1 
ATOM   9263  C  CB    B ARG B 2 162 ? 7.666   -12.888 1.101   0.50 30.80 ? 162 ARG B CB    1 
ATOM   9264  C  CG    A ARG B 2 162 ? 6.174   -13.318 0.654   0.50 34.11 ? 162 ARG B CG    1 
ATOM   9265  C  CG    B ARG B 2 162 ? 6.249   -12.716 0.541   0.50 35.06 ? 162 ARG B CG    1 
ATOM   9266  C  CD    A ARG B 2 162 ? 5.221   -13.743 1.773   0.50 36.47 ? 162 ARG B CD    1 
ATOM   9267  C  CD    B ARG B 2 162 ? 5.157   -13.012 1.572   0.50 38.25 ? 162 ARG B CD    1 
ATOM   9268  N  NE    A ARG B 2 162 ? 4.850   -12.635 2.645   0.50 40.43 ? 162 ARG B NE    1 
ATOM   9269  N  NE    B ARG B 2 162 ? 4.911   -11.890 2.471   0.50 42.06 ? 162 ARG B NE    1 
ATOM   9270  C  CZ    A ARG B 2 162 ? 4.089   -12.746 3.727   0.50 40.99 ? 162 ARG B CZ    1 
ATOM   9271  C  CZ    B ARG B 2 162 ? 4.002   -11.885 3.438   0.50 41.45 ? 162 ARG B CZ    1 
ATOM   9272  N  NH1   A ARG B 2 162 ? 3.590   -13.912 4.106   0.50 37.31 ? 162 ARG B NH1   1 
ATOM   9273  N  NH1   B ARG B 2 162 ? 3.213   -12.926 3.650   0.50 37.06 ? 162 ARG B NH1   1 
ATOM   9274  N  NH2   A ARG B 2 162 ? 3.827   -11.661 4.450   0.50 40.88 ? 162 ARG B NH2   1 
ATOM   9275  N  NH2   B ARG B 2 162 ? 3.883   -10.809 4.211   0.50 41.36 ? 162 ARG B NH2   1 
ATOM   9276  N  N     A ILE B 2 163 ? 9.841   -13.136 3.244   0.50 26.05 ? 163 ILE B N     1 
ATOM   9277  N  N     B ILE B 2 163 ? 9.842   -12.940 3.415   0.50 26.26 ? 163 ILE B N     1 
ATOM   9278  C  CA    A ILE B 2 163 ? 11.194  -13.213 3.783   0.50 31.40 ? 163 ILE B CA    1 
ATOM   9279  C  CA    B ILE B 2 163 ? 11.196  -13.093 3.935   0.50 31.27 ? 163 ILE B CA    1 
ATOM   9280  C  C     A ILE B 2 163 ? 12.037  -14.133 2.912   0.50 26.56 ? 163 ILE B C     1 
ATOM   9281  C  C     B ILE B 2 163 ? 12.084  -13.734 2.876   0.50 27.87 ? 163 ILE B C     1 
ATOM   9282  O  O     A ILE B 2 163 ? 11.599  -15.224 2.533   0.50 31.37 ? 163 ILE B O     1 
ATOM   9283  O  O     B ILE B 2 163 ? 11.661  -14.640 2.151   0.50 28.60 ? 163 ILE B O     1 
ATOM   9284  C  CB    A ILE B 2 163 ? 11.177  -13.700 5.245   0.50 28.57 ? 163 ILE B CB    1 
ATOM   9285  C  CB    B ILE B 2 163 ? 11.176  -13.923 5.233   0.50 28.61 ? 163 ILE B CB    1 
ATOM   9286  C  CG1   A ILE B 2 163 ? 10.544  -12.640 6.153   0.50 34.70 ? 163 ILE B CG1   1 
ATOM   9287  C  CG1   B ILE B 2 163 ? 10.397  -13.186 6.330   0.50 34.01 ? 163 ILE B CG1   1 
ATOM   9288  C  CG2   A ILE B 2 163 ? 12.579  -14.057 5.714   0.50 24.62 ? 163 ILE B CG2   1 
ATOM   9289  C  CG2   B ILE B 2 163 ? 12.588  -14.250 5.698   0.50 24.49 ? 163 ILE B CG2   1 
ATOM   9290  C  CD1   A ILE B 2 163 ? 11.272  -11.305 6.127   0.50 34.02 ? 163 ILE B CD1   1 
ATOM   9291  C  CD1   B ILE B 2 163 ? 11.019  -11.868 6.743   0.50 35.37 ? 163 ILE B CD1   1 
ATOM   9292  N  N     A MET B 2 164 ? 13.254  -13.696 2.599   0.50 25.20 ? 164 MET B N     1 
ATOM   9293  N  N     B MET B 2 164 ? 13.327  -13.257 2.781   0.50 23.37 ? 164 MET B N     1 
ATOM   9294  C  CA    A MET B 2 164 ? 14.199  -14.488 1.823   0.50 26.21 ? 164 MET B CA    1 
ATOM   9295  C  CA    B MET B 2 164 ? 14.313  -13.789 1.845   0.50 26.50 ? 164 MET B CA    1 
ATOM   9296  C  C     A MET B 2 164 ? 15.303  -14.991 2.742   0.50 25.60 ? 164 MET B C     1 
ATOM   9297  C  C     B MET B 2 164 ? 15.492  -14.330 2.645   0.50 27.05 ? 164 MET B C     1 
ATOM   9298  O  O     A MET B 2 164 ? 15.953  -14.199 3.432   0.50 27.14 ? 164 MET B O     1 
ATOM   9299  O  O     B MET B 2 164 ? 16.238  -13.560 3.260   0.50 26.49 ? 164 MET B O     1 
ATOM   9300  C  CB    A MET B 2 164 ? 14.795  -13.673 0.676   0.50 28.11 ? 164 MET B CB    1 
ATOM   9301  C  CB    B MET B 2 164 ? 14.761  -12.719 0.852   0.50 26.44 ? 164 MET B CB    1 
ATOM   9302  C  CG    A MET B 2 164 ? 15.891  -14.407 -0.083  0.50 27.79 ? 164 MET B CG    1 
ATOM   9303  C  CG    B MET B 2 164 ? 15.825  -13.201 -0.116  0.50 31.52 ? 164 MET B CG    1 
ATOM   9304  S  SD    A MET B 2 164 ? 15.285  -15.781 -1.083  0.50 31.33 ? 164 MET B SD    1 
ATOM   9305  S  SD    B MET B 2 164 ? 15.317  -14.666 -1.037  0.50 35.96 ? 164 MET B SD    1 
ATOM   9306  C  CE    A MET B 2 164 ? 14.315  -14.899 -2.304  0.50 35.09 ? 164 MET B CE    1 
ATOM   9307  C  CE    B MET B 2 164 ? 14.291  -13.932 -2.308  0.50 35.41 ? 164 MET B CE    1 
ATOM   9308  N  N     A ASN B 2 165 ? 15.510  -16.304 2.744   0.50 26.07 ? 165 ASN B N     1 
ATOM   9309  N  N     B ASN B 2 165 ? 15.661  -15.651 2.626   0.50 25.28 ? 165 ASN B N     1 
ATOM   9310  C  CA    A ASN B 2 165 ? 16.501  -16.956 3.590   0.50 26.93 ? 165 ASN B CA    1 
ATOM   9311  C  CA    B ASN B 2 165 ? 16.670  -16.345 3.414   0.50 26.56 ? 165 ASN B CA    1 
ATOM   9312  C  C     A ASN B 2 165 ? 17.345  -17.879 2.724   0.50 29.37 ? 165 ASN B C     1 
ATOM   9313  C  C     B ASN B 2 165 ? 17.530  -17.217 2.505   0.50 28.24 ? 165 ASN B C     1 
ATOM   9314  O  O     A ASN B 2 165 ? 16.800  -18.648 1.929   0.50 27.08 ? 165 ASN B O     1 
ATOM   9315  O  O     B ASN B 2 165 ? 17.021  -17.829 1.562   0.50 25.79 ? 165 ASN B O     1 
ATOM   9316  C  CB    A ASN B 2 165 ? 15.810  -17.732 4.718   0.50 25.30 ? 165 ASN B CB    1 
ATOM   9317  C  CB    B ASN B 2 165 ? 15.996  -17.194 4.500   0.50 26.13 ? 165 ASN B CB    1 
ATOM   9318  C  CG    A ASN B 2 165 ? 16.737  -18.703 5.412   0.50 34.25 ? 165 ASN B CG    1 
ATOM   9319  C  CG    B ASN B 2 165 ? 16.958  -18.123 5.203   0.50 32.17 ? 165 ASN B CG    1 
ATOM   9320  O  OD1   A ASN B 2 165 ? 16.570  -19.919 5.310   0.50 37.60 ? 165 ASN B OD1   1 
ATOM   9321  O  OD1   B ASN B 2 165 ? 16.709  -19.324 5.312   0.50 37.48 ? 165 ASN B OD1   1 
ATOM   9322  N  ND2   A ASN B 2 165 ? 17.725  -18.172 6.121   0.50 29.40 ? 165 ASN B ND2   1 
ATOM   9323  N  ND2   B ASN B 2 165 ? 18.065  -17.575 5.684   0.50 27.85 ? 165 ASN B ND2   1 
ATOM   9324  N  N     A THR B 2 166 ? 18.668  -17.800 2.859   0.50 29.90 ? 166 THR B N     1 
ATOM   9325  N  N     B THR B 2 166 ? 18.837  -17.268 2.780   0.50 27.88 ? 166 THR B N     1 
ATOM   9326  C  CA    A THR B 2 166 ? 19.556  -18.585 2.014   0.50 27.36 ? 166 THR B CA    1 
ATOM   9327  C  CA    B THR B 2 166 ? 19.754  -18.096 2.005   0.50 28.14 ? 166 THR B CA    1 
ATOM   9328  C  C     A THR B 2 166 ? 20.507  -19.425 2.853   0.50 29.51 ? 166 THR B C     1 
ATOM   9329  C  C     B THR B 2 166 ? 20.588  -18.977 2.924   0.50 28.87 ? 166 THR B C     1 
ATOM   9330  O  O     A THR B 2 166 ? 20.883  -19.046 3.969   0.50 28.19 ? 166 THR B O     1 
ATOM   9331  O  O     B THR B 2 166 ? 20.766  -18.689 4.112   0.50 25.61 ? 166 THR B O     1 
ATOM   9332  C  CB    A THR B 2 166 ? 20.383  -17.701 1.061   0.50 27.58 ? 166 THR B CB    1 
ATOM   9333  C  CB    B THR B 2 166 ? 20.712  -17.264 1.122   0.50 28.19 ? 166 THR B CB    1 
ATOM   9334  O  OG1   A THR B 2 166 ? 21.373  -16.974 1.802   0.50 29.03 ? 166 THR B OG1   1 
ATOM   9335  O  OG1   B THR B 2 166 ? 21.621  -16.523 1.949   0.50 27.37 ? 166 THR B OG1   1 
ATOM   9336  C  CG2   A THR B 2 166 ? 19.489  -16.726 0.313   0.50 29.58 ? 166 THR B CG2   1 
ATOM   9337  C  CG2   B THR B 2 166 ? 19.945  -16.310 0.222   0.50 28.21 ? 166 THR B CG2   1 
ATOM   9338  N  N     A PHE B 2 167 ? 20.877  -20.581 2.301   0.50 23.79 ? 167 PHE B N     1 
ATOM   9339  N  N     B PHE B 2 167 ? 21.090  -20.069 2.344   0.50 25.22 ? 167 PHE B N     1 
ATOM   9340  C  CA    A PHE B 2 167 ? 22.006  -21.374 2.767   0.50 24.80 ? 167 PHE B CA    1 
ATOM   9341  C  CA    B PHE B 2 167 ? 22.148  -20.905 2.909   0.50 23.95 ? 167 PHE B CA    1 
ATOM   9342  C  C     A PHE B 2 167 ? 23.108  -21.208 1.734   0.50 23.92 ? 167 PHE B C     1 
ATOM   9343  C  C     B PHE B 2 167 ? 23.300  -20.802 1.914   0.50 25.13 ? 167 PHE B C     1 
ATOM   9344  O  O     A PHE B 2 167 ? 22.930  -21.590 0.572   0.50 23.76 ? 167 PHE B O     1 
ATOM   9345  O  O     B PHE B 2 167 ? 23.351  -21.563 0.947   0.50 25.50 ? 167 PHE B O     1 
ATOM   9346  C  CB    A PHE B 2 167 ? 21.632  -22.848 2.936   0.50 26.43 ? 167 PHE B CB    1 
ATOM   9347  C  CB    B PHE B 2 167 ? 21.706  -22.363 3.095   0.50 26.83 ? 167 PHE B CB    1 
ATOM   9348  C  CG    A PHE B 2 167 ? 20.642  -23.101 4.038   0.50 28.42 ? 167 PHE B CG    1 
ATOM   9349  C  CG    B PHE B 2 167 ? 20.647  -22.561 4.144   0.50 28.50 ? 167 PHE B CG    1 
ATOM   9350  C  CD1   A PHE B 2 167 ? 19.280  -23.062 3.786   0.50 29.30 ? 167 PHE B CD1   1 
ATOM   9351  C  CD1   B PHE B 2 167 ? 19.310  -22.361 3.845   0.50 30.94 ? 167 PHE B CD1   1 
ATOM   9352  C  CD2   A PHE B 2 167 ? 21.074  -23.378 5.323   0.50 29.11 ? 167 PHE B CD2   1 
ATOM   9353  C  CD2   B PHE B 2 167 ? 20.988  -22.973 5.422   0.50 29.95 ? 167 PHE B CD2   1 
ATOM   9354  C  CE1   A PHE B 2 167 ? 18.366  -23.287 4.796   0.50 26.91 ? 167 PHE B CE1   1 
ATOM   9355  C  CE1   B PHE B 2 167 ? 18.332  -22.552 4.805   0.50 27.93 ? 167 PHE B CE1   1 
ATOM   9356  C  CE2   A PHE B 2 167 ? 20.165  -23.607 6.338   0.50 27.73 ? 167 PHE B CE2   1 
ATOM   9357  C  CE2   B PHE B 2 167 ? 20.013  -23.165 6.385   0.50 26.99 ? 167 PHE B CE2   1 
ATOM   9358  C  CZ    A PHE B 2 167 ? 18.808  -23.560 6.072   0.50 32.41 ? 167 PHE B CZ    1 
ATOM   9359  C  CZ    B PHE B 2 167 ? 18.686  -22.952 6.073   0.50 29.49 ? 167 PHE B CZ    1 
ATOM   9360  N  N     A SER B 2 168 ? 24.229  -20.620 2.146   0.50 24.40 ? 168 SER B N     1 
ATOM   9361  N  N     B SER B 2 168 ? 24.215  -19.863 2.146   0.50 26.78 ? 168 SER B N     1 
ATOM   9362  C  CA    A SER B 2 168 ? 25.245  -20.147 1.212   0.50 25.92 ? 168 SER B CA    1 
ATOM   9363  C  CA    B SER B 2 168 ? 25.193  -19.458 1.141   0.50 25.50 ? 168 SER B CA    1 
ATOM   9364  C  C     A SER B 2 168 ? 26.602  -20.705 1.605   0.50 21.81 ? 168 SER B C     1 
ATOM   9365  C  C     B SER B 2 168 ? 26.554  -20.079 1.443   0.50 21.75 ? 168 SER B C     1 
ATOM   9366  O  O     A SER B 2 168 ? 27.107  -20.407 2.692   0.50 25.41 ? 168 SER B O     1 
ATOM   9367  O  O     B SER B 2 168 ? 27.140  -19.820 2.497   0.50 19.45 ? 168 SER B O     1 
ATOM   9368  C  CB    A SER B 2 168 ? 25.277  -18.617 1.182   0.50 27.37 ? 168 SER B CB    1 
ATOM   9369  C  CB    B SER B 2 168 ? 25.295  -17.934 1.087   0.50 27.45 ? 168 SER B CB    1 
ATOM   9370  O  OG    A SER B 2 168 ? 24.066  -18.101 0.659   0.50 23.31 ? 168 SER B OG    1 
ATOM   9371  O  OG    B SER B 2 168 ? 24.024  -17.359 0.826   0.50 24.11 ? 168 SER B OG    1 
ATOM   9372  N  N     A VAL B 2 169 ? 27.203  -21.482 0.709   0.50 23.26 ? 169 VAL B N     1 
ATOM   9373  N  N     B VAL B 2 169 ? 27.072  -20.858 0.498   0.50 25.03 ? 169 VAL B N     1 
ATOM   9374  C  CA    A VAL B 2 169 ? 28.468  -22.156 0.974   0.50 25.42 ? 169 VAL B CA    1 
ATOM   9375  C  CA    B VAL B 2 169 ? 28.295  -21.624 0.705   0.50 25.11 ? 169 VAL B CA    1 
ATOM   9376  C  C     A VAL B 2 169 ? 29.614  -21.234 0.570   0.50 23.66 ? 169 VAL B C     1 
ATOM   9377  C  C     B VAL B 2 169 ? 29.478  -20.793 0.217   0.50 23.77 ? 169 VAL B C     1 
ATOM   9378  O  O     A VAL B 2 169 ? 29.707  -20.811 -0.588  0.50 25.30 ? 169 VAL B O     1 
ATOM   9379  O  O     B VAL B 2 169 ? 29.592  -20.490 -0.974  0.50 25.16 ? 169 VAL B O     1 
ATOM   9380  C  CB    A VAL B 2 169 ? 28.544  -23.499 0.233   0.50 27.40 ? 169 VAL B CB    1 
ATOM   9381  C  CB    B VAL B 2 169 ? 28.226  -22.981 -0.004  0.50 25.98 ? 169 VAL B CB    1 
ATOM   9382  C  CG1   A VAL B 2 169 ? 29.891  -24.156 0.458   0.50 24.91 ? 169 VAL B CG1   1 
ATOM   9383  C  CG1   B VAL B 2 169 ? 29.367  -23.877 0.443   0.50 25.53 ? 169 VAL B CG1   1 
ATOM   9384  C  CG2   A VAL B 2 169 ? 27.423  -24.423 0.700   0.50 25.18 ? 169 VAL B CG2   1 
ATOM   9385  C  CG2   B VAL B 2 169 ? 26.883  -23.643 0.274   0.50 27.32 ? 169 VAL B CG2   1 
ATOM   9386  N  N     A MET B 2 170 ? 30.486  -20.920 1.535   0.50 22.35 ? 170 MET B N     1 
ATOM   9387  N  N     B MET B 2 170 ? 30.369  -20.429 1.147   0.50 24.54 ? 170 MET B N     1 
ATOM   9388  C  CA    A MET B 2 170 ? 31.630  -20.039 1.338   0.50 26.89 ? 170 MET B CA    1 
ATOM   9389  C  CA    B MET B 2 170 ? 31.534  -19.603 0.858   0.50 21.85 ? 170 MET B CA    1 
ATOM   9390  C  C     A MET B 2 170 ? 32.810  -20.832 0.777   0.50 23.98 ? 170 MET B C     1 
ATOM   9391  C  C     B MET B 2 170 ? 32.697  -20.479 0.396   0.50 24.24 ? 170 MET B C     1 
ATOM   9392  O  O     A MET B 2 170 ? 33.095  -21.934 1.252   0.50 26.27 ? 170 MET B O     1 
ATOM   9393  O  O     B MET B 2 170 ? 32.854  -21.604 0.876   0.50 25.24 ? 170 MET B O     1 
ATOM   9394  C  CB    A MET B 2 170 ? 32.025  -19.382 2.661   0.50 25.58 ? 170 MET B CB    1 
ATOM   9395  C  CB    B MET B 2 170 ? 31.941  -18.813 2.100   0.50 28.28 ? 170 MET B CB    1 
ATOM   9396  C  CG    A MET B 2 170 ? 30.867  -18.705 3.389   0.50 23.42 ? 170 MET B CG    1 
ATOM   9397  C  CG    B MET B 2 170 ? 30.761  -18.322 2.922   0.50 25.50 ? 170 MET B CG    1 
ATOM   9398  S  SD    A MET B 2 170 ? 30.462  -17.087 2.702   0.50 35.86 ? 170 MET B SD    1 
ATOM   9399  S  SD    B MET B 2 170 ? 29.759  -17.134 2.013   0.50 38.73 ? 170 MET B SD    1 
ATOM   9400  C  CE    A MET B 2 170 ? 28.833  -16.801 3.395   0.50 28.90 ? 170 MET B CE    1 
ATOM   9401  C  CE    B MET B 2 170 ? 30.874  -15.734 1.950   0.50 30.81 ? 170 MET B CE    1 
ATOM   9402  N  N     A PRO B 2 171 ? 33.507  -20.302 -0.224  0.50 27.67 ? 171 PRO B N     1 
ATOM   9403  N  N     B PRO B 2 171 ? 33.522  -19.990 -0.527  0.50 27.05 ? 171 PRO B N     1 
ATOM   9404  C  CA    A PRO B 2 171 ? 34.577  -21.068 -0.870  0.50 27.77 ? 171 PRO B CA    1 
ATOM   9405  C  CA    B PRO B 2 171 ? 34.601  -20.816 -1.078  0.50 28.17 ? 171 PRO B CA    1 
ATOM   9406  C  C     A PRO B 2 171 ? 35.841  -21.134 -0.024  0.50 25.57 ? 171 PRO B C     1 
ATOM   9407  C  C     B PRO B 2 171 ? 35.824  -20.871 -0.172  0.50 26.11 ? 171 PRO B C     1 
ATOM   9408  O  O     A PRO B 2 171 ? 36.106  -20.288 0.832   0.50 25.31 ? 171 PRO B O     1 
ATOM   9409  O  O     B PRO B 2 171 ? 36.023  -20.043 0.719   0.50 26.10 ? 171 PRO B O     1 
ATOM   9410  C  CB    A PRO B 2 171 ? 34.832  -20.291 -2.167  0.50 26.94 ? 171 PRO B CB    1 
ATOM   9411  C  CB    B PRO B 2 171 ? 34.937  -20.112 -2.398  0.50 26.82 ? 171 PRO B CB    1 
ATOM   9412  C  CG    A PRO B 2 171 ? 34.454  -18.887 -1.835  0.50 26.63 ? 171 PRO B CG    1 
ATOM   9413  C  CG    B PRO B 2 171 ? 34.623  -18.677 -2.137  0.50 23.54 ? 171 PRO B CG    1 
ATOM   9414  C  CD    A PRO B 2 171 ? 33.282  -19.002 -0.883  0.50 21.69 ? 171 PRO B CD    1 
ATOM   9415  C  CD    B PRO B 2 171 ? 33.403  -18.699 -1.227  0.50 24.08 ? 171 PRO B CD    1 
ATOM   9416  N  N     A SER B 2 172 ? 36.638  -22.169 -0.295  0.50 28.65 ? 172 SER B N     1 
ATOM   9417  N  N     B SER B 2 172 ? 36.662  -21.876 -0.436  0.50 28.56 ? 172 SER B N     1 
ATOM   9418  C  CA    A SER B 2 172 ? 37.905  -22.343 0.382   0.50 27.02 ? 172 SER B CA    1 
ATOM   9419  C  CA    B SER B 2 172 ? 37.927  -22.049 0.263   0.50 27.80 ? 172 SER B CA    1 
ATOM   9420  C  C     A SER B 2 172 ? 38.898  -23.002 -0.564  0.50 28.68 ? 172 SER B C     1 
ATOM   9421  C  C     B SER B 2 172 ? 38.915  -22.743 -0.660  0.50 28.46 ? 172 SER B C     1 
ATOM   9422  O  O     A SER B 2 172 ? 38.534  -23.977 -1.242  0.50 28.35 ? 172 SER B O     1 
ATOM   9423  O  O     B SER B 2 172 ? 38.543  -23.717 -1.330  0.50 29.05 ? 172 SER B O     1 
ATOM   9424  C  CB    A SER B 2 172 ? 37.768  -23.187 1.642   0.50 30.14 ? 172 SER B CB    1 
ATOM   9425  C  CB    B SER B 2 172 ? 37.772  -22.867 1.543   0.50 29.34 ? 172 SER B CB    1 
ATOM   9426  O  OG    A SER B 2 172 ? 39.009  -23.290 2.320   0.50 30.12 ? 172 SER B OG    1 
ATOM   9427  O  OG    B SER B 2 172 ? 39.028  -23.068 2.169   0.50 29.79 ? 172 SER B OG    1 
ATOM   9428  N  N     A PRO B 2 173 ? 40.138  -22.511 -0.623  0.50 33.15 ? 173 PRO B N     1 
ATOM   9429  N  N     B PRO B 2 173 ? 40.167  -22.282 -0.706  0.50 33.34 ? 173 PRO B N     1 
ATOM   9430  C  CA    A PRO B 2 173 ? 41.162  -23.195 -1.431  0.50 32.25 ? 173 PRO B CA    1 
ATOM   9431  C  CA    B PRO B 2 173 ? 41.175  -22.969 -1.534  0.50 32.19 ? 173 PRO B CA    1 
ATOM   9432  C  C     A PRO B 2 173 ? 41.442  -24.618 -0.977  0.50 31.98 ? 173 PRO B C     1 
ATOM   9433  C  C     B PRO B 2 173 ? 41.441  -24.401 -1.104  0.50 32.13 ? 173 PRO B C     1 
ATOM   9434  O  O     A PRO B 2 173 ? 41.968  -25.413 -1.768  0.50 30.99 ? 173 PRO B O     1 
ATOM   9435  O  O     B PRO B 2 173 ? 41.934  -25.196 -1.918  0.50 30.99 ? 173 PRO B O     1 
ATOM   9436  C  CB    A PRO B 2 173 ? 42.400  -22.304 -1.259  0.50 35.08 ? 173 PRO B CB    1 
ATOM   9437  C  CB    B PRO B 2 173 ? 42.429  -22.097 -1.365  0.50 35.21 ? 173 PRO B CB    1 
ATOM   9438  C  CG    A PRO B 2 173 ? 41.873  -20.974 -0.831  0.50 33.82 ? 173 PRO B CG    1 
ATOM   9439  C  CG    B PRO B 2 173 ? 41.934  -20.778 -0.866  0.50 33.84 ? 173 PRO B CG    1 
ATOM   9440  C  CD    A PRO B 2 173 ? 40.633  -21.256 -0.033  0.50 29.41 ? 173 PRO B CD    1 
ATOM   9441  C  CD    B PRO B 2 173 ? 40.703  -21.073 -0.059  0.50 29.21 ? 173 PRO B CD    1 
ATOM   9442  N  N     A LYS B 2 174 ? 41.118  -24.962 0.273   0.50 29.53 ? 174 LYS B N     1 
ATOM   9443  N  N     B LYS B 2 174 ? 41.139  -24.755 0.148   0.50 29.56 ? 174 LYS B N     1 
ATOM   9444  C  CA    A LYS B 2 174 ? 41.355  -26.308 0.779   0.50 29.96 ? 174 LYS B CA    1 
ATOM   9445  C  CA    B LYS B 2 174 ? 41.391  -26.112 0.621   0.50 29.36 ? 174 LYS B CA    1 
ATOM   9446  C  C     A LYS B 2 174 ? 40.402  -27.327 0.173   0.50 33.48 ? 174 LYS B C     1 
ATOM   9447  C  C     B LYS B 2 174 ? 40.482  -27.123 -0.063  0.50 33.44 ? 174 LYS B C     1 
ATOM   9448  O  O     A LYS B 2 174 ? 40.655  -28.532 0.274   0.50 39.01 ? 174 LYS B O     1 
ATOM   9449  O  O     B LYS B 2 174 ? 40.887  -28.269 -0.284  0.50 38.69 ? 174 LYS B O     1 
ATOM   9450  C  CB    A LYS B 2 174 ? 41.228  -26.332 2.305   0.50 33.39 ? 174 LYS B CB    1 
ATOM   9451  C  CB    B LYS B 2 174 ? 41.207  -26.190 2.140   0.50 33.83 ? 174 LYS B CB    1 
ATOM   9452  C  CG    A LYS B 2 174 ? 42.151  -25.365 3.031   0.50 31.80 ? 174 LYS B CG    1 
ATOM   9453  C  CG    B LYS B 2 174 ? 42.128  -25.279 2.942   0.50 31.82 ? 174 LYS B CG    1 
ATOM   9454  C  CD    A LYS B 2 174 ? 41.977  -25.473 4.536   0.50 35.14 ? 174 LYS B CD    1 
ATOM   9455  C  CD    B LYS B 2 174 ? 42.019  -25.566 4.432   0.50 35.13 ? 174 LYS B CD    1 
ATOM   9456  C  CE    A LYS B 2 174 ? 42.832  -24.462 5.277   0.50 38.09 ? 174 LYS B CE    1 
ATOM   9457  C  CE    B LYS B 2 174 ? 42.841  -24.588 5.257   0.50 38.13 ? 174 LYS B CE    1 
ATOM   9458  N  NZ    A LYS B 2 174 ? 44.283  -24.723 5.114   0.50 33.26 ? 174 LYS B NZ    1 
ATOM   9459  N  NZ    B LYS B 2 174 ? 42.651  -24.806 6.722   0.50 35.95 ? 174 LYS B NZ    1 
ATOM   9460  N  N     A VAL B 2 175 ? 39.308  -26.873 -0.434  0.50 31.99 ? 175 VAL B N     1 
ATOM   9461  N  N     B VAL B 2 175 ? 39.263  -26.722 -0.410  0.50 31.80 ? 175 VAL B N     1 
ATOM   9462  C  CA    A VAL B 2 175 ? 38.390  -27.760 -1.126  0.50 35.42 ? 175 VAL B CA    1 
ATOM   9463  C  CA    B VAL B 2 175 ? 38.293  -27.642 -0.997  0.50 35.96 ? 175 VAL B CA    1 
ATOM   9464  C  C     A VAL B 2 175 ? 38.360  -27.494 -2.628  0.50 32.40 ? 175 VAL B C     1 
ATOM   9465  C  C     B VAL B 2 175 ? 38.327  -27.589 -2.517  0.50 32.31 ? 175 VAL B C     1 
ATOM   9466  O  O     A VAL B 2 175 ? 38.173  -28.434 -3.409  0.50 38.81 ? 175 VAL B O     1 
ATOM   9467  O  O     B VAL B 2 175 ? 38.410  -28.623 -3.184  0.50 39.52 ? 175 VAL B O     1 
ATOM   9468  C  CB    A VAL B 2 175 ? 36.973  -27.648 -0.521  0.50 34.44 ? 175 VAL B CB    1 
ATOM   9469  C  CB    B VAL B 2 175 ? 36.881  -27.333 -0.451  0.50 33.32 ? 175 VAL B CB    1 
ATOM   9470  C  CG1   A VAL B 2 175 ? 36.009  -28.616 -1.194  0.50 34.21 ? 175 VAL B CG1   1 
ATOM   9471  C  CG1   B VAL B 2 175 ? 35.852  -28.231 -1.114  0.50 34.02 ? 175 VAL B CG1   1 
ATOM   9472  C  CG2   A VAL B 2 175 ? 37.024  -27.899 0.983   0.50 30.59 ? 175 VAL B CG2   1 
ATOM   9473  C  CG2   B VAL B 2 175 ? 36.860  -27.504 1.063   0.50 30.77 ? 175 VAL B CG2   1 
ATOM   9474  N  N     A SER B 2 176 ? 38.564  -26.250 -3.054  0.50 36.44 ? 176 SER B N     1 
ATOM   9475  N  N     B SER B 2 176 ? 38.270  -26.390 -3.088  0.50 36.63 ? 176 SER B N     1 
ATOM   9476  C  CA    A SER B 2 176 ? 38.606  -25.894 -4.469  0.50 35.70 ? 176 SER B CA    1 
ATOM   9477  C  CA    B SER B 2 176 ? 38.237  -26.210 -4.531  0.50 38.47 ? 176 SER B CA    1 
ATOM   9478  C  C     A SER B 2 176 ? 39.648  -24.794 -4.626  0.50 39.41 ? 176 SER B C     1 
ATOM   9479  C  C     B SER B 2 176 ? 39.327  -25.232 -4.935  0.50 38.35 ? 176 SER B C     1 
ATOM   9480  O  O     A SER B 2 176 ? 39.399  -23.641 -4.259  0.50 37.33 ? 176 SER B O     1 
ATOM   9481  O  O     B SER B 2 176 ? 39.448  -24.153 -4.345  0.50 38.81 ? 176 SER B O     1 
ATOM   9482  C  CB    A SER B 2 176 ? 37.240  -25.443 -4.969  0.50 41.01 ? 176 SER B CB    1 
ATOM   9483  C  CB    B SER B 2 176 ? 36.867  -25.704 -4.991  0.50 40.84 ? 176 SER B CB    1 
ATOM   9484  O  OG    A SER B 2 176 ? 37.309  -24.963 -6.297  0.50 40.55 ? 176 SER B OG    1 
ATOM   9485  O  OG    B SER B 2 176 ? 36.841  -25.510 -6.392  0.50 39.03 ? 176 SER B OG    1 
ATOM   9486  N  N     A ASP B 2 177 ? 40.814  -25.150 -5.166  0.50 36.34 ? 177 ASP B N     1 
ATOM   9487  N  N     B ASP B 2 177 ? 40.117  -25.612 -5.939  0.50 41.01 ? 177 ASP B N     1 
ATOM   9488  C  CA    A ASP B 2 177 ? 41.872  -24.168 -5.404  0.50 39.18 ? 177 ASP B CA    1 
ATOM   9489  C  CA    B ASP B 2 177 ? 41.250  -24.809 -6.396  0.50 37.88 ? 177 ASP B CA    1 
ATOM   9490  C  C     A ASP B 2 177 ? 41.708  -23.582 -6.806  0.50 34.73 ? 177 ASP B C     1 
ATOM   9491  C  C     B ASP B 2 177 ? 40.850  -24.069 -7.670  0.50 39.31 ? 177 ASP B C     1 
ATOM   9492  O  O     A ASP B 2 177 ? 42.503  -23.810 -7.720  0.50 38.49 ? 177 ASP B O     1 
ATOM   9493  O  O     B ASP B 2 177 ? 41.182  -24.462 -8.790  0.50 47.49 ? 177 ASP B O     1 
ATOM   9494  C  CB    A ASP B 2 177 ? 43.245  -24.796 -5.209  0.50 35.71 ? 177 ASP B CB    1 
ATOM   9495  C  CB    B ASP B 2 177 ? 42.478  -25.690 -6.606  0.50 41.84 ? 177 ASP B CB    1 
ATOM   9496  C  CG    A ASP B 2 177 ? 44.340  -23.754 -5.086  0.50 31.65 ? 177 ASP B CG    1 
ATOM   9497  C  CG    B ASP B 2 177 ? 42.118  -27.101 -7.029  0.50 44.41 ? 177 ASP B CG    1 
ATOM   9498  O  OD1   A ASP B 2 177 ? 44.010  -22.552 -5.174  0.50 32.77 ? 177 ASP B OD1   1 
ATOM   9499  O  OD1   B ASP B 2 177 ? 41.173  -27.676 -6.444  0.50 41.57 ? 177 ASP B OD1   1 
ATOM   9500  O  OD2   A ASP B 2 177 ? 45.518  -24.134 -4.895  0.50 29.54 ? 177 ASP B OD2   1 
ATOM   9501  O  OD2   B ASP B 2 177 ? 42.782  -27.635 -7.942  0.50 38.12 ? 177 ASP B OD2   1 
ATOM   9502  N  N     A THR B 2 178 ? 40.637  -22.808 -6.956  0.50 39.26 ? 178 THR B N     1 
ATOM   9503  N  N     B THR B 2 178 ? 40.117  -22.973 -7.481  0.50 40.99 ? 178 THR B N     1 
ATOM   9504  C  CA    A THR B 2 178 ? 40.329  -22.094 -8.187  0.50 34.40 ? 178 THR B CA    1 
ATOM   9505  C  CA    B THR B 2 178 ? 39.712  -22.087 -8.569  0.50 34.92 ? 178 THR B CA    1 
ATOM   9506  C  C     A THR B 2 178 ? 40.280  -20.607 -7.871  0.50 38.67 ? 178 THR B C     1 
ATOM   9507  C  C     B THR B 2 178 ? 39.959  -20.664 -8.092  0.50 38.13 ? 178 THR B C     1 
ATOM   9508  O  O     A THR B 2 178 ? 39.605  -20.191 -6.923  0.50 32.80 ? 178 THR B O     1 
ATOM   9509  O  O     B THR B 2 178 ? 39.207  -20.149 -7.260  0.50 34.41 ? 178 THR B O     1 
ATOM   9510  C  CB    A THR B 2 178 ? 39.004  -22.571 -8.786  0.50 38.97 ? 178 THR B CB    1 
ATOM   9511  C  CB    B THR B 2 178 ? 38.245  -22.294 -8.949  0.50 35.98 ? 178 THR B CB    1 
ATOM   9512  O  OG1   A THR B 2 178 ? 38.969  -24.005 -8.778  0.50 36.08 ? 178 THR B OG1   1 
ATOM   9513  O  OG1   B THR B 2 178 ? 37.957  -23.696 -9.003  0.50 40.53 ? 178 THR B OG1   1 
ATOM   9514  C  CG2   A THR B 2 178 ? 38.861  -22.080 -10.215 0.50 36.33 ? 178 THR B CG2   1 
ATOM   9515  C  CG2   B THR B 2 178 ? 37.954  -21.679 -10.306 0.50 36.88 ? 178 THR B CG2   1 
ATOM   9516  N  N     A VAL B 2 179 ? 40.998  -19.808 -8.664  0.50 29.98 ? 179 VAL B N     1 
ATOM   9517  N  N     B VAL B 2 179 ? 41.012  -20.030 -8.614  0.50 30.14 ? 179 VAL B N     1 
ATOM   9518  C  CA    A VAL B 2 179 ? 41.284  -18.429 -8.274  0.50 32.28 ? 179 VAL B CA    1 
ATOM   9519  C  CA    B VAL B 2 179 ? 41.472  -18.767 -8.052  0.50 31.41 ? 179 VAL B CA    1 
ATOM   9520  C  C     A VAL B 2 179 ? 40.183  -17.442 -8.624  0.50 27.00 ? 179 VAL B C     1 
ATOM   9521  C  C     B VAL B 2 179 ? 40.480  -17.628 -8.255  0.50 26.88 ? 179 VAL B C     1 
ATOM   9522  O  O     A VAL B 2 179 ? 40.237  -16.294 -8.171  0.50 23.34 ? 179 VAL B O     1 
ATOM   9523  O  O     B VAL B 2 179 ? 40.598  -16.594 -7.592  0.50 25.74 ? 179 VAL B O     1 
ATOM   9524  C  CB    A VAL B 2 179 ? 42.604  -17.961 -8.915  0.50 27.63 ? 179 VAL B CB    1 
ATOM   9525  C  CB    B VAL B 2 179 ? 42.845  -18.389 -8.639  0.50 29.96 ? 179 VAL B CB    1 
ATOM   9526  C  CG1   A VAL B 2 179 ? 43.731  -18.912 -8.542  0.50 29.72 ? 179 VAL B CG1   1 
ATOM   9527  C  CG1   B VAL B 2 179 ? 43.956  -19.040 -7.835  0.50 25.92 ? 179 VAL B CG1   1 
ATOM   9528  C  CG2   A VAL B 2 179 ? 42.458  -17.872 -10.422 0.50 27.19 ? 179 VAL B CG2   1 
ATOM   9529  C  CG2   B VAL B 2 179 ? 42.930  -18.810 -10.093 0.50 21.32 ? 179 VAL B CG2   1 
ATOM   9530  N  N     A VAL B 2 180 ? 39.188  -17.836 -9.423  0.50 29.40 ? 180 VAL B N     1 
ATOM   9531  N  N     B VAL B 2 180 ? 39.508  -17.775 -9.154  0.50 30.04 ? 180 VAL B N     1 
ATOM   9532  C  CA    A VAL B 2 180 ? 38.113  -16.900 -9.753  0.50 29.55 ? 180 VAL B CA    1 
ATOM   9533  C  CA    B VAL B 2 180 ? 38.540  -16.708 -9.395  0.50 27.98 ? 180 VAL B CA    1 
ATOM   9534  C  C     A VAL B 2 180 ? 37.016  -16.869 -8.701  0.50 28.52 ? 180 VAL B C     1 
ATOM   9535  C  C     B VAL B 2 180 ? 37.362  -16.839 -8.435  0.50 27.33 ? 180 VAL B C     1 
ATOM   9536  O  O     A VAL B 2 180 ? 36.123  -16.014 -8.774  0.50 31.41 ? 180 VAL B O     1 
ATOM   9537  O  O     B VAL B 2 180 ? 36.378  -16.101 -8.542  0.50 30.40 ? 180 VAL B O     1 
ATOM   9538  C  CB    A VAL B 2 180 ? 37.503  -17.235 -11.126 0.50 32.11 ? 180 VAL B CB    1 
ATOM   9539  C  CB    B VAL B 2 180 ? 38.054  -16.710 -10.857 0.50 29.40 ? 180 VAL B CB    1 
ATOM   9540  C  CG1   A VAL B 2 180 ? 38.528  -16.999 -12.218 0.50 27.34 ? 180 VAL B CG1   1 
ATOM   9541  C  CG1   B VAL B 2 180 ? 39.158  -16.242 -11.793 0.50 23.46 ? 180 VAL B CG1   1 
ATOM   9542  C  CG2   A VAL B 2 180 ? 37.006  -18.675 -11.151 0.50 32.23 ? 180 VAL B CG2   1 
ATOM   9543  C  CG2   B VAL B 2 180 ? 37.563  -18.095 -11.251 0.50 33.36 ? 180 VAL B CG2   1 
ATOM   9544  N  N     A GLU B 2 181 ? 37.064  -17.760 -7.720  0.50 26.90 ? 181 GLU B N     1 
ATOM   9545  N  N     B GLU B 2 181 ? 37.443  -17.777 -7.499  0.50 26.04 ? 181 GLU B N     1 
ATOM   9546  C  CA    A GLU B 2 181 ? 36.027  -17.869 -6.702  0.50 30.00 ? 181 GLU B CA    1 
ATOM   9547  C  CA    B GLU B 2 181 ? 36.331  -17.985 -6.575  0.50 29.96 ? 181 GLU B CA    1 
ATOM   9548  C  C     A GLU B 2 181 ? 36.027  -16.699 -5.716  0.50 27.04 ? 181 GLU B C     1 
ATOM   9549  C  C     B GLU B 2 181 ? 36.132  -16.799 -5.630  0.50 27.11 ? 181 GLU B C     1 
ATOM   9550  O  O     A GLU B 2 181 ? 34.965  -16.369 -5.176  0.50 31.79 ? 181 GLU B O     1 
ATOM   9551  O  O     B GLU B 2 181 ? 34.981  -16.446 -5.349  0.50 31.54 ? 181 GLU B O     1 
ATOM   9552  C  CB    A GLU B 2 181 ? 36.167  -19.201 -5.962  0.50 30.38 ? 181 GLU B CB    1 
ATOM   9553  C  CB    B GLU B 2 181 ? 36.518  -19.283 -5.784  0.50 31.14 ? 181 GLU B CB    1 
ATOM   9554  C  CG    A GLU B 2 181 ? 36.266  -20.396 -6.902  0.50 35.16 ? 181 GLU B CG    1 
ATOM   9555  C  CG    B GLU B 2 181 ? 36.052  -20.519 -6.537  0.50 35.05 ? 181 GLU B CG    1 
ATOM   9556  C  CD    A GLU B 2 181 ? 35.630  -21.646 -6.334  0.50 33.84 ? 181 GLU B CD    1 
ATOM   9557  C  CD    B GLU B 2 181 ? 36.447  -21.809 -5.848  0.50 35.57 ? 181 GLU B CD    1 
ATOM   9558  O  OE1   A GLU B 2 181 ? 35.161  -21.603 -5.177  0.50 24.69 ? 181 GLU B OE1   1 
ATOM   9559  O  OE1   B GLU B 2 181 ? 37.108  -21.744 -4.791  0.50 36.91 ? 181 GLU B OE1   1 
ATOM   9560  O  OE2   A GLU B 2 181 ? 35.596  -22.668 -7.051  0.50 32.79 ? 181 GLU B OE2   1 
ATOM   9561  O  OE2   B GLU B 2 181 ? 36.099  -22.890 -6.371  0.50 33.15 ? 181 GLU B OE2   1 
ATOM   9562  N  N     A PRO B 2 182 ? 37.170  -16.060 -5.423  0.50 27.45 ? 182 PRO B N     1 
ATOM   9563  N  N     B PRO B 2 182 ? 37.190  -16.164 -5.108  0.50 27.85 ? 182 PRO B N     1 
ATOM   9564  C  CA    A PRO B 2 182 ? 37.096  -14.795 -4.670  0.50 25.30 ? 182 PRO B CA    1 
ATOM   9565  C  CA    B PRO B 2 182 ? 36.962  -14.929 -4.338  0.50 25.66 ? 182 PRO B CA    1 
ATOM   9566  C  C     A PRO B 2 182 ? 36.273  -13.726 -5.366  0.50 28.28 ? 182 PRO B C     1 
ATOM   9567  C  C     B PRO B 2 182 ? 36.302  -13.826 -5.144  0.50 28.06 ? 182 PRO B C     1 
ATOM   9568  O  O     A PRO B 2 182 ? 35.467  -13.051 -4.710  0.50 25.42 ? 182 PRO B O     1 
ATOM   9569  O  O     B PRO B 2 182 ? 35.594  -12.992 -4.563  0.50 25.31 ? 182 PRO B O     1 
ATOM   9570  C  CB    A PRO B 2 182 ? 38.567  -14.388 -4.535  0.50 28.65 ? 182 PRO B CB    1 
ATOM   9571  C  CB    B PRO B 2 182 ? 38.373  -14.537 -3.882  0.50 28.57 ? 182 PRO B CB    1 
ATOM   9572  C  CG    A PRO B 2 182 ? 39.289  -15.674 -4.498  0.50 26.86 ? 182 PRO B CG    1 
ATOM   9573  C  CG    B PRO B 2 182 ? 39.092  -15.831 -3.793  0.50 28.22 ? 182 PRO B CG    1 
ATOM   9574  C  CD    A PRO B 2 182 ? 38.548  -16.593 -5.433  0.50 30.09 ? 182 PRO B CD    1 
ATOM   9575  C  CD    B PRO B 2 182 ? 38.575  -16.647 -4.943  0.50 29.97 ? 182 PRO B CD    1 
ATOM   9576  N  N     A TYR B 2 183 ? 36.464  -13.542 -6.676  0.50 23.82 ? 183 TYR B N     1 
ATOM   9577  N  N     B TYR B 2 183 ? 36.517  -13.789 -6.461  0.50 24.16 ? 183 TYR B N     1 
ATOM   9578  C  CA    A TYR B 2 183 ? 35.617  -12.623 -7.432  0.50 25.39 ? 183 TYR B CA    1 
ATOM   9579  C  CA    B TYR B 2 183 ? 35.772  -12.871 -7.317  0.50 25.31 ? 183 TYR B CA    1 
ATOM   9580  C  C     A TYR B 2 183 ? 34.145  -12.982 -7.273  0.50 26.17 ? 183 TYR B C     1 
ATOM   9581  C  C     B TYR B 2 183 ? 34.271  -13.090 -7.171  0.50 26.22 ? 183 TYR B C     1 
ATOM   9582  O  O     A TYR B 2 183 ? 33.307  -12.117 -7.003  0.50 25.61 ? 183 TYR B O     1 
ATOM   9583  O  O     B TYR B 2 183 ? 33.527  -12.178 -6.797  0.50 25.45 ? 183 TYR B O     1 
ATOM   9584  C  CB    A TYR B 2 183 ? 35.985  -12.645 -8.918  0.50 25.34 ? 183 TYR B CB    1 
ATOM   9585  C  CB    B TYR B 2 183 ? 36.178  -13.056 -8.782  0.50 27.27 ? 183 TYR B CB    1 
ATOM   9586  C  CG    A TYR B 2 183 ? 37.330  -12.062 -9.308  0.50 25.75 ? 183 TYR B CG    1 
ATOM   9587  C  CG    B TYR B 2 183 ? 37.491  -12.435 -9.209  0.50 24.97 ? 183 TYR B CG    1 
ATOM   9588  C  CD1   A TYR B 2 183 ? 38.074  -11.291 -8.427  0.50 25.86 ? 183 TYR B CD1   1 
ATOM   9589  C  CD1   B TYR B 2 183 ? 38.020  -11.334 -8.551  0.50 25.72 ? 183 TYR B CD1   1 
ATOM   9590  C  CD2   A TYR B 2 183 ? 37.842  -12.276 -10.585 0.50 26.11 ? 183 TYR B CD2   1 
ATOM   9591  C  CD2   B TYR B 2 183 ? 38.183  -12.938 -10.307 0.50 25.44 ? 183 TYR B CD2   1 
ATOM   9592  C  CE1   A TYR B 2 183 ? 39.300  -10.762 -8.806  0.50 27.26 ? 183 TYR B CE1   1 
ATOM   9593  C  CE1   B TYR B 2 183 ? 39.217  -10.767 -8.961  0.50 27.36 ? 183 TYR B CE1   1 
ATOM   9594  C  CE2   A TYR B 2 183 ? 39.054  -11.754 -10.972 0.50 29.25 ? 183 TYR B CE2   1 
ATOM   9595  C  CE2   B TYR B 2 183 ? 39.372  -12.381 -10.724 0.50 27.29 ? 183 TYR B CE2   1 
ATOM   9596  C  CZ    A TYR B 2 183 ? 39.780  -10.997 -10.083 0.50 32.05 ? 183 TYR B CZ    1 
ATOM   9597  C  CZ    B TYR B 2 183 ? 39.886  -11.296 -10.050 0.50 31.86 ? 183 TYR B CZ    1 
ATOM   9598  O  OH    A TYR B 2 183 ? 40.991  -10.481 -10.482 0.50 28.75 ? 183 TYR B OH    1 
ATOM   9599  O  OH    B TYR B 2 183 ? 41.073  -10.744 -10.471 0.50 28.90 ? 183 TYR B OH    1 
ATOM   9600  N  N     A ASN B 2 184 ? 33.815  -14.263 -7.450  0.50 27.19 ? 184 ASN B N     1 
ATOM   9601  N  N     B ASN B 2 184 ? 33.810  -14.308 -7.470  0.50 27.20 ? 184 ASN B N     1 
ATOM   9602  C  CA    A ASN B 2 184 ? 32.415  -14.670 -7.477  0.50 27.61 ? 184 ASN B CA    1 
ATOM   9603  C  CA    B ASN B 2 184 ? 32.377  -14.576 -7.505  0.50 27.57 ? 184 ASN B CA    1 
ATOM   9604  C  C     A ASN B 2 184 ? 31.778  -14.567 -6.097  0.50 28.29 ? 184 ASN B C     1 
ATOM   9605  C  C     B ASN B 2 184 ? 31.737  -14.409 -6.134  0.50 28.24 ? 184 ASN B C     1 
ATOM   9606  O  O     A ASN B 2 184 ? 30.603  -14.203 -5.979  0.50 29.57 ? 184 ASN B O     1 
ATOM   9607  O  O     B ASN B 2 184 ? 30.582  -13.980 -6.038  0.50 29.48 ? 184 ASN B O     1 
ATOM   9608  C  CB    A ASN B 2 184 ? 32.293  -16.094 -8.020  0.50 28.01 ? 184 ASN B CB    1 
ATOM   9609  C  CB    B ASN B 2 184 ? 32.118  -15.987 -8.038  0.50 28.00 ? 184 ASN B CB    1 
ATOM   9610  C  CG    A ASN B 2 184 ? 32.797  -16.221 -9.451  0.50 29.98 ? 184 ASN B CG    1 
ATOM   9611  C  CG    B ASN B 2 184 ? 32.696  -16.209 -9.429  0.50 30.05 ? 184 ASN B CG    1 
ATOM   9612  O  OD1   A ASN B 2 184 ? 32.962  -15.225 -10.159 0.50 28.72 ? 184 ASN B OD1   1 
ATOM   9613  O  OD1   B ASN B 2 184 ? 32.740  -15.297 -10.257 0.50 27.97 ? 184 ASN B OD1   1 
ATOM   9614  N  ND2   A ASN B 2 184 ? 33.034  -17.451 -9.882  0.50 27.82 ? 184 ASN B ND2   1 
ATOM   9615  N  ND2   B ASN B 2 184 ? 33.140  -17.432 -9.688  0.50 27.68 ? 184 ASN B ND2   1 
ATOM   9616  N  N     A ALA B 2 185 ? 32.533  -14.887 -5.044  0.50 27.95 ? 185 ALA B N     1 
ATOM   9617  N  N     B ALA B 2 185 ? 32.464  -14.747 -5.065  0.50 28.07 ? 185 ALA B N     1 
ATOM   9618  C  CA    A ALA B 2 185 ? 32.012  -14.741 -3.689  0.50 25.27 ? 185 ALA B CA    1 
ATOM   9619  C  CA    B ALA B 2 185 ? 31.908  -14.625 -3.721  0.50 25.39 ? 185 ALA B CA    1 
ATOM   9620  C  C     A ALA B 2 185 ? 31.773  -13.275 -3.348  0.50 30.86 ? 185 ALA B C     1 
ATOM   9621  C  C     B ALA B 2 185 ? 31.734  -13.167 -3.318  0.50 30.95 ? 185 ALA B C     1 
ATOM   9622  O  O     A ALA B 2 185 ? 30.724  -12.918 -2.799  0.50 28.25 ? 185 ALA B O     1 
ATOM   9623  O  O     B ALA B 2 185 ? 30.750  -12.812 -2.656  0.50 27.94 ? 185 ALA B O     1 
ATOM   9624  C  CB    A ALA B 2 185 ? 32.972  -15.377 -2.688  0.50 29.22 ? 185 ALA B CB    1 
ATOM   9625  C  CB    B ALA B 2 185 ? 32.802  -15.354 -2.721  0.50 28.94 ? 185 ALA B CB    1 
ATOM   9626  N  N     A THR B 2 186 ? 32.738  -12.410 -3.670  0.50 30.79 ? 186 THR B N     1 
ATOM   9627  N  N     B THR B 2 186 ? 32.679  -12.307 -3.705  0.50 30.83 ? 186 THR B N     1 
ATOM   9628  C  CA    A THR B 2 186 ? 32.599  -10.990 -3.359  0.50 26.04 ? 186 THR B CA    1 
ATOM   9629  C  CA    B THR B 2 186 ? 32.606  -10.904 -3.310  0.50 26.03 ? 186 THR B CA    1 
ATOM   9630  C  C     A THR B 2 186 ? 31.443  -10.369 -4.133  0.50 29.95 ? 186 THR B C     1 
ATOM   9631  C  C     B THR B 2 186 ? 31.491  -10.176 -4.050  0.50 29.85 ? 186 THR B C     1 
ATOM   9632  O  O     A THR B 2 186 ? 30.646  -9.606  -3.576  0.50 28.31 ? 186 THR B O     1 
ATOM   9633  O  O     B THR B 2 186 ? 30.777  -9.359  -3.459  0.50 28.66 ? 186 THR B O     1 
ATOM   9634  C  CB    A THR B 2 186 ? 33.906  -10.255 -3.659  0.50 31.45 ? 186 THR B CB    1 
ATOM   9635  C  CB    B THR B 2 186 ? 33.950  -10.219 -3.558  0.50 31.47 ? 186 THR B CB    1 
ATOM   9636  O  OG1   A THR B 2 186 ? 34.941  -10.749 -2.799  0.50 27.17 ? 186 THR B OG1   1 
ATOM   9637  O  OG1   B THR B 2 186 ? 34.967  -10.870 -2.789  0.50 27.16 ? 186 THR B OG1   1 
ATOM   9638  C  CG2   A THR B 2 186 ? 33.742  -8.756  -3.439  0.50 28.05 ? 186 THR B CG2   1 
ATOM   9639  C  CG2   B THR B 2 186 ? 33.885  -8.750  -3.161  0.50 27.69 ? 186 THR B CG2   1 
ATOM   9640  N  N     A LEU B 2 187 ? 31.344  -10.676 -5.431  0.50 28.92 ? 187 LEU B N     1 
ATOM   9641  N  N     B LEU B 2 187 ? 31.332  -10.454 -5.346  0.50 28.73 ? 187 LEU B N     1 
ATOM   9642  C  CA    A LEU B 2 187 ? 30.182  -10.242 -6.200  0.50 26.97 ? 187 LEU B CA    1 
ATOM   9643  C  CA    B LEU B 2 187 ? 30.264  -9.818  -6.111  0.50 24.35 ? 187 LEU B CA    1 
ATOM   9644  C  C     A LEU B 2 187 ? 28.890  -10.802 -5.616  0.50 23.61 ? 187 LEU B C     1 
ATOM   9645  C  C     B LEU B 2 187 ? 28.890  -10.186 -5.557  0.50 25.54 ? 187 LEU B C     1 
ATOM   9646  O  O     A LEU B 2 187 ? 27.846  -10.148 -5.688  0.50 27.17 ? 187 LEU B O     1 
ATOM   9647  O  O     B LEU B 2 187 ? 27.972  -9.360  -5.562  0.50 28.36 ? 187 LEU B O     1 
ATOM   9648  C  CB    A LEU B 2 187 ? 30.336  -10.660 -7.664  0.50 25.41 ? 187 LEU B CB    1 
ATOM   9649  C  CB    B LEU B 2 187 ? 30.382  -10.205 -7.585  0.50 27.44 ? 187 LEU B CB    1 
ATOM   9650  C  CG    A LEU B 2 187 ? 31.403  -9.898  -8.456  0.50 25.64 ? 187 LEU B CG    1 
ATOM   9651  C  CG    B LEU B 2 187 ? 31.744  -9.840  -8.188  0.50 23.47 ? 187 LEU B CG    1 
ATOM   9652  C  CD1   A LEU B 2 187 ? 31.623  -10.531 -9.826  0.50 26.30 ? 187 LEU B CD1   1 
ATOM   9653  C  CD1   B LEU B 2 187 ? 31.824  -10.207 -9.662  0.50 27.27 ? 187 LEU B CD1   1 
ATOM   9654  C  CD2   A LEU B 2 187 ? 31.007  -8.441  -8.598  0.50 25.33 ? 187 LEU B CD2   1 
ATOM   9655  C  CD2   B LEU B 2 187 ? 32.030  -8.364  -7.977  0.50 27.40 ? 187 LEU B CD2   1 
ATOM   9656  N  N     A SER B 2 188 ? 28.942  -11.998 -5.022  0.50 25.99 ? 188 SER B N     1 
ATOM   9657  N  N     B SER B 2 188 ? 28.735  -11.414 -5.055  0.50 23.76 ? 188 SER B N     1 
ATOM   9658  C  CA    A SER B 2 188 ? 27.740  -12.607 -4.460  0.50 28.56 ? 188 SER B CA    1 
ATOM   9659  C  CA    B SER B 2 188 ? 27.446  -11.828 -4.505  0.50 29.86 ? 188 SER B CA    1 
ATOM   9660  C  C     A SER B 2 188 ? 27.421  -12.054 -3.077  0.50 26.11 ? 188 SER B C     1 
ATOM   9661  C  C     B SER B 2 188 ? 27.175  -11.150 -3.169  0.50 27.06 ? 188 SER B C     1 
ATOM   9662  O  O     A SER B 2 188 ? 26.247  -11.892 -2.732  0.50 28.46 ? 188 SER B O     1 
ATOM   9663  O  O     B SER B 2 188 ? 26.065  -10.663 -2.928  0.50 23.42 ? 188 SER B O     1 
ATOM   9664  C  CB    A SER B 2 188 ? 27.894  -14.129 -4.403  0.50 31.52 ? 188 SER B CB    1 
ATOM   9665  C  CB    B SER B 2 188 ? 27.391  -13.348 -4.356  0.50 28.56 ? 188 SER B CB    1 
ATOM   9666  O  OG    A SER B 2 188 ? 28.108  -14.666 -5.700  0.50 29.85 ? 188 SER B OG    1 
ATOM   9667  O  OG    B SER B 2 188 ? 27.061  -13.963 -5.589  0.50 29.61 ? 188 SER B OG    1 
ATOM   9668  N  N     A VAL B 2 189 ? 28.446  -11.764 -2.273  0.50 30.45 ? 189 VAL B N     1 
ATOM   9669  N  N     B VAL B 2 189 ? 28.180  -11.106 -2.289  0.50 28.53 ? 189 VAL B N     1 
ATOM   9670  C  CA    A VAL B 2 189 ? 28.209  -11.187 -0.952  0.50 31.73 ? 189 VAL B CA    1 
ATOM   9671  C  CA    B VAL B 2 189 ? 28.004  -10.478 -0.980  0.50 33.04 ? 189 VAL B CA    1 
ATOM   9672  C  C     A VAL B 2 189 ? 27.637  -9.781  -1.086  0.50 30.50 ? 189 VAL B C     1 
ATOM   9673  C  C     B VAL B 2 189 ? 27.528  -9.039  -1.139  0.50 29.08 ? 189 VAL B C     1 
ATOM   9674  O  O     A VAL B 2 189 ? 26.790  -9.360  -0.290  0.50 27.79 ? 189 VAL B O     1 
ATOM   9675  O  O     B VAL B 2 189 ? 26.710  -8.548  -0.352  0.50 27.20 ? 189 VAL B O     1 
ATOM   9676  C  CB    A VAL B 2 189 ? 29.507  -11.208 -0.122  0.50 26.81 ? 189 VAL B CB    1 
ATOM   9677  C  CB    B VAL B 2 189 ? 29.311  -10.571 -0.170  0.50 27.25 ? 189 VAL B CB    1 
ATOM   9678  C  CG1   A VAL B 2 189 ? 29.355  -10.392 1.150   0.50 28.13 ? 189 VAL B CG1   1 
ATOM   9679  C  CG1   B VAL B 2 189 ? 29.262  -9.662  1.049   0.50 28.89 ? 189 VAL B CG1   1 
ATOM   9680  C  CG2   A VAL B 2 189 ? 29.893  -12.638 0.217   0.50 26.70 ? 189 VAL B CG2   1 
ATOM   9681  C  CG2   B VAL B 2 189 ? 29.561  -12.009 0.252   0.50 26.05 ? 189 VAL B CG2   1 
ATOM   9682  N  N     A HIS B 2 190 ? 28.077  -9.041  -2.105  0.50 26.19 ? 190 HIS B N     1 
ATOM   9683  N  N     B HIS B 2 190 ? 28.011  -8.354  -2.177  0.50 28.39 ? 190 HIS B N     1 
ATOM   9684  C  CA    A HIS B 2 190 ? 27.496  -7.733  -2.397  0.50 29.83 ? 190 HIS B CA    1 
ATOM   9685  C  CA    B HIS B 2 190 ? 27.511  -7.022  -2.502  0.50 29.24 ? 190 HIS B CA    1 
ATOM   9686  C  C     A HIS B 2 190 ? 25.991  -7.832  -2.615  0.50 30.21 ? 190 HIS B C     1 
ATOM   9687  C  C     B HIS B 2 190 ? 26.008  -7.031  -2.758  0.50 33.72 ? 190 HIS B C     1 
ATOM   9688  O  O     A HIS B 2 190 ? 25.228  -6.990  -2.124  0.50 32.54 ? 190 HIS B O     1 
ATOM   9689  O  O     B HIS B 2 190 ? 25.324  -6.039  -2.478  0.50 38.14 ? 190 HIS B O     1 
ATOM   9690  C  CB    A HIS B 2 190 ? 28.183  -7.135  -3.627  0.50 29.18 ? 190 HIS B CB    1 
ATOM   9691  C  CB    B HIS B 2 190 ? 28.263  -6.481  -3.721  0.50 31.49 ? 190 HIS B CB    1 
ATOM   9692  C  CG    A HIS B 2 190 ? 27.658  -5.794  -4.035  0.50 36.57 ? 190 HIS B CG    1 
ATOM   9693  C  CG    B HIS B 2 190 ? 27.931  -5.063  -4.065  0.50 35.03 ? 190 HIS B CG    1 
ATOM   9694  N  ND1   A HIS B 2 190 ? 27.183  -4.870  -3.131  0.50 35.45 ? 190 HIS B ND1   1 
ATOM   9695  N  ND1   B HIS B 2 190 ? 27.915  -4.051  -3.129  0.50 36.06 ? 190 HIS B ND1   1 
ATOM   9696  C  CD2   A HIS B 2 190 ? 27.552  -5.214  -5.255  0.50 35.81 ? 190 HIS B CD2   1 
ATOM   9697  C  CD2   B HIS B 2 190 ? 27.618  -4.484  -5.248  0.50 35.52 ? 190 HIS B CD2   1 
ATOM   9698  C  CE1   A HIS B 2 190 ? 26.796  -3.783  -3.775  0.50 36.72 ? 190 HIS B CE1   1 
ATOM   9699  C  CE1   B HIS B 2 190 ? 27.598  -2.912  -3.718  0.50 37.86 ? 190 HIS B CE1   1 
ATOM   9700  N  NE2   A HIS B 2 190 ? 27.011  -3.966  -5.066  0.50 37.84 ? 190 HIS B NE2   1 
ATOM   9701  N  NE2   B HIS B 2 190 ? 27.412  -3.147  -5.005  0.50 37.31 ? 190 HIS B NE2   1 
ATOM   9702  N  N     A GLN B 2 191 ? 25.544  -8.862  -3.340  0.50 24.04 ? 191 GLN B N     1 
ATOM   9703  N  N     B GLN B 2 191 ? 25.472  -8.136  -3.285  0.50 25.97 ? 191 GLN B N     1 
ATOM   9704  C  CA    A GLN B 2 191 ? 24.119  -9.010  -3.619  0.50 26.68 ? 191 GLN B CA    1 
ATOM   9705  C  CA    B GLN B 2 191 ? 24.027  -8.247  -3.453  0.50 29.80 ? 191 GLN B CA    1 
ATOM   9706  C  C     A GLN B 2 191 ? 23.353  -9.468  -2.383  0.50 27.87 ? 191 GLN B C     1 
ATOM   9707  C  C     B GLN B 2 191 ? 23.345  -8.741  -2.180  0.50 28.46 ? 191 GLN B C     1 
ATOM   9708  O  O     A GLN B 2 191 ? 22.245  -8.984  -2.124  0.50 30.39 ? 191 GLN B O     1 
ATOM   9709  O  O     B GLN B 2 191 ? 22.270  -8.243  -1.827  0.50 27.60 ? 191 GLN B O     1 
ATOM   9710  C  CB    A GLN B 2 191 ? 23.905  -9.990  -4.773  0.50 27.73 ? 191 GLN B CB    1 
ATOM   9711  C  CB    B GLN B 2 191 ? 23.698  -9.176  -4.623  0.50 28.71 ? 191 GLN B CB    1 
ATOM   9712  C  CG    A GLN B 2 191 ? 24.616  -9.607  -6.068  0.50 29.62 ? 191 GLN B CG    1 
ATOM   9713  C  CG    B GLN B 2 191 ? 24.193  -8.684  -5.983  0.50 29.29 ? 191 GLN B CG    1 
ATOM   9714  C  CD    A GLN B 2 191 ? 23.933  -8.474  -6.814  0.50 33.58 ? 191 GLN B CD    1 
ATOM   9715  C  CD    B GLN B 2 191 ? 23.295  -7.617  -6.597  0.50 33.34 ? 191 GLN B CD    1 
ATOM   9716  O  OE1   A GLN B 2 191 ? 22.739  -8.229  -6.641  0.50 37.16 ? 191 GLN B OE1   1 
ATOM   9717  O  OE1   B GLN B 2 191 ? 22.129  -7.871  -6.902  0.50 38.04 ? 191 GLN B OE1   1 
ATOM   9718  N  NE2   A GLN B 2 191 ? 24.692  -7.774  -7.655  0.50 39.59 ? 191 GLN B NE2   1 
ATOM   9719  N  NE2   B GLN B 2 191 ? 23.836  -6.417  -6.777  0.50 33.29 ? 191 GLN B NE2   1 
ATOM   9720  N  N     A LEU B 2 192 ? 23.926  -10.399 -1.609  0.50 28.04 ? 192 LEU B N     1 
ATOM   9721  N  N     B LEU B 2 192 ? 23.955  -9.706  -1.476  0.50 26.34 ? 192 LEU B N     1 
ATOM   9722  C  CA    A LEU B 2 192 ? 23.240  -10.922 -0.427  0.50 24.51 ? 192 LEU B CA    1 
ATOM   9723  C  CA    B LEU B 2 192 ? 23.307  -10.315 -0.312  0.50 24.83 ? 192 LEU B CA    1 
ATOM   9724  C  C     A LEU B 2 192 ? 23.062  -9.858  0.649   0.50 28.04 ? 192 LEU B C     1 
ATOM   9725  C  C     B LEU B 2 192 ? 23.132  -9.327  0.833   0.50 29.18 ? 192 LEU B C     1 
ATOM   9726  O  O     A LEU B 2 192 ? 22.146  -9.960  1.476   0.50 25.39 ? 192 LEU B O     1 
ATOM   9727  O  O     B LEU B 2 192 ? 22.197  -9.466  1.635   0.50 25.50 ? 192 LEU B O     1 
ATOM   9728  C  CB    A LEU B 2 192 ? 24.009  -12.111 0.155   0.50 27.49 ? 192 LEU B CB    1 
ATOM   9729  C  CB    B LEU B 2 192 ? 24.110  -11.520 0.176   0.50 27.51 ? 192 LEU B CB    1 
ATOM   9730  C  CG    A LEU B 2 192 ? 24.069  -13.439 -0.605  0.50 24.39 ? 192 LEU B CG    1 
ATOM   9731  C  CG    B LEU B 2 192 ? 24.364  -12.653 -0.818  0.50 23.13 ? 192 LEU B CG    1 
ATOM   9732  C  CD1   A LEU B 2 192 ? 25.039  -14.385 0.090   0.50 28.52 ? 192 LEU B CD1   1 
ATOM   9733  C  CD1   B LEU B 2 192 ? 24.970  -13.844 -0.097  0.50 29.88 ? 192 LEU B CD1   1 
ATOM   9734  C  CD2   A LEU B 2 192 ? 22.692  -14.081 -0.702  0.50 21.43 ? 192 LEU B CD2   1 
ATOM   9735  C  CD2   B LEU B 2 192 ? 23.072  -13.036 -1.516  0.50 25.39 ? 192 LEU B CD2   1 
ATOM   9736  N  N     A VAL B 2 193 ? 23.941  -8.855  0.675   0.50 25.98 ? 193 VAL B N     1 
ATOM   9737  N  N     B VAL B 2 193 ? 24.037  -8.354  0.949   0.50 28.69 ? 193 VAL B N     1 
ATOM   9738  C  CA    A VAL B 2 193 ? 23.827  -7.790  1.666   0.50 31.23 ? 193 VAL B CA    1 
ATOM   9739  C  CA    B VAL B 2 193 ? 23.890  -7.311  1.960   0.50 29.26 ? 193 VAL B CA    1 
ATOM   9740  C  C     A VAL B 2 193 ? 22.553  -6.984  1.443   0.50 34.07 ? 193 VAL B C     1 
ATOM   9741  C  C     B VAL B 2 193 ? 22.566  -6.581  1.779   0.50 34.66 ? 193 VAL B C     1 
ATOM   9742  O  O     A VAL B 2 193 ? 21.851  -6.625  2.399   0.50 36.79 ? 193 VAL B O     1 
ATOM   9743  O  O     B VAL B 2 193 ? 21.905  -6.201  2.754   0.50 33.41 ? 193 VAL B O     1 
ATOM   9744  C  CB    A VAL B 2 193 ? 25.081  -6.896  1.624   0.50 32.77 ? 193 VAL B CB    1 
ATOM   9745  C  CB    B VAL B 2 193 ? 25.090  -6.346  1.893   0.50 33.90 ? 193 VAL B CB    1 
ATOM   9746  C  CG1   A VAL B 2 193 ? 24.806  -5.567  2.295   0.50 33.33 ? 193 VAL B CG1   1 
ATOM   9747  C  CG1   B VAL B 2 193 ? 24.767  -5.023  2.563   0.50 35.59 ? 193 VAL B CG1   1 
ATOM   9748  C  CG2   A VAL B 2 193 ? 26.253  -7.595  2.291   0.50 30.10 ? 193 VAL B CG2   1 
ATOM   9749  C  CG2   B VAL B 2 193 ? 26.315  -6.985  2.525   0.50 32.15 ? 193 VAL B CG2   1 
ATOM   9750  N  N     A GLU B 2 194 ? 22.217  -6.715  0.183   0.50 34.24 ? 194 GLU B N     1 
ATOM   9751  N  N     B GLU B 2 194 ? 22.135  -6.414  0.530   0.50 36.22 ? 194 GLU B N     1 
ATOM   9752  C  CA    A GLU B 2 194 ? 21.085  -5.852  -0.133  0.50 34.00 ? 194 GLU B CA    1 
ATOM   9753  C  CA    B GLU B 2 194 ? 20.953  -5.607  0.258   0.50 34.37 ? 194 GLU B CA    1 
ATOM   9754  C  C     A GLU B 2 194 ? 19.764  -6.599  -0.252  0.50 34.77 ? 194 GLU B C     1 
ATOM   9755  C  C     B GLU B 2 194 ? 19.666  -6.418  0.359   0.50 35.68 ? 194 GLU B C     1 
ATOM   9756  O  O     A GLU B 2 194 ? 18.714  -6.029  0.067   0.50 36.43 ? 194 GLU B O     1 
ATOM   9757  O  O     B GLU B 2 194 ? 18.713  -5.996  1.025   0.50 39.43 ? 194 GLU B O     1 
ATOM   9758  C  CB    A GLU B 2 194 ? 21.343  -5.104  -1.445  0.50 35.42 ? 194 GLU B CB    1 
ATOM   9759  C  CB    B GLU B 2 194 ? 21.067  -4.959  -1.124  0.50 34.51 ? 194 GLU B CB    1 
ATOM   9760  C  CG    A GLU B 2 194 ? 22.758  -4.566  -1.605  0.50 40.18 ? 194 GLU B CG    1 
ATOM   9761  C  CG    B GLU B 2 194 ? 22.307  -4.098  -1.312  0.50 42.16 ? 194 GLU B CG    1 
ATOM   9762  C  CD    A GLU B 2 194 ? 23.045  -3.373  -0.712  0.50 45.51 ? 194 GLU B CD    1 
ATOM   9763  C  CD    B GLU B 2 194 ? 22.290  -2.843  -0.456  0.50 47.85 ? 194 GLU B CD    1 
ATOM   9764  O  OE1   A GLU B 2 194 ? 22.080  -2.725  -0.248  0.50 48.29 ? 194 GLU B OE1   1 
ATOM   9765  O  OE1   B GLU B 2 194 ? 21.192  -2.295  -0.223  0.50 44.63 ? 194 GLU B OE1   1 
ATOM   9766  O  OE2   A GLU B 2 194 ? 24.238  -3.085  -0.474  0.50 40.73 ? 194 GLU B OE2   1 
ATOM   9767  O  OE2   B GLU B 2 194 ? 23.377  -2.408  -0.016  0.50 45.88 ? 194 GLU B OE2   1 
ATOM   9768  N  N     A ASN B 2 195 ? 19.781  -7.858  -0.698  0.50 30.75 ? 195 ASN B N     1 
ATOM   9769  N  N     B ASN B 2 195 ? 19.614  -7.586  -0.287  0.50 31.21 ? 195 ASN B N     1 
ATOM   9770  C  CA    A ASN B 2 195 ? 18.573  -8.496  -1.203  0.50 36.15 ? 195 ASN B CA    1 
ATOM   9771  C  CA    B ASN B 2 195 ? 18.337  -8.202  -0.636  0.50 34.48 ? 195 ASN B CA    1 
ATOM   9772  C  C     A ASN B 2 195 ? 17.970  -9.558  -0.296  0.50 33.77 ? 195 ASN B C     1 
ATOM   9773  C  C     B ASN B 2 195 ? 18.100  -9.557  0.026   0.50 34.00 ? 195 ASN B C     1 
ATOM   9774  O  O     A ASN B 2 195 ? 16.807  -9.918  -0.497  0.50 35.52 ? 195 ASN B O     1 
ATOM   9775  O  O     B ASN B 2 195 ? 17.327  -10.363 -0.500  0.50 33.78 ? 195 ASN B O     1 
ATOM   9776  C  CB    A ASN B 2 195 ? 18.844  -9.127  -2.576  0.50 35.71 ? 195 ASN B CB    1 
ATOM   9777  C  CB    B ASN B 2 195 ? 18.231  -8.343  -2.154  0.50 36.25 ? 195 ASN B CB    1 
ATOM   9778  C  CG    A ASN B 2 195 ? 18.830  -8.109  -3.693  0.50 40.59 ? 195 ASN B CG    1 
ATOM   9779  C  CG    B ASN B 2 195 ? 18.808  -7.154  -2.885  0.50 34.15 ? 195 ASN B CG    1 
ATOM   9780  O  OD1   A ASN B 2 195 ? 19.802  -7.967  -4.434  0.50 39.03 ? 195 ASN B OD1   1 
ATOM   9781  O  OD1   B ASN B 2 195 ? 19.944  -7.195  -3.364  0.50 37.19 ? 195 ASN B OD1   1 
ATOM   9782  N  ND2   A ASN B 2 195 ? 17.720  -7.392  -3.822  0.50 34.73 ? 195 ASN B ND2   1 
ATOM   9783  N  ND2   B ASN B 2 195 ? 18.034  -6.079  -2.966  0.50 30.30 ? 195 ASN B ND2   1 
ATOM   9784  N  N     A THR B 2 196 ? 18.710  -10.075 0.678   0.50 31.47 ? 196 THR B N     1 
ATOM   9785  N  N     B THR B 2 196 ? 18.742  -9.841  1.155   0.50 28.95 ? 196 THR B N     1 
ATOM   9786  C  CA    A THR B 2 196 ? 18.181  -11.100 1.562   0.50 26.48 ? 196 THR B CA    1 
ATOM   9787  C  CA    B THR B 2 196 ? 18.411  -11.030 1.927   0.50 27.73 ? 196 THR B CA    1 
ATOM   9788  C  C     A THR B 2 196 ? 17.942  -10.526 2.952   0.50 26.66 ? 196 THR B C     1 
ATOM   9789  C  C     B THR B 2 196 ? 18.213  -10.631 3.380   0.50 27.23 ? 196 THR B C     1 
ATOM   9790  O  O     A THR B 2 196 ? 18.474  -9.477  3.320   0.50 23.79 ? 196 THR B O     1 
ATOM   9791  O  O     B THR B 2 196 ? 18.931  -9.771  3.899   0.50 24.12 ? 196 THR B O     1 
ATOM   9792  C  CB    A THR B 2 196 ? 19.126  -12.303 1.651   0.50 28.66 ? 196 THR B CB    1 
ATOM   9793  C  CB    B THR B 2 196 ? 19.492  -12.124 1.832   0.50 29.74 ? 196 THR B CB    1 
ATOM   9794  O  OG1   A THR B 2 196 ? 20.352  -11.905 2.277   0.50 33.13 ? 196 THR B OG1   1 
ATOM   9795  O  OG1   B THR B 2 196 ? 20.502  -11.902 2.826   0.50 31.99 ? 196 THR B OG1   1 
ATOM   9796  C  CG2   A THR B 2 196 ? 19.420  -12.848 0.263   0.50 28.12 ? 196 THR B CG2   1 
ATOM   9797  C  CG2   B THR B 2 196 ? 20.129  -12.140 0.447   0.50 30.91 ? 196 THR B CG2   1 
ATOM   9798  N  N     A ASP B 2 197 ? 17.111  -11.227 3.722   0.50 28.68 ? 197 ASP B N     1 
ATOM   9799  N  N     B ASP B 2 197 ? 17.225  -11.250 4.028   0.50 29.27 ? 197 ASP B N     1 
ATOM   9800  C  CA    A ASP B 2 197 ? 16.826  -10.823 5.089   0.50 27.70 ? 197 ASP B CA    1 
ATOM   9801  C  CA    B ASP B 2 197 ? 16.942  -10.957 5.427   0.50 28.24 ? 197 ASP B CA    1 
ATOM   9802  C  C     A ASP B 2 197 ? 17.622  -11.605 6.121   0.50 28.88 ? 197 ASP B C     1 
ATOM   9803  C  C     B ASP B 2 197 ? 17.785  -11.792 6.375   0.50 28.85 ? 197 ASP B C     1 
ATOM   9804  O  O     A ASP B 2 197 ? 17.816  -11.107 7.235   0.50 25.71 ? 197 ASP B O     1 
ATOM   9805  O  O     B ASP B 2 197 ? 18.168  -11.312 7.447   0.50 26.89 ? 197 ASP B O     1 
ATOM   9806  C  CB    A ASP B 2 197 ? 15.325  -10.970 5.378   0.50 29.00 ? 197 ASP B CB    1 
ATOM   9807  C  CB    B ASP B 2 197 ? 15.457  -11.185 5.725   0.50 26.80 ? 197 ASP B CB    1 
ATOM   9808  C  CG    A ASP B 2 197 ? 14.469  -10.255 4.348   0.50 30.22 ? 197 ASP B CG    1 
ATOM   9809  C  CG    B ASP B 2 197 ? 14.567  -10.205 4.994   0.50 26.67 ? 197 ASP B CG    1 
ATOM   9810  O  OD1   A ASP B 2 197 ? 14.511  -9.007  4.301   0.50 26.00 ? 197 ASP B OD1   1 
ATOM   9811  O  OD1   B ASP B 2 197 ? 14.663  -8.996  5.279   0.50 29.52 ? 197 ASP B OD1   1 
ATOM   9812  O  OD2   A ASP B 2 197 ? 13.788  -10.944 3.556   0.50 31.36 ? 197 ASP B OD2   1 
ATOM   9813  O  OD2   B ASP B 2 197 ? 13.798  -10.639 4.108   0.50 35.06 ? 197 ASP B OD2   1 
ATOM   9814  N  N     A GLU B 2 198 ? 18.087  -12.804 5.777   0.50 28.09 ? 198 GLU B N     1 
ATOM   9815  N  N     B GLU B 2 198 ? 18.054  -13.045 6.013   0.50 28.33 ? 198 GLU B N     1 
ATOM   9816  C  CA    A GLU B 2 198 ? 18.874  -13.628 6.688   0.50 29.13 ? 198 GLU B CA    1 
ATOM   9817  C  CA    B GLU B 2 198 ? 18.831  -13.960 6.839   0.50 29.14 ? 198 GLU B CA    1 
ATOM   9818  C  C     A GLU B 2 198 ? 19.608  -14.682 5.873   0.50 26.22 ? 198 GLU B C     1 
ATOM   9819  C  C     B GLU B 2 198 ? 19.713  -14.798 5.933   0.50 26.09 ? 198 GLU B C     1 
ATOM   9820  O  O     A GLU B 2 198 ? 19.000  -15.345 5.029   0.50 24.33 ? 198 GLU B O     1 
ATOM   9821  O  O     B GLU B 2 198 ? 19.244  -15.308 4.913   0.50 24.28 ? 198 GLU B O     1 
ATOM   9822  C  CB    A GLU B 2 198 ? 17.977  -14.276 7.755   0.50 30.93 ? 198 GLU B CB    1 
ATOM   9823  C  CB    B GLU B 2 198 ? 17.926  -14.879 7.670   0.50 29.10 ? 198 GLU B CB    1 
ATOM   9824  C  CG    A GLU B 2 198 ? 16.631  -14.752 7.230   0.50 31.09 ? 198 GLU B CG    1 
ATOM   9825  C  CG    B GLU B 2 198 ? 16.578  -14.279 8.027   0.50 22.93 ? 198 GLU B CG    1 
ATOM   9826  C  CD    A GLU B 2 198 ? 15.620  -15.005 8.332   0.50 29.27 ? 198 GLU B CD    1 
ATOM   9827  C  CD    B GLU B 2 198 ? 15.729  -15.211 8.855   0.50 32.53 ? 198 GLU B CD    1 
ATOM   9828  O  OE1   A GLU B 2 198 ? 15.719  -14.370 9.407   0.50 28.41 ? 198 GLU B OE1   1 
ATOM   9829  O  OE1   B GLU B 2 198 ? 16.277  -15.849 9.780   0.50 33.58 ? 198 GLU B OE1   1 
ATOM   9830  O  OE2   A GLU B 2 198 ? 14.723  -15.848 8.127   0.50 31.64 ? 198 GLU B OE2   1 
ATOM   9831  O  OE2   B GLU B 2 198 ? 14.516  -15.307 8.577   0.50 31.07 ? 198 GLU B OE2   1 
ATOM   9832  N  N     A THR B 2 199 ? 20.911  -14.826 6.116   0.50 27.65 ? 199 THR B N     1 
ATOM   9833  N  N     B THR B 2 199 ? 20.982  -14.944 6.303   0.50 27.30 ? 199 THR B N     1 
ATOM   9834  C  CA    A THR B 2 199 ? 21.753  -15.743 5.354   0.50 24.18 ? 199 THR B CA    1 
ATOM   9835  C  CA    B THR B 2 199 ? 21.921  -15.761 5.543   0.50 24.19 ? 199 THR B CA    1 
ATOM   9836  C  C     A THR B 2 199 ? 22.578  -16.590 6.310   0.50 23.44 ? 199 THR B C     1 
ATOM   9837  C  C     B THR B 2 199 ? 22.672  -16.665 6.503   0.50 23.84 ? 199 THR B C     1 
ATOM   9838  O  O     A THR B 2 199 ? 23.265  -16.053 7.184   0.50 27.31 ? 199 THR B O     1 
ATOM   9839  O  O     B THR B 2 199 ? 23.344  -16.181 7.420   0.50 27.12 ? 199 THR B O     1 
ATOM   9840  C  CB    A THR B 2 199 ? 22.683  -14.986 4.395   0.50 24.21 ? 199 THR B CB    1 
ATOM   9841  C  CB    B THR B 2 199 ? 22.904  -14.900 4.745   0.50 24.89 ? 199 THR B CB    1 
ATOM   9842  O  OG1   A THR B 2 199 ? 21.917  -14.414 3.329   0.50 25.69 ? 199 THR B OG1   1 
ATOM   9843  O  OG1   B THR B 2 199 ? 22.195  -14.161 3.746   0.50 23.27 ? 199 THR B OG1   1 
ATOM   9844  C  CG2   A THR B 2 199 ? 23.737  -15.926 3.808   0.50 26.14 ? 199 THR B CG2   1 
ATOM   9845  C  CG2   B THR B 2 199 ? 23.952  -15.782 4.061   0.50 26.85 ? 199 THR B CG2   1 
ATOM   9846  N  N     A TYR B 2 200 ? 22.503  -17.910 6.146   0.50 21.45 ? 200 TYR B N     1 
ATOM   9847  N  N     B TYR B 2 200 ? 22.544  -17.973 6.302   0.50 21.26 ? 200 TYR B N     1 
ATOM   9848  C  CA    A TYR B 2 200 ? 23.348  -18.823 6.903   0.50 23.53 ? 200 TYR B CA    1 
ATOM   9849  C  CA    B TYR B 2 200 ? 23.363  -18.953 7.008   0.50 23.49 ? 200 TYR B CA    1 
ATOM   9850  C  C     A TYR B 2 200 ? 24.693  -18.981 6.201   0.50 22.93 ? 200 TYR B C     1 
ATOM   9851  C  C     B TYR B 2 200 ? 24.656  -19.114 6.220   0.50 22.96 ? 200 TYR B C     1 
ATOM   9852  O  O     A TYR B 2 200 ? 24.746  -19.176 4.983   0.50 23.54 ? 200 TYR B O     1 
ATOM   9853  O  O     B TYR B 2 200 ? 24.706  -19.838 5.223   0.50 25.11 ? 200 TYR B O     1 
ATOM   9854  C  CB    A TYR B 2 200 ? 22.666  -20.182 7.055   0.50 24.96 ? 200 TYR B CB    1 
ATOM   9855  C  CB    B TYR B 2 200 ? 22.623  -20.275 7.159   0.50 25.10 ? 200 TYR B CB    1 
ATOM   9856  C  CG    A TYR B 2 200 ? 21.426  -20.151 7.922   0.50 25.04 ? 200 TYR B CG    1 
ATOM   9857  C  CG    B TYR B 2 200 ? 21.464  -20.209 8.127   0.50 24.93 ? 200 TYR B CG    1 
ATOM   9858  C  CD1   A TYR B 2 200 ? 21.521  -19.939 9.291   0.50 25.81 ? 200 TYR B CD1   1 
ATOM   9859  C  CD1   B TYR B 2 200 ? 21.680  -20.244 9.497   0.50 26.33 ? 200 TYR B CD1   1 
ATOM   9860  C  CD2   A TYR B 2 200 ? 20.162  -20.334 7.374   0.50 30.62 ? 200 TYR B CD2   1 
ATOM   9861  C  CD2   B TYR B 2 200 ? 20.157  -20.101 7.672   0.50 30.94 ? 200 TYR B CD2   1 
ATOM   9862  C  CE1   A TYR B 2 200 ? 20.392  -19.908 10.092  0.50 25.73 ? 200 TYR B CE1   1 
ATOM   9863  C  CE1   B TYR B 2 200 ? 20.623  -20.181 10.388  0.50 26.00 ? 200 TYR B CE1   1 
ATOM   9864  C  CE2   A TYR B 2 200 ? 19.025  -20.307 8.169   0.50 27.92 ? 200 TYR B CE2   1 
ATOM   9865  C  CE2   B TYR B 2 200 ? 19.092  -20.041 8.556   0.50 27.82 ? 200 TYR B CE2   1 
ATOM   9866  C  CZ    A TYR B 2 200 ? 19.150  -20.094 9.525   0.50 24.68 ? 200 TYR B CZ    1 
ATOM   9867  C  CZ    B TYR B 2 200 ? 19.334  -20.080 9.911   0.50 25.39 ? 200 TYR B CZ    1 
ATOM   9868  O  OH    A TYR B 2 200 ? 18.029  -20.063 10.320  0.50 26.81 ? 200 TYR B OH    1 
ATOM   9869  O  OH    B TYR B 2 200 ? 18.284  -20.019 10.801  0.50 26.74 ? 200 TYR B OH    1 
ATOM   9870  N  N     A CYS B 2 201 ? 25.779  -18.901 6.975   0.50 25.47 ? 201 CYS B N     1 
ATOM   9871  N  N     B CYS B 2 201 ? 25.703  -18.419 6.657   0.50 25.17 ? 201 CYS B N     1 
ATOM   9872  C  CA    A CYS B 2 201 ? 27.145  -18.947 6.447   0.50 25.91 ? 201 CYS B CA    1 
ATOM   9873  C  CA    B CYS B 2 201 ? 26.997  -18.487 5.987   0.50 23.83 ? 201 CYS B CA    1 
ATOM   9874  C  C     A CYS B 2 201 ? 27.733  -20.329 6.712   0.50 26.47 ? 201 CYS B C     1 
ATOM   9875  C  C     B CYS B 2 201 ? 27.638  -19.841 6.258   0.50 25.87 ? 201 CYS B C     1 
ATOM   9876  O  O     A CYS B 2 201 ? 28.127  -20.639 7.840   0.50 28.89 ? 201 CYS B O     1 
ATOM   9877  O  O     B CYS B 2 201 ? 28.116  -20.098 7.369   0.50 27.91 ? 201 CYS B O     1 
ATOM   9878  C  CB    A CYS B 2 201 ? 28.009  -17.861 7.079   0.50 20.76 ? 201 CYS B CB    1 
ATOM   9879  C  CB    B CYS B 2 201 ? 27.896  -17.351 6.461   0.50 26.33 ? 201 CYS B CB    1 
ATOM   9880  S  SG    A CYS B 2 201 ? 27.533  -16.179 6.656   0.50 29.61 ? 201 CYS B SG    1 
ATOM   9881  S  SG    B CYS B 2 201 ? 27.500  -15.756 5.719   0.50 31.76 ? 201 CYS B SG    1 
ATOM   9882  N  N     A ILE B 2 202 ? 27.821  -21.146 5.663   0.50 22.62 ? 202 ILE B N     1 
ATOM   9883  N  N     B ILE B 2 202 ? 27.641  -20.710 5.247   0.50 23.20 ? 202 ILE B N     1 
ATOM   9884  C  CA    A ILE B 2 202 ? 28.353  -22.499 5.751   0.50 19.66 ? 202 ILE B CA    1 
ATOM   9885  C  CA    B ILE B 2 202 ? 28.241  -22.033 5.340   0.50 18.71 ? 202 ILE B CA    1 
ATOM   9886  C  C     A ILE B 2 202 ? 29.649  -22.519 4.947   0.50 23.00 ? 202 ILE B C     1 
ATOM   9887  C  C     B ILE B 2 202 ? 29.599  -21.971 4.657   0.50 23.00 ? 202 ILE B C     1 
ATOM   9888  O  O     A ILE B 2 202 ? 29.631  -22.645 3.721   0.50 20.83 ? 202 ILE B O     1 
ATOM   9889  O  O     B ILE B 2 202 ? 29.693  -21.564 3.495   0.50 22.99 ? 202 ILE B O     1 
ATOM   9890  C  CB    A ILE B 2 202 ? 27.349  -23.542 5.245   0.50 24.13 ? 202 ILE B CB    1 
ATOM   9891  C  CB    B ILE B 2 202 ? 27.339  -23.101 4.699   0.50 21.34 ? 202 ILE B CB    1 
ATOM   9892  C  CG1   A ILE B 2 202 ? 26.093  -23.531 6.123   0.50 23.54 ? 202 ILE B CG1   1 
ATOM   9893  C  CG1   B ILE B 2 202 ? 26.002  -23.177 5.438   0.50 27.45 ? 202 ILE B CG1   1 
ATOM   9894  C  CG2   A ILE B 2 202 ? 27.974  -24.926 5.243   0.50 24.99 ? 202 ILE B CG2   1 
ATOM   9895  C  CG2   B ILE B 2 202 ? 28.028  -24.457 4.709   0.50 25.92 ? 202 ILE B CG2   1 
ATOM   9896  C  CD1   A ILE B 2 202 ? 25.128  -24.650 5.821   0.50 27.80 ? 202 ILE B CD1   1 
ATOM   9897  C  CD1   B ILE B 2 202 ? 25.052  -24.220 4.889   0.50 29.56 ? 202 ILE B CD1   1 
ATOM   9898  N  N     A ASP B 2 203 ? 30.776  -22.397 5.642   0.50 22.02 ? 203 ASP B N     1 
ATOM   9899  N  N     B ASP B 2 203 ? 30.649  -22.364 5.379   0.50 21.52 ? 203 ASP B N     1 
ATOM   9900  C  CA    A ASP B 2 203 ? 32.076  -22.165 5.021   0.50 23.88 ? 203 ASP B CA    1 
ATOM   9901  C  CA    B ASP B 2 203 ? 32.034  -22.080 5.007   0.50 23.89 ? 203 ASP B CA    1 
ATOM   9902  C  C     A ASP B 2 203 ? 32.764  -23.496 4.731   0.50 26.65 ? 203 ASP B C     1 
ATOM   9903  C  C     B ASP B 2 203 ? 32.765  -23.390 4.737   0.50 26.69 ? 203 ASP B C     1 
ATOM   9904  O  O     A ASP B 2 203 ? 32.972  -24.305 5.641   0.50 27.85 ? 203 ASP B O     1 
ATOM   9905  O  O     B ASP B 2 203 ? 33.005  -24.175 5.660   0.50 27.76 ? 203 ASP B O     1 
ATOM   9906  C  CB    A ASP B 2 203 ? 32.925  -21.292 5.946   0.50 27.27 ? 203 ASP B CB    1 
ATOM   9907  C  CB    B ASP B 2 203 ? 32.720  -21.288 6.121   0.50 27.75 ? 203 ASP B CB    1 
ATOM   9908  C  CG    A ASP B 2 203 ? 34.356  -21.127 5.476   0.50 26.09 ? 203 ASP B CG    1 
ATOM   9909  C  CG    B ASP B 2 203 ? 34.029  -20.669 5.686   0.50 26.75 ? 203 ASP B CG    1 
ATOM   9910  O  OD1   A ASP B 2 203 ? 34.656  -21.397 4.295   0.50 25.60 ? 203 ASP B OD1   1 
ATOM   9911  O  OD1   B ASP B 2 203 ? 34.413  -20.837 4.510   0.50 26.08 ? 203 ASP B OD1   1 
ATOM   9912  O  OD2   A ASP B 2 203 ? 35.186  -20.710 6.310   0.50 28.55 ? 203 ASP B OD2   1 
ATOM   9913  O  OD2   B ASP B 2 203 ? 34.665  -20.002 6.529   0.50 22.04 ? 203 ASP B OD2   1 
ATOM   9914  N  N     A ASN B 2 204 ? 33.140  -23.711 3.468   0.50 22.90 ? 204 ASN B N     1 
ATOM   9915  N  N     B ASN B 2 204 ? 33.144  -23.614 3.477   0.50 22.87 ? 204 ASN B N     1 
ATOM   9916  C  CA    A ASN B 2 204 ? 33.861  -24.931 3.114   0.50 27.56 ? 204 ASN B CA    1 
ATOM   9917  C  CA    B ASN B 2 204 ? 33.853  -24.844 3.132   0.50 27.58 ? 204 ASN B CA    1 
ATOM   9918  C  C     A ASN B 2 204 ? 35.199  -25.027 3.836   0.50 30.19 ? 204 ASN B C     1 
ATOM   9919  C  C     B ASN B 2 204 ? 35.203  -24.939 3.832   0.50 30.17 ? 204 ASN B C     1 
ATOM   9920  O  O     A ASN B 2 204 ? 35.703  -26.135 4.061   0.50 27.57 ? 204 ASN B O     1 
ATOM   9921  O  O     B ASN B 2 204 ? 35.697  -26.049 4.073   0.50 27.63 ? 204 ASN B O     1 
ATOM   9922  C  CB    A ASN B 2 204 ? 34.069  -25.006 1.600   0.50 26.37 ? 204 ASN B CB    1 
ATOM   9923  C  CB    B ASN B 2 204 ? 34.029  -24.947 1.617   0.50 26.36 ? 204 ASN B CB    1 
ATOM   9924  C  CG    A ASN B 2 204 ? 32.922  -25.698 0.889   0.50 31.07 ? 204 ASN B CG    1 
ATOM   9925  C  CG    B ASN B 2 204 ? 32.924  -25.750 0.959   0.50 31.10 ? 204 ASN B CG    1 
ATOM   9926  O  OD1   A ASN B 2 204 ? 32.066  -26.312 1.527   0.50 29.46 ? 204 ASN B OD1   1 
ATOM   9927  O  OD1   B ASN B 2 204 ? 32.141  -26.416 1.639   0.50 29.24 ? 204 ASN B OD1   1 
ATOM   9928  N  ND2   A ASN B 2 204 ? 32.908  -25.617 -0.438  0.50 30.61 ? 204 ASN B ND2   1 
ATOM   9929  N  ND2   B ASN B 2 204 ? 32.867  -25.710 -0.369  0.50 30.60 ? 204 ASN B ND2   1 
ATOM   9930  N  N     A GLU B 2 205 ? 35.792  -23.887 4.199   0.50 29.06 ? 205 GLU B N     1 
ATOM   9931  N  N     B GLU B 2 205 ? 35.819  -23.800 4.159   0.50 29.02 ? 205 GLU B N     1 
ATOM   9932  C  CA    A GLU B 2 205 ? 37.017  -23.910 4.994   0.50 29.89 ? 205 GLU B CA    1 
ATOM   9933  C  CA    B GLU B 2 205 ? 37.052  -23.833 4.942   0.50 29.93 ? 205 GLU B CA    1 
ATOM   9934  C  C     A GLU B 2 205 ? 36.769  -24.552 6.353   0.50 31.24 ? 205 GLU B C     1 
ATOM   9935  C  C     B GLU B 2 205 ? 36.808  -24.461 6.308   0.50 31.25 ? 205 GLU B C     1 
ATOM   9936  O  O     A GLU B 2 205 ? 37.548  -25.399 6.804   0.50 31.39 ? 205 GLU B O     1 
ATOM   9937  O  O     B GLU B 2 205 ? 37.590  -25.302 6.766   0.50 31.36 ? 205 GLU B O     1 
ATOM   9938  C  CB    A GLU B 2 205 ? 37.563  -22.491 5.156   0.50 26.16 ? 205 GLU B CB    1 
ATOM   9939  C  CB    B GLU B 2 205 ? 37.625  -22.421 5.088   0.50 26.14 ? 205 GLU B CB    1 
ATOM   9940  C  CG    A GLU B 2 205 ? 38.779  -22.383 6.063   0.50 32.29 ? 205 GLU B CG    1 
ATOM   9941  C  CG    B GLU B 2 205 ? 38.887  -22.343 5.940   0.50 32.65 ? 205 GLU B CG    1 
ATOM   9942  C  CD    A GLU B 2 205 ? 40.066  -22.139 5.292   0.50 31.69 ? 205 GLU B CD    1 
ATOM   9943  C  CD    B GLU B 2 205 ? 40.079  -21.770 5.184   0.50 32.19 ? 205 GLU B CD    1 
ATOM   9944  O  OE1   A GLU B 2 205 ? 40.038  -22.179 4.045   0.50 29.14 ? 205 GLU B OE1   1 
ATOM   9945  O  OE1   B GLU B 2 205 ? 39.961  -21.528 3.967   0.50 25.94 ? 205 GLU B OE1   1 
ATOM   9946  O  OE2   A GLU B 2 205 ? 41.103  -21.889 5.937   0.50 40.47 ? 205 GLU B OE2   1 
ATOM   9947  O  OE2   B GLU B 2 205 ? 41.134  -21.552 5.813   0.50 39.55 ? 205 GLU B OE2   1 
ATOM   9948  N  N     A ALA B 2 206 ? 35.681  -24.158 7.019   0.50 25.74 ? 206 ALA B N     1 
ATOM   9949  N  N     B ALA B 2 206 ? 35.716  -24.070 6.970   0.50 25.74 ? 206 ALA B N     1 
ATOM   9950  C  CA    A ALA B 2 206 ? 35.333  -24.767 8.298   0.50 30.63 ? 206 ALA B CA    1 
ATOM   9951  C  CA    B ALA B 2 206 ? 35.384  -24.649 8.267   0.50 30.62 ? 206 ALA B CA    1 
ATOM   9952  C  C     A ALA B 2 206 ? 34.965  -26.236 8.129   0.50 29.97 ? 206 ALA B C     1 
ATOM   9953  C  C     B ALA B 2 206 ? 34.999  -26.118 8.139   0.50 30.09 ? 206 ALA B C     1 
ATOM   9954  O  O     A ALA B 2 206 ? 35.340  -27.075 8.957   0.50 31.93 ? 206 ALA B O     1 
ATOM   9955  O  O     B ALA B 2 206 ? 35.360  -26.937 8.993   0.50 32.06 ? 206 ALA B O     1 
ATOM   9956  C  CB    A ALA B 2 206 ? 34.186  -23.998 8.951   0.50 31.69 ? 206 ALA B CB    1 
ATOM   9957  C  CB    B ALA B 2 206 ? 34.255  -23.852 8.921   0.50 31.70 ? 206 ALA B CB    1 
ATOM   9958  N  N     A LEU B 2 207 ? 34.236  -26.567 7.062   0.50 26.33 ? 207 LEU B N     1 
ATOM   9959  N  N     B LEU B 2 207 ? 34.273  -26.473 7.079   0.50 26.30 ? 207 LEU B N     1 
ATOM   9960  C  CA    A LEU B 2 207 ? 33.852  -27.957 6.844   0.50 29.92 ? 207 LEU B CA    1 
ATOM   9961  C  CA    B LEU B 2 207 ? 33.840  -27.857 6.918   0.50 29.89 ? 207 LEU B CA    1 
ATOM   9962  C  C     A LEU B 2 207 ? 35.075  -28.833 6.600   0.50 30.99 ? 207 LEU B C     1 
ATOM   9963  C  C     B LEU B 2 207 ? 35.030  -28.779 6.679   0.50 31.03 ? 207 LEU B C     1 
ATOM   9964  O  O     A LEU B 2 207 ? 35.147  -29.964 7.095   0.50 32.04 ? 207 LEU B O     1 
ATOM   9965  O  O     B LEU B 2 207 ? 35.141  -29.842 7.303   0.50 31.88 ? 207 LEU B O     1 
ATOM   9966  C  CB    A LEU B 2 207 ? 32.876  -28.054 5.674   0.50 28.75 ? 207 LEU B CB    1 
ATOM   9967  C  CB    B LEU B 2 207 ? 32.833  -27.961 5.776   0.50 28.63 ? 207 LEU B CB    1 
ATOM   9968  C  CG    A LEU B 2 207 ? 31.566  -27.278 5.821   0.50 29.25 ? 207 LEU B CG    1 
ATOM   9969  C  CG    B LEU B 2 207 ? 31.550  -27.146 5.947   0.50 29.24 ? 207 LEU B CG    1 
ATOM   9970  C  CD1   A LEU B 2 207 ? 30.744  -27.404 4.555   0.50 28.80 ? 207 LEU B CD1   1 
ATOM   9971  C  CD1   B LEU B 2 207 ? 30.687  -27.266 4.709   0.50 28.71 ? 207 LEU B CD1   1 
ATOM   9972  C  CD2   A LEU B 2 207 ? 30.780  -27.766 7.026   0.50 33.57 ? 207 LEU B CD2   1 
ATOM   9973  C  CD2   B LEU B 2 207 ? 30.785  -27.587 7.190   0.50 33.18 ? 207 LEU B CD2   1 
ATOM   9974  N  N     A TYR B 2 208 ? 36.051  -28.324 5.845   0.50 30.45 ? 208 TYR B N     1 
ATOM   9975  N  N     B TYR B 2 208 ? 35.935  -28.385 5.780   0.50 30.36 ? 208 TYR B N     1 
ATOM   9976  C  CA    A TYR B 2 208 ? 37.284  -29.076 5.632   0.50 33.66 ? 208 TYR B CA    1 
ATOM   9977  C  CA    B TYR B 2 208 ? 37.147  -29.172 5.571   0.50 33.87 ? 208 TYR B CA    1 
ATOM   9978  C  C     A TYR B 2 208 ? 38.029  -29.280 6.944   0.50 32.47 ? 208 TYR B C     1 
ATOM   9979  C  C     B TYR B 2 208 ? 37.970  -29.255 6.849   0.50 32.43 ? 208 TYR B C     1 
ATOM   9980  O  O     A TYR B 2 208 ? 38.437  -30.400 7.271   0.50 35.97 ? 208 TYR B O     1 
ATOM   9981  O  O     B TYR B 2 208 ? 38.544  -30.304 7.160   0.50 36.18 ? 208 TYR B O     1 
ATOM   9982  C  CB    A TYR B 2 208 ? 38.173  -28.359 4.615   0.50 34.53 ? 208 TYR B CB    1 
ATOM   9983  C  CB    B TYR B 2 208 ? 37.976  -28.574 4.435   0.50 34.21 ? 208 TYR B CB    1 
ATOM   9984  C  CG    A TYR B 2 208 ? 39.521  -29.022 4.411   0.50 35.05 ? 208 TYR B CG    1 
ATOM   9985  C  CG    B TYR B 2 208 ? 39.227  -29.365 4.115   0.50 34.96 ? 208 TYR B CG    1 
ATOM   9986  C  CD1   A TYR B 2 208 ? 40.626  -28.645 5.165   0.50 37.29 ? 208 TYR B CD1   1 
ATOM   9987  C  CD1   B TYR B 2 208 ? 39.175  -30.470 3.276   0.50 38.09 ? 208 TYR B CD1   1 
ATOM   9988  C  CD2   A TYR B 2 208 ? 39.687  -30.024 3.465   0.50 37.55 ? 208 TYR B CD2   1 
ATOM   9989  C  CD2   B TYR B 2 208 ? 40.457  -29.006 4.649   0.50 36.88 ? 208 TYR B CD2   1 
ATOM   9990  C  CE1   A TYR B 2 208 ? 41.857  -29.249 4.984   0.50 38.56 ? 208 TYR B CE1   1 
ATOM   9991  C  CE1   B TYR B 2 208 ? 40.312  -31.198 2.979   0.50 39.83 ? 208 TYR B CE1   1 
ATOM   9992  C  CE2   A TYR B 2 208 ? 40.915  -30.631 3.274   0.50 39.66 ? 208 TYR B CE2   1 
ATOM   9993  C  CE2   B TYR B 2 208 ? 41.601  -29.728 4.358   0.50 38.51 ? 208 TYR B CE2   1 
ATOM   9994  C  CZ    A TYR B 2 208 ? 41.996  -30.240 4.036   0.50 39.46 ? 208 TYR B CZ    1 
ATOM   9995  C  CZ    B TYR B 2 208 ? 41.522  -30.822 3.522   0.50 39.94 ? 208 TYR B CZ    1 
ATOM   9996  O  OH    A TYR B 2 208 ? 43.220  -30.842 3.850   0.50 47.81 ? 208 TYR B OH    1 
ATOM   9997  O  OH    B TYR B 2 208 ? 42.656  -31.545 3.229   0.50 44.48 ? 208 TYR B OH    1 
ATOM   9998  N  N     A ASP B 2 209 ? 38.212  -28.203 7.712   0.50 32.86 ? 209 ASP B N     1 
ATOM   9999  N  N     B ASP B 2 209 ? 38.022  -28.160 7.614   0.50 33.09 ? 209 ASP B N     1 
ATOM   10000 C  CA    A ASP B 2 209 ? 38.961  -28.300 8.960   0.50 32.81 ? 209 ASP B CA    1 
ATOM   10001 C  CA    B ASP B 2 209 ? 38.812  -28.149 8.840   0.50 32.13 ? 209 ASP B CA    1 
ATOM   10002 C  C     A ASP B 2 209 ? 38.293  -29.265 9.933   0.50 36.98 ? 209 ASP B C     1 
ATOM   10003 C  C     B ASP B 2 209 ? 38.260  -29.129 9.869   0.50 37.04 ? 209 ASP B C     1 
ATOM   10004 O  O     A ASP B 2 209 ? 38.975  -29.977 10.678  0.50 34.84 ? 209 ASP B O     1 
ATOM   10005 O  O     B ASP B 2 209 ? 39.027  -29.839 10.529  0.50 34.70 ? 209 ASP B O     1 
ATOM   10006 C  CB    A ASP B 2 209 ? 39.115  -26.914 9.589   0.50 35.34 ? 209 ASP B CB    1 
ATOM   10007 C  CB    B ASP B 2 209 ? 38.864  -26.735 9.418   0.50 34.89 ? 209 ASP B CB    1 
ATOM   10008 C  CG    A ASP B 2 209 ? 40.012  -25.996 8.770   0.50 37.70 ? 209 ASP B CG    1 
ATOM   10009 C  CG    B ASP B 2 209 ? 39.922  -25.871 8.754   0.50 37.78 ? 209 ASP B CG    1 
ATOM   10010 O  OD1   A ASP B 2 209 ? 40.540  -26.446 7.732   0.50 31.39 ? 209 ASP B OD1   1 
ATOM   10011 O  OD1   B ASP B 2 209 ? 40.972  -26.419 8.363   0.50 26.75 ? 209 ASP B OD1   1 
ATOM   10012 O  OD2   A ASP B 2 209 ? 40.187  -24.823 9.164   0.50 38.55 ? 209 ASP B OD2   1 
ATOM   10013 O  OD2   B ASP B 2 209 ? 39.707  -24.646 8.629   0.50 37.85 ? 209 ASP B OD2   1 
ATOM   10014 N  N     A ILE B 2 210 ? 36.960  -29.310 9.933   0.50 33.13 ? 210 ILE B N     1 
ATOM   10015 N  N     B ILE B 2 210 ? 36.935  -29.183 10.021  0.50 33.02 ? 210 ILE B N     1 
ATOM   10016 C  CA    A ILE B 2 210 ? 36.250  -30.258 10.786  0.50 36.10 ? 210 ILE B CA    1 
ATOM   10017 C  CA    B ILE B 2 210 ? 36.340  -30.087 11.002  0.50 35.68 ? 210 ILE B CA    1 
ATOM   10018 C  C     A ILE B 2 210 ? 36.471  -31.684 10.296  0.50 38.39 ? 210 ILE B C     1 
ATOM   10019 C  C     B ILE B 2 210 ? 36.666  -31.535 10.658  0.50 38.91 ? 210 ILE B C     1 
ATOM   10020 O  O     A ILE B 2 210 ? 36.794  -32.585 11.080  0.50 40.06 ? 210 ILE B O     1 
ATOM   10021 O  O     B ILE B 2 210 ? 37.120  -32.307 11.510  0.50 38.44 ? 210 ILE B O     1 
ATOM   10022 C  CB    A ILE B 2 210 ? 34.753  -29.907 10.850  0.50 34.98 ? 210 ILE B CB    1 
ATOM   10023 C  CB    B ILE B 2 210 ? 34.821  -29.857 11.098  0.50 35.51 ? 210 ILE B CB    1 
ATOM   10024 C  CG1   A ILE B 2 210 ? 34.540  -28.633 11.673  0.50 34.41 ? 210 ILE B CG1   1 
ATOM   10025 C  CG1   B ILE B 2 210 ? 34.529  -28.491 11.725  0.50 34.33 ? 210 ILE B CG1   1 
ATOM   10026 C  CG2   A ILE B 2 210 ? 33.953  -31.068 11.432  0.50 35.67 ? 210 ILE B CG2   1 
ATOM   10027 C  CG2   B ILE B 2 210 ? 34.164  -30.972 11.906  0.50 34.69 ? 210 ILE B CG2   1 
ATOM   10028 C  CD1   A ILE B 2 210 ? 33.135  -28.068 11.576  0.50 29.98 ? 210 ILE B CD1   1 
ATOM   10029 C  CD1   B ILE B 2 210 ? 33.085  -28.049 11.586  0.50 29.97 ? 210 ILE B CD1   1 
ATOM   10030 N  N     A CYS B 2 211 ? 36.301  -31.912 8.992   0.50 37.58 ? 211 CYS B N     1 
ATOM   10031 N  N     B CYS B 2 211 ? 36.441  -31.925 9.402   0.50 38.10 ? 211 CYS B N     1 
ATOM   10032 C  CA    A CYS B 2 211 ? 36.459  -33.259 8.453   0.50 40.98 ? 211 CYS B CA    1 
ATOM   10033 C  CA    B CYS B 2 211 ? 36.724  -33.297 8.991   0.50 40.02 ? 211 CYS B CA    1 
ATOM   10034 C  C     A CYS B 2 211 ? 37.893  -33.758 8.574   0.50 39.49 ? 211 CYS B C     1 
ATOM   10035 C  C     B CYS B 2 211 ? 38.194  -33.644 9.200   0.50 40.16 ? 211 CYS B C     1 
ATOM   10036 O  O     A CYS B 2 211 ? 38.113  -34.959 8.766   0.50 46.37 ? 211 CYS B O     1 
ATOM   10037 O  O     B CYS B 2 211 ? 38.523  -34.651 9.838   0.50 42.66 ? 211 CYS B O     1 
ATOM   10038 C  CB    A CYS B 2 211 ? 36.015  -33.301 6.989   0.50 37.33 ? 211 CYS B CB    1 
ATOM   10039 C  CB    B CYS B 2 211 ? 36.329  -33.497 7.528   0.50 40.31 ? 211 CYS B CB    1 
ATOM   10040 S  SG    A CYS B 2 211 ? 34.230  -33.166 6.726   0.50 41.49 ? 211 CYS B SG    1 
ATOM   10041 S  SG    B CYS B 2 211 ? 34.560  -33.364 7.204   0.50 40.52 ? 211 CYS B SG    1 
ATOM   10042 N  N     A PHE B 2 212 ? 38.877  -32.864 8.476   0.50 42.58 ? 212 PHE B N     1 
ATOM   10043 N  N     B PHE B 2 212 ? 39.095  -32.805 8.685   0.50 42.90 ? 212 PHE B N     1 
ATOM   10044 C  CA    A PHE B 2 212 ? 40.270  -33.288 8.382   0.50 43.56 ? 212 PHE B CA    1 
ATOM   10045 C  CA    B PHE B 2 212 ? 40.516  -33.135 8.719   0.50 43.83 ? 212 PHE B CA    1 
ATOM   10046 C  C     A PHE B 2 212 ? 40.948  -33.440 9.740   0.50 44.56 ? 212 PHE B C     1 
ATOM   10047 C  C     B PHE B 2 212 ? 41.073  -33.087 10.138  0.50 45.25 ? 212 PHE B C     1 
ATOM   10048 O  O     A PHE B 2 212 ? 41.663  -34.424 9.962   0.50 45.09 ? 212 PHE B O     1 
ATOM   10049 O  O     B PHE B 2 212 ? 41.825  -33.981 10.543  0.50 47.17 ? 212 PHE B O     1 
ATOM   10050 C  CB    A PHE B 2 212 ? 41.061  -32.301 7.519   0.50 40.71 ? 212 PHE B CB    1 
ATOM   10051 C  CB    B PHE B 2 212 ? 41.294  -32.189 7.804   0.50 41.21 ? 212 PHE B CB    1 
ATOM   10052 C  CG    A PHE B 2 212 ? 42.528  -32.612 7.438   0.50 44.04 ? 212 PHE B CG    1 
ATOM   10053 C  CG    B PHE B 2 212 ? 42.751  -32.527 7.681   0.50 44.20 ? 212 PHE B CG    1 
ATOM   10054 C  CD1   A PHE B 2 212 ? 42.991  -33.617 6.606   0.50 47.41 ? 212 PHE B CD1   1 
ATOM   10055 C  CD1   B PHE B 2 212 ? 43.188  -33.422 6.719   0.50 47.61 ? 212 PHE B CD1   1 
ATOM   10056 C  CD2   A PHE B 2 212 ? 43.444  -31.897 8.189   0.50 44.54 ? 212 PHE B CD2   1 
ATOM   10057 C  CD2   B PHE B 2 212 ? 43.685  -31.949 8.525   0.50 45.06 ? 212 PHE B CD2   1 
ATOM   10058 C  CE1   A PHE B 2 212 ? 44.343  -33.907 6.530   0.50 47.87 ? 212 PHE B CE1   1 
ATOM   10059 C  CE1   B PHE B 2 212 ? 44.530  -33.737 6.603   0.50 47.67 ? 212 PHE B CE1   1 
ATOM   10060 C  CE2   A PHE B 2 212 ? 44.796  -32.182 8.119   0.50 47.56 ? 212 PHE B CE2   1 
ATOM   10061 C  CE2   B PHE B 2 212 ? 45.028  -32.263 8.415   0.50 46.38 ? 212 PHE B CE2   1 
ATOM   10062 C  CZ    A PHE B 2 212 ? 45.246  -33.186 7.287   0.50 47.40 ? 212 PHE B CZ    1 
ATOM   10063 C  CZ    B PHE B 2 212 ? 45.450  -33.155 7.451   0.50 47.66 ? 212 PHE B CZ    1 
ATOM   10064 N  N     A ARG B 2 213 ? 40.757  -32.485 10.650  0.50 44.19 ? 213 ARG B N     1 
ATOM   10065 N  N     B ARG B 2 213 ? 40.723  -32.055 10.907  0.50 43.47 ? 213 ARG B N     1 
ATOM   10066 C  CA    A ARG B 2 213 ? 41.443  -32.510 11.937  0.50 42.96 ? 213 ARG B CA    1 
ATOM   10067 C  CA    B ARG B 2 213 ? 41.304  -31.879 12.234  0.50 44.62 ? 213 ARG B CA    1 
ATOM   10068 C  C     A ARG B 2 213 ? 40.572  -32.996 13.085  0.50 47.30 ? 213 ARG B C     1 
ATOM   10069 C  C     B ARG B 2 213 ? 40.558  -32.647 13.319  0.50 46.38 ? 213 ARG B C     1 
ATOM   10070 O  O     A ARG B 2 213 ? 41.100  -33.560 14.048  0.50 49.50 ? 213 ARG B O     1 
ATOM   10071 O  O     B ARG B 2 213 ? 41.188  -33.163 14.249  0.50 49.13 ? 213 ARG B O     1 
ATOM   10072 C  CB    A ARG B 2 213 ? 41.984  -31.118 12.285  0.50 45.91 ? 213 ARG B CB    1 
ATOM   10073 C  CB    B ARG B 2 213 ? 41.353  -30.392 12.605  0.50 40.91 ? 213 ARG B CB    1 
ATOM   10074 C  CG    A ARG B 2 213 ? 43.131  -30.647 11.406  0.50 42.50 ? 213 ARG B CG    1 
ATOM   10075 C  CG    B ARG B 2 213 ? 42.381  -29.586 11.824  0.50 45.86 ? 213 ARG B CG    1 
ATOM   10076 C  CD    A ARG B 2 213 ? 43.563  -29.238 11.783  0.50 42.49 ? 213 ARG B CD    1 
ATOM   10077 C  CD    B ARG B 2 213 ? 42.681  -28.248 12.495  0.50 45.93 ? 213 ARG B CD    1 
ATOM   10078 N  NE    A ARG B 2 213 ? 44.406  -28.624 10.764  0.50 43.77 ? 213 ARG B NE    1 
ATOM   10079 N  NE    B ARG B 2 213 ? 41.618  -27.265 12.310  0.50 42.93 ? 213 ARG B NE    1 
ATOM   10080 C  CZ    A ARG B 2 213 ? 45.727  -28.541 10.831  0.50 41.95 ? 213 ARG B CZ    1 
ATOM   10081 C  CZ    B ARG B 2 213 ? 40.660  -27.014 13.192  0.50 40.96 ? 213 ARG B CZ    1 
ATOM   10082 N  NH1   A ARG B 2 213 ? 46.401  -29.036 11.856  0.50 38.21 ? 213 ARG B NH1   1 
ATOM   10083 N  NH1   B ARG B 2 213 ? 40.581  -27.674 14.336  0.50 40.16 ? 213 ARG B NH1   1 
ATOM   10084 N  NH2   A ARG B 2 213 ? 46.389  -27.936 9.849   0.50 34.00 ? 213 ARG B NH2   1 
ATOM   10085 N  NH2   B ARG B 2 213 ? 39.758  -26.075 12.920  0.50 42.83 ? 213 ARG B NH2   1 
ATOM   10086 N  N     A THR B 2 214 ? 39.257  -32.790 13.021  0.50 44.50 ? 214 THR B N     1 
ATOM   10087 N  N     B THR B 2 214 ? 39.231  -32.737 13.231  0.50 44.70 ? 214 THR B N     1 
ATOM   10088 C  CA    A THR B 2 214 ? 38.389  -33.254 14.096  0.50 44.93 ? 214 THR B CA    1 
ATOM   10089 C  CA    B THR B 2 214 ? 38.438  -33.360 14.285  0.50 45.14 ? 214 THR B CA    1 
ATOM   10090 C  C     A THR B 2 214 ? 37.920  -34.685 13.862  0.50 41.55 ? 214 THR B C     1 
ATOM   10091 C  C     B THR B 2 214 ? 38.020  -34.786 13.949  0.50 41.80 ? 214 THR B C     1 
ATOM   10092 O  O     A THR B 2 214 ? 38.028  -35.531 14.756  0.50 49.38 ? 214 THR B O     1 
ATOM   10093 O  O     B THR B 2 214 ? 38.172  -35.686 14.782  0.50 49.29 ? 214 THR B O     1 
ATOM   10094 C  CB    A THR B 2 214 ? 37.187  -32.317 14.250  0.50 38.54 ? 214 THR B CB    1 
ATOM   10095 C  CB    B THR B 2 214 ? 37.196  -32.507 14.586  0.50 37.92 ? 214 THR B CB    1 
ATOM   10096 O  OG1   A THR B 2 214 ? 37.651  -30.988 14.518  0.50 43.51 ? 214 THR B OG1   1 
ATOM   10097 O  OG1   B THR B 2 214 ? 37.606  -31.194 14.985  0.50 44.26 ? 214 THR B OG1   1 
ATOM   10098 C  CG2   A THR B 2 214 ? 36.297  -32.778 15.391  0.50 41.13 ? 214 THR B CG2   1 
ATOM   10099 C  CG2   B THR B 2 214 ? 36.368  -33.135 15.696  0.50 41.31 ? 214 THR B CG2   1 
ATOM   10100 N  N     A LEU B 2 215 ? 37.413  -34.973 12.665  0.50 47.20 ? 215 LEU B N     1 
ATOM   10101 N  N     B LEU B 2 215 ? 37.505  -35.018 12.743  0.50 47.13 ? 215 LEU B N     1 
ATOM   10102 C  CA    A LEU B 2 215 ? 36.944  -36.310 12.330  0.50 44.58 ? 215 LEU B CA    1 
ATOM   10103 C  CA    B LEU B 2 215 ? 36.991  -36.331 12.371  0.50 44.59 ? 215 LEU B CA    1 
ATOM   10104 C  C     A LEU B 2 215 ? 38.061  -37.231 11.859  0.50 47.20 ? 215 LEU B C     1 
ATOM   10105 C  C     B LEU B 2 215 ? 38.071  -37.288 11.881  0.50 47.18 ? 215 LEU B C     1 
ATOM   10106 O  O     A LEU B 2 215 ? 37.842  -38.444 11.777  0.50 48.45 ? 215 LEU B O     1 
ATOM   10107 O  O     B LEU B 2 215 ? 37.734  -38.398 11.452  0.50 48.40 ? 215 LEU B O     1 
ATOM   10108 C  CB    A LEU B 2 215 ? 35.864  -36.229 11.251  0.50 41.74 ? 215 LEU B CB    1 
ATOM   10109 C  CB    B LEU B 2 215 ? 35.911  -36.188 11.296  0.50 41.73 ? 215 LEU B CB    1 
ATOM   10110 C  CG    A LEU B 2 215 ? 34.648  -35.361 11.583  0.50 44.81 ? 215 LEU B CG    1 
ATOM   10111 C  CG    B LEU B 2 215 ? 34.644  -35.430 11.701  0.50 44.77 ? 215 LEU B CG    1 
ATOM   10112 C  CD1   A LEU B 2 215 ? 33.691  -35.311 10.401  0.50 43.58 ? 215 LEU B CD1   1 
ATOM   10113 C  CD1   B LEU B 2 215 ? 33.609  -35.499 10.589  0.50 43.94 ? 215 LEU B CD1   1 
ATOM   10114 C  CD2   A LEU B 2 215 ? 33.945  -35.876 12.829  0.50 42.75 ? 215 LEU B CD2   1 
ATOM   10115 C  CD2   B LEU B 2 215 ? 34.079  -35.976 13.004  0.50 42.54 ? 215 LEU B CD2   1 
ATOM   10116 N  N     A LYS B 2 216 ? 39.239  -36.686 11.548  0.50 49.48 ? 216 LYS B N     1 
ATOM   10117 N  N     B LYS B 2 216 ? 39.343  -36.886 11.917  0.50 50.44 ? 216 LYS B N     1 
ATOM   10118 C  CA    A LYS B 2 216 ? 40.388  -37.450 11.057  0.50 46.03 ? 216 LYS B CA    1 
ATOM   10119 C  CA    B LYS B 2 216 ? 40.479  -37.739 11.561  0.50 46.08 ? 216 LYS B CA    1 
ATOM   10120 C  C     A LYS B 2 216 ? 40.041  -38.184 9.757   0.50 51.21 ? 216 LYS B C     1 
ATOM   10121 C  C     B LYS B 2 216 ? 40.442  -38.197 10.105  0.50 51.21 ? 216 LYS B C     1 
ATOM   10122 O  O     A LYS B 2 216 ? 39.866  -39.403 9.709   0.50 51.73 ? 216 LYS B O     1 
ATOM   10123 O  O     B LYS B 2 216 ? 41.088  -39.187 9.746   0.50 49.24 ? 216 LYS B O     1 
ATOM   10124 C  CB    A LYS B 2 216 ? 40.903  -38.423 12.126  0.50 46.35 ? 216 LYS B CB    1 
ATOM   10125 C  CB    B LYS B 2 216 ? 40.570  -38.959 12.487  0.50 49.05 ? 216 LYS B CB    1 
ATOM   10126 C  CG    A LYS B 2 216 ? 42.136  -37.930 12.874  0.50 51.21 ? 216 LYS B CG    1 
ATOM   10127 C  CG    B LYS B 2 216 ? 40.570  -38.625 13.973  0.50 49.35 ? 216 LYS B CG    1 
ATOM   10128 C  CD    A LYS B 2 216 ? 41.840  -36.680 13.685  0.50 49.92 ? 216 LYS B CD    1 
ATOM   10129 C  CD    B LYS B 2 216 ? 41.747  -37.740 14.342  0.50 44.96 ? 216 LYS B CD    1 
ATOM   10130 C  CE    A LYS B 2 216 ? 43.125  -36.019 14.174  0.50 52.51 ? 216 LYS B CE    1 
ATOM   10131 C  CE    B LYS B 2 216 ? 41.844  -37.549 15.846  0.50 53.03 ? 216 LYS B CE    1 
ATOM   10132 N  NZ    A LYS B 2 216 ? 43.911  -36.898 15.084  0.50 59.22 ? 216 LYS B NZ    1 
ATOM   10133 N  NZ    B LYS B 2 216 ? 42.100  -38.833 16.557  0.50 53.05 ? 216 LYS B NZ    1 
ATOM   10134 N  N     A LEU B 2 217 ? 39.947  -37.387 8.695   0.50 49.68 ? 217 LEU B N     1 
