data_9F6U
# 
_entry.id   9F6U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F6U         pdb_00009f6u 10.2210/pdb9f6u/pdb 
WWPDB D_1292138317 ?            ?                   
EMDB  EMD-50240    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 2 'Structure model' em_admin 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_em_admin.last_update'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F6U 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_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 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'cryoEM structure of Asgard tubulin heterodimer AtubA/B with GDP' 
_pdbx_database_related.db_id          EMD-50240 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              pilhofer@mol.biol.ethz.ch 
_pdbx_contact_author.name_first         Martin 
_pdbx_contact_author.name_last          Pilhofer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3649-3340 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wollweber, F.'          1 ? 
'Xu, J.'                 2 ? 
'Ponce-Toled, R.I.'      3 ? 
'Rodrigues-Oliveira, T.' 4 ? 
'Malit, J.J.L.'          5 ? 
'Kokhanovska, A.'        6 ? 
'Schleper, C.'           7 ? 
'Pilhofer, M.'           8 ? 
# 
_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            Cell 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1097-4172 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            188 
_citation.language                  ? 
_citation.page_first                2451 
_citation.page_last                 ? 
_citation.title                     'Microtubules in Asgard archaea.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cell.2025.02.027 
_citation.pdbx_database_id_PubMed   40120574 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wollweber, F.'          1  ? 
primary 'Xu, J.'                 2  ? 
primary 'Ponce-Toledo, R.I.'     3  ? 
primary 'Marxer, F.'             4  ? 
primary 'Rodrigues-Oliveira, T.' 5  ? 
primary 'Possnecker, A.'         6  ? 
primary 'Luo, Z.H.'              7  ? 
primary 'Malit, J.J.L.'          8  ? 
primary 'Kokhanovska, A.'        9  ? 
primary 'Wieczorek, M.'          10 ? 
primary 'Schleper, C.'           11 ? 
primary 'Pilhofer, M.'           12 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Asgard tubulin A (AtubA) from Candidatus Lokiarchaeum ossiferum' 46040.281 1 ? ? ? ? 
2 polymer     man 'Asgard tubulin B (AtubB) from Candidatus Lokiarchaeum ossiferum' 46883.527 1 ? ? ? ? 
3 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                                        443.201   1 ? ? ? ? 
4 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                                       523.180   1 ? ? ? ? 
# 
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 
;MAGEIVCIQVGQAGNQIAGAFWQKICAEHGIDPVNGKAIDVVGDTDIFFNTIGDKYIPRAVVVDLEPAVVENIREKFGTL
FDPKSIVSGADGAGNNFAIGFNEHGAETLEKVMQVVEQRVSETESIGGFILTHSCGGGTGSGFGSKILKTIRERYPKVPI
FTFSIFPSPKISETVVEPYNAIMTLSNLIKYASCSIVLDNEALFSIAEKKLEVENPSLEDLNLIIAQVLTNVTASLRFSG
TLNLDLGKLVTNLVPFSNLHFLMASTAPLVLAGKESYEKMTAKELSAQVFGDEYICAACKPTTGRYLAASVLFRGAVKTS
DVNEAMATVKEQNSFVNWIPTGFKISKSETSPKDSALGVIMLGNNSEIVSVFERIGANFDRLWSRKAFAHWFTDSGFEEK
DLDDARALVQKVIDDYRKLTEDA
;
;MAGEIVCIQVGQAGNQIAGAFWQKICAEHGIDPVNGKAIDVVGDTDIFFNTIGDKYIPRAVVVDLEPAVVENIREKFGTL
FDPKSIVSGADGAGNNFAIGFNEHGAETLEKVMQVVEQRVSETESIGGFILTHSCGGGTGSGFGSKILKTIRERYPKVPI
FTFSIFPSPKISETVVEPYNAIMTLSNLIKYASCSIVLDNEALFSIAEKKLEVENPSLEDLNLIIAQVLTNVTASLRFSG
TLNLDLGKLVTNLVPFSNLHFLMASTAPLVLAGKESYEKMTAKELSAQVFGDEYICAACKPTTGRYLAASVLFRGAVKTS
DVNEAMATVKEQNSFVNWIPTGFKISKSETSPKDSALGVIMLGNNSEIVSVFERIGANFDRLWSRKAFAHWFTDSGFEEK
DLDDARALVQKVIDDYRKLTEDA
;
A ? 
2 'polypeptide(L)' no no 
;MGREVIMLHVGQAGIQVGAMYWKQICAEHNLDHNGAPIGGDIKGDPDCFFMKASGGKYVPRALLIDLEPKVVRQVGNEQL
PSFFDPKNLIHGLYGGANSFAKGYLGEGRDMIDNIMEQLKKEVAKCESLQGFIMTHAVGGGSGGGLGCLIMEKIKEEYPK
KILWSYSILPSPLLSDAVVEPYNAILSLDKMIQYTDETVVIDNHALFQIVTKNMGIDDPIYDDLNHVISQALSDITASLR
FKGSLNTDMKEFLVNLVPYPRSHFLMASFAPMATAEDRQYAKLTTSNLANALFEENYMMAAVDVTKGTFLACSLLFRGEN
TAQDITNALLDIKGRIKFSSFIPTGIKYGMTGTAPEGLERSGSALINHTGVAEIFNRILAQFNLMFDKGAFLNWYEIEGM
SKDDFAGARDNVQKLSDEYKRDEE
;
;MGREVIMLHVGQAGIQVGAMYWKQICAEHNLDHNGAPIGGDIKGDPDCFFMKASGGKYVPRALLIDLEPKVVRQVGNEQL
PSFFDPKNLIHGLYGGANSFAKGYLGEGRDMIDNIMEQLKKEVAKCESLQGFIMTHAVGGGSGGGLGCLIMEKIKEEYPK
KILWSYSILPSPLLSDAVVEPYNAILSLDKMIQYTDETVVIDNHALFQIVTKNMGIDDPIYDDLNHVISQALSDITASLR
FKGSLNTDMKEFLVNLVPYPRSHFLMASFAPMATAEDRQYAKLTTSNLANALFEENYMMAAVDVTKGTFLACSLLFRGEN
TAQDITNALLDIKGRIKFSSFIPTGIKYGMTGTAPEGLERSGSALINHTGVAEIFNRILAQFNLMFDKGAFLNWYEIEGM
SKDDFAGARDNVQKLSDEYKRDEE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "GUANOSINE-5'-DIPHOSPHATE"  GDP 
4 "GUANOSINE-5'-TRIPHOSPHATE" GTP 
# 
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   ALA n 
1 3   GLY n 
1 4   GLU n 
1 5   ILE n 
1 6   VAL n 
1 7   CYS n 
1 8   ILE n 
1 9   GLN n 
1 10  VAL n 
1 11  GLY n 
1 12  GLN n 
1 13  ALA n 
1 14  GLY n 
1 15  ASN n 
1 16  GLN n 
1 17  ILE n 
1 18  ALA n 
1 19  GLY n 
1 20  ALA n 
1 21  PHE n 
1 22  TRP n 
1 23  GLN n 
1 24  LYS n 
1 25  ILE n 
1 26  CYS n 
1 27  ALA n 
1 28  GLU n 
1 29  HIS n 
1 30  GLY n 
1 31  ILE n 
1 32  ASP n 
1 33  PRO n 
1 34  VAL n 
1 35  ASN n 
1 36  GLY n 
1 37  LYS n 
1 38  ALA n 
1 39  ILE n 
1 40  ASP n 
1 41  VAL n 
1 42  VAL n 
1 43  GLY n 
1 44  ASP n 
1 45  THR n 
1 46  ASP n 
1 47  ILE n 
1 48  PHE n 
1 49  PHE n 
1 50  ASN n 
1 51  THR n 
1 52  ILE n 
1 53  GLY n 
1 54  ASP n 
1 55  LYS n 
1 56  TYR n 
1 57  ILE n 
1 58  PRO n 
1 59  ARG n 
1 60  ALA n 
1 61  VAL n 
1 62  VAL n 
1 63  VAL n 
1 64  ASP n 
1 65  LEU n 
1 66  GLU n 
1 67  PRO n 
1 68  ALA n 
1 69  VAL n 
1 70  VAL n 
1 71  GLU n 
1 72  ASN n 
1 73  ILE n 
1 74  ARG n 
1 75  GLU n 
1 76  LYS n 
1 77  PHE n 
1 78  GLY n 
1 79  THR n 
1 80  LEU n 
1 81  PHE n 
1 82  ASP n 
1 83  PRO n 
1 84  LYS n 
1 85  SER n 
1 86  ILE n 
1 87  VAL n 
1 88  SER n 
1 89  GLY n 
1 90  ALA n 
1 91  ASP n 
1 92  GLY n 
1 93  ALA n 
1 94  GLY n 
1 95  ASN n 
1 96  ASN n 
1 97  PHE n 
1 98  ALA n 
1 99  ILE n 
1 100 GLY n 
1 101 PHE n 
1 102 ASN n 
1 103 GLU n 
1 104 HIS n 
1 105 GLY n 
1 106 ALA n 
1 107 GLU n 
1 108 THR n 
1 109 LEU n 
1 110 GLU n 
1 111 LYS n 
1 112 VAL n 
1 113 MET n 
1 114 GLN n 
1 115 VAL n 
1 116 VAL n 
1 117 GLU n 
1 118 GLN n 
1 119 ARG n 
1 120 VAL n 
1 121 SER n 
1 122 GLU n 
1 123 THR n 
1 124 GLU n 
1 125 SER n 
1 126 ILE n 
1 127 GLY n 
1 128 GLY n 
1 129 PHE n 
1 130 ILE n 
1 131 LEU n 
1 132 THR n 
1 133 HIS n 
1 134 SER n 
1 135 CYS n 
1 136 GLY n 
1 137 GLY n 
1 138 GLY n 
1 139 THR n 
1 140 GLY n 
1 141 SER n 
1 142 GLY n 
1 143 PHE n 
1 144 GLY n 
1 145 SER n 
1 146 LYS n 
1 147 ILE n 
1 148 LEU n 
1 149 LYS n 
1 150 THR n 
1 151 ILE n 
1 152 ARG n 
1 153 GLU n 
1 154 ARG n 
1 155 TYR n 
1 156 PRO n 
1 157 LYS n 
1 158 VAL n 
1 159 PRO n 
1 160 ILE n 
1 161 PHE n 
1 162 THR n 
1 163 PHE n 
1 164 SER n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 SER n 
1 169 PRO n 
1 170 LYS n 
1 171 ILE n 
1 172 SER n 
1 173 GLU n 
1 174 THR n 
1 175 VAL n 
1 176 VAL n 
1 177 GLU n 
1 178 PRO n 
1 179 TYR n 
1 180 ASN n 
1 181 ALA n 
1 182 ILE n 
1 183 MET n 
1 184 THR n 
1 185 LEU n 
1 186 SER n 
1 187 ASN n 
1 188 LEU n 
1 189 ILE n 
1 190 LYS n 
1 191 TYR n 
1 192 ALA n 
1 193 SER n 
1 194 CYS n 
1 195 SER n 
1 196 ILE n 
1 197 VAL n 
1 198 LEU n 
1 199 ASP n 
1 200 ASN n 
1 201 GLU n 
1 202 ALA n 
1 203 LEU n 
1 204 PHE n 
1 205 SER n 
1 206 ILE n 
1 207 ALA n 
1 208 GLU n 
1 209 LYS n 
1 210 LYS n 
1 211 LEU n 
1 212 GLU n 
1 213 VAL n 
1 214 GLU n 
1 215 ASN n 
1 216 PRO n 
1 217 SER n 
1 218 LEU n 
1 219 GLU n 
1 220 ASP n 
1 221 LEU n 
1 222 ASN n 
1 223 LEU n 
1 224 ILE n 
1 225 ILE n 
1 226 ALA n 
1 227 GLN n 
1 228 VAL n 
1 229 LEU n 
1 230 THR n 
1 231 ASN n 
1 232 VAL n 
1 233 THR n 
1 234 ALA n 
1 235 SER n 
1 236 LEU n 
1 237 ARG n 
1 238 PHE n 
1 239 SER n 
1 240 GLY n 
1 241 THR n 
1 242 LEU n 
1 243 ASN n 
1 244 LEU n 
1 245 ASP n 
1 246 LEU n 
1 247 GLY n 
1 248 LYS n 
1 249 LEU n 
1 250 VAL n 
1 251 THR n 
1 252 ASN n 
1 253 LEU n 
1 254 VAL n 
1 255 PRO n 
1 256 PHE n 
1 257 SER n 
1 258 ASN n 
1 259 LEU n 
1 260 HIS n 
1 261 PHE n 
1 262 LEU n 
1 263 MET n 
1 264 ALA n 
1 265 SER n 
1 266 THR n 
1 267 ALA n 
1 268 PRO n 
1 269 LEU n 
1 270 VAL n 
1 271 LEU n 
1 272 ALA n 
1 273 GLY n 
1 274 LYS n 
1 275 GLU n 
1 276 SER n 
1 277 TYR n 
1 278 GLU n 
1 279 LYS n 
1 280 MET n 
1 281 THR n 
1 282 ALA n 
1 283 LYS n 
1 284 GLU n 
1 285 LEU n 
1 286 SER n 
1 287 ALA n 
1 288 GLN n 
1 289 VAL n 
1 290 PHE n 
1 291 GLY n 
1 292 ASP n 
1 293 GLU n 
1 294 TYR n 
1 295 ILE n 
1 296 CYS n 
1 297 ALA n 
1 298 ALA n 
1 299 CYS n 
1 300 LYS n 
1 301 PRO n 
1 302 THR n 
1 303 THR n 
1 304 GLY n 
1 305 ARG n 
1 306 TYR n 
1 307 LEU n 
1 308 ALA n 
1 309 ALA n 
1 310 SER n 
1 311 VAL n 
1 312 LEU n 
1 313 PHE n 
1 314 ARG n 
1 315 GLY n 
1 316 ALA n 
1 317 VAL n 
1 318 LYS n 
1 319 THR n 
1 320 SER n 
1 321 ASP n 
1 322 VAL n 
1 323 ASN n 
1 324 GLU n 
1 325 ALA n 
1 326 MET n 
1 327 ALA n 
1 328 THR n 
1 329 VAL n 
1 330 LYS n 
1 331 GLU n 
1 332 GLN n 
1 333 ASN n 
1 334 SER n 
1 335 PHE n 
1 336 VAL n 
1 337 ASN n 
1 338 TRP n 
1 339 ILE n 
1 340 PRO n 
1 341 THR n 
1 342 GLY n 
1 343 PHE n 
1 344 LYS n 
1 345 ILE n 
1 346 SER n 
1 347 LYS n 
1 348 SER n 
1 349 GLU n 
1 350 THR n 
1 351 SER n 
1 352 PRO n 
1 353 LYS n 
1 354 ASP n 
1 355 SER n 
1 356 ALA n 
1 357 LEU n 
1 358 GLY n 
1 359 VAL n 
1 360 ILE n 
1 361 MET n 
1 362 LEU n 
1 363 GLY n 
1 364 ASN n 
1 365 ASN n 
1 366 SER n 
1 367 GLU n 
1 368 ILE n 
1 369 VAL n 
1 370 SER n 
1 371 VAL n 
1 372 PHE n 
1 373 GLU n 
1 374 ARG n 
1 375 ILE n 
1 376 GLY n 
1 377 ALA n 
1 378 ASN n 
1 379 PHE n 
1 380 ASP n 
1 381 ARG n 
1 382 LEU n 
1 383 TRP n 
1 384 SER n 
1 385 ARG n 
1 386 LYS n 
1 387 ALA n 
1 388 PHE n 
1 389 ALA n 
1 390 HIS n 
1 391 TRP n 
1 392 PHE n 
1 393 THR n 
1 394 ASP n 
1 395 SER n 
1 396 GLY n 
1 397 PHE n 
1 398 GLU n 
1 399 GLU n 
1 400 LYS n 
1 401 ASP n 
1 402 LEU n 
1 403 ASP n 
1 404 ASP n 
1 405 ALA n 
1 406 ARG n 
1 407 ALA n 
1 408 LEU n 
1 409 VAL n 
1 410 GLN n 
1 411 LYS n 
1 412 VAL n 
1 413 ILE n 
1 414 ASP n 
1 415 ASP n 
1 416 TYR n 
1 417 ARG n 
1 418 LYS n 
1 419 LEU n 
1 420 THR n 
1 421 GLU n 
1 422 ASP n 
1 423 ALA n 
2 1   MET n 
2 2   GLY n 
2 3   ARG n 
2 4   GLU n 
2 5   VAL n 
2 6   ILE n 
2 7   MET n 
2 8   LEU n 
2 9   HIS n 
2 10  VAL n 
2 11  GLY n 
2 12  GLN n 
2 13  ALA n 
2 14  GLY n 
2 15  ILE n 
2 16  GLN n 
2 17  VAL n 
2 18  GLY n 
2 19  ALA n 
2 20  MET n 
2 21  TYR n 
2 22  TRP n 
2 23  LYS n 
2 24  GLN n 
2 25  ILE n 
2 26  CYS n 
2 27  ALA n 
2 28  GLU n 
2 29  HIS n 
2 30  ASN n 
2 31  LEU n 
2 32  ASP n 
2 33  HIS n 
2 34  ASN n 
2 35  GLY n 
2 36  ALA n 
2 37  PRO n 
2 38  ILE n 
2 39  GLY n 
2 40  GLY n 
2 41  ASP n 
2 42  ILE n 
2 43  LYS n 
2 44  GLY n 
2 45  ASP n 
2 46  PRO n 
2 47  ASP n 
2 48  CYS n 
2 49  PHE n 
2 50  PHE n 
2 51  MET n 
2 52  LYS n 
2 53  ALA n 
2 54  SER n 
2 55  GLY n 
2 56  GLY n 
2 57  LYS n 
2 58  TYR n 
2 59  VAL n 
2 60  PRO n 
2 61  ARG n 
2 62  ALA n 
2 63  LEU n 
2 64  LEU n 
2 65  ILE n 
2 66  ASP n 
2 67  LEU n 
2 68  GLU n 
2 69  PRO n 
2 70  LYS n 
2 71  VAL n 
2 72  VAL n 
2 73  ARG n 
2 74  GLN n 
2 75  VAL n 
2 76  GLY n 
2 77  ASN n 
2 78  GLU n 
2 79  GLN n 
2 80  LEU n 
2 81  PRO n 
2 82  SER n 
2 83  PHE n 
2 84  PHE n 
2 85  ASP n 
2 86  PRO n 
2 87  LYS n 
2 88  ASN n 
2 89  LEU n 
2 90  ILE n 
2 91  HIS n 
2 92  GLY n 
2 93  LEU n 
2 94  TYR n 
2 95  GLY n 
2 96  GLY n 
2 97  ALA n 
2 98  ASN n 
2 99  SER n 
2 100 PHE n 
2 101 ALA n 
2 102 LYS n 
2 103 GLY n 
2 104 TYR n 
2 105 LEU n 
2 106 GLY n 
2 107 GLU n 
2 108 GLY n 
2 109 ARG n 
2 110 ASP n 
2 111 MET n 
2 112 ILE n 
2 113 ASP n 
2 114 ASN n 
2 115 ILE n 
2 116 MET n 
2 117 GLU n 
2 118 GLN n 
2 119 LEU n 
2 120 LYS n 
2 121 LYS n 
2 122 GLU n 
2 123 VAL n 
2 124 ALA n 
2 125 LYS n 
2 126 CYS n 
2 127 GLU n 
2 128 SER n 
2 129 LEU n 
2 130 GLN n 
2 131 GLY n 
2 132 PHE n 
2 133 ILE n 
2 134 MET n 
2 135 THR n 
2 136 HIS n 
2 137 ALA n 
2 138 VAL n 
2 139 GLY n 
2 140 GLY n 
2 141 GLY n 
2 142 SER n 
2 143 GLY n 
2 144 GLY n 
2 145 GLY n 
2 146 LEU n 
2 147 GLY n 
2 148 CYS n 
2 149 LEU n 
2 150 ILE n 
2 151 MET n 
2 152 GLU n 
2 153 LYS n 
2 154 ILE n 
2 155 LYS n 
2 156 GLU n 
2 157 GLU n 
2 158 TYR n 
2 159 PRO n 
2 160 LYS n 
2 161 LYS n 
2 162 ILE n 
2 163 LEU n 
2 164 TRP n 
2 165 SER n 
2 166 TYR n 
2 167 SER n 
2 168 ILE n 
2 169 LEU n 
2 170 PRO n 
2 171 SER n 
2 172 PRO n 
2 173 LEU n 
2 174 LEU n 
2 175 SER n 
2 176 ASP n 
2 177 ALA n 
2 178 VAL n 
2 179 VAL n 
2 180 GLU n 
2 181 PRO n 
2 182 TYR n 
2 183 ASN n 
2 184 ALA n 
2 185 ILE n 
2 186 LEU n 
2 187 SER n 
2 188 LEU n 
2 189 ASP n 
2 190 LYS n 
2 191 MET n 
2 192 ILE n 
2 193 GLN n 
2 194 TYR n 
2 195 THR n 
2 196 ASP n 
2 197 GLU n 
2 198 THR n 
2 199 VAL n 
2 200 VAL n 
2 201 ILE n 
2 202 ASP n 
2 203 ASN n 
2 204 HIS n 
2 205 ALA n 
2 206 LEU n 
2 207 PHE n 
2 208 GLN n 
2 209 ILE n 
2 210 VAL n 
2 211 THR n 
2 212 LYS n 
2 213 ASN n 
2 214 MET n 
2 215 GLY n 
2 216 ILE n 
2 217 ASP n 
2 218 ASP n 
2 219 PRO n 
2 220 ILE n 
2 221 TYR n 
2 222 ASP n 
2 223 ASP n 
2 224 LEU n 
2 225 ASN n 
2 226 HIS n 
2 227 VAL n 
2 228 ILE n 
2 229 SER n 
2 230 GLN n 
2 231 ALA n 
2 232 LEU n 
2 233 SER n 
2 234 ASP n 
2 235 ILE n 
2 236 THR n 
2 237 ALA n 
2 238 SER n 
2 239 LEU n 
2 240 ARG n 
2 241 PHE n 
2 242 LYS n 
2 243 GLY n 
2 244 SER n 
2 245 LEU n 
2 246 ASN n 
2 247 THR n 
2 248 ASP n 
2 249 MET n 
2 250 LYS n 
2 251 GLU n 
2 252 PHE n 
2 253 LEU n 
2 254 VAL n 
2 255 ASN n 
2 256 LEU n 
2 257 VAL n 
2 258 PRO n 
2 259 TYR n 
2 260 PRO n 
2 261 ARG n 
2 262 SER n 
2 263 HIS n 
2 264 PHE n 
2 265 LEU n 
2 266 MET n 
2 267 ALA n 
2 268 SER n 
2 269 PHE n 
2 270 ALA n 
2 271 PRO n 
2 272 MET n 
2 273 ALA n 
2 274 THR n 
2 275 ALA n 
2 276 GLU n 
2 277 ASP n 
2 278 ARG n 
2 279 GLN n 
2 280 TYR n 
2 281 ALA n 
2 282 LYS n 
2 283 LEU n 
2 284 THR n 
2 285 THR n 
2 286 SER n 
2 287 ASN n 
2 288 LEU n 
2 289 ALA n 
2 290 ASN n 
2 291 ALA n 
2 292 LEU n 
2 293 PHE n 
2 294 GLU n 
2 295 GLU n 
2 296 ASN n 
2 297 TYR n 
2 298 MET n 
2 299 MET n 
2 300 ALA n 
2 301 ALA n 
2 302 VAL n 
2 303 ASP n 
2 304 VAL n 
2 305 THR n 
2 306 LYS n 
2 307 GLY n 
2 308 THR n 
2 309 PHE n 
2 310 LEU n 
2 311 ALA n 
2 312 CYS n 
2 313 SER n 
2 314 LEU n 
2 315 LEU n 
2 316 PHE n 
2 317 ARG n 
2 318 GLY n 
2 319 GLU n 
2 320 ASN n 
2 321 THR n 
2 322 ALA n 
2 323 GLN n 
2 324 ASP n 
2 325 ILE n 
2 326 THR n 
2 327 ASN n 
2 328 ALA n 
2 329 LEU n 
2 330 LEU n 
2 331 ASP n 
2 332 ILE n 
2 333 LYS n 
2 334 GLY n 
2 335 ARG n 
2 336 ILE n 
2 337 LYS n 
2 338 PHE n 
2 339 SER n 
2 340 SER n 
2 341 PHE n 
2 342 ILE n 
2 343 PRO n 
2 344 THR n 
2 345 GLY n 
2 346 ILE n 
2 347 LYS n 
2 348 TYR n 
2 349 GLY n 
2 350 MET n 
2 351 THR n 
2 352 GLY n 
2 353 THR n 
2 354 ALA n 
2 355 PRO n 
2 356 GLU n 
2 357 GLY n 
2 358 LEU n 
2 359 GLU n 
2 360 ARG n 
2 361 SER n 
2 362 GLY n 
2 363 SER n 
2 364 ALA n 
2 365 LEU n 
2 366 ILE n 
2 367 ASN n 
2 368 HIS n 
2 369 THR n 
2 370 GLY n 
2 371 VAL n 
2 372 ALA n 
2 373 GLU n 
2 374 ILE n 
2 375 PHE n 
2 376 ASN n 
2 377 ARG n 
2 378 ILE n 
2 379 LEU n 
2 380 ALA n 
2 381 GLN n 
2 382 PHE n 
2 383 ASN n 
2 384 LEU n 
2 385 MET n 
2 386 PHE n 
2 387 ASP n 
2 388 LYS n 
2 389 GLY n 
2 390 ALA n 
2 391 PHE n 
2 392 LEU n 
2 393 ASN n 
2 394 TRP n 
2 395 TYR n 
2 396 GLU n 
2 397 ILE n 
2 398 GLU n 
2 399 GLY n 
2 400 MET n 
2 401 SER n 
2 402 LYS n 
2 403 ASP n 
2 404 ASP n 
2 405 PHE n 
2 406 ALA n 
2 407 GLY n 
2 408 ALA n 
2 409 ARG n 
2 410 ASP n 
2 411 ASN n 
2 412 VAL n 
2 413 GLN n 
2 414 LYS n 
2 415 LEU n 
2 416 SER n 
2 417 ASP n 
2 418 GLU n 
2 419 TYR n 
2 420 LYS n 
2 421 ARG n 
2 422 ASP n 
2 423 GLU n 
2 424 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 423 ? ? ? ? ? ? ? ? ? 'Candidatus Lokiarchaeum ossiferum' 2951803 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 424 ? ? ? ? ? ? ? ? ? 'Candidatus Lokiarchaeum ossiferum' 2951803 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
GTP non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O14 P3' 523.180 
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
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   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   CYS 7   7   7   CYS CYS A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  TRP 22  22  22  TRP TRP A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  CYS 26  26  26  CYS CYS A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  HIS 29  29  29  HIS HIS A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  PHE 48  48  48  PHE PHE 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  ILE 52  52  52  ILE ILE A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ARG 74  74  74  ARG ARG A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  PHE 77  77  77  PHE PHE A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 MET 113 113 113 MET MET A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 GLU 124 124 124 GLU GLU A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 CYS 135 135 135 CYS CYS A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 PHE 143 143 143 PHE PHE A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 ARG 154 154 154 ARG ARG A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 PHE 163 163 163 PHE PHE A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 PRO 169 169 169 PRO PRO A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 VAL 176 176 176 VAL VAL A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 TYR 179 179 179 TYR TYR A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 MET 183 183 183 MET MET A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 CYS 194 194 194 CYS CYS A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 PHE 204 204 204 PHE PHE A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 LYS 209 209 209 LYS LYS A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 ASN 215 215 215 ASN ASN A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 ASN 222 222 222 ASN ASN A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 PHE 238 238 238 PHE PHE A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 THR 241 241 241 THR THR A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 PHE 256 256 256 PHE PHE A . n 
A 1 257 SER 257 257 257 SER SER 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 HIS 260 260 260 HIS HIS A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 MET 263 263 263 MET MET A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 ALA 267 267 267 ALA ALA 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 VAL 270 270 270 VAL VAL A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 TYR 277 277 277 TYR TYR A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 MET 280 280 280 MET MET A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 PHE 290 290 290 PHE PHE A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 TYR 294 294 294 TYR TYR A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 CYS 296 296 296 CYS CYS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 CYS 299 299 299 CYS CYS A . n 
A 1 300 LYS 300 300 300 LYS LYS A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 GLY 304 304 304 GLY GLY A . n 
A 1 305 ARG 305 305 305 ARG ARG A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 VAL 317 317 317 VAL VAL A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 SER 320 320 320 SER SER A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 ASN 323 323 323 ASN ASN A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 MET 326 326 326 MET MET A . n 
A 1 327 ALA 327 327 327 ALA ALA A . n 
A 1 328 THR 328 328 328 THR THR A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 LYS 330 330 330 LYS LYS A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 GLN 332 332 332 GLN GLN A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 VAL 336 336 336 VAL VAL A . n 
A 1 337 ASN 337 337 337 ASN ASN A . n 
A 1 338 TRP 338 338 338 TRP TRP A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 THR 341 341 341 THR THR A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 LYS 347 347 347 LYS LYS A . n 
A 1 348 SER 348 348 348 SER SER A . n 
A 1 349 GLU 349 349 349 GLU GLU A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 PRO 352 352 352 PRO PRO A . n 
A 1 353 LYS 353 353 353 LYS LYS A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 VAL 359 359 359 VAL VAL A . n 
A 1 360 ILE 360 360 360 ILE ILE A . n 
A 1 361 MET 361 361 361 MET MET A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 ASN 365 365 365 ASN ASN A . n 
A 1 366 SER 366 366 366 SER SER A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 VAL 369 369 369 VAL VAL A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 VAL 371 371 371 VAL VAL A . n 
A 1 372 PHE 372 372 372 PHE PHE A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 ARG 374 374 374 ARG ARG A . n 
A 1 375 ILE 375 375 375 ILE ILE A . n 
A 1 376 GLY 376 376 376 GLY GLY A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 ASN 378 378 378 ASN ASN A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 ASP 380 380 380 ASP ASP A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 LEU 382 382 382 LEU LEU A . n 
A 1 383 TRP 383 383 383 TRP TRP A . n 
A 1 384 SER 384 384 384 SER SER A . n 
A 1 385 ARG 385 385 385 ARG ARG A . n 
A 1 386 LYS 386 386 386 LYS LYS A . n 
A 1 387 ALA 387 387 387 ALA ALA A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 HIS 390 390 390 HIS HIS A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 GLU 399 399 399 GLU GLU A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 ASP 401 401 401 ASP ASP A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 ASP 404 404 404 ASP ASP A . n 
A 1 405 ALA 405 405 405 ALA ALA A . n 
A 1 406 ARG 406 406 406 ARG ARG A . n 
A 1 407 ALA 407 407 407 ALA ALA A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 VAL 409 409 409 VAL VAL A . n 
A 1 410 GLN 410 410 410 GLN GLN A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 VAL 412 412 412 VAL VAL A . n 
A 1 413 ILE 413 413 413 ILE ILE A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 TYR 416 416 416 TYR TYR A . n 
A 1 417 ARG 417 417 417 ARG ARG A . n 
A 1 418 LYS 418 418 418 LYS LYS A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 THR 420 420 420 THR THR A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 ASP 422 422 422 ASP ASP A . n 
A 1 423 ALA 423 423 423 ALA ALA A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   GLY 2   2   2   GLY GLY B . n 
B 2 3   ARG 3   3   3   ARG ARG B . n 
B 2 4   GLU 4   4   4   GLU GLU B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   MET 7   7   7   MET MET B . n 
B 2 8   LEU 8   8   8   LEU LEU B . n 
B 2 9   HIS 9   9   9   HIS HIS B . n 
B 2 10  VAL 10  10  10  VAL VAL B . n 
B 2 11  GLY 11  11  11  GLY GLY B . n 
B 2 12  GLN 12  12  12  GLN GLN B . n 
B 2 13  ALA 13  13  13  ALA ALA B . n 
B 2 14  GLY 14  14  14  GLY GLY B . n 
B 2 15  ILE 15  15  15  ILE ILE B . n 
B 2 16  GLN 16  16  16  GLN GLN B . n 
B 2 17  VAL 17  17  17  VAL VAL B . n 
B 2 18  GLY 18  18  18  GLY GLY B . n 
B 2 19  ALA 19  19  19  ALA ALA B . n 
B 2 20  MET 20  20  20  MET MET B . n 
B 2 21  TYR 21  21  21  TYR TYR B . n 
B 2 22  TRP 22  22  22  TRP TRP B . n 
B 2 23  LYS 23  23  23  LYS LYS B . n 
B 2 24  GLN 24  24  24  GLN GLN B . n 
B 2 25  ILE 25  25  25  ILE ILE B . n 
B 2 26  CYS 26  26  26  CYS CYS B . n 
B 2 27  ALA 27  27  27  ALA ALA B . n 
B 2 28  GLU 28  28  28  GLU GLU B . n 
B 2 29  HIS 29  29  29  HIS HIS B . n 
B 2 30  ASN 30  30  30  ASN ASN B . n 
B 2 31  LEU 31  31  31  LEU LEU B . n 
B 2 32  ASP 32  32  32  ASP ASP B . n 
B 2 33  HIS 33  33  33  HIS HIS B . n 
B 2 34  ASN 34  34  34  ASN ASN B . n 
B 2 35  GLY 35  35  35  GLY GLY B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  PRO 37  37  37  PRO PRO B . n 
B 2 38  ILE 38  38  38  ILE ILE B . n 
B 2 39  GLY 39  39  39  GLY GLY B . n 
B 2 40  GLY 40  40  40  GLY GLY B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  ILE 42  42  42  ILE ILE B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  ASP 45  45  45  ASP ASP B . n 
B 2 46  PRO 46  46  46  PRO PRO B . n 
B 2 47  ASP 47  47  47  ASP ASP B . n 
B 2 48  CYS 48  48  48  CYS CYS B . n 
B 2 49  PHE 49  49  49  PHE PHE B . n 
B 2 50  PHE 50  50  50  PHE PHE B . n 
B 2 51  MET 51  51  51  MET MET B . n 
B 2 52  LYS 52  52  52  LYS LYS B . n 
B 2 53  ALA 53  53  53  ALA ALA B . n 
B 2 54  SER 54  54  54  SER SER B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  LYS 57  57  57  LYS LYS B . n 
B 2 58  TYR 58  58  58  TYR TYR B . n 
B 2 59  VAL 59  59  59  VAL VAL B . n 
B 2 60  PRO 60  60  60  PRO PRO B . n 
B 2 61  ARG 61  61  61  ARG ARG B . n 
B 2 62  ALA 62  62  62  ALA ALA B . n 
B 2 63  LEU 63  63  63  LEU LEU B . n 
B 2 64  LEU 64  64  64  LEU LEU B . n 
B 2 65  ILE 65  65  65  ILE ILE B . n 
B 2 66  ASP 66  66  66  ASP ASP B . n 
B 2 67  LEU 67  67  67  LEU LEU B . n 
B 2 68  GLU 68  68  68  GLU GLU B . n 
B 2 69  PRO 69  69  69  PRO PRO B . n 
B 2 70  LYS 70  70  70  LYS LYS B . n 
B 2 71  VAL 71  71  71  VAL VAL B . n 
B 2 72  VAL 72  72  72  VAL VAL B . n 
B 2 73  ARG 73  73  73  ARG ARG B . n 
B 2 74  GLN 74  74  74  GLN GLN B . n 
B 2 75  VAL 75  75  75  VAL VAL B . n 
B 2 76  GLY 76  76  76  GLY GLY B . n 
B 2 77  ASN 77  77  77  ASN ASN B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  GLN 79  79  79  GLN GLN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  PRO 81  81  81  PRO PRO B . n 
B 2 82  SER 82  82  82  SER SER B . n 
B 2 83  PHE 83  83  83  PHE PHE B . n 
B 2 84  PHE 84  84  84  PHE PHE B . n 
B 2 85  ASP 85  85  85  ASP ASP B . n 
B 2 86  PRO 86  86  86  PRO PRO B . n 
B 2 87  LYS 87  87  87  LYS LYS B . n 
B 2 88  ASN 88  88  88  ASN ASN B . n 
B 2 89  LEU 89  89  89  LEU LEU B . n 
B 2 90  ILE 90  90  90  ILE ILE B . n 
B 2 91  HIS 91  91  91  HIS HIS B . n 
B 2 92  GLY 92  92  92  GLY GLY B . n 
B 2 93  LEU 93  93  93  LEU LEU B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  GLY 95  95  95  GLY GLY 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  ASN 98  98  98  ASN ASN B . n 
B 2 99  SER 99  99  99  SER SER B . n 
B 2 100 PHE 100 100 100 PHE PHE B . n 
B 2 101 ALA 101 101 101 ALA ALA B . n 
B 2 102 LYS 102 102 102 LYS LYS B . n 
B 2 103 GLY 103 103 103 GLY GLY B . n 
B 2 104 TYR 104 104 104 TYR TYR B . n 
B 2 105 LEU 105 105 105 LEU LEU B . n 
B 2 106 GLY 106 106 106 GLY GLY B . n 
B 2 107 GLU 107 107 107 GLU GLU B . n 
B 2 108 GLY 108 108 108 GLY GLY B . n 
B 2 109 ARG 109 109 109 ARG ARG B . n 
B 2 110 ASP 110 110 110 ASP ASP B . n 
B 2 111 MET 111 111 111 MET MET B . n 
B 2 112 ILE 112 112 112 ILE ILE B . n 
B 2 113 ASP 113 113 113 ASP ASP B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 ILE 115 115 115 ILE ILE B . n 
B 2 116 MET 116 116 116 MET MET B . n 
B 2 117 GLU 117 117 117 GLU GLU B . n 
B 2 118 GLN 118 118 118 GLN GLN B . n 
B 2 119 LEU 119 119 119 LEU LEU B . n 
B 2 120 LYS 120 120 120 LYS LYS B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 GLU 122 122 122 GLU GLU B . n 
B 2 123 VAL 123 123 123 VAL VAL B . n 
B 2 124 ALA 124 124 124 ALA ALA B . n 
B 2 125 LYS 125 125 125 LYS LYS B . n 
B 2 126 CYS 126 126 126 CYS CYS B . n 
B 2 127 GLU 127 127 127 GLU GLU B . n 
B 2 128 SER 128 128 128 SER SER B . n 
B 2 129 LEU 129 129 129 LEU LEU B . n 
B 2 130 GLN 130 130 130 GLN GLN B . n 
B 2 131 GLY 131 131 131 GLY GLY B . n 
B 2 132 PHE 132 132 132 PHE PHE B . n 
B 2 133 ILE 133 133 133 ILE ILE B . n 
B 2 134 MET 134 134 134 MET MET B . n 
B 2 135 THR 135 135 135 THR THR B . n 
B 2 136 HIS 136 136 136 HIS HIS B . n 
B 2 137 ALA 137 137 137 ALA ALA B . n 
B 2 138 VAL 138 138 138 VAL VAL B . n 
B 2 139 GLY 139 139 139 GLY GLY 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 SER 142 142 142 SER SER B . n 
B 2 143 GLY 143 143 143 GLY GLY B . n 
B 2 144 GLY 144 144 144 GLY GLY B . n 
B 2 145 GLY 145 145 145 GLY GLY B . n 
B 2 146 LEU 146 146 146 LEU LEU B . n 
B 2 147 GLY 147 147 147 GLY GLY B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 LEU 149 149 149 LEU LEU B . n 
B 2 150 ILE 150 150 150 ILE ILE B . n 
B 2 151 MET 151 151 151 MET MET B . n 
B 2 152 GLU 152 152 152 GLU GLU B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 ILE 154 154 154 ILE ILE B . n 
B 2 155 LYS 155 155 155 LYS LYS B . n 
B 2 156 GLU 156 156 156 GLU GLU B . n 
B 2 157 GLU 157 157 157 GLU GLU B . n 
B 2 158 TYR 158 158 158 TYR TYR B . n 
B 2 159 PRO 159 159 159 PRO PRO B . n 
B 2 160 LYS 160 160 160 LYS LYS B . n 
B 2 161 LYS 161 161 161 LYS LYS B . n 
B 2 162 ILE 162 162 162 ILE ILE B . n 
B 2 163 LEU 163 163 163 LEU LEU B . n 
B 2 164 TRP 164 164 164 TRP TRP B . n 
B 2 165 SER 165 165 165 SER SER B . n 
B 2 166 TYR 166 166 166 TYR TYR B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 ILE 168 168 168 ILE ILE B . n 
B 2 169 LEU 169 169 169 LEU LEU B . n 
B 2 170 PRO 170 170 170 PRO PRO B . n 
B 2 171 SER 171 171 171 SER SER B . n 
B 2 172 PRO 172 172 172 PRO PRO B . n 
B 2 173 LEU 173 173 173 LEU LEU B . n 
B 2 174 LEU 174 174 174 LEU LEU B . n 
B 2 175 SER 175 175 175 SER SER B . n 
B 2 176 ASP 176 176 176 ASP ASP B . n 
B 2 177 ALA 177 177 177 ALA ALA B . n 
B 2 178 VAL 178 178 178 VAL VAL B . n 
B 2 179 VAL 179 179 179 VAL VAL B . n 
B 2 180 GLU 180 180 180 GLU GLU B . n 
B 2 181 PRO 181 181 181 PRO PRO B . n 
B 2 182 TYR 182 182 182 TYR TYR B . n 
B 2 183 ASN 183 183 183 ASN ASN B . n 
B 2 184 ALA 184 184 184 ALA ALA B . n 
B 2 185 ILE 185 185 185 ILE ILE B . n 
B 2 186 LEU 186 186 186 LEU LEU B . n 
B 2 187 SER 187 187 187 SER SER B . n 
B 2 188 LEU 188 188 188 LEU LEU B . n 
B 2 189 ASP 189 189 189 ASP ASP B . n 
B 2 190 LYS 190 190 190 LYS LYS B . n 
B 2 191 MET 191 191 191 MET MET B . n 
B 2 192 ILE 192 192 192 ILE ILE B . n 
B 2 193 GLN 193 193 193 GLN GLN B . n 
B 2 194 TYR 194 194 194 TYR TYR B . n 
B 2 195 THR 195 195 195 THR THR B . n 
B 2 196 ASP 196 196 196 ASP ASP B . n 
B 2 197 GLU 197 197 197 GLU GLU B . n 
B 2 198 THR 198 198 198 THR THR B . n 
B 2 199 VAL 199 199 199 VAL VAL B . n 
B 2 200 VAL 200 200 200 VAL VAL B . n 
B 2 201 ILE 201 201 201 ILE ILE B . n 
B 2 202 ASP 202 202 202 ASP ASP B . n 
B 2 203 ASN 203 203 203 ASN ASN B . n 
B 2 204 HIS 204 204 204 HIS HIS B . n 
B 2 205 ALA 205 205 205 ALA ALA B . n 
B 2 206 LEU 206 206 206 LEU LEU B . n 
B 2 207 PHE 207 207 207 PHE PHE B . n 
B 2 208 GLN 208 208 208 GLN GLN B . n 
B 2 209 ILE 209 209 209 ILE ILE B . n 
B 2 210 VAL 210 210 210 VAL VAL B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 LYS 212 212 212 LYS LYS B . n 
B 2 213 ASN 213 213 213 ASN ASN B . n 
B 2 214 MET 214 214 214 MET MET B . n 
B 2 215 GLY 215 215 215 GLY GLY B . n 
B 2 216 ILE 216 216 216 ILE ILE B . n 
B 2 217 ASP 217 217 217 ASP ASP B . n 
B 2 218 ASP 218 218 218 ASP ASP B . n 
B 2 219 PRO 219 219 219 PRO PRO B . n 
B 2 220 ILE 220 220 220 ILE ILE B . n 
B 2 221 TYR 221 221 221 TYR TYR B . n 
B 2 222 ASP 222 222 222 ASP ASP B . n 
B 2 223 ASP 223 223 223 ASP ASP B . n 
B 2 224 LEU 224 224 224 LEU LEU B . n 
B 2 225 ASN 225 225 225 ASN ASN B . n 
B 2 226 HIS 226 226 226 HIS HIS B . n 
B 2 227 VAL 227 227 227 VAL VAL B . n 
B 2 228 ILE 228 228 228 ILE ILE B . n 
B 2 229 SER 229 229 229 SER SER B . n 
B 2 230 GLN 230 230 230 GLN GLN B . n 
B 2 231 ALA 231 231 231 ALA ALA B . n 
B 2 232 LEU 232 232 232 LEU LEU B . n 
B 2 233 SER 233 233 233 SER SER B . n 
B 2 234 ASP 234 234 234 ASP ASP B . n 
B 2 235 ILE 235 235 235 ILE ILE B . n 
B 2 236 THR 236 236 236 THR THR B . n 
B 2 237 ALA 237 237 237 ALA ALA B . n 
B 2 238 SER 238 238 238 SER SER B . n 
B 2 239 LEU 239 239 239 LEU LEU B . n 
B 2 240 ARG 240 240 240 ARG ARG B . n 
B 2 241 PHE 241 241 241 PHE PHE B . n 
B 2 242 LYS 242 242 242 LYS LYS B . n 
B 2 243 GLY 243 243 243 GLY GLY B . n 
B 2 244 SER 244 244 244 SER SER B . n 
B 2 245 LEU 245 245 245 LEU LEU B . n 
B 2 246 ASN 246 246 246 ASN ASN B . n 
B 2 247 THR 247 247 247 THR THR B . n 
B 2 248 ASP 248 248 248 ASP ASP B . n 
B 2 249 MET 249 249 249 MET MET B . n 
B 2 250 LYS 250 250 250 LYS LYS B . n 
B 2 251 GLU 251 251 251 GLU GLU B . n 
B 2 252 PHE 252 252 252 PHE PHE B . n 
B 2 253 LEU 253 253 253 LEU LEU B . n 
B 2 254 VAL 254 254 254 VAL VAL B . n 
B 2 255 ASN 255 255 255 ASN ASN B . n 
B 2 256 LEU 256 256 256 LEU LEU B . n 
B 2 257 VAL 257 257 257 VAL VAL B . n 
B 2 258 PRO 258 258 258 PRO PRO B . n 
B 2 259 TYR 259 259 259 TYR TYR B . n 
B 2 260 PRO 260 260 260 PRO PRO B . n 
B 2 261 ARG 261 261 261 ARG ARG B . n 
B 2 262 SER 262 262 262 SER SER B . n 
B 2 263 HIS 263 263 263 HIS HIS B . n 
B 2 264 PHE 264 264 264 PHE PHE B . n 
B 2 265 LEU 265 265 265 LEU LEU B . n 
B 2 266 MET 266 266 266 MET MET B . n 
B 2 267 ALA 267 267 267 ALA ALA B . n 
B 2 268 SER 268 268 268 SER SER B . n 
B 2 269 PHE 269 269 269 PHE PHE B . n 
B 2 270 ALA 270 270 270 ALA ALA B . n 
B 2 271 PRO 271 271 271 PRO PRO B . n 
B 2 272 MET 272 272 272 MET MET B . n 
B 2 273 ALA 273 273 273 ALA ALA B . n 
B 2 274 THR 274 274 274 THR THR B . n 
B 2 275 ALA 275 275 275 ALA ALA B . n 
B 2 276 GLU 276 276 276 GLU GLU B . n 
B 2 277 ASP 277 277 277 ASP ASP B . n 
B 2 278 ARG 278 278 278 ARG ARG B . n 
B 2 279 GLN 279 279 279 GLN GLN B . n 
B 2 280 TYR 280 280 280 TYR TYR B . n 
B 2 281 ALA 281 281 281 ALA ALA B . n 
B 2 282 LYS 282 282 282 LYS LYS B . n 
B 2 283 LEU 283 283 283 LEU LEU B . n 
B 2 284 THR 284 284 284 THR THR B . n 
B 2 285 THR 285 285 285 THR THR B . n 
B 2 286 SER 286 286 286 SER SER B . n 
B 2 287 ASN 287 287 287 ASN ASN B . n 
B 2 288 LEU 288 288 288 LEU LEU B . n 
B 2 289 ALA 289 289 289 ALA ALA B . n 
B 2 290 ASN 290 290 290 ASN ASN B . n 
B 2 291 ALA 291 291 291 ALA ALA B . n 
B 2 292 LEU 292 292 292 LEU LEU B . n 
B 2 293 PHE 293 293 293 PHE PHE B . n 
B 2 294 GLU 294 294 294 GLU GLU B . n 
B 2 295 GLU 295 295 295 GLU GLU B . n 
B 2 296 ASN 296 296 296 ASN ASN B . n 
B 2 297 TYR 297 297 297 TYR TYR B . n 
B 2 298 MET 298 298 298 MET MET B . n 
B 2 299 MET 299 299 299 MET MET B . n 
B 2 300 ALA 300 300 300 ALA ALA B . n 
B 2 301 ALA 301 301 301 ALA ALA B . n 
B 2 302 VAL 302 302 302 VAL VAL B . n 
B 2 303 ASP 303 303 303 ASP ASP B . n 
B 2 304 VAL 304 304 304 VAL VAL B . n 
B 2 305 THR 305 305 305 THR THR B . n 
B 2 306 LYS 306 306 306 LYS LYS B . n 
B 2 307 GLY 307 307 307 GLY GLY B . n 
B 2 308 THR 308 308 308 THR THR B . n 
B 2 309 PHE 309 309 309 PHE PHE B . n 
B 2 310 LEU 310 310 310 LEU LEU B . n 
B 2 311 ALA 311 311 311 ALA ALA B . n 
B 2 312 CYS 312 312 312 CYS CYS B . n 
B 2 313 SER 313 313 313 SER SER B . n 
B 2 314 LEU 314 314 314 LEU LEU B . n 
B 2 315 LEU 315 315 315 LEU LEU B . n 
B 2 316 PHE 316 316 316 PHE PHE B . n 
B 2 317 ARG 317 317 317 ARG ARG B . n 
B 2 318 GLY 318 318 318 GLY GLY B . n 
B 2 319 GLU 319 319 319 GLU GLU B . n 
B 2 320 ASN 320 320 320 ASN ASN B . n 
B 2 321 THR 321 321 321 THR THR B . n 
B 2 322 ALA 322 322 322 ALA ALA B . n 
B 2 323 GLN 323 323 323 GLN GLN B . n 
B 2 324 ASP 324 324 324 ASP ASP B . n 
B 2 325 ILE 325 325 325 ILE ILE B . n 
B 2 326 THR 326 326 326 THR THR B . n 
B 2 327 ASN 327 327 327 ASN ASN B . n 
B 2 328 ALA 328 328 328 ALA ALA B . n 
B 2 329 LEU 329 329 329 LEU LEU B . n 
B 2 330 LEU 330 330 330 LEU LEU B . n 
B 2 331 ASP 331 331 331 ASP ASP B . n 
B 2 332 ILE 332 332 332 ILE ILE B . n 
B 2 333 LYS 333 333 333 LYS LYS B . n 
B 2 334 GLY 334 334 334 GLY GLY B . n 
B 2 335 ARG 335 335 335 ARG ARG B . n 
B 2 336 ILE 336 336 336 ILE ILE B . n 
B 2 337 LYS 337 337 337 LYS LYS B . n 
B 2 338 PHE 338 338 338 PHE PHE B . n 
B 2 339 SER 339 339 339 SER SER B . n 
B 2 340 SER 340 340 340 SER SER B . n 
B 2 341 PHE 341 341 341 PHE PHE B . n 
B 2 342 ILE 342 342 342 ILE ILE B . n 
B 2 343 PRO 343 343 343 PRO PRO B . n 
B 2 344 THR 344 344 344 THR THR B . n 
B 2 345 GLY 345 345 345 GLY GLY B . n 
B 2 346 ILE 346 346 346 ILE ILE B . n 
B 2 347 LYS 347 347 347 LYS LYS B . n 
B 2 348 TYR 348 348 348 TYR TYR B . n 
B 2 349 GLY 349 349 349 GLY GLY B . n 
B 2 350 MET 350 350 350 MET MET B . n 
B 2 351 THR 351 351 351 THR THR B . n 
B 2 352 GLY 352 352 352 GLY GLY B . n 
B 2 353 THR 353 353 353 THR THR B . n 
B 2 354 ALA 354 354 354 ALA ALA B . n 
B 2 355 PRO 355 355 355 PRO PRO B . n 
B 2 356 GLU 356 356 356 GLU GLU B . n 
B 2 357 GLY 357 357 357 GLY GLY B . n 
B 2 358 LEU 358 358 358 LEU LEU B . n 
B 2 359 GLU 359 359 359 GLU GLU B . n 
B 2 360 ARG 360 360 360 ARG ARG B . n 
B 2 361 SER 361 361 361 SER SER B . n 
B 2 362 GLY 362 362 362 GLY GLY B . n 
B 2 363 SER 363 363 363 SER SER B . n 
B 2 364 ALA 364 364 364 ALA ALA B . n 
B 2 365 LEU 365 365 365 LEU LEU B . n 
B 2 366 ILE 366 366 366 ILE ILE B . n 
B 2 367 ASN 367 367 367 ASN ASN B . n 
B 2 368 HIS 368 368 368 HIS HIS B . n 
B 2 369 THR 369 369 369 THR THR B . n 
B 2 370 GLY 370 370 370 GLY GLY B . n 
B 2 371 VAL 371 371 371 VAL VAL B . n 
B 2 372 ALA 372 372 372 ALA ALA B . n 
B 2 373 GLU 373 373 373 GLU GLU B . n 
B 2 374 ILE 374 374 374 ILE ILE B . n 
B 2 375 PHE 375 375 375 PHE PHE B . n 
B 2 376 ASN 376 376 376 ASN ASN B . n 
B 2 377 ARG 377 377 377 ARG ARG B . n 
B 2 378 ILE 378 378 378 ILE ILE B . n 
B 2 379 LEU 379 379 379 LEU LEU B . n 
B 2 380 ALA 380 380 380 ALA ALA B . n 
B 2 381 GLN 381 381 381 GLN GLN B . n 
B 2 382 PHE 382 382 382 PHE PHE B . n 
B 2 383 ASN 383 383 383 ASN ASN B . n 
B 2 384 LEU 384 384 384 LEU LEU B . n 
B 2 385 MET 385 385 385 MET MET B . n 
B 2 386 PHE 386 386 386 PHE PHE B . n 
B 2 387 ASP 387 387 387 ASP ASP B . n 
B 2 388 LYS 388 388 388 LYS LYS B . n 
B 2 389 GLY 389 389 389 GLY GLY B . n 
B 2 390 ALA 390 390 390 ALA ALA B . n 
B 2 391 PHE 391 391 391 PHE PHE B . n 
B 2 392 LEU 392 392 392 LEU LEU B . n 
B 2 393 ASN 393 393 393 ASN ASN B . n 
B 2 394 TRP 394 394 394 TRP TRP B . n 
B 2 395 TYR 395 395 395 TYR TYR B . n 
B 2 396 GLU 396 396 396 GLU GLU B . n 
B 2 397 ILE 397 397 397 ILE ILE B . n 
B 2 398 GLU 398 398 398 GLU GLU B . n 
B 2 399 GLY 399 399 399 GLY GLY B . n 
B 2 400 MET 400 400 400 MET MET B . n 
B 2 401 SER 401 401 401 SER SER B . n 
B 2 402 LYS 402 402 402 LYS LYS B . n 
B 2 403 ASP 403 403 403 ASP ASP B . n 
B 2 404 ASP 404 404 404 ASP ASP B . n 
B 2 405 PHE 405 405 405 PHE PHE B . n 
B 2 406 ALA 406 406 406 ALA ALA B . n 
B 2 407 GLY 407 407 407 GLY GLY B . n 
B 2 408 ALA 408 408 408 ALA ALA B . n 
B 2 409 ARG 409 409 409 ARG ARG B . n 
B 2 410 ASP 410 410 410 ASP ASP B . n 
B 2 411 ASN 411 411 411 ASN ASN B . n 
B 2 412 VAL 412 412 412 VAL VAL B . n 
B 2 413 GLN 413 413 413 GLN GLN B . n 
B 2 414 LYS 414 414 414 LYS LYS B . n 
B 2 415 LEU 415 415 415 LEU LEU B . n 
B 2 416 SER 416 416 416 SER SER B . n 
B 2 417 ASP 417 417 417 ASP ASP B . n 
B 2 418 GLU 418 418 418 GLU GLU B . n 
B 2 419 TYR 419 419 419 TYR TYR B . n 
B 2 420 LYS 420 420 420 LYS LYS B . n 
B 2 421 ARG 421 421 421 ARG ARG B . n 
B 2 422 ASP 422 422 422 ASP ASP B . n 
B 2 423 GLU 423 423 423 GLU GLU B . n 
B 2 424 GLU 424 424 424 GLU GLU B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GTP ? ? GTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 GDP 1 501 425 GDP GDP A . 
D 4 GTP 1 501 425 GTP GTP B . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F6U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F6U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F6U 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9F6U 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.018  ? 6700 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 1.549  ? 9076 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 11.945 ? 2452 ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.077  ? 1017 ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.008  ? 1169 ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9F6U 
_struct.title                        'cryoEM structure of Asgard tubulin heterodimer AtubA/B with GDP' 
_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        9F6U 
_struct_keywords.text            'cryoEM, tubulin, Asgard archaea, microtubule, CYTOSOLIC PROTEIN' 
_struct_keywords.pdbx_keywords   'CYTOSOLIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
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 PDB 9F6U 9F6U ? 1 ? 1 
2 PDB 9F6U 9F6U ? 2 ? 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 9F6U A 1 ? 423 ? 9F6U 1 ? 423 ? 1 423 
2 2 9F6U B 1 ? 424 ? 9F6U 1 ? 424 ? 1 424 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 11  ? GLY A 30  ? GLY A 11  GLY A 30  1 ? 20 
HELX_P HELX_P2  AA2 ASP A 44  ? ILE A 47  ? ASP A 44  ILE A 47  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 66  ? VAL A 69  ? GLU A 66  VAL A 69  5 ? 4  
HELX_P HELX_P4  AA4 VAL A 70  ? GLU A 75  ? VAL A 70  GLU A 75  1 ? 6  
HELX_P HELX_P5  AA5 ASP A 82  ? LYS A 84  ? ASP A 82  LYS A 84  5 ? 3  
HELX_P HELX_P6  AA6 ASN A 96  ? ASN A 102 ? ASN A 96  ASN A 102 1 ? 7  
HELX_P HELX_P7  AA7 GLY A 105 ? GLU A 122 ? GLY A 105 GLU A 122 1 ? 18 
HELX_P HELX_P8  AA8 SER A 141 ? TYR A 155 ? SER A 141 TYR A 155 1 ? 15 
HELX_P HELX_P9  AA9 VAL A 176 ? ALA A 192 ? VAL A 176 ALA A 192 1 ? 17 
HELX_P HELX_P10 AB1 ASN A 200 ? LYS A 210 ? ASN A 200 LYS A 210 1 ? 11 
HELX_P HELX_P11 AB2 SER A 217 ? ALA A 234 ? SER A 217 ALA A 234 1 ? 18 
HELX_P HELX_P12 AB3 SER A 235 ? ARG A 237 ? SER A 235 ARG A 237 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 245 ? VAL A 254 ? ASP A 245 VAL A 254 1 ? 10 
HELX_P HELX_P14 AB5 THR A 281 ? PHE A 290 ? THR A 281 PHE A 290 1 ? 10 
HELX_P HELX_P15 AB6 GLY A 291 ? ILE A 295 ? GLY A 291 ILE A 295 5 ? 5  
HELX_P HELX_P16 AB7 LYS A 300 ? GLY A 304 ? LYS A 300 GLY A 304 5 ? 5  
HELX_P HELX_P17 AB8 LYS A 318 ? GLU A 331 ? LYS A 318 GLU A 331 1 ? 14 
HELX_P HELX_P18 AB9 PHE A 335 ? ILE A 339 ? PHE A 335 ILE A 339 5 ? 5  
HELX_P HELX_P19 AC1 ILE A 368 ? LEU A 382 ? ILE A 368 LEU A 382 1 ? 15 
HELX_P HELX_P20 AC2 GLU A 398 ? THR A 420 ? GLU A 398 THR A 420 1 ? 23 
HELX_P HELX_P21 AC3 GLY B 11  ? HIS B 29  ? GLY B 11  HIS B 29  1 ? 19 
HELX_P HELX_P22 AC4 LYS B 70  ? GLU B 78  ? LYS B 70  GLU B 78  1 ? 9  
HELX_P HELX_P23 AC5 ASP B 85  ? LYS B 87  ? ASP B 85  LYS B 87  5 ? 3  
HELX_P HELX_P24 AC6 SER B 99  ? GLY B 106 ? SER B 99  GLY B 106 1 ? 8  
HELX_P HELX_P25 AC7 ASP B 110 ? ALA B 124 ? ASP B 110 ALA B 124 1 ? 15 
HELX_P HELX_P26 AC8 GLY B 140 ? TYR B 158 ? GLY B 140 TYR B 158 1 ? 19 
HELX_P HELX_P27 AC9 VAL B 179 ? THR B 195 ? VAL B 179 THR B 195 1 ? 17 
HELX_P HELX_P28 AD1 ASN B 203 ? ASN B 213 ? ASN B 203 ASN B 213 1 ? 11 
HELX_P HELX_P29 AD2 ILE B 220 ? THR B 236 ? ILE B 220 THR B 236 1 ? 17 
HELX_P HELX_P30 AD3 ALA B 237 ? PHE B 241 ? ALA B 237 PHE B 241 5 ? 5  
HELX_P HELX_P31 AD4 ASP B 248 ? VAL B 257 ? ASP B 248 VAL B 257 1 ? 10 
HELX_P HELX_P32 AD5 THR B 284 ? LEU B 292 ? THR B 284 LEU B 292 1 ? 9  
HELX_P HELX_P33 AD6 PHE B 293 ? MET B 298 ? PHE B 293 MET B 298 5 ? 6  
HELX_P HELX_P34 AD7 THR B 321 ? LEU B 330 ? THR B 321 LEU B 330 1 ? 10 
HELX_P HELX_P35 AD8 GLY B 370 ? LYS B 388 ? GLY B 370 LYS B 388 1 ? 19 
HELX_P HELX_P36 AD9 LEU B 392 ? ILE B 397 ? LEU B 392 ILE B 397 1 ? 6  
HELX_P HELX_P37 AE1 SER B 401 ? ARG B 421 ? SER B 401 ARG B 421 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 267 A . ? ALA 267 A PRO 268 A ? PRO 268 A 1 -7.13 
2 ALA 270 B . ? ALA 270 B PRO 271 B ? PRO 271 B 1 -4.52 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 2  ? 
AA3 ? 10 ? 
AA4 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? parallel      
AA2 1 2  ? anti-parallel 
AA3 1 2  ? parallel      
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? parallel      
AA3 5 6  ? parallel      
AA3 6 7  ? parallel      
AA3 7 8  ? anti-parallel 
AA3 8 9  ? anti-parallel 
AA3 9 10 ? parallel      
AA4 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  ILE A 86  ? SER A 88  ? ILE A 86  SER A 88  
AA1 2  ALA A 60  ? ASP A 64  ? ALA A 60  ASP A 64  
AA1 3  GLU A 4   ? VAL A 10  ? GLU A 4   VAL A 10  
AA1 4  ILE A 126 ? SER A 134 ? ILE A 126 SER A 134 
AA1 5  ILE A 160 ? PHE A 166 ? ILE A 160 PHE A 166 
AA1 6  CYS A 194 ? ASP A 199 ? CYS A 194 ASP A 199 
AA1 7  PHE A 261 ? ALA A 267 ? PHE A 261 ALA A 267 
AA1 8  GLY A 358 ? ASN A 365 ? GLY A 358 ASN A 365 
AA1 9  TYR A 306 ? ARG A 314 ? TYR A 306 ARG A 314 
AA1 10 PHE A 343 ? SER A 348 ? PHE A 343 SER A 348 
AA2 1  PHE A 49  ? THR A 51  ? PHE A 49  THR A 51  
AA2 2  TYR A 56  ? PRO A 58  ? TYR A 56  PRO A 58  
AA3 1  LEU B 89  ? HIS B 91  ? LEU B 89  HIS B 91  
AA3 2  ALA B 62  ? ASP B 66  ? ALA B 62  ASP B 66  
AA3 3  GLU B 4   ? VAL B 10  ? GLU B 4   VAL B 10  
AA3 4  LEU B 129 ? ALA B 137 ? LEU B 129 ALA B 137 
AA3 5  ILE B 162 ? LEU B 169 ? ILE B 162 LEU B 169 
AA3 6  GLU B 197 ? ASP B 202 ? GLU B 197 ASP B 202 
AA3 7  PHE B 264 ? ALA B 270 ? PHE B 264 ALA B 270 
AA3 8  ARG B 360 ? HIS B 368 ? ARG B 360 HIS B 368 
AA3 9  PHE B 309 ? GLY B 318 ? PHE B 309 GLY B 318 
AA3 10 LYS B 347 ? THR B 351 ? LYS B 347 THR B 351 
AA4 1  PHE B 50  ? LYS B 52  ? PHE B 50  LYS B 52  
AA4 2  TYR B 58  ? PRO B 60  ? TYR B 58  PRO B 60  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O VAL A 87  ? O VAL A 87  N VAL A 62  ? N VAL A 62  
AA1 2 3  O VAL A 61  ? O VAL A 61  N GLN A 9   ? N GLN A 9   
AA1 3 4  N ILE A 8   ? N ILE A 8   O ILE A 130 ? O ILE A 130 
AA1 4 5  N PHE A 129 ? N PHE A 129 O PHE A 161 ? O PHE A 161 
AA1 5 6  N PHE A 166 ? N PHE A 166 O LEU A 198 ? O LEU A 198 
AA1 6 7  N SER A 195 ? N SER A 195 O LEU A 262 ? O LEU A 262 
AA1 7 8  N ALA A 267 ? N ALA A 267 O VAL A 359 ? O VAL A 359 
AA1 8 9  O ASN A 364 ? O ASN A 364 N ALA A 308 ? N ALA A 308 
AA1 9 10 N VAL A 311 ? N VAL A 311 O LYS A 344 ? O LYS A 344 
AA2 1 2  N ASN A 50  ? N ASN A 50  O ILE A 57  ? O ILE A 57  
AA3 1 2  O ILE B 90  ? O ILE B 90  N LEU B 64  ? N LEU B 64  
AA3 2 3  O ILE B 65  ? O ILE B 65  N HIS B 9   ? N HIS B 9   
AA3 3 4  N GLU B 4   ? N GLU B 4   O GLN B 130 ? O GLN B 130 
AA3 4 5  N MET B 134 ? N MET B 134 O TYR B 166 ? O TYR B 166 
AA3 5 6  N LEU B 169 ? N LEU B 169 O ILE B 201 ? O ILE B 201 
AA3 6 7  N THR B 198 ? N THR B 198 O LEU B 265 ? O LEU B 265 
AA3 7 8  N MET B 266 ? N MET B 266 O ILE B 366 ? O ILE B 366 
AA3 8 9  O ASN B 367 ? O ASN B 367 N LEU B 310 ? N LEU B 310 
AA3 9 10 N LEU B 314 ? N LEU B 314 O LYS B 347 ? O LYS B 347 
AA4 1 2  N MET B 51  ? N MET B 51  O VAL B 59  ? O VAL B 59  
# 
_pdbx_entry_details.entry_id                   9F6U 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A CYS 194 ? ? SG A CYS 194 ? ? 1.710 1.812 -0.102 0.016 N 
2 1 CB A TRP 338 ? ? CG A TRP 338 ? ? 1.372 1.498 -0.126 0.018 N 
3 1 CB A TRP 391 ? ? CG A TRP 391 ? ? 1.378 1.498 -0.120 0.018 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 34  ? ? 67.80   -66.46  
2  1 LYS A 37  ? ? 56.96   -130.91 
3  1 LYS A 55  ? ? -174.55 141.94  
4  1 ASN A 215 ? ? -157.69 77.81   
5  1 LEU A 259 ? ? -116.25 50.10   
6  1 TRP A 383 ? ? -130.75 -49.86  
7  1 THR A 420 ? ? -107.71 73.78   
8  1 LYS B 70  ? ? -128.28 -63.48  
9  1 SER B 175 ? ? -175.03 139.56  
10 1 LEU B 245 ? ? 63.93   -135.37 
11 1 TYR B 259 ? ? 70.22   161.87  
12 1 ARG B 261 ? ? 67.84   -36.75  
13 1 THR B 274 ? ? 40.60   -117.13 
14 1 LYS B 282 ? ? -125.49 -76.99  
15 1 LEU B 283 ? ? 49.37   12.09   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9F6U 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9F6U 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.6 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               71297 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            6.8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Asgard tubulin heterodimer AtubA/B from Candidatus Lokiarchaeum ossiferum' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_imaging.entry_id                        9F6U 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             2800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        UltrAuFoil 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9F6U 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE-PROPANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9F6U 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
# 
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  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GDP PB     P N N 88  
GDP O1B    O N N 89  
GDP O2B    O N N 90  
GDP O3B    O N N 91  
GDP O3A    O N N 92  
GDP PA     P N N 93  
GDP O1A    O N N 94  
GDP O2A    O N N 95  
GDP "O5'"  O N N 96  
GDP "C5'"  C N N 97  
GDP "C4'"  C N R 98  
GDP "O4'"  O N N 99  
GDP "C3'"  C N S 100 
GDP "O3'"  O N N 101 
GDP "C2'"  C N R 102 
GDP "O2'"  O N N 103 
GDP "C1'"  C N R 104 
GDP N9     N Y N 105 
GDP C8     C Y N 106 
GDP N7     N Y N 107 
GDP C5     C Y N 108 
GDP C6     C N N 109 
GDP O6     O N N 110 
GDP N1     N N N 111 
GDP C2     C N N 112 
GDP N2     N N N 113 
GDP N3     N N N 114 
GDP C4     C Y N 115 
GDP HOB2   H N N 116 
GDP HOB3   H N N 117 
GDP HOA2   H N N 118 
GDP "H5'"  H N N 119 
GDP "H5''" H N N 120 
GDP "H4'"  H N N 121 
GDP "H3'"  H N N 122 
GDP "HO3'" H N N 123 
GDP "H2'"  H N N 124 
GDP "HO2'" H N N 125 
GDP "H1'"  H N N 126 
GDP H8     H N N 127 
GDP HN1    H N N 128 
GDP HN21   H N N 129 
GDP HN22   H N N 130 
GLN N      N N N 131 
GLN CA     C N S 132 
GLN C      C N N 133 
GLN O      O N N 134 
GLN CB     C N N 135 
GLN CG     C N N 136 
GLN CD     C N N 137 
GLN OE1    O N N 138 
GLN NE2    N N N 139 
GLN OXT    O N N 140 
GLN H      H N N 141 
GLN H2     H N N 142 
GLN HA     H N N 143 
GLN HB2    H N N 144 
GLN HB3    H N N 145 
GLN HG2    H N N 146 
GLN HG3    H N N 147 
GLN HE21   H N N 148 
GLN HE22   H N N 149 
GLN HXT    H N N 150 
GLU N      N N N 151 
GLU CA     C N S 152 
GLU C      C N N 153 
GLU O      O N N 154 
GLU CB     C N N 155 
GLU CG     C N N 156 
GLU CD     C N N 157 
GLU OE1    O N N 158 
GLU OE2    O N N 159 
GLU OXT    O N N 160 
GLU H      H N N 161 
GLU H2     H N N 162 
GLU HA     H N N 163 
GLU HB2    H N N 164 
GLU HB3    H N N 165 
GLU HG2    H N N 166 
GLU HG3    H N N 167 
GLU HE2    H N N 168 
GLU HXT    H N N 169 
GLY N      N N N 170 
GLY CA     C N N 171 
GLY C      C N N 172 
GLY O      O N N 173 
GLY OXT    O N N 174 
GLY H      H N N 175 
GLY H2     H N N 176 
GLY HA2    H N N 177 
GLY HA3    H N N 178 
GLY HXT    H N N 179 
GTP PG     P N N 180 
GTP O1G    O N N 181 
GTP O2G    O N N 182 
GTP O3G    O N N 183 
GTP O3B    O N N 184 
GTP PB     P N N 185 
GTP O1B    O N N 186 
GTP O2B    O N N 187 
GTP O3A    O N N 188 
GTP PA     P N N 189 
GTP O1A    O N N 190 
GTP O2A    O N N 191 
GTP "O5'"  O N N 192 
GTP "C5'"  C N N 193 
GTP "C4'"  C N R 194 
GTP "O4'"  O N N 195 
GTP "C3'"  C N S 196 
GTP "O3'"  O N N 197 
GTP "C2'"  C N R 198 
GTP "O2'"  O N N 199 
GTP "C1'"  C N R 200 
GTP N9     N Y N 201 
GTP C8     C Y N 202 
GTP N7     N Y N 203 
GTP C5     C Y N 204 
GTP C6     C N N 205 
GTP O6     O N N 206 
GTP N1     N N N 207 
GTP C2     C N N 208 
GTP N2     N N N 209 
GTP N3     N N N 210 
GTP C4     C Y N 211 
GTP HOG2   H N N 212 
GTP HOG3   H N N 213 
GTP HOB2   H N N 214 
GTP HOA2   H N N 215 
GTP "H5'"  H N N 216 
GTP "H5''" H N N 217 
GTP "H4'"  H N N 218 
GTP "H3'"  H N N 219 
GTP "HO3'" H N N 220 
GTP "H2'"  H N N 221 
GTP "HO2'" H N N 222 
GTP "H1'"  H N N 223 
GTP H8     H N N 224 
GTP HN1    H N N 225 
GTP HN21   H N N 226 
GTP HN22   H N N 227 
HIS N      N N N 228 
HIS CA     C N S 229 
HIS C      C N N 230 
HIS O      O N N 231 
HIS CB     C N N 232 
HIS CG     C Y N 233 
HIS ND1    N Y N 234 
HIS CD2    C Y N 235 
HIS CE1    C Y N 236 
HIS NE2    N Y N 237 
HIS OXT    O N N 238 
HIS H      H N N 239 
HIS H2     H N N 240 
HIS HA     H N N 241 
HIS HB2    H N N 242 
HIS HB3    H N N 243 
HIS HD1    H N N 244 
HIS HD2    H N N 245 
HIS HE1    H N N 246 
HIS HE2    H N N 247 
HIS HXT    H N N 248 
ILE N      N N N 249 
ILE CA     C N S 250 
ILE C      C N N 251 
ILE O      O N N 252 
ILE CB     C N S 253 
ILE CG1    C N N 254 
ILE CG2    C N N 255 
ILE CD1    C N N 256 
ILE OXT    O N N 257 
ILE H      H N N 258 
ILE H2     H N N 259 
ILE HA     H N N 260 
ILE HB     H N N 261 
ILE HG12   H N N 262 
ILE HG13   H N N 263 
ILE HG21   H N N 264 
ILE HG22   H N N 265 
ILE HG23   H N N 266 
ILE HD11   H N N 267 
ILE HD12   H N N 268 
ILE HD13   H N N 269 
ILE HXT    H N N 270 
LEU N      N N N 271 
LEU CA     C N S 272 
LEU C      C N N 273 
LEU O      O N N 274 
LEU CB     C N N 275 
LEU CG     C N N 276 
LEU CD1    C N N 277 
LEU CD2    C N N 278 
LEU OXT    O N N 279 
LEU H      H N N 280 
LEU H2     H N N 281 
LEU HA     H N N 282 
LEU HB2    H N N 283 
LEU HB3    H N N 284 
LEU HG     H N N 285 
LEU HD11   H N N 286 
LEU HD12   H N N 287 
LEU HD13   H N N 288 
LEU HD21   H N N 289 
LEU HD22   H N N 290 
LEU HD23   H N N 291 
LEU HXT    H N N 292 
LYS N      N N N 293 
LYS CA     C N S 294 
LYS C      C N N 295 
LYS O      O N N 296 
LYS CB     C N N 297 
LYS CG     C N N 298 
LYS CD     C N N 299 
LYS CE     C N N 300 
LYS NZ     N N N 301 
LYS OXT    O N N 302 
LYS H      H N N 303 
LYS H2     H N N 304 
LYS HA     H N N 305 
LYS HB2    H N N 306 
LYS HB3    H N N 307 
LYS HG2    H N N 308 
LYS HG3    H N N 309 
LYS HD2    H N N 310 
LYS HD3    H N N 311 
LYS HE2    H N N 312 
LYS HE3    H N N 313 
LYS HZ1    H N N 314 
LYS HZ2    H N N 315 
LYS HZ3    H N N 316 
LYS HXT    H N N 317 
MET N      N N N 318 
MET CA     C N S 319 
MET C      C N N 320 
MET O      O N N 321 
MET CB     C N N 322 
MET CG     C N N 323 
MET SD     S N N 324 
MET CE     C N N 325 
MET OXT    O N N 326 
MET H      H N N 327 
MET H2     H N N 328 
MET HA     H N N 329 
MET HB2    H N N 330 
MET HB3    H N N 331 
MET HG2    H N N 332 
MET HG3    H N N 333 
MET HE1    H N N 334 
MET HE2    H N N 335 
MET HE3    H N N 336 
MET HXT    H N N 337 
PHE N      N N N 338 
PHE CA     C N S 339 
PHE C      C N N 340 
PHE O      O N N 341 
PHE CB     C N N 342 
PHE CG     C Y N 343 
PHE CD1    C Y N 344 
PHE CD2    C Y N 345 
PHE CE1    C Y N 346 
PHE CE2    C Y N 347 
PHE CZ     C Y N 348 
PHE OXT    O N N 349 
PHE H      H N N 350 
PHE H2     H N N 351 
PHE HA     H N N 352 
PHE HB2    H N N 353 
PHE HB3    H N N 354 
PHE HD1    H N N 355 
PHE HD2    H N N 356 
PHE HE1    H N N 357 
PHE HE2    H N N 358 
PHE HZ     H N N 359 
PHE HXT    H N N 360 
PRO N      N N N 361 
PRO CA     C N S 362 
PRO C      C N N 363 
PRO O      O N N 364 
PRO CB     C N N 365 
PRO CG     C N N 366 
PRO CD     C N N 367 
PRO OXT    O N N 368 
PRO H      H N N 369 
PRO HA     H N N 370 
PRO HB2    H N N 371 
PRO HB3    H N N 372 
PRO HG2    H N N 373 
PRO HG3    H N N 374 
PRO HD2    H N N 375 
PRO HD3    H N N 376 
PRO HXT    H N N 377 
SER N      N N N 378 
SER CA     C N S 379 
SER C      C N N 380 
SER O      O N N 381 
SER CB     C N N 382 
SER OG     O N N 383 
SER OXT    O N N 384 
SER H      H N N 385 
SER H2     H N N 386 
SER HA     H N N 387 
SER HB2    H N N 388 
SER HB3    H N N 389 
SER HG     H N N 390 
SER HXT    H N N 391 
THR N      N N N 392 
THR CA     C N S 393 
THR C      C N N 394 
THR O      O N N 395 
THR CB     C N R 396 
THR OG1    O N N 397 
THR CG2    C N N 398 
THR OXT    O N N 399 
THR H      H N N 400 
THR H2     H N N 401 
THR HA     H N N 402 
THR HB     H N N 403 
THR HG1    H N N 404 
THR HG21   H N N 405 
THR HG22   H N N 406 
THR HG23   H N N 407 
THR HXT    H N N 408 
TRP N      N N N 409 
TRP CA     C N S 410 
TRP C      C N N 411 
TRP O      O N N 412 
TRP CB     C N N 413 
TRP CG     C Y N 414 
TRP CD1    C Y N 415 
TRP CD2    C Y N 416 
TRP NE1    N Y N 417 
TRP CE2    C Y N 418 
TRP CE3    C Y N 419 
TRP CZ2    C Y N 420 
TRP CZ3    C Y N 421 
TRP CH2    C Y N 422 
TRP OXT    O N N 423 
TRP H      H N N 424 
TRP H2     H N N 425 
TRP HA     H N N 426 
TRP HB2    H N N 427 
TRP HB3    H N N 428 
TRP HD1    H N N 429 
TRP HE1    H N N 430 
TRP HE3    H N N 431 
TRP HZ2    H N N 432 
TRP HZ3    H N N 433 
TRP HH2    H N N 434 
TRP HXT    H N N 435 
TYR N      N N N 436 
TYR CA     C N S 437 
TYR C      C N N 438 
TYR O      O N N 439 
TYR CB     C N N 440 
TYR CG     C Y N 441 
TYR CD1    C Y N 442 
TYR CD2    C Y N 443 
TYR CE1    C Y N 444 
TYR CE2    C Y N 445 
TYR CZ     C Y N 446 
TYR OH     O N N 447 
TYR OXT    O N N 448 
TYR H      H N N 449 
TYR H2     H N N 450 
TYR HA     H N N 451 
TYR HB2    H N N 452 
TYR HB3    H N N 453 
TYR HD1    H N N 454 
TYR HD2    H N N 455 
TYR HE1    H N N 456 
TYR HE2    H N N 457 
TYR HH     H N N 458 
TYR HXT    H N N 459 
VAL N      N N N 460 
VAL CA     C N S 461 
VAL C      C N N 462 
VAL O      O N N 463 
VAL CB     C N N 464 
VAL CG1    C N N 465 
VAL CG2    C N N 466 
VAL OXT    O N N 467 
VAL H      H N N 468 
VAL H2     H N N 469 
VAL HA     H N N 470 
VAL HB     H N N 471 
VAL HG11   H N N 472 
VAL HG12   H N N 473 
VAL HG13   H N N 474 
VAL HG21   H N N 475 
VAL HG22   H N N 476 
VAL HG23   H N N 477 
VAL HXT    H N N 478 
# 
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 
ILE N     CA     sing N N 245 
ILE N     H      sing N N 246 
ILE N     H2     sing N N 247 
ILE CA    C      sing N N 248 
ILE CA    CB     sing N N 249 
ILE CA    HA     sing N N 250 
ILE C     O      doub N N 251 
ILE C     OXT    sing N N 252 
ILE CB    CG1    sing N N 253 
ILE CB    CG2    sing N N 254 
ILE CB    HB     sing N N 255 
ILE CG1   CD1    sing N N 256 
ILE CG1   HG12   sing N N 257 
ILE CG1   HG13   sing N N 258 
ILE CG2   HG21   sing N N 259 
ILE CG2   HG22   sing N N 260 
ILE CG2   HG23   sing N N 261 
ILE CD1   HD11   sing N N 262 
ILE CD1   HD12   sing N N 263 
ILE CD1   HD13   sing N N 264 
ILE OXT   HXT    sing N N 265 
LEU N     CA     sing N N 266 
LEU N     H      sing N N 267 
LEU N     H2     sing N N 268 
LEU CA    C      sing N N 269 
LEU CA    CB     sing N N 270 
LEU CA    HA     sing N N 271 
LEU C     O      doub N N 272 
LEU C     OXT    sing N N 273 
LEU CB    CG     sing N N 274 
LEU CB    HB2    sing N N 275 
LEU CB    HB3    sing N N 276 
LEU CG    CD1    sing N N 277 
LEU CG    CD2    sing N N 278 
LEU CG    HG     sing N N 279 
LEU CD1   HD11   sing N N 280 
LEU CD1   HD12   sing N N 281 
LEU CD1   HD13   sing N N 282 
LEU CD2   HD21   sing N N 283 
LEU CD2   HD22   sing N N 284 
LEU CD2   HD23   sing N N 285 
LEU OXT   HXT    sing N N 286 
LYS N     CA     sing N N 287 
LYS N     H      sing N N 288 
LYS N     H2     sing N N 289 
LYS CA    C      sing N N 290 
LYS CA    CB     sing N N 291 
LYS CA    HA     sing N N 292 
LYS C     O      doub N N 293 
LYS C     OXT    sing N N 294 
LYS CB    CG     sing N N 295 
LYS CB    HB2    sing N N 296 
LYS CB    HB3    sing N N 297 
LYS CG    CD     sing N N 298 
LYS CG    HG2    sing N N 299 
LYS CG    HG3    sing N N 300 
LYS CD    CE     sing N N 301 
LYS CD    HD2    sing N N 302 
LYS CD    HD3    sing N N 303 
LYS CE    NZ     sing N N 304 
LYS CE    HE2    sing N N 305 
LYS CE    HE3    sing N N 306 
LYS NZ    HZ1    sing N N 307 
LYS NZ    HZ2    sing N N 308 
LYS NZ    HZ3    sing N N 309 
LYS OXT   HXT    sing N N 310 
MET N     CA     sing N N 311 
MET N     H      sing N N 312 
MET N     H2     sing N N 313 
MET CA    C      sing N N 314 
MET CA    CB     sing N N 315 
MET CA    HA     sing N N 316 
MET C     O      doub N N 317 
MET C     OXT    sing N N 318 
MET CB    CG     sing N N 319 
MET CB    HB2    sing N N 320 
MET CB    HB3    sing N N 321 
MET CG    SD     sing N N 322 
MET CG    HG2    sing N N 323 
MET CG    HG3    sing N N 324 
MET SD    CE     sing N N 325 
MET CE    HE1    sing N N 326 
MET CE    HE2    sing N N 327 
MET CE    HE3    sing N N 328 
MET OXT   HXT    sing N N 329 
PHE N     CA     sing N N 330 
PHE N     H      sing N N 331 
PHE N     H2     sing N N 332 
PHE CA    C      sing N N 333 
PHE CA    CB     sing N N 334 
PHE CA    HA     sing N N 335 
PHE C     O      doub N N 336 
PHE C     OXT    sing N N 337 
PHE CB    CG     sing N N 338 
PHE CB    HB2    sing N N 339 
PHE CB    HB3    sing N N 340 
PHE CG    CD1    doub Y N 341 
PHE CG    CD2    sing Y N 342 
PHE CD1   CE1    sing Y N 343 
PHE CD1   HD1    sing N N 344 
PHE CD2   CE2    doub Y N 345 
PHE CD2   HD2    sing N N 346 
PHE CE1   CZ     doub Y N 347 
PHE CE1   HE1    sing N N 348 
PHE CE2   CZ     sing Y N 349 
PHE CE2   HE2    sing N N 350 
PHE CZ    HZ     sing N N 351 
PHE OXT   HXT    sing N N 352 
PRO N     CA     sing N N 353 
PRO N     CD     sing N N 354 
PRO N     H      sing N N 355 
PRO CA    C      sing N N 356 
PRO CA    CB     sing N N 357 
PRO CA    HA     sing N N 358 
PRO C     O      doub N N 359 
PRO C     OXT    sing N N 360 
PRO CB    CG     sing N N 361 
PRO CB    HB2    sing N N 362 
PRO CB    HB3    sing N N 363 
PRO CG    CD     sing N N 364 
PRO CG    HG2    sing N N 365 
PRO CG    HG3    sing N N 366 
PRO CD    HD2    sing N N 367 
PRO CD    HD3    sing N N 368 
PRO OXT   HXT    sing N N 369 
SER N     CA     sing N N 370 
SER N     H      sing N N 371 
SER N     H2     sing N N 372 
SER CA    C      sing N N 373 
SER CA    CB     sing N N 374 
SER CA    HA     sing N N 375 
SER C     O      doub N N 376 
SER C     OXT    sing N N 377 
SER CB    OG     sing N N 378 
SER CB    HB2    sing N N 379 
SER CB    HB3    sing N N 380 
SER OG    HG     sing N N 381 
SER OXT   HXT    sing N N 382 
THR N     CA     sing N N 383 
THR N     H      sing N N 384 
THR N     H2     sing N N 385 
THR CA    C      sing N N 386 
THR CA    CB     sing N N 387 
THR CA    HA     sing N N 388 
THR C     O      doub N N 389 
THR C     OXT    sing N N 390 
THR CB    OG1    sing N N 391 
THR CB    CG2    sing N N 392 
THR CB    HB     sing N N 393 
THR OG1   HG1    sing N N 394 
THR CG2   HG21   sing N N 395 
THR CG2   HG22   sing N N 396 
THR CG2   HG23   sing N N 397 
THR OXT   HXT    sing N N 398 
TRP N     CA     sing N N 399 
TRP N     H      sing N N 400 
TRP N     H2     sing N N 401 
TRP CA    C      sing N N 402 
TRP CA    CB     sing N N 403 
TRP CA    HA     sing N N 404 
TRP C     O      doub N N 405 
TRP C     OXT    sing N N 406 
TRP CB    CG     sing N N 407 
TRP CB    HB2    sing N N 408 
TRP CB    HB3    sing N N 409 
TRP CG    CD1    doub Y N 410 
TRP CG    CD2    sing Y N 411 
TRP CD1   NE1    sing Y N 412 
TRP CD1   HD1    sing N N 413 
TRP CD2   CE2    doub Y N 414 
TRP CD2   CE3    sing Y N 415 
TRP NE1   CE2    sing Y N 416 
TRP NE1   HE1    sing N N 417 
TRP CE2   CZ2    sing Y N 418 
TRP CE3   CZ3    doub Y N 419 
TRP CE3   HE3    sing N N 420 
TRP CZ2   CH2    doub Y N 421 
TRP CZ2   HZ2    sing N N 422 
TRP CZ3   CH2    sing Y N 423 
TRP CZ3   HZ3    sing N N 424 
TRP CH2   HH2    sing N N 425 
TRP OXT   HXT    sing N N 426 
TYR N     CA     sing N N 427 
TYR N     H      sing N N 428 
TYR N     H2     sing N N 429 
TYR CA    C      sing N N 430 
TYR CA    CB     sing N N 431 
TYR CA    HA     sing N N 432 
TYR C     O      doub N N 433 
TYR C     OXT    sing N N 434 
TYR CB    CG     sing N N 435 
TYR CB    HB2    sing N N 436 
TYR CB    HB3    sing N N 437 
TYR CG    CD1    doub Y N 438 
TYR CG    CD2    sing Y N 439 
TYR CD1   CE1    sing Y N 440 
TYR CD1   HD1    sing N N 441 
TYR CD2   CE2    doub Y N 442 
TYR CD2   HD2    sing N N 443 
TYR CE1   CZ     doub Y N 444 
TYR CE1   HE1    sing N N 445 
TYR CE2   CZ     sing Y N 446 
TYR CE2   HE2    sing N N 447 
TYR CZ    OH     sing N N 448 
TYR OH    HH     sing N N 449 
TYR OXT   HXT    sing N N 450 
VAL N     CA     sing N N 451 
VAL N     H      sing N N 452 
VAL N     H2     sing N N 453 
VAL CA    C      sing N N 454 
VAL CA    CB     sing N N 455 
VAL CA    HA     sing N N 456 
VAL C     O      doub N N 457 
VAL C     OXT    sing N N 458 
VAL CB    CG1    sing N N 459 
VAL CB    CG2    sing N N 460 
VAL CB    HB     sing N N 461 
VAL CG1   HG11   sing N N 462 
VAL CG1   HG12   sing N N 463 
VAL CG1   HG13   sing N N 464 
VAL CG2   HG21   sing N N 465 
VAL CG2   HG22   sing N N 466 
VAL CG2   HG23   sing N N 467 
VAL OXT   HXT    sing N N 468 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9F6U 
_em_admin.last_update        2025-05-14 
_em_admin.map_release_date   2025-04-02 
_em_admin.title              'cryoEM structure of Asgard tubulin heterodimer AtubA/B with GDP' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          2951803 
_em_entity_assembly_naturalsource.organism             'Candidatus Lokiarchaeum ossiferum' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'European Research Council (ERC)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           101000232 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9F6U 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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     . ALA A 1 2   ? 113.100 97.216  117.221 1.00 50.61  ? 2   ALA A N     1 
ATOM   2    C CA    . ALA A 1 2   ? 112.508 98.524  117.373 1.00 50.61  ? 2   ALA A CA    1 
ATOM   3    C C     . ALA A 1 2   ? 111.136 98.512  116.709 1.00 50.61  ? 2   ALA A C     1 
ATOM   4    O O     . ALA A 1 2   ? 110.885 97.629  115.891 1.00 50.61  ? 2   ALA A O     1 
ATOM   5    C CB    . ALA A 1 2   ? 113.418 99.572  116.773 1.00 69.01  ? 2   ALA A CB    1 
ATOM   6    N N     . GLY A 1 3   ? 110.252 99.457  117.052 1.00 49.70  ? 3   GLY A N     1 
ATOM   7    C CA    . GLY A 1 3   ? 108.885 99.512  116.530 1.00 49.70  ? 3   GLY A CA    1 
ATOM   8    C C     . GLY A 1 3   ? 108.013 98.419  117.119 1.00 49.70  ? 3   GLY A C     1 
ATOM   9    O O     . GLY A 1 3   ? 107.110 97.892  116.455 1.00 49.70  ? 3   GLY A O     1 
ATOM   10   N N     . GLU A 1 4   ? 108.309 98.035  118.349 1.00 52.31  ? 4   GLU A N     1 
ATOM   11   C CA    . GLU A 1 4   ? 107.700 96.929  119.057 1.00 52.31  ? 4   GLU A CA    1 
ATOM   12   C C     . GLU A 1 4   ? 106.455 97.387  119.808 1.00 52.31  ? 4   GLU A C     1 
ATOM   13   O O     . GLU A 1 4   ? 106.277 98.568  120.078 1.00 52.31  ? 4   GLU A O     1 
ATOM   14   C CB    . GLU A 1 4   ? 108.774 96.352  119.942 1.00 70.27  ? 4   GLU A CB    1 
ATOM   15   C CG    . GLU A 1 4   ? 109.945 95.735  119.109 1.00 70.27  ? 4   GLU A CG    1 
ATOM   16   C CD    . GLU A 1 4   ? 111.244 95.507  119.891 1.00 70.27  ? 4   GLU A CD    1 
ATOM   17   O OE1   . GLU A 1 4   ? 111.666 96.420  120.601 1.00 70.27  ? 4   GLU A OE1   1 
ATOM   18   O OE2   . GLU A 1 4   ? 111.861 94.442  119.774 1.00 70.27  ? 4   GLU A OE2   1 
ATOM   19   N N     . ILE A 1 5   ? 105.543 96.464  120.095 1.00 47.95  ? 5   ILE A N     1 
ATOM   20   C CA    . ILE A 1 5   ? 104.265 96.843  120.708 1.00 47.95  ? 5   ILE A CA    1 
ATOM   21   C C     . ILE A 1 5   ? 104.030 96.200  122.066 1.00 47.95  ? 5   ILE A C     1 
ATOM   22   O O     . ILE A 1 5   ? 104.142 94.983  122.220 1.00 47.95  ? 5   ILE A O     1 
ATOM   23   C CB    . ILE A 1 5   ? 103.094 96.525  119.783 1.00 70.99  ? 5   ILE A CB    1 
ATOM   24   C CG1   . ILE A 1 5   ? 103.224 97.414  118.545 1.00 70.99  ? 5   ILE A CG1   1 
ATOM   25   C CG2   . ILE A 1 5   ? 101.798 96.765  120.513 1.00 70.99  ? 5   ILE A CG2   1 
ATOM   26   C CD1   . ILE A 1 5   ? 102.289 97.073  117.411 1.00 70.99  ? 5   ILE A CD1   1 
ATOM   27   N N     . VAL A 1 6   ? 103.665 97.010  123.047 1.00 45.90  ? 6   VAL A N     1 
ATOM   28   C CA    . VAL A 1 6   ? 103.357 96.491  124.364 1.00 45.90  ? 6   VAL A CA    1 
ATOM   29   C C     . VAL A 1 6   ? 101.865 96.471  124.502 1.00 45.90  ? 6   VAL A C     1 
ATOM   30   O O     . VAL A 1 6   ? 101.192 97.483  124.323 1.00 45.90  ? 6   VAL A O     1 
ATOM   31   C CB    . VAL A 1 6   ? 104.006 97.316  125.473 1.00 66.76  ? 6   VAL A CB    1 
ATOM   32   C CG1   . VAL A 1 6   ? 103.599 96.770  126.823 1.00 66.76  ? 6   VAL A CG1   1 
ATOM   33   C CG2   . VAL A 1 6   ? 105.515 97.273  125.339 1.00 66.76  ? 6   VAL A CG2   1 
ATOM   34   N N     . CYS A 1 7   ? 101.337 95.333  124.800 1.00 49.28  ? 7   CYS A N     1 
ATOM   35   C CA    . CYS A 1 7   ? 99.912  95.197  124.898 1.00 49.28  ? 7   CYS A CA    1 
ATOM   36   C C     . CYS A 1 7   ? 99.498  95.127  126.349 1.00 49.28  ? 7   CYS A C     1 
ATOM   37   O O     . CYS A 1 7   ? 100.078 94.372  127.129 1.00 49.28  ? 7   CYS A O     1 
ATOM   38   C CB    . CYS A 1 7   ? 99.466  93.949  124.158 1.00 66.38  ? 7   CYS A CB    1 
ATOM   39   S SG    . CYS A 1 7   ? 99.857  94.010  122.398 1.00 66.38  ? 7   CYS A SG    1 
ATOM   40   N N     . ILE A 1 8   ? 98.486  95.891  126.716 1.00 47.24  ? 8   ILE A N     1 
ATOM   41   C CA    . ILE A 1 8   ? 98.031  95.902  128.082 1.00 47.24  ? 8   ILE A CA    1 
ATOM   42   C C     . ILE A 1 8   ? 96.599  95.408  128.120 1.00 47.24  ? 8   ILE A C     1 
ATOM   43   O O     . ILE A 1 8   ? 95.707  95.977  127.486 1.00 47.24  ? 8   ILE A O     1 
ATOM   44   C CB    . ILE A 1 8   ? 98.205  97.288  128.685 1.00 69.94  ? 8   ILE A CB    1 
ATOM   45   C CG1   . ILE A 1 8   ? 99.681  97.665  128.562 1.00 69.94  ? 8   ILE A CG1   1 
ATOM   46   C CG2   . ILE A 1 8   ? 97.763  97.286  130.138 1.00 69.94  ? 8   ILE A CG2   1 
ATOM   47   C CD1   . ILE A 1 8   ? 100.001 99.081  128.843 1.00 69.94  ? 8   ILE A CD1   1 
ATOM   48   N N     . GLN A 1 9   ? 96.400  94.363  128.870 1.00 49.13  ? 9   GLN A N     1 
ATOM   49   C CA    . GLN A 1 9   ? 95.161  93.624  128.975 1.00 49.13  ? 9   GLN A CA    1 
ATOM   50   C C     . GLN A 1 9   ? 94.460  93.905  130.312 1.00 49.13  ? 9   GLN A C     1 
ATOM   51   O O     . GLN A 1 9   ? 94.992  93.560  131.369 1.00 49.13  ? 9   GLN A O     1 
ATOM   52   C CB    . GLN A 1 9   ? 95.585  92.182  128.847 1.00 68.65  ? 9   GLN A CB    1 
ATOM   53   C CG    . GLN A 1 9   ? 94.610  91.154  128.920 1.00 68.65  ? 9   GLN A CG    1 
ATOM   54   C CD    . GLN A 1 9   ? 95.338  89.882  128.721 1.00 68.65  ? 9   GLN A CD    1 
ATOM   55   O OE1   . GLN A 1 9   ? 96.226  89.798  127.876 1.00 68.65  ? 9   GLN A OE1   1 
ATOM   56   N NE2   . GLN A 1 9   ? 95.019  88.891  129.502 1.00 68.65  ? 9   GLN A NE2   1 
ATOM   57   N N     . VAL A 1 10  ? 93.273  94.524  130.301 1.00 48.77  ? 10  VAL A N     1 
ATOM   58   C CA    . VAL A 1 10  ? 92.676  94.947  131.564 1.00 48.77  ? 10  VAL A CA    1 
ATOM   59   C C     . VAL A 1 10  ? 91.260  94.419  131.770 1.00 48.77  ? 10  VAL A C     1 
ATOM   60   O O     . VAL A 1 10  ? 90.360  94.680  130.963 1.00 48.77  ? 10  VAL A O     1 
ATOM   61   C CB    . VAL A 1 10  ? 92.676  96.477  131.674 1.00 70.94  ? 10  VAL A CB    1 
ATOM   62   C CG1   . VAL A 1 10  ? 92.093  96.918  133.025 1.00 70.94  ? 10  VAL A CG1   1 
ATOM   63   C CG2   . VAL A 1 10  ? 94.082  97.019  131.455 1.00 70.94  ? 10  VAL A CG2   1 
ATOM   64   N N     . GLY A 1 11  ? 91.050  93.750  132.903 1.00 53.96  ? 11  GLY A N     1 
ATOM   65   C CA    . GLY A 1 11  ? 89.737  93.275  133.297 1.00 53.96  ? 11  GLY A CA    1 
ATOM   66   C C     . GLY A 1 11  ? 89.407  91.949  132.650 1.00 53.96  ? 11  GLY A C     1 
ATOM   67   O O     . GLY A 1 11  ? 90.124  91.466  131.780 1.00 53.96  ? 11  GLY A O     1 
ATOM   68   N N     . GLN A 1 12  ? 88.290  91.351  133.076 1.00 55.07  ? 12  GLN A N     1 
ATOM   69   C CA    . GLN A 1 12  ? 87.949  90.041  132.558 1.00 55.07  ? 12  GLN A CA    1 
ATOM   70   C C     . GLN A 1 12  ? 87.653  90.078  131.085 1.00 55.07  ? 12  GLN A C     1 
ATOM   71   O O     . GLN A 1 12  ? 88.102  89.193  130.355 1.00 55.07  ? 12  GLN A O     1 
ATOM   72   C CB    . GLN A 1 12  ? 86.782  89.413  133.278 1.00 76.95  ? 12  GLN A CB    1 
ATOM   73   C CG    . GLN A 1 12  ? 86.463  88.048  132.722 1.00 76.95  ? 12  GLN A CG    1 
ATOM   74   C CD    . GLN A 1 12  ? 85.486  87.307  133.556 1.00 76.95  ? 12  GLN A CD    1 
ATOM   75   O OE1   . GLN A 1 12  ? 85.738  87.029  134.729 1.00 76.95  ? 12  GLN A OE1   1 
ATOM   76   N NE2   . GLN A 1 12  ? 84.349  86.975  132.968 1.00 76.95  ? 12  GLN A NE2   1 
ATOM   77   N N     . ALA A 1 13  ? 86.923  91.063  130.604 1.00 57.08  ? 13  ALA A N     1 
ATOM   78   C CA    . ALA A 1 13  ? 86.681  91.048  129.170 1.00 57.08  ? 13  ALA A CA    1 
ATOM   79   C C     . ALA A 1 13  ? 88.000  91.052  128.415 1.00 57.08  ? 13  ALA A C     1 
ATOM   80   O O     . ALA A 1 13  ? 88.151  90.389  127.375 1.00 57.08  ? 13  ALA A O     1 
ATOM   81   C CB    . ALA A 1 13  ? 85.857  92.247  128.734 1.00 77.84  ? 13  ALA A CB    1 
ATOM   82   N N     . GLY A 1 14  ? 88.963  91.810  128.937 1.00 56.72  ? 14  GLY A N     1 
ATOM   83   C CA    . GLY A 1 14  ? 90.268  91.887  128.314 1.00 56.72  ? 14  GLY A CA    1 
ATOM   84   C C     . GLY A 1 14  ? 90.934  90.531  128.305 1.00 56.72  ? 14  GLY A C     1 
ATOM   85   O O     . GLY A 1 14  ? 91.447  90.081  127.283 1.00 56.72  ? 14  GLY A O     1 
ATOM   86   N N     . ASN A 1 15  ? 90.883  89.849  129.429 1.00 54.86  ? 15  ASN A N     1 
ATOM   87   C CA    . ASN A 1 15  ? 91.519  88.565  129.507 1.00 54.86  ? 15  ASN A CA    1 
ATOM   88   C C     . ASN A 1 15  ? 90.897  87.600  128.551 1.00 54.86  ? 15  ASN A C     1 
ATOM   89   O O     . ASN A 1 15  ? 91.589  86.815  127.917 1.00 54.86  ? 15  ASN A O     1 
ATOM   90   C CB    . ASN A 1 15  ? 91.391  88.005  130.897 1.00 74.33  ? 15  ASN A CB    1 
ATOM   91   C CG    . ASN A 1 15  ? 92.255  88.698  131.890 1.00 74.33  ? 15  ASN A CG    1 
ATOM   92   O OD1   . ASN A 1 15  ? 93.230  89.369  131.554 1.00 74.33  ? 15  ASN A OD1   1 
ATOM   93   N ND2   . ASN A 1 15  ? 91.915  88.520  133.146 1.00 74.33  ? 15  ASN A ND2   1 
ATOM   94   N N     . GLN A 1 16  ? 89.603  87.634  128.407 1.00 53.82  ? 16  GLN A N     1 
ATOM   95   C CA    . GLN A 1 16  ? 89.004  86.625  127.558 1.00 53.82  ? 16  GLN A CA    1 
ATOM   96   C C     . GLN A 1 16  ? 89.307  86.870  126.088 1.00 53.82  ? 16  GLN A C     1 
ATOM   97   O O     . GLN A 1 16  ? 89.606  85.913  125.335 1.00 53.82  ? 16  GLN A O     1 
ATOM   98   C CB    . GLN A 1 16  ? 87.521  86.560  127.817 1.00 75.20  ? 16  GLN A CB    1 
ATOM   99   C CG    . GLN A 1 16  ? 87.214  86.082  129.223 1.00 75.20  ? 16  GLN A CG    1 
ATOM   100  C CD    . GLN A 1 16  ? 87.804  84.728  129.502 1.00 75.20  ? 16  GLN A CD    1 
ATOM   101  O OE1   . GLN A 1 16  ? 87.679  83.815  128.689 1.00 75.20  ? 16  GLN A OE1   1 
ATOM   102  N NE2   . GLN A 1 16  ? 88.450  84.583  130.642 1.00 75.20  ? 16  GLN A NE2   1 
ATOM   103  N N     . ILE A 1 17  ? 89.326  88.136  125.662 1.00 55.01  ? 17  ILE A N     1 
ATOM   104  C CA    . ILE A 1 17  ? 89.665  88.376  124.263 1.00 55.01  ? 17  ILE A CA    1 
ATOM   105  C C     . ILE A 1 17  ? 91.115  88.054  124.021 1.00 55.01  ? 17  ILE A C     1 
ATOM   106  O O     . ILE A 1 17  ? 91.468  87.439  123.012 1.00 55.01  ? 17  ILE A O     1 
ATOM   107  C CB    . ILE A 1 17  ? 89.410  89.813  123.811 1.00 81.44  ? 17  ILE A CB    1 
ATOM   108  C CG1   . ILE A 1 17  ? 87.965  90.209  124.003 1.00 81.44  ? 17  ILE A CG1   1 
ATOM   109  C CG2   . ILE A 1 17  ? 89.844  89.975  122.349 1.00 81.44  ? 17  ILE A CG2   1 
ATOM   110  C CD1   . ILE A 1 17  ? 86.972  89.357  123.323 1.00 81.44  ? 17  ILE A CD1   1 
ATOM   111  N N     . ALA A 1 18  ? 91.973  88.499  124.925 1.00 55.01  ? 18  ALA A N     1 
ATOM   112  C CA    . ALA A 1 18  ? 93.389  88.294  124.763 1.00 55.01  ? 18  ALA A CA    1 
ATOM   113  C C     . ALA A 1 18  ? 93.716  86.827  124.710 1.00 55.01  ? 18  ALA A C     1 
ATOM   114  O O     . ALA A 1 18  ? 94.584  86.408  123.950 1.00 55.01  ? 18  ALA A O     1 
ATOM   115  C CB    . ALA A 1 18  ? 94.125  88.950  125.903 1.00 75.01  ? 18  ALA A CB    1 
ATOM   116  N N     . GLY A 1 19  ? 93.035  86.022  125.487 1.00 52.64  ? 19  GLY A N     1 
ATOM   117  C CA    . GLY A 1 19  ? 93.326  84.621  125.405 1.00 52.64  ? 19  GLY A CA    1 
ATOM   118  C C     . GLY A 1 19  ? 93.161  84.126  124.019 1.00 52.64  ? 19  GLY A C     1 
ATOM   119  O O     . GLY A 1 19  ? 94.080  83.532  123.447 1.00 52.64  ? 19  GLY A O     1 
ATOM   120  N N     . ALA A 1 20  ? 91.994  84.397  123.447 1.00 53.27  ? 20  ALA A N     1 
ATOM   121  C CA    . ALA A 1 20  ? 91.768  83.918  122.094 1.00 53.27  ? 20  ALA A CA    1 
ATOM   122  C C     . ALA A 1 20  ? 92.773  84.526  121.128 1.00 53.27  ? 20  ALA A C     1 
ATOM   123  O O     . ALA A 1 20  ? 93.257  83.853  120.200 1.00 53.27  ? 20  ALA A O     1 
ATOM   124  C CB    . ALA A 1 20  ? 90.351  84.233  121.664 1.00 72.64  ? 20  ALA A CB    1 
ATOM   125  N N     . PHE A 1 21  ? 93.120  85.790  121.352 1.00 55.08  ? 21  PHE A N     1 
ATOM   126  C CA    . PHE A 1 21  ? 94.013  86.489  120.454 1.00 55.08  ? 21  PHE A CA    1 
ATOM   127  C C     . PHE A 1 21  ? 95.370  85.874  120.432 1.00 55.08  ? 21  PHE A C     1 
ATOM   128  O O     . PHE A 1 21  ? 95.894  85.555  119.366 1.00 55.08  ? 21  PHE A O     1 
ATOM   129  C CB    . PHE A 1 21  ? 94.148  87.904  120.892 1.00 76.86  ? 21  PHE A CB    1 
ATOM   130  C CG    . PHE A 1 21  ? 95.168  88.665  120.160 1.00 76.86  ? 21  PHE A CG    1 
ATOM   131  C CD1   . PHE A 1 21  ? 94.921  89.184  118.922 1.00 76.86  ? 21  PHE A CD1   1 
ATOM   132  C CD2   . PHE A 1 21  ? 96.362  88.918  120.747 1.00 76.86  ? 21  PHE A CD2   1 
ATOM   133  C CE1   . PHE A 1 21  ? 95.857  89.920  118.293 1.00 76.86  ? 21  PHE A CE1   1 
ATOM   134  C CE2   . PHE A 1 21  ? 97.298  89.653  120.122 1.00 76.86  ? 21  PHE A CE2   1 
ATOM   135  C CZ    . PHE A 1 21  ? 97.051  90.157  118.896 1.00 76.86  ? 21  PHE A CZ    1 
ATOM   136  N N     . TRP A 1 22  ? 95.965  85.711  121.591 1.00 53.09  ? 22  TRP A N     1 
ATOM   137  C CA    . TRP A 1 22  ? 97.331  85.231  121.617 1.00 53.09  ? 22  TRP A CA    1 
ATOM   138  C C     . TRP A 1 22  ? 97.421  83.783  121.181 1.00 53.09  ? 22  TRP A C     1 
ATOM   139  O O     . TRP A 1 22  ? 98.423  83.391  120.581 1.00 53.09  ? 22  TRP A O     1 
ATOM   140  C CB    . TRP A 1 22  ? 97.944  85.425  122.984 1.00 73.51  ? 22  TRP A CB    1 
ATOM   141  C CG    . TRP A 1 22  ? 98.253  86.829  123.256 1.00 73.51  ? 22  TRP A CG    1 
ATOM   142  C CD1   . TRP A 1 22  ? 97.601  87.641  124.100 1.00 73.51  ? 22  TRP A CD1   1 
ATOM   143  C CD2   . TRP A 1 22  ? 99.282  87.610  122.669 1.00 73.51  ? 22  TRP A CD2   1 
ATOM   144  N NE1   . TRP A 1 22  ? 98.158  88.882  124.094 1.00 73.51  ? 22  TRP A NE1   1 
ATOM   145  C CE2   . TRP A 1 22  ? 99.197  88.884  123.217 1.00 73.51  ? 22  TRP A CE2   1 
ATOM   146  C CE3   . TRP A 1 22  ? 100.272 87.353  121.733 1.00 73.51  ? 22  TRP A CE3   1 