ATOM   10135 N  N     B LEU B 2 217 ? 39.702  -37.495 9.251   0.50 50.80 ? 217 LEU B N     1 
ATOM   10136 C  CA    A LEU B 2 217 ? 39.763  -37.882 7.334   0.50 50.52 ? 217 LEU B CA    1 
ATOM   10137 C  CA    B LEU B 2 217 ? 39.584  -37.880 7.852   0.50 49.51 ? 217 LEU B CA    1 
ATOM   10138 C  C     A LEU B 2 217 ? 40.766  -37.150 6.452   0.50 49.47 ? 217 LEU B C     1 
ATOM   10139 C  C     B LEU B 2 217 ? 40.758  -37.324 7.053   0.50 50.99 ? 217 LEU B C     1 
ATOM   10140 O  O     A LEU B 2 217 ? 40.598  -35.958 6.175   0.50 43.79 ? 217 LEU B O     1 
ATOM   10141 O  O     B LEU B 2 217 ? 41.083  -36.136 7.152   0.50 42.75 ? 217 LEU B O     1 
ATOM   10142 C  CB    A LEU B 2 217 ? 38.329  -37.663 6.849   0.50 47.57 ? 217 LEU B CB    1 
ATOM   10143 C  CB    B LEU B 2 217 ? 38.255  -37.382 7.284   0.50 47.24 ? 217 LEU B CB    1 
ATOM   10144 C  CG    A LEU B 2 217 ? 37.223  -38.311 7.691   0.50 48.49 ? 217 LEU B CG    1 
ATOM   10145 C  CG    B LEU B 2 217 ? 37.032  -37.804 8.106   0.50 46.82 ? 217 LEU B CG    1 
ATOM   10146 C  CD1   A LEU B 2 217 ? 35.844  -37.899 7.202   0.50 46.31 ? 217 LEU B CD1   1 
ATOM   10147 C  CD1   B LEU B 2 217 ? 35.758  -37.149 7.593   0.50 43.68 ? 217 LEU B CD1   1 
ATOM   10148 C  CD2   A LEU B 2 217 ? 37.357  -39.828 7.693   0.50 48.33 ? 217 LEU B CD2   1 
ATOM   10149 C  CD2   B LEU B 2 217 ? 36.891  -39.320 8.116   0.50 48.50 ? 217 LEU B CD2   1 
ATOM   10150 N  N     A THR B 2 218 ? 41.814  -37.859 6.021   0.50 49.71 ? 218 THR B N     1 
ATOM   10151 N  N     B THR B 2 218 ? 41.398  -38.188 6.260   0.50 48.61 ? 218 THR B N     1 
ATOM   10152 C  CA    A THR B 2 218 ? 42.929  -37.212 5.336   0.50 42.70 ? 218 THR B CA    1 
ATOM   10153 C  CA    B THR B 2 218 ? 42.604  -37.786 5.542   0.50 46.92 ? 218 THR B CA    1 
ATOM   10154 C  C     A THR B 2 218 ? 42.541  -36.627 3.984   0.50 47.05 ? 218 THR B C     1 
ATOM   10155 C  C     B THR B 2 218 ? 42.271  -36.999 4.279   0.50 44.74 ? 218 THR B C     1 
ATOM   10156 O  O     A THR B 2 218 ? 43.220  -35.713 3.504   0.50 41.57 ? 218 THR B O     1 
ATOM   10157 O  O     B THR B 2 218 ? 42.889  -35.964 4.005   0.50 47.99 ? 218 THR B O     1 
ATOM   10158 C  CB    A THR B 2 218 ? 44.087  -38.198 5.155   0.50 49.10 ? 218 THR B CB    1 
ATOM   10159 C  CB    B THR B 2 218 ? 43.447  -39.017 5.197   0.50 52.35 ? 218 THR B CB    1 
ATOM   10160 O  OG1   A THR B 2 218 ? 43.594  -39.430 4.613   0.50 52.67 ? 218 THR B OG1   1 
ATOM   10161 O  OG1   B THR B 2 218 ? 43.822  -39.698 6.401   0.50 54.54 ? 218 THR B OG1   1 
ATOM   10162 C  CG2   A THR B 2 218 ? 44.778  -38.467 6.485   0.50 48.89 ? 218 THR B CG2   1 
ATOM   10163 C  CG2   B THR B 2 218 ? 44.704  -38.609 4.443   0.50 49.66 ? 218 THR B CG2   1 
ATOM   10164 N  N     A THR B 2 219 ? 41.479  -37.126 3.355   0.50 49.93 ? 219 THR B N     1 
ATOM   10165 N  N     B THR B 2 219 ? 41.310  -37.478 3.491   0.50 48.10 ? 219 THR B N     1 
ATOM   10166 C  CA    A THR B 2 219 ? 41.032  -36.628 2.052   0.50 50.58 ? 219 THR B CA    1 
ATOM   10167 C  CA    B THR B 2 219 ? 40.912  -36.832 2.239   0.50 50.46 ? 219 THR B CA    1 
ATOM   10168 C  C     A THR B 2 219 ? 39.513  -36.566 2.036   0.50 47.59 ? 219 THR B C     1 
ATOM   10169 C  C     B THR B 2 219 ? 39.401  -36.652 2.250   0.50 47.51 ? 219 THR B C     1 
ATOM   10170 O  O     A THR B 2 219 ? 38.841  -37.460 1.508   0.50 45.64 ? 219 THR B O     1 
ATOM   10171 O  O     B THR B 2 219 ? 38.667  -37.424 1.619   0.50 45.83 ? 219 THR B O     1 
ATOM   10172 C  CB    A THR B 2 219 ? 41.558  -37.504 0.910   0.50 49.48 ? 219 THR B CB    1 
ATOM   10173 C  CB    B THR B 2 219 ? 41.354  -37.646 1.019   0.50 50.15 ? 219 THR B CB    1 
ATOM   10174 O  OG1   A THR B 2 219 ? 41.427  -38.887 1.261   0.50 57.33 ? 219 THR B OG1   1 
ATOM   10175 O  OG1   B THR B 2 219 ? 40.701  -38.921 1.032   0.50 56.80 ? 219 THR B OG1   1 
ATOM   10176 C  CG2   A THR B 2 219 ? 43.020  -37.195 0.619   0.50 50.82 ? 219 THR B CG2   1 
ATOM   10177 C  CG2   B THR B 2 219 ? 42.861  -37.857 1.026   0.50 48.03 ? 219 THR B CG2   1 
ATOM   10178 N  N     A PRO B 2 220 ? 38.933  -35.512 2.606   0.50 47.03 ? 220 PRO B N     1 
ATOM   10179 N  N     B PRO B 2 220 ? 38.902  -35.635 2.952   0.50 47.07 ? 220 PRO B N     1 
ATOM   10180 C  CA    A PRO B 2 220 ? 37.472  -35.395 2.618   0.50 45.16 ? 220 PRO B CA    1 
ATOM   10181 C  CA    B PRO B 2 220 ? 37.448  -35.453 3.056   0.50 45.44 ? 220 PRO B CA    1 
ATOM   10182 C  C     A PRO B 2 220 ? 36.905  -35.212 1.219   0.50 43.39 ? 220 PRO B C     1 
ATOM   10183 C  C     B PRO B 2 220 ? 36.812  -35.226 1.692   0.50 42.91 ? 220 PRO B C     1 
ATOM   10184 O  O     A PRO B 2 220 ? 37.521  -34.601 0.341   0.50 45.12 ? 220 PRO B O     1 
ATOM   10185 O  O     B PRO B 2 220 ? 37.290  -34.421 0.889   0.50 45.78 ? 220 PRO B O     1 
ATOM   10186 C  CB    A PRO B 2 220 ? 37.222  -34.152 3.482   0.50 41.79 ? 220 PRO B CB    1 
ATOM   10187 C  CB    B PRO B 2 220 ? 37.308  -34.221 3.958   0.50 40.90 ? 220 PRO B CB    1 
ATOM   10188 C  CG    A PRO B 2 220 ? 38.462  -33.994 4.294   0.50 45.00 ? 220 PRO B CG    1 
ATOM   10189 C  CG    B PRO B 2 220 ? 38.597  -34.141 4.702   0.50 44.94 ? 220 PRO B CG    1 
ATOM   10190 C  CD    A PRO B 2 220 ? 39.574  -34.454 3.404   0.50 43.94 ? 220 PRO B CD    1 
ATOM   10191 C  CD    B PRO B 2 220 ? 39.639  -34.641 3.749   0.50 43.59 ? 220 PRO B CD    1 
ATOM   10192 N  N     A THR B 2 221 ? 35.710  -35.757 1.022   0.50 42.54 ? 221 THR B N     1 
ATOM   10193 N  N     B THR B 2 221 ? 35.731  -35.953 1.435   0.50 44.05 ? 221 THR B N     1 
ATOM   10194 C  CA    A THR B 2 221 ? 34.967  -35.648 -0.223  0.50 38.74 ? 221 THR B CA    1 
ATOM   10195 C  CA    B THR B 2 221 ? 34.967  -35.823 0.207   0.50 39.14 ? 221 THR B CA    1 
ATOM   10196 C  C     A THR B 2 221 ? 33.775  -34.719 -0.022  0.50 38.58 ? 221 THR B C     1 
ATOM   10197 C  C     B THR B 2 221 ? 33.862  -34.785 0.394   0.50 39.25 ? 221 THR B C     1 
ATOM   10198 O  O     A THR B 2 221 ? 33.518  -34.226 1.081   0.50 35.11 ? 221 THR B O     1 
ATOM   10199 O  O     B THR B 2 221 ? 33.565  -34.350 1.509   0.50 33.07 ? 221 THR B O     1 
ATOM   10200 C  CB    A THR B 2 221 ? 34.504  -37.027 -0.701  0.50 43.24 ? 221 THR B CB    1 
ATOM   10201 C  CB    B THR B 2 221 ? 34.376  -37.177 -0.197  0.50 41.19 ? 221 THR B CB    1 
ATOM   10202 O  OG1   A THR B 2 221 ? 33.556  -37.566 0.230   0.50 41.53 ? 221 THR B OG1   1 
ATOM   10203 O  OG1   B THR B 2 221 ? 35.302  -38.219 0.139   0.50 46.73 ? 221 THR B OG1   1 
ATOM   10204 C  CG2   A THR B 2 221 ? 35.687  -37.978 -0.816  0.50 42.24 ? 221 THR B CG2   1 
ATOM   10205 C  CG2   B THR B 2 221 ? 34.102  -37.231 -1.697  0.50 47.09 ? 221 THR B CG2   1 
ATOM   10206 N  N     A TYR B 2 222 ? 33.031  -34.491 -1.107  0.50 37.15 ? 222 TYR B N     1 
ATOM   10207 N  N     B TYR B 2 222 ? 33.258  -34.375 -0.725  0.50 36.44 ? 222 TYR B N     1 
ATOM   10208 C  CA    A TYR B 2 222 ? 31.778  -33.754 -1.005  0.50 38.65 ? 222 TYR B CA    1 
ATOM   10209 C  CA    B TYR B 2 222 ? 32.115  -33.472 -0.656  0.50 38.96 ? 222 TYR B CA    1 
ATOM   10210 C  C     A TYR B 2 222 ? 30.722  -34.504 -0.204  0.50 39.53 ? 222 TYR B C     1 
ATOM   10211 C  C     B TYR B 2 222 ? 30.960  -34.104 0.107   0.50 37.99 ? 222 TYR B C     1 
ATOM   10212 O  O     A TYR B 2 222 ? 29.647  -33.948 0.042   0.50 40.60 ? 222 TYR B O     1 
ATOM   10213 O  O     B TYR B 2 222 ? 30.306  -33.439 0.919   0.50 40.79 ? 222 TYR B O     1 
ATOM   10214 C  CB    A TYR B 2 222 ? 31.238  -33.429 -2.398  0.50 34.41 ? 222 TYR B CB    1 
ATOM   10215 C  CB    B TYR B 2 222 ? 31.672  -33.071 -2.061  0.50 33.72 ? 222 TYR B CB    1 
ATOM   10216 C  CG    A TYR B 2 222 ? 31.854  -32.200 -3.030  0.50 37.29 ? 222 TYR B CG    1 
ATOM   10217 C  CG    B TYR B 2 222 ? 32.464  -31.921 -2.635  0.50 34.58 ? 222 TYR B CG    1 
ATOM   10218 C  CD1   A TYR B 2 222 ? 32.297  -31.140 -2.249  0.50 34.64 ? 222 TYR B CD1   1 
ATOM   10219 C  CD1   B TYR B 2 222 ? 32.255  -30.625 -2.183  0.50 35.83 ? 222 TYR B CD1   1 
ATOM   10220 C  CD2   A TYR B 2 222 ? 31.993  -32.099 -4.409  0.50 29.53 ? 222 TYR B CD2   1 
ATOM   10221 C  CD2   B TYR B 2 222 ? 33.416  -32.126 -3.627  0.50 29.09 ? 222 TYR B CD2   1 
ATOM   10222 C  CE1   A TYR B 2 222 ? 32.858  -30.012 -2.824  0.50 36.24 ? 222 TYR B CE1   1 
ATOM   10223 C  CE1   B TYR B 2 222 ? 32.973  -29.566 -2.695  0.50 35.07 ? 222 TYR B CE1   1 
ATOM   10224 C  CE2   A TYR B 2 222 ? 32.554  -30.975 -4.995  0.50 35.28 ? 222 TYR B CE2   1 
ATOM   10225 C  CE2   B TYR B 2 222 ? 34.143  -31.069 -4.146  0.50 28.26 ? 222 TYR B CE2   1 
ATOM   10226 C  CZ    A TYR B 2 222 ? 32.986  -29.936 -4.197  0.50 31.72 ? 222 TYR B CZ    1 
ATOM   10227 C  CZ    B TYR B 2 222 ? 33.913  -29.792 -3.678  0.50 29.02 ? 222 TYR B CZ    1 
ATOM   10228 O  OH    A TYR B 2 222 ? 33.544  -28.815 -4.768  0.50 28.28 ? 222 TYR B OH    1 
ATOM   10229 O  OH    B TYR B 2 222 ? 34.620  -28.730 -4.180  0.50 27.45 ? 222 TYR B OH    1 
ATOM   10230 N  N     A GLY B 2 223 ? 30.997  -35.742 0.199   0.50 38.79 ? 223 GLY B N     1 
ATOM   10231 N  N     B GLY B 2 223 ? 30.690  -35.387 -0.146  0.50 39.70 ? 223 GLY B N     1 
ATOM   10232 C  CA    A GLY B 2 223 ? 30.105  -36.474 1.073   0.50 38.05 ? 223 GLY B CA    1 
ATOM   10233 C  CA    B GLY B 2 223 ? 29.670  -36.083 0.620   0.50 36.63 ? 223 GLY B CA    1 
ATOM   10234 C  C     A GLY B 2 223 ? 30.349  -36.133 2.528   0.50 39.31 ? 223 GLY B C     1 
ATOM   10235 C  C     B GLY B 2 223 ? 29.924  -36.020 2.113   0.50 39.39 ? 223 GLY B C     1 
ATOM   10236 O  O     A GLY B 2 223 ? 29.405  -35.851 3.272   0.50 38.78 ? 223 GLY B O     1 
ATOM   10237 O  O     B GLY B 2 223 ? 28.989  -35.906 2.908   0.50 35.95 ? 223 GLY B O     1 
ATOM   10238 N  N     A ASP B 2 224 ? 31.619  -36.161 2.943   0.50 39.55 ? 224 ASP B N     1 
ATOM   10239 N  N     B ASP B 2 224 ? 31.197  -36.086 2.511   0.50 40.54 ? 224 ASP B N     1 
ATOM   10240 C  CA    A ASP B 2 224 ? 31.968  -35.767 4.304   0.50 38.78 ? 224 ASP B CA    1 
ATOM   10241 C  CA    B ASP B 2 224 ? 31.555  -35.892 3.912   0.50 37.21 ? 224 ASP B CA    1 
ATOM   10242 C  C     A ASP B 2 224 ? 31.514  -34.343 4.601   0.50 37.36 ? 224 ASP B C     1 
ATOM   10243 C  C     B ASP B 2 224 ? 31.218  -34.478 4.370   0.50 37.08 ? 224 ASP B C     1 
ATOM   10244 O  O     A ASP B 2 224 ? 30.993  -34.062 5.687   0.50 41.88 ? 224 ASP B O     1 
ATOM   10245 O  O     B ASP B 2 224 ? 30.582  -34.286 5.413   0.50 41.93 ? 224 ASP B O     1 
ATOM   10246 C  CB    A ASP B 2 224 ? 33.477  -35.897 4.518   0.50 35.14 ? 224 ASP B CB    1 
ATOM   10247 C  CB    B ASP B 2 224 ? 33.043  -36.181 4.113   0.50 38.51 ? 224 ASP B CB    1 
ATOM   10248 C  CG    A ASP B 2 224 ? 33.970  -37.321 4.358   0.50 42.68 ? 224 ASP B CG    1 
ATOM   10249 C  CG    B ASP B 2 224 ? 33.373  -37.653 3.992   0.50 41.70 ? 224 ASP B CG    1 
ATOM   10250 O  OD1   A ASP B 2 224 ? 33.363  -38.235 4.957   0.50 40.61 ? 224 ASP B OD1   1 
ATOM   10251 O  OD1   B ASP B 2 224 ? 33.033  -38.418 4.919   0.50 41.19 ? 224 ASP B OD1   1 
ATOM   10252 O  OD2   A ASP B 2 224 ? 34.965  -37.523 3.630   0.50 38.84 ? 224 ASP B OD2   1 
ATOM   10253 O  OD2   B ASP B 2 224 ? 33.966  -38.046 2.968   0.50 44.37 ? 224 ASP B OD2   1 
ATOM   10254 N  N     A LEU B 2 225 ? 31.707  -33.429 3.648   0.50 33.20 ? 225 LEU B N     1 
ATOM   10255 N  N     B LEU B 2 225 ? 31.648  -33.473 3.604   0.50 33.20 ? 225 LEU B N     1 
ATOM   10256 C  CA    A LEU B 2 225 ? 31.310  -32.041 3.860   0.50 33.46 ? 225 LEU B CA    1 
ATOM   10257 C  CA    B LEU B 2 225 ? 31.349  -32.090 3.964   0.50 33.45 ? 225 LEU B CA    1 
ATOM   10258 C  C     A LEU B 2 225 ? 29.796  -31.914 3.967   0.50 34.44 ? 225 LEU B C     1 
ATOM   10259 C  C     B LEU B 2 225 ? 29.846  -31.856 4.041   0.50 34.46 ? 225 LEU B C     1 
ATOM   10260 O  O     A LEU B 2 225 ? 29.276  -31.367 4.947   0.50 38.81 ? 225 LEU B O     1 
ATOM   10261 O  O     B LEU B 2 225 ? 29.357  -31.204 4.972   0.50 38.68 ? 225 LEU B O     1 
ATOM   10262 C  CB    A LEU B 2 225 ? 31.836  -31.158 2.726   0.50 37.38 ? 225 LEU B CB    1 
ATOM   10263 C  CB    B LEU B 2 225 ? 31.982  -31.130 2.955   0.50 37.21 ? 225 LEU B CB    1 
ATOM   10264 C  CG    A LEU B 2 225 ? 33.326  -31.202 2.389   0.50 36.84 ? 225 LEU B CG    1 
ATOM   10265 C  CG    B LEU B 2 225 ? 33.476  -31.260 2.659   0.50 35.92 ? 225 LEU B CG    1 
ATOM   10266 C  CD1   A LEU B 2 225 ? 33.686  -30.048 1.456   0.50 34.99 ? 225 LEU B CD1   1 
ATOM   10267 C  CD1   B LEU B 2 225 ? 33.945  -30.089 1.796   0.50 35.87 ? 225 LEU B CD1   1 
ATOM   10268 C  CD2   A LEU B 2 225 ? 34.177  -31.169 3.645   0.50 36.56 ? 225 LEU B CD2   1 
ATOM   10269 C  CD2   B LEU B 2 225 ? 34.285  -31.345 3.940   0.50 36.57 ? 225 LEU B CD2   1 
ATOM   10270 N  N     A ASN B 2 226 ? 29.072  -32.416 2.962   0.50 32.31 ? 226 ASN B N     1 
ATOM   10271 N  N     B ASN B 2 226 ? 29.098  -32.392 3.072   0.50 32.27 ? 226 ASN B N     1 
ATOM   10272 C  CA    A ASN B 2 226 ? 27.623  -32.269 2.930   0.50 36.86 ? 226 ASN B CA    1 
ATOM   10273 C  CA    B ASN B 2 226 ? 27.652  -32.199 3.045   0.50 36.87 ? 226 ASN B CA    1 
ATOM   10274 C  C     A ASN B 2 226 ? 26.931  -33.043 4.044   0.50 36.54 ? 226 ASN B C     1 
ATOM   10275 C  C     B ASN B 2 226 ? 26.959  -32.893 4.212   0.50 36.33 ? 226 ASN B C     1 
ATOM   10276 O  O     A ASN B 2 226 ? 25.801  -32.699 4.408   0.50 33.29 ? 226 ASN B O     1 
ATOM   10277 O  O     B ASN B 2 226 ? 25.862  -32.482 4.605   0.50 32.85 ? 226 ASN B O     1 
ATOM   10278 C  CB    A ASN B 2 226 ? 27.087  -32.704 1.566   0.50 33.35 ? 226 ASN B CB    1 
ATOM   10279 C  CB    B ASN B 2 226 ? 27.084  -32.699 1.716   0.50 33.38 ? 226 ASN B CB    1 
ATOM   10280 C  CG    A ASN B 2 226 ? 27.536  -31.781 0.448   0.50 36.89 ? 226 ASN B CG    1 
ATOM   10281 C  CG    B ASN B 2 226 ? 27.578  -31.893 0.533   0.50 36.90 ? 226 ASN B CG    1 
ATOM   10282 O  OD1   A ASN B 2 226 ? 28.356  -30.889 0.658   0.50 35.31 ? 226 ASN B OD1   1 
ATOM   10283 O  OD1   B ASN B 2 226 ? 28.023  -30.757 0.685   0.50 34.86 ? 226 ASN B OD1   1 
ATOM   10284 N  ND2   A ASN B 2 226 ? 27.004  -31.995 -0.748  0.50 29.82 ? 226 ASN B ND2   1 
ATOM   10285 N  ND2   B ASN B 2 226 ? 27.495  -32.474 -0.656  0.50 34.18 ? 226 ASN B ND2   1 
ATOM   10286 N  N     A HIS B 2 227 ? 27.575  -34.079 4.589   0.50 36.47 ? 227 HIS B N     1 
ATOM   10287 N  N     B HIS B 2 227 ? 27.572  -33.940 4.771   0.50 36.72 ? 227 HIS B N     1 
ATOM   10288 C  CA    A HIS B 2 227 ? 27.061  -34.706 5.802   0.50 38.58 ? 227 HIS B CA    1 
ATOM   10289 C  CA    B HIS B 2 227 ? 26.996  -34.588 5.946   0.50 38.43 ? 227 HIS B CA    1 
ATOM   10290 C  C     A HIS B 2 227 ? 26.941  -33.695 6.932   0.50 41.35 ? 227 HIS B C     1 
ATOM   10291 C  C     B HIS B 2 227 ? 26.908  -33.620 7.118   0.50 41.53 ? 227 HIS B C     1 
ATOM   10292 O  O     A HIS B 2 227 ? 26.037  -33.801 7.771   0.50 40.27 ? 227 HIS B O     1 
ATOM   10293 O  O     B HIS B 2 227 ? 25.894  -33.578 7.827   0.50 39.43 ? 227 HIS B O     1 
ATOM   10294 C  CB    A HIS B 2 227 ? 27.967  -35.864 6.221   0.50 41.46 ? 227 HIS B CB    1 
ATOM   10295 C  CB    B HIS B 2 227 ? 27.822  -35.814 6.332   0.50 41.50 ? 227 HIS B CB    1 
ATOM   10296 C  CG    A HIS B 2 227 ? 27.621  -36.449 7.555   0.50 44.62 ? 227 HIS B CG    1 
ATOM   10297 C  CG    B HIS B 2 227 ? 27.445  -36.399 7.657   0.50 44.56 ? 227 HIS B CG    1 
ATOM   10298 N  ND1   A HIS B 2 227 ? 26.589  -37.346 7.729   0.50 46.04 ? 227 HIS B ND1   1 
ATOM   10299 N  ND1   B HIS B 2 227 ? 26.325  -37.182 7.835   0.50 46.13 ? 227 HIS B ND1   1 
ATOM   10300 C  CD2   A HIS B 2 227 ? 28.169  -36.263 8.779   0.50 47.59 ? 227 HIS B CD2   1 
ATOM   10301 C  CD2   B HIS B 2 227 ? 28.035  -36.305 8.873   0.50 47.61 ? 227 HIS B CD2   1 
ATOM   10302 C  CE1   A HIS B 2 227 ? 26.519  -37.691 9.002   0.50 48.65 ? 227 HIS B CE1   1 
ATOM   10303 C  CE1   B HIS B 2 227 ? 26.245  -37.552 9.100   0.50 49.04 ? 227 HIS B CE1   1 
ATOM   10304 N  NE2   A HIS B 2 227 ? 27.466  -37.048 9.661   0.50 49.70 ? 227 HIS B NE2   1 
ATOM   10305 N  NE2   B HIS B 2 227 ? 27.270  -37.034 9.751   0.50 49.78 ? 227 HIS B NE2   1 
ATOM   10306 N  N     A LEU B 2 228 ? 27.837  -32.707 6.966   0.50 33.30 ? 228 LEU B N     1 
ATOM   10307 N  N     B LEU B 2 228 ? 27.966  -32.836 7.341   0.50 34.35 ? 228 LEU B N     1 
ATOM   10308 C  CA    A LEU B 2 228 ? 27.746  -31.642 7.955   0.50 37.66 ? 228 LEU B CA    1 
ATOM   10309 C  CA    B LEU B 2 228 ? 27.916  -31.816 8.380   0.50 37.34 ? 228 LEU B CA    1 
ATOM   10310 C  C     A LEU B 2 228 ? 26.707  -30.600 7.558   0.50 34.51 ? 228 LEU B C     1 
ATOM   10311 C  C     B LEU B 2 228 ? 26.934  -30.709 8.024   0.50 34.71 ? 228 LEU B C     1 
ATOM   10312 O  O     A LEU B 2 228 ? 25.993  -30.072 8.419   0.50 34.05 ? 228 LEU B O     1 
ATOM   10313 O  O     B LEU B 2 228 ? 26.323  -30.112 8.918   0.50 35.09 ? 228 LEU B O     1 
ATOM   10314 C  CB    A LEU B 2 228 ? 29.116  -30.991 8.140   0.50 39.22 ? 228 LEU B CB    1 
ATOM   10315 C  CB    B LEU B 2 228 ? 29.310  -31.237 8.613   0.50 39.81 ? 228 LEU B CB    1 
ATOM   10316 C  CG    A LEU B 2 228 ? 30.247  -31.964 8.478   0.50 40.13 ? 228 LEU B CG    1 
ATOM   10317 C  CG    B LEU B 2 228 ? 30.377  -32.216 9.107   0.50 42.41 ? 228 LEU B CG    1 
ATOM   10318 C  CD1   A LEU B 2 228 ? 31.597  -31.267 8.429   0.50 36.08 ? 228 LEU B CD1   1 
ATOM   10319 C  CD1   B LEU B 2 228 ? 31.737  -31.537 9.180   0.50 39.54 ? 228 LEU B CD1   1 
ATOM   10320 C  CD2   A LEU B 2 228 ? 30.012  -32.592 9.845   0.50 38.83 ? 228 LEU B CD2   1 
ATOM   10321 C  CD2   B LEU B 2 228 ? 29.990  -32.788 10.457  0.50 38.74 ? 228 LEU B CD2   1 
ATOM   10322 N  N     A VAL B 2 229 ? 26.601  -30.300 6.262   0.50 26.98 ? 229 VAL B N     1 
ATOM   10323 N  N     B VAL B 2 229 ? 26.770  -30.422 6.730   0.50 28.57 ? 229 VAL B N     1 
ATOM   10324 C  CA    A VAL B 2 229 ? 25.675  -29.266 5.807   0.50 27.74 ? 229 VAL B CA    1 
ATOM   10325 C  CA    B VAL B 2 229 ? 25.800  -29.415 6.313   0.50 30.91 ? 229 VAL B CA    1 
ATOM   10326 C  C     A VAL B 2 229 ? 24.231  -29.703 6.023   0.50 31.77 ? 229 VAL B C     1 
ATOM   10327 C  C     B VAL B 2 229 ? 24.379  -29.888 6.599   0.50 31.27 ? 229 VAL B C     1 
ATOM   10328 O  O     A VAL B 2 229 ? 23.408  -28.941 6.540   0.50 33.02 ? 229 VAL B O     1 
ATOM   10329 O  O     B VAL B 2 229 ? 23.539  -29.116 7.077   0.50 34.11 ? 229 VAL B O     1 
ATOM   10330 C  CB    A VAL B 2 229 ? 25.942  -28.917 4.333   0.50 32.63 ? 229 VAL B CB    1 
ATOM   10331 C  CB    B VAL B 2 229 ? 25.991  -29.075 4.825   0.50 30.58 ? 229 VAL B CB    1 
ATOM   10332 C  CG1   A VAL B 2 229 ? 24.935  -27.890 3.840   0.50 29.87 ? 229 VAL B CG1   1 
ATOM   10333 C  CG1   B VAL B 2 229 ? 25.002  -28.004 4.391   0.50 31.39 ? 229 VAL B CG1   1 
ATOM   10334 C  CG2   A VAL B 2 229 ? 27.360  -28.394 4.165   0.50 28.88 ? 229 VAL B CG2   1 
ATOM   10335 C  CG2   B VAL B 2 229 ? 27.419  -28.618 4.567   0.50 28.32 ? 229 VAL B CG2   1 
ATOM   10336 N  N     A SER B 2 230 ? 23.901  -30.936 5.629   0.50 31.86 ? 230 SER B N     1 
ATOM   10337 N  N     B SER B 2 230 ? 24.089  -31.162 6.317   0.50 31.92 ? 230 SER B N     1 
ATOM   10338 C  CA    A SER B 2 230 ? 22.523  -31.404 5.735   0.50 36.53 ? 230 SER B CA    1 
ATOM   10339 C  CA    B SER B 2 230 ? 22.724  -31.659 6.465   0.50 36.61 ? 230 SER B CA    1 
ATOM   10340 C  C     A SER B 2 230 ? 22.069  -31.502 7.185   0.50 33.80 ? 230 SER B C     1 
ATOM   10341 C  C     B SER B 2 230 ? 22.311  -31.722 7.929   0.50 32.31 ? 230 SER B C     1 
ATOM   10342 O  O     A SER B 2 230 ? 20.891  -31.272 7.479   0.50 37.35 ? 230 SER B O     1 
ATOM   10343 O  O     B SER B 2 230 ? 21.147  -31.474 8.261   0.50 34.21 ? 230 SER B O     1 
ATOM   10344 C  CB    A SER B 2 230 ? 22.374  -32.757 5.037   0.50 34.65 ? 230 SER B CB    1 
ATOM   10345 C  CB    B SER B 2 230 ? 22.584  -33.033 5.806   0.50 32.32 ? 230 SER B CB    1 
ATOM   10346 O  OG    A SER B 2 230 ? 23.290  -33.700 5.560   0.50 34.68 ? 230 SER B OG    1 
ATOM   10347 O  OG    B SER B 2 230 ? 23.293  -34.023 6.527   0.50 34.18 ? 230 SER B OG    1 
ATOM   10348 N  N     A ALA B 2 231 ? 22.981  -31.837 8.101   0.50 28.52 ? 231 ALA B N     1 
ATOM   10349 N  N     B ALA B 2 231 ? 23.244  -32.057 8.822   0.50 28.67 ? 231 ALA B N     1 
ATOM   10350 C  CA    A ALA B 2 231 ? 22.626  -31.884 9.515   0.50 35.07 ? 231 ALA B CA    1 
ATOM   10351 C  CA    B ALA B 2 231 ? 22.939  -31.987 10.246  0.50 36.62 ? 231 ALA B CA    1 
ATOM   10352 C  C     A ALA B 2 231 ? 22.344  -30.488 10.057  0.50 34.61 ? 231 ALA B C     1 
ATOM   10353 C  C     B ALA B 2 231 ? 22.677  -30.551 10.681  0.50 34.21 ? 231 ALA B C     1 
ATOM   10354 O  O     A ALA B 2 231 ? 21.371  -30.288 10.794  0.50 34.99 ? 231 ALA B O     1 
ATOM   10355 O  O     B ALA B 2 231 ? 21.912  -30.317 11.622  0.50 38.34 ? 231 ALA B O     1 
ATOM   10356 C  CB    A ALA B 2 231 ? 23.739  -32.559 10.315  0.50 36.87 ? 231 ALA B CB    1 
ATOM   10357 C  CB    B ALA B 2 231 ? 24.078  -32.594 11.066  0.50 34.40 ? 231 ALA B CB    1 
ATOM   10358 N  N     A THR B 2 232 ? 23.188  -29.514 9.706   0.50 34.11 ? 232 THR B N     1 
ATOM   10359 N  N     B THR B 2 232 ? 23.286  -29.582 9.994   0.50 33.01 ? 232 THR B N     1 
ATOM   10360 C  CA    A THR B 2 232 ? 22.950  -28.129 10.101  0.50 33.35 ? 232 THR B CA    1 
ATOM   10361 C  CA    B THR B 2 232 ? 23.116  -28.175 10.341  0.50 33.27 ? 232 THR B CA    1 
ATOM   10362 C  C     A THR B 2 232 ? 21.602  -27.637 9.592   0.50 32.50 ? 232 THR B C     1 
ATOM   10363 C  C     B THR B 2 232 ? 21.786  -27.628 9.835   0.50 32.36 ? 232 THR B C     1 
ATOM   10364 O  O     A THR B 2 232 ? 20.832  -27.016 10.334  0.50 31.98 ? 232 THR B O     1 
ATOM   10365 O  O     B THR B 2 232 ? 21.066  -26.952 10.577  0.50 31.98 ? 232 THR B O     1 
ATOM   10366 C  CB    A THR B 2 232 ? 24.075  -27.234 9.575   0.50 33.24 ? 232 THR B CB    1 
ATOM   10367 C  CB    B THR B 2 232 ? 24.280  -27.352 9.780   0.50 33.56 ? 232 THR B CB    1 
ATOM   10368 O  OG1   A THR B 2 232 ? 25.265  -27.460 10.340  0.50 35.81 ? 232 THR B OG1   1 
ATOM   10369 O  OG1   B THR B 2 232 ? 25.512  -27.823 10.341  0.50 36.08 ? 232 THR B OG1   1 
ATOM   10370 C  CG2   A THR B 2 232 ? 23.683  -25.763 9.668   0.50 30.08 ? 232 THR B CG2   1 
ATOM   10371 C  CG2   B THR B 2 232 ? 24.106  -25.875 10.116  0.50 32.03 ? 232 THR B CG2   1 
ATOM   10372 N  N     A MET B 2 233 ? 21.301  -27.904 8.320   0.50 31.62 ? 233 MET B N     1 
ATOM   10373 N  N     B MET B 2 233 ? 21.444  -27.901 8.572   0.50 31.81 ? 233 MET B N     1 
ATOM   10374 C  CA    A MET B 2 233 ? 20.031  -27.472 7.753   0.50 28.86 ? 233 MET B CA    1 
ATOM   10375 C  CA    B MET B 2 233 ? 20.172  -27.415 8.044   0.50 29.96 ? 233 MET B CA    1 
ATOM   10376 C  C     A MET B 2 233 ? 18.847  -28.173 8.402   0.50 35.08 ? 233 MET B C     1 
ATOM   10377 C  C     B MET B 2 233 ? 18.996  -28.044 8.781   0.50 34.95 ? 233 MET B C     1 
ATOM   10378 O  O     A MET B 2 233 ? 17.735  -27.633 8.384   0.50 36.66 ? 233 MET B O     1 
ATOM   10379 O  O     B MET B 2 233 ? 17.995  -27.370 9.058   0.50 34.37 ? 233 MET B O     1 
ATOM   10380 C  CB    A MET B 2 233 ? 20.030  -27.711 6.247   0.50 32.09 ? 233 MET B CB    1 
ATOM   10381 C  CB    B MET B 2 233 ? 20.078  -27.688 6.543   0.50 30.81 ? 233 MET B CB    1 
ATOM   10382 C  CG    A MET B 2 233 ? 21.183  -27.023 5.538   0.50 29.91 ? 233 MET B CG    1 
ATOM   10383 C  CG    B MET B 2 233 ? 20.988  -26.803 5.698   0.50 31.48 ? 233 MET B CG    1 
ATOM   10384 S  SD    A MET B 2 233 ? 21.353  -27.572 3.840   0.50 35.00 ? 233 MET B SD    1 
ATOM   10385 S  SD    B MET B 2 233 ? 20.711  -26.969 3.925   0.50 32.59 ? 233 MET B SD    1 
ATOM   10386 C  CE    A MET B 2 233 ? 19.779  -27.040 3.189   0.50 30.63 ? 233 MET B CE    1 
ATOM   10387 C  CE    B MET B 2 233 ? 19.040  -26.342 3.765   0.50 32.41 ? 233 MET B CE    1 
ATOM   10388 N  N     A SER B 2 234 ? 19.056  -29.364 8.969   0.50 33.74 ? 234 SER B N     1 
ATOM   10389 N  N     B SER B 2 234 ? 19.099  -29.334 9.110   0.50 33.76 ? 234 SER B N     1 
ATOM   10390 C  CA    A SER B 2 234 ? 18.009  -29.985 9.772   0.50 32.52 ? 234 SER B CA    1 
ATOM   10391 C  CA    B SER B 2 234 ? 18.055  -29.985 9.895   0.50 32.44 ? 234 SER B CA    1 
ATOM   10392 C  C     A SER B 2 234 ? 17.792  -29.216 11.068  0.50 34.36 ? 234 SER B C     1 
ATOM   10393 C  C     B SER B 2 234 ? 17.879  -29.295 11.241  0.50 34.16 ? 234 SER B C     1 
ATOM   10394 O  O     A SER B 2 234 ? 16.646  -29.002 11.487  0.50 35.61 ? 234 SER B O     1 
ATOM   10395 O  O     B SER B 2 234 ? 16.751  -29.032 11.678  0.50 35.84 ? 234 SER B O     1 
ATOM   10396 C  CB    A SER B 2 234 ? 18.362  -31.443 10.062  0.50 37.12 ? 234 SER B CB    1 
ATOM   10397 C  CB    B SER B 2 234 ? 18.387  -31.465 10.090  0.50 37.12 ? 234 SER B CB    1 
ATOM   10398 O  OG    A SER B 2 234 ? 17.498  -31.990 11.044  0.50 40.60 ? 234 SER B OG    1 
ATOM   10399 O  OG    B SER B 2 234 ? 17.593  -32.037 11.117  0.50 40.52 ? 234 SER B OG    1 
ATOM   10400 N  N     A GLY B 2 235 ? 18.875  -28.774 11.704  0.50 32.10 ? 235 GLY B N     1 
ATOM   10401 N  N     B GLY B 2 235 ? 18.989  -28.979 11.906  0.50 31.85 ? 235 GLY B N     1 
ATOM   10402 C  CA    A GLY B 2 235 ? 18.770  -28.063 12.961  0.50 33.94 ? 235 GLY B CA    1 
ATOM   10403 C  CA    B GLY B 2 235 ? 18.900  -28.370 13.223  0.50 32.83 ? 235 GLY B CA    1 
ATOM   10404 C  C     A GLY B 2 235 ? 18.072  -26.723 12.849  0.50 35.09 ? 235 GLY B C     1 
ATOM   10405 C  C     B GLY B 2 235 ? 18.364  -26.951 13.181  0.50 35.98 ? 235 GLY B C     1 
ATOM   10406 O  O     A GLY B 2 235 ? 17.083  -26.476 13.544  0.50 30.24 ? 235 GLY B O     1 
ATOM   10407 O  O     B GLY B 2 235 ? 17.502  -26.579 13.982  0.50 30.97 ? 235 GLY B O     1 
ATOM   10408 N  N     A VAL B 2 236 ? 18.567  -25.846 11.971  0.50 32.45 ? 236 VAL B N     1 
ATOM   10409 N  N     B VAL B 2 236 ? 18.863  -26.136 12.246  0.50 29.87 ? 236 VAL B N     1 
ATOM   10410 C  CA    A VAL B 2 236 ? 18.012  -24.498 11.875  0.50 32.42 ? 236 VAL B CA    1 
ATOM   10411 C  CA    B VAL B 2 236 ? 18.470  -24.730 12.225  0.50 32.18 ? 236 VAL B CA    1 
ATOM   10412 C  C     A VAL B 2 236 ? 16.611  -24.460 11.282  0.50 31.14 ? 236 VAL B C     1 
ATOM   10413 C  C     B VAL B 2 236 ? 17.003  -24.544 11.849  0.50 29.71 ? 236 VAL B C     1 
ATOM   10414 O  O     A VAL B 2 236 ? 16.001  -23.385 11.235  0.50 27.57 ? 236 VAL B O     1 
ATOM   10415 O  O     B VAL B 2 236 ? 16.435  -23.480 12.115  0.50 28.97 ? 236 VAL B O     1 
ATOM   10416 C  CB    A VAL B 2 236 ? 18.936  -23.577 11.051  0.50 29.89 ? 236 VAL B CB    1 
ATOM   10417 C  CB    B VAL B 2 236 ? 19.369  -23.914 11.275  0.50 32.77 ? 236 VAL B CB    1 
ATOM   10418 C  CG1   A VAL B 2 236 ? 20.253  -23.359 11.781  0.50 33.83 ? 236 VAL B CG1   1 
ATOM   10419 C  CG1   B VAL B 2 236 ? 20.825  -23.989 11.717  0.50 34.45 ? 236 VAL B CG1   1 
ATOM   10420 C  CG2   A VAL B 2 236 ? 19.179  -24.159 9.672   0.50 32.57 ? 236 VAL B CG2   1 
ATOM   10421 C  CG2   B VAL B 2 236 ? 19.208  -24.389 9.844   0.50 32.39 ? 236 VAL B CG2   1 
ATOM   10422 N  N     A THR B 2 237 ? 16.083  -25.592 10.818  0.50 30.95 ? 237 THR B N     1 
ATOM   10423 N  N     B THR B 2 237 ? 16.372  -25.545 11.238  0.50 30.75 ? 237 THR B N     1 
ATOM   10424 C  CA    A THR B 2 237 ? 14.716  -25.659 10.315  0.50 34.23 ? 237 THR B CA    1 
ATOM   10425 C  CA    B THR B 2 237 ? 14.966  -25.470 10.862  0.50 34.42 ? 237 THR B CA    1 
ATOM   10426 C  C     A THR B 2 237 ? 13.803  -26.491 11.207  0.50 38.80 ? 237 THR B C     1 
ATOM   10427 C  C     B THR B 2 237 ? 14.062  -26.288 11.780  0.50 35.50 ? 237 THR B C     1 
ATOM   10428 O  O     A THR B 2 237 ? 12.654  -26.750 10.829  0.50 37.32 ? 237 THR B O     1 
ATOM   10429 O  O     B THR B 2 237 ? 12.884  -26.480 11.460  0.50 34.54 ? 237 THR B O     1 
ATOM   10430 C  CB    A THR B 2 237 ? 14.696  -26.217 8.889   0.50 37.28 ? 237 THR B CB    1 
ATOM   10431 C  CB    B THR B 2 237 ? 14.776  -25.932 9.415   0.50 36.82 ? 237 THR B CB    1 
ATOM   10432 O  OG1   A THR B 2 237 ? 15.229  -27.547 8.884   0.50 36.34 ? 237 THR B OG1   1 
ATOM   10433 O  OG1   B THR B 2 237 ? 15.076  -27.330 9.316   0.50 33.96 ? 237 THR B OG1   1 
ATOM   10434 C  CG2   A THR B 2 237 ? 15.515  -25.329 7.958   0.50 32.88 ? 237 THR B CG2   1 
ATOM   10435 C  CG2   B THR B 2 237 ? 15.686  -25.143 8.472   0.50 33.27 ? 237 THR B CG2   1 
ATOM   10436 N  N     A THR B 2 238 ? 14.284  -26.915 12.378  0.50 31.37 ? 238 THR B N     1 
ATOM   10437 N  N     B THR B 2 238 ? 14.584  -26.770 12.911  0.50 31.79 ? 238 THR B N     1 
ATOM   10438 C  CA    A THR B 2 238 ? 13.483  -27.758 13.261  0.50 37.48 ? 238 THR B CA    1 
ATOM   10439 C  CA    B THR B 2 238 ? 13.797  -27.639 13.781  0.50 36.10 ? 238 THR B CA    1 
ATOM   10440 C  C     A THR B 2 238 ? 12.196  -27.056 13.681  0.50 38.28 ? 238 THR B C     1 
ATOM   10441 C  C     B THR B 2 238 ? 12.540  -26.940 14.287  0.50 37.01 ? 238 THR B C     1 
ATOM   10442 O  O     A THR B 2 238 ? 11.090  -27.554 13.435  0.50 34.65 ? 238 THR B O     1 
ATOM   10443 O  O     B THR B 2 238 ? 11.452  -27.527 14.282  0.50 38.60 ? 238 THR B O     1 
ATOM   10444 C  CB    A THR B 2 238 ? 14.306  -28.155 14.488  0.50 37.88 ? 238 THR B CB    1 
ATOM   10445 C  CB    B THR B 2 238 ? 14.652  -28.120 14.952  0.50 39.52 ? 238 THR B CB    1 
ATOM   10446 O  OG1   A THR B 2 238 ? 15.320  -29.095 14.106  0.50 35.97 ? 238 THR B OG1   1 
ATOM   10447 O  OG1   B THR B 2 238 ? 15.739  -28.911 14.453  0.50 36.94 ? 238 THR B OG1   1 
ATOM   10448 C  CG2   A THR B 2 238 ? 13.410  -28.774 15.554  0.50 40.57 ? 238 THR B CG2   1 
ATOM   10449 C  CG2   B THR B 2 238 ? 13.822  -28.960 15.917  0.50 39.00 ? 238 THR B CG2   1 
ATOM   10450 N  N     A CYS B 2 239 ? 12.321  -25.884 14.304  0.50 37.36 ? 239 CYS B N     1 
ATOM   10451 N  N     B CYS B 2 239 ? 12.667  -25.681 14.716  0.50 41.69 ? 239 CYS B N     1 
ATOM   10452 C  CA    A CYS B 2 239 ? 11.168  -25.175 14.844  0.50 40.58 ? 239 CYS B CA    1 
ATOM   10453 C  CA    B CYS B 2 239 ? 11.506  -24.947 15.210  0.50 38.07 ? 239 CYS B CA    1 
ATOM   10454 C  C     A CYS B 2 239 ? 10.297  -24.550 13.765  0.50 40.98 ? 239 CYS B C     1 
ATOM   10455 C  C     B CYS B 2 239 ? 10.463  -24.762 14.115  0.50 42.02 ? 239 CYS B C     1 
ATOM   10456 O  O     A CYS B 2 239 ? 9.296   -23.905 14.100  0.50 36.71 ? 239 CYS B O     1 
ATOM   10457 O  O     B CYS B 2 239 ? 9.257   -24.767 14.388  0.50 36.75 ? 239 CYS B O     1 
ATOM   10458 C  CB    A CYS B 2 239 ? 11.632  -24.109 15.832  0.50 38.78 ? 239 CYS B CB    1 
ATOM   10459 C  CB    B CYS B 2 239 ? 11.939  -23.593 15.768  0.50 39.91 ? 239 CYS B CB    1 
ATOM   10460 S  SG    A CYS B 2 239 ? 12.695  -24.762 17.133  0.50 39.58 ? 239 CYS B SG    1 
ATOM   10461 S  SG    B CYS B 2 239 ? 13.033  -23.699 17.199  0.50 46.17 ? 239 CYS B SG    1 
ATOM   10462 N  N     A LEU B 2 240 ? 10.655  -24.719 12.494  0.50 33.20 ? 240 LEU B N     1 
ATOM   10463 N  N     B LEU B 2 240 ? 10.908  -24.607 12.867  0.50 32.65 ? 240 LEU B N     1 
ATOM   10464 C  CA    A LEU B 2 240 ? 9.767   -24.411 11.384  0.50 38.34 ? 240 LEU B CA    1 
ATOM   10465 C  CA    B LEU B 2 240 ? 9.972   -24.475 11.757  0.50 36.73 ? 240 LEU B CA    1 
ATOM   10466 C  C     A LEU B 2 240 ? 8.928   -25.608 10.959  0.50 37.15 ? 240 LEU B C     1 
ATOM   10467 C  C     B LEU B 2 240 ? 9.184   -25.758 11.523  0.50 35.98 ? 240 LEU B C     1 
ATOM   10468 O  O     A LEU B 2 240 ? 7.858   -25.421 10.369  0.50 39.95 ? 240 LEU B O     1 
ATOM   10469 O  O     B LEU B 2 240 ? 8.077   -25.711 10.975  0.50 37.41 ? 240 LEU B O     1 
ATOM   10470 C  CB    A LEU B 2 240 ? 10.576  -23.920 10.179  0.50 39.58 ? 240 LEU B CB    1 
ATOM   10471 C  CB    B LEU B 2 240 ? 10.716  -24.083 10.480  0.50 40.06 ? 240 LEU B CB    1 
ATOM   10472 C  CG    A LEU B 2 240 ? 11.392  -22.645 10.379  0.50 37.79 ? 240 LEU B CG    1 
ATOM   10473 C  CG    B LEU B 2 240 ? 11.319  -22.680 10.409  0.50 37.84 ? 240 LEU B CG    1 
ATOM   10474 C  CD1   A LEU B 2 240 ? 12.303  -22.396 9.192   0.50 40.22 ? 240 LEU B CD1   1 
ATOM   10475 C  CD1   B LEU B 2 240 ? 12.297  -22.578 9.254   0.50 40.12 ? 240 LEU B CD1   1 
ATOM   10476 C  CD2   A LEU B 2 240 ? 10.452  -21.480 10.581  0.50 39.23 ? 240 LEU B CD2   1 
ATOM   10477 C  CD2   B LEU B 2 240 ? 10.217  -21.650 10.263  0.50 40.74 ? 240 LEU B CD2   1 
ATOM   10478 N  N     A ARG B 2 241 ? 9.387   -26.827 11.251  0.50 38.19 ? 241 ARG B N     1 
ATOM   10479 N  N     B ARG B 2 241 ? 9.723   -26.905 11.935  0.50 35.53 ? 241 ARG B N     1 
ATOM   10480 C  CA    A ARG B 2 241 ? 8.761   -28.047 10.759  0.50 39.58 ? 241 ARG B CA    1 
ATOM   10481 C  CA    B ARG B 2 241 ? 9.176   -28.199 11.544  0.50 41.90 ? 241 ARG B CA    1 
ATOM   10482 C  C     A ARG B 2 241 ? 8.039   -28.844 11.835  0.50 38.29 ? 241 ARG B C     1 
ATOM   10483 C  C     B ARG B 2 241 ? 8.560   -28.986 12.694  0.50 40.01 ? 241 ARG B C     1 
ATOM   10484 O  O     A ARG B 2 241 ? 7.366   -29.825 11.502  0.50 38.23 ? 241 ARG B O     1 
ATOM   10485 O  O     B ARG B 2 241 ? 8.086   -30.106 12.469  0.50 41.03 ? 241 ARG B O     1 
ATOM   10486 C  CB    A ARG B 2 241 ? 9.813   -28.953 10.098  0.50 34.08 ? 241 ARG B CB    1 
ATOM   10487 C  CB    B ARG B 2 241 ? 10.265  -29.043 10.869  0.50 35.21 ? 241 ARG B CB    1 
ATOM   10488 C  CG    A ARG B 2 241 ? 10.538  -28.319 8.925   0.50 38.81 ? 241 ARG B CG    1 
ATOM   10489 C  CG    B ARG B 2 241 ? 10.867  -28.387 9.640   0.50 35.41 ? 241 ARG B CG    1 
ATOM   10490 C  CD    A ARG B 2 241 ? 11.649  -29.214 8.393   0.50 35.18 ? 241 ARG B CD    1 
ATOM   10491 C  CD    B ARG B 2 241 ? 11.832  -29.312 8.912   0.50 34.83 ? 241 ARG B CD    1 
ATOM   10492 N  NE    A ARG B 2 241 ? 12.703  -29.443 9.376   0.50 35.80 ? 241 ARG B NE    1 
ATOM   10493 N  NE    B ARG B 2 241 ? 13.050  -29.562 9.676   0.50 35.87 ? 241 ARG B NE    1 
ATOM   10494 C  CZ    A ARG B 2 241 ? 13.045  -30.634 9.849   0.50 39.70 ? 241 ARG B CZ    1 
ATOM   10495 C  CZ    B ARG B 2 241 ? 13.330  -30.703 10.290  0.50 39.25 ? 241 ARG B CZ    1 
ATOM   10496 N  NH1   A ARG B 2 241 ? 12.444  -31.740 9.438   0.50 39.49 ? 241 ARG B NH1   1 
ATOM   10497 N  NH1   B ARG B 2 241 ? 12.498  -31.730 10.253  0.50 41.11 ? 241 ARG B NH1   1 
ATOM   10498 N  NH2   A ARG B 2 241 ? 14.022  -30.720 10.747  0.50 35.70 ? 241 ARG B NH2   1 
ATOM   10499 N  NH2   B ARG B 2 241 ? 14.478  -30.819 10.951  0.50 34.63 ? 241 ARG B NH2   1 
ATOM   10500 N  N     A PHE B 2 242 ? 8.174   -28.469 13.102  0.50 37.37 ? 242 PHE B N     1 
ATOM   10501 N  N     B PHE B 2 242 ? 8.564   -28.449 13.916  0.50 40.80 ? 242 PHE B N     1 
ATOM   10502 C  CA    A PHE B 2 242 ? 7.546   -29.158 14.218  0.50 45.06 ? 242 PHE B CA    1 
ATOM   10503 C  CA    B PHE B 2 242 ? 7.950   -29.134 15.052  0.50 43.77 ? 242 PHE B CA    1 
ATOM   10504 C  C     A PHE B 2 242 ? 6.845   -28.140 15.104  0.50 45.09 ? 242 PHE B C     1 
ATOM   10505 C  C     B PHE B 2 242 ? 7.320   -28.100 15.972  0.50 43.60 ? 242 PHE B C     1 
ATOM   10506 O  O     A PHE B 2 242 ? 7.230   -26.966 15.121  0.50 48.96 ? 242 PHE B O     1 
ATOM   10507 O  O     B PHE B 2 242 ? 7.930   -27.047 16.213  0.50 41.63 ? 242 PHE B O     1 
ATOM   10508 C  CB    A PHE B 2 242 ? 8.585   -29.948 15.031  0.50 43.01 ? 242 PHE B CB    1 
ATOM   10509 C  CB    B PHE B 2 242 ? 8.958   -29.982 15.837  0.50 43.82 ? 242 PHE B CB    1 
ATOM   10510 C  CG    A PHE B 2 242 ? 9.170   -31.120 14.290  0.50 41.06 ? 242 PHE B CG    1 
ATOM   10511 C  CG    B PHE B 2 242 ? 9.558   -31.111 15.042  0.50 38.88 ? 242 PHE B CG    1 
ATOM   10512 C  CD1   A PHE B 2 242 ? 8.530   -32.349 14.295  0.50 40.32 ? 242 PHE B CD1   1 
ATOM   10513 C  CD1   B PHE B 2 242 ? 8.795   -32.212 14.692  0.50 38.70 ? 242 PHE B CD1   1 
ATOM   10514 C  CD2   A PHE B 2 242 ? 10.359  -30.993 13.586  0.50 39.63 ? 242 PHE B CD2   1 
ATOM   10515 C  CD2   B PHE B 2 242 ? 10.889  -31.073 14.652  0.50 44.20 ? 242 PHE B CD2   1 
ATOM   10516 C  CE1   A PHE B 2 242 ? 9.062   -33.429 13.613  0.50 42.54 ? 242 PHE B CE1   1 
ATOM   10517 C  CE1   B PHE B 2 242 ? 9.345   -33.251 13.962  0.50 42.80 ? 242 PHE B CE1   1 
ATOM   10518 C  CE2   A PHE B 2 242 ? 10.898  -32.070 12.904  0.50 44.06 ? 242 PHE B CE2   1 
ATOM   10519 C  CE2   B PHE B 2 242 ? 11.444  -32.109 13.928  0.50 38.91 ? 242 PHE B CE2   1 
ATOM   10520 C  CZ    A PHE B 2 242 ? 10.248  -33.289 12.917  0.50 44.30 ? 242 PHE B CZ    1 
ATOM   10521 C  CZ    B PHE B 2 242 ? 10.672  -33.199 13.581  0.50 43.21 ? 242 PHE B CZ    1 
ATOM   10522 N  N     A PRO B 2 243 ? 5.797   -28.554 15.844  0.50 46.22 ? 243 PRO B N     1 
ATOM   10523 N  N     B PRO B 2 243 ? 6.116   -28.370 16.505  0.50 46.11 ? 243 PRO B N     1 
ATOM   10524 C  CA    A PRO B 2 243 ? 4.976   -27.577 16.579  0.50 49.25 ? 243 PRO B CA    1 
ATOM   10525 C  CA    B PRO B 2 243 ? 5.409   -27.364 17.314  0.50 50.03 ? 243 PRO B CA    1 
ATOM   10526 C  C     A PRO B 2 243 ? 5.773   -26.668 17.505  0.50 49.59 ? 243 PRO B C     1 
ATOM   10527 C  C     B PRO B 2 243 ? 6.214   -26.872 18.507  0.50 50.59 ? 243 PRO B C     1 
ATOM   10528 O  O     A PRO B 2 243 ? 5.971   -25.489 17.198  0.50 49.13 ? 243 PRO B O     1 
ATOM   10529 O  O     B PRO B 2 243 ? 6.614   -25.704 18.553  0.50 48.03 ? 243 PRO B O     1 
ATOM   10530 C  CB    A PRO B 2 243 ? 3.998   -28.460 17.369  0.50 42.72 ? 243 PRO B CB    1 
ATOM   10531 C  CB    B PRO B 2 243 ? 4.143   -28.106 17.766  0.50 43.85 ? 243 PRO B CB    1 
ATOM   10532 C  CG    A PRO B 2 243 ? 4.605   -29.830 17.368  0.50 47.08 ? 243 PRO B CG    1 
ATOM   10533 C  CG    B PRO B 2 243 ? 3.957   -29.197 16.765  0.50 45.11 ? 243 PRO B CG    1 
ATOM   10534 C  CD    A PRO B 2 243 ? 5.324   -29.932 16.060  0.50 49.36 ? 243 PRO B CD    1 
ATOM   10535 C  CD    B PRO B 2 243 ? 5.343   -29.617 16.370  0.50 50.01 ? 243 PRO B CD    1 
ATOM   10536 N  N     A GLY B 2 244 ? 6.226   -27.196 18.639  0.50 50.81 ? 244 GLY B N     1 
ATOM   10537 N  N     B GLY B 2 244 ? 6.452   -27.751 19.473  0.50 51.80 ? 244 GLY B N     1 
ATOM   10538 C  CA    A GLY B 2 244 ? 7.008   -26.405 19.570  0.50 52.55 ? 244 GLY B CA    1 
ATOM   10539 C  CA    B GLY B 2 244 ? 7.234   -27.374 20.640  0.50 56.31 ? 244 GLY B CA    1 
ATOM   10540 C  C     A GLY B 2 244 ? 6.197   -25.357 20.305  0.50 56.84 ? 244 GLY B C     1 
ATOM   10541 C  C     B GLY B 2 244 ? 6.549   -26.273 21.425  0.50 55.98 ? 244 GLY B C     1 
ATOM   10542 O  O     A GLY B 2 244 ? 5.084   -25.018 19.893  0.50 58.03 ? 244 GLY B O     1 
ATOM   10543 O  O     B GLY B 2 244 ? 5.426   -26.433 21.917  0.50 56.91 ? 244 GLY B O     1 
ATOM   10544 N  N     A GLN B 2 245 ? 6.751   -24.830 21.400  0.50 62.13 ? 245 GLN B N     1 
ATOM   10545 N  N     B GLN B 2 245 ? 7.229   -25.132 21.546  0.50 62.83 ? 245 GLN B N     1 
ATOM   10546 C  CA    A GLN B 2 245 ? 6.018   -23.852 22.196  0.50 63.15 ? 245 GLN B CA    1 
ATOM   10547 C  CA    B GLN B 2 245 ? 6.671   -23.971 22.236  0.50 61.55 ? 245 GLN B CA    1 
ATOM   10548 C  C     A GLN B 2 245 ? 5.881   -22.519 21.470  0.50 60.34 ? 245 GLN B C     1 
ATOM   10549 C  C     B GLN B 2 245 ? 6.885   -22.651 21.511  0.50 57.27 ? 245 GLN B C     1 
ATOM   10550 O  O     A GLN B 2 245 ? 4.878   -21.818 21.650  0.50 63.39 ? 245 GLN B O     1 
ATOM   10551 O  O     B GLN B 2 245 ? 6.195   -21.678 21.839  0.50 60.39 ? 245 GLN B O     1 
ATOM   10552 C  CB    A GLN B 2 245 ? 6.705   -23.652 23.546  0.50 63.57 ? 245 GLN B CB    1 
ATOM   10553 C  CB    B GLN B 2 245 ? 7.250   -23.856 23.651  0.50 63.17 ? 245 GLN B CB    1 
ATOM   10554 C  CG    A GLN B 2 245 ? 5.917   -22.786 24.511  0.50 57.26 ? 245 GLN B CG    1 
ATOM   10555 C  CG    B GLN B 2 245 ? 6.304   -24.319 24.752  0.50 59.90 ? 245 GLN B CG    1 
ATOM   10556 C  CD    A GLN B 2 245 ? 6.616   -22.618 25.842  0.50 58.44 ? 245 GLN B CD    1 
ATOM   10557 C  CD    B GLN B 2 245 ? 5.163   -23.344 24.993  0.50 60.57 ? 245 GLN B CD    1 
ATOM   10558 O  OE1   A GLN B 2 245 ? 5.974   -22.374 26.864  0.50 48.57 ? 245 GLN B OE1   1 
ATOM   10559 O  OE1   B GLN B 2 245 ? 5.175   -22.219 24.492  0.50 55.61 ? 245 GLN B OE1   1 
ATOM   10560 N  NE2   A GLN B 2 245 ? 7.939   -22.747 25.840  0.50 62.71 ? 245 GLN B NE2   1 
ATOM   10561 N  NE2   B GLN B 2 245 ? 4.171   -23.772 25.768  0.50 56.22 ? 245 GLN B NE2   1 
ATOM   10562 N  N     A LEU B 2 246 ? 6.868   -22.150 20.661  0.50 53.03 ? 246 LEU B N     1 
ATOM   10563 N  N     B LEU B 2 246 ? 7.805   -22.566 20.554  0.50 53.57 ? 246 LEU B N     1 
ATOM   10564 C  CA    A LEU B 2 246 ? 6.783   -20.947 19.849  0.50 52.32 ? 246 LEU B CA    1 
ATOM   10565 C  CA    B LEU B 2 246 ? 8.004   -21.359 19.761  0.50 54.10 ? 246 LEU B CA    1 
ATOM   10566 C  C     A LEU B 2 246 ? 6.210   -21.280 18.479  0.50 52.16 ? 246 LEU B C     1 
ATOM   10567 C  C     B LEU B 2 246 ? 7.069   -21.405 18.559  0.50 52.22 ? 246 LEU B C     1 
ATOM   10568 O  O     A LEU B 2 246 ? 6.322   -22.409 17.993  0.50 54.61 ? 246 LEU B O     1 
ATOM   10569 O  O     B LEU B 2 246 ? 7.276   -22.199 17.635  0.50 53.15 ? 246 LEU B O     1 
ATOM   10570 C  CB    A LEU B 2 246 ? 8.158   -20.297 19.677  0.50 49.90 ? 246 LEU B CB    1 
ATOM   10571 C  CB    B LEU B 2 246 ? 9.457   -21.237 19.304  0.50 49.38 ? 246 LEU B CB    1 
ATOM   10572 C  CG    A LEU B 2 246 ? 8.945   -19.842 20.905  0.50 52.61 ? 246 LEU B CG    1 
ATOM   10573 C  CG    B LEU B 2 246 ? 10.484  -20.549 20.202  0.50 43.81 ? 246 LEU B CG    1 
ATOM   10574 C  CD1   A LEU B 2 246 ? 10.361  -19.480 20.491  0.50 45.93 ? 246 LEU B CD1   1 
ATOM   10575 C  CD1   B LEU B 2 246 ? 11.836  -20.514 19.510  0.50 43.51 ? 246 LEU B CD1   1 
ATOM   10576 C  CD2   A LEU B 2 246 ? 8.264   -18.661 21.582  0.50 48.92 ? 246 LEU B CD2   1 
ATOM   10577 C  CD2   B LEU B 2 246 ? 10.031  -19.144 20.563  0.50 46.56 ? 246 LEU B CD2   1 
ATOM   10578 N  N     A ASN B 2 247 ? 5.588   -20.284 17.861  0.50 52.18 ? 247 ASN B N     1 
ATOM   10579 N  N     B ASN B 2 247 ? 6.040   -20.558 18.569  0.50 51.68 ? 247 ASN B N     1 
ATOM   10580 C  CA    A ASN B 2 247 ? 5.193   -20.378 16.456  0.50 48.35 ? 247 ASN B CA    1 
ATOM   10581 C  CA    B ASN B 2 247 ? 5.215   -20.394 17.379  0.50 52.66 ? 247 ASN B CA    1 
ATOM   10582 C  C     A ASN B 2 247 ? 6.255   -19.718 15.580  0.50 43.61 ? 247 ASN B C     1 
ATOM   10583 C  C     B ASN B 2 247 ? 6.101   -19.845 16.268  0.50 42.40 ? 247 ASN B C     1 
ATOM   10584 O  O     A ASN B 2 247 ? 6.019   -18.727 14.889  0.50 43.01 ? 247 ASN B O     1 
ATOM   10585 O  O     B ASN B 2 247 ? 6.123   -18.636 16.016  0.50 45.55 ? 247 ASN B O     1 
ATOM   10586 C  CB    A ASN B 2 247 ? 3.819   -19.748 16.246  0.50 45.08 ? 247 ASN B CB    1 
ATOM   10587 C  CB    B ASN B 2 247 ? 4.024   -19.475 17.655  0.50 46.62 ? 247 ASN B CB    1 
ATOM   10588 C  CG    A ASN B 2 247 ? 3.285   -19.969 14.844  0.50 44.85 ? 247 ASN B CG    1 
ATOM   10589 C  CG    B ASN B 2 247 ? 2.729   -20.007 17.062  0.50 47.27 ? 247 ASN B CG    1 
ATOM   10590 O  OD1   A ASN B 2 247 ? 3.721   -20.880 14.138  0.50 48.43 ? 247 ASN B OD1   1 
ATOM   10591 O  OD1   B ASN B 2 247 ? 2.736   -20.657 16.013  0.50 36.18 ? 247 ASN B OD1   1 
ATOM   10592 N  ND2   A ASN B 2 247 ? 2.337   -19.134 14.433  0.50 38.61 ? 247 ASN B ND2   1 
ATOM   10593 N  ND2   B ASN B 2 247 ? 1.611   -19.740 17.736  0.50 33.54 ? 247 ASN B ND2   1 
ATOM   10594 N  N     A ALA B 2 248 ? 7.455   -20.293 15.636  0.50 43.65 ? 248 ALA B N     1 
ATOM   10595 N  N     B ALA B 2 248 ? 6.826   -20.738 15.599  0.50 47.34 ? 248 ALA B N     1 
ATOM   10596 C  CA    A ALA B 2 248 ? 8.607   -19.706 14.967  0.50 40.28 ? 248 ALA B CA    1 
ATOM   10597 C  CA    B ALA B 2 248 ? 8.001   -20.384 14.819  0.50 41.41 ? 248 ALA B CA    1 
ATOM   10598 C  C     A ALA B 2 248 ? 8.445   -19.767 13.454  0.50 40.51 ? 248 ALA B C     1 
ATOM   10599 C  C     B ALA B 2 248 ? 7.651   -19.941 13.405  0.50 41.16 ? 248 ALA B C     1 
ATOM   10600 O  O     A ALA B 2 248 ? 8.140   -20.821 12.887  0.50 35.97 ? 248 ALA B O     1 
ATOM   10601 O  O     B ALA B 2 248 ? 6.704   -20.436 12.787  0.50 39.81 ? 248 ALA B O     1 
ATOM   10602 C  CB    A ALA B 2 248 ? 9.890   -20.422 15.389  0.50 35.85 ? 248 ALA B CB    1 
ATOM   10603 C  CB    B ALA B 2 248 ? 8.969   -21.564 14.753  0.50 41.81 ? 248 ALA B CB    1 
ATOM   10604 N  N     A ASP B 2 249 ? 8.650   -18.626 12.804  0.50 33.23 ? 249 ASP B N     1 
ATOM   10605 N  N     B ASP B 2 249 ? 8.446   -19.001 12.898  0.50 35.72 ? 249 ASP B N     1 
ATOM   10606 C  CA    A ASP B 2 249 ? 8.641   -18.523 11.356  0.50 35.97 ? 249 ASP B CA    1 
ATOM   10607 C  CA    B ASP B 2 249 ? 8.410   -18.567 11.508  0.50 35.59 ? 249 ASP B CA    1 
ATOM   10608 C  C     A ASP B 2 249 ? 9.861   -17.724 10.919  0.50 32.17 ? 249 ASP B C     1 
ATOM   10609 C  C     B ASP B 2 249 ? 9.621   -17.679 11.263  0.50 34.13 ? 249 ASP B C     1 
ATOM   10610 O  O     A ASP B 2 249 ? 10.695  -17.324 11.738  0.50 31.01 ? 249 ASP B O     1 
ATOM   10611 O  O     B ASP B 2 249 ? 10.217  -17.139 12.202  0.50 26.67 ? 249 ASP B O     1 
ATOM   10612 C  CB    A ASP B 2 249 ? 7.345   -17.881 10.846  0.50 35.25 ? 249 ASP B CB    1 
ATOM   10613 C  CB    B ASP B 2 249 ? 7.112   -17.833 11.163  0.50 35.50 ? 249 ASP B CB    1 
ATOM   10614 C  CG    A ASP B 2 249 ? 7.010   -16.594 11.564  0.50 36.16 ? 249 ASP B CG    1 
ATOM   10615 C  CG    B ASP B 2 249 ? 6.796   -16.726 12.135  0.50 36.50 ? 249 ASP B CG    1 
ATOM   10616 O  OD1   A ASP B 2 249 ? 7.862   -15.683 11.586  0.50 27.60 ? 249 ASP B OD1   1 
ATOM   10617 O  OD1   B ASP B 2 249 ? 7.201   -16.831 13.311  0.50 39.84 ? 249 ASP B OD1   1 
ATOM   10618 O  OD2   A ASP B 2 249 ? 5.886   -16.491 12.101  0.50 35.56 ? 249 ASP B OD2   1 
ATOM   10619 O  OD2   B ASP B 2 249 ? 6.131   -15.752 11.724  0.50 36.96 ? 249 ASP B OD2   1 
ATOM   10620 N  N     A LEU B 2 250 ? 9.956   -17.484 9.612   0.50 31.45 ? 250 LEU B N     1 
ATOM   10621 N  N     B LEU B 2 250 ? 9.974   -17.535 9.984   0.50 30.58 ? 250 LEU B N     1 
ATOM   10622 C  CA    A LEU B 2 250 ? 11.109  -16.780 9.068   0.50 32.56 ? 250 LEU B CA    1 
ATOM   10623 C  CA    B LEU B 2 250 ? 11.226  -16.883 9.614   0.50 31.43 ? 250 LEU B CA    1 
ATOM   10624 C  C     A LEU B 2 250 ? 11.145  -15.314 9.478   0.50 31.72 ? 250 LEU B C     1 
ATOM   10625 C  C     B LEU B 2 250 ? 11.236  -15.392 9.922   0.50 30.81 ? 250 LEU B C     1 
ATOM   10626 O  O     A LEU B 2 250 ? 12.227  -14.715 9.488   0.50 27.43 ? 250 LEU B O     1 
ATOM   10627 O  O     B LEU B 2 250 ? 12.319  -14.808 10.035  0.50 30.59 ? 250 LEU B O     1 
ATOM   10628 C  CB    A LEU B 2 250 ? 11.117  -16.903 7.544   0.50 31.43 ? 250 LEU B CB    1 
ATOM   10629 C  CB    B LEU B 2 250 ? 11.513  -17.100 8.126   0.50 33.99 ? 250 LEU B CB    1 
ATOM   10630 C  CG    A LEU B 2 250 ? 11.236  -18.343 7.038   0.50 32.23 ? 250 LEU B CG    1 
ATOM   10631 C  CG    B LEU B 2 250 ? 11.854  -18.520 7.667   0.50 31.94 ? 250 LEU B CG    1 
ATOM   10632 C  CD1   A LEU B 2 250 ? 11.089  -18.417 5.526   0.50 32.95 ? 250 LEU B CD1   1 
ATOM   10633 C  CD1   B LEU B 2 250 ? 12.076  -18.555 6.161   0.50 37.44 ? 250 LEU B CD1   1 
ATOM   10634 C  CD2   A LEU B 2 250 ? 12.560  -18.946 7.481   0.50 36.12 ? 250 LEU B CD2   1 
ATOM   10635 C  CD2   B LEU B 2 250 ? 13.080  -19.043 8.401   0.50 35.43 ? 250 LEU B CD2   1 
ATOM   10636 N  N     A ARG B 2 251 ? 9.999   -14.722 9.814   0.50 30.71 ? 251 ARG B N     1 
ATOM   10637 N  N     B ARG B 2 251 ? 10.069  -14.759 10.054  0.50 30.47 ? 251 ARG B N     1 
ATOM   10638 C  CA    A ARG B 2 251 ? 9.976   -13.317 10.200  0.50 29.44 ? 251 ARG B CA    1 
ATOM   10639 C  CA    B ARG B 2 251 ? 10.059  -13.314 10.258  0.50 29.41 ? 251 ARG B CA    1 
ATOM   10640 C  C     A ARG B 2 251 ? 10.283  -13.133 11.681  0.50 29.79 ? 251 ARG B C     1 
ATOM   10641 C  C     B ARG B 2 251 ? 10.403  -12.941 11.694  0.50 29.34 ? 251 ARG B C     1 
ATOM   10642 O  O     A ARG B 2 251 ? 11.083  -12.263 12.040  0.50 26.34 ? 251 ARG B O     1 
ATOM   10643 O  O     B ARG B 2 251 ? 11.158  -11.988 11.921  0.50 25.48 ? 251 ARG B O     1 
ATOM   10644 C  CB    A ARG B 2 251 ? 8.627   -12.682 9.847   0.50 30.15 ? 251 ARG B CB    1 
ATOM   10645 C  CB    B ARG B 2 251 ? 8.706   -12.722 9.864   0.50 30.14 ? 251 ARG B CB    1 
ATOM   10646 C  CG    A ARG B 2 251 ? 8.674   -11.159 9.816   0.50 26.97 ? 251 ARG B CG    1 
ATOM   10647 C  CG    B ARG B 2 251 ? 8.645   -11.215 10.059  0.50 26.29 ? 251 ARG B CG    1 
ATOM   10648 C  CD    A ARG B 2 251 ? 7.372   -10.556 9.324   0.50 29.80 ? 251 ARG B CD    1 
ATOM   10649 C  CD    B ARG B 2 251 ? 7.369   -10.607 9.512   0.50 29.84 ? 251 ARG B CD    1 
ATOM   10650 N  NE    A ARG B 2 251 ? 6.909   -11.173 8.088   0.50 34.60 ? 251 ARG B NE    1 
ATOM   10651 N  NE    B ARG B 2 251 ? 7.308   -10.647 8.057   0.50 32.49 ? 251 ARG B NE    1 
ATOM   10652 C  CZ    A ARG B 2 251 ? 7.044   -10.643 6.881   0.50 29.57 ? 251 ARG B CZ    1 
ATOM   10653 C  CZ    B ARG B 2 251 ? 7.943   -9.802  7.258   0.50 33.68 ? 251 ARG B CZ    1 
ATOM   10654 N  NH1   A ARG B 2 251 ? 7.635   -9.474  6.702   0.50 32.03 ? 251 ARG B NH1   1 
ATOM   10655 N  NH1   B ARG B 2 251 ? 8.733   -8.855  7.739   0.50 33.89 ? 251 ARG B NH1   1 
ATOM   10656 N  NH2   A ARG B 2 251 ? 6.571   -11.302 5.827   0.50 36.61 ? 251 ARG B NH2   1 
ATOM   10657 N  NH2   B ARG B 2 251 ? 7.787   -9.912  5.942   0.50 33.15 ? 251 ARG B NH2   1 
ATOM   10658 N  N     A LYS B 2 252 ? 9.658   -13.939 12.552  0.50 27.81 ? 252 LYS B N     1 
ATOM   10659 N  N     B LYS B 2 252 ? 9.858   -13.670 12.676  0.50 28.06 ? 252 LYS B N     1 
ATOM   10660 C  CA    A LYS B 2 252 ? 10.027  -13.927 13.965  0.50 23.77 ? 252 LYS B CA    1 
ATOM   10661 C  CA    B LYS B 2 252 ? 10.208  -13.401 14.068  0.50 23.23 ? 252 LYS B CA    1 
ATOM   10662 C  C     A LYS B 2 252 ? 11.512  -14.205 14.156  0.50 30.88 ? 252 LYS B C     1 
ATOM   10663 C  C     B LYS B 2 252 ? 11.686  -13.660 14.326  0.50 29.08 ? 252 LYS B C     1 
ATOM   10664 O  O     A LYS B 2 252 ? 12.130  -13.666 15.081  0.50 29.64 ? 252 LYS B O     1 
ATOM   10665 O  O     B LYS B 2 252 ? 12.343  -12.888 15.034  0.50 29.94 ? 252 LYS B O     1 
ATOM   10666 C  CB    A LYS B 2 252 ? 9.213   -14.959 14.744  0.50 27.88 ? 252 LYS B CB    1 
ATOM   10667 C  CB    B LYS B 2 252 ? 9.347   -14.245 15.006  0.50 29.75 ? 252 LYS B CB    1 
ATOM   10668 C  CG    A LYS B 2 252 ? 7.726   -14.674 14.844  0.50 27.65 ? 252 LYS B CG    1 
ATOM   10669 C  CG    B LYS B 2 252 ? 7.883   -13.858 15.003  0.50 22.91 ? 252 LYS B CG    1 
ATOM   10670 C  CD    A LYS B 2 252 ? 7.075   -15.654 15.812  0.50 29.88 ? 252 LYS B CD    1 
ATOM   10671 C  CD    B LYS B 2 252 ? 7.126   -14.548 16.117  0.50 25.10 ? 252 LYS B CD    1 
ATOM   10672 C  CE    A LYS B 2 252 ? 5.564   -15.654 15.689  0.50 35.40 ? 252 LYS B CE    1 
ATOM   10673 C  CE    B LYS B 2 252 ? 5.656   -14.573 15.795  0.50 32.18 ? 252 LYS B CE    1 
ATOM   10674 N  NZ    A LYS B 2 252 ? 5.111   -16.230 14.388  0.50 35.02 ? 252 LYS B NZ    1 
ATOM   10675 N  NZ    B LYS B 2 252 ? 5.465   -15.124 14.421  0.50 30.03 ? 252 LYS B NZ    1 
ATOM   10676 N  N     A LEU B 2 253 ? 12.095  -15.054 13.307  0.50 30.86 ? 253 LEU B N     1 
ATOM   10677 N  N     B LEU B 2 253 ? 12.223  -14.748 13.764  0.50 32.71 ? 253 LEU B N     1 
ATOM   10678 C  CA    A LEU B 2 253 ? 13.542  -15.240 13.329  0.50 31.38 ? 253 LEU B CA    1 
ATOM   10679 C  CA    B LEU B 2 253 ? 13.652  -15.032 13.879  0.50 29.49 ? 253 LEU B CA    1 
ATOM   10680 C  C     A LEU B 2 253 ? 14.253  -13.946 12.958  0.50 27.51 ? 253 LEU B C     1 
ATOM   10681 C  C     B LEU B 2 253 ? 14.488  -13.848 13.407  0.50 26.79 ? 253 LEU B C     1 
ATOM   10682 O  O     A LEU B 2 253 ? 15.134  -13.478 13.686  0.50 27.83 ? 253 LEU B O     1 
ATOM   10683 O  O     B LEU B 2 253 ? 15.474  -13.475 14.054  0.50 27.89 ? 253 LEU B O     1 
ATOM   10684 C  CB    A LEU B 2 253 ? 13.944  -16.370 12.377  0.50 30.70 ? 253 LEU B CB    1 
ATOM   10685 C  CB    B LEU B 2 253 ? 13.987  -16.298 13.082  0.50 33.76 ? 253 LEU B CB    1 
ATOM   10686 C  CG    A LEU B 2 253 ? 15.444  -16.615 12.188  0.50 32.58 ? 253 LEU B CG    1 
ATOM   10687 C  CG    B LEU B 2 253 ? 15.442  -16.710 12.824  0.50 33.01 ? 253 LEU B CG    1 
ATOM   10688 C  CD1   A LEU B 2 253 ? 16.044  -17.279 13.420  0.50 30.71 ? 253 LEU B CD1   1 
ATOM   10689 C  CD1   B LEU B 2 253 ? 16.215  -16.871 14.117  0.50 28.68 ? 253 LEU B CD1   1 
ATOM   10690 C  CD2   A LEU B 2 253 ? 15.708  -17.453 10.941  0.50 29.34 ? 253 LEU B CD2   1 
ATOM   10691 C  CD2   B LEU B 2 253 ? 15.483  -18.009 12.025  0.50 32.45 ? 253 LEU B CD2   1 
ATOM   10692 N  N     A ALA B 2 254 ? 13.860  -13.341 11.835  0.50 22.80 ? 254 ALA B N     1 
ATOM   10693 N  N     B ALA B 2 254 ? 14.089  -13.226 12.295  0.50 25.19 ? 254 ALA B N     1 
ATOM   10694 C  CA    A ALA B 2 254 ? 14.530  -12.137 11.351  0.50 23.32 ? 254 ALA B CA    1 
ATOM   10695 C  CA    B ALA B 2 254 ? 14.802  -12.057 11.791  0.50 23.70 ? 254 ALA B CA    1 
ATOM   10696 C  C     A ALA B 2 254 ? 14.431  -10.991 12.351  0.50 26.94 ? 254 ALA B C     1 
ATOM   10697 C  C     B ALA B 2 254 ? 14.664  -10.868 12.736  0.50 27.06 ? 254 ALA B C     1 
ATOM   10698 O  O     A ALA B 2 254 ? 15.426  -10.315 12.637  0.50 24.60 ? 254 ALA B O     1 
ATOM   10699 O  O     B ALA B 2 254 ? 15.643  -10.159 13.003  0.50 23.50 ? 254 ALA B O     1 
ATOM   10700 C  CB    A ALA B 2 254 ? 13.937  -11.723 10.007  0.50 25.61 ? 254 ALA B CB    1 
ATOM   10701 C  CB    B ALA B 2 254 ? 14.283  -11.695 10.400  0.50 23.27 ? 254 ALA B CB    1 
ATOM   10702 N  N     A VAL B 2 255 ? 13.230  -10.750 12.886  0.50 23.10 ? 255 VAL B N     1 
ATOM   10703 N  N     B VAL B 2 255 ? 13.448  -10.625 13.238  0.50 22.15 ? 255 VAL B N     1 
ATOM   10704 C  CA    A VAL B 2 255 ? 13.012  -9.576  13.727  0.50 23.15 ? 255 VAL B CA    1 
ATOM   10705 C  CA    B VAL B 2 255 ? 13.212  -9.506  14.151  0.50 22.33 ? 255 VAL B CA    1 
ATOM   10706 C  C     A VAL B 2 255 ? 13.853  -9.645  14.992  0.50 23.31 ? 255 VAL B C     1 
ATOM   10707 C  C     B VAL B 2 255 ? 14.077  -9.639  15.395  0.50 23.32 ? 255 VAL B C     1 
ATOM   10708 O  O     A VAL B 2 255 ? 14.334  -8.617  15.482  0.50 20.47 ? 255 VAL B O     1 
ATOM   10709 O  O     B VAL B 2 255 ? 14.594  -8.647  15.921  0.50 25.50 ? 255 VAL B O     1 
ATOM   10710 C  CB    A VAL B 2 255 ? 11.510  -9.426  14.050  0.50 23.42 ? 255 VAL B CB    1 
ATOM   10711 C  CB    B VAL B 2 255 ? 11.716  -9.426  14.517  0.50 23.26 ? 255 VAL B CB    1 
ATOM   10712 C  CG1   A VAL B 2 255 ? 11.278  -8.285  15.031  0.50 24.20 ? 255 VAL B CG1   1 
ATOM   10713 C  CG1   B VAL B 2 255 ? 11.505  -8.516  15.722  0.50 19.69 ? 255 VAL B CG1   1 
ATOM   10714 C  CG2   A VAL B 2 255 ? 10.724  -9.188  12.777  0.50 27.45 ? 255 VAL B CG2   1 
ATOM   10715 C  CG2   B VAL B 2 255 ? 10.907  -8.940  13.331  0.50 24.00 ? 255 VAL B CG2   1 
ATOM   10716 N  N     A ASN B 2 256 ? 14.072  -10.847 15.524  0.50 23.34 ? 256 ASN B N     1 
ATOM   10717 N  N     B ASN B 2 256 ? 14.257  -10.866 15.875  0.50 23.56 ? 256 ASN B N     1 
ATOM   10718 C  CA    A ASN B 2 256 ? 14.781  -11.028 16.784  0.50 26.19 ? 256 ASN B CA    1 
ATOM   10719 C  CA    B ASN B 2 256 ? 14.961  -11.124 17.123  0.50 26.63 ? 256 ASN B CA    1 
ATOM   10720 C  C     A ASN B 2 256 ? 16.237  -11.453 16.613  0.50 24.15 ? 256 ASN B C     1 
ATOM   10721 C  C     B ASN B 2 256 ? 16.477  -11.204 16.967  0.50 23.48 ? 256 ASN B C     1 
ATOM   10722 O  O     A ASN B 2 256 ? 16.955  -11.554 17.612  0.50 25.22 ? 256 ASN B O     1 
ATOM   10723 O  O     B ASN B 2 256 ? 17.201  -10.909 17.925  0.50 21.55 ? 256 ASN B O     1 
ATOM   10724 C  CB    A ASN B 2 256 ? 14.046  -12.052 17.653  0.50 25.72 ? 256 ASN B CB    1 
ATOM   10725 C  CB    B ASN B 2 256 ? 14.452  -12.429 17.733  0.50 23.59 ? 256 ASN B CB    1 
ATOM   10726 C  CG    A ASN B 2 256 ? 12.694  -11.544 18.127  0.50 23.46 ? 256 ASN B CG    1 
ATOM   10727 C  CG    B ASN B 2 256 ? 13.082  -12.279 18.382  0.50 24.78 ? 256 ASN B CG    1 
ATOM   10728 O  OD1   A ASN B 2 256 ? 12.610  -10.788 19.098  0.50 22.58 ? 256 ASN B OD1   1 
ATOM   10729 O  OD1   B ASN B 2 256 ? 12.850  -11.357 19.162  0.50 24.01 ? 256 ASN B OD1   1 
ATOM   10730 N  ND2   A ASN B 2 256 ? 11.634  -11.946 17.440  0.50 24.77 ? 256 ASN B ND2   1 
ATOM   10731 N  ND2   B ASN B 2 256 ? 12.173  -13.190 18.065  0.50 26.64 ? 256 ASN B ND2   1 
ATOM   10732 N  N     A MET B 2 257 ? 16.687  -11.709 15.383  0.50 19.77 ? 257 MET B N     1 
ATOM   10733 N  N     B MET B 2 257 ? 16.977  -11.588 15.789  0.50 20.43 ? 257 MET B N     1 
ATOM   10734 C  CA    A MET B 2 257 ? 18.073  -12.081 15.123  0.50 25.73 ? 257 MET B CA    1 
ATOM   10735 C  CA    B MET B 2 257 ? 18.398  -11.876 15.613  0.50 23.55 ? 257 MET B CA    1 
ATOM   10736 C  C     A MET B 2 257 ? 18.858  -11.025 14.359  0.50 20.03 ? 257 MET B C     1 
ATOM   10737 C  C     B MET B 2 257 ? 19.175  -10.797 14.867  0.50 25.13 ? 257 MET B C     1 
ATOM   10738 O  O     A MET B 2 257 ? 20.087  -11.132 14.283  0.50 26.94 ? 257 MET B O     1 
ATOM   10739 O  O     B MET B 2 257 ? 20.409  -10.775 14.963  0.50 25.72 ? 257 MET B O     1 
ATOM   10740 C  CB    A MET B 2 257 ? 18.142  -13.400 14.337  0.50 20.97 ? 257 MET B CB    1 
ATOM   10741 C  CB    B MET B 2 257 ? 18.581  -13.203 14.868  0.50 22.86 ? 257 MET B CB    1 
ATOM   10742 C  CG    A MET B 2 257 ? 17.760  -14.635 15.134  0.50 29.42 ? 257 MET B CG    1 
ATOM   10743 C  CG    B MET B 2 257 ? 18.201  -14.428 15.676  0.50 27.12 ? 257 MET B CG    1 
ATOM   10744 S  SD    A MET B 2 257 ? 18.969  -15.053 16.400  0.50 26.49 ? 257 MET B SD    1 
ATOM   10745 S  SD    B MET B 2 257 ? 19.319  -14.748 17.048  0.50 25.73 ? 257 MET B SD    1 
ATOM   10746 C  CE    A MET B 2 257 ? 20.451  -15.239 15.404  0.50 28.34 ? 257 MET B CE    1 
ATOM   10747 C  CE    B MET B 2 257 ? 20.850  -15.038 16.163  0.50 27.20 ? 257 MET B CE    1 
ATOM   10748 N  N     A VAL B 2 258 ? 18.198  -10.019 13.800  0.50 23.74 ? 258 VAL B N     1 
ATOM   10749 N  N     B VAL B 2 258 ? 18.504  -9.916  14.132  0.50 22.65 ? 258 VAL B N     1 
ATOM   10750 C  CA    A VAL B 2 258 ? 18.822  -9.054  12.905  0.50 25.90 ? 258 VAL B CA    1 
ATOM   10751 C  CA    B VAL B 2 258 ? 19.183  -8.930  13.292  0.50 25.04 ? 258 VAL B CA    1 
ATOM   10752 C  C     A VAL B 2 258 ? 18.619  -7.656  13.481  0.50 25.02 ? 258 VAL B C     1 
ATOM   10753 C  C     B VAL B 2 258 ? 18.909  -7.520  13.806  0.50 24.73 ? 258 VAL B C     1 
ATOM   10754 O  O     A VAL B 2 258 ? 17.573  -7.036  13.282  0.50 22.49 ? 258 VAL B O     1 
ATOM   10755 O  O     B VAL B 2 258 ? 17.927  -6.890  13.384  0.50 23.42 ? 258 VAL B O     1 
ATOM   10756 C  CB    A VAL B 2 258 ? 18.245  -9.156  11.482  0.50 23.61 ? 258 VAL B CB    1 
ATOM   10757 C  CB    B VAL B 2 258 ? 18.753  -9.069  11.822  0.50 24.20 ? 258 VAL B CB    1 
ATOM   10758 C  CG1   A VAL B 2 258 ? 18.896  -8.128  10.565  0.50 27.56 ? 258 VAL B CG1   1 
ATOM   10759 C  CG1   B VAL B 2 258 ? 19.520  -8.093  10.943  0.50 25.63 ? 258 VAL B CG1   1 
ATOM   10760 C  CG2   A VAL B 2 258 ? 18.434  -10.565 10.937  0.50 22.35 ? 258 VAL B CG2   1 
ATOM   10761 C  CG2   B VAL B 2 258 ? 18.954  -10.500 11.336  0.50 24.11 ? 258 VAL B CG2   1 
ATOM   10762 N  N     A PRO B 2 259 ? 19.617  -7.116  14.197  0.50 23.09 ? 259 PRO B N     1 
ATOM   10763 N  N     B PRO B 2 259 ? 19.741  -6.980  14.705  0.50 24.05 ? 259 PRO B N     1 
ATOM   10764 C  CA    A PRO B 2 259 ? 19.442  -5.801  14.835  0.50 22.87 ? 259 PRO B CA    1 
ATOM   10765 C  CA    B PRO B 2 259 ? 19.504  -5.618  15.206  0.50 22.85 ? 259 PRO B CA    1 
ATOM   10766 C  C     A PRO B 2 259 ? 19.626  -4.643  13.869  0.50 24.72 ? 259 PRO B C     1 
ATOM   10767 C  C     B PRO B 2 259 ? 19.906  -4.520  14.240  0.50 24.77 ? 259 PRO B C     1 
ATOM   10768 O  O     A PRO B 2 259 ? 19.043  -3.569  14.049  0.50 21.02 ? 259 PRO B O     1 
ATOM   10769 O  O     B PRO B 2 259 ? 19.556  -3.355  14.475  0.50 20.27 ? 259 PRO B O     1 
ATOM   10770 C  CB    A PRO B 2 259 ? 20.520  -5.801  15.924  0.50 24.29 ? 259 PRO B CB    1 
ATOM   10771 C  CB    B PRO B 2 259 ? 20.353  -5.564  16.484  0.50 24.61 ? 259 PRO B CB    1 
ATOM   10772 C  CG    A PRO B 2 259 ? 21.602  -6.676  15.364  0.50 26.49 ? 259 PRO B CG    1 
ATOM   10773 C  CG    B PRO B 2 259 ? 21.407  -6.599  16.288  0.50 27.78 ? 259 PRO B CG    1 
ATOM   10774 C  CD    A PRO B 2 259 ? 20.913  -7.734  14.538  0.50 27.18 ? 259 PRO B CD    1 
ATOM   10775 C  CD    B PRO B 2 259 ? 20.785  -7.682  15.471  0.50 25.13 ? 259 PRO B CD    1 
ATOM   10776 N  N     A PHE B 2 260 ? 20.452  -4.846  12.845  0.50 26.28 ? 260 PHE B N     1 
ATOM   10777 N  N     B PHE B 2 260 ? 20.625  -4.844  13.163  0.50 26.42 ? 260 PHE B N     1 
ATOM   10778 C  CA    A PHE B 2 260 ? 20.653  -3.862  11.798  0.50 24.33 ? 260 PHE B CA    1 
ATOM   10779 C  CA    B PHE B 2 260 ? 21.064  -3.850  12.199  0.50 24.29 ? 260 PHE B CA    1 
ATOM   10780 C  C     A PHE B 2 260 ? 20.537  -4.565  10.453  0.50 24.40 ? 260 PHE B C     1 
ATOM   10781 C  C     B PHE B 2 260 ? 20.984  -4.518  10.832  0.50 24.11 ? 260 PHE B C     1 
ATOM   10782 O  O     A PHE B 2 260 ? 20.954  -5.721  10.325  0.50 23.40 ? 260 PHE B O     1 
ATOM   10783 O  O     B PHE B 2 260 ? 21.464  -5.655  10.675  0.50 24.21 ? 260 PHE B O     1 
ATOM   10784 C  CB    A PHE B 2 260 ? 22.017  -3.173  11.943  0.50 27.39 ? 260 PHE B CB    1 
ATOM   10785 C  CB    B PHE B 2 260 ? 22.480  -3.357  12.506  0.50 27.45 ? 260 PHE B CB    1 
ATOM   10786 C  CG    A PHE B 2 260 ? 22.229  -2.542  13.290  0.50 25.89 ? 260 PHE B CG    1 
ATOM   10787 C  CG    B PHE B 2 260 ? 22.653  -2.904  13.929  0.50 23.91 ? 260 PHE B CG    1 
ATOM   10788 C  CD1   A PHE B 2 260 ? 21.667  -1.312  13.591  0.50 25.57 ? 260 PHE B CD1   1 
ATOM   10789 C  CD1   B PHE B 2 260 ? 22.209  -1.654  14.327  0.50 24.96 ? 260 PHE B CD1   1 
ATOM   10790 C  CD2   A PHE B 2 260 ? 22.984  -3.183  14.258  0.50 20.98 ? 260 PHE B CD2   1 
ATOM   10791 C  CD2   B PHE B 2 260 ? 23.222  -3.739  14.874  0.50 23.94 ? 260 PHE B CD2   1 
ATOM   10792 C  CE1   A PHE B 2 260 ? 21.852  -0.733  14.833  0.50 24.73 ? 260 PHE B CE1   1 
ATOM   10793 C  CE1   B PHE B 2 260 ? 22.346  -1.235  15.636  0.50 25.66 ? 260 PHE B CE1   1 
ATOM   10794 C  CE2   A PHE B 2 260 ? 23.171  -2.609  15.501  0.50 27.98 ? 260 PHE B CE2   1 
ATOM   10795 C  CE2   B PHE B 2 260 ? 23.357  -3.325  16.193  0.50 26.96 ? 260 PHE B CE2   1 
ATOM   10796 C  CZ    A PHE B 2 260 ? 22.606  -1.382  15.790  0.50 25.82 ? 260 PHE B CZ    1 
ATOM   10797 C  CZ    B PHE B 2 260 ? 22.919  -2.070  16.569  0.50 21.22 ? 260 PHE B CZ    1 
ATOM   10798 N  N     A PRO B 2 261 ? 19.970  -3.903  9.441   0.50 24.53 ? 261 PRO B N     1 
ATOM   10799 N  N     B PRO B 2 261 ? 20.392  -3.855  9.834   0.50 24.75 ? 261 PRO B N     1 
ATOM   10800 C  CA    A PRO B 2 261 ? 19.521  -4.643  8.247   0.50 25.10 ? 261 PRO B CA    1 
ATOM   10801 C  CA    B PRO B 2 261 ? 19.962  -4.591  8.628   0.50 25.15 ? 261 PRO B CA    1 
ATOM   10802 C  C     A PRO B 2 261 ? 20.619  -5.405  7.525   0.50 21.97 ? 261 PRO B C     1 
ATOM   10803 C  C     B PRO B 2 261 ? 21.082  -5.323  7.906   0.50 25.51 ? 261 PRO B C     1 
ATOM   10804 O  O     A PRO B 2 261 ? 20.342  -6.488  6.998   0.50 20.22 ? 261 PRO B O     1 
ATOM   10805 O  O     B PRO B 2 261 ? 20.922  -6.509  7.593   0.50 20.71 ? 261 PRO B O     1 
ATOM   10806 C  CB    A PRO B 2 261 ? 18.914  -3.546  7.359   0.50 25.62 ? 261 PRO B CB    1 
ATOM   10807 C  CB    B PRO B 2 261 ? 19.324  -3.497  7.758   0.50 25.46 ? 261 PRO B CB    1 
ATOM   10808 C  CG    A PRO B 2 261 ? 19.435  -2.249  7.910   0.50 33.29 ? 261 PRO B CG    1 
ATOM   10809 C  CG    B PRO B 2 261 ? 19.784  -2.192  8.342   0.50 31.76 ? 261 PRO B CG    1 
ATOM   10810 C  CD    A PRO B 2 261 ? 19.647  -2.469  9.367   0.50 24.20 ? 261 PRO B CD    1 
ATOM   10811 C  CD    B PRO B 2 261 ? 20.022  -2.431  9.791   0.50 24.71 ? 261 PRO B CD    1 
ATOM   10812 N  N     A ARG B 2 262 ? 21.855  -4.895  7.497   0.50 26.30 ? 262 ARG B N     1 
ATOM   10813 N  N     B ARG B 2 262 ? 22.217  -4.663  7.643   0.50 23.51 ? 262 ARG B N     1 
ATOM   10814 C  CA    A ARG B 2 262 ? 22.920  -5.562  6.749   0.50 26.09 ? 262 ARG B CA    1 
ATOM   10815 C  CA    B ARG B 2 262 ? 23.303  -5.312  6.906   0.50 27.70 ? 262 ARG B CA    1 
ATOM   10816 C  C     A ARG B 2 262 ? 23.581  -6.697  7.523   0.50 25.85 ? 262 ARG B C     1 
ATOM   10817 C  C     B ARG B 2 262 ? 23.911  -6.486  7.663   0.50 25.54 ? 262 ARG B C     1 
ATOM   10818 O  O     A ARG B 2 262 ? 24.257  -7.533  6.912   0.50 27.84 ? 262 ARG B O     1 
ATOM   10819 O  O     B ARG B 2 262 ? 24.500  -7.374  7.036   0.50 28.01 ? 262 ARG B O     1 
ATOM   10820 C  CB    A ARG B 2 262 ? 23.986  -4.546  6.326   0.50 28.33 ? 262 ARG B CB    1 
ATOM   10821 C  CB    B ARG B 2 262 ? 24.410  -4.306  6.573   0.50 26.28 ? 262 ARG B CB    1 
ATOM   10822 C  CG    A ARG B 2 262 ? 23.493  -3.512  5.328   0.50 26.62 ? 262 ARG B CG    1 
ATOM   10823 C  CG    B ARG B 2 262 ? 24.004  -3.214  5.598   0.50 26.76 ? 262 ARG B CG    1 
ATOM   10824 C  CD    A ARG B 2 262 ? 24.451  -2.332  5.219   0.50 33.25 ? 262 ARG B CD    1 
ATOM   10825 C  CD    B ARG B 2 262 ? 24.968  -2.028  5.647   0.50 31.65 ? 262 ARG B CD    1 
ATOM   10826 N  NE    A ARG B 2 262 ? 25.741  -2.714  4.657   0.50 29.84 ? 262 ARG B NE    1 
ATOM   10827 N  NE    B ARG B 2 262 ? 26.347  -2.398  5.341   0.50 31.50 ? 262 ARG B NE    1 
ATOM   10828 C  CZ    A ARG B 2 262 ? 26.059  -2.611  3.374   0.50 40.45 ? 262 ARG B CZ    1 
ATOM   10829 C  CZ    B ARG B 2 262 ? 26.931  -2.214  4.164   0.50 37.77 ? 262 ARG B CZ    1 
ATOM   10830 N  NH1   A ARG B 2 262 ? 25.201  -2.140  2.484   0.50 40.88 ? 262 ARG B NH1   1 
ATOM   10831 N  NH1   B ARG B 2 262 ? 26.280  -1.674  3.145   0.50 39.07 ? 262 ARG B NH1   1 
ATOM   10832 N  NH2   A ARG B 2 262 ? 27.269  -2.994  2.974   0.50 34.03 ? 262 ARG B NH2   1 
ATOM   10833 N  NH2   B ARG B 2 262 ? 28.202  -2.574  4.005   0.50 31.34 ? 262 ARG B NH2   1 
ATOM   10834 N  N     A LEU B 2 263 ? 23.410  -6.755  8.842   0.50 25.01 ? 263 LEU B N     1 
ATOM   10835 N  N     B LEU B 2 263 ? 23.787  -6.516  8.988   0.50 25.61 ? 263 LEU B N     1 
ATOM   10836 C  CA    A LEU B 2 263 ? 24.061  -7.789  9.651   0.50 22.99 ? 263 LEU B CA    1 
ATOM   10837 C  CA    B LEU B 2 263 ? 24.427  -7.555  9.795   0.50 23.62 ? 263 LEU B CA    1 
ATOM   10838 C  C     A LEU B 2 263 ? 23.099  -8.959  9.857   0.50 24.97 ? 263 LEU B C     1 
ATOM   10839 C  C     B LEU B 2 263 ? 23.462  -8.728  9.972   0.50 24.37 ? 263 LEU B C     1 
ATOM   10840 O  O     A LEU B 2 263 ? 22.525  -9.171  10.930  0.50 25.36 ? 263 LEU B O     1 
ATOM   10841 O  O     B LEU B 2 263 ? 22.977  -9.032  11.065  0.50 28.80 ? 263 LEU B O     1 
ATOM   10842 C  CB    A LEU B 2 263 ? 24.542  -7.206  10.975  0.50 21.18 ? 263 LEU B CB    1 
ATOM   10843 C  CB    B LEU B 2 263 ? 24.882  -6.980  11.130  0.50 22.18 ? 263 LEU B CB    1 
ATOM   10844 C  CG    A LEU B 2 263 ? 25.407  -5.947  10.830  0.50 26.38 ? 263 LEU B CG    1 
ATOM   10845 C  CG    B LEU B 2 263 ? 25.639  -5.651  10.990  0.50 25.47 ? 263 LEU B CG    1 
ATOM   10846 C  CD1   A LEU B 2 263 ? 26.044  -5.537  12.146  0.50 26.07 ? 263 LEU B CD1   1 
ATOM   10847 C  CD1   B LEU B 2 263 ? 26.139  -5.133  12.326  0.50 26.63 ? 263 LEU B CD1   1 
ATOM   10848 C  CD2   A LEU B 2 263 ? 26.471  -6.151  9.772   0.50 29.11 ? 263 LEU B CD2   1 
ATOM   10849 C  CD2   B LEU B 2 263 ? 26.793  -5.782  10.007  0.50 28.82 ? 263 LEU B CD2   1 
ATOM   10850 N  N     A HIS B 2 264 ? 22.928  -9.733  8.784   0.50 25.10 ? 264 HIS B N     1 
ATOM   10851 N  N     B HIS B 2 264 ? 23.185  -9.390  8.853   0.50 24.05 ? 264 HIS B N     1 
ATOM   10852 C  CA    A HIS B 2 264 ? 22.027  -10.879 8.783   0.50 26.33 ? 264 HIS B CA    1 
ATOM   10853 C  CA    B HIS B 2 264 ? 22.243  -10.500 8.798   0.50 26.70 ? 264 HIS B CA    1 
ATOM   10854 C  C     A HIS B 2 264 ? 22.746  -12.158 8.362   0.50 24.34 ? 264 HIS B C     1 
ATOM   10855 C  C     B HIS B 2 264 ? 22.918  -11.769 8.292   0.50 23.39 ? 264 HIS B C     1 
ATOM   10856 O  O     A HIS B 2 264 ? 22.122  -13.098 7.864   0.50 23.57 ? 264 HIS B O     1 
ATOM   10857 O  O     B HIS B 2 264 ? 22.327  -12.561 7.556   0.50 25.82 ? 264 HIS B O     1 
ATOM   10858 C  CB    A HIS B 2 264 ? 20.813  -10.616 7.892   0.50 25.88 ? 264 HIS B CB    1 
ATOM   10859 C  CB    B HIS B 2 264 ? 21.030  -10.145 7.940   0.50 24.58 ? 264 HIS B CB    1 
ATOM   10860 C  CG    A HIS B 2 264 ? 21.157  -10.220 6.488   0.50 26.60 ? 264 HIS B CG    1 
ATOM   10861 C  CG    B HIS B 2 264 ? 21.362  -9.811  6.518   0.50 26.06 ? 264 HIS B CG    1 
ATOM   10862 N  ND1   A HIS B 2 264 ? 20.990  -8.935  6.018   0.50 25.15 ? 264 HIS B ND1   1 
ATOM   10863 N  ND1   B HIS B 2 264 ? 21.395  -8.516  6.048   0.50 25.70 ? 264 HIS B ND1   1 
ATOM   10864 C  CD2   A HIS B 2 264 ? 21.646  -10.940 5.450   0.50 27.02 ? 264 HIS B CD2   1 
ATOM   10865 C  CD2   B HIS B 2 264 ? 21.661  -10.603 5.461   0.50 27.48 ? 264 HIS B CD2   1 
ATOM   10866 C  CE1   A HIS B 2 264 ? 21.369  -8.878  4.753   0.50 27.86 ? 264 HIS B CE1   1 
ATOM   10867 C  CE1   B HIS B 2 264 ? 21.709  -8.524  4.765   0.50 26.68 ? 264 HIS B CE1   1 
ATOM   10868 N  NE2   A HIS B 2 264 ? 21.769  -10.082 4.383   0.50 25.96 ? 264 HIS B NE2   1 
ATOM   10869 N  NE2   B HIS B 2 264 ? 21.875  -9.778  4.384   0.50 26.18 ? 264 HIS B NE2   1 
ATOM   10870 N  N     A PHE B 2 265 ? 24.055  -12.212 8.580   0.50 23.41 ? 265 PHE B N     1 
ATOM   10871 N  N     B PHE B 2 265 ? 24.163  -11.983 8.704   0.50 24.52 ? 265 PHE B N     1 
ATOM   10872 C  CA    A PHE B 2 265 ? 24.873  -13.368 8.233   0.50 22.85 ? 265 PHE B CA    1 
ATOM   10873 C  CA    B PHE B 2 265 ? 24.952  -13.147 8.310   0.50 23.12 ? 265 PHE B CA    1 
ATOM   10874 C  C     A PHE B 2 265 ? 25.122  -14.181 9.496   0.50 24.01 ? 265 PHE B C     1 
ATOM   10875 C  C     B PHE B 2 265 ? 25.233  -13.962 9.560   0.50 23.93 ? 265 PHE B C     1 
ATOM   10876 O  O     A PHE B 2 265 ? 25.855  -13.743 10.388  0.50 27.04 ? 265 PHE B O     1 
ATOM   10877 O  O     B PHE B 2 265 ? 25.964  -13.509 10.448  0.50 26.50 ? 265 PHE B O     1 
ATOM   10878 C  CB    A PHE B 2 265 ? 26.184  -12.923 7.591   0.50 22.94 ? 265 PHE B CB    1 
ATOM   10879 C  CB    B PHE B 2 265 ? 26.245  -12.719 7.621   0.50 22.90 ? 265 PHE B CB    1 
ATOM   10880 C  CG    A PHE B 2 265 ? 26.007  -12.346 6.220   0.50 21.26 ? 265 PHE B CG    1 
ATOM   10881 C  CG    B PHE B 2 265 ? 26.015  -11.908 6.386   0.50 22.09 ? 265 PHE B CG    1 
ATOM   10882 C  CD1   A PHE B 2 265 ? 26.076  -13.157 5.101   0.50 21.53 ? 265 PHE B CD1   1 
ATOM   10883 C  CD1   B PHE B 2 265 ? 25.812  -12.528 5.166   0.50 23.37 ? 265 PHE B CD1   1 
ATOM   10884 C  CD2   A PHE B 2 265 ? 25.727  -10.999 6.053   0.50 27.52 ? 265 PHE B CD2   1 
ATOM   10885 C  CD2   B PHE B 2 265 ? 25.963  -10.525 6.450   0.50 23.88 ? 265 PHE B CD2   1 
ATOM   10886 C  CE1   A PHE B 2 265 ? 25.894  -12.630 3.834   0.50 26.00 ? 265 PHE B CE1   1 
ATOM   10887 C  CE1   B PHE B 2 265 ? 25.573  -11.783 4.028   0.50 26.63 ? 265 PHE B CE1   1 
ATOM   10888 C  CE2   A PHE B 2 265 ? 25.538  -10.466 4.789   0.50 25.98 ? 265 PHE B CE2   1 
ATOM   10889 C  CE2   B PHE B 2 265 ? 25.726  -9.774  5.314   0.50 27.23 ? 265 PHE B CE2   1 
ATOM   10890 C  CZ    A PHE B 2 265 ? 25.622  -11.282 3.680   0.50 28.16 ? 265 PHE B CZ    1 
ATOM   10891 C  CZ    B PHE B 2 265 ? 25.533  -10.404 4.101   0.50 24.20 ? 265 PHE B CZ    1 
ATOM   10892 N  N     A PHE B 2 266 ? 24.520  -15.364 9.564   0.50 22.89 ? 266 PHE B N     1 
ATOM   10893 N  N     B PHE B 2 266 ? 24.661  -15.160 9.626   0.50 23.05 ? 266 PHE B N     1 
ATOM   10894 C  CA    A PHE B 2 266 ? 24.569  -16.194 10.757  0.50 23.75 ? 266 PHE B CA    1 
ATOM   10895 C  CA    B PHE B 2 266 ? 24.652  -15.956 10.845  0.50 23.28 ? 266 PHE B CA    1 
ATOM   10896 C  C     A PHE B 2 266 ? 25.708  -17.202 10.672  0.50 26.95 ? 266 PHE B C     1 
ATOM   10897 C  C     B PHE B 2 266 ? 25.779  -16.976 10.831  0.50 26.55 ? 266 PHE B C     1 
ATOM   10898 O  O     A PHE B 2 266 ? 26.150  -17.593 9.589   0.50 24.98 ? 266 PHE B O     1 
ATOM   10899 O  O     B PHE B 2 266 ? 25.979  -17.682 9.836   0.50 25.80 ? 266 PHE B O     1 
ATOM   10900 C  CB    A PHE B 2 266 ? 23.248  -16.937 10.961  0.50 21.12 ? 266 PHE B CB    1 
ATOM   10901 C  CB    B PHE B 2 266 ? 23.312  -16.673 11.017  0.50 21.41 ? 266 PHE B CB    1 
ATOM   10902 C  CG    A PHE B 2 266 ? 22.045  -16.039 11.050  0.50 24.59 ? 266 PHE B CG    1 
ATOM   10903 C  CG    B PHE B 2 266 ? 22.142  -15.745 11.157  0.50 24.48 ? 266 PHE B CG    1 
ATOM   10904 C  CD1   A PHE B 2 266 ? 22.140  -14.772 11.605  0.50 25.64 ? 266 PHE B CD1   1 
ATOM   10905 C  CD1   B PHE B 2 266 ? 22.304  -14.472 11.684  0.50 25.46 ? 266 PHE B CD1   1 
ATOM   10906 C  CD2   A PHE B 2 266 ? 20.814  -16.470 10.581  0.50 25.22 ? 266 PHE B CD2   1 
ATOM   10907 C  CD2   B PHE B 2 266 ? 20.878  -16.143 10.758  0.50 25.97 ? 266 PHE B CD2   1 
ATOM   10908 C  CE1   A PHE B 2 266 ? 21.025  -13.945 11.686  0.50 25.48 ? 266 PHE B CE1   1 
ATOM   10909 C  CE1   B PHE B 2 266 ? 21.221  -13.612 11.810  0.50 24.97 ? 266 PHE B CE1   1 
ATOM   10910 C  CE2   A PHE B 2 266 ? 19.698  -15.655 10.662  0.50 27.25 ? 266 PHE B CE2   1 
ATOM   10911 C  CE2   B PHE B 2 266 ? 19.794  -15.293 10.884  0.50 28.58 ? 266 PHE B CE2   1 
ATOM   10912 C  CZ    A PHE B 2 266 ? 19.804  -14.389 11.214  0.50 24.89 ? 266 PHE B CZ    1 
ATOM   10913 C  CZ    B PHE B 2 266 ? 19.967  -14.026 11.411  0.50 24.35 ? 266 PHE B CZ    1 
ATOM   10914 N  N     A MET B 2 267 ? 26.167  -17.635 11.844  0.50 24.62 ? 267 MET B N     1 
ATOM   10915 N  N     B MET B 2 267 ? 26.510  -17.036 11.931  0.50 25.15 ? 267 MET B N     1 
ATOM   10916 C  CA    A MET B 2 267 ? 27.201  -18.654 11.978  0.50 22.20 ? 267 MET B CA    1 
ATOM   10917 C  CA    B MET B 2 267 ? 27.419  -18.140 12.191  0.50 24.10 ? 267 MET B CA    1 
ATOM   10918 C  C     A MET B 2 267 ? 26.577  -19.896 12.599  0.50 22.74 ? 267 MET B C     1 
ATOM   10919 C  C     B MET B 2 267 ? 26.627  -19.323 12.735  0.50 24.66 ? 267 MET B C     1 
ATOM   10920 O  O     A MET B 2 267 ? 26.424  -19.963 13.827  0.50 31.16 ? 267 MET B O     1 
ATOM   10921 O  O     B MET B 2 267 ? 25.986  -19.193 13.785  0.50 24.65 ? 267 MET B O     1 
ATOM   10922 C  CB    A MET B 2 267 ? 28.350  -18.136 12.847  0.50 28.12 ? 267 MET B CB    1 
ATOM   10923 C  CB    B MET B 2 267 ? 28.479  -17.714 13.196  0.50 28.91 ? 267 MET B CB    1 
ATOM   10924 C  CG    A MET B 2 267 ? 29.604  -18.991 12.840  0.50 30.97 ? 267 MET B CG    1 
ATOM   10925 C  CG    B MET B 2 267 ? 29.263  -18.851 13.822  0.50 31.78 ? 267 MET B CG    1 
ATOM   10926 S  SD    A MET B 2 267 ? 30.890  -18.305 13.911  0.50 34.45 ? 267 MET B SD    1 
ATOM   10927 S  SD    B MET B 2 267 ? 30.414  -18.249 15.077  0.50 45.30 ? 267 MET B SD    1 
ATOM   10928 C  CE    A MET B 2 267 ? 30.731  -16.559 13.559  0.50 25.44 ? 267 MET B CE    1 
ATOM   10929 C  CE    B MET B 2 267 ? 30.637  -16.556 14.550  0.50 30.03 ? 267 MET B CE    1 
ATOM   10930 N  N     A PRO B 2 268 ? 26.183  -20.888 11.811  0.50 26.09 ? 268 PRO B N     1 
ATOM   10931 N  N     B PRO B 2 268 ? 26.622  -20.467 12.062  0.50 25.96 ? 268 PRO B N     1 
ATOM   10932 C  CA    A PRO B 2 268 ? 25.568  -22.086 12.385  0.50 24.23 ? 268 PRO B CA    1 
ATOM   10933 C  CA    B PRO B 2 268 ? 25.945  -21.641 12.620  0.50 24.46 ? 268 PRO B CA    1 
ATOM   10934 C  C     A PRO B 2 268 ? 26.603  -23.060 12.931  0.50 28.99 ? 268 PRO B C     1 
ATOM   10935 C  C     B PRO B 2 268 ? 26.907  -22.604 13.301  0.50 25.67 ? 268 PRO B C     1 
ATOM   10936 O  O     A PRO B 2 268 ? 27.759  -23.104 12.500  0.50 27.55 ? 268 PRO B O     1 
ATOM   10937 O  O     B PRO B 2 268 ? 28.083  -22.692 12.929  0.50 28.21 ? 268 PRO B O     1 
ATOM   10938 C  CB    A PRO B 2 268 ? 24.815  -22.691 11.197  0.50 29.54 ? 268 PRO B CB    1 
ATOM   10939 C  CB    B PRO B 2 268 ? 25.287  -22.282 11.389  0.50 25.52 ? 268 PRO B CB    1 
ATOM   10940 C  CG    A PRO B 2 268 ? 25.618  -22.289 10.023  0.50 26.11 ? 268 PRO B CG    1 
ATOM   10941 C  CG    B PRO B 2 268 ? 25.866  -21.553 10.171  0.50 28.18 ? 268 PRO B CG    1 
ATOM   10942 C  CD    A PRO B 2 268 ? 26.177  -20.920 10.339  0.50 26.75 ? 268 PRO B CD    1 
ATOM   10943 C  CD    B PRO B 2 268 ? 26.993  -20.690 10.657  0.50 22.43 ? 268 PRO B CD    1 
ATOM   10944 N  N     A GLY B 2 269 ? 26.150  -23.860 13.895  0.50 26.61 ? 269 GLY B N     1 
ATOM   10945 N  N     B GLY B 2 269 ? 26.410  -23.337 14.295  0.50 28.47 ? 269 GLY B N     1 
ATOM   10946 C  CA    A GLY B 2 269 ? 26.989  -24.873 14.509  0.50 23.48 ? 269 GLY B CA    1 
ATOM   10947 C  CA    B GLY B 2 269 ? 27.199  -24.351 14.970  0.50 24.49 ? 269 GLY B CA    1 
ATOM   10948 C  C     A GLY B 2 269 ? 26.150  -26.067 14.907  0.50 27.71 ? 269 GLY B C     1 
ATOM   10949 C  C     B GLY B 2 269 ? 26.320  -25.520 15.361  0.50 30.34 ? 269 GLY B C     1 
ATOM   10950 O  O     A GLY B 2 269 ? 24.919  -25.990 14.981  0.50 30.95 ? 269 GLY B O     1 
ATOM   10951 O  O     B GLY B 2 269 ? 25.098  -25.391 15.490  0.50 29.15 ? 269 GLY B O     1 
ATOM   10952 N  N     A PHE B 2 270 ? 26.832  -27.177 15.173  0.50 28.98 ? 270 PHE B N     1 
ATOM   10953 N  N     B PHE B 2 270 ? 26.962  -26.668 15.564  0.50 26.82 ? 270 PHE B N     1 
ATOM   10954 C  CA    A PHE B 2 270 ? 26.152  -28.439 15.416  0.50 33.55 ? 270 PHE B CA    1 
ATOM   10955 C  CA    B PHE B 2 270 ? 26.255  -27.919 15.793  0.50 32.47 ? 270 PHE B CA    1 
ATOM   10956 C  C     A PHE B 2 270 ? 26.966  -29.280 16.385  0.50 36.76 ? 270 PHE B C     1 
ATOM   10957 C  C     B PHE B 2 270 ? 27.034  -28.768 16.787  0.50 36.81 ? 270 PHE B C     1 
ATOM   10958 O  O     A PHE B 2 270 ? 28.195  -29.335 16.292  0.50 35.88 ? 270 PHE B O     1 
ATOM   10959 O  O     B PHE B 2 270 ? 28.237  -28.582 16.986  0.50 34.05 ? 270 PHE B O     1 
ATOM   10960 C  CB    A PHE B 2 270 ? 25.933  -29.208 14.107  0.50 32.74 ? 270 PHE B CB    1 
ATOM   10961 C  CB    B PHE B 2 270 ? 26.050  -28.689 14.478  0.50 31.18 ? 270 PHE B CB    1 
ATOM   10962 C  CG    A PHE B 2 270 ? 24.936  -30.326 14.216  0.50 30.96 ? 270 PHE B CG    1 
ATOM   10963 C  CG    B PHE B 2 270 ? 25.032  -29.793 14.567  0.50 32.00 ? 270 PHE B CG    1 
ATOM   10964 C  CD1   A PHE B 2 270 ? 25.313  -31.567 14.703  0.50 35.59 ? 270 PHE B CD1   1 
ATOM   10965 C  CD1   B PHE B 2 270 ? 23.676  -29.507 14.527  0.50 34.54 ? 270 PHE B CD1   1 
ATOM   10966 C  CD2   A PHE B 2 270 ? 23.620  -30.136 13.826  0.50 36.88 ? 270 PHE B CD2   1 
ATOM   10967 C  CD2   B PHE B 2 270 ? 25.430  -31.115 14.678  0.50 34.20 ? 270 PHE B CD2   1 
ATOM   10968 C  CE1   A PHE B 2 270 ? 24.394  -32.596 14.806  0.50 41.75 ? 270 PHE B CE1   1 
ATOM   10969 C  CE1   B PHE B 2 270 ? 22.736  -30.521 14.606  0.50 35.51 ? 270 PHE B CE1   1 
ATOM   10970 C  CE2   A PHE B 2 270 ? 22.698  -31.162 13.922  0.50 33.13 ? 270 PHE B CE2   1 
ATOM   10971 C  CE2   B PHE B 2 270 ? 24.496  -32.133 14.758  0.50 41.72 ? 270 PHE B CE2   1 
ATOM   10972 C  CZ    A PHE B 2 270 ? 23.086  -32.393 14.412  0.50 34.35 ? 270 PHE B CZ    1 
ATOM   10973 C  CZ    B PHE B 2 270 ? 23.147  -31.836 14.720  0.50 35.61 ? 270 PHE B CZ    1 
ATOM   10974 N  N     A ALA B 2 271 ? 26.269  -29.942 17.310  0.50 40.17 ? 271 ALA B N     1 
ATOM   10975 N  N     B ALA B 2 271 ? 26.324  -29.710 17.417  0.50 40.51 ? 271 ALA B N     1 
ATOM   10976 C  CA    A ALA B 2 271 ? 26.887  -30.850 18.258  0.50 41.42 ? 271 ALA B CA    1 
ATOM   10977 C  CA    B ALA B 2 271 ? 26.934  -30.654 18.341  0.50 41.20 ? 271 ALA B CA    1 
ATOM   10978 C  C     A ALA B 2 271 ? 25.988  -32.067 18.432  0.50 45.01 ? 271 ALA B C     1 
ATOM   10979 C  C     B ALA B 2 271 ? 25.993  -31.830 18.526  0.50 45.07 ? 271 ALA B C     1 
ATOM   10980 O  O     A ALA B 2 271 ? 24.757  -31.927 18.489  0.50 41.95 ? 271 ALA B O     1 
ATOM   10981 O  O     B ALA B 2 271 ? 24.774  -31.623 18.597  0.50 42.19 ? 271 ALA B O     1 
ATOM   10982 C  CB    A ALA B 2 271 ? 27.131  -30.182 19.618  0.50 40.88 ? 271 ALA B CB    1 
ATOM   10983 C  CB    B ALA B 2 271 ? 27.239  -30.003 19.695  0.50 40.91 ? 271 ALA B CB    1 
ATOM   10984 N  N     A PRO B 2 272 ? 26.568  -33.269 18.505  0.50 45.67 ? 272 PRO B N     1 
ATOM   10985 N  N     B PRO B 2 272 ? 26.504  -33.065 18.595  0.50 45.65 ? 272 PRO B N     1 
ATOM   10986 C  CA    A PRO B 2 272 ? 28.000  -33.574 18.399  0.50 46.28 ? 272 PRO B CA    1 
ATOM   10987 C  CA    B PRO B 2 272 ? 27.913  -33.457 18.462  0.50 46.14 ? 272 PRO B CA    1 
ATOM   10988 C  C     A PRO B 2 272 ? 28.469  -33.670 16.950  0.50 47.69 ? 272 PRO B C     1 
ATOM   10989 C  C     B PRO B 2 272 ? 28.344  -33.601 17.006  0.50 47.76 ? 272 PRO B C     1 
ATOM   10990 O  O     A PRO B 2 272 ? 27.690  -34.004 16.061  0.50 46.97 ? 272 PRO B O     1 
ATOM   10991 O  O     B PRO B 2 272 ? 27.520  -33.847 16.128  0.50 46.50 ? 272 PRO B O     1 
ATOM   10992 C  CB    A PRO B 2 272 ? 28.109  -34.920 19.122  0.50 47.32 ? 272 PRO B CB    1 
ATOM   10993 C  CB    B PRO B 2 272 ? 27.960  -34.795 19.206  0.50 47.34 ? 272 PRO B CB    1 
ATOM   10994 C  CG    A PRO B 2 272 ? 26.802  -35.589 18.815  0.50 52.20 ? 272 PRO B CG    1 
ATOM   10995 C  CG    B PRO B 2 272 ? 26.606  -35.388 18.950  0.50 52.64 ? 272 PRO B CG    1 
ATOM   10996 C  CD    A PRO B 2 272 ? 25.778  -34.474 18.819  0.50 50.83 ? 272 PRO B CD    1 
ATOM   10997 C  CD    B PRO B 2 272 ? 25.653  -34.213 18.962  0.50 50.04 ? 272 PRO B CD    1 
ATOM   10998 N  N     A LEU B 2 273 ? 29.738  -33.369 16.685  0.50 42.74 ? 273 LEU B N     1 
ATOM   10999 N  N     B LEU B 2 273 ? 29.635  -33.444 16.725  0.50 42.71 ? 273 LEU B N     1 
ATOM   11000 C  CA    A LEU B 2 273 ? 30.302  -33.605 15.362  0.50 47.39 ? 273 LEU B CA    1 
ATOM   11001 C  CA    B LEU B 2 273 ? 30.156  -33.648 15.382  0.50 47.36 ? 273 LEU B CA    1 
ATOM   11002 C  C     A LEU B 2 273 ? 30.542  -35.095 15.173  0.50 45.53 ? 273 LEU B C     1 
ATOM   11003 C  C     B LEU B 2 273 ? 30.288  -35.138 15.092  0.50 45.51 ? 273 LEU B C     1 
ATOM   11004 O  O     A LEU B 2 273 ? 31.076  -35.764 16.064  0.50 47.52 ? 273 LEU B O     1 
ATOM   11005 O  O     B LEU B 2 273 ? 30.540  -35.946 15.992  0.50 48.45 ? 273 LEU B O     1 
ATOM   11006 C  CB    A LEU B 2 273 ? 31.609  -32.834 15.190  0.50 45.40 ? 273 LEU B CB    1 
ATOM   11007 C  CB    B LEU B 2 273 ? 31.518  -32.970 15.225  0.50 45.36 ? 273 LEU B CB    1 
ATOM   11008 C  CG    A LEU B 2 273 ? 31.533  -31.308 15.170  0.50 44.13 ? 273 LEU B CG    1 
ATOM   11009 C  CG    B LEU B 2 273 ? 31.620  -31.491 15.602  0.50 43.89 ? 273 LEU B CG    1 
ATOM   11010 C  CD1   A LEU B 2 273 ? 32.921  -30.713 15.015  0.50 43.86 ? 273 LEU B CD1   1 
ATOM   11011 C  CD1   B LEU B 2 273 ? 33.073  -31.095 15.788  0.50 44.14 ? 273 LEU B CD1   1 
ATOM   11012 C  CD2   A LEU B 2 273 ? 30.614  -30.831 14.058  0.50 41.12 ? 273 LEU B CD2   1 
ATOM   11013 C  CD2   B LEU B 2 273 ? 30.958  -30.618 14.547  0.50 39.52 ? 273 LEU B CD2   1 
ATOM   11014 N  N     A THR B 2 274 ? 30.141  -35.620 14.016  0.50 49.74 ? 274 THR B N     1 
ATOM   11015 N  N     B THR B 2 274 ? 30.121  -35.498 13.821  0.50 49.51 ? 274 THR B N     1 
ATOM   11016 C  CA    A THR B 2 274 ? 30.261  -37.046 13.749  0.50 50.83 ? 274 THR B CA    1 
ATOM   11017 C  CA    B THR B 2 274 ? 30.216  -36.894 13.413  0.50 49.84 ? 274 THR B CA    1 
ATOM   11018 C  C     A THR B 2 274 ? 30.392  -37.268 12.250  0.50 51.45 ? 274 THR B C     1 
ATOM   11019 C  C     B THR B 2 274 ? 30.406  -36.968 11.906  0.50 52.35 ? 274 THR B C     1 
ATOM   11020 O  O     A THR B 2 274 ? 29.896  -36.477 11.443  0.50 51.76 ? 274 THR B O     1 
ATOM   11021 O  O     B THR B 2 274 ? 30.181  -35.994 11.182  0.50 49.44 ? 274 THR B O     1 
ATOM   11022 C  CB    A THR B 2 274 ? 29.057  -37.829 14.292  0.50 50.78 ? 274 THR B CB    1 
ATOM   11023 C  CB    B THR B 2 274 ? 28.975  -37.691 13.829  0.50 52.46 ? 274 THR B CB    1 
ATOM   11024 O  OG1   A THR B 2 274 ? 28.681  -37.310 15.572  0.50 45.67 ? 274 THR B OG1   1 
ATOM   11025 O  OG1   B THR B 2 274 ? 29.172  -39.078 13.523  0.50 54.93 ? 274 THR B OG1   1 
ATOM   11026 C  CG2   A THR B 2 274 ? 29.398  -39.305 14.443  0.50 53.21 ? 274 THR B CG2   1 
ATOM   11027 C  CG2   B THR B 2 274 ? 27.745  -37.183 13.089  0.50 49.57 ? 274 THR B CG2   1 
ATOM   11028 N  N     A SER B 2 275 ? 31.069  -38.354 11.888  0.50 51.20 ? 275 SER B N     1 
ATOM   11029 N  N     B SER B 2 275 ? 30.821  -38.148 11.443  0.50 51.48 ? 275 SER B N     1 
ATOM   11030 C  CA    A SER B 2 275 ? 31.236  -38.745 10.497  0.50 52.52 ? 275 SER B CA    1 
ATOM   11031 C  CA    B SER B 2 275 ? 31.024  -38.388 10.020  0.50 51.63 ? 275 SER B CA    1 
ATOM   11032 C  C     A SER B 2 275 ? 30.132  -39.710 10.082  0.50 53.37 ? 275 SER B C     1 
ATOM   11033 C  C     B SER B 2 275 ? 29.876  -39.203 9.439   0.50 52.83 ? 275 SER B C     1 
ATOM   11034 O  O     A SER B 2 275 ? 29.591  -40.456 10.902  0.50 55.83 ? 275 SER B O     1 
ATOM   11035 O  O     B SER B 2 275 ? 28.740  -39.112 9.914   0.50 53.83 ? 275 SER B O     1 
ATOM   11036 C  CB    A SER B 2 275 ? 32.602  -39.396 10.281  0.50 52.01 ? 275 SER B CB    1 
ATOM   11037 C  CB    B SER B 2 275 ? 32.355  -39.102 9.779   0.50 53.19 ? 275 SER B CB    1 
ATOM   11038 O  OG    A SER B 2 275 ? 33.649  -38.538 10.698  0.50 48.80 ? 275 SER B OG    1 
ATOM   11039 O  OG    B SER B 2 275 ? 32.524  -39.410 8.405   0.50 51.62 ? 275 SER B OG    1 
ATOM   11040 N  N     A ARG B 2 276 ? 29.804  -39.692 8.793   0.50 53.89 ? 276 ARG B N     1 
ATOM   11041 N  N     B ARG B 2 276 ? 30.165  -40.006 8.416   0.50 53.97 ? 276 ARG B N     1 
ATOM   11042 C  CA    A ARG B 2 276 ? 28.761  -40.570 8.286   0.50 54.84 ? 276 ARG B CA    1 
ATOM   11043 C  CA    B ARG B 2 276 ? 29.132  -40.791 7.750   0.50 55.45 ? 276 ARG B CA    1 
ATOM   11044 C  C     A ARG B 2 276 ? 29.241  -42.018 8.263   0.50 60.06 ? 276 ARG B C     1 
ATOM   11045 C  C     B ARG B 2 276 ? 29.218  -42.268 8.117   0.50 60.00 ? 276 ARG B C     1 
ATOM   11046 O  O     A ARG B 2 276 ? 30.436  -42.302 8.143   0.50 57.79 ? 276 ARG B O     1 
ATOM   11047 O  O     B ARG B 2 276 ? 29.320  -43.127 7.235   0.50 63.73 ? 276 ARG B O     1 
ATOM   11048 C  CB    A ARG B 2 276 ? 28.319  -40.135 6.887   0.50 55.13 ? 276 ARG B CB    1 
ATOM   11049 C  CB    B ARG B 2 276 ? 29.222  -40.613 6.230   0.50 55.41 ? 276 ARG B CB    1 
ATOM   11050 C  CG    A ARG B 2 276 ? 29.387  -40.244 5.804   0.50 54.13 ? 276 ARG B CG    1 
ATOM   11051 C  CG    B ARG B 2 276 ? 30.609  -40.261 5.700   0.50 49.39 ? 276 ARG B CG    1 
ATOM   11052 C  CD    A ARG B 2 276 ? 28.808  -39.875 4.445   0.50 49.60 ? 276 ARG B CD    1 
ATOM   11053 C  CD    B ARG B 2 276 ? 31.596  -41.415 5.830   0.50 53.71 ? 276 ARG B CD    1 
ATOM   11054 N  NE    A ARG B 2 276 ? 29.773  -40.025 3.363   0.50 46.36 ? 276 ARG B NE    1 
ATOM   11055 N  NE    B ARG B 2 276 ? 32.858  -41.144 5.150   0.50 48.09 ? 276 ARG B NE    1 
ATOM   11056 C  CZ    A ARG B 2 276 ? 29.505  -39.796 2.084   0.50 42.87 ? 276 ARG B CZ    1 
ATOM   11057 C  CZ    B ARG B 2 276 ? 33.155  -41.562 3.927   0.50 57.43 ? 276 ARG B CZ    1 
ATOM   11058 N  NH1   A ARG B 2 276 ? 28.308  -39.393 1.689   0.50 38.78 ? 276 ARG B NH1   1 
ATOM   11059 N  NH1   B ARG B 2 276 ? 32.299  -42.277 3.214   0.50 57.31 ? 276 ARG B NH1   1 
ATOM   11060 N  NH2   A ARG B 2 276 ? 30.462  -39.977 1.178   0.50 54.41 ? 276 ARG B NH2   1 
ATOM   11061 N  NH2   B ARG B 2 276 ? 34.341  -41.260 3.406   0.50 50.80 ? 276 ARG B NH2   1 
ATOM   11062 N  N     A GLY B 2 277 ? 28.295  -42.933 8.390   0.50 56.34 ? 277 GLY B N     1 
ATOM   11063 N  N     B GLY B 2 277 ? 29.169  -42.576 9.411   0.50 58.39 ? 277 GLY B N     1 
ATOM   11064 C  CA    A GLY B 2 277 ? 28.593  -44.361 8.419   0.50 52.73 ? 277 GLY B CA    1 
ATOM   11065 C  CA    B GLY B 2 277 ? 29.210  -43.957 9.847   0.50 59.83 ? 277 GLY B CA    1 
ATOM   11066 C  C     A GLY B 2 277 ? 28.899  -44.931 9.788   0.50 59.46 ? 277 GLY B C     1 
ATOM   11067 C  C     B GLY B 2 277 ? 29.381  -44.123 11.343  0.50 62.30 ? 277 GLY B C     1 
ATOM   11068 O  O     A GLY B 2 277 ? 28.354  -45.968 10.167  0.50 54.83 ? 277 GLY B O     1 
ATOM   11069 O  O     B GLY B 2 277 ? 28.715  -44.961 11.960  0.50 65.17 ? 277 GLY B O     1 
ATOM   11070 N  N     A SER B 2 278 ? 29.766  -44.261 10.541  0.50 61.60 ? 278 SER B N     1 
ATOM   11071 N  N     B SER B 2 278 ? 30.270  -43.330 11.936  0.50 58.79 ? 278 SER B N     1 
ATOM   11072 C  CA    A SER B 2 278 ? 30.171  -44.728 11.862  0.50 61.80 ? 278 SER B CA    1 
ATOM   11073 C  CA    B SER B 2 278 ? 30.552  -43.414 13.366  0.50 60.55 ? 278 SER B CA    1 
ATOM   11074 C  C     A SER B 2 278 ? 29.023  -44.641 12.864  0.50 62.19 ? 278 SER B C     1 
ATOM   11075 C  C     B SER B 2 278 ? 29.321  -43.089 14.208  0.50 58.20 ? 278 SER B C     1 
ATOM   11076 O  O     A SER B 2 278 ? 29.228  -44.296 14.028  0.50 58.68 ? 278 SER B O     1 
ATOM   11077 O  O     B SER B 2 278 ? 28.338  -42.543 13.707  0.50 55.63 ? 278 SER B O     1 
ATOM   11078 C  CB    A SER B 2 278 ? 31.367  -43.920 12.367  0.50 61.44 ? 278 SER B CB    1 
ATOM   11079 C  CB    B SER B 2 278 ? 31.700  -42.472 13.738  0.50 58.55 ? 278 SER B CB    1 
ATOM   11080 O  OG    A SER B 2 278 ? 32.405  -43.894 11.401  0.50 58.85 ? 278 SER B OG    1 
ATOM   11081 O  OG    B SER B 2 278 ? 32.905  -42.854 13.097  0.50 55.94 ? 278 SER B OG    1 
ATOM   11082 N  N     A LEU B 2 284 ? 25.908  -38.221 25.459  0.50 65.72 ? 284 LEU B N     1 
ATOM   11083 N  N     B LEU B 2 284 ? 25.661  -38.014 24.959  0.50 64.94 ? 284 LEU B N     1 
ATOM   11084 C  CA    A LEU B 2 284 ? 26.113  -36.779 25.539  0.50 63.85 ? 284 LEU B CA    1 
ATOM   11085 C  CA    B LEU B 2 284 ? 26.117  -36.763 25.556  0.50 63.84 ? 284 LEU B CA    1 
ATOM   11086 C  C     A LEU B 2 284 ? 25.178  -36.136 26.559  0.50 63.21 ? 284 LEU B C     1 
ATOM   11087 C  C     B LEU B 2 284 ? 25.085  -36.217 26.538  0.50 63.26 ? 284 LEU B C     1 
ATOM   11088 O  O     A LEU B 2 284 ? 23.958  -36.143 26.389  0.50 64.24 ? 284 LEU B O     1 
ATOM   11089 O  O     B LEU B 2 284 ? 23.915  -36.601 26.501  0.50 64.67 ? 284 LEU B O     1 
ATOM   11090 C  CB    A LEU B 2 284 ? 25.915  -36.131 24.166  0.50 62.57 ? 284 LEU B CB    1 
ATOM   11091 C  CB    B LEU B 2 284 ? 26.408  -35.715 24.478  0.50 62.37 ? 284 LEU B CB    1 
ATOM   11092 C  CG    A LEU B 2 284 ? 27.153  -36.000 23.276  0.50 57.94 ? 284 LEU B CG    1 
ATOM   11093 C  CG    B LEU B 2 284 ? 27.558  -35.958 23.497  0.50 58.12 ? 284 LEU B CG    1 
ATOM   11094 C  CD1   A LEU B 2 284 ? 28.241  -35.216 23.996  0.50 58.54 ? 284 LEU B CD1   1 
ATOM   11095 C  CD1   B LEU B 2 284 ? 27.137  -36.879 22.361  0.50 61.19 ? 284 LEU B CD1   1 
ATOM   11096 C  CD2   A LEU B 2 284 ? 27.667  -37.362 22.837  0.50 60.88 ? 284 LEU B CD2   1 
ATOM   11097 C  CD2   B LEU B 2 284 ? 28.077  -34.634 22.955  0.50 57.94 ? 284 LEU B CD2   1 
ATOM   11098 N  N     A THR B 2 285 ? 25.759  -35.582 27.617  0.50 61.18 ? 285 THR B N     1 
ATOM   11099 N  N     B THR B 2 285 ? 25.524  -35.318 27.410  0.50 60.54 ? 285 THR B N     1 
ATOM   11100 C  CA    A THR B 2 285 ? 24.998  -34.905 28.654  0.50 61.35 ? 285 THR B CA    1 
ATOM   11101 C  CA    B THR B 2 285 ? 24.657  -34.663 28.376  0.50 61.40 ? 285 THR B CA    1 
ATOM   11102 C  C     A THR B 2 285 ? 24.755  -33.447 28.272  0.50 62.08 ? 285 THR B C     1 
ATOM   11103 C  C     B THR B 2 285 ? 24.527  -33.184 28.039  0.50 61.67 ? 285 THR B C     1 
ATOM   11104 O  O     A THR B 2 285 ? 25.341  -32.914 27.326  0.50 58.52 ? 285 THR B O     1 
ATOM   11105 O  O     B THR B 2 285 ? 25.226  -32.651 27.173  0.50 58.30 ? 285 THR B O     1 
ATOM   11106 C  CB    A THR B 2 285 ? 25.724  -34.992 29.997  0.50 60.24 ? 285 THR B CB    1 
ATOM   11107 C  CB    B THR B 2 285 ? 25.191  -34.836 29.803  0.50 57.58 ? 285 THR B CB    1 
ATOM   11108 O  OG1   A THR B 2 285 ? 27.082  -34.563 29.836  0.50 61.31 ? 285 THR B OG1   1 
ATOM   11109 O  OG1   B THR B 2 285 ? 26.433  -34.135 29.939  0.50 61.90 ? 285 THR B OG1   1 
ATOM   11110 C  CG2   A THR B 2 285 ? 25.709  -36.422 30.520  0.50 62.50 ? 285 THR B CG2   1 
ATOM   11111 C  CG2   B THR B 2 285 ? 25.410  -36.309 30.116  0.50 62.43 ? 285 THR B CG2   1 
ATOM   11112 N  N     A VAL B 2 286 ? 23.870  -32.799 29.033  0.50 59.50 ? 286 VAL B N     1 
ATOM   11113 N  N     B VAL B 2 286 ? 23.611  -32.521 28.746  0.50 60.67 ? 286 VAL B N     1 
ATOM   11114 C  CA    A VAL B 2 286 ? 23.503  -31.414 28.732  0.50 62.01 ? 286 VAL B CA    1 
ATOM   11115 C  CA    B VAL B 2 286 ? 23.396  -31.089 28.528  0.50 61.58 ? 286 VAL B CA    1 
ATOM   11116 C  C     A VAL B 2 286 ? 24.680  -30.456 28.894  0.50 58.64 ? 286 VAL B C     1 
ATOM   11117 C  C     B VAL B 2 286 ? 24.661  -30.272 28.782  0.50 58.62 ? 286 VAL B C     1 
ATOM   11118 O  O     A VAL B 2 286 ? 24.900  -29.630 27.993  0.50 56.47 ? 286 VAL B O     1 
ATOM   11119 O  O     B VAL B 2 286 ? 24.972  -29.391 27.965  0.50 55.90 ? 286 VAL B O     1 
ATOM   11120 C  CB    A VAL B 2 286 ? 22.281  -30.996 29.567  0.50 58.35 ? 286 VAL B CB    1 
ATOM   11121 C  CB    B VAL B 2 286 ? 22.195  -30.602 29.354  0.50 58.77 ? 286 VAL B CB    1 
ATOM   11122 C  CG1   A VAL B 2 286 ? 21.823  -29.594 29.178  0.50 54.42 ? 286 VAL B CG1   1 
ATOM   11123 C  CG1   B VAL B 2 286 ? 21.890  -29.144 29.043  0.50 52.66 ? 286 VAL B CG1   1 
ATOM   11124 C  CG2   A VAL B 2 286 ? 21.154  -32.002 29.395  0.50 57.71 ? 286 VAL B CG2   1 
ATOM   11125 C  CG2   B VAL B 2 286 ? 20.977  -31.475 29.079  0.50 59.46 ? 286 VAL B CG2   1 
ATOM   11126 N  N     A PRO B 2 287 ? 25.458  -30.493 29.986  0.50 56.90 ? 287 PRO B N     1 
ATOM   11127 N  N     B PRO B 2 287 ? 25.424  -30.494 29.863  0.50 56.88 ? 287 PRO B N     1 
ATOM   11128 C  CA    A PRO B 2 287 ? 26.609  -29.576 30.072  0.50 55.18 ? 287 PRO B CA    1 
ATOM   11129 C  CA    B PRO B 2 287 ? 26.672  -29.725 30.025  0.50 55.24 ? 287 PRO B CA    1 
ATOM   11130 C  C     A PRO B 2 287 ? 27.623  -29.776 28.961  0.50 59.09 ? 287 PRO B C     1 
ATOM   11131 C  C     B PRO B 2 287 ? 27.671  -29.944 28.903  0.50 59.09 ? 287 PRO B C     1 
ATOM   11132 O  O     A PRO B 2 287 ? 28.320  -28.823 28.591  0.50 53.10 ? 287 PRO B O     1 
ATOM   11133 O  O     B PRO B 2 287 ? 28.402  -29.010 28.545  0.50 53.14 ? 287 PRO B O     1 
ATOM   11134 C  CB    A PRO B 2 287 ? 27.210  -29.893 31.449  0.50 59.42 ? 287 PRO B CB    1 
ATOM   11135 C  CB    B PRO B 2 287 ? 27.221  -30.224 31.368  0.50 59.20 ? 287 PRO B CB    1 
ATOM   11136 C  CG    A PRO B 2 287 ? 26.084  -30.467 32.228  0.50 58.78 ? 287 PRO B CG    1 
ATOM   11137 C  CG    B PRO B 2 287 ? 26.032  -30.712 32.101  0.50 58.94 ? 287 PRO B CG    1 
ATOM   11138 C  CD    A PRO B 2 287 ? 25.294  -31.261 31.235  0.50 58.76 ? 287 PRO B CD    1 
ATOM   11139 C  CD    B PRO B 2 287 ? 25.138  -31.308 31.060  0.50 58.75 ? 287 PRO B CD    1 
ATOM   11140 N  N     A GLU B 2 288 ? 27.729  -30.990 28.419  0.50 55.36 ? 288 GLU B N     1 
ATOM   11141 N  N     B GLU B 2 288 ? 27.733  -31.152 28.340  0.50 55.22 ? 288 GLU B N     1 
ATOM   11142 C  CA    A GLU B 2 288 ? 28.604  -31.208 27.273  0.50 57.35 ? 288 GLU B CA    1 
ATOM   11143 C  CA    B GLU B 2 288 ? 28.620  -31.415 27.215  0.50 57.40 ? 288 GLU B CA    1 
ATOM   11144 C  C     A GLU B 2 288 ? 28.031  -30.568 26.015  0.50 55.19 ? 288 GLU B C     1 
ATOM   11145 C  C     B GLU B 2 288 ? 28.115  -30.797 25.918  0.50 55.51 ? 288 GLU B C     1 
ATOM   11146 O  O     A GLU B 2 288 ? 28.768  -29.956 25.233  0.50 53.12 ? 288 GLU B O     1 
ATOM   11147 O  O     B GLU B 2 288 ? 28.910  -30.590 24.997  0.50 54.00 ? 288 GLU B O     1 
ATOM   11148 C  CB    A GLU B 2 288 ? 28.829  -32.706 27.063  0.50 55.59 ? 288 GLU B CB    1 
ATOM   11149 C  CB    B GLU B 2 288 ? 28.804  -32.925 27.034  0.50 55.63 ? 288 GLU B CB    1 
ATOM   11150 C  CG    A GLU B 2 288 ? 29.657  -33.373 28.153  0.50 55.17 ? 288 GLU B CG    1 
ATOM   11151 C  CG    B GLU B 2 288 ? 30.012  -33.314 26.193  0.50 58.67 ? 288 GLU B CG    1 
ATOM   11152 C  CD    A GLU B 2 288 ? 29.743  -34.878 27.981  0.50 58.33 ? 288 GLU B CD    1 
ATOM   11153 C  CD    B GLU B 2 288 ? 30.368  -34.782 26.322  0.50 57.21 ? 288 GLU B CD    1 
ATOM   11154 O  OE1   A GLU B 2 288 ? 28.687  -35.525 27.825  0.50 57.28 ? 288 GLU B OE1   1 
ATOM   11155 O  OE1   B GLU B 2 288 ? 29.643  -35.513 27.027  0.50 58.89 ? 288 GLU B OE1   1 
ATOM   11156 O  OE2   A GLU B 2 288 ? 30.870  -35.416 27.992  0.50 67.16 ? 288 GLU B OE2   1 
ATOM   11157 O  OE2   B GLU B 2 288 ? 31.380  -35.203 25.722  0.50 61.79 ? 288 GLU B OE2   1 
ATOM   11158 N  N     A LEU B 2 289 ? 26.717  -30.690 25.808  0.50 53.73 ? 289 LEU B N     1 
ATOM   11159 N  N     B LEU B 2 289 ? 26.820  -30.495 25.826  0.50 53.75 ? 289 LEU B N     1 
ATOM   11160 C  CA    A LEU B 2 289 ? 26.101  -30.149 24.599  0.50 53.20 ? 289 LEU B CA    1 
ATOM   11161 C  CA    B LEU B 2 289 ? 26.292  -29.867 24.621  0.50 53.32 ? 289 LEU B CA    1 
ATOM   11162 C  C     A LEU B 2 289 ? 26.213  -28.631 24.550  0.50 48.42 ? 289 LEU B C     1 
ATOM   11163 C  C     B LEU B 2 289 ? 26.434  -28.353 24.681  0.50 48.54 ? 289 LEU B C     1 
ATOM   11164 O  O     A LEU B 2 289 ? 26.591  -28.060 23.522  0.50 48.71 ? 289 LEU B O     1 
ATOM   11165 O  O     B LEU B 2 289 ? 26.897  -27.727 23.722  0.50 48.47 ? 289 LEU B O     1 
ATOM   11166 C  CB    A LEU B 2 289 ? 24.639  -30.585 24.511  0.50 51.47 ? 289 LEU B CB    1 
ATOM   11167 C  CB    B LEU B 2 289 ? 24.830  -30.261 24.414  0.50 50.69 ? 289 LEU B CB    1 
ATOM   11168 C  CG    A LEU B 2 289 ? 24.399  -32.026 24.060  0.50 54.59 ? 289 LEU B CG    1 
ATOM   11169 C  CG    B LEU B 2 289 ? 24.584  -31.669 23.873  0.50 54.28 ? 289 LEU B CG    1 
ATOM   11170 C  CD1   A LEU B 2 289 ? 22.912  -32.305 23.941  0.50 51.02 ? 289 LEU B CD1   1 
ATOM   11171 C  CD1   B LEU B 2 289 ? 23.092  -31.949 23.776  0.50 49.69 ? 289 LEU B CD1   1 
ATOM   11172 C  CD2   A LEU B 2 289 ? 25.104  -32.294 22.740  0.50 51.58 ? 289 LEU B CD2   1 
ATOM   11173 C  CD2   B LEU B 2 289 ? 25.250  -31.831 22.520  0.50 51.38 ? 289 LEU B CD2   1 
ATOM   11174 N  N     A THR B 2 290 ? 25.884  -27.956 25.655  0.50 48.23 ? 290 THR B N     1 
ATOM   11175 N  N     B THR B 2 290 ? 26.045  -27.747 25.804  0.50 48.41 ? 290 THR B N     1 
ATOM   11176 C  CA    A THR B 2 290 ? 26.015  -26.502 25.683  0.50 48.88 ? 290 THR B CA    1 
ATOM   11177 C  CA    B THR B 2 290 ? 26.145  -26.299 25.934  0.50 49.24 ? 290 THR B CA    1 
ATOM   11178 C  C     A THR B 2 290 ? 27.468  -26.075 25.533  0.50 49.47 ? 290 THR B C     1 
ATOM   11179 C  C     B THR B 2 290 ? 27.586  -25.810 25.898  0.50 49.31 ? 290 THR B C     1 
ATOM   11180 O  O     A THR B 2 290 ? 27.751  -25.038 24.925  0.50 49.03 ? 290 THR B O     1 
ATOM   11181 O  O     B THR B 2 290 ? 27.818  -24.623 25.654  0.50 52.53 ? 290 THR B O     1 
ATOM   11182 C  CB    A THR B 2 290 ? 25.427  -25.937 26.977  0.50 49.78 ? 290 THR B CB    1 
ATOM   11183 C  CB    B THR B 2 290 ? 25.476  -25.827 27.227  0.50 49.51 ? 290 THR B CB    1 
ATOM   11184 O  OG1   A THR B 2 290 ? 26.256  -26.309 28.084  0.50 52.62 ? 290 THR B OG1   1 
ATOM   11185 O  OG1   B THR B 2 290 ? 26.176  -26.363 28.356  0.50 53.17 ? 290 THR B OG1   1 
ATOM   11186 C  CG2   A THR B 2 290 ? 24.021  -26.475 27.200  0.50 50.58 ? 290 THR B CG2   1 
ATOM   11187 C  CG2   B THR B 2 290 ? 24.027  -26.286 27.268  0.50 50.66 ? 290 THR B CG2   1 
ATOM   11188 N  N     A GLN B 2 291 ? 28.398  -26.864 26.071  0.50 50.37 ? 291 GLN B N     1 
ATOM   11189 N  N     B GLN B 2 291 ? 28.556  -26.693 26.127  0.50 50.69 ? 291 GLN B N     1 
ATOM   11190 C  CA    A GLN B 2 291 ? 29.818  -26.576 25.895  0.50 55.32 ? 291 GLN B CA    1 
ATOM   11191 C  CA    B GLN B 2 291 ? 29.951  -26.278 26.054  0.50 55.11 ? 291 GLN B CA    1 
ATOM   11192 C  C     A GLN B 2 291 ? 30.226  -26.706 24.432  0.50 51.09 ? 291 GLN B C     1 
ATOM   11193 C  C     B GLN B 2 291 ? 30.482  -26.377 24.628  0.50 52.07 ? 291 GLN B C     1 
ATOM   11194 O  O     A GLN B 2 291 ? 30.716  -25.749 23.819  0.50 49.38 ? 291 GLN B O     1 
ATOM   11195 O  O     B GLN B 2 291 ? 31.166  -25.463 24.154  0.50 53.00 ? 291 GLN B O     1 
ATOM   11196 C  CB    A GLN B 2 291 ? 30.646  -27.516 26.776  0.50 56.71 ? 291 GLN B CB    1 
ATOM   11197 C  CB    B GLN B 2 291 ? 30.797  -27.111 27.019  0.50 56.96 ? 291 GLN B CB    1 
ATOM   11198 C  CG    A GLN B 2 291 ? 32.124  -27.581 26.423  0.50 56.26 ? 291 GLN B CG    1 
ATOM   11199 C  CG    B GLN B 2 291 ? 32.250  -26.683 27.105  0.50 59.45 ? 291 GLN B CG    1 
ATOM   11200 C  CD    A GLN B 2 291 ? 32.863  -28.643 27.220  0.50 55.52 ? 291 GLN B CD    1 
ATOM   11201 C  CD    B GLN B 2 291 ? 33.019  -27.455 28.164  0.50 61.45 ? 291 GLN B CD    1 
ATOM   11202 O  OE1   A GLN B 2 291 ? 32.299  -29.263 28.124  0.50 60.02 ? 291 GLN B OE1   1 
ATOM   11203 O  OE1   B GLN B 2 291 ? 32.428  -28.055 29.064  0.50 52.58 ? 291 GLN B OE1   1 
ATOM   11204 N  NE2   A GLN B 2 291 ? 34.131  -28.856 26.887  0.50 56.89 ? 291 GLN B NE2   1 
ATOM   11205 N  NE2   B GLN B 2 291 ? 34.345  -27.446 28.059  0.50 58.38 ? 291 GLN B NE2   1 
ATOM   11206 N  N     A GLN B 2 292 ? 30.015  -27.889 23.850  0.50 52.92 ? 292 GLN B N     1 
ATOM   11207 N  N     B GLN B 2 292 ? 30.169  -27.470 23.927  0.50 51.65 ? 292 GLN B N     1 
ATOM   11208 C  CA    A GLN B 2 292 ? 30.475  -28.144 22.489  0.50 55.01 ? 292 GLN B CA    1 
ATOM   11209 C  CA    B GLN B 2 292 ? 30.581  -27.592 22.532  0.50 54.49 ? 292 GLN B CA    1 
ATOM   11210 C  C     A GLN B 2 292 ? 29.788  -27.238 21.474  0.50 51.86 ? 292 GLN B C     1 
ATOM   11211 C  C     B GLN B 2 292 ? 29.918  -26.536 21.655  0.50 51.81 ? 292 GLN B C     1 
ATOM   11212 O  O     A GLN B 2 292 ? 30.374  -26.920 20.434  0.50 50.04 ? 292 GLN B O     1 
ATOM   11213 O  O     B GLN B 2 292 ? 30.504  -26.105 20.655  0.50 49.48 ? 292 GLN B O     1 
ATOM   11214 C  CB    A GLN B 2 292 ? 30.251  -29.616 22.131  0.50 51.97 ? 292 GLN B CB    1 
ATOM   11215 C  CB    B GLN B 2 292 ? 30.263  -28.992 22.000  0.50 52.84 ? 292 GLN B CB    1 
ATOM   11216 C  CG    A GLN B 2 292 ? 30.988  -30.586 23.045  0.50 56.85 ? 292 GLN B CG    1 
ATOM   11217 C  CG    B GLN B 2 292 ? 31.084  -30.109 22.625  0.50 55.76 ? 292 GLN B CG    1 
ATOM   11218 C  CD    A GLN B 2 292 ? 30.708  -32.041 22.719  0.50 56.41 ? 292 GLN B CD    1 
ATOM   11219 C  CD    B GLN B 2 292 ? 31.002  -31.403 21.834  0.50 56.46 ? 292 GLN B CD    1 
ATOM   11220 O  OE1   A GLN B 2 292 ? 31.020  -32.934 23.506  0.50 63.36 ? 292 GLN B OE1   1 
ATOM   11221 O  OE1   B GLN B 2 292 ? 30.834  -31.388 20.614  0.50 57.79 ? 292 GLN B OE1   1 
ATOM   11222 N  NE2   A GLN B 2 292 ? 30.121  -32.287 21.553  0.50 51.64 ? 292 GLN B NE2   1 
ATOM   11223 N  NE2   B GLN B 2 292 ? 31.118  -32.530 22.527  0.50 57.55 ? 292 GLN B NE2   1 
ATOM   11224 N  N     A MET B 2 293 ? 28.561  -26.798 21.760  0.50 47.23 ? 293 MET B N     1 
ATOM   11225 N  N     B MET B 2 293 ? 28.703  -26.108 22.014  0.50 46.15 ? 293 MET B N     1 
ATOM   11226 C  CA    A MET B 2 293 ? 27.827  -25.980 20.800  0.50 47.20 ? 293 MET B CA    1 
ATOM   11227 C  CA    B MET B 2 293 ? 28.013  -25.080 21.240  0.50 48.18 ? 293 MET B CA    1 
ATOM   11228 C  C     A MET B 2 293 ? 28.464  -24.609 20.613  0.50 45.99 ? 293 MET B C     1 
ATOM   11229 C  C     B MET B 2 293 ? 28.831  -23.804 21.137  0.50 44.74 ? 293 MET B C     1 
ATOM   11230 O  O     A MET B 2 293 ? 28.336  -24.011 19.538  0.50 39.47 ? 293 MET B O     1 
ATOM   11231 O  O     B MET B 2 293 ? 28.773  -23.111 20.115  0.50 45.25 ? 293 MET B O     1 
ATOM   11232 C  CB    A MET B 2 293 ? 26.376  -25.821 21.247  0.50 41.70 ? 293 MET B CB    1 
ATOM   11233 C  CB    B MET B 2 293 ? 26.659  -24.753 21.866  0.50 45.84 ? 293 MET B CB    1 
ATOM   11234 C  CG    A MET B 2 293 ? 25.359  -25.977 20.136  0.50 43.22 ? 293 MET B CG    1 
ATOM   11235 C  CG    B MET B 2 293 ? 25.567  -25.761 21.618  0.50 43.19 ? 293 MET B CG    1 
ATOM   11236 S  SD    A MET B 2 293 ? 23.756  -25.313 20.616  0.50 44.47 ? 293 MET B SD    1 
ATOM   11237 S  SD    B MET B 2 293 ? 23.973  -25.042 22.043  0.50 46.93 ? 293 MET B SD    1 
ATOM   11238 C  CE    A MET B 2 293 ? 23.755  -25.676 22.371  0.50 44.88 ? 293 MET B CE    1 
ATOM   11239 C  CE    B MET B 2 293 ? 24.411  -24.079 23.485  0.50 39.00 ? 293 MET B CE    1 
ATOM   11240 N  N     A PHE B 2 294 ? 29.136  -24.092 21.640  0.50 45.26 ? 294 PHE B N     1 
ATOM   11241 N  N     B PHE B 2 294 ? 29.581  -23.469 22.184  0.50 45.53 ? 294 PHE B N     1 
ATOM   11242 C  CA    A PHE B 2 294 ? 29.785  -22.789 21.581  0.50 47.80 ? 294 PHE B CA    1 
ATOM   11243 C  CA    B PHE B 2 294 ? 30.335  -22.225 22.246  0.50 44.51 ? 294 PHE B CA    1 
ATOM   11244 C  C     A PHE B 2 294 ? 31.280  -22.884 21.303  0.50 43.56 ? 294 PHE B C     1 
ATOM   11245 C  C     B PHE B 2 294 ? 31.829  -22.440 22.017  0.50 46.72 ? 294 PHE B C     1 
ATOM   11246 O  O     A PHE B 2 294 ? 31.963  -21.854 21.293  0.50 45.90 ? 294 PHE B O     1 
ATOM   11247 O  O     B PHE B 2 294 ? 32.652  -21.635 22.465  0.50 50.80 ? 294 PHE B O     1 
ATOM   11248 C  CB    A PHE B 2 294 ? 29.549  -22.024 22.887  0.50 42.87 ? 294 PHE B CB    1 
ATOM   11249 C  CB    B PHE B 2 294 ? 30.076  -21.533 23.582  0.50 46.36 ? 294 PHE B CB    1 
ATOM   11250 C  CG    A PHE B 2 294 ? 28.135  -21.543 23.063  0.50 40.19 ? 294 PHE B CG    1 
ATOM   11251 C  CG    B PHE B 2 294 ? 28.676  -20.998 23.718  0.50 42.57 ? 294 PHE B CG    1 
ATOM   11252 C  CD1   A PHE B 2 294 ? 27.157  -22.386 23.565  0.50 44.89 ? 294 PHE B CD1   1 
ATOM   11253 C  CD1   B PHE B 2 294 ? 27.652  -21.807 24.186  0.50 46.08 ? 294 PHE B CD1   1 
ATOM   11254 C  CD2   A PHE B 2 294 ? 27.785  -20.245 22.735  0.50 36.68 ? 294 PHE B CD2   1 
ATOM   11255 C  CD2   B PHE B 2 294 ? 28.381  -19.693 23.361  0.50 34.73 ? 294 PHE B CD2   1 
ATOM   11256 C  CE1   A PHE B 2 294 ? 25.856  -21.946 23.731  0.50 42.80 ? 294 PHE B CE1   1 
ATOM   11257 C  CE1   B PHE B 2 294 ? 26.364  -21.317 24.314  0.50 42.42 ? 294 PHE B CE1   1 
ATOM   11258 C  CE2   A PHE B 2 294 ? 26.485  -19.799 22.897  0.50 38.24 ? 294 PHE B CE2   1 
ATOM   11259 C  CE2   B PHE B 2 294 ? 27.092  -19.199 23.482  0.50 39.53 ? 294 PHE B CE2   1 
ATOM   11260 C  CZ    A PHE B 2 294 ? 25.520  -20.652 23.396  0.50 40.09 ? 294 PHE B CZ    1 
ATOM   11261 C  CZ    B PHE B 2 294 ? 26.083  -20.013 23.959  0.50 38.33 ? 294 PHE B CZ    1 
ATOM   11262 N  N     A ASP B 2 295 ? 31.799  -24.087 21.081  0.50 44.03 ? 295 ASP B N     1 
ATOM   11263 N  N     B ASP B 2 295 ? 32.187  -23.510 21.313  0.50 44.42 ? 295 ASP B N     1 
ATOM   11264 C  CA    A ASP B 2 295 ? 33.213  -24.274 20.792  0.50 44.81 ? 295 ASP B CA    1 
ATOM   11265 C  CA    B ASP B 2 295 ? 33.568  -23.834 20.986  0.50 43.43 ? 295 ASP B CA    1 
ATOM   11266 C  C     A ASP B 2 295 ? 33.509  -23.890 19.347  0.50 39.97 ? 295 ASP B C     1 
ATOM   11267 C  C     B ASP B 2 295 ? 33.812  -23.505 19.519  0.50 39.69 ? 295 ASP B C     1 
ATOM   11268 O  O     A ASP B 2 295 ? 32.722  -24.178 18.441  0.50 38.31 ? 295 ASP B O     1 
ATOM   11269 O  O     B ASP B 2 295 ? 33.000  -23.861 18.658  0.50 37.71 ? 295 ASP B O     1 
ATOM   11270 C  CB    A ASP B 2 295 ? 33.607  -25.731 21.047  0.50 49.81 ? 295 ASP B CB    1 
ATOM   11271 C  CB    B ASP B 2 295 ? 33.850  -25.314 21.264  0.50 49.80 ? 295 ASP B CB    1 
ATOM   11272 C  CG    A ASP B 2 295 ? 35.106  -25.924 21.187  0.50 47.31 ? 295 ASP B CG    1 
ATOM   11273 C  CG    B ASP B 2 295 ? 35.332  -25.630 21.350  0.50 46.81 ? 295 ASP B CG    1 
ATOM   11274 O  OD1   A ASP B 2 295 ? 35.860  -25.481 20.296  0.50 43.24 ? 295 ASP B OD1   1 
ATOM   11275 O  OD1   B ASP B 2 295 ? 36.119  -25.077 20.555  0.50 47.39 ? 295 ASP B OD1   1 
ATOM   11276 O  OD2   A ASP B 2 295 ? 35.531  -26.528 22.195  0.50 51.53 ? 295 ASP B OD2   1 
ATOM   11277 O  OD2   B ASP B 2 295 ? 35.709  -26.447 22.217  0.50 51.85 ? 295 ASP B OD2   1 
ATOM   11278 N  N     A SER B 2 296 ? 34.652  -23.230 19.138  0.50 42.75 ? 296 SER B N     1 
ATOM   11279 N  N     B SER B 2 296 ? 34.931  -22.828 19.237  0.50 42.91 ? 296 SER B N     1 
ATOM   11280 C  CA    A SER B 2 296 ? 35.046  -22.840 17.785  0.50 38.64 ? 296 SER B CA    1 
ATOM   11281 C  CA    B SER B 2 296 ? 35.221  -22.425 17.863  0.50 39.18 ? 296 SER B CA    1 
ATOM   11282 C  C     A SER B 2 296 ? 35.149  -24.042 16.857  0.50 38.01 ? 296 SER B C     1 
ATOM   11283 C  C     B SER B 2 296 ? 35.331  -23.627 16.934  0.50 37.03 ? 296 SER B C     1 
ATOM   11284 O  O     A SER B 2 296 ? 34.864  -23.927 15.660  0.50 33.98 ? 296 SER B O     1 
ATOM   11285 O  O     B SER B 2 296 ? 35.000  -23.525 15.747  0.50 34.90 ? 296 SER B O     1 
ATOM   11286 C  CB    A SER B 2 296 ? 36.377  -22.090 17.817  0.50 37.20 ? 296 SER B CB    1 
ATOM   11287 C  CB    B SER B 2 296 ? 36.509  -21.602 17.809  0.50 35.68 ? 296 SER B CB    1 
ATOM   11288 O  OG    A SER B 2 296 ? 37.020  -22.155 16.557  0.50 46.18 ? 296 SER B OG    1 
ATOM   11289 O  OG    B SER B 2 296 ? 37.650  -22.420 17.997  0.50 44.75 ? 296 SER B OG    1 
ATOM   11290 N  N     A LYS B 2 297 ? 35.540  -25.202 17.391  0.50 38.04 ? 297 LYS B N     1 
ATOM   11291 N  N     B LYS B 2 297 ? 35.772  -24.773 17.456  0.50 37.03 ? 297 LYS B N     1 
ATOM   11292 C  CA    A LYS B 2 297 ? 35.668  -26.404 16.575  0.50 37.14 ? 297 LYS B CA    1 
ATOM   11293 C  CA    B LYS B 2 297 ? 35.933  -25.969 16.638  0.50 37.58 ? 297 LYS B CA    1 
ATOM   11294 C  C     A LYS B 2 297 ? 34.342  -26.845 15.970  0.50 39.31 ? 297 LYS B C     1 
ATOM   11295 C  C     B LYS B 2 297 ? 34.607  -26.599 16.237  0.50 39.90 ? 297 LYS B C     1 
ATOM   11296 O  O     A LYS B 2 297 ? 34.343  -27.619 15.007  0.50 38.34 ? 297 LYS B O     1 
ATOM   11297 O  O     B LYS B 2 297 ? 34.609  -27.536 15.432  0.50 34.67 ? 297 LYS B O     1 
ATOM   11298 C  CB    A LYS B 2 297 ? 36.251  -27.545 17.411  0.50 42.91 ? 297 LYS B CB    1 
ATOM   11299 C  CB    B LYS B 2 297 ? 36.782  -27.000 17.380  0.50 45.03 ? 297 LYS B CB    1 
ATOM   11300 C  CG    A LYS B 2 297 ? 37.700  -27.350 17.829  0.50 47.10 ? 297 LYS B CG    1 
ATOM   11301 C  CG    B LYS B 2 297 ? 38.118  -26.465 17.857  0.50 43.92 ? 297 LYS B CG    1 
ATOM   11302 C  CD    A LYS B 2 297 ? 38.657  -27.761 16.721  0.50 46.91 ? 297 LYS B CD    1 
ATOM   11303 C  CD    B LYS B 2 297 ? 38.960  -27.566 18.480  0.50 50.50 ? 297 LYS B CD    1 
ATOM   11304 C  CE    A LYS B 2 297 ? 40.069  -27.937 17.256  0.50 39.58 ? 297 LYS B CE    1 
ATOM   11305 C  CE    B LYS B 2 297 ? 40.375  -27.082 18.729  0.50 51.62 ? 297 LYS B CE    1 
ATOM   11306 N  NZ    A LYS B 2 297 ? 40.952  -28.640 16.284  0.50 50.63 ? 297 LYS B NZ    1 
ATOM   11307 N  NZ    B LYS B 2 297 ? 40.935  -26.456 17.498  0.50 42.68 ? 297 LYS B NZ    1 
ATOM   11308 N  N     A ASN B 2 298 ? 33.216  -26.375 16.506  0.50 40.34 ? 298 ASN B N     1 
ATOM   11309 N  N     B ASN B 2 298 ? 33.486  -26.123 16.776  0.50 40.00 ? 298 ASN B N     1 
ATOM   11310 C  CA    A ASN B 2 298 ? 31.899  -26.818 16.070  0.50 35.11 ? 298 ASN B CA    1 
ATOM   11311 C  CA    B ASN B 2 298 ? 32.168  -26.623 16.411  0.50 36.21 ? 298 ASN B CA    1 
ATOM   11312 C  C     A ASN B 2 298 ? 31.212  -25.842 15.123  0.50 30.61 ? 298 ASN B C     1 
ATOM   11313 C  C     B ASN B 2 298 ? 31.406  -25.673 15.500  0.50 31.61 ? 298 ASN B C     1 
ATOM   11314 O  O     A ASN B 2 298 ? 30.117  -26.143 14.639  0.50 32.59 ? 298 ASN B O     1 
ATOM   11315 O  O     B ASN B 2 298 ? 30.261  -25.964 15.143  0.50 32.01 ? 298 ASN B O     1 
ATOM   11316 C  CB    A ASN B 2 298 ? 31.002  -27.067 17.285  0.50 39.13 ? 298 ASN B CB    1 
ATOM   11317 C  CB    B ASN B 2 298 ? 31.343  -26.903 17.671  0.50 39.25 ? 298 ASN B CB    1 
ATOM   11318 C  CG    A ASN B 2 298 ? 31.391  -28.317 18.049  0.50 43.61 ? 298 ASN B CG    1 
ATOM   11319 C  CG    B ASN B 2 298 ? 31.676  -28.242 18.300  0.50 43.37 ? 298 ASN B CG    1 
ATOM   11320 O  OD1   A ASN B 2 298 ? 32.271  -28.287 18.908  0.50 42.92 ? 298 ASN B OD1   1 
ATOM   11321 O  OD1   B ASN B 2 298 ? 32.796  -28.465 18.755  0.50 44.84 ? 298 ASN B OD1   1 
ATOM   11322 N  ND2   A ASN B 2 298 ? 30.727  -29.424 17.744  0.50 44.20 ? 298 ASN B ND2   1 
ATOM   11323 N  ND2   B ASN B 2 298 ? 30.700  -29.140 18.332  0.50 43.99 ? 298 ASN B ND2   1 
ATOM   11324 N  N     A MET B 2 299 ? 31.818  -24.693 14.841  0.50 29.39 ? 299 MET B N     1 
ATOM   11325 N  N     B MET B 2 299 ? 32.006  -24.550 15.119  0.50 29.55 ? 299 MET B N     1 
ATOM   11326 C  CA    A MET B 2 299 ? 31.191  -23.705 13.976  0.50 30.23 ? 299 MET B CA    1 
ATOM   11327 C  CA    B MET B 2 299 ? 31.338  -23.591 14.253  0.50 30.62 ? 299 MET B CA    1 
ATOM   11328 C  C     A MET B 2 299 ? 31.303  -24.117 12.514  0.50 32.86 ? 299 MET B C     1 
ATOM   11329 C  C     B MET B 2 299 ? 31.442  -24.023 12.797  0.50 32.74 ? 299 MET B C     1 
ATOM   11330 O  O     A MET B 2 299 ? 32.321  -24.669 12.085  0.50 31.41 ? 299 MET B O     1 
ATOM   11331 O  O     B MET B 2 299 ? 32.471  -24.545 12.360  0.50 32.06 ? 299 MET B O     1 
ATOM   11332 C  CB    A MET B 2 299 ? 31.831  -22.332 14.188  0.50 29.26 ? 299 MET B CB    1 
ATOM   11333 C  CB    B MET B 2 299 ? 31.948  -22.199 14.432  0.50 28.84 ? 299 MET B CB    1 
ATOM   11334 C  CG    A MET B 2 299 ? 31.663  -21.800 15.601  0.50 35.12 ? 299 MET B CG    1 
ATOM   11335 C  CG    B MET B 2 299 ? 31.752  -21.622 15.824  0.50 34.94 ? 299 MET B CG    1 
ATOM   11336 S  SD    A MET B 2 299 ? 29.928  -21.755 16.085  0.50 39.01 ? 299 MET B SD    1 
ATOM   11337 S  SD    B MET B 2 299 ? 30.005  -21.494 16.250  0.50 38.45 ? 299 MET B SD    1 
ATOM   11338 C  CE    A MET B 2 299 ? 30.067  -21.795 17.870  0.50 37.50 ? 299 MET B CE    1 
ATOM   11339 C  CE    B MET B 2 299 ? 30.099  -21.051 17.982  0.50 41.04 ? 299 MET B CE    1 
ATOM   11340 N  N     A MET B 2 300 ? 30.248  -23.847 11.745  0.50 29.16 ? 300 MET B N     1 
ATOM   11341 N  N     B MET B 2 300 ? 30.367  -23.803 12.043  0.50 28.85 ? 300 MET B N     1 
ATOM   11342 C  CA    A MET B 2 300 ? 30.279  -24.125 10.313  0.50 30.61 ? 300 MET B CA    1 
ATOM   11343 C  CA    B MET B 2 300 ? 30.380  -24.068 10.611  0.50 31.01 ? 300 MET B CA    1 
ATOM   11344 C  C     A MET B 2 300 ? 30.907  -22.995 9.507   0.50 28.80 ? 300 MET B C     1 
ATOM   11345 C  C     B MET B 2 300 ? 30.901  -22.884 9.806   0.50 29.58 ? 300 MET B C     1 
ATOM   11346 O  O     A MET B 2 300 ? 30.900  -23.057 8.274   0.50 30.17 ? 300 MET B O     1 
ATOM   11347 O  O     B MET B 2 300 ? 30.917  -22.946 8.574   0.50 28.18 ? 300 MET B O     1 
ATOM   11348 C  CB    A MET B 2 300 ? 28.866  -24.413 9.793   0.50 29.34 ? 300 MET B CB    1 
ATOM   11349 C  CB    B MET B 2 300 ? 28.981  -24.467 10.131  0.50 29.51 ? 300 MET B CB    1 
ATOM   11350 C  CG    A MET B 2 300 ? 28.205  -25.639 10.426  0.50 33.68 ? 300 MET B CG    1 
ATOM   11351 C  CG    B MET B 2 300 ? 28.432  -25.724 10.815  0.50 34.80 ? 300 MET B CG    1 
ATOM   11352 S  SD    A MET B 2 300 ? 29.032  -27.198 10.035  0.50 36.89 ? 300 MET B SD    1 
ATOM   11353 S  SD    B MET B 2 300 ? 29.471  -27.192 10.607  0.50 35.81 ? 300 MET B SD    1 
ATOM   11354 C  CE    A MET B 2 300 ? 28.279  -28.291 11.234  0.50 35.13 ? 300 MET B CE    1 
ATOM   11355 C  CE    B MET B 2 300 ? 28.676  -28.342 11.725  0.50 33.57 ? 300 MET B CE    1 
ATOM   11356 N  N     A ALA B 2 301 ? 31.431  -21.967 10.169  0.50 28.13 ? 301 ALA B N     1 
ATOM   11357 N  N     B ALA B 2 301 ? 31.315  -21.811 10.471  0.50 28.25 ? 301 ALA B N     1 
ATOM   11358 C  CA    A ALA B 2 301 ? 32.210  -20.920 9.521   0.50 28.12 ? 301 ALA B CA    1 
ATOM   11359 C  CA    B ALA B 2 301 ? 32.040  -20.714 9.848   0.50 28.27 ? 301 ALA B CA    1 
ATOM   11360 C  C     A ALA B 2 301 ? 33.492  -20.726 10.315  0.50 27.45 ? 301 ALA B C     1 
ATOM   11361 C  C     B ALA B 2 301 ? 33.450  -20.672 10.418  0.50 27.39 ? 301 ALA B C     1 
ATOM   11362 O  O     A ALA B 2 301 ? 33.443  -20.480 11.524  0.50 23.51 ? 301 ALA B O     1 
ATOM   11363 O  O     B ALA B 2 301 ? 33.653  -20.935 11.608  0.50 25.43 ? 301 ALA B O     1 
ATOM   11364 C  CB    A ALA B 2 301 ? 31.428  -19.606 9.432   0.50 28.72 ? 301 ALA B CB    1 
ATOM   11365 C  CB    B ALA B 2 301 ? 31.337  -19.375 10.084  0.50 29.60 ? 301 ALA B CB    1 
ATOM   11366 N  N     A ALA B 2 302 ? 34.635  -20.821 9.633   0.50 26.06 ? 302 ALA B N     1 
ATOM   11367 N  N     B ALA B 2 302 ? 34.428  -20.340 9.571   0.50 22.78 ? 302 ALA B N     1 
ATOM   11368 C  CA    A ALA B 2 302 ? 35.931  -20.865 10.304  0.50 20.81 ? 302 ALA B CA    1 
ATOM   11369 C  CA    B ALA B 2 302 ? 35.833  -20.351 9.981   0.50 24.90 ? 302 ALA B CA    1 
ATOM   11370 C  C     A ALA B 2 302 ? 36.293  -19.538 10.958  0.50 26.32 ? 302 ALA B C     1 
ATOM   11371 C  C     B ALA B 2 302 ? 36.172  -19.013 10.630  0.50 29.92 ? 302 ALA B C     1 
ATOM   11372 O  O     A ALA B 2 302 ? 37.315  -18.931 10.621  0.50 30.34 ? 302 ALA B O     1 
ATOM   11373 O  O     B ALA B 2 302 ? 36.732  -18.103 10.015  0.50 32.70 ? 302 ALA B O     1 
ATOM   11374 C  CB    A ALA B 2 302 ? 37.026  -21.275 9.316   0.50 28.89 ? 302 ALA B CB    1 
ATOM   11375 C  CB    B ALA B 2 302 ? 36.746  -20.650 8.797   0.50 26.94 ? 302 ALA B CB    1 
ATOM   11376 N  N     A CYS B 2 303 ? 35.461  -19.079 11.889  0.50 28.58 ? 303 CYS B N     1 
ATOM   11377 N  N     B CYS B 2 303 ? 35.808  -18.898 11.904  0.50 28.74 ? 303 CYS B N     1 
ATOM   11378 C  CA    A CYS B 2 303 ? 35.749  -17.914 12.709  0.50 27.32 ? 303 CYS B CA    1 
ATOM   11379 C  CA    B CYS B 2 303 ? 36.193  -17.746 12.703  0.50 28.14 ? 303 CYS B CA    1 
ATOM   11380 C  C     A CYS B 2 303 ? 35.747  -18.339 14.169  0.50 31.56 ? 303 CYS B C     1 
ATOM   11381 C  C     B CYS B 2 303 ? 36.136  -18.140 14.170  0.50 29.80 ? 303 CYS B C     1 
ATOM   11382 O  O     A CYS B 2 303 ? 34.939  -19.181 14.577  0.50 31.81 ? 303 CYS B O     1 
ATOM   11383 O  O     B CYS B 2 303 ? 35.521  -19.143 14.539  0.50 34.63 ? 303 CYS B O     1 
ATOM   11384 C  CB    A CYS B 2 303 ? 34.719  -16.800 12.494  0.50 30.28 ? 303 CYS B CB    1 
ATOM   11385 C  CB    B CYS B 2 303 ? 35.304  -16.530 12.421  0.50 28.75 ? 303 CYS B CB    1 
ATOM   11386 S  SG    A CYS B 2 303 ? 34.105  -16.636 10.809  0.50 26.93 ? 303 CYS B SG    1 
ATOM   11387 S  SG    B CYS B 2 303 ? 33.544  -16.790 12.698  0.50 35.39 ? 303 CYS B SG    1 
ATOM   11388 N  N     A ASP B 2 304 ? 36.655  -17.761 14.953  0.50 30.67 ? 304 ASP B N     1 
ATOM   11389 N  N     B ASP B 2 304 ? 36.798  -17.338 14.999  0.50 30.11 ? 304 ASP B N     1 
ATOM   11390 C  CA    A ASP B 2 304 ? 36.711  -18.037 16.381  0.50 33.58 ? 304 ASP B CA    1 
ATOM   11391 C  CA    B ASP B 2 304 ? 36.855  -17.597 16.428  0.50 34.79 ? 304 ASP B CA    1 
ATOM   11392 C  C     A ASP B 2 304 ? 35.767  -17.076 17.094  0.50 32.33 ? 304 ASP B C     1 
ATOM   11393 C  C     B ASP B 2 304 ? 35.793  -16.759 17.123  0.50 31.61 ? 304 ASP B C     1 
ATOM   11394 O  O     A ASP B 2 304 ? 36.023  -15.862 17.095  0.50 31.04 ? 304 ASP B O     1 
ATOM   11395 O  O     B ASP B 2 304 ? 35.931  -15.528 17.180  0.50 30.03 ? 304 ASP B O     1 
ATOM   11396 C  CB    A ASP B 2 304 ? 38.134  -17.888 16.904  0.50 32.72 ? 304 ASP B CB    1 
ATOM   11397 C  CB    B ASP B 2 304 ? 38.247  -17.267 16.973  0.50 34.68 ? 304 ASP B CB    1 
ATOM   11398 C  CG    A ASP B 2 304 ? 38.334  -18.549 18.255  0.50 39.57 ? 304 ASP B CG    1 
ATOM   11399 C  CG    B ASP B 2 304 ? 38.474  -17.795 18.381  0.50 39.17 ? 304 ASP B CG    1 
ATOM   11400 O  OD1   A ASP B 2 304 ? 37.396  -18.537 19.082  0.50 38.75 ? 304 ASP B OD1   1 
ATOM   11401 O  OD1   B ASP B 2 304 ? 37.484  -18.039 19.104  0.50 38.58 ? 304 ASP B OD1   1 
ATOM   11402 O  OD2   A ASP B 2 304 ? 39.435  -19.086 18.492  0.50 41.33 ? 304 ASP B OD2   1 
ATOM   11403 O  OD2   B ASP B 2 304 ? 39.652  -17.959 18.768  0.50 39.10 ? 304 ASP B OD2   1 
ATOM   11404 N  N     A PRO B 2 305 ? 34.677  -17.553 17.698  0.50 30.96 ? 305 PRO B N     1 
ATOM   11405 N  N     B PRO B 2 305 ? 34.723  -17.360 17.650  0.50 30.94 ? 305 PRO B N     1 
ATOM   11406 C  CA    A PRO B 2 305 ? 33.722  -16.620 18.315  0.50 32.54 ? 305 PRO B CA    1 
ATOM   11407 C  CA    B PRO B 2 305 ? 33.732  -16.559 18.386  0.50 32.54 ? 305 PRO B CA    1 
ATOM   11408 C  C     A PRO B 2 305 ? 34.315  -15.823 19.459  0.50 28.30 ? 305 PRO B C     1 
ATOM   11409 C  C     B PRO B 2 305 ? 34.344  -15.765 19.524  0.50 28.27 ? 305 PRO B C     1 
ATOM   11410 O  O     A PRO B 2 305 ? 33.798  -14.747 19.776  0.50 28.89 ? 305 PRO B O     1 
ATOM   11411 O  O     B PRO B 2 305 ? 33.818  -14.706 19.884  0.50 29.05 ? 305 PRO B O     1 
ATOM   11412 C  CB    A PRO B 2 305 ? 32.593  -17.540 18.794  0.50 33.46 ? 305 PRO B CB    1 
ATOM   11413 C  CB    B PRO B 2 305 ? 32.740  -17.611 18.898  0.50 33.72 ? 305 PRO B CB    1 
ATOM   11414 C  CG    A PRO B 2 305 ? 33.257  -18.866 19.000  0.50 33.97 ? 305 PRO B CG    1 
ATOM   11415 C  CG    B PRO B 2 305 ? 32.903  -18.771 17.977  0.50 36.15 ? 305 PRO B CG    1 
ATOM   11416 C  CD    A PRO B 2 305 ? 34.319  -18.962 17.939  0.50 37.30 ? 305 PRO B CD    1 
ATOM   11417 C  CD    B PRO B 2 305 ? 34.351  -18.783 17.582  0.50 36.37 ? 305 PRO B CD    1 
ATOM   11418 N  N     A ARG B 2 306 ? 35.396  -16.305 20.074  0.50 30.40 ? 306 ARG B N     1 
ATOM   11419 N  N     B ARG B 2 306 ? 35.455  -16.239 20.086  0.50 30.38 ? 306 ARG B N     1 
ATOM   11420 C  CA    A ARG B 2 306 ? 36.054  -15.598 21.164  0.50 34.66 ? 306 ARG B CA    1 
ATOM   11421 C  CA    B ARG B 2 306 ? 36.188  -15.531 21.125  0.50 34.64 ? 306 ARG B CA    1 
ATOM   11422 C  C     A ARG B 2 306 ? 36.882  -14.410 20.691  0.50 34.15 ? 306 ARG B C     1 
ATOM   11423 C  C     B ARG B 2 306 ? 37.094  -14.438 20.566  0.50 33.90 ? 306 ARG B C     1 
ATOM   11424 O  O     A ARG B 2 306 ? 37.457  -13.706 21.527  0.50 35.60 ? 306 ARG B O     1 
ATOM   11425 O  O     B ARG B 2 306 ? 37.940  -13.918 21.301  0.50 34.08 ? 306 ARG B O     1 
ATOM   11426 C  CB    A ARG B 2 306 ? 36.931  -16.572 21.957  0.50 37.53 ? 306 ARG B CB    1 
ATOM   11427 C  CB    B ARG B 2 306 ? 37.008  -16.522 21.958  0.50 37.53 ? 306 ARG B CB    1 
ATOM   11428 C  CG    A ARG B 2 306 ? 36.151  -17.732 22.561  0.50 40.98 ? 306 ARG B CG    1 
ATOM   11429 C  CG    B ARG B 2 306 ? 36.187  -17.339 22.954  0.50 41.69 ? 306 ARG B CG    1 
ATOM   11430 C  CD    A ARG B 2 306 ? 37.014  -18.579 23.486  0.50 45.94 ? 306 ARG B CD    1 
ATOM   11431 C  CD    B ARG B 2 306 ? 35.441  -18.488 22.290  0.50 41.16 ? 306 ARG B CD    1 
ATOM   11432 N  NE    A ARG B 2 306 ? 36.291  -19.741 23.991  0.50 52.08 ? 306 ARG B NE    1 
ATOM   11433 N  NE    B ARG B 2 306 ? 34.463  -19.091 23.187  0.50 54.21 ? 306 ARG B NE    1 
ATOM   11434 C  CZ    A ARG B 2 306 ? 35.592  -19.762 25.118  0.50 53.68 ? 306 ARG B CZ    1 
ATOM   11435 C  CZ    B ARG B 2 306 ? 34.722  -20.092 24.017  0.50 57.18 ? 306 ARG B CZ    1 
ATOM   11436 N  NH1   A ARG B 2 306 ? 35.509  -18.701 25.901  0.50 51.26 ? 306 ARG B NH1   1 
ATOM   11437 N  NH1   B ARG B 2 306 ? 35.924  -20.642 24.083  0.50 58.26 ? 306 ARG B NH1   1 
ATOM   11438 N  NH2   A ARG B 2 306 ? 34.961  -20.880 25.469  0.50 52.94 ? 306 ARG B NH2   1 
ATOM   11439 N  NH2   B ARG B 2 306 ? 33.751  -20.554 24.799  0.50 48.99 ? 306 ARG B NH2   1 
ATOM   11440 N  N     A HIS B 2 307 ? 36.962  -14.172 19.381  0.50 29.16 ? 307 HIS B N     1 
ATOM   11441 N  N     B HIS B 2 307 ? 36.949  -14.093 19.288  0.50 29.12 ? 307 HIS B N     1 
ATOM   11442 C  CA    A HIS B 2 307 ? 37.560  -12.955 18.850  0.50 29.83 ? 307 HIS B CA    1 
ATOM   11443 C  CA    B HIS B 2 307 ? 37.583  -12.916 18.711  0.50 30.05 ? 307 HIS B CA    1 
ATOM   11444 C  C     A HIS B 2 307 ? 36.546  -11.838 18.657  0.50 32.68 ? 307 HIS B C     1 
ATOM   11445 C  C     B HIS B 2 307 ? 36.607  -11.763 18.544  0.50 32.48 ? 307 HIS B C     1 
ATOM   11446 O  O     A HIS B 2 307 ? 36.944  -10.692 18.417  0.50 32.89 ? 307 HIS B O     1 
ATOM   11447 O  O     B HIS B 2 307 ? 36.957  -10.749 17.931  0.50 32.73 ? 307 HIS B O     1 
ATOM   11448 C  CB    A HIS B 2 307 ? 38.254  -13.237 17.511  0.50 29.65 ? 307 HIS B CB    1 
ATOM   11449 C  CB    B HIS B 2 307 ? 38.213  -13.250 17.355  0.50 29.45 ? 307 HIS B CB    1 
ATOM   11450 C  CG    A HIS B 2 307 ? 39.467  -14.105 17.626  0.50 34.87 ? 307 HIS B CG    1 
ATOM   11451 C  CG    B HIS B 2 307 ? 39.458  -14.074 17.449  0.50 35.15 ? 307 HIS B CG    1 
ATOM   11452 N  ND1   A HIS B 2 307 ? 40.042  -14.725 16.538  0.50 34.99 ? 307 HIS B ND1   1 
ATOM   11453 N  ND1   B HIS B 2 307 ? 40.250  -14.350 16.354  0.50 32.77 ? 307 HIS B ND1   1 
ATOM   11454 C  CD2   A HIS B 2 307 ? 40.220  -14.449 18.697  0.50 36.39 ? 307 HIS B CD2   1 
ATOM   11455 C  CD2   B HIS B 2 307 ? 40.048  -14.684 18.504  0.50 36.22 ? 307 HIS B CD2   1 
ATOM   11456 C  CE1   A HIS B 2 307 ? 41.093  -15.420 16.934  0.50 34.22 ? 307 HIS B CE1   1 
ATOM   11457 C  CE1   B HIS B 2 307 ? 41.273  -15.096 16.731  0.50 35.08 ? 307 HIS B CE1   1 
ATOM   11458 N  NE2   A HIS B 2 307 ? 41.224  -15.268 18.240  0.50 39.54 ? 307 HIS B NE2   1 
ATOM   11459 N  NE2   B HIS B 2 307 ? 41.176  -15.311 18.031  0.50 39.42 ? 307 HIS B NE2   1 
ATOM   11460 N  N     A GLY B 2 308 ? 35.253  -12.142 18.749  0.50 31.12 ? 308 GLY B N     1 
ATOM   11461 N  N     B GLY B 2 308 ? 35.400  -11.894 19.063  0.50 30.89 ? 308 GLY B N     1 
ATOM   11462 C  CA    A GLY B 2 308 ? 34.225  -11.133 18.619  0.50 25.80 ? 308 GLY B CA    1 
ATOM   11463 C  CA    B GLY B 2 308 ? 34.383  -10.881 18.875  0.50 26.13 ? 308 GLY B CA    1 
ATOM   11464 C  C     A GLY B 2 308 ? 33.168  -11.255 19.699  0.50 23.09 ? 308 GLY B C     1 
ATOM   11465 C  C     B GLY B 2 308 ? 33.345  -10.904 19.973  0.50 23.88 ? 308 GLY B C     1 
ATOM   11466 O  O     A GLY B 2 308 ? 33.330  -12.027 20.648  0.50 24.86 ? 308 GLY B O     1 
ATOM   11467 O  O     B GLY B 2 308 ? 33.624  -11.294 21.110  0.50 23.28 ? 308 GLY B O     1 
ATOM   11468 N  N     A ARG B 2 309 ? 32.089  -10.492 19.567  0.50 25.21 ? 309 ARG B N     1 
ATOM   11469 N  N     B ARG B 2 309 ? 32.136  -10.479 19.622  0.50 25.18 ? 309 ARG B N     1 
ATOM   11470 C  CA    A ARG B 2 309 ? 30.987  -10.510 20.517  0.50 27.57 ? 309 ARG B CA    1 
ATOM   11471 C  CA    B ARG B 2 309 ? 31.048  -10.350 20.578  0.50 27.58 ? 309 ARG B CA    1 
ATOM   11472 C  C     A ARG B 2 309 ? 29.727  -11.025 19.835  0.50 31.14 ? 309 ARG B C     1 
ATOM   11473 C  C     B ARG B 2 309 ? 29.748  -10.805 19.934  0.50 31.51 ? 309 ARG B C     1 
ATOM   11474 O  O     A ARG B 2 309 ? 29.555  -10.880 18.622  0.50 23.84 ? 309 ARG B O     1 
ATOM   11475 O  O     B ARG B 2 309 ? 29.462  -10.454 18.786  0.50 23.82 ? 309 ARG B O     1 
ATOM   11476 C  CB    A ARG B 2 309 ? 30.729  -9.114  21.099  0.50 31.36 ? 309 ARG B CB    1 
ATOM   11477 C  CB    B ARG B 2 309 ? 30.921  -8.904  21.074  0.50 31.30 ? 309 ARG B CB    1 
ATOM   11478 C  CG    A ARG B 2 309 ? 31.775  -8.643  22.103  0.50 33.90 ? 309 ARG B CG    1 
ATOM   11479 C  CG    B ARG B 2 309 ? 32.040  -8.491  22.020  0.50 33.21 ? 309 ARG B CG    1 
ATOM   11480 C  CD    A ARG B 2 309 ? 31.349  -7.338  22.775  0.50 36.61 ? 309 ARG B CD    1 
ATOM   11481 C  CD    B ARG B 2 309 ? 31.850  -7.084  22.564  0.50 37.20 ? 309 ARG B CD    1 
ATOM   11482 N  NE    A ARG B 2 309 ? 32.317  -6.899  23.774  0.50 38.10 ? 309 ARG B NE    1 
ATOM   11483 N  NE    B ARG B 2 309 ? 32.772  -6.814  23.662  0.50 39.12 ? 309 ARG B NE    1 
ATOM   11484 C  CZ    A ARG B 2 309 ? 32.183  -7.075  25.082  0.50 36.53 ? 309 ARG B CZ    1 
ATOM   11485 C  CZ    B ARG B 2 309 ? 33.012  -5.611  24.165  0.50 39.12 ? 309 ARG B CZ    1 
ATOM   11486 N  NH1   A ARG B 2 309 ? 31.110  -7.655  25.597  0.50 34.09 ? 309 ARG B NH1   1 
ATOM   11487 N  NH1   B ARG B 2 309 ? 32.427  -4.529  23.678  0.50 41.31 ? 309 ARG B NH1   1 
ATOM   11488 N  NH2   A ARG B 2 309 ? 33.150  -6.655  25.894  0.50 38.78 ? 309 ARG B NH2   1 
ATOM   11489 N  NH2   B ARG B 2 309 ? 33.862  -5.490  25.181  0.50 38.81 ? 309 ARG B NH2   1 
ATOM   11490 N  N     A TYR B 2 310 ? 28.845  -11.627 20.629  0.50 29.66 ? 310 TYR B N     1 
ATOM   11491 N  N     B TYR B 2 310 ? 28.973  -11.592 20.682  0.50 29.72 ? 310 TYR B N     1 
ATOM   11492 C  CA    A TYR B 2 310 ? 27.557  -12.096 20.137  0.50 29.93 ? 310 TYR B CA    1 
ATOM   11493 C  CA    B TYR B 2 310 ? 27.667  -12.051 20.226  0.50 30.05 ? 310 TYR B CA    1 
ATOM   11494 C  C     A TYR B 2 310 ? 26.530  -10.977 20.229  0.50 27.25 ? 310 TYR B C     1 
ATOM   11495 C  C     B TYR B 2 310 ? 26.656  -10.920 20.346  0.50 27.68 ? 310 TYR B C     1 
ATOM   11496 O  O     A TYR B 2 310 ? 26.317  -10.409 21.307  0.50 27.28 ? 310 TYR B O     1 
ATOM   11497 O  O     B TYR B 2 310 ? 26.447  -10.378 21.438  0.50 27.02 ? 310 TYR B O     1 
ATOM   11498 C  CB    A TYR B 2 310 ? 27.069  -13.305 20.934  0.50 25.64 ? 310 TYR B CB    1 
ATOM   11499 C  CB    B TYR B 2 310 ? 27.188  -13.246 21.044  0.50 25.78 ? 310 TYR B CB    1 
ATOM   11500 C  CG    A TYR B 2 310 ? 27.800  -14.595 20.653  0.50 31.39 ? 310 TYR B CG    1 
ATOM   11501 C  CG    B TYR B 2 310 ? 27.949  -14.532 20.839  0.50 31.81 ? 310 TYR B CG    1 
ATOM   11502 C  CD1   A TYR B 2 310 ? 27.627  -15.267 19.452  0.50 32.72 ? 310 TYR B CD1   1 
ATOM   11503 C  CD1   B TYR B 2 310 ? 27.723  -15.326 19.724  0.50 32.92 ? 310 TYR B CD1   1 
ATOM   11504 C  CD2   A TYR B 2 310 ? 28.640  -15.159 21.604  0.50 33.92 ? 310 TYR B CD2   1 
ATOM   11505 C  CD2   B TYR B 2 310 ? 28.866  -14.973 21.784  0.50 34.48 ? 310 TYR B CD2   1 
ATOM   11506 C  CE1   A TYR B 2 310 ? 28.288  -16.456 19.200  0.50 32.55 ? 310 TYR B CE1   1 
ATOM   11507 C  CE1   B TYR B 2 310 ? 28.408  -16.511 19.545  0.50 33.11 ? 310 TYR B CE1   1 
ATOM   11508 C  CE2   A TYR B 2 310 ? 29.302  -16.345 21.361  0.50 34.82 ? 310 TYR B CE2   1 
ATOM   11509 C  CE2   B TYR B 2 310 ? 29.553  -16.156 21.614  0.50 35.40 ? 310 TYR B CE2   1 
ATOM   11510 C  CZ    A TYR B 2 310 ? 29.123  -16.989 20.160  0.50 30.09 ? 310 TYR B CZ    1 
ATOM   11511 C  CZ    B TYR B 2 310 ? 29.319  -16.920 20.494  0.50 29.34 ? 310 TYR B CZ    1 
ATOM   11512 O  OH    A TYR B 2 310 ? 29.777  -18.171 19.917  0.50 37.41 ? 310 TYR B OH    1 
ATOM   11513 O  OH    B TYR B 2 310 ? 29.997  -18.099 20.322  0.50 35.80 ? 310 TYR B OH    1 
ATOM   11514 N  N     A LEU B 2 311 ? 25.903  -10.659 19.098  0.50 25.85 ? 311 LEU B N     1 
ATOM   11515 N  N     B LEU B 2 311 ? 26.022  -10.574 19.229  0.50 25.81 ? 311 LEU B N     1 
ATOM   11516 C  CA    A LEU B 2 311 ? 24.765  -9.750  19.112  0.50 25.80 ? 311 LEU B CA    1 
ATOM   11517 C  CA    B LEU B 2 311 ? 24.914  -9.633  19.273  0.50 25.85 ? 311 LEU B CA    1 
ATOM   11518 C  C     A LEU B 2 311 ? 23.504  -10.479 19.556  0.50 28.08 ? 311 LEU B C     1 
ATOM   11519 C  C     B LEU B 2 311 ? 23.646  -10.330 19.745  0.50 28.50 ? 311 LEU B C     1 
ATOM   11520 O  O     A LEU B 2 311 ? 22.798  -10.024 20.463  0.50 28.10 ? 311 LEU B O     1 
ATOM   11521 O  O     B LEU B 2 311 ? 22.950  -9.839  20.641  0.50 27.10 ? 311 LEU B O     1 
ATOM   11522 C  CB    A LEU B 2 311 ? 24.565  -9.133  17.729  0.50 27.20 ? 311 LEU B CB    1 
ATOM   11523 C  CB    B LEU B 2 311 ? 24.704  -9.012  17.894  0.50 27.03 ? 311 LEU B CB    1 
ATOM   11524 C  CG    A LEU B 2 311 ? 25.684  -8.232  17.206  0.50 25.18 ? 311 LEU B CG    1 
ATOM   11525 C  CG    B LEU B 2 311 ? 26.004  -8.724  17.140  0.50 22.17 ? 311 LEU B CG    1 
ATOM   11526 C  CD1   A LEU B 2 311 ? 25.440  -7.881  15.749  0.50 27.13 ? 311 LEU B CD1   1 
ATOM   11527 C  CD1   B LEU B 2 311 ? 25.720  -8.248  15.728  0.50 26.47 ? 311 LEU B CD1   1 
ATOM   11528 C  CD2   A LEU B 2 311 ? 25.767  -6.975  18.056  0.50 20.20 ? 311 LEU B CD2   1 
ATOM   11529 C  CD2   B LEU B 2 311 ? 26.831  -7.705  17.904  0.50 28.22 ? 311 LEU B CD2   1 
ATOM   11530 N  N     A THR B 2 312 ? 23.220  -11.618 18.926  0.50 26.82 ? 312 THR B N     1 
ATOM   11531 N  N     B THR B 2 312 ? 23.354  -11.489 19.157  0.50 26.32 ? 312 THR B N     1 
ATOM   11532 C  CA    A THR B 2 312 ? 22.058  -12.444 19.217  0.50 24.52 ? 312 THR B CA    1 
ATOM   11533 C  CA    B THR B 2 312 ? 22.175  -12.288 19.450  0.50 24.52 ? 312 THR B CA    1 
ATOM   11534 C  C     A THR B 2 312 ? 22.434  -13.898 18.974  0.50 27.68 ? 312 THR B C     1 
ATOM   11535 C  C     B THR B 2 312 ? 22.555  -13.753 19.292  0.50 26.91 ? 312 THR B C     1 
ATOM   11536 O  O     A THR B 2 312 ? 23.305  -14.197 18.149  0.50 27.71 ? 312 THR B O     1 
ATOM   11537 O  O     B THR B 2 312 ? 23.434  -14.094 18.492  0.50 28.21 ? 312 THR B O     1 
ATOM   11538 C  CB    A THR B 2 312 ? 20.852  -12.075 18.342  0.50 26.77 ? 312 THR B CB    1 
ATOM   11539 C  CB    B THR B 2 312 ? 21.012  -11.945 18.510  0.50 26.73 ? 312 THR B CB    1 
ATOM   11540 O  OG1   A THR B 2 312 ? 21.247  -12.074 16.963  0.50 25.75 ? 312 THR B OG1   1 
ATOM   11541 O  OG1   B THR B 2 312 ? 21.460  -12.044 17.151  0.50 25.41 ? 312 THR B OG1   1 
ATOM   11542 C  CG2   A THR B 2 312 ? 20.290  -10.705 18.715  0.50 26.42 ? 312 THR B CG2   1 
ATOM   11543 C  CG2   B THR B 2 312 ? 20.490  -10.533 18.768  0.50 25.84 ? 312 THR B CG2   1 
ATOM   11544 N  N     A VAL B 2 313 ? 21.774  -14.798 19.700  0.50 25.40 ? 313 VAL B N     1 
ATOM   11545 N  N     B VAL B 2 313 ? 21.899  -14.616 20.066  0.50 25.17 ? 313 VAL B N     1 
ATOM   11546 C  CA    A VAL B 2 313 ? 21.981  -16.236 19.562  0.50 24.78 ? 313 VAL B CA    1 
ATOM   11547 C  CA    B VAL B 2 313 ? 22.158  -16.053 20.034  0.50 26.24 ? 313 VAL B CA    1 
ATOM   11548 C  C     A VAL B 2 313 ? 20.636  -16.935 19.716  0.50 25.71 ? 313 VAL B C     1 
ATOM   11549 C  C     B VAL B 2 313 ? 20.831  -16.793 20.134  0.50 27.82 ? 313 VAL B C     1 
ATOM   11550 O  O     A VAL B 2 313 ? 19.808  -16.532 20.540  0.50 28.18 ? 313 VAL B O     1 
ATOM   11551 O  O     B VAL B 2 313 ? 19.955  -16.414 20.917  0.50 28.71 ? 313 VAL B O     1 
ATOM   11552 C  CB    A VAL B 2 313 ? 22.997  -16.776 20.597  0.50 30.52 ? 313 VAL B CB    1 
ATOM   11553 C  CB    B VAL B 2 313 ? 23.110  -16.492 21.171  0.50 31.68 ? 313 VAL B CB    1 
ATOM   11554 C  CG1   A VAL B 2 313 ? 23.059  -18.295 20.559  0.50 30.19 ? 313 VAL B CG1   1 
ATOM   11555 C  CG1   B VAL B 2 313 ? 23.266  -18.006 21.194  0.50 27.10 ? 313 VAL B CG1   1 
ATOM   11556 C  CG2   A VAL B 2 313 ? 24.378  -16.197 20.362  0.50 27.81 ? 313 VAL B CG2   1 
ATOM   11557 C  CG2   B VAL B 2 313 ? 24.471  -15.828 21.033  0.50 29.28 ? 313 VAL B CG2   1 
ATOM   11558 N  N     A ALA B 2 314 ? 20.411  -17.967 18.906  0.50 26.50 ? 314 ALA B N     1 
ATOM   11559 N  N     B ALA B 2 314 ? 20.681  -17.844 19.332  0.50 26.43 ? 314 ALA B N     1 
ATOM   11560 C  CA    A ALA B 2 314 ? 19.294  -18.887 19.081  0.50 25.31 ? 314 ALA B CA    1 
ATOM   11561 C  CA    B ALA B 2 314 ? 19.579  -18.786 19.461  0.50 26.86 ? 314 ALA B CA    1 
ATOM   11562 C  C     A ALA B 2 314 ? 19.840  -20.305 19.056  0.50 31.42 ? 314 ALA B C     1 
ATOM   11563 C  C     B ALA B 2 314 ? 20.141  -20.197 19.536  0.50 33.20 ? 314 ALA B C     1 
ATOM   11564 O  O     A ALA B 2 314 ? 20.530  -20.691 18.106  0.50 29.05 ? 314 ALA B O     1 
ATOM   11565 O  O     B ALA B 2 314 ? 21.145  -20.515 18.889  0.50 26.53 ? 314 ALA B O     1 
ATOM   11566 C  CB    A ALA B 2 314 ? 18.231  -18.701 17.996  0.50 27.48 ? 314 ALA B CB    1 
ATOM   11567 C  CB    B ALA B 2 314 ? 18.589  -18.676 18.298  0.50 27.15 ? 314 ALA B CB    1 
ATOM   11568 N  N     A ALA B 2 315 ? 19.548  -21.072 20.104  0.50 28.18 ? 315 ALA B N     1 
ATOM   11569 N  N     B ALA B 2 315 ? 19.496  -21.036 20.339  0.50 27.79 ? 315 ALA B N     1 
ATOM   11570 C  CA    A ALA B 2 315 ? 20.065  -22.426 20.250  0.50 31.58 ? 315 ALA B CA    1 
ATOM   11571 C  CA    B ALA B 2 315 ? 19.878  -22.430 20.480  0.50 32.02 ? 315 ALA B CA    1 
ATOM   11572 C  C     A ALA B 2 315 ? 18.904  -23.383 20.463  0.50 37.41 ? 315 ALA B C     1 
ATOM   11573 C  C     B ALA B 2 315 ? 18.650  -23.306 20.289  0.50 37.56 ? 315 ALA B C     1 
ATOM   11574 O  O     A ALA B 2 315 ? 18.040  -23.139 21.311  0.50 34.73 ? 315 ALA B O     1 
ATOM   11575 O  O     B ALA B 2 315 ? 17.531  -22.920 20.638  0.50 34.59 ? 315 ALA B O     1 
ATOM   11576 C  CB    A ALA B 2 315 ? 21.054  -22.523 21.416  0.50 35.80 ? 315 ALA B CB    1 
ATOM   11577 C  CB    B ALA B 2 315 ? 20.516  -22.705 21.849  0.50 33.64 ? 315 ALA B CB    1 
ATOM   11578 N  N     A ILE B 2 316 ? 18.890  -24.468 19.698  0.50 36.01 ? 316 ILE B N     1 
ATOM   11579 N  N     B ILE B 2 316 ? 18.870  -24.488 19.720  0.50 36.02 ? 316 ILE B N     1 
ATOM   11580 C  CA    A ILE B 2 316 ? 17.823  -25.459 19.749  0.50 36.88 ? 316 ILE B CA    1 
ATOM   11581 C  CA    B ILE B 2 316 ? 17.817  -25.475 19.503  0.50 37.42 ? 316 ILE B CA    1 
ATOM   11582 C  C     A ILE B 2 316 ? 18.431  -26.803 20.123  0.50 42.05 ? 316 ILE B C     1 
ATOM   11583 C  C     B ILE B 2 316 ? 18.337  -26.798 20.051  0.50 42.02 ? 316 ILE B C     1 
ATOM   11584 O  O     A ILE B 2 316 ? 19.469  -27.198 19.577  0.50 40.60 ? 316 ILE B O     1 
ATOM   11585 O  O     B ILE B 2 316 ? 19.134  -27.481 19.397  0.50 42.03 ? 316 ILE B O     1 
ATOM   11586 C  CB    A ILE B 2 316 ? 17.063  -25.537 18.410  0.50 42.53 ? 316 ILE B CB    1 
ATOM   11587 C  CB    B ILE B 2 316 ? 17.420  -25.600 18.027  0.50 40.58 ? 316 ILE B CB    1 
ATOM   11588 C  CG1   A ILE B 2 316 ? 16.092  -26.722 18.400  0.50 39.47 ? 316 ILE B CG1   1 
ATOM   11589 C  CG1   B ILE B 2 316 ? 16.876  -24.267 17.504  0.50 32.53 ? 316 ILE B CG1   1 
ATOM   11590 C  CG2   A ILE B 2 316 ? 18.041  -25.585 17.239  0.50 36.18 ? 316 ILE B CG2   1 
ATOM   11591 C  CG2   B ILE B 2 316 ? 16.384  -26.694 17.850  0.50 41.11 ? 316 ILE B CG2   1 
ATOM   11592 C  CD1   A ILE B 2 316 ? 16.509  -27.849 17.482  0.50 45.66 ? 316 ILE B CD1   1 
ATOM   11593 C  CD1   B ILE B 2 316 ? 16.523  -24.283 16.033  0.50 42.16 ? 316 ILE B CD1   1 
ATOM   11594 N  N     A PHE B 2 317 ? 17.797  -27.490 21.065  0.50 38.11 ? 317 PHE B N     1 
ATOM   11595 N  N     B PHE B 2 317 ? 17.908  -27.152 21.259  0.50 38.24 ? 317 PHE B N     1 
ATOM   11596 C  CA    A PHE B 2 317 ? 18.169  -28.838 21.461  0.50 39.42 ? 317 PHE B CA    1 
ATOM   11597 C  CA    B PHE B 2 317 ? 18.246  -28.431 21.866  0.50 39.49 ? 317 PHE B CA    1 
ATOM   11598 C  C     A PHE B 2 317 ? 17.122  -29.821 20.954  0.50 40.80 ? 317 PHE B C     1 
ATOM   11599 C  C     B PHE B 2 317 ? 17.194  -29.461 21.477  0.50 40.05 ? 317 PHE B C     1 
ATOM   11600 O  O     A PHE B 2 317 ? 15.964  -29.463 20.725  0.50 45.13 ? 317 PHE B O     1 
ATOM   11601 O  O     B PHE B 2 317 ? 15.997  -29.242 21.690  0.50 43.79 ? 317 PHE B O     1 
ATOM   11602 C  CB    A PHE B 2 317 ? 18.300  -28.954 22.984  0.50 40.14 ? 317 PHE B CB    1 
ATOM   11603 C  CB    B PHE B 2 317 ? 18.318  -28.312 23.389  0.50 41.17 ? 317 PHE B CB    1 
ATOM   11604 C  CG    A PHE B 2 317 ? 19.336  -28.045 23.581  0.50 39.66 ? 317 PHE B CG    1 
ATOM   11605 C  CG    B PHE B 2 317 ? 19.366  -27.353 23.882  0.50 41.97 ? 317 PHE B CG    1 
ATOM   11606 C  CD1   A PHE B 2 317 ? 19.059  -26.705 23.806  0.50 40.09 ? 317 PHE B CD1   1 
ATOM   11607 C  CD1   B PHE B 2 317 ? 19.120  -25.990 23.912  0.50 40.14 ? 317 PHE B CD1   1 
ATOM   11608 C  CD2   A PHE B 2 317 ? 20.581  -28.536 23.941  0.50 33.48 ? 317 PHE B CD2   1 
ATOM   11609 C  CD2   B PHE B 2 317 ? 20.589  -27.818 24.339  0.50 42.08 ? 317 PHE B CD2   1 
ATOM   11610 C  CE1   A PHE B 2 317 ? 20.010  -25.866 24.361  0.50 40.23 ? 317 PHE B CE1   1 
ATOM   11611 C  CE1   B PHE B 2 317 ? 20.079  -25.108 24.374  0.50 38.63 ? 317 PHE B CE1   1 
ATOM   11612 C  CE2   A PHE B 2 317 ? 21.534  -27.702 24.503  0.50 40.14 ? 317 PHE B CE2   1 
ATOM   11613 C  CE2   B PHE B 2 317 ? 21.549  -26.940 24.806  0.50 39.60 ? 317 PHE B CE2   1 
ATOM   11614 C  CZ    A PHE B 2 317 ? 21.246  -26.366 24.715  0.50 39.51 ? 317 PHE B CZ    1 
ATOM   11615 C  CZ    B PHE B 2 317 ? 21.293  -25.584 24.822  0.50 40.21 ? 317 PHE B CZ    1 
ATOM   11616 N  N     A ARG B 2 318 ? 17.541  -31.070 20.775  0.50 42.27 ? 318 ARG B N     1 
ATOM   11617 N  N     B ARG B 2 318 ? 17.639  -30.582 20.918  0.50 41.68 ? 318 ARG B N     1 
ATOM   11618 C  CA    A ARG B 2 318 ? 16.649  -32.116 20.297  0.50 45.34 ? 318 ARG B CA    1 
ATOM   11619 C  CA    B ARG B 2 318 ? 16.743  -31.613 20.412  0.50 44.02 ? 318 ARG B CA    1 
ATOM   11620 C  C     A ARG B 2 318 ? 16.889  -33.388 21.092  0.50 43.55 ? 318 ARG B C     1 
ATOM   11621 C  C     B ARG B 2 318 ? 16.937  -32.898 21.204  0.50 42.94 ? 318 ARG B C     1 
ATOM   11622 O  O     A ARG B 2 318 ? 18.032  -33.725 21.411  0.50 39.71 ? 318 ARG B O     1 
ATOM   11623 O  O     B ARG B 2 318 ? 18.074  -33.317 21.445  0.50 40.10 ? 318 ARG B O     1 
ATOM   11624 C  CB    A ARG B 2 318 ? 16.842  -32.378 18.796  0.50 43.83 ? 318 ARG B CB    1 
ATOM   11625 C  CB    B ARG B 2 318 ? 16.989  -31.869 18.922  0.50 42.45 ? 318 ARG B CB    1 
ATOM   11626 C  CG    A ARG B 2 318 ? 16.201  -31.330 17.902  0.50 41.93 ? 318 ARG B CG    1 
ATOM   11627 C  CG    B ARG B 2 318 ? 16.880  -30.631 18.049  0.50 35.06 ? 318 ARG B CG    1 
ATOM   11628 C  CD    A ARG B 2 318 ? 16.821  -31.301 16.511  0.50 41.79 ? 318 ARG B CD    1 
ATOM   11629 C  CD    B ARG B 2 318 ? 16.828  -31.014 16.580  0.50 42.05 ? 318 ARG B CD    1 
ATOM   11630 N  NE    A ARG B 2 318 ? 16.556  -32.514 15.748  0.50 43.99 ? 318 ARG B NE    1 
ATOM   11631 N  NE    B ARG B 2 318 ? 15.700  -31.894 16.300  0.50 36.91 ? 318 ARG B NE    1 
ATOM   11632 C  CZ    A ARG B 2 318 ? 15.571  -32.651 14.872  0.50 44.57 ? 318 ARG B CZ    1 
ATOM   11633 C  CZ    B ARG B 2 318 ? 15.452  -32.450 15.122  0.50 44.74 ? 318 ARG B CZ    1 
ATOM   11634 N  NH1   A ARG B 2 318 ? 14.722  -31.667 14.629  0.50 48.26 ? 318 ARG B NH1   1 
ATOM   11635 N  NH1   B ARG B 2 318 ? 16.230  -32.229 14.076  0.50 41.84 ? 318 ARG B NH1   1 
ATOM   11636 N  NH2   A ARG B 2 318 ? 15.435  -33.804 14.224  0.50 38.17 ? 318 ARG B NH2   1 
ATOM   11637 N  NH2   B ARG B 2 318 ? 14.397  -33.250 14.992  0.50 44.84 ? 318 ARG B NH2   1 
ATOM   11638 N  N     A GLY B 2 319 ? 15.802  -34.088 21.412  0.50 45.67 ? 319 GLY B N     1 
ATOM   11639 N  N     B GLY B 2 319 ? 15.832  -33.516 21.604  0.50 44.72 ? 319 GLY B N     1 
ATOM   11640 C  CA    A GLY B 2 319 ? 15.886  -35.302 22.198  0.50 44.29 ? 319 GLY B CA    1 
ATOM   11641 C  CA    B GLY B 2 319 ? 15.852  -34.789 22.297  0.50 44.68 ? 319 GLY B CA    1 
ATOM   11642 C  C     A GLY B 2 319 ? 15.129  -35.206 23.507  0.50 48.85 ? 319 GLY B C     1 
ATOM   11643 C  C     B GLY B 2 319 ? 15.118  -34.724 23.621  0.50 49.29 ? 319 GLY B C     1 
ATOM   11644 O  O     A GLY B 2 319 ? 14.281  -34.324 23.677  0.50 48.41 ? 319 GLY B O     1 
ATOM   11645 O  O     B GLY B 2 319 ? 14.408  -33.762 23.931  0.50 46.21 ? 319 GLY B O     1 
ATOM   11646 N  N     A ARG B 2 320 ? 15.426  -36.107 24.440  0.50 48.30 ? 320 ARG B N     1 
ATOM   11647 N  N     B ARG B 2 320 ? 15.300  -35.779 24.414  0.50 48.20 ? 320 ARG B N     1 
ATOM   11648 C  CA    A ARG B 2 320 ? 14.778  -36.144 25.745  0.50 50.36 ? 320 ARG B CA    1 
ATOM   11649 C  CA    B ARG B 2 320 ? 14.663  -35.914 25.717  0.50 50.20 ? 320 ARG B CA    1 
ATOM   11650 C  C     A ARG B 2 320 ? 15.762  -35.658 26.799  0.50 49.88 ? 320 ARG B C     1 
ATOM   11651 C  C     B ARG B 2 320 ? 15.657  -35.497 26.794  0.50 49.86 ? 320 ARG B C     1 
ATOM   11652 O  O     A ARG B 2 320 ? 16.815  -36.273 27.002  0.50 49.92 ? 320 ARG B O     1 
ATOM   11653 O  O     B ARG B 2 320 ? 16.707  -36.130 26.955  0.50 50.04 ? 320 ARG B O     1 
ATOM   11654 C  CB    A ARG B 2 320 ? 14.287  -37.553 26.078  0.50 48.12 ? 320 ARG B CB    1 
ATOM   11655 C  CB    B ARG B 2 320 ? 14.182  -37.349 25.941  0.50 48.10 ? 320 ARG B CB    1 
ATOM   11656 C  CG    A ARG B 2 320 ? 13.129  -38.036 25.222  0.50 50.25 ? 320 ARG B CG    1 
ATOM   11657 C  CG    B ARG B 2 320 ? 13.417  -37.563 27.236  0.50 55.98 ? 320 ARG B CG    1 
ATOM   11658 C  CD    A ARG B 2 320 ? 11.935  -37.100 25.324  0.50 53.91 ? 320 ARG B CD    1 
ATOM   11659 C  CD    B ARG B 2 320 ? 12.841  -38.974 27.300  0.50 60.92 ? 320 ARG B CD    1 
ATOM   11660 N  NE    A ARG B 2 320 ? 10.702  -37.743 24.884  0.50 53.98 ? 320 ARG B NE    1 
ATOM   11661 N  NE    B ARG B 2 320 ? 11.814  -39.194 26.287  0.50 59.02 ? 320 ARG B NE    1 
ATOM   11662 C  CZ    A ARG B 2 320 ? 10.296  -37.808 23.623  0.50 55.26 ? 320 ARG B CZ    1 
ATOM   11663 C  CZ    B ARG B 2 320 ? 10.509  -39.128 26.517  0.50 60.04 ? 320 ARG B CZ    1 
ATOM   11664 N  NH1   A ARG B 2 320 ? 11.003  -37.275 22.641  0.50 49.78 ? 320 ARG B NH1   1 
ATOM   11665 N  NH1   B ARG B 2 320 ? 10.032  -38.870 27.724  0.50 61.72 ? 320 ARG B NH1   1 
ATOM   11666 N  NH2   A ARG B 2 320 ? 9.153   -38.428 23.342  0.50 54.25 ? 320 ARG B NH2   1 
ATOM   11667 N  NH2   B ARG B 2 320 ? 9.662   -39.329 25.512  0.50 56.02 ? 320 ARG B NH2   1 
ATOM   11668 N  N     A MET B 2 321 ? 15.414  -34.562 27.468  0.50 47.70 ? 321 MET B N     1 
ATOM   11669 N  N     B MET B 2 321 ? 15.324  -34.437 27.528  0.50 47.62 ? 321 MET B N     1 
ATOM   11670 C  CA    A MET B 2 321 ? 16.265  -33.981 28.496  0.50 46.99 ? 321 MET B CA    1 
ATOM   11671 C  CA    B MET B 2 321 ? 16.265  -33.833 28.460  0.50 47.11 ? 321 MET B CA    1 
ATOM   11672 C  C     A MET B 2 321 ? 15.437  -32.989 29.297  0.50 52.91 ? 321 MET B C     1 
ATOM   11673 C  C     B MET B 2 321 ? 15.501  -32.968 29.449  0.50 52.90 ? 321 MET B C     1 
ATOM   11674 O  O     A MET B 2 321 ? 14.429  -32.463 28.815  0.50 52.96 ? 321 MET B O     1 
ATOM   11675 O  O     B MET B 2 321 ? 14.394  -32.499 29.169  0.50 53.65 ? 321 MET B O     1 
ATOM   11676 C  CB    A MET B 2 321 ? 17.497  -33.298 27.891  0.50 51.71 ? 321 MET B CB    1 
ATOM   11677 C  CB    B MET B 2 321 ? 17.312  -32.994 27.720  0.50 50.95 ? 321 MET B CB    1 
ATOM   11678 C  CG    A MET B 2 321 ? 17.189  -32.032 27.108  0.50 48.77 ? 321 MET B CG    1 
ATOM   11679 C  CG    B MET B 2 321 ? 16.730  -31.757 27.050  0.50 45.87 ? 321 MET B CG    1 
ATOM   11680 S  SD    A MET B 2 321 ? 18.538  -31.543 26.012  0.50 42.31 ? 321 MET B SD    1 
ATOM   11681 S  SD    B MET B 2 321 ? 17.805  -31.046 25.788  0.50 52.59 ? 321 MET B SD    1 
ATOM   11682 C  CE    A MET B 2 321 ? 18.168  -32.524 24.560  0.50 38.37 ? 321 MET B CE    1 
ATOM   11683 C  CE    B MET B 2 321 ? 17.751  -32.326 24.541  0.50 37.58 ? 321 MET B CE    1 
ATOM   11684 N  N     A SER B 2 322 ? 15.875  -32.745 30.529  0.50 56.46 ? 322 SER B N     1 
ATOM   11685 N  N     B SER B 2 322 ? 16.115  -32.756 30.611  0.50 56.80 ? 322 SER B N     1 
ATOM   11686 C  CA    A SER B 2 322 ? 15.182  -31.819 31.420  0.50 55.80 ? 322 SER B CA    1 
ATOM   11687 C  CA    B SER B 2 322 ? 15.544  -31.871 31.618  0.50 56.02 ? 322 SER B CA    1 
ATOM   11688 C  C     A SER B 2 322 ? 15.278  -30.406 30.859  0.50 57.19 ? 322 SER B C     1 
ATOM   11689 C  C     B SER B 2 322 ? 15.574  -30.433 31.116  0.50 57.30 ? 322 SER B C     1 
ATOM   11690 O  O     A SER B 2 322 ? 16.372  -29.837 30.771  0.50 57.33 ? 322 SER B O     1 
ATOM   11691 O  O     B SER B 2 322 ? 16.641  -29.907 30.782  0.50 57.05 ? 322 SER B O     1 
ATOM   11692 C  CB    A SER B 2 322 ? 15.778  -31.892 32.823  0.50 57.39 ? 322 SER B CB    1 
ATOM   11693 C  CB    B SER B 2 322 ? 16.312  -31.997 32.932  0.50 58.13 ? 322 SER B CB    1 
ATOM   11694 O  OG    A SER B 2 322 ? 15.185  -30.933 33.682  0.50 57.58 ? 322 SER B OG    1 
ATOM   11695 O  OG    B SER B 2 322 ? 15.906  -31.006 33.859  0.50 58.37 ? 322 SER B OG    1 
ATOM   11696 N  N     A MET B 2 323 ? 14.132  -29.836 30.476  0.50 54.35 ? 323 MET B N     1 
ATOM   11697 N  N     B MET B 2 323 ? 14.400  -29.800 31.057  0.50 53.96 ? 323 MET B N     1 
ATOM   11698 C  CA    A MET B 2 323 ? 14.123  -28.461 29.988  0.50 56.54 ? 323 MET B CA    1 
ATOM   11699 C  CA    B MET B 2 323 ? 14.334  -28.409 30.621  0.50 56.92 ? 323 MET B CA    1 
ATOM   11700 C  C     A MET B 2 323 ? 14.570  -27.486 31.068  0.50 59.34 ? 323 MET B C     1 
ATOM   11701 C  C     B MET B 2 323 ? 15.132  -27.509 31.554  0.50 59.79 ? 323 MET B C     1 
ATOM   11702 O  O     A MET B 2 323 ? 15.062  -26.395 30.754  0.50 58.50 ? 323 MET B O     1 
ATOM   11703 O  O     B MET B 2 323 ? 15.903  -26.653 31.103  0.50 57.42 ? 323 MET B O     1 
ATOM   11704 C  CB    A MET B 2 323 ? 12.729  -28.090 29.482  0.50 59.24 ? 323 MET B CB    1 
ATOM   11705 C  CB    B MET B 2 323 ? 12.879  -27.948 30.552  0.50 58.62 ? 323 MET B CB    1 
ATOM   11706 C  CG    A MET B 2 323 ? 12.141  -29.072 28.483  0.50 58.48 ? 323 MET B CG    1 
ATOM   11707 C  CG    B MET B 2 323 ? 12.690  -26.591 29.893  0.50 59.63 ? 323 MET B CG    1 
ATOM   11708 S  SD    A MET B 2 323 ? 10.509  -28.562 27.908  0.50 60.99 ? 323 MET B SD    1 
ATOM   11709 S  SD    B MET B 2 323 ? 12.499  -26.731 28.107  0.50 65.81 ? 323 MET B SD    1 
ATOM   11710 C  CE    A MET B 2 323 ? 10.016  -30.000 26.959  0.50 57.51 ? 323 MET B CE    1 
ATOM   11711 C  CE    B MET B 2 323 ? 10.949  -27.625 28.025  0.50 58.60 ? 323 MET B CE    1 
ATOM   11712 N  N     A LYS B 2 324 ? 14.406  -27.856 32.341  0.50 55.56 ? 324 LYS B N     1 
ATOM   11713 N  N     B LYS B 2 324 ? 14.961  -27.694 32.867  0.50 55.38 ? 324 LYS B N     1 
ATOM   11714 C  CA    A LYS B 2 324 ? 14.897  -27.014 33.426  0.50 55.92 ? 324 LYS B CA    1 
ATOM   11715 C  CA    B LYS B 2 324 ? 15.663  -26.854 33.831  0.50 57.27 ? 324 LYS B CA    1 
ATOM   11716 C  C     A LYS B 2 324 ? 16.420  -26.996 33.463  0.50 53.92 ? 324 LYS B C     1 
ATOM   11717 C  C     B LYS B 2 324 ? 17.172  -27.039 33.743  0.50 54.99 ? 324 LYS B C     1 
ATOM   11718 O  O     A LYS B 2 324 ? 17.028  -25.948 33.708  0.50 51.73 ? 324 LYS B O     1 
ATOM   11719 O  O     B LYS B 2 324 ? 17.926  -26.088 33.973  0.50 53.94 ? 324 LYS B O     1 
ATOM   11720 C  CB    A LYS B 2 324 ? 14.333  -27.492 34.764  0.50 55.82 ? 324 LYS B CB    1 
ATOM   11721 C  CB    B LYS B 2 324 ? 15.168  -27.155 35.247  0.50 56.70 ? 324 LYS B CB    1 
ATOM   11722 C  CG    A LYS B 2 324 ? 14.890  -26.752 35.971  0.50 53.90 ? 324 LYS B CG    1 
ATOM   11723 C  CG    B LYS B 2 324 ? 15.672  -26.183 36.302  0.50 54.37 ? 324 LYS B CG    1 
ATOM   11724 C  CD    A LYS B 2 324 ? 14.274  -27.252 37.268  0.50 55.79 ? 324 LYS B CD    1 
ATOM   11725 C  CD    B LYS B 2 324 ? 15.175  -26.564 37.685  0.50 60.02 ? 324 LYS B CD    1 
ATOM   11726 C  CE    A LYS B 2 324 ? 14.914  -26.582 38.477  0.50 58.21 ? 324 LYS B CE    1 
ATOM   11727 C  CE    B LYS B 2 324 ? 15.639  -25.566 38.733  0.50 58.54 ? 324 LYS B CE    1 
ATOM   11728 N  NZ    A LYS B 2 324 ? 14.832  -25.096 38.407  0.50 56.02 ? 324 LYS B NZ    1 
ATOM   11729 N  NZ    B LYS B 2 324 ? 15.161  -25.933 40.095  0.50 56.78 ? 324 LYS B NZ    1 
ATOM   11730 N  N     A GLU B 2 325 ? 17.054  -28.147 33.224  0.50 55.53 ? 325 GLU B N     1 
ATOM   11731 N  N     B GLU B 2 325 ? 17.632  -28.249 33.412  0.50 56.13 ? 325 GLU B N     1 
ATOM   11732 C  CA    A GLU B 2 325 ? 18.512  -28.196 33.222  0.50 58.39 ? 325 GLU B CA    1 
ATOM   11733 C  CA    B GLU B 2 325 ? 19.065  -28.463 33.242  0.50 59.39 ? 325 GLU B CA    1 
ATOM   11734 C  C     A GLU B 2 325 ? 19.086  -27.372 32.075  0.50 56.35 ? 325 GLU B C     1 
ATOM   11735 C  C     B GLU B 2 325 ? 19.591  -27.699 32.033  0.50 56.58 ? 325 GLU B C     1 
ATOM   11736 O  O     A GLU B 2 325 ? 20.107  -26.694 32.240  0.50 55.00 ? 325 GLU B O     1 
ATOM   11737 O  O     B GLU B 2 325 ? 20.714  -27.182 32.058  0.50 56.62 ? 325 GLU B O     1 
ATOM   11738 C  CB    A GLU B 2 325 ? 18.990  -29.645 33.138  0.50 58.17 ? 325 GLU B CB    1 
ATOM   11739 C  CB    B GLU B 2 325 ? 19.365  -29.956 33.106  0.50 57.35 ? 325 GLU B CB    1 
ATOM   11740 C  CG    A GLU B 2 325 ? 20.486  -29.818 33.345  0.50 55.93 ? 325 GLU B CG    1 
ATOM   11741 C  CG    B GLU B 2 325 ? 20.836  -30.307 33.265  0.50 56.60 ? 325 GLU B CG    1 
ATOM   11742 C  CD    A GLU B 2 325 ? 20.925  -31.265 33.255  0.50 59.14 ? 325 GLU B CD    1 
ATOM   11743 C  CD    B GLU B 2 325 ? 21.121  -31.772 32.993  0.50 61.16 ? 325 GLU B CD    1 
ATOM   11744 O  OE1   A GLU B 2 325 ? 20.055  -32.142 33.068  0.50 63.85 ? 325 GLU B OE1   1 
ATOM   11745 O  OE1   B GLU B 2 325 ? 20.388  -32.382 32.186  0.50 60.05 ? 325 GLU B OE1   1 
ATOM   11746 O  OE2   A GLU B 2 325 ? 22.140  -31.527 33.370  0.50 61.99 ? 325 GLU B OE2   1 
ATOM   11747 O  OE2   B GLU B 2 325 ? 22.076  -32.314 33.588  0.50 63.49 ? 325 GLU B OE2   1 
ATOM   11748 N  N     A VAL B 2 326 ? 18.439  -27.419 30.908  0.50 55.39 ? 326 VAL B N     1 
ATOM   11749 N  N     B VAL B 2 326 ? 18.792  -27.617 30.967  0.50 56.25 ? 326 VAL B N     1 
ATOM   11750 C  CA    A VAL B 2 326 ? 18.872  -26.604 29.776  0.50 52.53 ? 326 VAL B CA    1 
ATOM   11751 C  CA    B VAL B 2 326 ? 19.164  -26.790 29.823  0.50 52.07 ? 326 VAL B CA    1 
ATOM   11752 C  C     A VAL B 2 326 ? 18.880  -25.129 30.155  0.50 54.59 ? 326 VAL B C     1 
ATOM   11753 C  C     B VAL B 2 326 ? 19.259  -25.329 30.243  0.50 53.14 ? 326 VAL B C     1 
ATOM   11754 O  O     A VAL B 2 326 ? 19.822  -24.395 29.832  0.50 53.06 ? 326 VAL B O     1 
ATOM   11755 O  O     B VAL B 2 326 ? 20.219  -24.627 29.905  0.50 52.40 ? 326 VAL B O     1 
ATOM   11756 C  CB    A VAL B 2 326 ? 17.972  -26.871 28.555  0.50 52.43 ? 326 VAL B CB    1 
ATOM   11757 C  CB    B VAL B 2 326 ? 18.162  -26.982 28.671  0.50 52.62 ? 326 VAL B CB    1 
ATOM   11758 C  CG1   A VAL B 2 326 ? 18.288  -25.895 27.435  0.50 49.90 ? 326 VAL B CG1   1 
ATOM   11759 C  CG1   B VAL B 2 326 ? 18.516  -26.077 27.502  0.50 49.98 ? 326 VAL B CG1   1 
ATOM   11760 C  CG2   A VAL B 2 326 ? 18.135  -28.307 28.078  0.50 50.90 ? 326 VAL B CG2   1 
ATOM   11761 C  CG2   B VAL B 2 326 ? 18.133  -28.436 28.232  0.50 51.09 ? 326 VAL B CG2   1 
ATOM   11762 N  N     A ASP B 2 327 ? 17.836  -24.676 30.856  0.50 54.33 ? 327 ASP B N     1 
ATOM   11763 N  N     B ASP B 2 327 ? 18.265  -24.854 31.000  0.50 55.24 ? 327 ASP B N     1 
ATOM   11764 C  CA    A ASP B 2 327 ? 17.773  -23.282 31.285  0.50 52.78 ? 327 ASP B CA    1 
ATOM   11765 C  CA    B ASP B 2 327 ? 18.285  -23.471 31.466  0.50 52.92 ? 327 ASP B CA    1 
ATOM   11766 C  C     A ASP B 2 327 ? 18.942  -22.929 32.195  0.50 52.93 ? 327 ASP B C     1 
ATOM   11767 C  C     B ASP B 2 327 ? 19.443  -23.227 32.423  0.50 52.37 ? 327 ASP B C     1 
ATOM   11768 O  O     A ASP B 2 327 ? 19.542  -21.856 32.061  0.50 49.02 ? 327 ASP B O     1 
ATOM   11769 O  O     B ASP B 2 327 ? 20.071  -22.162 32.392  0.50 46.47 ? 327 ASP B O     1 
ATOM   11770 C  CB    A ASP B 2 327 ? 16.447  -23.012 31.997  0.50 54.27 ? 327 ASP B CB    1 
ATOM   11771 C  CB    B ASP B 2 327 ? 16.955  -23.119 32.134  0.50 54.33 ? 327 ASP B CB    1 
ATOM   11772 C  CG    A ASP B 2 327 ? 15.252  -23.119 31.070  0.50 53.33 ? 327 ASP B CG    1 
ATOM   11773 C  CG    B ASP B 2 327 ? 15.815  -23.005 31.141  0.50 54.14 ? 327 ASP B CG    1 
ATOM   11774 O  OD1   A ASP B 2 327 ? 15.455  -23.282 29.847  0.50 53.52 ? 327 ASP B OD1   1 
ATOM   11775 O  OD1   B ASP B 2 327 ? 16.015  -23.350 29.956  0.50 54.22 ? 327 ASP B OD1   1 
ATOM   11776 O  OD2   A ASP B 2 327 ? 14.108  -23.044 31.568  0.50 54.46 ? 327 ASP B OD2   1 
ATOM   11777 O  OD2   B ASP B 2 327 ? 14.719  -22.563 31.545  0.50 50.00 ? 327 ASP B OD2   1 
ATOM   11778 N  N     A GLU B 2 328 ? 19.282  -23.821 33.128  0.50 53.54 ? 328 GLU B N     1 
ATOM   11779 N  N     B GLU B 2 328 ? 19.742  -24.201 33.285  0.50 53.13 ? 328 GLU B N     1 
ATOM   11780 C  CA    A GLU B 2 328 ? 20.370  -23.535 34.056  0.50 52.52 ? 328 GLU B CA    1 
ATOM   11781 C  CA    B GLU B 2 328 ? 20.868  -24.054 34.201  0.50 53.88 ? 328 GLU B CA    1 
ATOM   11782 C  C     A GLU B 2 328 ? 21.718  -23.528 33.346  0.50 52.65 ? 328 GLU B C     1 
ATOM   11783 C  C     B GLU B 2 328 ? 22.190  -24.035 33.443  0.50 54.27 ? 328 GLU B C     1 
ATOM   11784 O  O     A GLU B 2 328 ? 22.570  -22.677 33.629  0.50 48.95 ? 328 GLU B O     1 
ATOM   11785 O  O     B GLU B 2 328 ? 23.045  -23.176 33.689  0.50 49.23 ? 328 GLU B O     1 
ATOM   11786 C  CB    A GLU B 2 328 ? 20.364  -24.551 35.197  0.50 57.27 ? 328 GLU B CB    1 
ATOM   11787 C  CB    B GLU B 2 328 ? 20.859  -25.177 35.238  0.50 56.80 ? 328 GLU B CB    1 
ATOM   11788 C  CG    A GLU B 2 328 ? 19.196  -24.387 36.158  0.50 56.72 ? 328 GLU B CG    1 
ATOM   11789 C  CG    B GLU B 2 328 ? 19.801  -25.029 36.318  0.50 58.64 ? 328 GLU B CG    1 
ATOM   11790 C  CD    A GLU B 2 328 ? 19.167  -25.455 37.232  0.50 62.74 ? 328 GLU B CD    1 
ATOM   11791 C  CD    B GLU B 2 328 ? 19.982  -26.027 37.443  0.50 63.85 ? 328 GLU B CD    1 
ATOM   11792 O  OE1   A GLU B 2 328 ? 19.611  -26.590 36.955  0.50 60.67 ? 328 GLU B OE1   1 
ATOM   11793 O  OE1   B GLU B 2 328 ? 21.035  -26.698 37.475  0.50 62.40 ? 328 GLU B OE1   1 
ATOM   11794 O  OE2   A GLU B 2 328 ? 18.702  -25.158 38.353  0.50 65.92 ? 328 GLU B OE2   1 
ATOM   11795 O  OE2   B GLU B 2 328 ? 19.075  -26.141 38.294  0.50 69.82 ? 328 GLU B OE2   1 
ATOM   11796 N  N     A GLN B 2 329 ? 21.930  -24.467 32.421  0.50 51.33 ? 329 GLN B N     1 
ATOM   11797 N  N     B GLN B 2 329 ? 22.375  -24.981 32.518  0.50 53.48 ? 329 GLN B N     1 
ATOM   11798 C  CA    A GLN B 2 329 ? 23.198  -24.514 31.700  0.50 54.11 ? 329 GLN B CA    1 
ATOM   11799 C  CA    B GLN B 2 329 ? 23.608  -25.020 31.739  0.50 52.17 ? 329 GLN B CA    1 
ATOM   11800 C  C     A GLN B 2 329 ? 23.354  -23.313 30.777  0.50 52.68 ? 329 GLN B C     1 
ATOM   11801 C  C     B GLN B 2 329 ? 23.750  -23.780 30.869  0.50 52.91 ? 329 GLN B C     1 
ATOM   11802 O  O     A GLN B 2 329 ? 24.438  -22.722 30.698  0.50 51.64 ? 329 GLN B O     1 
ATOM   11803 O  O     B GLN B 2 329 ? 24.842  -23.209 30.766  0.50 53.12 ? 329 GLN B O     1 
ATOM   11804 C  CB    A GLN B 2 329 ? 23.306  -25.818 30.912  0.50 53.94 ? 329 GLN B CB    1 
ATOM   11805 C  CB    B GLN B 2 329 ? 23.653  -26.284 30.882  0.50 54.40 ? 329 GLN B CB    1 
ATOM   11806 C  CG    A GLN B 2 329 ? 24.454  -26.710 31.355  0.50 55.09 ? 329 GLN B CG    1 
ATOM   11807 C  CG    B GLN B 2 329 ? 24.000  -27.530 31.666  0.50 54.17 ? 329 GLN B CG    1 
ATOM   11808 C  CD    A GLN B 2 329 ? 24.439  -26.986 32.847  0.50 55.54 ? 329 GLN B CD    1 
ATOM   11809 C  CD    B GLN B 2 329 ? 25.300  -27.378 32.426  0.50 57.26 ? 329 GLN B CD    1 
ATOM   11810 O  OE1   A GLN B 2 329 ? 25.474  -26.930 33.509  0.50 60.22 ? 329 GLN B OE1   1 
ATOM   11811 O  OE1   B GLN B 2 329 ? 26.336  -27.046 31.846  0.50 52.87 ? 329 GLN B OE1   1 
ATOM   11812 N  NE2   A GLN B 2 329 ? 23.263  -27.291 33.382  0.50 56.13 ? 329 GLN B NE2   1 
ATOM   11813 N  NE2   B GLN B 2 329 ? 25.252  -27.607 33.734  0.50 58.79 ? 329 GLN B NE2   1 
ATOM   11814 N  N     A MET B 2 330 ? 22.283  -22.934 30.073  0.50 50.15 ? 330 MET B N     1 
ATOM   11815 N  N     B MET B 2 330 ? 22.656  -23.344 30.237  0.50 52.02 ? 330 MET B N     1 
ATOM   11816 C  CA    A MET B 2 330 ? 22.370  -21.794 29.165  0.50 50.51 ? 330 MET B CA    1 
ATOM   11817 C  CA    B MET B 2 330 ? 22.715  -22.132 29.427  0.50 51.72 ? 330 MET B CA    1 
ATOM   11818 C  C     A MET B 2 330 ? 22.626  -20.503 29.929  0.50 52.76 ? 330 MET B C     1 
ATOM   11819 C  C     B MET B 2 330 ? 23.039  -20.912 30.273  0.50 52.89 ? 330 MET B C     1 
ATOM   11820 O  O     A MET B 2 330 ? 23.407  -19.654 29.484  0.50 51.20 ? 330 MET B O     1 
ATOM   11821 O  O     B MET B 2 330 ? 23.714  -19.990 29.801  0.50 48.75 ? 330 MET B O     1 
ATOM   11822 C  CB    A MET B 2 330 ? 21.097  -21.688 28.326  0.50 46.15 ? 330 MET B CB    1 
ATOM   11823 C  CB    B MET B 2 330 ? 21.398  -21.924 28.679  0.50 46.44 ? 330 MET B CB    1 
ATOM   11824 C  CG    A MET B 2 330 ? 20.967  -22.780 27.272  0.50 47.11 ? 330 MET B CG    1 
ATOM   11825 C  CG    B MET B 2 330 ? 21.279  -22.743 27.406  0.50 47.51 ? 330 MET B CG    1 
ATOM   11826 S  SD    A MET B 2 330 ? 22.327  -22.774 26.084  0.50 52.65 ? 330 MET B SD    1 
ATOM   11827 S  SD    B MET B 2 330 ? 22.662  -22.452 26.285  0.50 49.50 ? 330 MET B SD    1 
ATOM   11828 C  CE    A MET B 2 330 ? 22.077  -21.188 25.298  0.50 44.90 ? 330 MET B CE    1 
ATOM   11829 C  CE    B MET B 2 330 ? 22.628  -20.669 26.159  0.50 43.52 ? 330 MET B CE    1 
ATOM   11830 N  N     A LEU B 2 331 ? 21.980  -20.336 31.086  0.50 51.86 ? 331 LEU B N     1 
ATOM   11831 N  N     B LEU B 2 331 ? 22.573  -20.890 31.523  0.50 51.08 ? 331 LEU B N     1 
ATOM   11832 C  CA    A LEU B 2 331 ? 22.297  -19.200 31.943  0.50 51.95 ? 331 LEU B CA    1 
ATOM   11833 C  CA    B LEU B 2 331 ? 22.886  -19.773 32.406  0.50 53.18 ? 331 LEU B CA    1 
ATOM   11834 C  C     A LEU B 2 331 ? 23.732  -19.269 32.446  0.50 52.80 ? 331 LEU B C     1 
ATOM   11835 C  C     B LEU B 2 331 ? 24.373  -19.739 32.740  0.50 53.45 ? 331 LEU B C     1 
ATOM   11836 O  O     A LEU B 2 331 ? 24.364  -18.230 32.663  0.50 51.81 ? 331 LEU B O     1 
ATOM   11837 O  O     B LEU B 2 331 ? 24.970  -18.660 32.831  0.50 53.90 ? 331 LEU B O     1 
ATOM   11838 C  CB    A LEU B 2 331 ? 21.322  -19.136 33.120  0.50 52.40 ? 331 LEU B CB    1 
ATOM   11839 C  CB    B LEU B 2 331 ? 22.046  -19.870 33.679  0.50 52.79 ? 331 LEU B CB    1 
ATOM   11840 C  CG    A LEU B 2 331 ? 19.932  -18.577 32.819  0.50 47.41 ? 331 LEU B CG    1 
ATOM   11841 C  CG    B LEU B 2 331 ? 21.653  -18.567 34.374  0.50 51.73 ? 331 LEU B CG    1 
ATOM   11842 C  CD1   A LEU B 2 331 ? 19.051  -18.645 34.055  0.50 47.92 ? 331 LEU B CD1   1 
ATOM   11843 C  CD1   B LEU B 2 331 ? 20.967  -17.627 33.395  0.50 48.32 ? 331 LEU B CD1   1 
ATOM   11844 C  CD2   A LEU B 2 331 ? 20.038  -17.146 32.312  0.50 52.61 ? 331 LEU B CD2   1 
ATOM   11845 C  CD2   B LEU B 2 331 ? 20.746  -18.861 35.560  0.50 51.54 ? 331 LEU B CD2   1 
ATOM   11846 N  N     A ASN B 2 332 ? 24.263  -20.481 32.628  0.50 53.72 ? 332 ASN B N     1 
ATOM   11847 N  N     B ASN B 2 332 ? 24.990  -20.911 32.906  0.50 52.92 ? 332 ASN B N     1 
ATOM   11848 C  CA    A ASN B 2 332 ? 25.644  -20.634 33.072  0.50 52.79 ? 332 ASN B CA    1 
ATOM   11849 C  CA    B ASN B 2 332 ? 26.400  -20.962 33.279  0.50 55.38 ? 332 ASN B CA    1 
ATOM   11850 C  C     A ASN B 2 332 ? 26.623  -20.189 31.993  0.50 52.68 ? 332 ASN B C     1 
ATOM   11851 C  C     B ASN B 2 332 ? 27.299  -20.495 32.141  0.50 51.80 ? 332 ASN B C     1 
ATOM   11852 O  O     A ASN B 2 332 ? 27.638  -19.550 32.294  0.50 54.22 ? 332 ASN B O     1 
ATOM   11853 O  O     B ASN B 2 332 ? 28.292  -19.798 32.377  0.50 56.71 ? 332 ASN B O     1 
ATOM   11854 C  CB    A ASN B 2 332 ? 25.900  -22.090 33.469  0.50 52.52 ? 332 ASN B CB    1 
ATOM   11855 C  CB    B ASN B 2 332 ? 26.777  -22.378 33.713  0.50 54.28 ? 332 ASN B CB    1 
ATOM   11856 C  CG    A ASN B 2 332 ? 27.274  -22.303 34.076  0.50 55.32 ? 332 ASN B CG    1 
ATOM   11857 C  CG    B ASN B 2 332 ? 26.128  -22.778 35.023  0.50 53.53 ? 332 ASN B CG    1 
ATOM   11858 O  OD1   A ASN B 2 332 ? 27.804  -21.436 34.772  0.50 52.78 ? 332 ASN B OD1   1 
ATOM   11859 O  OD1   B ASN B 2 332 ? 25.936  -21.949 35.913  0.50 49.36 ? 332 ASN B OD1   1 
ATOM   11860 N  ND2   A ASN B 2 332 ? 27.858  -23.468 33.817  0.50 53.48 ? 332 ASN B ND2   1 
ATOM   11861 N  ND2   B ASN B 2 332 ? 25.786  -24.055 35.147  0.50 54.91 ? 332 ASN B ND2   1 
ATOM   11862 N  N     A VAL B 2 333 ? 26.329  -20.511 30.729  0.50 54.15 ? 333 VAL B N     1 
ATOM   11863 N  N     B VAL B 2 333 ? 26.971  -20.867 30.901  0.50 52.79 ? 333 VAL B N     1 
ATOM   11864 C  CA    A VAL B 2 333 ? 27.215  -20.136 29.629  0.50 49.37 ? 333 VAL B CA    1 
ATOM   11865 C  CA    B VAL B 2 333 ? 27.811  -20.478 29.771  0.50 50.21 ? 333 VAL B CA    1 
ATOM   11866 C  C     A VAL B 2 333 ? 27.303  -18.619 29.505  0.50 52.37 ? 333 VAL B C     1 
ATOM   11867 C  C     B VAL B 2 333 ? 27.753  -18.975 29.539  0.50 52.48 ? 333 VAL B C     1 
ATOM   11868 O  O     A VAL B 2 333 ? 28.368  -18.066 29.204  0.50 54.50 ? 333 VAL B O     1 
ATOM   11869 O  O     B VAL B 2 333 ? 28.753  -18.362 29.144  0.50 55.08 ? 333 VAL B O     1 
ATOM   11870 C  CB    A VAL B 2 333 ? 26.737  -20.788 28.317  0.50 47.35 ? 333 VAL B CB    1 
ATOM   11871 C  CB    B VAL B 2 333 ? 27.405  -21.250 28.503  0.50 50.22 ? 333 VAL B CB    1 
ATOM   11872 C  CG1   A VAL B 2 333 ? 27.537  -20.272 27.133  0.50 50.69 ? 333 VAL B CG1   1 
ATOM   11873 C  CG1   B VAL B 2 333 ? 28.336  -20.899 27.363  0.50 52.36 ? 333 VAL B CG1   1 
ATOM   11874 C  CG2   A VAL B 2 333 ? 26.845  -22.300 28.410  0.50 50.95 ? 333 VAL B CG2   1 
ATOM   11875 C  CG2   B VAL B 2 333 ? 27.430  -22.742 28.758  0.50 52.55 ? 333 VAL B CG2   1 
ATOM   11876 N  N     A GLN B 2 334 ? 26.195  -17.922 29.748  0.50 48.29 ? 334 GLN B N     1 
ATOM   11877 N  N     B GLN B 2 334 ? 26.598  -18.353 29.780  0.50 50.20 ? 334 GLN B N     1 
ATOM   11878 C  CA    A GLN B 2 334 ? 26.185  -16.468 29.666  0.50 48.29 ? 334 GLN B CA    1 
ATOM   11879 C  CA    B GLN B 2 334 ? 26.480  -16.918 29.557  0.50 48.56 ? 334 GLN B CA    1 