ATOM   147  C CZ2   . TRP A 1 22  ? 100.049 89.897  122.872 1.00 73.51  ? 22  TRP A CZ2   1 
ATOM   148  C CZ3   . TRP A 1 22  ? 101.130 88.373  121.387 1.00 73.51  ? 22  TRP A CZ3   1 
ATOM   149  C CH2   . TRP A 1 22  ? 101.011 89.624  121.953 1.00 73.51  ? 22  TRP A CH2   1 
ATOM   150  N N     . GLN A 1 23  ? 96.386  82.986  121.415 1.00 53.82  ? 23  GLN A N     1 
ATOM   151  C CA    . GLN A 1 23  ? 96.450  81.642  120.881 1.00 53.82  ? 23  GLN A CA    1 
ATOM   152  C C     . GLN A 1 23  ? 96.489  81.676  119.364 1.00 53.82  ? 23  GLN A C     1 
ATOM   153  O O     . GLN A 1 23  ? 97.308  80.984  118.730 1.00 53.82  ? 23  GLN A O     1 
ATOM   154  C CB    . GLN A 1 23  ? 95.251  80.836  121.339 1.00 75.20  ? 23  GLN A CB    1 
ATOM   155  C CG    . GLN A 1 23  ? 95.181  80.549  122.788 1.00 75.20  ? 23  GLN A CG    1 
ATOM   156  C CD    . GLN A 1 23  ? 93.861  79.924  123.132 1.00 75.20  ? 23  GLN A CD    1 
ATOM   157  O OE1   . GLN A 1 23  ? 92.926  79.963  122.337 1.00 75.20  ? 23  GLN A OE1   1 
ATOM   158  N NE2   . GLN A 1 23  ? 93.769  79.340  124.317 1.00 75.20  ? 23  GLN A NE2   1 
ATOM   159  N N     . LYS A 1 24  ? 95.643  82.515  118.765 1.00 56.27  ? 24  LYS A N     1 
ATOM   160  C CA    . LYS A 1 24  ? 95.596  82.560  117.319 1.00 56.27  ? 24  LYS A CA    1 
ATOM   161  C C     . LYS A 1 24  ? 96.859  83.138  116.739 1.00 56.27  ? 24  LYS A C     1 
ATOM   162  O O     . LYS A 1 24  ? 97.381  82.630  115.742 1.00 56.27  ? 24  LYS A O     1 
ATOM   163  C CB    . LYS A 1 24  ? 94.411  83.356  116.859 1.00 84.40  ? 24  LYS A CB    1 
ATOM   164  C CG    . LYS A 1 24  ? 93.091  82.676  117.036 1.00 84.40  ? 24  LYS A CG    1 
ATOM   165  C CD    . LYS A 1 24  ? 91.964  83.582  116.548 1.00 84.40  ? 24  LYS A CD    1 
ATOM   166  C CE    . LYS A 1 24  ? 90.582  82.960  116.738 1.00 84.40  ? 24  LYS A CE    1 
ATOM   167  N NZ    . LYS A 1 24  ? 90.382  81.758  115.870 1.00 84.40  ? 24  LYS A NZ    1 
ATOM   168  N N     . ILE A 1 25  ? 97.382  84.176  117.348 1.00 55.79  ? 25  ILE A N     1 
ATOM   169  C CA    . ILE A 1 25  ? 98.583  84.760  116.809 1.00 55.79  ? 25  ILE A CA    1 
ATOM   170  C C     . ILE A 1 25  ? 99.731  83.787  116.891 1.00 55.79  ? 25  ILE A C     1 
ATOM   171  O O     . ILE A 1 25  ? 100.553 83.707  115.964 1.00 55.79  ? 25  ILE A O     1 
ATOM   172  C CB    . ILE A 1 25  ? 98.942  86.057  117.518 1.00 82.60  ? 25  ILE A CB    1 
ATOM   173  C CG1   . ILE A 1 25  ? 97.912  87.138  117.241 1.00 82.60  ? 25  ILE A CG1   1 
ATOM   174  C CG2   . ILE A 1 25  ? 100.337 86.478  117.168 1.00 82.60  ? 25  ILE A CG2   1 
ATOM   175  C CD1   . ILE A 1 25  ? 97.665  87.488  115.796 1.00 82.60  ? 25  ILE A CD1   1 
ATOM   176  N N     . CYS A 1 26  ? 99.863  83.081  118.006 1.00 57.33  ? 26  CYS A N     1 
ATOM   177  C CA    . CYS A 1 26  ? 100.971 82.160  118.090 1.00 57.33  ? 26  CYS A CA    1 
ATOM   178  C C     . CYS A 1 26  ? 100.871 81.154  116.968 1.00 57.33  ? 26  CYS A C     1 
ATOM   179  O O     . CYS A 1 26  ? 101.838 80.912  116.236 1.00 57.33  ? 26  CYS A O     1 
ATOM   180  C CB    . CYS A 1 26  ? 100.967 81.474  119.444 1.00 77.22  ? 26  CYS A CB    1 
ATOM   181  S SG    . CYS A 1 26  ? 101.368 82.544  120.789 1.00 77.22  ? 26  CYS A SG    1 
ATOM   182  N N     . ALA A 1 27  ? 99.678  80.641  116.750 1.00 58.89  ? 27  ALA A N     1 
ATOM   183  C CA    . ALA A 1 27  ? 99.532  79.641  115.722 1.00 58.89  ? 27  ALA A CA    1 
ATOM   184  C C     . ALA A 1 27  ? 99.956  80.168  114.376 1.00 58.89  ? 27  ALA A C     1 
ATOM   185  O O     . ALA A 1 27  ? 100.573 79.442  113.596 1.00 58.89  ? 27  ALA A O     1 
ATOM   186  C CB    . ALA A 1 27  ? 98.091  79.182  115.676 1.00 80.30  ? 27  ALA A CB    1 
ATOM   187  N N     . GLU A 1 28  ? 99.641  81.430  114.086 1.00 62.82  ? 28  GLU A N     1 
ATOM   188  C CA    . GLU A 1 28  ? 100.006 82.015  112.791 1.00 62.82  ? 28  GLU A CA    1 
ATOM   189  C C     . GLU A 1 28  ? 101.513 82.145  112.638 1.00 62.82  ? 28  GLU A C     1 
ATOM   190  O O     . GLU A 1 28  ? 102.040 81.934  111.544 1.00 62.82  ? 28  GLU A O     1 
ATOM   191  C CB    . GLU A 1 28  ? 99.355  83.393  112.603 1.00 84.38  ? 28  GLU A CB    1 
ATOM   192  C CG    . GLU A 1 28  ? 97.817  83.434  112.465 1.00 84.38  ? 28  GLU A CG    1 
ATOM   193  C CD    . GLU A 1 28  ? 97.284  82.785  111.207 1.00 84.38  ? 28  GLU A CD    1 
ATOM   194  O OE1   . GLU A 1 28  ? 98.082  82.434  110.346 1.00 84.38  ? 28  GLU A OE1   1 
ATOM   195  O OE2   . GLU A 1 28  ? 96.059  82.641  111.077 1.00 84.38  ? 28  GLU A OE2   1 
ATOM   196  N N     . HIS A 1 29  ? 102.216 82.512  113.706 1.00 58.20  ? 29  HIS A N     1 
ATOM   197  C CA    . HIS A 1 29  ? 103.659 82.621  113.602 1.00 58.20  ? 29  HIS A CA    1 
ATOM   198  C C     . HIS A 1 29  ? 104.334 81.259  113.636 1.00 58.20  ? 29  HIS A C     1 
ATOM   199  O O     . HIS A 1 29  ? 105.429 81.101  113.075 1.00 58.20  ? 29  HIS A O     1 
ATOM   200  C CB    . HIS A 1 29  ? 104.258 83.462  114.716 1.00 79.15  ? 29  HIS A CB    1 
ATOM   201  C CG    . HIS A 1 29  ? 104.169 84.936  114.525 1.00 79.15  ? 29  HIS A CG    1 
ATOM   202  N ND1   . HIS A 1 29  ? 104.804 85.617  113.514 1.00 79.15  ? 29  HIS A ND1   1 
ATOM   203  C CD2   . HIS A 1 29  ? 103.581 85.872  115.289 1.00 79.15  ? 29  HIS A CD2   1 
ATOM   204  C CE1   . HIS A 1 29  ? 104.589 86.907  113.645 1.00 79.15  ? 29  HIS A CE1   1 
ATOM   205  N NE2   . HIS A 1 29  ? 103.852 87.090  114.721 1.00 79.15  ? 29  HIS A NE2   1 
ATOM   206  N N     . GLY A 1 30  ? 103.703 80.269  114.247 1.00 59.54  ? 30  GLY A N     1 
ATOM   207  C CA    . GLY A 1 30  ? 104.301 78.964  114.392 1.00 59.54  ? 30  GLY A CA    1 
ATOM   208  C C     . GLY A 1 30  ? 104.760 78.705  115.787 1.00 59.54  ? 30  GLY A C     1 
ATOM   209  O O     . GLY A 1 30  ? 105.574 77.793  116.010 1.00 59.54  ? 30  GLY A O     1 
ATOM   210  N N     . ILE A 1 31  ? 104.287 79.480  116.735 1.00 61.50  ? 31  ILE A N     1 
ATOM   211  C CA    . ILE A 1 31  ? 104.687 79.338  118.123 1.00 61.50  ? 31  ILE A CA    1 
ATOM   212  C C     . ILE A 1 31  ? 103.614 78.586  118.881 1.00 61.50  ? 31  ILE A C     1 
ATOM   213  O O     . ILE A 1 31  ? 102.431 78.920  118.789 1.00 61.50  ? 31  ILE A O     1 
ATOM   214  C CB    . ILE A 1 31  ? 104.938 80.702  118.782 1.00 91.05  ? 31  ILE A CB    1 
ATOM   215  C CG1   . ILE A 1 31  ? 105.916 81.531  117.952 1.00 91.05  ? 31  ILE A CG1   1 
ATOM   216  C CG2   . ILE A 1 31  ? 105.455 80.509  120.203 1.00 91.05  ? 31  ILE A CG2   1 
ATOM   217  C CD1   . ILE A 1 31  ? 106.163 82.910  118.513 1.00 91.05  ? 31  ILE A CD1   1 
ATOM   218  N N     . ASP A 1 32  ? 104.026 77.617  119.667 1.00 64.38  ? 32  ASP A N     1 
ATOM   219  C CA    . ASP A 1 32  ? 103.072 76.813  120.400 1.00 64.38  ? 32  ASP A CA    1 
ATOM   220  C C     . ASP A 1 32  ? 102.421 77.620  121.507 1.00 64.38  ? 32  ASP A C     1 
ATOM   221  O O     . ASP A 1 32  ? 103.098 78.024  122.462 1.00 64.38  ? 32  ASP A O     1 
ATOM   222  C CB    . ASP A 1 32  ? 103.747 75.576  120.973 1.00 82.77  ? 32  ASP A CB    1 
ATOM   223  C CG    . ASP A 1 32  ? 104.407 74.724  119.906 1.00 82.77  ? 32  ASP A CG    1 
ATOM   224  O OD1   . ASP A 1 32  ? 104.699 75.254  118.814 1.00 82.77  ? 32  ASP A OD1   1 
ATOM   225  O OD2   . ASP A 1 32  ? 104.637 73.523  120.162 1.00 82.77  ? 32  ASP A OD2   1 
ATOM   226  N N     . PRO A 1 33  ? 101.114 77.825  121.436 1.00 61.61  ? 33  PRO A N     1 
ATOM   227  C CA    . PRO A 1 33  ? 100.432 78.584  122.473 1.00 61.61  ? 33  PRO A CA    1 
ATOM   228  C C     . PRO A 1 33  ? 100.565 77.886  123.803 1.00 61.61  ? 33  PRO A C     1 
ATOM   229  O O     . PRO A 1 33  ? 100.692 76.675  123.856 1.00 61.61  ? 33  PRO A O     1 
ATOM   230  C CB    . PRO A 1 33  ? 98.977  78.598  121.998 1.00 406.79 ? 33  PRO A CB    1 
ATOM   231  C CG    . PRO A 1 33  ? 98.852  77.417  121.091 1.00 406.79 ? 33  PRO A CG    1 
ATOM   232  C CD    . PRO A 1 33  ? 100.181 77.295  120.421 1.00 406.79 ? 33  PRO A CD    1 
ATOM   233  N N     . VAL A 1 34  ? 100.554 78.657  124.881 1.00 65.49  ? 34  VAL A N     1 
ATOM   234  C CA    . VAL A 1 34  ? 100.714 78.111  126.228 1.00 65.49  ? 34  VAL A CA    1 
ATOM   235  C C     . VAL A 1 34  ? 102.120 77.568  126.417 1.00 65.49  ? 34  VAL A C     1 
ATOM   236  O O     . VAL A 1 34  ? 102.895 78.103  127.219 1.00 65.49  ? 34  VAL A O     1 
ATOM   237  C CB    . VAL A 1 34  ? 99.683  77.017  126.540 1.00 95.26  ? 34  VAL A CB    1 
ATOM   238  C CG1   . VAL A 1 34  ? 99.946  76.433  127.920 1.00 95.26  ? 34  VAL A CG1   1 
ATOM   239  C CG2   . VAL A 1 34  ? 98.277  77.566  126.439 1.00 95.26  ? 34  VAL A CG2   1 
ATOM   240  N N     . ASN A 1 35  ? 102.460 76.505  125.694 1.00 65.37  ? 35  ASN A N     1 
ATOM   241  C CA    . ASN A 1 35  ? 103.780 75.912  125.842 1.00 65.37  ? 35  ASN A CA    1 
ATOM   242  C C     . ASN A 1 35  ? 104.112 75.081  124.623 1.00 65.37  ? 35  ASN A C     1 
ATOM   243  O O     . ASN A 1 35  ? 103.243 74.794  123.805 1.00 65.37  ? 35  ASN A O     1 
ATOM   244  C CB    . ASN A 1 35  ? 103.847 75.064  127.093 1.00 88.57  ? 35  ASN A CB    1 
ATOM   245  C CG    . ASN A 1 35  ? 102.700 74.084  127.196 1.00 88.57  ? 35  ASN A CG    1 
ATOM   246  O OD1   . ASN A 1 35  ? 101.829 74.038  126.329 1.00 88.57  ? 35  ASN A OD1   1 
ATOM   247  N ND2   . ASN A 1 35  ? 102.693 73.287  128.264 1.00 88.57  ? 35  ASN A ND2   1 
ATOM   248  N N     . GLY A 1 36  ? 105.373 74.663  124.518 1.00 64.00  ? 36  GLY A N     1 
ATOM   249  C CA    . GLY A 1 36  ? 105.821 73.889  123.377 1.00 64.00  ? 36  GLY A CA    1 
ATOM   250  C C     . GLY A 1 36  ? 106.753 74.646  122.470 1.00 64.00  ? 36  GLY A C     1 
ATOM   251  O O     . GLY A 1 36  ? 107.064 74.166  121.371 1.00 64.00  ? 36  GLY A O     1 
ATOM   252  N N     . LYS A 1 37  ? 107.193 75.820  122.885 1.00 59.78  ? 37  LYS A N     1 
ATOM   253  C CA    . LYS A 1 37  ? 108.144 76.605  122.106 1.00 59.78  ? 37  LYS A CA    1 
ATOM   254  C C     . LYS A 1 37  ? 107.581 76.867  120.719 1.00 59.78  ? 37  LYS A C     1 
ATOM   255  O O     . LYS A 1 37  ? 106.421 77.292  120.593 1.00 59.78  ? 37  LYS A O     1 
ATOM   256  C CB    . LYS A 1 37  ? 109.475 75.894  122.049 1.00 89.67  ? 37  LYS A CB    1 
ATOM   257  C CG    . LYS A 1 37  ? 109.980 75.394  123.360 1.00 89.67  ? 37  LYS A CG    1 
ATOM   258  C CD    . LYS A 1 37  ? 110.781 74.116  123.194 1.00 89.67  ? 37  LYS A CD    1 
ATOM   259  C CE    . LYS A 1 37  ? 111.149 73.525  124.545 1.00 89.67  ? 37  LYS A CE    1 
ATOM   260  N NZ    . LYS A 1 37  ? 111.985 72.302  124.406 1.00 89.67  ? 37  LYS A NZ    1 
ATOM   261  N N     . ALA A 1 38  ? 108.359 76.620  119.665 1.00 59.96  ? 38  ALA A N     1 
ATOM   262  C CA    . ALA A 1 38  ? 107.884 76.860  118.309 1.00 59.96  ? 38  ALA A CA    1 
ATOM   263  C C     . ALA A 1 38  ? 108.629 76.063  117.247 1.00 59.96  ? 38  ALA A C     1 
ATOM   264  O O     . ALA A 1 38  ? 109.531 75.280  117.533 1.00 59.96  ? 38  ALA A O     1 
ATOM   265  C CB    . ALA A 1 38  ? 107.979 78.342  117.987 1.00 81.76  ? 38  ALA A CB    1 
ATOM   266  N N     . ILE A 1 39  ? 108.242 76.287  115.996 1.00 64.18  ? 39  ILE A N     1 
ATOM   267  C CA    . ILE A 1 39  ? 108.806 75.574  114.875 1.00 64.18  ? 39  ILE A CA    1 
ATOM   268  C C     . ILE A 1 39  ? 108.959 76.502  113.700 1.00 64.18  ? 39  ILE A C     1 
ATOM   269  O O     . ILE A 1 39  ? 107.957 76.908  113.110 1.00 64.18  ? 39  ILE A O     1 
ATOM   270  C CB    . ILE A 1 39  ? 107.908 74.420  114.483 1.00 95.02  ? 39  ILE A CB    1 
ATOM   271  C CG1   . ILE A 1 39  ? 107.742 73.497  115.686 1.00 95.02  ? 39  ILE A CG1   1 
ATOM   272  C CG2   . ILE A 1 39  ? 108.497 73.711  113.270 1.00 95.02  ? 39  ILE A CG2   1 
ATOM   273  C CD1   . ILE A 1 39  ? 106.693 72.442  115.527 1.00 95.02  ? 39  ILE A CD1   1 
ATOM   274  N N     . ASP A 1 40  ? 110.188 76.792  113.311 1.00 64.87  ? 40  ASP A N     1 
ATOM   275  C CA    . ASP A 1 40  ? 110.430 77.574  112.104 1.00 64.87  ? 40  ASP A CA    1 
ATOM   276  C C     . ASP A 1 40  ? 109.562 78.835  112.021 1.00 64.87  ? 40  ASP A C     1 
ATOM   277  O O     . ASP A 1 40  ? 108.811 79.043  111.073 1.00 64.87  ? 40  ASP A O     1 
ATOM   278  C CB    . ASP A 1 40  ? 110.217 76.689  110.890 1.00 83.40  ? 40  ASP A CB    1 
ATOM   279  C CG    . ASP A 1 40  ? 111.151 75.519  110.907 1.00 83.40  ? 40  ASP A CG    1 
ATOM   280  O OD1   . ASP A 1 40  ? 112.278 75.694  111.379 1.00 83.40  ? 40  ASP A OD1   1 
ATOM   281  O OD2   . ASP A 1 40  ? 110.768 74.430  110.479 1.00 83.40  ? 40  ASP A OD2   1 
ATOM   282  N N     . VAL A 1 41  ? 109.694 79.688  113.028 1.00 60.67  ? 41  VAL A N     1 
ATOM   283  C CA    . VAL A 1 41  ? 108.864 80.873  113.141 1.00 60.67  ? 41  VAL A CA    1 
ATOM   284  C C     . VAL A 1 41  ? 109.043 81.828  111.986 1.00 60.67  ? 41  VAL A C     1 
ATOM   285  O O     . VAL A 1 41  ? 110.162 82.154  111.601 1.00 60.67  ? 41  VAL A O     1 
ATOM   286  C CB    . VAL A 1 41  ? 109.200 81.582  114.446 1.00 88.25  ? 41  VAL A CB    1 
ATOM   287  C CG1   . VAL A 1 41  ? 108.515 82.896  114.529 1.00 88.25  ? 41  VAL A CG1   1 
ATOM   288  C CG2   . VAL A 1 41  ? 108.747 80.756  115.528 1.00 88.25  ? 41  VAL A CG2   1 
ATOM   289  N N     . VAL A 1 42  ? 107.933 82.327  111.471 1.00 56.27  ? 42  VAL A N     1 
ATOM   290  C CA    . VAL A 1 42  ? 107.936 83.279  110.372 1.00 56.27  ? 42  VAL A CA    1 
ATOM   291  C C     . VAL A 1 42  ? 107.186 84.538  110.764 1.00 56.27  ? 42  VAL A C     1 
ATOM   292  O O     . VAL A 1 42  ? 106.350 84.506  111.663 1.00 56.27  ? 42  VAL A O     1 
ATOM   293  C CB    . VAL A 1 42  ? 107.284 82.676  109.143 1.00 81.85  ? 42  VAL A CB    1 
ATOM   294  C CG1   . VAL A 1 42  ? 108.046 81.461  108.714 1.00 81.85  ? 42  VAL A CG1   1 
ATOM   295  C CG2   . VAL A 1 42  ? 105.847 82.309  109.463 1.00 81.85  ? 42  VAL A CG2   1 
ATOM   296  N N     . GLY A 1 43  ? 107.426 85.639  110.040 1.00 59.10  ? 43  GLY A N     1 
ATOM   297  C CA    . GLY A 1 43  ? 106.750 86.903  110.299 1.00 59.10  ? 43  GLY A CA    1 
ATOM   298  C C     . GLY A 1 43  ? 107.568 87.747  111.255 1.00 59.10  ? 43  GLY A C     1 
ATOM   299  O O     . GLY A 1 43  ? 108.525 87.273  111.863 1.00 59.10  ? 43  GLY A O     1 
ATOM   300  N N     . ASP A 1 44  ? 107.208 89.024  111.429 1.00 60.34  ? 44  ASP A N     1 
ATOM   301  C CA    . ASP A 1 44  ? 108.058 89.850  112.301 1.00 60.34  ? 44  ASP A CA    1 
ATOM   302  C C     . ASP A 1 44  ? 107.644 89.642  113.749 1.00 60.34  ? 44  ASP A C     1 
ATOM   303  O O     . ASP A 1 44  ? 106.975 90.457  114.384 1.00 60.34  ? 44  ASP A O     1 
ATOM   304  C CB    . ASP A 1 44  ? 108.039 91.318  111.906 1.00 77.58  ? 44  ASP A CB    1 
ATOM   305  C CG    . ASP A 1 44  ? 109.122 92.124  112.627 1.00 77.58  ? 44  ASP A CG    1 
ATOM   306  O OD1   . ASP A 1 44  ? 109.860 91.543  113.433 1.00 77.58  ? 44  ASP A OD1   1 
ATOM   307  O OD2   . ASP A 1 44  ? 109.245 93.327  112.369 1.00 77.58  ? 44  ASP A OD2   1 
ATOM   308  N N     . THR A 1 45  ? 108.103 88.521  114.261 1.00 57.21  ? 45  THR A N     1 
ATOM   309  C CA    . THR A 1 45  ? 107.685 87.996  115.537 1.00 57.21  ? 45  THR A CA    1 
ATOM   310  C C     . THR A 1 45  ? 107.971 88.943  116.674 1.00 57.21  ? 45  THR A C     1 
ATOM   311  O O     . THR A 1 45  ? 107.108 89.144  117.542 1.00 57.21  ? 45  THR A O     1 
ATOM   312  C CB    . THR A 1 45  ? 108.386 86.673  115.765 1.00 80.09  ? 45  THR A CB    1 
ATOM   313  O OG1   . THR A 1 45  ? 107.948 85.769  114.756 1.00 80.09  ? 45  THR A OG1   1 
ATOM   314  C CG2   . THR A 1 45  ? 108.040 86.100  117.122 1.00 80.09  ? 45  THR A CG2   1 
ATOM   315  N N     . ASP A 1 46  ? 109.143 89.572  116.664 1.00 56.49  ? 46  ASP A N     1 
ATOM   316  C CA    . ASP A 1 46  ? 109.584 90.389  117.784 1.00 56.49  ? 46  ASP A CA    1 
ATOM   317  C C     . ASP A 1 46  ? 108.758 91.649  118.014 1.00 56.49  ? 46  ASP A C     1 
ATOM   318  O O     . ASP A 1 46  ? 108.934 92.302  119.047 1.00 56.49  ? 46  ASP A O     1 
ATOM   319  C CB    . ASP A 1 46  ? 111.032 90.742  117.609 1.00 72.63  ? 46  ASP A CB    1 
ATOM   320  C CG    . ASP A 1 46  ? 111.920 89.558  117.868 1.00 72.63  ? 46  ASP A CG    1 
ATOM   321  O OD1   . ASP A 1 46  ? 111.469 88.598  118.511 1.00 72.63  ? 46  ASP A OD1   1 
ATOM   322  O OD2   . ASP A 1 46  ? 113.066 89.575  117.434 1.00 72.63  ? 46  ASP A OD2   1 
ATOM   323  N N     . ILE A 1 47  ? 107.867 92.019  117.102 1.00 56.33  ? 47  ILE A N     1 
ATOM   324  C CA    . ILE A 1 47  ? 107.008 93.154  117.390 1.00 56.33  ? 47  ILE A CA    1 
ATOM   325  C C     . ILE A 1 47  ? 106.110 92.838  118.560 1.00 56.33  ? 47  ILE A C     1 
ATOM   326  O O     . ILE A 1 47  ? 105.838 93.692  119.402 1.00 56.33  ? 47  ILE A O     1 
ATOM   327  C CB    . ILE A 1 47  ? 106.145 93.525  116.191 1.00 83.40  ? 47  ILE A CB    1 
ATOM   328  C CG1   . ILE A 1 47  ? 107.017 93.989  115.068 1.00 83.40  ? 47  ILE A CG1   1 
ATOM   329  C CG2   . ILE A 1 47  ? 105.131 94.626  116.603 1.00 83.40  ? 47  ILE A CG2   1 
ATOM   330  C CD1   . ILE A 1 47  ? 106.285 94.104  113.768 1.00 83.40  ? 47  ILE A CD1   1 
ATOM   331  N N     . PHE A 1 48  ? 105.579 91.640  118.592 1.00 53.30  ? 48  PHE A N     1 
ATOM   332  C CA    . PHE A 1 48  ? 104.630 91.286  119.600 1.00 53.30  ? 48  PHE A CA    1 
ATOM   333  C C     . PHE A 1 48  ? 105.157 90.308  120.619 1.00 53.30  ? 48  PHE A C     1 
ATOM   334  O O     . PHE A 1 48  ? 104.573 90.195  121.698 1.00 53.30  ? 48  PHE A O     1 
ATOM   335  C CB    . PHE A 1 48  ? 103.398 90.731  118.920 1.00 74.37  ? 48  PHE A CB    1 
ATOM   336  C CG    . PHE A 1 48  ? 102.686 91.728  118.088 1.00 74.37  ? 48  PHE A CG    1 
ATOM   337  C CD1   . PHE A 1 48  ? 101.730 92.543  118.641 1.00 74.37  ? 48  PHE A CD1   1 
ATOM   338  C CD2   . PHE A 1 48  ? 102.954 91.857  116.739 1.00 74.37  ? 48  PHE A CD2   1 
ATOM   339  C CE1   . PHE A 1 48  ? 101.061 93.462  117.878 1.00 74.37  ? 48  PHE A CE1   1 
ATOM   340  C CE2   . PHE A 1 48  ? 102.285 92.781  115.967 1.00 74.37  ? 48  PHE A CE2   1 
ATOM   341  C CZ    . PHE A 1 48  ? 101.343 93.583  116.539 1.00 74.37  ? 48  PHE A CZ    1 
ATOM   342  N N     . PHE A 1 49  ? 106.231 89.608  120.327 1.00 52.39  ? 49  PHE A N     1 
ATOM   343  C CA    . PHE A 1 49  ? 106.749 88.617  121.239 1.00 52.39  ? 49  PHE A CA    1 
ATOM   344  C C     . PHE A 1 49  ? 108.158 88.926  121.635 1.00 52.39  ? 49  PHE A C     1 
ATOM   345  O O     . PHE A 1 49  ? 108.917 89.521  120.886 1.00 52.39  ? 49  PHE A O     1 
ATOM   346  C CB    . PHE A 1 49  ? 106.779 87.263  120.663 1.00 73.10  ? 49  PHE A CB    1 
ATOM   347  C CG    . PHE A 1 49  ? 105.469 86.696  120.436 1.00 73.10  ? 49  PHE A CG    1 
ATOM   348  C CD1   . PHE A 1 49  ? 104.795 86.978  119.287 1.00 73.10  ? 49  PHE A CD1   1 
ATOM   349  C CD2   . PHE A 1 49  ? 104.912 85.844  121.351 1.00 73.10  ? 49  PHE A CD2   1 
ATOM   350  C CE1   . PHE A 1 49  ? 103.574 86.436  119.058 1.00 73.10  ? 49  PHE A CE1   1 
ATOM   351  C CE2   . PHE A 1 49  ? 103.695 85.300  121.131 1.00 73.10  ? 49  PHE A CE2   1 
ATOM   352  C CZ    . PHE A 1 49  ? 103.018 85.595  119.974 1.00 73.10  ? 49  PHE A CZ    1 
ATOM   353  N N     . ASN A 1 50  ? 108.513 88.512  122.792 1.00 55.85  ? 50  ASN A N     1 
ATOM   354  C CA    . ASN A 1 50  ? 109.868 88.692  123.225 1.00 55.85  ? 50  ASN A CA    1 
ATOM   355  C C     . ASN A 1 50  ? 110.525 87.360  123.038 1.00 55.85  ? 50  ASN A C     1 
ATOM   356  O O     . ASN A 1 50  ? 110.104 86.369  123.621 1.00 55.85  ? 50  ASN A O     1 
ATOM   357  C CB    . ASN A 1 50  ? 109.946 89.167  124.655 1.00 75.67  ? 50  ASN A CB    1 
ATOM   358  C CG    . ASN A 1 50  ? 111.296 89.517  125.005 1.00 75.67  ? 50  ASN A CG    1 
ATOM   359  O OD1   . ASN A 1 50  ? 112.130 89.655  124.122 1.00 75.67  ? 50  ASN A OD1   1 
ATOM   360  N ND2   . ASN A 1 50  ? 111.571 89.654  126.284 1.00 75.67  ? 50  ASN A ND2   1 
ATOM   361  N N     . THR A 1 51  ? 111.474 87.287  122.145 1.00 62.37  ? 51  THR A N     1 
ATOM   362  C CA    . THR A 1 51  ? 112.116 86.007  121.982 1.00 62.37  ? 51  THR A CA    1 
ATOM   363  C C     . THR A 1 51  ? 113.062 85.864  123.133 1.00 62.37  ? 51  THR A C     1 
ATOM   364  O O     . THR A 1 51  ? 113.873 86.749  123.386 1.00 62.37  ? 51  THR A O     1 
ATOM   365  C CB    . THR A 1 51  ? 112.893 85.879  120.682 1.00 87.32  ? 51  THR A CB    1 
ATOM   366  O OG1   . THR A 1 51  ? 112.022 86.076  119.557 1.00 87.32  ? 51  THR A OG1   1 
ATOM   367  C CG2   . THR A 1 51  ? 113.481 84.472  120.615 1.00 87.32  ? 51  THR A CG2   1 
ATOM   368  N N     . ILE A 1 52  ? 112.962 84.761  123.841 1.00 68.62  ? 52  ILE A N     1 
ATOM   369  C CA    . ILE A 1 52  ? 113.764 84.531  125.013 1.00 68.62  ? 52  ILE A CA    1 
ATOM   370  C C     . ILE A 1 52  ? 114.907 83.599  124.749 1.00 68.62  ? 52  ILE A C     1 
ATOM   371  O O     . ILE A 1 52  ? 116.033 83.842  125.175 1.00 68.62  ? 52  ILE A O     1 
ATOM   372  C CB    . ILE A 1 52  ? 112.873 83.966  126.120 1.00 101.59 ? 52  ILE A CB    1 
ATOM   373  C CG1   . ILE A 1 52  ? 111.888 85.045  126.521 1.00 101.59 ? 52  ILE A CG1   1 
ATOM   374  C CG2   . ILE A 1 52  ? 113.727 83.446  127.266 1.00 101.59 ? 52  ILE A CG2   1 
ATOM   375  C CD1   . ILE A 1 52  ? 110.812 84.562  127.397 1.00 101.59 ? 52  ILE A CD1   1 
ATOM   376  N N     . GLY A 1 53  ? 114.635 82.537  124.025 1.00 67.83  ? 53  GLY A N     1 
ATOM   377  C CA    . GLY A 1 53  ? 115.584 81.477  123.789 1.00 67.83  ? 53  GLY A CA    1 
ATOM   378  C C     . GLY A 1 53  ? 114.887 80.172  124.019 1.00 67.83  ? 53  GLY A C     1 
ATOM   379  O O     . GLY A 1 53  ? 114.691 79.725  125.145 1.00 67.83  ? 53  GLY A O     1 
ATOM   380  N N     . ASP A 1 54  ? 114.511 79.555  122.898 1.00 65.79  ? 54  ASP A N     1 
ATOM   381  C CA    . ASP A 1 54  ? 113.704 78.341  122.888 1.00 65.79  ? 54  ASP A CA    1 
ATOM   382  C C     . ASP A 1 54  ? 112.453 78.598  123.694 1.00 65.79  ? 54  ASP A C     1 
ATOM   383  O O     . ASP A 1 54  ? 111.994 77.760  124.477 1.00 65.79  ? 54  ASP A O     1 
ATOM   384  C CB    . ASP A 1 54  ? 114.467 77.130  123.421 1.00 84.59  ? 54  ASP A CB    1 
ATOM   385  C CG    . ASP A 1 54  ? 113.809 75.812  123.017 1.00 84.59  ? 54  ASP A CG    1 
ATOM   386  O OD1   . ASP A 1 54  ? 113.222 75.766  121.931 1.00 84.59  ? 54  ASP A OD1   1 
ATOM   387  O OD2   . ASP A 1 54  ? 113.842 74.844  123.794 1.00 84.59  ? 54  ASP A OD2   1 
ATOM   388  N N     . LYS A 1 55  ? 111.968 79.819  123.539 1.00 62.57  ? 55  LYS A N     1 
ATOM   389  C CA    . LYS A 1 55  ? 110.802 80.333  124.210 1.00 62.57  ? 55  LYS A CA    1 
ATOM   390  C C     . LYS A 1 55  ? 110.502 81.710  123.665 1.00 62.57  ? 55  LYS A C     1 
ATOM   391  O O     . LYS A 1 55  ? 111.414 82.500  123.408 1.00 62.57  ? 55  LYS A O     1 
ATOM   392  C CB    . LYS A 1 55  ? 111.023 80.388  125.718 1.00 93.85  ? 55  LYS A CB    1 
ATOM   393  C CG    . LYS A 1 55  ? 109.778 80.785  126.507 1.00 93.85  ? 55  LYS A CG    1 
ATOM   394  C CD    . LYS A 1 55  ? 110.013 80.687  128.007 1.00 93.85  ? 55  LYS A CD    1 
ATOM   395  C CE    . LYS A 1 55  ? 108.755 81.036  128.789 1.00 93.85  ? 55  LYS A CE    1 
ATOM   396  N NZ    . LYS A 1 55  ? 108.951 80.880  130.257 1.00 93.85  ? 55  LYS A NZ    1 
ATOM   397  N N     . TYR A 1 56  ? 109.225 81.996  123.518 1.00 60.75  ? 56  TYR A N     1 
ATOM   398  C CA    . TYR A 1 56  ? 108.723 83.308  123.169 1.00 60.75  ? 56  TYR A CA    1 
ATOM   399  C C     . TYR A 1 56  ? 107.615 83.674  124.140 1.00 60.75  ? 56  TYR A C     1 
ATOM   400  O O     . TYR A 1 56  ? 106.783 82.822  124.457 1.00 60.75  ? 56  TYR A O     1 
ATOM   401  C CB    . TYR A 1 56  ? 108.106 83.291  121.824 1.00 84.11  ? 56  TYR A CB    1 
ATOM   402  C CG    . TYR A 1 56  ? 108.999 82.898  120.776 1.00 84.11  ? 56  TYR A CG    1 
ATOM   403  C CD1   . TYR A 1 56  ? 109.235 81.568  120.526 1.00 84.11  ? 56  TYR A CD1   1 
ATOM   404  C CD2   . TYR A 1 56  ? 109.586 83.845  119.993 1.00 84.11  ? 56  TYR A CD2   1 
ATOM   405  C CE1   . TYR A 1 56  ? 110.074 81.189  119.530 1.00 84.11  ? 56  TYR A CE1   1 
ATOM   406  C CE2   . TYR A 1 56  ? 110.417 83.484  118.980 1.00 84.11  ? 56  TYR A CE2   1 
ATOM   407  C CZ    . TYR A 1 56  ? 110.667 82.155  118.751 1.00 84.11  ? 56  TYR A CZ    1 
ATOM   408  O OH    . TYR A 1 56  ? 111.522 81.794  117.739 1.00 84.11  ? 56  TYR A OH    1 
ATOM   409  N N     . ILE A 1 57  ? 107.539 84.935  124.555 1.00 56.29  ? 57  ILE A N     1 
ATOM   410  C CA    . ILE A 1 57  ? 106.369 85.333  125.331 1.00 56.29  ? 57  ILE A CA    1 
ATOM   411  C C     . ILE A 1 57  ? 105.736 86.551  124.721 1.00 56.29  ? 57  ILE A C     1 
ATOM   412  O O     . ILE A 1 57  ? 106.423 87.345  124.099 1.00 56.29  ? 57  ILE A O     1 
ATOM   413  C CB    . ILE A 1 57  ? 106.710 85.646  126.768 1.00 83.34  ? 57  ILE A CB    1 
ATOM   414  C CG1   . ILE A 1 57  ? 107.701 86.785  126.806 1.00 83.34  ? 57  ILE A CG1   1 
ATOM   415  C CG2   . ILE A 1 57  ? 107.196 84.396  127.438 1.00 83.34  ? 57  ILE A CG2   1 
ATOM   416  C CD1   . ILE A 1 57  ? 107.961 87.332  128.190 1.00 83.34  ? 57  ILE A CD1   1 
ATOM   417  N N     . PRO A 1 58  ? 104.455 86.709  124.843 1.00 49.44  ? 58  PRO A N     1 
ATOM   418  C CA    . PRO A 1 58  ? 103.809 87.938  124.457 1.00 49.44  ? 58  PRO A CA    1 
ATOM   419  C C     . PRO A 1 58  ? 104.377 89.097  125.250 1.00 49.44  ? 58  PRO A C     1 
ATOM   420  O O     . PRO A 1 58  ? 104.555 89.000  126.463 1.00 49.44  ? 58  PRO A O     1 
ATOM   421  C CB    . PRO A 1 58  ? 102.358 87.684  124.842 1.00 326.43 ? 58  PRO A CB    1 
ATOM   422  C CG    . PRO A 1 58  ? 102.236 86.221  124.862 1.00 326.43 ? 58  PRO A CG    1 
ATOM   423  C CD    . PRO A 1 58  ? 103.540 85.705  125.316 1.00 326.43 ? 58  PRO A CD    1 
ATOM   424  N N     . ARG A 1 59  ? 104.586 90.226  124.579 1.00 51.64  ? 59  ARG A N     1 
ATOM   425  C CA    . ARG A 1 59  ? 105.029 91.430  125.262 1.00 51.64  ? 59  ARG A CA    1 
ATOM   426  C C     . ARG A 1 59  ? 103.806 92.065  125.865 1.00 51.64  ? 59  ARG A C     1 
ATOM   427  O O     . ARG A 1 59  ? 103.266 93.036  125.329 1.00 51.64  ? 59  ARG A O     1 
ATOM   428  C CB    . ARG A 1 59  ? 105.656 92.421  124.303 1.00 75.88  ? 59  ARG A CB    1 
ATOM   429  C CG    . ARG A 1 59  ? 106.934 92.028  123.656 1.00 75.88  ? 59  ARG A CG    1 
ATOM   430  C CD    . ARG A 1 59  ? 107.410 93.161  122.818 1.00 75.88  ? 59  ARG A CD    1 
ATOM   431  N NE    . ARG A 1 59  ? 108.602 92.850  122.050 1.00 75.88  ? 59  ARG A NE    1 
ATOM   432  C CZ    . ARG A 1 59  ? 109.859 92.977  122.451 1.00 75.88  ? 59  ARG A CZ    1 
ATOM   433  N NH1   . ARG A 1 59  ? 110.179 93.363  123.685 1.00 75.88  ? 59  ARG A NH1   1 
ATOM   434  N NH2   . ARG A 1 59  ? 110.818 92.713  121.577 1.00 75.88  ? 59  ARG A NH2   1 
ATOM   435  N N     . ALA A 1 60  ? 103.349 91.522  126.978 1.00 46.91  ? 60  ALA A N     1 
ATOM   436  C CA    . ALA A 1 60  ? 102.071 91.986  127.452 1.00 46.91  ? 60  ALA A CA    1 
ATOM   437  C C     . ALA A 1 60  ? 101.982 92.019  128.964 1.00 46.91  ? 60  ALA A C     1 
ATOM   438  O O     . ALA A 1 60  ? 102.743 91.364  129.673 1.00 46.91  ? 60  ALA A O     1 
ATOM   439  C CB    . ALA A 1 60  ? 100.967 91.125  126.877 1.00 63.97  ? 60  ALA A CB    1 
ATOM   440  N N     . VAL A 1 61  ? 101.025 92.825  129.422 1.00 46.62  ? 61  VAL A N     1 
ATOM   441  C CA    . VAL A 1 61  ? 100.731 93.138  130.818 1.00 46.62  ? 61  VAL A CA    1 
ATOM   442  C C     . VAL A 1 61  ? 99.306  92.736  131.141 1.00 46.62  ? 61  VAL A C     1 
ATOM   443  O O     . VAL A 1 61  ? 98.389  93.125  130.415 1.00 46.62  ? 61  VAL A O     1 
ATOM   444  C CB    . VAL A 1 61  ? 100.865 94.645  131.033 1.00 67.81  ? 61  VAL A CB    1 
ATOM   445  C CG1   . VAL A 1 61  ? 100.550 95.039  132.475 1.00 67.81  ? 61  VAL A CG1   1 
ATOM   446  C CG2   . VAL A 1 61  ? 102.237 95.106  130.576 1.00 67.81  ? 61  VAL A CG2   1 
ATOM   447  N N     . VAL A 1 62  ? 99.089  92.018  132.241 1.00 47.69  ? 62  VAL A N     1 
ATOM   448  C CA    . VAL A 1 62  ? 97.729  91.630  132.623 1.00 47.69  ? 62  VAL A CA    1 
ATOM   449  C C     . VAL A 1 62  ? 97.283  92.281  133.917 1.00 47.69  ? 62  VAL A C     1 
ATOM   450  O O     . VAL A 1 62  ? 97.916  92.105  134.959 1.00 47.69  ? 62  VAL A O     1 
ATOM   451  C CB    . VAL A 1 62  ? 97.615  90.132  132.761 1.00 69.37  ? 62  VAL A CB    1 
ATOM   452  C CG1   . VAL A 1 62  ? 96.272  89.764  133.307 1.00 69.37  ? 62  VAL A CG1   1 
ATOM   453  C CG2   . VAL A 1 62  ? 97.753  89.582  131.452 1.00 69.37  ? 62  VAL A CG2   1 
ATOM   454  N N     . VAL A 1 63  ? 96.155  92.963  133.875 1.00 48.91  ? 63  VAL A N     1 
ATOM   455  C CA    . VAL A 1 63  ? 95.656  93.674  135.030 1.00 48.91  ? 63  VAL A CA    1 
ATOM   456  C C     . VAL A 1 63  ? 94.350  93.098  135.511 1.00 48.91  ? 63  VAL A C     1 
ATOM   457  O O     . VAL A 1 63  ? 93.294  93.308  134.903 1.00 48.91  ? 63  VAL A O     1 
ATOM   458  C CB    . VAL A 1 63  ? 95.473  95.145  134.708 1.00 71.14  ? 63  VAL A CB    1 
ATOM   459  C CG1   . VAL A 1 63  ? 94.950  95.876  135.934 1.00 71.14  ? 63  VAL A CG1   1 
ATOM   460  C CG2   . VAL A 1 63  ? 96.803  95.710  134.227 1.00 71.14  ? 63  VAL A CG2   1 
ATOM   461  N N     . ASP A 1 64  ? 94.414  92.476  136.670 1.00 53.90  ? 64  ASP A N     1 
ATOM   462  C CA    . ASP A 1 64  ? 93.280  91.850  137.307 1.00 53.90  ? 64  ASP A CA    1 
ATOM   463  C C     . ASP A 1 64  ? 93.026  92.552  138.608 1.00 53.90  ? 64  ASP A C     1 
ATOM   464  O O     . ASP A 1 64  ? 93.570  92.160  139.629 1.00 53.90  ? 64  ASP A O     1 
ATOM   465  C CB    . ASP A 1 64  ? 93.576  90.403  137.612 1.00 69.30  ? 64  ASP A CB    1 
ATOM   466  C CG    . ASP A 1 64  ? 93.750  89.550  136.389 1.00 69.30  ? 64  ASP A CG    1 
ATOM   467  O OD1   . ASP A 1 64  ? 92.974  89.696  135.444 1.00 69.30  ? 64  ASP A OD1   1 
ATOM   468  O OD2   . ASP A 1 64  ? 94.657  88.708  136.396 1.00 69.30  ? 64  ASP A OD2   1 
ATOM   469  N N     . LEU A 1 65  ? 92.192  93.566  138.621 1.00 57.12  ? 65  LEU A N     1 
ATOM   470  C CA    . LEU A 1 65  ? 92.046  94.234  139.889 1.00 57.12  ? 65  LEU A CA    1 
ATOM   471  C C     . LEU A 1 65  ? 91.556  93.251  140.903 1.00 57.12  ? 65  LEU A C     1 
ATOM   472  O O     . LEU A 1 65  ? 92.196  93.038  141.935 1.00 57.12  ? 65  LEU A O     1 
ATOM   473  C CB    . LEU A 1 65  ? 91.101  95.405  139.785 1.00 84.57  ? 65  LEU A CB    1 
ATOM   474  C CG    . LEU A 1 65  ? 90.796  96.165  141.065 1.00 84.57  ? 65  LEU A CG    1 
ATOM   475  C CD1   . LEU A 1 65  ? 92.062  96.731  141.701 1.00 84.57  ? 65  LEU A CD1   1 
ATOM   476  C CD2   . LEU A 1 65  ? 89.800  97.285  140.728 1.00 84.57  ? 65  LEU A CD2   1 
ATOM   477  N N     . GLU A 1 66  ? 90.515  92.576  140.584 1.00 54.29  ? 66  GLU A N     1 
ATOM   478  C CA    . GLU A 1 66  ? 90.027  91.584  141.504 1.00 54.29  ? 66  GLU A CA    1 
ATOM   479  C C     . GLU A 1 66  ? 90.936  90.372  141.437 1.00 54.29  ? 66  GLU A C     1 
ATOM   480  O O     . GLU A 1 66  ? 91.109  89.806  140.362 1.00 54.29  ? 66  GLU A O     1 
ATOM   481  C CB    . GLU A 1 66  ? 88.599  91.179  141.156 1.00 72.93  ? 66  GLU A CB    1 
ATOM   482  C CG    . GLU A 1 66  ? 87.941  90.330  142.218 1.00 72.93  ? 66  GLU A CG    1 
ATOM   483  C CD    . GLU A 1 66  ? 86.551  89.925  141.866 1.00 72.93  ? 66  GLU A CD    1 
ATOM   484  O OE1   . GLU A 1 66  ? 86.093  90.261  140.778 1.00 72.93  ? 66  GLU A OE1   1 
ATOM   485  O OE2   . GLU A 1 66  ? 85.914  89.265  142.683 1.00 72.93  ? 66  GLU A OE2   1 
ATOM   486  N N     . PRO A 1 67  ? 91.470  89.923  142.559 1.00 52.65  ? 67  PRO A N     1 
ATOM   487  C CA    . PRO A 1 67  ? 92.383  88.776  142.587 1.00 52.65  ? 67  PRO A CA    1 
ATOM   488  C C     . PRO A 1 67  ? 91.720  87.478  142.178 1.00 52.65  ? 67  PRO A C     1 
ATOM   489  O O     . PRO A 1 67  ? 92.404  86.511  141.820 1.00 52.65  ? 67  PRO A O     1 
ATOM   490  C CB    . PRO A 1 67  ? 92.824  88.744  144.052 1.00 347.63 ? 67  PRO A CB    1 
ATOM   491  C CG    . PRO A 1 67  ? 91.692  89.417  144.789 1.00 347.63 ? 67  PRO A CG    1 
ATOM   492  C CD    . PRO A 1 67  ? 91.176  90.471  143.875 1.00 347.63 ? 67  PRO A CD    1 
ATOM   493  N N     . ALA A 1 68  ? 90.395  87.461  142.184 1.00 51.39  ? 68  ALA A N     1 
ATOM   494  C CA    . ALA A 1 68  ? 89.600  86.283  141.892 1.00 51.39  ? 68  ALA A CA    1 
ATOM   495  C C     . ALA A 1 68  ? 89.779  85.760  140.492 1.00 51.39  ? 68  ALA A C     1 
ATOM   496  O O     . ALA A 1 68  ? 89.404  84.622  140.224 1.00 51.39  ? 68  ALA A O     1 
ATOM   497  C CB    . ALA A 1 68  ? 88.132  86.612  142.079 1.00 70.08  ? 68  ALA A CB    1 
ATOM   498  N N     . VAL A 1 69  ? 90.302  86.554  139.582 1.00 51.39  ? 69  VAL A N     1 
ATOM   499  C CA    . VAL A 1 69  ? 90.393  86.097  138.212 1.00 51.39  ? 69  VAL A CA    1 
ATOM   500  C C     . VAL A 1 69  ? 91.824  85.906  137.733 1.00 51.39  ? 69  VAL A C     1 
ATOM   501  O O     . VAL A 1 69  ? 92.044  85.789  136.538 1.00 51.39  ? 69  VAL A O     1 
ATOM   502  C CB    . VAL A 1 69  ? 89.648  87.040  137.267 1.00 74.75  ? 69  VAL A CB    1 
ATOM   503  C CG1   . VAL A 1 69  ? 88.169  87.021  137.585 1.00 74.75  ? 69  VAL A CG1   1 
ATOM   504  C CG2   . VAL A 1 69  ? 90.211  88.438  137.372 1.00 74.75  ? 69  VAL A CG2   1 
ATOM   505  N N     . VAL A 1 70  ? 92.811  85.857  138.618 1.00 51.59  ? 70  VAL A N     1 
ATOM   506  C CA    . VAL A 1 70  ? 94.172  85.739  138.099 1.00 51.59  ? 70  VAL A CA    1 
ATOM   507  C C     . VAL A 1 70  ? 94.401  84.396  137.417 1.00 51.59  ? 70  VAL A C     1 
ATOM   508  O O     . VAL A 1 70  ? 95.161  84.315  136.445 1.00 51.59  ? 70  VAL A O     1 
ATOM   509  C CB    . VAL A 1 70  ? 95.220  85.992  139.199 1.00 75.04  ? 70  VAL A CB    1 
ATOM   510  C CG1   . VAL A 1 70  ? 95.092  87.411  139.699 1.00 75.04  ? 70  VAL A CG1   1 
ATOM   511  C CG2   . VAL A 1 70  ? 95.078  85.002  140.337 1.00 75.04  ? 70  VAL A CG2   1 
ATOM   512  N N     . GLU A 1 71  ? 93.710  83.350  137.866 1.00 51.41  ? 71  GLU A N     1 
ATOM   513  C CA    . GLU A 1 71  ? 93.841  82.024  137.284 1.00 51.41  ? 71  GLU A CA    1 
ATOM   514  C C     . GLU A 1 71  ? 93.333  81.946  135.853 1.00 51.41  ? 71  GLU A C     1 
ATOM   515  O O     . GLU A 1 71  ? 93.717  81.023  135.120 1.00 51.41  ? 71  GLU A O     1 
ATOM   516  C CB    . GLU A 1 71  ? 93.128  81.000  138.163 1.00 69.06  ? 71  GLU A CB    1 
ATOM   517  C CG    . GLU A 1 71  ? 93.884  80.720  139.445 1.00 69.06  ? 71  GLU A CG    1 
ATOM   518  C CD    . GLU A 1 71  ? 93.669  81.771  140.463 1.00 69.06  ? 71  GLU A CD    1 
ATOM   519  O OE1   . GLU A 1 71  ? 92.795  82.606  140.247 1.00 69.06  ? 71  GLU A OE1   1 
ATOM   520  O OE2   . GLU A 1 71  ? 94.377  81.778  141.467 1.00 69.06  ? 71  GLU A OE2   1 
ATOM   521  N N     . ASN A 1 72  ? 92.519  82.910  135.416 1.00 55.00  ? 72  ASN A N     1 
ATOM   522  C CA    . ASN A 1 72  ? 92.096  82.859  134.031 1.00 55.00  ? 72  ASN A CA    1 
ATOM   523  C C     . ASN A 1 72  ? 93.298  83.033  133.132 1.00 55.00  ? 72  ASN A C     1 
ATOM   524  O O     . ASN A 1 72  ? 93.297  82.529  132.012 1.00 55.00  ? 72  ASN A O     1 
ATOM   525  C CB    . ASN A 1 72  ? 91.013  83.892  133.749 1.00 74.52  ? 72  ASN A CB    1 
ATOM   526  C CG    . ASN A 1 72  ? 89.676  83.504  134.358 1.00 74.52  ? 72  ASN A CG    1 
ATOM   527  O OD1   . ASN A 1 72  ? 89.402  82.332  134.638 1.00 74.52  ? 72  ASN A OD1   1 
ATOM   528  N ND2   . ASN A 1 72  ? 88.832  84.497  134.566 1.00 74.52  ? 72  ASN A ND2   1 
ATOM   529  N N     . ILE A 1 73  ? 94.344  83.701  133.606 1.00 55.09  ? 73  ILE A N     1 
ATOM   530  C CA    . ILE A 1 73  ? 95.564  83.751  132.845 1.00 55.09  ? 73  ILE A CA    1 
ATOM   531  C C     . ILE A 1 73  ? 96.545  82.714  133.347 1.00 55.09  ? 73  ILE A C     1 
ATOM   532  O O     . ILE A 1 73  ? 97.094  81.948  132.556 1.00 55.09  ? 73  ILE A O     1 
ATOM   533  C CB    . ILE A 1 73  ? 96.165  85.176  132.784 1.00 81.56  ? 73  ILE A CB    1 
ATOM   534  C CG1   . ILE A 1 73  ? 95.119  86.204  132.256 1.00 81.56  ? 73  ILE A CG1   1 
ATOM   535  C CG2   . ILE A 1 73  ? 97.466  85.191  131.937 1.00 81.56  ? 73  ILE A CG2   1 
ATOM   536  C CD1   . ILE A 1 73  ? 94.821  86.206  130.911 1.00 81.56  ? 73  ILE A CD1   1 
ATOM   537  N N     . ARG A 1 74  ? 96.686  82.588  134.660 1.00 58.94  ? 74  ARG A N     1 
ATOM   538  C CA    . ARG A 1 74  ? 97.704  81.672  135.150 1.00 58.94  ? 74  ARG A CA    1 
ATOM   539  C C     . ARG A 1 74  ? 97.481  80.255  134.648 1.00 58.94  ? 74  ARG A C     1 
ATOM   540  O O     . ARG A 1 74  ? 98.445  79.554  134.328 1.00 58.94  ? 74  ARG A O     1 
ATOM   541  C CB    . ARG A 1 74  ? 97.739  81.652  136.665 1.00 86.60  ? 74  ARG A CB    1 
ATOM   542  C CG    . ARG A 1 74  ? 98.230  82.908  137.305 1.00 86.60  ? 74  ARG A CG    1 
ATOM   543  C CD    . ARG A 1 74  ? 98.104  82.816  138.784 1.00 86.60  ? 74  ARG A CD    1 
ATOM   544  N NE    . ARG A 1 74  ? 98.575  84.033  139.416 1.00 86.60  ? 74  ARG A NE    1 
ATOM   545  C CZ    . ARG A 1 74  ? 98.487  84.283  140.713 1.00 86.60  ? 74  ARG A CZ    1 
ATOM   546  N NH1   . ARG A 1 74  ? 97.953  83.409  141.546 1.00 86.60  ? 74  ARG A NH1   1 
ATOM   547  N NH2   . ARG A 1 74  ? 98.949  85.438  141.183 1.00 86.60  ? 74  ARG A NH2   1 
ATOM   548  N N     . GLU A 1 75  ? 96.238  79.803  134.591 1.00 58.73  ? 75  GLU A N     1 
ATOM   549  C CA    . GLU A 1 75  ? 96.019  78.446  134.149 1.00 58.73  ? 75  GLU A CA    1 
ATOM   550  C C     . GLU A 1 75  ? 95.333  78.354  132.809 1.00 58.73  ? 75  GLU A C     1 
ATOM   551  O O     . GLU A 1 75  ? 95.731  77.537  131.986 1.00 58.73  ? 75  GLU A O     1 
ATOM   552  C CB    . GLU A 1 75  ? 95.204  77.685  135.183 1.00 78.89  ? 75  GLU A CB    1 
ATOM   553  C CG    . GLU A 1 75  ? 95.906  77.531  136.519 1.00 78.89  ? 75  GLU A CG    1 
ATOM   554  C CD    . GLU A 1 75  ? 95.107  76.709  137.495 1.00 78.89  ? 75  GLU A CD    1 
ATOM   555  O OE1   . GLU A 1 75  ? 93.999  76.295  137.148 1.00 78.89  ? 75  GLU A OE1   1 
ATOM   556  O OE2   . GLU A 1 75  ? 95.587  76.474  138.604 1.00 78.89  ? 75  GLU A OE2   1 
ATOM   557  N N     . LYS A 1 76  ? 94.316  79.160  132.550 1.00 56.43  ? 76  LYS A N     1 
ATOM   558  C CA    . LYS A 1 76  ? 93.606  78.928  131.302 1.00 56.43  ? 76  LYS A CA    1 
ATOM   559  C C     . LYS A 1 76  ? 94.391  79.425  130.103 1.00 56.43  ? 76  LYS A C     1 
ATOM   560  O O     . LYS A 1 76  ? 94.572  78.687  129.131 1.00 56.43  ? 76  LYS A O     1 
ATOM   561  C CB    . LYS A 1 76  ? 92.221  79.550  131.331 1.00 84.64  ? 76  LYS A CB    1 
ATOM   562  C CG    . LYS A 1 76  ? 91.249  78.851  132.266 1.00 84.64  ? 76  LYS A CG    1 
ATOM   563  C CD    . LYS A 1 76  ? 89.885  79.541  132.256 1.00 84.64  ? 76  LYS A CD    1 
ATOM   564  C CE    . LYS A 1 76  ? 88.918  78.876  133.225 1.00 84.64  ? 76  LYS A CE    1 
ATOM   565  N NZ    . LYS A 1 76  ? 87.602  79.565  133.251 1.00 84.64  ? 76  LYS A NZ    1 