ATOM   11880 C  C     A GLN B 2 334 ? 26.789  -15.799 30.894  0.50 57.10 ? 334 GLN B C     1 
ATOM   11881 C  C     B GLN B 2 334 ? 27.278  -16.121 30.580  0.50 54.45 ? 334 GLN B C     1 
ATOM   11882 O  O     A GLN B 2 334 ? 27.019  -14.585 30.866  0.50 53.72 ? 334 GLN B O     1 
ATOM   11883 O  O     B GLN B 2 334 ? 27.823  -15.062 30.248  0.50 53.09 ? 334 GLN B O     1 
ATOM   11884 C  CB    A GLN B 2 334 ? 24.756  -15.969 29.453  0.50 53.56 ? 334 GLN B CB    1 
ATOM   11885 C  CB    B GLN B 2 334 ? 25.007  -16.508 29.583  0.50 52.60 ? 334 GLN B CB    1 
ATOM   11886 C  CG    A GLN B 2 334 ? 24.101  -16.517 28.196  0.50 41.59 ? 334 GLN B CG    1 
ATOM   11887 C  CG    B GLN B 2 334 ? 24.731  -15.086 29.114  0.50 50.00 ? 334 GLN B CG    1 
ATOM   11888 C  CD    A GLN B 2 334 ? 22.589  -16.515 28.284  0.50 44.00 ? 334 GLN B CD    1 
ATOM   11889 C  CD    B GLN B 2 334 ? 23.246  -14.799 28.990  0.50 49.08 ? 334 GLN B CD    1 
ATOM   11890 O  OE1   A GLN B 2 334 ? 21.953  -15.461 28.261  0.50 40.77 ? 334 GLN B OE1   1 
ATOM   11891 O  OE1   B GLN B 2 334 ? 22.804  -13.664 29.162  0.50 58.25 ? 334 GLN B OE1   1 
ATOM   11892 N  NE2   A GLN B 2 334 ? 22.004  -17.702 28.395  0.50 38.58 ? 334 GLN B NE2   1 
ATOM   11893 N  NE2   B GLN B 2 334 ? 22.467  -15.832 28.689  0.50 45.48 ? 334 GLN B NE2   1 
ATOM   11894 N  N     A ASN B 2 335 ? 27.046  -16.551 31.965  0.50 56.60 ? 335 ASN B N     1 
ATOM   11895 N  N     B ASN B 2 335 ? 27.369  -16.613 31.819  0.50 56.97 ? 335 ASN B N     1 
ATOM   11896 C  CA    A ASN B 2 335 ? 27.721  -15.999 33.133  0.50 57.09 ? 335 ASN B CA    1 
ATOM   11897 C  CA    B ASN B 2 335 ? 28.090  -15.886 32.860  0.50 56.13 ? 335 ASN B CA    1 
ATOM   11898 C  C     A ASN B 2 335 ? 29.231  -16.189 33.061  0.50 54.14 ? 335 ASN B C     1 
ATOM   11899 C  C     B ASN B 2 335 ? 29.600  -16.022 32.698  0.50 55.59 ? 335 ASN B C     1 
ATOM   11900 O  O     A ASN B 2 335 ? 29.987  -15.280 33.419  0.50 57.94 ? 335 ASN B O     1 
ATOM   11901 O  O     B ASN B 2 335 ? 30.326  -15.022 32.732  0.50 56.04 ? 335 ASN B O     1 
ATOM   11902 C  CB    A ASN B 2 335 ? 27.177  -16.640 34.412  0.50 54.63 ? 335 ASN B CB    1 
ATOM   11903 C  CB    B ASN B 2 335 ? 27.653  -16.377 34.241  0.50 56.07 ? 335 ASN B CB    1 
ATOM   11904 C  CG    A ASN B 2 335 ? 25.685  -16.436 34.578  0.50 57.66 ? 335 ASN B CG    1 
ATOM   11905 C  CG    B ASN B 2 335 ? 26.234  -15.972 34.580  0.50 55.64 ? 335 ASN B CG    1 
ATOM   11906 O  OD1   A ASN B 2 335 ? 25.135  -15.419 34.156  0.50 59.59 ? 335 ASN B OD1   1 
ATOM   11907 O  OD1   B ASN B 2 335 ? 25.369  -16.818 34.801  0.50 59.89 ? 335 ASN B OD1   1 
ATOM   11908 N  ND2   A ASN B 2 335 ? 25.018  -17.411 35.187  0.50 61.94 ? 335 ASN B ND2   1 
ATOM   11909 N  ND2   B ASN B 2 335 ? 25.987  -14.669 34.626  0.50 62.34 ? 335 ASN B ND2   1 
ATOM   11910 N  N     A LYS B 2 336 ? 29.684  -17.353 32.598  0.50 53.60 ? 336 LYS B N     1 
ATOM   11911 N  N     B LYS B 2 336 ? 30.090  -17.252 32.520  0.50 54.13 ? 336 LYS B N     1 
ATOM   11912 C  CA    A LYS B 2 336 ? 31.107  -17.635 32.471  0.50 54.54 ? 336 LYS B CA    1 
ATOM   11913 C  CA    B LYS B 2 336 ? 31.526  -17.466 32.375  0.50 55.60 ? 336 LYS B CA    1 
ATOM   11914 C  C     A LYS B 2 336 ? 31.704  -17.140 31.159  0.50 59.34 ? 336 LYS B C     1 
ATOM   11915 C  C     B LYS B 2 336 ? 32.095  -16.791 31.131  0.50 58.11 ? 336 LYS B C     1 
ATOM   11916 O  O     A LYS B 2 336 ? 32.933  -17.140 31.019  0.50 55.71 ? 336 LYS B O     1 
ATOM   11917 O  O     B LYS B 2 336 ? 33.305  -16.547 31.073  0.50 57.98 ? 336 LYS B O     1 
ATOM   11918 C  CB    A LYS B 2 336 ? 31.357  -19.140 32.617  0.50 56.84 ? 336 LYS B CB    1 
ATOM   11919 C  CB    B LYS B 2 336 ? 31.833  -18.966 32.345  0.50 55.51 ? 336 LYS B CB    1 
ATOM   11920 C  CG    A LYS B 2 336 ? 30.913  -19.707 33.961  0.50 56.40 ? 336 LYS B CG    1 
ATOM   11921 C  CG    B LYS B 2 336 ? 31.553  -19.684 33.660  0.50 60.25 ? 336 LYS B CG    1 
ATOM   11922 C  CD    A LYS B 2 336 ? 31.266  -21.181 34.091  0.50 57.59 ? 336 LYS B CD    1 
ATOM   11923 C  CD    B LYS B 2 336 ? 32.056  -21.121 33.629  0.50 60.35 ? 336 LYS B CD    1 
ATOM   11924 C  CE    A LYS B 2 336 ? 30.647  -21.997 32.968  0.50 55.65 ? 336 LYS B CE    1 
ATOM   11925 C  CE    B LYS B 2 336 ? 31.879  -21.802 34.978  0.50 54.81 ? 336 LYS B CE    1 
ATOM   11926 N  NZ    A LYS B 2 336 ? 30.997  -23.439 33.071  0.50 47.95 ? 336 LYS B NZ    1 
ATOM   11927 N  NZ    B LYS B 2 336 ? 30.448  -21.874 35.385  0.50 55.51 ? 336 LYS B NZ    1 
ATOM   11928 N  N     A ASN B 2 337 ? 30.876  -16.726 30.196  0.50 52.65 ? 337 ASN B N     1 
ATOM   11929 N  N     B ASN B 2 337 ? 31.257  -16.480 30.144  0.50 52.93 ? 337 ASN B N     1 
ATOM   11930 C  CA    A ASN B 2 337 ? 31.344  -16.138 28.945  0.50 52.32 ? 337 ASN B CA    1 
ATOM   11931 C  CA    B ASN B 2 337 ? 31.673  -15.814 28.915  0.50 51.57 ? 337 ASN B CA    1 
ATOM   11932 C  C     A ASN B 2 337 ? 30.747  -14.750 28.729  0.50 46.67 ? 337 ASN B C     1 
ATOM   11933 C  C     B ASN B 2 337 ? 30.926  -14.498 28.737  0.50 45.85 ? 337 ASN B C     1 
ATOM   11934 O  O     A ASN B 2 337 ? 30.531  -14.335 27.589  0.50 45.16 ? 337 ASN B O     1 
ATOM   11935 O  O     B ASN B 2 337 ? 30.472  -14.161 27.641  0.50 44.94 ? 337 ASN B O     1 
ATOM   11936 C  CB    A ASN B 2 337 ? 31.013  -17.034 27.751  0.50 48.44 ? 337 ASN B CB    1 
ATOM   11937 C  CB    B ASN B 2 337 ? 31.455  -16.719 27.704  0.50 46.85 ? 337 ASN B CB    1 
ATOM   11938 C  CG    A ASN B 2 337 ? 31.432  -18.475 27.960  0.50 50.67 ? 337 ASN B CG    1 
ATOM   11939 C  CG    B ASN B 2 337 ? 32.139  -18.064 27.848  0.50 50.86 ? 337 ASN B CG    1 
ATOM   11940 O  OD1   A ASN B 2 337 ? 32.325  -18.771 28.751  0.50 56.90 ? 337 ASN B OD1   1 
ATOM   11941 O  OD1   B ASN B 2 337 ? 33.243  -18.270 27.341  0.50 48.01 ? 337 ASN B OD1   1 
ATOM   11942 N  ND2   A ASN B 2 337 ? 30.787  -19.383 27.238  0.50 51.03 ? 337 ASN B ND2   1 
ATOM   11943 N  ND2   B ASN B 2 337 ? 31.485  -18.989 28.543  0.50 51.22 ? 337 ASN B ND2   1 
ATOM   11944 N  N     A SER B 2 338 ? 30.478  -14.022 29.816  0.50 47.89 ? 338 SER B N     1 
ATOM   11945 N  N     B SER B 2 338 ? 30.797  -13.733 29.824  0.50 46.99 ? 338 SER B N     1 
ATOM   11946 C  CA    A SER B 2 338 ? 29.771  -12.750 29.705  0.50 43.19 ? 338 SER B CA    1 
ATOM   11947 C  CA    B SER B 2 338 ? 29.959  -12.537 29.793  0.50 43.34 ? 338 SER B CA    1 
ATOM   11948 C  C     A SER B 2 338 ? 30.547  -11.711 28.903  0.50 41.12 ? 338 SER B C     1 
ATOM   11949 C  C     B SER B 2 338 ? 30.544  -11.461 28.885  0.50 40.73 ? 338 SER B C     1 
ATOM   11950 O  O     A SER B 2 338 ? 29.953  -10.730 28.445  0.50 39.63 ? 338 SER B O     1 
ATOM   11951 O  O     B SER B 2 338 ? 29.799  -10.741 28.211  0.50 39.72 ? 338 SER B O     1 
ATOM   11952 C  CB    A SER B 2 338 ? 29.447  -12.208 31.100  0.50 51.82 ? 338 SER B CB    1 
ATOM   11953 C  CB    B SER B 2 338 ? 29.762  -11.998 31.209  0.50 52.35 ? 338 SER B CB    1 
ATOM   11954 O  OG    A SER B 2 338 ? 30.574  -12.286 31.954  0.50 55.67 ? 338 SER B OG    1 
ATOM   11955 O  OG    B SER B 2 338 ? 31.009  -11.751 31.835  0.50 56.05 ? 338 SER B OG    1 
ATOM   11956 N  N     A SER B 2 339 ? 31.851  -11.903 28.714  0.50 38.58 ? 339 SER B N     1 
ATOM   11957 N  N     B SER B 2 339 ? 31.871  -11.335 28.850  0.50 40.85 ? 339 SER B N     1 
ATOM   11958 C  CA    A SER B 2 339 ? 32.639  -10.979 27.909  0.50 42.00 ? 339 SER B CA    1 
ATOM   11959 C  CA    B SER B 2 339 ? 32.499  -10.288 28.052  0.50 41.87 ? 339 SER B CA    1 
ATOM   11960 C  C     A SER B 2 339 ? 32.555  -11.271 26.415  0.50 38.06 ? 339 SER B C     1 
ATOM   11961 C  C     B SER B 2 339 ? 32.342  -10.508 26.552  0.50 38.07 ? 339 SER B C     1 
ATOM   11962 O  O     A SER B 2 339 ? 33.176  -10.551 25.625  0.50 38.33 ? 339 SER B O     1 
ATOM   11963 O  O     B SER B 2 339 ? 32.720  -9.627  25.772  0.50 38.30 ? 339 SER B O     1 
ATOM   11964 C  CB    A SER B 2 339 ? 34.101  -11.005 28.361  0.50 41.85 ? 339 SER B CB    1 
ATOM   11965 C  CB    B SER B 2 339 ? 33.985  -10.180 28.398  0.50 38.32 ? 339 SER B CB    1 
ATOM   11966 O  OG    A SER B 2 339 ? 34.615  -12.325 28.354  0.50 45.58 ? 339 SER B OG    1 
ATOM   11967 O  OG    B SER B 2 339 ? 34.728  -11.213 27.773  0.50 45.54 ? 339 SER B OG    1 
ATOM   11968 N  N     A TYR B 2 340 ? 31.814  -12.302 26.011  0.50 33.87 ? 340 TYR B N     1 
ATOM   11969 N  N     B TYR B 2 340 ? 31.805  -11.651 26.131  0.50 34.11 ? 340 TYR B N     1 
ATOM   11970 C  CA    A TYR B 2 340 ? 31.600  -12.608 24.603  0.50 35.92 ? 340 TYR B CA    1 
ATOM   11971 C  CA    B TYR B 2 340 ? 31.641  -11.959 24.719  0.50 37.15 ? 340 TYR B CA    1 
ATOM   11972 C  C     A TYR B 2 340 ? 30.168  -12.352 24.154  0.50 35.64 ? 340 TYR B C     1 
ATOM   11973 C  C     B TYR B 2 340 ? 30.235  -11.674 24.207  0.50 34.31 ? 340 TYR B C     1 
ATOM   11974 O  O     A TYR B 2 340 ? 29.832  -12.647 23.002  0.50 32.53 ? 340 TYR B O     1 
ATOM   11975 O  O     B TYR B 2 340 ? 29.948  -11.949 23.040  0.50 32.37 ? 340 TYR B O     1 
ATOM   11976 C  CB    A TYR B 2 340 ? 31.987  -14.062 24.311  0.50 33.91 ? 340 TYR B CB    1 
ATOM   11977 C  CB    B TYR B 2 340 ? 32.014  -13.422 24.461  0.50 33.98 ? 340 TYR B CB    1 
ATOM   11978 C  CG    A TYR B 2 340 ? 33.441  -14.363 24.589  0.50 38.91 ? 340 TYR B CG    1 
ATOM   11979 C  CG    B TYR B 2 340 ? 33.431  -13.742 24.881  0.50 39.90 ? 340 TYR B CG    1 
ATOM   11980 C  CD1   A TYR B 2 340 ? 34.451  -13.623 23.987  0.50 38.49 ? 340 TYR B CD1   1 
ATOM   11981 C  CD1   B TYR B 2 340 ? 34.514  -13.265 24.152  0.50 39.06 ? 340 TYR B CD1   1 
ATOM   11982 C  CD2   A TYR B 2 340 ? 33.806  -15.389 25.449  0.50 41.54 ? 340 TYR B CD2   1 
ATOM   11983 C  CD2   B TYR B 2 340 ? 33.689  -14.506 26.012  0.50 40.65 ? 340 TYR B CD2   1 
ATOM   11984 C  CE1   A TYR B 2 340 ? 35.785  -13.892 24.239  0.50 40.18 ? 340 TYR B CE1   1 
ATOM   11985 C  CE1   B TYR B 2 340 ? 35.813  -13.545 24.533  0.50 39.88 ? 340 TYR B CE1   1 
ATOM   11986 C  CE2   A TYR B 2 340 ? 35.136  -15.665 25.705  0.50 44.08 ? 340 TYR B CE2   1 
ATOM   11987 C  CE2   B TYR B 2 340 ? 34.985  -14.793 26.399  0.50 43.96 ? 340 TYR B CE2   1 
ATOM   11988 C  CZ    A TYR B 2 340 ? 36.122  -14.916 25.095  0.50 40.96 ? 340 TYR B CZ    1 
ATOM   11989 C  CZ    B TYR B 2 340 ? 36.043  -14.308 25.655  0.50 38.64 ? 340 TYR B CZ    1 
ATOM   11990 O  OH    A TYR B 2 340 ? 37.448  -15.191 25.346  0.50 36.42 ? 340 TYR B OH    1 
ATOM   11991 O  OH    B TYR B 2 340 ? 37.337  -14.588 26.030  0.50 43.50 ? 340 TYR B OH    1 
ATOM   11992 N  N     A PHE B 2 341 ? 29.317  -11.826 25.032  0.50 29.22 ? 341 PHE B N     1 
ATOM   11993 N  N     B PHE B 2 341 ? 29.356  -11.135 25.046  0.50 31.63 ? 341 PHE B N     1 
ATOM   11994 C  CA    A PHE B 2 341 ? 27.973  -11.382 24.685  0.50 32.06 ? 341 PHE B CA    1 
ATOM   11995 C  CA    B PHE B 2 341 ? 28.040  -10.684 24.623  0.50 30.36 ? 341 PHE B CA    1 
ATOM   11996 C  C     A PHE B 2 341 ? 27.886  -9.888  24.946  0.50 32.84 ? 341 PHE B C     1 
ATOM   11997 C  C     B PHE B 2 341 ? 27.976  -9.164  24.700  0.50 34.74 ? 341 PHE B C     1 
ATOM   11998 O  O     A PHE B 2 341 ? 28.297  -9.424  26.015  0.50 35.74 ? 341 PHE B O     1 
ATOM   11999 O  O     B PHE B 2 341 ? 28.612  -8.543  25.555  0.50 32.79 ? 341 PHE B O     1 
ATOM   12000 C  CB    A PHE B 2 341 ? 26.903  -12.117 25.505  0.50 31.02 ? 341 PHE B CB    1 
ATOM   12001 C  CB    B PHE B 2 341 ? 26.936  -11.300 25.489  0.50 32.11 ? 341 PHE B CB    1 
ATOM   12002 C  CG    A PHE B 2 341 ? 26.888  -13.604 25.298  0.50 33.82 ? 341 PHE B CG    1 
ATOM   12003 C  CG    B PHE B 2 341 ? 26.885  -12.799 25.427  0.50 31.90 ? 341 PHE B CG    1 
ATOM   12004 C  CD1   A PHE B 2 341 ? 27.801  -14.418 25.948  0.50 34.84 ? 341 PHE B CD1   1 
ATOM   12005 C  CD1   B PHE B 2 341 ? 27.631  -13.567 26.303  0.50 31.18 ? 341 PHE B CD1   1 
ATOM   12006 C  CD2   A PHE B 2 341 ? 25.951  -14.191 24.463  0.50 31.91 ? 341 PHE B CD2   1 
ATOM   12007 C  CD2   B PHE B 2 341 ? 26.098  -13.440 24.485  0.50 34.53 ? 341 PHE B CD2   1 
ATOM   12008 C  CE1   A PHE B 2 341 ? 27.789  -15.788 25.760  0.50 34.47 ? 341 PHE B CE1   1 
ATOM   12009 C  CE1   B PHE B 2 341 ? 27.589  -14.947 26.245  0.50 37.29 ? 341 PHE B CE1   1 
ATOM   12010 C  CE2   A PHE B 2 341 ? 25.933  -15.558 24.272  0.50 31.64 ? 341 PHE B CE2   1 
ATOM   12011 C  CE2   B PHE B 2 341 ? 26.054  -14.819 24.421  0.50 32.17 ? 341 PHE B CE2   1 
ATOM   12012 C  CZ    A PHE B 2 341 ? 26.850  -16.358 24.923  0.50 34.83 ? 341 PHE B CZ    1 
ATOM   12013 C  CZ    B PHE B 2 341 ? 26.798  -15.575 25.304  0.50 35.53 ? 341 PHE B CZ    1 
ATOM   12014 N  N     A VAL B 2 342 ? 27.360  -9.134  23.975  0.50 28.12 ? 342 VAL B N     1 
ATOM   12015 N  N     B VAL B 2 342 ? 27.217  -8.562  23.786  0.50 27.87 ? 342 VAL B N     1 
ATOM   12016 C  CA    A VAL B 2 342 ? 27.214  -7.700  24.179  0.50 27.79 ? 342 VAL B CA    1 
ATOM   12017 C  CA    B VAL B 2 342 ? 27.016  -7.120  23.847  0.50 30.41 ? 342 VAL B CA    1 
ATOM   12018 C  C     A VAL B 2 342 ? 26.265  -7.460  25.344  0.50 32.77 ? 342 VAL B C     1 
ATOM   12019 C  C     B VAL B 2 342 ? 26.102  -6.803  25.020  0.50 34.73 ? 342 VAL B C     1 
ATOM   12020 O  O     A VAL B 2 342 ? 25.362  -8.259  25.617  0.50 27.12 ? 342 VAL B O     1 
ATOM   12021 O  O     B VAL B 2 342 ? 25.049  -7.431  25.195  0.50 29.78 ? 342 VAL B O     1 
ATOM   12022 C  CB    A VAL B 2 342 ? 26.711  -6.983  22.915  0.50 30.28 ? 342 VAL B CB    1 
ATOM   12023 C  CB    B VAL B 2 342 ? 26.450  -6.584  22.524  0.50 29.73 ? 342 VAL B CB    1 
ATOM   12024 C  CG1   A VAL B 2 342 ? 27.737  -7.090  21.797  0.50 30.60 ? 342 VAL B CG1   1 
ATOM   12025 C  CG1   B VAL B 2 342 ? 27.526  -6.601  21.448  0.50 31.49 ? 342 VAL B CG1   1 
ATOM   12026 C  CG2   A VAL B 2 342 ? 25.364  -7.545  22.480  0.50 31.25 ? 342 VAL B CG2   1 
ATOM   12027 C  CG2   B VAL B 2 342 ? 25.241  -7.397  22.088  0.50 32.54 ? 342 VAL B CG2   1 
ATOM   12028 N  N     A GLU B 2 343 ? 26.474  -6.348  26.042  0.50 34.17 ? 343 GLU B N     1 
ATOM   12029 N  N     B GLU B 2 343 ? 26.516  -5.845  25.844  0.50 31.94 ? 343 GLU B N     1 
ATOM   12030 C  CA    A GLU B 2 343 ? 25.664  -6.033  27.208  0.50 37.25 ? 343 GLU B CA    1 
ATOM   12031 C  CA    B GLU B 2 343 ? 25.786  -5.497  27.055  0.50 36.57 ? 343 GLU B CA    1 
ATOM   12032 C  C     A GLU B 2 343 ? 24.485  -5.128  26.890  0.50 32.98 ? 343 GLU B C     1 
ATOM   12033 C  C     B GLU B 2 343 ? 24.663  -4.501  26.807  0.50 33.43 ? 343 GLU B C     1 
ATOM   12034 O  O     A GLU B 2 343 ? 23.638  -4.917  27.764  0.50 30.88 ? 343 GLU B O     1 
ATOM   12035 O  O     B GLU B 2 343 ? 23.953  -4.148  27.755  0.50 36.38 ? 343 GLU B O     1 
ATOM   12036 C  CB    A GLU B 2 343 ? 26.528  -5.378  28.294  0.50 36.96 ? 343 GLU B CB    1 
ATOM   12037 C  CB    B GLU B 2 343 ? 26.746  -4.941  28.115  0.50 34.72 ? 343 GLU B CB    1 
ATOM   12038 C  CG    A GLU B 2 343 ? 26.795  -3.900  28.074  0.50 39.53 ? 343 GLU B CG    1 
ATOM   12039 C  CG    B GLU B 2 343 ? 27.539  -3.716  27.679  0.50 42.66 ? 343 GLU B CG    1 
ATOM   12040 C  CD    A GLU B 2 343 ? 27.800  -3.634  26.967  0.50 41.52 ? 343 GLU B CD    1 
ATOM   12041 C  CD    B GLU B 2 343 ? 28.799  -4.068  26.907  0.50 41.58 ? 343 GLU B CD    1 
ATOM   12042 O  OE1   A GLU B 2 343 ? 28.521  -4.575  26.569  0.50 39.84 ? 343 GLU B OE1   1 
ATOM   12043 O  OE1   B GLU B 2 343 ? 29.118  -5.272  26.798  0.50 36.87 ? 343 GLU B OE1   1 
ATOM   12044 O  OE2   A GLU B 2 343 ? 27.873  -2.480  26.498  0.50 42.12 ? 343 GLU B OE2   1 
ATOM   12045 O  OE2   B GLU B 2 343 ? 29.471  -3.136  26.413  0.50 44.34 ? 343 GLU B OE2   1 
ATOM   12046 N  N     A TRP B 2 344 ? 24.401  -4.594  25.669  0.50 31.87 ? 344 TRP B N     1 
ATOM   12047 N  N     B TRP B 2 344 ? 24.480  -4.047  25.568  0.50 30.87 ? 344 TRP B N     1 
ATOM   12048 C  CA    A TRP B 2 344 ? 23.352  -3.650  25.307  0.50 33.07 ? 344 TRP B CA    1 
ATOM   12049 C  CA    B TRP B 2 344 ? 23.427  -3.098  25.233  0.50 32.75 ? 344 TRP B CA    1 
ATOM   12050 C  C     A TRP B 2 344 ? 22.220  -4.295  24.511  0.50 28.51 ? 344 TRP B C     1 
ATOM   12051 C  C     B TRP B 2 344 ? 22.238  -3.741  24.529  0.50 28.35 ? 344 TRP B C     1 
ATOM   12052 O  O     A TRP B 2 344 ? 21.464  -3.586  23.837  0.50 29.22 ? 344 TRP B O     1 
ATOM   12053 O  O     B TRP B 2 344 ? 21.307  -3.027  24.143  0.50 27.98 ? 344 TRP B O     1 
ATOM   12054 C  CB    A TRP B 2 344 ? 23.938  -2.459  24.540  0.50 28.71 ? 344 TRP B CB    1 
ATOM   12055 C  CB    B TRP B 2 344 ? 23.987  -1.954  24.377  0.50 29.93 ? 344 TRP B CB    1 
ATOM   12056 C  CG    A TRP B 2 344 ? 24.986  -2.789  23.499  0.50 36.12 ? 344 TRP B CG    1 
ATOM   12057 C  CG    B TRP B 2 344 ? 25.035  -2.356  23.371  0.50 35.89 ? 344 TRP B CG    1 
ATOM   12058 C  CD1   A TRP B 2 344 ? 26.327  -2.955  23.710  0.50 35.14 ? 344 TRP B CD1   1 
ATOM   12059 C  CD1   B TRP B 2 344 ? 26.378  -2.481  23.592  0.50 35.52 ? 344 TRP B CD1   1 
ATOM   12060 C  CD2   A TRP B 2 344 ? 24.782  -2.951  22.088  0.50 33.17 ? 344 TRP B CD2   1 
ATOM   12061 C  CD2   B TRP B 2 344 ? 24.827  -2.658  21.986  0.50 33.59 ? 344 TRP B CD2   1 
ATOM   12062 N  NE1   A TRP B 2 344 ? 26.965  -3.224  22.522  0.50 34.59 ? 344 TRP B NE1   1 
ATOM   12063 N  NE1   B TRP B 2 344 ? 27.016  -2.851  22.433  0.50 33.42 ? 344 TRP B NE1   1 
ATOM   12064 C  CE2   A TRP B 2 344 ? 26.039  -3.228  21.512  0.50 32.97 ? 344 TRP B CE2   1 
ATOM   12065 C  CE2   B TRP B 2 344 ? 26.087  -2.968  21.433  0.50 33.02 ? 344 TRP B CE2   1 
ATOM   12066 C  CE3   A TRP B 2 344 ? 23.658  -2.892  21.257  0.50 33.29 ? 344 TRP B CE3   1 
ATOM   12067 C  CE3   B TRP B 2 344 ? 23.699  -2.700  21.160  0.50 32.79 ? 344 TRP B CE3   1 
ATOM   12068 C  CZ2   A TRP B 2 344 ? 26.201  -3.448  20.146  0.50 30.75 ? 344 TRP B CZ2   1 
ATOM   12069 C  CZ2   B TRP B 2 344 ? 26.248  -3.316  20.093  0.50 30.73 ? 344 TRP B CZ2   1 
ATOM   12070 C  CZ3   A TRP B 2 344 ? 23.821  -3.116  19.903  0.50 30.61 ? 344 TRP B CZ3   1 
ATOM   12071 C  CZ3   B TRP B 2 344 ? 23.861  -3.050  19.833  0.50 30.67 ? 344 TRP B CZ3   1 
ATOM   12072 C  CH2   A TRP B 2 344 ? 25.083  -3.388  19.361  0.50 34.47 ? 344 TRP B CH2   1 
ATOM   12073 C  CH2   B TRP B 2 344 ? 25.126  -3.350  19.312  0.50 34.47 ? 344 TRP B CH2   1 
ATOM   12074 N  N     A ILE B 2 345 ? 22.083  -5.616  24.579  0.50 27.19 ? 345 ILE B N     1 
ATOM   12075 N  N     B ILE B 2 345 ? 22.242  -5.059  24.353  0.50 28.04 ? 345 ILE B N     1 
ATOM   12076 C  CA    A ILE B 2 345 ? 20.892  -6.301  24.077  0.50 25.39 ? 345 ILE B CA    1 
ATOM   12077 C  CA    B ILE B 2 345 ? 21.049  -5.783  23.915  0.50 27.83 ? 345 ILE B CA    1 
ATOM   12078 C  C     A ILE B 2 345 ? 20.434  -7.273  25.157  0.50 26.37 ? 345 ILE B C     1 
ATOM   12079 C  C     B ILE B 2 345 ? 20.684  -6.765  25.021  0.50 25.63 ? 345 ILE B C     1 
ATOM   12080 O  O     A ILE B 2 345 ? 20.952  -8.395  25.233  0.50 25.80 ? 345 ILE B O     1 
ATOM   12081 O  O     B ILE B 2 345 ? 21.128  -7.922  24.995  0.50 25.15 ? 345 ILE B O     1 
ATOM   12082 C  CB    A ILE B 2 345 ? 21.158  -7.029  22.747  0.50 26.18 ? 345 ILE B CB    1 
ATOM   12083 C  CB    B ILE B 2 345 ? 21.267  -6.497  22.569  0.50 27.36 ? 345 ILE B CB    1 
ATOM   12084 C  CG1   A ILE B 2 345 ? 21.609  -6.049  21.662  0.50 26.66 ? 345 ILE B CG1   1 
ATOM   12085 C  CG1   B ILE B 2 345 ? 21.611  -5.487  21.474  0.50 24.89 ? 345 ILE B CG1   1 
ATOM   12086 C  CG2   A ILE B 2 345 ? 19.903  -7.747  22.276  0.50 31.24 ? 345 ILE B CG2   1 
ATOM   12087 C  CG2   B ILE B 2 345 ? 20.021  -7.269  22.164  0.50 30.56 ? 345 ILE B CG2   1 
ATOM   12088 C  CD1   A ILE B 2 345 ? 21.870  -6.710  20.314  0.50 26.32 ? 345 ILE B CD1   1 
ATOM   12089 C  CD1   B ILE B 2 345 ? 21.652  -6.095  20.079  0.50 27.81 ? 345 ILE B CD1   1 
ATOM   12090 N  N     A PRO B 2 346 ? 19.484  -6.891  26.013  0.50 26.00 ? 346 PRO B N     1 
ATOM   12091 N  N     B PRO B 2 346 ? 19.903  -6.347  26.018  0.50 27.22 ? 346 PRO B N     1 
ATOM   12092 C  CA    A PRO B 2 346 ? 19.071  -7.782  27.103  0.50 26.10 ? 346 PRO B CA    1 
ATOM   12093 C  CA    B PRO B 2 346 ? 19.575  -7.249  27.128  0.50 22.55 ? 346 PRO B CA    1 
ATOM   12094 C  C     A PRO B 2 346 ? 18.365  -9.018  26.573  0.50 25.25 ? 346 PRO B C     1 
ATOM   12095 C  C     B PRO B 2 346 ? 18.832  -8.484  26.641  0.50 23.99 ? 346 PRO B C     1 
ATOM   12096 O  O     A PRO B 2 346 ? 17.632  -8.963  25.583  0.50 31.21 ? 346 PRO B O     1 
ATOM   12097 O  O     B PRO B 2 346 ? 18.098  -8.439  25.653  0.50 22.97 ? 346 PRO B O     1 
ATOM   12098 C  CB    A PRO B 2 346 ? 18.110  -6.919  27.935  0.50 28.13 ? 346 PRO B CB    1 
ATOM   12099 C  CB    B PRO B 2 346 ? 18.686  -6.391  28.037  0.50 30.54 ? 346 PRO B CB    1 
ATOM   12100 C  CG    A PRO B 2 346 ? 18.248  -5.509  27.402  0.50 23.29 ? 346 PRO B CG    1 
ATOM   12101 C  CG    B PRO B 2 346 ? 18.955  -4.969  27.637  0.50 26.24 ? 346 PRO B CG    1 
ATOM   12102 C  CD    A PRO B 2 346 ? 18.704  -5.644  25.985  0.50 27.29 ? 346 PRO B CD    1 
ATOM   12103 C  CD    B PRO B 2 346 ? 19.291  -5.017  26.174  0.50 27.61 ? 346 PRO B CD    1 
ATOM   12104 N  N     A ASN B 2 347 ? 18.595  -10.141 27.256  0.50 23.38 ? 347 ASN B N     1 
ATOM   12105 N  N     B ASN B 2 347 ? 19.038  -9.594  27.354  0.50 22.65 ? 347 ASN B N     1 
ATOM   12106 C  CA    A ASN B 2 347 ? 17.971  -11.422 26.919  0.50 22.28 ? 347 ASN B CA    1 
ATOM   12107 C  CA    B ASN B 2 347 ? 18.369  -10.872 27.093  0.50 22.39 ? 347 ASN B CA    1 
ATOM   12108 C  C     A ASN B 2 347 ? 18.178  -11.758 25.443  0.50 27.94 ? 347 ASN B C     1 
ATOM   12109 C  C     B ASN B 2 347 ? 18.496  -11.286 25.625  0.50 29.03 ? 347 ASN B C     1 
ATOM   12110 O  O     A ASN B 2 347 ? 17.234  -12.055 24.706  0.50 23.32 ? 347 ASN B O     1 
ATOM   12111 O  O     B ASN B 2 347 ? 17.506  -11.492 24.917  0.50 27.72 ? 347 ASN B O     1 
ATOM   12112 C  CB    A ASN B 2 347 ? 16.483  -11.407 27.287  0.50 25.38 ? 347 ASN B CB    1 
ATOM   12113 C  CB    B ASN B 2 347 ? 16.899  -10.812 27.516  0.50 28.54 ? 347 ASN B CB    1 
ATOM   12114 C  CG    A ASN B 2 347 ? 15.836  -12.786 27.213  0.50 37.46 ? 347 ASN B CG    1 
ATOM   12115 C  CG    B ASN B 2 347 ? 16.259  -12.179 27.585  0.50 34.48 ? 347 ASN B CG    1 
ATOM   12116 O  OD1   A ASN B 2 347 ? 16.479  -13.777 26.864  0.50 29.23 ? 347 ASN B OD1   1 
ATOM   12117 O  OD1   B ASN B 2 347 ? 16.821  -13.111 28.164  0.50 32.27 ? 347 ASN B OD1   1 
ATOM   12118 N  ND2   A ASN B 2 347 ? 14.555  -12.851 27.559  0.50 34.47 ? 347 ASN B ND2   1 
ATOM   12119 N  ND2   B ASN B 2 347 ? 15.080  -12.314 26.981  0.50 35.56 ? 347 ASN B ND2   1 
ATOM   12120 N  N     A ASN B 2 348 ? 19.440  -11.693 25.009  0.50 30.26 ? 348 ASN B N     1 
ATOM   12121 N  N     B ASN B 2 348 ? 19.745  -11.411 25.172  0.50 28.23 ? 348 ASN B N     1 
ATOM   12122 C  CA    A ASN B 2 348 ? 19.793  -11.881 23.606  0.50 27.72 ? 348 ASN B CA    1 
ATOM   12123 C  CA    B ASN B 2 348 ? 20.033  -11.670 23.766  0.50 29.02 ? 348 ASN B CA    1 
ATOM   12124 C  C     A ASN B 2 348 ? 20.035  -13.337 23.237  0.50 30.41 ? 348 ASN B C     1 
ATOM   12125 C  C     B ASN B 2 348 ? 20.402  -13.124 23.486  0.50 28.69 ? 348 ASN B C     1 
ATOM   12126 O  O     A ASN B 2 348 ? 20.375  -13.619 22.083  0.50 27.91 ? 348 ASN B O     1 
ATOM   12127 O  O     B ASN B 2 348 ? 21.043  -13.404 22.468  0.50 32.99 ? 348 ASN B O     1 
ATOM   12128 C  CB    A ASN B 2 348 ? 21.028  -11.041 23.246  0.50 26.05 ? 348 ASN B CB    1 
ATOM   12129 C  CB    B ASN B 2 348 ? 21.144  -10.738 23.276  0.50 25.65 ? 348 ASN B CB    1 
ATOM   12130 C  CG    A ASN B 2 348 ? 22.291  -11.512 23.939  0.50 25.17 ? 348 ASN B CG    1 
ATOM   12131 C  CG    B ASN B 2 348 ? 22.407  -10.841 24.106  0.50 26.48 ? 348 ASN B CG    1 
ATOM   12132 O  OD1   A ASN B 2 348 ? 22.248  -12.290 24.891  0.50 30.30 ? 348 ASN B OD1   1 
ATOM   12133 O  OD1   B ASN B 2 348 ? 22.402  -11.390 25.209  0.50 26.88 ? 348 ASN B OD1   1 
ATOM   12134 N  ND2   A ASN B 2 348 ? 23.433  -11.023 23.466  0.50 29.30 ? 348 ASN B ND2   1 
ATOM   12135 N  ND2   B ASN B 2 348 ? 23.500  -10.298 23.581  0.50 26.71 ? 348 ASN B ND2   1 
ATOM   12136 N  N     A VAL B 2 349 ? 19.853  -14.266 24.170  0.50 27.35 ? 349 VAL B N     1 
ATOM   12137 N  N     B VAL B 2 349 ? 20.003  -14.055 24.349  0.50 26.35 ? 349 VAL B N     1 
ATOM   12138 C  CA    A VAL B 2 349 ? 19.949  -15.695 23.896  0.50 25.43 ? 349 VAL B CA    1 
ATOM   12139 C  CA    B VAL B 2 349 ? 20.289  -15.478 24.162  0.50 28.04 ? 349 VAL B CA    1 
ATOM   12140 C  C     A VAL B 2 349 ? 18.568  -16.307 24.082  0.50 34.96 ? 349 VAL B C     1 
ATOM   12141 C  C     B VAL B 2 349 ? 18.997  -16.255 24.374  0.50 34.02 ? 349 VAL B C     1 
ATOM   12142 O  O     A VAL B 2 349 ? 17.889  -16.034 25.081  0.50 27.41 ? 349 VAL B O     1 
ATOM   12143 O  O     B VAL B 2 349 ? 18.500  -16.343 25.504  0.50 27.17 ? 349 VAL B O     1 
ATOM   12144 C  CB    A VAL B 2 349 ? 20.987  -16.374 24.804  0.50 29.93 ? 349 VAL B CB    1 
ATOM   12145 C  CB    B VAL B 2 349 ? 21.385  -15.982 25.109  0.50 30.95 ? 349 VAL B CB    1 
ATOM   12146 C  CG1   A VAL B 2 349 ? 21.083  -17.850 24.482  0.50 29.34 ? 349 VAL B CG1   1 
ATOM   12147 C  CG1   B VAL B 2 349 ? 21.571  -17.477 24.942  0.50 29.17 ? 349 VAL B CG1   1 
ATOM   12148 C  CG2   A VAL B 2 349 ? 22.342  -15.703 24.651  0.50 32.26 ? 349 VAL B CG2   1 
ATOM   12149 C  CG2   B VAL B 2 349 ? 22.686  -15.253 24.845  0.50 31.93 ? 349 VAL B CG2   1 
ATOM   12150 N  N     A LYS B 2 350 ? 18.150  -17.122 23.115  0.50 30.13 ? 350 LYS B N     1 
ATOM   12151 N  N     B LYS B 2 350 ? 18.464  -16.833 23.301  0.50 28.92 ? 350 LYS B N     1 
ATOM   12152 C  CA    A LYS B 2 350 ? 16.842  -17.762 23.131  0.50 32.65 ? 350 LYS B CA    1 
ATOM   12153 C  CA    B LYS B 2 350 ? 17.207  -17.568 23.342  0.50 32.41 ? 350 LYS B CA    1 
ATOM   12154 C  C     A LYS B 2 350 ? 17.002  -19.249 22.853  0.50 33.25 ? 350 LYS B C     1 
ATOM   12155 C  C     B LYS B 2 350 ? 17.471  -19.067 23.277  0.50 31.70 ? 350 LYS B C     1 
ATOM   12156 O  O     A LYS B 2 350 ? 17.741  -19.648 21.947  0.50 27.03 ? 350 LYS B O     1 
ATOM   12157 O  O     B LYS B 2 350 ? 18.336  -19.527 22.524  0.50 30.06 ? 350 LYS B O     1 
ATOM   12158 C  CB    A LYS B 2 350 ? 15.899  -17.131 22.096  0.50 28.76 ? 350 LYS B CB    1 
ATOM   12159 C  CB    B LYS B 2 350 ? 16.286  -17.146 22.191  0.50 30.32 ? 350 LYS B CB    1 
ATOM   12160 C  CG    A LYS B 2 350 ? 14.503  -17.730 22.074  0.50 36.91 ? 350 LYS B CG    1 
ATOM   12161 C  CG    B LYS B 2 350 ? 14.966  -17.900 22.119  0.50 34.30 ? 350 LYS B CG    1 
ATOM   12162 C  CD    A LYS B 2 350 ? 13.752  -17.437 23.369  0.50 32.07 ? 350 LYS B CD    1 
ATOM   12163 C  CD    B LYS B 2 350 ? 14.136  -17.703 23.386  0.50 33.32 ? 350 LYS B CD    1 
ATOM   12164 C  CE    A LYS B 2 350 ? 12.332  -17.971 23.306  0.50 40.66 ? 350 LYS B CE    1 
ATOM   12165 C  CE    B LYS B 2 350 ? 12.750  -18.305 23.235  0.50 40.22 ? 350 LYS B CE    1 
ATOM   12166 N  NZ    A LYS B 2 350 ? 12.314  -19.450 23.114  0.50 43.63 ? 350 LYS B NZ    1 
ATOM   12167 N  NZ    B LYS B 2 350 ? 11.935  -18.158 24.477  0.50 38.88 ? 350 LYS B NZ    1 
ATOM   12168 N  N     A THR B 2 351 ? 16.294  -20.064 23.628  0.50 29.68 ? 351 THR B N     1 
ATOM   12169 N  N     B THR B 2 351 ? 16.714  -19.821 24.069  0.50 31.79 ? 351 THR B N     1 
ATOM   12170 C  CA    A THR B 2 351 ? 16.426  -21.511 23.584  0.50 31.70 ? 351 THR B CA    1 
ATOM   12171 C  CA    B THR B 2 351 ? 16.833  -21.270 24.157  0.50 29.74 ? 351 THR B CA    1 
ATOM   12172 C  C     A THR B 2 351 ? 15.080  -22.152 23.267  0.50 38.67 ? 351 THR B C     1 
ATOM   12173 C  C     B THR B 2 351 ? 15.525  -21.907 23.711  0.50 39.31 ? 351 THR B C     1 
ATOM   12174 O  O     A THR B 2 351 ? 14.023  -21.643 23.651  0.50 34.85 ? 351 THR B O     1 
ATOM   12175 O  O     B THR B 2 351 ? 14.445  -21.479 24.135  0.50 35.90 ? 351 THR B O     1 
ATOM   12176 C  CB    A THR B 2 351 ? 16.959  -22.054 24.920  0.50 34.08 ? 351 THR B CB    1 
ATOM   12177 C  CB    B THR B 2 351 ? 17.179  -21.704 25.588  0.50 38.00 ? 351 THR B CB    1 
ATOM   12178 O  OG1   A THR B 2 351 ? 18.093  -21.283 25.333  0.50 43.85 ? 351 THR B OG1   1 
ATOM   12179 O  OG1   B THR B 2 351 ? 18.541  -21.367 25.877  0.50 45.66 ? 351 THR B OG1   1 
ATOM   12180 C  CG2   A THR B 2 351 ? 17.373  -23.512 24.790  0.50 30.93 ? 351 THR B CG2   1 
ATOM   12181 C  CG2   B THR B 2 351 ? 16.981  -23.200 25.764  0.50 38.66 ? 351 THR B CG2   1 
ATOM   12182 N  N     A ALA B 2 352 ? 15.133  -23.272 22.549  0.50 41.17 ? 352 ALA B N     1 
ATOM   12183 N  N     B ALA B 2 352 ? 15.624  -22.923 22.854  0.50 39.31 ? 352 ALA B N     1 
ATOM   12184 C  CA    A ALA B 2 352 ? 13.967  -24.099 22.288  0.50 39.66 ? 352 ALA B CA    1 
ATOM   12185 C  CA    B ALA B 2 352 ? 14.467  -23.658 22.366  0.50 39.46 ? 352 ALA B CA    1 
ATOM   12186 C  C     A ALA B 2 352 ? 14.394  -25.558 22.297  0.50 43.01 ? 352 ALA B C     1 
ATOM   12187 C  C     B ALA B 2 352 ? 14.705  -25.151 22.535  0.50 41.06 ? 352 ALA B C     1 
ATOM   12188 O  O     A ALA B 2 352 ? 15.507  -25.895 21.884  0.50 33.78 ? 352 ALA B O     1 
ATOM   12189 O  O     B ALA B 2 352 ? 15.847  -25.618 22.527  0.50 36.09 ? 352 ALA B O     1 
ATOM   12190 C  CB    A ALA B 2 352 ? 13.303  -23.753 20.953  0.50 39.40 ? 352 ALA B CB    1 
ATOM   12191 C  CB    B ALA B 2 352 ? 14.177  -23.344 20.897  0.50 37.56 ? 352 ALA B CB    1 
ATOM   12192 N  N     A VAL B 2 353 ? 13.502  -26.421 22.776  0.50 35.99 ? 353 VAL B N     1 
ATOM   12193 N  N     B VAL B 2 353 ? 13.613  -25.900 22.686  0.50 39.11 ? 353 VAL B N     1 
ATOM   12194 C  CA    A VAL B 2 353 ? 13.772  -27.848 22.892  0.50 38.09 ? 353 VAL B CA    1 
ATOM   12195 C  CA    B VAL B 2 353 ? 13.689  -27.342 22.870  0.50 38.04 ? 353 VAL B CA    1 
ATOM   12196 C  C     A VAL B 2 353 ? 12.781  -28.610 22.020  0.50 42.65 ? 353 VAL B C     1 
ATOM   12197 C  C     B VAL B 2 353 ? 12.735  -28.028 21.901  0.50 43.55 ? 353 VAL B C     1 
ATOM   12198 O  O     A VAL B 2 353 ? 11.587  -28.291 21.993  0.50 45.43 ? 353 VAL B O     1 
ATOM   12199 O  O     B VAL B 2 353 ? 11.724  -27.458 21.476  0.50 47.97 ? 353 VAL B O     1 
ATOM   12200 C  CB    A VAL B 2 353 ? 13.700  -28.315 24.361  0.50 38.95 ? 353 VAL B CB    1 
ATOM   12201 C  CB    B VAL B 2 353 ? 13.379  -27.748 24.329  0.50 41.32 ? 353 VAL B CB    1 
ATOM   12202 C  CG1   A VAL B 2 353 ? 14.802  -27.659 25.177  0.50 38.74 ? 353 VAL B CG1   1 
ATOM   12203 C  CG1   B VAL B 2 353 ? 11.880  -27.713 24.587  0.50 45.98 ? 353 VAL B CG1   1 
ATOM   12204 C  CG2   A VAL B 2 353 ? 12.347  -27.982 24.960  0.50 47.54 ? 353 VAL B CG2   1 
ATOM   12205 C  CG2   B VAL B 2 353 ? 13.959  -29.121 24.643  0.50 41.42 ? 353 VAL B CG2   1 
ATOM   12206 N  N     A CYS B 2 354 ? 13.282  -29.606 21.295  0.50 37.59 ? 354 CYS B N     1 
ATOM   12207 N  N     B CYS B 2 354 ? 13.081  -29.260 21.535  0.50 39.17 ? 354 CYS B N     1 
ATOM   12208 C  CA    A CYS B 2 354 ? 12.461  -30.424 20.414  0.50 42.51 ? 354 CYS B CA    1 
ATOM   12209 C  CA    B CYS B 2 354 ? 12.216  -30.110 20.729  0.50 41.05 ? 354 CYS B CA    1 
ATOM   12210 C  C     A CYS B 2 354 ? 12.545  -31.881 20.845  0.50 45.75 ? 354 CYS B C     1 
ATOM   12211 C  C     B CYS B 2 354 ? 12.504  -31.554 21.107  0.50 46.02 ? 354 CYS B C     1 
ATOM   12212 O  O     A CYS B 2 354 ? 13.612  -32.361 21.241  0.50 43.42 ? 354 CYS B O     1 
ATOM   12213 O  O     B CYS B 2 354 ? 13.667  -31.962 21.144  0.50 41.85 ? 354 CYS B O     1 
ATOM   12214 C  CB    A CYS B 2 354 ? 12.895  -30.281 18.951  0.50 45.44 ? 354 CYS B CB    1 
ATOM   12215 C  CB    B CYS B 2 354 ? 12.443  -29.888 19.230  0.50 45.76 ? 354 CYS B CB    1 
ATOM   12216 S  SG    A CYS B 2 354 ? 11.877  -31.216 17.784  0.50 46.87 ? 354 CYS B SG    1 
ATOM   12217 S  SG    B CYS B 2 354 ? 11.457  -30.971 18.170  0.50 46.55 ? 354 CYS B SG    1 
ATOM   12218 N  N     A ASP B 2 355 ? 11.411  -32.582 20.760  0.50 44.16 ? 355 ASP B N     1 
ATOM   12219 N  N     B ASP B 2 355 ? 11.450  -32.318 21.395  0.50 43.86 ? 355 ASP B N     1 
ATOM   12220 C  CA    A ASP B 2 355 ? 11.332  -33.952 21.254  0.50 42.06 ? 355 ASP B CA    1 
ATOM   12221 C  CA    B ASP B 2 355 ? 11.620  -33.677 21.892  0.50 41.05 ? 355 ASP B CA    1 
ATOM   12222 C  C     A ASP B 2 355 ? 12.010  -34.942 20.316  0.50 42.96 ? 355 ASP B C     1 
ATOM   12223 C  C     B ASP B 2 355 ? 11.979  -34.680 20.803  0.50 44.16 ? 355 ASP B C     1 
ATOM   12224 O  O     A ASP B 2 355 ? 12.687  -35.869 20.776  0.50 43.12 ? 355 ASP B O     1 
ATOM   12225 O  O     B ASP B 2 355 ? 12.289  -35.831 21.129  0.50 46.13 ? 355 ASP B O     1 
ATOM   12226 C  CB    A ASP B 2 355 ? 9.871   -34.352 21.459  0.50 40.28 ? 355 ASP B CB    1 
ATOM   12227 C  CB    B ASP B 2 355 ? 10.349  -34.135 22.612  0.50 44.10 ? 355 ASP B CB    1 
ATOM   12228 C  CG    A ASP B 2 355 ? 9.183   -33.519 22.517  0.50 41.60 ? 355 ASP B CG    1 
ATOM   12229 C  CG    B ASP B 2 355 ? 10.134  -33.413 23.926  0.50 47.25 ? 355 ASP B CG    1 
ATOM   12230 O  OD1   A ASP B 2 355 ? 9.872   -32.720 23.185  0.50 44.78 ? 355 ASP B OD1   1 
ATOM   12231 O  OD1   B ASP B 2 355 ? 11.122  -32.873 24.473  0.50 46.28 ? 355 ASP B OD1   1 
ATOM   12232 O  OD2   A ASP B 2 355 ? 7.954   -33.659 22.679  0.50 54.50 ? 355 ASP B OD2   1 
ATOM   12233 O  OD2   B ASP B 2 355 ? 8.983   -33.391 24.414  0.50 46.04 ? 355 ASP B OD2   1 
ATOM   12234 N  N     A ILE B 2 356 ? 11.836  -34.775 19.009  0.50 42.24 ? 356 ILE B N     1 
ATOM   12235 N  N     B ILE B 2 356 ? 11.949  -34.284 19.535  0.50 41.47 ? 356 ILE B N     1 
ATOM   12236 C  CA    A ILE B 2 356 ? 12.284  -35.757 18.026  0.50 47.79 ? 356 ILE B CA    1 
ATOM   12237 C  CA    B ILE B 2 356 ? 12.270  -35.197 18.441  0.50 45.16 ? 356 ILE B CA    1 
ATOM   12238 C  C     A ILE B 2 356 ? 13.707  -35.389 17.606  0.50 44.57 ? 356 ILE B C     1 
ATOM   12239 C  C     B ILE B 2 356 ? 13.692  -34.927 17.962  0.50 44.20 ? 356 ILE B C     1 
ATOM   12240 O  O     A ILE B 2 356 ? 13.895  -34.361 16.934  0.50 48.94 ? 356 ILE B O     1 
ATOM   12241 O  O     B ILE B 2 356 ? 13.927  -33.948 17.239  0.50 48.22 ? 356 ILE B O     1 
ATOM   12242 C  CB    A ILE B 2 356 ? 11.335  -35.821 16.822  0.50 45.93 ? 356 ILE B CB    1 
ATOM   12243 C  CB    B ILE B 2 356 ? 11.259  -35.065 17.291  0.50 41.62 ? 356 ILE B CB    1 
ATOM   12244 C  CG1   A ILE B 2 356 ? 11.973  -36.602 15.668  0.50 43.21 ? 356 ILE B CG1   1 
ATOM   12245 C  CG1   B ILE B 2 356 ? 9.844   -35.349 17.799  0.50 44.69 ? 356 ILE B CG1   1 
ATOM   12246 C  CG2   A ILE B 2 356 ? 10.887  -34.425 16.400  0.50 41.97 ? 356 ILE B CG2   1 
ATOM   12247 C  CG2   B ILE B 2 356 ? 11.617  -36.014 16.153  0.50 44.88 ? 356 ILE B CG2   1 
ATOM   12248 C  CD1   A ILE B 2 356 ? 12.249  -38.057 15.991  0.50 45.52 ? 356 ILE B CD1   1 
ATOM   12249 C  CD1   B ILE B 2 356 ? 8.790   -35.297 16.721  0.50 43.67 ? 356 ILE B CD1   1 
ATOM   12250 N  N     A PRO B 2 357 ? 14.716  -36.170 17.979  0.50 46.46 ? 357 PRO B N     1 
ATOM   12251 N  N     B PRO B 2 357 ? 14.666  -35.751 18.340  0.50 44.43 ? 357 PRO B N     1 
ATOM   12252 C  CA    A PRO B 2 357 ? 16.082  -35.896 17.528  0.50 46.35 ? 357 PRO B CA    1 
ATOM   12253 C  CA    B PRO B 2 357 ? 16.039  -35.543 17.880  0.50 47.11 ? 357 PRO B CA    1 
ATOM   12254 C  C     A PRO B 2 357 ? 16.260  -36.319 16.082  0.50 47.37 ? 357 PRO B C     1 
ATOM   12255 C  C     B PRO B 2 357 ? 16.267  -36.222 16.543  0.50 45.95 ? 357 PRO B C     1 
ATOM   12256 O  O     A PRO B 2 357 ? 15.369  -36.962 15.506  0.50 48.26 ? 357 PRO B O     1 
ATOM   12257 O  O     B PRO B 2 357 ? 15.478  -37.091 16.141  0.50 44.81 ? 357 PRO B O     1 
ATOM   12258 C  CB    A PRO B 2 357 ? 16.936  -36.752 18.474  0.50 47.33 ? 357 PRO B CB    1 
ATOM   12259 C  CB    B PRO B 2 357 ? 16.873  -36.199 18.988  0.50 48.95 ? 357 PRO B CB    1 
ATOM   12260 C  CG    A PRO B 2 357 ? 16.053  -37.895 18.824  0.50 47.24 ? 357 PRO B CG    1 
ATOM   12261 C  CG    B PRO B 2 357 ? 16.008  -37.329 19.448  0.50 47.95 ? 357 PRO B CG    1 
ATOM   12262 C  CD    A PRO B 2 357 ? 14.650  -37.344 18.869  0.50 44.77 ? 357 PRO B CD    1 
ATOM   12263 C  CD    B PRO B 2 357 ? 14.573  -36.862 19.305  0.50 42.55 ? 357 PRO B CD    1 
ATOM   12264 N  N     A PRO B 2 358 ? 17.396  -35.977 15.447  0.50 45.57 ? 358 PRO B N     1 
ATOM   12265 N  N     B PRO B 2 358 ? 17.330  -35.856 15.823  0.50 46.12 ? 358 PRO B N     1 
ATOM   12266 C  CA    A PRO B 2 358 ? 17.625  -36.439 14.071  0.50 46.64 ? 358 PRO B CA    1 
ATOM   12267 C  CA    B PRO B 2 358 ? 17.632  -36.536 14.559  0.50 47.06 ? 358 PRO B CA    1 
ATOM   12268 C  C     A PRO B 2 358 ? 17.946  -37.924 14.002  0.50 49.48 ? 358 PRO B C     1 
ATOM   12269 C  C     B PRO B 2 358 ? 17.958  -38.006 14.785  0.50 49.57 ? 358 PRO B C     1 
ATOM   12270 O  O     A PRO B 2 358 ? 17.558  -38.696 14.884  0.50 50.02 ? 358 PRO B O     1 
ATOM   12271 O  O     B PRO B 2 358 ? 18.279  -38.437 15.895  0.50 46.95 ? 358 PRO B O     1 
ATOM   12272 C  CB    A PRO B 2 358 ? 18.811  -35.583 13.608  0.50 49.14 ? 358 PRO B CB    1 
ATOM   12273 C  CB    B PRO B 2 358 ? 18.852  -35.775 14.022  0.50 49.31 ? 358 PRO B CB    1 
ATOM   12274 C  CG    A PRO B 2 358 ? 19.542  -35.264 14.863  0.50 45.88 ? 358 PRO B CG    1 
ATOM   12275 C  CG    B PRO B 2 358 ? 18.849  -34.468 14.748  0.50 46.98 ? 358 PRO B CG    1 
ATOM   12276 C  CD    A PRO B 2 358 ? 18.481  -35.094 15.914  0.50 46.95 ? 358 PRO B CD    1 
ATOM   12277 C  CD    B PRO B 2 358 ? 18.269  -34.755 16.096  0.50 47.13 ? 358 PRO B CD    1 
ATOM   12278 N  N     A ARG B 2 359 ? 18.660  -38.332 12.958  0.50 54.96 ? 359 ARG B N     1 
ATOM   12279 N  N     B ARG B 2 359 ? 17.869  -38.779 13.706  0.50 51.39 ? 359 ARG B N     1 
ATOM   12280 C  CA    A ARG B 2 359 ? 18.987  -39.735 12.762  0.50 51.70 ? 359 ARG B CA    1 
ATOM   12281 C  CA    B ARG B 2 359 ? 18.148  -40.207 13.783  0.50 51.60 ? 359 ARG B CA    1 
ATOM   12282 C  C     A ARG B 2 359 ? 20.206  -40.128 13.591  0.50 53.61 ? 359 ARG B C     1 
ATOM   12283 C  C     B ARG B 2 359 ? 19.627  -40.448 14.062  0.50 52.12 ? 359 ARG B C     1 
ATOM   12284 O  O     A ARG B 2 359 ? 20.981  -39.283 14.046  0.50 50.33 ? 359 ARG B O     1 
ATOM   12285 O  O     B ARG B 2 359 ? 20.496  -39.722 13.571  0.50 53.58 ? 359 ARG B O     1 
ATOM   12286 C  CB    A ARG B 2 359 ? 19.252  -40.031 11.285  0.50 57.76 ? 359 ARG B CB    1 
ATOM   12287 C  CB    B ARG B 2 359 ? 17.733  -40.902 12.485  0.50 58.63 ? 359 ARG B CB    1 
ATOM   12288 C  CG    A ARG B 2 359 ? 20.657  -39.667 10.818  0.50 59.71 ? 359 ARG B CG    1 
ATOM   12289 C  CG    B ARG B 2 359 ? 17.869  -42.419 12.517  0.50 56.26 ? 359 ARG B CG    1 
ATOM   12290 C  CD    A ARG B 2 359 ? 20.840  -38.162 10.698  0.50 59.40 ? 359 ARG B CD    1 
ATOM   12291 C  CD    B ARG B 2 359 ? 17.207  -43.069 11.310  0.50 58.30 ? 359 ARG B CD    1 
ATOM   12292 N  NE    A ARG B 2 359 ? 22.244  -37.771 10.725  0.50 61.73 ? 359 ARG B NE    1 
ATOM   12293 N  NE    B ARG B 2 359 ? 17.354  -44.520 11.321  0.50 56.30 ? 359 ARG B NE    1 
ATOM   12294 C  CZ    A ARG B 2 359 ? 22.938  -37.557 11.835  0.50 60.04 ? 359 ARG B CZ    1 
ATOM   12295 C  CZ    B ARG B 2 359 ? 16.621  -45.341 12.061  0.50 57.18 ? 359 ARG B CZ    1 
ATOM   12296 N  NH1   A ARG B 2 359 ? 22.392  -37.708 13.031  0.50 50.01 ? 359 ARG B NH1   1 
ATOM   12297 N  NH1   B ARG B 2 359 ? 15.683  -44.886 12.876  0.50 61.81 ? 359 ARG B NH1   1 
ATOM   12298 N  NH2   A ARG B 2 359 ? 24.210  -37.180 11.743  0.50 48.76 ? 359 ARG B NH2   1 
ATOM   12299 N  NH2   B ARG B 2 359 ? 16.834  -46.652 11.982  0.50 39.34 ? 359 ARG B NH2   1 
ATOM   12300 N  N     A GLY B 2 360 ? 20.366  -41.437 13.780  0.50 55.28 ? 360 GLY B N     1 
ATOM   12301 N  N     B GLY B 2 360 ? 19.909  -41.475 14.865  0.50 54.19 ? 360 GLY B N     1 
ATOM   12302 C  CA    A GLY B 2 360 ? 21.502  -41.982 14.499  0.50 54.86 ? 360 GLY B CA    1 
ATOM   12303 C  CA    B GLY B 2 360 ? 21.265  -41.795 15.256  0.50 52.39 ? 360 GLY B CA    1 
ATOM   12304 C  C     A GLY B 2 360 ? 21.644  -41.474 15.919  0.50 52.12 ? 360 GLY B C     1 
ATOM   12305 C  C     B GLY B 2 360 ? 21.806  -40.987 16.413  0.50 53.10 ? 360 GLY B C     1 
ATOM   12306 O  O     A GLY B 2 360 ? 21.473  -42.230 16.880  0.50 49.20 ? 360 GLY B O     1 
ATOM   12307 O  O     B GLY B 2 360 ? 22.910  -41.282 16.892  0.50 45.99 ? 360 GLY B O     1 
ATOM   12308 N  N     A LEU B 2 361 ? 21.956  -40.187 16.056  0.50 52.13 ? 361 LEU B N     1 
ATOM   12309 N  N     B LEU B 2 361 ? 21.074  -39.977 16.880  0.50 51.58 ? 361 LEU B N     1 
ATOM   12310 C  CA    A LEU B 2 361 ? 22.166  -39.581 17.361  0.50 52.23 ? 361 LEU B CA    1 
ATOM   12311 C  CA    B LEU B 2 361 ? 21.486  -39.156 18.009  0.50 51.06 ? 361 LEU B CA    1 
ATOM   12312 C  C     A LEU B 2 361 ? 20.886  -39.619 18.192  0.50 50.97 ? 361 LEU B C     1 
ATOM   12313 C  C     B LEU B 2 361 ? 20.364  -39.137 19.033  0.50 49.39 ? 361 LEU B C     1 
ATOM   12314 O  O     A LEU B 2 361 ? 19.774  -39.750 17.672  0.50 50.83 ? 361 LEU B O     1 
ATOM   12315 O  O     B LEU B 2 361 ? 19.197  -38.946 18.677  0.50 52.19 ? 361 LEU B O     1 
ATOM   12316 C  CB    A LEU B 2 361 ? 22.640  -38.137 17.202  0.50 53.97 ? 361 LEU B CB    1 
ATOM   12317 C  CB    B LEU B 2 361 ? 21.822  -37.728 17.566  0.50 51.81 ? 361 LEU B CB    1 
ATOM   12318 C  CG    A LEU B 2 361 ? 23.768  -37.904 16.195  0.50 51.39 ? 361 LEU B CG    1 
ATOM   12319 C  CG    B LEU B 2 361 ? 22.931  -37.560 16.523  0.50 51.54 ? 361 LEU B CG    1 
ATOM   12320 C  CD1   A LEU B 2 361 ? 23.896  -36.426 15.862  0.50 51.83 ? 361 LEU B CD1   1 
ATOM   12321 C  CD1   B LEU B 2 361 ? 23.031  -36.108 16.082  0.50 47.74 ? 361 LEU B CD1   1 
ATOM   12322 C  CD2   A LEU B 2 361 ? 25.084  -38.450 16.730  0.50 46.66 ? 361 LEU B CD2   1 
ATOM   12323 C  CD2   B LEU B 2 361 ? 24.264  -38.050 17.068  0.50 50.30 ? 361 LEU B CD2   1 
ATOM   12324 N  N     A LYS B 2 362 ? 21.060  -39.508 19.508  0.50 50.00 ? 362 LYS B N     1 
ATOM   12325 N  N     B LYS B 2 362 ? 20.715  -39.343 20.300  0.50 50.72 ? 362 LYS B N     1 
ATOM   12326 C  CA    A LYS B 2 362 ? 19.945  -39.373 20.436  0.50 51.52 ? 362 LYS B CA    1 
ATOM   12327 C  CA    B LYS B 2 362 ? 19.728  -39.247 21.366  0.50 51.12 ? 362 LYS B CA    1 
ATOM   12328 C  C     A LYS B 2 362 ? 19.817  -37.974 21.011  0.50 52.79 ? 362 LYS B C     1 
ATOM   12329 C  C     B LYS B 2 362 ? 19.572  -37.825 21.881  0.50 52.02 ? 362 LYS B C     1 
ATOM   12330 O  O     A LYS B 2 362 ? 18.701  -37.539 21.303  0.50 54.32 ? 362 LYS B O     1 
ATOM   12331 O  O     B LYS B 2 362 ? 18.505  -37.477 22.399  0.50 52.50 ? 362 LYS B O     1 
ATOM   12332 C  CB    A LYS B 2 362 ? 20.081  -40.376 21.590  0.50 57.20 ? 362 LYS B CB    1 
ATOM   12333 C  CB    B LYS B 2 362 ? 20.096  -40.186 22.519  0.50 56.03 ? 362 LYS B CB    1 
ATOM   12334 C  CG    A LYS B 2 362 ? 18.767  -40.704 22.288  0.50 58.57 ? 362 LYS B CG    1 
ATOM   12335 C  CG    B LYS B 2 362 ? 20.128  -41.657 22.120  0.50 56.50 ? 362 LYS B CG    1 
ATOM   12336 C  CD    A LYS B 2 362 ? 18.973  -41.711 23.410  0.50 59.69 ? 362 LYS B CD    1 
ATOM   12337 C  CD    B LYS B 2 362 ? 20.035  -42.571 23.333  0.50 62.75 ? 362 LYS B CD    1 
ATOM   12338 C  CE    A LYS B 2 362 ? 17.656  -42.343 23.842  0.50 61.45 ? 362 LYS B CE    1 
ATOM   12339 C  CE    B LYS B 2 362 ? 18.660  -42.501 23.980  0.50 60.62 ? 362 LYS B CE    1 
ATOM   12340 N  NZ    A LYS B 2 362 ? 16.673  -41.339 24.339  0.50 52.18 ? 362 LYS B NZ    1 
ATOM   12341 N  NZ    B LYS B 2 362 ? 17.584  -42.987 23.068  0.50 59.05 ? 362 LYS B NZ    1 
ATOM   12342 N  N     A MET B 2 363 ? 20.930  -37.265 21.178  0.50 45.40 ? 363 MET B N     1 
ATOM   12343 N  N     B MET B 2 363 ? 20.603  -36.994 21.735  0.50 48.96 ? 363 MET B N     1 
ATOM   12344 C  CA    A MET B 2 363 ? 20.944  -35.869 21.583  0.50 49.82 ? 363 MET B CA    1 
ATOM   12345 C  CA    B MET B 2 363 ? 20.534  -35.592 22.117  0.50 47.94 ? 363 MET B CA    1 
ATOM   12346 C  C     A MET B 2 363 ? 21.354  -35.002 20.399  0.50 47.35 ? 363 MET B C     1 
ATOM   12347 C  C     B MET B 2 363 ? 21.519  -34.798 21.272  0.50 48.73 ? 363 MET B C     1 
ATOM   12348 O  O     A MET B 2 363 ? 22.052  -35.458 19.488  0.50 40.55 ? 363 MET B O     1 
ATOM   12349 O  O     B MET B 2 363 ? 22.626  -35.265 20.988  0.50 42.08 ? 363 MET B O     1 
ATOM   12350 C  CB    A MET B 2 363 ? 21.910  -35.638 22.751  0.50 49.90 ? 363 MET B CB    1 
ATOM   12351 C  CB    B MET B 2 363 ? 20.825  -35.397 23.610  0.50 48.60 ? 363 MET B CB    1 
ATOM   12352 C  CG    A MET B 2 363 ? 21.754  -36.605 23.915  0.50 50.52 ? 363 MET B CG    1 
ATOM   12353 C  CG    B MET B 2 363 ? 19.575  -35.424 24.480  0.50 53.62 ? 363 MET B CG    1 
ATOM   12354 S  SD    A MET B 2 363 ? 20.750  -35.966 25.271  0.50 59.93 ? 363 MET B SD    1 
ATOM   12355 S  SD    B MET B 2 363 ? 19.907  -35.627 26.238  0.50 61.53 ? 363 MET B SD    1 
ATOM   12356 C  CE    A MET B 2 363 ? 19.093  -36.159 24.618  0.50 50.40 ? 363 MET B CE    1 
ATOM   12357 C  CE    B MET B 2 363 ? 20.501  -37.317 26.275  0.50 60.10 ? 363 MET B CE    1 
ATOM   12358 N  N     A SER B 2 364 ? 20.915  -33.746 20.417  0.50 46.28 ? 364 SER B N     1 
ATOM   12359 N  N     B SER B 2 364 ? 21.103  -33.600 20.870  0.50 46.60 ? 364 SER B N     1 
ATOM   12360 C  CA    A SER B 2 364 ? 21.252  -32.814 19.352  0.50 44.69 ? 364 SER B CA    1 
ATOM   12361 C  CA    B SER B 2 364 ? 21.914  -32.756 20.007  0.50 44.38 ? 364 SER B CA    1 
ATOM   12362 C  C     A SER B 2 364 ? 21.274  -31.400 19.911  0.50 42.47 ? 364 SER B C     1 
ATOM   12363 C  C     B SER B 2 364 ? 21.451  -31.317 20.156  0.50 42.56 ? 364 SER B C     1 
ATOM   12364 O  O     A SER B 2 364 ? 20.527  -31.069 20.836  0.50 41.77 ? 364 SER B O     1 
ATOM   12365 O  O     B SER B 2 364 ? 20.290  -31.055 20.482  0.50 41.80 ? 364 SER B O     1 
ATOM   12366 C  CB    A SER B 2 364 ? 20.263  -32.909 18.185  0.50 43.53 ? 364 SER B CB    1 
ATOM   12367 C  CB    B SER B 2 364 ? 21.815  -33.192 18.541  0.50 42.84 ? 364 SER B CB    1 
ATOM   12368 O  OG    A SER B 2 364 ? 20.605  -32.011 17.144  0.50 47.84 ? 364 SER B OG    1 
ATOM   12369 O  OG    B SER B 2 364 ? 20.486  -33.059 18.067  0.50 44.27 ? 364 SER B OG    1 
ATOM   12370 N  N     A ALA B 2 365 ? 22.143  -30.570 19.338  0.50 41.36 ? 365 ALA B N     1 
ATOM   12371 N  N     B ALA B 2 365 ? 22.370  -30.390 19.911  0.50 38.47 ? 365 ALA B N     1 
ATOM   12372 C  CA    A ALA B 2 365 ? 22.277  -29.178 19.759  0.50 36.32 ? 365 ALA B CA    1 
ATOM   12373 C  CA    B ALA B 2 365 ? 22.072  -28.970 19.943  0.50 36.12 ? 365 ALA B CA    1 
ATOM   12374 C  C     A ALA B 2 365 ? 22.763  -28.376 18.562  0.50 39.61 ? 365 ALA B C     1 
ATOM   12375 C  C     B ALA B 2 365 ? 22.333  -28.363 18.573  0.50 39.75 ? 365 ALA B C     1 
ATOM   12376 O  O     A ALA B 2 365 ? 23.900  -28.559 18.115  0.50 33.35 ? 365 ALA B O     1 
ATOM   12377 O  O     B ALA B 2 365 ? 23.014  -28.951 17.727  0.50 35.93 ? 365 ALA B O     1 
ATOM   12378 C  CB    A ALA B 2 365 ? 23.238  -29.047 20.937  0.50 44.54 ? 365 ALA B CB    1 
ATOM   12379 C  CB    B ALA B 2 365 ? 22.904  -28.246 21.009  0.50 41.40 ? 365 ALA B CB    1 
ATOM   12380 N  N     A THR B 2 366 ? 21.908  -27.498 18.047  0.50 36.67 ? 366 THR B N     1 
ATOM   12381 N  N     B THR B 2 366 ? 21.770  -27.179 18.358  0.50 36.70 ? 366 THR B N     1 
ATOM   12382 C  CA    A THR B 2 366 ? 22.228  -26.652 16.906  0.50 34.53 ? 366 THR B CA    1 
ATOM   12383 C  CA    B THR B 2 366 ? 21.994  -26.426 17.133  0.50 36.29 ? 366 THR B CA    1 
ATOM   12384 C  C     A THR B 2 366 ? 22.265  -25.194 17.349  0.50 34.52 ? 366 THR B C     1 
ATOM   12385 C  C     B THR B 2 366 ? 22.154  -24.959 17.496  0.50 34.49 ? 366 THR B C     1 
ATOM   12386 O  O     A THR B 2 366 ? 21.404  -24.743 18.112  0.50 33.80 ? 366 THR B O     1 
ATOM   12387 O  O     B THR B 2 366 ? 21.321  -24.397 18.212  0.50 34.65 ? 366 THR B O     1 
ATOM   12388 C  CB    A THR B 2 366 ? 21.209  -26.849 15.778  0.50 34.13 ? 366 THR B CB    1 
ATOM   12389 C  CB    B THR B 2 366 ? 20.847  -26.611 16.135  0.50 35.20 ? 366 THR B CB    1 
ATOM   12390 O  OG1   A THR B 2 366 ? 21.220  -28.219 15.359  0.50 33.79 ? 366 THR B OG1   1 
ATOM   12391 O  OG1   B THR B 2 366 ? 20.654  -28.007 15.888  0.50 38.34 ? 366 THR B OG1   1 
ATOM   12392 C  CG2   A THR B 2 366 ? 21.540  -25.966 14.584  0.50 31.61 ? 366 THR B CG2   1 
ATOM   12393 C  CG2   B THR B 2 366 ? 21.175  -25.918 14.823  0.50 31.41 ? 366 THR B CG2   1 
ATOM   12394 N  N     A PHE B 2 367 ? 23.269  -24.466 16.867  0.50 33.98 ? 367 PHE B N     1 
ATOM   12395 N  N     B PHE B 2 367 ? 23.226  -24.353 17.000  0.50 33.67 ? 367 PHE B N     1 
ATOM   12396 C  CA    A PHE B 2 367 ? 23.563  -23.106 17.293  0.50 32.25 ? 367 PHE B CA    1 
ATOM   12397 C  CA    B PHE B 2 367 ? 23.632  -23.006 17.366  0.50 32.28 ? 367 PHE B CA    1 
ATOM   12398 C  C     A PHE B 2 367 ? 23.380  -22.147 16.123  0.50 29.06 ? 367 PHE B C     1 
ATOM   12399 C  C     B PHE B 2 367 ? 23.470  -22.087 16.162  0.50 29.11 ? 367 PHE B C     1 
ATOM   12400 O  O     A PHE B 2 367 ? 23.820  -22.431 15.005  0.50 31.18 ? 367 PHE B O     1 
ATOM   12401 O  O     B PHE B 2 367 ? 23.907  -22.423 15.057  0.50 31.27 ? 367 PHE B O     1 
ATOM   12402 C  CB    A PHE B 2 367 ? 24.997  -23.037 17.849  0.50 32.10 ? 367 PHE B CB    1 
ATOM   12403 C  CB    B PHE B 2 367 ? 25.084  -23.016 17.852  0.50 32.12 ? 367 PHE B CB    1 
ATOM   12404 C  CG    A PHE B 2 367 ? 25.609  -21.662 17.833  0.50 32.69 ? 367 PHE B CG    1 
ATOM   12405 C  CG    B PHE B 2 367 ? 25.562  -21.705 18.398  0.50 36.12 ? 367 PHE B CG    1 
ATOM   12406 C  CD1   A PHE B 2 367 ? 25.418  -20.789 18.891  0.50 34.00 ? 367 PHE B CD1   1 
ATOM   12407 C  CD1   B PHE B 2 367 ? 26.132  -20.759 17.566  0.50 31.97 ? 367 PHE B CD1   1 
ATOM   12408 C  CD2   A PHE B 2 367 ? 26.417  -21.262 16.781  0.50 33.56 ? 367 PHE B CD2   1 
ATOM   12409 C  CD2   B PHE B 2 367 ? 25.470  -21.429 19.752  0.50 39.12 ? 367 PHE B CD2   1 
ATOM   12410 C  CE1   A PHE B 2 367 ? 25.998  -19.533 18.884  0.50 35.13 ? 367 PHE B CE1   1 
ATOM   12411 C  CE1   B PHE B 2 367 ? 26.586  -19.555 18.072  0.50 35.85 ? 367 PHE B CE1   1 
ATOM   12412 C  CE2   A PHE B 2 367 ? 26.999  -20.008 16.768  0.50 30.80 ? 367 PHE B CE2   1 
ATOM   12413 C  CE2   B PHE B 2 367 ? 25.925  -20.227 20.264  0.50 37.34 ? 367 PHE B CE2   1 
ATOM   12414 C  CZ    A PHE B 2 367 ? 26.787  -19.143 17.820  0.50 35.48 ? 367 PHE B CZ    1 
ATOM   12415 C  CZ    B PHE B 2 367 ? 26.484  -19.290 19.423  0.50 34.60 ? 367 PHE B CZ    1 
ATOM   12416 N  N     A ILE B 2 368 ? 22.713  -21.022 16.377  0.50 29.80 ? 368 ILE B N     1 
ATOM   12417 N  N     B ILE B 2 368 ? 22.828  -20.941 16.372  0.50 29.90 ? 368 ILE B N     1 
ATOM   12418 C  CA    A ILE B 2 368 ? 22.560  -19.951 15.397  0.50 25.73 ? 368 ILE B CA    1 
ATOM   12419 C  CA    B ILE B 2 368 ? 22.688  -19.910 15.345  0.50 25.74 ? 368 ILE B CA    1 
ATOM   12420 C  C     A ILE B 2 368 ? 23.057  -18.667 16.041  0.50 30.26 ? 368 ILE B C     1 
ATOM   12421 C  C     B ILE B 2 368 ? 23.105  -18.596 15.992  0.50 30.33 ? 368 ILE B C     1 
ATOM   12422 O  O     A ILE B 2 368 ? 22.462  -18.189 17.013  0.50 31.31 ? 368 ILE B O     1 
ATOM   12423 O  O     B ILE B 2 368 ? 22.294  -17.935 16.647  0.50 28.54 ? 368 ILE B O     1 
ATOM   12424 C  CB    A ILE B 2 368 ? 21.107  -19.777 14.927  0.50 30.86 ? 368 ILE B CB    1 
ATOM   12425 C  CB    B ILE B 2 368 ? 21.267  -19.818 14.783  0.50 30.54 ? 368 ILE B CB    1 
ATOM   12426 C  CG1   A ILE B 2 368 ? 20.437  -21.131 14.692  0.50 34.64 ? 368 ILE B CG1   1 
ATOM   12427 C  CG1   B ILE B 2 368 ? 20.788  -21.185 14.290  0.50 34.45 ? 368 ILE B CG1   1 
ATOM   12428 C  CG2   A ILE B 2 368 ? 21.066  -18.924 13.660  0.50 28.44 ? 368 ILE B CG2   1 
ATOM   12429 C  CG2   B ILE B 2 368 ? 21.216  -18.792 13.651  0.50 27.89 ? 368 ILE B CG2   1 
ATOM   12430 C  CD1   A ILE B 2 368 ? 18.952  -21.030 14.403  0.50 30.39 ? 368 ILE B CD1   1 
ATOM   12431 C  CD1   B ILE B 2 368 ? 19.300  -21.242 14.002  0.50 32.64 ? 368 ILE B CD1   1 
ATOM   12432 N  N     A GLY B 2 369 ? 24.125  -18.102 15.499  0.50 27.78 ? 369 GLY B N     1 
ATOM   12433 N  N     B GLY B 2 369 ? 24.362  -18.206 15.804  0.50 27.31 ? 369 GLY B N     1 
ATOM   12434 C  CA    A GLY B 2 369 ? 24.767  -16.938 16.088  0.50 25.38 ? 369 GLY B CA    1 
ATOM   12435 C  CA    B GLY B 2 369 ? 24.907  -17.012 16.420  0.50 26.01 ? 369 GLY B CA    1 
ATOM   12436 C  C     A GLY B 2 369 ? 24.808  -15.752 15.146  0.50 25.33 ? 369 GLY B C     1 
ATOM   12437 C  C     B GLY B 2 369 ? 25.163  -15.925 15.389  0.50 26.82 ? 369 GLY B C     1 
ATOM   12438 O  O     A GLY B 2 369 ? 24.997  -15.912 13.938  0.50 22.64 ? 369 GLY B O     1 
ATOM   12439 O  O     B GLY B 2 369 ? 25.763  -16.178 14.342  0.50 22.34 ? 369 GLY B O     1 
ATOM   12440 N  N     A ASN B 2 370 ? 24.625  -14.562 15.710  0.50 24.85 ? 370 ASN B N     1 
ATOM   12441 N  N     B ASN B 2 370 ? 24.699  -14.719 15.706  0.50 24.91 ? 370 ASN B N     1 
ATOM   12442 C  CA    A ASN B 2 370 ? 24.916  -13.298 15.040  0.50 27.27 ? 370 ASN B CA    1 
ATOM   12443 C  CA    B ASN B 2 370 ? 25.048  -13.517 14.952  0.50 27.11 ? 370 ASN B CA    1 
ATOM   12444 C  C     A ASN B 2 370 ? 26.119  -12.717 15.784  0.50 28.10 ? 370 ASN B C     1 
ATOM   12445 C  C     B ASN B 2 370 ? 26.123  -12.791 15.756  0.50 28.08 ? 370 ASN B C     1 
ATOM   12446 O  O     A ASN B 2 370 ? 25.970  -11.993 16.771  0.50 25.85 ? 370 ASN B O     1 
ATOM   12447 O  O     B ASN B 2 370 ? 25.823  -12.092 16.727  0.50 25.58 ? 370 ASN B O     1 
ATOM   12448 C  CB    A ASN B 2 370 ? 23.703  -12.361 15.055  0.50 26.34 ? 370 ASN B CB    1 
ATOM   12449 C  CB    B ASN B 2 370 ? 23.822  -12.642 14.707  0.50 26.00 ? 370 ASN B CB    1 
ATOM   12450 C  CG    A ASN B 2 370 ? 23.816  -11.236 14.040  0.50 26.06 ? 370 ASN B CG    1 
ATOM   12451 C  CG    B ASN B 2 370 ? 24.105  -11.500 13.749  0.50 27.09 ? 370 ASN B CG    1 
ATOM   12452 O  OD1   A ASN B 2 370 ? 24.912  -10.801 13.691  0.50 29.94 ? 370 ASN B OD1   1 
ATOM   12453 O  OD1   B ASN B 2 370 ? 25.158  -11.458 13.113  0.50 26.98 ? 370 ASN B OD1   1 
ATOM   12454 N  ND2   A ASN B 2 370 ? 22.674  -10.760 13.562  0.50 26.00 ? 370 ASN B ND2   1 
ATOM   12455 N  ND2   B ASN B 2 370 ? 23.160  -10.574 13.631  0.50 27.22 ? 370 ASN B ND2   1 
ATOM   12456 N  N     A SER B 2 371 ? 27.316  -13.063 15.311  0.50 24.69 ? 371 SER B N     1 
ATOM   12457 N  N     B SER B 2 371 ? 27.380  -12.972 15.350  0.50 24.58 ? 371 SER B N     1 
ATOM   12458 C  CA    A SER B 2 371 ? 28.574  -12.773 15.987  0.50 26.28 ? 371 SER B CA    1 
ATOM   12459 C  CA    B SER B 2 371 ? 28.542  -12.474 16.073  0.50 26.28 ? 371 SER B CA    1 
ATOM   12460 C  C     A SER B 2 371 ? 29.401  -11.790 15.169  0.50 30.96 ? 371 SER B C     1 
ATOM   12461 C  C     B SER B 2 371 ? 29.398  -11.595 15.172  0.50 30.94 ? 371 SER B C     1 
ATOM   12462 O  O     A SER B 2 371 ? 29.508  -11.922 13.945  0.50 23.32 ? 371 SER B O     1 
ATOM   12463 O  O     B SER B 2 371 ? 29.499  -11.828 13.962  0.50 23.32 ? 371 SER B O     1 
ATOM   12464 C  CB    A SER B 2 371 ? 29.376  -14.061 16.207  0.50 24.06 ? 371 SER B CB    1 
ATOM   12465 C  CB    B SER B 2 371 ? 29.393  -13.631 16.604  0.50 27.28 ? 371 SER B CB    1 
ATOM   12466 O  OG    A SER B 2 371 ? 30.641  -13.799 16.792  0.50 27.30 ? 371 SER B OG    1 
ATOM   12467 O  OG    B SER B 2 371 ? 30.699  -13.192 16.938  0.50 28.78 ? 371 SER B OG    1 
ATOM   12468 N  N     A THR B 2 372 ? 30.001  -10.807 15.849  0.50 23.03 ? 372 THR B N     1 
ATOM   12469 N  N     B THR B 2 372 ? 30.031  -10.584 15.773  0.50 23.53 ? 372 THR B N     1 
ATOM   12470 C  CA    A THR B 2 372 ? 30.850  -9.858  15.135  0.50 23.86 ? 372 THR B CA    1 
ATOM   12471 C  CA    B THR B 2 372 ? 30.924  -9.735  14.992  0.50 23.47 ? 372 THR B CA    1 
ATOM   12472 C  C     A THR B 2 372 ? 32.112  -10.519 14.591  0.50 26.89 ? 372 THR B C     1 
ATOM   12473 C  C     B THR B 2 372 ? 32.186  -10.469 14.550  0.50 26.91 ? 372 THR B C     1 
ATOM   12474 O  O     A THR B 2 372 ? 32.764  -9.949  13.711  0.50 28.01 ? 372 THR B O     1 
ATOM   12475 O  O     B THR B 2 372 ? 32.894  -9.964  13.673  0.50 27.95 ? 372 THR B O     1 
ATOM   12476 C  CB    A THR B 2 372 ? 31.225  -8.676  16.036  0.50 27.05 ? 372 THR B CB    1 
ATOM   12477 C  CB    B THR B 2 372 ? 31.309  -8.475  15.777  0.50 26.85 ? 372 THR B CB    1 
ATOM   12478 O  OG1   A THR B 2 372 ? 32.201  -9.090  17.000  0.50 25.67 ? 372 THR B OG1   1 
ATOM   12479 O  OG1   B THR B 2 372 ? 32.158  -8.826  16.876  0.50 24.74 ? 372 THR B OG1   1 
ATOM   12480 C  CG2   A THR B 2 372 ? 29.988  -8.129  16.764  0.50 26.96 ? 372 THR B CG2   1 
ATOM   12481 C  CG2   B THR B 2 372 ? 30.066  -7.760  16.305  0.50 28.23 ? 372 THR B CG2   1 
ATOM   12482 N  N     A ALA B 2 373 ? 32.459  -11.714 15.081  0.50 28.58 ? 373 ALA B N     1 
ATOM   12483 N  N     B ALA B 2 373 ? 32.476  -11.643 15.122  0.50 28.54 ? 373 ALA B N     1 
ATOM   12484 C  CA    A ALA B 2 373 ? 33.628  -12.434 14.587  0.50 27.46 ? 373 ALA B CA    1 
ATOM   12485 C  CA    B ALA B 2 373 ? 33.636  -12.432 14.716  0.50 27.58 ? 373 ALA B CA    1 
ATOM   12486 C  C     A ALA B 2 373 ? 33.455  -12.946 13.164  0.50 30.55 ? 373 ALA B C     1 
ATOM   12487 C  C     B ALA B 2 373 ? 33.517  -12.983 13.302  0.50 30.58 ? 373 ALA B C     1 
ATOM   12488 O  O     A ALA B 2 373 ? 34.439  -13.399 12.569  0.50 28.39 ? 373 ALA B O     1 
ATOM   12489 O  O     B ALA B 2 373 ? 34.527  -13.430 12.747  0.50 28.70 ? 373 ALA B O     1 
ATOM   12490 C  CB    A ALA B 2 373 ? 33.960  -13.609 15.509  0.50 24.35 ? 373 ALA B CB    1 
ATOM   12491 C  CB    B ALA B 2 373 ? 33.860  -13.590 15.690  0.50 24.78 ? 373 ALA B CB    1 
ATOM   12492 N  N     A ILE B 2 374 ? 32.244  -12.892 12.605  0.50 29.05 ? 374 ILE B N     1 
ATOM   12493 N  N     B ILE B 2 374 ? 32.318  -12.973 12.711  0.50 28.90 ? 374 ILE B N     1 
ATOM   12494 C  CA    A ILE B 2 374 ? 32.030  -13.294 11.222  0.50 26.00 ? 374 ILE B CA    1 
ATOM   12495 C  CA    B ILE B 2 374 ? 32.169  -13.361 11.313  0.50 25.98 ? 374 ILE B CA    1 
ATOM   12496 C  C     A ILE B 2 374 ? 32.810  -12.425 10.247  0.50 29.54 ? 374 ILE B C     1 
ATOM   12497 C  C     B ILE B 2 374 ? 33.028  -12.487 10.410  0.50 29.53 ? 374 ILE B C     1 
ATOM   12498 O  O     A ILE B 2 374 ? 32.946  -12.789 9.073   0.50 24.75 ? 374 ILE B O     1 
ATOM   12499 O  O     B ILE B 2 374 ? 33.322  -12.873 9.272   0.50 24.34 ? 374 ILE B O     1 
ATOM   12500 C  CB    A ILE B 2 374 ? 30.523  -13.267 10.881  0.50 28.24 ? 374 ILE B CB    1 
ATOM   12501 C  CB    B ILE B 2 374 ? 30.681  -13.301 10.900  0.50 28.18 ? 374 ILE B CB    1 
ATOM   12502 C  CG1   A ILE B 2 374 ? 30.209  -14.199 9.709   0.50 28.60 ? 374 ILE B CG1   1 
ATOM   12503 C  CG1   B ILE B 2 374 ? 30.448  -13.999 9.557   0.50 28.38 ? 374 ILE B CG1   1 
ATOM   12504 C  CG2   A ILE B 2 374 ? 30.077  -11.864 10.552  0.50 24.89 ? 374 ILE B CG2   1 
ATOM   12505 C  CG2   B ILE B 2 374 ? 30.207  -11.871 10.827  0.50 25.72 ? 374 ILE B CG2   1 
ATOM   12506 C  CD1   A ILE B 2 374 ? 30.096  -15.650 10.102  0.50 27.95 ? 374 ILE B CD1   1 
ATOM   12507 C  CD1   B ILE B 2 374 ? 30.660  -15.484 9.606   0.50 29.38 ? 374 ILE B CD1   1 
ATOM   12508 N  N     A GLN B 2 375 ? 33.329  -11.279 10.705  0.50 29.63 ? 375 GLN B N     1 
ATOM   12509 N  N     B GLN B 2 375 ? 33.454  -11.316 10.902  0.50 29.36 ? 375 GLN B N     1 
ATOM   12510 C  CA    A GLN B 2 375 ? 34.176  -10.455 9.848   0.50 28.06 ? 375 GLN B CA    1 
ATOM   12511 C  CA    B GLN B 2 375 ? 34.307  -10.429 10.114  0.50 28.29 ? 375 GLN B CA    1 
ATOM   12512 C  C     A GLN B 2 375 ? 35.437  -11.195 9.420   0.50 27.51 ? 375 GLN B C     1 
ATOM   12513 C  C     B GLN B 2 375 ? 35.592  -11.116 9.668   0.50 27.44 ? 375 GLN B C     1 
ATOM   12514 O  O     A GLN B 2 375 ? 35.951  -10.947 8.325   0.50 26.86 ? 375 GLN B O     1 
ATOM   12515 O  O     B GLN B 2 375 ? 36.168  -10.732 8.646   0.50 25.90 ? 375 GLN B O     1 
ATOM   12516 C  CB    A GLN B 2 375 ? 34.545  -9.154  10.559  0.50 30.02 ? 375 GLN B CB    1 
ATOM   12517 C  CB    B GLN B 2 375 ? 34.638  -9.167  10.913  0.50 30.00 ? 375 GLN B CB    1 
ATOM   12518 C  CG    A GLN B 2 375 ? 35.289  -9.355  11.870  0.50 25.97 ? 375 GLN B CG    1 
ATOM   12519 C  CG    B GLN B 2 375 ? 35.535  -9.406  12.116  0.50 26.43 ? 375 GLN B CG    1 
ATOM   12520 C  CD    A GLN B 2 375 ? 35.691  -8.048  12.525  0.50 34.92 ? 375 GLN B CD    1 
ATOM   12521 C  CD    B GLN B 2 375 ? 35.938  -8.118  12.813  0.50 35.27 ? 375 GLN B CD    1 
ATOM   12522 O  OE1   A GLN B 2 375 ? 36.155  -7.122  11.857  0.50 32.66 ? 375 GLN B OE1   1 
ATOM   12523 O  OE1   B GLN B 2 375 ? 37.104  -7.722  12.779  0.50 31.53 ? 375 GLN B OE1   1 
ATOM   12524 N  NE2   A GLN B 2 375 ? 35.513  -7.965  13.842  0.50 31.88 ? 375 GLN B NE2   1 
ATOM   12525 N  NE2   B GLN B 2 375 ? 34.976  -7.460  13.453  0.50 27.77 ? 375 GLN B NE2   1 
ATOM   12526 N  N     A GLU B 2 376 ? 35.946  -12.104 10.260  0.50 27.78 ? 376 GLU B N     1 
ATOM   12527 N  N     B GLU B 2 376 ? 36.060  -12.123 10.413  0.50 27.61 ? 376 GLU B N     1 
ATOM   12528 C  CA    A GLU B 2 376 ? 37.154  -12.851 9.908   0.50 27.03 ? 376 GLU B CA    1 
ATOM   12529 C  CA    B GLU B 2 376 ? 37.244  -12.867 9.986   0.50 26.96 ? 376 GLU B CA    1 
ATOM   12530 C  C     A GLU B 2 376 ? 36.955  -13.659 8.631   0.50 31.46 ? 376 GLU B C     1 
ATOM   12531 C  C     B GLU B 2 376 ? 36.999  -13.573 8.657   0.50 31.49 ? 376 GLU B C     1 
ATOM   12532 O  O     A GLU B 2 376 ? 37.885  -13.806 7.824   0.50 26.84 ? 376 GLU B O     1 
ATOM   12533 O  O     B GLU B 2 376 ? 37.900  -13.659 7.810   0.50 26.75 ? 376 GLU B O     1 
ATOM   12534 C  CB    A GLU B 2 376 ? 37.558  -13.764 11.067  0.50 32.65 ? 376 GLU B CB    1 
ATOM   12535 C  CB    B GLU B 2 376 ? 37.649  -13.874 11.065  0.50 32.68 ? 376 GLU B CB    1 
ATOM   12536 C  CG    A GLU B 2 376 ? 38.038  -13.017 12.305  0.50 29.75 ? 376 GLU B CG    1 
ATOM   12537 C  CG    B GLU B 2 376 ? 38.188  -13.246 12.349  0.50 29.60 ? 376 GLU B CG    1 
ATOM   12538 C  CD    A GLU B 2 376 ? 38.415  -13.943 13.444  0.50 33.25 ? 376 GLU B CD    1 
ATOM   12539 C  CD    B GLU B 2 376 ? 38.719  -14.275 13.334  0.50 34.40 ? 376 GLU B CD    1 
ATOM   12540 O  OE1   A GLU B 2 376 ? 38.112  -15.154 13.364  0.50 32.77 ? 376 GLU B OE1   1 
ATOM   12541 O  OE1   B GLU B 2 376 ? 38.050  -15.306 13.552  0.50 32.01 ? 376 GLU B OE1   1 
ATOM   12542 O  OE2   A GLU B 2 376 ? 39.014  -13.455 14.424  0.50 28.70 ? 376 GLU B OE2   1 
ATOM   12543 O  OE2   B GLU B 2 376 ? 39.817  -14.058 13.887  0.50 36.67 ? 376 GLU B OE2   1 
ATOM   12544 N  N     A LEU B 2 377 ? 35.748  -14.193 8.431   0.50 26.19 ? 377 LEU B N     1 
ATOM   12545 N  N     B LEU B 2 377 ? 35.778  -14.073 8.453   0.50 26.17 ? 377 LEU B N     1 
ATOM   12546 C  CA    A LEU B 2 377 ? 35.425  -14.850 7.168   0.50 27.11 ? 377 LEU B CA    1 
ATOM   12547 C  CA    B LEU B 2 377 ? 35.440  -14.753 7.206   0.50 27.15 ? 377 LEU B CA    1 
ATOM   12548 C  C     A LEU B 2 377 ? 35.509  -13.866 6.009   0.50 30.99 ? 377 LEU B C     1 
ATOM   12549 C  C     B LEU B 2 377 ? 35.436  -13.779 6.033   0.50 31.00 ? 377 LEU B C     1 
ATOM   12550 O  O     A LEU B 2 377 ? 36.176  -14.128 5.001   0.50 30.41 ? 377 LEU B O     1 
ATOM   12551 O  O     B LEU B 2 377 ? 36.003  -14.066 4.971   0.50 30.17 ? 377 LEU B O     1 
ATOM   12552 C  CB    A LEU B 2 377 ? 34.031  -15.480 7.250   0.50 31.55 ? 377 LEU B CB    1 
ATOM   12553 C  CB    B LEU B 2 377 ? 34.080  -15.439 7.344   0.50 31.53 ? 377 LEU B CB    1 
ATOM   12554 C  CG    A LEU B 2 377 ? 33.363  -16.147 6.039   0.50 25.08 ? 377 LEU B CG    1 
ATOM   12555 C  CG    B LEU B 2 377 ? 33.839  -16.816 6.718   0.50 32.14 ? 377 LEU B CG    1 
ATOM   12556 C  CD1   A LEU B 2 377 ? 32.319  -17.142 6.531   0.50 28.78 ? 377 LEU B CD1   1 
ATOM   12557 C  CD1   B LEU B 2 377 ? 32.448  -17.320 7.099   0.50 28.02 ? 377 LEU B CD1   1 
ATOM   12558 C  CD2   A LEU B 2 377 ? 32.696  -15.136 5.123   0.50 26.50 ? 377 LEU B CD2   1 
ATOM   12559 C  CD2   B LEU B 2 377 ? 33.994  -16.785 5.213   0.50 21.02 ? 377 LEU B CD2   1 
ATOM   12560 N  N     A PHE B 2 378 ? 34.822  -12.727 6.130   0.50 27.78 ? 378 PHE B N     1 
ATOM   12561 N  N     B PHE B 2 378 ? 34.791  -12.621 6.202   0.50 27.66 ? 378 PHE B N     1 
ATOM   12562 C  CA    A PHE B 2 378 ? 34.807  -11.770 5.032   0.50 29.15 ? 378 PHE B CA    1 
ATOM   12563 C  CA    B PHE B 2 378 ? 34.734  -11.652 5.112   0.50 28.85 ? 378 PHE B CA    1 
ATOM   12564 C  C     A PHE B 2 378 ? 36.184  -11.148 4.810   0.50 25.57 ? 378 PHE B C     1 
ATOM   12565 C  C     B PHE B 2 378 ? 36.122  -11.110 4.780   0.50 25.59 ? 378 PHE B C     1 
ATOM   12566 O  O     A PHE B 2 378 ? 36.528  -10.804 3.674   0.50 26.53 ? 378 PHE B O     1 
ATOM   12567 O  O     B PHE B 2 378 ? 36.468  -10.948 3.603   0.50 26.35 ? 378 PHE B O     1 
ATOM   12568 C  CB    A PHE B 2 378 ? 33.743  -10.701 5.287   0.50 28.57 ? 378 PHE B CB    1 
ATOM   12569 C  CB    B PHE B 2 378 ? 33.771  -10.518 5.467   0.50 28.36 ? 378 PHE B CB    1 
ATOM   12570 C  CG    A PHE B 2 378 ? 32.332  -11.246 5.319   0.50 28.89 ? 378 PHE B CG    1 
ATOM   12571 C  CG    B PHE B 2 378 ? 32.316  -10.915 5.408   0.50 29.41 ? 378 PHE B CG    1 
ATOM   12572 C  CD1   A PHE B 2 378 ? 31.769  -11.817 4.189   0.50 26.98 ? 378 PHE B CD1   1 
ATOM   12573 C  CD1   B PHE B 2 378 ? 31.737  -11.292 4.206   0.50 26.18 ? 378 PHE B CD1   1 
ATOM   12574 C  CD2   A PHE B 2 378 ? 31.572  -11.184 6.477   0.50 25.80 ? 378 PHE B CD2   1 
ATOM   12575 C  CD2   B PHE B 2 378 ? 31.528  -10.903 6.550   0.50 25.83 ? 378 PHE B CD2   1 
ATOM   12576 C  CE1   A PHE B 2 378 ? 30.479  -12.325 4.214   0.50 22.18 ? 378 PHE B CE1   1 
ATOM   12577 C  CE1   B PHE B 2 378 ? 30.404  -11.660 4.145   0.50 26.73 ? 378 PHE B CE1   1 
ATOM   12578 C  CE2   A PHE B 2 378 ? 30.281  -11.681 6.506   0.50 24.26 ? 378 PHE B CE2   1 
ATOM   12579 C  CE2   B PHE B 2 378 ? 30.193  -11.265 6.495   0.50 23.93 ? 378 PHE B CE2   1 
ATOM   12580 C  CZ    A PHE B 2 378 ? 29.735  -12.251 5.376   0.50 30.68 ? 378 PHE B CZ    1 
ATOM   12581 C  CZ    B PHE B 2 378 ? 29.629  -11.640 5.293   0.50 27.38 ? 378 PHE B CZ    1 
ATOM   12582 N  N     A LYS B 2 379 ? 36.986  -11.011 5.871   0.50 24.88 ? 379 LYS B N     1 
ATOM   12583 N  N     B LYS B 2 379 ? 36.937  -10.835 5.804   0.50 24.66 ? 379 LYS B N     1 
ATOM   12584 C  CA    A LYS B 2 379 ? 38.369  -10.571 5.699   0.50 26.02 ? 379 LYS B CA    1 
ATOM   12585 C  CA    B LYS B 2 379 ? 38.291  -10.343 5.569   0.50 25.94 ? 379 LYS B CA    1 
ATOM   12586 C  C     A LYS B 2 379 ? 39.169  -11.579 4.886   0.50 27.87 ? 379 LYS B C     1 
ATOM   12587 C  C     B LYS B 2 379 ? 39.148  -11.364 4.836   0.50 27.73 ? 379 LYS B C     1 
ATOM   12588 O  O     A LYS B 2 379 ? 39.947  -11.197 4.004   0.50 29.41 ? 379 LYS B O     1 
ATOM   12589 O  O     B LYS B 2 379 ? 40.050  -10.983 4.082   0.50 28.85 ? 379 LYS B O     1 
ATOM   12590 C  CB    A LYS B 2 379 ? 39.044  -10.360 7.055   0.50 32.65 ? 379 LYS B CB    1 
ATOM   12591 C  CB    B LYS B 2 379 ? 38.960  -9.972  6.891   0.50 32.91 ? 379 LYS B CB    1 
ATOM   12592 C  CG    A LYS B 2 379 ? 38.508  -9.218  7.904   0.50 29.69 ? 379 LYS B CG    1 
ATOM   12593 C  CG    B LYS B 2 379 ? 38.430  -8.715  7.552   0.50 28.45 ? 379 LYS B CG    1 
ATOM   12594 C  CD    A LYS B 2 379 ? 39.371  -9.071  9.152   0.50 30.48 ? 379 LYS B CD    1 
ATOM   12595 C  CD    B LYS B 2 379 ? 39.138  -8.500  8.878   0.50 31.20 ? 379 LYS B CD    1 
ATOM   12596 C  CE    A LYS B 2 379 ? 38.703  -8.228  10.220  0.50 33.30 ? 379 LYS B CE    1 
ATOM   12597 C  CE    B LYS B 2 379 ? 39.070  -7.057  9.317   0.50 31.78 ? 379 LYS B CE    1 
ATOM   12598 N  NZ    A LYS B 2 379 ? 39.555  -8.101  11.439  0.50 39.36 ? 379 LYS B NZ    1 
ATOM   12599 N  NZ    B LYS B 2 379 ? 39.784  -6.835  10.605  0.50 37.71 ? 379 LYS B NZ    1 
ATOM   12600 N  N     A ARG B 2 380 ? 39.011  -12.872 5.189   0.50 26.46 ? 380 ARG B N     1 
ATOM   12601 N  N     B ARG B 2 380 ? 38.910  -12.658 5.068   0.50 27.00 ? 380 ARG B N     1 
ATOM   12602 C  CA    A ARG B 2 380 ? 39.746  -13.908 4.468   0.50 29.10 ? 380 ARG B CA    1 
ATOM   12603 C  CA    B ARG B 2 380 ? 39.646  -13.690 4.342   0.50 29.20 ? 380 ARG B CA    1 
ATOM   12604 C  C     A ARG B 2 380 ? 39.419  -13.876 2.981   0.50 27.85 ? 380 ARG B C     1 
ATOM   12605 C  C     B ARG B 2 380 ? 39.379  -13.592 2.845   0.50 28.28 ? 380 ARG B C     1 
ATOM   12606 O  O     A ARG B 2 380 ? 40.319  -13.925 2.131   0.50 24.46 ? 380 ARG B O     1 
ATOM   12607 O  O     B ARG B 2 380 ? 40.309  -13.612 2.029   0.50 23.67 ? 380 ARG B O     1 
ATOM   12608 C  CB    A ARG B 2 380 ? 39.424  -15.282 5.059   0.50 29.80 ? 380 ARG B CB    1 
ATOM   12609 C  CB    B ARG B 2 380 ? 39.264  -15.074 4.872   0.50 29.97 ? 380 ARG B CB    1 
ATOM   12610 C  CG    A ARG B 2 380 ? 40.186  -16.439 4.423   0.50 26.77 ? 380 ARG B CG    1 
ATOM   12611 C  CG    B ARG B 2 380 ? 40.118  -16.220 4.339   0.50 26.62 ? 380 ARG B CG    1 
ATOM   12612 C  CD    A ARG B 2 380 ? 39.595  -17.783 4.841   0.50 27.60 ? 380 ARG B CD    1 
ATOM   12613 C  CD    B ARG B 2 380 ? 39.569  -17.570 4.791   0.50 28.03 ? 380 ARG B CD    1 
ATOM   12614 N  NE    A ARG B 2 380 ? 38.527  -18.218 3.948   0.50 28.13 ? 380 ARG B NE    1 
ATOM   12615 N  NE    B ARG B 2 380 ? 38.536  -18.073 3.892   0.50 28.40 ? 380 ARG B NE    1 
ATOM   12616 C  CZ    A ARG B 2 380 ? 37.404  -18.803 4.343   0.50 31.22 ? 380 ARG B CZ    1 
ATOM   12617 C  CZ    B ARG B 2 380 ? 37.432  -18.696 4.285   0.50 31.18 ? 380 ARG B CZ    1 
ATOM   12618 N  NH1   A ARG B 2 380 ? 37.139  -19.000 5.625   0.50 23.36 ? 380 ARG B NH1   1 
ATOM   12619 N  NH1   B ARG B 2 380 ? 37.152  -18.868 5.568   0.50 23.39 ? 380 ARG B NH1   1 
ATOM   12620 N  NH2   A ARG B 2 380 ? 36.520  -19.194 3.428   0.50 28.22 ? 380 ARG B NH2   1 
ATOM   12621 N  NH2   B ARG B 2 380 ? 36.580  -19.148 3.367   0.50 28.24 ? 380 ARG B NH2   1 
ATOM   12622 N  N     A ILE B 2 381 ? 38.129  -13.790 2.649   0.50 25.55 ? 381 ILE B N     1 
ATOM   12623 N  N     B ILE B 2 381 ? 38.103  -13.478 2.470   0.50 26.49 ? 381 ILE B N     1 
ATOM   12624 C  CA    A ILE B 2 381 ? 37.723  -13.721 1.249   0.50 27.47 ? 381 ILE B CA    1 
ATOM   12625 C  CA    B ILE B 2 381 ? 37.738  -13.304 1.068   0.50 27.28 ? 381 ILE B CA    1 
ATOM   12626 C  C     A ILE B 2 381 ? 38.235  -12.438 0.607   0.50 22.69 ? 381 ILE B C     1 
ATOM   12627 C  C     B ILE B 2 381 ? 38.176  -11.936 0.558   0.50 24.23 ? 381 ILE B C     1 
ATOM   12628 O  O     A ILE B 2 381 ? 38.722  -12.448 -0.530  0.50 27.01 ? 381 ILE B O     1 
ATOM   12629 O  O     B ILE B 2 381 ? 38.534  -11.788 -0.619  0.50 26.33 ? 381 ILE B O     1 
ATOM   12630 C  CB    A ILE B 2 381 ? 36.191  -13.836 1.131   0.50 27.14 ? 381 ILE B CB    1 
ATOM   12631 C  CB    B ILE B 2 381 ? 36.220  -13.520 0.905   0.50 27.17 ? 381 ILE B CB    1 
ATOM   12632 C  CG1   A ILE B 2 381 ? 35.690  -15.097 1.835   0.50 27.24 ? 381 ILE B CG1   1 
ATOM   12633 C  CG1   B ILE B 2 381 ? 35.872  -14.992 1.127   0.50 25.43 ? 381 ILE B CG1   1 
ATOM   12634 C  CG2   A ILE B 2 381 ? 35.763  -13.837 -0.329  0.50 25.21 ? 381 ILE B CG2   1 
ATOM   12635 C  CG2   B ILE B 2 381 ? 35.733  -13.047 -0.458  0.50 25.32 ? 381 ILE B CG2   1 
ATOM   12636 C  CD1   A ILE B 2 381 ? 34.189  -15.283 1.761   0.50 26.76 ? 381 ILE B CD1   1 
ATOM   12637 C  CD1   B ILE B 2 381 ? 34.384  -15.260 1.205   0.50 29.11 ? 381 ILE B CD1   1 
ATOM   12638 N  N     A SER B 2 382 ? 38.131  -11.312 1.322   0.50 21.80 ? 382 SER B N     1 
ATOM   12639 N  N     B SER B 2 382 ? 38.162  -10.920 1.425   0.50 21.35 ? 382 SER B N     1 
ATOM   12640 C  CA    A SER B 2 382 ? 38.509  -10.026 0.743   0.50 26.18 ? 382 SER B CA    1 
ATOM   12641 C  CA    B SER B 2 382 ? 38.581  -9.582  1.017   0.50 25.97 ? 382 SER B CA    1 
ATOM   12642 C  C     A SER B 2 382 ? 40.007  -9.958  0.472   0.50 25.63 ? 382 SER B C     1 
ATOM   12643 C  C     B SER B 2 382 ? 40.032  -9.576  0.554   0.50 26.02 ? 382 SER B C     1 
ATOM   12644 O  O     A SER B 2 382 ? 40.438  -9.321  -0.497  0.50 26.05 ? 382 SER B O     1 
ATOM   12645 O  O     B SER B 2 382 ? 40.355  -9.038  -0.512  0.50 25.80 ? 382 SER B O     1 
ATOM   12646 C  CB    A SER B 2 382 ? 38.082  -8.884  1.665   0.50 27.88 ? 382 SER B CB    1 
ATOM   12647 C  CB    B SER B 2 382 ? 38.395  -8.603  2.175   0.50 24.03 ? 382 SER B CB    1 
ATOM   12648 O  OG    A SER B 2 382 ? 38.245  -7.623  1.032   0.50 26.17 ? 382 SER B OG    1 
ATOM   12649 O  OG    B SER B 2 382 ? 38.921  -7.329  1.847   0.50 23.11 ? 382 SER B OG    1 
ATOM   12650 N  N     A GLU B 2 383 ? 40.815  -10.591 1.326   0.50 28.80 ? 383 GLU B N     1 
ATOM   12651 N  N     B GLU B 2 383 ? 40.922  -10.159 1.359   0.50 29.22 ? 383 GLU B N     1 
ATOM   12652 C  CA    A GLU B 2 383 ? 42.252  -10.652 1.075   0.50 31.74 ? 383 GLU B CA    1 
ATOM   12653 C  CA    B GLU B 2 383 ? 42.342  -10.173 1.021   0.50 30.02 ? 383 GLU B CA    1 
ATOM   12654 C  C     A GLU B 2 383 ? 42.549  -11.401 -0.218  0.50 25.72 ? 383 GLU B C     1 
ATOM   12655 C  C     B GLU B 2 383 ? 42.592  -10.927 -0.279  0.50 24.83 ? 383 GLU B C     1 
ATOM   12656 O  O     A GLU B 2 383 ? 43.395  -10.974 -1.015  0.50 29.94 ? 383 GLU B O     1 
ATOM   12657 O  O     B GLU B 2 383 ? 43.363  -10.468 -1.131  0.50 27.94 ? 383 GLU B O     1 
ATOM   12658 C  CB    A GLU B 2 383 ? 42.962  -11.316 2.255   0.50 27.18 ? 383 GLU B CB    1 
ATOM   12659 C  CB    B GLU B 2 383 ? 43.134  -10.794 2.172   0.50 27.88 ? 383 GLU B CB    1 
ATOM   12660 C  CG    A GLU B 2 383 ? 44.476  -11.281 2.175   0.50 31.44 ? 383 GLU B CG    1 
ATOM   12661 C  CG    B GLU B 2 383 ? 44.600  -10.421 2.215   0.50 32.07 ? 383 GLU B CG    1 
ATOM   12662 C  CD    A GLU B 2 383 ? 45.134  -12.093 3.273   0.50 30.47 ? 383 GLU B CD    1 
ATOM   12663 C  CD    B GLU B 2 383 ? 45.276  -10.931 3.472   0.50 31.28 ? 383 GLU B CD    1 
ATOM   12664 O  OE1   A GLU B 2 383 ? 44.524  -13.084 3.728   0.50 29.41 ? 383 GLU B OE1   1 
ATOM   12665 O  OE1   B GLU B 2 383 ? 44.618  -11.654 4.254   0.50 30.95 ? 383 GLU B OE1   1 
ATOM   12666 O  OE2   A GLU B 2 383 ? 46.261  -11.740 3.682   0.50 34.59 ? 383 GLU B OE2   1 
ATOM   12667 O  OE2   B GLU B 2 383 ? 46.461  -10.610 3.680   0.50 29.74 ? 383 GLU B OE2   1 
ATOM   12668 N  N     A GLN B 2 384 ? 41.856  -12.521 -0.445  0.50 25.02 ? 384 GLN B N     1 
ATOM   12669 N  N     B GLN B 2 384 ? 41.939  -12.081 -0.454  0.50 24.74 ? 384 GLN B N     1 
ATOM   12670 C  CA    A GLN B 2 384 ? 42.034  -13.275 -1.682  0.50 26.49 ? 384 GLN B CA    1 
ATOM   12671 C  CA    B GLN B 2 384 ? 42.127  -12.865 -1.673  0.50 27.28 ? 384 GLN B CA    1 
ATOM   12672 C  C     A GLN B 2 384 ? 41.503  -12.508 -2.886  0.50 29.51 ? 384 GLN B C     1 
ATOM   12673 C  C     B GLN B 2 384 ? 41.584  -12.131 -2.894  0.50 29.01 ? 384 GLN B C     1 
ATOM   12674 O  O     A GLN B 2 384 ? 42.038  -12.643 -3.994  0.50 28.57 ? 384 GLN B O     1 
ATOM   12675 O  O     B GLN B 2 384 ? 42.205  -12.147 -3.965  0.50 27.73 ? 384 GLN B O     1 
ATOM   12676 C  CB    A GLN B 2 384 ? 41.343  -14.636 -1.564  0.50 24.37 ? 384 GLN B CB    1 
ATOM   12677 C  CB    B GLN B 2 384 ? 41.459  -14.232 -1.521  0.50 24.82 ? 384 GLN B CB    1 
ATOM   12678 C  CG    A GLN B 2 384 ? 41.901  -15.518 -0.450  0.50 26.35 ? 384 GLN B CG    1 
ATOM   12679 C  CG    B GLN B 2 384 ? 42.102  -15.128 -0.470  0.50 26.66 ? 384 GLN B CG    1 
ATOM   12680 C  CD    A GLN B 2 384 ? 41.036  -16.734 -0.172  0.50 29.49 ? 384 GLN B CD    1 
ATOM   12681 C  CD    B GLN B 2 384 ? 41.329  -16.413 -0.245  0.50 28.56 ? 384 GLN B CD    1 
ATOM   12682 O  OE1   A GLN B 2 384 ? 39.934  -16.862 -0.705  0.50 30.29 ? 384 GLN B OE1   1 
ATOM   12683 O  OE1   B GLN B 2 384 ? 40.107  -16.450 -0.390  0.50 30.67 ? 384 GLN B OE1   1 
ATOM   12684 N  NE2   A GLN B 2 384 ? 41.532  -17.633 0.671   0.50 29.17 ? 384 GLN B NE2   1 
ATOM   12685 N  NE2   B GLN B 2 384 ? 42.040  -17.475 0.107   0.50 32.20 ? 384 GLN B NE2   1 
ATOM   12686 N  N     A PHE B 2 385 ? 40.460  -11.699 -2.688  0.50 23.45 ? 385 PHE B N     1 
ATOM   12687 N  N     B PHE B 2 385 ? 40.421  -11.491 -2.752  0.50 23.78 ? 385 PHE B N     1 
ATOM   12688 C  CA    A PHE B 2 385 ? 39.910  -10.896 -3.776  0.50 26.47 ? 385 PHE B CA    1 
ATOM   12689 C  CA    B PHE B 2 385 ? 39.875  -10.682 -3.837  0.50 26.54 ? 385 PHE B CA    1 
ATOM   12690 C  C     A PHE B 2 385 ? 40.831  -9.733  -4.122  0.50 26.48 ? 385 PHE B C     1 
ATOM   12691 C  C     B PHE B 2 385 ? 40.863  -9.604  -4.263  0.50 26.44 ? 385 PHE B C     1 
ATOM   12692 O  O     A PHE B 2 385 ? 41.000  -9.397  -5.301  0.50 27.19 ? 385 PHE B O     1 
ATOM   12693 O  O     B PHE B 2 385 ? 41.155  -9.447  -5.454  0.50 27.07 ? 385 PHE B O     1 
ATOM   12694 C  CB    A PHE B 2 385 ? 38.518  -10.394 -3.383  0.50 28.06 ? 385 PHE B CB    1 
ATOM   12695 C  CB    B PHE B 2 385 ? 38.549  -10.052 -3.398  0.50 28.33 ? 385 PHE B CB    1 
ATOM   12696 C  CG    A PHE B 2 385 ? 37.863  -9.511  -4.414  0.50 26.51 ? 385 PHE B CG    1 
ATOM   12697 C  CG    B PHE B 2 385 ? 38.005  -9.031  -4.363  0.50 25.78 ? 385 PHE B CG    1 
ATOM   12698 C  CD1   A PHE B 2 385 ? 38.116  -8.150  -4.445  0.50 27.32 ? 385 PHE B CD1   1 
ATOM   12699 C  CD1   B PHE B 2 385 ? 38.409  -7.706  -4.302  0.50 28.22 ? 385 PHE B CD1   1 
ATOM   12700 C  CD2   A PHE B 2 385 ? 36.971  -10.039 -5.332  0.50 29.39 ? 385 PHE B CD2   1 
ATOM   12701 C  CD2   B PHE B 2 385 ? 37.075  -9.394  -5.321  0.50 30.06 ? 385 PHE B CD2   1 
ATOM   12702 C  CE1   A PHE B 2 385 ? 37.513  -7.338  -5.387  0.50 31.23 ? 385 PHE B CE1   1 
ATOM   12703 C  CE1   B PHE B 2 385 ? 37.914  -6.775  -5.194  0.50 32.29 ? 385 PHE B CE1   1 
ATOM   12704 C  CE2   A PHE B 2 385 ? 36.357  -9.227  -6.273  0.50 26.63 ? 385 PHE B CE2   1 
ATOM   12705 C  CE2   B PHE B 2 385 ? 36.568  -8.461  -6.208  0.50 25.03 ? 385 PHE B CE2   1 
ATOM   12706 C  CZ    A PHE B 2 385 ? 36.630  -7.876  -6.297  0.50 23.70 ? 385 PHE B CZ    1 
ATOM   12707 C  CZ    B PHE B 2 385 ? 36.988  -7.154  -6.144  0.50 25.40 ? 385 PHE B CZ    1 
ATOM   12708 N  N     A THR B 2 386 ? 41.417  -9.093  -3.106  0.50 26.89 ? 386 THR B N     1 
ATOM   12709 N  N     B THR B 2 386 ? 41.374  -8.839  -3.297  0.50 26.57 ? 386 THR B N     1 
ATOM   12710 C  CA    A THR B 2 386 ? 42.312  -7.969  -3.358  0.50 26.58 ? 386 THR B CA    1 
ATOM   12711 C  CA    B THR B 2 386 ? 42.269  -7.737  -3.622  0.50 27.25 ? 386 THR B CA    1 
ATOM   12712 C  C     A THR B 2 386 ? 43.531  -8.405  -4.163  0.50 27.46 ? 386 THR B C     1 
ATOM   12713 C  C     B THR B 2 386 ? 43.612  -8.237  -4.149  0.50 27.61 ? 386 THR B C     1 
ATOM   12714 O  O     A THR B 2 386 ? 43.933  -7.720  -5.113  0.50 25.35 ? 386 THR B O     1 
ATOM   12715 O  O     B THR B 2 386 ? 44.220  -7.579  -5.001  0.50 25.25 ? 386 THR B O     1 
ATOM   12716 C  CB    A THR B 2 386 ? 42.745  -7.334  -2.037  0.50 27.00 ? 386 THR B CB    1 
ATOM   12717 C  CB    B THR B 2 386 ? 42.456  -6.843  -2.394  0.50 26.10 ? 386 THR B CB    1 
ATOM   12718 O  OG1   A THR B 2 386 ? 41.653  -6.592  -1.482  0.50 29.77 ? 386 THR B OG1   1 
ATOM   12719 O  OG1   B THR B 2 386 ? 41.202  -6.235  -2.053  0.50 33.97 ? 386 THR B OG1   1 
ATOM   12720 C  CG2   A THR B 2 386 ? 43.934  -6.399  -2.245  0.50 30.55 ? 386 THR B CG2   1 
ATOM   12721 C  CG2   B THR B 2 386 ? 43.486  -5.749  -2.658  0.50 30.60 ? 386 THR B CG2   1 
ATOM   12722 N  N     A ALA B 2 387 ? 44.126  -9.545  -3.800  0.50 21.35 ? 387 ALA B N     1 
ATOM   12723 N  N     B ALA B 2 387 ? 44.077  -9.399  -3.677  0.50 20.89 ? 387 ALA B N     1 
ATOM   12724 C  CA    A ALA B 2 387 ? 45.310  -10.026 -4.507  0.50 26.63 ? 387 ALA B CA    1 
ATOM   12725 C  CA    B ALA B 2 387 ? 45.332  -9.952  -4.183  0.50 27.46 ? 387 ALA B CA    1 
ATOM   12726 C  C     A ALA B 2 387 ? 45.003  -10.303 -5.973  0.50 26.97 ? 387 ALA B C     1 
ATOM   12727 C  C     B ALA B 2 387 ? 45.251  -10.270 -5.671  0.50 26.46 ? 387 ALA B C     1 
ATOM   12728 O  O     A ALA B 2 387 ? 45.765  -9.909  -6.865  0.50 23.82 ? 387 ALA B O     1 
ATOM   12729 O  O     B ALA B 2 387 ? 46.251  -10.140 -6.391  0.50 21.33 ? 387 ALA B O     1 
ATOM   12730 C  CB    A ALA B 2 387 ? 45.851  -11.283 -3.827  0.50 26.84 ? 387 ALA B CB    1 
ATOM   12731 C  CB    B ALA B 2 387 ? 45.706  -11.205 -3.394  0.50 28.03 ? 387 ALA B CB    1 
ATOM   12732 N  N     A MET B 2 388 ? 43.889  -10.990 -6.241  0.50 27.70 ? 388 MET B N     1 
ATOM   12733 N  N     B MET B 2 388 ? 44.081  -10.706 -6.146  0.50 27.27 ? 388 MET B N     1 
ATOM   12734 C  CA    A MET B 2 388 ? 43.520  -11.301 -7.620  0.50 26.82 ? 388 MET B CA    1 
ATOM   12735 C  CA    B MET B 2 388 ? 43.876  -10.893 -7.580  0.50 26.40 ? 388 MET B CA    1 
ATOM   12736 C  C     A MET B 2 388 ? 43.211  -10.035 -8.408  0.50 27.42 ? 388 MET B C     1 
ATOM   12737 C  C     B MET B 2 388 ? 43.547  -9.571  -8.257  0.50 28.58 ? 388 MET B C     1 
ATOM   12738 O  O     A MET B 2 388 ? 43.684  -9.865  -9.539  0.50 24.72 ? 388 MET B O     1 
ATOM   12739 O  O     B MET B 2 388 ? 44.104  -9.248  -9.313  0.50 24.30 ? 388 MET B O     1 
ATOM   12740 C  CB    A MET B 2 388 ? 42.322  -12.253 -7.645  0.50 25.38 ? 388 MET B CB    1 
ATOM   12741 C  CB    B MET B 2 388 ? 42.755  -11.905 -7.829  0.50 26.02 ? 388 MET B CB    1 
ATOM   12742 C  CG    A MET B 2 388 ? 42.685  -13.714 -7.417  0.50 27.63 ? 388 MET B CG    1 
ATOM   12743 C  CG    B MET B 2 388 ? 43.052  -13.312 -7.334  0.50 28.86 ? 388 MET B CG    1 
ATOM   12744 S  SD    A MET B 2 388 ? 43.484  -14.443 -8.864  0.50 31.11 ? 388 MET B SD    1 
ATOM   12745 S  SD    B MET B 2 388 ? 44.083  -14.256 -8.473  0.50 29.87 ? 388 MET B SD    1 
ATOM   12746 C  CE    A MET B 2 388 ? 42.164  -14.277 -10.065 0.50 28.56 ? 388 MET B CE    1 
ATOM   12747 C  CE    B MET B 2 388 ? 42.905  -14.631 -9.768  0.50 30.00 ? 388 MET B CE    1 
ATOM   12748 N  N     A PHE B 2 389 ? 42.420  -9.129  -7.822  0.50 24.95 ? 389 PHE B N     1 
ATOM   12749 N  N     B PHE B 2 389 ? 42.642  -8.794  -7.653  0.50 24.24 ? 389 PHE B N     1 
ATOM   12750 C  CA    A PHE B 2 389 ? 41.947  -7.965  -8.568  0.50 24.42 ? 389 PHE B CA    1 
ATOM   12751 C  CA    B PHE B 2 389 ? 42.161  -7.567  -8.280  0.50 24.96 ? 389 PHE B CA    1 
ATOM   12752 C  C     A PHE B 2 389 ? 43.050  -6.937  -8.794  0.50 27.10 ? 389 PHE B C     1 
ATOM   12753 C  C     B PHE B 2 389 ? 43.285  -6.555  -8.476  0.50 26.65 ? 389 PHE B C     1 
ATOM   12754 O  O     A PHE B 2 389 ? 43.037  -6.240  -9.814  0.50 25.47 ? 389 PHE B O     1 
ATOM   12755 O  O     B PHE B 2 389 ? 43.273  -5.801  -9.455  0.50 26.51 ? 389 PHE B O     1 
ATOM   12756 C  CB    A PHE B 2 389 ? 40.764  -7.317  -7.848  0.50 27.97 ? 389 PHE B CB    1 
ATOM   12757 C  CB    B PHE B 2 389 ? 41.031  -6.971  -7.437  0.50 27.55 ? 389 PHE B CB    1 
ATOM   12758 C  CG    A PHE B 2 389 ? 40.230  -6.097  -8.543  0.50 30.77 ? 389 PHE B CG    1 
ATOM   12759 C  CG    B PHE B 2 389 ? 40.280  -5.864  -8.117  0.50 30.71 ? 389 PHE B CG    1 
ATOM   12760 C  CD1   A PHE B 2 389 ? 39.473  -6.215  -9.695  0.50 26.89 ? 389 PHE B CD1   1 
ATOM   12761 C  CD1   B PHE B 2 389 ? 39.906  -5.975  -9.444  0.50 26.81 ? 389 PHE B CD1   1 
ATOM   12762 C  CD2   A PHE B 2 389 ? 40.490  -4.831  -8.047  0.50 30.12 ? 389 PHE B CD2   1 
ATOM   12763 C  CD2   B PHE B 2 389 ? 39.932  -4.720  -7.421  0.50 29.37 ? 389 PHE B CD2   1 
ATOM   12764 C  CE1   A PHE B 2 389 ? 38.981  -5.094  -10.334 0.50 30.47 ? 389 PHE B CE1   1 
ATOM   12765 C  CE1   B PHE B 2 389 ? 39.213  -4.959  -10.070 0.50 29.69 ? 389 PHE B CE1   1 
ATOM   12766 C  CE2   A PHE B 2 389 ? 40.003  -3.705  -8.686  0.50 32.12 ? 389 PHE B CE2   1 
ATOM   12767 C  CE2   B PHE B 2 389 ? 39.238  -3.699  -8.043  0.50 35.33 ? 389 PHE B CE2   1 
ATOM   12768 C  CZ    A PHE B 2 389 ? 39.249  -3.837  -9.830  0.50 32.11 ? 389 PHE B CZ    1 
ATOM   12769 C  CZ    B PHE B 2 389 ? 38.880  -3.818  -9.369  0.50 33.85 ? 389 PHE B CZ    1 
ATOM   12770 N  N     A ARG B 2 390 ? 43.993  -6.811  -7.856  0.50 25.67 ? 390 ARG B N     1 
ATOM   12771 N  N     B ARG B 2 390 ? 44.259  -6.527  -7.563  0.50 23.76 ? 390 ARG B N     1 
ATOM   12772 C  CA    A ARG B 2 390 ? 45.095  -5.873  -8.047  0.50 27.61 ? 390 ARG B CA    1 
ATOM   12773 C  CA    B ARG B 2 390 ? 45.404  -5.634  -7.715  0.50 28.50 ? 390 ARG B CA    1 
ATOM   12774 C  C     A ARG B 2 390 ? 45.922  -6.225  -9.278  0.50 27.62 ? 390 ARG B C     1 
ATOM   12775 C  C     B ARG B 2 390 ? 46.135  -5.886  -9.028  0.50 29.02 ? 390 ARG B C     1 
ATOM   12776 O  O     A ARG B 2 390 ? 46.449  -5.329  -9.949  0.50 32.54 ? 390 ARG B O     1 
ATOM   12777 O  O     B ARG B 2 390 ? 46.618  -4.945  -9.670  0.50 33.70 ? 390 ARG B O     1 
ATOM   12778 C  CB    A ARG B 2 390 ? 45.986  -5.839  -6.802  0.50 26.83 ? 390 ARG B CB    1 
ATOM   12779 C  CB    B ARG B 2 390 ? 46.359  -5.802  -6.530  0.50 24.88 ? 390 ARG B CB    1 
ATOM   12780 C  CG    A ARG B 2 390 ? 45.587  -4.786  -5.769  0.50 22.67 ? 390 ARG B CG    1 
ATOM   12781 C  CG    B ARG B 2 390 ? 45.984  -4.979  -5.301  0.50 25.49 ? 390 ARG B CG    1 
ATOM   12782 C  CD    A ARG B 2 390 ? 46.454  -4.897  -4.524  0.50 24.24 ? 390 ARG B CD    1 
ATOM   12783 C  CD    B ARG B 2 390 ? 46.831  -5.368  -4.095  0.50 25.76 ? 390 ARG B CD    1 
ATOM   12784 N  NE    A ARG B 2 390 ? 46.174  -3.845  -3.554  0.50 32.43 ? 390 ARG B NE    1 
ATOM   12785 N  NE    B ARG B 2 390 ? 46.606  -4.479  -2.961  0.50 31.20 ? 390 ARG B NE    1 
ATOM   12786 C  CZ    A ARG B 2 390 ? 46.421  -3.941  -2.254  0.50 30.81 ? 390 ARG B CZ    1 
ATOM   12787 C  CZ    B ARG B 2 390 ? 47.189  -4.605  -1.776  0.50 31.88 ? 390 ARG B CZ    1 
ATOM   12788 N  NH1   A ARG B 2 390 ? 46.935  -5.041  -1.727  0.50 30.81 ? 390 ARG B NH1   1 
ATOM   12789 N  NH1   B ARG B 2 390 ? 48.040  -5.587  -1.522  0.50 24.37 ? 390 ARG B NH1   1 
ATOM   12790 N  NH2   A ARG B 2 390 ? 46.139  -2.910  -1.462  0.50 32.47 ? 390 ARG B NH2   1 
ATOM   12791 N  NH2   B ARG B 2 390 ? 46.912  -3.722  -0.820  0.50 33.44 ? 390 ARG B NH2   1 
ATOM   12792 N  N     A ARG B 2 391 ? 46.049  -7.513  -9.589  0.50 24.15 ? 391 ARG B N     1 
ATOM   12793 N  N     B ARG B 2 391 ? 46.232  -7.146  -9.442  0.50 24.77 ? 391 ARG B N     1 
ATOM   12794 C  CA    A ARG B 2 391 ? 46.768  -7.950  -10.780 0.50 28.92 ? 391 ARG B CA    1 
ATOM   12795 C  CA    B ARG B 2 391 ? 46.884  -7.490  -10.699 0.50 28.38 ? 391 ARG B CA    1 
ATOM   12796 C  C     A ARG B 2 391 ? 45.855  -8.129  -11.983 0.50 30.17 ? 391 ARG B C     1 
ATOM   12797 C  C     B ARG B 2 391 ? 45.916  -7.506  -11.872 0.50 29.09 ? 391 ARG B C     1 
ATOM   12798 O  O     A ARG B 2 391 ? 46.325  -8.585  -13.029 0.50 26.85 ? 391 ARG B O     1 
ATOM   12799 O  O     B ARG B 2 391 ? 46.345  -7.763  -13.001 0.50 29.40 ? 391 ARG B O     1 
ATOM   12800 C  CB    A ARG B 2 391 ? 47.518  -9.264  -10.517 0.50 26.71 ? 391 ARG B CB    1 
ATOM   12801 C  CB    B ARG B 2 391 ? 47.584  -8.853  -10.594 0.50 27.14 ? 391 ARG B CB    1 
ATOM   12802 C  CG    A ARG B 2 391 ? 48.794  -9.131  -9.691  0.50 26.97 ? 391 ARG B CG    1 
ATOM   12803 C  CG    B ARG B 2 391 ? 48.850  -8.862  -9.739  0.50 27.39 ? 391 ARG B CG    1 
ATOM   12804 C  CD    A ARG B 2 391 ? 48.477  -8.949  -8.214  0.50 23.91 ? 391 ARG B CD    1 
ATOM   12805 C  CD    B ARG B 2 391 ? 48.516  -8.879  -8.253  0.50 23.94 ? 391 ARG B CD    1 
ATOM   12806 N  NE    A ARG B 2 391 ? 49.660  -8.849  -7.367  0.50 24.61 ? 391 ARG B NE    1 
ATOM   12807 N  NE    B ARG B 2 391 ? 49.681  -8.728  -7.388  0.50 24.55 ? 391 ARG B NE    1 
ATOM   12808 C  CZ    A ARG B 2 391 ? 49.609  -8.592  -6.067  0.50 27.24 ? 391 ARG B CZ    1 
ATOM   12809 C  CZ    B ARG B 2 391 ? 49.601  -8.546  -6.077  0.50 27.25 ? 391 ARG B CZ    1 
ATOM   12810 N  NH1   A ARG B 2 391 ? 48.457  -8.389  -5.451  0.50 24.64 ? 391 ARG B NH1   1 
ATOM   12811 N  NH1   B ARG B 2 391 ? 48.432  -8.472  -5.463  0.50 24.60 ? 391 ARG B NH1   1 
ATOM   12812 N  NH2   A ARG B 2 391 ? 50.741  -8.535  -5.369  0.50 25.11 ? 391 ARG B NH2   1 
ATOM   12813 N  NH2   B ARG B 2 391 ? 50.719  -8.433  -5.365  0.50 25.13 ? 391 ARG B NH2   1 
ATOM   12814 N  N     A LYS B 2 392 ? 44.565  -7.799  -11.854 0.50 27.83 ? 392 LYS B N     1 
ATOM   12815 N  N     B LYS B 2 392 ? 44.629  -7.239  -11.630 0.50 27.97 ? 392 LYS B N     1 
ATOM   12816 C  CA    A LYS B 2 392 ? 43.604  -7.883  -12.958 0.50 30.34 ? 392 LYS B CA    1 
ATOM   12817 C  CA    B LYS B 2 392 ? 43.603  -7.249  -12.675 0.50 32.83 ? 392 LYS B CA    1 
ATOM   12818 C  C     A LYS B 2 392 ? 43.559  -9.280  -13.568 0.50 25.81 ? 392 LYS B C     1 
ATOM   12819 C  C     B LYS B 2 392 ? 43.550  -8.593  -13.395 0.50 25.09 ? 392 LYS B C     1 
ATOM   12820 O  O     A LYS B 2 392 ? 43.258  -9.442  -14.753 0.50 31.82 ? 392 LYS B O     1 
ATOM   12821 O  O     B LYS B 2 392 ? 43.270  -8.657  -14.592 0.50 28.55 ? 392 LYS B O     1 
ATOM   12822 C  CB    A LYS B 2 392 ? 43.906  -6.838  -14.037 0.50 33.43 ? 392 LYS B CB    1 
ATOM   12823 C  CB    B LYS B 2 392 ? 43.819  -6.112  -13.680 0.50 38.29 ? 392 LYS B CB    1 
ATOM   12824 C  CG    A LYS B 2 392 ? 43.806  -5.401  -13.546 0.50 38.74 ? 392 LYS B CG    1 
ATOM   12825 C  CG    B LYS B 2 392 ? 43.941  -4.731  -13.048 0.50 35.91 ? 392 LYS B CG    1 
ATOM   12826 C  CD    A LYS B 2 392 ? 42.357  -4.951  -13.456 0.50 42.90 ? 392 LYS B CD    1 
ATOM   12827 C  CD    B LYS B 2 392 ? 42.578  -4.081  -12.857 0.50 42.44 ? 392 LYS B CD    1 
ATOM   12828 C  CE    A LYS B 2 392 ? 42.184  -3.797  -12.483 0.50 41.80 ? 392 LYS B CE    1 
ATOM   12829 C  CE    B LYS B 2 392 ? 42.682  -2.777  -12.079 0.50 41.10 ? 392 LYS B CE    1 
ATOM   12830 N  NZ    A LYS B 2 392 ? 42.337  -4.247  -11.067 0.50 33.55 ? 392 LYS B NZ    1 
ATOM   12831 N  NZ    B LYS B 2 392 ? 42.771  -3.007  -10.605 0.50 41.00 ? 392 LYS B NZ    1 
ATOM   12832 N  N     A ALA B 2 393 ? 43.843  -10.297 -12.760 0.50 27.85 ? 393 ALA B N     1 
ATOM   12833 N  N     B ALA B 2 393 ? 43.801  -9.673  -12.660 0.50 26.85 ? 393 ALA B N     1 
ATOM   12834 C  CA    A ALA B 2 393 ? 43.949  -11.662 -13.258 0.50 32.50 ? 393 ALA B CA    1 
ATOM   12835 C  CA    B ALA B 2 393 ? 43.899  -10.995 -13.263 0.50 31.38 ? 393 ALA B CA    1 
ATOM   12836 C  C     A ALA B 2 393 ? 42.590  -12.164 -13.731 0.50 33.58 ? 393 ALA B C     1 
ATOM   12837 C  C     B ALA B 2 393 ? 42.530  -11.494 -13.711 0.50 35.16 ? 393 ALA B C     1 
ATOM   12838 O  O     A ALA B 2 393 ? 41.624  -12.187 -12.959 0.50 34.93 ? 393 ALA B O     1 
ATOM   12839 O  O     B ALA B 2 393 ? 41.560  -11.457 -12.946 0.50 33.84 ? 393 ALA B O     1 
ATOM   12840 C  CB    A ALA B 2 393 ? 44.512  -12.575 -12.172 0.50 32.76 ? 393 ALA B CB    1 
ATOM   12841 C  CB    B ALA B 2 393 ? 44.518  -11.979 -12.271 0.50 32.84 ? 393 ALA B CB    1 
ATOM   12842 N  N     A PHE B 2 394 ? 42.516  -12.548 -15.006 0.50 29.27 ? 394 PHE B N     1 
ATOM   12843 N  N     B PHE B 2 394 ? 42.458  -11.952 -14.963 0.50 29.41 ? 394 PHE B N     1 
ATOM   12844 C  CA    A PHE B 2 394 ? 41.330  -13.149 -15.614 0.50 37.30 ? 394 PHE B CA    1 
ATOM   12845 C  CA    B PHE B 2 394 ? 41.277  -12.597 -15.536 0.50 35.94 ? 394 PHE B CA    1 
ATOM   12846 C  C     A PHE B 2 394 ? 40.126  -12.212 -15.607 0.50 37.08 ? 394 PHE B C     1 
ATOM   12847 C  C     B PHE B 2 394 ? 40.047  -11.694 -15.529 0.50 37.60 ? 394 PHE B C     1 
ATOM   12848 O  O     A PHE B 2 394 ? 38.989  -12.662 -15.776 0.50 37.62 ? 394 PHE B O     1 
ATOM   12849 O  O     B PHE B 2 394 ? 38.920  -12.176 -15.683 0.50 36.64 ? 394 PHE B O     1 
ATOM   12850 C  CB    A PHE B 2 394 ? 40.966  -14.473 -14.929 0.50 36.40 ? 394 PHE B CB    1 
ATOM   12851 C  CB    B PHE B 2 394 ? 40.967  -13.917 -14.818 0.50 37.44 ? 394 PHE B CB    1 
ATOM   12852 C  CG    A PHE B 2 394 ? 42.086  -15.473 -14.910 0.50 39.97 ? 394 PHE B CG    1 
ATOM   12853 C  CG    B PHE B 2 394 ? 42.111  -14.891 -14.821 0.50 38.43 ? 394 PHE B CG    1 
ATOM   12854 C  CD1   A PHE B 2 394 ? 42.995  -15.538 -15.954 0.50 41.03 ? 394 PHE B CD1   1 
ATOM   12855 C  CD1   B PHE B 2 394 ? 42.984  -14.953 -15.896 0.50 41.04 ? 394 PHE B CD1   1 
ATOM   12856 C  CD2   A PHE B 2 394 ? 42.234  -16.347 -13.844 0.50 40.75 ? 394 PHE B CD2   1 
ATOM   12857 C  CD2   B PHE B 2 394 ? 42.317  -15.739 -13.746 0.50 40.40 ? 394 PHE B CD2   1 
ATOM   12858 C  CE1   A PHE B 2 394 ? 44.028  -16.457 -15.936 0.50 39.32 ? 394 PHE B CE1   1 
ATOM   12859 C  CE1   B PHE B 2 394 ? 44.039  -15.845 -15.899 0.50 37.75 ? 394 PHE B CE1   1 
ATOM   12860 C  CE2   A PHE B 2 394 ? 43.263  -17.270 -13.821 0.50 35.42 ? 394 PHE B CE2   1 
ATOM   12861 C  CE2   B PHE B 2 394 ? 43.368  -16.635 -13.743 0.50 35.59 ? 394 PHE B CE2   1 
ATOM   12862 C  CZ    A PHE B 2 394 ? 44.161  -17.325 -14.867 0.50 38.98 ? 394 PHE B CZ    1 
ATOM   12863 C  CZ    B PHE B 2 394 ? 44.232  -16.688 -14.821 0.50 40.74 ? 394 PHE B CZ    1 
ATOM   12864 N  N     A LEU B 2 395 ? 40.355  -10.907 -15.432 0.50 35.30 ? 395 LEU B N     1 
ATOM   12865 N  N     B LEU B 2 395 ? 40.237  -10.383 -15.366 0.50 33.02 ? 395 LEU B N     1 
ATOM   12866 C  CA    A LEU B 2 395 ? 39.243  -9.966  -15.341 0.50 37.58 ? 395 LEU B CA    1 
ATOM   12867 C  CA    B LEU B 2 395 ? 39.101  -9.470  -15.325 0.50 39.95 ? 395 LEU B CA    1 
ATOM   12868 C  C     A LEU B 2 395 ? 38.458  -9.888  -16.644 0.50 38.58 ? 395 LEU B C     1 
ATOM   12869 C  C     B LEU B 2 395 ? 38.389  -9.375  -16.668 0.50 37.64 ? 395 LEU B C     1 
ATOM   12870 O  O     A LEU B 2 395 ? 37.255  -9.603  -16.626 0.50 37.13 ? 395 LEU B O     1 
ATOM   12871 O  O     B LEU B 2 395 ? 37.231  -8.947  -16.711 0.50 37.20 ? 395 LEU B O     1 
ATOM   12872 C  CB    A LEU B 2 395 ? 39.761  -8.580  -14.954 0.50 41.13 ? 395 LEU B CB    1 
ATOM   12873 C  CB    B LEU B 2 395 ? 39.561  -8.082  -14.875 0.50 40.94 ? 395 LEU B CB    1 
ATOM   12874 C  CG    A LEU B 2 395 ? 38.708  -7.528  -14.601 0.50 43.60 ? 395 LEU B CG    1 
ATOM   12875 C  CG    B LEU B 2 395 ? 38.515  -7.184  -14.211 0.50 43.67 ? 395 LEU B CG    1 
ATOM   12876 C  CD1   A LEU B 2 395 ? 38.251  -7.688  -13.158 0.50 40.78 ? 395 LEU B CD1   1 
ATOM   12877 C  CD1   B LEU B 2 395 ? 38.142  -7.729  -12.842 0.50 40.36 ? 395 LEU B CD1   1 
ATOM   12878 C  CD2   A LEU B 2 395 ? 39.231  -6.123  -14.853 0.50 44.42 ? 395 LEU B CD2   1 
ATOM   12879 C  CD2   B LEU B 2 395 ? 39.021  -5.757  -14.102 0.50 42.68 ? 395 LEU B CD2   1 
ATOM   12880 N  N     A HIS B 2 396 ? 39.114  -10.140 -17.781 0.50 38.84 ? 396 HIS B N     1 
ATOM   12881 N  N     B HIS B 2 396 ? 39.051  -9.768  -17.760 0.50 39.48 ? 396 HIS B N     1 
ATOM   12882 C  CA    A HIS B 2 396 ? 38.437  -10.053 -19.071 0.50 42.11 ? 396 HIS B CA    1 
ATOM   12883 C  CA    B HIS B 2 396 ? 38.428  -9.717  -19.077 0.50 41.57 ? 396 HIS B CA    1 
ATOM   12884 C  C     A HIS B 2 396 ? 37.371  -11.127 -19.245 0.50 36.02 ? 396 HIS B C     1 
ATOM   12885 C  C     B HIS B 2 396 ? 37.371  -10.798 -19.264 0.50 36.45 ? 396 HIS B C     1 
ATOM   12886 O  O     A HIS B 2 396 ? 36.476  -10.960 -20.080 0.50 38.91 ? 396 HIS B O     1 
ATOM   12887 O  O     B HIS B 2 396 ? 36.469  -10.623 -20.090 0.50 39.65 ? 396 HIS B O     1 
ATOM   12888 C  CB    A HIS B 2 396 ? 39.458  -10.141 -20.206 0.50 41.66 ? 396 HIS B CB    1 
ATOM   12889 C  CB    B HIS B 2 396 ? 39.495  -9.831  -20.168 0.50 41.72 ? 396 HIS B CB    1 
ATOM   12890 C  CG    A HIS B 2 396 ? 40.282  -11.389 -20.180 0.50 44.47 ? 396 HIS B CG    1 
ATOM   12891 C  CG    B HIS B 2 396 ? 40.368  -11.040 -20.037 0.50 44.23 ? 396 HIS B CG    1 
ATOM   12892 N  ND1   A HIS B 2 396 ? 40.094  -12.424 -21.071 0.50 48.01 ? 396 HIS B ND1   1 
ATOM   12893 N  ND1   B HIS B 2 396 ? 40.210  -12.161 -20.822 0.50 47.86 ? 396 HIS B ND1   1 
ATOM   12894 C  CD2   A HIS B 2 396 ? 41.294  -11.772 -19.367 0.50 47.28 ? 396 HIS B CD2   1 
ATOM   12895 C  CD2   B HIS B 2 396 ? 41.405  -11.305 -19.207 0.50 46.54 ? 396 HIS B CD2   1 
ATOM   12896 C  CE1   A HIS B 2 396 ? 40.957  -13.389 -20.810 0.50 45.56 ? 396 HIS B CE1   1 
ATOM   12897 C  CE1   B HIS B 2 396 ? 41.115  -13.063 -20.486 0.50 45.34 ? 396 HIS B CE1   1 
ATOM   12898 N  NE2   A HIS B 2 396 ? 41.696  -13.019 -19.779 0.50 44.84 ? 396 HIS B NE2   1 
ATOM   12899 N  NE2   B HIS B 2 396 ? 41.851  -12.569 -19.507 0.50 45.48 ? 396 HIS B NE2   1 
ATOM   12900 N  N     A TRP B 2 397 ? 37.441  -12.220 -18.482 0.50 38.69 ? 397 TRP B N     1 
ATOM   12901 N  N     B TRP B 2 397 ? 37.460  -11.910 -18.526 0.50 38.58 ? 397 TRP B N     1 
ATOM   12902 C  CA    A TRP B 2 397 ? 36.372  -13.212 -18.502 0.50 41.65 ? 397 TRP B CA    1 
ATOM   12903 C  CA    B TRP B 2 397 ? 36.376  -12.888 -18.541 0.50 42.13 ? 397 TRP B CA    1 
ATOM   12904 C  C     A TRP B 2 397 ? 35.052  -12.661 -17.970 0.50 35.03 ? 397 TRP B C     1 
ATOM   12905 C  C     B TRP B 2 397 ? 35.063  -12.269 -18.076 0.50 34.46 ? 397 TRP B C     1 
ATOM   12906 O  O     A TRP B 2 397 ? 34.014  -13.305 -18.153 0.50 39.97 ? 397 TRP B O     1 
ATOM   12907 O  O     B TRP B 2 397 ? 33.986  -12.736 -18.459 0.50 36.80 ? 397 TRP B O     1 
ATOM   12908 C  CB    A TRP B 2 397 ? 36.779  -14.448 -17.691 0.50 39.67 ? 397 TRP B CB    1 
ATOM   12909 C  CB    B TRP B 2 397 ? 36.722  -14.093 -17.660 0.50 40.24 ? 397 TRP B CB    1 
ATOM   12910 C  CG    A TRP B 2 397 ? 37.926  -15.218 -18.283 0.50 44.17 ? 397 TRP B CG    1 
ATOM   12911 C  CG    B TRP B 2 397 ? 37.809  -14.983 -18.196 0.50 43.92 ? 397 TRP B CG    1 
ATOM   12912 C  CD1   A TRP B 2 397 ? 38.463  -15.063 -19.528 0.50 46.43 ? 397 TRP B CD1   1 
ATOM   12913 C  CD1   B TRP B 2 397 ? 38.616  -14.739 -19.267 0.50 45.76 ? 397 TRP B CD1   1 
ATOM   12914 C  CD2   A TRP B 2 397 ? 38.678  -16.264 -17.650 0.50 46.85 ? 397 TRP B CD2   1 
ATOM   12915 C  CD2   B TRP B 2 397 ? 38.199  -16.266 -17.683 0.50 47.22 ? 397 TRP B CD2   1 
ATOM   12916 N  NE1   A TRP B 2 397 ? 39.500  -15.947 -19.711 0.50 53.01 ? 397 TRP B NE1   1 
ATOM   12917 N  NE1   B TRP B 2 397 ? 39.488  -15.786 -19.452 0.50 53.18 ? 397 TRP B NE1   1 
ATOM   12918 C  CE2   A TRP B 2 397 ? 39.653  -16.695 -18.572 0.50 49.55 ? 397 TRP B CE2   1 
ATOM   12919 C  CE2   B TRP B 2 397 ? 39.253  -16.736 -18.492 0.50 49.30 ? 397 TRP B CE2   1 
ATOM   12920 C  CE3   A TRP B 2 397 ? 38.620  -16.877 -16.394 0.50 47.86 ? 397 TRP B CE3   1 
ATOM   12921 C  CE3   B TRP B 2 397 ? 37.762  -17.060 -16.617 0.50 47.75 ? 397 TRP B CE3   1 
ATOM   12922 C  CZ2   A TRP B 2 397 ? 40.563  -17.710 -18.278 0.50 43.04 ? 397 TRP B CZ2   1 
ATOM   12923 C  CZ2   B TRP B 2 397 ? 39.877  -17.965 -18.270 0.50 45.90 ? 397 TRP B CZ2   1 
ATOM   12924 C  CZ3   A TRP B 2 397 ? 39.525  -17.886 -16.104 0.50 43.94 ? 397 TRP B CZ3   1 
ATOM   12925 C  CZ3   B TRP B 2 397 ? 38.383  -18.282 -16.398 0.50 45.31 ? 397 TRP B CZ3   1 
ATOM   12926 C  CH2   A TRP B 2 397 ? 40.482  -18.291 -17.042 0.50 47.93 ? 397 TRP B CH2   1 
ATOM   12927 C  CH2   B TRP B 2 397 ? 39.428  -18.720 -17.220 0.50 47.72 ? 397 TRP B CH2   1 
ATOM   12928 N  N     A TYR B 2 398 ? 35.067  -11.494 -17.324 0.50 35.11 ? 398 TYR B N     1 
ATOM   12929 N  N     B TYR B 2 398 ? 35.131  -11.216 -17.263 0.50 36.13 ? 398 TYR B N     1 
ATOM   12930 C  CA    A TYR B 2 398 ? 33.860  -10.861 -16.802 0.50 40.39 ? 398 TYR B CA    1 
ATOM   12931 C  CA    B TYR B 2 398 ? 33.952  -10.582 -16.689 0.50 40.25 ? 398 TYR B CA    1 
ATOM   12932 C  C     A TYR B 2 398 ? 33.378  -9.734  -17.710 0.50 38.36 ? 398 TYR B C     1 
ATOM   12933 C  C     B TYR B 2 398 ? 33.536  -9.317  -17.432 0.50 38.77 ? 398 TYR B C     1 
ATOM   12934 O  O     A TYR B 2 398 ? 32.227  -9.745  -18.157 0.50 42.64 ? 398 TYR B O     1 
ATOM   12935 O  O     B TYR B 2 398 ? 32.354  -9.149  -17.743 0.50 43.68 ? 398 TYR B O     1 
ATOM   12936 C  CB    A TYR B 2 398 ? 34.108  -10.331 -15.382 0.50 36.05 ? 398 TYR B CB    1 
ATOM   12937 C  CB    B TYR B 2 398 ? 34.199  -10.271 -15.207 0.50 35.84 ? 398 TYR B CB    1 
ATOM   12938 C  CG    A TYR B 2 398 ? 34.461  -11.408 -14.384 0.50 36.11 ? 398 TYR B CG    1 
ATOM   12939 C  CG    B TYR B 2 398 ? 34.296  -11.511 -14.345 0.50 35.92 ? 398 TYR B CG    1 
ATOM   12940 C  CD1   A TYR B 2 398 ? 35.748  -11.927 -14.320 0.50 35.19 ? 398 TYR B CD1   1 
ATOM   12941 C  CD1   B TYR B 2 398 ? 35.492  -12.213 -14.227 0.50 34.81 ? 398 TYR B CD1   1 
ATOM   12942 C  CD2   A TYR B 2 398 ? 33.507  -11.908 -13.506 0.50 32.42 ? 398 TYR B CD2   1 
ATOM   12943 C  CD2   B TYR B 2 398 ? 33.188  -11.988 -13.660 0.50 31.92 ? 398 TYR B CD2   1 
ATOM   12944 C  CE1   A TYR B 2 398 ? 36.076  -12.913 -13.415 0.50 30.47 ? 398 TYR B CE1   1 
ATOM   12945 C  CE1   B TYR B 2 398 ? 35.579  -13.353 -13.443 0.50 29.87 ? 398 TYR B CE1   1 
ATOM   12946 C  CE2   A TYR B 2 398 ? 33.826  -12.894 -12.591 0.50 22.22 ? 398 TYR B CE2   1 
ATOM   12947 C  CE2   B TYR B 2 398 ? 33.266  -13.121 -12.873 0.50 21.58 ? 398 TYR B CE2   1 
ATOM   12948 C  CZ    A TYR B 2 398 ? 35.114  -13.391 -12.549 0.50 29.01 ? 398 TYR B CZ    1 
ATOM   12949 C  CZ    B TYR B 2 398 ? 34.460  -13.799 -12.763 0.50 27.79 ? 398 TYR B CZ    1 
ATOM   12950 O  OH    A TYR B 2 398 ? 35.452  -14.374 -11.649 0.50 22.51 ? 398 TYR B OH    1 
ATOM   12951 O  OH    B TYR B 2 398 ? 34.533  -14.930 -11.981 0.50 27.65 ? 398 TYR B OH    1 
ATOM   12952 N  N     A THR B 2 399 ? 34.245  -8.755  -17.990 0.50 38.40 ? 399 THR B N     1 
ATOM   12953 N  N     B THR B 2 399 ? 34.483  -8.421  -17.730 0.50 37.51 ? 399 THR B N     1 
ATOM   12954 C  CA    A THR B 2 399 ? 33.864  -7.643  -18.855 0.50 42.14 ? 399 THR B CA    1 
ATOM   12955 C  CA    B THR B 2 399 ? 34.123  -7.168  -18.388 0.50 38.94 ? 399 THR B CA    1 
ATOM   12956 C  C     A THR B 2 399 ? 33.483  -8.107  -20.255 0.50 40.92 ? 399 THR B C     1 
ATOM   12957 C  C     B THR B 2 399 ? 33.653  -7.394  -19.820 0.50 43.29 ? 399 THR B C     1 
ATOM   12958 O  O     A THR B 2 399 ? 32.737  -7.406  -20.947 0.50 44.34 ? 399 THR B O     1 
ATOM   12959 O  O     B THR B 2 399 ? 32.853  -6.606  -20.338 0.50 41.84 ? 399 THR B O     1 
ATOM   12960 C  CB    A THR B 2 399 ? 34.999  -6.621  -18.942 0.50 42.04 ? 399 THR B CB    1 
ATOM   12961 C  CB    B THR B 2 399 ? 35.302  -6.192  -18.368 0.50 41.52 ? 399 THR B CB    1 
ATOM   12962 O  OG1   A THR B 2 399 ? 36.127  -7.209  -19.603 0.50 35.16 ? 399 THR B OG1   1 
ATOM   12963 O  OG1   B THR B 2 399 ? 36.440  -6.787  -19.008 0.50 35.64 ? 399 THR B OG1   1 
ATOM   12964 C  CG2   A THR B 2 399 ? 35.411  -6.164  -17.548 0.50 41.95 ? 399 THR B CG2   1 
ATOM   12965 C  CG2   B THR B 2 399 ? 35.659  -5.821  -16.936 0.50 41.17 ? 399 THR B CG2   1 
ATOM   12966 N  N     A GLY B 2 400 ? 33.974  -9.269  -20.684 0.50 41.81 ? 400 GLY B N     1 
ATOM   12967 N  N     B GLY B 2 400 ? 34.131  -8.457  -20.471 0.50 37.03 ? 400 GLY B N     1 
ATOM   12968 C  CA    A GLY B 2 400 ? 33.577  -9.835  -21.961 0.50 41.90 ? 400 GLY B CA    1 
ATOM   12969 C  CA    B GLY B 2 400 ? 33.693  -8.767  -21.820 0.50 42.88 ? 400 GLY B CA    1 
ATOM   12970 C  C     A GLY B 2 400 ? 32.174  -10.405 -21.985 0.50 44.04 ? 400 GLY B C     1 
ATOM   12971 C  C     B GLY B 2 400 ? 32.249  -9.210  -21.916 0.50 42.48 ? 400 GLY B C     1 
ATOM   12972 O  O     A GLY B 2 400 ? 31.689  -10.758 -23.066 0.50 41.20 ? 400 GLY B O     1 
ATOM   12973 O  O     B GLY B 2 400 ? 31.677  -9.188  -23.011 0.50 42.72 ? 400 GLY B O     1 
ATOM   12974 N  N     A GLU B 2 401 ? 31.519  -10.513 -20.828 0.50 42.14 ? 401 GLU B N     1 
ATOM   12975 N  N     B GLU B 2 401 ? 31.648  -9.619  -20.800 0.50 43.17 ? 401 GLU B N     1 
ATOM   12976 C  CA    A GLU B 2 401 ? 30.131  -10.943 -20.752 0.50 36.75 ? 401 GLU B CA    1 
ATOM   12977 C  CA    B GLU B 2 401 ? 30.235  -9.970  -20.763 0.50 41.53 ? 401 GLU B CA    1 
ATOM   12978 C  C     A GLU B 2 401 ? 29.157  -9.785  -20.582 0.50 44.40 ? 401 GLU B C     1 
ATOM   12979 C  C     B GLU B 2 401 ? 29.339  -8.761  -20.533 0.50 43.58 ? 401 GLU B C     1 
ATOM   12980 O  O     A GLU B 2 401 ? 27.949  -9.983  -20.755 0.50 47.60 ? 401 GLU B O     1 
ATOM   12981 O  O     B GLU B 2 401 ? 28.128  -8.925  -20.351 0.50 43.39 ? 401 GLU B O     1 
ATOM   12982 C  CB    A GLU B 2 401 ? 29.940  -11.935 -19.596 0.50 36.37 ? 401 GLU B CB    1 
ATOM   12983 C  CB    B GLU B 2 401 ? 29.974  -11.019 -19.679 0.50 38.34 ? 401 GLU B CB    1 
ATOM   12984 C  CG    A GLU B 2 401 ? 30.642  -13.270 -19.784 0.50 38.28 ? 401 GLU B CG    1 
ATOM   12985 C  CG    B GLU B 2 401 ? 30.572  -12.386 -19.968 0.50 38.74 ? 401 GLU B CG    1 
ATOM   12986 C  CD    A GLU B 2 401 ? 29.955  -14.165 -20.802 0.50 41.82 ? 401 GLU B CD    1 
ATOM   12987 C  CD    B GLU B 2 401 ? 29.970  -13.047 -21.194 0.50 40.10 ? 401 GLU B CD    1 
ATOM   12988 O  OE1   A GLU B 2 401 ? 28.735  -14.010 -21.016 0.50 40.65 ? 401 GLU B OE1   1 
ATOM   12989 O  OE1   B GLU B 2 401 ? 28.865  -12.647 -21.615 0.50 36.62 ? 401 GLU B OE1   1 
ATOM   12990 O  OE2   A GLU B 2 401 ? 30.641  -15.028 -21.390 0.50 44.51 ? 401 GLU B OE2   1 
ATOM   12991 O  OE2   B GLU B 2 401 ? 30.605  -13.973 -21.740 0.50 42.19 ? 401 GLU B OE2   1 
ATOM   12992 N  N     A GLY B 2 402 ? 29.643  -8.591  -20.248 0.50 43.38 ? 402 GLY B N     1 
ATOM   12993 N  N     B GLY B 2 402 ? 29.903  -7.557  -20.539 0.50 42.23 ? 402 GLY B N     1 
ATOM   12994 C  CA    A GLY B 2 402 ? 28.772  -7.445  -20.078 0.50 44.78 ? 402 GLY B CA    1 
ATOM   12995 C  CA    B GLY B 2 402 ? 29.147  -6.356  -20.269 0.50 47.52 ? 402 GLY B CA    1 
ATOM   12996 C  C     A GLY B 2 402 ? 29.109  -6.579  -18.881 0.50 46.34 ? 402 GLY B C     1 
ATOM   12997 C  C     B GLY B 2 402 ? 29.305  -5.802  -18.872 0.50 46.88 ? 402 GLY B C     1 
ATOM   12998 O  O     A GLY B 2 402 ? 28.692  -5.419  -18.817 0.50 49.05 ? 402 GLY B O     1 
ATOM   12999 O  O     B GLY B 2 402 ? 28.754  -4.732  -18.586 0.50 51.05 ? 402 GLY B O     1 
ATOM   13000 N  N     A MET B 2 403 ? 29.856  -7.128  -17.924 0.50 45.70 ? 403 MET B N     1 
ATOM   13001 N  N     B MET B 2 403 ? 30.027  -6.493  -17.992 0.50 46.52 ? 403 MET B N     1 
ATOM   13002 C  CA    A MET B 2 403 ? 30.210  -6.378  -16.728 0.50 44.60 ? 403 MET B CA    1 
ATOM   13003 C  CA    B MET B 2 403 ? 30.243  -5.982  -16.647 0.50 43.68 ? 403 MET B CA    1 
ATOM   13004 C  C     A MET B 2 403 ? 31.182  -5.251  -17.062 0.50 45.74 ? 403 MET B C     1 
ATOM   13005 C  C     B MET B 2 403 ? 31.115  -4.736  -16.681 0.50 45.27 ? 403 MET B C     1 
ATOM   13006 O  O     A MET B 2 403 ? 31.831  -5.238  -18.111 0.50 49.18 ? 403 MET B O     1 
ATOM   13007 O  O     B MET B 2 403 ? 31.957  -4.558  -17.565 0.50 47.95 ? 403 MET B O     1 
ATOM   13008 C  CB    A MET B 2 403 ? 30.846  -7.288  -15.675 0.50 43.93 ? 403 MET B CB    1 
ATOM   13009 C  CB    B MET B 2 403 ? 30.901  -7.038  -15.757 0.50 44.27 ? 403 MET B CB    1 
ATOM   13010 C  CG    A MET B 2 403 ? 30.011  -8.483  -15.265 0.50 38.48 ? 403 MET B CG    1 
ATOM   13011 C  CG    B MET B 2 403 ? 29.931  -7.845  -14.921 0.50 40.56 ? 403 MET B CG    1 
ATOM   13012 S  SD    A MET B 2 403 ? 30.660  -9.309  -13.794 0.50 40.95 ? 403 MET B SD    1 
ATOM   13013 S  SD    B MET B 2 403 ? 30.715  -8.656  -13.513 0.50 40.52 ? 403 MET B SD    1 
ATOM   13014 C  CE    A MET B 2 403 ? 30.646  -7.962  -12.610 0.50 35.13 ? 403 MET B CE    1 
ATOM   13015 C  CE    B MET B 2 403 ? 31.133  -7.243  -12.496 0.50 35.07 ? 403 MET B CE    1 
ATOM   13016 N  N     A ASP B 2 404 ? 31.277  -4.295  -16.143 0.50 46.17 ? 404 ASP B N     1 
ATOM   13017 N  N     B ASP B 2 404 ? 30.902  -3.867  -15.703 0.50 46.56 ? 404 ASP B N     1 
ATOM   13018 C  CA    A ASP B 2 404 ? 32.284  -3.248  -16.191 0.50 45.55 ? 404 ASP B CA    1 
ATOM   13019 C  CA    B ASP B 2 404 ? 31.720  -2.678  -15.532 0.50 44.78 ? 404 ASP B CA    1 
ATOM   13020 C  C     A ASP B 2 404 ? 33.121  -3.307  -14.920 0.50 47.81 ? 404 ASP B C     1 
ATOM   13021 C  C     B ASP B 2 404 ? 32.790  -2.951  -14.484 0.50 47.84 ? 404 ASP B C     1 
ATOM   13022 O  O     A ASP B 2 404 ? 32.691  -3.846  -13.895 0.50 46.38 ? 404 ASP B O     1 
ATOM   13023 O  O     B ASP B 2 404 ? 32.525  -3.595  -13.465 0.50 44.79 ? 404 ASP B O     1 
ATOM   13024 C  CB    A ASP B 2 404 ? 31.646  -1.860  -16.352 0.50 45.92 ? 404 ASP B CB    1 
ATOM   13025 C  CB    B ASP B 2 404 ? 30.864  -1.481  -15.117 0.50 47.13 ? 404 ASP B CB    1 
ATOM   13026 C  CG    A ASP B 2 404 ? 31.004  -1.666  -17.719 0.50 50.18 ? 404 ASP B CG    1 
ATOM   13027 C  CG    B ASP B 2 404 ? 31.572  -0.164  -15.336 0.50 45.57 ? 404 ASP B CG    1 
ATOM   13028 O  OD1   A ASP B 2 404 ? 31.127  -2.567  -18.574 0.50 51.56 ? 404 ASP B OD1   1 
ATOM   13029 O  OD1   B ASP B 2 404 ? 32.676  -0.181  -15.917 0.50 41.51 ? 404 ASP B OD1   1 
ATOM   13030 O  OD2   A ASP B 2 404 ? 30.375  -0.611  -17.940 0.50 51.85 ? 404 ASP B OD2   1 
ATOM   13031 O  OD2   B ASP B 2 404 ? 31.027  0.884   -14.930 0.50 50.28 ? 404 ASP B OD2   1 
ATOM   13032 N  N     A GLU B 2 405 ? 34.332  -2.749  -14.997 0.50 46.81 ? 405 GLU B N     1 
ATOM   13033 N  N     B GLU B 2 405 ? 34.007  -2.467  -14.748 0.50 48.09 ? 405 GLU B N     1 
ATOM   13034 C  CA    A GLU B 2 405 ? 35.245  -2.798  -13.859 0.50 47.69 ? 405 GLU B CA    1 
ATOM   13035 C  CA    B GLU B 2 405 ? 35.098  -2.668  -13.800 0.50 47.50 ? 405 GLU B CA    1 
ATOM   13036 C  C     A GLU B 2 405 ? 34.674  -2.122  -12.620 0.50 45.65 ? 405 GLU B C     1 
ATOM   13037 C  C     B GLU B 2 405 ? 34.782  -2.052  -12.445 0.50 45.65 ? 405 GLU B C     1 
ATOM   13038 O  O     A GLU B 2 405 ? 35.119  -2.418  -11.505 0.50 43.93 ? 405 GLU B O     1 
ATOM   13039 O  O     B GLU B 2 405 ? 35.262  -2.537  -11.413 0.50 43.74 ? 405 GLU B O     1 
ATOM   13040 C  CB    A GLU B 2 405 ? 36.585  -2.155  -14.219 0.50 46.26 ? 405 GLU B CB    1 
ATOM   13041 C  CB    B GLU B 2 405 ? 36.399  -2.085  -14.358 0.50 45.90 ? 405 GLU B CB    1 
ATOM   13042 C  CG    A GLU B 2 405 ? 37.405  -2.930  -15.237 0.50 48.57 ? 405 GLU B CG    1 
ATOM   13043 C  CG    B GLU B 2 405 ? 37.620  -2.379  -13.495 0.50 42.92 ? 405 GLU B CG    1 
ATOM   13044 C  CD    A GLU B 2 405 ? 38.870  -2.536  -15.221 0.50 48.40 ? 405 GLU B CD    1 
ATOM   13045 C  CD    B GLU B 2 405 ? 38.861  -1.631  -13.941 0.50 46.96 ? 405 GLU B CD    1 
ATOM   13046 O  OE1   A GLU B 2 405 ? 39.410  -2.304  -14.119 0.50 45.61 ? 405 GLU B OE1   1 
ATOM   13047 O  OE1   B GLU B 2 405 ? 38.826  -0.983  -15.010 0.50 39.02 ? 405 GLU B OE1   1 
ATOM   13048 O  OE2   A GLU B 2 405 ? 39.479  -2.452  -16.309 0.50 52.08 ? 405 GLU B OE2   1 
ATOM   13049 O  OE2   B GLU B 2 405 ? 39.875  -1.689  -13.215 0.50 44.20 ? 405 GLU B OE2   1 
ATOM   13050 N  N     A MET B 2 406 ? 33.697  -1.228  -12.785 0.50 45.81 ? 406 MET B N     1 
ATOM   13051 N  N     B MET B 2 406 ? 33.963  -0.998  -12.422 0.50 45.23 ? 406 MET B N     1 
ATOM   13052 C  CA    A MET B 2 406 ? 33.135  -0.532  -11.635 0.50 42.71 ? 406 MET B CA    1 
ATOM   13053 C  CA    B MET B 2 406 ? 33.659  -0.312  -11.175 0.50 42.90 ? 406 MET B CA    1 
ATOM   13054 C  C     A MET B 2 406 ? 32.347  -1.477  -10.735 0.50 41.65 ? 406 MET B C     1 
ATOM   13055 C  C     B MET B 2 406 ? 32.834  -1.162  -10.217 0.50 43.02 ? 406 MET B C     1 
ATOM   13056 O  O     A MET B 2 406 ? 32.237  -1.232  -9.528  0.50 40.75 ? 406 MET B O     1 
ATOM   13057 O  O     B MET B 2 406 ? 32.870  -0.911  -9.008  0.50 39.73 ? 406 MET B O     1 
ATOM   13058 C  CB    A MET B 2 406 ? 32.250  0.621   -12.106 0.50 47.05 ? 406 MET B CB    1 
ATOM   13059 C  CB    B MET B 2 406 ? 32.936  1.003   -11.466 0.50 44.86 ? 406 MET B CB    1 
ATOM   13060 C  CG    A MET B 2 406 ? 32.085  1.740   -11.091 0.50 44.41 ? 406 MET B CG    1 
ATOM   13061 C  CG    B MET B 2 406 ? 33.841  2.223   -11.436 0.50 47.77 ? 406 MET B CG    1 
ATOM   13062 S  SD    A MET B 2 406 ? 32.782  3.302   -11.668 0.50 66.21 ? 406 MET B SD    1 
ATOM   13063 S  SD    B MET B 2 406 ? 34.311  2.682   -9.756  0.50 58.26 ? 406 MET B SD    1 
ATOM   13064 C  CE    A MET B 2 406 ? 34.513  2.870   -11.836 0.50 43.05 ? 406 MET B CE    1 
ATOM   13065 C  CE    B MET B 2 406 ? 32.700  2.970   -9.029  0.50 50.44 ? 406 MET B CE    1 
ATOM   13066 N  N     A GLU B 2 407 ? 31.797  -2.558  -11.295 0.50 36.70 ? 407 GLU B N     1 
ATOM   13067 N  N     B GLU B 2 407 ? 32.094  -2.157  -10.717 0.50 38.46 ? 407 GLU B N     1 
ATOM   13068 C  CA    A GLU B 2 407 ? 31.071  -3.522  -10.477 0.50 38.58 ? 407 GLU B CA    1 
ATOM   13069 C  CA    B GLU B 2 407 ? 31.347  -3.025  -9.811  0.50 38.64 ? 407 GLU B CA    1 
ATOM   13070 C  C     A GLU B 2 407 ? 31.999  -4.319  -9.571  0.50 37.70 ? 407 GLU B C     1 
ATOM   13071 C  C     B GLU B 2 407 ? 32.293  -3.811  -8.913  0.50 38.83 ? 407 GLU B C     1 
ATOM   13072 O  O     A GLU B 2 407 ? 31.555  -4.813  -8.532  0.50 23.69 ? 407 GLU B O     1 
ATOM   13073 O  O     B GLU B 2 407 ? 31.983  -4.065  -7.744  0.50 31.32 ? 407 GLU B O     1 
ATOM   13074 C  CB    A GLU B 2 407 ? 30.261  -4.469  -11.364 0.50 37.41 ? 407 GLU B CB    1 
ATOM   13075 C  CB    B GLU B 2 407 ? 30.434  -3.970  -10.595 0.50 38.58 ? 407 GLU B CB    1 
ATOM   13076 C  CG    A GLU B 2 407 ? 29.171  -3.774  -12.169 0.50 37.75 ? 407 GLU B CG    1 
ATOM   13077 C  CG    B GLU B 2 407 ? 29.487  -4.776  -9.706  0.50 37.04 ? 407 GLU B CG    1 
ATOM   13078 C  CD    A GLU B 2 407 ? 28.363  -4.737  -13.015 0.50 38.08 ? 407 GLU B CD    1 
ATOM   13079 C  CD    B GLU B 2 407 ? 28.403  -5.502  -10.485 0.50 41.41 ? 407 GLU B CD    1 
ATOM   13080 O  OE1   A GLU B 2 407 ? 27.478  -5.421  -12.459 0.50 29.79 ? 407 GLU B OE1   1 
ATOM   13081 O  OE1   B GLU B 2 407 ? 28.433  -5.464  -11.735 0.50 31.37 ? 407 GLU B OE1   1 
ATOM   13082 O  OE2   A GLU B 2 407 ? 28.619  -4.820  -14.236 0.50 35.76 ? 407 GLU B OE2   1 
ATOM   13083 O  OE2   B GLU B 2 407 ? 27.516  -6.108  -9.843  0.50 28.12 ? 407 GLU B OE2   1 
ATOM   13084 N  N     A PHE B 2 408 ? 33.273  -4.455  -9.936  0.50 33.47 ? 408 PHE B N     1 
ATOM   13085 N  N     B PHE B 2 408 ? 33.459  -4.193  -9.441  0.50 33.25 ? 408 PHE B N     1 
ATOM   13086 C  CA    A PHE B 2 408 ? 34.228  -5.100  -9.042  0.50 33.62 ? 408 PHE B CA    1 
ATOM   13087 C  CA    B PHE B 2 408 ? 34.473  -4.840  -8.615  0.50 34.05 ? 408 PHE B CA    1 
ATOM   13088 C  C     A PHE B 2 408 ? 34.566  -4.198  -7.862  0.50 34.37 ? 408 PHE B C     1 
ATOM   13089 C  C     B PHE B 2 408 ? 34.929  -3.920  -7.490  0.50 35.30 ? 408 PHE B C     1 
ATOM   13090 O  O     A PHE B 2 408 ? 34.566  -4.642  -6.708  0.50 34.84 ? 408 PHE B O     1 
ATOM   13091 O  O     B PHE B 2 408 ? 35.058  -4.346  -6.336  0.50 33.54 ? 408 PHE B O     1 
ATOM   13092 C  CB    A PHE B 2 408 ? 35.496  -5.478  -9.811  0.50 30.83 ? 408 PHE B CB    1 
ATOM   13093 C  CB    B PHE B 2 408 ? 35.664  -5.263  -9.482  0.50 30.90 ? 408 PHE B CB    1 
ATOM   13094 C  CG    A PHE B 2 408 ? 35.371  -6.754  -10.588 0.50 30.97 ? 408 PHE B CG    1 
ATOM   13095 C  CG    B PHE B 2 408 ? 35.517  -6.630  -10.094 0.50 29.69 ? 408 PHE B CG    1 
ATOM   13096 C  CD1   A PHE B 2 408 ? 34.891  -6.747  -11.886 0.50 35.00 ? 408 PHE B CD1   1 
ATOM   13097 C  CD1   B PHE B 2 408 ? 34.617  -6.855  -11.124 0.50 32.15 ? 408 PHE B CD1   1 
ATOM   13098 C  CD2   A PHE B 2 408 ? 35.727  -7.964  -10.016 0.50 25.47 ? 408 PHE B CD2   1 
ATOM   13099 C  CD2   B PHE B 2 408 ? 36.286  -7.689  -9.643  0.50 25.71 ? 408 PHE B CD2   1 
ATOM   13100 C  CE1   A PHE B 2 408 ? 34.770  -7.923  -12.600 0.50 31.85 ? 408 PHE B CE1   1 
ATOM   13101 C  CE1   B PHE B 2 408 ? 34.484  -8.113  -11.685 0.50 29.37 ? 408 PHE B CE1   1 
ATOM   13102 C  CE2   A PHE B 2 408 ? 35.611  -9.145  -10.727 0.50 29.10 ? 408 PHE B CE2   1 
ATOM   13103 C  CE2   B PHE B 2 408 ? 36.159  -8.948  -10.202 0.50 29.81 ? 408 PHE B CE2   1 
ATOM   13104 C  CZ    A PHE B 2 408 ? 35.132  -9.123  -12.019 0.50 31.61 ? 408 PHE B CZ    1 
ATOM   13105 C  CZ    B PHE B 2 408 ? 35.258  -9.160  -11.223 0.50 29.75 ? 408 PHE B CZ    1 
ATOM   13106 N  N     A THR B 2 409 ? 34.863  -2.926  -8.136  0.50 37.22 ? 409 THR B N     1 
ATOM   13107 N  N     B THR B 2 409 ? 35.181  -2.647  -7.810  0.50 37.39 ? 409 THR B N     1 
ATOM   13108 C  CA    A THR B 2 409 ? 35.227  -2.006  -7.064  0.50 38.25 ? 409 THR B CA    1 
ATOM   13109 C  CA    B THR B 2 409 ? 35.565  -1.692  -6.776  0.50 39.19 ? 409 THR B CA    1 
ATOM   13110 C  C     A THR B 2 409 ? 34.061  -1.776  -6.109  0.50 36.29 ? 409 THR B C     1 
ATOM   13111 C  C     B THR B 2 409 ? 34.401  -1.378  -5.844  0.50 36.74 ? 409 THR B C     1 
ATOM   13112 O  O     A THR B 2 409 ? 34.256  -1.687  -4.891  0.50 38.23 ? 409 THR B O     1 
ATOM   13113 O  O     B THR B 2 409 ? 34.618  -1.082  -4.663  0.50 39.39 ? 409 THR B O     1 
ATOM   13114 C  CB    A THR B 2 409 ? 35.707  -0.676  -7.648  0.50 38.58 ? 409 THR B CB    1 
ATOM   13115 C  CB    B THR B 2 409 ? 36.093  -0.404  -7.408  0.50 38.71 ? 409 THR B CB    1 
ATOM   13116 O  OG1   A THR B 2 409 ? 34.710  -0.153  -8.535  0.50 43.43 ? 409 THR B OG1   1 
ATOM   13117 O  OG1   B THR B 2 409 ? 35.037  0.255   -8.117  0.50 43.15 ? 409 THR B OG1   1 
ATOM   13118 C  CG2   A THR B 2 409 ? 37.006  -0.864  -8.408  0.50 35.79 ? 409 THR B CG2   1 
ATOM   13119 C  CG2   B THR B 2 409 ? 37.226  -0.710  -8.371  0.50 35.78 ? 409 THR B CG2   1 
ATOM   13120 N  N     A GLU B 2 410 ? 32.839  -1.686  -6.641  0.50 35.79 ? 410 GLU B N     1 
ATOM   13121 N  N     B GLU B 2 410 ? 33.167  -1.429  -6.349  0.50 36.24 ? 410 GLU B N     1 
ATOM   13122 C  CA    A GLU B 2 410 ? 31.683  -1.416  -5.792  0.50 35.60 ? 410 GLU B CA    1 
ATOM   13123 C  CA    B GLU B 2 410 ? 32.017  -1.210  -5.479  0.50 34.81 ? 410 GLU B CA    1 
ATOM   13124 C  C     A GLU B 2 410 ? 31.377  -2.594  -4.872  0.50 35.92 ? 410 GLU B C     1 
ATOM   13125 C  C     B GLU B 2 410 ? 31.780  -2.412  -4.571  0.50 36.85 ? 410 GLU B C     1 
ATOM   13126 O  O     A GLU B 2 410 ? 31.117  -2.403  -3.679  0.50 34.71 ? 410 GLU B O     1 
ATOM   13127 O  O     B GLU B 2 410 ? 31.485  -2.249  -3.382  0.50 34.63 ? 410 GLU B O     1 
ATOM   13128 C  CB    A GLU B 2 410 ? 30.472  -1.069  -6.655  0.50 39.50 ? 410 GLU B CB    1 
ATOM   13129 C  CB    B GLU B 2 410 ? 30.775  -0.899  -6.313  0.50 38.44 ? 410 GLU B CB    1 
ATOM   13130 C  CG    A GLU B 2 410 ? 30.540  0.321   -7.269  0.50 40.41 ? 410 GLU B CG    1 
ATOM   13131 C  CG    B GLU B 2 410 ? 30.831  0.458   -7.002  0.50 39.82 ? 410 GLU B CG    1 
ATOM   13132 C  CD    A GLU B 2 410 ? 29.334  0.641   -8.132  0.50 51.88 ? 410 GLU B CD    1 
ATOM   13133 C  CD    B GLU B 2 410 ? 29.499  0.880   -7.596  0.50 51.70 ? 410 GLU B CD    1 
ATOM   13134 O  OE1   A GLU B 2 410 ? 29.091  -0.094  -9.114  0.50 44.10 ? 410 GLU B OE1   1 
ATOM   13135 O  OE1   B GLU B 2 410 ? 28.467  0.249   -7.271  0.50 46.49 ? 410 GLU B OE1   1 
ATOM   13136 O  OE2   A GLU B 2 410 ? 28.625  1.626   -7.821  0.50 50.97 ? 410 GLU B OE2   1 
ATOM   13137 O  OE2   B GLU B 2 410 ? 29.488  1.847   -8.390  0.50 50.27 ? 410 GLU B OE2   1 
ATOM   13138 N  N     A ALA B 2 411 ? 31.402  -3.818  -5.404  0.50 34.07 ? 411 ALA B N     1 
ATOM   13139 N  N     B ALA B 2 411 ? 31.912  -3.627  -5.108  0.50 33.36 ? 411 ALA B N     1 
ATOM   13140 C  CA    A ALA B 2 411 ? 31.229  -4.988  -4.550  0.50 33.85 ? 411 ALA B CA    1 
ATOM   13141 C  CA    B ALA B 2 411 ? 31.818  -4.815  -4.266  0.50 35.09 ? 411 ALA B CA    1 
ATOM   13142 C  C     A ALA B 2 411 ? 32.361  -5.103  -3.539  0.50 35.06 ? 411 ALA B C     1 
ATOM   13143 C  C     B ALA B 2 411 ? 32.942  -4.848  -3.239  0.50 34.49 ? 411 ALA B C     1 
ATOM   13144 O  O     A ALA B 2 411 ? 32.146  -5.570  -2.415  0.50 28.22 ? 411 ALA B O     1 
ATOM   13145 O  O     B ALA B 2 411 ? 32.728  -5.238  -2.086  0.50 33.41 ? 411 ALA B O     1 
ATOM   13146 C  CB    A ALA B 2 411 ? 31.144  -6.256  -5.400  0.50 30.38 ? 411 ALA B CB    1 
ATOM   13147 C  CB    B ALA B 2 411 ? 31.843  -6.078  -5.126  0.50 33.13 ? 411 ALA B CB    1 
ATOM   13148 N  N     A GLU B 2 412 ? 33.567  -4.682  -3.924  0.50 37.34 ? 412 GLU B N     1 
ATOM   13149 N  N     B GLU B 2 412 ? 34.147  -4.440  -3.645  0.50 36.50 ? 412 GLU B N     1 
ATOM   13150 C  CA    A GLU B 2 412 ? 34.693  -4.660  -2.997  0.50 34.95 ? 412 GLU B CA    1 
ATOM   13151 C  CA    B GLU B 2 412 ? 35.284  -4.409  -2.729  0.50 37.03 ? 412 GLU B CA    1 
ATOM   13152 C  C     A GLU B 2 412 ? 34.525  -3.563  -1.951  0.50 34.16 ? 412 GLU B C     1 
ATOM   13153 C  C     B GLU B 2 412 ? 35.034  -3.454  -1.568  0.50 36.08 ? 412 GLU B C     1 
ATOM   13154 O  O     A GLU B 2 412 ? 34.834  -3.768  -0.771  0.50 34.88 ? 412 GLU B O     1 
ATOM   13155 O  O     B GLU B 2 412 ? 35.339  -3.773  -0.411  0.50 34.17 ? 412 GLU B O     1 
ATOM   13156 C  CB    A GLU B 2 412 ? 35.992  -4.474  -3.783  0.50 37.98 ? 412 GLU B CB    1 
ATOM   13157 C  CB    B GLU B 2 412 ? 36.546  -4.013  -3.500  0.50 38.82 ? 412 GLU B CB    1 
ATOM   13158 C  CG    A GLU B 2 412 ? 37.205  -4.109  -2.952  0.50 38.73 ? 412 GLU B CG    1 
ATOM   13159 C  CG    B GLU B 2 412 ? 37.756  -3.681  -2.647  0.50 38.84 ? 412 GLU B CG    1 
ATOM   13160 C  CD    A GLU B 2 412 ? 38.435  -3.849  -3.809  0.50 41.19 ? 412 GLU B CD    1 
ATOM   13161 C  CD    B GLU B 2 412 ? 39.044  -3.602  -3.457  0.50 40.49 ? 412 GLU B CD    1 
ATOM   13162 O  OE1   A GLU B 2 412 ? 38.284  -3.269  -4.906  0.50 38.15 ? 412 GLU B OE1   1 
ATOM   13163 O  OE1   B GLU B 2 412 ? 39.203  -2.638  -4.234  0.50 30.90 ? 412 GLU B OE1   1 
ATOM   13164 O  OE2   A GLU B 2 412 ? 39.549  -4.232  -3.393  0.50 44.10 ? 412 GLU B OE2   1 
ATOM   13165 O  OE2   B GLU B 2 412 ? 39.895  -4.510  -3.322  0.50 42.22 ? 412 GLU B OE2   1 
ATOM   13166 N  N     A SER B 2 413 ? 34.036  -2.393  -2.367  0.50 35.69 ? 413 SER B N     1 
ATOM   13167 N  N     B SER B 2 413 ? 34.468  -2.281  -1.854  0.50 33.09 ? 413 SER B N     1 
ATOM   13168 C  CA    A SER B 2 413 ? 33.807  -1.303  -1.424  0.50 35.36 ? 413 SER B CA    1 
ATOM   13169 C  CA    B SER B 2 413 ? 34.235  -1.297  -0.804  0.50 33.78 ? 413 SER B CA    1 
ATOM   13170 C  C     A SER B 2 413 ? 32.722  -1.661  -0.417  0.50 32.45 ? 413 SER B C     1 
ATOM   13171 C  C     B SER B 2 413 ? 33.094  -1.722  0.113   0.50 32.51 ? 413 SER B C     1 
ATOM   13172 O  O     A SER B 2 413 ? 32.825  -1.321  0.767   0.50 32.18 ? 413 SER B O     1 
ATOM   13173 O  O     B SER B 2 413 ? 33.138  -1.465  1.322   0.50 33.99 ? 413 SER B O     1 
ATOM   13174 C  CB    A SER B 2 413 ? 33.435  -0.029  -2.181  0.50 36.13 ? 413 SER B CB    1 
ATOM   13175 C  CB    B SER B 2 413 ? 33.945  0.069   -1.427  0.50 34.96 ? 413 SER B CB    1 
ATOM   13176 O  OG    A SER B 2 413 ? 32.794  0.903   -1.330  0.50 36.62 ? 413 SER B OG    1 
ATOM   13177 O  OG    B SER B 2 413 ? 33.880  1.082   -0.440  0.50 43.94 ? 413 SER B OG    1 
ATOM   13178 N  N     A ASN B 2 414 ? 31.675  -2.351  -0.868  0.50 32.01 ? 414 ASN B N     1 
ATOM   13179 N  N     B ASN B 2 414 ? 32.066  -2.373  -0.441  0.50 35.19 ? 414 ASN B N     1 
ATOM   13180 C  CA    A ASN B 2 414 ? 30.594  -2.721  0.042   0.50 33.00 ? 414 ASN B CA    1 
ATOM   13181 C  CA    B ASN B 2 414 ? 30.925  -2.792  0.372   0.50 32.00 ? 414 ASN B CA    1 
ATOM   13182 C  C     A ASN B 2 414 ? 31.023  -3.818  1.011   0.50 33.00 ? 414 ASN B C     1 
ATOM   13183 C  C     B ASN B 2 414 ? 31.346  -3.792  1.444   0.50 32.95 ? 414 ASN B C     1 
ATOM   13184 O  O     A ASN B 2 414 ? 30.537  -3.868  2.149   0.50 29.83 ? 414 ASN B O     1 
ATOM   13185 O  O     B ASN B 2 414 ? 30.835  -3.757  2.571   0.50 27.38 ? 414 ASN B O     1 
ATOM   13186 C  CB    A ASN B 2 414 ? 29.373  -3.162  -0.765  0.50 33.56 ? 414 ASN B CB    1 
ATOM   13187 C  CB    B ASN B 2 414 ? 29.837  -3.379  -0.532  0.50 33.65 ? 414 ASN B CB    1 
ATOM   13188 C  CG    A ASN B 2 414 ? 28.084  -3.027  0.012   0.50 36.82 ? 414 ASN B CG    1 
ATOM   13189 C  CG    B ASN B 2 414 ? 28.505  -3.566  0.184   0.50 36.36 ? 414 ASN B CG    1 
ATOM   13190 O  OD1   A ASN B 2 414 ? 28.004  -2.250  0.962   0.50 36.10 ? 414 ASN B OD1   1 
ATOM   13191 O  OD1   B ASN B 2 414 ? 28.426  -4.236  1.211   0.50 34.52 ? 414 ASN B OD1   1 
ATOM   13192 N  ND2   A ASN B 2 414 ? 27.064  -3.780  -0.386  0.50 35.35 ? 414 ASN B ND2   1 
ATOM   13193 N  ND2   B ASN B 2 414 ? 27.450  -2.972  -0.364  0.50 35.74 ? 414 ASN B ND2   1 
ATOM   13194 N  N     A MET B 2 415 ? 31.928  -4.701  0.583   0.50 31.53 ? 415 MET B N     1 
ATOM   13195 N  N     B MET B 2 415 ? 32.276  -4.693  1.116   0.50 32.45 ? 415 MET B N     1 
ATOM   13196 C  CA    A MET B 2 415 ? 32.342  -5.819  1.425   0.50 30.32 ? 415 MET B CA    1 
ATOM   13197 C  CA    B MET B 2 415 ? 32.729  -5.659  2.113   0.50 31.56 ? 415 MET B CA    1 
ATOM   13198 C  C     A MET B 2 415 ? 33.185  -5.352  2.605   0.50 31.96 ? 415 MET B C     1 
ATOM   13199 C  C     B MET B 2 415 ? 33.644  -5.008  3.141   0.50 33.25 ? 415 MET B C     1 
ATOM   13200 O  O     A MET B 2 415 ? 32.987  -5.809  3.738   0.50 31.58 ? 415 MET B O     1 
ATOM   13201 O  O     B MET B 2 415 ? 33.615  -5.374  4.323   0.50 28.73 ? 415 MET B O     1 
ATOM   13202 C  CB    A MET B 2 415 ? 33.115  -6.838  0.589   0.50 37.17 ? 415 MET B CB    1 
ATOM   13203 C  CB    B MET B 2 415 ? 33.429  -6.840  1.443   0.50 34.65 ? 415 MET B CB    1 
ATOM   13204 C  CG    A MET B 2 415 ? 33.624  -8.041  1.368   0.50 32.45 ? 415 MET B CG    1 
ATOM   13205 C  CG    B MET B 2 415 ? 32.602  -8.113  1.483   0.50 34.12 ? 415 MET B CG    1 
ATOM   13206 S  SD    A MET B 2 415 ? 32.949  -9.574  0.700   0.50 30.26 ? 415 MET B SD    1 
ATOM   13207 S  SD    B MET B 2 415 ? 33.592  -9.590  1.753   0.50 34.44 ? 415 MET B SD    1 
ATOM   13208 C  CE    A MET B 2 415 ? 34.166  -10.760 1.262   0.50 27.60 ? 415 MET B CE    1 
ATOM   13209 C  CE    B MET B 2 415 ? 34.584  -9.619  0.265   0.50 29.63 ? 415 MET B CE    1 
ATOM   13210 N  N     A ASN B 2 416 ? 34.137  -4.450  2.361   0.50 28.01 ? 416 ASN B N     1 
ATOM   13211 N  N     B ASN B 2 416 ? 34.473  -4.053  2.711   0.50 31.46 ? 416 ASN B N     1 
ATOM   13212 C  CA    A ASN B 2 416 ? 35.006  -3.994  3.440   0.50 32.68 ? 416 ASN B CA    1 
ATOM   13213 C  CA    B ASN B 2 416 ? 35.212  -3.237  3.670   0.50 32.31 ? 416 ASN B CA    1 
ATOM   13214 C  C     A ASN B 2 416 ? 34.281  -3.051  4.394   0.50 27.33 ? 416 ASN B C     1 
ATOM   13215 C  C     B ASN B 2 416 ? 34.256  -2.498  4.597   0.50 28.45 ? 416 ASN B C     1 
ATOM   13216 O  O     A ASN B 2 416 ? 34.679  -2.928  5.558   0.50 29.17 ? 416 ASN B O     1 
ATOM   13217 O  O     B ASN B 2 416 ? 34.447  -2.474  5.818   0.50 30.13 ? 416 ASN B O     1 
ATOM   13218 C  CB    A ASN B 2 416 ? 36.254  -3.335  2.860   0.50 26.94 ? 416 ASN B CB    1 
ATOM   13219 C  CB    B ASN B 2 416 ? 36.122  -2.248  2.940   0.50 25.09 ? 416 ASN B CB    1 
ATOM   13220 C  CG    A ASN B 2 416 ? 37.179  -4.339  2.205   0.50 27.07 ? 416 ASN B CG    1 
ATOM   13221 C  CG    B ASN B 2 416 ? 37.356  -2.905  2.364   0.50 27.26 ? 416 ASN B CG    1 
ATOM   13222 O  OD1   A ASN B 2 416 ? 37.282  -5.484  2.653   0.50 31.76 ? 416 ASN B OD1   1 
ATOM   13223 O  OD1   B ASN B 2 416 ? 37.849  -3.898  2.895   0.50 27.40 ? 416 ASN B OD1   1 
ATOM   13224 N  ND2   A ASN B 2 416 ? 37.851  -3.923  1.139   0.50 30.72 ? 416 ASN B ND2   1 
ATOM   13225 N  ND2   B ASN B 2 416 ? 37.870  -2.347  1.273   0.50 36.62 ? 416 ASN B ND2   1 
ATOM   13226 N  N     A ASP B 2 417 ? 33.229  -2.374  3.926   0.50 33.92 ? 417 ASP B N     1 
ATOM   13227 N  N     B ASP B 2 417 ? 33.213  -1.887  4.027   0.50 34.15 ? 417 ASP B N     1 
ATOM   13228 C  CA    A ASP B 2 417 ? 32.356  -1.646  4.843   0.50 29.34 ? 417 ASP B CA    1 
ATOM   13229 C  CA    B ASP B 2 417 ? 32.228  -1.177  4.837   0.50 29.88 ? 417 ASP B CA    1 
ATOM   13230 C  C     A ASP B 2 417 ? 31.730  -2.591  5.861   0.50 32.14 ? 417 ASP B C     1 
ATOM   13231 C  C     B ASP B 2 417 ? 31.378  -2.132  5.665   0.50 31.21 ? 417 ASP B C     1 
ATOM   13232 O  O     A ASP B 2 417 ? 31.674  -2.281  7.058   0.50 30.66 ? 417 ASP B O     1 
ATOM   13233 O  O     B ASP B 2 417 ? 30.920  -1.763  6.752   0.50 25.90 ? 417 ASP B O     1 
ATOM   13234 C  CB    A ASP B 2 417 ? 31.266  -0.909  4.063   0.50 34.05 ? 417 ASP B CB    1 
ATOM   13235 C  CB    B ASP B 2 417 ? 31.340  -0.311  3.945   0.50 35.04 ? 417 ASP B CB    1 
ATOM   13236 C  CG    A ASP B 2 417 ? 31.678  0.495   3.654   0.50 35.08 ? 417 ASP B CG    1 
ATOM   13237 C  CG    B ASP B 2 417 ? 32.095  0.846   3.320   0.50 33.87 ? 417 ASP B CG    1 
ATOM   13238 O  OD1   A ASP B 2 417 ? 32.401  1.160   4.426   0.50 37.38 ? 417 ASP B OD1   1 
ATOM   13239 O  OD1   B ASP B 2 417 ? 33.320  0.947   3.536   0.50 29.47 ? 417 ASP B OD1   1 
ATOM   13240 O  OD2   A ASP B 2 417 ? 31.272  0.936   2.561   0.50 33.29 ? 417 ASP B OD2   1 
ATOM   13241 O  OD2   B ASP B 2 417 ? 31.464  1.658   2.617   0.50 33.75 ? 417 ASP B OD2   1 
ATOM   13242 N  N     A LEU B 2 418 ? 31.257  -3.752  5.396   0.50 27.94 ? 418 LEU B N     1 
ATOM   13243 N  N     B LEU B 2 418 ? 31.149  -3.351  5.168   0.50 29.24 ? 418 LEU B N     1 
ATOM   13244 C  CA    A LEU B 2 418 ? 30.663  -4.748  6.280   0.50 29.91 ? 418 LEU B CA    1 
ATOM   13245 C  CA    B LEU B 2 418 ? 30.478  -4.369  5.969   0.50 28.48 ? 418 LEU B CA    1 
ATOM   13246 C  C     A LEU B 2 418 ? 31.622  -5.152  7.392   0.50 30.47 ? 418 LEU B C     1 
ATOM   13247 C  C     B LEU B 2 418 ? 31.339  -4.771  7.161   0.50 30.15 ? 418 LEU B C     1 
ATOM   13248 O  O     A LEU B 2 418 ? 31.210  -5.327  8.546   0.50 26.08 ? 418 LEU B O     1 
ATOM   13249 O  O     B LEU B 2 418 ? 30.870  -4.770  8.307   0.50 23.77 ? 418 LEU B O     1 
ATOM   13250 C  CB    A LEU B 2 418 ? 30.239  -5.971  5.463   0.50 27.24 ? 418 LEU B CB    1 
ATOM   13251 C  CB    B LEU B 2 418 ? 30.143  -5.584  5.100   0.50 27.20 ? 418 LEU B CB    1 
ATOM   13252 C  CG    A LEU B 2 418 ? 29.397  -7.056  6.135   0.50 29.57 ? 418 LEU B CG    1 
ATOM   13253 C  CG    B LEU B 2 418 ? 29.486  -6.799  5.759   0.50 29.18 ? 418 LEU B CG    1 
ATOM   13254 C  CD1   A LEU B 2 418 ? 28.032  -6.507  6.523   0.50 28.47 ? 418 LEU B CD1   1 
ATOM   13255 C  CD1   B LEU B 2 418 ? 28.198  -6.405  6.475   0.50 28.77 ? 418 LEU B CD1   1 
ATOM   13256 C  CD2   A LEU B 2 418 ? 29.251  -8.261  5.221   0.50 27.59 ? 418 LEU B CD2   1 
ATOM   13257 C  CD2   B LEU B 2 418 ? 29.212  -7.878  4.723   0.50 26.56 ? 418 LEU B CD2   1 
ATOM   13258 N  N     A VAL B 2 419 ? 32.910  -5.295  7.066   0.50 26.25 ? 419 VAL B N     1 
ATOM   13259 N  N     B VAL B 2 419 ? 32.606  -5.116  6.905   0.50 27.01 ? 419 VAL B N     1 
ATOM   13260 C  CA    A VAL B 2 419 ? 33.905  -5.645  8.078   0.50 28.18 ? 419 VAL B CA    1 
ATOM   13261 C  CA    B VAL B 2 419 ? 33.570  -5.319  7.986   0.50 27.00 ? 419 VAL B CA    1 
ATOM   13262 C  C     A VAL B 2 419 ? 34.021  -4.540  9.122   0.50 25.38 ? 419 VAL B C     1 
ATOM   13263 C  C     B VAL B 2 419 ? 33.617  -4.095  8.891   0.50 23.60 ? 419 VAL B C     1 
ATOM   13264 O  O     A VAL B 2 419 ? 34.138  -4.810  10.325  0.50 28.66 ? 419 VAL B O     1 
ATOM   13265 O  O     B VAL B 2 419 ? 33.697  -4.209  10.121  0.50 28.31 ? 419 VAL B O     1 
ATOM   13266 C  CB    A VAL B 2 419 ? 35.263  -5.937  7.410   0.50 27.52 ? 419 VAL B CB    1 
ATOM   13267 C  CB    B VAL B 2 419 ? 34.960  -5.645  7.401   0.50 29.23 ? 419 VAL B CB    1 
ATOM   13268 C  CG1   A VAL B 2 419 ? 36.323  -6.219  8.461   0.50 24.17 ? 419 VAL B CG1   1 
ATOM   13269 C  CG1   B VAL B 2 419 ? 36.062  -5.238  8.368   0.50 24.17 ? 419 VAL B CG1   1 
ATOM   13270 C  CG2   A VAL B 2 419 ? 35.139  -7.110  6.445   0.50 28.98 ? 419 VAL B CG2   1 
ATOM   13271 C  CG2   B VAL B 2 419 ? 35.064  -7.129  7.066   0.50 28.58 ? 419 VAL B CG2   1 
ATOM   13272 N  N     A SER B 2 420 ? 33.994  -3.280  8.681   0.50 24.52 ? 420 SER B N     1 
ATOM   13273 N  N     B SER B 2 420 ? 33.549  -2.903  8.296   0.50 26.41 ? 420 SER B N     1 
ATOM   13274 C  CA    A SER B 2 420 ? 34.064  -2.165  9.618   0.50 27.33 ? 420 SER B CA    1 
ATOM   13275 C  CA    B SER B 2 420 ? 33.610  -1.679  9.086   0.50 28.68 ? 420 SER B CA    1 
ATOM   13276 C  C     A SER B 2 420 ? 32.831  -2.111  10.509  0.50 24.46 ? 420 SER B C     1 
ATOM   13277 C  C     B SER B 2 420 ? 32.431  -1.578  10.045  0.50 25.03 ? 420 SER B C     1 
ATOM   13278 O  O     A SER B 2 420 ? 32.932  -1.739  11.683  0.50 24.92 ? 420 SER B O     1 
ATOM   13279 O  O     B SER B 2 420 ? 32.576  -1.075  11.165  0.50 23.16 ? 420 SER B O     1 
ATOM   13280 C  CB    A SER B 2 420 ? 34.219  -0.844  8.862   0.50 26.74 ? 420 SER B CB    1 
ATOM   13281 C  CB    B SER B 2 420 ? 33.648  -0.462  8.165   0.50 25.43 ? 420 SER B CB    1 
ATOM   13282 O  OG    A SER B 2 420 ? 35.204  -0.941  7.844   0.50 28.67 ? 420 SER B OG    1 
ATOM   13283 O  OG    B SER B 2 420 ? 33.763  0.733   8.910   0.50 26.30 ? 420 SER B OG    1 
ATOM   13284 N  N     A GLU B 2 421 ? 31.666  -2.480  9.972   0.50 26.79 ? 421 GLU B N     1 
ATOM   13285 N  N     B GLU B 2 421 ? 31.255  -2.044  9.620   0.50 26.00 ? 421 GLU B N     1 
ATOM   13286 C  CA    A GLU B 2 421 ? 30.435  -2.423  10.756  0.50 26.16 ? 421 GLU B CA    1 
ATOM   13287 C  CA    B GLU B 2 421 ? 30.081  -1.987  10.484  0.50 26.08 ? 421 GLU B CA    1 
ATOM   13288 C  C     A GLU B 2 421 ? 30.450  -3.443  11.890  0.50 28.36 ? 421 GLU B C     1 
ATOM   13289 C  C     B GLU B 2 421 ? 30.129  -3.055  11.572  0.50 27.31 ? 421 GLU B C     1 
ATOM   13290 O  O     A GLU B 2 421 ? 30.067  -3.124  13.022  0.50 28.31 ? 421 GLU B O     1 
ATOM   13291 O  O     B GLU B 2 421 ? 29.659  -2.821  12.691  0.50 30.32 ? 421 GLU B O     1 
ATOM   13292 C  CB    A GLU B 2 421 ? 29.229  -2.626  9.837   0.50 28.39 ? 421 GLU B CB    1 
ATOM   13293 C  CB    B GLU B 2 421 ? 28.805  -2.120  9.650   0.50 29.41 ? 421 GLU B CB    1 
ATOM   13294 C  CG    A GLU B 2 421 ? 29.038  -1.491  8.831   0.50 28.04 ? 421 GLU B CG    1 
ATOM   13295 C  CG    B GLU B 2 421 ? 27.531  -1.865  10.441  0.50 24.31 ? 421 GLU B CG    1 
ATOM   13296 C  CD    A GLU B 2 421 ? 28.027  -1.805  7.744   0.50 32.68 ? 421 GLU B CD    1 
ATOM   13297 C  CD    B GLU B 2 421 ? 26.294  -1.813  9.569   0.50 22.95 ? 421 GLU B CD    1 
ATOM   13298 O  OE1   A GLU B 2 421 ? 27.032  -2.510  8.026   0.50 32.62 ? 421 GLU B OE1   1 
ATOM   13299 O  OE1   B GLU B 2 421 ? 26.385  -1.335  8.424   0.50 30.57 ? 421 GLU B OE1   1 
ATOM   13300 O  OE2   A GLU B 2 421 ? 28.232  -1.343  6.596   0.50 30.94 ? 421 GLU B OE2   1 
ATOM   13301 O  OE2   B GLU B 2 421 ? 25.224  -2.250  10.034  0.50 30.06 ? 421 GLU B OE2   1 
ATOM   13302 N  N     A TYR B 2 422 ? 30.896  -4.672  11.615  0.50 21.90 ? 422 TYR B N     1 
ATOM   13303 N  N     B TYR B 2 422 ? 30.685  -4.233  11.265  0.50 21.78 ? 422 TYR B N     1 
ATOM   13304 C  CA    A TYR B 2 422 ? 31.020  -5.660  12.684  0.50 27.53 ? 422 TYR B CA    1 
ATOM   13305 C  CA    B TYR B 2 422 ? 30.857  -5.257  12.292  0.50 24.79 ? 422 TYR B CA    1 
ATOM   13306 C  C     A TYR B 2 422 ? 32.007  -5.201  13.750  0.50 32.31 ? 422 TYR B C     1 
ATOM   13307 C  C     B TYR B 2 422 ? 31.772  -4.773  13.411  0.50 30.99 ? 422 TYR B C     1 
ATOM   13308 O  O     A TYR B 2 422 ? 31.759  -5.371  14.951  0.50 23.43 ? 422 TYR B O     1 
ATOM   13309 O  O     B TYR B 2 422 ? 31.497  -5.002  14.597  0.50 28.59 ? 422 TYR B O     1 
ATOM   13310 C  CB    A TYR B 2 422 ? 31.449  -7.011  12.111  0.50 28.62 ? 422 TYR B CB    1 
ATOM   13311 C  CB    B TYR B 2 422 ? 31.423  -6.537  11.677  0.50 27.28 ? 422 TYR B CB    1 
ATOM   13312 C  CG    A TYR B 2 422 ? 30.340  -7.742  11.391  0.50 28.87 ? 422 TYR B CG    1 
ATOM   13313 C  CG    B TYR B 2 422 ? 30.392  -7.458  11.066  0.50 28.39 ? 422 TYR B CG    1 
ATOM   13314 C  CD1   A TYR B 2 422 ? 29.253  -8.249  12.087  0.50 25.70 ? 422 TYR B CD1   1 
ATOM   13315 C  CD1   B TYR B 2 422 ? 29.362  -7.988  11.833  0.50 25.63 ? 422 TYR B CD1   1 
ATOM   13316 C  CD2   A TYR B 2 422 ? 30.385  -7.931  10.019  0.50 29.52 ? 422 TYR B CD2   1 
ATOM   13317 C  CD2   B TYR B 2 422 ? 30.466  -7.821  9.729   0.50 30.59 ? 422 TYR B CD2   1 
ATOM   13318 C  CE1   A TYR B 2 422 ? 28.232  -8.918  11.432  0.50 29.09 ? 422 TYR B CE1   1 
ATOM   13319 C  CE1   B TYR B 2 422 ? 28.419  -8.838  11.276  0.50 29.22 ? 422 TYR B CE1   1 
ATOM   13320 C  CE2   A TYR B 2 422 ? 29.374  -8.598  9.356   0.50 27.80 ? 422 TYR B CE2   1 
ATOM   13321 C  CE2   B TYR B 2 422 ? 29.532  -8.670  9.166   0.50 27.54 ? 422 TYR B CE2   1 
ATOM   13322 C  CZ    A TYR B 2 422 ? 28.299  -9.087  10.067  0.50 26.78 ? 422 TYR B CZ    1 
ATOM   13323 C  CZ    B TYR B 2 422 ? 28.510  -9.172  9.942   0.50 27.38 ? 422 TYR B CZ    1 
ATOM   13324 O  OH    A TYR B 2 422 ? 27.298  -9.754  9.403   0.50 30.62 ? 422 TYR B OH    1 
ATOM   13325 O  OH    B TYR B 2 422 ? 27.590  -10.024 9.378   0.50 27.41 ? 422 TYR B OH    1 
ATOM   13326 N  N     A GLN B 2 423 ? 33.133  -4.619  13.331  0.50 28.30 ? 423 GLN B N     1 
ATOM   13327 N  N     B GLN B 2 423 ? 32.874  -4.109  13.049  0.50 26.27 ? 423 GLN B N     1 
ATOM   13328 C  CA    A GLN B 2 423 ? 34.123  -4.140  14.290  0.50 28.94 ? 423 GLN B CA    1 
ATOM   13329 C  CA    B GLN B 2 423 ? 33.842  -3.670  14.049  0.50 28.39 ? 423 GLN B CA    1 
ATOM   13330 C  C     A GLN B 2 423 ? 33.577  -2.981  15.116  0.50 30.41 ? 423 GLN B C     1 
ATOM   13331 C  C     B GLN B 2 423 ? 33.277  -2.550  14.915  0.50 29.09 ? 423 GLN B C     1 
ATOM   13332 O  O     A GLN B 2 423 ? 33.877  -2.867  16.311  0.50 30.27 ? 423 GLN B O     1 
ATOM   13333 O  O     B GLN B 2 423 ? 33.576  -2.474  16.113  0.50 31.02 ? 423 GLN B O     1 
ATOM   13334 C  CB    A GLN B 2 423 ? 35.402  -3.727  13.556  0.50 29.31 ? 423 GLN B CB    1 
ATOM   13335 C  CB    B GLN B 2 423 ? 35.133  -3.222  13.359  0.50 27.38 ? 423 GLN B CB    1 
ATOM   13336 C  CG    A GLN B 2 423 ? 36.574  -3.394  14.473  0.50 32.27 ? 423 GLN B CG    1 
ATOM   13337 C  CG    B GLN B 2 423 ? 36.257  -2.818  14.309  0.50 33.48 ? 423 GLN B CG    1 
ATOM   13338 C  CD    A GLN B 2 423 ? 37.142  -4.619  15.171  0.50 33.99 ? 423 GLN B CD    1 
ATOM   13339 C  CD    B GLN B 2 423 ? 36.879  -4.004  15.027  0.50 32.09 ? 423 GLN B CD    1 
ATOM   13340 O  OE1   A GLN B 2 423 ? 36.970  -5.747  14.709  0.50 35.58 ? 423 GLN B OE1   1 
ATOM   13341 O  OE1   B GLN B 2 423 ? 37.656  -4.759  14.442  0.50 39.76 ? 423 GLN B OE1   1 
ATOM   13342 N  NE2   A GLN B 2 423 ? 37.823  -4.403  16.291  0.50 30.60 ? 423 GLN B NE2   1 
ATOM   13343 N  NE2   B GLN B 2 423 ? 36.535  -4.176  16.300  0.50 39.50 ? 423 GLN B NE2   1 
ATOM   13344 N  N     A GLN B 2 424 ? 32.775  -2.113  14.494  0.50 26.21 ? 424 GLN B N     1 
ATOM   13345 N  N     B GLN B 2 424 ? 32.454  -1.678  14.326  0.50 27.32 ? 424 GLN B N     1 
ATOM   13346 C  CA    A GLN B 2 424 ? 32.164  -0.998  15.211  0.50 31.44 ? 424 GLN B CA    1 
ATOM   13347 C  CA    B GLN B 2 424 ? 31.889  -0.559  15.076  0.50 30.88 ? 424 GLN B CA    1 
ATOM   13348 C  C     A GLN B 2 424 ? 31.336  -1.494  16.389  0.50 30.50 ? 424 GLN B C     1 
ATOM   13349 C  C     B GLN B 2 424 ? 31.073  -1.034  16.269  0.50 30.01 ? 424 GLN B C     1 
ATOM   13350 O  O     A GLN B 2 424 ? 31.618  -1.170  17.548  0.50 29.04 ? 424 GLN B O     1 
ATOM   13351 O  O     B GLN B 2 424 ? 31.017  -0.345  17.293  0.50 31.43 ? 424 GLN B O     1 
ATOM   13352 C  CB    A GLN B 2 424 ? 31.301  -0.176  14.253  0.50 34.91 ? 424 GLN B CB    1 
ATOM   13353 C  CB    B GLN B 2 424 ? 31.028  0.306   14.155  0.50 34.68 ? 424 GLN B CB    1 
ATOM   13354 C  CG    A GLN B 2 424 ? 30.339  0.777   14.941  0.50 31.52 ? 424 GLN B CG    1 
ATOM   13355 C  CG    B GLN B 2 424 ? 30.324  1.459   14.852  0.50 31.45 ? 424 GLN B CG    1 
ATOM   13356 C  CD    A GLN B 2 424 ? 29.233  1.251   14.018  0.50 34.54 ? 424 GLN B CD    1 
ATOM   13357 C  CD    B GLN B 2 424 ? 29.368  2.195   13.937  0.50 38.45 ? 424 GLN B CD    1 
ATOM   13358 O  OE1   A GLN B 2 424 ? 29.344  1.149   12.796  0.50 36.90 ? 424 GLN B OE1   1 
ATOM   13359 O  OE1   B GLN B 2 424 ? 29.680  2.453   12.774  0.50 37.03 ? 424 GLN B OE1   1 
ATOM   13360 N  NE2   A GLN B 2 424 ? 28.157  1.773   14.600  0.50 31.76 ? 424 GLN B NE2   1 
ATOM   13361 N  NE2   B GLN B 2 424 ? 28.188  2.532   14.456  0.50 32.34 ? 424 GLN B NE2   1 
ATOM   13362 N  N     A TYR B 2 425 ? 30.308  -2.298  16.109  0.50 29.15 ? 425 TYR B N     1 
ATOM   13363 N  N     B TYR B 2 425 ? 30.450  -2.208  16.167  0.50 29.19 ? 425 TYR B N     1 
ATOM   13364 C  CA    A TYR B 2 425 ? 29.465  -2.817  17.180  0.50 34.40 ? 425 TYR B CA    1 
ATOM   13365 C  CA    B TYR B 2 425 ? 29.632  -2.731  17.254  0.50 34.40 ? 425 TYR B CA    1 
ATOM   13366 C  C     A TYR B 2 425 ? 30.213  -3.792  18.078  0.50 31.42 ? 425 TYR B C     1 
ATOM   13367 C  C     B TYR B 2 425 ? 30.372  -3.717  18.146  0.50 31.78 ? 425 TYR B C     1 
ATOM   13368 O  O     A TYR B 2 425 ? 29.793  -4.013  19.218  0.50 36.26 ? 425 TYR B O     1 
ATOM   13369 O  O     B TYR B 2 425 ? 29.880  -4.032  19.233  0.50 36.16 ? 425 TYR B O     1 
ATOM   13370 C  CB    A TYR B 2 425 ? 28.214  -3.470  16.588  0.50 31.00 ? 425 TYR B CB    1 
ATOM   13371 C  CB    B TYR B 2 425 ? 28.358  -3.375  16.692  0.50 31.33 ? 425 TYR B CB    1 
ATOM   13372 C  CG    A TYR B 2 425 ? 27.376  -2.497  15.788  0.50 28.60 ? 425 TYR B CG    1 
ATOM   13373 C  CG    B TYR B 2 425 ? 27.476  -2.355  16.011  0.50 29.29 ? 425 TYR B CG    1 
ATOM   13374 C  CD1   A TYR B 2 425 ? 26.780  -1.401  16.402  0.50 31.10 ? 425 TYR B CD1   1 
ATOM   13375 C  CD1   B TYR B 2 425 ? 26.949  -1.287  16.726  0.50 31.55 ? 425 TYR B CD1   1 
ATOM   13376 C  CD2   A TYR B 2 425 ? 27.187  -2.666  14.423  0.50 27.08 ? 425 TYR B CD2   1 
ATOM   13377 C  CD2   B TYR B 2 425 ? 27.189  -2.443  14.656  0.50 26.92 ? 425 TYR B CD2   1 
ATOM   13378 C  CE1   A TYR B 2 425 ? 26.020  -0.503  15.681  0.50 30.85 ? 425 TYR B CE1   1 
ATOM   13379 C  CE1   B TYR B 2 425 ? 26.156  -0.342  16.118  0.50 29.80 ? 425 TYR B CE1   1 
ATOM   13380 C  CE2   A TYR B 2 425 ? 26.427  -1.774  13.692  0.50 27.41 ? 425 TYR B CE2   1 
ATOM   13381 C  CE2   B TYR B 2 425 ? 26.392  -1.501  14.036  0.50 28.38 ? 425 TYR B CE2   1 
ATOM   13382 C  CZ    A TYR B 2 425 ? 25.846  -0.693  14.327  0.50 28.69 ? 425 TYR B CZ    1 
ATOM   13383 C  CZ    B TYR B 2 425 ? 25.880  -0.451  14.772  0.50 28.62 ? 425 TYR B CZ    1 
ATOM   13384 O  OH    A TYR B 2 425 ? 25.089  0.198   13.603  0.50 32.50 ? 425 TYR B OH    1 
ATOM   13385 O  OH    B TYR B 2 425 ? 25.088  0.492   14.164  0.50 31.80 ? 425 TYR B OH    1 
ATOM   13386 N  N     A GLN B 2 426 ? 31.317  -4.368  17.597  0.50 31.57 ? 426 GLN B N     1 
ATOM   13387 N  N     B GLN B 2 426 ? 31.541  -4.202  17.727  0.50 31.38 ? 426 GLN B N     1 
ATOM   13388 C  CA    A GLN B 2 426 ? 32.166  -5.186  18.456  0.50 28.08 ? 426 GLN B CA    1 
ATOM   13389 C  CA    B GLN B 2 426 ? 32.380  -4.970  18.638  0.50 27.79 ? 426 GLN B CA    1 
ATOM   13390 C  C     A GLN B 2 426 ? 32.812  -4.356  19.557  0.50 35.94 ? 426 GLN B C     1 
ATOM   13391 C  C     B GLN B 2 426 ? 33.126  -4.062  19.608  0.50 37.33 ? 426 GLN B C     1 
ATOM   13392 O  O     A GLN B 2 426 ? 33.110  -4.882  20.636  0.50 37.32 ? 426 GLN B O     1 
ATOM   13393 O  O     B GLN B 2 426 ? 33.447  -4.482  20.726  0.50 38.89 ? 426 GLN B O     1 
ATOM   13394 C  CB    A GLN B 2 426 ? 33.231  -5.882  17.605  0.50 32.68 ? 426 GLN B CB    1 
ATOM   13395 C  CB    B GLN B 2 426 ? 33.365  -5.834  17.844  0.50 33.07 ? 426 GLN B CB    1 
ATOM   13396 C  CG    A GLN B 2 426 ? 34.197  -6.775  18.353  0.50 32.63 ? 426 GLN B CG    1 
ATOM   13397 C  CG    B GLN B 2 426 ? 34.235  -6.746  18.695  0.50 32.58 ? 426 GLN B CG    1 
ATOM   13398 C  CD    A GLN B 2 426 ? 35.091  -7.552  17.406  0.50 36.81 ? 426 GLN B CD    1 
ATOM   13399 C  CD    B GLN B 2 426 ? 35.063  -7.704  17.861  0.50 35.90 ? 426 GLN B CD    1 
ATOM   13400 O  OE1   A GLN B 2 426 ? 34.616  -8.132  16.427  0.50 32.64 ? 426 GLN B OE1   1 
ATOM   13401 O  OE1   B GLN B 2 426 ? 34.536  -8.395  16.987  0.50 30.86 ? 426 GLN B OE1   1 
ATOM   13402 N  NE2   A GLN B 2 426 ? 36.394  -7.555  17.681  0.50 32.14 ? 426 GLN B NE2   1 
ATOM   13403 N  NE2   B GLN B 2 426 ? 36.368  -7.747  18.122  0.50 33.41 ? 426 GLN B NE2   1 
ATOM   13404 N  N     A ASP B 2 427 ? 33.024  -3.063  19.313  0.50 36.36 ? 427 ASP B N     1 
ATOM   13405 N  N     B ASP B 2 427 ? 33.391  -2.815  19.210  0.50 37.07 ? 427 ASP B N     1 
ATOM   13406 C  CA    A ASP B 2 427 ? 33.620  -2.163  20.291  0.50 37.73 ? 427 ASP B CA    1 
ATOM   13407 C  CA    B ASP B 2 427 ? 34.107  -1.865  20.052  0.50 37.06 ? 427 ASP B CA    1 
ATOM   13408 C  C     A ASP B 2 427 ? 32.601  -1.252  20.963  0.50 38.31 ? 427 ASP B C     1 
ATOM   13409 C  C     B ASP B 2 427 ? 33.190  -1.014  20.919  0.50 38.47 ? 427 ASP B C     1 
ATOM   13410 O  O     A ASP B 2 427 ? 32.971  -0.494  21.865  0.50 40.09 ? 427 ASP B O     1 
ATOM   13411 O  O     B ASP B 2 427 ? 33.648  -0.478  21.934  0.50 39.19 ? 427 ASP B O     1 
ATOM   13412 C  CB    A ASP B 2 427 ? 34.711  -1.310  19.633  0.50 31.31 ? 427 ASP B CB    1 
ATOM   13413 C  CB    B ASP B 2 427 ? 34.966  -0.932  19.193  0.50 30.05 ? 427 ASP B CB    1 
ATOM   13414 C  CG    A ASP B 2 427 ? 35.953  -2.110  19.299  0.50 34.34 ? 427 ASP B CG    1 
ATOM   13415 C  CG    B ASP B 2 427 ? 35.984  -1.678  18.355  0.50 39.73 ? 427 ASP B CG    1 
ATOM   13416 O  OD1   A ASP B 2 427 ? 36.280  -3.046  20.059  0.50 39.62 ? 427 ASP B OD1   1 
ATOM   13417 O  OD1   B ASP B 2 427 ? 36.519  -2.700  18.836  0.50 37.12 ? 427 ASP B OD1   1 
ATOM   13418 O  OD2   A ASP B 2 427 ? 36.604  -1.807  18.277  0.50 41.28 ? 427 ASP B OD2   1 
ATOM   13419 O  OD2   B ASP B 2 427 ? 36.250  -1.239  17.213  0.50 35.65 ? 427 ASP B OD2   1 
ATOM   13420 N  N     A ALA B 2 428 ? 31.339  -1.297  20.544  0.50 37.64 ? 428 ALA B N     1 
ATOM   13421 N  N     B ALA B 2 428 ? 31.922  -0.866  20.539  0.50 37.99 ? 428 ALA B N     1 
ATOM   13422 C  CA    A ALA B 2 428 ? 30.318  -0.464  21.162  0.50 41.81 ? 428 ALA B CA    1 
ATOM   13423 C  CA    B ALA B 2 428 ? 31.021  0.024   21.259  0.50 41.35 ? 428 ALA B CA    1 
ATOM   13424 C  C     A ALA B 2 428 ? 30.037  -0.935  22.583  0.50 43.93 ? 428 ALA B C     1 
ATOM   13425 C  C     B ALA B 2 428 ? 30.822  -0.448  22.695  0.50 45.12 ? 428 ALA B C     1 
ATOM   13426 O  O     A ALA B 2 428 ? 29.950  -2.136  22.852  0.50 46.61 ? 428 ALA B O     1 
ATOM   13427 O  O     B ALA B 2 428 ? 30.942  -1.636  23.008  0.50 45.47 ? 428 ALA B O     1 
ATOM   13428 C  CB    A ALA B 2 428 ? 29.032  -0.489  20.336  0.50 35.18 ? 428 ALA B CB    1 
ATOM   13429 C  CB    B ALA B 2 428 ? 29.672  0.109   20.543  0.50 40.42 ? 428 ALA B CB    1 
ATOM   13430 N  N     A THR B 2 429 ? 29.904  0.022   23.498  0.50 45.40 ? 429 THR B N     1 
ATOM   13431 N  N     B THR B 2 429 ? 30.530  0.508   23.577  0.50 43.42 ? 429 THR B N     1 
ATOM   13432 C  CA    A THR B 2 429 ? 29.641  -0.252  24.902  0.50 47.53 ? 429 THR B CA    1 
ATOM   13433 C  CA    B THR B 2 429 ? 30.241  0.232   24.975  0.50 49.14 ? 429 THR B CA    1 
ATOM   13434 C  C     A THR B 2 429 ? 28.308  0.367   25.304  0.50 44.56 ? 429 THR B C     1 
ATOM   13435 C  C     B THR B 2 429 ? 28.898  0.848   25.339  0.50 46.44 ? 429 THR B C     1 
ATOM   13436 O  O     A THR B 2 429 ? 27.692  1.122   24.548  0.50 45.21 ? 429 THR B O     1 
ATOM   13437 O  O     B THR B 2 429 ? 28.467  1.835   24.736  0.50 45.96 ? 429 THR B O     1 
ATOM   13438 C  CB    A THR B 2 429 ? 30.764  0.293   25.796  0.50 51.39 ? 429 THR B CB    1 
ATOM   13439 C  CB    B THR B 2 429 ? 31.328  0.786   25.913  0.50 50.68 ? 429 THR B CB    1 
ATOM   13440 O  OG1   A THR B 2 429 ? 30.658  1.720   25.880  0.50 48.37 ? 429 THR B OG1   1 
ATOM   13441 O  OG1   B THR B 2 429 ? 31.200  2.210   26.007  0.50 51.41 ? 429 THR B OG1   1 
ATOM   13442 C  CG2   A THR B 2 429 ? 32.127  -0.072  25.225  0.50 48.13 ? 429 THR B CG2   1 
ATOM   13443 C  CG2   B THR B 2 429 ? 32.716  0.442   25.392  0.50 47.17 ? 429 THR B CG2   1 
ATOM   13444 N  N     A ALA B 2 430 ? 27.863  0.038   26.517  0.50 49.73 ? 430 ALA B N     1 
ATOM   13445 N  N     B ALA B 2 430 ? 28.242  0.257   26.338  0.50 51.10 ? 430 ALA B N     1 
ATOM   13446 C  CA    A ALA B 2 430 ? 26.640  0.624   27.055  0.50 52.55 ? 430 ALA B CA    1 
ATOM   13447 C  CA    B ALA B 2 430 ? 26.947  0.769   26.785  0.50 52.18 ? 430 ALA B CA    1 
ATOM   13448 C  C     A ALA B 2 430 ? 26.927  1.873   27.881  0.50 60.08 ? 430 ALA B C     1 
ATOM   13449 C  C     B ALA B 2 430 ? 27.124  1.943   27.745  0.50 59.52 ? 430 ALA B C     1 
ATOM   13450 O  O     A ALA B 2 430 ? 26.339  2.931   27.632  0.50 60.52 ? 430 ALA B O     1 
ATOM   13451 O  O     B ALA B 2 430 ? 26.887  3.099   27.379  0.50 61.86 ? 430 ALA B O     1 
ATOM   13452 C  CB    A ALA B 2 430 ? 25.881  -0.404  27.900  0.50 44.97 ? 430 ALA B CB    1 
ATOM   13453 C  CB    B ALA B 2 430 ? 26.131  -0.353  27.437  0.50 46.51 ? 430 ALA B CB    1 
ATOM   13454 N  N     A ASP B 2 431 ? 27.825  1.759   28.859  0.50 60.37 ? 431 ASP B N     1 
ATOM   13455 N  N     B ASP B 2 431 ? 27.541  1.654   28.977  0.50 60.77 ? 431 ASP B N     1 
ATOM   13456 C  CA    A ASP B 2 431 ? 28.174  2.860   29.759  0.50 61.01 ? 431 ASP B CA    1 
ATOM   13457 C  CA    B ASP B 2 431 ? 27.673  2.656   30.035  0.50 60.35 ? 431 ASP B CA    1 
ATOM   13458 C  C     A ASP B 2 431 ? 26.945  3.458   30.436  0.50 59.59 ? 431 ASP B C     1 
ATOM   13459 C  C     B ASP B 2 431 ? 26.355  3.389   30.271  0.50 59.11 ? 431 ASP B C     1 
ATOM   13460 O  O     A ASP B 2 431 ? 26.814  3.408   31.659  0.50 57.98 ? 431 ASP B O     1 
ATOM   13461 O  O     B ASP B 2 431 ? 25.277  2.820   30.095  0.50 49.12 ? 431 ASP B O     1 
ATOM   13462 C  CB    A ASP B 2 431 ? 28.943  3.948   29.005  0.50 63.97 ? 431 ASP B CB    1 
ATOM   13463 C  CB    B ASP B 2 431 ? 28.783  3.659   29.704  0.50 62.93 ? 431 ASP B CB    1 
ATOM   13464 C  CG    A ASP B 2 431 ? 30.426  3.648   28.900  0.50 64.40 ? 431 ASP B CG    1 
ATOM   13465 C  CG    B ASP B 2 431 ? 30.147  3.004   29.600  0.50 62.29 ? 431 ASP B CG    1 
ATOM   13466 O  OD1   A ASP B 2 431 ? 31.051  3.369   29.946  0.50 62.38 ? 431 ASP B OD1   1 
ATOM   13467 O  OD1   B ASP B 2 431 ? 30.448  2.118   30.427  0.50 65.62 ? 431 ASP B OD1   1 
ATOM   13468 O  OD2   A ASP B 2 431 ? 30.965  3.685   27.773  0.50 60.82 ? 431 ASP B OD2   1 
ATOM   13469 O  OD2   B ASP B 2 431 ? 30.917  3.374   28.688  0.50 65.25 ? 431 ASP B OD2   1 
ATOM   13470 N  N     A ASP C 3 13  ? 54.537  -5.197  -37.094 0.50 41.41 ? 13  ASP F N     1 
ATOM   13471 N  N     B ASP C 3 13  ? 53.213  -5.781  -36.968 0.50 42.09 ? 13  ASP F N     1 
ATOM   13472 C  CA    A ASP C 3 13  ? 54.908  -5.450  -35.707 0.50 38.42 ? 13  ASP F CA    1 
ATOM   13473 C  CA    B ASP C 3 13  ? 53.686  -5.851  -35.591 0.50 40.59 ? 13  ASP F CA    1 
ATOM   13474 C  C     A ASP C 3 13  ? 54.362  -6.797  -35.251 0.50 36.42 ? 13  ASP F C     1 
ATOM   13475 C  C     B ASP C 3 13  ? 53.572  -7.277  -35.066 0.50 39.36 ? 13  ASP F C     1 
ATOM   13476 O  O     A ASP C 3 13  ? 53.163  -6.938  -35.009 0.50 41.30 ? 13  ASP F O     1 
ATOM   13477 O  O     B ASP C 3 13  ? 52.550  -7.664  -34.497 0.50 38.66 ? 13  ASP F O     1 
ATOM   13478 C  CB    A ASP C 3 13  ? 54.389  -4.330  -34.799 0.50 41.35 ? 13  ASP F CB    1 
ATOM   13479 C  CB    B ASP C 3 13  ? 52.896  -4.885  -34.703 0.50 36.21 ? 13  ASP F CB    1 
ATOM   13480 C  CG    A ASP C 3 13  ? 55.064  -4.316  -33.439 0.50 39.69 ? 13  ASP F CG    1 
ATOM   13481 C  CG    B ASP C 3 13  ? 53.540  -4.677  -33.341 0.50 42.48 ? 13  ASP F CG    1 
ATOM   13482 O  OD1   A ASP C 3 13  ? 55.952  -5.161  -33.201 0.50 36.98 ? 13  ASP F OD1   1 
ATOM   13483 O  OD1   B ASP C 3 13  ? 54.511  -5.392  -33.014 0.50 36.86 ? 13  ASP F OD1   1 
ATOM   13484 O  OD2   A ASP C 3 13  ? 54.706  -3.449  -32.609 0.50 42.74 ? 13  ASP F OD2   1 
ATOM   13485 O  OD2   B ASP C 3 13  ? 53.072  -3.786  -32.597 0.50 46.47 ? 13  ASP F OD2   1 
ATOM   13486 N  N     A LEU C 3 14  ? 55.246  -7.785  -35.137 0.50 36.83 ? 14  LEU F N     1 
ATOM   13487 N  N     B LEU C 3 14  ? 54.637  -8.057  -35.256 0.50 36.55 ? 14  LEU F N     1 
ATOM   13488 C  CA    A LEU C 3 14  ? 54.842  -9.109  -34.687 0.50 34.76 ? 14  LEU F CA    1 
ATOM   13489 C  CA    B LEU C 3 14  ? 54.613  -9.456  -34.847 0.50 35.09 ? 14  LEU F CA    1 
ATOM   13490 C  C     A LEU C 3 14  ? 54.815  -9.237  -33.169 0.50 37.98 ? 14  LEU F C     1 
ATOM   13491 C  C     B LEU C 3 14  ? 54.679  -9.621  -33.335 0.50 38.83 ? 14  LEU F C     1 
ATOM   13492 O  O     A LEU C 3 14  ? 54.216  -10.188 -32.653 0.50 37.14 ? 14  LEU F O     1 
ATOM   13493 O  O     B LEU C 3 14  ? 54.389  -10.713 -32.832 0.50 34.88 ? 14  LEU F O     1 
ATOM   13494 C  CB    A LEU C 3 14  ? 55.771  -10.173 -35.282 0.50 36.00 ? 14  LEU F CB    1 
ATOM   13495 C  CB    B LEU C 3 14  ? 55.761  -10.211 -35.514 0.50 36.63 ? 14  LEU F CB    1 
ATOM   13496 C  CG    A LEU C 3 14  ? 55.802  -10.181 -36.815 0.50 35.19 ? 14  LEU F CG    1 
ATOM   13497 C  CG    B LEU C 3 14  ? 55.739  -10.131 -37.043 0.50 34.78 ? 14  LEU F CG    1 
ATOM   13498 C  CD1   A LEU C 3 14  ? 56.683  -11.307 -37.347 0.50 36.76 ? 14  LEU F CD1   1 
ATOM   13499 C  CD1   B LEU C 3 14  ? 56.758  -11.081 -37.657 0.50 36.89 ? 14  LEU F CD1   1 
ATOM   13500 C  CD2   A LEU C 3 14  ? 54.393  -10.277 -37.383 0.50 30.27 ? 14  LEU F CD2   1 
ATOM   13501 C  CD2   B LEU C 3 14  ? 54.342  -10.418 -37.578 0.50 30.36 ? 14  LEU F CD2   1 
ATOM   13502 N  N     A GLY C 3 15  ? 55.435  -8.298  -32.448 0.50 35.83 ? 15  GLY F N     1 
ATOM   13503 N  N     B GLY C 3 15  ? 55.049  -8.567  -32.605 0.50 36.64 ? 15  GLY F N     1 
ATOM   13504 C  CA    A GLY C 3 15  ? 55.388  -8.339  -30.995 0.50 40.00 ? 15  GLY F CA    1 
ATOM   13505 C  CA    B GLY C 3 15  ? 55.054  -8.652  -31.154 0.50 40.44 ? 15  GLY F CA    1 
ATOM   13506 C  C     A GLY C 3 15  ? 53.975  -8.247  -30.452 0.50 37.70 ? 15  GLY F C     1 
ATOM   13507 C  C     B GLY C 3 15  ? 53.663  -8.833  -30.579 0.50 39.29 ? 15  GLY F C     1 
ATOM   13508 O  O     A GLY C 3 15  ? 53.645  -8.875  -29.443 0.50 38.06 ? 15  GLY F O     1 
ATOM   13509 O  O     B GLY C 3 15  ? 53.428  -9.719  -29.753 0.50 40.06 ? 15  GLY F O     1 
ATOM   13510 N  N     A LYS C 3 16  ? 53.121  -7.457  -31.108 0.50 36.59 ? 16  LYS F N     1 
ATOM   13511 N  N     B LYS C 3 16  ? 52.716  -7.995  -31.014 0.50 35.36 ? 16  LYS F N     1 
ATOM   13512 C  CA    A LYS C 3 16  ? 51.715  -7.412  -30.726 0.50 39.04 ? 16  LYS F CA    1 
ATOM   13513 C  CA    B LYS C 3 16  ? 51.352  -8.093  -30.504 0.50 38.64 ? 16  LYS F CA    1 
ATOM   13514 C  C     A LYS C 3 16  ? 50.995  -8.708  -31.069 0.50 40.45 ? 16  LYS F C     1 
ATOM   13515 C  C     B LYS C 3 16  ? 50.730  -9.444  -30.829 0.50 38.00 ? 16  LYS F C     1 
ATOM   13516 O  O     A LYS C 3 16  ? 49.940  -8.989  -30.493 0.50 33.90 ? 16  LYS F O     1 
ATOM   13517 O  O     B LYS C 3 16  ? 49.926  -9.960  -30.044 0.50 34.96 ? 16  LYS F O     1 
ATOM   13518 C  CB    A LYS C 3 16  ? 51.022  -6.220  -31.396 0.50 40.64 ? 16  LYS F CB    1 
ATOM   13519 C  CB    B LYS C 3 16  ? 50.495  -6.959  -31.067 0.50 40.78 ? 16  LYS F CB    1 
ATOM   13520 C  CG    A LYS C 3 16  ? 49.616  -5.905  -30.871 0.50 41.33 ? 16  LYS F CG    1 
ATOM   13521 C  CG    B LYS C 3 16  ? 51.027  -5.570  -30.749 0.50 37.41 ? 16  LYS F CG    1 
ATOM   13522 C  CD    A LYS C 3 16  ? 48.531  -6.466  -31.786 0.50 43.91 ? 16  LYS F CD    1 
ATOM   13523 C  CD    B LYS C 3 16  ? 51.412  -5.461  -29.282 0.50 38.72 ? 16  LYS F CD    1 
ATOM   13524 C  CE    A LYS C 3 16  ? 47.138  -6.045  -31.342 0.50 46.76 ? 16  LYS F CE    1 
ATOM   13525 C  CE    B LYS C 3 16  ? 51.967  -4.089  -28.950 0.50 30.87 ? 16  LYS F CE    1 
ATOM   13526 N  NZ    A LYS C 3 16  ? 46.741  -6.634  -30.028 0.50 44.03 ? 16  LYS F NZ    1 
ATOM   13527 N  NZ    B LYS C 3 16  ? 52.500  -4.037  -27.561 0.50 38.40 ? 16  LYS F NZ    1 
ATOM   13528 N  N     A LYS C 3 17  ? 51.539  -9.506  -31.987 0.50 32.66 ? 17  LYS F N     1 
ATOM   13529 N  N     B LYS C 3 17  ? 51.088  -10.033 -31.971 0.50 35.33 ? 17  LYS F N     1 
ATOM   13530 C  CA    A LYS C 3 17  ? 50.944  -10.799 -32.296 0.50 36.08 ? 17  LYS F CA    1 
ATOM   13531 C  CA    B LYS C 3 17  ? 50.628  -11.384 -32.270 0.50 35.46 ? 17  LYS F CA    1 
ATOM   13532 C  C     A LYS C 3 17  ? 51.479  -11.913 -31.407 0.50 32.24 ? 17  LYS F C     1 
ATOM   13533 C  C     B LYS C 3 17  ? 51.262  -12.399 -31.327 0.50 33.93 ? 17  LYS F C     1 
ATOM   13534 O  O     A LYS C 3 17  ? 50.746  -12.865 -31.111 0.50 35.87 ? 17  LYS F O     1 
ATOM   13535 O  O     B LYS C 3 17  ? 50.606  -13.359 -30.906 0.50 34.21 ? 17  LYS F O     1 
ATOM   13536 C  CB    A LYS C 3 17  ? 51.171  -11.154 -33.768 0.50 37.07 ? 17  LYS F CB    1 
ATOM   13537 C  CB    B LYS C 3 17  ? 50.937  -11.739 -33.724 0.50 35.56 ? 17  LYS F CB    1 
ATOM   13538 C  CG    A LYS C 3 17  ? 50.430  -12.404 -34.206 0.50 34.06 ? 17  LYS F CG    1 
ATOM   13539 C  CG    B LYS C 3 17  ? 50.157  -10.944 -34.754 0.50 35.19 ? 17  LYS F CG    1 
ATOM   13540 C  CD    A LYS C 3 17  ? 50.289  -12.488 -35.715 0.50 38.59 ? 17  LYS F CD    1 
ATOM   13541 C  CD    B LYS C 3 17  ? 50.492  -11.434 -36.155 0.50 34.69 ? 17  LYS F CD    1 
ATOM   13542 C  CE    A LYS C 3 17  ? 49.421  -13.674 -36.100 0.50 27.49 ? 17  LYS F CE    1 
ATOM   13543 C  CE    B LYS C 3 17  ? 49.668  -10.729 -37.213 0.50 39.81 ? 17  LYS F CE    1 
ATOM   13544 N  NZ    A LYS C 3 17  ? 49.960  -14.944 -35.531 0.50 39.25 ? 17  LYS F NZ    1 
ATOM   13545 N  NZ    B LYS C 3 17  ? 49.863  -11.351 -38.553 0.50 42.83 ? 17  LYS F NZ    1 
ATOM   13546 N  N     A LEU C 3 18  ? 52.733  -11.813 -30.964 0.50 31.73 ? 18  LEU F N     1 
ATOM   13547 N  N     B LEU C 3 18  ? 52.539  -12.206 -30.991 0.50 30.33 ? 18  LEU F N     1 
ATOM   13548 C  CA    A LEU C 3 18  ? 53.265  -12.807 -30.038 0.50 31.98 ? 18  LEU F CA    1 
ATOM   13549 C  CA    B LEU C 3 18  ? 53.182  -13.080 -30.016 0.50 31.94 ? 18  LEU F CA    1 
ATOM   13550 C  C     A LEU C 3 18  ? 52.558  -12.730 -28.689 0.50 31.71 ? 18  LEU F C     1 
ATOM   13551 C  C     B LEU C 3 18  ? 52.500  -12.969 -28.659 0.50 31.57 ? 18  LEU F C     1 
ATOM   13552 O  O     A LEU C 3 18  ? 52.259  -13.764 -28.080 0.50 31.67 ? 18  LEU F O     1 
ATOM   13553 O  O     B LEU C 3 18  ? 52.345  -13.969 -27.949 0.50 32.27 ? 18  LEU F O     1 
ATOM   13554 C  CB    A LEU C 3 18  ? 54.773  -12.614 -29.873 0.50 30.16 ? 18  LEU F CB    1 
ATOM   13555 C  CB    B LEU C 3 18  ? 54.670  -12.742 -29.911 0.50 30.30 ? 18  LEU F CB    1 
ATOM   13556 C  CG    A LEU C 3 18  ? 55.537  -13.705 -29.119 0.50 29.30 ? 18  LEU F CG    1 
ATOM   13557 C  CG    B LEU C 3 18  ? 55.556  -13.689 -29.099 0.50 29.31 ? 18  LEU F CG    1 
ATOM   13558 C  CD1   A LEU C 3 18  ? 55.340  -15.061 -29.770 0.50 33.58 ? 18  LEU F CD1   1 
ATOM   13559 C  CD1   B LEU C 3 18  ? 55.417  -15.120 -29.583 0.50 33.15 ? 18  LEU F CD1   1 
ATOM   13560 C  CD2   A LEU C 3 18  ? 57.017  -13.362 -29.035 0.50 27.84 ? 18  LEU F CD2   1 
ATOM   13561 C  CD2   B LEU C 3 18  ? 57.007  -13.243 -29.165 0.50 27.95 ? 18  LEU F CD2   1 
ATOM   13562 N  N     A LEU C 3 19  ? 52.269  -11.513 -28.217 0.50 33.30 ? 19  LEU F N     1 
ATOM   13563 N  N     B LEU C 3 19  ? 52.072  -11.759 -28.290 0.50 32.42 ? 19  LEU F N     1 
ATOM   13564 C  CA    A LEU C 3 19  ? 51.611  -11.343 -26.924 0.50 32.59 ? 19  LEU F CA    1 
ATOM   13565 C  CA    B LEU C 3 19  ? 51.358  -11.575 -27.031 0.50 32.36 ? 19  LEU F CA    1 
ATOM   13566 C  C     A LEU C 3 19  ? 50.278  -12.077 -26.883 0.50 33.26 ? 19  LEU F C     1 
ATOM   13567 C  C     B LEU C 3 19  ? 50.045  -12.344 -27.024 0.50 33.76 ? 19  LEU F C     1 
ATOM   13568 O  O     A LEU C 3 19  ? 49.978  -12.788 -25.917 0.50 32.66 ? 19  LEU F O     1 
ATOM   13569 O  O     B LEU C 3 19  ? 49.711  -13.006 -26.034 0.50 34.24 ? 19  LEU F O     1 
ATOM   13570 C  CB    A LEU C 3 19  ? 51.411  -9.857  -26.627 0.50 32.63 ? 19  LEU F CB    1 
ATOM   13571 C  CB    B LEU C 3 19  ? 51.108  -10.089 -26.779 0.50 32.63 ? 19  LEU F CB    1 
ATOM   13572 C  CG    A LEU C 3 19  ? 52.616  -9.069  -26.112 0.50 29.96 ? 19  LEU F CG    1 
ATOM   13573 C  CG    B LEU C 3 19  ? 52.330  -9.240  -26.432 0.50 32.92 ? 19  LEU F CG    1 
ATOM   13574 C  CD1   A LEU C 3 19  ? 52.372  -7.574  -26.259 0.50 30.40 ? 19  LEU F CD1   1 
ATOM   13575 C  CD1   B LEU C 3 19  ? 51.961  -7.767  -26.372 0.50 30.64 ? 19  LEU F CD1   1 
ATOM   13576 C  CD2   A LEU C 3 19  ? 52.889  -9.424  -24.667 0.50 27.72 ? 19  LEU F CD2   1 
ATOM   13577 C  CD2   B LEU C 3 19  ? 52.924  -9.702  -25.120 0.50 25.76 ? 19  LEU F CD2   1 
ATOM   13578 N  N     A GLU C 3 20  ? 49.465  -11.918 -27.929 0.50 34.36 ? 20  GLU F N     1 
ATOM   13579 N  N     B GLU C 3 20  ? 49.287  -12.271 -28.121 0.50 33.90 ? 20  GLU F N     1 
ATOM   13580 C  CA    A GLU C 3 20  ? 48.170  -12.589 -27.963 0.50 32.92 ? 20  GLU F CA    1 
ATOM   13581 C  CA    B GLU C 3 20  ? 48.031  -13.010 -28.206 0.50 32.54 ? 20  GLU F CA    1 
ATOM   13582 C  C     A GLU C 3 20  ? 48.321  -14.090 -28.154 0.50 34.12 ? 20  GLU F C     1 
ATOM   13583 C  C     B GLU C 3 20  ? 48.273  -14.511 -28.132 0.50 34.99 ? 20  GLU F C     1 
ATOM   13584 O  O     A GLU C 3 20  ? 47.511  -14.865 -27.632 0.50 37.39 ? 20  GLU F O     1 
ATOM   13585 O  O     B GLU C 3 20  ? 47.624  -15.221 -27.355 0.50 36.07 ? 20  GLU F O     1 
ATOM   13586 C  CB    A GLU C 3 20  ? 47.302  -11.992 -29.070 0.50 35.52 ? 20  GLU F CB    1 
ATOM   13587 C  CB    B GLU C 3 20  ? 47.296  -12.650 -29.499 0.50 36.26 ? 20  GLU F CB    1 
ATOM   13588 C  CG    A GLU C 3 20  ? 46.976  -10.521 -28.868 0.50 35.53 ? 20  GLU F CG    1 
ATOM   13589 C  CG    B GLU C 3 20  ? 46.582  -11.313 -29.469 0.50 36.34 ? 20  GLU F CG    1 
ATOM   13590 C  CD    A GLU C 3 20  ? 46.119  -9.954  -29.982 0.50 45.44 ? 20  GLU F CD    1 
ATOM   13591 C  CD    B GLU C 3 20  ? 45.681  -11.109 -30.674 0.50 45.37 ? 20  GLU F CD    1 
ATOM   13592 O  OE1   A GLU C 3 20  ? 46.605  -9.872  -31.133 0.50 41.39 ? 20  GLU F OE1   1 
ATOM   13593 O  OE1   B GLU C 3 20  ? 46.173  -11.237 -31.818 0.50 38.20 ? 20  GLU F OE1   1 
ATOM   13594 O  OE2   A GLU C 3 20  ? 44.953  -9.601  -29.706 0.50 46.48 ? 20  GLU F OE2   1 
ATOM   13595 O  OE2   B GLU C 3 20  ? 44.478  -10.831 -30.475 0.50 46.82 ? 20  GLU F OE2   1 
ATOM   13596 N  N     A ALA C 3 21  ? 49.350  -14.520 -28.885 0.50 34.72 ? 21  ALA F N     1 
ATOM   13597 N  N     B ALA C 3 21  ? 49.213  -15.013 -28.936 0.50 34.30 ? 21  ALA F N     1 
ATOM   13598 C  CA    A ALA C 3 21  ? 49.537  -15.946 -29.126 0.50 36.76 ? 21  ALA F CA    1 
ATOM   13599 C  CA    B ALA C 3 21  ? 49.490  -16.444 -28.948 0.50 37.56 ? 21  ALA F CA    1 
ATOM   13600 C  C     A ALA C 3 21  ? 49.939  -16.677 -27.852 0.50 35.85 ? 21  ALA F C     1 
ATOM   13601 C  C     B ALA C 3 21  ? 50.069  -16.917 -27.622 0.50 36.26 ? 21  ALA F C     1 
ATOM   13602 O  O     A ALA C 3 21  ? 49.440  -17.775 -27.578 0.50 36.09 ? 21  ALA F O     1 
ATOM   13603 O  O     B ALA C 3 21  ? 49.815  -18.054 -27.207 0.50 36.40 ? 21  ALA F O     1 
ATOM   13604 C  CB    A ALA C 3 21  ? 50.581  -16.159 -30.222 0.50 36.54 ? 21  ALA F CB    1 
ATOM   13605 C  CB    B ALA C 3 21  ? 50.437  -16.786 -30.098 0.50 37.71 ? 21  ALA F CB    1 
ATOM   13606 N  N     A ALA C 3 22  ? 50.847  -16.092 -27.066 0.50 32.97 ? 22  ALA F N     1 
ATOM   13607 N  N     B ALA C 3 22  ? 50.856  -16.074 -26.950 0.50 32.91 ? 22  ALA F N     1 
ATOM   13608 C  CA    A ALA C 3 22  ? 51.249  -16.721 -25.812 0.50 31.49 ? 22  ALA F CA    1 
ATOM   13609 C  CA    B ALA C 3 22  ? 51.293  -16.412 -25.601 0.50 32.04 ? 22  ALA F CA    1 
ATOM   13610 C  C     A ALA C 3 22  ? 50.072  -16.828 -24.852 0.50 29.69 ? 22  ALA F C     1 
ATOM   13611 C  C     B ALA C 3 22  ? 50.112  -16.442 -24.642 0.50 29.02 ? 22  ALA F C     1 
ATOM   13612 O  O     A ALA C 3 22  ? 49.881  -17.864 -24.204 0.50 30.32 ? 22  ALA F O     1 
ATOM   13613 O  O     B ALA C 3 22  ? 50.045  -17.301 -23.756 0.50 32.92 ? 22  ALA F O     1 
ATOM   13614 C  CB    A ALA C 3 22  ? 52.395  -15.938 -25.173 0.50 33.17 ? 22  ALA F CB    1 
ATOM   13615 C  CB    B ALA C 3 22  ? 52.349  -15.420 -25.119 0.50 32.40 ? 22  ALA F CB    1 
ATOM   13616 N  N     A ARG C 3 23  ? 49.266  -15.768 -24.757 0.50 30.82 ? 23  ARG F N     1 
ATOM   13617 N  N     B ARG C 3 23  ? 49.166  -15.517 -24.810 0.50 31.55 ? 23  ARG F N     1 
ATOM   13618 C  CA    A ARG C 3 23  ? 48.100  -15.792 -23.876 0.50 35.50 ? 23  ARG F CA    1 
ATOM   13619 C  CA    B ARG C 3 23  ? 47.986  -15.504 -23.950 0.50 35.04 ? 23  ARG F CA    1 
ATOM   13620 C  C     A ARG C 3 23  ? 47.151  -16.927 -24.239 0.50 36.69 ? 23  ARG F C     1 
ATOM   13621 C  C     B ARG C 3 23  ? 47.067  -16.680 -24.261 0.50 36.49 ? 23  ARG F C     1 
ATOM   13622 O  O     A ARG C 3 23  ? 46.624  -17.613 -23.356 0.50 35.37 ? 23  ARG F O     1 
ATOM   13623 O  O     B ARG C 3 23  ? 46.596  -17.372 -23.351 0.50 35.73 ? 23  ARG F O     1 
ATOM   13624 C  CB    A ARG C 3 23  ? 47.369  -14.449 -23.936 0.50 35.14 ? 23  ARG F CB    1 