ATOM   566  N N     . PHE A 1 77  ? 94.848  80.673  130.125 1.00 57.30  ? 77  PHE A N     1 
ATOM   567  C CA    . PHE A 1 77  ? 95.729  81.097  129.055 1.00 57.30  ? 77  PHE A CA    1 
ATOM   568  C C     . PHE A 1 77  ? 96.924  80.191  129.074 1.00 57.30  ? 77  PHE A C     1 
ATOM   569  O O     . PHE A 1 77  ? 97.323  79.649  128.051 1.00 57.30  ? 77  PHE A O     1 
ATOM   570  C CB    . PHE A 1 77  ? 96.148  82.549  129.238 1.00 79.95  ? 77  PHE A CB    1 
ATOM   571  C CG    . PHE A 1 77  ? 95.007  83.508  129.202 1.00 79.95  ? 77  PHE A CG    1 
ATOM   572  C CD1   . PHE A 1 77  ? 94.541  84.023  128.046 1.00 79.95  ? 77  PHE A CD1   1 
ATOM   573  C CD2   . PHE A 1 77  ? 94.362  83.833  130.310 1.00 79.95  ? 77  PHE A CD2   1 
ATOM   574  C CE1   . PHE A 1 77  ? 93.483  84.901  128.066 1.00 79.95  ? 77  PHE A CE1   1 
ATOM   575  C CE2   . PHE A 1 77  ? 93.230  84.689  130.314 1.00 79.95  ? 77  PHE A CE2   1 
ATOM   576  C CZ    . PHE A 1 77  ? 92.861  85.244  129.186 1.00 79.95  ? 77  PHE A CZ    1 
ATOM   577  N N     . GLY A 1 78  ? 97.473  79.974  130.252 1.00 52.55  ? 78  GLY A N     1 
ATOM   578  C CA    . GLY A 1 78  ? 98.583  79.071  130.440 1.00 52.55  ? 78  GLY A CA    1 
ATOM   579  C C     . GLY A 1 78  ? 99.939  79.763  130.453 1.00 52.55  ? 78  GLY A C     1 
ATOM   580  O O     . GLY A 1 78  ? 100.049 80.993  130.473 1.00 52.55  ? 78  GLY A O     1 
ATOM   581  N N     . THR A 1 79  ? 100.996 78.931  130.364 1.00 54.82  ? 79  THR A N     1 
ATOM   582  C CA    . THR A 1 79  ? 102.400 79.320  130.561 1.00 54.82  ? 79  THR A CA    1 
ATOM   583  C C     . THR A 1 79  ? 102.934 80.217  129.462 1.00 54.82  ? 79  THR A C     1 
ATOM   584  O O     . THR A 1 79  ? 104.055 80.726  129.565 1.00 54.82  ? 79  THR A O     1 
ATOM   585  C CB    . THR A 1 79  ? 103.265 78.072  130.689 1.00 76.75  ? 79  THR A CB    1 
ATOM   586  O OG1   . THR A 1 79  ? 103.093 77.239  129.537 1.00 76.75  ? 79  THR A OG1   1 
ATOM   587  C CG2   . THR A 1 79  ? 102.845 77.299  131.915 1.00 76.75  ? 79  THR A CG2   1 
ATOM   588  N N     . LEU A 1 80  ? 102.133 80.411  128.430 1.00 52.54  ? 80  LEU A N     1 
ATOM   589  C CA    . LEU A 1 80  ? 102.443 81.335  127.360 1.00 52.54  ? 80  LEU A CA    1 
ATOM   590  C C     . LEU A 1 80  ? 102.589 82.751  127.869 1.00 52.54  ? 80  LEU A C     1 
ATOM   591  O O     . LEU A 1 80  ? 103.397 83.499  127.340 1.00 52.54  ? 80  LEU A O     1 
ATOM   592  C CB    . LEU A 1 80  ? 101.341 81.303  126.304 1.00 77.79  ? 80  LEU A CB    1 
ATOM   593  C CG    . LEU A 1 80  ? 101.482 82.173  125.044 1.00 77.79  ? 80  LEU A CG    1 
ATOM   594  C CD1   . LEU A 1 80  ? 102.721 81.752  124.207 1.00 77.79  ? 80  LEU A CD1   1 
ATOM   595  C CD2   . LEU A 1 80  ? 100.177 82.107  124.216 1.00 77.79  ? 80  LEU A CD2   1 
ATOM   596  N N     . PHE A 1 81  ? 101.719 83.229  128.745 1.00 50.74  ? 81  PHE A N     1 
ATOM   597  C CA    . PHE A 1 81  ? 101.915 84.607  129.180 1.00 50.74  ? 81  PHE A CA    1 
ATOM   598  C C     . PHE A 1 81  ? 102.698 84.575  130.497 1.00 50.74  ? 81  PHE A C     1 
ATOM   599  O O     . PHE A 1 81  ? 102.231 84.013  131.479 1.00 50.74  ? 81  PHE A O     1 
ATOM   600  C CB    . PHE A 1 81  ? 100.633 85.416  129.338 1.00 70.80  ? 81  PHE A CB    1 
ATOM   601  C CG    . PHE A 1 81  ? 99.671  85.315  128.231 1.00 70.80  ? 81  PHE A CG    1 
ATOM   602  C CD1   . PHE A 1 81  ? 100.008 84.775  127.009 1.00 70.80  ? 81  PHE A CD1   1 
ATOM   603  C CD2   . PHE A 1 81  ? 98.403  85.791  128.413 1.00 70.80  ? 81  PHE A CD2   1 
ATOM   604  C CE1   . PHE A 1 81  ? 99.077  84.690  125.999 1.00 70.80  ? 81  PHE A CE1   1 
ATOM   605  C CE2   . PHE A 1 81  ? 97.468  85.716  127.415 1.00 70.80  ? 81  PHE A CE2   1 
ATOM   606  C CZ    . PHE A 1 81  ? 97.800  85.160  126.206 1.00 70.80  ? 81  PHE A CZ    1 
ATOM   607  N N     . ASP A 1 82  ? 103.879 85.179  130.527 1.00 57.15  ? 82  ASP A N     1 
ATOM   608  C CA    . ASP A 1 82  ? 104.805 85.097  131.658 1.00 57.15  ? 82  ASP A CA    1 
ATOM   609  C C     . ASP A 1 82  ? 104.116 85.613  132.905 1.00 57.15  ? 82  ASP A C     1 
ATOM   610  O O     . ASP A 1 82  ? 103.843 86.809  132.991 1.00 57.15  ? 82  ASP A O     1 
ATOM   611  C CB    . ASP A 1 82  ? 106.086 85.906  131.376 1.00 73.48  ? 82  ASP A CB    1 
ATOM   612  C CG    . ASP A 1 82  ? 107.168 85.753  132.472 1.00 73.48  ? 82  ASP A CG    1 
ATOM   613  O OD1   . ASP A 1 82  ? 106.834 85.631  133.665 1.00 73.48  ? 82  ASP A OD1   1 
ATOM   614  O OD2   . ASP A 1 82  ? 108.370 85.750  132.142 1.00 73.48  ? 82  ASP A OD2   1 
ATOM   615  N N     . PRO A 1 83  ? 103.928 84.766  133.916 1.00 53.65  ? 83  PRO A N     1 
ATOM   616  C CA    . PRO A 1 83  ? 103.125 85.086  135.101 1.00 53.65  ? 83  PRO A CA    1 
ATOM   617  C C     . PRO A 1 83  ? 103.667 86.228  135.916 1.00 53.65  ? 83  PRO A C     1 
ATOM   618  O O     . PRO A 1 83  ? 102.935 86.798  136.735 1.00 53.65  ? 83  PRO A O     1 
ATOM   619  C CB    . PRO A 1 83  ? 103.174 83.776  135.893 1.00 354.25 ? 83  PRO A CB    1 
ATOM   620  C CG    . PRO A 1 83  ? 104.431 83.121  135.434 1.00 354.25 ? 83  PRO A CG    1 
ATOM   621  C CD    . PRO A 1 83  ? 104.558 83.460  133.998 1.00 354.25 ? 83  PRO A CD    1 
ATOM   622  N N     . LYS A 1 84  ? 104.929 86.591  135.715 1.00 53.57  ? 84  LYS A N     1 
ATOM   623  C CA    . LYS A 1 84  ? 105.485 87.711  136.450 1.00 53.57  ? 84  LYS A CA    1 
ATOM   624  C C     . LYS A 1 84  ? 104.868 89.023  136.000 1.00 53.57  ? 84  LYS A C     1 
ATOM   625  O O     . LYS A 1 84  ? 104.988 90.036  136.699 1.00 53.57  ? 84  LYS A O     1 
ATOM   626  C CB    . LYS A 1 84  ? 106.992 87.758  136.271 1.00 80.35  ? 84  LYS A CB    1 
ATOM   627  C CG    . LYS A 1 84  ? 107.731 86.566  136.850 1.00 80.35  ? 84  LYS A CG    1 
ATOM   628  C CD    . LYS A 1 84  ? 109.276 86.733  136.758 1.00 80.35  ? 84  LYS A CD    1 
ATOM   629  C CE    . LYS A 1 84  ? 109.777 86.789  135.303 1.00 80.35  ? 84  LYS A CE    1 
ATOM   630  N NZ    . LYS A 1 84  ? 109.439 85.553  134.553 1.00 80.35  ? 84  LYS A NZ    1 
ATOM   631  N N     . SER A 1 85  ? 104.199 89.010  134.848 1.00 51.14  ? 85  SER A N     1 
ATOM   632  C CA    . SER A 1 85  ? 103.530 90.159  134.264 1.00 51.14  ? 85  SER A CA    1 
ATOM   633  C C     . SER A 1 85  ? 102.066 90.234  134.647 1.00 51.14  ? 85  SER A C     1 
ATOM   634  O O     . SER A 1 85  ? 101.326 91.036  134.066 1.00 51.14  ? 85  SER A O     1 
ATOM   635  C CB    . SER A 1 85  ? 103.655 90.132  132.752 1.00 68.88  ? 85  SER A CB    1 
ATOM   636  O OG    . SER A 1 85  ? 104.994 90.292  132.333 1.00 68.88  ? 85  SER A OG    1 
ATOM   637  N N     . ILE A 1 86  ? 101.615 89.403  135.588 1.00 52.05  ? 86  ILE A N     1 
ATOM   638  C CA    . ILE A 1 86  ? 100.249 89.511  136.068 1.00 52.05  ? 86  ILE A CA    1 
ATOM   639  C C     . ILE A 1 86  ? 100.232 90.385  137.298 1.00 52.05  ? 86  ILE A C     1 
ATOM   640  O O     . ILE A 1 86  ? 100.932 90.128  138.285 1.00 52.05  ? 86  ILE A O     1 
ATOM   641  C CB    . ILE A 1 86  ? 99.611  88.151  136.376 1.00 77.06  ? 86  ILE A CB    1 
ATOM   642  C CG1   . ILE A 1 86  ? 99.598  87.277  135.121 1.00 77.06  ? 86  ILE A CG1   1 
ATOM   643  C CG2   . ILE A 1 86  ? 98.148  88.384  136.906 1.00 77.06  ? 86  ILE A CG2   1 
ATOM   644  C CD1   . ILE A 1 86  ? 99.169  85.837  135.336 1.00 77.06  ? 86  ILE A CD1   1 
ATOM   645  N N     . VAL A 1 87  ? 99.400  91.406  137.238 1.00 51.13  ? 87  VAL A N     1 
ATOM   646  C CA    . VAL A 1 87  ? 99.230  92.387  138.291 1.00 51.13  ? 87  VAL A CA    1 
ATOM   647  C C     . VAL A 1 87  ? 97.811  92.311  138.796 1.00 51.13  ? 87  VAL A C     1 
ATOM   648  O O     . VAL A 1 87  ? 96.867  92.355  138.003 1.00 51.13  ? 87  VAL A O     1 
ATOM   649  C CB    . VAL A 1 87  ? 99.490  93.794  137.765 1.00 74.37  ? 87  VAL A CB    1 
ATOM   650  C CG1   . VAL A 1 87  ? 99.289  94.797  138.877 1.00 74.37  ? 87  VAL A CG1   1 
ATOM   651  C CG2   . VAL A 1 87  ? 100.858 93.852  137.177 1.00 74.37  ? 87  VAL A CG2   1 
ATOM   652  N N     . SER A 1 88  ? 97.650  92.245  140.107 1.00 51.25  ? 88  SER A N     1 
ATOM   653  C CA    . SER A 1 88  ? 96.320  92.192  140.667 1.00 51.25  ? 88  SER A CA    1 
ATOM   654  C C     . SER A 1 88  ? 96.277  92.937  141.985 1.00 51.25  ? 88  SER A C     1 
ATOM   655  O O     . SER A 1 88  ? 97.310  93.210  142.600 1.00 51.25  ? 88  SER A O     1 
ATOM   656  C CB    . SER A 1 88  ? 95.882  90.756  140.867 1.00 69.03  ? 88  SER A CB    1 
ATOM   657  O OG    . SER A 1 88  ? 96.721  90.097  141.794 1.00 69.03  ? 88  SER A OG    1 
ATOM   658  N N     . GLY A 1 89  ? 95.063  93.289  142.405 1.00 52.54  ? 89  GLY A N     1 
ATOM   659  C CA    . GLY A 1 89  ? 94.855  94.009  143.641 1.00 52.54  ? 89  GLY A CA    1 
ATOM   660  C C     . GLY A 1 89  ? 94.360  93.132  144.780 1.00 52.54  ? 89  GLY A C     1 
ATOM   661  O O     . GLY A 1 89  ? 94.246  91.911  144.670 1.00 52.54  ? 89  GLY A O     1 
ATOM   662  N N     . ALA A 1 90  ? 94.062  93.794  145.904 1.00 49.59  ? 90  ALA A N     1 
ATOM   663  C CA    . ALA A 1 90  ? 93.565  93.113  147.094 1.00 49.59  ? 90  ALA A CA    1 
ATOM   664  C C     . ALA A 1 90  ? 92.100  92.746  146.969 1.00 49.59  ? 90  ALA A C     1 
ATOM   665  O O     . ALA A 1 90  ? 91.649  91.770  147.575 1.00 49.59  ? 90  ALA A O     1 
ATOM   666  C CB    . ALA A 1 90  ? 93.761  93.995  148.322 1.00 67.62  ? 90  ALA A CB    1 
ATOM   667  N N     . ASP A 1 91  ? 91.349  93.525  146.212 1.00 53.79  ? 91  ASP A N     1 
ATOM   668  C CA    . ASP A 1 91  ? 89.927  93.321  146.080 1.00 53.79  ? 91  ASP A CA    1 
ATOM   669  C C     . ASP A 1 91  ? 89.538  93.800  144.704 1.00 53.79  ? 91  ASP A C     1 
ATOM   670  O O     . ASP A 1 91  ? 90.367  94.320  143.962 1.00 53.79  ? 91  ASP A O     1 
ATOM   671  C CB    . ASP A 1 91  ? 89.188  94.079  147.182 1.00 69.16  ? 91  ASP A CB    1 
ATOM   672  C CG    . ASP A 1 91  ? 87.829  93.507  147.507 1.00 69.16  ? 91  ASP A CG    1 
ATOM   673  O OD1   . ASP A 1 91  ? 87.235  92.838  146.659 1.00 69.16  ? 91  ASP A OD1   1 
ATOM   674  O OD2   . ASP A 1 91  ? 87.348  93.744  148.619 1.00 69.16  ? 91  ASP A OD2   1 
ATOM   675  N N     . GLY A 1 92  ? 88.270  93.653  144.379 1.00 54.14  ? 92  GLY A N     1 
ATOM   676  C CA    . GLY A 1 92  ? 87.761  94.053  143.091 1.00 54.14  ? 92  GLY A CA    1 
ATOM   677  C C     . GLY A 1 92  ? 86.941  95.314  143.143 1.00 54.14  ? 92  GLY A C     1 
ATOM   678  O O     . GLY A 1 92  ? 87.197  96.219  143.940 1.00 54.14  ? 92  GLY A O     1 
ATOM   679  N N     . ALA A 1 93  ? 85.954  95.375  142.263 1.00 55.02  ? 93  ALA A N     1 
ATOM   680  C CA    . ALA A 1 93  ? 85.075  96.517  142.125 1.00 55.02  ? 93  ALA A CA    1 
ATOM   681  C C     . ALA A 1 93  ? 83.777  96.003  141.560 1.00 55.02  ? 93  ALA A C     1 
ATOM   682  O O     . ALA A 1 93  ? 83.770  95.026  140.823 1.00 55.02  ? 93  ALA A O     1 
ATOM   683  C CB    . ALA A 1 93  ? 85.673  97.572  141.195 1.00 75.03  ? 93  ALA A CB    1 
ATOM   684  N N     . GLY A 1 94  ? 82.682  96.657  141.878 1.00 58.08  ? 94  GLY A N     1 
ATOM   685  C CA    . GLY A 1 94  ? 81.442  96.321  141.229 1.00 58.08  ? 94  GLY A CA    1 
ATOM   686  C C     . GLY A 1 94  ? 81.477  97.049  139.923 1.00 58.08  ? 94  GLY A C     1 
ATOM   687  O O     . GLY A 1 94  ? 82.462  97.697  139.596 1.00 58.08  ? 94  GLY A O     1 
ATOM   688  N N     . ASN A 1 95  ? 80.387  97.008  139.176 1.00 57.42  ? 95  ASN A N     1 
ATOM   689  C CA    . ASN A 1 95  ? 80.460  97.672  137.880 1.00 57.42  ? 95  ASN A CA    1 
ATOM   690  C C     . ASN A 1 95  ? 80.161  99.160  138.012 1.00 57.42  ? 95  ASN A C     1 
ATOM   691  O O     . ASN A 1 95  ? 79.128  99.682  137.588 1.00 57.42  ? 95  ASN A O     1 
ATOM   692  C CB    . ASN A 1 95  ? 79.585  96.971  136.876 1.00 77.79  ? 95  ASN A CB    1 
ATOM   693  C CG    . ASN A 1 95  ? 80.169  95.642  136.504 1.00 77.79  ? 95  ASN A CG    1 
ATOM   694  O OD1   . ASN A 1 95  ? 81.394  95.492  136.288 1.00 77.79  ? 95  ASN A OD1   1 
ATOM   695  N ND2   . ASN A 1 95  ? 79.314  94.647  136.458 1.00 77.79  ? 95  ASN A ND2   1 
ATOM   696  N N     . ASN A 1 96  ? 81.144  99.833  138.596 1.00 61.74  ? 96  ASN A N     1 
ATOM   697  C CA    . ASN A 1 96  ? 81.129  101.259 138.836 1.00 61.74  ? 96  ASN A CA    1 
ATOM   698  C C     . ASN A 1 96  ? 82.475  101.804 138.439 1.00 61.74  ? 96  ASN A C     1 
ATOM   699  O O     . ASN A 1 96  ? 83.486  101.561 139.103 1.00 61.74  ? 96  ASN A O     1 
ATOM   700  C CB    . ASN A 1 96  ? 80.850  101.599 140.270 1.00 83.65  ? 96  ASN A CB    1 
ATOM   701  C CG    . ASN A 1 96  ? 80.799  103.086 140.481 1.00 83.65  ? 96  ASN A CG    1 
ATOM   702  O OD1   . ASN A 1 96  ? 80.957  103.884 139.538 1.00 83.65  ? 96  ASN A OD1   1 
ATOM   703  N ND2   . ASN A 1 96  ? 80.570  103.478 141.714 1.00 83.65  ? 96  ASN A ND2   1 
ATOM   704  N N     . PHE A 1 97  ? 82.441  102.568 137.367 1.00 60.40  ? 97  PHE A N     1 
ATOM   705  C CA    . PHE A 1 97  ? 83.623  103.168 136.823 1.00 60.40  ? 97  PHE A CA    1 
ATOM   706  C C     . PHE A 1 97  ? 84.363  103.906 137.885 1.00 60.40  ? 97  PHE A C     1 
ATOM   707  O O     . PHE A 1 97  ? 85.587  103.866 137.940 1.00 60.40  ? 97  PHE A O     1 
ATOM   708  C CB    . PHE A 1 97  ? 83.208  104.115 135.740 1.00 84.28  ? 97  PHE A CB    1 
ATOM   709  C CG    . PHE A 1 97  ? 84.327  104.820 135.114 1.00 84.28  ? 97  PHE A CG    1 
ATOM   710  C CD1   . PHE A 1 97  ? 85.016  104.227 134.092 1.00 84.28  ? 97  PHE A CD1   1 
ATOM   711  C CD2   . PHE A 1 97  ? 84.692  106.083 135.525 1.00 84.28  ? 97  PHE A CD2   1 
ATOM   712  C CE1   . PHE A 1 97  ? 86.046  104.872 133.491 1.00 84.28  ? 97  PHE A CE1   1 
ATOM   713  C CE2   . PHE A 1 97  ? 85.734  106.736 134.920 1.00 84.28  ? 97  PHE A CE2   1 
ATOM   714  C CZ    . PHE A 1 97  ? 86.409  106.129 133.901 1.00 84.28  ? 97  PHE A CZ    1 
ATOM   715  N N     . ALA A 1 98  ? 83.627  104.608 138.722 1.00 61.80  ? 98  ALA A N     1 
ATOM   716  C CA    . ALA A 1 98  ? 84.248  105.400 139.760 1.00 61.80  ? 98  ALA A CA    1 
ATOM   717  C C     . ALA A 1 98  ? 85.058  104.533 140.692 1.00 61.80  ? 98  ALA A C     1 
ATOM   718  O O     . ALA A 1 98  ? 86.088  104.978 141.201 1.00 61.80  ? 98  ALA A O     1 
ATOM   719  C CB    . ALA A 1 98  ? 83.191  106.162 140.548 1.00 84.27  ? 98  ALA A CB    1 
ATOM   720  N N     . ILE A 1 99  ? 84.628  103.306 140.957 1.00 63.66  ? 99  ILE A N     1 
ATOM   721  C CA    . ILE A 1 99  ? 85.428  102.557 141.890 1.00 63.66  ? 99  ILE A CA    1 
ATOM   722  C C     . ILE A 1 99  ? 86.737  102.252 141.262 1.00 63.66  ? 99  ILE A C     1 
ATOM   723  O O     . ILE A 1 99  ? 87.781  102.404 141.876 1.00 63.66  ? 99  ILE A O     1 
ATOM   724  C CB    . ILE A 1 99  ? 84.777  101.255 142.332 1.00 94.25  ? 99  ILE A CB    1 
ATOM   725  C CG1   . ILE A 1 99  ? 83.523  101.533 143.112 1.00 94.25  ? 99  ILE A CG1   1 
ATOM   726  C CG2   . ILE A 1 99  ? 85.801  100.482 143.206 1.00 94.25  ? 99  ILE A CG2   1 
ATOM   727  C CD1   . ILE A 1 99  ? 82.684  100.294 143.361 1.00 94.25  ? 99  ILE A CD1   1 
ATOM   728  N N     . GLY A 1 100 ? 86.723  101.782 140.033 1.00 61.63  ? 100 GLY A N     1 
ATOM   729  C CA    . GLY A 1 100 ? 88.002  101.438 139.444 1.00 61.63  ? 100 GLY A CA    1 
ATOM   730  C C     . GLY A 1 100 ? 88.854  102.651 139.115 1.00 61.63  ? 100 GLY A C     1 
ATOM   731  O O     . GLY A 1 100 ? 90.085  102.582 139.153 1.00 61.63  ? 100 GLY A O     1 
ATOM   732  N N     . PHE A 1 101 ? 88.224  103.779 138.821 1.00 61.94  ? 101 PHE A N     1 
ATOM   733  C CA    . PHE A 1 101 ? 88.928  104.954 138.341 1.00 61.94  ? 101 PHE A CA    1 
ATOM   734  C C     . PHE A 1 101 ? 89.369  105.979 139.397 1.00 61.94  ? 101 PHE A C     1 
ATOM   735  O O     . PHE A 1 101 ? 90.443  106.567 139.256 1.00 61.94  ? 101 PHE A O     1 
ATOM   736  C CB    . PHE A 1 101 ? 88.064  105.664 137.346 1.00 86.43  ? 101 PHE A CB    1 
ATOM   737  C CG    . PHE A 1 101 ? 88.748  106.756 136.723 1.00 86.43  ? 101 PHE A CG    1 
ATOM   738  C CD1   . PHE A 1 101 ? 89.672  106.515 135.759 1.00 86.43  ? 101 PHE A CD1   1 
ATOM   739  C CD2   . PHE A 1 101 ? 88.493  108.026 137.093 1.00 86.43  ? 101 PHE A CD2   1 
ATOM   740  C CE1   . PHE A 1 101 ? 90.320  107.533 135.153 1.00 86.43  ? 101 PHE A CE1   1 
ATOM   741  C CE2   . PHE A 1 101 ? 89.132  109.047 136.503 1.00 86.43  ? 101 PHE A CE2   1 
ATOM   742  C CZ    . PHE A 1 101 ? 90.054  108.806 135.530 1.00 86.43  ? 101 PHE A CZ    1 
ATOM   743  N N     . ASN A 1 102 ? 88.561  106.276 140.422 1.00 63.46  ? 102 ASN A N     1 
ATOM   744  C CA    . ASN A 1 102 ? 88.862  107.383 141.351 1.00 63.46  ? 102 ASN A CA    1 
ATOM   745  C C     . ASN A 1 102 ? 89.505  106.970 142.680 1.00 63.46  ? 102 ASN A C     1 
ATOM   746  O O     . ASN A 1 102 ? 88.802  106.644 143.636 1.00 63.46  ? 102 ASN A O     1 
ATOM   747  C CB    . ASN A 1 102 ? 87.603  108.143 141.716 1.00 85.98  ? 102 ASN A CB    1 
ATOM   748  C CG    . ASN A 1 102 ? 87.001  108.900 140.601 1.00 85.98  ? 102 ASN A CG    1 
ATOM   749  O OD1   . ASN A 1 102 ? 87.663  109.560 139.806 1.00 85.98  ? 102 ASN A OD1   1 
ATOM   750  N ND2   . ASN A 1 102 ? 85.700  108.857 140.572 1.00 85.98  ? 102 ASN A ND2   1 
ATOM   751  N N     . GLU A 1 103 ? 90.826  107.103 142.783 1.00 67.94  ? 103 GLU A N     1 
ATOM   752  C CA    . GLU A 1 103 ? 91.577  106.842 144.025 1.00 67.94  ? 103 GLU A CA    1 
ATOM   753  C C     . GLU A 1 103 ? 91.370  105.447 144.616 1.00 67.94  ? 103 GLU A C     1 
ATOM   754  O O     . GLU A 1 103 ? 91.283  105.286 145.835 1.00 67.94  ? 103 GLU A O     1 
ATOM   755  C CB    . GLU A 1 103 ? 91.251  107.885 145.099 1.00 91.26  ? 103 GLU A CB    1 
ATOM   756  C CG    . GLU A 1 103 ? 91.617  109.316 144.723 1.00 91.26  ? 103 GLU A CG    1 
ATOM   757  C CD    . GLU A 1 103 ? 91.405  110.313 145.851 1.00 91.26  ? 103 GLU A CD    1 
ATOM   758  O OE1   . GLU A 1 103 ? 90.828  109.952 146.880 1.00 91.26  ? 103 GLU A OE1   1 
ATOM   759  O OE2   . GLU A 1 103 ? 91.823  111.464 145.701 1.00 91.26  ? 103 GLU A OE2   1 
ATOM   760  N N     . HIS A 1 104 ? 91.361  104.427 143.774 1.00 70.64  ? 104 HIS A N     1 
ATOM   761  C CA    . HIS A 1 104 ? 91.229  103.061 144.248 1.00 70.64  ? 104 HIS A CA    1 
ATOM   762  C C     . HIS A 1 104 ? 92.306  102.195 143.630 1.00 70.64  ? 104 HIS A C     1 
ATOM   763  O O     . HIS A 1 104 ? 92.658  102.350 142.461 1.00 70.64  ? 104 HIS A O     1 
ATOM   764  C CB    . HIS A 1 104 ? 89.888  102.440 143.891 1.00 96.07  ? 104 HIS A CB    1 
ATOM   765  C CG    . HIS A 1 104 ? 88.705  102.984 144.631 1.00 96.07  ? 104 HIS A CG    1 
ATOM   766  N ND1   . HIS A 1 104 ? 88.331  102.520 145.874 1.00 96.07  ? 104 HIS A ND1   1 
ATOM   767  C CD2   . HIS A 1 104 ? 87.776  103.902 144.282 1.00 96.07  ? 104 HIS A CD2   1 
ATOM   768  C CE1   . HIS A 1 104 ? 87.236  103.144 146.268 1.00 96.07  ? 104 HIS A CE1   1 
ATOM   769  N NE2   . HIS A 1 104 ? 86.878  103.987 145.321 1.00 96.07  ? 104 HIS A NE2   1 
ATOM   770  N N     . GLY A 1 105 ? 92.811  101.269 144.421 1.00 65.65  ? 105 GLY A N     1 
ATOM   771  C CA    . GLY A 1 105 ? 93.813  100.385 143.896 1.00 65.65  ? 105 GLY A CA    1 
ATOM   772  C C     . GLY A 1 105 ? 95.102  101.113 143.628 1.00 65.65  ? 105 GLY A C     1 
ATOM   773  O O     . GLY A 1 105 ? 95.840  100.723 142.730 1.00 65.65  ? 105 GLY A O     1 
ATOM   774  N N     . ALA A 1 106 ? 95.403  102.163 144.397 1.00 66.19  ? 106 ALA A N     1 
ATOM   775  C CA    . ALA A 1 106 ? 96.591  102.970 144.133 1.00 66.19  ? 106 ALA A CA    1 
ATOM   776  C C     . ALA A 1 106 ? 97.848  102.138 144.154 1.00 66.19  ? 106 ALA A C     1 
ATOM   777  O O     . ALA A 1 106 ? 98.756  102.330 143.340 1.00 66.19  ? 106 ALA A O     1 
ATOM   778  C CB    . ALA A 1 106 ? 96.705  104.074 145.163 1.00 90.26  ? 106 ALA A CB    1 
ATOM   779  N N     . GLU A 1 107 ? 97.906  101.207 145.071 1.00 66.47  ? 107 GLU A N     1 
ATOM   780  C CA    . GLU A 1 107 ? 99.041  100.321 145.166 1.00 66.47  ? 107 GLU A CA    1 
ATOM   781  C C     . GLU A 1 107 ? 99.065  99.378  143.980 1.00 66.47  ? 107 GLU A C     1 
ATOM   782  O O     . GLU A 1 107 ? 100.131 99.055  143.432 1.00 66.47  ? 107 GLU A O     1 
ATOM   783  C CB    . GLU A 1 107 ? 98.930  99.570  146.481 1.00 89.29  ? 107 GLU A CB    1 
ATOM   784  C CG    . GLU A 1 107 ? 98.988  100.498 147.691 1.00 89.29  ? 107 GLU A CG    1 
ATOM   785  C CD    . GLU A 1 107 ? 97.700  101.266 147.925 1.00 89.29  ? 107 GLU A CD    1 
ATOM   786  O OE1   . GLU A 1 107 ? 96.687  100.934 147.309 1.00 89.29  ? 107 GLU A OE1   1 
ATOM   787  O OE2   . GLU A 1 107 ? 97.713  102.209 148.712 1.00 89.29  ? 107 GLU A OE2   1 
ATOM   788  N N     . THR A 1 108 ? 97.877  98.945  143.572 1.00 64.90  ? 108 THR A N     1 
ATOM   789  C CA    . THR A 1 108 ? 97.762  98.069  142.432 1.00 64.90  ? 108 THR A CA    1 
ATOM   790  C C     . THR A 1 108 ? 98.265  98.786  141.215 1.00 64.90  ? 108 THR A C     1 
ATOM   791  O O     . THR A 1 108 ? 99.021  98.220  140.430 1.00 64.90  ? 108 THR A O     1 
ATOM   792  C CB    . THR A 1 108 ? 96.310  97.617  142.225 1.00 90.86  ? 108 THR A CB    1 
ATOM   793  O OG1   . THR A 1 108 ? 95.836  96.955  143.404 1.00 90.86  ? 108 THR A OG1   1 
ATOM   794  C CG2   . THR A 1 108 ? 96.221  96.628  141.048 1.00 90.86  ? 108 THR A CG2   1 
ATOM   795  N N     . LEU A 1 109 ? 97.872  100.049 141.072 1.00 63.82  ? 109 LEU A N     1 
ATOM   796  C CA    . LEU A 1 109 ? 98.241  100.866 139.927 1.00 63.82  ? 109 LEU A CA    1 
ATOM   797  C C     . LEU A 1 109 ? 99.728  101.109 139.888 1.00 63.82  ? 109 LEU A C     1 
ATOM   798  O O     . LEU A 1 109 ? 100.331 101.103 138.809 1.00 63.82  ? 109 LEU A O     1 
ATOM   799  C CB    . LEU A 1 109 ? 97.484  102.192 139.973 1.00 94.49  ? 109 LEU A CB    1 
ATOM   800  C CG    . LEU A 1 109 ? 95.979  102.115 139.666 1.00 94.49  ? 109 LEU A CG    1 
ATOM   801  C CD1   . LEU A 1 109 ? 95.292  103.385 140.110 1.00 94.49  ? 109 LEU A CD1   1 
ATOM   802  C CD2   . LEU A 1 109 ? 95.739  101.893 138.149 1.00 94.49  ? 109 LEU A CD2   1 
ATOM   803  N N     . GLU A 1 110 ? 100.343 101.319 141.037 1.00 65.24  ? 110 GLU A N     1 
ATOM   804  C CA    . GLU A 1 110 ? 101.778 101.439 140.983 1.00 65.24  ? 110 GLU A CA    1 
ATOM   805  C C     . GLU A 1 110 ? 102.358 100.178 140.410 1.00 65.24  ? 110 GLU A C     1 
ATOM   806  O O     . GLU A 1 110 ? 103.196 100.233 139.513 1.00 65.24  ? 110 GLU A O     1 
ATOM   807  C CB    . GLU A 1 110 ? 102.384 101.711 142.352 1.00 87.64  ? 110 GLU A CB    1 
ATOM   808  C CG    . GLU A 1 110 ? 103.900 101.924 142.272 1.00 87.64  ? 110 GLU A CG    1 
ATOM   809  C CD    . GLU A 1 110 ? 104.542 102.227 143.596 1.00 87.64  ? 110 GLU A CD    1 
ATOM   810  O OE1   . GLU A 1 110 ? 103.839 102.260 144.605 1.00 87.64  ? 110 GLU A OE1   1 
ATOM   811  O OE2   . GLU A 1 110 ? 105.755 102.437 143.622 1.00 87.64  ? 110 GLU A OE2   1 
ATOM   812  N N     . LYS A 1 111 ? 101.895 99.027  140.887 1.00 63.76  ? 111 LYS A N     1 
ATOM   813  C CA    . LYS A 1 111 ? 102.445 97.803  140.337 1.00 63.76  ? 111 LYS A CA    1 
ATOM   814  C C     . LYS A 1 111 ? 102.104 97.662  138.867 1.00 63.76  ? 111 LYS A C     1 
ATOM   815  O O     . LYS A 1 111 ? 102.925 97.150  138.099 1.00 63.76  ? 111 LYS A O     1 
ATOM   816  C CB    . LYS A 1 111 ? 101.988 96.558  141.089 1.00 95.64  ? 111 LYS A CB    1 
ATOM   817  C CG    . LYS A 1 111 ? 102.690 95.277  140.539 1.00 95.64  ? 111 LYS A CG    1 
ATOM   818  C CD    . LYS A 1 111 ? 102.405 93.996  141.330 1.00 95.64  ? 111 LYS A CD    1 
ATOM   819  C CE    . LYS A 1 111 ? 103.102 92.783  140.679 1.00 95.64  ? 111 LYS A CE    1 
ATOM   820  N NZ    . LYS A 1 111 ? 102.851 91.501  141.406 1.00 95.64  ? 111 LYS A NZ    1 
ATOM   821  N N     . VAL A 1 112 ? 100.907 98.097  138.450 1.00 63.02  ? 112 VAL A N     1 
ATOM   822  C CA    . VAL A 1 112 ? 100.558 97.972  137.045 1.00 63.02  ? 112 VAL A CA    1 
ATOM   823  C C     . VAL A 1 112 ? 101.583 98.684  136.240 1.00 63.02  ? 112 VAL A C     1 
ATOM   824  O O     . VAL A 1 112 ? 102.111 98.154  135.259 1.00 63.02  ? 112 VAL A O     1 
ATOM   825  C CB    . VAL A 1 112 ? 99.190  98.566  136.684 1.00 91.66  ? 112 VAL A CB    1 
ATOM   826  C CG1   . VAL A 1 112 ? 99.031  98.561  135.141 1.00 91.66  ? 112 VAL A CG1   1 
ATOM   827  C CG2   . VAL A 1 112 ? 98.062  97.793  137.273 1.00 91.66  ? 112 VAL A CG2   1 
ATOM   828  N N     . MET A 1 113 ? 101.878 99.899  136.632 1.00 64.16  ? 113 MET A N     1 
ATOM   829  C CA    . MET A 1 113 ? 102.800 100.621 135.810 1.00 64.16  ? 113 MET A CA    1 
ATOM   830  C C     . MET A 1 113 ? 104.207 100.100 135.956 1.00 64.16  ? 113 MET A C     1 
ATOM   831  O O     . MET A 1 113 ? 104.946 100.122 134.981 1.00 64.16  ? 113 MET A O     1 
ATOM   832  C CB    . MET A 1 113 ? 102.680 102.098 136.078 1.00 92.17  ? 113 MET A CB    1 
ATOM   833  C CG    . MET A 1 113 ? 101.348 102.622 135.548 1.00 92.17  ? 113 MET A CG    1 
ATOM   834  S SD    . MET A 1 113 ? 100.996 102.154 133.815 1.00 92.17  ? 113 MET A SD    1 
ATOM   835  C CE    . MET A 1 113 ? 102.245 103.040 132.883 1.00 92.17  ? 113 MET A CE    1 
ATOM   836  N N     . GLN A 1 114 ? 104.586 99.558  137.095 1.00 63.17  ? 114 GLN A N     1 
ATOM   837  C CA    . GLN A 1 114 ? 105.920 99.002  137.145 1.00 63.17  ? 114 GLN A CA    1 
ATOM   838  C C     . GLN A 1 114 ? 106.041 97.915  136.121 1.00 63.17  ? 114 GLN A C     1 
ATOM   839  O O     . GLN A 1 114 ? 107.052 97.806  135.419 1.00 63.17  ? 114 GLN A O     1 
ATOM   840  C CB    . GLN A 1 114 ? 106.223 98.424  138.505 1.00 88.26  ? 114 GLN A CB    1 
ATOM   841  C CG    . GLN A 1 114 ? 106.373 99.425  139.598 1.00 88.26  ? 114 GLN A CG    1 
ATOM   842  C CD    . GLN A 1 114 ? 106.442 98.749  140.941 1.00 88.26  ? 114 GLN A CD    1 
ATOM   843  O OE1   . GLN A 1 114 ? 106.098 97.572  141.062 1.00 88.26  ? 114 GLN A OE1   1 
ATOM   844  N NE2   . GLN A 1 114 ? 106.883 99.478  141.959 1.00 88.26  ? 114 GLN A NE2   1 
ATOM   845  N N     . VAL A 1 115 ? 105.008 97.121  135.994 1.00 59.40  ? 115 VAL A N     1 
ATOM   846  C CA    . VAL A 1 115 ? 105.072 96.062  135.023 1.00 59.40  ? 115 VAL A CA    1 
ATOM   847  C C     . VAL A 1 115 ? 105.051 96.621  133.614 1.00 59.40  ? 115 VAL A C     1 
ATOM   848  O O     . VAL A 1 115 ? 105.733 96.092  132.725 1.00 59.40  ? 115 VAL A O     1 
ATOM   849  C CB    . VAL A 1 115 ? 103.956 95.046  135.272 1.00 86.40  ? 115 VAL A CB    1 
ATOM   850  C CG1   . VAL A 1 115 ? 103.892 94.049  134.137 1.00 86.40  ? 115 VAL A CG1   1 
ATOM   851  C CG2   . VAL A 1 115 ? 104.271 94.320  136.565 1.00 86.40  ? 115 VAL A CG2   1 
ATOM   852  N N     . VAL A 1 116 ? 104.263 97.659  133.361 1.00 56.80  ? 116 VAL A N     1 
ATOM   853  C CA    . VAL A 1 116 ? 104.286 98.223  132.019 1.00 56.80  ? 116 VAL A CA    1 
ATOM   854  C C     . VAL A 1 116 ? 105.675 98.686  131.706 1.00 56.80  ? 116 VAL A C     1 
ATOM   855  O O     . VAL A 1 116 ? 106.196 98.454  130.613 1.00 56.80  ? 116 VAL A O     1 
ATOM   856  C CB    . VAL A 1 116 ? 103.309 99.395  131.845 1.00 82.62  ? 116 VAL A CB    1 
ATOM   857  C CG1   . VAL A 1 116 ? 103.535 100.076 130.465 1.00 82.62  ? 116 VAL A CG1   1 
ATOM   858  C CG2   . VAL A 1 116 ? 101.875 98.927  131.967 1.00 82.62  ? 116 VAL A CG2   1 
ATOM   859  N N     . GLU A 1 117 ? 106.293 99.339  132.659 1.00 59.70  ? 117 GLU A N     1 
ATOM   860  C CA    . GLU A 1 117 ? 107.617 99.859  132.453 1.00 59.70  ? 117 GLU A CA    1 
ATOM   861  C C     . GLU A 1 117 ? 108.591 98.738  132.151 1.00 59.70  ? 117 GLU A C     1 
ATOM   862  O O     . GLU A 1 117 ? 109.496 98.921  131.341 1.00 59.70  ? 117 GLU A O     1 
ATOM   863  C CB    . GLU A 1 117 ? 108.054 100.671 133.670 1.00 80.19  ? 117 GLU A CB    1 
ATOM   864  C CG    . GLU A 1 117 ? 107.310 102.016 133.856 1.00 80.19  ? 117 GLU A CG    1 
ATOM   865  C CD    . GLU A 1 117 ? 107.649 102.696 135.174 1.00 80.19  ? 117 GLU A CD    1 
ATOM   866  O OE1   . GLU A 1 117 ? 108.365 102.085 135.967 1.00 80.19  ? 117 GLU A OE1   1 
ATOM   867  O OE2   . GLU A 1 117 ? 107.202 103.826 135.420 1.00 80.19  ? 117 GLU A OE2   1 
ATOM   868  N N     . GLN A 1 118 ? 108.439 97.573  132.794 1.00 60.91  ? 118 GLN A N     1 
ATOM   869  C CA    . GLN A 1 118 ? 109.344 96.463  132.482 1.00 60.91  ? 118 GLN A CA    1 
ATOM   870  C C     . GLN A 1 118 ? 109.182 96.034  131.056 1.00 60.91  ? 118 GLN A C     1 
ATOM   871  O O     . GLN A 1 118 ? 110.167 95.793  130.361 1.00 60.91  ? 118 GLN A O     1 
ATOM   872  C CB    . GLN A 1 118 ? 109.098 95.231  133.336 1.00 85.11  ? 118 GLN A CB    1 
ATOM   873  C CG    . GLN A 1 118 ? 109.438 95.332  134.783 1.00 85.11  ? 118 GLN A CG    1 
ATOM   874  C CD    . GLN A 1 118 ? 109.027 94.074  135.555 1.00 85.11  ? 118 GLN A CD    1 
ATOM   875  O OE1   . GLN A 1 118 ? 108.902 92.972  134.990 1.00 85.11  ? 118 GLN A OE1   1 
ATOM   876  N NE2   . GLN A 1 118 ? 108.803 94.241  136.854 1.00 85.11  ? 118 GLN A NE2   1 
ATOM   877  N N     . ARG A 1 119 ? 107.948 95.937  130.590 1.00 61.56  ? 119 ARG A N     1 
ATOM   878  C CA    . ARG A 1 119 ? 107.809 95.482  129.225 1.00 61.56  ? 119 ARG A CA    1 
ATOM   879  C C     . ARG A 1 119 ? 108.377 96.505  128.267 1.00 61.56  ? 119 ARG A C     1 
ATOM   880  O O     . ARG A 1 119 ? 108.902 96.141  127.210 1.00 61.56  ? 119 ARG A O     1 
ATOM   881  C CB    . ARG A 1 119 ? 106.364 95.177  128.889 1.00 90.45  ? 119 ARG A CB    1 
ATOM   882  C CG    . ARG A 1 119 ? 105.755 94.061  129.745 1.00 90.45  ? 119 ARG A CG    1 
ATOM   883  C CD    . ARG A 1 119 ? 106.376 92.653  129.560 1.00 90.45  ? 119 ARG A CD    1 
ATOM   884  N NE    . ARG A 1 119 ? 107.630 92.435  130.296 1.00 90.45  ? 119 ARG A NE    1 
ATOM   885  C CZ    . ARG A 1 119 ? 107.711 92.267  131.611 1.00 90.45  ? 119 ARG A CZ    1 
ATOM   886  N NH1   . ARG A 1 119 ? 106.644 92.321  132.360 1.00 90.45  ? 119 ARG A NH1   1 
ATOM   887  N NH2   . ARG A 1 119 ? 108.887 92.051  132.189 1.00 90.45  ? 119 ARG A NH2   1 
ATOM   888  N N     . VAL A 1 120 ? 108.294 97.777  128.629 1.00 58.21  ? 120 VAL A N     1 
ATOM   889  C CA    . VAL A 1 120 ? 108.883 98.833  127.817 1.00 58.21  ? 120 VAL A CA    1 
ATOM   890  C C     . VAL A 1 120 ? 110.405 98.790  127.841 1.00 58.21  ? 120 VAL A C     1 
ATOM   891  O O     . VAL A 1 120 ? 111.035 98.924  126.801 1.00 58.21  ? 120 VAL A O     1 
ATOM   892  C CB    . VAL A 1 120 ? 108.358 100.193 128.289 1.00 84.67  ? 120 VAL A CB    1 
ATOM   893  C CG1   . VAL A 1 120 ? 109.145 101.325 127.666 1.00 84.67  ? 120 VAL A CG1   1 
ATOM   894  C CG2   . VAL A 1 120 ? 106.885 100.315 127.924 1.00 84.67  ? 120 VAL A CG2   1 
ATOM   895  N N     . SER A 1 121 ? 111.035 98.613  129.003 1.00 57.81  ? 121 SER A N     1 
ATOM   896  C CA    . SER A 1 121 ? 112.498 98.632  129.037 1.00 57.81  ? 121 SER A CA    1 
ATOM   897  C C     . SER A 1 121 ? 113.100 97.452  128.298 1.00 57.81  ? 121 SER A C     1 
ATOM   898  O O     . SER A 1 121 ? 114.222 97.548  127.801 1.00 57.81  ? 121 SER A O     1 
ATOM   899  C CB    . SER A 1 121 ? 113.015 98.641  130.462 1.00 77.87  ? 121 SER A CB    1 
ATOM   900  O OG    . SER A 1 121 ? 112.842 97.379  131.053 1.00 77.87  ? 121 SER A OG    1 
ATOM   901  N N     . GLU A 1 122 ? 112.352 96.379  128.144 1.00 60.55  ? 122 GLU A N     1 
ATOM   902  C CA    . GLU A 1 122 ? 112.792 95.203  127.420 1.00 60.55  ? 122 GLU A CA    1 
ATOM   903  C C     . GLU A 1 122 ? 112.614 95.342  125.930 1.00 60.55  ? 122 GLU A C     1 
ATOM   904  O O     . GLU A 1 122 ? 112.932 94.416  125.177 1.00 60.55  ? 122 GLU A O     1 
ATOM   905  C CB    . GLU A 1 122 ? 111.996 93.994  127.872 1.00 81.34  ? 122 GLU A CB    1 
ATOM   906  C CG    . GLU A 1 122 ? 112.247 93.554  129.279 1.00 81.34  ? 122 GLU A CG    1 
ATOM   907  C CD    . GLU A 1 122 ? 111.300 92.465  129.699 1.00 81.34  ? 122 GLU A CD    1 
ATOM   908  O OE1   . GLU A 1 122 ? 110.414 92.107  128.918 1.00 81.34  ? 122 GLU A OE1   1 
ATOM   909  O OE2   . GLU A 1 122 ? 111.434 91.975  130.817 1.00 81.34  ? 122 GLU A OE2   1 
ATOM   910  N N     . THR A 1 123 ? 112.081 96.456  125.503 1.00 56.10  ? 123 THR A N     1 
ATOM   911  C CA    . THR A 1 123 ? 111.760 96.716  124.120 1.00 56.10  ? 123 THR A CA    1 
ATOM   912  C C     . THR A 1 123 ? 112.715 97.788  123.569 1.00 56.10  ? 123 THR A C     1 
ATOM   913  O O     . THR A 1 123 ? 112.995 98.769  124.258 1.00 56.10  ? 123 THR A O     1 
ATOM   914  C CB    . THR A 1 123 ? 110.291 97.141  124.086 1.00 78.54  ? 123 THR A CB    1 
ATOM   915  O OG1   . THR A 1 123 ? 109.471 96.100  124.640 1.00 78.54  ? 123 THR A OG1   1 
ATOM   916  C CG2   . THR A 1 123 ? 109.883 97.312  122.773 1.00 78.54  ? 123 THR A CG2   1 
ATOM   917  N N     . GLU A 1 124 ? 113.271 97.601  122.360 1.00 57.43  ? 124 GLU A N     1 
ATOM   918  C CA    . GLU A 1 124 ? 114.256 98.583  121.882 1.00 57.43  ? 124 GLU A CA    1 
ATOM   919  C C     . GLU A 1 124 ? 113.627 99.954  121.706 1.00 57.43  ? 124 GLU A C     1 
ATOM   920  O O     . GLU A 1 124 ? 114.244 100.970 122.029 1.00 57.43  ? 124 GLU A O     1 
ATOM   921  C CB    . GLU A 1 124 ? 114.932 98.143  120.569 1.00 77.14  ? 124 GLU A CB    1 
ATOM   922  C CG    . GLU A 1 124 ? 116.074 99.117  120.102 1.00 77.14  ? 124 GLU A CG    1 
ATOM   923  C CD    . GLU A 1 124 ? 116.922 98.642  118.901 1.00 77.14  ? 124 GLU A CD    1 
ATOM   924  O OE1   . GLU A 1 124 ? 116.535 97.704  118.200 1.00 77.14  ? 124 GLU A OE1   1 
ATOM   925  O OE2   . GLU A 1 124 ? 118.005 99.207  118.689 1.00 77.14  ? 124 GLU A OE2   1 
ATOM   926  N N     . SER A 1 125 ? 112.416 100.002 121.180 1.00 54.51  ? 125 SER A N     1 
ATOM   927  C CA    . SER A 1 125 ? 111.675 101.248 121.067 1.00 54.51  ? 125 SER A CA    1 
ATOM   928  C C     . SER A 1 125 ? 110.205 100.903 121.035 1.00 54.51  ? 125 SER A C     1 
ATOM   929  O O     . SER A 1 125 ? 109.840 99.793  120.647 1.00 54.51  ? 125 SER A O     1 
ATOM   930  C CB    . SER A 1 125 ? 112.056 102.021 119.816 1.00 73.42  ? 125 SER A CB    1 
ATOM   931  O OG    . SER A 1 125 ? 111.590 101.378 118.652 1.00 73.42  ? 125 SER A OG    1 
ATOM   932  N N     . ILE A 1 126 ? 109.355 101.843 121.417 1.00 52.87  ? 126 ILE A N     1 
ATOM   933  C CA    . ILE A 1 126 ? 107.932 101.560 121.484 1.00 52.87  ? 126 ILE A CA    1 
ATOM   934  C C     . ILE A 1 126 ? 107.236 102.126 120.276 1.00 52.87  ? 126 ILE A C     1 
ATOM   935  O O     . ILE A 1 126 ? 107.214 103.337 120.077 1.00 52.87  ? 126 ILE A O     1 
ATOM   936  C CB    . ILE A 1 126 ? 107.324 102.121 122.760 1.00 78.27  ? 126 ILE A CB    1 
ATOM   937  C CG1   . ILE A 1 126 ? 108.116 101.633 123.966 1.00 78.27  ? 126 ILE A CG1   1 
ATOM   938  C CG2   . ILE A 1 126 ? 105.886 101.687 122.894 1.00 78.27  ? 126 ILE A CG2   1 
ATOM   939  C CD1   . ILE A 1 126 ? 108.214 100.135 124.111 1.00 78.27  ? 126 ILE A CD1   1 
ATOM   940  N N     . GLY A 1 127 ? 106.667 101.249 119.476 1.00 49.95  ? 127 GLY A N     1 
ATOM   941  C CA    . GLY A 1 127 ? 105.947 101.613 118.293 1.00 49.95  ? 127 GLY A CA    1 
ATOM   942  C C     . GLY A 1 127 ? 104.561 102.010 118.628 1.00 49.95  ? 127 GLY A C     1 
ATOM   943  O O     . GLY A 1 127 ? 103.833 102.571 117.799 1.00 49.95  ? 127 GLY A O     1 
ATOM   944  N N     . GLY A 1 128 ? 104.204 101.738 119.863 1.00 50.43  ? 128 GLY A N     1 
ATOM   945  C CA    . GLY A 1 128 ? 102.903 102.084 120.387 1.00 50.43  ? 128 GLY A CA    1 
ATOM   946  C C     . GLY A 1 128 ? 102.463 101.092 121.439 1.00 50.43  ? 128 GLY A C     1 
ATOM   947  O O     . GLY A 1 128 ? 103.119 100.084 121.697 1.00 50.43  ? 128 GLY A O     1 
ATOM   948  N N     . PHE A 1 129 ? 101.323 101.411 122.048 1.00 49.70  ? 129 PHE A N     1 
ATOM   949  C CA    . PHE A 1 129 ? 100.686 100.578 123.039 1.00 49.70  ? 129 PHE A CA    1 
ATOM   950  C C     . PHE A 1 129 ? 99.315  100.201 122.534 1.00 49.70  ? 129 PHE A C     1 
ATOM   951  O O     . PHE A 1 129 ? 98.656  100.988 121.872 1.00 49.70  ? 129 PHE A O     1 
ATOM   952  C CB    . PHE A 1 129 ? 100.471 101.269 124.335 1.00 69.35  ? 129 PHE A CB    1 
ATOM   953  C CG    . PHE A 1 129 ? 101.664 101.612 125.067 1.00 69.35  ? 129 PHE A CG    1 
ATOM   954  C CD1   . PHE A 1 129 ? 102.229 100.733 125.928 1.00 69.35  ? 129 PHE A CD1   1 
ATOM   955  C CD2   . PHE A 1 129 ? 102.187 102.861 124.977 1.00 69.35  ? 129 PHE A CD2   1 
ATOM   956  C CE1   . PHE A 1 129 ? 103.326 101.066 126.652 1.00 69.35  ? 129 PHE A CE1   1 
ATOM   957  C CE2   . PHE A 1 129 ? 103.286 103.208 125.708 1.00 69.35  ? 129 PHE A CE2   1 
ATOM   958  C CZ    . PHE A 1 129 ? 103.858 102.306 126.545 1.00 69.35  ? 129 PHE A CZ    1 
ATOM   959  N N     . ILE A 1 130 ? 98.866  99.017  122.897 1.00 51.39  ? 130 ILE A N     1 
ATOM   960  C CA    . ILE A 1 130 ? 97.509  98.612  122.580 1.00 51.39  ? 130 ILE A CA    1 
ATOM   961  C C     . ILE A 1 130 ? 96.785  98.221  123.865 1.00 51.39  ? 130 ILE A C     1 
ATOM   962  O O     . ILE A 1 130 ? 97.290  97.403  124.637 1.00 51.39  ? 130 ILE A O     1 
ATOM   963  C CB    . ILE A 1 130 ? 97.466  97.455  121.565 1.00 76.08  ? 130 ILE A CB    1 
ATOM   964  C CG1   . ILE A 1 130 ? 98.117  97.878  120.234 1.00 76.08  ? 130 ILE A CG1   1 
ATOM   965  C CG2   . ILE A 1 130 ? 96.007  97.028  121.351 1.00 76.08  ? 130 ILE A CG2   1 
ATOM   966  C CD1   . ILE A 1 130 ? 98.251  96.771  119.177 1.00 76.08  ? 130 ILE A CD1   1 
ATOM   967  N N     . LEU A 1 131 ? 95.597  98.781  124.104 1.00 52.84  ? 131 LEU A N     1 
ATOM   968  C CA    . LEU A 1 131 ? 94.835  98.378  125.282 1.00 52.84  ? 131 LEU A CA    1 
ATOM   969  C C     . LEU A 1 131 ? 93.621  97.578  124.868 1.00 52.84  ? 131 LEU A C     1 
ATOM   970  O O     . LEU A 1 131 ? 92.946  97.928  123.909 1.00 52.84  ? 131 LEU A O     1 
ATOM   971  C CB    . LEU A 1 131 ? 94.345  99.555  126.104 1.00 78.23  ? 131 LEU A CB    1 
ATOM   972  C CG    . LEU A 1 131 ? 95.326  100.653 126.500 1.00 78.23  ? 131 LEU A CG    1 
ATOM   973  C CD1   . LEU A 1 131 ? 94.623  101.720 127.329 1.00 78.23  ? 131 LEU A CD1   1 
ATOM   974  C CD2   . LEU A 1 131 ? 96.472  100.092 127.253 1.00 78.23  ? 131 LEU A CD2   1 
ATOM   975  N N     . THR A 1 132 ? 93.301  96.547  125.633 1.00 53.10  ? 132 THR A N     1 
ATOM   976  C CA    . THR A 1 132 ? 92.073  95.797  125.392 1.00 53.10  ? 132 THR A CA    1 
ATOM   977  C C     . THR A 1 132 ? 91.200  95.695  126.644 1.00 53.10  ? 132 THR A C     1 
ATOM   978  O O     . THR A 1 132 ? 91.644  95.210  127.692 1.00 53.10  ? 132 THR A O     1 
ATOM   979  C CB    . THR A 1 132 ? 92.364  94.406  124.822 1.00 74.34  ? 132 THR A CB    1 
ATOM   980  O OG1   . THR A 1 132 ? 91.124  93.721  124.641 1.00 74.34  ? 132 THR A OG1   1 
ATOM   981  C CG2   . THR A 1 132 ? 93.277  93.563  125.723 1.00 74.34  ? 132 THR A CG2   1 
ATOM   982  N N     . HIS A 1 133 ? 89.954  96.170  126.546 1.00 57.81  ? 133 HIS A N     1 
ATOM   983  C CA    . HIS A 1 133 ? 89.052  96.156  127.701 1.00 57.81  ? 133 HIS A CA    1 
ATOM   984  C C     . HIS A 1 133 ? 87.601  96.387  127.282 1.00 57.81  ? 133 HIS A C     1 