ATOM   13625 C  CB    B ARG C 3 23  ? 47.230  -14.184 -24.108 0.50 35.37 ? 23  ARG F CB    1 
ATOM   13626 C  CG    A ARG C 3 23  ? 46.038  -14.441 -23.188 0.50 40.17 ? 23  ARG F CG    1 
ATOM   13627 C  CG    B ARG C 3 23  ? 45.951  -14.121 -23.282 0.50 39.67 ? 23  ARG F CG    1 
ATOM   13628 C  CD    A ARG C 3 23  ? 45.163  -13.261 -23.578 0.50 41.89 ? 23  ARG F CD    1 
ATOM   13629 C  CD    B ARG C 3 23  ? 45.018  -13.028 -23.765 0.50 43.07 ? 23  ARG F CD    1 
ATOM   13630 N  NE    A ARG C 3 23  ? 45.769  -11.978 -23.245 0.50 44.04 ? 23  ARG F NE    1 
ATOM   13631 N  NE    B ARG C 3 23  ? 45.643  -11.712 -23.732 0.50 42.48 ? 23  ARG F NE    1 
ATOM   13632 C  CZ    A ARG C 3 23  ? 46.347  -11.169 -24.122 0.50 42.30 ? 23  ARG F CZ    1 
ATOM   13633 C  CZ    B ARG C 3 23  ? 45.761  -10.969 -22.640 0.50 45.47 ? 23  ARG F CZ    1 
ATOM   13634 N  NH1   A ARG C 3 23  ? 46.422  -11.481 -25.406 0.50 46.65 ? 23  ARG F NH1   1 
ATOM   13635 N  NH1   B ARG C 3 23  ? 45.332  -11.397 -21.463 0.50 40.73 ? 23  ARG F NH1   1 
ATOM   13636 N  NH2   A ARG C 3 23  ? 46.861  -10.017 -23.702 0.50 44.83 ? 23  ARG F NH2   1 
ATOM   13637 N  NH2   B ARG C 3 23  ? 46.326  -9.768  -22.730 0.50 41.56 ? 23  ARG F NH2   1 
ATOM   13638 N  N     A ALA C 3 24  ? 46.931  -17.149 -25.538 0.50 38.18 ? 24  ALA F N     1 
ATOM   13639 N  N     B ALA C 3 24  ? 46.801  -16.920 -25.544 0.50 38.45 ? 24  ALA F N     1 
ATOM   13640 C  CA    A ALA C 3 24  ? 45.958  -18.147 -25.968 0.50 38.68 ? 24  ALA F CA    1 
ATOM   13641 C  CA    B ALA C 3 24  ? 45.840  -17.930 -25.967 0.50 39.06 ? 24  ALA F CA    1 
ATOM   13642 C  C     A ALA C 3 24  ? 46.488  -19.569 -25.840 0.50 39.52 ? 24  ALA F C     1 
ATOM   13643 C  C     B ALA C 3 24  ? 46.430  -19.330 -26.045 0.50 39.14 ? 24  ALA F C     1 
ATOM   13644 O  O     A ALA C 3 24  ? 45.696  -20.508 -25.700 0.50 37.72 ? 24  ALA F O     1 
ATOM   13645 O  O     B ALA C 3 24  ? 45.724  -20.258 -26.452 0.50 37.40 ? 24  ALA F O     1 
ATOM   13646 C  CB    A ALA C 3 24  ? 45.530  -17.875 -27.411 0.50 41.10 ? 24  ALA F CB    1 
ATOM   13647 C  CB    B ALA C 3 24  ? 45.241  -17.550 -27.324 0.50 40.15 ? 24  ALA F CB    1 
ATOM   13648 N  N     A GLY C 3 25  ? 47.804  -19.753 -25.885 0.50 38.55 ? 25  GLY F N     1 
ATOM   13649 N  N     B GLY C 3 25  ? 47.694  -19.507 -25.672 0.50 38.70 ? 25  GLY F N     1 
ATOM   13650 C  CA    A GLY C 3 25  ? 48.374  -21.079 -25.779 0.50 37.70 ? 25  GLY F CA    1 
ATOM   13651 C  CA    B GLY C 3 25  ? 48.301  -20.828 -25.688 0.50 37.37 ? 25  GLY F CA    1 
ATOM   13652 C  C     A GLY C 3 25  ? 48.645  -21.767 -27.096 0.50 41.58 ? 25  GLY F C     1 
ATOM   13653 C  C     B GLY C 3 25  ? 48.438  -21.438 -27.067 0.50 41.19 ? 25  GLY F C     1 
ATOM   13654 O  O     A GLY C 3 25  ? 48.640  -23.003 -27.152 0.50 36.68 ? 25  GLY F O     1 
ATOM   13655 O  O     B GLY C 3 25  ? 48.251  -22.652 -27.226 0.50 38.86 ? 25  GLY F O     1 
ATOM   13656 N  N     A GLN C 3 26  ? 48.891  -21.007 -28.162 0.50 42.64 ? 26  GLN F N     1 
ATOM   13657 N  N     B GLN C 3 26  ? 48.762  -20.625 -28.070 0.50 42.48 ? 26  GLN F N     1 
ATOM   13658 C  CA    A GLN C 3 26  ? 49.138  -21.564 -29.489 0.50 38.77 ? 26  GLN F CA    1 
ATOM   13659 C  CA    B GLN C 3 26  ? 48.938  -21.090 -29.445 0.50 39.99 ? 26  GLN F CA    1 
ATOM   13660 C  C     A GLN C 3 26  ? 50.640  -21.780 -29.641 0.50 37.33 ? 26  GLN F C     1 
ATOM   13661 C  C     B GLN C 3 26  ? 50.428  -21.342 -29.656 0.50 38.20 ? 26  GLN F C     1 
ATOM   13662 O  O     A GLN C 3 26  ? 51.391  -20.843 -29.921 0.50 37.55 ? 26  GLN F O     1 
ATOM   13663 O  O     B GLN C 3 26  ? 51.177  -20.457 -30.073 0.50 38.90 ? 26  GLN F O     1 
ATOM   13664 C  CB    A GLN C 3 26  ? 48.579  -20.636 -30.562 0.50 43.69 ? 26  GLN F CB    1 
ATOM   13665 C  CB    B GLN C 3 26  ? 48.376  -20.071 -30.429 0.50 42.17 ? 26  GLN F CB    1 
ATOM   13666 C  CG    A GLN C 3 26  ? 47.082  -20.379 -30.425 0.50 43.93 ? 26  GLN F CG    1 
ATOM   13667 C  CG    B GLN C 3 26  ? 46.874  -19.848 -30.288 0.50 44.72 ? 26  GLN F CG    1 
ATOM   13668 C  CD    A GLN C 3 26  ? 46.632  -19.115 -31.138 0.50 44.93 ? 26  GLN F CD    1 
ATOM   13669 C  CD    B GLN C 3 26  ? 46.385  -18.625 -31.045 0.50 43.37 ? 26  GLN F CD    1 
ATOM   13670 O  OE1   A GLN C 3 26  ? 47.377  -18.138 -31.228 0.50 47.19 ? 26  GLN F OE1   1 
ATOM   13671 O  OE1   B GLN C 3 26  ? 46.816  -17.502 -30.780 0.50 42.50 ? 26  GLN F OE1   1 
ATOM   13672 N  NE2   A GLN C 3 26  ? 45.407  -19.131 -31.651 0.50 48.86 ? 26  GLN F NE2   1 
ATOM   13673 N  NE2   B GLN C 3 26  ? 45.484  -18.839 -31.995 0.50 47.81 ? 26  GLN F NE2   1 
ATOM   13674 N  N     A ASP C 3 27  ? 51.078  -23.027 -29.457 0.50 39.51 ? 27  ASP F N     1 
ATOM   13675 N  N     B ASP C 3 27  ? 50.856  -22.572 -29.364 0.50 39.39 ? 27  ASP F N     1 
ATOM   13676 C  CA    A ASP C 3 27  ? 52.507  -23.323 -29.439 0.50 37.36 ? 27  ASP F CA    1 
ATOM   13677 C  CA    B ASP C 3 27  ? 52.281  -22.889 -29.370 0.50 35.76 ? 27  ASP F CA    1 
ATOM   13678 C  C     A ASP C 3 27  ? 53.138  -23.117 -30.811 0.50 41.86 ? 27  ASP F C     1 
ATOM   13679 C  C     B ASP C 3 27  ? 52.874  -22.784 -30.770 0.50 41.91 ? 27  ASP F C     1 
ATOM   13680 O  O     A ASP C 3 27  ? 54.195  -22.486 -30.929 0.50 36.86 ? 27  ASP F O     1 
ATOM   13681 O  O     B ASP C 3 27  ? 54.008  -22.318 -30.933 0.50 37.17 ? 27  ASP F O     1 
ATOM   13682 C  CB    A ASP C 3 27  ? 52.742  -24.756 -28.957 0.50 39.57 ? 27  ASP F CB    1 
ATOM   13683 C  CB    B ASP C 3 27  ? 52.509  -24.288 -28.796 0.50 39.15 ? 27  ASP F CB    1 
ATOM   13684 C  CG    A ASP C 3 27  ? 52.137  -25.021 -27.594 0.50 44.77 ? 27  ASP F CG    1 
ATOM   13685 C  CG    B ASP C 3 27  ? 51.833  -24.485 -27.452 0.50 44.82 ? 27  ASP F CG    1 
ATOM   13686 O  OD1   A ASP C 3 27  ? 51.373  -24.165 -27.102 0.50 48.23 ? 27  ASP F OD1   1 
ATOM   13687 O  OD1   B ASP C 3 27  ? 50.907  -23.711 -27.128 0.50 47.40 ? 27  ASP F OD1   1 
ATOM   13688 O  OD2   A ASP C 3 27  ? 52.429  -26.089 -27.014 0.50 51.58 ? 27  ASP F OD2   1 
ATOM   13689 O  OD2   B ASP C 3 27  ? 52.230  -25.413 -26.715 0.50 48.23 ? 27  ASP F OD2   1 
ATOM   13690 N  N     A ASP C 3 28  ? 52.508  -23.655 -31.860 0.50 39.08 ? 28  ASP F N     1 
ATOM   13691 N  N     B ASP C 3 28  ? 52.131  -23.225 -31.789 0.50 38.13 ? 28  ASP F N     1 
ATOM   13692 C  CA    A ASP C 3 28  ? 53.090  -23.583 -33.198 0.50 39.91 ? 28  ASP F CA    1 
ATOM   13693 C  CA    B ASP C 3 28  ? 52.618  -23.123 -33.162 0.50 40.53 ? 28  ASP F CA    1 
ATOM   13694 C  C     A ASP C 3 28  ? 53.216  -22.142 -33.676 0.50 39.90 ? 28  ASP F C     1 
ATOM   13695 C  C     B ASP C 3 28  ? 52.807  -21.668 -33.566 0.50 37.88 ? 28  ASP F C     1 
ATOM   13696 O  O     A ASP C 3 28  ? 54.190  -21.787 -34.352 0.50 38.23 ? 28  ASP F O     1 
ATOM   13697 O  O     B ASP C 3 28  ? 53.834  -21.300 -34.147 0.50 40.39 ? 28  ASP F O     1 
ATOM   13698 C  CB    A ASP C 3 28  ? 52.251  -24.398 -34.182 0.50 43.28 ? 28  ASP F CB    1 
ATOM   13699 C  CB    B ASP C 3 28  ? 51.650  -23.820 -34.119 0.50 41.08 ? 28  ASP F CB    1 
ATOM   13700 C  CG    A ASP C 3 28  ? 52.476  -25.891 -34.044 0.50 52.87 ? 28  ASP F CG    1 
ATOM   13701 C  CG    B ASP C 3 28  ? 51.607  -25.319 -33.916 0.50 46.92 ? 28  ASP F CG    1 
ATOM   13702 O  OD1   A ASP C 3 28  ? 53.606  -26.296 -33.691 0.50 50.26 ? 28  ASP F OD1   1 
ATOM   13703 O  OD1   B ASP C 3 28  ? 52.661  -25.907 -33.592 0.50 55.18 ? 28  ASP F OD1   1 
ATOM   13704 O  OD2   A ASP C 3 28  ? 51.520  -26.660 -34.289 0.50 53.15 ? 28  ASP F OD2   1 
ATOM   13705 O  OD2   B ASP C 3 28  ? 50.517  -25.908 -34.079 0.50 55.36 ? 28  ASP F OD2   1 
ATOM   13706 N  N     A GLU C 3 29  ? 52.239  -21.298 -33.339 0.50 37.47 ? 29  GLU F N     1 
ATOM   13707 N  N     B GLU C 3 29  ? 51.821  -20.824 -33.261 0.50 37.51 ? 29  GLU F N     1 
ATOM   13708 C  CA    A GLU C 3 29  ? 52.285  -19.908 -33.773 0.50 34.68 ? 29  GLU F CA    1 
ATOM   13709 C  CA    B GLU C 3 29  ? 51.912  -19.411 -33.602 0.50 37.24 ? 29  GLU F CA    1 
ATOM   13710 C  C     A GLU C 3 29  ? 53.419  -19.154 -33.089 0.50 41.54 ? 29  GLU F C     1 
ATOM   13711 C  C     B GLU C 3 29  ? 53.047  -18.716 -32.862 0.50 39.10 ? 29  GLU F C     1 
ATOM   13712 O  O     A GLU C 3 29  ? 54.068  -18.303 -33.708 0.50 37.52 ? 29  GLU F O     1 
ATOM   13713 O  O     B GLU C 3 29  ? 53.512  -17.665 -33.313 0.50 38.75 ? 29  GLU F O     1 
ATOM   13714 C  CB    A GLU C 3 29  ? 50.941  -19.233 -33.501 0.50 39.61 ? 29  GLU F CB    1 
ATOM   13715 C  CB    B GLU C 3 29  ? 50.582  -18.717 -33.301 0.50 39.06 ? 29  GLU F CB    1 
ATOM   13716 C  CG    A GLU C 3 29  ? 50.749  -17.907 -34.214 0.50 39.88 ? 29  GLU F CG    1 
ATOM   13717 C  CG    B GLU C 3 29  ? 50.332  -17.456 -34.109 0.50 42.73 ? 29  GLU F CG    1 
ATOM   13718 C  CD    A GLU C 3 29  ? 50.569  -18.067 -35.713 0.50 45.03 ? 29  GLU F CD    1 
ATOM   13719 C  CD    B GLU C 3 29  ? 49.783  -17.745 -35.492 0.50 46.15 ? 29  GLU F CD    1 
ATOM   13720 O  OE1   A GLU C 3 29  ? 50.233  -19.184 -36.162 0.50 49.63 ? 29  GLU F OE1   1 
ATOM   13721 O  OE1   B GLU C 3 29  ? 49.240  -18.851 -35.701 0.50 50.74 ? 29  GLU F OE1   1 
ATOM   13722 O  OE2   A GLU C 3 29  ? 50.765  -17.074 -36.444 0.50 43.18 ? 29  GLU F OE2   1 
ATOM   13723 O  OE2   B GLU C 3 29  ? 49.893  -16.866 -36.372 0.50 50.21 ? 29  GLU F OE2   1 
ATOM   13724 N  N     A VAL C 3 30  ? 53.680  -19.462 -31.815 0.50 39.24 ? 30  VAL F N     1 
ATOM   13725 N  N     B VAL C 3 30  ? 53.510  -19.281 -31.746 0.50 39.12 ? 30  VAL F N     1 
ATOM   13726 C  CA    A VAL C 3 30  ? 54.774  -18.809 -31.100 0.50 38.61 ? 30  VAL F CA    1 
ATOM   13727 C  CA    B VAL C 3 30  ? 54.653  -18.713 -31.038 0.50 38.46 ? 30  VAL F CA    1 
ATOM   13728 C  C     A VAL C 3 30  ? 56.113  -19.151 -31.744 0.50 37.46 ? 30  VAL F C     1 
ATOM   13729 C  C     B VAL C 3 30  ? 55.959  -19.095 -31.728 0.50 37.64 ? 30  VAL F C     1 
ATOM   13730 O  O     A VAL C 3 30  ? 56.990  -18.289 -31.883 0.50 30.88 ? 30  VAL F O     1 
ATOM   13731 O  O     B VAL C 3 30  ? 56.833  -18.248 -31.943 0.50 30.86 ? 30  VAL F O     1 
ATOM   13732 C  CB    A VAL C 3 30  ? 54.738  -19.190 -29.608 0.50 33.89 ? 30  VAL F CB    1 
ATOM   13733 C  CB    B VAL C 3 30  ? 54.639  -19.154 -29.562 0.50 33.87 ? 30  VAL F CB    1 
ATOM   13734 C  CG1   A VAL C 3 30  ? 56.002  -18.725 -28.903 0.50 34.89 ? 30  VAL F CG1   1 
ATOM   13735 C  CG1   B VAL C 3 30  ? 55.962  -18.819 -28.894 0.50 34.88 ? 30  VAL F CG1   1 
ATOM   13736 C  CG2   A VAL C 3 30  ? 53.506  -18.590 -28.940 0.50 36.42 ? 30  VAL F CG2   1 
ATOM   13737 C  CG2   B VAL C 3 30  ? 53.484  -18.488 -28.824 0.50 36.23 ? 30  VAL F CG2   1 
ATOM   13738 N  N     A ARG C 3 31  ? 56.291  -20.408 -32.159 0.50 38.54 ? 31  ARG F N     1 
ATOM   13739 N  N     B ARG C 3 31  ? 56.109  -20.374 -32.086 0.50 38.51 ? 31  ARG F N     1 
ATOM   13740 C  CA    A ARG C 3 31  ? 57.498  -20.774 -32.896 0.50 39.69 ? 31  ARG F CA    1 
ATOM   13741 C  CA    B ARG C 3 31  ? 57.309  -20.814 -32.793 0.50 39.93 ? 31  ARG F CA    1 
ATOM   13742 C  C     A ARG C 3 31  ? 57.586  -20.020 -34.217 0.50 38.45 ? 31  ARG F C     1 
ATOM   13743 C  C     B ARG C 3 31  ? 57.494  -20.056 -34.102 0.50 38.43 ? 31  ARG F C     1 
ATOM   13744 O  O     A ARG C 3 31  ? 58.675  -19.605 -34.633 0.50 38.40 ? 31  ARG F O     1 
ATOM   13745 O  O     B ARG C 3 31  ? 58.608  -19.627 -34.428 0.50 38.46 ? 31  ARG F O     1 
ATOM   13746 C  CB    A ARG C 3 31  ? 57.531  -22.283 -33.148 0.50 37.29 ? 31  ARG F CB    1 
ATOM   13747 C  CB    B ARG C 3 31  ? 57.242  -22.318 -33.065 0.50 37.83 ? 31  ARG F CB    1 
ATOM   13748 C  CG    A ARG C 3 31  ? 57.562  -23.147 -31.899 0.50 39.65 ? 31  ARG F CG    1 
ATOM   13749 C  CG    B ARG C 3 31  ? 58.004  -23.199 -32.084 0.50 37.79 ? 31  ARG F CG    1 
ATOM   13750 C  CD    A ARG C 3 31  ? 57.587  -24.624 -32.272 0.50 40.58 ? 31  ARG F CD    1 
ATOM   13751 C  CD    B ARG C 3 31  ? 57.317  -23.279 -30.731 0.50 43.79 ? 31  ARG F CD    1 
ATOM   13752 N  NE    A ARG C 3 31  ? 57.390  -25.496 -31.120 0.50 47.49 ? 31  ARG F NE    1 
ATOM   13753 N  NE    B ARG C 3 31  ? 57.734  -24.458 -29.978 0.50 44.45 ? 31  ARG F NE    1 
ATOM   13754 C  CZ    A ARG C 3 31  ? 58.362  -25.918 -30.323 0.50 46.23 ? 31  ARG F CZ    1 
ATOM   13755 C  CZ    B ARG C 3 31  ? 56.995  -25.549 -29.825 0.50 39.59 ? 31  ARG F CZ    1 
ATOM   13756 N  NH1   A ARG C 3 31  ? 59.618  -25.546 -30.507 0.50 37.79 ? 31  ARG F NH1   1 
ATOM   13757 N  NH1   B ARG C 3 31  ? 55.782  -25.643 -30.345 0.50 39.65 ? 31  ARG F NH1   1 
ATOM   13758 N  NH2   A ARG C 3 31  ? 58.067  -26.736 -29.316 0.50 46.97 ? 31  ARG F NH2   1 
ATOM   13759 N  NH2   B ARG C 3 31  ? 57.484  -26.571 -29.128 0.50 47.62 ? 31  ARG F NH2   1 
ATOM   13760 N  N     A ILE C 3 32  ? 56.447  -19.834 -34.891 0.50 37.41 ? 32  ILE F N     1 
ATOM   13761 N  N     B ILE C 3 32  ? 56.412  -19.874 -34.864 0.50 37.40 ? 32  ILE F N     1 
ATOM   13762 C  CA    A ILE C 3 32  ? 56.439  -19.132 -36.174 0.50 34.39 ? 32  ILE F CA    1 
ATOM   13763 C  CA    B ILE C 3 32  ? 56.535  -19.279 -36.192 0.50 34.45 ? 32  ILE F CA    1 
ATOM   13764 C  C     A ILE C 3 32  ? 56.896  -17.691 -35.995 0.50 37.10 ? 32  ILE F C     1 
ATOM   13765 C  C     B ILE C 3 32  ? 56.821  -17.786 -36.090 0.50 37.20 ? 32  ILE F C     1 
ATOM   13766 O  O     A ILE C 3 32  ? 57.770  -17.200 -36.720 0.50 31.65 ? 32  ILE F O     1 
ATOM   13767 O  O     B ILE C 3 32  ? 57.649  -17.249 -36.837 0.50 31.56 ? 32  ILE F O     1 
ATOM   13768 C  CB    A ILE C 3 32  ? 55.039  -19.196 -36.812 0.50 35.87 ? 32  ILE F CB    1 
ATOM   13769 C  CB    B ILE C 3 32  ? 55.269  -19.556 -37.023 0.50 36.16 ? 32  ILE F CB    1 
ATOM   13770 C  CG1   A ILE C 3 32  ? 54.754  -20.595 -37.359 0.50 41.32 ? 32  ILE F CG1   1 
ATOM   13771 C  CG1   B ILE C 3 32  ? 54.979  -21.058 -37.066 0.50 42.54 ? 32  ILE F CG1   1 
ATOM   13772 C  CG2   A ILE C 3 32  ? 54.895  -18.138 -37.898 0.50 39.74 ? 32  ILE F CG2   1 
ATOM   13773 C  CG2   B ILE C 3 32  ? 55.422  -18.999 -38.430 0.50 44.63 ? 32  ILE F CG2   1 
ATOM   13774 C  CD1   A ILE C 3 32  ? 53.397  -20.730 -38.013 0.50 36.39 ? 32  ILE F CD1   1 
ATOM   13775 C  CD1   B ILE C 3 32  ? 56.183  -21.908 -37.418 0.50 33.78 ? 32  ILE F CD1   1 
ATOM   13776 N  N     A LEU C 3 33  ? 56.301  -16.988 -35.028 0.50 29.13 ? 33  LEU F N     1 
ATOM   13777 N  N     B LEU C 3 33  ? 56.136  -17.090 -35.178 0.50 29.82 ? 33  LEU F N     1 
ATOM   13778 C  CA    A LEU C 3 33  ? 56.589  -15.570 -34.855 0.50 33.22 ? 33  LEU F CA    1 
ATOM   13779 C  CA    B LEU C 3 33  ? 56.390  -15.665 -35.001 0.50 32.33 ? 33  LEU F CA    1 
ATOM   13780 C  C     A LEU C 3 33  ? 58.046  -15.345 -34.465 0.50 32.75 ? 33  LEU F C     1 
ATOM   13781 C  C     B LEU C 3 33  ? 57.850  -15.410 -34.650 0.50 33.02 ? 33  LEU F C     1 
ATOM   13782 O  O     A LEU C 3 33  ? 58.693  -14.418 -34.966 0.50 35.64 ? 33  LEU F O     1 
ATOM   13783 O  O     B LEU C 3 33  ? 58.485  -14.518 -35.224 0.50 35.27 ? 33  LEU F O     1 
ATOM   13784 C  CB    A LEU C 3 33  ? 55.639  -14.974 -33.813 0.50 27.11 ? 33  LEU F CB    1 
ATOM   13785 C  CB    B LEU C 3 33  ? 55.462  -15.091 -33.927 0.50 27.36 ? 33  LEU F CB    1 
ATOM   13786 C  CG    A LEU C 3 33  ? 54.154  -15.145 -34.154 0.50 29.46 ? 33  LEU F CG    1 
ATOM   13787 C  CG    B LEU C 3 33  ? 54.060  -14.718 -34.410 0.50 28.68 ? 33  LEU F CG    1 
ATOM   13788 C  CD1   A LEU C 3 33  ? 53.280  -15.000 -32.912 0.50 36.20 ? 33  LEU F CD1   1 
ATOM   13789 C  CD1   B LEU C 3 33  ? 53.104  -14.578 -33.238 0.50 36.85 ? 33  LEU F CD1   1 
ATOM   13790 C  CD2   A LEU C 3 33  ? 53.722  -14.162 -35.233 0.50 31.06 ? 33  LEU F CD2   1 
ATOM   13791 C  CD2   B LEU C 3 33  ? 54.096  -13.432 -35.215 0.50 31.34 ? 33  LEU F CD2   1 
ATOM   13792 N  N     A MET C 3 34  ? 58.587  -16.195 -33.586 0.50 28.80 ? 34  MET F N     1 
ATOM   13793 N  N     B MET C 3 34  ? 58.408  -16.201 -33.728 0.50 28.88 ? 34  MET F N     1 
ATOM   13794 C  CA    A MET C 3 34  ? 59.974  -16.025 -33.162 0.50 34.33 ? 34  MET F CA    1 
ATOM   13795 C  CA    B MET C 3 34  ? 59.797  -16.001 -33.330 0.50 34.56 ? 34  MET F CA    1 
ATOM   13796 C  C     A MET C 3 34  ? 60.937  -16.237 -34.322 0.50 28.40 ? 34  MET F C     1 
ATOM   13797 C  C     B MET C 3 34  ? 60.744  -16.236 -34.498 0.50 27.96 ? 34  MET F C     1 
ATOM   13798 O  O     A MET C 3 34  ? 61.953  -15.539 -34.430 0.50 32.56 ? 34  MET F O     1 
ATOM   13799 O  O     B MET C 3 34  ? 61.687  -15.463 -34.706 0.50 32.48 ? 34  MET F O     1 
ATOM   13800 C  CB    A MET C 3 34  ? 60.302  -16.982 -32.017 0.50 28.55 ? 34  MET F CB    1 
ATOM   13801 C  CB    B MET C 3 34  ? 60.152  -16.920 -32.163 0.50 28.51 ? 34  MET F CB    1 
ATOM   13802 C  CG    A MET C 3 34  ? 59.676  -16.587 -30.680 0.50 32.24 ? 34  MET F CG    1 
ATOM   13803 C  CG    B MET C 3 34  ? 59.425  -16.586 -30.865 0.50 32.49 ? 34  MET F CG    1 
ATOM   13804 S  SD    A MET C 3 34  ? 60.463  -17.418 -29.287 0.50 36.89 ? 34  MET F SD    1 
ATOM   13805 S  SD    B MET C 3 34  ? 60.063  -17.555 -29.490 0.50 39.21 ? 34  MET F SD    1 
ATOM   13806 C  CE    A MET C 3 34  ? 60.230  -19.132 -29.742 0.50 33.85 ? 34  MET F CE    1 
ATOM   13807 C  CE    B MET C 3 34  ? 60.171  -19.169 -30.259 0.50 35.56 ? 34  MET F CE    1 
ATOM   13808 N  N     A ALA C 3 35  ? 60.641  -17.201 -35.198 0.50 33.72 ? 35  ALA F N     1 
ATOM   13809 N  N     B ALA C 3 35  ? 60.513  -17.300 -35.271 0.50 33.43 ? 35  ALA F N     1 
ATOM   13810 C  CA    A ALA C 3 35  ? 61.514  -17.444 -36.343 0.50 27.77 ? 35  ALA F CA    1 
ATOM   13811 C  CA    B ALA C 3 35  ? 61.345  -17.572 -36.438 0.50 28.55 ? 35  ALA F CA    1 
ATOM   13812 C  C     A ALA C 3 35  ? 61.535  -16.257 -37.296 0.50 29.56 ? 35  ALA F C     1 
ATOM   13813 C  C     B ALA C 3 35  ? 61.203  -16.514 -37.523 0.50 31.33 ? 35  ALA F C     1 
ATOM   13814 O  O     A ALA C 3 35  ? 62.543  -16.025 -37.975 0.50 35.35 ? 35  ALA F O     1 
ATOM   13815 O  O     B ALA C 3 35  ? 62.019  -16.488 -38.451 0.50 32.74 ? 35  ALA F O     1 
ATOM   13816 C  CB    A ALA C 3 35  ? 61.076  -18.709 -37.081 0.50 31.36 ? 35  ALA F CB    1 
ATOM   13817 C  CB    B ALA C 3 35  ? 61.011  -18.949 -37.014 0.50 31.28 ? 35  ALA F CB    1 
ATOM   13818 N  N     A ASN C 3 36  ? 60.440  -15.502 -37.370 0.50 29.66 ? 36  ASN F N     1 
ATOM   13819 N  N     B ASN C 3 36  ? 60.191  -15.651 -37.436 0.50 29.60 ? 36  ASN F N     1 
ATOM   13820 C  CA    A ASN C 3 36  ? 60.356  -14.329 -38.230 0.50 32.03 ? 36  ASN F CA    1 
ATOM   13821 C  CA    B ASN C 3 36  ? 59.986  -14.577 -38.397 0.50 31.76 ? 36  ASN F CA    1 
ATOM   13822 C  C     A ASN C 3 36  ? 60.795  -13.046 -37.529 0.50 32.55 ? 36  ASN F C     1 
ATOM   13823 C  C     B ASN C 3 36  ? 60.279  -13.203 -37.802 0.50 30.64 ? 36  ASN F C     1 
ATOM   13824 O  O     A ASN C 3 36  ? 60.535  -11.952 -38.042 0.50 29.05 ? 36  ASN F O     1 
ATOM   13825 O  O     B ASN C 3 36  ? 59.827  -12.187 -38.341 0.50 31.73 ? 36  ASN F O     1 
ATOM   13826 C  CB    A ASN C 3 36  ? 58.934  -14.180 -38.776 0.50 36.31 ? 36  ASN F CB    1 
ATOM   13827 C  CB    B ASN C 3 36  ? 58.563  -14.634 -38.952 0.50 37.16 ? 36  ASN F CB    1 
ATOM   13828 C  CG    A ASN C 3 36  ? 58.711  -14.984 -40.049 0.50 37.70 ? 36  ASN F CG    1 
ATOM   13829 C  CG    B ASN C 3 36  ? 58.380  -15.753 -39.963 0.50 37.54 ? 36  ASN F CG    1 
ATOM   13830 O  OD1   A ASN C 3 36  ? 59.532  -14.953 -40.966 0.50 38.15 ? 36  ASN F OD1   1 
ATOM   13831 O  OD1   B ASN C 3 36  ? 58.137  -16.903 -39.599 0.50 36.36 ? 36  ASN F OD1   1 
ATOM   13832 N  ND2   A ASN C 3 36  ? 57.601  -15.713 -40.107 0.50 37.85 ? 36  ASN F ND2   1 
ATOM   13833 N  ND2   B ASN C 3 36  ? 58.500  -15.417 -41.242 0.50 35.73 ? 36  ASN F ND2   1 
ATOM   13834 N  N     A GLY C 3 37  ? 61.445  -13.154 -36.370 0.50 30.32 ? 37  GLY F N     1 
ATOM   13835 N  N     B GLY C 3 37  ? 61.023  -13.150 -36.701 0.50 33.05 ? 37  GLY F N     1 
ATOM   13836 C  CA    A GLY C 3 37  ? 62.081  -12.020 -35.735 0.50 26.20 ? 37  GLY F CA    1 
ATOM   13837 C  CA    B GLY C 3 37  ? 61.502  -11.898 -36.154 0.50 25.75 ? 37  GLY F CA    1 
ATOM   13838 C  C     A GLY C 3 37  ? 61.273  -11.300 -34.677 0.50 28.05 ? 37  GLY F C     1 
ATOM   13839 C  C     B GLY C 3 37  ? 60.677  -11.285 -35.045 0.50 30.04 ? 37  GLY F C     1 
ATOM   13840 O  O     A GLY C 3 37  ? 61.731  -10.261 -34.185 0.50 26.19 ? 37  GLY F O     1 
ATOM   13841 O  O     B GLY C 3 37  ? 60.868  -10.100 -34.745 0.50 32.25 ? 37  GLY F O     1 
ATOM   13842 N  N     A ALA C 3 38  ? 60.099  -11.814 -34.305 0.50 31.87 ? 38  ALA F N     1 
ATOM   13843 N  N     B ALA C 3 38  ? 59.776  -12.040 -34.424 0.50 31.66 ? 38  ALA F N     1 
ATOM   13844 C  CA    A ALA C 3 38  ? 59.244  -11.125 -33.343 0.50 28.84 ? 38  ALA F CA    1 
ATOM   13845 C  CA    B ALA C 3 38  ? 58.958  -11.477 -33.358 0.50 30.03 ? 38  ALA F CA    1 
ATOM   13846 C  C     A ALA C 3 38  ? 60.002  -10.827 -32.055 0.50 25.19 ? 38  ALA F C     1 
ATOM   13847 C  C     B ALA C 3 38  ? 59.807  -11.173 -32.130 0.50 25.36 ? 38  ALA F C     1 
ATOM   13848 O  O     A ALA C 3 38  ? 60.906  -11.565 -31.653 0.50 25.20 ? 38  ALA F O     1 
ATOM   13849 O  O     B ALA C 3 38  ? 60.649  -11.976 -31.722 0.50 26.05 ? 38  ALA F O     1 
ATOM   13850 C  CB    A ALA C 3 38  ? 58.001  -11.962 -33.033 0.50 30.14 ? 38  ALA F CB    1 
ATOM   13851 C  CB    B ALA C 3 38  ? 57.826  -12.431 -32.983 0.50 29.29 ? 38  ALA F CB    1 
ATOM   13852 N  N     A ASP C 3 39  ? 59.630  -9.723  -31.410 0.50 27.74 ? 39  ASP F N     1 
ATOM   13853 N  N     B ASP C 3 39  ? 59.576  -9.999  -31.545 0.50 28.57 ? 39  ASP F N     1 
ATOM   13854 C  CA    A ASP C 3 39  ? 60.279  -9.285  -30.176 0.50 28.57 ? 39  ASP F CA    1 
ATOM   13855 C  CA    B ASP C 3 39  ? 60.257  -9.594  -30.320 0.50 28.55 ? 39  ASP F CA    1 
ATOM   13856 C  C     A ASP C 3 39  ? 59.778  -10.163 -29.033 0.50 28.83 ? 39  ASP F C     1 
ATOM   13857 C  C     B ASP C 3 39  ? 59.701  -10.399 -29.149 0.50 28.44 ? 39  ASP F C     1 
ATOM   13858 O  O     A ASP C 3 39  ? 58.653  -10.003 -28.556 0.50 28.67 ? 39  ASP F O     1 
ATOM   13859 O  O     B ASP C 3 39  ? 58.563  -10.181 -28.720 0.50 28.74 ? 39  ASP F O     1 
ATOM   13860 C  CB    A ASP C 3 39  ? 59.995  -7.807  -29.924 0.50 26.72 ? 39  ASP F CB    1 
ATOM   13861 C  CB    B ASP C 3 39  ? 60.072  -8.092  -30.108 0.50 27.10 ? 39  ASP F CB    1 
ATOM   13862 C  CG    A ASP C 3 39  ? 60.834  -7.223  -28.798 0.50 30.07 ? 39  ASP F CG    1 
ATOM   13863 C  CG    B ASP C 3 39  ? 60.817  -7.560  -28.892 0.50 30.30 ? 39  ASP F CG    1 
ATOM   13864 O  OD1   A ASP C 3 39  ? 61.456  -7.988  -28.025 0.50 29.53 ? 39  ASP F OD1   1 
ATOM   13865 O  OD1   B ASP C 3 39  ? 61.467  -8.346  -28.165 0.50 30.65 ? 39  ASP F OD1   1 
ATOM   13866 O  OD2   A ASP C 3 39  ? 60.875  -5.978  -28.689 0.50 27.14 ? 39  ASP F OD2   1 
ATOM   13867 O  OD2   B ASP C 3 39  ? 60.749  -6.332  -28.664 0.50 27.45 ? 39  ASP F OD2   1 
ATOM   13868 N  N     A VAL C 3 40  ? 60.625  -11.096 -28.590 0.50 27.52 ? 40  VAL F N     1 
ATOM   13869 N  N     B VAL C 3 40  ? 60.503  -11.333 -28.629 0.50 27.32 ? 40  VAL F N     1 
ATOM   13870 C  CA    A VAL C 3 40  ? 60.265  -11.994 -27.495 0.50 26.91 ? 40  VAL F CA    1 
ATOM   13871 C  CA    B VAL C 3 40  ? 60.096  -12.132 -27.477 0.50 26.89 ? 40  VAL F CA    1 
ATOM   13872 C  C     A VAL C 3 40  ? 60.015  -11.216 -26.208 0.50 27.54 ? 40  VAL F C     1 
ATOM   13873 C  C     B VAL C 3 40  ? 59.860  -11.260 -26.249 0.50 27.69 ? 40  VAL F C     1 
ATOM   13874 O  O     A VAL C 3 40  ? 59.242  -11.653 -25.344 0.50 29.06 ? 40  VAL F O     1 
ATOM   13875 O  O     B VAL C 3 40  ? 59.087  -11.633 -25.358 0.50 29.12 ? 40  VAL F O     1 
ATOM   13876 C  CB    A VAL C 3 40  ? 61.369  -13.062 -27.324 0.50 25.87 ? 40  VAL F CB    1 
ATOM   13877 C  CB    B VAL C 3 40  ? 61.154  -13.231 -27.214 0.50 25.49 ? 40  VAL F CB    1 
ATOM   13878 C  CG1   A VAL C 3 40  ? 61.248  -13.793 -25.998 0.50 28.34 ? 40  VAL F CG1   1 
ATOM   13879 C  CG1   B VAL C 3 40  ? 60.946  -13.910 -25.866 0.50 29.14 ? 40  VAL F CG1   1 
ATOM   13880 C  CG2   A VAL C 3 40  ? 61.318  -14.057 -28.472 0.50 28.52 ? 40  VAL F CG2   1 
ATOM   13881 C  CG2   B VAL C 3 40  ? 61.119  -14.271 -28.327 0.50 27.80 ? 40  VAL F CG2   1 
ATOM   13882 N  N     A ASN C 3 41  ? 60.636  -10.046 -26.066 0.50 23.41 ? 41  ASN F N     1 
ATOM   13883 N  N     B ASN C 3 41  ? 60.492  -10.087 -26.187 0.50 23.67 ? 41  ASN F N     1 
ATOM   13884 C  CA    A ASN C 3 41  ? 60.531  -9.239  -24.858 0.50 30.25 ? 41  ASN F CA    1 
ATOM   13885 C  CA    B ASN C 3 41  ? 60.326  -9.156  -25.079 0.50 29.82 ? 41  ASN F CA    1 
ATOM   13886 C  C     A ASN C 3 41  ? 59.770  -7.934  -25.088 0.50 26.34 ? 41  ASN F C     1 
ATOM   13887 C  C     B ASN C 3 41  ? 59.312  -8.056  -25.384 0.50 25.74 ? 41  ASN F C     1 
ATOM   13888 O  O     A ASN C 3 41  ? 60.035  -6.927  -24.426 0.50 27.44 ? 41  ASN F O     1 
ATOM   13889 O  O     B ASN C 3 41  ? 59.401  -6.957  -24.825 0.50 25.29 ? 41  ASN F O     1 
ATOM   13890 C  CB    A ASN C 3 41  ? 61.923  -8.965  -24.293 0.50 27.32 ? 41  ASN F CB    1 
ATOM   13891 C  CB    B ASN C 3 41  ? 61.676  -8.552  -24.694 0.50 25.84 ? 41  ASN F CB    1 
ATOM   13892 C  CG    A ASN C 3 41  ? 62.530  -10.189 -23.638 0.50 27.58 ? 41  ASN F CG    1 
ATOM   13893 C  CG    B ASN C 3 41  ? 62.592  -9.558  -24.027 0.50 27.22 ? 41  ASN F CG    1 
ATOM   13894 O  OD1   A ASN C 3 41  ? 61.906  -10.819 -22.783 0.50 21.78 ? 41  ASN F OD1   1 
ATOM   13895 O  OD1   B ASN C 3 41  ? 62.486  -9.804  -22.827 0.50 28.04 ? 41  ASN F OD1   1 
ATOM   13896 N  ND2   A ASN C 3 41  ? 63.746  -10.545 -24.047 0.50 25.14 ? 41  ASN F ND2   1 
ATOM   13897 N  ND2   B ASN C 3 41  ? 63.497  -10.149 -24.803 0.50 28.16 ? 41  ASN F ND2   1 
ATOM   13898 N  N     A ALA C 3 42  ? 58.818  -7.939  -26.019 0.50 26.02 ? 42  ALA F N     1 
ATOM   13899 N  N     B ALA C 3 42  ? 58.346  -8.334  -26.257 0.50 28.94 ? 42  ALA F N     1 
ATOM   13900 C  CA    A ALA C 3 42  ? 57.939  -6.796  -26.193 0.50 25.25 ? 42  ALA F CA    1 
ATOM   13901 C  CA    B ALA C 3 42  ? 57.284  -7.378  -26.533 0.50 29.46 ? 42  ALA F CA    1 
ATOM   13902 C  C     A ALA C 3 42  ? 57.022  -6.652  -24.979 0.50 25.50 ? 42  ALA F C     1 
ATOM   13903 C  C     B ALA C 3 42  ? 56.379  -7.226  -25.317 0.50 24.84 ? 42  ALA F C     1 
ATOM   13904 O  O     A ALA C 3 42  ? 56.918  -7.542  -24.131 0.50 18.96 ? 42  ALA F O     1 
ATOM   13905 O  O     B ALA C 3 42  ? 56.098  -8.193  -24.606 0.50 24.61 ? 42  ALA F O     1 
ATOM   13906 C  CB    A ALA C 3 42  ? 57.112  -6.940  -27.470 0.50 33.49 ? 42  ALA F CB    1 
ATOM   13907 C  CB    B ALA C 3 42  ? 56.463  -7.825  -27.742 0.50 28.65 ? 42  ALA F CB    1 
ATOM   13908 N  N     A THR C 3 43  ? 56.358  -5.504  -24.893 0.50 25.76 ? 43  THR F N     1 
ATOM   13909 N  N     B THR C 3 43  ? 55.919  -6.002  -25.083 0.50 31.43 ? 43  THR F N     1 
ATOM   13910 C  CA    A THR C 3 43  ? 55.435  -5.231  -23.800 0.50 28.46 ? 43  THR F CA    1 
ATOM   13911 C  CA    B THR C 3 43  ? 55.072  -5.688  -23.943 0.50 24.92 ? 43  THR F CA    1 
ATOM   13912 C  C     A THR C 3 43  ? 54.118  -4.712  -24.352 0.50 32.59 ? 43  THR F C     1 
ATOM   13913 C  C     B THR C 3 43  ? 53.769  -5.065  -24.423 0.50 32.67 ? 43  THR F C     1 
ATOM   13914 O  O     A THR C 3 43  ? 54.088  -4.028  -25.378 0.50 30.51 ? 43  THR F O     1 
ATOM   13915 O  O     B THR C 3 43  ? 53.728  -4.402  -25.464 0.50 32.02 ? 43  THR F O     1 
ATOM   13916 C  CB    A THR C 3 43  ? 55.999  -4.195  -22.813 0.50 31.95 ? 43  THR F CB    1 
ATOM   13917 C  CB    B THR C 3 43  ? 55.782  -4.726  -22.982 0.50 29.43 ? 43  THR F CB    1 
ATOM   13918 O  OG1   A THR C 3 43  ? 56.022  -2.904  -23.436 0.50 40.34 ? 43  THR F OG1   1 
ATOM   13919 O  OG1   B THR C 3 43  ? 56.125  -3.523  -23.683 0.50 37.65 ? 43  THR F OG1   1 
ATOM   13920 C  CG2   A THR C 3 43  ? 57.412  -4.572  -22.372 0.50 33.79 ? 43  THR F CG2   1 
ATOM   13921 C  CG2   B THR C 3 43  ? 57.054  -5.364  -22.428 0.50 34.39 ? 43  THR F CG2   1 
ATOM   13922 N  N     A ASP C 3 44  ? 53.026  -5.034  -23.658 0.50 32.92 ? 44  ASP F N     1 
ATOM   13923 N  N     B ASP C 3 44  ? 52.700  -5.279  -23.657 0.50 32.43 ? 44  ASP F N     1 
ATOM   13924 C  CA    A ASP C 3 44  ? 51.761  -4.361  -23.915 0.50 32.07 ? 44  ASP F CA    1 
ATOM   13925 C  CA    B ASP C 3 44  ? 51.422  -4.651  -23.960 0.50 32.38 ? 44  ASP F CA    1 
ATOM   13926 C  C     A ASP C 3 44  ? 51.766  -3.047  -23.135 0.50 33.10 ? 44  ASP F C     1 
ATOM   13927 C  C     B ASP C 3 44  ? 51.374  -3.275  -23.292 0.50 32.59 ? 44  ASP F C     1 
ATOM   13928 O  O     A ASP C 3 44  ? 52.781  -2.652  -22.554 0.50 31.54 ? 44  ASP F O     1 
ATOM   13929 O  O     B ASP C 3 44  ? 52.407  -2.722  -22.906 0.50 32.59 ? 44  ASP F O     1 
ATOM   13930 C  CB    A ASP C 3 44  ? 50.573  -5.276  -23.595 0.50 30.18 ? 44  ASP F CB    1 
ATOM   13931 C  CB    B ASP C 3 44  ? 50.259  -5.564  -23.544 0.50 30.16 ? 44  ASP F CB    1 
ATOM   13932 C  CG    A ASP C 3 44  ? 50.376  -5.533  -22.099 0.50 29.56 ? 44  ASP F CG    1 
ATOM   13933 C  CG    B ASP C 3 44  ? 50.298  -5.957  -22.074 0.50 29.04 ? 44  ASP F CG    1 
ATOM   13934 O  OD1   A ASP C 3 44  ? 51.171  -5.055  -21.264 0.50 30.62 ? 44  ASP F OD1   1 
ATOM   13935 O  OD1   B ASP C 3 44  ? 50.508  -5.087  -21.205 0.50 26.09 ? 44  ASP F OD1   1 
ATOM   13936 O  OD2   A ASP C 3 44  ? 49.392  -6.226  -21.757 0.50 19.58 ? 44  ASP F OD2   1 
ATOM   13937 O  OD2   B ASP C 3 44  ? 50.076  -7.148  -21.784 0.50 32.27 ? 44  ASP F OD2   1 
ATOM   13938 N  N     A ALA C 3 45  ? 50.627  -2.354  -23.106 0.50 31.09 ? 45  ALA F N     1 
ATOM   13939 N  N     B ALA C 3 45  ? 50.178  -2.716  -23.142 0.50 29.50 ? 45  ALA F N     1 
ATOM   13940 C  CA    A ALA C 3 45  ? 50.587  -1.037  -22.478 0.50 33.90 ? 45  ALA F CA    1 
ATOM   13941 C  CA    B ALA C 3 45  ? 49.969  -1.369  -22.607 0.50 33.46 ? 45  ALA F CA    1 
ATOM   13942 C  C     A ALA C 3 45  ? 50.907  -1.105  -20.989 0.50 33.21 ? 45  ALA F C     1 
ATOM   13943 C  C     B ALA C 3 45  ? 50.175  -1.273  -21.105 0.50 34.61 ? 45  ALA F C     1 
ATOM   13944 O  O     A ALA C 3 45  ? 51.437  -0.140  -20.427 0.50 31.15 ? 45  ALA F O     1 
ATOM   13945 O  O     B ALA C 3 45  ? 49.920  -0.197  -20.540 0.50 36.26 ? 45  ALA F O     1 
ATOM   13946 C  CB    A ALA C 3 45  ? 49.221  -0.390  -22.695 0.50 30.61 ? 45  ALA F CB    1 
ATOM   13947 C  CB    B ALA C 3 45  ? 48.565  -0.882  -22.966 0.50 35.76 ? 45  ALA F CB    1 
ATOM   13948 N  N     A SER C 3 46  ? 50.605  -2.227  -20.338 0.50 29.13 ? 46  SER F N     1 
ATOM   13949 N  N     B SER C 3 46  ? 50.619  -2.337  -20.438 0.50 29.27 ? 46  SER F N     1 
ATOM   13950 C  CA    A SER C 3 46  ? 50.839  -2.384  -18.911 0.50 35.99 ? 46  SER F CA    1 
ATOM   13951 C  CA    B SER C 3 46  ? 50.879  -2.284  -19.008 0.50 35.95 ? 46  SER F CA    1 
ATOM   13952 C  C     A SER C 3 46  ? 52.188  -3.023  -18.604 0.50 34.67 ? 46  SER F C     1 
ATOM   13953 C  C     B SER C 3 46  ? 52.170  -2.979  -18.605 0.50 34.67 ? 46  SER F C     1 
ATOM   13954 O  O     A SER C 3 46  ? 52.380  -3.533  -17.495 0.50 33.30 ? 46  SER F O     1 
ATOM   13955 O  O     B SER C 3 46  ? 52.467  -3.035  -17.407 0.50 34.04 ? 46  SER F O     1 
ATOM   13956 C  CB    A SER C 3 46  ? 49.715  -3.207  -18.275 0.50 32.17 ? 46  SER F CB    1 
ATOM   13957 C  CB    B SER C 3 46  ? 49.700  -2.888  -18.225 0.50 31.92 ? 46  SER F CB    1 
ATOM   13958 O  OG    A SER C 3 46  ? 49.804  -4.570  -18.649 0.50 35.41 ? 46  SER F OG    1 
ATOM   13959 O  OG    B SER C 3 46  ? 48.970  -3.804  -19.022 0.50 31.40 ? 46  SER F OG    1 
ATOM   13960 N  N     A GLY C 3 47  ? 53.121  -3.009  -19.557 0.50 28.76 ? 47  GLY F N     1 
ATOM   13961 N  N     B GLY C 3 47  ? 52.942  -3.506  -19.552 0.50 29.34 ? 47  GLY F N     1 
ATOM   13962 C  CA    A GLY C 3 47  ? 54.440  -3.565  -19.345 0.50 27.42 ? 47  GLY F CA    1 
ATOM   13963 C  CA    B GLY C 3 47  ? 54.231  -4.087  -19.254 0.50 27.38 ? 47  GLY F CA    1 
ATOM   13964 C  C     A GLY C 3 47  ? 54.515  -5.074  -19.304 0.50 27.68 ? 47  GLY F C     1 
ATOM   13965 C  C     B GLY C 3 47  ? 54.290  -5.597  -19.205 0.50 28.08 ? 47  GLY F C     1 
ATOM   13966 O  O     A GLY C 3 47  ? 55.591  -5.614  -19.020 0.50 24.74 ? 47  GLY F O     1 
ATOM   13967 O  O     B GLY C 3 47  ? 55.339  -6.139  -18.835 0.50 29.52 ? 47  GLY F O     1 
ATOM   13968 N  N     A LEU C 3 48  ? 53.416  -5.774  -19.573 0.50 26.08 ? 48  LEU F N     1 
ATOM   13969 N  N     B LEU C 3 48  ? 53.214  -6.294  -19.568 0.50 26.54 ? 48  LEU F N     1 
ATOM   13970 C  CA    A LEU C 3 48  ? 53.439  -7.230  -19.599 0.50 27.88 ? 48  LEU F CA    1 
ATOM   13971 C  CA    B LEU C 3 48  ? 53.226  -7.752  -19.571 0.50 26.40 ? 48  LEU F CA    1 
ATOM   13972 C  C     A LEU C 3 48  ? 54.165  -7.736  -20.842 0.50 27.51 ? 48  LEU F C     1 
ATOM   13973 C  C     B LEU C 3 48  ? 53.876  -8.277  -20.848 0.50 26.60 ? 48  LEU F C     1 
ATOM   13974 O  O     A LEU C 3 48  ? 53.966  -7.220  -21.945 0.50 26.45 ? 48  LEU F O     1 
ATOM   13975 O  O     B LEU C 3 48  ? 53.539  -7.841  -21.952 0.50 27.39 ? 48  LEU F O     1 
ATOM   13976 C  CB    A LEU C 3 48  ? 52.013  -7.777  -19.574 0.50 24.09 ? 48  LEU F CB    1 
ATOM   13977 C  CB    B LEU C 3 48  ? 51.808  -8.306  -19.443 0.50 25.57 ? 48  LEU F CB    1 
ATOM   13978 C  CG    A LEU C 3 48  ? 51.204  -7.564  -18.294 0.50 27.37 ? 48  LEU F CG    1 
ATOM   13979 C  CG    B LEU C 3 48  ? 51.108  -8.226  -18.084 0.50 26.98 ? 48  LEU F CG    1 
ATOM   13980 C  CD1   A LEU C 3 48  ? 49.725  -7.791  -18.561 0.50 23.76 ? 48  LEU F CD1   1 
ATOM   13981 C  CD1   B LEU C 3 48  ? 49.813  -9.021  -18.117 0.50 19.85 ? 48  LEU F CD1   1 
ATOM   13982 C  CD2   A LEU C 3 48  ? 51.697  -8.493  -17.197 0.50 25.14 ? 48  LEU F CD2   1 
ATOM   13983 C  CD2   B LEU C 3 48  ? 52.019  -8.723  -16.969 0.50 23.05 ? 48  LEU F CD2   1 
ATOM   13984 N  N     A THR C 3 49  ? 54.994  -8.758  -20.661 0.50 28.45 ? 49  THR F N     1 
ATOM   13985 N  N     B THR C 3 49  ? 54.798  -9.218  -20.691 0.50 25.41 ? 49  THR F N     1 
ATOM   13986 C  CA    A THR C 3 49  ? 55.703  -9.437  -21.738 0.50 27.28 ? 49  THR F CA    1 
ATOM   13987 C  CA    B THR C 3 49  ? 55.495  -9.844  -21.808 0.50 28.52 ? 49  THR F CA    1 
ATOM   13988 C  C     A THR C 3 49  ? 54.997  -10.736 -22.094 0.50 27.68 ? 49  THR F C     1 
ATOM   13989 C  C     B THR C 3 49  ? 54.784  -11.127 -22.206 0.50 27.60 ? 49  THR F C     1 
ATOM   13990 O  O     A THR C 3 49  ? 54.108  -11.194 -21.370 0.50 27.05 ? 49  THR F O     1 
ATOM   13991 O  O     B THR C 3 49  ? 53.822  -11.547 -21.556 0.50 25.20 ? 49  THR F O     1 
ATOM   13992 C  CB    A THR C 3 49  ? 57.150  -9.723  -21.321 0.50 26.86 ? 49  THR F CB    1 
ATOM   13993 C  CB    B THR C 3 49  ? 56.945  -10.128 -21.419 0.50 26.91 ? 49  THR F CB    1 
ATOM   13994 O  OG1   A THR C 3 49  ? 57.164  -10.704 -20.274 0.50 25.75 ? 49  THR F OG1   1 
ATOM   13995 O  OG1   B THR C 3 49  ? 56.978  -11.146 -20.413 0.50 21.35 ? 49  THR F OG1   1 
ATOM   13996 C  CG2   A THR C 3 49  ? 57.845  -8.453  -20.853 0.50 27.86 ? 49  THR F CG2   1 
ATOM   13997 C  CG2   B THR C 3 49  ? 57.624  -8.868  -20.903 0.50 27.85 ? 49  THR F CG2   1 
ATOM   13998 N  N     A PRO C 3 50  ? 55.354  -11.361 -23.222 0.50 24.64 ? 50  PRO F N     1 
ATOM   13999 N  N     B PRO C 3 50  ? 55.215  -11.781 -23.292 0.50 25.30 ? 50  PRO F N     1 
ATOM   14000 C  CA    A PRO C 3 50  ? 54.787  -12.687 -23.520 0.50 23.09 ? 50  PRO F CA    1 
ATOM   14001 C  CA    B PRO C 3 50  ? 54.687  -13.125 -23.569 0.50 21.84 ? 50  PRO F CA    1 
ATOM   14002 C  C     A PRO C 3 50  ? 55.058  -13.715 -22.436 0.50 26.18 ? 50  PRO F C     1 
ATOM   14003 C  C     B PRO C 3 50  ? 54.971  -14.119 -22.458 0.50 26.66 ? 50  PRO F C     1 
ATOM   14004 O  O     A PRO C 3 50  ? 54.241  -14.625 -22.241 0.50 28.91 ? 50  PRO F O     1 
ATOM   14005 O  O     B PRO C 3 50  ? 54.163  -15.029 -22.231 0.50 29.79 ? 50  PRO F O     1 
ATOM   14006 C  CB    A PRO C 3 50  ? 55.467  -13.064 -24.842 0.50 26.71 ? 50  PRO F CB    1 
ATOM   14007 C  CB    B PRO C 3 50  ? 55.399  -13.515 -24.871 0.50 26.95 ? 50  PRO F CB    1 
ATOM   14008 C  CG    A PRO C 3 50  ? 55.730  -11.754 -25.494 0.50 27.48 ? 50  PRO F CG    1 
ATOM   14009 C  CG    B PRO C 3 50  ? 55.650  -12.223 -25.543 0.50 26.07 ? 50  PRO F CG    1 
ATOM   14010 C  CD    A PRO C 3 50  ? 56.128  -10.836 -24.364 0.50 26.78 ? 50  PRO F CD    1 
ATOM   14011 C  CD    B PRO C 3 50  ? 56.012  -11.279 -24.427 0.50 27.52 ? 50  PRO F CD    1 
ATOM   14012 N  N     A LEU C 3 51  ? 56.177  -13.603 -21.717 0.50 24.50 ? 51  LEU F N     1 
ATOM   14013 N  N     B LEU C 3 51  ? 56.099  -13.982 -21.758 0.50 25.93 ? 51  LEU F N     1 
ATOM   14014 C  CA    A LEU C 3 51  ? 56.428  -14.538 -20.625 0.50 24.95 ? 51  LEU F CA    1 
ATOM   14015 C  CA    B LEU C 3 51  ? 56.370  -14.879 -20.640 0.50 24.32 ? 51  LEU F CA    1 
ATOM   14016 C  C     A LEU C 3 51  ? 55.426  -14.339 -19.491 0.50 24.10 ? 51  LEU F C     1 
ATOM   14017 C  C     B LEU C 3 51  ? 55.405  -14.622 -19.487 0.50 24.29 ? 51  LEU F C     1 
ATOM   14018 O  O     A LEU C 3 51  ? 54.978  -15.315 -18.881 0.50 25.23 ? 51  LEU F O     1 
ATOM   14019 O  O     B LEU C 3 51  ? 54.959  -15.567 -18.828 0.50 25.31 ? 51  LEU F O     1 
ATOM   14020 C  CB    A LEU C 3 51  ? 57.859  -14.390 -20.117 0.50 24.06 ? 51  LEU F CB    1 
ATOM   14021 C  CB    B LEU C 3 51  ? 57.819  -14.729 -20.180 0.50 22.92 ? 51  LEU F CB    1 
ATOM   14022 C  CG    A LEU C 3 51  ? 58.304  -15.391 -19.052 0.50 30.05 ? 51  LEU F CG    1 
ATOM   14023 C  CG    B LEU C 3 51  ? 58.267  -15.621 -19.023 0.50 30.19 ? 51  LEU F CG    1 
ATOM   14024 C  CD1   A LEU C 3 51  ? 58.055  -16.818 -19.510 0.50 25.98 ? 51  LEU F CD1   1 
ATOM   14025 C  CD1   B LEU C 3 51  ? 58.049  -17.091 -19.349 0.50 25.26 ? 51  LEU F CD1   1 
ATOM   14026 C  CD2   A LEU C 3 51  ? 59.771  -15.178 -18.710 0.50 22.87 ? 51  LEU F CD2   1 
ATOM   14027 C  CD2   B LEU C 3 51  ? 59.725  -15.346 -18.678 0.50 23.10 ? 51  LEU F CD2   1 
ATOM   14028 N  N     A HIS C 3 52  ? 55.066  -13.083 -19.201 0.50 26.22 ? 52  HIS F N     1 
ATOM   14029 N  N     B HIS C 3 52  ? 55.076  -13.350 -19.233 0.50 25.54 ? 52  HIS F N     1 
ATOM   14030 C  CA    A HIS C 3 52  ? 54.029  -12.798 -18.208 0.50 25.97 ? 52  HIS F CA    1 
ATOM   14031 C  CA    B HIS C 3 52  ? 54.081  -13.007 -18.217 0.50 25.68 ? 52  HIS F CA    1 
ATOM   14032 C  C     A HIS C 3 52  ? 52.728  -13.513 -18.544 0.50 29.05 ? 52  HIS F C     1 
ATOM   14033 C  C     B HIS C 3 52  ? 52.744  -13.678 -18.502 0.50 29.03 ? 52  HIS F C     1 
ATOM   14034 O  O     A HIS C 3 52  ? 52.124  -14.171 -17.688 0.50 28.11 ? 52  HIS F O     1 
ATOM   14035 O  O     B HIS C 3 52  ? 52.127  -14.268 -17.607 0.50 28.20 ? 52  HIS F O     1 
ATOM   14036 C  CB    A HIS C 3 52  ? 53.760  -11.292 -18.129 0.50 25.02 ? 52  HIS F CB    1 
ATOM   14037 C  CB    B HIS C 3 52  ? 53.883  -11.489 -18.157 0.50 25.69 ? 52  HIS F CB    1 
ATOM   14038 C  CG    A HIS C 3 52  ? 54.774  -10.514 -17.351 0.50 27.17 ? 52  HIS F CG    1 
ATOM   14039 C  CG    B HIS C 3 52  ? 54.911  -10.759 -17.352 0.50 27.31 ? 52  HIS F CG    1 
ATOM   14040 N  ND1   A HIS C 3 52  ? 55.720  -9.715  -17.955 0.50 26.61 ? 52  HIS F ND1   1 
ATOM   14041 N  ND1   B HIS C 3 52  ? 55.951  -10.062 -17.930 0.50 26.48 ? 52  HIS F ND1   1 
ATOM   14042 C  CD2   A HIS C 3 52  ? 54.965  -10.382 -16.017 0.50 25.69 ? 52  HIS F CD2   1 
ATOM   14043 C  CD2   B HIS C 3 52  ? 55.040  -10.588 -16.015 0.50 25.50 ? 52  HIS F CD2   1 
ATOM   14044 C  CE1   A HIS C 3 52  ? 56.457  -9.133  -17.026 0.50 29.20 ? 52  HIS F CE1   1 
ATOM   14045 C  CE1   B HIS C 3 52  ? 56.684  -9.506  -16.981 0.50 29.39 ? 52  HIS F CE1   1 
ATOM   14046 N  NE2   A HIS C 3 52  ? 56.019  -9.520  -15.841 0.50 24.25 ? 52  HIS F NE2   1 
ATOM   14047 N  NE2   B HIS C 3 52  ? 56.149  -9.805  -15.810 0.50 25.16 ? 52  HIS F NE2   1 
ATOM   14048 N  N     A LEU C 3 53  ? 52.263  -13.363 -19.786 0.50 29.33 ? 53  LEU F N     1 
ATOM   14049 N  N     B LEU C 3 53  ? 52.264  -13.566 -19.743 0.50 29.24 ? 53  LEU F N     1 
ATOM   14050 C  CA    A LEU C 3 53  ? 50.942  -13.853 -20.158 0.50 31.01 ? 53  LEU F CA    1 
ATOM   14051 C  CA    B LEU C 3 53  ? 50.951  -14.106 -20.083 0.50 31.68 ? 53  LEU F CA    1 
ATOM   14052 C  C     A LEU C 3 53  ? 50.917  -15.364 -20.333 0.50 30.32 ? 53  LEU F C     1 
ATOM   14053 C  C     B LEU C 3 53  ? 50.959  -15.628 -20.046 0.50 30.51 ? 53  LEU F C     1 
ATOM   14054 O  O     A LEU C 3 53  ? 49.885  -15.995 -20.081 0.50 31.36 ? 53  LEU F O     1 
ATOM   14055 O  O     B LEU C 3 53  ? 50.039  -16.250 -19.501 0.50 29.16 ? 53  LEU F O     1 
ATOM   14056 C  CB    A LEU C 3 53  ? 50.472  -13.163 -21.437 0.50 25.93 ? 53  LEU F CB    1 
ATOM   14057 C  CB    B LEU C 3 53  ? 50.511  -13.599 -21.456 0.50 26.23 ? 53  LEU F CB    1 
ATOM   14058 C  CG    A LEU C 3 53  ? 50.469  -11.633 -21.402 0.50 28.85 ? 53  LEU F CG    1 
ATOM   14059 C  CG    B LEU C 3 53  ? 50.200  -12.105 -21.581 0.50 30.49 ? 53  LEU F CG    1 
ATOM   14060 C  CD1   A LEU C 3 53  ? 49.882  -11.072 -22.682 0.50 29.93 ? 53  LEU F CD1   1 
ATOM   14061 C  CD1   B LEU C 3 53  ? 49.746  -11.777 -22.992 0.50 29.15 ? 53  LEU F CD1   1 
ATOM   14062 C  CD2   A LEU C 3 53  ? 49.706  -11.117 -20.185 0.50 29.18 ? 53  LEU F CD2   1 
ATOM   14063 C  CD2   B LEU C 3 53  ? 49.141  -11.686 -20.571 0.50 32.64 ? 53  LEU F CD2   1 
ATOM   14064 N  N     A ALA C 3 54  ? 52.028  -15.958 -20.766 0.50 27.46 ? 54  ALA F N     1 
ATOM   14065 N  N     B ALA C 3 54  ? 51.992  -16.244 -20.625 0.50 28.21 ? 54  ALA F N     1 
ATOM   14066 C  CA    A ALA C 3 54  ? 52.105  -17.413 -20.814 0.50 29.55 ? 54  ALA F CA    1 
ATOM   14067 C  CA    B ALA C 3 54  ? 52.121  -17.695 -20.555 0.50 29.78 ? 54  ALA F CA    1 
ATOM   14068 C  C     A ALA C 3 54  ? 52.030  -18.006 -19.413 0.50 30.78 ? 54  ALA F C     1 
ATOM   14069 C  C     B ALA C 3 54  ? 52.158  -18.172 -19.108 0.50 31.03 ? 54  ALA F C     1 
ATOM   14070 O  O     A ALA C 3 54  ? 51.334  -19.005 -19.185 0.50 29.04 ? 54  ALA F O     1 
ATOM   14071 O  O     B ALA C 3 54  ? 51.546  -19.192 -18.763 0.50 27.65 ? 54  ALA F O     1 
ATOM   14072 C  CB    A ALA C 3 54  ? 53.392  -17.844 -21.515 0.50 28.77 ? 54  ALA F CB    1 
ATOM   14073 C  CB    B ALA C 3 54  ? 53.376  -18.146 -21.302 0.50 29.55 ? 54  ALA F CB    1 
ATOM   14074 N  N     A ALA C 3 55  ? 52.733  -17.395 -18.458 0.50 25.30 ? 55  ALA F N     1 
ATOM   14075 N  N     B ALA C 3 55  ? 52.868  -17.441 -18.247 0.50 26.06 ? 55  ALA F N     1 
ATOM   14076 C  CA    A ALA C 3 55  ? 52.737  -17.904 -17.091 0.50 27.18 ? 55  ALA F CA    1 
ATOM   14077 C  CA    B ALA C 3 55  ? 52.917  -17.794 -16.833 0.50 27.56 ? 55  ALA F CA    1 
ATOM   14078 C  C     A ALA C 3 55  ? 51.386  -17.695 -16.416 0.50 29.05 ? 55  ALA F C     1 
ATOM   14079 C  C     B ALA C 3 55  ? 51.565  -17.583 -16.163 0.50 28.64 ? 55  ALA F C     1 
ATOM   14080 O  O     A ALA C 3 55  ? 50.913  -18.569 -15.680 0.50 31.00 ? 55  ALA F O     1 
ATOM   14081 O  O     B ALA C 3 55  ? 51.185  -18.347 -15.268 0.50 31.83 ? 55  ALA F O     1 
ATOM   14082 C  CB    A ALA C 3 55  ? 53.849  -17.230 -16.288 0.50 25.14 ? 55  ALA F CB    1 
ATOM   14083 C  CB    B ALA C 3 55  ? 53.997  -16.976 -16.124 0.50 23.82 ? 55  ALA F CB    1 
ATOM   14084 N  N     A THR C 3 56  ? 50.750  -16.545 -16.655 0.50 31.14 ? 56  THR F N     1 
ATOM   14085 N  N     B THR C 3 56  ? 50.824  -16.555 -16.580 0.50 31.17 ? 56  THR F N     1 
ATOM   14086 C  CA    A THR C 3 56  ? 49.463  -16.260 -16.029 0.50 32.75 ? 56  THR F CA    1 
ATOM   14087 C  CA    B THR C 3 56  ? 49.519  -16.286 -15.985 0.50 32.72 ? 56  THR F CA    1 
ATOM   14088 C  C     A THR C 3 56  ? 48.389  -17.249 -16.474 0.50 32.30 ? 56  THR F C     1 
ATOM   14089 C  C     B THR C 3 56  ? 48.501  -17.344 -16.396 0.50 32.20 ? 56  THR F C     1 
ATOM   14090 O  O     A THR C 3 56  ? 47.488  -17.581 -15.693 0.50 33.12 ? 56  THR F O     1 
ATOM   14091 O  O     B THR C 3 56  ? 47.885  -17.997 -15.545 0.50 33.70 ? 56  THR F O     1 
ATOM   14092 C  CB    A THR C 3 56  ? 49.042  -14.820 -16.343 0.50 32.09 ? 56  THR F CB    1 
ATOM   14093 C  CB    B THR C 3 56  ? 49.035  -14.890 -16.386 0.50 32.09 ? 56  THR F CB    1 
ATOM   14094 O  OG1   A THR C 3 56  ? 49.978  -13.909 -15.751 0.50 28.47 ? 56  THR F OG1   1 
ATOM   14095 O  OG1   B THR C 3 56  ? 49.874  -13.898 -15.783 0.50 28.51 ? 56  THR F OG1   1 
ATOM   14096 C  CG2   A THR C 3 56  ? 47.650  -14.518 -15.804 0.50 34.79 ? 56  THR F CG2   1 
ATOM   14097 C  CG2   B THR C 3 56  ? 47.596  -14.672 -15.938 0.50 34.94 ? 56  THR F CG2   1 
ATOM   14098 N  N     A TYR C 3 57  ? 48.481  -17.754 -17.703 0.50 35.80 ? 57  TYR F N     1 
ATOM   14099 N  N     B TYR C 3 57  ? 48.318  -17.534 -17.701 0.50 35.83 ? 57  TYR F N     1 
ATOM   14100 C  CA    A TYR C 3 57  ? 47.479  -18.655 -18.259 0.50 29.92 ? 57  TYR F CA    1 
ATOM   14101 C  CA    B TYR C 3 57  ? 47.275  -18.405 -18.234 0.50 30.06 ? 57  TYR F CA    1 
ATOM   14102 C  C     A TYR C 3 57  ? 47.920  -20.115 -18.260 0.50 32.23 ? 57  TYR F C     1 
ATOM   14103 C  C     B TYR C 3 57  ? 47.681  -19.876 -18.290 0.50 32.31 ? 57  TYR F C     1 
ATOM   14104 O  O     A TYR C 3 57  ? 47.265  -20.948 -18.894 0.50 36.91 ? 57  TYR F O     1 
ATOM   14105 O  O     B TYR C 3 57  ? 46.942  -20.681 -18.868 0.50 36.98 ? 57  TYR F O     1 
ATOM   14106 C  CB    A TYR C 3 57  ? 47.109  -18.216 -19.677 0.50 35.09 ? 57  TYR F CB    1 
ATOM   14107 C  CB    B TYR C 3 57  ? 46.855  -17.921 -19.625 0.50 33.26 ? 57  TYR F CB    1 
ATOM   14108 C  CG    A TYR C 3 57  ? 46.239  -16.983 -19.731 0.50 35.75 ? 57  TYR F CG    1 
ATOM   14109 C  CG    B TYR C 3 57  ? 46.107  -16.606 -19.612 0.50 37.47 ? 57  TYR F CG    1 
ATOM   14110 C  CD1   A TYR C 3 57  ? 46.790  -15.715 -19.595 0.50 37.85 ? 57  TYR F CD1   1 
ATOM   14111 C  CD1   B TYR C 3 57  ? 46.790  -15.396 -19.614 0.50 37.31 ? 57  TYR F CD1   1 
ATOM   14112 C  CD2   A TYR C 3 57  ? 44.864  -17.085 -19.920 0.50 41.34 ? 57  TYR F CD2   1 
ATOM   14113 C  CD2   B TYR C 3 57  ? 44.716  -16.574 -19.594 0.50 41.81 ? 57  TYR F CD2   1 
ATOM   14114 C  CE1   A TYR C 3 57  ? 46.003  -14.584 -19.644 0.50 37.33 ? 57  TYR F CE1   1 
ATOM   14115 C  CE1   B TYR C 3 57  ? 46.115  -14.192 -19.602 0.50 36.98 ? 57  TYR F CE1   1 
ATOM   14116 C  CE2   A TYR C 3 57  ? 44.065  -15.957 -19.970 0.50 38.87 ? 57  TYR F CE2   1 
ATOM   14117 C  CE2   B TYR C 3 57  ? 44.030  -15.371 -19.581 0.50 37.84 ? 57  TYR F CE2   1 
ATOM   14118 C  CZ    A TYR C 3 57  ? 44.642  -14.710 -19.832 0.50 42.46 ? 57  TYR F CZ    1 
ATOM   14119 C  CZ    B TYR C 3 57  ? 44.736  -14.185 -19.585 0.50 42.72 ? 57  TYR F CZ    1 
ATOM   14120 O  OH    A TYR C 3 57  ? 43.859  -13.582 -19.882 0.50 41.11 ? 57  TYR F OH    1 
ATOM   14121 O  OH    B TYR C 3 57  ? 44.066  -12.984 -19.573 0.50 41.75 ? 57  TYR F OH    1 
ATOM   14122 N  N     A GLY C 3 58  ? 49.014  -20.443 -17.576 0.50 24.48 ? 58  GLY F N     1 
ATOM   14123 N  N     B GLY C 3 58  ? 48.827  -20.243 -17.718 0.50 24.91 ? 58  GLY F N     1 
ATOM   14124 C  CA    A GLY C 3 58  ? 49.403  -21.828 -17.391 0.50 28.16 ? 58  GLY F CA    1 
ATOM   14125 C  CA    B GLY C 3 58  ? 49.194  -21.637 -17.549 0.50 27.48 ? 58  GLY F CA    1 
ATOM   14126 C  C     A GLY C 3 58  ? 49.851  -22.567 -18.634 0.50 30.62 ? 58  GLY F C     1 
ATOM   14127 C  C     B GLY C 3 58  ? 49.553  -22.394 -18.814 0.50 31.71 ? 58  GLY F C     1 
ATOM   14128 O  O     A GLY C 3 58  ? 49.863  -23.801 -18.633 0.50 27.29 ? 58  GLY F O     1 
ATOM   14129 O  O     B GLY C 3 58  ? 48.843  -23.325 -19.205 0.50 30.20 ? 58  GLY F O     1 
ATOM   14130 N  N     A HIS C 3 59  ? 50.221  -21.853 -19.700 0.50 30.01 ? 59  HIS F N     1 
ATOM   14131 N  N     B HIS C 3 59  ? 50.662  -22.021 -19.454 0.50 29.94 ? 59  HIS F N     1 
ATOM   14132 C  CA    A HIS C 3 59  ? 50.709  -22.489 -20.926 0.50 32.64 ? 59  HIS F CA    1 
ATOM   14133 C  CA    B HIS C 3 59  ? 51.141  -22.686 -20.670 0.50 31.66 ? 59  HIS F CA    1 
ATOM   14134 C  C     A HIS C 3 59  ? 52.193  -22.795 -20.744 0.50 32.60 ? 59  HIS F C     1 
ATOM   14135 C  C     B HIS C 3 59  ? 52.595  -23.089 -20.438 0.50 33.57 ? 59  HIS F C     1 
ATOM   14136 O  O     A HIS C 3 59  ? 53.078  -22.047 -21.172 0.50 27.26 ? 59  HIS F O     1 
ATOM   14137 O  O     B HIS C 3 59  ? 53.515  -22.313 -20.713 0.50 31.60 ? 59  HIS F O     1 
ATOM   14138 C  CB    A HIS C 3 59  ? 50.455  -21.599 -22.136 0.50 28.41 ? 59  HIS F CB    1 
ATOM   14139 C  CB    B HIS C 3 59  ? 50.985  -21.782 -21.891 0.50 28.86 ? 59  HIS F CB    1 
ATOM   14140 C  CG    A HIS C 3 59  ? 49.015  -21.241 -22.328 0.50 32.33 ? 59  HIS F CG    1 
ATOM   14141 C  CG    B HIS C 3 59  ? 49.588  -21.284 -22.098 0.50 30.99 ? 59  HIS F CG    1 
ATOM   14142 N  ND1   A HIS C 3 59  ? 48.036  -22.185 -22.551 0.50 29.51 ? 59  HIS F ND1   1 
ATOM   14143 N  ND1   B HIS C 3 59  ? 48.504  -22.130 -22.195 0.50 30.16 ? 59  HIS F ND1   1 
ATOM   14144 C  CD2   A HIS C 3 59  ? 48.387  -20.041 -22.328 0.50 35.84 ? 59  HIS F CD2   1 
ATOM   14145 C  CD2   B HIS C 3 59  ? 49.098  -20.028 -22.220 0.50 28.33 ? 59  HIS F CD2   1 
ATOM   14146 C  CE1   A HIS C 3 59  ? 46.867  -21.582 -22.681 0.50 31.71 ? 59  HIS F CE1   1 
ATOM   14147 C  CE1   B HIS C 3 59  ? 47.405  -21.417 -22.368 0.50 32.68 ? 59  HIS F CE1   1 
ATOM   14148 N  NE2   A HIS C 3 59  ? 47.052  -20.281 -22.548 0.50 33.76 ? 59  HIS F NE2   1 
ATOM   14149 N  NE2   B HIS C 3 59  ? 47.738  -20.138 -22.387 0.50 36.98 ? 59  HIS F NE2   1 
ATOM   14150 N  N     A LEU C 3 60  ? 52.455  -23.942 -20.110 0.50 28.15 ? 60  LEU F N     1 
ATOM   14151 N  N     B LEU C 3 60  ? 52.792  -24.319 -19.956 0.50 27.94 ? 60  LEU F N     1 
ATOM   14152 C  CA    A LEU C 3 60  ? 53.807  -24.286 -19.675 0.50 29.58 ? 60  LEU F CA    1 
ATOM   14153 C  CA    B LEU C 3 60  ? 54.122  -24.764 -19.551 0.50 28.97 ? 60  LEU F CA    1 
ATOM   14154 C  C     A LEU C 3 60  ? 54.787  -24.337 -20.842 0.50 34.22 ? 60  LEU F C     1 
ATOM   14155 C  C     B LEU C 3 60  ? 55.087  -24.823 -20.731 0.50 35.13 ? 60  LEU F C     1 
ATOM   14156 O  O     A LEU C 3 60  ? 55.874  -23.752 -20.779 0.50 31.33 ? 60  LEU F O     1 
ATOM   14157 O  O     B LEU C 3 60  ? 56.259  -24.445 -20.604 0.50 27.63 ? 60  LEU F O     1 
ATOM   14158 C  CB    A LEU C 3 60  ? 53.783  -25.623 -18.936 0.50 34.04 ? 60  LEU F CB    1 
ATOM   14159 C  CB    B LEU C 3 60  ? 54.026  -26.132 -18.878 0.50 36.96 ? 60  LEU F CB    1 
ATOM   14160 C  CG    A LEU C 3 60  ? 55.074  -26.444 -18.908 0.50 38.37 ? 60  LEU F CG    1 
ATOM   14161 C  CG    B LEU C 3 60  ? 55.344  -26.758 -18.423 0.50 38.30 ? 60  LEU F CG    1 
ATOM   14162 C  CD1   A LEU C 3 60  ? 56.129  -25.795 -18.027 0.50 33.86 ? 60  LEU F CD1   1 
ATOM   14163 C  CD1   B LEU C 3 60  ? 55.837  -26.084 -17.158 0.50 36.43 ? 60  LEU F CD1   1 
ATOM   14164 C  CD2   A LEU C 3 60  ? 54.780  -27.870 -18.454 0.50 37.50 ? 60  LEU F CD2   1 
ATOM   14165 C  CD2   B LEU C 3 60  ? 55.190  -28.260 -18.221 0.50 38.87 ? 60  LEU F CD2   1 
ATOM   14166 N  N     A GLU C 3 61  ? 54.432  -25.045 -21.916 0.50 34.90 ? 61  GLU F N     1 
ATOM   14167 N  N     B GLU C 3 61  ? 54.622  -25.303 -21.887 0.50 36.10 ? 61  GLU F N     1 
ATOM   14168 C  CA    A GLU C 3 61  ? 55.399  -25.242 -22.991 0.50 37.48 ? 61  GLU F CA    1 
ATOM   14169 C  CA    B GLU C 3 61  ? 55.533  -25.482 -23.015 0.50 36.96 ? 61  GLU F CA    1 
ATOM   14170 C  C     A GLU C 3 61  ? 55.699  -23.947 -23.739 0.50 35.04 ? 61  GLU F C     1 
ATOM   14171 C  C     B GLU C 3 61  ? 55.928  -24.141 -23.626 0.50 35.11 ? 61  GLU F C     1 
ATOM   14172 O  O     A GLU C 3 61  ? 56.776  -23.826 -24.331 0.50 29.96 ? 61  GLU F O     1 
ATOM   14173 O  O     B GLU C 3 61  ? 57.081  -23.958 -24.035 0.50 28.89 ? 61  GLU F O     1 
ATOM   14174 C  CB    A GLU C 3 61  ? 54.911  -26.328 -23.959 0.50 42.35 ? 61  GLU F CB    1 
ATOM   14175 C  CB    B GLU C 3 61  ? 54.909  -26.401 -24.069 0.50 42.38 ? 61  GLU F CB    1 
ATOM   14176 C  CG    A GLU C 3 61  ? 54.756  -27.721 -23.331 0.50 41.85 ? 61  GLU F CG    1 
ATOM   14177 C  CG    B GLU C 3 61  ? 54.650  -27.834 -23.595 0.50 42.64 ? 61  GLU F CG    1 
ATOM   14178 C  CD    A GLU C 3 61  ? 53.575  -27.830 -22.375 0.50 48.55 ? 61  GLU F CD    1 
ATOM   14179 C  CD    B GLU C 3 61  ? 53.452  -27.954 -22.665 0.50 48.87 ? 61  GLU F CD    1 
ATOM   14180 O  OE1   A GLU C 3 61  ? 52.646  -26.995 -22.466 0.50 46.88 ? 61  GLU F OE1   1 
ATOM   14181 O  OE1   B GLU C 3 61  ? 52.542  -27.099 -22.743 0.50 47.52 ? 61  GLU F OE1   1 
ATOM   14182 O  OE2   A GLU C 3 61  ? 53.580  -28.749 -21.524 0.50 45.01 ? 61  GLU F OE2   1 
ATOM   14183 O  OE2   B GLU C 3 61  ? 53.423  -28.906 -21.850 0.50 47.01 ? 61  GLU F OE2   1 
ATOM   14184 N  N     A ILE C 3 62  ? 54.789  -22.969 -23.713 0.50 30.98 ? 62  ILE F N     1 
ATOM   14185 N  N     B ILE C 3 62  ? 54.992  -23.188 -23.689 0.50 31.88 ? 62  ILE F N     1 
ATOM   14186 C  CA    A ILE C 3 62  ? 55.121  -21.658 -24.263 0.50 29.96 ? 62  ILE F CA    1 
ATOM   14187 C  CA    B ILE C 3 62  ? 55.332  -21.859 -24.192 0.50 30.91 ? 62  ILE F CA    1 
ATOM   14188 C  C     A ILE C 3 62  ? 56.123  -20.948 -23.362 0.50 34.34 ? 62  ILE F C     1 
ATOM   14189 C  C     B ILE C 3 62  ? 56.330  -21.180 -23.263 0.50 34.92 ? 62  ILE F C     1 
ATOM   14190 O  O     A ILE C 3 62  ? 57.070  -20.312 -23.842 0.50 31.10 ? 62  ILE F O     1 
ATOM   14191 O  O     B ILE C 3 62  ? 57.277  -20.525 -23.717 0.50 29.92 ? 62  ILE F O     1 
ATOM   14192 C  CB    A ILE C 3 62  ? 53.849  -20.817 -24.477 0.50 30.17 ? 62  ILE F CB    1 
ATOM   14193 C  CB    B ILE C 3 62  ? 54.060  -21.013 -24.382 0.50 29.84 ? 62  ILE F CB    1 
ATOM   14194 C  CG1   A ILE C 3 62  ? 53.059  -21.341 -25.676 0.50 31.54 ? 62  ILE F CG1   1 
ATOM   14195 C  CG1   B ILE C 3 62  ? 53.262  -21.507 -25.589 0.50 31.23 ? 62  ILE F CG1   1 
ATOM   14196 C  CG2   A ILE C 3 62  ? 54.201  -19.352 -24.691 0.50 29.63 ? 62  ILE F CG2   1 
ATOM   14197 C  CG2   B ILE C 3 62  ? 54.411  -19.541 -24.553 0.50 29.80 ? 62  ILE F CG2   1 
ATOM   14198 C  CD1   A ILE C 3 62  ? 51.868  -20.480 -26.031 0.50 33.21 ? 62  ILE F CD1   1 
ATOM   14199 C  CD1   B ILE C 3 62  ? 52.033  -20.668 -25.886 0.50 33.27 ? 62  ILE F CD1   1 
ATOM   14200 N  N     A VAL C 3 63  ? 55.940  -21.054 -22.043 0.50 30.29 ? 63  VAL F N     1 
ATOM   14201 N  N     B VAL C 3 63  ? 56.143  -21.337 -21.949 0.50 31.69 ? 63  VAL F N     1 
ATOM   14202 C  CA    A VAL C 3 63  ? 56.921  -20.521 -21.099 0.50 26.52 ? 63  VAL F CA    1 
ATOM   14203 C  CA    B VAL C 3 63  ? 57.110  -20.817 -20.983 0.50 27.60 ? 63  VAL F CA    1 
ATOM   14204 C  C     A VAL C 3 63  ? 58.300  -21.107 -21.377 0.50 29.27 ? 63  VAL F C     1 
ATOM   14205 C  C     B VAL C 3 63  ? 58.502  -21.359 -21.282 0.50 28.69 ? 63  VAL F C     1 
ATOM   14206 O  O     A VAL C 3 63  ? 59.305  -20.388 -21.422 0.50 28.99 ? 63  VAL F O     1 
ATOM   14207 O  O     B VAL C 3 63  ? 59.485  -20.611 -21.340 0.50 28.48 ? 63  VAL F O     1 
ATOM   14208 C  CB    A VAL C 3 63  ? 56.481  -20.804 -19.650 0.50 27.62 ? 63  VAL F CB    1 
ATOM   14209 C  CB    B VAL C 3 63  ? 56.673  -21.160 -19.547 0.50 25.57 ? 63  VAL F CB    1 
ATOM   14210 C  CG1   A VAL C 3 63  ? 57.566  -20.380 -18.673 0.50 32.11 ? 63  VAL F CG1   1 
ATOM   14211 C  CG1   B VAL C 3 63  ? 57.842  -20.999 -18.586 0.50 32.34 ? 63  VAL F CG1   1 
ATOM   14212 C  CG2   A VAL C 3 63  ? 55.168  -20.099 -19.342 0.50 30.37 ? 63  VAL F CG2   1 
ATOM   14213 C  CG2   B VAL C 3 63  ? 55.514  -20.273 -19.120 0.50 30.45 ? 63  VAL F CG2   1 
ATOM   14214 N  N     A GLU C 3 64  ? 58.366  -22.425 -21.568 0.50 28.95 ? 64  GLU F N     1 
ATOM   14215 N  N     B GLU C 3 64  ? 58.605  -22.673 -21.479 0.50 29.51 ? 64  GLU F N     1 
ATOM   14216 C  CA    A GLU C 3 64  ? 59.652  -23.093 -21.734 0.50 29.77 ? 64  GLU F CA    1 
ATOM   14217 C  CA    B GLU C 3 64  ? 59.899  -23.265 -21.794 0.50 30.17 ? 64  GLU F CA    1 
ATOM   14218 C  C     A GLU C 3 64  ? 60.373  -22.604 -22.985 0.50 30.76 ? 64  GLU F C     1 
ATOM   14219 C  C     B GLU C 3 64  ? 60.403  -22.818 -23.162 0.50 30.68 ? 64  GLU F C     1 
ATOM   14220 O  O     A GLU C 3 64  ? 61.547  -22.220 -22.928 0.50 31.27 ? 64  GLU F O     1 
ATOM   14221 O  O     B GLU C 3 64  ? 61.617  -22.779 -23.387 0.50 37.73 ? 64  GLU F O     1 
ATOM   14222 C  CB    A GLU C 3 64  ? 59.444  -24.608 -21.777 0.50 30.13 ? 64  GLU F CB    1 
ATOM   14223 C  CB    B GLU C 3 64  ? 59.811  -24.790 -21.720 0.50 30.92 ? 64  GLU F CB    1 
ATOM   14224 C  CG    A GLU C 3 64  ? 58.944  -25.195 -20.456 0.50 31.77 ? 64  GLU F CG    1 
ATOM   14225 C  CG    B GLU C 3 64  ? 59.641  -25.324 -20.298 0.50 34.57 ? 64  GLU F CG    1 
ATOM   14226 C  CD    A GLU C 3 64  ? 58.494  -26.637 -20.582 0.50 37.64 ? 64  GLU F CD    1 
ATOM   14227 C  CD    B GLU C 3 64  ? 59.759  -26.834 -20.217 0.50 40.45 ? 64  GLU F CD    1 
ATOM   14228 O  OE1   A GLU C 3 64  ? 57.933  -26.994 -21.640 0.50 38.18 ? 64  GLU F OE1   1 
ATOM   14229 O  OE1   B GLU C 3 64  ? 59.179  -27.527 -21.080 0.50 44.98 ? 64  GLU F OE1   1 
ATOM   14230 O  OE2   A GLU C 3 64  ? 58.702  -27.414 -19.622 0.50 37.31 ? 64  GLU F OE2   1 
ATOM   14231 O  OE2   B GLU C 3 64  ? 60.436  -27.329 -19.291 0.50 33.53 ? 64  GLU F OE2   1 
ATOM   14232 N  N     A VAL C 3 65  ? 59.679  -22.601 -24.126 0.50 27.51 ? 65  VAL F N     1 
ATOM   14233 N  N     B VAL C 3 65  ? 59.495  -22.466 -24.074 0.50 27.67 ? 65  VAL F N     1 
ATOM   14234 C  CA    A VAL C 3 65  ? 60.305  -22.206 -25.385 0.50 34.30 ? 65  VAL F CA    1 
ATOM   14235 C  CA    B VAL C 3 65  ? 59.903  -22.018 -25.403 0.50 34.26 ? 65  VAL F CA    1 
ATOM   14236 C  C     A VAL C 3 65  ? 60.710  -20.737 -25.357 0.50 31.56 ? 65  VAL F C     1 
ATOM   14237 C  C     B VAL C 3 65  ? 60.506  -20.620 -25.334 0.50 31.44 ? 65  VAL F C     1 
ATOM   14238 O  O     A VAL C 3 65  ? 61.690  -20.342 -26.001 0.50 27.43 ? 65  VAL F O     1 
ATOM   14239 O  O     B VAL C 3 65  ? 61.595  -20.370 -25.865 0.50 27.52 ? 65  VAL F O     1 
ATOM   14240 C  CB    A VAL C 3 65  ? 59.359  -22.521 -26.564 0.50 29.86 ? 65  VAL F CB    1 
ATOM   14241 C  CB    B VAL C 3 65  ? 58.711  -22.071 -26.375 0.50 23.48 ? 65  VAL F CB    1 
ATOM   14242 C  CG1   A VAL C 3 65  ? 60.023  -22.202 -27.894 0.50 33.37 ? 65  VAL F CG1   1 
ATOM   14243 C  CG1   B VAL C 3 65  ? 58.952  -21.155 -27.556 0.50 30.51 ? 65  VAL F CG1   1 
ATOM   14244 C  CG2   A VAL C 3 65  ? 58.950  -23.983 -26.527 0.50 30.85 ? 65  VAL F CG2   1 
ATOM   14245 C  CG2   B VAL C 3 65  ? 58.489  -23.498 -26.847 0.50 33.85 ? 65  VAL F CG2   1 
ATOM   14246 N  N     A LEU C 3 66  ? 59.985  -19.907 -24.602 0.50 27.69 ? 66  LEU F N     1 
ATOM   14247 N  N     B LEU C 3 66  ? 59.809  -19.690 -24.676 0.50 27.39 ? 66  LEU F N     1 
ATOM   14248 C  CA    A LEU C 3 66  ? 60.353  -18.498 -24.501 0.50 27.54 ? 66  LEU F CA    1 
ATOM   14249 C  CA    B LEU C 3 66  ? 60.297  -18.318 -24.599 0.50 27.88 ? 66  LEU F CA    1 
ATOM   14250 C  C     A LEU C 3 66  ? 61.647  -18.314 -23.715 0.50 29.83 ? 66  LEU F C     1 
ATOM   14251 C  C     B LEU C 3 66  ? 61.610  -18.240 -23.829 0.50 29.76 ? 66  LEU F C     1 
ATOM   14252 O  O     A LEU C 3 66  ? 62.467  -17.449 -24.052 0.50 28.16 ? 66  LEU F O     1 
ATOM   14253 O  O     B LEU C 3 66  ? 62.509  -17.472 -24.194 0.50 28.33 ? 66  LEU F O     1 
ATOM   14254 C  CB    A LEU C 3 66  ? 59.216  -17.701 -23.858 0.50 27.41 ? 66  LEU F CB    1 
ATOM   14255 C  CB    B LEU C 3 66  ? 59.237  -17.422 -23.957 0.50 26.96 ? 66  LEU F CB    1 
ATOM   14256 C  CG    A LEU C 3 66  ? 58.014  -17.372 -24.745 0.50 31.58 ? 66  LEU F CG    1 
ATOM   14257 C  CG    B LEU C 3 66  ? 57.907  -17.334 -24.709 0.50 31.63 ? 66  LEU F CG    1 
ATOM   14258 C  CD1   A LEU C 3 66  ? 56.870  -16.804 -23.914 0.50 27.69 ? 66  LEU F CD1   1 
ATOM   14259 C  CD1   B LEU C 3 66  ? 56.820  -16.751 -23.820 0.50 27.67 ? 66  LEU F CD1   1 
ATOM   14260 C  CD2   A LEU C 3 66  ? 58.406  -16.398 -25.850 0.50 27.01 ? 66  LEU F CD2   1 
ATOM   14261 C  CD2   B LEU C 3 66  ? 58.051  -16.508 -25.984 0.50 26.12 ? 66  LEU F CD2   1 
ATOM   14262 N  N     A LEU C 3 67  ? 61.850  -19.111 -22.663 0.50 28.01 ? 67  LEU F N     1 
ATOM   14263 N  N     B LEU C 3 67  ? 61.747  -19.035 -22.765 0.50 27.99 ? 67  LEU F N     1 
ATOM   14264 C  CA    A LEU C 3 67  ? 63.061  -18.964 -21.861 0.50 26.08 ? 67  LEU F CA    1 
ATOM   14265 C  CA    B LEU C 3 67  ? 62.991  -19.031 -22.003 0.50 26.06 ? 67  LEU F CA    1 
ATOM   14266 C  C     A LEU C 3 67  ? 64.306  -19.312 -22.666 0.50 28.00 ? 67  LEU F C     1 
ATOM   14267 C  C     B LEU C 3 67  ? 64.160  -19.621 -22.777 0.50 27.90 ? 67  LEU F C     1 
ATOM   14268 O  O     A LEU C 3 67  ? 65.320  -18.612 -22.577 0.50 23.48 ? 67  LEU F O     1 
ATOM   14269 O  O     B LEU C 3 67  ? 65.300  -19.500 -22.319 0.50 22.83 ? 67  LEU F O     1 
ATOM   14270 C  CB    A LEU C 3 67  ? 62.974  -19.830 -20.607 0.50 27.17 ? 67  LEU F CB    1 
ATOM   14271 C  CB    B LEU C 3 67  ? 62.811  -19.783 -20.687 0.50 27.70 ? 67  LEU F CB    1 
ATOM   14272 C  CG    A LEU C 3 67  ? 62.038  -19.272 -19.533 0.50 27.34 ? 67  LEU F CG    1 
ATOM   14273 C  CG    B LEU C 3 67  ? 61.904  -19.072 -19.681 0.50 26.62 ? 67  LEU F CG    1 
ATOM   14274 C  CD1   A LEU C 3 67  ? 61.687  -20.343 -18.511 0.50 30.22 ? 67  LEU F CD1   1 
ATOM   14275 C  CD1   B LEU C 3 67  ? 61.656  -19.947 -18.460 0.50 30.34 ? 67  LEU F CD1   1 
ATOM   14276 C  CD2   A LEU C 3 67  ? 62.665  -18.064 -18.850 0.50 29.70 ? 67  LEU F CD2   1 
ATOM   14277 C  CD2   B LEU C 3 67  ? 62.500  -17.736 -19.266 0.50 29.35 ? 67  LEU F CD2   1 
ATOM   14278 N  N     A LYS C 3 68  ? 64.248  -20.380 -23.461 0.50 24.67 ? 68  LYS F N     1 
ATOM   14279 N  N     B LYS C 3 68  ? 63.908  -20.261 -23.916 0.50 27.75 ? 68  LYS F N     1 
ATOM   14280 C  CA    A LYS C 3 68  ? 65.374  -20.770 -24.305 0.50 27.84 ? 68  LYS F CA    1 
ATOM   14281 C  CA    B LYS C 3 68  ? 64.961  -20.714 -24.816 0.50 28.38 ? 68  LYS F CA    1 
ATOM   14282 C  C     A LYS C 3 68  ? 65.621  -19.804 -25.459 0.50 27.01 ? 68  LYS F C     1 
ATOM   14283 C  C     B LYS C 3 68  ? 65.206  -19.751 -25.969 0.50 28.18 ? 68  LYS F C     1 
ATOM   14284 O  O     A LYS C 3 68  ? 66.550  -20.038 -26.244 0.50 26.96 ? 68  LYS F O     1 
ATOM   14285 O  O     B LYS C 3 68  ? 66.124  -19.978 -26.767 0.50 26.25 ? 68  LYS F O     1 
ATOM   14286 C  CB    A LYS C 3 68  ? 65.144  -22.179 -24.857 0.50 30.16 ? 68  LYS F CB    1 
ATOM   14287 C  CB    B LYS C 3 68  ? 64.626  -22.101 -25.371 0.50 27.27 ? 68  LYS F CB    1 
ATOM   14288 C  CG    A LYS C 3 68  ? 65.006  -23.257 -23.792 0.50 29.33 ? 68  LYS F CG    1 
ATOM   14289 C  CG    B LYS C 3 68  ? 65.140  -23.249 -24.519 0.50 28.03 ? 68  LYS F CG    1 
ATOM   14290 C  CD    A LYS C 3 68  ? 64.208  -24.445 -24.311 0.50 35.32 ? 68  LYS F CD    1 
ATOM   14291 C  CD    B LYS C 3 68  ? 64.759  -24.586 -25.129 0.50 41.50 ? 68  LYS F CD    1 
ATOM   14292 C  CE    A LYS C 3 68  ? 64.092  -25.547 -23.266 0.50 39.56 ? 68  LYS F CE    1 
ATOM   14293 C  CE    B LYS C 3 68  ? 65.414  -25.738 -24.387 0.50 37.15 ? 68  LYS F CE    1 
ATOM   14294 N  NZ    A LYS C 3 68  ? 63.245  -26.681 -23.742 0.50 33.64 ? 68  LYS F NZ    1 
ATOM   14295 N  NZ    B LYS C 3 68  ? 64.775  -27.036 -24.722 0.50 32.96 ? 68  LYS F NZ    1 
ATOM   14296 N  N     A HIS C 3 69  ? 64.829  -18.740 -25.588 0.50 27.84 ? 69  HIS F N     1 
ATOM   14297 N  N     B HIS C 3 69  ? 64.410  -18.694 -26.082 0.50 27.58 ? 69  HIS F N     1 
ATOM   14298 C  CA    A HIS C 3 69  ? 64.966  -17.761 -26.663 0.50 27.76 ? 69  HIS F CA    1 
ATOM   14299 C  CA    B HIS C 3 69  ? 64.564  -17.699 -27.133 0.50 26.79 ? 69  HIS F CA    1 
ATOM   14300 C  C     A HIS C 3 69  ? 64.992  -16.340 -26.110 0.50 24.16 ? 69  HIS F C     1 
ATOM   14301 C  C     B HIS C 3 69  ? 64.655  -16.301 -26.546 0.50 22.76 ? 69  HIS F C     1 
ATOM   14302 O  O     A HIS C 3 69  ? 64.329  -15.436 -26.619 0.50 22.99 ? 69  HIS F O     1 
ATOM   14303 O  O     B HIS C 3 69  ? 64.043  -15.358 -27.050 0.50 23.86 ? 69  HIS F O     1 
ATOM   14304 C  CB    A HIS C 3 69  ? 63.850  -17.909 -27.692 0.50 27.57 ? 69  HIS F CB    1 
ATOM   14305 C  CB    B HIS C 3 69  ? 63.425  -17.785 -28.143 0.50 29.43 ? 69  HIS F CB    1 
ATOM   14306 C  CG    A HIS C 3 69  ? 64.080  -19.014 -28.673 0.50 33.17 ? 69  HIS F CG    1 
ATOM   14307 C  CG    B HIS C 3 69  ? 63.373  -19.085 -28.880 0.50 30.44 ? 69  HIS F CG    1 
ATOM   14308 N  ND1   A HIS C 3 69  ? 63.725  -20.320 -28.418 0.50 28.43 ? 69  HIS F ND1   1 
ATOM   14309 N  ND1   B HIS C 3 69  ? 62.817  -20.223 -28.339 0.50 31.12 ? 69  HIS F ND1   1 
ATOM   14310 C  CD2   A HIS C 3 69  ? 64.638  -19.009 -29.907 0.50 30.96 ? 69  HIS F CD2   1 
ATOM   14311 C  CD2   B HIS C 3 69  ? 63.821  -19.433 -30.110 0.50 32.32 ? 69  HIS F CD2   1 
ATOM   14312 C  CE1   A HIS C 3 69  ? 64.053  -21.072 -29.453 0.50 29.46 ? 69  HIS F CE1   1 
ATOM   14313 C  CE1   B HIS C 3 69  ? 62.917  -21.214 -29.205 0.50 27.53 ? 69  HIS F CE1   1 
ATOM   14314 N  NE2   A HIS C 3 69  ? 64.606  -20.301 -30.371 0.50 30.66 ? 69  HIS F NE2   1 
ATOM   14315 N  NE2   B HIS C 3 69  ? 63.522  -20.761 -30.288 0.50 33.86 ? 69  HIS F NE2   1 
ATOM   14316 N  N     A GLY C 3 70  ? 65.774  -16.125 -25.053 0.50 21.89 ? 70  GLY F N     1 
ATOM   14317 N  N     B GLY C 3 70  ? 65.415  -16.148 -25.464 0.50 23.19 ? 70  GLY F N     1 
ATOM   14318 C  CA    A GLY C 3 70  ? 66.162  -14.789 -24.644 0.50 22.81 ? 70  GLY F CA    1 
ATOM   14319 C  CA    B GLY C 3 70  ? 65.796  -14.834 -24.982 0.50 22.29 ? 70  GLY F CA    1 
ATOM   14320 C  C     A GLY C 3 70  ? 65.168  -14.008 -23.806 0.50 22.36 ? 70  GLY F C     1 
ATOM   14321 C  C     B GLY C 3 70  ? 64.837  -14.158 -24.029 0.50 22.64 ? 70  GLY F C     1 
ATOM   14322 O  O     A GLY C 3 70  ? 65.472  -12.867 -23.435 0.50 22.68 ? 70  GLY F O     1 
ATOM   14323 O  O     B GLY C 3 70  ? 64.953  -12.945 -23.819 0.50 23.75 ? 70  GLY F O     1 
ATOM   14324 N  N     A ALA C 3 71  ? 63.999  -14.564 -23.497 0.50 24.28 ? 71  ALA F N     1 
ATOM   14325 N  N     B ALA C 3 71  ? 63.894  -14.886 -23.442 0.50 23.87 ? 71  ALA F N     1 
ATOM   14326 C  CA    A ALA C 3 71  ? 63.022  -13.830 -22.696 0.50 24.31 ? 71  ALA F CA    1 
ATOM   14327 C  CA    B ALA C 3 71  ? 62.995  -14.267 -22.475 0.50 23.84 ? 71  ALA F CA    1 
ATOM   14328 C  C     A ALA C 3 71  ? 63.606  -13.439 -21.340 0.50 20.81 ? 71  ALA F C     1 
ATOM   14329 C  C     B ALA C 3 71  ? 63.755  -13.893 -21.207 0.50 22.41 ? 71  ALA F C     1 
ATOM   14330 O  O     A ALA C 3 71  ? 64.400  -14.177 -20.750 0.50 23.74 ? 71  ALA F O     1 
ATOM   14331 O  O     B ALA C 3 71  ? 64.502  -14.707 -20.652 0.50 23.67 ? 71  ALA F O     1 
ATOM   14332 C  CB    A ALA C 3 71  ? 61.756  -14.667 -22.506 0.50 23.29 ? 71  ALA F CB    1 
ATOM   14333 C  CB    B ALA C 3 71  ? 61.836  -15.202 -22.140 0.50 24.95 ? 71  ALA F CB    1 
ATOM   14334 N  N     A ASP C 3 72  ? 63.212  -12.265 -20.847 0.50 24.08 ? 72  ASP F N     1 
ATOM   14335 N  N     B ASP C 3 72  ? 63.578  -12.653 -20.758 0.50 23.79 ? 72  ASP F N     1 
ATOM   14336 C  CA    A ASP C 3 72  ? 63.699  -11.755 -19.564 0.50 25.72 ? 72  ASP F CA    1 
ATOM   14337 C  CA    B ASP C 3 72  ? 64.054  -12.258 -19.439 0.50 24.42 ? 72  ASP F CA    1 
ATOM   14338 C  C     A ASP C 3 72  ? 62.819  -12.328 -18.458 0.50 24.54 ? 72  ASP F C     1 
ATOM   14339 C  C     B ASP C 3 72  ? 63.158  -12.908 -18.390 0.50 26.81 ? 72  ASP F C     1 
ATOM   14340 O  O     A ASP C 3 72  ? 61.692  -11.873 -18.247 0.50 24.18 ? 72  ASP F O     1 
ATOM   14341 O  O     B ASP C 3 72  ? 61.953  -12.645 -18.347 0.50 24.95 ? 72  ASP F O     1 
ATOM   14342 C  CB    A ASP C 3 72  ? 63.696  -10.230 -19.548 0.50 22.17 ? 72  ASP F CB    1 
ATOM   14343 C  CB    B ASP C 3 72  ? 64.043  -10.737 -19.300 0.50 24.90 ? 72  ASP F CB    1 
ATOM   14344 C  CG    A ASP C 3 72  ? 64.375  -9.653  -18.315 0.50 26.57 ? 72  ASP F CG    1 
ATOM   14345 C  CG    B ASP C 3 72  ? 64.769  -10.250 -18.056 0.50 26.98 ? 72  ASP F CG    1 
ATOM   14346 O  OD1   A ASP C 3 72  ? 64.625  -10.402 -17.345 0.50 24.93 ? 72  ASP F OD1   1 
ATOM   14347 O  OD1   B ASP C 3 72  ? 64.882  -11.017 -17.074 0.50 23.61 ? 72  ASP F OD1   1 
ATOM   14348 O  OD2   A ASP C 3 72  ? 64.672  -8.438  -18.315 0.50 29.65 ? 72  ASP F OD2   1 
ATOM   14349 O  OD2   B ASP C 3 72  ? 65.235  -9.088  -18.065 0.50 26.31 ? 72  ASP F OD2   1 
ATOM   14350 N  N     A VAL C 3 73  ? 63.352  -13.320 -17.739 0.50 25.84 ? 73  VAL F N     1 
ATOM   14351 N  N     B VAL C 3 73  ? 63.742  -13.775 -17.559 0.50 25.47 ? 73  VAL F N     1 
ATOM   14352 C  CA    A VAL C 3 73  ? 62.594  -14.034 -16.715 0.50 25.69 ? 73  VAL F CA    1 
ATOM   14353 C  CA    B VAL C 3 73  ? 62.954  -14.504 -16.570 0.50 25.77 ? 73  VAL F CA    1 
ATOM   14354 C  C     A VAL C 3 73  ? 62.273  -13.146 -15.517 0.50 26.89 ? 73  VAL F C     1 
ATOM   14355 C  C     B VAL C 3 73  ? 62.512  -13.603 -15.425 0.50 27.05 ? 73  VAL F C     1 
ATOM   14356 O  O     A VAL C 3 73  ? 61.367  -13.465 -14.735 0.50 23.41 ? 73  VAL F O     1 
ATOM   14357 O  O     B VAL C 3 73  ? 61.608  -13.970 -14.664 0.50 23.57 ? 73  VAL F O     1 
ATOM   14358 C  CB    A VAL C 3 73  ? 63.381  -15.292 -16.295 0.50 24.08 ? 73  VAL F CB    1 
ATOM   14359 C  CB    B VAL C 3 73  ? 63.757  -15.708 -16.043 0.50 25.34 ? 73  VAL F CB    1 
ATOM   14360 C  CG1   A VAL C 3 73  ? 64.703  -14.900 -15.649 0.50 23.56 ? 73  VAL F CG1   1 
ATOM   14361 C  CG1   B VAL C 3 73  ? 64.843  -15.244 -15.091 0.50 27.32 ? 73  VAL F CG1   1 
ATOM   14362 C  CG2   A VAL C 3 73  ? 62.559  -16.188 -15.378 0.50 29.80 ? 73  VAL F CG2   1 
ATOM   14363 C  CG2   B VAL C 3 73  ? 62.843  -16.731 -15.386 0.50 28.28 ? 73  VAL F CG2   1 
ATOM   14364 N  N     A ASN C 3 74  ? 62.978  -12.027 -15.353 0.50 23.38 ? 74  ASN F N     1 
ATOM   14365 N  N     B ASN C 3 74  ? 63.121  -12.426 -15.284 0.50 22.14 ? 74  ASN F N     1 
ATOM   14366 C  CA    A ASN C 3 74  ? 62.708  -11.098 -14.263 0.50 28.37 ? 74  ASN F CA    1 
ATOM   14367 C  CA    B ASN C 3 74  ? 62.827  -11.527 -14.175 0.50 28.74 ? 74  ASN F CA    1 
ATOM   14368 C  C     A ASN C 3 74  ? 62.111  -9.786  -14.754 0.50 28.29 ? 74  ASN F C     1 
ATOM   14369 C  C     B ASN C 3 74  ? 62.273  -10.186 -14.639 0.50 27.11 ? 74  ASN F C     1 
ATOM   14370 O  O     A ASN C 3 74  ? 62.206  -8.768  -14.060 0.50 27.12 ? 74  ASN F O     1 
ATOM   14371 O  O     B ASN C 3 74  ? 62.411  -9.188  -13.924 0.50 24.15 ? 74  ASN F O     1 
ATOM   14372 C  CB    A ASN C 3 74  ? 63.978  -10.838 -13.456 0.50 26.61 ? 74  ASN F CB    1 
ATOM   14373 C  CB    B ASN C 3 74  ? 64.078  -11.312 -13.323 0.50 26.50 ? 74  ASN F CB    1 
ATOM   14374 C  CG    A ASN C 3 74  ? 64.359  -12.015 -12.587 0.50 27.22 ? 74  ASN F CG    1 
ATOM   14375 C  CG    B ASN C 3 74  ? 64.431  -12.525 -12.498 0.50 27.89 ? 74  ASN F CG    1 
ATOM   14376 O  OD1   A ASN C 3 74  ? 63.491  -12.695 -12.038 0.50 26.38 ? 74  ASN F OD1   1 
ATOM   14377 O  OD1   B ASN C 3 74  ? 63.559  -13.141 -11.884 0.50 28.32 ? 74  ASN F OD1   1 
ATOM   14378 N  ND2   A ASN C 3 74  ? 65.661  -12.267 -12.459 0.50 23.44 ? 74  ASN F ND2   1 
ATOM   14379 N  ND2   B ASN C 3 74  ? 65.712  -12.880 -12.475 0.50 24.60 ? 74  ASN F ND2   1 
ATOM   14380 N  N     A ALA C 3 75  ? 61.500  -9.794  -15.935 0.50 23.14 ? 75  ALA F N     1 
ATOM   14381 N  N     B ALA C 3 75  ? 61.649  -10.141 -15.815 0.50 22.51 ? 75  ALA F N     1 
ATOM   14382 C  CA    A ALA C 3 75  ? 60.818  -8.609  -16.435 0.50 28.75 ? 75  ALA F CA    1 
ATOM   14383 C  CA    B ALA C 3 75  ? 61.042  -8.908  -16.300 0.50 27.46 ? 75  ALA F CA    1 
ATOM   14384 C  C     A ALA C 3 75  ? 59.621  -8.278  -15.556 0.50 23.80 ? 75  ALA F C     1 
ATOM   14385 C  C     B ALA C 3 75  ? 59.946  -8.443  -15.344 0.50 23.80 ? 75  ALA F C     1 
ATOM   14386 O  O     A ALA C 3 75  ? 58.812  -9.154  -15.235 0.50 18.94 ? 75  ALA F O     1 
ATOM   14387 O  O     B ALA C 3 75  ? 59.398  -9.222  -14.562 0.50 17.26 ? 75  ALA F O     1 
ATOM   14388 C  CB    A ALA C 3 75  ? 60.369  -8.829  -17.880 0.50 23.58 ? 75  ALA F CB    1 
ATOM   14389 C  CB    B ALA C 3 75  ? 60.467  -9.108  -17.703 0.50 23.43 ? 75  ALA F CB    1 
ATOM   14390 N  N     A ILE C 3 76  ? 59.512  -7.012  -15.161 0.50 25.85 ? 76  ILE F N     1 
ATOM   14391 N  N     B ILE C 3 76  ? 59.632  -7.149  -15.406 0.50 24.88 ? 76  ILE F N     1 
ATOM   14392 C  CA    A ILE C 3 76  ? 58.399  -6.535  -14.347 0.50 23.33 ? 76  ILE F CA    1 
ATOM   14393 C  CA    B ILE C 3 76  ? 58.641  -6.545  -14.523 0.50 23.71 ? 76  ILE F CA    1 
ATOM   14394 C  C     A ILE C 3 76  ? 57.490  -5.674  -15.215 0.50 27.37 ? 76  ILE F C     1 
ATOM   14395 C  C     B ILE C 3 76  ? 57.712  -5.654  -15.335 0.50 27.23 ? 76  ILE F C     1 
ATOM   14396 O  O     A ILE C 3 76  ? 57.962  -4.962  -16.110 0.50 29.39 ? 76  ILE F O     1 
ATOM   14397 O  O     B ILE C 3 76  ? 58.141  -5.009  -16.299 0.50 28.97 ? 76  ILE F O     1 
ATOM   14398 C  CB    A ILE C 3 76  ? 58.881  -5.752  -13.105 0.50 26.76 ? 76  ILE F CB    1 
ATOM   14399 C  CB    B ILE C 3 76  ? 59.299  -5.731  -13.389 0.50 27.64 ? 76  ILE F CB    1 
ATOM   14400 C  CG1   A ILE C 3 76  ? 59.511  -4.415  -13.509 0.50 24.74 ? 76  ILE F CG1   1 
ATOM   14401 C  CG1   B ILE C 3 76  ? 60.253  -4.681  -13.963 0.50 28.66 ? 76  ILE F CG1   1 
ATOM   14402 C  CG2   A ILE C 3 76  ? 59.871  -6.576  -12.306 0.50 27.95 ? 76  ILE F CG2   1 
ATOM   14403 C  CG2   B ILE C 3 76  ? 60.024  -6.648  -12.420 0.50 27.94 ? 76  ILE F CG2   1 
ATOM   14404 C  CD1   A ILE C 3 76  ? 59.734  -3.468  -12.357 0.50 26.29 ? 76  ILE F CD1   1 
ATOM   14405 C  CD1   B ILE C 3 76  ? 60.752  -3.693  -12.927 0.50 26.37 ? 76  ILE F CD1   1 
ATOM   14406 N  N     A ASP C 3 77  ? 56.183  -5.754  -14.959 0.50 21.51 ? 77  ASP F N     1 
ATOM   14407 N  N     B ASP C 3 77  ? 56.437  -5.618  -14.942 0.50 22.34 ? 77  ASP F N     1 
ATOM   14408 C  CA    A ASP C 3 77  ? 55.222  -4.910  -15.657 0.50 29.06 ? 77  ASP F CA    1 
ATOM   14409 C  CA    B ASP C 3 77  ? 55.481  -4.681  -15.509 0.50 27.89 ? 77  ASP F CA    1 
ATOM   14410 C  C     A ASP C 3 77  ? 55.152  -3.552  -14.951 0.50 26.14 ? 77  ASP F C     1 
ATOM   14411 C  C     B ASP C 3 77  ? 55.532  -3.373  -14.716 0.50 27.26 ? 77  ASP F C     1 
ATOM   14412 O  O     A ASP C 3 77  ? 56.003  -3.215  -14.123 0.50 25.62 ? 77  ASP F O     1 
ATOM   14413 O  O     B ASP C 3 77  ? 56.399  -3.175  -13.861 0.50 25.07 ? 77  ASP F O     1 
ATOM   14414 C  CB    A ASP C 3 77  ? 53.866  -5.618  -15.772 0.50 24.42 ? 77  ASP F CB    1 
ATOM   14415 C  CB    B ASP C 3 77  ? 54.081  -5.300  -15.547 0.50 27.18 ? 77  ASP F CB    1 
ATOM   14416 C  CG    A ASP C 3 77  ? 53.088  -5.665  -14.461 0.50 25.39 ? 77  ASP F CG    1 
ATOM   14417 C  CG    B ASP C 3 77  ? 53.561  -5.685  -14.168 0.50 26.58 ? 77  ASP F CG    1 
ATOM   14418 O  OD1   A ASP C 3 77  ? 53.641  -5.321  -13.396 0.50 25.40 ? 77  ASP F OD1   1 
ATOM   14419 O  OD1   B ASP C 3 77  ? 54.173  -5.295  -13.152 0.50 26.98 ? 77  ASP F OD1   1 
ATOM   14420 O  OD2   A ASP C 3 77  ? 51.903  -6.064  -14.507 0.50 20.83 ? 77  ASP F OD2   1 
ATOM   14421 O  OD2   B ASP C 3 77  ? 52.535  -6.393  -14.108 0.50 25.04 ? 77  ASP F OD2   1 
ATOM   14422 N  N     A ILE C 3 78  ? 54.138  -2.743  -15.270 0.50 24.04 ? 78  ILE F N     1 
ATOM   14423 N  N     B ILE C 3 78  ? 54.591  -2.463  -14.980 0.50 26.02 ? 78  ILE F N     1 
ATOM   14424 C  CA    A ILE C 3 78  ? 54.055  -1.412  -14.674 0.50 32.49 ? 78  ILE F CA    1 
ATOM   14425 C  CA    B ILE C 3 78  ? 54.628  -1.168  -14.311 0.50 32.54 ? 78  ILE F CA    1 
ATOM   14426 C  C     A ILE C 3 78  ? 53.665  -1.450  -13.206 0.50 30.04 ? 78  ILE F C     1 
ATOM   14427 C  C     B ILE C 3 78  ? 54.348  -1.292  -12.817 0.50 30.72 ? 78  ILE F C     1 
ATOM   14428 O  O     A ILE C 3 78  ? 53.706  -0.411  -12.538 0.50 39.05 ? 78  ILE F O     1 
ATOM   14429 O  O     B ILE C 3 78  ? 54.705  -0.392  -12.048 0.50 33.21 ? 78  ILE F O     1 
ATOM   14430 C  CB    A ILE C 3 78  ? 53.064  -0.505  -15.433 0.50 31.52 ? 78  ILE F CB    1 
ATOM   14431 C  CB    B ILE C 3 78  ? 53.639  -0.189  -14.971 0.50 34.44 ? 78  ILE F CB    1 
ATOM   14432 C  CG1   A ILE C 3 78  ? 51.640  -1.049  -15.318 0.50 38.18 ? 78  ILE F CG1   1 
ATOM   14433 C  CG1   B ILE C 3 78  ? 52.210  -0.724  -14.877 0.50 34.38 ? 78  ILE F CG1   1 
ATOM   14434 C  CG2   A ILE C 3 78  ? 53.488  -0.358  -16.887 0.50 40.02 ? 78  ILE F CG2   1 
ATOM   14435 C  CG2   B ILE C 3 78  ? 54.031  0.059   -16.418 0.50 37.92 ? 78  ILE F CG2   1 
ATOM   14436 C  CD1   A ILE C 3 78  ? 50.570  -0.035  -15.680 0.50 34.79 ? 78  ILE F CD1   1 
ATOM   14437 C  CD1   B ILE C 3 78  ? 51.154  0.264   -15.333 0.50 38.79 ? 78  ILE F CD1   1 
ATOM   14438 N  N     A MET C 3 79  ? 53.291  -2.617  -12.688 0.50 28.74 ? 79  MET F N     1 
ATOM   14439 N  N     B MET C 3 79  ? 53.731  -2.388  -12.382 0.50 27.42 ? 79  MET F N     1 
ATOM   14440 C  CA    A MET C 3 79  ? 52.975  -2.790  -11.275 0.50 30.90 ? 79  MET F CA    1 
ATOM   14441 C  CA    B MET C 3 79  ? 53.458  -2.628  -10.969 0.50 30.18 ? 79  MET F CA    1 
ATOM   14442 C  C     A MET C 3 79  ? 54.041  -3.590  -10.537 0.50 29.60 ? 79  MET F C     1 
ATOM   14443 C  C     B MET C 3 79  ? 54.565  -3.421  -10.283 0.50 30.66 ? 79  MET F C     1 
ATOM   14444 O  O     A MET C 3 79  ? 53.851  -3.930  -9.365  0.50 28.74 ? 79  MET F O     1 
ATOM   14445 O  O     B MET C 3 79  ? 54.403  -3.818  -9.124  0.50 26.12 ? 79  MET F O     1 
ATOM   14446 C  CB    A MET C 3 79  ? 51.610  -3.462  -11.118 0.50 30.91 ? 79  MET F CB    1 
ATOM   14447 C  CB    B MET C 3 79  ? 52.123  -3.360  -10.809 0.50 32.21 ? 79  MET F CB    1 
ATOM   14448 C  CG    A MET C 3 79  ? 50.476  -2.706  -11.789 0.50 37.62 ? 79  MET F CG    1 
ATOM   14449 C  CG    B MET C 3 79  ? 50.969  -2.701  -11.540 0.50 36.21 ? 79  MET F CG    1 
ATOM   14450 S  SD    A MET C 3 79  ? 50.382  -0.991  -11.241 0.50 46.25 ? 79  MET F SD    1 
ATOM   14451 S  SD    B MET C 3 79  ? 50.814  -0.945  -11.161 0.50 45.75 ? 79  MET F SD    1 
ATOM   14452 C  CE    A MET C 3 79  ? 49.102  -0.352  -12.320 0.50 45.09 ? 79  MET F CE    1 
ATOM   14453 C  CE    B MET C 3 79  ? 50.102  -1.001  -9.518  0.50 41.91 ? 79  MET F CE    1 
ATOM   14454 N  N     A GLY C 3 80  ? 55.157  -3.903  -11.194 0.50 29.30 ? 80  GLY F N     1 
ATOM   14455 N  N     B GLY C 3 80  ? 55.681  -3.661  -10.968 0.50 24.53 ? 80  GLY F N     1 
ATOM   14456 C  CA    A GLY C 3 80  ? 56.232  -4.618  -10.538 0.50 26.06 ? 80  GLY F CA    1 
ATOM   14457 C  CA    B GLY C 3 80  ? 56.740  -4.468  -10.403 0.50 27.54 ? 80  GLY F CA    1 
ATOM   14458 C  C     A GLY C 3 80  ? 56.057  -6.115  -10.456 0.50 23.45 ? 80  GLY F C     1 
ATOM   14459 C  C     B GLY C 3 80  ? 56.468  -5.954  -10.371 0.50 24.66 ? 80  GLY F C     1 
ATOM   14460 O  O     A GLY C 3 80  ? 56.782  -6.769  -9.702  0.50 27.65 ? 80  GLY F O     1 
ATOM   14461 O  O     B GLY C 3 80  ? 57.212  -6.688  -9.713  0.50 29.80 ? 80  GLY F O     1 
ATOM   14462 N  N     A SER C 3 81  ? 55.128  -6.685  -11.215 0.50 24.89 ? 81  SER F N     1 
ATOM   14463 N  N     B SER C 3 81  ? 55.435  -6.426  -11.063 0.50 24.08 ? 81  SER F N     1 
ATOM   14464 C  CA    A SER C 3 81  ? 54.861  -8.116  -11.162 0.50 23.57 ? 81  SER F CA    1 
ATOM   14465 C  CA    B SER C 3 81  ? 55.125  -7.849  -11.089 0.50 22.69 ? 81  SER F CA    1 
ATOM   14466 C  C     A SER C 3 81  ? 55.805  -8.850  -12.105 0.50 24.27 ? 81  SER F C     1 
ATOM   14467 C  C     B SER C 3 81  ? 56.053  -8.576  -12.051 0.50 24.94 ? 81  SER F C     1 
ATOM   14468 O  O     A SER C 3 81  ? 55.814  -8.580  -13.309 0.50 22.14 ? 81  SER F O     1 
ATOM   14469 O  O     B SER C 3 81  ? 56.252  -8.135  -13.185 0.50 21.93 ? 81  SER F O     1 
ATOM   14470 C  CB    A SER C 3 81  ? 53.411  -8.412  -11.538 0.50 25.66 ? 81  SER F CB    1 
ATOM   14471 C  CB    B SER C 3 81  ? 53.672  -8.076  -11.507 0.50 25.21 ? 81  SER F CB    1 
ATOM   14472 O  OG    A SER C 3 81  ? 52.501  -7.739  -10.689 0.50 27.62 ? 81  SER F OG    1 
ATOM   14473 O  OG    B SER C 3 81  ? 52.764  -7.500  -10.588 0.50 28.84 ? 81  SER F OG    1 
ATOM   14474 N  N     A THR C 3 82  ? 56.592  -9.766  -11.557 0.50 25.24 ? 82  THR F N     1 
ATOM   14475 N  N     B THR C 3 82  ? 56.609  -9.687  -11.597 0.50 25.19 ? 82  THR F N     1 
ATOM   14476 C  CA    A THR C 3 82  ? 57.395  -10.672 -12.357 0.50 26.42 ? 82  THR F CA    1 
ATOM   14477 C  CA    B THR C 3 82  ? 57.395  -10.598 -12.410 0.50 26.46 ? 82  THR F CA    1 
ATOM   14478 C  C     A THR C 3 82  ? 56.543  -11.857 -12.805 0.50 24.09 ? 82  THR F C     1 
ATOM   14479 C  C     B THR C 3 82  ? 56.536  -11.770 -12.859 0.50 24.10 ? 82  THR F C     1 
ATOM   14480 O  O     A THR C 3 82  ? 55.457  -12.089 -12.267 0.50 25.78 ? 82  THR F O     1 
ATOM   14481 O  O     B THR C 3 82  ? 55.433  -11.978 -12.344 0.50 25.76 ? 82  THR F O     1 
ATOM   14482 C  CB    A THR C 3 82  ? 58.599  -11.161 -11.555 0.50 26.27 ? 82  THR F CB    1 
ATOM   14483 C  CB    B THR C 3 82  ? 58.604  -11.119 -11.621 0.50 26.23 ? 82  THR F CB    1 
ATOM   14484 O  OG1   A THR C 3 82  ? 58.156  -11.774 -10.337 0.50 24.09 ? 82  THR F OG1   1 
ATOM   14485 O  OG1   B THR C 3 82  ? 58.156  -11.851 -10.472 0.50 24.14 ? 82  THR F OG1   1 
ATOM   14486 C  CG2   A THR C 3 82  ? 59.542  -10.008 -11.230 0.50 27.28 ? 82  THR F CG2   1 
ATOM   14487 C  CG2   B THR C 3 82  ? 59.499  -9.972  -11.172 0.50 27.31 ? 82  THR F CG2   1 
ATOM   14488 N  N     A PRO C 3 83  ? 57.001  -12.615 -13.809 0.50 23.63 ? 83  PRO F N     1 
ATOM   14489 N  N     B PRO C 3 83  ? 56.993  -12.550 -13.844 0.50 23.64 ? 83  PRO F N     1 
ATOM   14490 C  CA    A PRO C 3 83  ? 56.274  -13.842 -14.169 0.50 23.59 ? 83  PRO F CA    1 
ATOM   14491 C  CA    B PRO C 3 83  ? 56.288  -13.803 -14.147 0.50 23.56 ? 83  PRO F CA    1 
ATOM   14492 C  C     A PRO C 3 83  ? 56.127  -14.811 -13.009 0.50 21.00 ? 83  PRO F C     1 
ATOM   14493 C  C     B PRO C 3 83  ? 56.238  -14.756 -12.966 0.50 20.98 ? 83  PRO F C     1 
ATOM   14494 O  O     A PRO C 3 83  ? 55.121  -15.529 -12.939 0.50 24.80 ? 83  PRO F O     1 
ATOM   14495 O  O     B PRO C 3 83  ? 55.291  -15.547 -12.865 0.50 25.03 ? 83  PRO F O     1 
ATOM   14496 C  CB    A PRO C 3 83  ? 57.128  -14.439 -15.298 0.50 25.20 ? 83  PRO F CB    1 
ATOM   14497 C  CB    B PRO C 3 83  ? 57.094  -14.387 -15.317 0.50 25.24 ? 83  PRO F CB    1 
ATOM   14498 C  CG    A PRO C 3 83  ? 57.832  -13.265 -15.895 0.50 25.51 ? 83  PRO F CG    1 
ATOM   14499 C  CG    B PRO C 3 83  ? 57.722  -13.194 -15.966 0.50 25.40 ? 83  PRO F CG    1 
ATOM   14500 C  CD    A PRO C 3 83  ? 58.110  -12.337 -14.742 0.50 24.96 ? 83  PRO F CD    1 
ATOM   14501 C  CD    B PRO C 3 83  ? 58.053  -12.263 -14.830 0.50 24.99 ? 83  PRO F CD    1 
ATOM   14502 N  N     A LEU C 3 84  ? 57.095  -14.844 -12.088 0.50 25.78 ? 84  LEU F N     1 
ATOM   14503 N  N     B LEU C 3 84  ? 57.220  -14.700 -12.058 0.50 25.56 ? 84  LEU F N     1 
ATOM   14504 C  CA    A LEU C 3 84  ? 56.976  -15.718 -10.924 0.50 24.75 ? 84  LEU F CA    1 
ATOM   14505 C  CA    B LEU C 3 84  ? 57.150  -15.538 -10.864 0.50 24.40 ? 84  LEU F CA    1 
ATOM   14506 C  C     A LEU C 3 84  ? 55.827  -15.287 -10.017 0.50 23.46 ? 84  LEU F C     1 
ATOM   14507 C  C     B LEU C 3 84  ? 56.056  -15.058 -9.916  0.50 23.73 ? 84  LEU F C     1 
ATOM   14508 O  O     A LEU C 3 84  ? 55.096  -16.135 -9.494  0.50 23.26 ? 84  LEU F O     1 
ATOM   14509 O  O     B LEU C 3 84  ? 55.371  -15.877 -9.295  0.50 21.59 ? 84  LEU F O     1 
ATOM   14510 C  CB    A LEU C 3 84  ? 58.290  -15.746 -10.145 0.50 26.19 ? 84  LEU F CB    1 
ATOM   14511 C  CB    B LEU C 3 84  ? 58.497  -15.577 -10.145 0.50 26.48 ? 84  LEU F CB    1 
ATOM   14512 C  CG    A LEU C 3 84  ? 58.271  -16.605 -8.879  0.50 23.00 ? 84  LEU F CG    1 
ATOM   14513 C  CG    B LEU C 3 84  ? 58.494  -16.501 -8.923  0.50 22.86 ? 84  LEU F CG    1 
ATOM   14514 C  CD1   A LEU C 3 84  ? 57.902  -18.043 -9.210  0.50 24.92 ? 84  LEU F CD1   1 
ATOM   14515 C  CD1   B LEU C 3 84  ? 57.994  -17.888 -9.304  0.50 24.98 ? 84  LEU F CD1   1 
ATOM   14516 C  CD2   A LEU C 3 84  ? 59.602  -16.541 -8.154  0.50 22.88 ? 84  LEU F CD2   1 
ATOM   14517 C  CD2   B LEU C 3 84  ? 59.865  -16.580 -8.281  0.50 23.86 ? 84  LEU F CD2   1 
ATOM   14518 N  N     A HIS C 3 85  ? 55.662  -13.977 -9.810  0.50 25.18 ? 85  HIS F N     1 
ATOM   14519 N  N     B HIS C 3 85  ? 55.891  -13.738 -9.779  0.50 23.75 ? 85  HIS F N     1 
ATOM   14520 C  CA    A HIS C 3 85  ? 54.525  -13.476 -9.037  0.50 23.72 ? 85  HIS F CA    1 
ATOM   14521 C  CA    B HIS C 3 85  ? 54.746  -13.201 -9.042  0.50 24.14 ? 85  HIS F CA    1 
ATOM   14522 C  C     A HIS C 3 85  ? 53.209  -13.991 -9.600  0.50 29.52 ? 85  HIS F C     1 
ATOM   14523 C  C     B HIS C 3 85  ? 53.447  -13.835 -9.517  0.50 28.89 ? 85  HIS F C     1 
ATOM   14524 O  O     A HIS C 3 85  ? 52.397  -14.585 -8.882  0.50 24.64 ? 85  HIS F O     1 
ATOM   14525 O  O     B HIS C 3 85  ? 52.661  -14.356 -8.718  0.50 25.66 ? 85  HIS F O     1 
ATOM   14526 C  CB    A HIS C 3 85  ? 54.515  -11.947 -9.032  0.50 24.61 ? 85  HIS F CB    1 
ATOM   14527 C  CB    B HIS C 3 85  ? 54.672  -11.680 -9.210  0.50 24.82 ? 85  HIS F CB    1 
ATOM   14528 C  CG    A HIS C 3 85  ? 55.477  -11.331 -8.068  0.50 27.24 ? 85  HIS F CG    1 
ATOM   14529 C  CG    B HIS C 3 85  ? 55.482  -10.909 -8.215  0.50 27.44 ? 85  HIS F CG    1 
ATOM   14530 N  ND1   A HIS C 3 85  ? 56.800  -11.108 -8.380  0.50 22.00 ? 85  HIS F ND1   1 
ATOM   14531 N  ND1   B HIS C 3 85  ? 56.659  -10.273 -8.548  0.50 22.55 ? 85  HIS F ND1   1 
ATOM   14532 C  CD2   A HIS C 3 85  ? 55.306  -10.877 -6.804  0.50 20.95 ? 85  HIS F CD2   1 
ATOM   14533 C  CD2   B HIS C 3 85  ? 55.274  -10.650 -6.902  0.50 21.24 ? 85  HIS F CD2   1 
ATOM   14534 C  CE1   A HIS C 3 85  ? 57.403  -10.543 -7.350  0.50 25.52 ? 85  HIS F CE1   1 
ATOM   14535 C  CE1   B HIS C 3 85  ? 57.146  -9.664  -7.482  0.50 24.15 ? 85  HIS F CE1   1 
ATOM   14536 N  NE2   A HIS C 3 85  ? 56.519  -10.394 -6.379  0.50 27.54 ? 85  HIS F NE2   1 
ATOM   14537 N  NE2   B HIS C 3 85  ? 56.322  -9.874  -6.470  0.50 24.58 ? 85  HIS F NE2   1 
ATOM   14538 N  N     A LEU C 3 86  ? 52.981  -13.761 -10.895 0.50 25.05 ? 86  LEU F N     1 
ATOM   14539 N  N     B LEU C 3 86  ? 53.215  -13.814 -10.831 0.50 24.89 ? 86  LEU F N     1 
ATOM   14540 C  CA    A LEU C 3 86  ? 51.703  -14.128 -11.490 0.50 28.01 ? 86  LEU F CA    1 
ATOM   14541 C  CA    B LEU C 3 86  ? 51.925  -14.240 -11.361 0.50 26.80 ? 86  LEU F CA    1 
ATOM   14542 C  C     A LEU C 3 86  ? 51.494  -15.636 -11.487 0.50 28.39 ? 86  LEU F C     1 
ATOM   14543 C  C     B LEU C 3 86  ? 51.746  -15.750 -11.263 0.50 28.07 ? 86  LEU F C     1 
ATOM   14544 O  O     A LEU C 3 86  ? 50.361  -16.102 -11.311 0.50 27.93 ? 86  LEU F O     1 
ATOM   14545 O  O     B LEU C 3 86  ? 50.650  -16.230 -10.943 0.50 27.38 ? 86  LEU F O     1 
ATOM   14546 C  CB    A LEU C 3 86  ? 51.610  -13.562 -12.906 0.50 23.98 ? 86  LEU F CB    1 
ATOM   14547 C  CB    B LEU C 3 86  ? 51.776  -13.761 -12.803 0.50 24.69 ? 86  LEU F CB    1 
ATOM   14548 C  CG    A LEU C 3 86  ? 51.852  -12.053 -12.995 0.50 27.55 ? 86  LEU F CG    1 
ATOM   14549 C  CG    B LEU C 3 86  ? 52.010  -12.261 -12.993 0.50 27.48 ? 86  LEU F CG    1 
ATOM   14550 C  CD1   A LEU C 3 86  ? 51.773  -11.575 -14.436 0.50 25.85 ? 86  LEU F CD1   1 
ATOM   14551 C  CD1   B LEU C 3 86  ? 51.904  -11.876 -14.461 0.50 25.39 ? 86  LEU F CD1   1 
ATOM   14552 C  CD2   A LEU C 3 86  ? 50.873  -11.283 -12.113 0.50 31.79 ? 86  LEU F CD2   1 
ATOM   14553 C  CD2   B LEU C 3 86  ? 51.047  -11.442 -12.142 0.50 32.16 ? 86  LEU F CD2   1 
ATOM   14554 N  N     A ALA C 3 87  ? 52.568  -16.411 -11.652 0.50 24.96 ? 87  ALA F N     1 
ATOM   14555 N  N     B ALA C 3 87  ? 52.808  -16.516 -11.525 0.50 25.04 ? 87  ALA F N     1 
ATOM   14556 C  CA    A ALA C 3 87  ? 52.446  -17.864 -11.595 0.50 26.35 ? 87  ALA F CA    1 
ATOM   14557 C  CA    B ALA C 3 87  ? 52.706  -17.970 -11.438 0.50 26.29 ? 87  ALA F CA    1 
ATOM   14558 C  C     A ALA C 3 87  ? 52.088  -18.337 -10.190 0.50 26.85 ? 87  ALA F C     1 
ATOM   14559 C  C     B ALA C 3 87  ? 52.451  -18.434 -10.007 0.50 26.60 ? 87  ALA F C     1 
ATOM   14560 O  O     A ALA C 3 87  ? 51.287  -19.265 -10.025 0.50 28.06 ? 87  ALA F O     1 
ATOM   14561 O  O     B ALA C 3 87  ? 51.780  -19.450 -9.796  0.50 26.34 ? 87  ALA F O     1 
ATOM   14562 C  CB    A ALA C 3 87  ? 53.744  -18.519 -12.060 0.50 27.09 ? 87  ALA F CB    1 
ATOM   14563 C  CB    B ALA C 3 87  ? 53.972  -18.620 -11.990 0.50 27.13 ? 87  ALA F CB    1 
ATOM   14564 N  N     A ALA C 3 88  ? 52.684  -17.723 -9.168  0.50 26.86 ? 88  ALA F N     1 
ATOM   14565 N  N     B ALA C 3 88  ? 52.984  -17.716 -9.020  0.50 27.13 ? 88  ALA F N     1 
ATOM   14566 C  CA    A ALA C 3 88  ? 52.388  -18.113 -7.792  0.50 25.83 ? 88  ALA F CA    1 
ATOM   14567 C  CA    B ALA C 3 88  ? 52.699  -18.023 -7.625  0.50 24.97 ? 88  ALA F CA    1 
ATOM   14568 C  C     A ALA C 3 88  ? 50.965  -17.736 -7.403  0.50 24.99 ? 88  ALA F C     1 
ATOM   14569 C  C     B ALA C 3 88  ? 51.312  -17.563 -7.197  0.50 26.55 ? 88  ALA F C     1 
ATOM   14570 O  O     A ALA C 3 88  ? 50.273  -18.510 -6.732  0.50 30.24 ? 88  ALA F O     1 
ATOM   14571 O  O     B ALA C 3 88  ? 50.755  -18.115 -6.244  0.50 27.70 ? 88  ALA F O     1 
ATOM   14572 C  CB    A ALA C 3 88  ? 53.397  -17.469 -6.844  0.50 23.97 ? 88  ALA F CB    1 
ATOM   14573 C  CB    B ALA C 3 88  ? 53.759  -17.385 -6.726  0.50 24.53 ? 88  ALA F CB    1 
ATOM   14574 N  N     A LEU C 3 89  ? 50.517  -16.545 -7.804  0.50 27.07 ? 89  LEU F N     1 
ATOM   14575 N  N     B LEU C 3 89  ? 50.750  -16.563 -7.877  0.50 27.72 ? 89  LEU F N     1 
ATOM   14576 C  CA    A LEU C 3 89  ? 49.150  -16.122 -7.521  0.50 23.78 ? 89  LEU F CA    1 
ATOM   14577 C  CA    B LEU C 3 89  ? 49.437  -16.041 -7.522  0.50 23.76 ? 89  LEU F CA    1 
ATOM   14578 C  C     A LEU C 3 89  ? 48.141  -17.095 -8.118  0.50 31.21 ? 89  LEU F C     1 
ATOM   14579 C  C     B LEU C 3 89  ? 48.318  -16.889 -8.113  0.50 30.54 ? 89  LEU F C     1 
ATOM   14580 O  O     A LEU C 3 89  ? 47.269  -17.618 -7.412  0.50 25.29 ? 89  LEU F O     1 
ATOM   14581 O  O     B LEU C 3 89  ? 47.303  -17.133 -7.449  0.50 26.53 ? 89  LEU F O     1 
ATOM   14582 C  CB    A LEU C 3 89  ? 48.920  -14.712 -8.064  0.50 26.12 ? 89  LEU F CB    1 
ATOM   14583 C  CB    B LEU C 3 89  ? 49.318  -14.588 -7.988  0.50 25.15 ? 89  LEU F CB    1 
ATOM   14584 C  CG    A LEU C 3 89  ? 47.474  -14.213 -8.044  0.50 28.11 ? 89  LEU F CG    1 
ATOM   14585 C  CG    B LEU C 3 89  ? 47.938  -13.933 -7.966  0.50 28.37 ? 89  LEU F CG    1 
ATOM   14586 C  CD1   A LEU C 3 89  ? 47.069  -13.791 -6.629  0.50 25.88 ? 89  LEU F CD1   1 
ATOM   14587 C  CD1   B LEU C 3 89  ? 47.582  -13.449 -6.556  0.50 25.10 ? 89  LEU F CD1   1 
ATOM   14588 C  CD2   A LEU C 3 89  ? 47.291  -13.076 -9.035  0.50 27.44 ? 89  LEU F CD2   1 
ATOM   14589 C  CD2   B LEU C 3 89  ? 47.885  -12.794 -8.969  0.50 24.56 ? 89  LEU F CD2   1 
ATOM   14590 N  N     A ILE C 3 90  ? 48.252  -17.356 -9.423  0.50 29.48 ? 90  ILE F N     1 
ATOM   14591 N  N     B ILE C 3 90  ? 48.491  -17.357 -9.349  0.50 28.94 ? 90  ILE F N     1 
ATOM   14592 C  CA    A ILE C 3 90  ? 47.297  -18.232 -10.093 0.50 29.16 ? 90  ILE F CA    1 
ATOM   14593 C  CA    B ILE C 3 90  ? 47.442  -18.114 -10.024 0.50 29.15 ? 90  ILE F CA    1 
ATOM   14594 C  C     A ILE C 3 90  ? 47.504  -19.683 -9.674  0.50 29.38 ? 90  ILE F C     1 
ATOM   14595 C  C     B ILE C 3 90  ? 47.477  -19.598 -9.669  0.50 29.37 ? 90  ILE F C     1 
ATOM   14596 O  O     A ILE C 3 90  ? 46.569  -20.492 -9.724  0.50 28.17 ? 90  ILE F O     1 
ATOM   14597 O  O     B ILE C 3 90  ? 46.441  -20.273 -9.745  0.50 28.60 ? 90  ILE F O     1 
ATOM   14598 C  CB    A ILE C 3 90  ? 47.404  -18.050 -11.619 0.50 27.29 ? 90  ILE F CB    1 
ATOM   14599 C  CB    B ILE C 3 90  ? 47.546  -17.902 -11.546 0.50 27.48 ? 90  ILE F CB    1 
ATOM   14600 C  CG1   A ILE C 3 90  ? 47.263  -16.571 -11.985 0.50 30.62 ? 90  ILE F CG1   1 
ATOM   14601 C  CG1   B ILE C 3 90  ? 47.456  -16.411 -11.876 0.50 30.56 ? 90  ILE F CG1   1 
ATOM   14602 C  CG2   A ILE C 3 90  ? 46.344  -18.864 -12.340 0.50 25.35 ? 90  ILE F CG2   1 
ATOM   14603 C  CG2   B ILE C 3 90  ? 46.449  -18.652 -12.288 0.50 25.36 ? 90  ILE F CG2   1 
ATOM   14604 C  CD1   A ILE C 3 90  ? 45.936  -15.953 -11.574 0.50 30.35 ? 90  ILE F CD1   1 
ATOM   14605 C  CD1   B ILE C 3 90  ? 46.129  -15.778 -11.474 0.50 30.26 ? 90  ILE F CD1   1 
ATOM   14606 N  N     A GLY C 3 91  ? 48.714  -20.041 -9.259  0.50 27.13 ? 91  GLY F N     1 
ATOM   14607 N  N     B GLY C 3 91  ? 48.629  -20.127 -9.277  0.50 27.14 ? 91  GLY F N     1 
ATOM   14608 C  CA    A GLY C 3 91  ? 48.952  -21.360 -8.705  0.50 30.04 ? 91  GLY F CA    1 
ATOM   14609 C  CA    B GLY C 3 91  ? 48.719  -21.487 -8.790  0.50 30.03 ? 91  GLY F CA    1 
ATOM   14610 C  C     A GLY C 3 91  ? 49.373  -22.407 -9.716  0.50 31.29 ? 91  GLY F C     1 
ATOM   14611 C  C     B GLY C 3 91  ? 49.388  -22.485 -9.709  0.50 31.28 ? 91  GLY F C     1 
ATOM   14612 O  O     A GLY C 3 91  ? 48.674  -23.408 -9.907  0.50 24.61 ? 91  GLY F O     1 
ATOM   14613 O  O     B GLY C 3 91  ? 49.407  -23.677 -9.380  0.50 24.13 ? 91  GLY F O     1 
ATOM   14614 N  N     A HIS C 3 92  ? 50.520  -22.191 -10.362 0.50 26.82 ? 92  HIS F N     1 
ATOM   14615 N  N     B HIS C 3 92  ? 49.945  -22.045 -10.836 0.50 25.44 ? 92  HIS F N     1 
ATOM   14616 C  CA    A HIS C 3 92  ? 51.063  -23.092 -11.380 0.50 29.60 ? 92  HIS F CA    1 
ATOM   14617 C  CA    B HIS C 3 92  ? 50.541  -22.949 -11.818 0.50 29.13 ? 92  HIS F CA    1 
ATOM   14618 C  C     A HIS C 3 92  ? 52.402  -23.634 -10.878 0.50 29.89 ? 92  HIS F C     1 
ATOM   14619 C  C     B HIS C 3 92  ? 51.871  -23.463 -11.280 0.50 27.98 ? 92  HIS F C     1 
ATOM   14620 O  O     A HIS C 3 92  ? 53.454  -23.041 -11.127 0.50 27.62 ? 92  HIS F O     1 
ATOM   14621 O  O     B HIS C 3 92  ? 52.900  -22.793 -11.386 0.50 26.81 ? 92  HIS F O     1 
ATOM   14622 C  CB    A HIS C 3 92  ? 51.216  -22.370 -12.717 0.50 26.29 ? 92  HIS F CB    1 
ATOM   14623 C  CB    B HIS C 3 92  ? 50.722  -22.231 -13.149 0.50 25.34 ? 92  HIS F CB    1 
ATOM   14624 C  CG    A HIS C 3 92  ? 49.919  -21.952 -13.335 0.50 24.55 ? 92  HIS F CG    1 
ATOM   14625 C  CG    B HIS C 3 92  ? 49.443  -21.739 -13.750 0.50 24.11 ? 92  HIS F CG    1 
ATOM   14626 N  ND1   A HIS C 3 92  ? 48.900  -22.841 -13.601 0.50 26.71 ? 92  HIS F ND1   1 
ATOM   14627 N  ND1   B HIS C 3 92  ? 48.369  -22.567 -13.996 0.50 27.24 ? 92  HIS F ND1   1 
ATOM   14628 C  CD2   A HIS C 3 92  ? 49.482  -20.742 -13.757 0.50 23.91 ? 92  HIS F CD2   1 
ATOM   14629 C  CD2   B HIS C 3 92  ? 49.070  -20.506 -14.167 0.50 25.59 ? 92  HIS F CD2   1 
ATOM   14630 C  CE1   A HIS C 3 92  ? 47.887  -22.195 -14.150 0.50 26.76 ? 92  HIS F CE1   1 
ATOM   14631 C  CE1   B HIS C 3 92  ? 47.386  -21.864 -14.531 0.50 22.94 ? 92  HIS F CE1   1 
ATOM   14632 N  NE2   A HIS C 3 92  ? 48.216  -20.920 -14.258 0.50 28.94 ? 92  HIS F NE2   1 
ATOM   14633 N  NE2   B HIS C 3 92  ? 47.787  -20.610 -14.647 0.50 26.99 ? 92  HIS F NE2   1 
ATOM   14634 N  N     A LEU C 3 93  ? 52.354  -24.775 -10.183 0.50 30.95 ? 93  LEU F N     1 
ATOM   14635 N  N     B LEU C 3 93  ? 51.852  -24.669 -10.706 0.50 32.26 ? 93  LEU F N     1 
ATOM   14636 C  CA    A LEU C 3 93  ? 53.540  -25.303 -9.509  0.50 27.01 ? 93  LEU F CA    1 
ATOM   14637 C  CA    B LEU C 3 93  ? 53.025  -25.189 -10.007 0.50 29.66 ? 93  LEU F CA    1 
ATOM   14638 C  C     A LEU C 3 93  ? 54.672  -25.583 -10.491 0.50 29.82 ? 93  LEU F C     1 
ATOM   14639 C  C     B LEU C 3 93  ? 54.168  -25.496 -10.970 0.50 30.62 ? 93  LEU F C     1 
ATOM   14640 O  O     A LEU C 3 93  ? 55.829  -25.227 -10.239 0.50 29.81 ? 93  LEU F O     1 
ATOM   14641 O  O     B LEU C 3 93  ? 55.322  -25.141 -10.708 0.50 28.60 ? 93  LEU F O     1 
ATOM   14642 C  CB    A LEU C 3 93  ? 53.182  -26.576 -8.742  0.50 30.28 ? 93  LEU F CB    1 
ATOM   14643 C  CB    B LEU C 3 93  ? 52.645  -26.439 -9.212  0.50 32.14 ? 93  LEU F CB    1 
ATOM   14644 C  CG    A LEU C 3 93  ? 54.355  -27.263 -8.037  0.50 34.05 ? 93  LEU F CG    1 
ATOM   14645 C  CG    B LEU C 3 93  ? 53.800  -27.196 -8.554  0.50 33.93 ? 93  LEU F CG    1 
ATOM   14646 C  CD1   A LEU C 3 93  ? 54.409  -26.862 -6.572  0.50 35.26 ? 93  LEU F CD1   1 
ATOM   14647 C  CD1   B LEU C 3 93  ? 54.543  -26.308 -7.567  0.50 34.17 ? 93  LEU F CD1   1 
ATOM   14648 C  CD2   A LEU C 3 93  ? 54.282  -28.776 -8.187  0.50 39.19 ? 93  LEU F CD2   1 
ATOM   14649 C  CD2   B LEU C 3 93  ? 53.289  -28.459 -7.871  0.50 37.30 ? 93  LEU F CD2   1 
ATOM   14650 N  N     A GLU C 3 94  ? 54.361  -26.239 -11.609 0.50 28.40 ? 94  GLU F N     1 
ATOM   14651 N  N     B GLU C 3 94  ? 53.873  -26.165 -12.088 0.50 30.07 ? 94  GLU F N     1 
ATOM   14652 C  CA    A GLU C 3 94  ? 55.402  -26.601 -12.566 0.50 30.16 ? 94  GLU F CA    1 
ATOM   14653 C  CA    B GLU C 3 94  ? 54.936  -26.540 -13.016 0.50 32.98 ? 94  GLU F CA    1 
ATOM   14654 C  C     A GLU C 3 94  ? 56.072  -25.360 -13.144 0.50 31.15 ? 94  GLU F C     1 
ATOM   14655 C  C     B GLU C 3 94  ? 55.645  -25.327 -13.608 0.50 30.88 ? 94  GLU F C     1 
ATOM   14656 O  O     A GLU C 3 94  ? 57.303  -25.262 -13.170 0.50 28.79 ? 94  GLU F O     1 
ATOM   14657 O  O     B GLU C 3 94  ? 56.803  -25.444 -14.023 0.50 30.33 ? 94  GLU F O     1 
ATOM   14658 C  CB    A GLU C 3 94  ? 54.816  -27.472 -13.679 0.50 33.36 ? 94  GLU F CB    1 
ATOM   14659 C  CB    B GLU C 3 94  ? 54.379  -27.424 -14.138 0.50 32.23 ? 94  GLU F CB    1 
ATOM   14660 C  CG    A GLU C 3 94  ? 54.340  -28.847 -13.222 0.50 36.75 ? 94  GLU F CG    1 
ATOM   14661 C  CG    B GLU C 3 94  ? 53.841  -28.777 -13.676 0.50 38.58 ? 94  GLU F CG    1 
ATOM   14662 C  CD    A GLU C 3 94  ? 52.998  -28.807 -12.509 0.50 34.53 ? 94  GLU F CD    1 
ATOM   14663 C  CD    B GLU C 3 94  ? 52.325  -28.807 -13.559 0.50 38.44 ? 94  GLU F CD    1 
ATOM   14664 O  OE1   A GLU C 3 94  ? 52.346  -27.742 -12.520 0.50 38.96 ? 94  GLU F OE1   1 
ATOM   14665 O  OE1   B GLU C 3 94  ? 51.692  -27.747 -13.755 0.50 36.58 ? 94  GLU F OE1   1 
ATOM   14666 O  OE2   A GLU C 3 94  ? 52.593  -29.843 -11.940 0.50 38.79 ? 94  GLU F OE2   1 
ATOM   14667 O  OE2   B GLU C 3 94  ? 51.768  -29.895 -13.273 0.50 28.98 ? 94  GLU F OE2   1 
ATOM   14668 N  N     A ILE C 3 95  ? 55.273  -24.392 -13.601 0.50 30.11 ? 95  ILE F N     1 
ATOM   14669 N  N     B ILE C 3 95  ? 54.988  -24.167 -13.645 0.50 30.14 ? 95  ILE F N     1 
ATOM   14670 C  CA    A ILE C 3 95  ? 55.838  -23.160 -14.148 0.50 27.50 ? 95  ILE F CA    1 
ATOM   14671 C  CA    B ILE C 3 95  ? 55.627  -22.964 -14.173 0.50 26.89 ? 95  ILE F CA    1 
ATOM   14672 C  C     A ILE C 3 95  ? 56.629  -22.412 -13.081 0.50 28.65 ? 95  ILE F C     1 
ATOM   14673 C  C     B ILE C 3 95  ? 56.562  -22.347 -13.139 0.50 28.59 ? 95  ILE F C     1 
ATOM   14674 O  O     A ILE C 3 95  ? 57.689  -21.836 -13.363 0.50 27.56 ? 95  ILE F O     1 
ATOM   14675 O  O     B ILE C 3 95  ? 57.701  -21.982 -13.456 0.50 27.83 ? 95  ILE F O     1 
ATOM   14676 C  CB    A ILE C 3 95  ? 54.724  -22.288 -14.756 0.50 30.01 ? 95  ILE F CB    1 
ATOM   14677 C  CB    B ILE C 3 95  ? 54.566  -21.958 -14.650 0.50 30.46 ? 95  ILE F CB    1 
ATOM   14678 C  CG1   A ILE C 3 95  ? 54.154  -22.960 -16.009 0.50 26.74 ? 95  ILE F CG1   1 
ATOM   14679 C  CG1   B ILE C 3 95  ? 53.756  -22.553 -15.804 0.50 30.98 ? 95  ILE F CG1   1 
ATOM   14680 C  CG2   A ILE C 3 95  ? 55.244  -20.896 -15.087 0.50 28.69 ? 95  ILE F CG2   1 
ATOM   14681 C  CG2   B ILE C 3 95  ? 55.222  -20.654 -15.078 0.50 28.47 ? 95  ILE F CG2   1 
ATOM   14682 C  CD1   A ILE C 3 95  ? 53.032  -22.187 -16.657 0.50 32.54 ? 95  ILE F CD1   1 
ATOM   14683 C  CD1   B ILE C 3 95  ? 52.684  -21.627 -16.332 0.50 32.83 ? 95  ILE F CD1   1 
ATOM   14684 N  N     A VAL C 3 96  ? 56.135  -22.414 -11.839 0.50 28.13 ? 96  VAL F N     1 
ATOM   14685 N  N     B VAL C 3 96  ? 56.097  -22.209 -11.892 0.50 27.56 ? 96  VAL F N     1 
ATOM   14686 C  CA    A VAL C 3 96  ? 56.916  -21.873 -10.727 0.50 28.35 ? 96  VAL F CA    1 
ATOM   14687 C  CA    B VAL C 3 96  ? 56.979  -21.766 -10.813 0.50 28.22 ? 96  VAL F CA    1 
ATOM   14688 C  C     A VAL C 3 96  ? 58.290  -22.530 -10.682 0.50 29.77 ? 96  VAL F C     1 
ATOM   14689 C  C     B VAL C 3 96  ? 58.238  -22.624 -10.773 0.50 29.58 ? 96  VAL F C     1 
ATOM   14690 O  O     A VAL C 3 96  ? 59.320  -21.858 -10.538 0.50 28.04 ? 96  VAL F O     1 
ATOM   14691 O  O     B VAL C 3 96  ? 59.351  -22.119 -10.569 0.50 27.89 ? 96  VAL F O     1 
ATOM   14692 C  CB    A VAL C 3 96  ? 56.161  -22.054 -9.398  0.50 27.01 ? 96  VAL F CB    1 
ATOM   14693 C  CB    B VAL C 3 96  ? 56.238  -21.791 -9.461  0.50 27.98 ? 96  VAL F CB    1 
ATOM   14694 C  CG1   A VAL C 3 96  ? 57.120  -21.922 -8.224  0.50 30.09 ? 96  VAL F CG1   1 
ATOM   14695 C  CG1   B VAL C 3 96  ? 57.231  -21.799 -8.308  0.50 29.90 ? 96  VAL F CG1   1 
ATOM   14696 C  CG2   A VAL C 3 96  ? 55.045  -21.025 -9.281  0.50 24.23 ? 96  VAL F CG2   1 
ATOM   14697 C  CG2   B VAL C 3 96  ? 55.315  -20.587 -9.340  0.50 20.78 ? 96  VAL F CG2   1 
ATOM   14698 N  N     A GLU C 3 97  ? 58.327  -23.858 -10.820 0.50 27.62 ? 97  GLU F N     1 
ATOM   14699 N  N     B GLU C 3 97  ? 58.087  -23.931 -10.989 0.50 26.69 ? 97  GLU F N     1 
ATOM   14700 C  CA    A GLU C 3 97  ? 59.609  -24.557 -10.798 0.50 26.44 ? 97  GLU F CA    1 
ATOM   14701 C  CA    B GLU C 3 97  ? 59.250  -24.810 -10.956 0.50 26.35 ? 97  GLU F CA    1 
ATOM   14702 C  C     A GLU C 3 97  ? 60.465  -24.184 -12.003 0.50 29.78 ? 97  GLU F C     1 
ATOM   14703 C  C     B GLU C 3 97  ? 60.158  -24.570 -12.158 0.50 30.60 ? 97  GLU F C     1 
ATOM   14704 O  O     A GLU C 3 97  ? 61.667  -23.934 -11.859 0.50 31.14 ? 97  GLU F O     1 
ATOM   14705 O  O     B GLU C 3 97  ? 61.386  -24.569 -12.018 0.50 30.52 ? 97  GLU F O     1 
ATOM   14706 C  CB    A GLU C 3 97  ? 59.391  -26.070 -10.737 0.50 28.41 ? 97  GLU F CB    1 
ATOM   14707 C  CB    B GLU C 3 97  ? 58.802  -26.271 -10.872 0.50 29.51 ? 97  GLU F CB    1 
ATOM   14708 C  CG    A GLU C 3 97  ? 59.252  -26.624 -9.320  0.50 34.08 ? 97  GLU F CG    1 
ATOM   14709 C  CG    B GLU C 3 97  ? 58.092  -26.598 -9.553  0.50 31.43 ? 97  GLU F CG    1 
ATOM   14710 C  CD    A GLU C 3 97  ? 59.403  -28.138 -9.253  0.50 35.59 ? 97  GLU F CD    1 
ATOM   14711 C  CD    B GLU C 3 97  ? 58.063  -28.083 -9.221  0.50 35.61 ? 97  GLU F CD    1 
ATOM   14712 O  OE1   A GLU C 3 97  ? 59.133  -28.816 -10.266 0.50 37.03 ? 97  GLU F OE1   1 
ATOM   14713 O  OE1   B GLU C 3 97  ? 57.847  -28.910 -10.130 0.50 29.80 ? 97  GLU F OE1   1 
ATOM   14714 O  OE2   A GLU C 3 97  ? 59.795  -28.653 -8.182  0.50 34.10 ? 97  GLU F OE2   1 
ATOM   14715 O  OE2   B GLU C 3 97  ? 58.259  -28.423 -8.036  0.50 31.12 ? 97  GLU F OE2   1 
ATOM   14716 N  N     A VAL C 3 98  ? 59.864  -24.124 -13.195 0.50 29.20 ? 98  VAL F N     1 
ATOM   14717 N  N     B VAL C 3 98  ? 59.580  -24.339 -13.340 0.50 28.36 ? 98  VAL F N     1 
ATOM   14718 C  CA    A VAL C 3 98  ? 60.630  -23.826 -14.405 0.50 28.96 ? 98  VAL F CA    1 
ATOM   14719 C  CA    B VAL C 3 98  ? 60.397  -24.015 -14.509 0.50 29.81 ? 98  VAL F CA    1 
ATOM   14720 C  C     A VAL C 3 98  ? 61.213  -22.419 -14.342 0.50 30.98 ? 98  VAL F C     1 
ATOM   14721 C  C     B VAL C 3 98  ? 61.107  -22.681 -14.308 0.50 29.64 ? 98  VAL F C     1 
ATOM   14722 O  O     A VAL C 3 98  ? 62.353  -22.185 -14.765 0.50 36.11 ? 98  VAL F O     1 
ATOM   14723 O  O     B VAL C 3 98  ? 62.316  -22.562 -14.545 0.50 37.04 ? 98  VAL F O     1 
ATOM   14724 C  CB    A VAL C 3 98  ? 59.753  -24.019 -15.658 0.50 29.11 ? 98  VAL F CB    1 
ATOM   14725 C  CB    B VAL C 3 98  ? 59.540  -24.009 -15.789 0.50 28.71 ? 98  VAL F CB    1 
ATOM   14726 C  CG1   A VAL C 3 98  ? 60.544  -23.700 -16.922 0.50 33.17 ? 98  VAL F CG1   1 
ATOM   14727 C  CG1   B VAL C 3 98  ? 60.261  -23.272 -16.910 0.50 33.44 ? 98  VAL F CG1   1 
ATOM   14728 C  CG2   A VAL C 3 98  ? 59.215  -25.438 -15.713 0.50 35.71 ? 98  VAL F CG2   1 
ATOM   14729 C  CG2   B VAL C 3 98  ? 59.229  -25.428 -16.220 0.50 36.14 ? 98  VAL F CG2   1 
ATOM   14730 N  N     A LEU C 3 99  ? 60.443  -21.457 -13.825 0.50 27.16 ? 99  LEU F N     1 
ATOM   14731 N  N     B LEU C 3 99  ? 60.366  -21.657 -13.869 0.50 27.51 ? 99  LEU F N     1 
ATOM   14732 C  CA    A LEU C 3 99  ? 60.952  -20.095 -13.698 0.50 29.15 ? 99  LEU F CA    1 
ATOM   14733 C  CA    B LEU C 3 99  ? 60.942  -20.323 -13.719 0.50 28.73 ? 99  LEU F CA    1 
ATOM   14734 C  C     A LEU C 3 99  ? 62.146  -20.046 -12.752 0.50 31.25 ? 99  LEU F C     1 
ATOM   14735 C  C     B LEU C 3 99  ? 62.135  -20.337 -12.770 0.50 31.05 ? 99  LEU F C     1 
ATOM   14736 O  O     A LEU C 3 99  ? 63.178  -19.437 -13.065 0.50 29.55 ? 99  LEU F O     1 
ATOM   14737 O  O     B LEU C 3 99  ? 63.194  -19.772 -13.075 0.50 29.48 ? 99  LEU F O     1 
ATOM   14738 C  CB    A LEU C 3 99  ? 59.839  -19.157 -13.224 0.50 23.82 ? 99  LEU F CB    1 
ATOM   14739 C  CB    B LEU C 3 99  ? 59.879  -19.337 -13.227 0.50 24.07 ? 99  LEU F CB    1 
ATOM   14740 C  CG    A LEU C 3 99  ? 58.703  -18.879 -14.215 0.50 23.06 ? 99  LEU F CG    1 
ATOM   14741 C  CG    B LEU C 3 99  ? 58.741  -18.956 -14.180 0.50 23.07 ? 99  LEU F CG    1 
ATOM   14742 C  CD1   A LEU C 3 99  ? 57.564  -18.134 -13.539 0.50 26.30 ? 99  LEU F CD1   1 
ATOM   14743 C  CD1   B LEU C 3 99  ? 57.722  -18.080 -13.469 0.50 26.31 ? 99  LEU F CD1   1 
ATOM   14744 C  CD2   A LEU C 3 99  ? 59.204  -18.091 -15.414 0.50 29.06 ? 99  LEU F CD2   1 
ATOM   14745 C  CD2   B LEU C 3 99  ? 59.275  -18.247 -15.412 0.50 29.39 ? 99  LEU F CD2   1 
ATOM   14746 N  N     A LEU C 3 100 ? 62.030  -20.705 -11.595 0.50 29.29 ? 100 LEU F N     1 
ATOM   14747 N  N     B LEU C 3 100 ? 61.986  -20.995 -11.616 0.50 29.42 ? 100 LEU F N     1 
ATOM   14748 C  CA    A LEU C 3 100 ? 63.122  -20.714 -10.625 0.50 27.60 ? 100 LEU F CA    1 
ATOM   14749 C  CA    B LEU C 3 100 ? 63.055  -20.999 -10.621 0.50 28.23 ? 100 LEU F CA    1 
ATOM   14750 C  C     A LEU C 3 100 ? 64.383  -21.345 -11.206 0.50 30.18 ? 100 LEU F C     1 
ATOM   14751 C  C     B LEU C 3 100 ? 64.319  -21.663 -11.154 0.50 31.09 ? 100 LEU F C     1 
ATOM   14752 O  O     A LEU C 3 100 ? 65.500  -20.919 -10.893 0.50 32.01 ? 100 LEU F O     1 
ATOM   14753 O  O     B LEU C 3 100 ? 65.434  -21.247 -10.819 0.50 30.01 ? 100 LEU F O     1 
ATOM   14754 C  CB    A LEU C 3 100 ? 62.691  -21.455 -9.361  0.50 27.19 ? 100 LEU F CB    1 
ATOM   14755 C  CB    B LEU C 3 100 ? 62.583  -21.699 -9.349  0.50 27.30 ? 100 LEU F CB    1 
ATOM   14756 C  CG    A LEU C 3 100 ? 61.618  -20.748 -8.520  0.50 28.79 ? 100 LEU F CG    1 
ATOM   14757 C  CG    B LEU C 3 100 ? 61.621  -20.882 -8.477  0.50 29.02 ? 100 LEU F CG    1 
ATOM   14758 C  CD1   A LEU C 3 100 ? 60.922  -21.726 -7.579  0.50 31.79 ? 100 LEU F CD1   1 
ATOM   14759 C  CD1   B LEU C 3 100 ? 60.951  -21.762 -7.429  0.50 31.72 ? 100 LEU F CD1   1 
ATOM   14760 C  CD2   A LEU C 3 100 ? 62.232  -19.602 -7.738  0.50 28.75 ? 100 LEU F CD2   1 
ATOM   14761 C  CD2   B LEU C 3 100 ? 62.363  -19.735 -7.813  0.50 28.56 ? 100 LEU F CD2   1 
ATOM   14762 N  N     A LYS C 3 101 ? 64.225  -22.369 -12.046 0.50 25.88 ? 101 LYS F N     1 
ATOM   14763 N  N     B LYS C 3 101 ? 64.170  -22.703 -11.976 0.50 25.80 ? 101 LYS F N     1 
ATOM   14764 C  CA    A LYS C 3 101 ? 65.372  -23.012 -12.673 0.50 33.89 ? 101 LYS F CA    1 
ATOM   14765 C  CA    B LYS C 3 101 ? 65.345  -23.386 -12.502 0.50 32.84 ? 101 LYS F CA    1 
ATOM   14766 C  C     A LYS C 3 101 ? 65.987  -22.169 -13.785 0.50 35.33 ? 101 LYS F C     1 
ATOM   14767 C  C     B LYS C 3 101 ? 66.156  -22.498 -13.438 0.50 35.37 ? 101 LYS F C     1 
ATOM   14768 O  O     A LYS C 3 101 ? 67.086  -22.492 -14.249 0.50 34.59 ? 101 LYS F O     1 
ATOM   14769 O  O     B LYS C 3 101 ? 67.337  -22.779 -13.667 0.50 31.60 ? 101 LYS F O     1 
ATOM   14770 C  CB    A LYS C 3 101 ? 64.964  -24.384 -13.223 0.50 33.68 ? 101 LYS F CB    1 
ATOM   14771 C  CB    B LYS C 3 101 ? 64.934  -24.667 -13.229 0.50 34.32 ? 101 LYS F CB    1 
ATOM   14772 C  CG    A LYS C 3 101 ? 66.126  -25.323 -13.530 0.50 45.45 ? 101 LYS F CG    1 
ATOM   14773 C  CG    B LYS C 3 101 ? 66.032  -25.719 -13.305 0.50 45.65 ? 101 LYS F CG    1 
ATOM   14774 C  CD    A LYS C 3 101 ? 65.660  -26.563 -14.280 0.50 43.93 ? 101 LYS F CD    1 
ATOM   14775 C  CD    B LYS C 3 101 ? 65.734  -26.753 -14.379 0.50 44.05 ? 101 LYS F CD    1 
ATOM   14776 C  CE    A LYS C 3 101 ? 66.845  -27.400 -14.744 0.50 47.21 ? 101 LYS F CE    1 
ATOM   14777 C  CE    B LYS C 3 101 ? 65.809  -26.127 -15.764 0.50 46.48 ? 101 LYS F CE    1 
ATOM   14778 N  NZ    A LYS C 3 101 ? 66.426  -28.530 -15.621 0.50 45.71 ? 101 LYS F NZ    1 
ATOM   14779 N  NZ    B LYS C 3 101 ? 65.558  -27.118 -16.850 0.50 42.39 ? 101 LYS F NZ    1 
ATOM   14780 N  N     A HIS C 3 102 ? 65.319  -21.096 -14.215 0.50 32.78 ? 102 HIS F N     1 
ATOM   14781 N  N     B HIS C 3 102 ? 65.554  -21.433 -13.974 0.50 32.56 ? 102 HIS F N     1 
ATOM   14782 C  CA    A HIS C 3 102 ? 65.805  -20.248 -15.298 0.50 32.55 ? 102 HIS F CA    1 
ATOM   14783 C  CA    B HIS C 3 102 ? 66.226  -20.524 -14.895 0.50 33.69 ? 102 HIS F CA    1 
ATOM   14784 C  C     A HIS C 3 102 ? 66.174  -18.843 -14.831 0.50 26.94 ? 102 HIS F C     1 
ATOM   14785 C  C     B HIS C 3 102 ? 66.579  -19.189 -14.248 0.50 27.37 ? 102 HIS F C     1 
ATOM   14786 O  O     A HIS C 3 102 ? 66.148  -17.905 -15.634 0.50 30.38 ? 102 HIS F O     1 
ATOM   14787 O  O     B HIS C 3 102 ? 66.843  -18.211 -14.954 0.50 29.65 ? 102 HIS F O     1 
ATOM   14788 C  CB    A HIS C 3 102 ? 64.768  -20.170 -16.418 0.50 30.01 ? 102 HIS F CB    1 
ATOM   14789 C  CB    B HIS C 3 102 ? 65.369  -20.305 -16.140 0.50 32.50 ? 102 HIS F CB    1 
ATOM   14790 C  CG    A HIS C 3 102 ? 64.807  -21.333 -17.358 0.50 37.11 ? 102 HIS F CG    1 
ATOM   14791 C  CG    B HIS C 3 102 ? 65.268  -21.513 -17.016 0.50 37.15 ? 102 HIS F CG    1 
ATOM   14792 N  ND1   A HIS C 3 102 ? 63.980  -22.428 -17.222 0.50 31.86 ? 102 HIS F ND1   1 
ATOM   14793 N  ND1   B HIS C 3 102 ? 64.493  -22.605 -16.690 0.50 33.92 ? 102 HIS F ND1   1 
ATOM   14794 C  CD2   A HIS C 3 102 ? 65.579  -21.578 -18.444 0.50 32.00 ? 102 HIS F CD2   1 
ATOM   14795 C  CD2   B HIS C 3 102 ? 65.856  -21.808 -18.200 0.50 32.27 ? 102 HIS F CD2   1 
ATOM   14796 C  CE1   A HIS C 3 102 ? 64.238  -23.295 -18.186 0.50 39.56 ? 102 HIS F CE1   1 
ATOM   14797 C  CE1   B HIS C 3 102 ? 64.602  -23.518 -17.639 0.50 37.95 ? 102 HIS F CE1   1 
ATOM   14798 N  NE2   A HIS C 3 102 ? 65.204  -22.803 -18.941 0.50 38.43 ? 102 HIS F NE2   1 
ATOM   14799 N  NE2   B HIS C 3 102 ? 65.424  -23.059 -18.566 0.50 37.98 ? 102 HIS F NE2   1 
ATOM   14800 N  N     A GLY C 3 103 ? 66.510  -18.673 -13.557 0.50 25.93 ? 103 GLY F N     1 
ATOM   14801 N  N     B GLY C 3 103 ? 66.592  -19.128 -12.920 0.50 27.04 ? 103 GLY F N     1 
ATOM   14802 C  CA    A GLY C 3 103 ? 67.002  -17.403 -13.061 0.50 25.60 ? 103 GLY F CA    1 
ATOM   14803 C  CA    B GLY C 3 103 ? 67.137  -17.982 -12.223 0.50 25.01 ? 103 GLY F CA    1 
ATOM   14804 C  C     A GLY C 3 103 ? 65.982  -16.466 -12.444 0.50 27.16 ? 103 GLY F C     1 
ATOM   14805 C  C     B GLY C 3 103 ? 66.152  -16.902 -11.841 0.50 24.68 ? 103 GLY F C     1 
ATOM   14806 O  O     A GLY C 3 103 ? 66.255  -15.264 -12.357 0.50 26.29 ? 103 GLY F O     1 
ATOM   14807 O  O     B GLY C 3 103 ? 66.583  -15.786 -11.527 0.50 23.86 ? 103 GLY F O     1 
ATOM   14808 N  N     A ALA C 3 104 ? 64.831  -16.968 -12.012 0.50 25.73 ? 104 ALA F N     1 
ATOM   14809 N  N     B ALA C 3 104 ? 64.851  -17.183 -11.879 0.50 26.44 ? 104 ALA F N     1 
ATOM   14810 C  CA    A ALA C 3 104 ? 63.814  -16.104 -11.425 0.50 28.43 ? 104 ALA F CA    1 
ATOM   14811 C  CA    B ALA C 3 104 ? 63.875  -16.255 -11.324 0.50 28.81 ? 104 ALA F CA    1 
ATOM   14812 C  C     A ALA C 3 104 ? 64.215  -15.653 -10.024 0.50 28.30 ? 104 ALA F C     1 
ATOM   14813 C  C     B ALA C 3 104 ? 64.254  -15.902 -9.892  0.50 27.90 ? 104 ALA F C     1 
ATOM   14814 O  O     A ALA C 3 104 ? 64.727  -16.437 -9.219  0.50 24.22 ? 104 ALA F O     1 
ATOM   14815 O  O     B ALA C 3 104 ? 64.625  -16.775 -9.102  0.50 24.32 ? 104 ALA F O     1 
ATOM   14816 C  CB    A ALA C 3 104 ? 62.467  -16.824 -11.372 0.50 30.89 ? 104 ALA F CB    1 
ATOM   14817 C  CB    B ALA C 3 104 ? 62.473  -16.866 -11.369 0.50 30.89 ? 104 ALA F CB    1 
ATOM   14818 N  N     A ASP C 3 105 ? 63.980  -14.373 -9.743  0.50 29.20 ? 105 ASP F N     1 
ATOM   14819 N  N     B ASP C 3 105 ? 64.202  -14.611 -9.573  0.50 28.07 ? 105 ASP F N     1 
ATOM   14820 C  CA    A ASP C 3 105 ? 64.188  -13.810 -8.413  0.50 26.85 ? 105 ASP F CA    1 
ATOM   14821 C  CA    B ASP C 3 105 ? 64.518  -14.135 -8.231  0.50 26.61 ? 105 ASP F CA    1 
ATOM   14822 C  C     A ASP C 3 105 ? 63.071  -14.297 -7.495  0.50 26.14 ? 105 ASP F C     1 
ATOM   14823 C  C     B ASP C 3 105 ? 63.321  -14.419 -7.332  0.50 26.49 ? 105 ASP F C     1 
ATOM   14824 O  O     A ASP C 3 105 ? 61.905  -13.935 -7.679  0.50 27.14 ? 105 ASP F O     1 
ATOM   14825 O  O     B ASP C 3 105 ? 62.283  -13.759 -7.439  0.50 26.26 ? 105 ASP F O     1 
ATOM   14826 C  CB    A ASP C 3 105 ? 64.215  -12.286 -8.500  0.50 26.54 ? 105 ASP F CB    1 
ATOM   14827 C  CB    B ASP C 3 105 ? 64.865  -12.648 -8.260  0.50 23.93 ? 105 ASP F CB    1 
ATOM   14828 C  CG    A ASP C 3 105 ? 64.491  -11.609 -7.160  0.50 24.79 ? 105 ASP F CG    1 
ATOM   14829 C  CG    B ASP C 3 105 ? 65.314  -12.113 -6.902  0.50 32.15 ? 105 ASP F CG    1 
ATOM   14830 O  OD1   A ASP C 3 105 ? 64.503  -12.287 -6.108  0.50 27.54 ? 105 ASP F OD1   1 
ATOM   14831 O  OD1   B ASP C 3 105 ? 65.186  -12.830 -5.882  0.50 29.65 ? 105 ASP F OD1   1 
ATOM   14832 O  OD2   A ASP C 3 105 ? 64.706  -10.377 -7.167  0.50 29.31 ? 105 ASP F OD2   1 
ATOM   14833 O  OD2   B ASP C 3 105 ? 65.808  -10.963 -6.858  0.50 34.24 ? 105 ASP F OD2   1 
ATOM   14834 N  N     A VAL C 3 106 ? 63.426  -15.110 -6.497  0.50 27.87 ? 106 VAL F N     1 
ATOM   14835 N  N     B VAL C 3 106 ? 63.469  -15.403 -6.441  0.50 27.98 ? 106 VAL F N     1 
ATOM   14836 C  CA    A VAL C 3 106 ? 62.411  -15.726 -5.649  0.50 26.17 ? 106 VAL F CA    1 
ATOM   14837 C  CA    B VAL C 3 106 ? 62.377  -15.816 -5.568  0.50 26.25 ? 106 VAL F CA    1 
ATOM   14838 C  C     A VAL C 3 106 ? 61.804  -14.707 -4.691  0.50 28.37 ? 106 VAL F C     1 
ATOM   14839 C  C     B VAL C 3 106 ? 61.957  -14.698 -4.622  0.50 28.07 ? 106 VAL F C     1 
ATOM   14840 O  O     A VAL C 3 106 ? 60.642  -14.842 -4.284  0.50 27.53 ? 106 VAL F O     1 
ATOM   14841 O  O     B VAL C 3 106 ? 60.827  -14.702 -4.120  0.50 27.78 ? 106 VAL F O     1 
ATOM   14842 C  CB    A VAL C 3 106 ? 63.007  -16.936 -4.897  0.50 29.02 ? 106 VAL F CB    1 
ATOM   14843 C  CB    B VAL C 3 106 ? 62.787  -17.091 -4.791  0.50 29.44 ? 106 VAL F CB    1 
ATOM   14844 C  CG1   A VAL C 3 106 ? 64.106  -16.496 -3.940  0.50 29.48 ? 106 VAL F CG1   1 
ATOM   14845 C  CG1   B VAL C 3 106 ? 63.922  -16.795 -3.822  0.50 28.61 ? 106 VAL F CG1   1 
ATOM   14846 C  CG2   A VAL C 3 106 ? 61.919  -17.705 -4.157  0.50 30.39 ? 106 VAL F CG2   1 
ATOM   14847 C  CG2   B VAL C 3 106 ? 61.592  -17.700 -4.066  0.50 29.92 ? 106 VAL F CG2   1 
ATOM   14848 N  N     A ASN C 3 107 ? 62.555  -13.668 -4.330  0.50 26.25 ? 107 ASN F N     1 
ATOM   14849 N  N     B ASN C 3 107 ? 62.829  -13.721 -4.386  0.50 26.33 ? 107 ASN F N     1 
ATOM   14850 C  CA    A ASN C 3 107 ? 62.084  -12.651 -3.399  0.50 27.28 ? 107 ASN F CA    1 
ATOM   14851 C  CA    B ASN C 3 107 ? 62.550  -12.628 -3.467  0.50 27.86 ? 107 ASN F CA    1 
ATOM   14852 C  C     A ASN C 3 107 ? 61.888  -11.294 -4.073  0.50 26.08 ? 107 ASN F C     1 
ATOM   14853 C  C     B ASN C 3 107 ? 62.200  -11.325 -4.180  0.50 25.45 ? 107 ASN F C     1 
ATOM   14854 O  O     A ASN C 3 107 ? 62.045  -10.251 -3.433  0.50 28.53 ? 107 ASN F O     1 
ATOM   14855 O  O     B ASN C 3 107 ? 62.367  -10.248 -3.598  0.50 29.29 ? 107 ASN F O     1 
ATOM   14856 C  CB    A ASN C 3 107 ? 63.045  -12.535 -2.218  0.50 28.51 ? 107 ASN F CB    1 
ATOM   14857 C  CB    B ASN C 3 107 ? 63.742  -12.427 -2.532  0.50 26.09 ? 107 ASN F CB    1 
ATOM   14858 C  CG    A ASN C 3 107 ? 63.048  -13.778 -1.344  0.50 26.82 ? 107 ASN F CG    1 
ATOM   14859 C  CG    B ASN C 3 107 ? 63.890  -13.560 -1.538  0.50 31.95 ? 107 ASN F CG    1 
ATOM   14860 O  OD1   A ASN C 3 107 ? 61.995  -14.258 -0.931  0.50 28.19 ? 107 ASN F OD1   1 
ATOM   14861 O  OD1   B ASN C 3 107 ? 62.911  -14.219 -1.183  0.50 25.00 ? 107 ASN F OD1   1 
ATOM   14862 N  ND2   A ASN C 3 107 ? 64.236  -14.307 -1.063  0.50 29.42 ? 107 ASN F ND2   1 
ATOM   14863 N  ND2   B ASN C 3 107 ? 65.115  -13.799 -1.088  0.50 30.26 ? 107 ASN F ND2   1 
ATOM   14864 N  N     A ALA C 3 108 ? 61.542  -11.291 -5.361  0.50 25.19 ? 108 ALA F N     1 
ATOM   14865 N  N     B ALA C 3 108 ? 61.711  -11.399 -5.420  0.50 24.69 ? 108 ALA F N     1 
ATOM   14866 C  CA    A ALA C 3 108 ? 61.191  -10.046 -6.032  0.50 25.89 ? 108 ALA F CA    1 
ATOM   14867 C  CA    B ALA C 3 108 ? 61.317  -10.193 -6.137  0.50 25.75 ? 108 ALA F CA    1 
ATOM   14868 C  C     A ALA C 3 108 ? 59.936  -9.444  -5.405  0.50 27.20 ? 108 ALA F C     1 
ATOM   14869 C  C     B ALA C 3 108 ? 60.154  -9.505  -5.429  0.50 27.12 ? 108 ALA F C     1 
ATOM   14870 O  O     A ALA C 3 108 ? 59.047  -10.157 -4.931  0.50 23.63 ? 108 ALA F O     1 
ATOM   14871 O  O     B ALA C 3 108 ? 59.252  -10.157 -4.895  0.50 24.33 ? 108 ALA F O     1 
ATOM   14872 C  CB    A ALA C 3 108 ? 60.979  -10.283 -7.529  0.50 24.58 ? 108 ALA F CB    1 
ATOM   14873 C  CB    B ALA C 3 108 ? 60.936  -10.526 -7.581  0.50 24.75 ? 108 ALA F CB    1 
ATOM   14874 N  N     A VAL C 3 109 ? 59.864  -8.115  -5.410  0.50 27.37 ? 109 VAL F N     1 
ATOM   14875 N  N     B VAL C 3 109 ? 60.178  -8.174  -5.434  0.50 28.21 ? 109 VAL F N     1 
ATOM   14876 C  CA    A VAL C 3 109 ? 58.838  -7.376  -4.682  0.50 28.10 ? 109 VAL F CA    1 
ATOM   14877 C  CA    B VAL C 3 109 ? 59.226  -7.351  -4.698  0.50 27.85 ? 109 VAL F CA    1 
ATOM   14878 C  C     A VAL C 3 109 ? 58.131  -6.435  -5.649  0.50 30.32 ? 109 VAL F C     1 
ATOM   14879 C  C     B VAL C 3 109 ? 58.502  -6.442  -5.683  0.50 31.32 ? 109 VAL F C     1 
ATOM   14880 O  O     A VAL C 3 109 ? 58.771  -5.566  -6.255  0.50 29.74 ? 109 VAL F O     1 
ATOM   14881 O  O     B VAL C 3 109 ? 59.138  -5.824  -6.544  0.50 30.97 ? 109 VAL F O     1 
ATOM   14882 C  CB    A VAL C 3 109 ? 59.436  -6.589  -3.502  0.50 27.99 ? 109 VAL F CB    1 
ATOM   14883 C  CB    B VAL C 3 109 ? 59.931  -6.522  -3.607  0.50 27.69 ? 109 VAL F CB    1 
ATOM   14884 C  CG1   A VAL C 3 109 ? 58.375  -5.725  -2.848  0.50 32.47 ? 109 VAL F CG1   1 
ATOM   14885 C  CG1   B VAL C 3 109 ? 58.920  -5.748  -2.784  0.50 32.35 ? 109 VAL F CG1   1 
ATOM   14886 C  CG2   A VAL C 3 109 ? 60.056  -7.539  -2.484  0.50 26.35 ? 109 VAL F CG2   1 
ATOM   14887 C  CG2   B VAL C 3 109 ? 60.776  -7.422  -2.715  0.50 27.75 ? 109 VAL F CG2   1 
ATOM   14888 N  N     A ASP C 3 110 ? 56.815  -6.592  -5.777  0.50 25.21 ? 110 ASP F N     1 
ATOM   14889 N  N     B ASP C 3 110 ? 57.180  -6.351  -5.546  0.50 24.45 ? 110 ASP F N     1 
ATOM   14890 C  CA    A ASP C 3 110 ? 56.026  -5.750  -6.666  0.50 26.88 ? 110 ASP F CA    1 
ATOM   14891 C  CA    B ASP C 3 110 ? 56.362  -5.506  -6.399  0.50 26.59 ? 110 ASP F CA    1 
ATOM   14892 C  C     A ASP C 3 110 ? 55.680  -4.437  -5.958  0.50 24.94 ? 110 ASP F C     1 
ATOM   14893 C  C     B ASP C 3 110 ? 56.018  -4.207  -5.663  0.50 24.94 ? 110 ASP F C     1 
ATOM   14894 O  O     A ASP C 3 110 ? 56.147  -4.156  -4.850  0.50 27.84 ? 110 ASP F O     1 
ATOM   14895 O  O     B ASP C 3 110 ? 56.512  -3.940  -4.562  0.50 28.27 ? 110 ASP F O     1 
ATOM   14896 C  CB    A ASP C 3 110 ? 54.793  -6.510  -7.161  0.50 24.40 ? 110 ASP F CB    1 
ATOM   14897 C  CB    B ASP C 3 110 ? 55.121  -6.282  -6.869  0.50 24.34 ? 110 ASP F CB    1 
ATOM   14898 C  CG    A ASP C 3 110 ? 53.827  -6.899  -6.038  0.50 26.46 ? 110 ASP F CG    1 
ATOM   14899 C  CG    B ASP C 3 110 ? 54.191  -6.695  -5.723  0.50 27.33 ? 110 ASP F CG    1 
ATOM   14900 O  OD1   A ASP C 3 110 ? 53.991  -6.438  -4.888  0.50 22.48 ? 110 ASP F OD1   1 
ATOM   14901 O  OD1   B ASP C 3 110 ? 54.126  -5.996  -4.692  0.50 21.58 ? 110 ASP F OD1   1 
ATOM   14902 O  OD2   A ASP C 3 110 ? 52.889  -7.675  -6.324  0.50 22.96 ? 110 ASP F OD2   1 
ATOM   14903 O  OD2   B ASP C 3 110 ? 53.516  -7.734  -5.863  0.50 23.17 ? 110 ASP F OD2   1 
ATOM   14904 N  N     A THR C 3 111 ? 54.841  -3.616  -6.589  0.50 27.28 ? 111 THR F N     1 
ATOM   14905 N  N     B THR C 3 111 ? 55.152  -3.390  -6.268  0.50 26.09 ? 111 THR F N     1 
ATOM   14906 C  CA    A THR C 3 111 ? 54.553  -2.280  -6.084  0.50 28.28 ? 111 THR F CA    1 
ATOM   14907 C  CA    B THR C 3 111 ? 54.851  -2.081  -5.700  0.50 27.61 ? 111 THR F CA    1 
ATOM   14908 C  C     A THR C 3 111 ? 53.620  -2.284  -4.878  0.50 26.12 ? 111 THR F C     1 
ATOM   14909 C  C     B THR C 3 111 ? 54.063  -2.174  -4.398  0.50 27.40 ? 111 THR F C     1 
ATOM   14910 O  O     A THR C 3 111 ? 53.334  -1.212  -4.336  0.50 31.58 ? 111 THR F O     1 
ATOM   14911 O  O     B THR C 3 111 ? 54.132  -1.247  -3.584  0.50 30.14 ? 111 THR F O     1 
ATOM   14912 C  CB    A THR C 3 111 ? 53.961  -1.409  -7.198  0.50 25.24 ? 111 THR F CB    1 
ATOM   14913 C  CB    B THR C 3 111 ? 54.094  -1.217  -6.714  0.50 27.24 ? 111 THR F CB    1 
ATOM   14914 O  OG1   A THR C 3 111 ? 54.021  -0.032  -6.810  0.50 40.99 ? 111 THR F OG1   1 
ATOM   14915 O  OG1   B THR C 3 111 ? 53.709  0.016   -6.094  0.50 37.92 ? 111 THR F OG1   1 
ATOM   14916 C  CG2   A THR C 3 111 ? 52.516  -1.779  -7.461  0.50 27.98 ? 111 THR F CG2   1 
ATOM   14917 C  CG2   B THR C 3 111 ? 52.852  -1.928  -7.218  0.50 27.99 ? 111 THR F CG2   1 
ATOM   14918 N  N     A TRP C 3 112 ? 53.143  -3.451  -4.447  0.50 25.33 ? 112 TRP F N     1 
ATOM   14919 N  N     B TRP C 3 112 ? 53.333  -3.265  -4.172  0.50 25.87 ? 112 TRP F N     1 
ATOM   14920 C  CA    A TRP C 3 112 ? 52.352  -3.570  -3.229  0.50 28.77 ? 112 TRP F CA    1 
ATOM   14921 C  CA    B TRP C 3 112 ? 52.662  -3.463  -2.891  0.50 27.42 ? 112 TRP F CA    1 
ATOM   14922 C  C     A TRP C 3 112 ? 53.145  -4.198  -2.093  0.50 30.00 ? 112 TRP F C     1 
ATOM   14923 C  C     B TRP C 3 112 ? 53.576  -4.097  -1.850  0.50 30.92 ? 112 TRP F C     1 
ATOM   14924 O  O     A TRP C 3 112 ? 52.565  -4.550  -1.060  0.50 31.09 ? 112 TRP F O     1 
ATOM   14925 O  O     B TRP C 3 112 ? 53.111  -4.416  -0.748  0.50 27.44 ? 112 TRP F O     1 
ATOM   14926 C  CB    A TRP C 3 112 ? 51.079  -4.376  -3.499  0.50 27.47 ? 112 TRP F CB    1 
ATOM   14927 C  CB    B TRP C 3 112 ? 51.409  -4.329  -3.071  0.50 25.75 ? 112 TRP F CB    1 
ATOM   14928 C  CG    A TRP C 3 112 ? 50.134  -3.674  -4.421  0.50 26.26 ? 112 TRP F CG    1 
ATOM   14929 C  CG    B TRP C 3 112 ? 50.471  -3.813  -4.119  0.50 27.13 ? 112 TRP F CG    1 
ATOM   14930 C  CD1   A TRP C 3 112 ? 49.263  -2.685  -4.090  0.50 26.38 ? 112 TRP F CD1   1 
ATOM   14931 C  CD1   B TRP C 3 112 ? 49.577  -2.791  -3.986  0.50 26.05 ? 112 TRP F CD1   1 
ATOM   14932 C  CD2   A TRP C 3 112 ? 49.971  -3.898  -5.827  0.50 28.52 ? 112 TRP F CD2   1 
ATOM   14933 C  CD2   B TRP C 3 112 ? 50.330  -4.297  -5.460  0.50 27.02 ? 112 TRP F CD2   1 
ATOM   14934 N  NE1   A TRP C 3 112 ? 48.559  -2.277  -5.198  0.50 29.55 ? 112 TRP F NE1   1 
ATOM   14935 N  NE1   B TRP C 3 112 ? 48.891  -2.607  -5.161  0.50 28.84 ? 112 TRP F NE1   1 
ATOM   14936 C  CE2   A TRP C 3 112 ? 48.979  -3.004  -6.280  0.50 26.27 ? 112 TRP F CE2   1 
ATOM   14937 C  CE2   B TRP C 3 112 ? 49.335  -3.518  -6.082  0.50 28.35 ? 112 TRP F CE2   1 
ATOM   14938 C  CE3   A TRP C 3 112 ? 50.569  -4.763  -6.747  0.50 30.94 ? 112 TRP F CE3   1 
ATOM   14939 C  CE3   B TRP C 3 112 ? 50.953  -5.311  -6.196  0.50 27.76 ? 112 TRP F CE3   1 
ATOM   14940 C  CZ2   A TRP C 3 112 ? 48.566  -2.956  -7.610  0.50 27.84 ? 112 TRP F CZ2   1 
ATOM   14941 C  CZ2   B TRP C 3 112 ? 48.947  -3.720  -7.406  0.50 30.48 ? 112 TRP F CZ2   1 
ATOM   14942 C  CZ3   A TRP C 3 112 ? 50.161  -4.713  -8.069  0.50 29.33 ? 112 TRP F CZ3   1 
ATOM   14943 C  CZ3   B TRP C 3 112 ? 50.564  -5.511  -7.511  0.50 28.97 ? 112 TRP F CZ3   1 
ATOM   14944 C  CH2   A TRP C 3 112 ? 49.170  -3.816  -8.488  0.50 27.51 ? 112 TRP F CH2   1 
ATOM   14945 C  CH2   B TRP C 3 112 ? 49.571  -4.719  -8.102  0.50 29.62 ? 112 TRP F CH2   1 
ATOM   14946 N  N     A GLY C 3 113 ? 54.460  -4.335  -2.253  0.50 30.18 ? 113 GLY F N     1 
ATOM   14947 N  N     B GLY C 3 113 ? 54.857  -4.280  -2.168  0.50 29.32 ? 113 GLY F N     1 
ATOM   14948 C  CA    A GLY C 3 113 ? 55.286  -4.971  -1.253  0.50 26.77 ? 113 GLY F CA    1 
ATOM   14949 C  CA    B GLY C 3 113 ? 55.775  -4.951  -1.276  0.50 26.08 ? 113 GLY F CA    1 
ATOM   14950 C  C     A GLY C 3 113 ? 55.209  -6.479  -1.221  0.50 27.98 ? 113 GLY F C     1 
ATOM   14951 C  C     B GLY C 3 113 ? 55.614  -6.451  -1.199  0.50 28.38 ? 113 GLY F C     1 
ATOM   14952 O  O     A GLY C 3 113 ? 55.861  -7.095  -0.369  0.50 31.16 ? 113 GLY F O     1 
ATOM   14953 O  O     B GLY C 3 113 ? 56.143  -7.064  -0.267  0.50 31.95 ? 113 GLY F O     1 
ATOM   14954 N  N     A ASP C 3 114 ? 54.439  -7.094  -2.115  0.50 26.96 ? 114 ASP F N     1 
ATOM   14955 N  N     B ASP C 3 114 ? 54.907  -7.063  -2.145  0.50 30.66 ? 114 ASP F N     1 
ATOM   14956 C  CA    A ASP C 3 114 ? 54.294  -8.544  -2.124  0.50 23.14 ? 114 ASP F CA    1 
ATOM   14957 C  CA    B ASP C 3 114 ? 54.622  -8.490  -2.102  0.50 24.22 ? 114 ASP F CA    1 
ATOM   14958 C  C     A ASP C 3 114 ? 55.473  -9.215  -2.818  0.50 26.15 ? 114 ASP F C     1 
ATOM   14959 C  C     B ASP C 3 114 ? 55.686  -9.292  -2.842  0.50 25.95 ? 114 ASP F C     1 
ATOM   14960 O  O     A ASP C 3 114 ? 55.891  -8.800  -3.904  0.50 26.48 ? 114 ASP F O     1 
ATOM   14961 O  O     B ASP C 3 114 ? 56.194  -8.867  -3.882  0.50 26.71 ? 114 ASP F O     1 
ATOM   14962 C  CB    A ASP C 3 114 ? 52.993  -8.945  -2.819  0.50 24.70 ? 114 ASP F CB    1 
ATOM   14963 C  CB    B ASP C 3 114 ? 53.248  -8.780  -2.706  0.50 23.98 ? 114 ASP F CB    1 
ATOM   14964 C  CG    A ASP C 3 114 ? 51.782  -8.832  -1.907  0.50 23.36 ? 114 ASP F CG    1 
ATOM   14965 C  CG    B ASP C 3 114 ? 52.110  -8.231  -1.860  0.50 25.46 ? 114 ASP F CG    1 
ATOM   14966 O  OD1   A ASP C 3 114 ? 51.928  -9.075  -0.689  0.50 21.60 ? 114 ASP F OD1   1 
ATOM   14967 O  OD1   B ASP C 3 114 ? 52.267  -8.176  -0.626  0.50 24.08 ? 114 ASP F OD1   1 
ATOM   14968 O  OD2   A ASP C 3 114 ? 50.690  -8.509  -2.414  0.50 23.07 ? 114 ASP F OD2   1 
ATOM   14969 O  OD2   B ASP C 3 114 ? 51.069  -7.853  -2.429  0.50 25.28 ? 114 ASP F OD2   1 
ATOM   14970 N  N     A THR C 3 115 ? 56.007  -10.245 -2.180  0.50 24.64 ? 115 THR F N     1 
ATOM   14971 N  N     B THR C 3 115 ? 56.005  -10.455 -2.300  0.50 24.80 ? 115 THR F N     1 
ATOM   14972 C  CA    A THR C 3 115 ? 56.842  -11.242 -2.830  0.50 26.10 ? 115 THR F CA    1 
ATOM   14973 C  CA    B THR C 3 115 ? 56.854  -11.458 -2.916  0.50 26.10 ? 115 THR F CA    1 
ATOM   14974 C  C     A THR C 3 115 ? 55.953  -12.336 -3.399  0.50 28.06 ? 115 THR F C     1 
ATOM   14975 C  C     B THR C 3 115 ? 56.006  -12.622 -3.409  0.50 27.48 ? 115 THR F C     1 
ATOM   14976 O  O     A THR C 3 115 ? 54.753  -12.382 -3.118  0.50 26.33 ? 115 THR F O     1 
ATOM   14977 O  O     B THR C 3 115 ? 54.838  -12.759 -3.029  0.50 26.27 ? 115 THR F O     1 
ATOM   14978 C  CB    A THR C 3 115 ? 57.835  -11.816 -1.820  0.50 27.63 ? 115 THR F CB    1 
ATOM   14979 C  CB    B THR C 3 115 ? 57.891  -11.967 -1.906  0.50 27.51 ? 115 THR F CB    1 
ATOM   14980 O  OG1   A THR C 3 115 ? 57.168  -12.776 -0.988  0.50 23.79 ? 115 THR F OG1   1 
ATOM   14981 O  OG1   B THR C 3 115 ? 57.233  -12.283 -0.670  0.50 24.85 ? 115 THR F OG1   1 
ATOM   14982 C  CG2   A THR C 3 115 ? 58.400  -10.710 -0.938  0.50 25.99 ? 115 THR F CG2   1 
ATOM   14983 C  CG2   B THR C 3 115 ? 58.965  -10.925 -1.658  0.50 24.86 ? 115 THR F CG2   1 
ATOM   14984 N  N     A PRO C 3 116 ? 56.493  -13.236 -4.229  0.50 25.09 ? 116 PRO F N     1 
ATOM   14985 N  N     B PRO C 3 116 ? 56.554  -13.481 -4.272  0.50 24.97 ? 116 PRO F N     1 
ATOM   14986 C  CA    A PRO C 3 116 ? 55.671  -14.381 -4.660  0.50 25.28 ? 116 PRO F CA    1 
ATOM   14987 C  CA    B PRO C 3 116 ? 55.843  -14.728 -4.594  0.50 26.54 ? 116 PRO F CA    1 
ATOM   14988 C  C     A PRO C 3 116 ? 55.152  -15.210 -3.493  0.50 25.57 ? 116 PRO F C     1 
ATOM   14989 C  C     B PRO C 3 116 ? 55.482  -15.554 -3.361  0.50 23.10 ? 116 PRO F C     1 
ATOM   14990 O  O     A PRO C 3 116 ? 53.996  -15.663 -3.516  0.50 21.74 ? 116 PRO F O     1 
ATOM   14991 O  O     B PRO C 3 116 ? 54.522  -16.336 -3.413  0.50 23.48 ? 116 PRO F O     1 
ATOM   14992 C  CB    A PRO C 3 116 ? 56.631  -15.177 -5.555  0.50 28.59 ? 116 PRO F CB    1 
ATOM   14993 C  CB    B PRO C 3 116 ? 56.833  -15.469 -5.502  0.50 27.80 ? 116 PRO F CB    1 
ATOM   14994 C  CG    A PRO C 3 116 ? 57.557  -14.152 -6.095  0.50 24.30 ? 116 PRO F CG    1 
ATOM   14995 C  CG    B PRO C 3 116 ? 57.637  -14.393 -6.129  0.50 24.28 ? 116 PRO F CG    1 
ATOM   14996 C  CD    A PRO C 3 116 ? 57.760  -13.159 -4.982  0.50 25.92 ? 116 PRO F CD    1 
ATOM   14997 C  CD    B PRO C 3 116 ? 57.770  -13.312 -5.092  0.50 25.96 ? 116 PRO F CD    1 
ATOM   14998 N  N     A LEU C 3 117 ? 55.975  -15.398 -2.457  0.50 24.73 ? 117 LEU F N     1 
ATOM   14999 N  N     B LEU C 3 117 ? 56.204  -15.390 -2.248  0.50 24.67 ? 117 LEU F N     1 
ATOM   15000 C  CA    A LEU C 3 117 ? 55.539  -16.158 -1.290  0.50 25.15 ? 117 LEU F CA    1 
ATOM   15001 C  CA    B LEU C 3 117 ? 55.829  -16.086 -1.022  0.50 23.85 ? 117 LEU F CA    1 
ATOM   15002 C  C     A LEU C 3 117 ? 54.296  -15.539 -0.659  0.50 25.98 ? 117 LEU F C     1 
ATOM   15003 C  C     B LEU C 3 117 ? 54.519  -15.541 -0.467  0.50 26.23 ? 117 LEU F C     1 
ATOM   15004 O  O     A LEU C 3 117 ? 53.371  -16.261 -0.268  0.50 27.37 ? 117 LEU F O     1 
ATOM   15005 O  O     B LEU C 3 117 ? 53.633  -16.312 -0.086  0.50 27.51 ? 117 LEU F O     1 
ATOM   15006 C  CB    A LEU C 3 117 ? 56.673  -16.253 -0.273  0.50 20.75 ? 117 LEU F CB    1 
ATOM   15007 C  CB    B LEU C 3 117 ? 56.942  -15.968 0.017   0.50 21.61 ? 117 LEU F CB    1 
ATOM   15008 C  CG    A LEU C 3 117 ? 56.330  -16.999 1.021   0.50 26.38 ? 117 LEU F CG    1 
ATOM   15009 C  CG    B LEU C 3 117 ? 56.702  -16.736 1.319   0.50 25.79 ? 117 LEU F CG    1 
ATOM   15010 C  CD1   A LEU C 3 117 ? 55.983  -18.450 0.735   0.50 22.46 ? 117 LEU F CD1   1 
ATOM   15011 C  CD1   B LEU C 3 117 ? 56.587  -18.221 1.027   0.50 21.92 ? 117 LEU F CD1   1 
ATOM   15012 C  CD2   A LEU C 3 117 ? 57.465  -16.901 2.025   0.50 26.17 ? 117 LEU F CD2   1 
ATOM   15013 C  CD2   B LEU C 3 117 ? 57.813  -16.467 2.313   0.50 28.42 ? 117 LEU F CD2   1 
ATOM   15014 N  N     A HIS C 3 118 ? 54.254  -14.204 -0.555  0.50 26.48 ? 118 HIS F N     1 
ATOM   15015 N  N     B HIS C 3 118 ? 54.383  -14.211 -0.407  0.50 26.38 ? 118 HIS F N     1 
ATOM   15016 C  CA    A HIS C 3 118 ? 53.042  -13.527 -0.098  0.50 24.29 ? 118 HIS F CA    1 
ATOM   15017 C  CA    B HIS C 3 118 ? 53.135  -13.607 0.052   0.50 24.28 ? 118 HIS F CA    1 
ATOM   15018 C  C     A HIS C 3 118 ? 51.818  -14.008 -0.865  0.50 25.14 ? 118 HIS F C     1 
ATOM   15019 C  C     B HIS C 3 118 ? 51.954  -14.091 -0.779  0.50 25.03 ? 118 HIS F C     1 
ATOM   15020 O  O     A HIS C 3 118 ? 50.765  -14.268 -0.275  0.50 25.43 ? 118 HIS F O     1 
ATOM   15021 O  O     B HIS C 3 118 ? 50.951  -14.569 -0.237  0.50 25.41 ? 118 HIS F O     1 
ATOM   15022 C  CB    A HIS C 3 118 ? 53.171  -12.009 -0.260  0.50 21.80 ? 118 HIS F CB    1 
ATOM   15023 C  CB    B HIS C 3 118 ? 53.219  -12.080 -0.015  0.50 21.14 ? 118 HIS F CB    1 
ATOM   15024 C  CG    A HIS C 3 118 ? 53.972  -11.333 0.809   0.50 25.43 ? 118 HIS F CG    1 
ATOM   15025 C  CG    B HIS C 3 118 ? 54.146  -11.466 0.987   0.50 26.21 ? 118 HIS F CG    1 
ATOM   15026 N  ND1   A HIS C 3 118 ? 55.139  -10.647 0.543   0.50 23.20 ? 118 HIS F ND1   1 
ATOM   15027 N  ND1   B HIS C 3 118 ? 55.500  -11.329 0.766   0.50 25.68 ? 118 HIS F ND1   1 
ATOM   15028 C  CD2   A HIS C 3 118 ? 53.759  -11.205 2.140   0.50 24.86 ? 118 HIS F CD2   1 
ATOM   15029 C  CD2   B HIS C 3 118 ? 53.907  -10.927 2.206   0.50 25.05 ? 118 HIS F CD2   1 
ATOM   15030 C  CE1   A HIS C 3 118 ? 55.620  -10.144 1.665   0.50 28.22 ? 118 HIS F CE1   1 
ATOM   15031 C  CE1   B HIS C 3 118 ? 56.057  -10.743 1.810   0.50 25.87 ? 118 HIS F CE1   1 
ATOM   15032 N  NE2   A HIS C 3 118 ? 54.798  -10.463 2.649   0.50 27.67 ? 118 HIS F NE2   1 
ATOM   15033 N  NE2   B HIS C 3 118 ? 55.112  -10.488 2.698   0.50 28.89 ? 118 HIS F NE2   1 
ATOM   15034 N  N     A LEU C 3 119 ? 51.943  -14.140 -2.189  0.50 24.21 ? 119 LEU F N     1 
ATOM   15035 N  N     B LEU C 3 119 ? 52.065  -13.983 -2.107  0.50 24.26 ? 119 LEU F N     1 
ATOM   15036 C  CA    A LEU C 3 119 ? 50.787  -14.457 -3.019  0.50 23.98 ? 119 LEU F CA    1 
ATOM   15037 C  CA    B LEU C 3 119 ? 50.922  -14.249 -2.974  0.50 24.69 ? 119 LEU F CA    1 
ATOM   15038 C  C     A LEU C 3 119 ? 50.399  -15.928 -2.924  0.50 25.20 ? 119 LEU F C     1 
ATOM   15039 C  C     B LEU C 3 119 ? 50.489  -15.709 -2.906  0.50 24.34 ? 119 LEU F C     1 
ATOM   15040 O  O     A LEU C 3 119 ? 49.207  -16.258 -2.921  0.50 24.73 ? 119 LEU F O     1 
ATOM   15041 O  O     B LEU C 3 119 ? 49.287  -16.004 -2.913  0.50 25.78 ? 119 LEU F O     1 
ATOM   15042 C  CB    A LEU C 3 119 ? 51.069  -14.057 -4.469  0.50 23.68 ? 119 LEU F CB    1 
ATOM   15043 C  CB    B LEU C 3 119 ? 51.254  -13.842 -4.410  0.50 23.53 ? 119 LEU F CB    1 
ATOM   15044 C  CG    A LEU C 3 119 ? 51.409  -12.575 -4.663  0.50 24.43 ? 119 LEU F CG    1 
ATOM   15045 C  CG    B LEU C 3 119 ? 51.581  -12.356 -4.589  0.50 24.39 ? 119 LEU F CG    1 
ATOM   15046 C  CD1   A LEU C 3 119 ? 51.721  -12.271 -6.117  0.50 27.38 ? 119 LEU F CD1   1 
ATOM   15047 C  CD1   B LEU C 3 119 ? 51.900  -12.038 -6.039  0.50 27.25 ? 119 LEU F CD1   1 
ATOM   15048 C  CD2   A LEU C 3 119 ? 50.282  -11.680 -4.165  0.50 22.58 ? 119 LEU F CD2   1 
ATOM   15049 C  CD2   B LEU C 3 119 ? 50.439  -11.482 -4.094  0.50 21.99 ? 119 LEU F CD2   1 
ATOM   15050 N  N     A ALA C 3 120 ? 51.383  -16.828 -2.851  0.50 23.38 ? 120 ALA F N     1 
ATOM   15051 N  N     B ALA C 3 120 ? 51.446  -16.637 -2.842  0.50 23.35 ? 120 ALA F N     1 
ATOM   15052 C  CA    A ALA C 3 120 ? 51.066  -18.245 -2.705  0.50 26.95 ? 120 ALA F CA    1 
ATOM   15053 C  CA    B ALA C 3 120 ? 51.088  -18.046 -2.716  0.50 26.84 ? 120 ALA F CA    1 
ATOM   15054 C  C     A ALA C 3 120 ? 50.408  -18.541 -1.359  0.50 26.44 ? 120 ALA F C     1 
ATOM   15055 C  C     B ALA C 3 120 ? 50.428  -18.329 -1.369  0.50 26.31 ? 120 ALA F C     1 
ATOM   15056 O  O     A ALA C 3 120 ? 49.608  -19.477 -1.250  0.50 24.05 ? 120 ALA F O     1 
ATOM   15057 O  O     B ALA C 3 120 ? 49.466  -19.102 -1.289  0.50 22.70 ? 120 ALA F O     1 
ATOM   15058 C  CB    A ALA C 3 120 ? 52.333  -19.082 -2.879  0.50 23.50 ? 120 ALA F CB    1 
ATOM   15059 C  CB    B ALA C 3 120 ? 52.330  -18.916 -2.907  0.50 23.25 ? 120 ALA F CB    1 
ATOM   15060 N  N     A ALA C 3 121 ? 50.724  -17.757 -0.328  0.50 25.66 ? 121 ALA F N     1 
ATOM   15061 N  N     B ALA C 3 121 ? 50.929  -17.709 -0.301  0.50 25.80 ? 121 ALA F N     1 
ATOM   15062 C  CA    A ALA C 3 121 ? 50.102  -17.970 0.975   0.50 19.59 ? 121 ALA F CA    1 
ATOM   15063 C  CA    B ALA C 3 121 ? 50.335  -17.906 1.018   0.50 20.11 ? 121 ALA F CA    1 
ATOM   15064 C  C     A ALA C 3 121 ? 48.659  -17.482 0.983   0.50 24.30 ? 121 ALA F C     1 
ATOM   15065 C  C     B ALA C 3 121 ? 48.915  -17.358 1.063   0.50 24.18 ? 121 ALA F C     1 
ATOM   15066 O  O     A ALA C 3 121 ? 47.769  -18.167 1.499   0.50 28.19 ? 121 ALA F O     1 
ATOM   15067 O  O     B ALA C 3 121 ? 48.001  -18.013 1.577   0.50 28.04 ? 121 ALA F O     1 
ATOM   15068 C  CB    A ALA C 3 121 ? 50.914  -17.266 2.061   0.50 21.86 ? 121 ALA F CB    1 
ATOM   15069 C  CB    B ALA C 3 121 ? 51.204  -17.241 2.085   0.50 21.97 ? 121 ALA F CB    1 
ATOM   15070 N  N     A ILE C 3 122 ? 48.414  -16.303 0.406   0.50 21.57 ? 122 ILE F N     1 
ATOM   15071 N  N     B ILE C 3 122 ? 48.716  -16.153 0.525   0.50 22.19 ? 122 ILE F N     1 
ATOM   15072 C  CA    A ILE C 3 122 ? 47.087  -15.697 0.408   0.50 24.74 ? 122 ILE F CA    1 
ATOM   15073 C  CA    B ILE C 3 122 ? 47.400  -15.519 0.548   0.50 24.54 ? 122 ILE F CA    1 
ATOM   15074 C  C     A ILE C 3 122 ? 46.066  -16.582 -0.297  0.50 29.21 ? 122 ILE F C     1 
ATOM   15075 C  C     B ILE C 3 122 ? 46.375  -16.382 -0.179  0.50 27.56 ? 122 ILE F C     1 
ATOM   15076 O  O     A ILE C 3 122 ? 44.896  -16.639 0.108   0.50 21.80 ? 122 ILE F O     1 
ATOM   15077 O  O     B ILE C 3 122 ? 45.323  -16.729 0.374   0.50 24.59 ? 122 ILE F O     1 
ATOM   15078 C  CB    A ILE C 3 122 ? 47.169  -14.293 -0.226  0.50 27.55 ? 122 ILE F CB    1 
ATOM   15079 C  CB    B ILE C 3 122 ? 47.481  -14.107 -0.058  0.50 26.79 ? 122 ILE F CB    1 
ATOM   15080 C  CG1   A ILE C 3 122 ? 47.884  -13.329 0.722   0.50 28.67 ? 122 ILE F CG1   1 
ATOM   15081 C  CG1   B ILE C 3 122 ? 48.184  -13.153 0.908   0.50 28.89 ? 122 ILE F CG1   1 
ATOM   15082 C  CG2   A ILE C 3 122 ? 45.788  -13.772 -0.610  0.50 27.62 ? 122 ILE F CG2   1 
ATOM   15083 C  CG2   B ILE C 3 122 ? 46.093  -13.602 -0.437  0.50 28.63 ? 122 ILE F CG2   1 
ATOM   15084 C  CD1   A ILE C 3 122 ? 48.271  -12.017 0.074   0.50 27.76 ? 122 ILE F CD1   1 
ATOM   15085 C  CD1   B ILE C 3 122 ? 48.572  -11.833 0.282   0.50 28.13 ? 122 ILE F CD1   1 
ATOM   15086 N  N     A MET C 3 123 ? 46.485  -17.302 -1.335  0.50 21.01 ? 123 MET F N     1 
ATOM   15087 N  N     B MET C 3 123 ? 46.671  -16.754 -1.421  0.50 24.21 ? 123 MET F N     1 
ATOM   15088 C  CA    A MET C 3 123 ? 45.575  -18.119 -2.123  0.50 19.48 ? 123 MET F CA    1 
ATOM   15089 C  CA    B MET C 3 123 ? 45.724  -17.489 -2.249  0.50 22.68 ? 123 MET F CA    1 
ATOM   15090 C  C     A MET C 3 123 ? 45.578  -19.584 -1.712  0.50 23.38 ? 123 MET F C     1 
ATOM   15091 C  C     B MET C 3 123 ? 45.600  -18.956 -1.863  0.50 21.22 ? 123 MET F C     1 
ATOM   15092 O  O     A MET C 3 123 ? 44.833  -20.376 -2.294  0.50 30.37 ? 123 MET F O     1 
ATOM   15093 O  O     B MET C 3 123 ? 44.816  -19.675 -2.489  0.50 29.11 ? 123 MET F O     1 
ATOM   15094 C  CB    A MET C 3 123 ? 45.916  -17.997 -3.613  0.50 25.68 ? 123 MET F CB    1 
ATOM   15095 C  CB    B MET C 3 123 ? 46.120  -17.373 -3.728  0.50 24.48 ? 123 MET F CB    1 
ATOM   15096 C  CG    A MET C 3 123 ? 45.955  -16.561 -4.121  0.50 23.94 ? 123 MET F CG    1 
ATOM   15097 C  CG    B MET C 3 123 ? 46.088  -15.947 -4.271  0.50 23.37 ? 123 MET F CG    1 
ATOM   15098 S  SD    A MET C 3 123 ? 44.362  -15.731 -3.938  0.50 26.16 ? 123 MET F SD    1 
ATOM   15099 S  SD    B MET C 3 123 ? 44.499  -15.121 -4.016  0.50 26.26 ? 123 MET F SD    1 
ATOM   15100 C  CE    A MET C 3 123 ? 43.361  -16.673 -5.087  0.50 24.97 ? 123 MET F CE    1 
ATOM   15101 C  CE    B MET C 3 123 ? 43.416  -16.150 -5.004  0.50 24.52 ? 123 MET F CE    1 
ATOM   15102 N  N     A GLY C 3 124 ? 46.394  -19.967 -0.734  0.50 25.15 ? 124 GLY F N     1 
ATOM   15103 N  N     B GLY C 3 124 ? 46.356  -19.423 -0.872  0.50 22.61 ? 124 GLY F N     1 
ATOM   15104 C  CA    A GLY C 3 124 ? 46.379  -21.333 -0.251  0.50 27.46 ? 124 GLY F CA    1 
ATOM   15105 C  CA    B GLY C 3 124 ? 46.186  -20.778 -0.385  0.50 27.22 ? 124 GLY F CA    1 
ATOM   15106 C  C     A GLY C 3 124 ? 47.121  -22.336 -1.104  0.50 29.05 ? 124 GLY F C     1 
ATOM   15107 C  C     B GLY C 3 124 ? 46.797  -21.860 -1.246  0.50 29.08 ? 124 GLY F C     1 
ATOM   15108 O  O     A GLY C 3 124 ? 46.876  -23.541 -0.973  0.50 21.49 ? 124 GLY F O     1 
ATOM   15109 O  O     B GLY C 3 124 ? 46.267  -22.976 -1.296  0.50 27.78 ? 124 GLY F O     1 
ATOM   15110 N  N     A HIS C 3 125 ? 48.023  -21.880 -1.979  0.50 31.15 ? 125 HIS F N     1 
ATOM   15111 N  N     B HIS C 3 125 ? 47.901  -21.569 -1.928  0.50 30.44 ? 125 HIS F N     1 
ATOM   15112 C  CA    A HIS C 3 125 ? 48.840  -22.778 -2.797  0.50 29.05 ? 125 HIS F CA    1 
ATOM   15113 C  CA    B HIS C 3 125 ? 48.580  -22.550 -2.773  0.50 28.18 ? 125 HIS F CA    1 
ATOM   15114 C  C     A HIS C 3 125 ? 49.969  -23.348 -1.937  0.50 33.01 ? 125 HIS F C     1 
ATOM   15115 C  C     B HIS C 3 125 ? 49.735  -23.130 -1.962  0.50 32.31 ? 125 HIS F C     1 
ATOM   15116 O  O     A HIS C 3 125 ? 51.150  -23.038 -2.106  0.50 27.18 ? 125 HIS F O     1 
ATOM   15117 O  O     B HIS C 3 125 ? 50.857  -22.620 -1.986  0.50 28.69 ? 125 HIS F O     1 
ATOM   15118 C  CB    A HIS C 3 125 ? 49.398  -22.050 -4.013  0.50 29.83 ? 125 HIS F CB    1 
ATOM   15119 C  CB    B HIS C 3 125 ? 49.040  -21.908 -4.077  0.50 30.78 ? 125 HIS F CB    1 
ATOM   15120 C  CG    A HIS C 3 125 ? 48.365  -21.333 -4.822  0.50 30.07 ? 125 HIS F CG    1 
ATOM   15121 C  CG    B HIS C 3 125 ? 47.914  -21.395 -4.921  0.50 30.97 ? 125 HIS F CG    1 
ATOM   15122 N  ND1   A HIS C 3 125 ? 47.304  -21.978 -5.420  0.50 32.84 ? 125 HIS F ND1   1 
ATOM   15123 N  ND1   B HIS C 3 125 ? 46.715  -22.064 -5.048  0.50 31.90 ? 125 HIS F ND1   1 
ATOM   15124 C  CD2   A HIS C 3 125 ? 48.239  -20.024 -5.145  0.50 22.48 ? 125 HIS F CD2   1 
ATOM   15125 C  CD2   B HIS C 3 125 ? 47.797  -20.271 -5.667  0.50 25.75 ? 125 HIS F CD2   1 
ATOM   15126 C  CE1   A HIS C 3 125 ? 46.563  -21.096 -6.068  0.50 28.00 ? 125 HIS F CE1   1 
ATOM   15127 C  CE1   B HIS C 3 125 ? 45.911  -21.379 -5.843  0.50 23.88 ? 125 HIS F CE1   1 
ATOM   15128 N  NE2   A HIS C 3 125 ? 47.114  -19.904 -5.924  0.50 26.67 ? 125 HIS F NE2   1 
ATOM   15129 N  NE2   B HIS C 3 125 ? 46.544  -20.288 -6.233  0.50 27.16 ? 125 HIS F NE2   1 
ATOM   15130 N  N     A LEU C 3 126 ? 49.579  -24.220 -1.004  0.50 27.70 ? 126 LEU F N     1 
ATOM   15131 N  N     B LEU C 3 126 ? 49.448  -24.223 -1.244  0.50 28.45 ? 126 LEU F N     1 
ATOM   15132 C  CA    A LEU C 3 126 ? 50.526  -24.700 -0.002  0.50 30.09 ? 126 LEU F CA    1 
ATOM   15133 C  CA    B LEU C 3 126 ? 50.402  -24.764 -0.278  0.50 29.92 ? 126 LEU F CA    1 
ATOM   15134 C  C     A LEU C 3 126 ? 51.634  -25.544 -0.618  0.50 30.12 ? 126 LEU F C     1 
ATOM   15135 C  C     B LEU C 3 126 ? 51.636  -25.348 -0.955  0.50 30.36 ? 126 LEU F C     1 
ATOM   15136 O  O     A LEU C 3 126 ? 52.730  -25.622 -0.054  0.50 32.29 ? 126 LEU F O     1 
ATOM   15137 O  O     B LEU C 3 126 ? 52.760  -25.126 -0.493  0.50 33.22 ? 126 LEU F O     1 
ATOM   15138 C  CB    A LEU C 3 126 ? 49.789  -25.487 1.080   0.50 22.31 ? 126 LEU F CB    1 
ATOM   15139 C  CB    B LEU C 3 126 ? 49.732  -25.826 0.592   0.50 22.74 ? 126 LEU F CB    1 
ATOM   15140 C  CG    A LEU C 3 126 ? 48.576  -24.743 1.653   0.50 25.80 ? 126 LEU F CG    1 
ATOM   15141 C  CG    B LEU C 3 126 ? 48.776  -25.304 1.662   0.50 30.19 ? 126 LEU F CG    1 
ATOM   15142 C  CD1   A LEU C 3 126 ? 47.996  -25.484 2.846   0.50 32.62 ? 126 LEU F CD1   1 
ATOM   15143 C  CD1   B LEU C 3 126 ? 48.419  -26.428 2.625   0.50 22.84 ? 126 LEU F CD1   1 
ATOM   15144 C  CD2   A LEU C 3 126 ? 48.946  -23.314 2.037   0.50 27.17 ? 126 LEU F CD2   1 
ATOM   15145 C  CD2   B LEU C 3 126 ? 49.406  -24.134 2.397   0.50 27.04 ? 126 LEU F CD2   1 
ATOM   15146 N  N     A GLU C 3 127 ? 51.376  -26.180 -1.763  0.50 36.10 ? 127 GLU F N     1 
ATOM   15147 N  N     B GLU C 3 127 ? 51.449  -26.116 -2.033  0.50 36.70 ? 127 GLU F N     1 
ATOM   15148 C  CA    A GLU C 3 127 ? 52.440  -26.892 -2.465  0.50 37.17 ? 127 GLU F CA    1 
ATOM   15149 C  CA    B GLU C 3 127 ? 52.594  -26.728 -2.702  0.50 37.39 ? 127 GLU F CA    1 
ATOM   15150 C  C     A GLU C 3 127 ? 53.492  -25.918 -2.984  0.50 32.93 ? 127 GLU F C     1 
ATOM   15151 C  C     B GLU C 3 127 ? 53.557  -25.678 -3.240  0.50 32.12 ? 127 GLU F C     1 
ATOM   15152 O  O     A GLU C 3 127 ? 54.690  -26.086 -2.729  0.50 35.48 ? 127 GLU F O     1 
ATOM   15153 O  O     B GLU C 3 127 ? 54.768  -25.918 -3.294  0.50 31.99 ? 127 GLU F O     1 
ATOM   15154 C  CB    A GLU C 3 127 ? 51.860  -27.719 -3.617  0.50 33.81 ? 127 GLU F CB    1 
ATOM   15155 C  CB    B GLU C 3 127 ? 52.125  -27.647 -3.834  0.50 33.08 ? 127 GLU F CB    1 
ATOM   15156 C  CG    A GLU C 3 127 ? 50.884  -28.811 -3.197  0.50 42.89 ? 127 GLU F CG    1 
ATOM   15157 C  CG    B GLU C 3 127 ? 52.179  -29.136 -3.508  0.50 37.73 ? 127 GLU F CG    1 
ATOM   15158 C  CD    A GLU C 3 127 ? 49.461  -28.306 -3.029  0.50 41.38 ? 127 GLU F CD    1 
ATOM   15159 C  CD    B GLU C 3 127 ? 51.010  -29.599 -2.656  0.50 41.47 ? 127 GLU F CD    1 
ATOM   15160 O  OE1   A GLU C 3 127 ? 49.150  -27.204 -3.528  0.50 37.44 ? 127 GLU F OE1   1 
ATOM   15161 O  OE1   B GLU C 3 127 ? 50.049  -28.821 -2.489  0.50 41.69 ? 127 GLU F OE1   1 
ATOM   15162 O  OE2   A GLU C 3 127 ? 48.653  -29.014 -2.394  0.50 44.85 ? 127 GLU F OE2   1 
ATOM   15163 O  OE2   B GLU C 3 127 ? 51.050  -30.744 -2.158  0.50 38.28 ? 127 GLU F OE2   1 
ATOM   15164 N  N     A ILE C 3 128 ? 53.058  -24.887 -3.714  0.50 29.12 ? 128 ILE F N     1 
ATOM   15165 N  N     B ILE C 3 128 ? 53.045  -24.511 -3.634  0.50 28.71 ? 128 ILE F N     1 
ATOM   15166 C  CA    A ILE C 3 128 ? 53.981  -23.871 -4.215  0.50 32.07 ? 128 ILE F CA    1 
ATOM   15167 C  CA    B ILE C 3 128 ? 53.921  -23.445 -4.114  0.50 31.25 ? 128 ILE F CA    1 
ATOM   15168 C  C     A ILE C 3 128 ? 54.667  -23.154 -3.061  0.50 30.06 ? 128 ILE F C     1 
ATOM   15169 C  C     B ILE C 3 128 ? 54.725  -22.860 -2.959  0.50 30.10 ? 128 ILE F C     1 
ATOM   15170 O  O     A ILE C 3 128 ? 55.829  -22.747 -3.174  0.50 29.75 ? 128 ILE F O     1 
ATOM   15171 O  O     B ILE C 3 128 ? 55.935  -22.640 -3.075  0.50 30.01 ? 128 ILE F O     1 
ATOM   15172 C  CB    A ILE C 3 128 ? 53.226  -22.894 -5.138  0.50 30.55 ? 128 ILE F CB    1 
ATOM   15173 C  CB    B ILE C 3 128 ? 53.103  -22.362 -4.840  0.50 26.68 ? 128 ILE F CB    1 
ATOM   15174 C  CG1   A ILE C 3 128 ? 52.771  -23.626 -6.402  0.50 27.22 ? 128 ILE F CG1   1 
ATOM   15175 C  CG1   B ILE C 3 128 ? 52.264  -22.984 -5.952  0.50 33.18 ? 128 ILE F CG1   1 
ATOM   15176 C  CG2   A ILE C 3 128 ? 54.089  -21.689 -5.505  0.50 28.06 ? 128 ILE F CG2   1 
ATOM   15177 C  CG2   B ILE C 3 128 ? 54.024  -21.296 -5.426  0.50 26.90 ? 128 ILE F CG2   1 
ATOM   15178 C  CD1   A ILE C 3 128 ? 51.763  -22.868 -7.205  0.50 31.60 ? 128 ILE F CD1   1 
ATOM   15179 C  CD1   B ILE C 3 128 ? 51.605  -21.966 -6.842  0.50 30.43 ? 128 ILE F CD1   1 
ATOM   15180 N  N     A VAL C 3 129 ? 53.972  -23.005 -1.930  0.50 29.40 ? 129 VAL F N     1 
ATOM   15181 N  N     B VAL C 3 129 ? 54.058  -22.597 -1.829  0.50 28.73 ? 129 VAL F N     1 
ATOM   15182 C  CA    A VAL C 3 129 ? 54.577  -22.397 -0.747  0.50 28.20 ? 129 VAL F CA    1 
ATOM   15183 C  CA    B VAL C 3 129 ? 54.746  -22.090 -0.642  0.50 27.17 ? 129 VAL F CA    1 
ATOM   15184 C  C     A VAL C 3 129 ? 55.832  -23.159 -0.341  0.50 27.29 ? 129 VAL F C     1 
ATOM   15185 C  C     B VAL C 3 129 ? 55.916  -22.995 -0.280  0.50 27.54 ? 129 VAL F C     1 
ATOM   15186 O  O     A VAL C 3 129 ? 56.894  -22.566 -0.110  0.50 31.10 ? 129 VAL F O     1 
ATOM   15187 O  O     B VAL C 3 129 ? 57.025  -22.528 0.007   0.50 30.99 ? 129 VAL F O     1 
ATOM   15188 C  CB    A VAL C 3 129 ? 53.558  -22.339 0.405   0.50 27.05 ? 129 VAL F CB    1 
ATOM   15189 C  CB    B VAL C 3 129 ? 53.759  -21.953 0.532   0.50 28.02 ? 129 VAL F CB    1 
ATOM   15190 C  CG1   A VAL C 3 129 ? 54.271  -22.163 1.731   0.50 26.20 ? 129 VAL F CG1   1 
ATOM   15191 C  CG1   B VAL C 3 129 ? 54.495  -21.588 1.808   0.50 28.76 ? 129 VAL F CG1   1 
ATOM   15192 C  CG2   A VAL C 3 129 ? 52.568  -21.205 0.173   0.50 24.51 ? 129 VAL F CG2   1 
ATOM   15193 C  CG2   B VAL C 3 129 ? 52.695  -20.913 0.211   0.50 24.38 ? 129 VAL F CG2   1 
ATOM   15194 N  N     A GLU C 3 130 ? 55.731  -24.486 -0.252  0.50 28.17 ? 130 GLU F N     1 
ATOM   15195 N  N     B GLU C 3 130 ? 55.688  -24.309 -0.303  0.50 27.71 ? 130 GLU F N     1 
ATOM   15196 C  CA    A GLU C 3 130 ? 56.886  -25.293 0.131   0.50 32.63 ? 130 GLU F CA    1 
ATOM   15197 C  CA    B GLU C 3 130 ? 56.759  -25.253 -0.000  0.50 32.72 ? 130 GLU F CA    1 
ATOM   15198 C  C     A GLU C 3 130 ? 58.028  -25.133 -0.865  0.50 30.61 ? 130 GLU F C     1 
ATOM   15199 C  C     B GLU C 3 130 ? 57.896  -25.138 -1.008  0.50 30.43 ? 130 GLU F C     1 
ATOM   15200 O  O     A GLU C 3 130 ? 59.197  -25.058 -0.471  0.50 33.98 ? 130 GLU F O     1 
ATOM   15201 O  O     B GLU C 3 130 ? 59.074  -25.130 -0.633  0.50 33.93 ? 130 GLU F O     1 
ATOM   15202 C  CB    A GLU C 3 130 ? 56.489  -26.765 0.245   0.50 35.28 ? 130 GLU F CB    1 
ATOM   15203 C  CB    B GLU C 3 130 ? 56.210  -26.680 0.024   0.50 34.08 ? 130 GLU F CB    1 
ATOM   15204 C  CG    A GLU C 3 130 ? 55.550  -27.077 1.395   0.50 37.79 ? 130 GLU F CG    1 
ATOM   15205 C  CG    B GLU C 3 130 ? 55.451  -27.042 1.288   0.50 37.78 ? 130 GLU F CG    1 
ATOM   15206 C  CD    A GLU C 3 130 ? 55.404  -28.564 1.634   0.50 47.26 ? 130 GLU F CD    1 
ATOM   15207 C  CD    B GLU C 3 130 ? 55.011  -28.491 1.299   0.50 48.50 ? 130 GLU F CD    1 
ATOM   15208 O  OE1   A GLU C 3 130 ? 55.679  -29.346 0.698   0.50 53.54 ? 130 GLU F OE1   1 
ATOM   15209 O  OE1   B GLU C 3 130 ? 54.565  -28.987 0.238   0.50 41.47 ? 130 GLU F OE1   1 
ATOM   15210 O  OE2   A GLU C 3 130 ? 55.019  -28.951 2.757   0.50 47.83 ? 130 GLU F OE2   1 
ATOM   15211 O  OE2   B GLU C 3 130 ? 55.122  -29.137 2.364   0.50 49.17 ? 130 GLU F OE2   1 
ATOM   15212 N  N     A VAL C 3 131 ? 57.705  -25.080 -2.159  0.50 31.14 ? 131 VAL F N     1 
ATOM   15213 N  N     B VAL C 3 131 ? 57.560  -25.054 -2.297  0.50 31.25 ? 131 VAL F N     1 
ATOM   15214 C  CA    A VAL C 3 131 ? 58.736  -24.951 -3.187  0.50 31.78 ? 131 VAL F CA    1 
ATOM   15215 C  CA    B VAL C 3 131 ? 58.585  -24.956 -3.335  0.50 31.86 ? 131 VAL F CA    1 
ATOM   15216 C  C     A VAL C 3 131 ? 59.528  -23.664 -2.994  0.50 32.87 ? 131 VAL F C     1 
ATOM   15217 C  C     B VAL C 3 131 ? 59.400  -23.680 -3.169  0.50 32.97 ? 131 VAL F C     1 
ATOM   15218 O  O     A VAL C 3 131 ? 60.765  -23.666 -3.026  0.50 33.99 ? 131 VAL F O     1 
ATOM   15219 O  O     B VAL C 3 131 ? 60.630  -23.690 -3.309  0.50 33.86 ? 131 VAL F O     1 
ATOM   15220 C  CB    A VAL C 3 131 ? 58.104  -25.018 -4.589  0.50 35.10 ? 131 VAL F CB    1 
ATOM   15221 C  CB    B VAL C 3 131 ? 57.939  -25.039 -4.731  0.50 34.95 ? 131 VAL F CB    1 
ATOM   15222 C  CG1   A VAL C 3 131 ? 59.117  -24.615 -5.648  0.50 33.79 ? 131 VAL F CG1   1 
ATOM   15223 C  CG1   B VAL C 3 131 ? 58.935  -24.635 -5.807  0.50 33.97 ? 131 VAL F CG1   1 
ATOM   15224 C  CG2   A VAL C 3 131 ? 57.574  -26.418 -4.860  0.50 36.99 ? 131 VAL F CG2   1 
ATOM   15225 C  CG2   B VAL C 3 131 ? 57.420  -26.447 -4.991  0.50 36.99 ? 131 VAL F CG2   1 
ATOM   15226 N  N     A LEU C 3 132 ? 58.827  -22.544 -2.799  0.50 27.40 ? 132 LEU F N     1 
ATOM   15227 N  N     B LEU C 3 132 ? 58.732  -22.562 -2.873  0.50 27.46 ? 132 LEU F N     1 
ATOM   15228 C  CA    A LEU C 3 132 ? 59.510  -21.263 -2.649  0.50 29.12 ? 132 LEU F CA    1 
ATOM   15229 C  CA    B LEU C 3 132 ? 59.441  -21.292 -2.756  0.50 29.04 ? 132 LEU F CA    1 
ATOM   15230 C  C     A LEU C 3 132 ? 60.404  -21.259 -1.415  0.50 34.41 ? 132 LEU F C     1 
ATOM   15231 C  C     B LEU C 3 132 ? 60.367  -21.285 -1.547  0.50 34.39 ? 132 LEU F C     1 
ATOM   15232 O  O     A LEU C 3 132 ? 61.532  -20.755 -1.460  0.50 32.38 ? 132 LEU F O     1 
ATOM   15233 O  O     B LEU C 3 132 ? 61.513  -20.831 -1.641  0.50 32.29 ? 132 LEU F O     1 
ATOM   15234 C  CB    A LEU C 3 132 ? 58.491  -20.124 -2.582  0.50 28.38 ? 132 LEU F CB    1 
ATOM   15235 C  CB    B LEU C 3 132 ? 58.443  -20.137 -2.678  0.50 28.37 ? 132 LEU F CB    1 
ATOM   15236 C  CG    A LEU C 3 132 ? 57.713  -19.777 -3.853  0.50 28.89 ? 132 LEU F CG    1 
ATOM   15237 C  CG    B LEU C 3 132 ? 57.609  -19.846 -3.928  0.50 28.90 ? 132 LEU F CG    1 
ATOM   15238 C  CD1   A LEU C 3 132 ? 56.499  -18.924 -3.513  0.50 26.80 ? 132 LEU F CD1   1 
ATOM   15239 C  CD1   B LEU C 3 132 ? 56.460  -18.911 -3.587  0.50 26.79 ? 132 LEU F CD1   1 
ATOM   15240 C  CD2   A LEU C 3 132 ? 58.601  -19.056 -4.858  0.50 27.98 ? 132 LEU F CD2   1 
ATOM   15241 C  CD2   B LEU C 3 132 ? 58.471  -19.252 -5.035  0.50 28.42 ? 132 LEU F CD2   1 
ATOM   15242 N  N     A LEU C 3 133 ? 59.917  -21.822 -0.306  0.50 31.85 ? 133 LEU F N     1 
ATOM   15243 N  N     B LEU C 3 133 ? 59.889  -21.784 -0.402  0.50 31.86 ? 133 LEU F N     1 
ATOM   15244 C  CA    A LEU C 3 133 ? 60.724  -21.905 0.909   0.50 34.70 ? 133 LEU F CA    1 
ATOM   15245 C  CA    B LEU C 3 133 ? 60.744  -21.877 0.778   0.50 34.74 ? 133 LEU F CA    1 
ATOM   15246 C  C     A LEU C 3 133 ? 62.033  -22.641 0.651   0.50 33.02 ? 133 LEU F C     1 
ATOM   15247 C  C     B LEU C 3 133 ? 61.984  -22.717 0.496   0.50 32.89 ? 133 LEU F C     1 
ATOM   15248 O  O     A LEU C 3 133 ? 63.106  -22.189 1.065   0.50 32.25 ? 133 LEU F O     1 
ATOM   15249 O  O     B LEU C 3 133 ? 63.079  -22.404 0.977   0.50 32.04 ? 133 LEU F O     1 
ATOM   15250 C  CB    A LEU C 3 133 ? 59.930  -22.595 2.019   0.50 28.56 ? 133 LEU F CB    1 
ATOM   15251 C  CB    B LEU C 3 133 ? 59.955  -22.455 1.954   0.50 28.72 ? 133 LEU F CB    1 
ATOM   15252 C  CG    A LEU C 3 133 ? 59.310  -21.685 3.077   0.50 32.26 ? 133 LEU F CG    1 
ATOM   15253 C  CG    B LEU C 3 133 ? 58.916  -21.511 2.559   0.50 29.82 ? 133 LEU F CG    1 
ATOM   15254 C  CD1   A LEU C 3 133 ? 58.575  -20.527 2.427   0.50 33.73 ? 133 LEU F CD1   1 
ATOM   15255 C  CD1   B LEU C 3 133 ? 58.030  -22.239 3.557   0.50 34.56 ? 133 LEU F CD1   1 
ATOM   15256 C  CD2   A LEU C 3 133 ? 58.377  -22.481 3.970   0.50 35.41 ? 133 LEU F CD2   1 
ATOM   15257 C  CD2   B LEU C 3 133 ? 59.607  -20.328 3.219   0.50 29.34 ? 133 LEU F CD2   1 
ATOM   15258 N  N     A LYS C 3 134 ? 61.963  -23.780 -0.041  0.50 32.83 ? 134 LYS F N     1 
ATOM   15259 N  N     B LYS C 3 134 ? 61.836  -23.781 -0.293  0.50 33.19 ? 134 LYS F N     1 
ATOM   15260 C  CA    A LYS C 3 134 ? 63.170  -24.551 -0.317  0.50 32.48 ? 134 LYS F CA    1 
ATOM   15261 C  CA    B LYS C 3 134 ? 62.972  -24.628 -0.635  0.50 32.96 ? 134 LYS F CA    1 
ATOM   15262 C  C     A LYS C 3 134 ? 64.138  -23.770 -1.198  0.50 32.86 ? 134 LYS F C     1 
ATOM   15263 C  C     B LYS C 3 134 ? 63.894  -23.998 -1.674  0.50 31.76 ? 134 LYS F C     1 
ATOM   15264 O  O     A LYS C 3 134 ? 65.358  -23.850 -1.013  0.50 27.98 ? 134 LYS F O     1 
ATOM   15265 O  O     B LYS C 3 134 ? 64.931  -24.591 -1.984  0.50 35.49 ? 134 LYS F O     1 
ATOM   15266 C  CB    A LYS C 3 134 ? 62.799  -25.885 -0.965  0.50 36.06 ? 134 LYS F CB    1 
ATOM   15267 C  CB    B LYS C 3 134 ? 62.473  -25.992 -1.116  0.50 36.24 ? 134 LYS F CB    1 
ATOM   15268 C  CG    A LYS C 3 134 ? 61.907  -26.755 -0.087  0.50 40.89 ? 134 LYS F CG    1 
ATOM   15269 C  CG    B LYS C 3 134 ? 61.743  -26.769 -0.021  0.50 40.59 ? 134 LYS F CG    1 
ATOM   15270 C  CD    A LYS C 3 134 ? 61.562  -28.076 -0.758  0.50 49.01 ? 134 LYS F CD    1 
ATOM   15271 C  CD    B LYS C 3 134 ? 61.343  -28.171 -0.454  0.50 49.51 ? 134 LYS F CD    1 
ATOM   15272 C  CE    A LYS C 3 134 ? 60.604  -28.887 0.103   0.50 55.49 ? 134 LYS F CE    1 
ATOM   15273 C  CE    B LYS C 3 134 ? 60.607  -28.890 0.671   0.50 56.50 ? 134 LYS F CE    1 
ATOM   15274 N  NZ    A LYS C 3 134 ? 60.214  -30.172 -0.539  0.50 66.11 ? 134 LYS F NZ    1 
ATOM   15275 N  NZ    B LYS C 3 134 ? 60.203  -30.277 0.305   0.50 62.50 ? 134 LYS F NZ    1 
ATOM   15276 N  N     A HIS C 3 135 ? 63.616  -22.991 -2.148  0.50 31.67 ? 135 HIS F N     1 
ATOM   15277 N  N     B HIS C 3 135 ? 63.554  -22.825 -2.208  0.50 31.75 ? 135 HIS F N     1 
ATOM   15278 C  CA    A HIS C 3 135 ? 64.446  -22.232 -3.077  0.50 29.43 ? 135 HIS F CA    1 
ATOM   15279 C  CA    B HIS C 3 135 ? 64.450  -22.066 -3.073  0.50 29.42 ? 135 HIS F CA    1 
ATOM   15280 C  C     A HIS C 3 135 ? 64.725  -20.808 -2.603  0.50 30.99 ? 135 HIS F C     1 
ATOM   15281 C  C     B HIS C 3 135 ? 64.969  -20.800 -2.398  0.50 31.39 ? 135 HIS F C     1 
ATOM   15282 O  O     A HIS C 3 135 ? 64.941  -19.914 -3.432  0.50 33.25 ? 135 HIS F O     1 
ATOM   15283 O  O     B HIS C 3 135 ? 65.631  -19.985 -3.048  0.50 32.29 ? 135 HIS F O     1 
ATOM   15284 C  CB    A HIS C 3 135 ? 63.803  -22.221 -4.464  0.50 29.92 ? 135 HIS F CB    1 
ATOM   15285 C  CB    B HIS C 3 135 ? 63.755  -21.716 -4.391  0.50 30.53 ? 135 HIS F CB    1 
ATOM   15286 C  CG    A HIS C 3 135 ? 63.946  -23.514 -5.205  0.50 33.28 ? 135 HIS F CG    1 
ATOM   15287 C  CG    B HIS C 3 135 ? 63.661  -22.863 -5.351  0.50 34.03 ? 135 HIS F CG    1 
ATOM   15288 N  ND1   A HIS C 3 135 ? 64.981  -23.757 -6.083  0.50 30.82 ? 135 HIS F ND1   1 
ATOM   15289 N  ND1   B HIS C 3 135 ? 62.847  -23.954 -5.133  0.50 32.16 ? 135 HIS F ND1   1 
ATOM   15290 C  CD2   A HIS C 3 135 ? 63.182  -24.632 -5.206  0.50 33.00 ? 135 HIS F CD2   1 
ATOM   15291 C  CD2   B HIS C 3 135 ? 64.278  -23.085 -6.537  0.50 30.92 ? 135 HIS F CD2   1 
ATOM   15292 C  CE1   A HIS C 3 135 ? 64.851  -24.970 -6.590  0.50 33.07 ? 135 HIS F CE1   1 
ATOM   15293 C  CE1   B HIS C 3 135 ? 62.965  -24.798 -6.143  0.50 30.46 ? 135 HIS F CE1   1 
ATOM   15294 N  NE2   A HIS C 3 135 ? 63.767  -25.523 -6.074  0.50 30.06 ? 135 HIS F NE2   1 
ATOM   15295 N  NE2   B HIS C 3 135 ? 63.828  -24.295 -7.008  0.50 30.03 ? 135 HIS F NE2   1 
ATOM   15296 N  N     A GLY C 3 136 ? 64.707  -20.564 -1.292  0.50 32.24 ? 136 GLY F N     1 
ATOM   15297 N  N     B GLY C 3 136 ? 64.678  -20.612 -1.116  0.50 32.26 ? 136 GLY F N     1 
ATOM   15298 C  CA    A GLY C 3 136 ? 65.264  -19.350 -0.730  0.50 29.44 ? 136 GLY F CA    1 
ATOM   15299 C  CA    B GLY C 3 136 ? 65.265  -19.535 -0.347  0.50 30.91 ? 136 GLY F CA    1 
ATOM   15300 C  C     A GLY C 3 136 ? 64.293  -18.253 -0.337  0.50 31.48 ? 136 GLY F C     1 
ATOM   15301 C  C     B GLY C 3 136 ? 64.435  -18.280 -0.178  0.50 31.20 ? 136 GLY F C     1 
ATOM   15302 O  O     A GLY C 3 136 ? 64.750  -17.169 0.044   0.50 28.75 ? 136 GLY F O     1 
ATOM   15303 O  O     B GLY C 3 136 ? 65.013  -17.220 0.087   0.50 29.25 ? 136 GLY F O     1 
ATOM   15304 N  N     A ALA C 3 137 ? 62.984  -18.485 -0.410  0.50 31.79 ? 137 ALA F N     1 
ATOM   15305 N  N     B ALA C 3 137 ? 63.112  -18.359 -0.317  0.50 31.85 ? 137 ALA F N     1 
ATOM   15306 C  CA    A ALA C 3 137 ? 62.027  -17.431 -0.087  0.50 31.22 ? 137 ALA F CA    1 
ATOM   15307 C  CA    B ALA C 3 137 ? 62.272  -17.180 -0.148  0.50 30.81 ? 137 ALA F CA    1 
ATOM   15308 C  C     A ALA C 3 137 ? 62.206  -16.959 1.352   0.50 31.48 ? 137 ALA F C     1 
ATOM   15309 C  C     B ALA C 3 137 ? 62.482  -16.568 1.233   0.50 28.85 ? 137 ALA F C     1 
ATOM   15310 O  O     A ALA C 3 137 ? 62.249  -17.769 2.284   0.50 30.29 ? 137 ALA F O     1 
ATOM   15311 O  O     B ALA C 3 137 ? 62.855  -17.253 2.190   0.50 33.24 ? 137 ALA F O     1 
ATOM   15312 C  CB    A ALA C 3 137 ? 60.597  -17.922 -0.308  0.50 29.95 ? 137 ALA F CB    1 
ATOM   15313 C  CB    B ALA C 3 137 ? 60.799  -17.537 -0.348  0.50 28.99 ? 137 ALA F CB    1 
ATOM   15314 N  N     A ASP C 3 138 ? 62.305  -15.639 1.523   0.50 29.08 ? 138 ASP F N     1 
ATOM   15315 N  N     B ASP C 3 138 ? 62.239  -15.263 1.331   0.50 29.05 ? 138 ASP F N     1 
ATOM   15316 C  CA    A ASP C 3 138 ? 62.570  -15.027 2.823   0.50 32.30 ? 138 ASP F CA    1 
ATOM   15317 C  CA    B ASP C 3 138 ? 62.534  -14.501 2.542   0.50 29.86 ? 138 ASP F CA    1 
ATOM   15318 C  C     A ASP C 3 138 ? 61.270  -14.911 3.614   0.50 31.90 ? 138 ASP F C     1 
ATOM   15319 C  C     B ASP C 3 138 ? 61.355  -14.611 3.502   0.50 31.75 ? 138 ASP F C     1 
ATOM   15320 O  O     A ASP C 3 138 ? 60.331  -14.230 3.186   0.50 30.19 ? 138 ASP F O     1 
ATOM   15321 O  O     B ASP C 3 138 ? 60.307  -13.995 3.285   0.50 29.93 ? 138 ASP F O     1 
ATOM   15322 C  CB    A ASP C 3 138 ? 63.220  -13.657 2.632   0.50 26.26 ? 138 ASP F CB    1 
ATOM   15323 C  CB    B ASP C 3 138 ? 62.831  -13.044 2.198   0.50 30.35 ? 138 ASP F CB    1 
ATOM   15324 C  CG    A ASP C 3 138 ? 63.496  -12.939 3.939   0.50 33.48 ? 138 ASP F CG    1 
ATOM   15325 C  CG    B ASP C 3 138 ? 63.429  -12.275 3.362   0.50 31.76 ? 138 ASP F CG    1 
ATOM   15326 O  OD1   A ASP C 3 138 ? 63.403  -13.562 5.020   0.50 33.49 ? 138 ASP F OD1   1 
ATOM   15327 O  OD1   B ASP C 3 138 ? 63.591  -12.862 4.453   0.50 36.10 ? 138 ASP F OD1   1 
ATOM   15328 O  OD2   A ASP C 3 138 ? 63.804  -11.730 3.884   0.50 38.08 ? 138 ASP F OD2   1 
ATOM   15329 O  OD2   B ASP C 3 138 ? 63.740  -11.077 3.186   0.50 27.30 ? 138 ASP F OD2   1 
ATOM   15330 N  N     A VAL C 3 139 ? 61.225  -15.564 4.777   0.50 29.58 ? 139 VAL F N     1 
ATOM   15331 N  N     B VAL C 3 139 ? 61.532  -15.390 4.573   0.50 29.17 ? 139 VAL F N     1 
ATOM   15332 C  CA    A VAL C 3 139 ? 60.016  -15.600 5.590   0.50 32.75 ? 139 VAL F CA    1 
ATOM   15333 C  CA    B VAL C 3 139 ? 60.469  -15.547 5.560   0.50 32.98 ? 139 VAL F CA    1 
ATOM   15334 C  C     A VAL C 3 139 ? 59.856  -14.298 6.364   0.50 31.99 ? 139 VAL F C     1 
ATOM   15335 C  C     B VAL C 3 139 ? 60.217  -14.240 6.302   0.50 30.76 ? 139 VAL F C     1 
ATOM   15336 O  O     A VAL C 3 139 ? 58.856  -14.098 7.064   0.50 34.51 ? 139 VAL F O     1 
ATOM   15337 O  O     B VAL C 3 139 ? 59.102  -13.996 6.780   0.50 35.77 ? 139 VAL F O     1 
ATOM   15338 C  CB    A VAL C 3 139 ? 60.015  -16.807 6.551   0.50 33.14 ? 139 VAL F CB    1 
ATOM   15339 C  CB    B VAL C 3 139 ? 60.813  -16.691 6.533   0.50 35.92 ? 139 VAL F CB    1 
ATOM   15340 C  CG1   A VAL C 3 139 ? 59.792  -18.112 5.786   0.50 38.22 ? 139 VAL F CG1   1 
ATOM   15341 C  CG1   B VAL C 3 139 ? 60.709  -18.035 5.831   0.50 35.63 ? 139 VAL F CG1   1 
ATOM   15342 C  CG2   A VAL C 3 139 ? 61.300  -16.863 7.355   0.50 33.28 ? 139 VAL F CG2   1 
ATOM   15343 C  CG2   B VAL C 3 139 ? 62.213  -16.500 7.106   0.50 30.80 ? 139 VAL F CG2   1 
ATOM   15344 N  N     A ASN C 3 140 ? 60.826  -13.399 6.241   0.50 31.95 ? 140 ASN F N     1 
ATOM   15345 N  N     B ASN C 3 140 ? 61.229  -13.381 6.410   0.50 32.02 ? 140 ASN F N     1 
ATOM   15346 C  CA    A ASN C 3 140 ? 60.824  -12.155 6.997   0.50 33.81 ? 140 ASN F CA    1 
ATOM   15347 C  CA    B ASN C 3 140 ? 61.106  -12.102 7.097   0.50 33.52 ? 140 ASN F CA    1 
ATOM   15348 C  C     A ASN C 3 140 ? 60.428  -10.939 6.168   0.50 29.78 ? 140 ASN F C     1 
ATOM   15349 C  C     B ASN C 3 140 ? 60.614  -10.976 6.197   0.50 29.77 ? 140 ASN F C     1 
ATOM   15350 O  O     A ASN C 3 140 ? 60.303  -9.846  6.726   0.50 32.46 ? 140 ASN F O     1 
ATOM   15351 O  O     B ASN C 3 140 ? 60.467  -9.846  6.674   0.50 32.66 ? 140 ASN F O     1 
ATOM   15352 C  CB    A ASN C 3 140 ? 62.199  -11.930 7.631   0.50 30.26 ? 140 ASN F CB    1 
ATOM   15353 C  CB    B ASN C 3 140 ? 62.451  -11.699 7.712   0.50 29.57 ? 140 ASN F CB    1 
ATOM   15354 C  CG    A ASN C 3 140 ? 62.448  -12.849 8.820   0.50 35.45 ? 140 ASN F CG    1 
ATOM   15355 C  CG    B ASN C 3 140 ? 62.757  -12.451 8.997   0.50 35.27 ? 140 ASN F CG    1 
ATOM   15356 O  OD1   A ASN C 3 140 ? 61.509  -13.362 9.436   0.50 34.16 ? 140 ASN F OD1   1 
ATOM   15357 O  OD1   B ASN C 3 140 ? 61.900  -13.143 9.550   0.50 34.72 ? 140 ASN F OD1   1 
ATOM   15358 N  ND2   A ASN C 3 140 ? 63.716  -13.055 9.150   0.50 34.55 ? 140 ASN F ND2   1 
ATOM   15359 N  ND2   B ASN C 3 140 ? 63.983  -12.301 9.488   0.50 30.21 ? 140 ASN F ND2   1 
ATOM   15360 N  N     A ALA C 3 141 ? 60.219  -11.096 4.863   0.50 27.12 ? 141 ALA F N     1 
ATOM   15361 N  N     B ALA C 3 141 ? 60.351  -11.248 4.922   0.50 26.87 ? 141 ALA F N     1 
ATOM   15362 C  CA    A ALA C 3 141 ? 59.888  -9.952  4.021   0.50 31.32 ? 141 ALA F CA    1 
ATOM   15363 C  CA    B ALA C 3 141 ? 60.004  -10.188 3.985   0.50 30.78 ? 141 ALA F CA    1 
ATOM   15364 C  C     A ALA C 3 141 ? 58.471  -9.464  4.304   0.50 28.53 ? 141 ALA F C     1 
ATOM   15365 C  C     B ALA C 3 141 ? 58.653  -9.573  4.333   0.50 28.86 ? 141 ALA F C     1 
ATOM   15366 O  O     A ALA C 3 141 ? 57.522  -10.254 4.317   0.50 30.43 ? 141 ALA F O     1 
ATOM   15367 O  O     B ALA C 3 141 ? 57.648  -10.281 4.443   0.50 30.48 ? 141 ALA F O     1 
ATOM   15368 C  CB    A ALA C 3 141 ? 60.034  -10.317 2.544   0.50 29.30 ? 141 ALA F CB    1 
ATOM   15369 C  CB    B ALA C 3 141 ? 59.980  -10.731 2.559   0.50 30.12 ? 141 ALA F CB    1 