ATOM   985  O O     . HIS A 1 133 ? 87.336  96.906  126.202 1.00 57.81  ? 133 HIS A O     1 
ATOM   986  C CB    . HIS A 1 133 ? 89.467  97.223  128.682 1.00 78.62  ? 133 HIS A CB    1 
ATOM   987  C CG    . HIS A 1 133 ? 89.320  98.592  128.127 1.00 78.62  ? 133 HIS A CG    1 
ATOM   988  N ND1   . HIS A 1 133 ? 88.154  99.311  128.249 1.00 78.62  ? 133 HIS A ND1   1 
ATOM   989  C CD2   . HIS A 1 133 ? 90.168  99.365  127.416 1.00 78.62  ? 133 HIS A CD2   1 
ATOM   990  C CE1   . HIS A 1 133 ? 88.294  100.479 127.652 1.00 78.62  ? 133 HIS A CE1   1 
ATOM   991  N NE2   . HIS A 1 133 ? 89.509  100.539 127.138 1.00 78.62  ? 133 HIS A NE2   1 
ATOM   992  N N     . SER A 1 134 ? 86.646  96.038  128.141 1.00 62.58  ? 134 SER A N     1 
ATOM   993  C CA    . SER A 1 134 ? 85.281  96.462  127.847 1.00 62.58  ? 134 SER A CA    1 
ATOM   994  C C     . SER A 1 134 ? 85.054  97.829  128.464 1.00 62.58  ? 134 SER A C     1 
ATOM   995  O O     . SER A 1 134 ? 85.814  98.268  129.325 1.00 62.58  ? 134 SER A O     1 
ATOM   996  C CB    . SER A 1 134 ? 84.248  95.474  128.366 1.00 84.29  ? 134 SER A CB    1 
ATOM   997  O OG    . SER A 1 134 ? 84.226  95.423  129.772 1.00 84.29  ? 134 SER A OG    1 
ATOM   998  N N     . CYS A 1 135 ? 84.003  98.503  128.036 1.00 61.33  ? 135 CYS A N     1 
ATOM   999  C CA    . CYS A 1 135 ? 83.783  99.864  128.494 1.00 61.33  ? 135 CYS A CA    1 
ATOM   1000 C C     . CYS A 1 135 ? 82.920  99.979  129.736 1.00 61.33  ? 135 CYS A C     1 
ATOM   1001 O O     . CYS A 1 135 ? 82.916  101.038 130.371 1.00 61.33  ? 135 CYS A O     1 
ATOM   1002 C CB    . CYS A 1 135 ? 83.154  100.681 127.369 1.00 82.61  ? 135 CYS A CB    1 
ATOM   1003 S SG    . CYS A 1 135 ? 84.231  100.856 125.948 1.00 82.61  ? 135 CYS A SG    1 
ATOM   1004 N N     . GLY A 1 136 ? 82.156  98.954  130.083 1.00 58.31  ? 136 GLY A N     1 
ATOM   1005 C CA    . GLY A 1 136 ? 81.264  99.064  131.223 1.00 58.31  ? 136 GLY A CA    1 
ATOM   1006 C C     . GLY A 1 136 ? 81.742  98.406  132.504 1.00 58.31  ? 136 GLY A C     1 
ATOM   1007 O O     . GLY A 1 136 ? 81.021  98.407  133.502 1.00 58.31  ? 136 GLY A O     1 
ATOM   1008 N N     . GLY A 1 137 ? 82.946  97.846  132.514 1.00 61.26  ? 137 GLY A N     1 
ATOM   1009 C CA    . GLY A 1 137 ? 83.402  97.081  133.668 1.00 61.26  ? 137 GLY A CA    1 
ATOM   1010 C C     . GLY A 1 137 ? 84.046  97.890  134.791 1.00 61.26  ? 137 GLY A C     1 
ATOM   1011 O O     . GLY A 1 137 ? 84.795  98.838  134.574 1.00 61.26  ? 137 GLY A O     1 
ATOM   1012 N N     . GLY A 1 138 ? 83.844  97.392  136.012 1.00 58.02  ? 138 GLY A N     1 
ATOM   1013 C CA    . GLY A 1 138 ? 84.419  98.008  137.194 1.00 58.02  ? 138 GLY A CA    1 
ATOM   1014 C C     . GLY A 1 138 ? 85.925  98.110  137.136 1.00 58.02  ? 138 GLY A C     1 
ATOM   1015 O O     . GLY A 1 138 ? 86.510  99.063  137.660 1.00 58.02  ? 138 GLY A O     1 
ATOM   1016 N N     . THR A 1 139 ? 86.572  97.145  136.511 1.00 59.36  ? 139 THR A N     1 
ATOM   1017 C CA    . THR A 1 139 ? 88.004  97.209  136.325 1.00 59.36  ? 139 THR A CA    1 
ATOM   1018 C C     . THR A 1 139 ? 88.307  97.530  134.897 1.00 59.36  ? 139 THR A C     1 
ATOM   1019 O O     . THR A 1 139 ? 89.123  98.413  134.608 1.00 59.36  ? 139 THR A O     1 
ATOM   1020 C CB    . THR A 1 139 ? 88.683  95.880  136.670 1.00 83.10  ? 139 THR A CB    1 
ATOM   1021 O OG1   . THR A 1 139 ? 88.403  95.535  138.024 1.00 83.10  ? 139 THR A OG1   1 
ATOM   1022 C CG2   . THR A 1 139 ? 90.214  95.978  136.462 1.00 83.10  ? 139 THR A CG2   1 
ATOM   1023 N N     . GLY A 1 140 ? 87.572  96.863  134.025 1.00 62.04  ? 140 GLY A N     1 
ATOM   1024 C CA    . GLY A 1 140 ? 87.760  96.975  132.600 1.00 62.04  ? 140 GLY A CA    1 
ATOM   1025 C C     . GLY A 1 140 ? 87.891  98.416  132.190 1.00 62.04  ? 140 GLY A C     1 
ATOM   1026 O O     . GLY A 1 140 ? 88.889  98.798  131.589 1.00 62.04  ? 140 GLY A O     1 
ATOM   1027 N N     . SER A 1 141 ? 86.918  99.233  132.515 1.00 61.41  ? 141 SER A N     1 
ATOM   1028 C CA    . SER A 1 141 ? 87.078  100.597 132.121 1.00 61.41  ? 141 SER A CA    1 
ATOM   1029 C C     . SER A 1 141 ? 87.533  101.450 133.274 1.00 61.41  ? 141 SER A C     1 
ATOM   1030 O O     . SER A 1 141 ? 88.186  102.465 133.050 1.00 61.41  ? 141 SER A O     1 
ATOM   1031 C CB    . SER A 1 141 ? 85.788  101.118 131.496 1.00 82.72  ? 141 SER A CB    1 
ATOM   1032 O OG    . SER A 1 141 ? 84.711  101.143 132.396 1.00 82.72  ? 141 SER A OG    1 
ATOM   1033 N N     . GLY A 1 142 ? 87.282  101.027 134.488 1.00 62.23  ? 142 GLY A N     1 
ATOM   1034 C CA    . GLY A 1 142 ? 87.747  101.797 135.617 1.00 62.23  ? 142 GLY A CA    1 
ATOM   1035 C C     . GLY A 1 142 ? 89.253  101.906 135.596 1.00 62.23  ? 142 GLY A C     1 
ATOM   1036 O O     . GLY A 1 142 ? 89.828  103.006 135.498 1.00 62.23  ? 142 GLY A O     1 
ATOM   1037 N N     . PHE A 1 143 ? 89.915  100.762 135.686 1.00 60.78  ? 143 PHE A N     1 
ATOM   1038 C CA    . PHE A 1 143 ? 91.352  100.796 135.596 1.00 60.78  ? 143 PHE A CA    1 
ATOM   1039 C C     . PHE A 1 143 ? 91.753  101.068 134.192 1.00 60.78  ? 143 PHE A C     1 
ATOM   1040 O O     . PHE A 1 143 ? 92.696  101.813 133.956 1.00 60.78  ? 143 PHE A O     1 
ATOM   1041 C CB    . PHE A 1 143 ? 91.999  99.518  136.041 1.00 84.81  ? 143 PHE A CB    1 
ATOM   1042 C CG    . PHE A 1 143 ? 92.493  99.568  137.377 1.00 84.81  ? 143 PHE A CG    1 
ATOM   1043 C CD1   . PHE A 1 143 ? 91.788  100.151 138.353 1.00 84.81  ? 143 PHE A CD1   1 
ATOM   1044 C CD2   . PHE A 1 143 ? 93.677  99.007  137.668 1.00 84.81  ? 143 PHE A CD2   1 
ATOM   1045 C CE1   . PHE A 1 143 ? 92.278  100.185 139.615 1.00 84.81  ? 143 PHE A CE1   1 
ATOM   1046 C CE2   . PHE A 1 143 ? 94.168  99.022  138.900 1.00 84.81  ? 143 PHE A CE2   1 
ATOM   1047 C CZ    . PHE A 1 143 ? 93.483  99.616  139.879 1.00 84.81  ? 143 PHE A CZ    1 
ATOM   1048 N N     . GLY A 1 144 ? 91.055  100.488 133.236 1.00 62.86  ? 144 GLY A N     1 
ATOM   1049 C CA    . GLY A 1 144 ? 91.477  100.686 131.861 1.00 62.86  ? 144 GLY A CA    1 
ATOM   1050 C C     . GLY A 1 144 ? 91.645  102.158 131.527 1.00 62.86  ? 144 GLY A C     1 
ATOM   1051 O O     . GLY A 1 144 ? 92.599  102.545 130.847 1.00 62.86  ? 144 GLY A O     1 
ATOM   1052 N N     . SER A 1 145 ? 90.752  103.001 132.056 1.00 60.14  ? 145 SER A N     1 
ATOM   1053 C CA    . SER A 1 145 ? 90.829  104.429 131.831 1.00 60.14  ? 145 SER A CA    1 
ATOM   1054 C C     . SER A 1 145 ? 91.931  105.058 132.653 1.00 60.14  ? 145 SER A C     1 
ATOM   1055 O O     . SER A 1 145 ? 92.642  105.950 132.163 1.00 60.14  ? 145 SER A O     1 
ATOM   1056 C CB    . SER A 1 145 ? 89.504  105.070 132.169 1.00 81.00  ? 145 SER A CB    1 
ATOM   1057 O OG    . SER A 1 145 ? 88.505  104.572 131.321 1.00 81.00  ? 145 SER A OG    1 
ATOM   1058 N N     . LYS A 1 146 ? 92.114  104.601 133.889 1.00 59.62  ? 146 LYS A N     1 
ATOM   1059 C CA    . LYS A 1 146 ? 93.191  105.185 134.663 1.00 59.62  ? 146 LYS A CA    1 
ATOM   1060 C C     . LYS A 1 146 ? 94.520  104.846 134.051 1.00 59.62  ? 146 LYS A C     1 
ATOM   1061 O O     . LYS A 1 146 ? 95.459  105.651 134.070 1.00 59.62  ? 146 LYS A O     1 
ATOM   1062 C CB    . LYS A 1 146 ? 93.151  104.679 136.083 1.00 89.43  ? 146 LYS A CB    1 
ATOM   1063 C CG    . LYS A 1 146 ? 94.245  105.236 136.990 1.00 89.43  ? 146 LYS A CG    1 
ATOM   1064 C CD    . LYS A 1 146 ? 94.210  106.760 137.150 1.00 89.43  ? 146 LYS A CD    1 
ATOM   1065 C CE    . LYS A 1 146 ? 92.975  107.233 137.885 1.00 89.43  ? 146 LYS A CE    1 
ATOM   1066 N NZ    . LYS A 1 146 ? 93.005  108.693 138.165 1.00 89.43  ? 146 LYS A NZ    1 
ATOM   1067 N N     . ILE A 1 147 ? 94.614  103.646 133.522 1.00 59.43  ? 147 ILE A N     1 
ATOM   1068 C CA    . ILE A 1 147 ? 95.820  103.202 132.877 1.00 59.43  ? 147 ILE A CA    1 
ATOM   1069 C C     . ILE A 1 147 ? 96.043  104.009 131.617 1.00 59.43  ? 147 ILE A C     1 
ATOM   1070 O O     . ILE A 1 147 ? 97.110  104.575 131.418 1.00 59.43  ? 147 ILE A O     1 
ATOM   1071 C CB    . ILE A 1 147 ? 95.733  101.696 132.623 1.00 87.99  ? 147 ILE A CB    1 
ATOM   1072 C CG1   . ILE A 1 147 ? 95.731  100.975 133.979 1.00 87.99  ? 147 ILE A CG1   1 
ATOM   1073 C CG2   . ILE A 1 147 ? 96.871  101.234 131.747 1.00 87.99  ? 147 ILE A CG2   1 
ATOM   1074 C CD1   . ILE A 1 147 ? 95.347  99.516  133.928 1.00 87.99  ? 147 ILE A CD1   1 
ATOM   1075 N N     . LEU A 1 148 ? 95.017  104.167 130.794 1.00 57.04  ? 148 LEU A N     1 
ATOM   1076 C CA    . LEU A 1 148 ? 95.192  104.942 129.575 1.00 57.04  ? 148 LEU A CA    1 
ATOM   1077 C C     . LEU A 1 148 ? 95.789  106.279 129.888 1.00 57.04  ? 148 LEU A C     1 
ATOM   1078 O O     . LEU A 1 148 ? 96.749  106.728 129.240 1.00 57.04  ? 148 LEU A O     1 
ATOM   1079 C CB    . LEU A 1 148 ? 93.860  105.140 128.875 1.00 84.45  ? 148 LEU A CB    1 
ATOM   1080 C CG    . LEU A 1 148 ? 93.828  105.997 127.623 1.00 84.45  ? 148 LEU A CG    1 
ATOM   1081 C CD1   . LEU A 1 148 ? 94.629  105.376 126.505 1.00 84.45  ? 148 LEU A CD1   1 
ATOM   1082 C CD2   . LEU A 1 148 ? 92.394  106.210 127.180 1.00 84.45  ? 148 LEU A CD2   1 
ATOM   1083 N N     . LYS A 1 149 ? 95.241  106.932 130.888 1.00 58.86  ? 149 LYS A N     1 
ATOM   1084 C CA    . LYS A 1 149 ? 95.732  108.255 131.191 1.00 58.86  ? 149 LYS A CA    1 
ATOM   1085 C C     . LYS A 1 149 ? 97.143  108.215 131.730 1.00 58.86  ? 149 LYS A C     1 
ATOM   1086 O O     . LYS A 1 149 ? 97.987  109.014 131.304 1.00 58.86  ? 149 LYS A O     1 
ATOM   1087 C CB    . LYS A 1 149 ? 94.799  108.964 132.157 1.00 88.29  ? 149 LYS A CB    1 
ATOM   1088 C CG    . LYS A 1 149 ? 95.221  110.395 132.496 1.00 88.29  ? 149 LYS A CG    1 
ATOM   1089 C CD    . LYS A 1 149 ? 94.169  111.090 133.348 1.00 88.29  ? 149 LYS A CD    1 
ATOM   1090 C CE    . LYS A 1 149 ? 94.523  112.552 133.650 1.00 88.29  ? 149 LYS A CE    1 
ATOM   1091 N NZ    . LYS A 1 149 ? 95.578  112.721 134.708 1.00 88.29  ? 149 LYS A NZ    1 
ATOM   1092 N N     . THR A 1 150 ? 97.436  107.318 132.652 1.00 59.88  ? 150 THR A N     1 
ATOM   1093 C CA    . THR A 1 150 ? 98.758  107.381 133.227 1.00 59.88  ? 150 THR A CA    1 
ATOM   1094 C C     . THR A 1 150 ? 99.808  106.972 132.207 1.00 59.88  ? 150 THR A C     1 
ATOM   1095 O O     . THR A 1 150 ? 100.949 107.472 132.230 1.00 59.88  ? 150 THR A O     1 
ATOM   1096 C CB    . THR A 1 150 ? 98.810  106.559 134.487 1.00 83.83  ? 150 THR A CB    1 
ATOM   1097 O OG1   . THR A 1 150 ? 99.897  107.015 135.300 1.00 83.83  ? 150 THR A OG1   1 
ATOM   1098 C CG2   . THR A 1 150 ? 99.023  105.135 134.175 1.00 83.83  ? 150 THR A CG2   1 
ATOM   1099 N N     . ILE A 1 151 ? 99.451  106.129 131.261 1.00 59.31  ? 151 ILE A N     1 
ATOM   1100 C CA    . ILE A 1 151 ? 100.426 105.805 130.244 1.00 59.31  ? 151 ILE A CA    1 
ATOM   1101 C C     . ILE A 1 151 ? 100.764 107.051 129.470 1.00 59.31  ? 151 ILE A C     1 
ATOM   1102 O O     . ILE A 1 151 ? 101.937 107.355 129.269 1.00 59.31  ? 151 ILE A O     1 
ATOM   1103 C CB    . ILE A 1 151 ? 99.948  104.718 129.272 1.00 87.81  ? 151 ILE A CB    1 
ATOM   1104 C CG1   . ILE A 1 151 ? 99.721  103.390 129.960 1.00 87.81  ? 151 ILE A CG1   1 
ATOM   1105 C CG2   . ILE A 1 151 ? 101.025 104.507 128.180 1.00 87.81  ? 151 ILE A CG2   1 
ATOM   1106 C CD1   . ILE A 1 151 ? 98.943  102.430 129.107 1.00 87.81  ? 151 ILE A CD1   1 
ATOM   1107 N N     . ARG A 1 152 ? 99.746  107.802 129.019 1.00 59.97  ? 152 ARG A N     1 
ATOM   1108 C CA    . ARG A 1 152 ? 100.077 108.984 128.219 1.00 59.97  ? 152 ARG A CA    1 
ATOM   1109 C C     . ARG A 1 152 ? 100.923 109.943 128.999 1.00 59.97  ? 152 ARG A C     1 
ATOM   1110 O O     . ARG A 1 152 ? 101.777 110.615 128.431 1.00 59.97  ? 152 ARG A O     1 
ATOM   1111 C CB    . ARG A 1 152 ? 98.857  109.752 127.732 1.00 88.12  ? 152 ARG A CB    1 
ATOM   1112 C CG    . ARG A 1 152 ? 97.968  109.113 126.712 1.00 88.12  ? 152 ARG A CG    1 
ATOM   1113 C CD    . ARG A 1 152 ? 98.634  108.788 125.414 1.00 88.12  ? 152 ARG A CD    1 
ATOM   1114 N NE    . ARG A 1 152 ? 99.293  109.903 124.782 1.00 88.12  ? 152 ARG A NE    1 
ATOM   1115 C CZ    . ARG A 1 152 ? 98.688  110.807 124.038 1.00 88.12  ? 152 ARG A CZ    1 
ATOM   1116 N NH1   . ARG A 1 152 ? 97.382  110.788 123.865 1.00 88.12  ? 152 ARG A NH1   1 
ATOM   1117 N NH2   . ARG A 1 152 ? 99.411  111.762 123.461 1.00 88.12  ? 152 ARG A NH2   1 
ATOM   1118 N N     . GLU A 1 153 ? 100.702 110.028 130.294 1.00 62.64  ? 153 GLU A N     1 
ATOM   1119 C CA    . GLU A 1 153 ? 101.503 110.936 131.087 1.00 62.64  ? 153 GLU A CA    1 
ATOM   1120 C C     . GLU A 1 153 ? 102.961 110.575 130.988 1.00 62.64  ? 153 GLU A C     1 
ATOM   1121 O O     . GLU A 1 153 ? 103.821 111.459 130.929 1.00 62.64  ? 153 GLU A O     1 
ATOM   1122 C CB    . GLU A 1 153 ? 101.069 110.899 132.543 1.00 84.14  ? 153 GLU A CB    1 
ATOM   1123 C CG    . GLU A 1 153 ? 99.701  111.505 132.826 1.00 84.14  ? 153 GLU A CG    1 
ATOM   1124 C CD    . GLU A 1 153 ? 99.206  111.214 134.231 1.00 84.14  ? 153 GLU A CD    1 
ATOM   1125 O OE1   . GLU A 1 153 ? 99.833  110.408 134.925 1.00 84.14  ? 153 GLU A OE1   1 
ATOM   1126 O OE2   . GLU A 1 153 ? 98.184  111.780 134.636 1.00 84.14  ? 153 GLU A OE2   1 
ATOM   1127 N N     . ARG A 1 154 ? 103.261 109.271 130.969 1.00 62.34  ? 154 ARG A N     1 
ATOM   1128 C CA    . ARG A 1 154 ? 104.660 108.832 130.849 1.00 62.34  ? 154 ARG A CA    1 
ATOM   1129 C C     . ARG A 1 154 ? 105.176 108.812 129.414 1.00 62.34  ? 154 ARG A C     1 
ATOM   1130 O O     . ARG A 1 154 ? 106.367 109.047 129.172 1.00 62.34  ? 154 ARG A O     1 
ATOM   1131 C CB    . ARG A 1 154 ? 104.835 107.428 131.402 1.00 91.60  ? 154 ARG A CB    1 
ATOM   1132 C CG    . ARG A 1 154 ? 104.776 107.286 132.885 1.00 91.60  ? 154 ARG A CG    1 
ATOM   1133 C CD    . ARG A 1 154 ? 104.770 105.821 133.221 1.00 91.60  ? 154 ARG A CD    1 
ATOM   1134 N NE    . ARG A 1 154 ? 104.829 105.561 134.654 1.00 91.60  ? 154 ARG A NE    1 
ATOM   1135 C CZ    . ARG A 1 154 ? 103.811 105.709 135.494 1.00 91.60  ? 154 ARG A CZ    1 
ATOM   1136 N NH1   . ARG A 1 154 ? 102.638 106.172 135.088 1.00 91.60  ? 154 ARG A NH1   1 
ATOM   1137 N NH2   . ARG A 1 154 ? 103.978 105.392 136.774 1.00 91.60  ? 154 ARG A NH2   1 
ATOM   1138 N N     . TYR A 1 155 ? 104.310 108.516 128.462 1.00 60.97  ? 155 TYR A N     1 
ATOM   1139 C CA    . TYR A 1 155 ? 104.699 108.349 127.073 1.00 60.97  ? 155 TYR A CA    1 
ATOM   1140 C C     . TYR A 1 155 ? 103.820 109.184 126.159 1.00 60.97  ? 155 TYR A C     1 
ATOM   1141 O O     . TYR A 1 155 ? 103.078 108.633 125.347 1.00 60.97  ? 155 TYR A O     1 
ATOM   1142 C CB    . TYR A 1 155 ? 104.570 106.888 126.677 1.00 84.42  ? 155 TYR A CB    1 
ATOM   1143 C CG    . TYR A 1 155 ? 105.256 105.963 127.565 1.00 84.42  ? 155 TYR A CG    1 
ATOM   1144 C CD1   . TYR A 1 155 ? 106.569 105.687 127.400 1.00 84.42  ? 155 TYR A CD1   1 
ATOM   1145 C CD2   . TYR A 1 155 ? 104.569 105.345 128.566 1.00 84.42  ? 155 TYR A CD2   1 
ATOM   1146 C CE1   . TYR A 1 155 ? 107.199 104.808 128.232 1.00 84.42  ? 155 TYR A CE1   1 
ATOM   1147 C CE2   . TYR A 1 155 ? 105.165 104.473 129.399 1.00 84.42  ? 155 TYR A CE2   1 
ATOM   1148 C CZ    . TYR A 1 155 ? 106.487 104.201 129.238 1.00 84.42  ? 155 TYR A CZ    1 
ATOM   1149 O OH    . TYR A 1 155 ? 107.089 103.311 130.091 1.00 84.42  ? 155 TYR A OH    1 
ATOM   1150 N N     . PRO A 1 156 ? 103.918 110.507 126.234 1.00 56.51  ? 156 PRO A N     1 
ATOM   1151 C CA    . PRO A 1 156 ? 103.024 111.412 125.489 1.00 56.51  ? 156 PRO A CA    1 
ATOM   1152 C C     . PRO A 1 156 ? 103.147 111.321 123.993 1.00 56.51  ? 156 PRO A C     1 
ATOM   1153 O O     . PRO A 1 156 ? 102.240 111.725 123.258 1.00 56.51  ? 156 PRO A O     1 
ATOM   1154 C CB    . PRO A 1 156 ? 103.471 112.778 125.992 1.00 373.12 ? 156 PRO A CB    1 
ATOM   1155 C CG    . PRO A 1 156 ? 104.872 112.550 126.487 1.00 373.12 ? 156 PRO A CG    1 
ATOM   1156 C CD    . PRO A 1 156 ? 104.886 111.208 127.062 1.00 373.12 ? 156 PRO A CD    1 
ATOM   1157 N N     . LYS A 1 157 ? 104.263 110.800 123.517 1.00 53.22  ? 157 LYS A N     1 
ATOM   1158 C CA    . LYS A 1 157 ? 104.530 110.680 122.097 1.00 53.22  ? 157 LYS A CA    1 
ATOM   1159 C C     . LYS A 1 157 ? 104.378 109.262 121.596 1.00 53.22  ? 157 LYS A C     1 
ATOM   1160 O O     . LYS A 1 157 ? 104.724 108.971 120.447 1.00 53.22  ? 157 LYS A O     1 
ATOM   1161 C CB    . LYS A 1 157 ? 105.946 111.154 121.781 1.00 79.83  ? 157 LYS A CB    1 
ATOM   1162 C CG    . LYS A 1 157 ? 106.242 112.598 122.123 1.00 79.83  ? 157 LYS A CG    1 
ATOM   1163 C CD    . LYS A 1 157 ? 105.402 113.542 121.302 1.00 79.83  ? 157 LYS A CD    1 
ATOM   1164 C CE    . LYS A 1 157 ? 105.857 114.968 121.492 1.00 79.83  ? 157 LYS A CE    1 
ATOM   1165 N NZ    . LYS A 1 157 ? 104.985 115.896 120.748 1.00 79.83  ? 157 LYS A NZ    1 
ATOM   1166 N N     . VAL A 1 158 ? 103.912 108.361 122.429 1.00 54.00  ? 158 VAL A N     1 
ATOM   1167 C CA    . VAL A 1 158 ? 103.759 106.990 122.006 1.00 54.00  ? 158 VAL A CA    1 
ATOM   1168 C C     . VAL A 1 158 ? 102.285 106.740 121.804 1.00 54.00  ? 158 VAL A C     1 
ATOM   1169 O O     . VAL A 1 158 ? 101.522 106.831 122.762 1.00 54.00  ? 158 VAL A O     1 
ATOM   1170 C CB    . VAL A 1 158 ? 104.309 106.065 123.054 1.00 78.54  ? 158 VAL A CB    1 
ATOM   1171 C CG1   . VAL A 1 158 ? 104.115 104.690 122.620 1.00 78.54  ? 158 VAL A CG1   1 
ATOM   1172 C CG2   . VAL A 1 158 ? 105.755 106.370 123.239 1.00 78.54  ? 158 VAL A CG2   1 
ATOM   1173 N N     . PRO A 1 159 ? 101.845 106.451 120.619 1.00 53.35  ? 159 PRO A N     1 
ATOM   1174 C CA    . PRO A 1 159 ? 100.423 106.320 120.368 1.00 53.35  ? 159 PRO A CA    1 
ATOM   1175 C C     . PRO A 1 159 ? 99.852  105.141 121.112 1.00 53.35  ? 159 PRO A C     1 
ATOM   1176 O O     . PRO A 1 159 ? 100.462 104.077 121.154 1.00 53.35  ? 159 PRO A O     1 
ATOM   1177 C CB    . PRO A 1 159 ? 100.364 106.103 118.865 1.00 352.25 ? 159 PRO A CB    1 
ATOM   1178 C CG    . PRO A 1 159 ? 101.669 105.501 118.553 1.00 352.25 ? 159 PRO A CG    1 
ATOM   1179 C CD    . PRO A 1 159 ? 102.658 106.102 119.483 1.00 352.25 ? 159 PRO A CD    1 
ATOM   1180 N N     . ILE A 1 160 ? 98.647  105.308 121.655 1.00 55.32  ? 160 ILE A N     1 
ATOM   1181 C CA    . ILE A 1 160 ? 97.935  104.204 122.276 1.00 55.32  ? 160 ILE A CA    1 
ATOM   1182 C C     . ILE A 1 160 ? 96.727  103.949 121.450 1.00 55.32  ? 160 ILE A C     1 
ATOM   1183 O O     . ILE A 1 160 ? 95.906  104.843 121.229 1.00 55.32  ? 160 ILE A O     1 
ATOM   1184 C CB    . ILE A 1 160 ? 97.500  104.484 123.701 1.00 81.90  ? 160 ILE A CB    1 
ATOM   1185 C CG1   . ILE A 1 160 ? 98.698  104.875 124.552 1.00 81.90  ? 160 ILE A CG1   1 
ATOM   1186 C CG2   . ILE A 1 160 ? 96.821  103.249 124.234 1.00 81.90  ? 160 ILE A CG2   1 
ATOM   1187 C CD1   . ILE A 1 160 ? 98.341  105.307 125.961 1.00 81.90  ? 160 ILE A CD1   1 
ATOM   1188 N N     . PHE A 1 161 ? 96.622  102.738 120.988 1.00 56.55  ? 161 PHE A N     1 
ATOM   1189 C CA    . PHE A 1 161 ? 95.534  102.309 120.160 1.00 56.55  ? 161 PHE A CA    1 
ATOM   1190 C C     . PHE A 1 161 ? 94.692  101.418 121.040 1.00 56.55  ? 161 PHE A C     1 
ATOM   1191 O O     . PHE A 1 161 ? 95.247  100.649 121.819 1.00 56.55  ? 161 PHE A O     1 
ATOM   1192 C CB    . PHE A 1 161 ? 96.089  101.532 118.991 1.00 78.91  ? 161 PHE A CB    1 
ATOM   1193 C CG    . PHE A 1 161 ? 95.107  101.243 117.949 1.00 78.91  ? 161 PHE A CG    1 
ATOM   1194 C CD1   . PHE A 1 161 ? 94.318  100.142 118.013 1.00 78.91  ? 161 PHE A CD1   1 
ATOM   1195 C CD2   . PHE A 1 161 ? 94.983  102.069 116.885 1.00 78.91  ? 161 PHE A CD2   1 
ATOM   1196 C CE1   . PHE A 1 161 ? 93.423  99.895  117.037 1.00 78.91  ? 161 PHE A CE1   1 
ATOM   1197 C CE2   . PHE A 1 161 ? 94.085  101.816 115.911 1.00 78.91  ? 161 PHE A CE2   1 
ATOM   1198 C CZ    . PHE A 1 161 ? 93.311  100.727 115.987 1.00 78.91  ? 161 PHE A CZ    1 
ATOM   1199 N N     . THR A 1 162 ? 93.370  101.511 120.991 1.00 56.01  ? 162 THR A N     1 
ATOM   1200 C CA    . THR A 1 162 ? 92.637  100.585 121.840 1.00 56.01  ? 162 THR A CA    1 
ATOM   1201 C C     . THR A 1 162 ? 91.551  99.850  121.082 1.00 56.01  ? 162 THR A C     1 
ATOM   1202 O O     . THR A 1 162 ? 91.049  100.298 120.065 1.00 56.01  ? 162 THR A O     1 
ATOM   1203 C CB    . THR A 1 162 ? 92.042  101.281 123.064 1.00 78.41  ? 162 THR A CB    1 
ATOM   1204 O OG1   . THR A 1 162 ? 90.962  102.124 122.684 1.00 78.41  ? 162 THR A OG1   1 
ATOM   1205 C CG2   . THR A 1 162 ? 93.088  102.166 123.734 1.00 78.41  ? 162 THR A CG2   1 
ATOM   1206 N N     . PHE A 1 163 ? 91.219  98.692  121.589 1.00 57.58  ? 163 PHE A N     1 
ATOM   1207 C CA    . PHE A 1 163 ? 90.114  97.907  121.083 1.00 57.58  ? 163 PHE A CA    1 
ATOM   1208 C C     . PHE A 1 163 ? 89.194  97.794  122.263 1.00 57.58  ? 163 PHE A C     1 
ATOM   1209 O O     . PHE A 1 163 ? 89.478  97.033  123.195 1.00 57.58  ? 163 PHE A O     1 
ATOM   1210 C CB    . PHE A 1 163 ? 90.545  96.524  120.636 1.00 80.34  ? 163 PHE A CB    1 
ATOM   1211 C CG    . PHE A 1 163 ? 91.464  96.496  119.433 1.00 80.34  ? 163 PHE A CG    1 
ATOM   1212 C CD1   . PHE A 1 163 ? 92.831  96.683  119.567 1.00 80.34  ? 163 PHE A CD1   1 
ATOM   1213 C CD2   . PHE A 1 163 ? 90.958  96.219  118.172 1.00 80.34  ? 163 PHE A CD2   1 
ATOM   1214 C CE1   . PHE A 1 163 ? 93.662  96.621  118.469 1.00 80.34  ? 163 PHE A CE1   1 
ATOM   1215 C CE2   . PHE A 1 163 ? 91.793  96.153  117.072 1.00 80.34  ? 163 PHE A CE2   1 
ATOM   1216 C CZ    . PHE A 1 163 ? 93.145  96.357  117.225 1.00 80.34  ? 163 PHE A CZ    1 
ATOM   1217 N N     . SER A 1 164 ? 88.123  98.555  122.261 1.00 61.21  ? 164 SER A N     1 
ATOM   1218 C CA    . SER A 1 164 ? 87.300  98.566  123.444 1.00 61.21  ? 164 SER A CA    1 
ATOM   1219 C C     . SER A 1 164 ? 85.945  98.007  123.128 1.00 61.21  ? 164 SER A C     1 
ATOM   1220 O O     . SER A 1 164 ? 85.427  98.176  122.027 1.00 61.21  ? 164 SER A O     1 
ATOM   1221 C CB    . SER A 1 164 ? 87.184  99.944  124.027 1.00 82.45  ? 164 SER A CB    1 
ATOM   1222 O OG    . SER A 1 164 ? 86.561  100.827 123.134 1.00 82.45  ? 164 SER A OG    1 
ATOM   1223 N N     . ILE A 1 165 ? 85.373  97.353  124.106 1.00 61.30  ? 165 ILE A N     1 
ATOM   1224 C CA    . ILE A 1 165 ? 84.100  96.725  123.884 1.00 61.30  ? 165 ILE A CA    1 
ATOM   1225 C C     . ILE A 1 165 ? 82.980  97.455  124.599 1.00 61.30  ? 165 ILE A C     1 
ATOM   1226 O O     . ILE A 1 165 ? 82.891  97.447  125.832 1.00 61.30  ? 165 ILE A O     1 
ATOM   1227 C CB    . ILE A 1 165 ? 84.130  95.262  124.283 1.00 90.76  ? 165 ILE A CB    1 
ATOM   1228 C CG1   . ILE A 1 165 ? 85.210  94.562  123.454 1.00 90.76  ? 165 ILE A CG1   1 
ATOM   1229 C CG2   . ILE A 1 165 ? 82.744  94.667  124.006 1.00 90.76  ? 165 ILE A CG2   1 
ATOM   1230 C CD1   . ILE A 1 165 ? 85.567  93.185  123.922 1.00 90.76  ? 165 ILE A CD1   1 
ATOM   1231 N N     . PHE A 1 166 ? 82.095  97.997  123.824 1.00 60.57  ? 166 PHE A N     1 
ATOM   1232 C CA    . PHE A 1 166 ? 81.008  98.741  124.386 1.00 60.57  ? 166 PHE A CA    1 
ATOM   1233 C C     . PHE A 1 166 ? 79.871  97.802  124.746 1.00 60.57  ? 166 PHE A C     1 
ATOM   1234 O O     . PHE A 1 166 ? 79.560  96.871  123.999 1.00 60.57  ? 166 PHE A O     1 
ATOM   1235 C CB    . PHE A 1 166 ? 80.563  99.815  123.417 1.00 84.52  ? 166 PHE A CB    1 
ATOM   1236 C CG    . PHE A 1 166 ? 81.517  100.957 123.350 1.00 84.52  ? 166 PHE A CG    1 
ATOM   1237 C CD1   . PHE A 1 166 ? 82.590  100.927 122.504 1.00 84.52  ? 166 PHE A CD1   1 
ATOM   1238 C CD2   . PHE A 1 166 ? 81.341  102.044 124.138 1.00 84.52  ? 166 PHE A CD2   1 
ATOM   1239 C CE1   . PHE A 1 166 ? 83.466  101.984 122.451 1.00 84.52  ? 166 PHE A CE1   1 
ATOM   1240 C CE2   . PHE A 1 166 ? 82.195  103.100 124.090 1.00 84.52  ? 166 PHE A CE2   1 
ATOM   1241 C CZ    . PHE A 1 166 ? 83.264  103.075 123.249 1.00 84.52  ? 166 PHE A CZ    1 
ATOM   1242 N N     . PRO A 1 167 ? 79.275  98.059  125.893 1.00 60.50  ? 167 PRO A N     1 
ATOM   1243 C CA    . PRO A 1 167 ? 78.205  97.254  126.445 1.00 60.50  ? 167 PRO A CA    1 
ATOM   1244 C C     . PRO A 1 167 ? 76.900  97.479  125.755 1.00 60.50  ? 167 PRO A C     1 
ATOM   1245 O O     . PRO A 1 167 ? 76.685  98.469  125.073 1.00 60.50  ? 167 PRO A O     1 
ATOM   1246 C CB    . PRO A 1 167 ? 78.116  97.779  127.869 1.00 399.46 ? 167 PRO A CB    1 
ATOM   1247 C CG    . PRO A 1 167 ? 78.573  99.191  127.750 1.00 399.46 ? 167 PRO A CG    1 
ATOM   1248 C CD    . PRO A 1 167 ? 79.650  99.166  126.747 1.00 399.46 ? 167 PRO A CD    1 
ATOM   1249 N N     . SER A 1 168 ? 76.004  96.555  126.014 1.00 65.55  ? 168 SER A N     1 
ATOM   1250 C CA    . SER A 1 168 ? 74.668  96.640  125.588 1.00 65.55  ? 168 SER A CA    1 
ATOM   1251 C C     . SER A 1 168 ? 73.887  95.950  126.686 1.00 65.55  ? 168 SER A C     1 
ATOM   1252 O O     . SER A 1 168 ? 74.221  94.814  127.036 1.00 65.55  ? 168 SER A O     1 
ATOM   1253 C CB    . SER A 1 168 ? 74.438  95.941  124.260 1.00 88.29  ? 168 SER A CB    1 
ATOM   1254 O OG    . SER A 1 168 ? 73.072  95.980  123.906 1.00 88.29  ? 168 SER A OG    1 
ATOM   1255 N N     . PRO A 1 169 ? 72.865  96.577  127.227 1.00 65.34  ? 169 PRO A N     1 
ATOM   1256 C CA    . PRO A 1 169 ? 72.040  96.026  128.311 1.00 65.34  ? 169 PRO A CA    1 
ATOM   1257 C C     . PRO A 1 169 ? 71.088  94.968  127.778 1.00 65.34  ? 169 PRO A C     1 
ATOM   1258 O O     . PRO A 1 169 ? 69.864  95.115  127.846 1.00 65.34  ? 169 PRO A O     1 
ATOM   1259 C CB    . PRO A 1 169 ? 71.305  97.271  128.818 1.00 431.41 ? 169 PRO A CB    1 
ATOM   1260 C CG    . PRO A 1 169 ? 71.131  98.103  127.575 1.00 431.41 ? 169 PRO A CG    1 
ATOM   1261 C CD    . PRO A 1 169 ? 72.392  97.888  126.769 1.00 431.41 ? 169 PRO A CD    1 
ATOM   1262 N N     . LYS A 1 170 ? 71.693  93.888  127.275 1.00 68.16  ? 170 LYS A N     1 
ATOM   1263 C CA    . LYS A 1 170 ? 71.026  92.849  126.504 1.00 68.16  ? 170 LYS A CA    1 
ATOM   1264 C C     . LYS A 1 170 ? 69.813  92.287  127.211 1.00 68.16  ? 170 LYS A C     1 
ATOM   1265 O O     . LYS A 1 170 ? 68.796  92.014  126.570 1.00 68.16  ? 170 LYS A O     1 
ATOM   1266 C CB    . LYS A 1 170 ? 72.036  91.736  126.202 1.00 102.24 ? 170 LYS A CB    1 
ATOM   1267 C CG    . LYS A 1 170 ? 71.541  90.625  125.271 1.00 102.24 ? 170 LYS A CG    1 
ATOM   1268 C CD    . LYS A 1 170 ? 72.686  89.666  124.959 1.00 102.24 ? 170 LYS A CD    1 
ATOM   1269 C CE    . LYS A 1 170 ? 72.373  88.708  123.871 1.00 102.24 ? 170 LYS A CE    1 
ATOM   1270 N NZ    . LYS A 1 170 ? 71.304  87.689  124.127 1.00 102.24 ? 170 LYS A NZ    1 
ATOM   1271 N N     . ILE A 1 171 ? 69.902  92.071  128.518 1.00 66.10  ? 171 ILE A N     1 
ATOM   1272 C CA    . ILE A 1 171 ? 68.747  91.537  129.227 1.00 66.10  ? 171 ILE A CA    1 
ATOM   1273 C C     . ILE A 1 171 ? 68.304  92.527  130.295 1.00 66.10  ? 171 ILE A C     1 
ATOM   1274 O O     . ILE A 1 171 ? 68.601  92.354  131.482 1.00 66.10  ? 171 ILE A O     1 
ATOM   1275 C CB    . ILE A 1 171 ? 69.078  90.163  129.845 1.00 97.86  ? 171 ILE A CB    1 
ATOM   1276 C CG1   . ILE A 1 171 ? 69.632  89.224  128.751 1.00 97.86  ? 171 ILE A CG1   1 
ATOM   1277 C CG2   . ILE A 1 171 ? 67.828  89.566  130.523 1.00 97.86  ? 171 ILE A CG2   1 
ATOM   1278 C CD1   . ILE A 1 171 ? 70.186  87.899  129.241 1.00 97.86  ? 171 ILE A CD1   1 
ATOM   1279 N N     . SER A 1 172 ? 67.544  93.540  129.878 1.00 62.81  ? 172 SER A N     1 
ATOM   1280 C CA    . SER A 1 172 ? 66.977  94.550  130.770 1.00 62.81  ? 172 SER A CA    1 
ATOM   1281 C C     . SER A 1 172 ? 67.982  95.109  131.775 1.00 62.81  ? 172 SER A C     1 
ATOM   1282 O O     . SER A 1 172 ? 67.658  95.293  132.950 1.00 62.81  ? 172 SER A O     1 
ATOM   1283 C CB    . SER A 1 172 ? 65.772  93.982  131.511 1.00 84.60  ? 172 SER A CB    1 
ATOM   1284 O OG    . SER A 1 172 ? 64.755  93.603  130.609 1.00 84.60  ? 172 SER A OG    1 
ATOM   1285 N N     . GLU A 1 173 ? 69.203  95.428  131.341 1.00 61.57  ? 173 GLU A N     1 
ATOM   1286 C CA    . GLU A 1 173 ? 70.169  95.892  132.341 1.00 61.57  ? 173 GLU A CA    1 
ATOM   1287 C C     . GLU A 1 173 ? 70.035  97.391  132.536 1.00 61.57  ? 173 GLU A C     1 
ATOM   1288 O O     . GLU A 1 173 ? 70.853  98.202  132.105 1.00 61.57  ? 173 GLU A O     1 
ATOM   1289 C CB    . GLU A 1 173 ? 71.588  95.484  132.000 1.00 82.71  ? 173 GLU A CB    1 
ATOM   1290 C CG    . GLU A 1 173 ? 71.796  93.988  132.037 1.00 82.71  ? 173 GLU A CG    1 
ATOM   1291 C CD    . GLU A 1 173 ? 73.210  93.598  131.750 1.00 82.71  ? 173 GLU A CD    1 
ATOM   1292 O OE1   . GLU A 1 173 ? 73.993  94.471  131.398 1.00 82.71  ? 173 GLU A OE1   1 
ATOM   1293 O OE2   . GLU A 1 173 ? 73.546  92.422  131.875 1.00 82.71  ? 173 GLU A OE2   1 
ATOM   1294 N N     . THR A 1 174 ? 68.980  97.740  133.257 1.00 59.23  ? 174 THR A N     1 
ATOM   1295 C CA    . THR A 1 174 ? 68.649  99.112  133.601 1.00 59.23  ? 174 THR A CA    1 
ATOM   1296 C C     . THR A 1 174 ? 69.477  99.476  134.819 1.00 59.23  ? 174 THR A C     1 
ATOM   1297 O O     . THR A 1 174 ? 68.966  99.626  135.931 1.00 59.23  ? 174 THR A O     1 
ATOM   1298 C CB    . THR A 1 174 ? 67.173  99.243  133.929 1.00 82.92  ? 174 THR A CB    1 
ATOM   1299 O OG1   . THR A 1 174 ? 66.884  98.390  135.042 1.00 82.92  ? 174 THR A OG1   1 
ATOM   1300 C CG2   . THR A 1 174 ? 66.325  98.821  132.743 1.00 82.92  ? 174 THR A CG2   1 
ATOM   1301 N N     . VAL A 1 175 ? 70.781  99.570  134.587 1.00 57.44  ? 175 VAL A N     1 
ATOM   1302 C CA    . VAL A 1 175 ? 71.778  99.724  135.631 1.00 57.44  ? 175 VAL A CA    1 
ATOM   1303 C C     . VAL A 1 175 ? 72.650  100.928 135.319 1.00 57.44  ? 175 VAL A C     1 
ATOM   1304 O O     . VAL A 1 175 ? 72.544  101.527 134.258 1.00 57.44  ? 175 VAL A O     1 
ATOM   1305 C CB    . VAL A 1 175 ? 72.633  98.458  135.760 1.00 83.55  ? 175 VAL A CB    1 
ATOM   1306 C CG1   . VAL A 1 175 ? 71.748  97.277  136.123 1.00 83.55  ? 175 VAL A CG1   1 
ATOM   1307 C CG2   . VAL A 1 175 ? 73.348  98.182  134.449 1.00 83.55  ? 175 VAL A CG2   1 
ATOM   1308 N N     . VAL A 1 176 ? 73.535  101.263 136.259 1.00 57.59  ? 176 VAL A N     1 
ATOM   1309 C CA    . VAL A 1 176 ? 74.426  102.413 136.141 1.00 57.59  ? 176 VAL A CA    1 
ATOM   1310 C C     . VAL A 1 176 ? 75.488  102.274 135.070 1.00 57.59  ? 176 VAL A C     1 
ATOM   1311 O O     . VAL A 1 176 ? 76.244  103.209 134.827 1.00 57.59  ? 176 VAL A O     1 
ATOM   1312 C CB    . VAL A 1 176 ? 75.149  102.661 137.475 1.00 83.77  ? 176 VAL A CB    1 
ATOM   1313 C CG1   . VAL A 1 176 ? 74.140  103.011 138.576 1.00 83.77  ? 176 VAL A CG1   1 
ATOM   1314 C CG2   . VAL A 1 176 ? 75.984  101.421 137.846 1.00 83.77  ? 176 VAL A CG2   1 
ATOM   1315 N N     . GLU A 1 177 ? 75.578  101.132 134.433 1.00 62.15  ? 177 GLU A N     1 
ATOM   1316 C CA    . GLU A 1 177 ? 76.610  100.934 133.429 1.00 62.15  ? 177 GLU A CA    1 
ATOM   1317 C C     . GLU A 1 177 ? 76.745  102.060 132.403 1.00 62.15  ? 177 GLU A C     1 
ATOM   1318 O O     . GLU A 1 177 ? 77.884  102.371 132.040 1.00 62.15  ? 177 GLU A O     1 
ATOM   1319 C CB    . GLU A 1 177 ? 76.382  99.584  132.742 1.00 83.48  ? 177 GLU A CB    1 
ATOM   1320 C CG    . GLU A 1 177 ? 77.479  99.231  131.799 1.00 83.48  ? 177 GLU A CG    1 
ATOM   1321 C CD    . GLU A 1 177 ? 77.348  97.845  131.288 1.00 83.48  ? 177 GLU A CD    1 
ATOM   1322 O OE1   . GLU A 1 177 ? 76.247  97.309  131.316 1.00 83.48  ? 177 GLU A OE1   1 
ATOM   1323 O OE2   . GLU A 1 177 ? 78.357  97.278  130.877 1.00 83.48  ? 177 GLU A OE2   1 
ATOM   1324 N N     . PRO A 1 178 ? 75.686  102.692 131.902 1.00 58.17  ? 178 PRO A N     1 
ATOM   1325 C CA    . PRO A 1 178 ? 75.855  103.787 130.951 1.00 58.17  ? 178 PRO A CA    1 
ATOM   1326 C C     . PRO A 1 178 ? 76.685  104.890 131.502 1.00 58.17  ? 178 PRO A C     1 
ATOM   1327 O O     . PRO A 1 178 ? 77.283  105.665 130.750 1.00 58.17  ? 178 PRO A O     1 
ATOM   1328 C CB    . PRO A 1 178 ? 74.421  104.237 130.703 1.00 384.09 ? 178 PRO A CB    1 
ATOM   1329 C CG    . PRO A 1 178 ? 73.618  103.010 130.987 1.00 384.09 ? 178 PRO A CG    1 
ATOM   1330 C CD    . PRO A 1 178 ? 74.290  102.375 132.129 1.00 384.09 ? 178 PRO A CD    1 
ATOM   1331 N N     . TYR A 1 179 ? 76.715  104.980 132.817 1.00 56.90  ? 179 TYR A N     1 
ATOM   1332 C CA    . TYR A 1 179 ? 77.534  105.947 133.519 1.00 56.90  ? 179 TYR A CA    1 
ATOM   1333 C C     . TYR A 1 179 ? 78.985  105.553 133.386 1.00 56.90  ? 179 TYR A C     1 
ATOM   1334 O O     . TYR A 1 179 ? 79.876  106.411 133.300 1.00 56.90  ? 179 TYR A O     1 
ATOM   1335 C CB    . TYR A 1 179 ? 77.069  105.961 134.975 1.00 78.78  ? 179 TYR A CB    1 
ATOM   1336 C CG    . TYR A 1 179 ? 77.806  106.776 135.984 1.00 78.78  ? 179 TYR A CG    1 
ATOM   1337 C CD1   . TYR A 1 179 ? 79.109  106.480 136.360 1.00 78.78  ? 179 TYR A CD1   1 
ATOM   1338 C CD2   . TYR A 1 179 ? 77.160  107.806 136.638 1.00 78.78  ? 179 TYR A CD2   1 
ATOM   1339 C CE1   . TYR A 1 179 ? 79.763  107.231 137.320 1.00 78.78  ? 179 TYR A CE1   1 
ATOM   1340 C CE2   . TYR A 1 179 ? 77.795  108.555 137.602 1.00 78.78  ? 179 TYR A CE2   1 
ATOM   1341 C CZ    . TYR A 1 179 ? 79.095  108.268 137.940 1.00 78.78  ? 179 TYR A CZ    1 
ATOM   1342 O OH    . TYR A 1 179 ? 79.711  109.029 138.901 1.00 78.78  ? 179 TYR A OH    1 
ATOM   1343 N N     . ASN A 1 180 ? 79.228  104.251 133.313 1.00 59.59  ? 180 ASN A N     1 
ATOM   1344 C CA    . ASN A 1 180 ? 80.588  103.812 133.183 1.00 59.59  ? 180 ASN A CA    1 
ATOM   1345 C C     . ASN A 1 180 ? 81.017  104.006 131.771 1.00 59.59  ? 180 ASN A C     1 
ATOM   1346 O O     . ASN A 1 180 ? 82.153  104.397 131.491 1.00 59.59  ? 180 ASN A O     1 
ATOM   1347 C CB    . ASN A 1 180 ? 80.691  102.351 133.527 1.00 80.73  ? 180 ASN A CB    1 
ATOM   1348 C CG    . ASN A 1 180 ? 80.301  102.064 134.902 1.00 80.73  ? 180 ASN A CG    1 
ATOM   1349 O OD1   . ASN A 1 180 ? 80.244  102.942 135.759 1.00 80.73  ? 180 ASN A OD1   1 
ATOM   1350 N ND2   . ASN A 1 180 ? 80.025  100.804 135.153 1.00 80.73  ? 180 ASN A ND2   1 
ATOM   1351 N N     . ALA A 1 181 ? 80.095  103.739 130.873 1.00 59.39  ? 181 ALA A N     1 
ATOM   1352 C CA    . ALA A 1 181 ? 80.407  103.820 129.466 1.00 59.39  ? 181 ALA A CA    1 
ATOM   1353 C C     . ALA A 1 181 ? 80.705  105.247 129.070 1.00 59.39  ? 181 ALA A C     1 
ATOM   1354 O O     . ALA A 1 181 ? 81.641  105.503 128.311 1.00 59.39  ? 181 ALA A O     1 
ATOM   1355 C CB    . ALA A 1 181 ? 79.255  103.262 128.641 1.00 80.99  ? 181 ALA A CB    1 
ATOM   1356 N N     . ILE A 1 182 ? 79.948  106.197 129.588 1.00 56.17  ? 182 ILE A N     1 
ATOM   1357 C CA    . ILE A 1 182 ? 80.216  107.539 129.142 1.00 56.17  ? 182 ILE A CA    1 
ATOM   1358 C C     . ILE A 1 182 ? 81.470  108.033 129.779 1.00 56.17  ? 182 ILE A C     1 
ATOM   1359 O O     . ILE A 1 182 ? 82.221  108.779 129.154 1.00 56.17  ? 182 ILE A O     1 
ATOM   1360 C CB    . ILE A 1 182 ? 79.043  108.483 129.406 1.00 83.16  ? 182 ILE A CB    1 
ATOM   1361 C CG1   . ILE A 1 182 ? 79.120  109.637 128.408 1.00 83.16  ? 182 ILE A CG1   1 
ATOM   1362 C CG2   . ILE A 1 182 ? 79.099  109.048 130.838 1.00 83.16  ? 182 ILE A CG2   1 
ATOM   1363 C CD1   . ILE A 1 182 ? 77.877  110.495 128.324 1.00 83.16  ? 182 ILE A CD1   1 
ATOM   1364 N N     . MET A 1 183 ? 81.729  107.666 131.021 1.00 58.84  ? 183 MET A N     1 
ATOM   1365 C CA    . MET A 1 183 ? 82.933  108.191 131.595 1.00 58.84  ? 183 MET A CA    1 
ATOM   1366 C C     . MET A 1 183 ? 84.153  107.628 130.907 1.00 58.84  ? 183 MET A C     1 
ATOM   1367 O O     . MET A 1 183 ? 85.129  108.360 130.675 1.00 58.84  ? 183 MET A O     1 
ATOM   1368 C CB    . MET A 1 183 ? 82.965  107.929 133.071 1.00 84.53  ? 183 MET A CB    1 
ATOM   1369 C CG    . MET A 1 183 ? 81.881  108.662 133.832 1.00 84.53  ? 183 MET A CG    1 
ATOM   1370 S SD    . MET A 1 183 ? 81.835  110.418 133.561 1.00 84.53  ? 183 MET A SD    1 
ATOM   1371 C CE    . MET A 1 183 ? 83.258  111.016 134.437 1.00 84.53  ? 183 MET A CE    1 
ATOM   1372 N N     . THR A 1 184 ? 84.107  106.377 130.478 1.00 60.24  ? 184 THR A N     1 
ATOM   1373 C CA    . THR A 1 184 ? 85.290  105.915 129.786 1.00 60.24  ? 184 THR A CA    1 
ATOM   1374 C C     . THR A 1 184 ? 85.359  106.491 128.397 1.00 60.24  ? 184 THR A C     1 
ATOM   1375 O O     . THR A 1 184 ? 86.447  106.797 127.923 1.00 60.24  ? 184 THR A O     1 
ATOM   1376 C CB    . THR A 1 184 ? 85.394  104.401 129.735 1.00 84.34  ? 184 THR A CB    1 
ATOM   1377 O OG1   . THR A 1 184 ? 86.711  104.049 129.317 1.00 84.34  ? 184 THR A OG1   1 
ATOM   1378 C CG2   . THR A 1 184 ? 84.446  103.801 128.777 1.00 84.34  ? 184 THR A CG2   1 
ATOM   1379 N N     . LEU A 1 185 ? 84.218  106.723 127.762 1.00 57.37  ? 185 LEU A N     1 
ATOM   1380 C CA    . LEU A 1 185 ? 84.253  107.290 126.436 1.00 57.37  ? 185 LEU A CA    1 
ATOM   1381 C C     . LEU A 1 185 ? 84.918  108.606 126.501 1.00 57.37  ? 185 LEU A C     1 
ATOM   1382 O O     . LEU A 1 185 ? 85.737  108.940 125.654 1.00 57.37  ? 185 LEU A O     1 
ATOM   1383 C CB    . LEU A 1 185 ? 82.851  107.431 125.891 1.00 84.94  ? 185 LEU A CB    1 
ATOM   1384 C CG    . LEU A 1 185 ? 82.692  107.992 124.504 1.00 84.94  ? 185 LEU A CG    1 
ATOM   1385 C CD1   . LEU A 1 185 ? 83.403  107.158 123.500 1.00 84.94  ? 185 LEU A CD1   1 
ATOM   1386 C CD2   . LEU A 1 185 ? 81.222  108.029 124.165 1.00 84.94  ? 185 LEU A CD2   1 
ATOM   1387 N N     . SER A 1 186 ? 84.618  109.347 127.531 1.00 56.23  ? 186 SER A N     1 
ATOM   1388 C CA    . SER A 1 186 ? 85.247  110.630 127.678 1.00 56.23  ? 186 SER A CA    1 
ATOM   1389 C C     . SER A 1 186 ? 86.732  110.464 127.754 1.00 56.23  ? 186 SER A C     1 
ATOM   1390 O O     . SER A 1 186 ? 87.486  111.186 127.092 1.00 56.23  ? 186 SER A O     1 
ATOM   1391 C CB    . SER A 1 186 ? 84.752  111.316 128.927 1.00 75.74  ? 186 SER A CB    1 
ATOM   1392 O OG    . SER A 1 186 ? 85.386  112.564 129.077 1.00 75.74  ? 186 SER A OG    1 
ATOM   1393 N N     . ASN A 1 187 ? 87.180  109.517 128.542 1.00 59.53  ? 187 ASN A N     1 
ATOM   1394 C CA    . ASN A 1 187 ? 88.606  109.426 128.631 1.00 59.53  ? 187 ASN A CA    1 
ATOM   1395 C C     . ASN A 1 187 ? 89.218  108.913 127.355 1.00 59.53  ? 187 ASN A C     1 
ATOM   1396 O O     . ASN A 1 187 ? 90.356  109.261 127.038 1.00 59.53  ? 187 ASN A O     1 
ATOM   1397 C CB    . ASN A 1 187 ? 88.981  108.623 129.834 1.00 80.65  ? 187 ASN A CB    1 
ATOM   1398 C CG    . ASN A 1 187 ? 88.778  109.418 131.065 1.00 80.65  ? 187 ASN A CG    1 
ATOM   1399 O OD1   . ASN A 1 187 ? 88.743  110.647 131.011 1.00 80.65  ? 187 ASN A OD1   1 
ATOM   1400 N ND2   . ASN A 1 187 ? 88.635  108.755 132.183 1.00 80.65  ? 187 ASN A ND2   1 
ATOM   1401 N N     . LEU A 1 188 ? 88.506  108.102 126.604 1.00 58.15  ? 188 LEU A N     1 
ATOM   1402 C CA    . LEU A 1 188 ? 89.082  107.644 125.354 1.00 58.15  ? 188 LEU A CA    1 
ATOM   1403 C C     . LEU A 1 188 ? 89.285  108.825 124.449 1.00 58.15  ? 188 LEU A C     1 
ATOM   1404 O O     . LEU A 1 188 ? 90.320  108.961 123.798 1.00 58.15  ? 188 LEU A O     1 
ATOM   1405 C CB    . LEU A 1 188 ? 88.187  106.618 124.675 1.00 86.09  ? 188 LEU A CB    1 
ATOM   1406 C CG    . LEU A 1 188 ? 88.070  105.229 125.303 1.00 86.09  ? 188 LEU A CG    1 
ATOM   1407 C CD1   . LEU A 1 188 ? 86.911  104.455 124.647 1.00 86.09  ? 188 LEU A CD1   1 
ATOM   1408 C CD2   . LEU A 1 188 ? 89.380  104.471 125.133 1.00 86.09  ? 188 LEU A CD2   1 
ATOM   1409 N N     . ILE A 1 189 ? 88.323  109.721 124.438 1.00 55.93  ? 189 ILE A N     1 
ATOM   1410 C CA    . ILE A 1 189 ? 88.468  110.894 123.605 1.00 55.93  ? 189 ILE A CA    1 
ATOM   1411 C C     . ILE A 1 189 ? 89.648  111.697 124.080 1.00 55.93  ? 189 ILE A C     1 
ATOM   1412 O O     . ILE A 1 189 ? 90.455  112.153 123.283 1.00 55.93  ? 189 ILE A O     1 
ATOM   1413 C CB    . ILE A 1 189 ? 87.205  111.758 123.618 1.00 82.80  ? 189 ILE A CB    1 
ATOM   1414 C CG1   . ILE A 1 189 ? 86.024  110.996 123.023 1.00 82.80  ? 189 ILE A CG1   1 
ATOM   1415 C CG2   . ILE A 1 189 ? 87.464  113.014 122.815 1.00 82.80  ? 189 ILE A CG2   1 
ATOM   1416 C CD1   . ILE A 1 189 ? 84.637  111.618 123.270 1.00 82.80  ? 189 ILE A CD1   1 
ATOM   1417 N N     . LYS A 1 190 ? 89.771  111.874 125.377 1.00 55.93  ? 190 LYS A N     1 
ATOM   1418 C CA    . LYS A 1 190 ? 90.839  112.716 125.876 1.00 55.93  ? 190 LYS A CA    1 
ATOM   1419 C C     . LYS A 1 190 ? 92.218  112.122 125.658 1.00 55.93  ? 190 LYS A C     1 
ATOM   1420 O O     . LYS A 1 190 ? 93.160  112.870 125.388 1.00 55.93  ? 190 LYS A O     1 
ATOM   1421 C CB    . LYS A 1 190 ? 90.666  113.015 127.356 1.00 83.89  ? 190 LYS A CB    1 
ATOM   1422 C CG    . LYS A 1 190 ? 89.537  113.936 127.684 1.00 83.89  ? 190 LYS A CG    1 
ATOM   1423 C CD    . LYS A 1 190 ? 89.414  114.246 129.179 1.00 83.89  ? 190 LYS A CD    1 
ATOM   1424 C CE    . LYS A 1 190 ? 88.146  115.086 129.439 1.00 83.89  ? 190 LYS A CE    1 
ATOM   1425 N NZ    . LYS A 1 190 ? 87.919  115.453 130.872 1.00 83.89  ? 190 LYS A NZ    1 
ATOM   1426 N N     . TYR A 1 191 ? 92.398  110.818 125.791 1.00 57.18  ? 191 TYR A N     1 
ATOM   1427 C CA    . TYR A 1 191 ? 93.766  110.312 125.773 1.00 57.18  ? 191 TYR A CA    1 
ATOM   1428 C C     . TYR A 1 191 ? 94.174  109.287 124.690 1.00 57.18  ? 191 TYR A C     1 
ATOM   1429 O O     . TYR A 1 191 ? 95.378  109.115 124.471 1.00 57.18  ? 191 TYR A O     1 
ATOM   1430 C CB    . TYR A 1 191 ? 94.076  109.730 127.141 1.00 79.17  ? 191 TYR A CB    1 
ATOM   1431 C CG    . TYR A 1 191 ? 93.872  110.765 128.144 1.00 79.17  ? 191 TYR A CG    1 
ATOM   1432 C CD1   . TYR A 1 191 ? 94.723  111.809 128.228 1.00 79.17  ? 191 TYR A CD1   1 
ATOM   1433 C CD2   . TYR A 1 191 ? 92.806  110.708 128.987 1.00 79.17  ? 191 TYR A CD2   1 
ATOM   1434 C CE1   . TYR A 1 191 ? 94.521  112.782 129.128 1.00 79.17  ? 191 TYR A CE1   1 
ATOM   1435 C CE2   . TYR A 1 191 ? 92.597  111.676 129.895 1.00 79.17  ? 191 TYR A CE2   1 
ATOM   1436 C CZ    . TYR A 1 191 ? 93.456  112.720 129.958 1.00 79.17  ? 191 TYR A CZ    1 
ATOM   1437 O OH    . TYR A 1 191 ? 93.233  113.717 130.863 1.00 79.17  ? 191 TYR A OH    1 
ATOM   1438 N N     . ALA A 1 192 ? 93.254  108.581 124.045 1.00 55.60  ? 192 ALA A N     1 
ATOM   1439 C CA    . ALA A 1 192 ? 93.690  107.563 123.103 1.00 55.60  ? 192 ALA A CA    1 
ATOM   1440 C C     . ALA A 1 192 ? 94.080  108.222 121.798 1.00 55.60  ? 192 ALA A C     1 
ATOM   1441 O O     . ALA A 1 192 ? 93.576  109.284 121.464 1.00 55.60  ? 192 ALA A O     1 
ATOM   1442 C CB    . ALA A 1 192 ? 92.592  106.521 122.869 1.00 75.82  ? 192 ALA A CB    1 
ATOM   1443 N N     . SER A 1 193 ? 94.994  107.604 121.065 1.00 56.25  ? 193 SER A N     1 
ATOM   1444 C CA    . SER A 1 193 ? 95.233  108.099 119.730 1.00 56.25  ? 193 SER A CA    1 
ATOM   1445 C C     . SER A 1 193 ? 94.115  107.658 118.831 1.00 56.25  ? 193 SER A C     1 
ATOM   1446 O O     . SER A 1 193 ? 93.582  108.452 118.052 1.00 56.25  ? 193 SER A O     1 
ATOM   1447 C CB    . SER A 1 193 ? 96.548  107.596 119.187 1.00 75.77  ? 193 SER A CB    1 
ATOM   1448 O OG    . SER A 1 193 ? 97.629  108.103 119.920 1.00 75.77  ? 193 SER A OG    1 
ATOM   1449 N N     . CYS A 1 194 ? 93.739  106.394 118.952 1.00 59.52  ? 194 CYS A N     1 
ATOM   1450 C CA    . CYS A 1 194 ? 92.674  105.819 118.162 1.00 59.52  ? 194 CYS A CA    1 
ATOM   1451 C C     . CYS A 1 194 ? 92.086  104.645 118.871 1.00 59.52  ? 194 CYS A C     1 
ATOM   1452 O O     . CYS A 1 194 ? 92.712  104.062 119.756 1.00 59.52  ? 194 CYS A O     1 
ATOM   1453 C CB    . CYS A 1 194 ? 93.160  105.277 116.854 1.00 80.17  ? 194 CYS A CB    1 
ATOM   1454 S SG    . CYS A 1 194 ? 94.009  106.391 115.873 1.00 80.17  ? 194 CYS A SG    1 
ATOM   1455 N N     . SER A 1 195 ? 90.919  104.235 118.401 1.00 58.66  ? 195 SER A N     1 
ATOM   1456 C CA    . SER A 1 195 ? 90.365  103.004 118.933 1.00 58.66  ? 195 SER A CA    1 
ATOM   1457 C C     . SER A 1 195 ? 89.371  102.354 117.998 1.00 58.66  ? 195 SER A C     1 
ATOM   1458 O O     . SER A 1 195 ? 88.731  103.012 117.177 1.00 58.66  ? 195 SER A O     1 
ATOM   1459 C CB    . SER A 1 195 ? 89.681  103.254 120.243 1.00 79.01  ? 195 SER A CB    1 
ATOM   1460 O OG    . SER A 1 195 ? 88.568  104.095 120.065 1.00 79.01  ? 195 SER A OG    1 
ATOM   1461 N N     . ILE A 1 196 ? 89.205  101.058 118.180 1.00 59.55  ? 196 ILE A N     1 
ATOM   1462 C CA    . ILE A 1 196 ? 88.181  100.323 117.473 1.00 59.55  ? 196 ILE A CA    1 
ATOM   1463 C C     . ILE A 1 196 ? 87.006  100.210 118.384 1.00 59.55  ? 196 ILE A C     1 
ATOM   1464 O O     . ILE A 1 196 ? 87.121  99.804  119.537 1.00 59.55  ? 196 ILE A O     1 
ATOM   1465 C CB    . ILE A 1 196 ? 88.599  98.912  117.045 1.00 88.16  ? 196 ILE A CB    1 
ATOM   1466 C CG1   . ILE A 1 196 ? 89.857  98.906  116.188 1.00 88.16  ? 196 ILE A CG1   1 
ATOM   1467 C CG2   . ILE A 1 196 ? 87.417  98.206  116.313 1.00 88.16  ? 196 ILE A CG2   1 
ATOM   1468 C CD1   . ILE A 1 196 ? 89.800  99.703  114.926 1.00 88.16  ? 196 ILE A CD1   1 
ATOM   1469 N N     . VAL A 1 197 ? 85.871  100.531 117.854 1.00 59.85  ? 197 VAL A N     1 
ATOM   1470 C CA    . VAL A 1 197 ? 84.649  100.461 118.593 1.00 59.85  ? 197 VAL A CA    1 
ATOM   1471 C C     . VAL A 1 197 ? 84.006  99.125  118.315 1.00 59.85  ? 197 VAL A C     1 
ATOM   1472 O O     . VAL A 1 197 ? 83.507  98.883  117.218 1.00 59.85  ? 197 VAL A O     1 
ATOM   1473 C CB    . VAL A 1 197 ? 83.761  101.611 118.156 1.00 87.05  ? 197 VAL A CB    1 
ATOM   1474 C CG1   . VAL A 1 197 ? 82.437  101.556 118.811 1.00 87.05  ? 197 VAL A CG1   1 
ATOM   1475 C CG2   . VAL A 1 197 ? 84.479  102.903 118.475 1.00 87.05  ? 197 VAL A CG2   1 
ATOM   1476 N N     . LEU A 1 198 ? 83.977  98.272  119.307 1.00 62.27  ? 198 LEU A N     1 
ATOM   1477 C CA    . LEU A 1 198 ? 83.332  96.987  119.175 1.00 62.27  ? 198 LEU A CA    1 
ATOM   1478 C C     . LEU A 1 198 ? 82.049  97.023  119.983 1.00 62.27  ? 198 LEU A C     1 
ATOM   1479 O O     . LEU A 1 198 ? 82.086  97.216  121.195 1.00 62.27  ? 198 LEU A O     1 
ATOM   1480 C CB    . LEU A 1 198 ? 84.266  95.907  119.682 1.00 92.19  ? 198 LEU A CB    1 
ATOM   1481 C CG    . LEU A 1 198 ? 85.619  95.827  118.996 1.00 92.19  ? 198 LEU A CG    1 
ATOM   1482 C CD1   . LEU A 1 198 ? 86.500  94.887  119.791 1.00 92.19  ? 198 LEU A CD1   1 
ATOM   1483 C CD2   . LEU A 1 198 ? 85.451  95.327  117.567 1.00 92.19  ? 198 LEU A CD2   1 
ATOM   1484 N N     . ASP A 1 199 ? 80.917  96.883  119.333 1.00 63.57  ? 199 ASP A N     1 
ATOM   1485 C CA    . ASP A 1 199 ? 79.658  96.968  120.045 1.00 63.57  ? 199 ASP A CA    1 
ATOM   1486 C C     . ASP A 1 199 ? 79.109  95.567  120.209 1.00 63.57  ? 199 ASP A C     1 
ATOM   1487 O O     . ASP A 1 199 ? 78.846  94.886  119.216 1.00 63.57  ? 199 ASP A O     1 
ATOM   1488 C CB    . ASP A 1 199 ? 78.669  97.877  119.308 1.00 81.73  ? 199 ASP A CB    1 
ATOM   1489 C CG    . ASP A 1 199 ? 77.369  98.112  120.096 1.00 81.73  ? 199 ASP A CG    1 
ATOM   1490 O OD1   . ASP A 1 199 ? 76.982  97.251  120.899 1.00 81.73  ? 199 ASP A OD1   1 
ATOM   1491 O OD2   . ASP A 1 199 ? 76.734  99.161  119.907 1.00 81.73  ? 199 ASP A OD2   1 
ATOM   1492 N N     . ASN A 1 200 ? 78.939  95.116  121.445 1.00 63.04  ? 200 ASN A N     1 
ATOM   1493 C CA    . ASN A 1 200 ? 78.450  93.754  121.570 1.00 63.04  ? 200 ASN A CA    1 
ATOM   1494 C C     . ASN A 1 200 ? 77.124  93.561  120.869 1.00 63.04  ? 200 ASN A C     1 
ATOM   1495 O O     . ASN A 1 200 ? 76.868  92.477  120.371 1.00 63.04  ? 200 ASN A O     1 
ATOM   1496 C CB    . ASN A 1 200 ? 78.331  93.315  123.013 1.00 85.41  ? 200 ASN A CB    1 
ATOM   1497 C CG    . ASN A 1 200 ? 79.644  92.805  123.604 1.00 85.41  ? 200 ASN A CG    1 
ATOM   1498 O OD1   . ASN A 1 200 ? 80.560  92.393  122.891 1.00 85.41  ? 200 ASN A OD1   1 
ATOM   1499 N ND2   . ASN A 1 200 ? 79.727  92.811  124.926 1.00 85.41  ? 200 ASN A ND2   1 
ATOM   1500 N N     . GLU A 1 201 ? 76.270  94.566  120.783 1.00 63.82  ? 201 GLU A N     1 
ATOM   1501 C CA    . GLU A 1 201 ? 74.980  94.312  120.143 1.00 63.82  ? 201 GLU A CA    1 
ATOM   1502 C C     . GLU A 1 201 ? 75.164  94.001  118.684 1.00 63.82  ? 201 GLU A C     1 
ATOM   1503 O O     . GLU A 1 201 ? 74.465  93.164  118.108 1.00 63.82  ? 201 GLU A O     1 
ATOM   1504 C CB    . GLU A 1 201 ? 74.071  95.521  120.266 1.00 85.73  ? 201 GLU A CB    1 
ATOM   1505 C CG    . GLU A 1 201 ? 72.661  95.279  119.787 1.00 85.73  ? 201 GLU A CG    1 
ATOM   1506 C CD    . GLU A 1 201 ? 71.944  94.311  120.675 1.00 85.73  ? 201 GLU A CD    1 
ATOM   1507 O OE1   . GLU A 1 201 ? 72.272  94.257  121.864 1.00 85.73  ? 201 GLU A OE1   1 
ATOM   1508 O OE2   . GLU A 1 201 ? 71.064  93.597  120.192 1.00 85.73  ? 201 GLU A OE2   1 
ATOM   1509 N N     . ALA A 1 202 ? 76.076  94.714  118.065 1.00 67.04  ? 202 ALA A N     1 
ATOM   1510 C CA    . ALA A 1 202 ? 76.320  94.518  116.658 1.00 67.04  ? 202 ALA A CA    1 
ATOM   1511 C C     . ALA A 1 202 ? 76.831  93.143  116.421 1.00 67.04  ? 202 ALA A C     1 
ATOM   1512 O O     . ALA A 1 202 ? 76.383  92.426  115.524 1.00 67.04  ? 202 ALA A O     1 
ATOM   1513 C CB    . ALA A 1 202 ? 77.374  95.493  116.188 1.00 91.42  ? 202 ALA A CB    1 
ATOM   1514 N N     . LEU A 1 203 ? 77.778  92.776  117.250 1.00 65.75  ? 203 LEU A N     1 
ATOM   1515 C CA    . LEU A 1 203 ? 78.457  91.523  117.098 1.00 65.75  ? 203 LEU A CA    1 
ATOM   1516 C C     . LEU A 1 203 ? 77.490  90.408  117.368 1.00 65.75  ? 203 LEU A C     1 
ATOM   1517 O O     . LEU A 1 203 ? 77.562  89.355  116.740 1.00 65.75  ? 203 LEU A O     1 
ATOM   1518 C CB    . LEU A 1 203 ? 79.658  91.503  118.040 1.00 97.34  ? 203 LEU A CB    1 
ATOM   1519 C CG    . LEU A 1 203 ? 80.761  92.536  117.738 1.00 97.34  ? 203 LEU A CG    1 
ATOM   1520 C CD1   . LEU A 1 203 ? 81.738  92.539  118.882 1.00 97.34  ? 203 LEU A CD1   1 
ATOM   1521 C CD2   . LEU A 1 203 ? 81.477  92.215  116.427 1.00 97.34  ? 203 LEU A CD2   1 
ATOM   1522 N N     . PHE A 1 204 ? 76.591  90.641  118.305 1.00 68.19  ? 204 PHE A N     1 
ATOM   1523 C CA    . PHE A 1 204 ? 75.578  89.671  118.605 1.00 68.19  ? 204 PHE A CA    1 
ATOM   1524 C C     . PHE A 1 204 ? 74.761  89.423  117.369 1.00 68.19  ? 204 PHE A C     1 
ATOM   1525 O O     . PHE A 1 204 ? 74.504  88.274  117.004 1.00 68.19  ? 204 PHE A O     1 
ATOM   1526 C CB    . PHE A 1 204 ? 74.718  90.180  119.749 1.00 95.15  ? 204 PHE A CB    1 
ATOM   1527 C CG    . PHE A 1 204 ? 73.828  89.154  120.330 1.00 95.15  ? 204 PHE A CG    1 
ATOM   1528 C CD1   . PHE A 1 204 ? 74.292  87.880  120.562 1.00 95.15  ? 204 PHE A CD1   1 
ATOM   1529 C CD2   . PHE A 1 204 ? 72.530  89.460  120.646 1.00 95.15  ? 204 PHE A CD2   1 
ATOM   1530 C CE1   . PHE A 1 204 ? 73.477  86.913  121.099 1.00 95.15  ? 204 PHE A CE1   1 
ATOM   1531 C CE2   . PHE A 1 204 ? 71.703  88.512  121.178 1.00 95.15  ? 204 PHE A CE2   1 
ATOM   1532 C CZ    . PHE A 1 204 ? 72.188  87.207  121.407 1.00 95.15  ? 204 PHE A CZ    1 
ATOM   1533 N N     . SER A 1 205 ? 74.361  90.488  116.692 1.00 70.90  ? 205 SER A N     1 
ATOM   1534 C CA    . SER A 1 205 ? 73.517  90.272  115.538 1.00 70.90  ? 205 SER A CA    1 
ATOM   1535 C C     . SER A 1 205 ? 74.274  89.544  114.458 1.00 70.90  ? 205 SER A C     1 
ATOM   1536 O O     . SER A 1 205 ? 73.698  88.723  113.741 1.00 70.90  ? 205 SER A O     1 
ATOM   1537 C CB    . SER A 1 205 ? 73.023  91.578  114.983 1.00 95.50  ? 205 SER A CB    1 
ATOM   1538 O OG    . SER A 1 205 ? 74.082  92.225  114.319 1.00 95.50  ? 205 SER A OG    1 
ATOM   1539 N N     . ILE A 1 206 ? 75.572  89.793  114.358 1.00 70.06  ? 206 ILE A N     1 
ATOM   1540 C CA    . ILE A 1 206 ? 76.356  89.102  113.349 1.00 70.06  ? 206 ILE A CA    1 
ATOM   1541 C C     . ILE A 1 206 ? 76.464  87.641  113.688 1.00 70.06  ? 206 ILE A C     1 
ATOM   1542 O O     . ILE A 1 206 ? 76.287  86.771  112.834 1.00 70.06  ? 206 ILE A O     1 
ATOM   1543 C CB    . ILE A 1 206 ? 77.745  89.722  113.209 1.00 103.72 ? 206 ILE A CB    1 
ATOM   1544 C CG1   . ILE A 1 206 ? 77.615  91.157  112.681 1.00 103.72 ? 206 ILE A CG1   1 
ATOM   1545 C CG2   . ILE A 1 206 ? 78.568  88.861  112.260 1.00 103.72 ? 206 ILE A CG2   1 
ATOM   1546 C CD1   . ILE A 1 206 ? 78.870  92.022  112.789 1.00 103.72 ? 206 ILE A CD1   1 
ATOM   1547 N N     . ALA A 1 207 ? 76.753  87.336  114.932 1.00 71.62  ? 207 ALA A N     1 
ATOM   1548 C CA    . ALA A 1 207 ? 76.867  85.940  115.286 1.00 71.62  ? 207 ALA A CA    1 
ATOM   1549 C C     . ALA A 1 207 ? 75.571  85.230  115.032 1.00 71.62  ? 207 ALA A C     1 
ATOM   1550 O O     . ALA A 1 207 ? 75.553  84.076  114.612 1.00 71.62  ? 207 ALA A O     1 
ATOM   1551 C CB    . ALA A 1 207 ? 77.259  85.800  116.738 1.00 97.66  ? 207 ALA A CB    1 
ATOM   1552 N N     . GLU A 1 208 ? 74.481  85.911  115.292 1.00 74.81  ? 208 GLU A N     1 
ATOM   1553 C CA    . GLU A 1 208 ? 73.177  85.324  115.123 1.00 74.81  ? 208 GLU A CA    1 
ATOM   1554 C C     . GLU A 1 208 ? 72.833  85.161  113.659 1.00 74.81  ? 208 GLU A C     1 
ATOM   1555 O O     . GLU A 1 208 ? 72.254  84.145  113.263 1.00 74.81  ? 208 GLU A O     1 
ATOM   1556 C CB    . GLU A 1 208 ? 72.140  86.197  115.817 1.00 100.49 ? 208 GLU A CB    1 
ATOM   1557 C CG    . GLU A 1 208 ? 72.213  86.224  117.352 1.00 100.49 ? 208 GLU A CG    1 
ATOM   1558 C CD    . GLU A 1 208 ? 71.341  87.313  117.922 1.00 100.49 ? 208 GLU A CD    1 
ATOM   1559 O OE1   . GLU A 1 208 ? 70.835  88.123  117.151 1.00 100.49 ? 208 GLU A OE1   1 
ATOM   1560 O OE2   . GLU A 1 208 ? 71.129  87.351  119.109 1.00 100.49 ? 208 GLU A OE2   1 
ATOM   1561 N N     . LYS A 1 209 ? 73.187  86.136  112.837 1.00 71.91  ? 209 LYS A N     1 
ATOM   1562 C CA    . LYS A 1 209 ? 72.744  86.146  111.448 1.00 71.91  ? 209 LYS A CA    1 
ATOM   1563 C C     . LYS A 1 209 ? 73.720  85.527  110.464 1.00 71.91  ? 209 LYS A C     1 
ATOM   1564 O O     . LYS A 1 209 ? 73.302  84.956  109.455 1.00 71.91  ? 209 LYS A O     1 
ATOM   1565 C CB    . LYS A 1 209 ? 72.476  87.579  111.008 1.00 107.86 ? 209 LYS A CB    1 
ATOM   1566 C CG    . LYS A 1 209 ? 71.264  88.211  111.659 1.00 107.86 ? 209 LYS A CG    1 
ATOM   1567 C CD    . LYS A 1 209 ? 71.080  89.642  111.184 1.00 107.86 ? 209 LYS A CD    1 
ATOM   1568 C CE    . LYS A 1 209 ? 69.868  90.290  111.836 1.00 107.86 ? 209 LYS A CE    1 
ATOM   1569 N NZ    . LYS A 1 209 ? 69.685  91.705  111.399 1.00 107.86 ? 209 LYS A NZ    1 
ATOM   1570 N N     . LYS A 1 210 ? 75.004  85.673  110.697 1.00 75.56  ? 210 LYS A N     1 
ATOM   1571 C CA    . LYS A 1 210 ? 75.976  85.162  109.760 1.00 75.56  ? 210 LYS A CA    1 
ATOM   1572 C C     . LYS A 1 210 ? 76.718  83.966  110.316 1.00 75.56  ? 210 LYS A C     1 
ATOM   1573 O O     . LYS A 1 210 ? 77.051  83.054  109.558 1.00 75.56  ? 210 LYS A O     1 
ATOM   1574 C CB    . LYS A 1 210 ? 76.952  86.276  109.373 1.00 113.34 ? 210 LYS A CB    1 
ATOM   1575 C CG    . LYS A 1 210 ? 76.270  87.504  108.753 1.00 113.34 ? 210 LYS A CG    1 
ATOM   1576 C CD    . LYS A 1 210 ? 75.560  87.171  107.446 1.00 113.34 ? 210 LYS A CD    1 
ATOM   1577 C CE    . LYS A 1 210 ? 75.043  88.427  106.782 1.00 113.34 ? 210 LYS A CE    1 
ATOM   1578 N NZ    . LYS A 1 210 ? 74.312  88.144  105.527 1.00 113.34 ? 210 LYS A NZ    1 
ATOM   1579 N N     . LEU A 1 211 ? 76.940  83.911  111.628 1.00 77.25  ? 211 LEU A N     1 
ATOM   1580 C CA    . LEU A 1 211 ? 77.592  82.731  112.170 1.00 77.25  ? 211 LEU A CA    1 
ATOM   1581 C C     . LEU A 1 211 ? 76.575  81.679  112.551 1.00 77.25  ? 211 LEU A C     1 
ATOM   1582 O O     . LEU A 1 211 ? 76.938  80.597  113.023 1.00 77.25  ? 211 LEU A O     1 
ATOM   1583 C CB    . LEU A 1 211 ? 78.469  83.060  113.381 1.00 114.37 ? 211 LEU A CB    1 
ATOM   1584 C CG    . LEU A 1 211 ? 79.679  83.998  113.221 1.00 114.37 ? 211 LEU A CG    1 
ATOM   1585 C CD1   . LEU A 1 211 ? 80.324  84.234  114.581 1.00 114.37 ? 211 LEU A CD1   1 
ATOM   1586 C CD2   . LEU A 1 211 ? 80.712  83.417  112.270 1.00 114.37 ? 211 LEU A CD2   1 
ATOM   1587 N N     . GLU A 1 212 ? 75.307  82.007  112.369 1.00 78.73  ? 212 GLU A N     1 
ATOM   1588 C CA    . GLU A 1 212 ? 74.179  81.129  112.618 1.00 78.73  ? 212 GLU A CA    1 
ATOM   1589 C C     . GLU A 1 212 ? 74.200  80.533  114.004 1.00 78.73  ? 212 GLU A C     1 
ATOM   1590 O O     . GLU A 1 212 ? 73.976  79.344  114.175 1.00 78.73  ? 212 GLU A O     1 
ATOM   1591 C CB    . GLU A 1 212 ? 74.127  80.022  111.585 1.00 105.76 ? 212 GLU A CB    1 
ATOM   1592 C CG    . GLU A 1 212 ? 73.982  80.526  110.174 1.00 105.76 ? 212 GLU A CG    1 
ATOM   1593 C CD    . GLU A 1 212 ? 73.821  79.411  109.163 1.00 105.76 ? 212 GLU A CD    1 
ATOM   1594 O OE1   . GLU A 1 212 ? 74.143  78.266  109.482 1.00 105.76 ? 212 GLU A OE1   1 
ATOM   1595 O OE2   . GLU A 1 212 ? 73.362  79.682  108.049 1.00 105.76 ? 212 GLU A OE2   1 
ATOM   1596 N N     . VAL A 1 213 ? 74.444  81.353  115.008 1.00 75.79  ? 213 VAL A N     1 
ATOM   1597 C CA    . VAL A 1 213 ? 74.481  80.865  116.379 1.00 75.79  ? 213 VAL A CA    1 
ATOM   1598 C C     . VAL A 1 213 ? 73.220  81.298  117.113 1.00 75.79  ? 213 VAL A C     1 
ATOM   1599 O O     . VAL A 1 213 ? 72.987  82.495  117.305 1.00 75.79  ? 213 VAL A O     1 
ATOM   1600 C CB    . VAL A 1 213 ? 75.721  81.373  117.120 1.00 110.24 ? 213 VAL A CB    1 
ATOM   1601 C CG1   . VAL A 1 213 ? 75.744  80.807  118.529 1.00 110.24 ? 213 VAL A CG1   1 
ATOM   1602 C CG2   . VAL A 1 213 ? 76.962  81.006  116.354 1.00 110.24 ? 213 VAL A CG2   1 
ATOM   1603 N N     . GLU A 1 214 ? 72.449  80.324  117.598 1.00 79.15  ? 214 GLU A N     1 
ATOM   1604 C CA    . GLU A 1 214 ? 71.165  80.612  118.239 1.00 79.15  ? 214 GLU A CA    1 
ATOM   1605 C C     . GLU A 1 214 ? 71.308  81.417  119.523 1.00 79.15  ? 214 GLU A C     1 
ATOM   1606 O O     . GLU A 1 214 ? 70.450  82.251  119.834 1.00 79.15  ? 214 GLU A O     1 
ATOM   1607 C CB    . GLU A 1 214 ? 70.437  79.308  118.544 1.00 106.32 ? 214 GLU A CB    1 
ATOM   1608 C CG    . GLU A 1 214 ? 69.985  78.541  117.315 1.00 106.32 ? 214 GLU A CG    1 
ATOM   1609 C CD    . GLU A 1 214 ? 71.087  77.739  116.700 1.00 106.32 ? 214 GLU A CD    1 
ATOM   1610 O OE1   . GLU A 1 214 ? 72.190  77.731  117.253 1.00 106.32 ? 214 GLU A OE1   1 
ATOM   1611 O OE2   . GLU A 1 214 ? 70.856  77.118  115.666 1.00 106.32 ? 214 GLU A OE2   1 
ATOM   1612 N N     . ASN A 1 215 ? 72.338  81.147  120.295 1.00 74.92  ? 215 ASN A N     1 
ATOM   1613 C CA    . ASN A 1 215 ? 72.502  81.854  121.542 1.00 74.92  ? 215 ASN A CA    1 
ATOM   1614 C C     . ASN A 1 215 ? 73.943  81.814  121.984 1.00 74.92  ? 215 ASN A C     1 
ATOM   1615 O O     . ASN A 1 215 ? 74.297  81.009  122.840 1.00 74.92  ? 215 ASN A O     1 
ATOM   1616 C CB    . ASN A 1 215 ? 71.643  81.237  122.615 1.00 101.50 ? 215 ASN A CB    1 
ATOM   1617 C CG    . ASN A 1 215 ? 71.673  82.037  123.874 1.00 101.50 ? 215 ASN A CG    1 
ATOM   1618 O OD1   . ASN A 1 215 ? 72.027  83.219  123.860 1.00 101.50 ? 215 ASN A OD1   1 
ATOM   1619 N ND2   . ASN A 1 215 ? 71.299  81.414  124.977 1.00 101.50 ? 215 ASN A ND2   1 
ATOM   1620 N N     . PRO A 1 216 ? 74.797  82.626  121.397 1.00 68.47  ? 216 PRO A N     1 
ATOM   1621 C CA    . PRO A 1 216 ? 76.231  82.543  121.655 1.00 68.47  ? 216 PRO A CA    1 
ATOM   1622 C C     . PRO A 1 216 ? 76.497  82.905  123.075 1.00 68.47  ? 216 PRO A C     1 
ATOM   1623 O O     . PRO A 1 216 ? 75.876  83.817  123.598 1.00 68.47  ? 216 PRO A O     1 
ATOM   1624 C CB    . PRO A 1 216 ? 76.812  83.592  120.717 1.00 452.08 ? 216 PRO A CB    1 
ATOM   1625 C CG    . PRO A 1 216 ? 75.670  84.540  120.506 1.00 452.08 ? 216 PRO A CG    1 
ATOM   1626 C CD    . PRO A 1 216 ? 74.417  83.743  120.558 1.00 452.08 ? 216 PRO A CD    1 
ATOM   1627 N N     . SER A 1 217 ? 77.388  82.172  123.711 1.00 67.21  ? 217 SER A N     1 
ATOM   1628 C CA    . SER A 1 217 ? 77.738  82.576  125.039 1.00 67.21  ? 217 SER A CA    1 
ATOM   1629 C C     . SER A 1 217 ? 78.640  83.751  124.867 1.00 67.21  ? 217 SER A C     1 
ATOM   1630 O O     . SER A 1 217 ? 79.170  83.971  123.792 1.00 67.21  ? 217 SER A O     1 
ATOM   1631 C CB    . SER A 1 217 ? 78.438  81.471  125.790 1.00 90.53  ? 217 SER A CB    1 
ATOM   1632 O OG    . SER A 1 217 ? 79.713  81.282  125.257 1.00 90.53  ? 217 SER A OG    1 
ATOM   1633 N N     . LEU A 1 218 ? 78.853  84.497  125.924 1.00 64.97  ? 218 LEU A N     1 
ATOM   1634 C CA    . LEU A 1 218 ? 79.715  85.642  125.772 1.00 64.97  ? 218 LEU A CA    1 
ATOM   1635 C C     . LEU A 1 218 ? 81.098  85.206  125.316 1.00 64.97  ? 218 LEU A C     1 
ATOM   1636 O O     . LEU A 1 218 ? 81.741  85.879  124.502 1.00 64.97  ? 218 LEU A O     1 
ATOM   1637 C CB    . LEU A 1 218 ? 79.747  86.389  127.086 1.00 96.19  ? 218 LEU A CB    1 
ATOM   1638 C CG    . LEU A 1 218 ? 80.388  87.753  127.123 1.00 96.19  ? 218 LEU A CG    1 
ATOM   1639 C CD1   . LEU A 1 218 ? 79.725  88.704  126.109 1.00 96.19  ? 218 LEU A CD1   1 
ATOM   1640 C CD2   . LEU A 1 218 ? 80.207  88.272  128.517 1.00 96.19  ? 218 LEU A CD2   1 
ATOM   1641 N N     . GLU A 1 219 ? 81.532  84.046  125.781 1.00 64.47  ? 219 GLU A N     1 
ATOM   1642 C CA    . GLU A 1 219 ? 82.818  83.497  125.415 1.00 64.47  ? 219 GLU A CA    1 
ATOM   1643 C C     . GLU A 1 219 ? 82.860  83.011  123.980 1.00 64.47  ? 219 GLU A C     1 
ATOM   1644 O O     . GLU A 1 219 ? 83.945  82.847  123.434 1.00 64.47  ? 219 GLU A O     1 
ATOM   1645 C CB    . GLU A 1 219 ? 83.155  82.378  126.393 1.00 86.60  ? 219 GLU A CB    1 
ATOM   1646 C CG    . GLU A 1 219 ? 83.377  82.874  127.830 1.00 86.60  ? 219 GLU A CG    1 
ATOM   1647 C CD    . GLU A 1 219 ? 82.089  83.129  128.596 1.00 86.60  ? 219 GLU A CD    1 
ATOM   1648 O OE1   . GLU A 1 219 ? 81.010  82.841  128.069 1.00 86.60  ? 219 GLU A OE1   1 
ATOM   1649 O OE2   . GLU A 1 219 ? 82.162  83.621  129.723 1.00 86.60  ? 219 GLU A OE2   1 
ATOM   1650 N N     . ASP A 1 220 ? 81.723  82.739  123.368 1.00 64.19  ? 220 ASP A N     1 
ATOM   1651 C CA    . ASP A 1 220 ? 81.735  82.362  121.973 1.00 64.19  ? 220 ASP A CA    1 
ATOM   1652 C C     . ASP A 1 220 ? 81.770  83.601  121.122 1.00 64.19  ? 220 ASP A C     1 
ATOM   1653 O O     . ASP A 1 220 ? 82.326  83.603  120.029 1.00 64.19  ? 220 ASP A O     1 
ATOM   1654 C CB    . ASP A 1 220 ? 80.484  81.575  121.587 1.00 82.53  ? 220 ASP A CB    1 
ATOM   1655 C CG    . ASP A 1 220 ? 80.337  80.272  122.315 1.00 82.53  ? 220 ASP A CG    1 
ATOM   1656 O OD1   . ASP A 1 220 ? 81.222  79.419  122.226 1.00 82.53  ? 220 ASP A OD1   1 
ATOM   1657 O OD2   . ASP A 1 220 ? 79.301  80.097  122.966 1.00 82.53  ? 220 ASP A OD2   1 
ATOM   1658 N N     . LEU A 1 221 ? 81.158  84.667  121.616 1.00 62.23  ? 221 LEU A N     1 
ATOM   1659 C CA    . LEU A 1 221 ? 81.166  85.897  120.860 1.00 62.23  ? 221 LEU A CA    1 
ATOM   1660 C C     . LEU A 1 221 ? 82.578  86.303  120.654 1.00 62.23  ? 221 LEU A C     1 
ATOM   1661 O O     . LEU A 1 221 ? 82.957  86.758  119.578 1.00 62.23  ? 221 LEU A O     1 
ATOM   1662 C CB    . LEU A 1 221 ? 80.418  87.021  121.583 1.00 92.13  ? 221 LEU A CB    1 
ATOM   1663 C CG    . LEU A 1 221 ? 80.144  88.309  120.775 1.00 92.13  ? 221 LEU A CG    1 
ATOM   1664 C CD1   . LEU A 1 221 ? 79.205  88.008  119.614 1.00 92.13  ? 221 LEU A CD1   1 
ATOM   1665 C CD2   . LEU A 1 221 ? 79.582  89.411  121.667 1.00 92.13  ? 221 LEU A CD2   1 
ATOM   1666 N N     . ASN A 1 222 ? 83.386  86.030  121.635 1.00 61.70  ? 222 ASN A N     1 
ATOM   1667 C CA    . ASN A 1 222 ? 84.752  86.436  121.594 1.00 61.70  ? 222 ASN A CA    1 
ATOM   1668 C C     . ASN A 1 222 ? 85.500  85.870  120.436 1.00 61.70  ? 222 ASN A C     1 
ATOM   1669 O O     . ASN A 1 222 ? 86.577  86.354  120.125 1.00 61.70  ? 222 ASN A O     1 
ATOM   1670 C CB    . ASN A 1 222 ? 85.401  85.985  122.839 1.00 83.59  ? 222 ASN A CB    1 
ATOM   1671 C CG    . ASN A 1 222 ? 84.929  86.739  123.936 1.00 83.59  ? 222 ASN A CG    1 
ATOM   1672 O OD1   . ASN A 1 222 ? 84.276  87.758  123.732 1.00 83.59  ? 222 ASN A OD1   1 
ATOM   1673 N ND2   . ASN A 1 222 ? 85.241  86.311  125.127 1.00 83.59  ? 222 ASN A ND2   1 
ATOM   1674 N N     . LEU A 1 223 ? 85.003  84.819  119.836 1.00 59.46  ? 223 LEU A N     1 
ATOM   1675 C CA    . LEU A 1 223 ? 85.705  84.278  118.708 1.00 59.46  ? 223 LEU A CA    1 
ATOM   1676 C C     . LEU A 1 223 ? 85.636  85.220  117.548 1.00 59.46  ? 223 LEU A C     1 
ATOM   1677 O O     . LEU A 1 223 ? 86.572  85.277  116.753 1.00 59.46  ? 223 LEU A O     1 
ATOM   1678 C CB    . LEU A 1 223 ? 85.110  82.939  118.321 1.00 88.03  ? 223 LEU A CB    1 
ATOM   1679 C CG    . LEU A 1 223 ? 85.285  81.797  119.326 1.00 88.03  ? 223 LEU A CG    1 
ATOM   1680 C CD1   . LEU A 1 223 ? 84.463  80.609  118.860 1.00 88.03  ? 223 LEU A CD1   1 
ATOM   1681 C CD2   . LEU A 1 223 ? 86.765  81.407  119.478 1.00 88.03  ? 223 LEU A CD2   1 
ATOM   1682 N N     . ILE A 1 224 ? 84.516  85.913  117.380 1.00 58.46  ? 224 ILE A N     1 
ATOM   1683 C CA    . ILE A 1 224 ? 84.445  86.825  116.262 1.00 58.46  ? 224 ILE A CA    1 
ATOM   1684 C C     . ILE A 1 224 ? 85.330  87.975  116.569 1.00 58.46  ? 224 ILE A C     1 
ATOM   1685 O O     . ILE A 1 224 ? 85.993  88.527  115.692 1.00 58.46  ? 224 ILE A O     1 
ATOM   1686 C CB    . ILE A 1 224 ? 83.007  87.289  115.941 1.00 86.55  ? 224 ILE A CB    1 
ATOM   1687 C CG1   . ILE A 1 224 ? 82.946  87.797  114.489 1.00 86.55  ? 224 ILE A CG1   1 
ATOM   1688 C CG2   . ILE A 1 224 ? 82.518  88.431  116.867 1.00 86.55  ? 224 ILE A CG2   1 
ATOM   1689 C CD1   . ILE A 1 224 ? 81.537  88.057  113.926 1.00 86.55  ? 224 ILE A CD1   1 
ATOM   1690 N N     . ILE A 1 225 ? 85.369  88.340  117.830 1.00 58.55  ? 225 ILE A N     1 
ATOM   1691 C CA    . ILE A 1 225 ? 86.175  89.461  118.204 1.00 58.55  ? 225 ILE A CA    1 
ATOM   1692 C C     . ILE A 1 225 ? 87.604  89.126  117.982 1.00 58.55  ? 225 ILE A C     1 
ATOM   1693 O O     . ILE A 1 225 ? 88.363  89.942  117.459 1.00 58.55  ? 225 ILE A O     1 
ATOM   1694 C CB    . ILE A 1 225 ? 85.945  89.875  119.649 1.00 86.68  ? 225 ILE A CB    1 
ATOM   1695 C CG1   . ILE A 1 225 ? 84.542  90.418  119.760 1.00 86.68  ? 225 ILE A CG1   1 
ATOM   1696 C CG2   . ILE A 1 225 ? 86.967  90.942  120.021 1.00 86.68  ? 225 ILE A CG2   1 
ATOM   1697 C CD1   . ILE A 1 225 ? 84.055  90.602  121.151 1.00 86.68  ? 225 ILE A CD1   1 
ATOM   1698 N N     . ALA A 1 226 ? 87.997  87.942  118.390 1.00 58.96  ? 226 ALA A N     1 
ATOM   1699 C CA    . ALA A 1 226 ? 89.368  87.560  118.185 1.00 58.96  ? 226 ALA A CA    1 
ATOM   1700 C C     . ALA A 1 226 ? 89.674  87.517  116.719 1.00 58.96  ? 226 ALA A C     1 
ATOM   1701 O O     . ALA A 1 226 ? 90.725  87.978  116.301 1.00 58.96  ? 226 ALA A O     1 
ATOM   1702 C CB    . ALA A 1 226 ? 89.646  86.224  118.827 1.00 80.40  ? 226 ALA A CB    1 
ATOM   1703 N N     . GLN A 1 227 ? 88.750  87.041  115.904 1.00 63.76  ? 227 GLN A N     1 
ATOM   1704 C CA    . GLN A 1 227 ? 89.078  86.998  114.495 1.00 63.76  ? 227 GLN A CA    1 
ATOM   1705 C C     . GLN A 1 227 ? 89.402  88.387  113.998 1.00 63.76  ? 227 GLN A C     1 
ATOM   1706 O O     . GLN A 1 227 ? 90.387  88.585  113.272 1.00 63.76  ? 227 GLN A O     1 
ATOM   1707 C CB    . GLN A 1 227 ? 87.943  86.383  113.677 1.00 89.09  ? 227 GLN A CB    1 
ATOM   1708 C CG    . GLN A 1 227 ? 88.296  86.228  112.206 1.00 89.09  ? 227 GLN A CG    1 
ATOM   1709 C CD    . GLN A 1 227 ? 87.196  85.653  111.292 1.00 89.09  ? 227 GLN A CD    1 
ATOM   1710 O OE1   . GLN A 1 227 ? 86.249  84.960  111.705 1.00 89.09  ? 227 GLN A OE1   1 
ATOM   1711 N NE2   . GLN A 1 227 ? 87.348  85.952  110.007 1.00 89.09  ? 227 GLN A NE2   1 
ATOM   1712 N N     . VAL A 1 228 ? 88.611  89.379  114.411 1.00 63.04  ? 228 VAL A N     1 
ATOM   1713 C CA    . VAL A 1 228 ? 88.885  90.746  113.969 1.00 63.04  ? 228 VAL A CA    1 
ATOM   1714 C C     . VAL A 1 228 ? 90.202  91.214  114.513 1.00 63.04  ? 228 VAL A C     1 
ATOM   1715 O O     . VAL A 1 228 ? 91.016  91.793  113.804 1.00 63.04  ? 228 VAL A O     1 
ATOM   1716 C CB    . VAL A 1 228 ? 87.779  91.714  114.394 1.00 91.69  ? 228 VAL A CB    1 
ATOM   1717 C CG1   . VAL A 1 228 ? 88.187  93.145  114.056 1.00 91.69  ? 228 VAL A CG1   1 
ATOM   1718 C CG2   . VAL A 1 228 ? 86.476  91.354  113.711 1.00 91.69  ? 228 VAL A CG2   1 
ATOM   1719 N N     . LEU A 1 229 ? 90.424  90.999  115.781 1.00 60.35  ? 229 LEU A N     1 
ATOM   1720 C CA    . LEU A 1 229 ? 91.605  91.536  116.404 1.00 60.35  ? 229 LEU A CA    1 
ATOM   1721 C C     . LEU A 1 229 ? 92.854  90.975  115.790 1.00 60.35  ? 229 LEU A C     1 
ATOM   1722 O O     . LEU A 1 229 ? 93.812  91.709  115.549 1.00 60.35  ? 229 LEU A O     1 
ATOM   1723 C CB    . LEU A 1 229 ? 91.565  91.247  117.887 1.00 89.35  ? 229 LEU A CB    1 
ATOM   1724 C CG    . LEU A 1 229 ? 92.709  91.742  118.738 1.00 89.35  ? 229 LEU A CG    1 
ATOM   1725 C CD1   . LEU A 1 229 ? 92.849  93.202  118.659 1.00 89.35  ? 229 LEU A CD1   1 
ATOM   1726 C CD2   . LEU A 1 229 ? 92.439  91.350  120.160 1.00 89.35  ? 229 LEU A CD2   1 
ATOM   1727 N N     . THR A 1 230 ? 92.874  89.682  115.511 1.00 62.99  ? 230 THR A N     1 
ATOM   1728 C CA    . THR A 1 230 ? 94.073  89.098  114.928 1.00 62.99  ? 230 THR A CA    1 
ATOM   1729 C C     . THR A 1 230 ? 94.282  89.563  113.506 1.00 62.99  ? 230 THR A C     1 
ATOM   1730 O O     . THR A 1 230 ? 95.417  89.836  113.107 1.00 62.99  ? 230 THR A O     1 
ATOM   1731 C CB    . THR A 1 230 ? 94.018  87.573  114.935 1.00 88.19  ? 230 THR A CB    1 
ATOM   1732 O OG1   . THR A 1 230 ? 92.881  87.131  114.186 1.00 88.19  ? 230 THR A OG1   1 
ATOM   1733 C CG2   . THR A 1 230 ? 93.929  87.043  116.339 1.00 88.19  ? 230 THR A CG2   1 
ATOM   1734 N N     . ASN A 1 231 ? 93.212  89.669  112.724 1.00 66.35  ? 231 ASN A N     1 
ATOM   1735 C CA    . ASN A 1 231 ? 93.411  90.024  111.330 1.00 66.35  ? 231 ASN A CA    1 
ATOM   1736 C C     . ASN A 1 231 ? 93.744  91.503  111.136 1.00 66.35  ? 231 ASN A C     1 
ATOM   1737 O O     . ASN A 1 231 ? 94.455  91.864  110.200 1.00 66.35  ? 231 ASN A O     1 
ATOM   1738 C CB    . ASN A 1 231 ? 92.197  89.585  110.556 1.00 89.89  ? 231 ASN A CB    1 
ATOM   1739 C CG    . ASN A 1 231 ? 92.170  88.119  110.394 1.00 89.89  ? 231 ASN A CG    1 
ATOM   1740 O OD1   . ASN A 1 231 ? 93.211  87.450  110.390 1.00 89.89  ? 231 ASN A OD1   1 
ATOM   1741 N ND2   . ASN A 1 231 ? 90.996  87.586  110.255 1.00 89.89  ? 231 ASN A ND2   1 
ATOM   1742 N N     . VAL A 1 232 ? 93.269  92.359  112.021 1.00 66.70  ? 232 VAL A N     1 
ATOM   1743 C CA    . VAL A 1 232 ? 93.650  93.751  111.975 1.00 66.70  ? 232 VAL A CA    1 
ATOM   1744 C C     . VAL A 1 232 ? 95.075  93.885  112.393 1.00 66.70  ? 232 VAL A C     1 
ATOM   1745 O O     . VAL A 1 232 ? 95.862  94.564  111.747 1.00 66.70  ? 232 VAL A O     1 
ATOM   1746 C CB    . VAL A 1 232 ? 92.755  94.582  112.908 1.00 97.02  ? 232 VAL A CB    1 
ATOM   1747 C CG1   . VAL A 1 232 ? 93.270  95.987  113.036 1.00 97.02  ? 232 VAL A CG1   1 
ATOM   1748 C CG2   . VAL A 1 232 ? 91.339  94.613  112.389 1.00 97.02  ? 232 VAL A CG2   1 
ATOM   1749 N N     . THR A 1 233 ? 95.421  93.248  113.492 1.00 62.93  ? 233 THR A N     1 
ATOM   1750 C CA    . THR A 1 233 ? 96.746  93.375  114.054 1.00 62.93  ? 233 THR A CA    1 
ATOM   1751 C C     . THR A 1 233 ? 97.761  92.827  113.103 1.00 62.93  ? 233 THR A C     1 
ATOM   1752 O O     . THR A 1 233 ? 98.860  93.375  112.977 1.00 62.93  ? 233 THR A O     1 
ATOM   1753 C CB    . THR A 1 233 ? 96.845  92.640  115.382 1.00 88.10  ? 233 THR A CB    1 
ATOM   1754 O OG1   . THR A 1 233 ? 95.883  93.172  116.304 1.00 88.10  ? 233 THR A OG1   1 
ATOM   1755 C CG2   . THR A 1 233 ? 98.207  92.839  115.959 1.00 88.10  ? 233 THR A CG2   1 
ATOM   1756 N N     . ALA A 1 234 ? 97.383  91.781  112.371 1.00 63.33  ? 234 ALA A N     1 
ATOM   1757 C CA    . ALA A 1 234 ? 98.292  91.087  111.462 1.00 63.33  ? 234 ALA A CA    1 
ATOM   1758 C C     . ALA A 1 234 ? 98.887  91.993  110.383 1.00 63.33  ? 234 ALA A C     1 
ATOM   1759 O O     . ALA A 1 234 ? 99.925  91.651  109.805 1.00 63.33  ? 234 ALA A O     1 
ATOM   1760 C CB    . ALA A 1 234 ? 97.570  89.921  110.795 1.00 86.36  ? 234 ALA A CB    1 
ATOM   1761 N N     . SER A 1 235 ? 98.281  93.148  110.101 1.00 62.25  ? 235 SER A N     1 
ATOM   1762 C CA    . SER A 1 235 ? 98.844  94.026  109.081 1.00 62.25  ? 235 SER A CA    1 
ATOM   1763 C C     . SER A 1 235 ? 100.230 94.457  109.446 1.00 62.25  ? 235 SER A C     1 
ATOM   1764 O O     . SER A 1 235 ? 101.000 94.865  108.585 1.00 62.25  ? 235 SER A O     1 
ATOM   1765 C CB    . SER A 1 235 ? 98.014  95.269  108.913 1.00 83.85  ? 235 SER A CB    1 
ATOM   1766 O OG    . SER A 1 235 ? 98.201  96.116  110.012 1.00 83.85  ? 235 SER A OG    1 
ATOM   1767 N N     . LEU A 1 236 ? 100.563 94.364  110.697 1.00 61.72  ? 236 LEU A N     1 
ATOM   1768 C CA    . LEU A 1 236 ? 101.850 94.760  111.157 1.00 61.72  ? 236 LEU A CA    1 
ATOM   1769 C C     . LEU A 1 236 ? 102.783 93.594  111.402 1.00 61.72  ? 236 LEU A C     1 
ATOM   1770 O O     . LEU A 1 236 ? 103.898 93.824  111.856 1.00 61.72  ? 236 LEU A O     1 
ATOM   1771 C CB    . LEU A 1 236 ? 101.703 95.564  112.430 1.00 91.38  ? 236 LEU A CB    1 
ATOM   1772 C CG    . LEU A 1 236 ? 100.807 96.804  112.347 1.00 91.38  ? 236 LEU A CG    1 
ATOM   1773 C CD1   . LEU A 1 236 ? 100.784 97.507  113.707 1.00 91.38  ? 236 LEU A CD1   1 
ATOM   1774 C CD2   . LEU A 1 236 ? 101.261 97.748  111.227 1.00 91.38  ? 236 LEU A CD2   1 
ATOM   1775 N N     . ARG A 1 237 ? 102.383 92.357  111.147 1.00 60.28  ? 237 ARG A N     1 
ATOM   1776 C CA    . ARG A 1 237 ? 103.300 91.258  111.420 1.00 60.28  ? 237 ARG A CA    1 
ATOM   1777 C C     . ARG A 1 237 ? 103.684 90.463  110.181 1.00 60.28  ? 237 ARG A C     1 
ATOM   1778 O O     . ARG A 1 237 ? 104.795 89.941  110.108 1.00 60.28  ? 237 ARG A O     1 
ATOM   1779 C CB    . ARG A 1 237 ? 102.720 90.331  112.483 1.00 88.57  ? 237 ARG A CB    1 
ATOM   1780 C CG    . ARG A 1 237 ? 101.660 89.447  111.995 1.00 88.57  ? 237 ARG A CG    1 
ATOM   1781 C CD    . ARG A 1 237 ? 101.052 88.597  113.065 1.00 88.57  ? 237 ARG A CD    1 
ATOM   1782 N NE    . ARG A 1 237 ? 100.372 89.362  114.101 1.00 88.57  ? 237 ARG A NE    1 
ATOM   1783 C CZ    . ARG A 1 237 ? 100.786 89.500  115.360 1.00 88.57  ? 237 ARG A CZ    1 
ATOM   1784 N NH1   . ARG A 1 237 ? 101.916 88.971  115.794 1.00 88.57  ? 237 ARG A NH1   1 
ATOM   1785 N NH2   . ARG A 1 237 ? 100.032 90.169  116.220 1.00 88.57  ? 237 ARG A NH2   1 
ATOM   1786 N N     . PHE A 1 238 ? 102.805 90.359  109.194 1.00 62.72  ? 238 PHE A N     1 
ATOM   1787 C CA    . PHE A 1 238 ? 103.146 89.657  107.964 1.00 62.72  ? 238 PHE A CA    1 
ATOM   1788 C C     . PHE A 1 238 ? 103.236 90.705  106.885 1.00 62.72  ? 238 PHE A C     1 
ATOM   1789 O O     . PHE A 1 238 ? 102.238 91.060  106.262 1.00 62.72  ? 238 PHE A O     1 
ATOM   1790 C CB    . PHE A 1 238 ? 102.177 88.585  107.602 1.00 87.52  ? 238 PHE A CB    1 
ATOM   1791 C CG    . PHE A 1 238 ? 102.110 87.516  108.597 1.00 87.52  ? 238 PHE A CG    1 
ATOM   1792 C CD1   . PHE A 1 238 ? 103.220 86.749  108.880 1.00 87.52  ? 238 PHE A CD1   1 
ATOM   1793 C CD2   . PHE A 1 238 ? 100.954 87.298  109.315 1.00 87.52  ? 238 PHE A CD2   1 
ATOM   1794 C CE1   . PHE A 1 238 ? 103.178 85.763  109.858 1.00 87.52  ? 238 PHE A CE1   1 
ATOM   1795 C CE2   . PHE A 1 238 ? 100.900 86.313  110.288 1.00 87.52  ? 238 PHE A CE2   1 
ATOM   1796 C CZ    . PHE A 1 238 ? 102.016 85.546  110.559 1.00 87.52  ? 238 PHE A CZ    1 
ATOM   1797 N N     . SER A 1 239 ? 104.465 91.156  106.665 1.00 61.42  ? 239 SER A N     1 
ATOM   1798 C CA    . SER A 1 239 ? 104.786 92.315  105.854 1.00 61.42  ? 239 SER A CA    1 
ATOM   1799 C C     . SER A 1 239 ? 104.218 92.221  104.457 1.00 61.42  ? 239 SER A C     1 
ATOM   1800 O O     . SER A 1 239 ? 104.327 91.186  103.798 1.00 61.42  ? 239 SER A O     1 
ATOM   1801 C CB    . SER A 1 239 ? 106.291 92.445  105.742 1.00 82.73  ? 239 SER A CB    1 
ATOM   1802 O OG    . SER A 1 239 ? 106.857 92.674  107.000 1.00 82.73  ? 239 SER A OG    1 
ATOM   1803 N N     . GLY A 1 240 ? 103.662 93.337  103.997 1.00 64.18  ? 240 GLY A N     1 
ATOM   1804 C CA    . GLY A 1 240 ? 103.057 93.414  102.700 1.00 64.18  ? 240 GLY A CA    1 
ATOM   1805 C C     . GLY A 1 240 ? 103.616 94.494  101.811 1.00 64.18  ? 240 GLY A C     1 
ATOM   1806 O O     . GLY A 1 240 ? 104.781 94.877  101.906 1.00 64.18  ? 240 GLY A O     1 
ATOM   1807 N N     . THR A 1 241 ? 102.731 94.994  100.945 1.00 67.16  ? 241 THR A N     1 
ATOM   1808 C CA    . THR A 1 241 ? 103.023 95.961  99.901  1.00 67.16  ? 241 THR A CA    1 
ATOM   1809 C C     . THR A 1 241 ? 103.199 97.394  100.389 1.00 67.16  ? 241 THR A C     1 
ATOM   1810 O O     . THR A 1 241 ? 103.803 98.191  99.666  1.00 67.16  ? 241 THR A O     1 
ATOM   1811 C CB    . THR A 1 241 ? 101.910 95.940  98.860  1.00 94.02  ? 241 THR A CB    1 
ATOM   1812 O OG1   . THR A 1 241 ? 100.670 96.254  99.495  1.00 94.02  ? 241 THR A OG1   1 
ATOM   1813 C CG2   . THR A 1 241 ? 101.803 94.589  98.240  1.00 94.02  ? 241 THR A CG2   1 
ATOM   1814 N N     . LEU A 1 242 ? 102.682 97.768  101.554 1.00 67.03  ? 242 LEU A N     1 
ATOM   1815 C CA    . LEU A 1 242 ? 102.888 99.113  102.074 1.00 67.03  ? 242 LEU A CA    1 
ATOM   1816 C C     . LEU A 1 242 ? 103.737 99.017  103.333 1.00 67.03  ? 242 LEU A C     1 
ATOM   1817 O O     . LEU A 1 242 ? 103.578 98.095  104.125 1.00 67.03  ? 242 LEU A O     1 
ATOM   1818 C CB    . LEU A 1 242 ? 101.569 99.814  102.402 1.00 99.24  ? 242 LEU A CB    1 
ATOM   1819 C CG    . LEU A 1 242 ? 100.457 99.862  101.359 1.00 99.24  ? 242 LEU A CG    1 
ATOM   1820 C CD1   . LEU A 1 242 ? 99.260  100.646 101.934 1.00 99.24  ? 242 LEU A CD1   1 
ATOM   1821 C CD2   . LEU A 1 242 ? 100.914 100.464 100.052 1.00 99.24  ? 242 LEU A CD2   1 