ATOM   15370 N  N     A GLN C 3 142 ? 58.327  -8.156  4.511   0.50 22.26 ? 142 GLN F N     1 
ATOM   15371 N  N     B GLN C 3 142 ? 58.632  -8.251  4.488   0.50 21.83 ? 142 GLN F N     1 
ATOM   15372 C  CA    A GLN C 3 142 ? 57.048  -7.537  4.835   0.50 29.28 ? 142 GLN F CA    1 
ATOM   15373 C  CA    B GLN C 3 142 ? 57.429  -7.509  4.836   0.50 28.82 ? 142 GLN F CA    1 
ATOM   15374 C  C     A GLN C 3 142 ? 56.461  -6.847  3.611   0.50 27.66 ? 142 GLN F C     1 
ATOM   15375 C  C     B GLN C 3 142 ? 56.842  -6.840  3.602   0.50 27.55 ? 142 GLN F C     1 
ATOM   15376 O  O     A GLN C 3 142 ? 57.193  -6.261  2.809   0.50 30.19 ? 142 GLN F O     1 
ATOM   15377 O  O     B GLN C 3 142 ? 57.579  -6.353  2.740   0.50 30.36 ? 142 GLN F O     1 
ATOM   15378 C  CB    A GLN C 3 142 ? 57.199  -6.504  5.954   0.50 33.62 ? 142 GLN F CB    1 
ATOM   15379 C  CB    B GLN C 3 142 ? 57.727  -6.433  5.881   0.50 32.70 ? 142 GLN F CB    1 
ATOM   15380 C  CG    A GLN C 3 142 ? 57.769  -7.021  7.261   0.50 29.16 ? 142 GLN F CG    1 
ATOM   15381 C  CG    B GLN C 3 142 ? 58.333  -6.923  7.175   0.50 27.02 ? 142 GLN F CG    1 
ATOM   15382 C  CD    A GLN C 3 142 ? 57.926  -5.911  8.285   0.50 30.34 ? 142 GLN F CD    1 
ATOM   15383 C  CD    B GLN C 3 142 ? 58.680  -5.774  8.103   0.50 32.26 ? 142 GLN F CD    1 
ATOM   15384 O  OE1   A GLN C 3 142 ? 58.812  -5.065  8.168   0.50 31.19 ? 142 GLN F OE1   1 
ATOM   15385 O  OE1   B GLN C 3 142 ? 59.812  -5.291  8.110   0.50 30.69 ? 142 GLN F OE1   1 
ATOM   15386 N  NE2   A GLN C 3 142 ? 57.052  -5.897  9.280   0.50 28.65 ? 142 GLN F NE2   1 
ATOM   15387 N  NE2   B GLN C 3 142 ? 57.701  -5.321  8.883   0.50 23.74 ? 142 GLN F NE2   1 
ATOM   15388 N  N     A ASP C 3 143 ? 55.135  -6.894  3.487   0.50 27.43 ? 143 ASP F N     1 
ATOM   15389 N  N     B ASP C 3 143 ? 55.514  -6.800  3.531   0.50 27.97 ? 143 ASP F N     1 
ATOM   15390 C  CA    A ASP C 3 143 ? 54.443  -6.133  2.455   0.50 30.42 ? 143 ASP F CA    1 
ATOM   15391 C  CA    B ASP C 3 143 ? 54.836  -6.041  2.490   0.50 30.30 ? 143 ASP F CA    1 
ATOM   15392 C  C     A ASP C 3 143 ? 54.307  -4.678  2.915   0.50 34.71 ? 143 ASP F C     1 
ATOM   15393 C  C     B ASP C 3 143 ? 54.723  -4.582  2.936   0.50 35.42 ? 143 ASP F C     1 
ATOM   15394 O  O     A ASP C 3 143 ? 54.895  -4.262  3.917   0.50 34.99 ? 143 ASP F O     1 
ATOM   15395 O  O     B ASP C 3 143 ? 55.370  -4.146  3.893   0.50 33.39 ? 143 ASP F O     1 
ATOM   15396 C  CB    A ASP C 3 143 ? 53.100  -6.786  2.115   0.50 27.46 ? 143 ASP F CB    1 
ATOM   15397 C  CB    B ASP C 3 143 ? 53.482  -6.671  2.164   0.50 28.20 ? 143 ASP F CB    1 
ATOM   15398 C  CG    A ASP C 3 143 ? 52.146  -6.860  3.305   0.50 33.98 ? 143 ASP F CG    1 
ATOM   15399 C  CG    B ASP C 3 143 ? 52.431  -6.403  3.227   0.50 34.94 ? 143 ASP F CG    1 
ATOM   15400 O  OD1   A ASP C 3 143 ? 52.331  -6.115  4.290   0.50 33.10 ? 143 ASP F OD1   1 
ATOM   15401 O  OD1   B ASP C 3 143 ? 52.801  -6.142  4.391   0.50 34.26 ? 143 ASP F OD1   1 
ATOM   15402 O  OD2   A ASP C 3 143 ? 51.199  -7.676  3.251   0.50 31.10 ? 143 ASP F OD2   1 
ATOM   15403 O  OD2   B ASP C 3 143 ? 51.228  -6.461  2.892   0.50 32.62 ? 143 ASP F OD2   1 
ATOM   15404 N  N     A LYS C 3 144 ? 53.524  -3.881  2.182   0.50 32.00 ? 144 LYS F N     1 
ATOM   15405 N  N     B LYS C 3 144 ? 53.888  -3.805  2.252   0.50 32.66 ? 144 LYS F N     1 
ATOM   15406 C  CA    A LYS C 3 144 ? 53.370  -2.473  2.537   0.50 36.70 ? 144 LYS F CA    1 
ATOM   15407 C  CA    B LYS C 3 144 ? 53.758  -2.389  2.567   0.50 36.72 ? 144 LYS F CA    1 
ATOM   15408 C  C     A LYS C 3 144 ? 52.733  -2.315  3.911   0.50 35.03 ? 144 LYS F C     1 
ATOM   15409 C  C     B LYS C 3 144 ? 52.880  -2.124  3.783   0.50 35.09 ? 144 LYS F C     1 
ATOM   15410 O  O     A LYS C 3 144 ? 53.097  -1.411  4.672   0.50 41.13 ? 144 LYS F O     1 
ATOM   15411 O  O     B LYS C 3 144 ? 52.707  -0.960  4.158   0.50 39.94 ? 144 LYS F O     1 
ATOM   15412 C  CB    A LYS C 3 144 ? 52.535  -1.746  1.484   0.50 36.34 ? 144 LYS F CB    1 
ATOM   15413 C  CB    B LYS C 3 144 ? 53.224  -1.633  1.351   0.50 35.39 ? 144 LYS F CB    1 
ATOM   15414 C  CG    A LYS C 3 144 ? 53.200  -1.598  0.131   0.50 35.60 ? 144 LYS F CG    1 
ATOM   15415 C  CG    B LYS C 3 144 ? 54.277  -1.442  0.281   0.50 40.23 ? 144 LYS F CG    1 
ATOM   15416 C  CD    A LYS C 3 144 ? 53.968  -0.290  0.036   0.50 44.31 ? 144 LYS F CD    1 
ATOM   15417 C  CD    B LYS C 3 144 ? 55.544  -0.873  0.898   0.50 43.04 ? 144 LYS F CD    1 
ATOM   15418 C  CE    A LYS C 3 144 ? 54.442  -0.037  -1.382  0.50 33.79 ? 144 LYS F CE    1 
ATOM   15419 C  CE    B LYS C 3 144 ? 56.706  -0.878  -0.076  0.50 34.91 ? 144 LYS F CE    1 
ATOM   15420 N  NZ    A LYS C 3 144 ? 55.049  1.313   -1.538  0.50 48.74 ? 144 LYS F NZ    1 
ATOM   15421 N  NZ    B LYS C 3 144 ? 57.925  -0.294  0.552   0.50 50.73 ? 144 LYS F NZ    1 
ATOM   15422 N  N     A PHE C 3 145 ? 51.778  -3.182  4.247   0.50 36.06 ? 145 PHE F N     1 
ATOM   15423 N  N     B PHE C 3 145 ? 52.325  -3.166  4.401   0.50 36.50 ? 145 PHE F N     1 
ATOM   15424 C  CA    A PHE C 3 145 ? 51.137  -3.135  5.555   0.50 39.86 ? 145 PHE F CA    1 
ATOM   15425 C  CA    B PHE C 3 145 ? 51.654  -3.055  5.689   0.50 36.92 ? 145 PHE F CA    1 
ATOM   15426 C  C     A PHE C 3 145 ? 51.996  -3.742  6.654   0.50 38.77 ? 145 PHE F C     1 
ATOM   15427 C  C     B PHE C 3 145 ? 52.463  -3.705  6.805   0.50 39.41 ? 145 PHE F C     1 
ATOM   15428 O  O     A PHE C 3 145 ? 51.663  -3.582  7.834   0.50 34.39 ? 145 PHE F O     1 
ATOM   15429 O  O     B PHE C 3 145 ? 51.927  -3.966  7.887   0.50 36.04 ? 145 PHE F O     1 
ATOM   15430 C  CB    A PHE C 3 145 ? 49.780  -3.844  5.506   0.50 39.81 ? 145 PHE F CB    1 
ATOM   15431 C  CB    B PHE C 3 145 ? 50.253  -3.668  5.622   0.50 41.23 ? 145 PHE F CB    1 
ATOM   15432 C  CG    A PHE C 3 145 ? 48.718  -3.072  4.774   0.50 45.86 ? 145 PHE F CG    1 
ATOM   15433 C  CG    B PHE C 3 145 ? 49.258  -2.829  4.871   0.50 42.60 ? 145 PHE F CG    1 
ATOM   15434 C  CD1   A PHE C 3 145 ? 48.776  -2.919  3.398   0.50 42.22 ? 145 PHE F CD1   1 
ATOM   15435 C  CD1   B PHE C 3 145 ? 49.319  -2.724  3.491   0.50 40.15 ? 145 PHE F CD1   1 
ATOM   15436 C  CD2   A PHE C 3 145 ? 47.656  -2.506  5.463   0.50 46.69 ? 145 PHE F CD2   1 
ATOM   15437 C  CD2   B PHE C 3 145 ? 48.252  -2.156  5.545   0.50 49.40 ? 145 PHE F CD2   1 
ATOM   15438 C  CE1   A PHE C 3 145 ? 47.799  -2.207  2.722   0.50 45.15 ? 145 PHE F CE1   1 
ATOM   15439 C  CE1   B PHE C 3 145 ? 48.402  -1.952  2.797   0.50 43.73 ? 145 PHE F CE1   1 
ATOM   15440 C  CE2   A PHE C 3 145 ? 46.676  -1.796  4.794   0.50 48.02 ? 145 PHE F CE2   1 
ATOM   15441 C  CE2   B PHE C 3 145 ? 47.331  -1.386  4.859   0.50 48.19 ? 145 PHE F CE2   1 
ATOM   15442 C  CZ    A PHE C 3 145 ? 46.747  -1.647  3.422   0.50 49.38 ? 145 PHE F CZ    1 
ATOM   15443 C  CZ    B PHE C 3 145 ? 47.407  -1.284  3.483   0.50 49.19 ? 145 PHE F CZ    1 
ATOM   15444 N  N     A GLY C 3 146 ? 53.083  -4.424  6.302   0.50 34.27 ? 146 GLY F N     1 
ATOM   15445 N  N     B GLY C 3 146 ? 53.746  -3.968  6.563   0.50 31.32 ? 146 GLY F N     1 
ATOM   15446 C  CA    A GLY C 3 146 ? 53.994  -4.968  7.287   0.50 33.49 ? 146 GLY F CA    1 
ATOM   15447 C  CA    B GLY C 3 146 ? 54.597  -4.604  7.547   0.50 30.85 ? 146 GLY F CA    1 
ATOM   15448 C  C     A GLY C 3 146 ? 53.614  -6.351  7.770   0.50 33.55 ? 146 GLY F C     1 
ATOM   15449 C  C     B GLY C 3 146 ? 54.322  -6.070  7.790   0.50 31.32 ? 146 GLY F C     1 
ATOM   15450 O  O     A GLY C 3 146 ? 53.690  -6.638  8.968   0.50 31.05 ? 146 GLY F O     1 
ATOM   15451 O  O     B GLY C 3 146 ? 54.915  -6.650  8.703   0.50 26.32 ? 146 GLY F O     1 
ATOM   15452 N  N     A LYS C 3 147 ? 53.199  -7.220  6.852   0.50 32.64 ? 147 LYS F N     1 
ATOM   15453 N  N     B LYS C 3 147 ? 53.445  -6.691  7.005   0.50 30.51 ? 147 LYS F N     1 
ATOM   15454 C  CA    A LYS C 3 147 ? 52.828  -8.590  7.184   0.50 27.00 ? 147 LYS F CA    1 
ATOM   15455 C  CA    B LYS C 3 147 ? 53.080  -8.087  7.211   0.50 31.16 ? 147 LYS F CA    1 
ATOM   15456 C  C     A LYS C 3 147 ? 53.723  -9.550  6.415   0.50 33.47 ? 147 LYS F C     1 
ATOM   15457 C  C     B LYS C 3 147 ? 54.011  -9.007  6.431   0.50 32.48 ? 147 LYS F C     1 
ATOM   15458 O  O     A LYS C 3 147 ? 53.757  -9.516  5.180   0.50 29.28 ? 147 LYS F O     1 
ATOM   15459 O  O     B LYS C 3 147 ? 54.362  -8.724  5.282   0.50 26.82 ? 147 LYS F O     1 
ATOM   15460 C  CB    A LYS C 3 147 ? 51.355  -8.854  6.865   0.50 32.21 ? 147 LYS F CB    1 
ATOM   15461 C  CB    B LYS C 3 147 ? 51.632  -8.331  6.780   0.50 31.55 ? 147 LYS F CB    1 
ATOM   15462 C  CG    A LYS C 3 147 ? 50.391  -8.006  7.679   0.50 31.46 ? 147 LYS F CG    1 
ATOM   15463 C  CG    B LYS C 3 147 ? 50.609  -7.468  7.506   0.50 31.51 ? 147 LYS F CG    1 
ATOM   15464 C  CD    A LYS C 3 147 ? 48.983  -8.572  7.635   0.50 34.90 ? 147 LYS F CD    1 
ATOM   15465 C  CD    B LYS C 3 147 ? 50.289  -8.019  8.885   0.50 32.50 ? 147 LYS F CD    1 
ATOM   15466 C  CE    A LYS C 3 147 ? 48.029  -7.722  8.456   0.50 31.61 ? 147 LYS F CE    1 
ATOM   15467 C  CE    B LYS C 3 147 ? 49.537  -6.991  9.721   0.50 39.41 ? 147 LYS F CE    1 
ATOM   15468 N  NZ    A LYS C 3 147 ? 48.419  -7.686  9.897   0.50 42.86 ? 147 LYS F NZ    1 
ATOM   15469 N  NZ    B LYS C 3 147 ? 48.494  -6.275  8.931   0.50 31.40 ? 147 LYS F NZ    1 
ATOM   15470 N  N     A THR C 3 148 ? 54.452  -10.394 7.141   0.50 31.44 ? 148 THR F N     1 
ATOM   15471 N  N     B THR C 3 148 ? 54.413  -10.107 7.061   0.50 32.14 ? 148 THR F N     1 
ATOM   15472 C  CA    A THR C 3 148 ? 55.155  -11.491 6.499   0.50 31.43 ? 148 THR F CA    1 
ATOM   15473 C  CA    B THR C 3 148 ? 55.115  -11.176 6.366   0.50 31.68 ? 148 THR F CA    1 
ATOM   15474 C  C     A THR C 3 148 ? 54.164  -12.581 6.107   0.50 30.16 ? 148 THR F C     1 
ATOM   15475 C  C     B THR C 3 148 ? 54.142  -12.303 6.036   0.50 29.88 ? 148 THR F C     1 
ATOM   15476 O  O     A THR C 3 148 ? 52.983  -12.542 6.463   0.50 29.90 ? 148 THR F O     1 
ATOM   15477 O  O     B THR C 3 148 ? 52.974  -12.290 6.433   0.50 30.45 ? 148 THR F O     1 
ATOM   15478 C  CB    A THR C 3 148 ? 56.230  -12.076 7.417   0.50 32.31 ? 148 THR F CB    1 
ATOM   15479 C  CB    B THR C 3 148 ? 56.284  -11.720 7.199   0.50 33.66 ? 148 THR F CB    1 
ATOM   15480 O  OG1   A THR C 3 148 ? 55.613  -12.650 8.578   0.50 32.30 ? 148 THR F OG1   1 
ATOM   15481 O  OG1   B THR C 3 148 ? 55.779  -12.427 8.340   0.50 33.16 ? 148 THR F OG1   1 
ATOM   15482 C  CG2   A THR C 3 148 ? 57.225  -11.003 7.844   0.50 32.46 ? 148 THR F CG2   1 
ATOM   15483 C  CG2   B THR C 3 148 ? 57.198  -10.590 7.658   0.50 32.80 ? 148 THR F CG2   1 
ATOM   15484 N  N     A ALA C 3 149 ? 54.663  -13.571 5.362   0.50 29.73 ? 149 ALA F N     1 
ATOM   15485 N  N     B ALA C 3 149 ? 54.644  -13.290 5.290   0.50 29.53 ? 149 ALA F N     1 
ATOM   15486 C  CA    A ALA C 3 149 ? 53.841  -14.730 5.036   0.50 31.69 ? 149 ALA F CA    1 
ATOM   15487 C  CA    B ALA C 3 149 ? 53.837  -14.466 4.986   0.50 31.66 ? 149 ALA F CA    1 
ATOM   15488 C  C     A ALA C 3 149 ? 53.250  -15.353 6.296   0.50 35.53 ? 149 ALA F C     1 
ATOM   15489 C  C     B ALA C 3 149 ? 53.365  -15.150 6.264   0.50 35.50 ? 149 ALA F C     1 
ATOM   15490 O  O     A ALA C 3 149 ? 52.064  -15.708 6.330   0.50 28.12 ? 149 ALA F O     1 
ATOM   15491 O  O     B ALA C 3 149 ? 52.211  -15.592 6.355   0.50 28.63 ? 149 ALA F O     1 
ATOM   15492 C  CB    A ALA C 3 149 ? 54.671  -15.755 4.262   0.50 32.02 ? 149 ALA F CB    1 
ATOM   15493 C  CB    B ALA C 3 149 ? 54.639  -15.435 4.118   0.50 31.18 ? 149 ALA F CB    1 
ATOM   15494 N  N     A PHE C 3 150 ? 54.056  -15.465 7.355   0.50 30.61 ? 150 PHE F N     1 
ATOM   15495 N  N     B PHE C 3 150 ? 54.241  -15.224 7.269   0.50 29.41 ? 150 PHE F N     1 
ATOM   15496 C  CA    A PHE C 3 150 ? 53.544  -16.013 8.607   0.50 32.73 ? 150 PHE F CA    1 
ATOM   15497 C  CA    B PHE C 3 150 ? 53.874  -15.847 8.537   0.50 33.62 ? 150 PHE F CA    1 
ATOM   15498 C  C     A PHE C 3 150 ? 52.527  -15.078 9.249   0.50 33.73 ? 150 PHE F C     1 
ATOM   15499 C  C     B PHE C 3 150 ? 52.683  -15.142 9.178   0.50 33.50 ? 150 PHE F C     1 
ATOM   15500 O  O     A PHE C 3 150 ? 51.488  -15.533 9.744   0.50 33.16 ? 150 PHE F O     1 
ATOM   15501 O  O     B PHE C 3 150 ? 51.764  -15.798 9.684   0.50 34.28 ? 150 PHE F O     1 
ATOM   15502 C  CB    A PHE C 3 150 ? 54.694  -16.295 9.570   0.50 38.93 ? 150 PHE F CB    1 
ATOM   15503 C  CB    B PHE C 3 150 ? 55.080  -15.843 9.477   0.50 37.89 ? 150 PHE F CB    1 
ATOM   15504 C  CG    A PHE C 3 150 ? 54.285  -17.094 10.770  0.50 32.49 ? 150 PHE F CG    1 
ATOM   15505 C  CG    B PHE C 3 150 ? 55.007  -16.874 10.565  0.50 31.26 ? 150 PHE F CG    1 
ATOM   15506 C  CD1   A PHE C 3 150 ? 54.141  -18.470 10.683  0.50 34.25 ? 150 PHE F CD1   1 
ATOM   15507 C  CD1   B PHE C 3 150 ? 54.682  -18.187 10.270  0.50 37.28 ? 150 PHE F CD1   1 
ATOM   15508 C  CD2   A PHE C 3 150 ? 54.032  -16.474 11.982  0.50 40.05 ? 150 PHE F CD2   1 
ATOM   15509 C  CD2   B PHE C 3 150 ? 55.288  -16.537 11.879  0.50 37.25 ? 150 PHE F CD2   1 
ATOM   15510 C  CE1   A PHE C 3 150 ? 53.759  -19.213 11.782  0.50 37.79 ? 150 PHE F CE1   1 
ATOM   15511 C  CE1   B PHE C 3 150 ? 54.621  -19.142 11.262  0.50 34.64 ? 150 PHE F CE1   1 
ATOM   15512 C  CE2   A PHE C 3 150 ? 53.652  -17.214 13.085  0.50 38.71 ? 150 PHE F CE2   1 
ATOM   15513 C  CE2   B PHE C 3 150 ? 55.229  -17.489 12.877  0.50 35.10 ? 150 PHE F CE2   1 
ATOM   15514 C  CZ    A PHE C 3 150 ? 53.513  -18.586 12.983  0.50 37.05 ? 150 PHE F CZ    1 
ATOM   15515 C  CZ    B PHE C 3 150 ? 54.894  -18.793 12.566  0.50 40.39 ? 150 PHE F CZ    1 
ATOM   15516 N  N     A ASP C 3 151 ? 52.815  -13.772 9.266   0.50 29.41 ? 151 ASP F N     1 
ATOM   15517 N  N     B ASP C 3 151 ? 52.677  -13.805 9.155   0.50 29.57 ? 151 ASP F N     1 
ATOM   15518 C  CA    A ASP C 3 151 ? 51.838  -12.796 9.742   0.50 33.58 ? 151 ASP F CA    1 
ATOM   15519 C  CA    B ASP C 3 151 ? 51.568  -13.052 9.737   0.50 33.78 ? 151 ASP F CA    1 
ATOM   15520 C  C     A ASP C 3 151 ? 50.498  -12.977 9.044   0.50 35.16 ? 151 ASP F C     1 
ATOM   15521 C  C     B ASP C 3 151 ? 50.248  -13.383 9.056   0.50 36.17 ? 151 ASP F C     1 
ATOM   15522 O  O     A ASP C 3 151 ? 49.439  -12.907 9.681   0.50 29.56 ? 151 ASP F O     1 
ATOM   15523 O  O     B ASP C 3 151 ? 49.221  -13.550 9.724   0.50 27.70 ? 151 ASP F O     1 
ATOM   15524 C  CB    A ASP C 3 151 ? 52.363  -11.376 9.521   0.50 31.96 ? 151 ASP F CB    1 
ATOM   15525 C  CB    B ASP C 3 151 ? 51.842  -11.552 9.639   0.50 33.37 ? 151 ASP F CB    1 
ATOM   15526 C  CG    A ASP C 3 151 ? 53.432  -10.987 10.517  0.50 35.93 ? 151 ASP F CG    1 
ATOM   15527 C  CG    B ASP C 3 151 ? 53.064  -11.132 10.414  0.50 34.64 ? 151 ASP F CG    1 
ATOM   15528 O  OD1   A ASP C 3 151 ? 53.123  -10.958 11.728  0.50 29.56 ? 151 ASP F OD1   1 
ATOM   15529 O  OD1   B ASP C 3 151 ? 53.346  -11.760 11.458  0.50 29.96 ? 151 ASP F OD1   1 
ATOM   15530 O  OD2   A ASP C 3 151 ? 54.580  -10.720 10.089  0.50 25.67 ? 151 ASP F OD2   1 
ATOM   15531 O  OD2   B ASP C 3 151 ? 53.742  -10.177 9.973   0.50 33.00 ? 151 ASP F OD2   1 
ATOM   15532 N  N     A ILE C 3 152 ? 50.529  -13.218 7.731   0.50 28.59 ? 152 ILE F N     1 
ATOM   15533 N  N     B ILE C 3 152 ? 50.254  -13.468 7.723   0.50 30.02 ? 152 ILE F N     1 
ATOM   15534 C  CA    A ILE C 3 152 ? 49.307  -13.515 6.989   0.50 28.58 ? 152 ILE F CA    1 
ATOM   15535 C  CA    B ILE C 3 152 ? 49.023  -13.742 6.986   0.50 28.60 ? 152 ILE F CA    1 
ATOM   15536 C  C     A ILE C 3 152 ? 48.651  -14.779 7.528   0.50 32.28 ? 152 ILE F C     1 
ATOM   15537 C  C     B ILE C 3 152 ? 48.453  -15.099 7.384   0.50 33.64 ? 152 ILE F C     1 
ATOM   15538 O  O     A ILE C 3 152 ? 47.423  -14.844 7.680   0.50 32.17 ? 152 ILE F O     1 
ATOM   15539 O  O     B ILE C 3 152 ? 47.230  -15.275 7.472   0.50 31.70 ? 152 ILE F O     1 
ATOM   15540 C  CB    A ILE C 3 152 ? 49.616  -13.643 5.485   0.50 30.42 ? 152 ILE F CB    1 
ATOM   15541 C  CB    B ILE C 3 152 ? 49.284  -13.638 5.470   0.50 31.13 ? 152 ILE F CB    1 
ATOM   15542 C  CG1   A ILE C 3 152 ? 50.220  -12.348 4.941   0.50 30.75 ? 152 ILE F CG1   1 
ATOM   15543 C  CG1   B ILE C 3 152 ? 49.366  -12.164 5.054   0.50 29.89 ? 152 ILE F CG1   1 
ATOM   15544 C  CG2   A ILE C 3 152 ? 48.360  -14.013 4.710   0.50 31.72 ? 152 ILE F CG2   1 
ATOM   15545 C  CG2   B ILE C 3 152 ? 48.208  -14.371 4.678   0.50 31.46 ? 152 ILE F CG2   1 
ATOM   15546 C  CD1   A ILE C 3 152 ? 50.801  -12.493 3.550   0.50 28.50 ? 152 ILE F CD1   1 
ATOM   15547 C  CD1   B ILE C 3 152 ? 50.159  -11.913 3.798   0.50 30.03 ? 152 ILE F CD1   1 
ATOM   15548 N  N     A SER C 3 153 ? 49.456  -15.803 7.829   0.50 32.13 ? 153 SER F N     1 
ATOM   15549 N  N     B SER C 3 153 ? 49.325  -16.075 7.654   0.50 32.81 ? 153 SER F N     1 
ATOM   15550 C  CA    A SER C 3 153 ? 48.902  -17.098 8.213   0.50 36.37 ? 153 SER F CA    1 
ATOM   15551 C  CA    B SER C 3 153 ? 48.844  -17.359 8.152   0.50 35.59 ? 153 SER F CA    1 
ATOM   15552 C  C     A SER C 3 153 ? 48.163  -17.021 9.544   0.50 35.01 ? 153 SER F C     1 
ATOM   15553 C  C     B SER C 3 153 ? 48.334  -17.247 9.584   0.50 35.39 ? 153 SER F C     1 
ATOM   15554 O  O     A SER C 3 153 ? 47.079  -17.594 9.691   0.50 35.88 ? 153 SER F O     1 
ATOM   15555 O  O     B SER C 3 153 ? 47.484  -18.042 10.001  0.50 35.07 ? 153 SER F O     1 
ATOM   15556 C  CB    A SER C 3 153 ? 50.012  -18.147 8.284   0.50 31.61 ? 153 SER F CB    1 
ATOM   15557 C  CB    B SER C 3 153 ? 49.950  -18.411 8.065   0.50 30.42 ? 153 SER F CB    1 
ATOM   15558 O  OG    A SER C 3 153 ? 50.837  -17.950 9.419   0.50 34.93 ? 153 SER F OG    1 
ATOM   15559 O  OG    B SER C 3 153 ? 50.959  -18.178 9.032   0.50 34.39 ? 153 SER F OG    1 
ATOM   15560 N  N     A ILE C 3 154 ? 48.736  -16.325 10.530  0.50 37.84 ? 154 ILE F N     1 
ATOM   15561 N  N     B ILE C 3 154 ? 48.840  -16.278 10.350  0.50 36.85 ? 154 ILE F N     1 
ATOM   15562 C  CA    A ILE C 3 154 ? 48.089  -16.249 11.837  0.50 35.22 ? 154 ILE F CA    1 
ATOM   15563 C  CA    B ILE C 3 154 ? 48.353  -16.071 11.712  0.50 36.42 ? 154 ILE F CA    1 
ATOM   15564 C  C     A ILE C 3 154 ? 46.830  -15.397 11.769  0.50 36.82 ? 154 ILE F C     1 
ATOM   15565 C  C     B ILE C 3 154 ? 47.083  -15.233 11.705  0.50 36.02 ? 154 ILE F C     1 
ATOM   15566 O  O     A ILE C 3 154 ? 45.849  -15.671 12.471  0.50 39.15 ? 154 ILE F O     1 
ATOM   15567 O  O     B ILE C 3 154 ? 46.101  -15.562 12.380  0.50 39.52 ? 154 ILE F O     1 
ATOM   15568 C  CB    A ILE C 3 154 ? 49.077  -15.717 12.892  0.50 36.42 ? 154 ILE F CB    1 
ATOM   15569 C  CB    B ILE C 3 154 ? 49.445  -15.424 12.584  0.50 36.07 ? 154 ILE F CB    1 
ATOM   15570 C  CG1   A ILE C 3 154 ? 50.292  -16.637 12.984  0.50 37.19 ? 154 ILE F CG1   1 
ATOM   15571 C  CG1   B ILE C 3 154 ? 50.668  -16.335 12.677  0.50 37.66 ? 154 ILE F CG1   1 
ATOM   15572 C  CG2   A ILE C 3 154 ? 48.408  -15.596 14.256  0.50 41.08 ? 154 ILE F CG2   1 
ATOM   15573 C  CG2   B ILE C 3 154 ? 48.907  -15.118 13.975  0.50 41.72 ? 154 ILE F CG2   1 
ATOM   15574 C  CD1   A ILE C 3 154 ? 49.940  -18.106 13.116  0.50 38.60 ? 154 ILE F CD1   1 
ATOM   15575 C  CD1   B ILE C 3 154 ? 50.370  -17.699 13.257  0.50 37.78 ? 154 ILE F CD1   1 
ATOM   15576 N  N     A ASP C 3 155 ? 46.820  -14.373 10.913  0.50 36.52 ? 155 ASP F N     1 
ATOM   15577 N  N     B ASP C 3 155 ? 47.081  -14.139 10.938  0.50 35.83 ? 155 ASP F N     1 
ATOM   15578 C  CA    A ASP C 3 155 ? 45.673  -13.473 10.847  0.50 36.85 ? 155 ASP F CA    1 
ATOM   15579 C  CA    B ASP C 3 155 ? 45.921  -13.256 10.885  0.50 36.65 ? 155 ASP F CA    1 
ATOM   15580 C  C     A ASP C 3 155 ? 44.435  -14.183 10.308  0.50 41.08 ? 155 ASP F C     1 
ATOM   15581 C  C     B ASP C 3 155 ? 44.701  -13.926 10.263  0.50 40.30 ? 155 ASP F C     1 
ATOM   15582 O  O     A ASP C 3 155 ? 43.350  -14.087 10.893  0.50 38.12 ? 155 ASP F O     1 
ATOM   15583 O  O     B ASP C 3 155 ? 43.574  -13.477 10.504  0.50 41.54 ? 155 ASP F O     1 
ATOM   15584 C  CB    A ASP C 3 155 ? 46.014  -12.253 9.992   0.50 36.74 ? 155 ASP F CB    1 
ATOM   15585 C  CB    B ASP C 3 155 ? 46.270  -11.980 10.116  0.50 36.53 ? 155 ASP F CB    1 
ATOM   15586 C  CG    A ASP C 3 155 ? 46.998  -11.323 10.672  0.50 39.65 ? 155 ASP F CG    1 
ATOM   15587 C  CG    B ASP C 3 155 ? 47.268  -11.107 10.857  0.50 40.06 ? 155 ASP F CG    1 
ATOM   15588 O  OD1   A ASP C 3 155 ? 47.587  -11.721 11.700  0.50 43.90 ? 155 ASP F OD1   1 
ATOM   15589 O  OD1   B ASP C 3 155 ? 47.679  -11.484 11.975  0.50 42.83 ? 155 ASP F OD1   1 
ATOM   15590 O  OD2   A ASP C 3 155 ? 47.177  -10.188 10.187  0.50 36.62 ? 155 ASP F OD2   1 
ATOM   15591 O  OD2   B ASP C 3 155 ? 47.643  -10.043 10.325  0.50 36.16 ? 155 ASP F OD2   1 
ATOM   15592 N  N     A ASN C 3 156 ? 44.572  -14.899 9.193   0.50 35.50 ? 156 ASN F N     1 
ATOM   15593 N  N     B ASN C 3 156 ? 44.893  -14.980 9.473   0.50 34.87 ? 156 ASN F N     1 
ATOM   15594 C  CA    A ASN C 3 156 ? 43.438  -15.585 8.586   0.50 37.96 ? 156 ASN F CA    1 
ATOM   15595 C  CA    B ASN C 3 156 ? 43.787  -15.766 8.941   0.50 38.80 ? 156 ASN F CA    1 
ATOM   15596 C  C     A ASN C 3 156 ? 43.231  -16.995 9.130   0.50 36.64 ? 156 ASN F C     1 
ATOM   15597 C  C     B ASN C 3 156 ? 43.608  -17.094 9.664   0.50 37.98 ? 156 ASN F C     1 
ATOM   15598 O  O     A ASN C 3 156 ? 42.452  -17.758 8.550   0.50 39.29 ? 156 ASN F O     1 
ATOM   15599 O  O     B ASN C 3 156 ? 42.709  -17.860 9.306   0.50 39.84 ? 156 ASN F O     1 
ATOM   15600 C  CB    A ASN C 3 156 ? 43.593  -15.629 7.062   0.50 36.41 ? 156 ASN F CB    1 
ATOM   15601 C  CB    B ASN C 3 156 ? 43.984  -16.024 7.445   0.50 36.11 ? 156 ASN F CB    1 
ATOM   15602 C  CG    A ASN C 3 156 ? 44.894  -16.270 6.617   0.50 36.61 ? 156 ASN F CG    1 
ATOM   15603 C  CG    B ASN C 3 156 ? 43.887  -14.761 6.615   0.50 39.49 ? 156 ASN F CG    1 
ATOM   15604 O  OD1   A ASN C 3 156 ? 45.541  -16.993 7.372   0.50 38.98 ? 156 ASN F OD1   1 
ATOM   15605 O  OD1   B ASN C 3 156 ? 42.985  -13.941 6.805   0.50 42.43 ? 156 ASN F OD1   1 
ATOM   15606 N  ND2   A ASN C 3 156 ? 45.278  -16.011 5.376   0.50 31.80 ? 156 ASN F ND2   1 
ATOM   15607 N  ND2   B ASN C 3 156 ? 44.820  -14.596 5.689   0.50 26.89 ? 156 ASN F ND2   1 
ATOM   15608 N  N     A GLY C 3 157 ? 43.912  -17.356 10.215  0.50 40.36 ? 157 GLY F N     1 
ATOM   15609 N  N     B GLY C 3 157 ? 44.439  -17.384 10.664  0.50 39.96 ? 157 GLY F N     1 
ATOM   15610 C  CA    A GLY C 3 157 ? 43.677  -18.635 10.870  0.50 35.57 ? 157 GLY F CA    1 
ATOM   15611 C  CA    B GLY C 3 157 ? 44.312  -18.625 11.410  0.50 34.74 ? 157 GLY F CA    1 
ATOM   15612 C  C     A GLY C 3 157 ? 43.943  -19.849 10.007  0.50 38.01 ? 157 GLY F C     1 
ATOM   15613 C  C     B GLY C 3 157 ? 44.492  -19.873 10.576  0.50 38.46 ? 157 GLY F C     1 
ATOM   15614 O  O     A GLY C 3 157 ? 43.165  -20.810 10.035  0.50 36.78 ? 157 GLY F O     1 
ATOM   15615 O  O     B GLY C 3 157 ? 43.947  -20.927 10.923  0.50 35.75 ? 157 GLY F O     1 
ATOM   15616 N  N     A ASN C 3 158 ? 45.029  -19.831 9.237   0.50 36.63 ? 158 ASN F N     1 
ATOM   15617 N  N     B ASN C 3 158 ? 45.243  -19.785 9.478   0.50 36.73 ? 158 ASN F N     1 
ATOM   15618 C  CA    A ASN C 3 158 ? 45.389  -20.948 8.366   0.50 36.93 ? 158 ASN F CA    1 
ATOM   15619 C  CA    B ASN C 3 158 ? 45.479  -20.929 8.598   0.50 36.95 ? 158 ASN F CA    1 
ATOM   15620 C  C     A ASN C 3 158 ? 46.470  -21.759 9.074   0.50 39.15 ? 158 ASN F C     1 
ATOM   15621 C  C     B ASN C 3 158 ? 46.552  -21.803 9.235   0.50 39.33 ? 158 ASN F C     1 
ATOM   15622 O  O     A ASN C 3 158 ? 47.663  -21.486 8.943   0.50 36.50 ? 158 ASN F O     1 
ATOM   15623 O  O     B ASN C 3 158 ? 47.751  -21.579 9.068   0.50 36.56 ? 158 ASN F O     1 
ATOM   15624 C  CB    A ASN C 3 158 ? 45.853  -20.447 7.003   0.50 33.62 ? 158 ASN F CB    1 
ATOM   15625 C  CB    B ASN C 3 158 ? 45.890  -20.461 7.206   0.50 33.73 ? 158 ASN F CB    1 
ATOM   15626 C  CG    A ASN C 3 158 ? 45.838  -21.533 5.947   0.50 36.32 ? 158 ASN F CG    1 
ATOM   15627 C  CG    B ASN C 3 158 ? 45.835  -21.572 6.175   0.50 36.37 ? 158 ASN F CG    1 
ATOM   15628 O  OD1   A ASN C 3 158 ? 46.070  -22.705 6.240   0.50 37.13 ? 158 ASN F OD1   1 
ATOM   15629 O  OD1   B ASN C 3 158 ? 45.831  -22.755 6.515   0.50 36.65 ? 158 ASN F OD1   1 
ATOM   15630 N  ND2   A ASN C 3 158 ? 45.553  -21.148 4.711   0.50 33.21 ? 158 ASN F ND2   1 
ATOM   15631 N  ND2   B ASN C 3 158 ? 45.791  -21.193 4.904   0.50 33.31 ? 158 ASN F ND2   1 
ATOM   15632 N  N     A GLU C 3 159 ? 46.042  -22.772 9.834   0.50 37.86 ? 159 GLU F N     1 
ATOM   15633 N  N     B GLU C 3 159 ? 46.111  -22.822 9.979   0.50 37.79 ? 159 GLU F N     1 
ATOM   15634 C  CA    A GLU C 3 159 ? 46.997  -23.588 10.578  0.50 35.11 ? 159 GLU F CA    1 
ATOM   15635 C  CA    B GLU C 3 159 ? 47.055  -23.693 10.674  0.50 35.16 ? 159 GLU F CA    1 
ATOM   15636 C  C     A GLU C 3 159 ? 47.860  -24.439 9.654   0.50 38.55 ? 159 GLU F C     1 
ATOM   15637 C  C     B GLU C 3 159 ? 47.860  -24.555 9.708   0.50 38.59 ? 159 GLU F C     1 
ATOM   15638 O  O     A GLU C 3 159 ? 49.029  -24.694 9.967   0.50 32.12 ? 159 GLU F O     1 
ATOM   15639 O  O     B GLU C 3 159 ? 49.016  -24.886 9.997   0.50 31.72 ? 159 GLU F O     1 
ATOM   15640 C  CB    A GLU C 3 159 ? 46.268  -24.483 11.578  0.50 43.03 ? 159 GLU F CB    1 
ATOM   15641 C  CB    B GLU C 3 159 ? 46.314  -24.574 11.678  0.50 42.96 ? 159 GLU F CB    1 
ATOM   15642 C  CG    A GLU C 3 159 ? 45.396  -23.732 12.561  0.50 42.64 ? 159 GLU F CG    1 
ATOM   15643 C  CG    B GLU C 3 159 ? 45.898  -23.847 12.942  0.50 42.36 ? 159 GLU F CG    1 
ATOM   15644 C  CD    A GLU C 3 159 ? 45.044  -24.566 13.775  0.50 48.90 ? 159 GLU F CD    1 
ATOM   15645 C  CD    B GLU C 3 159 ? 44.945  -24.660 13.793  0.50 48.88 ? 159 GLU F CD    1 
ATOM   15646 O  OE1   A GLU C 3 159 ? 45.900  -25.362 14.216  0.50 50.24 ? 159 GLU F OE1   1 
ATOM   15647 O  OE1   B GLU C 3 159 ? 44.124  -25.406 13.218  0.50 48.22 ? 159 GLU F OE1   1 
ATOM   15648 O  OE2   A GLU C 3 159 ? 43.911  -24.428 14.283  0.50 50.22 ? 159 GLU F OE2   1 
ATOM   15649 O  OE2   B GLU C 3 159 ? 45.019  -24.557 15.035  0.50 54.91 ? 159 GLU F OE2   1 
ATOM   15650 N  N     A ASP C 3 160 ? 47.305  -24.901 8.531   0.50 35.54 ? 160 ASP F N     1 
ATOM   15651 N  N     B ASP C 3 160 ? 47.271  -24.941 8.573   0.50 35.52 ? 160 ASP F N     1 
ATOM   15652 C  CA    A ASP C 3 160 ? 48.104  -25.658 7.571   0.50 37.70 ? 160 ASP F CA    1 
ATOM   15653 C  CA    B ASP C 3 160 ? 48.020  -25.705 7.579   0.50 37.69 ? 160 ASP F CA    1 
ATOM   15654 C  C     A ASP C 3 160 ? 49.249  -24.811 7.034   0.50 38.28 ? 160 ASP F C     1 
ATOM   15655 C  C     B ASP C 3 160 ? 49.203  -24.902 7.056   0.50 38.29 ? 160 ASP F C     1 
ATOM   15656 O  O     A ASP C 3 160 ? 50.398  -25.264 6.968   0.50 36.93 ? 160 ASP F O     1 
ATOM   15657 O  O     B ASP C 3 160 ? 50.332  -25.403 6.989   0.50 36.75 ? 160 ASP F O     1 
ATOM   15658 C  CB    A ASP C 3 160 ? 47.221  -26.150 6.425   0.50 38.79 ? 160 ASP F CB    1 
ATOM   15659 C  CB    B ASP C 3 160 ? 47.105  -26.114 6.424   0.50 38.81 ? 160 ASP F CB    1 
ATOM   15660 C  CG    A ASP C 3 160 ? 46.195  -27.167 6.873   0.50 41.15 ? 160 ASP F CG    1 
ATOM   15661 C  CG    B ASP C 3 160 ? 46.105  -27.178 6.817   0.50 41.14 ? 160 ASP F CG    1 
ATOM   15662 O  OD1   A ASP C 3 160 ? 46.595  -28.233 7.390   0.50 38.77 ? 160 ASP F OD1   1 
ATOM   15663 O  OD1   B ASP C 3 160 ? 46.031  -27.515 8.019   0.50 42.77 ? 160 ASP F OD1   1 
ATOM   15664 O  OD2   A ASP C 3 160 ? 44.986  -26.893 6.719   0.50 38.02 ? 160 ASP F OD2   1 
ATOM   15665 O  OD2   B ASP C 3 160 ? 45.398  -27.681 5.917   0.50 38.01 ? 160 ASP F OD2   1 
ATOM   15666 N  N     A LEU C 3 161 ? 48.947  -23.571 6.640   0.50 36.84 ? 161 LEU F N     1 
ATOM   15667 N  N     B LEU C 3 161 ? 48.954  -23.649 6.671   0.50 36.83 ? 161 LEU F N     1 
ATOM   15668 C  CA    A LEU C 3 161 ? 49.987  -22.655 6.183   0.50 32.36 ? 161 LEU F CA    1 
ATOM   15669 C  CA    B LEU C 3 161 ? 50.029  -22.784 6.196   0.50 32.31 ? 161 LEU F CA    1 
ATOM   15670 C  C     A LEU C 3 161 ? 50.976  -22.345 7.301   0.50 37.11 ? 161 LEU F C     1 
ATOM   15671 C  C     B LEU C 3 161 ? 51.010  -22.460 7.316   0.50 37.06 ? 161 LEU F C     1 
ATOM   15672 O  O     A LEU C 3 161 ? 52.192  -22.319 7.075   0.50 33.50 ? 161 LEU F O     1 
ATOM   15673 O  O     B LEU C 3 161 ? 52.222  -22.375 7.081   0.50 33.47 ? 161 LEU F O     1 
ATOM   15674 C  CB    A LEU C 3 161 ? 49.342  -21.373 5.657   0.50 31.29 ? 161 LEU F CB    1 
ATOM   15675 C  CB    B LEU C 3 161 ? 49.429  -21.507 5.608   0.50 31.30 ? 161 LEU F CB    1 
ATOM   15676 C  CG    A LEU C 3 161 ? 50.209  -20.172 5.278   0.50 33.73 ? 161 LEU F CG    1 
ATOM   15677 C  CG    B LEU C 3 161 ? 50.340  -20.413 5.054   0.50 34.21 ? 161 LEU F CG    1 
ATOM   15678 C  CD1   A LEU C 3 161 ? 51.164  -20.517 4.144   0.50 30.06 ? 161 LEU F CD1   1 
ATOM   15679 C  CD1   B LEU C 3 161 ? 51.267  -20.961 3.982   0.50 29.72 ? 161 LEU F CD1   1 
ATOM   15680 C  CD2   A LEU C 3 161 ? 49.313  -18.997 4.896   0.50 30.68 ? 161 LEU F CD2   1 
ATOM   15681 C  CD2   B LEU C 3 161 ? 49.483  -19.284 4.502   0.50 32.12 ? 161 LEU F CD2   1 
ATOM   15682 N  N     A ALA C 3 162 ? 50.470  -22.119 8.518   0.50 30.32 ? 162 ALA F N     1 
ATOM   15683 N  N     B ALA C 3 162 ? 50.504  -22.286 8.541   0.50 30.44 ? 162 ALA F N     1 
ATOM   15684 C  CA    A ALA C 3 162 ? 51.346  -21.789 9.639   0.50 34.33 ? 162 ALA F CA    1 
ATOM   15685 C  CA    B ALA C 3 162 ? 51.370  -21.958 9.671   0.50 34.55 ? 162 ALA F CA    1 
ATOM   15686 C  C     A ALA C 3 162 ? 52.349  -22.903 9.910   0.50 37.55 ? 162 ALA F C     1 
ATOM   15687 C  C     B ALA C 3 162 ? 52.433  -23.029 9.881   0.50 37.59 ? 162 ALA F C     1 
ATOM   15688 O  O     A ALA C 3 162 ? 53.534  -22.636 10.146  0.50 38.40 ? 162 ALA F O     1 
ATOM   15689 O  O     B ALA C 3 162 ? 53.621  -22.720 10.039  0.50 38.24 ? 162 ALA F O     1 
ATOM   15690 C  CB    A ALA C 3 162 ? 50.512  -21.503 10.889  0.50 35.36 ? 162 ALA F CB    1 
ATOM   15691 C  CB    B ALA C 3 162 ? 50.530  -21.777 10.936  0.50 34.93 ? 162 ALA F CB    1 
ATOM   15692 N  N     A GLU C 3 163 ? 51.894  -24.159 9.881   0.50 34.11 ? 163 GLU F N     1 
ATOM   15693 N  N     B GLU C 3 163 ? 52.026  -24.301 9.878   0.50 34.30 ? 163 GLU F N     1 
ATOM   15694 C  CA    A GLU C 3 163 ? 52.803  -25.281 10.103  0.50 39.31 ? 163 GLU F CA    1 
ATOM   15695 C  CA    B GLU C 3 163 ? 52.992  -25.378 10.065  0.50 39.50 ? 163 GLU F CA    1 
ATOM   15696 C  C     A GLU C 3 163 ? 53.921  -25.295 9.068   0.50 38.43 ? 163 GLU F C     1 
ATOM   15697 C  C     B GLU C 3 163 ? 53.936  -25.499 8.877   0.50 38.29 ? 163 GLU F C     1 
ATOM   15698 O  O     A GLU C 3 163 ? 55.091  -25.504 9.409   0.50 41.68 ? 163 GLU F O     1 
ATOM   15699 O  O     B GLU C 3 163 ? 55.083  -25.929 9.042   0.50 43.08 ? 163 GLU F O     1 
ATOM   15700 C  CB    A GLU C 3 163 ? 52.031  -26.602 10.067  0.50 39.61 ? 163 GLU F CB    1 
ATOM   15701 C  CB    B GLU C 3 163 ? 52.272  -26.703 10.302  0.50 39.98 ? 163 GLU F CB    1 
ATOM   15702 C  CG    A GLU C 3 163 ? 51.034  -26.787 11.201  0.50 42.06 ? 163 GLU F CG    1 
ATOM   15703 C  CG    B GLU C 3 163 ? 51.402  -26.721 11.546  0.50 41.91 ? 163 GLU F CG    1 
ATOM   15704 C  CD    A GLU C 3 163 ? 50.182  -28.035 11.032  0.50 41.27 ? 163 GLU F CD    1 
ATOM   15705 C  CD    B GLU C 3 163 ? 50.953  -28.119 11.915  0.50 42.15 ? 163 GLU F CD    1 
ATOM   15706 O  OE1   A GLU C 3 163 ? 50.551  -28.904 10.215  0.50 47.76 ? 163 GLU F OE1   1 
ATOM   15707 O  OE1   B GLU C 3 163 ? 51.638  -29.085 11.519  0.50 46.48 ? 163 GLU F OE1   1 
ATOM   15708 O  OE2   A GLU C 3 163 ? 49.141  -28.143 11.711  0.50 46.83 ? 163 GLU F OE2   1 
ATOM   15709 O  OE2   B GLU C 3 163 ? 49.916  -28.253 12.599  0.50 47.09 ? 163 GLU F OE2   1 
ATOM   15710 N  N     A ILE C 3 164 ? 53.579  -25.060 7.800   0.50 36.80 ? 164 ILE F N     1 
ATOM   15711 N  N     B ILE C 3 164 ? 53.476  -25.135 7.678   0.50 36.71 ? 164 ILE F N     1 
ATOM   15712 C  CA    A ILE C 3 164 ? 54.565  -25.132 6.727   0.50 37.87 ? 164 ILE F CA    1 
ATOM   15713 C  CA    B ILE C 3 164 ? 54.358  -25.144 6.513   0.50 38.00 ? 164 ILE F CA    1 
ATOM   15714 C  C     A ILE C 3 164 ? 55.617  -24.037 6.864   0.50 37.70 ? 164 ILE F C     1 
ATOM   15715 C  C     B ILE C 3 164 ? 55.492  -24.145 6.703   0.50 37.74 ? 164 ILE F C     1 
ATOM   15716 O  O     A ILE C 3 164 ? 56.777  -24.228 6.477   0.50 43.25 ? 164 ILE F O     1 
ATOM   15717 O  O     B ILE C 3 164 ? 56.667  -24.456 6.473   0.50 43.52 ? 164 ILE F O     1 
ATOM   15718 C  CB    A ILE C 3 164 ? 53.848  -25.069 5.365   0.50 38.20 ? 164 ILE F CB    1 
ATOM   15719 C  CB    B ILE C 3 164 ? 53.558  -24.855 5.230   0.50 38.19 ? 164 ILE F CB    1 
ATOM   15720 C  CG1   A ILE C 3 164 ? 52.881  -26.246 5.222   0.50 37.90 ? 164 ILE F CG1   1 
ATOM   15721 C  CG1   B ILE C 3 164 ? 52.679  -26.053 4.866   0.50 39.00 ? 164 ILE F CG1   1 
ATOM   15722 C  CG2   A ILE C 3 164 ? 54.847  -25.062 4.225   0.50 37.72 ? 164 ILE F CG2   1 
ATOM   15723 C  CG2   B ILE C 3 164 ? 54.492  -24.508 4.083   0.50 36.63 ? 164 ILE F CG2   1 
ATOM   15724 C  CD1   A ILE C 3 164 ? 52.001  -26.170 3.991   0.50 36.82 ? 164 ILE F CD1   1 
ATOM   15725 C  CD1   B ILE C 3 164 ? 53.460  -27.292 4.493   0.50 39.02 ? 164 ILE F CD1   1 
ATOM   15726 N  N     A LEU C 3 165 ? 55.249  -22.881 7.413   0.50 34.59 ? 165 LEU F N     1 
ATOM   15727 N  N     B LEU C 3 165 ? 55.158  -22.927 7.132   0.50 34.16 ? 165 LEU F N     1 
ATOM   15728 C  CA    A LEU C 3 165 ? 56.189  -21.773 7.515   0.50 38.40 ? 165 LEU F CA    1 
ATOM   15729 C  CA    B LEU C 3 165 ? 56.169  -21.896 7.330   0.50 38.39 ? 165 LEU F CA    1 
ATOM   15730 C  C     A LEU C 3 165 ? 57.060  -21.833 8.764   0.50 42.49 ? 165 LEU F C     1 
ATOM   15731 C  C     B LEU C 3 165 ? 57.093  -22.186 8.507   0.50 42.44 ? 165 LEU F C     1 
ATOM   15732 O  O     A LEU C 3 165 ? 58.124  -21.203 8.789   0.50 49.23 ? 165 LEU F O     1 
ATOM   15733 O  O     B LEU C 3 165 ? 58.149  -21.552 8.610   0.50 48.10 ? 165 LEU F O     1 
ATOM   15734 C  CB    A LEU C 3 165 ? 55.437  -20.440 7.479   0.50 34.79 ? 165 LEU F CB    1 
ATOM   15735 C  CB    B LEU C 3 165 ? 55.493  -20.536 7.518   0.50 34.79 ? 165 LEU F CB    1 
ATOM   15736 C  CG    A LEU C 3 165 ? 54.656  -20.181 6.189   0.50 31.13 ? 165 LEU F CG    1 
ATOM   15737 C  CG    B LEU C 3 165 ? 54.932  -19.890 6.248   0.50 32.37 ? 165 LEU F CG    1 
ATOM   15738 C  CD1   A LEU C 3 165 ? 53.965  -18.835 6.239   0.50 28.59 ? 165 LEU F CD1   1 
ATOM   15739 C  CD1   B LEU C 3 165 ? 53.718  -19.037 6.554   0.50 30.37 ? 165 LEU F CD1   1 
ATOM   15740 C  CD2   A LEU C 3 165 ? 55.579  -20.267 4.980   0.50 28.57 ? 165 LEU F CD2   1 
ATOM   15741 C  CD2   B LEU C 3 165 ? 56.004  -19.054 5.563   0.50 26.58 ? 165 LEU F CD2   1 
ATOM   15742 N  N     A GLN C 3 166 ? 56.644  -22.573 9.793   0.50 42.23 ? 166 GLN F N     1 
ATOM   15743 N  N     B GLN C 3 166 ? 56.736  -23.122 9.381   0.50 44.75 ? 166 GLN F N     1 
ATOM   15744 C  CA    A GLN C 3 166 ? 57.443  -22.675 11.009  0.50 44.40 ? 166 GLN F CA    1 
ATOM   15745 C  CA    B GLN C 3 166 ? 57.564  -23.468 10.539  0.50 47.55 ? 166 GLN F CA    1 
ATOM   15746 C  C     A GLN C 3 166 ? 58.640  -23.603 10.841  0.50 48.65 ? 166 GLN F C     1 
ATOM   15747 C  C     B GLN C 3 166 ? 58.321  -24.773 10.290  0.50 46.86 ? 166 GLN F C     1 
ATOM   15748 O  O     A GLN C 3 166 ? 59.674  -23.394 11.485  0.50 52.82 ? 166 GLN F O     1 
ATOM   15749 O  O     B GLN C 3 166 ? 58.136  -25.779 10.976  0.50 47.19 ? 166 GLN F O     1 
ATOM   15750 C  CB    A GLN C 3 166 ? 56.572  -23.158 12.169  0.50 42.22 ? 166 GLN F CB    1 
ATOM   15751 C  CB    B GLN C 3 166 ? 56.704  -23.562 11.795  0.50 40.45 ? 166 GLN F CB    1 
ATOM   15752 C  CG    A GLN C 3 166 ? 55.533  -22.151 12.625  0.50 41.64 ? 166 GLN F CG    1 
ATOM   15753 C  CG    B GLN C 3 166 ? 56.071  -22.251 12.220  0.50 41.15 ? 166 GLN F CG    1 
ATOM   15754 C  CD    A GLN C 3 166 ? 54.435  -22.782 13.457  0.50 38.65 ? 166 GLN F CD    1 
ATOM   15755 C  CD    B GLN C 3 166 ? 55.223  -22.398 13.468  0.50 39.25 ? 166 GLN F CD    1 
ATOM   15756 O  OE1   A GLN C 3 166 ? 54.641  -23.133 14.617  0.50 44.83 ? 166 GLN F OE1   1 
ATOM   15757 O  OE1   B GLN C 3 166 ? 54.002  -22.528 13.390  0.50 38.21 ? 166 GLN F OE1   1 
ATOM   15758 N  NE2   A GLN C 3 166 ? 53.258  -22.933 12.862  0.50 39.11 ? 166 GLN F NE2   1 
ATOM   15759 N  NE2   B GLN C 3 166 ? 55.868  -22.378 14.628  0.50 44.41 ? 166 GLN F NE2   1 
ATOM   15760 N  N     A LYS C 3 167 ? 58.524  -24.620 9.994   0.50 46.28 ? 167 LYS F N     1 
ATOM   15761 N  N     B LYS C 3 167 ? 59.195  -24.741 9.291   0.50 52.06 ? 167 LYS F N     1 
ATOM   15762 C  CA    A LYS C 3 167 ? 59.598  -25.591 9.810   0.50 49.73 ? 167 LYS F CA    1 
ATOM   15763 C  CA    B LYS C 3 167 ? 59.981  -25.915 8.927   0.50 48.97 ? 167 LYS F CA    1 
ATOM   15764 C  C     A LYS C 3 167 ? 60.763  -25.002 9.014   0.50 51.43 ? 167 LYS F C     1 
ATOM   15765 C  C     B LYS C 3 167 ? 61.475  -25.610 8.927   0.50 54.08 ? 167 LYS F C     1 
ATOM   15766 O  O     A LYS C 3 167 ? 60.574  -24.158 8.135   0.50 38.95 ? 167 LYS F O     1 
ATOM   15767 O  O     B LYS C 3 167 ? 62.289  -26.454 9.305   0.50 55.20 ? 167 LYS F O     1 
ATOM   15768 C  CB    A LYS C 3 167 ? 59.063  -26.845 9.113   0.50 46.66 ? 167 LYS F CB    1 
ATOM   15769 C  CB    B LYS C 3 167 ? 59.550  -26.441 7.556   0.50 47.80 ? 167 LYS F CB    1 
ATOM   15770 C  CG    A LYS C 3 167 ? 58.271  -26.541 7.858   0.50 48.37 ? 167 LYS F CG    1 
ATOM   15771 C  CG    B LYS C 3 167 ? 58.182  -27.109 7.553   0.50 49.57 ? 167 LYS F CG    1 
ATOM   15772 C  CD    A LYS C 3 167 ? 58.105  -27.760 6.975   0.50 51.02 ? 167 LYS F CD    1 
ATOM   15773 C  CD    B LYS C 3 167 ? 57.717  -27.462 6.143   0.50 51.24 ? 167 LYS F CD    1 
ATOM   15774 C  CE    A LYS C 3 167 ? 57.798  -27.339 5.546   0.50 51.64 ? 167 LYS F CE    1 
ATOM   15775 C  CE    B LYS C 3 167 ? 58.721  -28.344 5.406   0.50 50.10 ? 167 LYS F CE    1 
ATOM   15776 N  NZ    A LYS C 3 167 ? 58.814  -26.369 5.049   0.50 33.96 ? 167 LYS F NZ    1 
ATOM   15777 N  NZ    B LYS C 3 167 ? 59.657  -27.556 4.556   0.50 50.63 ? 167 LYS F NZ    1 
HETATM 15778 P  PG    A GTP D 4 .   ? 2.154   -11.796 17.912  0.50 19.10 ? 501 GTP A PG    1 
HETATM 15779 P  PG    B GTP D 4 .   ? 2.493   -11.283 18.092  0.50 22.31 ? 501 GTP A PG    1 
HETATM 15780 O  O1G   A GTP D 4 .   ? 2.265   -13.283 18.144  0.50 22.81 ? 501 GTP A O1G   1 
HETATM 15781 O  O1G   B GTP D 4 .   ? 2.551   -12.787 18.136  0.50 20.07 ? 501 GTP A O1G   1 
HETATM 15782 O  O2G   A GTP D 4 .   ? 1.407   -11.505 16.643  0.50 22.41 ? 501 GTP A O2G   1 
HETATM 15783 O  O2G   B GTP D 4 .   ? 1.723   -10.813 16.890  0.50 20.33 ? 501 GTP A O2G   1 
HETATM 15784 O  O3G   A GTP D 4 .   ? 3.526   -11.185 17.865  0.50 22.86 ? 501 GTP A O3G   1 
HETATM 15785 O  O3G   B GTP D 4 .   ? 3.886   -10.714 18.078  0.50 24.78 ? 501 GTP A O3G   1 
HETATM 15786 O  O3B   A GTP D 4 .   ? 1.294   -11.099 19.107  0.50 23.46 ? 501 GTP A O3B   1 
HETATM 15787 O  O3B   B GTP D 4 .   ? 1.715   -10.696 19.396  0.50 19.44 ? 501 GTP A O3B   1 
HETATM 15788 P  PB    A GTP D 4 .   ? 0.765   -11.811 20.455  0.50 21.81 ? 501 GTP A PB    1 
HETATM 15789 P  PB    B GTP D 4 .   ? 0.985   -11.593 20.515  0.50 22.10 ? 501 GTP A PB    1 
HETATM 15790 O  O1B   A GTP D 4 .   ? -0.235  -10.841 21.053  0.50 17.96 ? 501 GTP A O1B   1 
HETATM 15791 O  O1B   B GTP D 4 .   ? 0.301   -10.624 21.451  0.50 20.52 ? 501 GTP A O1B   1 
HETATM 15792 O  O2B   A GTP D 4 .   ? 0.134   -13.152 20.201  0.50 17.58 ? 501 GTP A O2B   1 
HETATM 15793 O  O2B   B GTP D 4 .   ? -0.014  -12.529 19.883  0.50 19.07 ? 501 GTP A O2B   1 
HETATM 15794 O  O3A   A GTP D 4 .   ? 2.057   -11.932 21.403  0.50 19.09 ? 501 GTP A O3A   1 
HETATM 15795 O  O3A   B GTP D 4 .   ? 2.166   -12.396 21.251  0.50 21.89 ? 501 GTP A O3A   1 
HETATM 15796 P  PA    A GTP D 4 .   ? 1.988   -12.492 22.914  0.50 24.05 ? 501 GTP A PA    1 
HETATM 15797 P  PA    B GTP D 4 .   ? 2.200   -12.778 22.817  0.50 24.85 ? 501 GTP A PA    1 
HETATM 15798 O  O1A   A GTP D 4 .   ? 0.689   -12.074 23.563  0.50 20.10 ? 501 GTP A O1A   1 
HETATM 15799 O  O1A   B GTP D 4 .   ? 0.842   -12.597 23.446  0.50 22.08 ? 501 GTP A O1A   1 
HETATM 15800 O  O2A   A GTP D 4 .   ? 2.181   -13.984 22.925  0.50 26.68 ? 501 GTP A O2A   1 
HETATM 15801 O  O2A   B GTP D 4 .   ? 2.700   -14.195 22.941  0.50 25.68 ? 501 GTP A O2A   1 
HETATM 15802 O  "O5'" A GTP D 4 .   ? 3.224   -11.722 23.601  0.50 20.91 ? 501 GTP A "O5'" 1 
HETATM 15803 O  "O5'" B GTP D 4 .   ? 3.234   -11.723 23.463  0.50 20.92 ? 501 GTP A "O5'" 1 
HETATM 15804 C  "C5'" A GTP D 4 .   ? 4.344   -12.380 24.128  0.50 20.19 ? 501 GTP A "C5'" 1 
HETATM 15805 C  "C5'" B GTP D 4 .   ? 4.445   -12.122 24.053  0.50 20.42 ? 501 GTP A "C5'" 1 
HETATM 15806 C  "C4'" A GTP D 4 .   ? 4.463   -12.016 25.601  0.50 22.75 ? 501 GTP A "C4'" 1 
HETATM 15807 C  "C4'" B GTP D 4 .   ? 4.452   -11.809 25.545  0.50 22.13 ? 501 GTP A "C4'" 1 
HETATM 15808 O  "O4'" A GTP D 4 .   ? 3.320   -12.503 26.291  0.50 20.30 ? 501 GTP A "O4'" 1 
HETATM 15809 O  "O4'" B GTP D 4 .   ? 3.267   -12.316 26.148  0.50 20.29 ? 501 GTP A "O4'" 1 
HETATM 15810 C  "C3'" A GTP D 4 .   ? 5.681   -12.675 26.212  0.50 20.30 ? 501 GTP A "C3'" 1 
HETATM 15811 C  "C3'" B GTP D 4 .   ? 5.627   -12.493 26.215  0.50 20.11 ? 501 GTP A "C3'" 1 
HETATM 15812 O  "O3'" A GTP D 4 .   ? 6.210   -11.800 27.173  0.50 24.53 ? 501 GTP A "O3'" 1 
HETATM 15813 O  "O3'" B GTP D 4 .   ? 6.111   -11.658 27.235  0.50 24.20 ? 501 GTP A "O3'" 1 
HETATM 15814 C  "C2'" A GTP D 4 .   ? 5.132   -13.902 26.893  0.50 25.07 ? 501 GTP A "C2'" 1 
HETATM 15815 C  "C2'" B GTP D 4 .   ? 5.022   -13.730 26.831  0.50 24.52 ? 501 GTP A "C2'" 1 
HETATM 15816 O  "O2'" A GTP D 4 .   ? 5.896   -14.235 28.037  0.50 21.05 ? 501 GTP A "O2'" 1 
HETATM 15817 O  "O2'" B GTP D 4 .   ? 5.725   -14.121 27.994  0.50 22.27 ? 501 GTP A "O2'" 1 
HETATM 15818 C  "C1'" A GTP D 4 .   ? 3.713   -13.480 27.238  0.50 20.70 ? 501 GTP A "C1'" 1 
HETATM 15819 C  "C1'" B GTP D 4 .   ? 3.602   -13.281 27.129  0.50 20.57 ? 501 GTP A "C1'" 1 
HETATM 15820 N  N9    A GTP D 4 .   ? 2.755   -14.594 27.142  0.50 25.48 ? 501 GTP A N9    1 
HETATM 15821 N  N9    B GTP D 4 .   ? 2.630   -14.383 27.025  0.50 26.16 ? 501 GTP A N9    1 
HETATM 15822 C  C8    A GTP D 4 .   ? 2.390   -15.329 26.046  0.50 21.96 ? 501 GTP A C8    1 
HETATM 15823 C  C8    B GTP D 4 .   ? 2.207   -15.041 25.901  0.50 22.08 ? 501 GTP A C8    1 
HETATM 15824 N  N7    A GTP D 4 .   ? 1.449   -16.226 26.430  0.50 23.20 ? 501 GTP A N7    1 
HETATM 15825 N  N7    B GTP D 4 .   ? 1.283   -15.960 26.266  0.50 23.39 ? 501 GTP A N7    1 
HETATM 15826 C  C5    A GTP D 4 .   ? 1.202   -16.055 27.749  0.50 24.17 ? 501 GTP A C5    1 
HETATM 15827 C  C5    B GTP D 4 .   ? 1.095   -15.878 27.604  0.50 23.78 ? 501 GTP A C5    1 
HETATM 15828 C  C6    A GTP D 4 .   ? 0.349   -16.678 28.653  0.50 23.95 ? 501 GTP A C6    1 
HETATM 15829 C  C6    B GTP D 4 .   ? 0.278   -16.563 28.494  0.50 23.88 ? 501 GTP A C6    1 
HETATM 15830 O  O6    A GTP D 4 .   ? -0.383  -17.596 28.285  0.50 26.64 ? 501 GTP A O6    1 
HETATM 15831 O  O6    B GTP D 4 .   ? -0.473  -17.449 28.089  0.50 26.46 ? 501 GTP A O6    1 
HETATM 15832 N  N1    A GTP D 4 .   ? 0.337   -16.261 29.970  0.50 23.00 ? 501 GTP A N1    1 
HETATM 15833 N  N1    B GTP D 4 .   ? 0.322   -16.244 29.837  0.50 22.87 ? 501 GTP A N1    1 
HETATM 15834 C  C2    A GTP D 4 .   ? 1.157   -15.232 30.383  0.50 23.78 ? 501 GTP A C2    1 
HETATM 15835 C  C2    B GTP D 4 .   ? 1.165   -15.249 30.288  0.50 23.77 ? 501 GTP A C2    1 
HETATM 15836 N  N2    A GTP D 4 .   ? 1.156   -14.818 31.646  0.50 21.34 ? 501 GTP A N2    1 
HETATM 15837 N  N2    B GTP D 4 .   ? 1.213   -14.931 31.579  0.50 21.40 ? 501 GTP A N2    1 
HETATM 15838 N  N3    A GTP D 4 .   ? 2.002   -14.624 29.481  0.50 22.74 ? 501 GTP A N3    1 
HETATM 15839 N  N3    B GTP D 4 .   ? 1.976   -14.577 29.397  0.50 22.71 ? 501 GTP A N3    1 
HETATM 15840 C  C4    A GTP D 4 .   ? 2.013   -15.027 28.196  0.50 21.09 ? 501 GTP A C4    1 
HETATM 15841 C  C4    B GTP D 4 .   ? 1.932   -14.884 28.085  0.50 21.04 ? 501 GTP A C4    1 
HETATM 15842 MG MG    A MG  E 5 .   ? 0.694   -14.433 18.651  0.50 25.07 2 502 MG  A MG    1 
HETATM 15843 MG MG    B MG  E 5 .   ? 1.215   -14.326 18.863  0.50 24.50 2 502 MG  A MG    1 
HETATM 15844 CA CA    A CA  F 6 .   ? -31.994 -14.683 34.401  0.50 43.43 2 503 CA  A CA    1 
HETATM 15845 CA CA    B CA  F 6 .   ? -31.936 -14.769 33.998  0.50 37.34 2 503 CA  A CA    1 
HETATM 15846 P  PB    A GDP G 7 .   ? 27.839  -23.693 -9.987  0.50 34.65 ? 501 GDP B PB    1 
HETATM 15847 P  PB    B GDP G 7 .   ? 27.615  -23.365 -10.101 0.50 34.89 ? 501 GDP B PB    1 
HETATM 15848 O  O1B   A GDP G 7 .   ? 28.314  -22.560 -10.861 0.50 28.15 ? 501 GDP B O1B   1 
HETATM 15849 O  O1B   B GDP G 7 .   ? 27.742  -22.547 -11.358 0.50 29.20 ? 501 GDP B O1B   1 
HETATM 15850 O  O2B   A GDP G 7 .   ? 26.954  -24.580 -10.815 0.50 26.12 ? 501 GDP B O2B   1 
HETATM 15851 O  O2B   B GDP G 7 .   ? 27.234  -24.780 -10.451 0.50 26.03 ? 501 GDP B O2B   1 
HETATM 15852 O  O3B   A GDP G 7 .   ? 27.055  -23.120 -8.829  0.50 29.12 ? 501 GDP B O3B   1 
HETATM 15853 O  O3B   B GDP G 7 .   ? 26.562  -22.728 -9.225  0.50 25.90 ? 501 GDP B O3B   1 
HETATM 15854 O  O3A   A GDP G 7 .   ? 29.127  -24.507 -9.458  0.50 32.09 ? 501 GDP B O3A   1 
HETATM 15855 O  O3A   B GDP G 7 .   ? 29.029  -23.372 -9.325  0.50 34.11 ? 501 GDP B O3A   1 
HETATM 15856 P  PA    A GDP G 7 .   ? 29.307  -25.008 -7.939  0.50 34.76 ? 501 GDP B PA    1 
HETATM 15857 P  PA    B GDP G 7 .   ? 29.328  -24.423 -8.147  0.50 32.16 ? 501 GDP B PA    1 
HETATM 15858 O  O1A   A GDP G 7 .   ? 30.066  -26.308 -7.895  0.50 28.01 ? 501 GDP B O1A   1 
HETATM 15859 O  O1A   B GDP G 7 .   ? 29.979  -25.676 -8.679  0.50 31.96 ? 501 GDP B O1A   1 
HETATM 15860 O  O2A   A GDP G 7 .   ? 27.961  -25.185 -7.283  0.50 33.37 ? 501 GDP B O2A   1 
HETATM 15861 O  O2A   B GDP G 7 .   ? 28.061  -24.771 -7.402  0.50 34.74 ? 501 GDP B O2A   1 
HETATM 15862 O  "O5'" A GDP G 7 .   ? 30.147  -23.839 -7.217  0.50 34.15 ? 501 GDP B "O5'" 1 
HETATM 15863 O  "O5'" B GDP G 7 .   ? 30.341  -23.626 -7.178  0.50 34.54 ? 501 GDP B "O5'" 1 
HETATM 15864 C  "C5'" A GDP G 7 .   ? 31.526  -24.022 -6.903  0.50 33.66 ? 501 GDP B "C5'" 1 
HETATM 15865 C  "C5'" B GDP G 7 .   ? 31.649  -24.129 -6.914  0.50 33.51 ? 501 GDP B "C5'" 1 
HETATM 15866 C  "C4'" A GDP G 7 .   ? 31.756  -23.771 -5.420  0.50 28.74 ? 501 GDP B "C4'" 1 
HETATM 15867 C  "C4'" B GDP G 7 .   ? 31.962  -23.994 -5.430  0.50 28.33 ? 501 GDP B "C4'" 1 
HETATM 15868 O  "O4'" A GDP G 7 .   ? 30.874  -24.627 -4.695  0.50 25.95 ? 501 GDP B "O4'" 1 
HETATM 15869 O  "O4'" B GDP G 7 .   ? 30.956  -24.702 -4.704  0.50 26.12 ? 501 GDP B "O4'" 1 
HETATM 15870 C  "C3'" A GDP G 7 .   ? 33.160  -24.175 -5.030  0.50 29.97 ? 501 GDP B "C3'" 1 
HETATM 15871 C  "C3'" B GDP G 7 .   ? 33.290  -24.644 -5.097  0.50 30.09 ? 501 GDP B "C3'" 1 
HETATM 15872 O  "O3'" A GDP G 7 .   ? 33.611  -23.341 -3.955  0.50 26.79 ? 501 GDP B "O3'" 1 
HETATM 15873 O  "O3'" B GDP G 7 .   ? 33.975  -23.854 -4.118  0.50 33.53 ? 501 GDP B "O3'" 1 
HETATM 15874 C  "C2'" A GDP G 7 .   ? 33.017  -25.598 -4.545  0.50 29.59 ? 501 GDP B "C2'" 1 
HETATM 15875 C  "C2'" B GDP G 7 .   ? 32.937  -25.980 -4.491  0.50 30.16 ? 501 GDP B "C2'" 1 
HETATM 15876 O  "O2'" A GDP G 7 .   ? 34.022  -25.902 -3.575  0.50 30.50 ? 501 GDP B "O2'" 1 
HETATM 15877 O  "O2'" B GDP G 7 .   ? 33.878  -26.328 -3.473  0.50 32.38 ? 501 GDP B "O2'" 1 
HETATM 15878 C  "C1'" A GDP G 7 .   ? 31.621  -25.587 -3.942  0.50 29.90 ? 501 GDP B "C1'" 1 
HETATM 15879 C  "C1'" B GDP G 7 .   ? 31.558  -25.727 -3.908  0.50 29.72 ? 501 GDP B "C1'" 1 
HETATM 15880 N  N9    A GDP G 7 .   ? 30.919  -26.887 -4.033  0.50 32.49 ? 501 GDP B N9    1 
HETATM 15881 N  N9    B GDP G 7 .   ? 30.689  -26.923 -3.935  0.50 33.34 ? 501 GDP B N9    1 
HETATM 15882 C  C8    A GDP G 7 .   ? 30.567  -27.552 -5.151  0.50 33.90 ? 501 GDP B C8    1 
HETATM 15883 C  C8    B GDP G 7 .   ? 30.160  -27.530 -5.016  0.50 33.97 ? 501 GDP B C8    1 
HETATM 15884 N  N7    A GDP G 7 .   ? 29.907  -28.700 -4.847  0.50 32.36 ? 501 GDP B N7    1 
HETATM 15885 N  N7    B GDP G 7 .   ? 29.391  -28.588 -4.649  0.50 31.98 ? 501 GDP B N7    1 
HETATM 15886 C  C5    A GDP G 7 .   ? 29.816  -28.769 -3.504  0.50 34.39 ? 501 GDP B C5    1 
HETATM 15887 C  C5    B GDP G 7 .   ? 29.413  -28.655 -3.302  0.50 33.54 ? 501 GDP B C5    1 
HETATM 15888 C  C6    A GDP G 7 .   ? 29.248  -29.705 -2.504  0.50 33.49 ? 501 GDP B C6    1 
HETATM 15889 C  C6    B GDP G 7 .   ? 28.824  -29.518 -2.251  0.50 32.87 ? 501 GDP B C6    1 
HETATM 15890 O  O6    A GDP G 7 .   ? 28.672  -30.754 -2.861  0.50 35.46 ? 501 GDP B O6    1 
HETATM 15891 O  O6    B GDP G 7 .   ? 28.089  -30.480 -2.552  0.50 34.13 ? 501 GDP B O6    1 
HETATM 15892 N  N1    A GDP G 7 .   ? 29.375  -29.396 -1.205  0.50 34.83 ? 501 GDP B N1    1 
HETATM 15893 N  N1    B GDP G 7 .   ? 29.104  -29.238 -0.969  0.50 33.92 ? 501 GDP B N1    1 
HETATM 15894 C  C2    A GDP G 7 .   ? 29.993  -28.275 -0.788  0.50 35.39 ? 501 GDP B C2    1 
HETATM 15895 C  C2    B GDP G 7 .   ? 29.893  -28.207 -0.614  0.50 35.10 ? 501 GDP B C2    1 
HETATM 15896 N  N2    A GDP G 7 .   ? 30.085  -28.026 0.541   0.50 30.11 ? 501 GDP B N2    1 
HETATM 15897 N  N2    B GDP G 7 .   ? 30.136  -27.981 0.700   0.50 30.02 ? 501 GDP B N2    1 
HETATM 15898 N  N3    A GDP G 7 .   ? 30.540  -27.378 -1.645  0.50 33.91 ? 501 GDP B N3    1 
HETATM 15899 N  N3    B GDP G 7 .   ? 30.470  -27.380 -1.520  0.50 34.18 ? 501 GDP B N3    1 
HETATM 15900 C  C4    A GDP G 7 .   ? 30.479  -27.567 -2.980  0.50 32.73 ? 501 GDP B C4    1 
HETATM 15901 C  C4    B GDP G 7 .   ? 30.268  -27.552 -2.844  0.50 33.02 ? 501 GDP B C4    1 
HETATM 15902 N  N1    A IBL H 8 .   ? 14.116  -17.444 16.861  0.50 36.28 ? 502 IBL B N1    1 
HETATM 15903 N  N1    B IBL H 8 .   ? 14.648  -17.301 17.768  0.50 38.89 ? 502 IBL B N1    1 
HETATM 15904 C  C7    A IBL H 8 .   ? 14.677  -21.103 16.882  0.50 44.72 ? 502 IBL B C7    1 
HETATM 15905 C  C7    B IBL H 8 .   ? 13.803  -19.861 15.288  0.50 43.32 ? 502 IBL B C7    1 
HETATM 15906 C  C8    A IBL H 8 .   ? 15.719  -21.819 18.865  0.50 33.93 ? 502 IBL B C8    1 
HETATM 15907 C  C8    B IBL H 8 .   ? 15.699  -20.814 14.305  0.50 44.32 ? 502 IBL B C8    1 
HETATM 15908 C  C9    A IBL H 8 .   ? 14.249  -21.440 15.593  0.50 38.11 ? 502 IBL B C9    1 
HETATM 15909 C  C9    B IBL H 8 .   ? 12.474  -19.567 14.967  0.50 42.92 ? 502 IBL B C9    1 
HETATM 15910 O  O1    A IBL H 8 .   ? 15.260  -22.120 17.570  0.50 44.52 ? 502 IBL B O1    1 
HETATM 15911 O  O1    B IBL H 8 .   ? 14.338  -20.938 14.643  0.50 43.92 ? 502 IBL B O1    1 
HETATM 15912 C  C1    A IBL H 8 .   ? 15.469  -13.979 20.148  0.50 25.36 ? 502 IBL B C1    1 
HETATM 15913 C  C1    B IBL H 8 .   ? 16.256  -13.623 20.644  0.50 29.49 ? 502 IBL B C1    1 
HETATM 15914 C  C5    A IBL H 8 .   ? 13.981  -18.842 16.499  0.50 39.62 ? 502 IBL B C5    1 
HETATM 15915 C  C5    B IBL H 8 .   ? 13.811  -18.068 16.870  0.50 35.79 ? 502 IBL B C5    1 
HETATM 15916 C  C6    A IBL H 8 .   ? 14.524  -19.804 17.354  0.50 36.94 ? 502 IBL B C6    1 
HETATM 15917 C  C6    B IBL H 8 .   ? 14.484  -19.124 16.254  0.50 42.77 ? 502 IBL B C6    1 
HETATM 15918 C  C4    A IBL H 8 .   ? 14.342  -15.949 18.593  0.50 37.06 ? 502 IBL B C4    1 
HETATM 15919 C  C4    B IBL H 8 .   ? 14.895  -15.494 19.147  0.50 36.79 ? 502 IBL B C4    1 
HETATM 15920 O  O4    A IBL H 8 .   ? 13.348  -13.838 21.332  0.50 18.60 ? 502 IBL B O4    1 
HETATM 15921 O  O4    B IBL H 8 .   ? 14.145  -13.195 21.806  0.50 28.18 ? 502 IBL B O4    1 
HETATM 15922 C  C3    A IBL H 8 .   ? 15.642  -15.510 18.317  0.50 28.25 ? 502 IBL B C3    1 
HETATM 15923 C  C3    B IBL H 8 .   ? 16.266  -15.320 18.948  0.50 32.65 ? 502 IBL B C3    1 
HETATM 15924 O  O3    A IBL H 8 .   ? 13.218  -20.954 13.589  0.50 42.01 ? 502 IBL B O3    1 
HETATM 15925 O  O3    B IBL H 8 .   ? 10.547  -18.269 15.193  0.50 42.62 ? 502 IBL B O3    1 
HETATM 15926 C  C2    A IBL H 8 .   ? 16.212  -14.526 19.108  0.50 35.10 ? 502 IBL B C2    1 
HETATM 15927 C  C2    B IBL H 8 .   ? 16.951  -14.383 19.707  0.50 36.70 ? 502 IBL B C2    1 
HETATM 15928 N  N     A IBL H 8 .   ? 13.869  -17.199 18.062  0.50 32.64 ? 502 IBL B N     1 
HETATM 15929 N  N     B IBL H 8 .   ? 14.068  -16.347 18.335  0.50 35.43 ? 502 IBL B N     1 
HETATM 15930 C  C     A IBL H 8 .   ? 17.207  -13.302 21.528  0.50 30.69 ? 502 IBL B C     1 
HETATM 15931 C  C     B IBL H 8 .   ? 17.915  -11.988 20.833  0.50 28.12 ? 502 IBL B C     1 
HETATM 15932 O  O     A IBL H 8 .   ? 15.958  -12.991 20.957  0.50 32.22 ? 502 IBL B O     1 
HETATM 15933 O  O     B IBL H 8 .   ? 16.849  -12.683 21.437  0.50 35.89 ? 502 IBL B O     1 
HETATM 15934 C  C10   A IBL H 8 .   ? 15.608  -22.982 14.572  0.50 40.34 ? 502 IBL B C10   1 
HETATM 15935 C  C10   B IBL H 8 .   ? 12.081  -19.960 12.745  0.50 42.24 ? 502 IBL B C10   1 
HETATM 15936 C  C11   A IBL H 8 .   ? 13.642  -20.468 14.786  0.50 40.60 ? 502 IBL B C11   1 
HETATM 15937 C  C11   B IBL H 8 .   ? 11.816  -18.517 15.623  0.50 40.76 ? 502 IBL B C11   1 
HETATM 15938 C  C12   A IBL H 8 .   ? 12.942  -20.010 12.585  0.50 42.63 ? 502 IBL B C12   1 
HETATM 15939 C  C12   B IBL H 8 .   ? 9.695   -17.647 16.125  0.50 45.10 ? 502 IBL B C12   1 
HETATM 15940 C  C13   A IBL H 8 .   ? 13.503  -19.150 15.227  0.50 45.02 ? 502 IBL B C13   1 
HETATM 15941 C  C13   B IBL H 8 .   ? 12.480  -17.759 16.581  0.50 38.20 ? 502 IBL B C13   1 
HETATM 15942 C  C14   A IBL H 8 .   ? 13.553  -15.354 19.578  0.50 26.73 ? 502 IBL B C14   1 
HETATM 15943 C  C14   B IBL H 8 .   ? 14.186  -14.762 20.102  0.50 32.88 ? 502 IBL B C14   1 
HETATM 15944 C  C15   A IBL H 8 .   ? 14.137  -14.361 20.366  0.50 32.47 ? 502 IBL B C15   1 
HETATM 15945 C  C15   B IBL H 8 .   ? 14.882  -13.824 20.861  0.50 31.45 ? 502 IBL B C15   1 
HETATM 15946 O  O2    A IBL H 8 .   ? 14.347  -22.726 15.148  0.50 38.91 ? 502 IBL B O2    1 
HETATM 15947 O  O2    B IBL H 8 .   ? 11.784  -20.332 14.072  0.50 40.10 ? 502 IBL B O2    1 
HETATM 15948 O  O     . HOH I 9 .   ? 7.806   -11.084 52.383  1.00 43.43 ? 601 HOH A O     1 
HETATM 15949 O  O     . HOH I 9 .   ? -31.746 -14.247 39.946  1.00 60.67 ? 602 HOH A O     1 
HETATM 15950 O  O     . HOH I 9 .   ? 3.712   -11.657 10.648  1.00 43.17 ? 603 HOH A O     1 
HETATM 15951 O  O     . HOH I 9 .   ? 9.860   -12.724 47.956  1.00 49.10 ? 604 HOH A O     1 
HETATM 15952 O  O     . HOH I 9 .   ? 12.498  -17.003 28.497  1.00 42.21 ? 605 HOH A O     1 
HETATM 15953 O  O     . HOH I 9 .   ? -26.717 -1.949  38.578  1.00 51.47 ? 606 HOH A O     1 
HETATM 15954 O  O     . HOH I 9 .   ? 4.314   -15.258 21.780  1.00 39.80 ? 607 HOH A O     1 
HETATM 15955 O  O     . HOH I 9 .   ? 2.479   14.234  33.745  1.00 45.07 ? 608 HOH A O     1 
HETATM 15956 O  O     . HOH I 9 .   ? 15.871  9.409   18.653  1.00 45.62 ? 609 HOH A O     1 
HETATM 15957 O  O     . HOH I 9 .   ? 2.830   13.275  51.169  1.00 47.34 ? 610 HOH A O     1 
HETATM 15958 O  O     . HOH I 9 .   ? -7.571  -18.779 45.650  1.00 42.27 ? 611 HOH A O     1 
HETATM 15959 O  O     . HOH I 9 .   ? 14.153  6.727   10.172  1.00 42.89 ? 612 HOH A O     1 
HETATM 15960 O  O     . HOH I 9 .   ? -7.622  -28.661 18.952  1.00 45.85 ? 613 HOH A O     1 
HETATM 15961 O  O     . HOH I 9 .   ? -23.986 -16.246 18.084  1.00 48.29 ? 614 HOH A O     1 
HETATM 15962 O  O     . HOH I 9 .   ? -1.397  -1.357  30.752  1.00 25.67 ? 615 HOH A O     1 
HETATM 15963 O  O     . HOH I 9 .   ? 14.355  -21.438 37.964  1.00 53.60 ? 616 HOH A O     1 
HETATM 15964 O  O     . HOH I 9 .   ? 3.950   2.171   49.091  1.00 38.39 ? 617 HOH A O     1 
HETATM 15965 O  O     . HOH I 9 .   ? 5.076   -14.382 19.285  1.00 42.32 ? 618 HOH A O     1 
HETATM 15966 O  O     . HOH I 9 .   ? -21.004 5.152   36.694  1.00 45.61 ? 619 HOH A O     1 
HETATM 15967 O  O     . HOH I 9 .   ? -12.330 -18.021 42.825  1.00 33.73 ? 620 HOH A O     1 
HETATM 15968 O  O     . HOH I 9 .   ? -17.621 7.019   42.001  1.00 50.98 ? 621 HOH A O     1 
HETATM 15969 O  O     . HOH I 9 .   ? 13.401  -9.576  25.832  1.00 36.59 ? 622 HOH A O     1 
HETATM 15970 O  O     . HOH I 9 .   ? 10.438  -7.268  37.151  1.00 40.26 ? 623 HOH A O     1 
HETATM 15971 O  O     . HOH I 9 .   ? 1.460   -15.559 17.110  1.00 26.21 ? 624 HOH A O     1 
HETATM 15972 O  O     . HOH I 9 .   ? 13.311  10.446  23.930  1.00 42.62 ? 625 HOH A O     1 
HETATM 15973 O  O     . HOH I 9 .   ? -12.608 -13.722 60.908  1.00 28.71 ? 626 HOH A O     1 
HETATM 15974 O  O     . HOH I 9 .   ? -29.940 -21.787 31.958  1.00 44.14 ? 627 HOH A O     1 
HETATM 15975 O  O     . HOH I 9 .   ? -13.712 -7.668  43.723  1.00 32.06 ? 628 HOH A O     1 
HETATM 15976 O  O     . HOH I 9 .   ? -26.203 -22.971 38.811  1.00 40.96 ? 629 HOH A O     1 
HETATM 15977 O  O     . HOH I 9 .   ? -6.597  -25.917 42.326  1.00 34.46 ? 630 HOH A O     1 
HETATM 15978 O  O     . HOH I 9 .   ? 1.111   4.181   17.456  1.00 32.47 ? 631 HOH A O     1 
HETATM 15979 O  O     . HOH I 9 .   ? -36.225 -12.224 27.015  1.00 54.94 ? 632 HOH A O     1 
HETATM 15980 O  O     . HOH I 9 .   ? -15.993 -20.082 61.037  1.00 34.70 ? 633 HOH A O     1 
HETATM 15981 O  O     . HOH I 9 .   ? -10.157 -3.109  8.680   1.00 38.61 ? 634 HOH A O     1 
HETATM 15982 O  O     . HOH I 9 .   ? -0.044  3.689   39.684  1.00 30.64 ? 635 HOH A O     1 
HETATM 15983 O  O     . HOH I 9 .   ? -23.099 -19.940 25.888  1.00 39.63 ? 636 HOH A O     1 
HETATM 15984 O  O     . HOH I 9 .   ? -14.071 6.725   50.288  1.00 38.63 ? 637 HOH A O     1 
HETATM 15985 O  O     . HOH I 9 .   ? -5.705  -30.019 47.799  1.00 42.93 ? 638 HOH A O     1 
HETATM 15986 O  O     . HOH I 9 .   ? -21.136 -3.940  37.956  1.00 43.44 ? 639 HOH A O     1 
HETATM 15987 O  O     . HOH I 9 .   ? -6.746  -21.627 26.281  1.00 40.64 ? 640 HOH A O     1 
HETATM 15988 O  O     . HOH I 9 .   ? -19.094 -26.139 25.409  1.00 43.30 ? 641 HOH A O     1 
HETATM 15989 O  O     . HOH I 9 .   ? 2.338   -15.361 11.322  1.00 41.12 ? 642 HOH A O     1 
HETATM 15990 O  O     . HOH I 9 .   ? -0.911  -15.758 18.827  1.00 23.01 ? 643 HOH A O     1 
HETATM 15991 O  O     . HOH I 9 .   ? -12.990 -4.778  42.947  1.00 30.88 ? 644 HOH A O     1 
HETATM 15992 O  O     . HOH I 9 .   ? -13.843 5.424   26.138  1.00 42.74 ? 645 HOH A O     1 
HETATM 15993 O  O     . HOH I 9 .   ? 15.371  -7.386  25.544  1.00 35.23 ? 646 HOH A O     1 
HETATM 15994 O  O     . HOH I 9 .   ? 5.860   12.563  24.491  1.00 41.39 ? 647 HOH A O     1 
HETATM 15995 O  O     . HOH I 9 .   ? 18.089  -0.679  13.290  1.00 31.32 ? 648 HOH A O     1 
HETATM 15996 O  O     . HOH I 9 .   ? -24.599 3.897   30.110  1.00 49.18 ? 649 HOH A O     1 
HETATM 15997 O  O     . HOH I 9 .   ? -4.728  -17.376 17.858  1.00 27.55 ? 650 HOH A O     1 
HETATM 15998 O  O     . HOH I 9 .   ? -17.280 -9.333  30.354  1.00 32.52 ? 651 HOH A O     1 
HETATM 15999 O  O     . HOH I 9 .   ? -1.475  -3.971  46.845  1.00 32.31 ? 652 HOH A O     1 
HETATM 16000 O  O     . HOH I 9 .   ? -1.034  -1.755  37.435  1.00 24.89 ? 653 HOH A O     1 
HETATM 16001 O  O     . HOH I 9 .   ? -0.836  5.753   17.612  1.00 41.01 ? 654 HOH A O     1 
HETATM 16002 O  O     . HOH I 9 .   ? -10.633 -27.665 34.159  1.00 47.69 ? 655 HOH A O     1 
HETATM 16003 O  O     . HOH I 9 .   ? 1.704   -5.314  48.574  1.00 45.56 ? 656 HOH A O     1 
HETATM 16004 O  O     . HOH I 9 .   ? 2.543   -24.034 49.671  1.00 37.16 ? 657 HOH A O     1 
HETATM 16005 O  O     . HOH I 9 .   ? 0.128   -13.646 45.760  1.00 40.51 ? 658 HOH A O     1 
HETATM 16006 O  O     . HOH I 9 .   ? -19.379 2.791   35.639  1.00 44.52 ? 659 HOH A O     1 
HETATM 16007 O  O     . HOH I 9 .   ? -16.290 -18.601 44.715  1.00 34.88 ? 660 HOH A O     1 
HETATM 16008 O  O     . HOH I 9 .   ? 12.825  8.870   41.932  1.00 52.85 ? 661 HOH A O     1 
HETATM 16009 O  O     . HOH I 9 .   ? -10.653 -22.384 47.903  1.00 39.45 ? 662 HOH A O     1 
HETATM 16010 O  O     . HOH I 9 .   ? -15.143 -19.334 15.680  1.00 39.67 ? 663 HOH A O     1 
HETATM 16011 O  O     . HOH I 9 .   ? 2.065   -15.231 20.229  1.00 25.56 ? 664 HOH A O     1 
HETATM 16012 O  O     . HOH I 9 .   ? -1.809  8.692   25.502  1.00 31.19 ? 665 HOH A O     1 
HETATM 16013 O  O     . HOH I 9 .   ? 0.629   1.096   42.185  1.00 24.53 ? 666 HOH A O     1 
HETATM 16014 O  O     . HOH I 9 .   ? 7.252   -12.459 29.811  1.00 25.52 ? 667 HOH A O     1 
HETATM 16015 O  O     . HOH I 9 .   ? 1.268   -2.352  48.597  1.00 38.60 ? 668 HOH A O     1 
HETATM 16016 O  O     . HOH I 9 .   ? -23.378 -7.954  25.131  1.00 36.27 ? 669 HOH A O     1 
HETATM 16017 O  O     . HOH I 9 .   ? -1.554  -10.681 24.085  1.00 19.30 ? 670 HOH A O     1 
HETATM 16018 O  O     . HOH I 9 .   ? -17.728 -5.490  46.634  1.00 31.59 ? 671 HOH A O     1 
HETATM 16019 O  O     . HOH I 9 .   ? -1.154  -0.616  27.048  1.00 29.51 ? 672 HOH A O     1 
HETATM 16020 O  O     . HOH I 9 .   ? -0.384  -13.417 17.339  1.00 23.40 ? 673 HOH A O     1 
HETATM 16021 O  O     . HOH I 9 .   ? 4.532   -8.960  27.784  1.00 22.26 ? 674 HOH A O     1 
HETATM 16022 O  O     . HOH I 9 .   ? 23.604  1.373   24.840  1.00 40.38 ? 675 HOH A O     1 
HETATM 16023 O  O     . HOH I 9 .   ? -25.841 1.052   16.606  1.00 53.30 ? 676 HOH A O     1 
HETATM 16024 O  O     . HOH I 9 .   ? -7.993  7.468   35.091  1.00 41.88 ? 677 HOH A O     1 
HETATM 16025 O  O     . HOH I 9 .   ? -18.914 -14.470 23.337  1.00 34.35 ? 678 HOH A O     1 
HETATM 16026 O  O     . HOH I 9 .   ? -18.690 -25.455 34.089  1.00 41.97 ? 679 HOH A O     1 
HETATM 16027 O  O     . HOH I 9 .   ? -20.361 3.268   43.305  1.00 39.35 ? 680 HOH A O     1 
HETATM 16028 O  O     . HOH I 9 .   ? -17.827 -9.704  45.607  1.00 34.23 ? 681 HOH A O     1 
HETATM 16029 O  O     . HOH I 9 .   ? -0.763  -5.133  39.718  1.00 23.52 ? 682 HOH A O     1 
HETATM 16030 O  O     . HOH I 9 .   ? -3.774  -21.260 29.992  1.00 38.63 ? 683 HOH A O     1 
HETATM 16031 O  O     . HOH I 9 .   ? 0.245   -28.306 37.042  1.00 44.86 ? 684 HOH A O     1 
HETATM 16032 O  O     . HOH I 9 .   ? -6.997  -18.905 54.651  1.00 37.24 ? 685 HOH A O     1 
HETATM 16033 O  O     . HOH I 9 .   ? -22.893 -20.859 49.861  1.00 38.58 ? 686 HOH A O     1 
HETATM 16034 O  O     . HOH I 9 .   ? -14.495 0.177   54.085  1.00 42.15 ? 687 HOH A O     1 
HETATM 16035 O  O     . HOH I 9 .   ? 14.649  5.198   34.453  1.00 48.41 ? 688 HOH A O     1 
HETATM 16036 O  O     . HOH I 9 .   ? -28.622 -12.749 20.712  1.00 53.49 ? 689 HOH A O     1 
HETATM 16037 O  O     . HOH I 9 .   ? 4.629   3.062   52.625  1.00 42.56 ? 690 HOH A O     1 
HETATM 16038 O  O     . HOH I 9 .   ? -12.559 -10.726 45.625  1.00 37.13 ? 691 HOH A O     1 
HETATM 16039 O  O     . HOH I 9 .   ? 13.673  -2.932  40.548  1.00 44.81 ? 692 HOH A O     1 
HETATM 16040 O  O     . HOH I 9 .   ? -8.799  8.938   37.183  1.00 43.40 ? 693 HOH A O     1 
HETATM 16041 O  O     . HOH I 9 .   ? 10.197  -8.460  34.867  1.00 34.36 ? 694 HOH A O     1 
HETATM 16042 O  O     . HOH I 9 .   ? -27.414 -24.049 25.922  1.00 49.75 ? 695 HOH A O     1 
HETATM 16043 O  O     . HOH I 9 .   ? -29.794 -20.242 22.244  1.00 45.43 ? 696 HOH A O     1 
HETATM 16044 O  O     . HOH I 9 .   ? -2.826  7.933   21.480  1.00 45.21 ? 697 HOH A O     1 
HETATM 16045 O  O     . HOH I 9 .   ? 11.599  -5.284  32.929  1.00 36.69 ? 698 HOH A O     1 
HETATM 16046 O  O     . HOH I 9 .   ? -19.655 -24.929 40.086  1.00 40.17 ? 699 HOH A O     1 
HETATM 16047 O  O     . HOH I 9 .   ? -6.381  -18.845 47.402  1.00 39.30 ? 700 HOH A O     1 
HETATM 16048 O  O     . HOH I 9 .   ? -4.303  -21.555 47.964  1.00 33.74 ? 701 HOH A O     1 
HETATM 16049 O  O     . HOH I 9 .   ? 16.360  -2.864  34.292  1.00 48.19 ? 702 HOH A O     1 
HETATM 16050 O  O     . HOH I 9 .   ? -31.438 -20.067 33.209  1.00 42.06 ? 703 HOH A O     1 
HETATM 16051 O  O     . HOH I 9 .   ? -8.467  -20.820 35.632  1.00 37.80 ? 704 HOH A O     1 
HETATM 16052 O  O     . HOH I 9 .   ? 13.760  0.195   39.406  1.00 40.98 ? 705 HOH A O     1 
HETATM 16053 O  O     . HOH I 9 .   ? 0.281   0.319   29.233  1.00 30.96 ? 706 HOH A O     1 
HETATM 16054 O  O     . HOH I 9 .   ? -7.803  -28.642 48.625  1.00 36.32 ? 707 HOH A O     1 
HETATM 16055 O  O     . HOH I 9 .   ? -7.858  -20.710 38.233  1.00 37.29 ? 708 HOH A O     1 
HETATM 16056 O  O     . HOH I 9 .   ? 10.461  7.731   39.151  1.00 45.15 ? 709 HOH A O     1 
HETATM 16057 O  O     . HOH I 9 .   ? -2.469  2.421   30.242  1.00 26.77 ? 710 HOH A O     1 
HETATM 16058 O  O     . HOH I 9 .   ? -14.312 -27.047 33.906  1.00 47.72 ? 711 HOH A O     1 
HETATM 16059 O  O     . HOH I 9 .   ? -7.914  4.252   50.452  1.00 38.46 ? 712 HOH A O     1 
HETATM 16060 O  O     . HOH I 9 .   ? 9.763   -4.649  8.766   1.00 33.73 ? 713 HOH A O     1 
HETATM 16061 O  O     . HOH I 9 .   ? 9.700   -15.264 18.873  1.00 42.97 ? 714 HOH A O     1 
HETATM 16062 O  O     . HOH I 9 .   ? -26.101 0.297   26.421  1.00 32.85 ? 715 HOH A O     1 
HETATM 16063 O  O     . HOH I 9 .   ? -13.179 -10.791 32.119  1.00 28.85 ? 716 HOH A O     1 
HETATM 16064 O  O     . HOH I 9 .   ? -16.377 -14.109 9.986   1.00 41.71 ? 717 HOH A O     1 
HETATM 16065 O  O     . HOH I 9 .   ? -9.687  9.212   25.001  1.00 43.65 ? 718 HOH A O     1 
HETATM 16066 O  O     . HOH I 9 .   ? -4.287  -24.676 16.614  1.00 50.70 ? 719 HOH A O     1 
HETATM 16067 O  O     . HOH I 9 .   ? -13.689 2.437   8.826   1.00 58.53 ? 720 HOH A O     1 
HETATM 16068 O  O     . HOH I 9 .   ? 11.159  -6.665  31.072  1.00 41.42 ? 721 HOH A O     1 
HETATM 16069 O  O     . HOH I 9 .   ? 11.506  -30.681 31.768  1.00 54.94 ? 722 HOH A O     1 
HETATM 16070 O  O     . HOH I 9 .   ? -7.950  -20.991 46.821  1.00 33.06 ? 723 HOH A O     1 
HETATM 16071 O  O     . HOH I 9 .   ? -25.741 -3.549  47.780  1.00 48.58 ? 724 HOH A O     1 
HETATM 16072 O  O     . HOH I 9 .   ? 4.575   -31.136 53.831  1.00 49.97 ? 725 HOH A O     1 
HETATM 16073 O  O     . HOH I 9 .   ? -20.212 -25.487 36.565  1.00 47.65 ? 726 HOH A O     1 
HETATM 16074 O  O     . HOH I 9 .   ? -29.380 -9.607  30.458  1.00 45.34 ? 727 HOH A O     1 
HETATM 16075 O  O     . HOH I 9 .   ? -23.943 -3.883  37.712  1.00 43.34 ? 728 HOH A O     1 
HETATM 16076 O  O     . HOH I 9 .   ? -7.290  -22.183 39.762  1.00 45.72 ? 729 HOH A O     1 
HETATM 16077 O  O     . HOH I 9 .   ? 12.204  -7.030  35.175  1.00 44.60 ? 730 HOH A O     1 
HETATM 16078 O  O     . HOH I 9 .   ? -29.205 -10.462 27.931  1.00 45.96 ? 731 HOH A O     1 
HETATM 16079 O  O     . HOH I 9 .   ? 15.075  5.143   9.123   1.00 53.15 ? 732 HOH A O     1 
HETATM 16080 O  O     . HOH I 9 .   ? -0.595  -28.981 34.832  1.00 47.35 ? 733 HOH A O     1 
HETATM 16081 O  O     . HOH I 9 .   ? -17.147 -7.195  48.193  1.00 37.73 ? 734 HOH A O     1 
HETATM 16082 O  O     . HOH I 9 .   ? -21.317 -6.453  51.180  1.00 44.90 ? 735 HOH A O     1 
HETATM 16083 O  O     . HOH I 9 .   ? 14.214  -8.395  27.471  1.00 35.59 ? 736 HOH A O     1 
HETATM 16084 O  O     . HOH I 9 .   ? 18.335  9.173   22.316  1.00 49.83 ? 737 HOH A O     1 
HETATM 16085 O  O     . HOH I 9 .   ? 15.579  8.582   23.826  1.00 48.39 ? 738 HOH A O     1 
HETATM 16086 O  O     . HOH I 9 .   ? 11.920  -8.097  28.346  1.00 42.10 ? 739 HOH A O     1 
HETATM 16087 O  O     . HOH I 9 .   ? 9.836   10.604  56.325  1.00 52.20 ? 740 HOH A O     1 
HETATM 16088 O  O     . HOH I 9 .   ? -19.140 -27.292 35.522  1.00 45.79 ? 741 HOH A O     1 
HETATM 16089 O  O     . HOH I 9 .   ? 13.793  2.223   40.642  1.00 48.05 ? 742 HOH A O     1 
HETATM 16090 O  O     . HOH I 9 .   ? -28.633 1.970   15.942  1.00 53.42 ? 743 HOH A O     1 
HETATM 16091 O  O     . HOH I 9 .   ? 15.686  3.098   9.140   1.00 55.27 ? 744 HOH A O     1 
HETATM 16092 O  O     . HOH I 9 .   ? 11.435  8.962   58.435  1.00 59.48 ? 745 HOH A O     1 
HETATM 16093 O  O     . HOH J 9 .   ? 5.175   -13.864 11.379  1.00 35.77 ? 601 HOH B O     1 
HETATM 16094 O  O     . HOH J 9 .   ? 31.041  -19.211 21.842  1.00 43.20 ? 602 HOH B O     1 
HETATM 16095 O  O     . HOH J 9 .   ? 6.968   -21.903 28.740  1.00 44.14 ? 603 HOH B O     1 
HETATM 16096 O  O     . HOH J 9 .   ? 29.857  2.328   -13.740 1.00 51.54 ? 604 HOH B O     1 
HETATM 16097 O  O     . HOH J 9 .   ? 20.037  -29.791 17.032  1.00 49.77 ? 605 HOH B O     1 
HETATM 16098 O  O     . HOH J 9 .   ? 29.814  -4.177  21.951  1.00 36.93 ? 606 HOH B O     1 
HETATM 16099 O  O     . HOH J 9 .   ? 26.259  -24.963 -13.383 1.00 44.11 ? 607 HOH B O     1 
HETATM 16100 O  O     . HOH J 9 .   ? 34.706  -24.368 -9.029  1.00 39.32 ? 608 HOH B O     1 
HETATM 16101 O  O     . HOH J 9 .   ? 25.833  -10.909 10.713  1.00 27.32 ? 609 HOH B O     1 
HETATM 16102 O  O     . HOH J 9 .   ? 31.262  -33.357 18.436  1.00 50.25 ? 610 HOH B O     1 
HETATM 16103 O  O     . HOH J 9 .   ? 41.309  -22.935 8.324   1.00 44.95 ? 611 HOH B O     1 
HETATM 16104 O  O     . HOH J 9 .   ? 27.561  -20.734 -7.721  1.00 35.22 ? 612 HOH B O     1 
HETATM 16105 O  O     . HOH J 9 .   ? 14.903  -13.173 24.063  1.00 34.92 ? 613 HOH B O     1 
HETATM 16106 O  O     . HOH J 9 .   ? 30.611  -7.229  -1.660  1.00 41.97 ? 614 HOH B O     1 
HETATM 16107 O  O     . HOH J 9 .   ? 28.916  -0.333  29.198  1.00 55.20 ? 615 HOH B O     1 
HETATM 16108 O  O     . HOH J 9 .   ? 27.449  -7.788  -7.277  1.00 41.17 ? 616 HOH B O     1 
HETATM 16109 O  O     . HOH J 9 .   ? 30.877  -43.735 1.971   1.00 57.16 ? 617 HOH B O     1 
HETATM 16110 O  O     . HOH J 9 .   ? 38.285  -5.319  11.728  1.00 42.21 ? 618 HOH B O     1 
HETATM 16111 O  O     . HOH J 9 .   ? 38.282  -17.754 8.201   1.00 39.39 ? 619 HOH B O     1 
HETATM 16112 O  O     . HOH J 9 .   ? 22.971  -2.593  8.624   1.00 27.44 ? 620 HOH B O     1 
HETATM 16113 O  O     . HOH J 9 .   ? 31.558  -21.308 -3.065  1.00 31.03 ? 621 HOH B O     1 
HETATM 16114 O  O     . HOH J 9 .   ? 36.596  -39.505 13.602  1.00 52.26 ? 622 HOH B O     1 
HETATM 16115 O  O     . HOH J 9 .   ? 42.143  -20.929 2.986   1.00 39.73 ? 623 HOH B O     1 
HETATM 16116 O  O     . HOH J 9 .   ? 24.606  -41.115 18.716  1.00 57.21 ? 624 HOH B O     1 
HETATM 16117 O  O     . HOH J 9 .   ? 11.381  -6.990  0.305   1.00 47.51 ? 625 HOH B O     1 
HETATM 16118 O  O     . HOH J 9 .   ? 1.819   -24.100 14.470  1.00 54.95 ? 626 HOH B O     1 
HETATM 16119 O  O     . HOH J 9 .   ? 9.208   -30.521 -5.948  1.00 44.58 ? 627 HOH B O     1 
HETATM 16120 O  O     . HOH J 9 .   ? 0.822   -29.422 7.755   1.00 53.08 ? 628 HOH B O     1 
HETATM 16121 O  O     . HOH J 9 .   ? 31.171  -14.304 19.224  1.00 31.70 ? 629 HOH B O     1 
HETATM 16122 O  O     . HOH J 9 .   ? 42.588  -19.501 6.213   1.00 38.33 ? 630 HOH B O     1 
HETATM 16123 O  O     . HOH J 9 .   ? 35.202  -24.152 -1.894  1.00 33.72 ? 631 HOH B O     1 
HETATM 16124 O  O     . HOH J 9 .   ? 7.016   -21.950 10.130  1.00 46.66 ? 632 HOH B O     1 
HETATM 16125 O  O     . HOH J 9 .   ? 0.370   -16.940 0.371   1.00 43.91 ? 633 HOH B O     1 
HETATM 16126 O  O     . HOH J 9 .   ? 15.362  -22.163 6.494   1.00 38.33 ? 634 HOH B O     1 
HETATM 16127 O  O     . HOH J 9 .   ? 19.424  -7.584  -9.046  1.00 45.19 ? 635 HOH B O     1 
HETATM 16128 O  O     . HOH J 9 .   ? 13.393  -33.136 26.396  1.00 48.18 ? 636 HOH B O     1 
HETATM 16129 O  O     . HOH J 9 .   ? 14.409  -14.625 -18.872 1.00 44.92 ? 637 HOH B O     1 
HETATM 16130 O  O     . HOH J 9 .   ? 0.400   -19.564 12.747  1.00 49.51 ? 638 HOH B O     1 
HETATM 16131 O  O     . HOH J 9 .   ? 38.497  -6.006  -1.013  1.00 44.00 ? 639 HOH B O     1 
HETATM 16132 O  O     . HOH J 9 .   ? 20.321  -4.668  4.186   1.00 31.05 ? 640 HOH B O     1 
HETATM 16133 O  O     . HOH J 9 .   ? -4.428  -17.949 0.262   1.00 54.43 ? 641 HOH B O     1 
HETATM 16134 O  O     . HOH J 9 .   ? 27.721  -25.010 30.884  1.00 62.50 ? 642 HOH B O     1 
HETATM 16135 O  O     . HOH J 9 .   ? 34.279  -6.414  28.280  1.00 54.41 ? 643 HOH B O     1 
HETATM 16136 O  O     . HOH J 9 .   ? 36.151  -21.664 13.999  1.00 43.29 ? 644 HOH B O     1 
HETATM 16137 O  O     . HOH J 9 .   ? 37.062  -11.869 29.366  1.00 51.94 ? 645 HOH B O     1 
HETATM 16138 O  O     . HOH J 9 .   ? 45.861  -2.458  -10.382 1.00 42.58 ? 646 HOH B O     1 
HETATM 16139 O  O     . HOH J 9 .   ? 15.896  -6.679  5.970   1.00 48.68 ? 647 HOH B O     1 
HETATM 16140 O  O     . HOH J 9 .   ? 38.584  -18.432 1.199   1.00 33.51 ? 648 HOH B O     1 
HETATM 16141 O  O     . HOH J 9 .   ? 19.680  -6.103  -6.774  1.00 55.55 ? 649 HOH B O     1 
HETATM 16142 O  O     . HOH J 9 .   ? 1.289   -16.244 -4.687  1.00 58.93 ? 650 HOH B O     1 
HETATM 16143 O  O     . HOH J 9 .   ? 23.140  -8.773  27.154  1.00 43.48 ? 651 HOH B O     1 
HETATM 16144 O  O     . HOH J 9 .   ? 40.599  -13.407 8.282   1.00 38.85 ? 652 HOH B O     1 
HETATM 16145 O  O     . HOH J 9 .   ? 33.061  -23.760 25.317  1.00 52.91 ? 653 HOH B O     1 
HETATM 16146 O  O     . HOH J 9 .   ? 27.631  -14.018 12.682  1.00 26.56 ? 654 HOH B O     1 
HETATM 16147 O  O     . HOH J 9 .   ? 5.831   -49.440 3.266   1.00 57.01 ? 655 HOH B O     1 
HETATM 16148 O  O     . HOH J 9 .   ? 23.716  -36.086 -2.574  1.00 49.33 ? 656 HOH B O     1 
HETATM 16149 O  O     . HOH J 9 .   ? 39.570  -29.987 -6.035  1.00 50.61 ? 657 HOH B O     1 
HETATM 16150 O  O     . HOH J 9 .   ? 42.911  -16.653 20.115  1.00 48.14 ? 658 HOH B O     1 
HETATM 16151 O  O     . HOH J 9 .   ? 40.664  -19.411 -4.330  1.00 40.98 ? 659 HOH B O     1 
HETATM 16152 O  O     . HOH J 9 .   ? 18.091  -6.882  4.672   1.00 40.85 ? 660 HOH B O     1 
HETATM 16153 O  O     . HOH J 9 .   ? 45.859  -8.871  -0.738  1.00 27.64 ? 661 HOH B O     1 
HETATM 16154 O  O     . HOH J 9 .   ? 42.935  -18.519 3.249   1.00 45.26 ? 662 HOH B O     1 
HETATM 16155 O  O     . HOH J 9 .   ? 0.123   -12.691 3.336   1.00 44.50 ? 663 HOH B O     1 
HETATM 16156 O  O     . HOH J 9 .   ? 26.986  -40.496 23.471  1.00 57.25 ? 664 HOH B O     1 
HETATM 16157 O  O     . HOH J 9 .   ? 49.310  -8.527  -14.152 1.00 35.33 ? 665 HOH B O     1 
HETATM 16158 O  O     . HOH J 9 .   ? 38.688  -35.387 17.944  1.00 52.89 ? 666 HOH B O     1 
HETATM 16159 O  O     . HOH J 9 .   ? 47.924  -6.779  -15.628 1.00 47.12 ? 667 HOH B O     1 
HETATM 16160 O  O     . HOH J 9 .   ? 38.896  -19.482 -2.390  1.00 37.55 ? 668 HOH B O     1 
HETATM 16161 O  O     . HOH J 9 .   ? 14.723  -13.375 -21.119 1.00 46.06 ? 669 HOH B O     1 
HETATM 16162 O  O     . HOH J 9 .   ? 9.605   -46.820 1.810   1.00 56.81 ? 670 HOH B O     1 
HETATM 16163 O  O     . HOH J 9 .   ? 11.234  -4.543  -1.011  1.00 51.83 ? 671 HOH B O     1 
HETATM 16164 O  O     . HOH J 9 .   ? 6.652   -50.029 5.135   1.00 53.69 ? 672 HOH B O     1 
HETATM 16165 O  O     . HOH J 9 .   ? 44.738  -6.908  1.353   1.00 45.96 ? 673 HOH B O     1 
HETATM 16166 O  O     . HOH J 9 .   ? 29.519  -2.322  31.053  1.00 55.84 ? 674 HOH B O     1 
HETATM 16167 O  O     . HOH K 9 .   ? 60.688  -5.017  -26.746 1.00 46.09 ? 201 HOH F O     1 
HETATM 16168 O  O     . HOH K 9 .   ? 51.544  0.929   4.175   1.00 47.36 ? 202 HOH F O     1 
HETATM 16169 O  O     . HOH K 9 .   ? 45.427  -9.743  -19.931 1.00 57.05 ? 203 HOH F O     1 
HETATM 16170 O  O     . HOH K 9 .   ? 63.279  -20.415 2.450   1.00 41.81 ? 204 HOH F O     1 
HETATM 16171 O  O     . HOH K 9 .   ? 66.089  -16.824 -21.368 1.00 34.84 ? 205 HOH F O     1 
HETATM 16172 O  O     . HOH K 9 .   ? 58.708  -7.252  0.925   1.00 36.32 ? 206 HOH F O     1 
HETATM 16173 O  O     . HOH K 9 .   ? 63.700  -7.459  -27.690 1.00 36.94 ? 207 HOH F O     1 
HETATM 16174 O  O     . HOH K 9 .   ? 63.507  -27.835 7.875   1.00 56.16 ? 208 HOH F O     1 
HETATM 16175 O  O     . HOH K 9 .   ? 63.116  -22.503 -31.795 1.00 50.97 ? 209 HOH F O     1 
HETATM 16176 O  O     . HOH K 9 .   ? 49.854  -5.386  -15.521 1.00 39.37 ? 210 HOH F O     1 
HETATM 16177 O  O     . HOH K 9 .   ? 50.159  -25.288 -4.543  1.00 41.36 ? 211 HOH F O     1 
HETATM 16178 O  O     . HOH K 9 .   ? 50.255  -8.414  1.175   1.00 34.69 ? 212 HOH F O     1 
HETATM 16179 O  O     . HOH K 9 .   ? 65.000  -8.122  -15.850 1.00 35.78 ? 213 HOH F O     1 
HETATM 16180 O  O     . HOH K 9 .   ? 66.101  -18.719 -8.952  1.00 34.79 ? 214 HOH F O     1 
HETATM 16181 O  O     . HOH K 9 .   ? 63.325  -6.463  -18.855 1.00 49.47 ? 215 HOH F O     1 
HETATM 16182 O  O     . HOH K 9 .   ? 64.694  -14.842 -37.947 1.00 39.07 ? 216 HOH F O     1 
HETATM 16183 O  O     . HOH K 9 .   ? 67.653  -29.056 -17.693 1.00 52.09 ? 217 HOH F O     1 
HETATM 16184 O  O     . HOH K 9 .   ? 52.127  -25.345 -14.148 1.00 39.29 ? 218 HOH F O     1 
HETATM 16185 O  O     . HOH K 9 .   ? 59.530  -7.077  -8.925  1.00 31.68 ? 219 HOH F O     1 
HETATM 16186 O  O     . HOH K 9 .   ? 57.070  -15.736 6.509   1.00 39.13 ? 220 HOH F O     1 
HETATM 16187 O  O     . HOH K 9 .   ? 50.705  -7.173  -12.595 1.00 31.90 ? 221 HOH F O     1 
HETATM 16188 O  O     . HOH K 9 .   ? 52.420  -24.784 -23.690 1.00 42.45 ? 222 HOH F O     1 
HETATM 16189 O  O     . HOH K 9 .   ? 47.704  -24.511 -21.673 1.00 50.44 ? 223 HOH F O     1 
HETATM 16190 O  O     . HOH K 9 .   ? 48.169  -8.425  -2.448  1.00 26.53 ? 224 HOH F O     1 
HETATM 16191 O  O     . HOH K 9 .   ? 58.132  -5.826  -18.864 1.00 38.74 ? 225 HOH F O     1 
HETATM 16192 O  O     . HOH K 9 .   ? 44.467  -22.617 -24.939 1.00 51.51 ? 226 HOH F O     1 
HETATM 16193 O  O     . HOH K 9 .   ? 65.954  -7.830  -20.445 1.00 33.28 ? 227 HOH F O     1 
HETATM 16194 O  O     . HOH K 9 .   ? 42.308  -14.795 13.127  1.00 46.07 ? 228 HOH F O     1 
HETATM 16195 O  O     . HOH K 9 .   ? 60.306  -16.036 -43.198 1.00 38.49 ? 229 HOH F O     1 
HETATM 16196 O  O     . HOH K 9 .   ? 60.742  -13.201 -9.889  1.00 37.23 ? 230 HOH F O     1 
HETATM 16197 O  O     . HOH K 9 .   ? 47.450  -0.527  -3.622  1.00 47.68 ? 231 HOH F O     1 
HETATM 16198 O  O     . HOH K 9 .   ? 52.298  -9.208  -8.407  1.00 24.52 ? 232 HOH F O     1 
HETATM 16199 O  O     . HOH K 9 .   ? 57.289  -12.896 4.102   1.00 34.77 ? 233 HOH F O     1 
HETATM 16200 O  O     . HOH K 9 .   ? 61.280  -5.655  -22.433 1.00 46.81 ? 234 HOH F O     1 
HETATM 16201 O  O     . HOH K 9 .   ? 59.034  -15.112 -2.151  1.00 25.56 ? 235 HOH F O     1 
HETATM 16202 O  O     . HOH K 9 .   ? 62.426  -5.488  8.713   1.00 40.70 ? 236 HOH F O     1 
HETATM 16203 O  O     . HOH K 9 .   ? 62.701  -13.268 -32.908 1.00 28.69 ? 237 HOH F O     1 
HETATM 16204 O  O     . HOH K 9 .   ? 59.335  -13.844 0.247   1.00 38.61 ? 238 HOH F O     1 
HETATM 16205 O  O     . HOH K 9 .   ? 42.912  -19.810 -4.432  1.00 30.34 ? 239 HOH F O     1 
HETATM 16206 O  O     . HOH K 9 .   ? 62.992  -8.759  -32.239 1.00 32.87 ? 240 HOH F O     1 
HETATM 16207 O  O     . HOH K 9 .   ? 61.866  -4.623  -30.888 1.00 50.34 ? 241 HOH F O     1 
HETATM 16208 O  O     . HOH K 9 .   ? 58.929  -4.604  -30.114 1.00 50.16 ? 242 HOH F O     1 
HETATM 16209 O  O     . HOH K 9 .   ? 59.897  -14.000 -12.395 1.00 23.68 ? 243 HOH F O     1 
HETATM 16210 O  O     . HOH K 9 .   ? 62.558  -6.939  -6.208  1.00 31.97 ? 244 HOH F O     1 
HETATM 16211 O  O     . HOH K 9 .   ? 61.995  -14.765 11.846  1.00 33.01 ? 245 HOH F O     1 
HETATM 16212 O  O     . HOH K 9 .   ? 59.970  -11.521 -20.468 1.00 26.58 ? 246 HOH F O     1 
HETATM 16213 O  O     . HOH K 9 .   ? 53.612  -28.661 -26.881 1.00 63.74 ? 247 HOH F O     1 
HETATM 16214 O  O     . HOH K 9 .   ? 63.561  -7.622  -11.840 1.00 48.33 ? 248 HOH F O     1 
HETATM 16215 O  O     . HOH K 9 .   ? 44.679  -24.448 0.608   1.00 33.83 ? 249 HOH F O     1 
HETATM 16216 O  O     . HOH K 9 .   ? 66.296  -14.793 -18.419 1.00 28.47 ? 250 HOH F O     1 
HETATM 16217 O  O     . HOH K 9 .   ? 50.434  -3.796  0.706   1.00 45.39 ? 251 HOH F O     1 
HETATM 16218 O  O     . HOH K 9 .   ? 58.747  -12.777 -22.693 1.00 26.92 ? 252 HOH F O     1 
HETATM 16219 O  O     . HOH K 9 .   ? 43.119  -23.650 9.566   1.00 48.47 ? 253 HOH F O     1 
HETATM 16220 O  O     . HOH K 9 .   ? 67.241  -17.656 -3.645  1.00 52.30 ? 254 HOH F O     1 
HETATM 16221 O  O     . HOH K 9 .   ? 48.721  -30.194 7.169   1.00 43.37 ? 255 HOH F O     1 
HETATM 16222 O  O     . HOH K 9 .   ? 44.321  -22.825 2.667   1.00 47.88 ? 256 HOH F O     1 
HETATM 16223 O  O     . HOH K 9 .   ? 48.315  -25.682 -13.289 1.00 43.91 ? 257 HOH F O     1 
HETATM 16224 O  O     . HOH K 9 .   ? 66.169  -16.594 -6.622  1.00 38.12 ? 258 HOH F O     1 
HETATM 16225 O  O     . HOH K 9 .   ? 58.100  -2.032  -16.280 1.00 46.60 ? 259 HOH F O     1 
HETATM 16226 O  O     . HOH K 9 .   ? 51.903  -5.019  10.651  1.00 47.94 ? 260 HOH F O     1 
HETATM 16227 O  O     . HOH K 9 .   ? 52.536  -15.587 -38.266 1.00 51.58 ? 261 HOH F O     1 
HETATM 16228 O  O     . HOH K 9 .   ? 42.455  -22.011 13.255  1.00 44.71 ? 262 HOH F O     1 
HETATM 16229 O  O     . HOH K 9 .   ? 61.604  -5.656  -17.116 1.00 33.60 ? 263 HOH F O     1 
HETATM 16230 O  O     . HOH K 9 .   ? 63.949  -7.203  -21.885 1.00 45.57 ? 264 HOH F O     1 
HETATM 16231 O  O     . HOH K 9 .   ? 67.694  -16.399 -1.318  1.00 54.00 ? 265 HOH F O     1 
HETATM 16232 O  O     . HOH K 9 .   ? 50.099  -28.585 6.414   1.00 43.80 ? 266 HOH F O     1 
HETATM 16233 O  O     . HOH K 9 .   ? 44.871  -20.945 14.063  1.00 51.20 ? 267 HOH F O     1 
HETATM 16234 O  O     . HOH K 9 .   ? 55.738  0.688   4.694   1.00 58.94 ? 268 HOH F O     1 
HETATM 16235 O  O     . HOH K 9 .   ? 41.169  -10.342 -32.557 1.00 63.60 ? 269 HOH F O     1 
HETATM 16236 O  O     . HOH K 9 .   ? 64.211  -5.339  -20.726 1.00 61.91 ? 270 HOH F O     1 
HETATM 16237 O  O     . HOH K 9 .   ? 65.828  -28.325 9.141   1.00 56.85 ? 271 HOH F O     1 
HETATM 16238 O  O     . HOH K 9 .   ? 40.547  -11.672 -30.820 1.00 54.29 ? 272 HOH F O     1 
HETATM 16239 O  O     . HOH K 9 .   ? 58.245  -2.310  -30.778 1.00 54.09 ? 273 HOH F O     1 
HETATM 16240 O  O     . HOH K 9 .   ? 60.192  -6.016  -20.275 1.00 43.16 ? 274 HOH F O     1 
HETATM 16241 O  O     . HOH K 9 .   ? 62.138  -6.930  -9.484  1.00 36.78 ? 275 HOH F O     1 
# 