ATOM   1822 N N     . ASN A 1 243 ? 104.600 99.984  103.573 1.00 66.41  ? 243 ASN A N     1 
ATOM   1823 C CA    . ASN A 1 243 ? 105.425 99.896  104.774 1.00 66.41  ? 243 ASN A CA    1 
ATOM   1824 C C     . ASN A 1 243 ? 104.705 100.501 105.965 1.00 66.41  ? 243 ASN A C     1 
ATOM   1825 O O     . ASN A 1 243 ? 104.852 101.687 106.268 1.00 66.41  ? 243 ASN A O     1 
ATOM   1826 C CB    . ASN A 1 243 ? 106.756 100.576 104.546 1.00 89.97  ? 243 ASN A CB    1 
ATOM   1827 C CG    . ASN A 1 243 ? 107.602 99.837  103.558 1.00 89.97  ? 243 ASN A CG    1 
ATOM   1828 O OD1   . ASN A 1 243 ? 107.799 98.624  103.667 1.00 89.97  ? 243 ASN A OD1   1 
ATOM   1829 N ND2   . ASN A 1 243 ? 108.099 100.551 102.571 1.00 89.97  ? 243 ASN A ND2   1 
ATOM   1830 N N     . LEU A 1 244 ? 103.937 99.675  106.665 1.00 61.97  ? 244 LEU A N     1 
ATOM   1831 C CA    . LEU A 1 244 ? 103.104 100.148 107.760 1.00 61.97  ? 244 LEU A CA    1 
ATOM   1832 C C     . LEU A 1 244 ? 103.699 99.857  109.124 1.00 61.97  ? 244 LEU A C     1 
ATOM   1833 O O     . LEU A 1 244 ? 104.541 98.982  109.297 1.00 61.97  ? 244 LEU A O     1 
ATOM   1834 C CB    . LEU A 1 244 ? 101.718 99.556  107.670 1.00 91.75  ? 244 LEU A CB    1 
ATOM   1835 C CG    . LEU A 1 244 ? 101.013 99.824  106.367 1.00 91.75  ? 244 LEU A CG    1 
ATOM   1836 C CD1   . LEU A 1 244 ? 99.713  99.096  106.384 1.00 91.75  ? 244 LEU A CD1   1 
ATOM   1837 C CD2   . LEU A 1 244 ? 100.790 101.279 106.152 1.00 91.75  ? 244 LEU A CD2   1 
ATOM   1838 N N     . ASP A 1 245 ? 103.227 100.624 110.089 1.00 60.40  ? 245 ASP A N     1 
ATOM   1839 C CA    . ASP A 1 245 ? 103.577 100.560 111.501 1.00 60.40  ? 245 ASP A CA    1 
ATOM   1840 C C     . ASP A 1 245 ? 102.329 100.972 112.256 1.00 60.40  ? 245 ASP A C     1 
ATOM   1841 O O     . ASP A 1 245 ? 101.327 101.356 111.646 1.00 60.40  ? 245 ASP A O     1 
ATOM   1842 C CB    . ASP A 1 245 ? 104.739 101.514 111.816 1.00 77.66  ? 245 ASP A CB    1 
ATOM   1843 C CG    . ASP A 1 245 ? 105.464 101.220 113.156 1.00 77.66  ? 245 ASP A CG    1 
ATOM   1844 O OD1   . ASP A 1 245 ? 104.879 100.599 114.048 1.00 77.66  ? 245 ASP A OD1   1 
ATOM   1845 O OD2   . ASP A 1 245 ? 106.616 101.655 113.312 1.00 77.66  ? 245 ASP A OD2   1 
ATOM   1846 N N     . LEU A 1 246 ? 102.379 100.940 113.573 1.00 55.19  ? 246 LEU A N     1 
ATOM   1847 C CA    . LEU A 1 246 ? 101.180 101.318 114.295 1.00 55.19  ? 246 LEU A CA    1 
ATOM   1848 C C     . LEU A 1 246 ? 100.988 102.807 114.227 1.00 55.19  ? 246 LEU A C     1 
ATOM   1849 O O     . LEU A 1 246 ? 99.861  103.298 114.039 1.00 55.19  ? 246 LEU A O     1 
ATOM   1850 C CB    . LEU A 1 246 ? 101.225 100.829 115.733 1.00 81.71  ? 246 LEU A CB    1 
ATOM   1851 C CG    . LEU A 1 246 ? 99.975  101.044 116.619 1.00 81.71  ? 246 LEU A CG    1 
ATOM   1852 C CD1   . LEU A 1 246 ? 98.688  100.486 115.984 1.00 81.71  ? 246 LEU A CD1   1 
ATOM   1853 C CD2   . LEU A 1 246 ? 100.184 100.368 117.981 1.00 81.71  ? 246 LEU A CD2   1 
ATOM   1854 N N     . GLY A 1 247 ? 102.077 103.548 114.343 1.00 54.79  ? 247 GLY A N     1 
ATOM   1855 C CA    . GLY A 1 247 ? 101.967 104.992 114.259 1.00 54.79  ? 247 GLY A CA    1 
ATOM   1856 C C     . GLY A 1 247 ? 101.459 105.421 112.903 1.00 54.79  ? 247 GLY A C     1 
ATOM   1857 O O     . GLY A 1 247 ? 100.676 106.369 112.780 1.00 54.79  ? 247 GLY A O     1 
ATOM   1858 N N     . LYS A 1 248 ? 101.880 104.722 111.873 1.00 56.82  ? 248 LYS A N     1 
ATOM   1859 C CA    . LYS A 1 248 ? 101.439 105.081 110.547 1.00 56.82  ? 248 LYS A CA    1 
ATOM   1860 C C     . LYS A 1 248 ? 99.963  104.835 110.379 1.00 56.82  ? 248 LYS A C     1 
ATOM   1861 O O     . LYS A 1 248 ? 99.283  105.644 109.754 1.00 56.82  ? 248 LYS A O     1 
ATOM   1862 C CB    . LYS A 1 248 ? 102.246 104.321 109.510 1.00 85.23  ? 248 LYS A CB    1 
ATOM   1863 C CG    . LYS A 1 248 ? 103.671 104.820 109.413 1.00 85.23  ? 248 LYS A CG    1 
ATOM   1864 C CD    . LYS A 1 248 ? 104.476 104.066 108.373 1.00 85.23  ? 248 LYS A CD    1 
ATOM   1865 C CE    . LYS A 1 248 ? 105.857 104.688 108.212 1.00 85.23  ? 248 LYS A CE    1 
ATOM   1866 N NZ    . LYS A 1 248 ? 106.703 103.980 107.214 1.00 85.23  ? 248 LYS A NZ    1 
ATOM   1867 N N     . LEU A 1 249 ? 99.439  103.747 110.929 1.00 58.25  ? 249 LEU A N     1 
ATOM   1868 C CA    . LEU A 1 249 ? 98.012  103.505 110.807 1.00 58.25  ? 249 LEU A CA    1 
ATOM   1869 C C     . LEU A 1 249 ? 97.238  104.635 111.446 1.00 58.25  ? 249 LEU A C     1 
ATOM   1870 O O     . LEU A 1 249 ? 96.222  105.095 110.910 1.00 58.25  ? 249 LEU A O     1 
ATOM   1871 C CB    . LEU A 1 249 ? 97.627  102.202 111.476 1.00 86.24  ? 249 LEU A CB    1 
ATOM   1872 C CG    . LEU A 1 249 ? 98.077  100.921 110.825 1.00 86.24  ? 249 LEU A CG    1 
ATOM   1873 C CD1   . LEU A 1 249 ? 97.811  99.764  111.770 1.00 86.24  ? 249 LEU A CD1   1 
ATOM   1874 C CD2   . LEU A 1 249 ? 97.347  100.709 109.520 1.00 86.24  ? 249 LEU A CD2   1 
ATOM   1875 N N     . VAL A 1 250 ? 97.733  105.117 112.576 1.00 57.71  ? 250 VAL A N     1 
ATOM   1876 C CA    . VAL A 1 250 ? 97.084  106.222 113.255 1.00 57.71  ? 250 VAL A CA    1 
ATOM   1877 C C     . VAL A 1 250 ? 97.047  107.447 112.366 1.00 57.71  ? 250 VAL A C     1 
ATOM   1878 O O     . VAL A 1 250 ? 95.994  108.074 112.202 1.00 57.71  ? 250 VAL A O     1 
ATOM   1879 C CB    . VAL A 1 250 ? 97.810  106.501 114.575 1.00 83.94  ? 250 VAL A CB    1 
ATOM   1880 C CG1   . VAL A 1 250 ? 97.336  107.765 115.188 1.00 83.94  ? 250 VAL A CG1   1 
ATOM   1881 C CG2   . VAL A 1 250 ? 97.607  105.331 115.532 1.00 83.94  ? 250 VAL A CG2   1 
ATOM   1882 N N     . THR A 1 251 ? 98.180  107.792 111.755 1.00 56.42  ? 251 THR A N     1 
ATOM   1883 C CA    . THR A 1 251 ? 98.201  108.970 110.893 1.00 56.42  ? 251 THR A CA    1 
ATOM   1884 C C     . THR A 1 251 ? 97.232  108.814 109.749 1.00 56.42  ? 251 THR A C     1 
ATOM   1885 O O     . THR A 1 251 ? 96.508  109.751 109.406 1.00 56.42  ? 251 THR A O     1 
ATOM   1886 C CB    . THR A 1 251 ? 99.575  109.239 110.310 1.00 78.99  ? 251 THR A CB    1 
ATOM   1887 O OG1   . THR A 1 251 ? 100.515 109.534 111.338 1.00 78.99  ? 251 THR A OG1   1 
ATOM   1888 C CG2   . THR A 1 251 ? 99.523  110.447 109.354 1.00 78.99  ? 251 THR A CG2   1 
ATOM   1889 N N     . ASN A 1 252 ? 97.202  107.647 109.135 1.00 57.08  ? 252 ASN A N     1 
ATOM   1890 C CA    . ASN A 1 252 ? 96.385  107.507 107.937 1.00 57.08  ? 252 ASN A CA    1 
ATOM   1891 C C     . ASN A 1 252 ? 94.896  107.436 108.209 1.00 57.08  ? 252 ASN A C     1 
ATOM   1892 O O     . ASN A 1 252 ? 94.120  107.911 107.380 1.00 57.08  ? 252 ASN A O     1 
ATOM   1893 C CB    . ASN A 1 252 ? 96.823  106.297 107.149 1.00 77.33  ? 252 ASN A CB    1 
ATOM   1894 C CG    . ASN A 1 252 ? 98.101  106.542 106.406 1.00 77.33  ? 252 ASN A CG    1 
ATOM   1895 O OD1   . ASN A 1 252 ? 98.504  107.696 106.177 1.00 77.33  ? 252 ASN A OD1   1 
ATOM   1896 N ND2   . ASN A 1 252 ? 98.750  105.466 106.004 1.00 77.33  ? 252 ASN A ND2   1 
ATOM   1897 N N     . LEU A 1 253 ? 94.460  106.865 109.324 1.00 56.57  ? 253 LEU A N     1 
ATOM   1898 C CA    . LEU A 1 253 ? 93.033  106.768 109.511 1.00 56.57  ? 253 LEU A CA    1 
ATOM   1899 C C     . LEU A 1 253 ? 92.383  107.886 110.326 1.00 56.57  ? 253 LEU A C     1 
ATOM   1900 O O     . LEU A 1 253 ? 91.151  107.915 110.390 1.00 56.57  ? 253 LEU A O     1 
ATOM   1901 C CB    . LEU A 1 253 ? 92.674  105.445 110.149 1.00 83.75  ? 253 LEU A CB    1 
ATOM   1902 C CG    . LEU A 1 253 ? 92.895  104.198 109.291 1.00 83.75  ? 253 LEU A CG    1 
ATOM   1903 C CD1   . LEU A 1 253 ? 92.619  102.961 110.132 1.00 83.75  ? 253 LEU A CD1   1 
ATOM   1904 C CD2   . LEU A 1 253 ? 91.977  104.191 108.050 1.00 83.75  ? 253 LEU A CD2   1 
ATOM   1905 N N     . VAL A 1 254 ? 93.122  108.794 110.948 1.00 58.98  ? 254 VAL A N     1 
ATOM   1906 C CA    . VAL A 1 254 ? 92.452  109.843 111.721 1.00 58.98  ? 254 VAL A CA    1 
ATOM   1907 C C     . VAL A 1 254 ? 92.905  111.265 111.408 1.00 58.98  ? 254 VAL A C     1 
ATOM   1908 O O     . VAL A 1 254 ? 93.927  111.706 111.919 1.00 58.98  ? 254 VAL A O     1 
ATOM   1909 C CB    . VAL A 1 254 ? 92.655  109.598 113.205 1.00 85.79  ? 254 VAL A CB    1 
ATOM   1910 C CG1   . VAL A 1 254 ? 91.945  110.678 113.987 1.00 85.79  ? 254 VAL A CG1   1 
ATOM   1911 C CG2   . VAL A 1 254 ? 92.119  108.231 113.548 1.00 85.79  ? 254 VAL A CG2   1 
ATOM   1912 N N     . PRO A 1 255 ? 92.151  112.014 110.625 1.00 62.20  ? 255 PRO A N     1 
ATOM   1913 C CA    . PRO A 1 255 ? 92.509  113.379 110.264 1.00 62.20  ? 255 PRO A CA    1 
ATOM   1914 C C     . PRO A 1 255 ? 92.281  114.433 111.308 1.00 62.20  ? 255 PRO A C     1 
ATOM   1915 O O     . PRO A 1 255 ? 92.753  115.559 111.116 1.00 62.20  ? 255 PRO A O     1 
ATOM   1916 C CB    . PRO A 1 255 ? 91.615  113.653 109.057 1.00 410.69 ? 255 PRO A CB    1 
ATOM   1917 C CG    . PRO A 1 255 ? 90.488  112.759 109.244 1.00 410.69 ? 255 PRO A CG    1 
ATOM   1918 C CD    . PRO A 1 255 ? 90.994  111.528 109.915 1.00 410.69 ? 255 PRO A CD    1 
ATOM   1919 N N     . PHE A 1 256 ? 91.535  114.178 112.353 1.00 64.56  ? 256 PHE A N     1 
ATOM   1920 C CA    . PHE A 1 256 ? 91.346  115.227 113.331 1.00 64.56  ? 256 PHE A CA    1 
ATOM   1921 C C     . PHE A 1 256 ? 91.476  114.673 114.727 1.00 64.56  ? 256 PHE A C     1 
ATOM   1922 O O     . PHE A 1 256 ? 91.135  113.520 114.992 1.00 64.56  ? 256 PHE A O     1 
ATOM   1923 C CB    . PHE A 1 256 ? 90.019  115.862 113.211 1.00 90.08  ? 256 PHE A CB    1 
ATOM   1924 C CG    . PHE A 1 256 ? 89.817  116.530 111.957 1.00 90.08  ? 256 PHE A CG    1 
ATOM   1925 C CD1   . PHE A 1 256 ? 90.231  117.786 111.800 1.00 90.08  ? 256 PHE A CD1   1 
ATOM   1926 C CD2   . PHE A 1 256 ? 89.204  115.891 110.940 1.00 90.08  ? 256 PHE A CD2   1 
ATOM   1927 C CE1   . PHE A 1 256 ? 90.043  118.416 110.637 1.00 90.08  ? 256 PHE A CE1   1 
ATOM   1928 C CE2   . PHE A 1 256 ? 89.002  116.501 109.768 1.00 90.08  ? 256 PHE A CE2   1 
ATOM   1929 C CZ    . PHE A 1 256 ? 89.428  117.770 109.602 1.00 90.08  ? 256 PHE A CZ    1 
ATOM   1930 N N     . SER A 1 257 ? 91.934  115.514 115.633 1.00 62.11  ? 257 SER A N     1 
ATOM   1931 C CA    . SER A 1 257 ? 91.902  115.097 117.009 1.00 62.11  ? 257 SER A CA    1 
ATOM   1932 C C     . SER A 1 257 ? 90.457  114.856 117.372 1.00 62.11  ? 257 SER A C     1 
ATOM   1933 O O     . SER A 1 257 ? 89.561  115.553 116.901 1.00 62.11  ? 257 SER A O     1 
ATOM   1934 C CB    . SER A 1 257 ? 92.484  116.159 117.904 1.00 83.66  ? 257 SER A CB    1 
ATOM   1935 O OG    . SER A 1 257 ? 93.829  116.401 117.584 1.00 83.66  ? 257 SER A OG    1 
ATOM   1936 N N     . ASN A 1 258 ? 90.235  113.846 118.169 1.00 62.20  ? 258 ASN A N     1 
ATOM   1937 C CA    . ASN A 1 258 ? 88.944  113.472 118.660 1.00 62.20  ? 258 ASN A CA    1 
ATOM   1938 C C     . ASN A 1 258 ? 88.012  112.822 117.667 1.00 62.20  ? 258 ASN A C     1 
ATOM   1939 O O     . ASN A 1 258 ? 86.916  112.440 118.072 1.00 62.20  ? 258 ASN A O     1 
ATOM   1940 C CB    . ASN A 1 258 ? 88.228  114.662 119.249 1.00 84.27  ? 258 ASN A CB    1 
ATOM   1941 C CG    . ASN A 1 258 ? 89.072  115.372 120.218 1.00 84.27  ? 258 ASN A CG    1 
ATOM   1942 O OD1   . ASN A 1 258 ? 89.852  114.766 120.957 1.00 84.27  ? 258 ASN A OD1   1 
ATOM   1943 N ND2   . ASN A 1 258 ? 88.942  116.669 120.241 1.00 84.27  ? 258 ASN A ND2   1 
ATOM   1944 N N     . LEU A 1 259 ? 88.400  112.599 116.433 1.00 64.99  ? 259 LEU A N     1 
ATOM   1945 C CA    . LEU A 1 259 ? 87.507  111.861 115.546 1.00 64.99  ? 259 LEU A CA    1 
ATOM   1946 C C     . LEU A 1 259 ? 88.187  110.576 115.165 1.00 64.99  ? 259 LEU A C     1 
ATOM   1947 O O     . LEU A 1 259 ? 88.325  110.240 113.993 1.00 64.99  ? 259 LEU A O     1 
ATOM   1948 C CB    . LEU A 1 259 ? 87.153  112.638 114.301 1.00 96.22  ? 259 LEU A CB    1 
ATOM   1949 C CG    . LEU A 1 259 ? 86.467  113.957 114.516 1.00 96.22  ? 259 LEU A CG    1 
ATOM   1950 C CD1   . LEU A 1 259 ? 86.320  114.616 113.222 1.00 96.22  ? 259 LEU A CD1   1 
ATOM   1951 C CD2   . LEU A 1 259 ? 85.128  113.765 115.084 1.00 96.22  ? 259 LEU A CD2   1 
ATOM   1952 N N     . HIS A 1 260 ? 88.658  109.896 116.169 1.00 59.86  ? 260 HIS A N     1 
ATOM   1953 C CA    . HIS A 1 260 ? 89.531  108.763 116.067 1.00 59.86  ? 260 HIS A CA    1 
ATOM   1954 C C     . HIS A 1 260 ? 88.835  107.458 116.333 1.00 59.86  ? 260 HIS A C     1 
ATOM   1955 O O     . HIS A 1 260 ? 89.498  106.427 116.500 1.00 59.86  ? 260 HIS A O     1 
ATOM   1956 C CB    . HIS A 1 260 ? 90.627  108.943 117.058 1.00 81.41  ? 260 HIS A CB    1 
ATOM   1957 C CG    . HIS A 1 260 ? 90.110  109.065 118.415 1.00 81.41  ? 260 HIS A CG    1 
ATOM   1958 N ND1   . HIS A 1 260 ? 88.971  109.776 118.684 1.00 81.41  ? 260 HIS A ND1   1 
ATOM   1959 C CD2   . HIS A 1 260 ? 90.547  108.579 119.591 1.00 81.41  ? 260 HIS A CD2   1 
ATOM   1960 C CE1   . HIS A 1 260 ? 88.723  109.730 119.974 1.00 81.41  ? 260 HIS A CE1   1 
ATOM   1961 N NE2   . HIS A 1 260 ? 89.667  109.009 120.549 1.00 81.41  ? 260 HIS A NE2   1 
ATOM   1962 N N     . PHE A 1 261 ? 87.522  107.467 116.392 1.00 60.41  ? 261 PHE A N     1 
ATOM   1963 C CA    . PHE A 1 261 ? 86.786  106.242 116.624 1.00 60.41  ? 261 PHE A CA    1 
ATOM   1964 C C     . PHE A 1 261 ? 86.591  105.515 115.324 1.00 60.41  ? 261 PHE A C     1 
ATOM   1965 O O     . PHE A 1 261 ? 86.007  106.061 114.390 1.00 60.41  ? 261 PHE A O     1 
ATOM   1966 C CB    . PHE A 1 261 ? 85.439  106.533 117.232 1.00 84.29  ? 261 PHE A CB    1 
ATOM   1967 C CG    . PHE A 1 261 ? 85.529  107.035 118.565 1.00 84.29  ? 261 PHE A CG    1 
ATOM   1968 C CD1   . PHE A 1 261 ? 85.983  106.233 119.568 1.00 84.29  ? 261 PHE A CD1   1 
ATOM   1969 C CD2   . PHE A 1 261 ? 85.176  108.318 118.840 1.00 84.29  ? 261 PHE A CD2   1 
ATOM   1970 C CE1   . PHE A 1 261 ? 86.084  106.693 120.831 1.00 84.29  ? 261 PHE A CE1   1 
ATOM   1971 C CE2   . PHE A 1 261 ? 85.266  108.793 120.109 1.00 84.29  ? 261 PHE A CE2   1 
ATOM   1972 C CZ    . PHE A 1 261 ? 85.726  107.976 121.109 1.00 84.29  ? 261 PHE A CZ    1 
ATOM   1973 N N     . LEU A 1 262 ? 87.045  104.284 115.269 1.00 56.66  ? 262 LEU A N     1 
ATOM   1974 C CA    . LEU A 1 262 ? 87.040  103.531 114.046 1.00 56.66  ? 262 LEU A CA    1 
ATOM   1975 C C     . LEU A 1 262 ? 86.074  102.357 114.042 1.00 56.66  ? 262 LEU A C     1 
ATOM   1976 O O     . LEU A 1 262 ? 85.799  101.727 115.060 1.00 56.66  ? 262 LEU A O     1 
ATOM   1977 C CB    . LEU A 1 262 ? 88.434  103.033 113.790 1.00 83.89  ? 262 LEU A CB    1 
ATOM   1978 C CG    . LEU A 1 262 ? 89.539  104.081 113.714 1.00 83.89  ? 262 LEU A CG    1 
ATOM   1979 C CD1   . LEU A 1 262 ? 90.873  103.393 113.618 1.00 83.89  ? 262 LEU A CD1   1 
ATOM   1980 C CD2   . LEU A 1 262 ? 89.334  105.005 112.528 1.00 83.89  ? 262 LEU A CD2   1 
ATOM   1981 N N     . MET A 1 263 ? 85.578  102.064 112.871 1.00 64.60  ? 263 MET A N     1 
ATOM   1982 C CA    . MET A 1 263 ? 84.785  100.895 112.623 1.00 64.60  ? 263 MET A CA    1 
ATOM   1983 C C     . MET A 1 263 ? 85.697  99.800  112.133 1.00 64.60  ? 263 MET A C     1 
ATOM   1984 O O     . MET A 1 263 ? 86.736  100.072 111.528 1.00 64.60  ? 263 MET A O     1 
ATOM   1985 C CB    . MET A 1 263 ? 83.763  101.155 111.553 1.00 92.81  ? 263 MET A CB    1 
ATOM   1986 C CG    . MET A 1 263 ? 82.793  102.141 111.889 1.00 92.81  ? 263 MET A CG    1 
ATOM   1987 S SD    . MET A 1 263 ? 81.635  102.332 110.565 1.00 92.81  ? 263 MET A SD    1 
ATOM   1988 C CE    . MET A 1 263 ? 80.823  103.829 111.122 1.00 92.81  ? 263 MET A CE    1 
ATOM   1989 N N     . ALA A 1 264 ? 85.277  98.557  112.321 1.00 63.97  ? 264 ALA A N     1 
ATOM   1990 C CA    . ALA A 1 264 ? 86.021  97.443  111.774 1.00 63.97  ? 264 ALA A CA    1 
ATOM   1991 C C     . ALA A 1 264 ? 85.085  96.387  111.205 1.00 63.97  ? 264 ALA A C     1 
ATOM   1992 O O     . ALA A 1 264 ? 83.994  96.149  111.728 1.00 63.97  ? 264 ALA A O     1 
ATOM   1993 C CB    . ALA A 1 264 ? 86.930  96.832  112.825 1.00 87.23  ? 264 ALA A CB    1 
ATOM   1994 N N     . SER A 1 265 ? 85.554  95.729  110.145 1.00 67.41  ? 265 SER A N     1 
ATOM   1995 C CA    . SER A 1 265 ? 84.826  94.662  109.473 1.00 67.41  ? 265 SER A CA    1 
ATOM   1996 C C     . SER A 1 265 ? 85.753  93.623  108.848 1.00 67.41  ? 265 SER A C     1 
ATOM   1997 O O     . SER A 1 265 ? 86.760  93.974  108.231 1.00 67.41  ? 265 SER A O     1 
ATOM   1998 C CB    . SER A 1 265 ? 83.963  95.248  108.386 1.00 90.80  ? 265 SER A CB    1 
ATOM   1999 O OG    . SER A 1 265 ? 83.304  94.225  107.689 1.00 90.80  ? 265 SER A OG    1 
ATOM   2000 N N     . THR A 1 266 ? 85.399  92.339  108.975 1.00 66.63  ? 266 THR A N     1 
ATOM   2001 C CA    . THR A 1 266 ? 86.203  91.294  108.354 1.00 66.63  ? 266 THR A CA    1 
ATOM   2002 C C     . THR A 1 266 ? 85.382  90.260  107.607 1.00 66.63  ? 266 THR A C     1 
ATOM   2003 O O     . THR A 1 266 ? 84.200  90.055  107.866 1.00 66.63  ? 266 THR A O     1 
ATOM   2004 C CB    . THR A 1 266 ? 87.052  90.539  109.354 1.00 93.28  ? 266 THR A CB    1 
ATOM   2005 O OG1   . THR A 1 266 ? 86.197  89.907  110.304 1.00 93.28  ? 266 THR A OG1   1 
ATOM   2006 C CG2   . THR A 1 266 ? 88.024  91.461  110.057 1.00 93.28  ? 266 THR A CG2   1 
ATOM   2007 N N     . ALA A 1 267 ? 86.062  89.561  106.710 1.00 67.35  ? 267 ALA A N     1 
ATOM   2008 C CA    . ALA A 1 267 ? 85.487  88.450  105.984 1.00 67.35  ? 267 ALA A CA    1 
ATOM   2009 C C     . ALA A 1 267 ? 86.596  87.484  105.624 1.00 67.35  ? 267 ALA A C     1 
ATOM   2010 O O     . ALA A 1 267 ? 87.761  87.881  105.551 1.00 67.35  ? 267 ALA A O     1 
ATOM   2011 C CB    . ALA A 1 267 ? 84.773  88.930  104.713 1.00 91.84  ? 267 ALA A CB    1 
ATOM   2012 N N     . PRO A 1 268 ? 86.285  86.240  105.403 1.00 70.84  ? 268 PRO A N     1 
ATOM   2013 C CA    . PRO A 1 268 ? 85.047  85.546  105.567 1.00 70.84  ? 268 PRO A CA    1 
ATOM   2014 C C     . PRO A 1 268 ? 84.948  85.425  107.021 1.00 70.84  ? 268 PRO A C     1 
ATOM   2015 O O     . PRO A 1 268 ? 85.975  85.452  107.680 1.00 70.84  ? 268 PRO A O     1 
ATOM   2016 C CB    . PRO A 1 268 ? 85.304  84.208  104.927 1.00 467.76 ? 268 PRO A CB    1 
ATOM   2017 C CG    . PRO A 1 268 ? 86.727  83.996  105.192 1.00 467.76 ? 268 PRO A CG    1 
ATOM   2018 C CD    . PRO A 1 268 ? 87.369  85.339  105.114 1.00 467.76 ? 268 PRO A CD    1 
ATOM   2019 N N     . LEU A 1 269 ? 83.772  85.294  107.585 1.00 79.60  ? 269 LEU A N     1 
ATOM   2020 C CA    . LEU A 1 269 ? 83.747  84.992  108.985 1.00 79.60  ? 269 LEU A CA    1 
ATOM   2021 C C     . LEU A 1 269 ? 83.976  83.520  109.069 1.00 79.60  ? 269 LEU A C     1 
ATOM   2022 O O     . LEU A 1 269 ? 83.505  82.765  108.220 1.00 79.60  ? 269 LEU A O     1 
ATOM   2023 C CB    . LEU A 1 269 ? 82.422  85.338  109.605 1.00 117.85 ? 269 LEU A CB    1 
ATOM   2024 C CG    . LEU A 1 269 ? 81.955  86.763  109.484 1.00 117.85 ? 269 LEU A CG    1 
ATOM   2025 C CD1   . LEU A 1 269 ? 80.590  86.845  110.145 1.00 117.85 ? 269 LEU A CD1   1 
ATOM   2026 C CD2   . LEU A 1 269 ? 82.956  87.704  110.136 1.00 117.85 ? 269 LEU A CD2   1 
ATOM   2027 N N     . VAL A 1 270 ? 84.675  83.093  110.075 1.00 89.82  ? 270 VAL A N     1 
ATOM   2028 C CA    . VAL A 1 270 ? 84.928  81.682  110.202 1.00 89.82  ? 270 VAL A CA    1 
ATOM   2029 C C     . VAL A 1 270 ? 83.951  81.102  111.187 1.00 89.82  ? 270 VAL A C     1 
ATOM   2030 O O     . VAL A 1 270 ? 83.843  81.566  112.322 1.00 89.82  ? 270 VAL A O     1 
ATOM   2031 C CB    . VAL A 1 270 ? 86.382  81.429  110.606 1.00 130.65 ? 270 VAL A CB    1 
ATOM   2032 C CG1   . VAL A 1 270 ? 86.631  79.936  110.815 1.00 130.65 ? 270 VAL A CG1   1 
ATOM   2033 C CG2   . VAL A 1 270 ? 87.281  82.000  109.494 1.00 130.65 ? 270 VAL A CG2   1 
ATOM   2034 N N     . LEU A 1 271 ? 83.217  80.116  110.746 1.00 97.30  ? 271 LEU A N     1 
ATOM   2035 C CA    . LEU A 1 271 ? 82.293  79.488  111.652 1.00 97.30  ? 271 LEU A CA    1 
ATOM   2036 C C     . LEU A 1 271 ? 83.115  78.790  112.710 1.00 97.30  ? 271 LEU A C     1 
ATOM   2037 O O     . LEU A 1 271 ? 84.139  78.181  112.410 1.00 97.30  ? 271 LEU A O     1 
ATOM   2038 C CB    . LEU A 1 271 ? 81.395  78.510  110.898 1.00 144.05 ? 271 LEU A CB    1 
ATOM   2039 C CG    . LEU A 1 271 ? 80.478  79.113  109.803 1.00 144.05 ? 271 LEU A CG    1 
ATOM   2040 C CD1   . LEU A 1 271 ? 79.762  78.006  109.041 1.00 144.05 ? 271 LEU A CD1   1 
ATOM   2041 C CD2   . LEU A 1 271 ? 79.454  80.062  110.410 1.00 144.05 ? 271 LEU A CD2   1 
ATOM   2042 N N     . ALA A 1 272 ? 82.662  78.873  113.955 1.00 97.23  ? 272 ALA A N     1 
ATOM   2043 C CA    . ALA A 1 272 ? 83.420  78.287  115.057 1.00 97.23  ? 272 ALA A CA    1 
ATOM   2044 C C     . ALA A 1 272 ? 83.668  76.803  114.854 1.00 97.23  ? 272 ALA A C     1 
ATOM   2045 O O     . ALA A 1 272 ? 84.719  76.287  115.248 1.00 97.23  ? 272 ALA A O     1 
ATOM   2046 C CB    . ALA A 1 272 ? 82.683  78.507  116.373 1.00 132.59 ? 272 ALA A CB    1 
ATOM   2047 N N     . GLY A 1 273 ? 82.721  76.105  114.244 1.00 98.05  ? 273 GLY A N     1 
ATOM   2048 C CA    . GLY A 1 273 ? 82.843  74.687  114.013 1.00 98.05  ? 273 GLY A CA    1 
ATOM   2049 C C     . GLY A 1 273 ? 83.532  74.331  112.723 1.00 98.05  ? 273 GLY A C     1 
ATOM   2050 O O     . GLY A 1 273 ? 83.580  73.153  112.366 1.00 98.05  ? 273 GLY A O     1 
ATOM   2051 N N     . LYS A 1 274 ? 84.039  75.322  111.989 1.00 100.02 ? 274 LYS A N     1 
ATOM   2052 C CA    . LYS A 1 274 ? 84.703  75.077  110.713 1.00 100.02 ? 274 LYS A CA    1 
ATOM   2053 C C     . LYS A 1 274 ? 83.809  74.258  109.797 1.00 100.02 ? 274 LYS A C     1 
ATOM   2054 O O     . LYS A 1 274 ? 84.262  73.330  109.126 1.00 100.02 ? 274 LYS A O     1 
ATOM   2055 C CB    . LYS A 1 274 ? 86.027  74.351  110.913 1.00 150.03 ? 274 LYS A CB    1 
ATOM   2056 C CG    . LYS A 1 274 ? 87.020  75.026  111.829 1.00 150.03 ? 274 LYS A CG    1 
ATOM   2057 C CD    . LYS A 1 274 ? 88.316  74.213  111.875 1.00 150.03 ? 274 LYS A CD    1 
ATOM   2058 C CE    . LYS A 1 274 ? 89.316  74.732  112.915 1.00 150.03 ? 274 LYS A CE    1 
ATOM   2059 N NZ    . LYS A 1 274 ? 89.861  76.070  112.571 1.00 150.03 ? 274 LYS A NZ    1 
ATOM   2060 N N     . GLU A 1 275 ? 82.524  74.606  109.782 1.00 99.74  ? 275 GLU A N     1 
ATOM   2061 C CA    . GLU A 1 275 ? 81.508  73.835  109.076 1.00 99.74  ? 275 GLU A CA    1 
ATOM   2062 C C     . GLU A 1 275 ? 81.486  74.040  107.565 1.00 99.74  ? 275 GLU A C     1 
ATOM   2063 O O     . GLU A 1 275 ? 81.036  73.149  106.838 1.00 99.74  ? 275 GLU A O     1 
ATOM   2064 C CB    . GLU A 1 275 ? 80.142  74.178  109.651 1.00 133.98 ? 275 GLU A CB    1 
ATOM   2065 C CG    . GLU A 1 275 ? 79.970  73.729  111.087 1.00 133.98 ? 275 GLU A CG    1 
ATOM   2066 C CD    . GLU A 1 275 ? 78.631  74.101  111.656 1.00 133.98 ? 275 GLU A CD    1 
ATOM   2067 O OE1   . GLU A 1 275 ? 77.804  74.636  110.919 1.00 133.98 ? 275 GLU A OE1   1 
ATOM   2068 O OE2   . GLU A 1 275 ? 78.412  73.867  112.844 1.00 133.98 ? 275 GLU A OE2   1 
ATOM   2069 N N     . SER A 1 276 ? 81.908  75.195  107.070 1.00 99.87  ? 276 SER A N     1 
ATOM   2070 C CA    . SER A 1 276 ? 81.816  75.423  105.639 1.00 99.87  ? 276 SER A CA    1 
ATOM   2071 C C     . SER A 1 276 ? 82.832  76.454  105.191 1.00 99.87  ? 276 SER A C     1 
ATOM   2072 O O     . SER A 1 276 ? 83.354  77.235  105.988 1.00 99.87  ? 276 SER A O     1 
ATOM   2073 C CB    . SER A 1 276 ? 80.420  75.886  105.245 1.00 134.52 ? 276 SER A CB    1 
ATOM   2074 O OG    . SER A 1 276 ? 80.147  77.167  105.773 1.00 134.52 ? 276 SER A OG    1 
ATOM   2075 N N     . TYR A 1 277 ? 83.077  76.456  103.887 1.00 101.20 ? 277 TYR A N     1 
ATOM   2076 C CA    . TYR A 1 277 ? 83.993  77.382  103.252 1.00 101.20 ? 277 TYR A CA    1 
ATOM   2077 C C     . TYR A 1 277 ? 83.345  77.976  102.002 1.00 101.20 ? 277 TYR A C     1 
ATOM   2078 O O     . TYR A 1 277 ? 82.553  77.320  101.321 1.00 101.20 ? 277 TYR A O     1 
ATOM   2079 C CB    . TYR A 1 277 ? 85.307  76.658  102.930 1.00 140.12 ? 277 TYR A CB    1 
ATOM   2080 C CG    . TYR A 1 277 ? 85.948  76.100  104.175 1.00 140.12 ? 277 TYR A CG    1 
ATOM   2081 C CD1   . TYR A 1 277 ? 85.611  74.844  104.645 1.00 140.12 ? 277 TYR A CD1   1 
ATOM   2082 C CD2   . TYR A 1 277 ? 86.860  76.850  104.891 1.00 140.12 ? 277 TYR A CD2   1 
ATOM   2083 C CE1   . TYR A 1 277 ? 86.165  74.349  105.793 1.00 140.12 ? 277 TYR A CE1   1 
ATOM   2084 C CE2   . TYR A 1 277 ? 87.423  76.362  106.039 1.00 140.12 ? 277 TYR A CE2   1 
ATOM   2085 C CZ    . TYR A 1 277 ? 87.075  75.113  106.489 1.00 140.12 ? 277 TYR A CZ    1 
ATOM   2086 O OH    . TYR A 1 277 ? 87.641  74.631  107.648 1.00 140.12 ? 277 TYR A OH    1 
ATOM   2087 N N     . GLU A 1 278 ? 83.682  79.229  101.711 1.00 96.13  ? 278 GLU A N     1 
ATOM   2088 C CA    . GLU A 1 278 ? 83.176  79.951  100.551 1.00 96.13  ? 278 GLU A CA    1 
ATOM   2089 C C     . GLU A 1 278 ? 84.260  80.069  99.487  1.00 96.13  ? 278 GLU A C     1 
ATOM   2090 O O     . GLU A 1 278 ? 85.447  79.950  99.779  1.00 96.13  ? 278 GLU A O     1 
ATOM   2091 C CB    . GLU A 1 278 ? 82.692  81.346  100.963 1.00 129.13 ? 278 GLU A CB    1 
ATOM   2092 C CG    . GLU A 1 278 ? 81.522  81.324  101.951 1.00 129.13 ? 278 GLU A CG    1 
ATOM   2093 C CD    . GLU A 1 278 ? 81.018  82.707  102.322 1.00 129.13 ? 278 GLU A CD    1 
ATOM   2094 O OE1   . GLU A 1 278 ? 81.633  83.696  101.920 1.00 129.13 ? 278 GLU A OE1   1 
ATOM   2095 O OE2   . GLU A 1 278 ? 80.003  82.801  103.015 1.00 129.13 ? 278 GLU A OE2   1 
ATOM   2096 N N     . LYS A 1 279 ? 83.859  80.277  98.242  1.00 90.84  ? 279 LYS A N     1 
ATOM   2097 C CA    . LYS A 1 279 ? 84.862  80.560  97.234  1.00 90.84  ? 279 LYS A CA    1 
ATOM   2098 C C     . LYS A 1 279 ? 85.490  81.892  97.585  1.00 90.84  ? 279 LYS A C     1 
ATOM   2099 O O     . LYS A 1 279 ? 84.791  82.883  97.792  1.00 90.84  ? 279 LYS A O     1 
ATOM   2100 C CB    . LYS A 1 279 ? 84.258  80.611  95.832  1.00 136.26 ? 279 LYS A CB    1 
ATOM   2101 C CG    . LYS A 1 279 ? 85.290  80.816  94.717  1.00 136.26 ? 279 LYS A CG    1 
ATOM   2102 C CD    . LYS A 1 279 ? 84.643  80.836  93.333  1.00 136.26 ? 279 LYS A CD    1 
ATOM   2103 C CE    . LYS A 1 279 ? 85.680  81.077  92.239  1.00 136.26 ? 279 LYS A CE    1 
ATOM   2104 N NZ    . LYS A 1 279 ? 85.068  81.112  90.881  1.00 136.26 ? 279 LYS A NZ    1 
ATOM   2105 N N     . MET A 1 280 ? 86.808  81.942  97.611  1.00 80.52  ? 280 MET A N     1 
ATOM   2106 C CA    . MET A 1 280 ? 87.479  83.148  98.067  1.00 80.52  ? 280 MET A CA    1 
ATOM   2107 C C     . MET A 1 280 ? 87.717  84.144  96.938  1.00 80.52  ? 280 MET A C     1 
ATOM   2108 O O     . MET A 1 280 ? 88.828  84.333  96.448  1.00 80.52  ? 280 MET A O     1 
ATOM   2109 C CB    . MET A 1 280 ? 88.746  82.736  98.770  1.00 115.68 ? 280 MET A CB    1 
ATOM   2110 C CG    . MET A 1 280 ? 88.408  81.787  99.913  1.00 115.68 ? 280 MET A CG    1 
ATOM   2111 S SD    . MET A 1 280 ? 87.259  82.512  101.076 1.00 115.68 ? 280 MET A SD    1 
ATOM   2112 C CE    . MET A 1 280 ? 88.321  83.720  101.780 1.00 115.68 ? 280 MET A CE    1 
ATOM   2113 N N     . THR A 1 281 ? 86.635  84.811  96.556  1.00 75.62  ? 281 THR A N     1 
ATOM   2114 C CA    . THR A 1 281 ? 86.601  85.777  95.467  1.00 75.62  ? 281 THR A CA    1 
ATOM   2115 C C     . THR A 1 281 ? 86.716  87.186  96.026  1.00 75.62  ? 281 THR A C     1 
ATOM   2116 O O     . THR A 1 281 ? 85.934  87.567  96.893  1.00 75.62  ? 281 THR A O     1 
ATOM   2117 C CB    . THR A 1 281 ? 85.295  85.627  94.690  1.00 105.87 ? 281 THR A CB    1 
ATOM   2118 O OG1   . THR A 1 281 ? 85.228  84.316  94.130  1.00 105.87 ? 281 THR A OG1   1 
ATOM   2119 C CG2   . THR A 1 281 ? 85.218  86.613  93.587  1.00 105.87 ? 281 THR A CG2   1 
ATOM   2120 N N     . ALA A 1 282 ? 87.652  87.981  95.517  1.00 71.37  ? 282 ALA A N     1 
ATOM   2121 C CA    . ALA A 1 282 ? 87.823  89.321  96.078  1.00 71.37  ? 282 ALA A CA    1 
ATOM   2122 C C     . ALA A 1 282 ? 86.538  90.090  96.033  1.00 71.37  ? 282 ALA A C     1 
ATOM   2123 O O     . ALA A 1 282 ? 86.226  90.848  96.946  1.00 71.37  ? 282 ALA A O     1 
ATOM   2124 C CB    . ALA A 1 282 ? 88.889  90.095  95.318  1.00 97.32  ? 282 ALA A CB    1 
ATOM   2125 N N     . LYS A 1 283 ? 85.778  89.905  94.975  1.00 70.99  ? 283 LYS A N     1 
ATOM   2126 C CA    . LYS A 1 283 ? 84.539  90.628  94.854  1.00 70.99  ? 283 LYS A CA    1 
ATOM   2127 C C     . LYS A 1 283 ? 83.570  90.228  95.933  1.00 70.99  ? 283 LYS A C     1 
ATOM   2128 O O     . LYS A 1 283 ? 82.859  91.075  96.495  1.00 70.99  ? 283 LYS A O     1 
ATOM   2129 C CB    . LYS A 1 283 ? 83.936  90.366  93.497  1.00 106.48 ? 283 LYS A CB    1 
ATOM   2130 C CG    . LYS A 1 283 ? 84.696  91.023  92.395  1.00 106.48 ? 283 LYS A CG    1 
ATOM   2131 C CD    . LYS A 1 283 ? 84.086  90.716  91.053  1.00 106.48 ? 283 LYS A CD    1 
ATOM   2132 C CE    . LYS A 1 283 ? 84.882  91.391  89.963  1.00 106.48 ? 283 LYS A CE    1 
ATOM   2133 N NZ    . LYS A 1 283 ? 84.363  91.086  88.610  1.00 106.48 ? 283 LYS A NZ    1 
ATOM   2134 N N     . GLU A 1 284 ? 83.521  88.939  96.230  1.00 72.32  ? 284 GLU A N     1 
ATOM   2135 C CA    . GLU A 1 284 ? 82.614  88.462  97.242  1.00 72.32  ? 284 GLU A CA    1 
ATOM   2136 C C     . GLU A 1 284 ? 83.050  88.936  98.591  1.00 72.32  ? 284 GLU A C     1 
ATOM   2137 O O     . GLU A 1 284 ? 82.237  89.347  99.430  1.00 72.32  ? 284 GLU A O     1 
ATOM   2138 C CB    . GLU A 1 284 ? 82.572  86.959  97.216  1.00 97.15  ? 284 GLU A CB    1 
ATOM   2139 C CG    . GLU A 1 284 ? 81.698  86.355  98.278  1.00 97.15  ? 284 GLU A CG    1 
ATOM   2140 C CD    . GLU A 1 284 ? 80.250  86.717  98.150  1.00 97.15  ? 284 GLU A CD    1 
ATOM   2141 O OE1   . GLU A 1 284 ? 79.789  86.958  97.033  1.00 97.15  ? 284 GLU A OE1   1 
ATOM   2142 O OE2   . GLU A 1 284 ? 79.576  86.772  99.184  1.00 97.15  ? 284 GLU A OE2   1 
ATOM   2143 N N     . LEU A 1 285 ? 84.327  88.923  98.800  1.00 70.66  ? 285 LEU A N     1 
ATOM   2144 C CA    . LEU A 1 285 ? 84.802  89.285  100.091 1.00 70.66  ? 285 LEU A CA    1 
ATOM   2145 C C     . LEU A 1 285 ? 84.566  90.750  100.345 1.00 70.66  ? 285 LEU A C     1 
ATOM   2146 O O     . LEU A 1 285 ? 84.129  91.122  101.438 1.00 70.66  ? 285 LEU A O     1 
ATOM   2147 C CB    . LEU A 1 285 ? 86.253  88.910  100.172 1.00 104.61 ? 285 LEU A CB    1 
ATOM   2148 C CG    . LEU A 1 285 ? 86.478  87.387  100.123 1.00 104.61 ? 285 LEU A CG    1 
ATOM   2149 C CD1   . LEU A 1 285 ? 87.937  87.093  99.831  1.00 104.61 ? 285 LEU A CD1   1 
ATOM   2150 C CD2   . LEU A 1 285 ? 86.056  86.724  101.449 1.00 104.61 ? 285 LEU A CD2   1 
ATOM   2151 N N     . SER A 1 286 ? 84.770  91.591  99.343  1.00 70.88  ? 286 SER A N     1 
ATOM   2152 C CA    . SER A 1 286 ? 84.528  93.004  99.559  1.00 70.88  ? 286 SER A CA    1 
ATOM   2153 C C     . SER A 1 286 ? 83.060  93.268  99.796  1.00 70.88  ? 286 SER A C     1 
ATOM   2154 O O     . SER A 1 286 ? 82.695  94.095  100.632 1.00 70.88  ? 286 SER A O     1 
ATOM   2155 C CB    . SER A 1 286 ? 85.016  93.816  98.376  1.00 95.47  ? 286 SER A CB    1 
ATOM   2156 O OG    . SER A 1 286 ? 86.424  93.775  98.272  1.00 95.47  ? 286 SER A OG    1 
ATOM   2157 N N     . ALA A 1 287 ? 82.199  92.543  99.086  1.00 70.79  ? 287 ALA A N     1 
ATOM   2158 C CA    . ALA A 1 287 ? 80.763  92.723  99.265  1.00 70.79  ? 287 ALA A CA    1 
ATOM   2159 C C     . ALA A 1 287 ? 80.355  92.467  100.691 1.00 70.79  ? 287 ALA A C     1 
ATOM   2160 O O     . ALA A 1 287 ? 79.456  93.119  101.215 1.00 70.79  ? 287 ALA A O     1 
ATOM   2161 C CB    . ALA A 1 287 ? 79.999  91.782  98.345  1.00 96.53  ? 287 ALA A CB    1 
ATOM   2162 N N     . GLN A 1 288 ? 80.981  91.502  101.314 1.00 70.58  ? 288 GLN A N     1 
ATOM   2163 C CA    . GLN A 1 288 ? 80.664  91.289  102.701 1.00 70.58  ? 288 GLN A CA    1 
ATOM   2164 C C     . GLN A 1 288 ? 81.298  92.356  103.568 1.00 70.58  ? 288 GLN A C     1 
ATOM   2165 O O     . GLN A 1 288 ? 80.635  92.941  104.424 1.00 70.58  ? 288 GLN A O     1 
ATOM   2166 C CB    . GLN A 1 288 ? 81.134  89.914  103.131 1.00 98.62  ? 288 GLN A CB    1 
ATOM   2167 C CG    . GLN A 1 288 ? 80.406  88.798  102.452 1.00 98.62  ? 288 GLN A CG    1 
ATOM   2168 C CD    . GLN A 1 288 ? 80.904  87.442  102.887 1.00 98.62  ? 288 GLN A CD    1 
ATOM   2169 O OE1   . GLN A 1 288 ? 81.383  87.272  104.018 1.00 98.62  ? 288 GLN A OE1   1 
ATOM   2170 N NE2   . GLN A 1 288 ? 80.800  86.463  101.989 1.00 98.62  ? 288 GLN A NE2   1 
ATOM   2171 N N     . VAL A 1 289 ? 82.541  92.698  103.310 1.00 68.85  ? 289 VAL A N     1 
ATOM   2172 C CA    . VAL A 1 289 ? 83.249  93.570  104.233 1.00 68.85  ? 289 VAL A CA    1 
ATOM   2173 C C     . VAL A 1 289 ? 82.613  94.941  104.327 1.00 68.85  ? 289 VAL A C     1 
ATOM   2174 O O     . VAL A 1 289 ? 82.514  95.510  105.418 1.00 68.85  ? 289 VAL A O     1 
ATOM   2175 C CB    . VAL A 1 289 ? 84.721  93.654  103.844 1.00 100.14 ? 289 VAL A CB    1 
ATOM   2176 C CG1   . VAL A 1 289 ? 85.408  94.745  104.586 1.00 100.14 ? 289 VAL A CG1   1 
ATOM   2177 C CG2   . VAL A 1 289 ? 85.359  92.371  104.211 1.00 100.14 ? 289 VAL A CG2   1 
ATOM   2178 N N     . PHE A 1 290 ? 82.166  95.488  103.215 1.00 73.13  ? 290 PHE A N     1 
ATOM   2179 C CA    . PHE A 1 290 ? 81.572  96.809  103.217 1.00 73.13  ? 290 PHE A CA    1 
ATOM   2180 C C     . PHE A 1 290 ? 80.070  96.770  103.322 1.00 73.13  ? 290 PHE A C     1 
ATOM   2181 O O     . PHE A 1 290 ? 79.414  97.778  103.073 1.00 73.13  ? 290 PHE A O     1 
ATOM   2182 C CB    . PHE A 1 290 ? 81.957  97.541  101.971 1.00 102.04 ? 290 PHE A CB    1 
ATOM   2183 C CG    . PHE A 1 290 ? 83.350  97.981  101.964 1.00 102.04 ? 290 PHE A CG    1 
ATOM   2184 C CD1   . PHE A 1 290 ? 83.674  99.205  102.453 1.00 102.04 ? 290 PHE A CD1   1 
ATOM   2185 C CD2   . PHE A 1 290 ? 84.343  97.183  101.450 1.00 102.04 ? 290 PHE A CD2   1 
ATOM   2186 C CE1   . PHE A 1 290 ? 84.953  99.647  102.436 1.00 102.04 ? 290 PHE A CE1   1 
ATOM   2187 C CE2   . PHE A 1 290 ? 85.641  97.619  101.433 1.00 102.04 ? 290 PHE A CE2   1 
ATOM   2188 C CZ    . PHE A 1 290 ? 85.944  98.858  101.926 1.00 102.04 ? 290 PHE A CZ    1 
ATOM   2189 N N     . GLY A 1 291 ? 79.512  95.647  103.638 1.00 72.04  ? 291 GLY A N     1 
ATOM   2190 C CA    . GLY A 1 291 ? 78.100  95.598  103.869 1.00 72.04  ? 291 GLY A CA    1 
ATOM   2191 C C     . GLY A 1 291 ? 77.799  95.998  105.294 1.00 72.04  ? 291 GLY A C     1 
ATOM   2192 O O     . GLY A 1 291 ? 78.613  95.867  106.187 1.00 72.04  ? 291 GLY A O     1 
ATOM   2193 N N     . ASP A 1 292 ? 76.588  96.454  105.522 1.00 72.23  ? 292 ASP A N     1 
ATOM   2194 C CA    . ASP A 1 292 ? 76.181  96.857  106.847 1.00 72.23  ? 292 ASP A CA    1 
ATOM   2195 C C     . ASP A 1 292 ? 76.067  95.658  107.733 1.00 72.23  ? 292 ASP A C     1 
ATOM   2196 O O     . ASP A 1 292 ? 76.341  95.718  108.932 1.00 72.23  ? 292 ASP A O     1 
ATOM   2197 C CB    . ASP A 1 292 ? 74.837  97.521  106.726 1.00 92.87  ? 292 ASP A CB    1 
ATOM   2198 C CG    . ASP A 1 292 ? 73.881  96.631  105.983 1.00 92.87  ? 292 ASP A CG    1 
ATOM   2199 O OD1   . ASP A 1 292 ? 74.378  95.833  105.170 1.00 92.87  ? 292 ASP A OD1   1 
ATOM   2200 O OD2   . ASP A 1 292 ? 72.675  96.686  106.207 1.00 92.87  ? 292 ASP A OD2   1 
ATOM   2201 N N     . GLU A 1 293 ? 75.738  94.552  107.114 1.00 72.58  ? 293 GLU A N     1 
ATOM   2202 C CA    . GLU A 1 293 ? 75.519  93.313  107.797 1.00 72.58  ? 293 GLU A CA    1 
ATOM   2203 C C     . GLU A 1 293 ? 76.739  92.800  108.524 1.00 72.58  ? 293 GLU A C     1 
ATOM   2204 O O     . GLU A 1 293 ? 76.599  91.923  109.378 1.00 72.58  ? 293 GLU A O     1 
ATOM   2205 C CB    . GLU A 1 293 ? 75.041  92.272  106.791 1.00 97.50  ? 293 GLU A CB    1 
ATOM   2206 C CG    . GLU A 1 293 ? 73.594  92.515  106.331 1.00 97.50  ? 293 GLU A CG    1 
ATOM   2207 C CD    . GLU A 1 293 ? 73.059  91.507  105.321 1.00 97.50  ? 293 GLU A CD    1 
ATOM   2208 O OE1   . GLU A 1 293 ? 73.840  90.809  104.675 1.00 97.50  ? 293 GLU A OE1   1 
ATOM   2209 O OE2   . GLU A 1 293 ? 71.843  91.410  105.198 1.00 97.50  ? 293 GLU A OE2   1 
ATOM   2210 N N     . TYR A 1 294 ? 77.927  93.278  108.211 1.00 70.08  ? 294 TYR A N     1 
ATOM   2211 C CA    . TYR A 1 294 ? 79.100  92.754  108.882 1.00 70.08  ? 294 TYR A CA    1 
ATOM   2212 C C     . TYR A 1 294 ? 79.823  93.762  109.746 1.00 70.08  ? 294 TYR A C     1 
ATOM   2213 O O     . TYR A 1 294 ? 80.942  93.497  110.173 1.00 70.08  ? 294 TYR A O     1 
ATOM   2214 C CB    . TYR A 1 294 ? 80.046  92.180  107.857 1.00 97.03  ? 294 TYR A CB    1 
ATOM   2215 C CG    . TYR A 1 294 ? 79.503  90.973  107.180 1.00 97.03  ? 294 TYR A CG    1 
ATOM   2216 C CD1   . TYR A 1 294 ? 78.724  91.080  106.051 1.00 97.03  ? 294 TYR A CD1   1 
ATOM   2217 C CD2   . TYR A 1 294 ? 79.799  89.727  107.654 1.00 97.03  ? 294 TYR A CD2   1 
ATOM   2218 C CE1   . TYR A 1 294 ? 78.251  89.964  105.428 1.00 97.03  ? 294 TYR A CE1   1 
ATOM   2219 C CE2   . TYR A 1 294 ? 79.335  88.610  107.032 1.00 97.03  ? 294 TYR A CE2   1 
ATOM   2220 C CZ    . TYR A 1 294 ? 78.562  88.728  105.930 1.00 97.03  ? 294 TYR A CZ    1 
ATOM   2221 O OH    . TYR A 1 294 ? 78.104  87.605  105.296 1.00 97.03  ? 294 TYR A OH    1 
ATOM   2222 N N     . ILE A 1 295 ? 79.236  94.884  110.043 1.00 68.05  ? 295 ILE A N     1 
ATOM   2223 C CA    . ILE A 1 295 ? 79.976  95.928  110.738 1.00 68.05  ? 295 ILE A CA    1 
ATOM   2224 C C     . ILE A 1 295 ? 79.838  95.793  112.252 1.00 68.05  ? 295 ILE A C     1 
ATOM   2225 O O     . ILE A 1 295 ? 78.723  95.762  112.779 1.00 68.05  ? 295 ILE A O     1 
ATOM   2226 C CB    . ILE A 1 295 ? 79.493  97.303  110.271 1.00 100.75 ? 295 ILE A CB    1 
ATOM   2227 C CG1   . ILE A 1 295 ? 79.498  97.357  108.741 1.00 100.75 ? 295 ILE A CG1   1 
ATOM   2228 C CG2   . ILE A 1 295 ? 80.342  98.447  110.868 1.00 100.75 ? 295 ILE A CG2   1 
ATOM   2229 C CD1   . ILE A 1 295 ? 80.831  97.143  108.053 1.00 100.75 ? 295 ILE A CD1   1 
ATOM   2230 N N     . CYS A 1 296 ? 80.968  95.836  112.968 1.00 67.18  ? 296 CYS A N     1 
ATOM   2231 C CA    . CYS A 1 296 ? 81.007  95.696  114.434 1.00 67.18  ? 296 CYS A CA    1 
ATOM   2232 C C     . CYS A 1 296 ? 80.348  96.842  115.214 1.00 67.18  ? 296 CYS A C     1 
ATOM   2233 O O     . CYS A 1 296 ? 80.224  96.759  116.442 1.00 67.18  ? 296 CYS A O     1 
ATOM   2234 C CB    . CYS A 1 296 ? 82.447  95.594  114.908 1.00 90.49  ? 296 CYS A CB    1 
ATOM   2235 S SG    . CYS A 1 296 ? 83.357  97.141  114.730 1.00 90.49  ? 296 CYS A SG    1 
ATOM   2236 N N     . ALA A 1 297 ? 79.998  97.929  114.550 1.00 68.94  ? 297 ALA A N     1 
ATOM   2237 C CA    . ALA A 1 297 ? 79.370  99.081  115.176 1.00 68.94  ? 297 ALA A CA    1 
ATOM   2238 C C     . ALA A 1 297 ? 77.838  99.110  115.072 1.00 68.94  ? 297 ALA A C     1 
ATOM   2239 O O     . ALA A 1 297 ? 77.211  99.944  115.733 1.00 68.94  ? 297 ALA A O     1 
ATOM   2240 C CB    . ALA A 1 297 ? 79.939  100.357 114.555 1.00 94.01  ? 297 ALA A CB    1 
ATOM   2241 N N     . ALA A 1 298 ? 77.212  98.255  114.257 1.00 65.33  ? 298 ALA A N     1 
ATOM   2242 C CA    . ALA A 1 298 ? 75.752  98.312  114.034 1.00 65.33  ? 298 ALA A CA    1 
ATOM   2243 C C     . ALA A 1 298 ? 75.314  99.700  113.627 1.00 65.33  ? 298 ALA A C     1 
ATOM   2244 O O     . ALA A 1 298 ? 74.309  100.215 114.105 1.00 65.33  ? 298 ALA A O     1 
ATOM   2245 C CB    . ALA A 1 298 ? 74.954  97.889  115.259 1.00 89.09  ? 298 ALA A CB    1 
ATOM   2246 N N     . CYS A 1 299 ? 76.062  100.300 112.729 1.00 67.61  ? 299 CYS A N     1 
ATOM   2247 C CA    . CYS A 1 299 ? 75.816  101.663 112.342 1.00 67.61  ? 299 CYS A CA    1 
ATOM   2248 C C     . CYS A 1 299 ? 75.364  101.872 110.909 1.00 67.61  ? 299 CYS A C     1 
ATOM   2249 O O     . CYS A 1 299 ? 74.953  102.987 110.582 1.00 67.61  ? 299 CYS A O     1 
ATOM   2250 C CB    . CYS A 1 299 ? 77.083  102.446 112.550 1.00 91.07  ? 299 CYS A CB    1 
ATOM   2251 S SG    . CYS A 1 299 ? 78.271  101.795 111.487 1.00 91.07  ? 299 CYS A SG    1 
ATOM   2252 N N     . LYS A 1 300 ? 75.422  100.877 110.066 1.00 66.70  ? 300 LYS A N     1 
ATOM   2253 C CA    . LYS A 1 300 ? 75.045  101.012 108.668 1.00 66.70  ? 300 LYS A CA    1 
ATOM   2254 C C     . LYS A 1 300 ? 75.856  102.057 107.905 1.00 66.70  ? 300 LYS A C     1 
ATOM   2255 O O     . LYS A 1 300 ? 75.259  102.965 107.321 1.00 66.70  ? 300 LYS A O     1 
ATOM   2256 C CB    . LYS A 1 300 ? 73.567  101.363 108.570 1.00 100.05 ? 300 LYS A CB    1 
ATOM   2257 C CG    . LYS A 1 300 ? 72.671  100.398 109.282 1.00 100.05 ? 300 LYS A CG    1 
ATOM   2258 C CD    . LYS A 1 300 ? 71.262  100.857 109.229 1.00 100.05 ? 300 LYS A CD    1 
ATOM   2259 C CE    . LYS A 1 300 ? 70.388  99.950  110.048 1.00 100.05 ? 300 LYS A CE    1 
ATOM   2260 N NZ    . LYS A 1 300 ? 68.968  100.407 110.056 1.00 100.05 ? 300 LYS A NZ    1 
ATOM   2261 N N     . PRO A 1 301 ? 77.182  101.878 107.778 1.00 68.64  ? 301 PRO A N     1 
ATOM   2262 C CA    . PRO A 1 301 ? 78.089  102.857 107.164 1.00 68.64  ? 301 PRO A CA    1 
ATOM   2263 C C     . PRO A 1 301 ? 77.823  103.075 105.733 1.00 68.64  ? 301 PRO A C     1 
ATOM   2264 O O     . PRO A 1 301 ? 78.304  104.040 105.144 1.00 68.64  ? 301 PRO A O     1 
ATOM   2265 C CB    . PRO A 1 301 ? 79.447  102.216 107.350 1.00 453.21 ? 301 PRO A CB    1 
ATOM   2266 C CG    . PRO A 1 301 ? 79.148  100.814 107.361 1.00 453.21 ? 301 PRO A CG    1 
ATOM   2267 C CD    . PRO A 1 301 ? 77.837  100.630 108.024 1.00 453.21 ? 301 PRO A CD    1 
ATOM   2268 N N     . THR A 1 302 ? 76.998  102.241 105.182 1.00 66.47  ? 302 THR A N     1 
ATOM   2269 C CA    . THR A 1 302 ? 76.592  102.295 103.818 1.00 66.47  ? 302 THR A CA    1 
ATOM   2270 C C     . THR A 1 302 ? 75.758  103.497 103.523 1.00 66.47  ? 302 THR A C     1 
ATOM   2271 O O     . THR A 1 302 ? 75.527  103.801 102.358 1.00 66.47  ? 302 THR A O     1 
ATOM   2272 C CB    . THR A 1 302 ? 75.793  101.057 103.539 1.00 93.06  ? 302 THR A CB    1 
ATOM   2273 O OG1   . THR A 1 302 ? 74.635  101.092 104.365 1.00 93.06  ? 302 THR A OG1   1 
ATOM   2274 C CG2   . THR A 1 302 ? 76.617  99.809  103.899 1.00 93.06  ? 302 THR A CG2   1 
ATOM   2275 N N     . THR A 1 303 ? 75.287  104.177 104.533 1.00 69.37  ? 303 THR A N     1 
ATOM   2276 C CA    . THR A 1 303 ? 74.545  105.399 104.356 1.00 69.37  ? 303 THR A CA    1 
ATOM   2277 C C     . THR A 1 303 ? 75.361  106.622 104.713 1.00 69.37  ? 303 THR A C     1 
ATOM   2278 O O     . THR A 1 303 ? 74.844  107.736 104.631 1.00 69.37  ? 303 THR A O     1 
ATOM   2279 C CB    . THR A 1 303 ? 73.310  105.388 105.225 1.00 97.12  ? 303 THR A CB    1 
ATOM   2280 O OG1   . THR A 1 303 ? 73.699  105.418 106.601 1.00 97.12  ? 303 THR A OG1   1 
ATOM   2281 C CG2   . THR A 1 303 ? 72.545  104.122 104.983 1.00 97.12  ? 303 THR A CG2   1 
ATOM   2282 N N     . GLY A 1 304 ? 76.609  106.443 105.145 1.00 69.77  ? 304 GLY A N     1 
ATOM   2283 C CA    . GLY A 1 304 ? 77.442  107.517 105.660 1.00 69.77  ? 304 GLY A CA    1 
ATOM   2284 C C     . GLY A 1 304 ? 78.498  107.966 104.693 1.00 69.77  ? 304 GLY A C     1 
ATOM   2285 O O     . GLY A 1 304 ? 78.377  107.784 103.480 1.00 69.77  ? 304 GLY A O     1 
ATOM   2286 N N     . ARG A 1 305 ? 79.550  108.563 105.235 1.00 71.31  ? 305 ARG A N     1 
ATOM   2287 C CA    . ARG A 1 305 ? 80.664  109.064 104.443 1.00 71.31  ? 305 ARG A CA    1 
ATOM   2288 C C     . ARG A 1 305 ? 81.984  108.710 105.116 1.00 71.31  ? 305 ARG A C     1 
ATOM   2289 O O     . ARG A 1 305 ? 82.103  108.807 106.334 1.00 71.31  ? 305 ARG A O     1 
ATOM   2290 C CB    . ARG A 1 305 ? 80.580  110.569 104.279 1.00 104.78 ? 305 ARG A CB    1 
ATOM   2291 C CG    . ARG A 1 305 ? 79.330  111.072 103.618 1.00 104.78 ? 305 ARG A CG    1 
ATOM   2292 C CD    . ARG A 1 305 ? 79.280  110.731 102.173 1.00 104.78 ? 305 ARG A CD    1 
ATOM   2293 N NE    . ARG A 1 305 ? 78.094  111.298 101.546 1.00 104.78 ? 305 ARG A NE    1 
ATOM   2294 C CZ    . ARG A 1 305 ? 76.890  110.729 101.517 1.00 104.78 ? 305 ARG A CZ    1 
ATOM   2295 N NH1   . ARG A 1 305 ? 76.660  109.551 102.072 1.00 104.78 ? 305 ARG A NH1   1 
ATOM   2296 N NH2   . ARG A 1 305 ? 75.889  111.363 100.916 1.00 104.78 ? 305 ARG A NH2   1 
ATOM   2297 N N     . TYR A 1 306 ? 82.985  108.297 104.343 1.00 68.61  ? 306 TYR A N     1 
ATOM   2298 C CA    . TYR A 1 306 ? 84.235  107.863 104.954 1.00 68.61  ? 306 TYR A CA    1 
ATOM   2299 C C     . TYR A 1 306 ? 85.221  108.990 105.073 1.00 68.61  ? 306 TYR A C     1 
ATOM   2300 O O     . TYR A 1 306 ? 85.648  109.568 104.087 1.00 68.61  ? 306 TYR A O     1 
ATOM   2301 C CB    . TYR A 1 306 ? 84.898  106.722 104.203 1.00 95.00  ? 306 TYR A CB    1 
ATOM   2302 C CG    . TYR A 1 306 ? 84.320  105.335 104.458 1.00 95.00  ? 306 TYR A CG    1 
ATOM   2303 C CD1   . TYR A 1 306 ? 84.790  104.549 105.495 1.00 95.00  ? 306 TYR A CD1   1 
ATOM   2304 C CD2   . TYR A 1 306 ? 83.328  104.813 103.647 1.00 95.00  ? 306 TYR A CD2   1 
ATOM   2305 C CE1   . TYR A 1 306 ? 84.278  103.298 105.712 1.00 95.00  ? 306 TYR A CE1   1 
ATOM   2306 C CE2   . TYR A 1 306 ? 82.820  103.561 103.871 1.00 95.00  ? 306 TYR A CE2   1 
ATOM   2307 C CZ    . TYR A 1 306 ? 83.292  102.817 104.895 1.00 95.00  ? 306 TYR A CZ    1 
ATOM   2308 O OH    . TYR A 1 306 ? 82.784  101.574 105.117 1.00 95.00  ? 306 TYR A OH    1 
ATOM   2309 N N     . LEU A 1 307 ? 85.625  109.226 106.280 1.00 67.39  ? 307 LEU A N     1 
ATOM   2310 C CA    . LEU A 1 307 ? 86.596  110.242 106.580 1.00 67.39  ? 307 LEU A CA    1 
ATOM   2311 C C     . LEU A 1 307 ? 87.969  109.734 106.194 1.00 67.39  ? 307 LEU A C     1 
ATOM   2312 O O     . LEU A 1 307 ? 88.808  110.495 105.703 1.00 67.39  ? 307 LEU A O     1 
ATOM   2313 C CB    . LEU A 1 307 ? 86.455  110.595 108.061 1.00 99.77  ? 307 LEU A CB    1 
ATOM   2314 C CG    . LEU A 1 307 ? 87.267  111.723 108.657 1.00 99.77  ? 307 LEU A CG    1 
ATOM   2315 C CD1   . LEU A 1 307 ? 87.036  113.017 107.900 1.00 99.77  ? 307 LEU A CD1   1 
ATOM   2316 C CD2   . LEU A 1 307 ? 86.901  111.903 110.154 1.00 99.77  ? 307 LEU A CD2   1 
ATOM   2317 N N     . ALA A 1 308 ? 88.207  108.438 106.392 1.00 59.91  ? 308 ALA A N     1 
ATOM   2318 C CA    . ALA A 1 308 ? 89.444  107.759 106.000 1.00 59.91  ? 308 ALA A CA    1 
ATOM   2319 C C     . ALA A 1 308 ? 89.186  106.267 105.979 1.00 59.91  ? 308 ALA A C     1 
ATOM   2320 O O     . ALA A 1 308 ? 88.344  105.779 106.731 1.00 59.91  ? 308 ALA A O     1 
ATOM   2321 C CB    . ALA A 1 308 ? 90.578  108.066 106.957 1.00 81.70  ? 308 ALA A CB    1 
ATOM   2322 N N     . ALA A 1 309 ? 89.903  105.523 105.155 1.00 57.54  ? 309 ALA A N     1 
ATOM   2323 C CA    . ALA A 1 309 ? 89.695  104.077 105.220 1.00 57.54  ? 309 ALA A CA    1 
ATOM   2324 C C     . ALA A 1 309 ? 90.849  103.287 104.627 1.00 57.54  ? 309 ALA A C     1 
ATOM   2325 O O     . ALA A 1 309 ? 91.620  103.801 103.817 1.00 57.54  ? 309 ALA A O     1 
ATOM   2326 C CB    . ALA A 1 309 ? 88.411  103.680 104.508 1.00 78.46  ? 309 ALA A CB    1 
ATOM   2327 N N     . SER A 1 310 ? 90.946  102.016 105.019 1.00 62.52  ? 310 SER A N     1 
ATOM   2328 C CA    . SER A 1 310 ? 91.946  101.146 104.417 1.00 62.52  ? 310 SER A CA    1 
ATOM   2329 C C     . SER A 1 310 ? 91.531  99.681  104.401 1.00 62.52  ? 310 SER A C     1 
ATOM   2330 O O     . SER A 1 310 ? 90.796  99.213  105.271 1.00 62.52  ? 310 SER A O     1 
ATOM   2331 C CB    . SER A 1 310 ? 93.266  101.301 105.137 1.00 84.21  ? 310 SER A CB    1 
ATOM   2332 O OG    . SER A 1 310 ? 93.188  100.888 106.469 1.00 84.21  ? 310 SER A OG    1 
ATOM   2333 N N     . VAL A 1 311 ? 92.026  98.949  103.418 1.00 63.19  ? 311 VAL A N     1 
ATOM   2334 C CA    . VAL A 1 311 ? 91.691  97.541  103.279 1.00 63.19  ? 311 VAL A CA    1 
ATOM   2335 C C     . VAL A 1 311 ? 92.918  96.671  103.110 1.00 63.19  ? 311 VAL A C     1 
ATOM   2336 O O     . VAL A 1 311 ? 93.712  96.881  102.189 1.00 63.19  ? 311 VAL A O     1 
ATOM   2337 C CB    . VAL A 1 311 ? 90.748  97.290  102.100 1.00 91.91  ? 311 VAL A CB    1 
ATOM   2338 C CG1   . VAL A 1 311 ? 90.475  95.775  101.957 1.00 91.91  ? 311 VAL A CG1   1 
ATOM   2339 C CG2   . VAL A 1 311 ? 89.474  98.003  102.313 1.00 91.91  ? 311 VAL A CG2   1 
ATOM   2340 N N     . LEU A 1 312 ? 93.008  95.619  103.914 1.00 65.12  ? 312 LEU A N     1 
ATOM   2341 C CA    . LEU A 1 312 ? 94.068  94.635  103.784 1.00 65.12  ? 312 LEU A CA    1 
ATOM   2342 C C     . LEU A 1 312 ? 93.559  93.310  103.278 1.00 65.12  ? 312 LEU A C     1 
ATOM   2343 O O     . LEU A 1 312 ? 92.581  92.771  103.793 1.00 65.12  ? 312 LEU A O     1 
ATOM   2344 C CB    . LEU A 1 312 ? 94.776  94.409  105.103 1.00 96.41  ? 312 LEU A CB    1 
ATOM   2345 C CG    . LEU A 1 312 ? 95.741  93.222  105.202 1.00 96.41  ? 312 LEU A CG    1 
ATOM   2346 C CD1   . LEU A 1 312 ? 96.924  93.359  104.294 1.00 96.41  ? 312 LEU A CD1   1 
ATOM   2347 C CD2   . LEU A 1 312 ? 96.235  93.092  106.614 1.00 96.41  ? 312 LEU A CD2   1 
ATOM   2348 N N     . PHE A 1 313 ? 94.228  92.768  102.298 1.00 67.01  ? 313 PHE A N     1 
ATOM   2349 C CA    . PHE A 1 313 ? 93.963  91.414  101.866 1.00 67.01  ? 313 PHE A CA    1 
ATOM   2350 C C     . PHE A 1 313 ? 95.100  90.504  102.328 1.00 67.01  ? 313 PHE A C     1 
ATOM   2351 O O     . PHE A 1 313 ? 96.257  90.701  101.933 1.00 67.01  ? 313 PHE A O     1 
ATOM   2352 C CB    . PHE A 1 313 ? 93.856  91.291  100.365 1.00 93.50  ? 313 PHE A CB    1 
ATOM   2353 C CG    . PHE A 1 313 ? 92.617  91.775  99.780  1.00 93.50  ? 313 PHE A CG    1 
ATOM   2354 C CD1   . PHE A 1 313 ? 92.448  93.069  99.545  1.00 93.50  ? 313 PHE A CD1   1 
ATOM   2355 C CD2   . PHE A 1 313 ? 91.681  90.901  99.331  1.00 93.50  ? 313 PHE A CD2   1 
ATOM   2356 C CE1   . PHE A 1 313 ? 91.329  93.494  98.934  1.00 93.50  ? 313 PHE A CE1   1 
ATOM   2357 C CE2   . PHE A 1 313 ? 90.581  91.311  98.741  1.00 93.50  ? 313 PHE A CE2   1 
ATOM   2358 C CZ    . PHE A 1 313 ? 90.391  92.607  98.536  1.00 93.50  ? 313 PHE A CZ    1 
ATOM   2359 N N     . ARG A 1 314 ? 94.764  89.486  103.127 1.00 69.11  ? 314 ARG A N     1 
ATOM   2360 C CA    . ARG A 1 314 ? 95.734  88.520  103.642 1.00 69.11  ? 314 ARG A CA    1 
ATOM   2361 C C     . ARG A 1 314 ? 95.683  87.233  102.837 1.00 69.11  ? 314 ARG A C     1 
ATOM   2362 O O     . ARG A 1 314 ? 94.713  86.484  102.946 1.00 69.11  ? 314 ARG A O     1 
ATOM   2363 C CB    . ARG A 1 314 ? 95.455  88.155  105.092 1.00 101.55 ? 314 ARG A CB    1 
ATOM   2364 C CG    . ARG A 1 314 ? 95.774  89.154  106.126 1.00 101.55 ? 314 ARG A CG    1 
ATOM   2365 C CD    . ARG A 1 314 ? 95.649  88.517  107.456 1.00 101.55 ? 314 ARG A CD    1 
ATOM   2366 N NE    . ARG A 1 314 ? 96.628  87.461  107.554 1.00 101.55 ? 314 ARG A NE    1 
ATOM   2367 C CZ    . ARG A 1 314 ? 96.781  86.580  108.534 1.00 101.55 ? 314 ARG A CZ    1 
ATOM   2368 N NH1   . ARG A 1 314 ? 96.021  86.583  109.624 1.00 101.55 ? 314 ARG A NH1   1 
ATOM   2369 N NH2   . ARG A 1 314 ? 97.726  85.662  108.404 1.00 101.55 ? 314 ARG A NH2   1 
ATOM   2370 N N     . GLY A 1 315 ? 96.741  86.930  102.102 1.00 74.39  ? 315 GLY A N     1 
ATOM   2371 C CA    . GLY A 1 315 ? 96.779  85.768  101.242 1.00 74.39  ? 315 GLY A CA    1 
ATOM   2372 C C     . GLY A 1 315 ? 96.957  86.195  99.801  1.00 74.39  ? 315 GLY A C     1 
ATOM   2373 O O     . GLY A 1 315 ? 97.002  87.379  99.485  1.00 74.39  ? 315 GLY A O     1 
ATOM   2374 N N     . ALA A 1 316 ? 97.059  85.231  98.915  1.00 77.80  ? 316 ALA A N     1 
ATOM   2375 C CA    . ALA A 1 316 ? 97.358  85.578  97.538  1.00 77.80  ? 316 ALA A CA    1 
ATOM   2376 C C     . ALA A 1 316 ? 96.102  85.898  96.764  1.00 77.80  ? 316 ALA A C     1 
ATOM   2377 O O     . ALA A 1 316 ? 95.300  85.015  96.456  1.00 77.80  ? 316 ALA A O     1 
ATOM   2378 C CB    . ALA A 1 316 ? 98.122  84.457  96.858  1.00 106.09 ? 316 ALA A CB    1 
ATOM   2379 N N     . VAL A 1 317 ? 95.978  87.146  96.388  1.00 76.80  ? 317 VAL A N     1 
ATOM   2380 C CA    . VAL A 1 317 ? 94.848  87.630  95.615  1.00 76.80  ? 317 VAL A CA    1 
ATOM   2381 C C     . VAL A 1 317 ? 95.428  88.375  94.434  1.00 76.80  ? 317 VAL A C     1 
ATOM   2382 O O     . VAL A 1 317 ? 96.440  89.063  94.586  1.00 76.80  ? 317 VAL A O     1 
ATOM   2383 C CB    . VAL A 1 317 ? 93.950  88.558  96.467  1.00 111.71 ? 317 VAL A CB    1 
ATOM   2384 C CG1   . VAL A 1 317 ? 94.730  89.792  96.943  1.00 111.71 ? 317 VAL A CG1   1 
ATOM   2385 C CG2   . VAL A 1 317 ? 92.711  88.969  95.695  1.00 111.71 ? 317 VAL A CG2   1 
ATOM   2386 N N     . LYS A 1 318 ? 94.815  88.246  93.261  1.00 79.61  ? 318 LYS A N     1 
ATOM   2387 C CA    . LYS A 1 318 ? 95.341  88.951  92.099  1.00 79.61  ? 318 LYS A CA    1 
ATOM   2388 C C     . LYS A 1 318 ? 94.951  90.421  92.098  1.00 79.61  ? 318 LYS A C     1 
ATOM   2389 O O     . LYS A 1 318 ? 93.823  90.765  92.446  1.00 79.61  ? 318 LYS A O     1 
ATOM   2390 C CB    . LYS A 1 318 ? 94.863  88.289  90.812  1.00 119.41 ? 318 LYS A CB    1 
ATOM   2391 C CG    . LYS A 1 318 ? 95.379  86.847  90.599  1.00 119.41 ? 318 LYS A CG    1 
ATOM   2392 C CD    . LYS A 1 318 ? 96.922  86.773  90.425  1.00 119.41 ? 318 LYS A CD    1 
ATOM   2393 C CE    . LYS A 1 318 ? 97.409  87.433  89.121  1.00 119.41 ? 318 LYS A CE    1 
ATOM   2394 N NZ    . LYS A 1 318 ? 98.886  87.388  88.981  1.00 119.41 ? 318 LYS A NZ    1 
ATOM   2395 N N     . THR A 1 319 ? 95.885  91.283  91.661  1.00 81.56  ? 319 THR A N     1 
ATOM   2396 C CA    . THR A 1 319 ? 95.612  92.712  91.602  1.00 81.56  ? 319 THR A CA    1 
ATOM   2397 C C     . THR A 1 319 ? 94.433  92.982  90.713  1.00 81.56  ? 319 THR A C     1 
ATOM   2398 O O     . THR A 1 319 ? 93.609  93.861  90.997  1.00 81.56  ? 319 THR A O     1 
ATOM   2399 C CB    . THR A 1 319 ? 96.804  93.498  91.082  1.00 114.18 ? 319 THR A CB    1 
ATOM   2400 O OG1   . THR A 1 319 ? 97.904  93.316  91.970  1.00 114.18 ? 319 THR A OG1   1 
ATOM   2401 C CG2   . THR A 1 319 ? 96.484  94.973  91.015  1.00 114.18 ? 319 THR A CG2   1 
ATOM   2402 N N     . SER A 1 320 ? 94.340  92.229  89.642  1.00 80.86  ? 320 SER A N     1 
ATOM   2403 C CA    . SER A 1 320 ? 93.279  92.398  88.699  1.00 80.86  ? 320 SER A CA    1 
ATOM   2404 C C     . SER A 1 320 ? 91.908  92.116  89.283  1.00 80.86  ? 320 SER A C     1 
ATOM   2405 O O     . SER A 1 320 ? 90.923  92.670  88.793  1.00 80.86  ? 320 SER A O     1 
ATOM   2406 C CB    . SER A 1 320 ? 93.536  91.495  87.537  1.00 108.91 ? 320 SER A CB    1 
ATOM   2407 O OG    . SER A 1 320 ? 93.468  90.164  87.962  1.00 108.91 ? 320 SER A OG    1 
ATOM   2408 N N     . ASP A 1 321 ? 91.789  91.291  90.307  1.00 81.39  ? 321 ASP A N     1 
ATOM   2409 C CA    . ASP A 1 321 ? 90.459  91.113  90.874  1.00 81.39  ? 321 ASP A CA    1 
ATOM   2410 C C     . ASP A 1 321 ? 90.176  92.178  91.914  1.00 81.39  ? 321 ASP A C     1 
ATOM   2411 O O     . ASP A 1 321 ? 89.039  92.655  92.048  1.00 81.39  ? 321 ASP A O     1 
ATOM   2412 C CB    . ASP A 1 321 ? 90.316  89.732  91.516  1.00 104.64 ? 321 ASP A CB    1 
ATOM   2413 C CG    . ASP A 1 321 ? 90.489  88.598  90.533  1.00 104.64 ? 321 ASP A CG    1 
ATOM   2414 O OD1   . ASP A 1 321 ? 89.864  88.607  89.472  1.00 104.64 ? 321 ASP A OD1   1 
ATOM   2415 O OD2   . ASP A 1 321 ? 91.229  87.669  90.857  1.00 104.64 ? 321 ASP A OD2   1 
ATOM   2416 N N     . VAL A 1 322 ? 91.216  92.579  92.630  1.00 79.63  ? 322 VAL A N     1 
ATOM   2417 C CA    . VAL A 1 322 ? 91.034  93.577  93.654  1.00 79.63  ? 322 VAL A CA    1 
ATOM   2418 C C     . VAL A 1 322 ? 90.548  94.838  93.025  1.00 79.63  ? 322 VAL A C     1 
ATOM   2419 O O     . VAL A 1 322 ? 89.610  95.457  93.512  1.00 79.63  ? 322 VAL A O     1 
ATOM   2420 C CB    . VAL A 1 322 ? 92.328  93.825  94.439  1.00 115.82 ? 322 VAL A CB    1 
ATOM   2421 C CG1   . VAL A 1 322 ? 92.137  95.009  95.397  1.00 115.82 ? 322 VAL A CG1   1 
ATOM   2422 C CG2   . VAL A 1 322 ? 92.698  92.605  95.215  1.00 115.82 ? 322 VAL A CG2   1 
ATOM   2423 N N     . ASN A 1 323 ? 91.147  95.229  91.928  1.00 83.97  ? 323 ASN A N     1 
ATOM   2424 C CA    . ASN A 1 323 ? 90.752  96.493  91.364  1.00 83.97  ? 323 ASN A CA    1 
ATOM   2425 C C     . ASN A 1 323 ? 89.291  96.534  90.986  1.00 83.97  ? 323 ASN A C     1 
ATOM   2426 O O     . ASN A 1 323 ? 88.664  97.592  91.114  1.00 83.97  ? 323 ASN A O     1 
ATOM   2427 C CB    . ASN A 1 323 ? 91.589  96.822  90.179  1.00 113.77 ? 323 ASN A CB    1 
ATOM   2428 C CG    . ASN A 1 323 ? 92.928  97.270  90.579  1.00 113.77 ? 323 ASN A CG    1 
ATOM   2429 O OD1   . ASN A 1 323 ? 93.161  97.642  91.731  1.00 113.77 ? 323 ASN A OD1   1 
ATOM   2430 N ND2   . ASN A 1 323 ? 93.845  97.253  89.639  1.00 113.77 ? 323 ASN A ND2   1 
ATOM   2431 N N     . GLU A 1 324 ? 88.710  95.431  90.531  1.00 84.49  ? 324 GLU A N     1 
ATOM   2432 C CA    . GLU A 1 324 ? 87.300  95.546  90.180  1.00 84.49  ? 324 GLU A CA    1 
ATOM   2433 C C     . GLU A 1 324 ? 86.450  95.559  91.430  1.00 84.49  ? 324 GLU A C     1 
ATOM   2434 O O     . GLU A 1 324 ? 85.438  96.279  91.508  1.00 84.49  ? 324 GLU A O     1 
ATOM   2435 C CB    . GLU A 1 324 ? 86.866  94.434  89.222  1.00 113.49 ? 324 GLU A CB    1 
ATOM   2436 C CG    . GLU A 1 324 ? 87.471  94.580  87.809  1.00 113.49 ? 324 GLU A CG    1 
ATOM   2437 C CD    . GLU A 1 324 ? 86.933  93.595  86.767  1.00 113.49 ? 324 GLU A CD    1 
ATOM   2438 O OE1   . GLU A 1 324 ? 86.166  92.684  87.106  1.00 113.49 ? 324 GLU A OE1   1 
ATOM   2439 O OE2   . GLU A 1 324 ? 87.284  93.751  85.594  1.00 113.49 ? 324 GLU A OE2   1 
ATOM   2440 N N     . ALA A 1 325 ? 86.877  94.813  92.436  1.00 83.39  ? 325 ALA A N     1 
ATOM   2441 C CA    . ALA A 1 325 ? 86.124  94.821  93.680  1.00 83.39  ? 325 ALA A CA    1 
ATOM   2442 C C     . ALA A 1 325 ? 86.103  96.221  94.282  1.00 83.39  ? 325 ALA A C     1 
ATOM   2443 O O     . ALA A 1 325 ? 85.066  96.708  94.762  1.00 83.39  ? 325 ALA A O     1 
ATOM   2444 C CB    . ALA A 1 325 ? 86.738  93.813  94.651  1.00 113.71 ? 325 ALA A CB    1 
ATOM   2445 N N     . MET A 1 326 ? 87.234  96.900  94.215  1.00 81.28  ? 326 MET A N     1 
ATOM   2446 C CA    . MET A 1 326 ? 87.341  98.228  94.782  1.00 81.28  ? 326 MET A CA    1 
ATOM   2447 C C     . MET A 1 326 ? 86.561  99.223  93.978  1.00 81.28  ? 326 MET A C     1 
ATOM   2448 O O     . MET A 1 326 ? 85.971  100.144 94.539  1.00 81.28  ? 326 MET A O     1 
ATOM   2449 C CB    . MET A 1 326 ? 88.788  98.644  94.848  1.00 116.77 ? 326 MET A CB    1 
ATOM   2450 C CG    . MET A 1 326 ? 89.550  97.848  95.819  1.00 116.77 ? 326 MET A CG    1 
ATOM   2451 S SD    . MET A 1 326 ? 89.006  98.187  97.467  1.00 116.77 ? 326 MET A SD    1 
ATOM   2452 C CE    . MET A 1 326 ? 89.829  96.890  98.352  1.00 116.77 ? 326 MET A CE    1 
ATOM   2453 N N     . ALA A 1 327 ? 86.546  99.072  92.670  1.00 79.62  ? 327 ALA A N     1 
ATOM   2454 C CA    . ALA A 1 327 ? 85.781  100.016 91.895  1.00 79.62  ? 327 ALA A CA    1 
ATOM   2455 C C     . ALA A 1 327 ? 84.352  99.971  92.342  1.00 79.62  ? 327 ALA A C     1 
ATOM   2456 O O     . ALA A 1 327 ? 83.720  101.015 92.527  1.00 79.62  ? 327 ALA A O     1 
ATOM   2457 C CB    . ALA A 1 327 ? 85.877  99.697  90.417  1.00 108.57 ? 327 ALA A CB    1 
ATOM   2458 N N     . THR A 1 328 ? 83.850  98.768  92.596  1.00 79.39  ? 328 THR A N     1 
ATOM   2459 C CA    . THR A 1 328 ? 82.470  98.663  93.038  1.00 79.39  ? 328 THR A CA    1 
ATOM   2460 C C     . THR A 1 328 ? 82.275  99.387  94.359  1.00 79.39  ? 328 THR A C     1 
ATOM   2461 O O     . THR A 1 328 ? 81.283  100.097 94.545  1.00 79.39  ? 328 THR A O     1 
ATOM   2462 C CB    . THR A 1 328 ? 82.053  97.204  93.179  1.00 111.15 ? 328 THR A CB    1 
ATOM   2463 O OG1   . THR A 1 328 ? 82.156  96.551  91.910  1.00 111.15 ? 328 THR A OG1   1 
ATOM   2464 C CG2   . THR A 1 328 ? 80.611  97.119  93.671  1.00 111.15 ? 328 THR A CG2   1 
ATOM   2465 N N     . VAL A 1 329 ? 83.227  99.240  95.283  1.00 79.93  ? 329 VAL A N     1 
ATOM   2466 C CA    . VAL A 1 329 ? 83.095  99.907  96.581  1.00 79.93  ? 329 VAL A CA    1 
ATOM   2467 C C     . VAL A 1 329 ? 83.102  101.427 96.456  1.00 79.93  ? 329 VAL A C     1 
ATOM   2468 O O     . VAL A 1 329 ? 82.280  102.110 97.075  1.00 79.93  ? 329 VAL A O     1 
ATOM   2469 C CB    . VAL A 1 329 ? 84.202  99.448  97.532  1.00 116.26 ? 329 VAL A CB    1 
ATOM   2470 C CG1   . VAL A 1 329 ? 84.189  100.289 98.806  1.00 116.26 ? 329 VAL A CG1   1 
ATOM   2471 C CG2   . VAL A 1 329 ? 84.017  97.987  97.861  1.00 116.26 ? 329 VAL A CG2   1 
ATOM   2472 N N     . LYS A 1 330 ? 84.044  101.987 95.695  1.00 79.29  ? 330 LYS A N     1 
ATOM   2473 C CA    . LYS A 1 330 ? 84.120  103.440 95.591  1.00 79.29  ? 330 LYS A CA    1 
ATOM   2474 C C     . LYS A 1 330 ? 82.872  104.006 94.970  1.00 79.29  ? 330 LYS A C     1 
ATOM   2475 O O     . LYS A 1 330 ? 82.499  105.134 95.270  1.00 79.29  ? 330 LYS A O     1 
ATOM   2476 C CB    . LYS A 1 330 ? 85.327  103.881 94.794  1.00 118.93 ? 330 LYS A CB    1 
ATOM   2477 C CG    . LYS A 1 330 ? 86.616  103.713 95.533  1.00 118.93 ? 330 LYS A CG    1 
ATOM   2478 C CD    . LYS A 1 330 ? 87.767  104.176 94.678  1.00 118.93 ? 330 LYS A CD    1 
ATOM   2479 C CE    . LYS A 1 330 ? 89.087  104.034 95.406  1.00 118.93 ? 330 LYS A CE    1 
ATOM   2480 N NZ    . LYS A 1 330 ? 90.239  104.488 94.568  1.00 118.93 ? 330 LYS A NZ    1 
ATOM   2481 N N     . GLU A 1 331 ? 82.200  103.244 94.135  1.00 81.42  ? 331 GLU A N     1 
ATOM   2482 C CA    . GLU A 1 331 ? 80.963  103.716 93.554  1.00 81.42  ? 331 GLU A CA    1 
ATOM   2483 C C     . GLU A 1 331 ? 79.832  103.792 94.561  1.00 81.42  ? 331 GLU A C     1 
ATOM   2484 O O     . GLU A 1 331 ? 78.802  104.399 94.268  1.00 81.42  ? 331 GLU A O     1 
ATOM   2485 C CB    . GLU A 1 331 ? 80.550  102.806 92.399  1.00 109.37 ? 331 GLU A CB    1 
ATOM   2486 C CG    . GLU A 1 331 ? 81.439  102.927 91.158  1.00 109.37 ? 331 GLU A CG    1 
ATOM   2487 C CD    . GLU A 1 331 ? 81.071  101.956 90.062  1.00 109.37 ? 331 GLU A CD    1 
ATOM   2488 O OE1   . GLU A 1 331 ? 80.182  101.129 90.271  1.00 109.37 ? 331 GLU A OE1   1 
ATOM   2489 O OE2   . GLU A 1 331 ? 81.672  102.025 88.988  1.00 109.37 ? 331 GLU A OE2   1 
ATOM   2490 N N     . GLN A 1 332 ? 79.962  103.149 95.707  1.00 77.74  ? 332 GLN A N     1 
ATOM   2491 C CA    . GLN A 1 332 ? 78.904  103.162 96.704  1.00 77.74  ? 332 GLN A CA    1 
ATOM   2492 C C     . GLN A 1 332 ? 79.199  104.049 97.886  1.00 77.74  ? 332 GLN A C     1 
ATOM   2493 O O     . GLN A 1 332 ? 78.305  104.702 98.398  1.00 77.74  ? 332 GLN A O     1 
ATOM   2494 C CB    . GLN A 1 332 ? 78.661  101.756 97.208  1.00 108.62 ? 332 GLN A CB    1 
ATOM   2495 C CG    . GLN A 1 332 ? 78.215  100.838 96.137  1.00 108.62 ? 332 GLN A CG    1 
ATOM   2496 C CD    . GLN A 1 332 ? 76.928  101.279 95.575  1.00 108.62 ? 332 GLN A CD    1 
ATOM   2497 O OE1   . GLN A 1 332 ? 75.974  101.475 96.309  1.00 108.62 ? 332 GLN A OE1   1 
ATOM   2498 N NE2   . GLN A 1 332 ? 76.875  101.453 94.269  1.00 108.62 ? 332 GLN A NE2   1 
ATOM   2499 N N     . ASN A 1 333 ? 80.430  104.108 98.326  1.00 77.27  ? 333 ASN A N     1 
ATOM   2500 C CA    . ASN A 1 333 ? 80.753  104.863 99.523  1.00 77.27  ? 333 ASN A CA    1 
ATOM   2501 C C     . ASN A 1 333 ? 81.749  105.979 99.254  1.00 77.27  ? 333 ASN A C     1 
ATOM   2502 O O     . ASN A 1 333 ? 82.947  105.725 99.070  1.00 77.27  ? 333 ASN A O     1 
ATOM   2503 C CB    . ASN A 1 333 ? 81.316  103.944 100.568 1.00 104.69 ? 333 ASN A CB    1 
ATOM   2504 C CG    . ASN A 1 333 ? 80.396  102.860 100.912 1.00 104.69 ? 333 ASN A CG    1 
ATOM   2505 O OD1   . ASN A 1 333 ? 79.288  103.089 101.380 1.00 104.69 ? 333 ASN A OD1   1 
ATOM   2506 N ND2   . ASN A 1 333 ? 80.844  101.646 100.721 1.00 104.69 ? 333 ASN A ND2   1 
ATOM   2507 N N     . SER A 1 334 ? 81.272  107.211 99.278  1.00 75.10  ? 334 SER A N     1 
ATOM   2508 C CA    . SER A 1 334 ? 82.152  108.317 98.971  1.00 75.10  ? 334 SER A CA    1 
ATOM   2509 C C     . SER A 1 334 ? 82.948  108.700 100.195 1.00 75.10  ? 334 SER A C     1 
ATOM   2510 O O     . SER A 1 334 ? 82.667  108.256 101.305 1.00 75.10  ? 334 SER A O     1 
ATOM   2511 C CB    . SER A 1 334 ? 81.352  109.481 98.469  1.00 101.15 ? 334 SER A CB    1 
ATOM   2512 O OG    . SER A 1 334 ? 80.539  109.967 99.484  1.00 101.15 ? 334 SER A OG    1 
ATOM   2513 N N     . PHE A 1 335 ? 83.920  109.583 99.995  1.00 73.48  ? 335 PHE A N     1 
ATOM   2514 C CA    . PHE A 1 335 ? 84.772  110.067 101.070 1.00 73.48  ? 335 PHE A CA    1 
ATOM   2515 C C     . PHE A 1 335 ? 84.598  111.547 101.399 1.00 73.48  ? 335 PHE A C     1 
ATOM   2516 O O     . PHE A 1 335 ? 84.284  112.395 100.562 1.00 73.48  ? 335 PHE A O     1 
ATOM   2517 C CB    . PHE A 1 335 ? 86.217  109.763 100.742 1.00 102.53 ? 335 PHE A CB    1 
ATOM   2518 C CG    . PHE A 1 335 ? 86.553  108.309 100.917 1.00 102.53 ? 335 PHE A CG    1 
ATOM   2519 C CD1   . PHE A 1 335 ? 86.092  107.345 100.023 1.00 102.53 ? 335 PHE A CD1   1 
ATOM   2520 C CD2   . PHE A 1 335 ? 87.330  107.901 101.994 1.00 102.53 ? 335 PHE A CD2   1 
ATOM   2521 C CE1   . PHE A 1 335 ? 86.407  106.012 100.211 1.00 102.53 ? 335 PHE A CE1   1 
ATOM   2522 C CE2   . PHE A 1 335 ? 87.647  106.574 102.181 1.00 102.53 ? 335 PHE A CE2   1 
ATOM   2523 C CZ    . PHE A 1 335 ? 87.182  105.627 101.293 1.00 102.53 ? 335 PHE A CZ    1 
ATOM   2524 N N     . VAL A 1 336 ? 84.823  111.826 102.664 1.00 79.42  ? 336 VAL A N     1 
ATOM   2525 C CA    . VAL A 1 336 ? 84.635  113.150 103.215 1.00 79.42  ? 336 VAL A CA    1 
ATOM   2526 C C     . VAL A 1 336 ? 85.733  114.053 102.710 1.00 79.42  ? 336 VAL A C     1 
ATOM   2527 O O     . VAL A 1 336 ? 86.908  113.662 102.653 1.00 79.42  ? 336 VAL A O     1 
ATOM   2528 C CB    . VAL A 1 336 ? 84.634  113.086 104.746 1.00 115.52 ? 336 VAL A CB    1 
ATOM   2529 C CG1   . VAL A 1 336 ? 84.478  114.480 105.378 1.00 115.52 ? 336 VAL A CG1   1 
ATOM   2530 C CG2   . VAL A 1 336 ? 83.559  112.143 105.180 1.00 115.52 ? 336 VAL A CG2   1 
ATOM   2531 N N     . ASN A 1 337 ? 85.328  115.241 102.276 1.00 83.67  ? 337 ASN A N     1 
ATOM   2532 C CA    . ASN A 1 337 ? 86.196  116.284 101.758 1.00 83.67  ? 337 ASN A CA    1 
ATOM   2533 C C     . ASN A 1 337 ? 86.946  115.812 100.536 1.00 83.67  ? 337 ASN A C     1 
ATOM   2534 O O     . ASN A 1 337 ? 87.901  116.438 100.111 1.00 83.67  ? 337 ASN A O     1 
ATOM   2535 C CB    . ASN A 1 337 ? 87.159  116.790 102.832 1.00 113.36 ? 337 ASN A CB    1 
ATOM   2536 C CG    . ASN A 1 337 ? 86.455  117.322 103.986 1.00 113.36 ? 337 ASN A CG    1 
ATOM   2537 O OD1   . ASN A 1 337 ? 85.344  117.812 103.863 1.00 113.36 ? 337 ASN A OD1   1 
ATOM   2538 N ND2   . ASN A 1 337 ? 87.075  117.255 105.115 1.00 113.36 ? 337 ASN A ND2   1 
ATOM   2539 N N     . TRP A 1 338 ? 86.499  114.708 99.982  1.00 85.20  ? 338 TRP A N     1 
ATOM   2540 C CA    . TRP A 1 338 ? 87.076  114.196 98.793  1.00 85.20  ? 338 TRP A CA    1 
ATOM   2541 C C     . TRP A 1 338 ? 88.557  114.065 98.933  1.00 85.20  ? 338 TRP A C     1 
ATOM   2542 O O     . TRP A 1 338 ? 89.264  114.278 97.958  1.00 85.20  ? 338 TRP A O     1 
ATOM   2543 C CB    . TRP A 1 338 ? 86.788  115.103 97.630  1.00 117.97 ? 338 TRP A CB    1 
ATOM   2544 C CG    . TRP A 1 338 ? 85.495  115.558 97.691  1.00 117.97 ? 338 TRP A CG    1 
ATOM   2545 C CD1   . TRP A 1 338 ? 84.393  114.855 97.417  1.00 117.97 ? 338 TRP A CD1   1 
ATOM   2546 C CD2   . TRP A 1 338 ? 85.076  116.832 98.109  1.00 117.97 ? 338 TRP A CD2   1 
ATOM   2547 N NE1   . TRP A 1 338 ? 83.287  115.614 97.627  1.00 117.97 ? 338 TRP A NE1   1 
ATOM   2548 C CE2   . TRP A 1 338 ? 83.685  116.845 98.059  1.00 117.97 ? 338 TRP A CE2   1 
ATOM   2549 C CE3   . TRP A 1 338 ? 85.744  117.979 98.513  1.00 117.97 ? 338 TRP A CE3   1 
ATOM   2550 C CZ2   . TRP A 1 338 ? 82.939  117.957 98.410  1.00 117.97 ? 338 TRP A CZ2   1 
ATOM   2551 C CZ3   . TRP A 1 338 ? 85.009  119.093 98.862  1.00 117.97 ? 338 TRP A CZ3   1 
ATOM   2552 C CH2   . TRP A 1 338 ? 83.625  119.075 98.811  1.00 117.97 ? 338 TRP A CH2   1 
ATOM   2553 N N     . ILE A 1 339 ? 89.057  113.727 100.116 1.00 83.23  ? 339 ILE A N     1 
ATOM   2554 C CA    . ILE A 1 339 ? 90.511  113.675 100.165 1.00 83.23  ? 339 ILE A CA    1 
ATOM   2555 C C     . ILE A 1 339 ? 90.937  112.504 99.293  1.00 83.23  ? 339 ILE A C     1 
ATOM   2556 O O     . ILE A 1 339 ? 90.662  111.349 99.633  1.00 83.23  ? 339 ILE A O     1 
ATOM   2557 C CB    . ILE A 1 339 ? 91.029  113.541 101.590 1.00 123.22 ? 339 ILE A CB    1 
ATOM   2558 C CG1   . ILE A 1 339 ? 90.547  114.700 102.444 1.00 123.22 ? 339 ILE A CG1   1 
ATOM   2559 C CG2   . ILE A 1 339 ? 92.534  113.439 101.586 1.00 123.22 ? 339 ILE A CG2   1 
ATOM   2560 C CD1   . ILE A 1 339 ? 90.938  116.089 101.981 1.00 123.22 ? 339 ILE A CD1   1 
ATOM   2561 N N     . PRO A 1 340 ? 91.651  112.771 98.200  1.00 81.84  ? 340 PRO A N     1 
ATOM   2562 C CA    . PRO A 1 340 ? 91.958  111.767 97.178  1.00 81.84  ? 340 PRO A CA    1 
ATOM   2563 C C     . PRO A 1 340 ? 92.953  110.763 97.638  1.00 81.84  ? 340 PRO A C     1 
ATOM   2564 O O     . PRO A 1 340 ? 93.161  109.745 96.974  1.00 81.84  ? 340 PRO A O     1 
ATOM   2565 C CB    . PRO A 1 340 ? 92.530  112.622 96.046  1.00 540.37 ? 340 PRO A CB    1 
ATOM   2566 C CG    . PRO A 1 340 ? 93.111  113.824 96.752  1.00 540.37 ? 340 PRO A CG    1 
ATOM   2567 C CD    . PRO A 1 340 ? 92.258  114.071 97.939  1.00 540.37 ? 340 PRO A CD    1 
ATOM   2568 N N     . THR A 1 341 ? 93.596  111.051 98.739  1.00 77.83  ? 341 THR A N     1 
ATOM   2569 C CA    . THR A 1 341 ? 94.615  110.211 99.277  1.00 77.83  ? 341 THR A CA    1 
ATOM   2570 C C     . THR A 1 341 ? 94.126  109.401 100.431 1.00 77.83  ? 341 THR A C     1 
ATOM   2571 O O     . THR A 1 341 ? 94.906  108.658 101.004 1.00 77.83  ? 341 THR A O     1 
ATOM   2572 C CB    . THR A 1 341 ? 95.753  111.051 99.773  1.00 108.96 ? 341 THR A CB    1 
ATOM   2573 O OG1   . THR A 1 341 ? 95.250  111.912 100.797 1.00 108.96 ? 341 THR A OG1   1 
ATOM   2574 C CG2   . THR A 1 341 ? 96.326  111.887 98.650  1.00 108.96 ? 341 THR A CG2   1 
ATOM   2575 N N     . GLY A 1 342 ? 92.860  109.526 100.794 1.00 78.66  ? 342 GLY A N     1 
ATOM   2576 C CA    . GLY A 1 342 ? 92.348  108.935 102.024 1.00 78.66  ? 342 GLY A CA    1 
ATOM   2577 C C     . GLY A 1 342 ? 92.026  107.448 102.014 1.00 78.66  ? 342 GLY A C     1 
ATOM   2578 O O     . GLY A 1 342 ? 91.662  106.915 103.069 1.00 78.66  ? 342 GLY A O     1 
ATOM   2579 N N     . PHE A 1 343 ? 92.129  106.759 100.883 1.00 76.16  ? 343 PHE A N     1 
ATOM   2580 C CA    . PHE A 1 343 ? 91.782  105.340 100.825 1.00 76.16  ? 343 PHE A CA    1 
ATOM   2581 C C     . PHE A 1 343 ? 92.956  104.458 100.430 1.00 76.16  ? 343 PHE A C     1 
ATOM   2582 O O     . PHE A 1 343 ? 93.429  104.535 99.296  1.00 76.16  ? 343 PHE A O     1 
ATOM   2583 C CB    . PHE A 1 343 ? 90.656  105.104 99.850  1.00 106.27 ? 343 PHE A CB    1 
ATOM   2584 C CG    . PHE A 1 343 ? 90.276  103.728 99.795  1.00 106.27 ? 343 PHE A CG    1 
ATOM   2585 C CD1   . PHE A 1 343 ? 89.855  103.107 100.932 1.00 106.27 ? 343 PHE A CD1   1 
ATOM   2586 C CD2   . PHE A 1 343 ? 90.356  103.032 98.666  1.00 106.27 ? 343 PHE A CD2   1 
ATOM   2587 C CE1   . PHE A 1 343 ? 89.508  101.802 100.938 1.00 106.27 ? 343 PHE A CE1   1 
ATOM   2588 C CE2   . PHE A 1 343 ? 90.013  101.726 98.643  1.00 106.27 ? 343 PHE A CE2   1 
ATOM   2589 C CZ    . PHE A 1 343 ? 89.585  101.096 99.788  1.00 106.27 ? 343 PHE A CZ    1 
ATOM   2590 N N     . LYS A 1 344 ? 93.422  103.609 101.336 1.00 66.83  ? 344 LYS A N     1 
ATOM   2591 C CA    . LYS A 1 344 ? 94.589  102.797 101.030 1.00 66.83  ? 344 LYS A CA    1 
ATOM   2592 C C     . LYS A 1 344 ? 94.323  101.299 101.024 1.00 66.83  ? 344 LYS A C     1 
ATOM   2593 O O     . LYS A 1 344 ? 93.520  100.787 101.801 1.00 66.83  ? 344 LYS A O     1 
ATOM   2594 C CB    . LYS A 1 344 ? 95.704  103.079 101.983 1.00 100.24 ? 344 LYS A CB    1 
ATOM   2595 C CG    . LYS A 1 344 ? 96.169  104.527 101.976 1.00 100.24 ? 344 LYS A CG    1 
ATOM   2596 C CD    . LYS A 1 344 ? 96.644  104.918 100.589 1.00 100.24 ? 344 LYS A CD    1 
ATOM   2597 C CE    . LYS A 1 344 ? 97.268  106.270 100.516 1.00 100.24 ? 344 LYS A CE    1 
ATOM   2598 N NZ    . LYS A 1 344 ? 97.211  106.726 99.128  1.00 100.24 ? 344 LYS A NZ    1 
ATOM   2599 N N     . ILE A 1 345 ? 95.024  100.591 100.144 1.00 64.13  ? 345 ILE A N     1 
ATOM   2600 C CA    . ILE A 1 345 ? 94.918  99.146  100.022 1.00 64.13  ? 345 ILE A CA    1 
ATOM   2601 C C     . ILE A 1 345 ? 96.281  98.545  100.199 1.00 64.13  ? 345 ILE A C     1 
ATOM   2602 O O     . ILE A 1 345 ? 97.253  99.017  99.623  1.00 64.13  ? 345 ILE A O     1 
ATOM   2603 C CB    . ILE A 1 345 ? 94.381  98.714  98.665  1.00 94.95  ? 345 ILE A CB    1 
ATOM   2604 C CG1   . ILE A 1 345 ? 93.045  99.339  98.418  1.00 94.95  ? 345 ILE A CG1   1 
ATOM   2605 C CG2   . ILE A 1 345 ? 94.254  97.195  98.631  1.00 94.95  ? 345 ILE A CG2   1 
ATOM   2606 C CD1   . ILE A 1 345 ? 92.600  99.236  97.023  1.00 94.95  ? 345 ILE A CD1   1 
ATOM   2607 N N     . SER A 1 346 ? 96.355  97.499  100.971 1.00 69.04  ? 346 SER A N     1 
ATOM   2608 C CA    . SER A 1 346 ? 97.605  96.811  101.166 1.00 69.04  ? 346 SER A CA    1 
ATOM   2609 C C     . SER A 1 346 ? 97.378  95.323  101.045 1.00 69.04  ? 346 SER A C     1 
ATOM   2610 O O     . SER A 1 346 ? 96.272  94.828  101.279 1.00 69.04  ? 346 SER A O     1 
ATOM   2611 C CB    . SER A 1 346 ? 98.190  97.112  102.503 1.00 92.99  ? 346 SER A CB    1 
ATOM   2612 O OG    . SER A 1 346 ? 97.370  96.585  103.523 1.00 92.99  ? 346 SER A OG    1 
ATOM   2613 N N     . LYS A 1 347 ? 98.428  94.603  100.662 1.00 71.66  ? 347 LYS A N     1 
ATOM   2614 C CA    . LYS A 1 347 ? 98.347  93.156  100.541 1.00 71.66  ? 347 LYS A CA    1 
ATOM   2615 C C     . LYS A 1 347 ? 99.568  92.497  101.148 1.00 71.66  ? 347 LYS A C     1 
ATOM   2616 O O     . LYS A 1 347 ? 100.662 93.037  101.082 1.00 71.66  ? 347 LYS A O     1 
ATOM   2617 C CB    . LYS A 1 347 ? 98.239  92.744  99.082  1.00 107.49 ? 347 LYS A CB    1 
ATOM   2618 C CG    . LYS A 1 347 ? 97.021  93.297  98.370  1.00 107.49 ? 347 LYS A CG    1 
ATOM   2619 C CD    . LYS A 1 347 ? 96.985  92.945  96.900  1.00 107.49 ? 347 LYS A CD    1 
ATOM   2620 C CE    . LYS A 1 347 ? 98.006  93.778  96.121  1.00 107.49 ? 347 LYS A CE    1 
ATOM   2621 N NZ    . LYS A 1 347 ? 97.800  93.675  94.664  1.00 107.49 ? 347 LYS A NZ    1 
ATOM   2622 N N     . SER A 1 348 ? 99.393  91.311  101.700 1.00 69.48  ? 348 SER A N     1 
ATOM   2623 C CA    . SER A 1 348 ? 100.542 90.504  102.057 1.00 69.48  ? 348 SER A CA    1 
ATOM   2624 C C     . SER A 1 348 ? 100.126 89.061  101.864 1.00 69.48  ? 348 SER A C     1 
ATOM   2625 O O     . SER A 1 348 ? 98.951  88.732  102.015 1.00 69.48  ? 348 SER A O     1 
ATOM   2626 C CB    . SER A 1 348 ? 101.054 90.756  103.473 1.00 93.59  ? 348 SER A CB    1 
ATOM   2627 O OG    . SER A 1 348 ? 100.202 90.285  104.497 1.00 93.59  ? 348 SER A OG    1 
ATOM   2628 N N     . GLU A 1 349 ? 101.094 88.195  101.543 1.00 71.54  ? 349 GLU A N     1 
ATOM   2629 C CA    . GLU A 1 349 ? 100.804 86.821  101.153 1.00 71.54  ? 349 GLU A CA    1 
ATOM   2630 C C     . GLU A 1 349 ? 100.475 85.876  102.287 1.00 71.54  ? 349 GLU A C     1 
ATOM   2631 O O     . GLU A 1 349 ? 100.045 84.751  102.026 1.00 71.54  ? 349 GLU A O     1 
ATOM   2632 C CB    . GLU A 1 349 ? 101.968 86.230  100.383 1.00 96.10  ? 349 GLU A CB    1 
ATOM   2633 C CG    . GLU A 1 349 ? 103.224 85.996  101.177 1.00 96.10  ? 349 GLU A CG    1 
ATOM   2634 C CD    . GLU A 1 349 ? 104.109 87.187  101.219 1.00 96.10  ? 349 GLU A CD    1 
ATOM   2635 O OE1   . GLU A 1 349 ? 103.610 88.287  101.009 1.00 96.10  ? 349 GLU A OE1   1 
ATOM   2636 O OE2   . GLU A 1 349 ? 105.308 87.028  101.455 1.00 96.10  ? 349 GLU A OE2   1 
ATOM   2637 N N     . THR A 1 350 ? 100.666 86.249  103.522 1.00 70.84  ? 350 THR A N     1 
ATOM   2638 C CA    . THR A 1 350 ? 100.419 85.245  104.534 1.00 70.84  ? 350 THR A CA    1 
ATOM   2639 C C     . THR A 1 350 ? 98.929  85.156  104.778 1.00 70.84  ? 350 THR A C     1 
ATOM   2640 O O     . THR A 1 350 ? 98.332  86.034  105.415 1.00 70.84  ? 350 THR A O     1 
ATOM   2641 C CB    . THR A 1 350 ? 101.168 85.540  105.818 1.00 99.18  ? 350 THR A CB    1 
ATOM   2642 O OG1   . THR A 1 350 ? 102.561 85.595  105.547 1.00 99.18  ? 350 THR A OG1   1 
ATOM   2643 C CG2   . THR A 1 350 ? 100.928 84.428  106.781 1.00 99.18  ? 350 THR A CG2   1 
ATOM   2644 N N     . SER A 1 351 ? 98.354  84.073  104.291 1.00 71.67  ? 351 SER A N     1 
ATOM   2645 C CA    . SER A 1 351 ? 96.954  83.783  104.447 1.00 71.67  ? 351 SER A CA    1 
ATOM   2646 C C     . SER A 1 351 ? 96.672  83.440  105.906 1.00 71.67  ? 351 SER A C     1 
ATOM   2647 O O     . SER A 1 351 ? 97.573  83.008  106.613 1.00 71.67  ? 351 SER A O     1 
ATOM   2648 C CB    . SER A 1 351 ? 96.586  82.613  103.556 1.00 96.53  ? 351 SER A CB    1 
ATOM   2649 O OG    . SER A 1 351 ? 97.248  81.452  103.989 1.00 96.53  ? 351 SER A OG    1 
ATOM   2650 N N     . PRO A 1 352 ? 95.449  83.665  106.376 1.00 74.34  ? 352 PRO A N     1 
ATOM   2651 C CA    . PRO A 1 352 ? 95.033  83.272  107.716 1.00 74.34  ? 352 PRO A CA    1 
ATOM   2652 C C     . PRO A 1 352 ? 94.764  81.800  107.745 1.00 74.34  ? 352 PRO A C     1 
ATOM   2653 O O     . PRO A 1 352 ? 94.420  81.192  106.737 1.00 74.34  ? 352 PRO A O     1 
ATOM   2654 C CB    . PRO A 1 352 ? 93.729  84.029  107.895 1.00 490.84 ? 352 PRO A CB    1 
ATOM   2655 C CG    . PRO A 1 352 ? 93.186  84.110  106.501 1.00 490.84 ? 352 PRO A CG    1 
ATOM   2656 C CD    . PRO A 1 352 ? 94.370  84.282  105.609 1.00 490.84 ? 352 PRO A CD    1 
ATOM   2657 N N     . LYS A 1 353 ? 94.855  81.226  108.915 1.00 77.27  ? 353 LYS A N     1 
ATOM   2658 C CA    . LYS A 1 353 ? 94.407  79.865  108.950 1.00 77.27  ? 353 LYS A CA    1 
ATOM   2659 C C     . LYS A 1 353 ? 92.913  79.872  108.721 1.00 77.27  ? 353 LYS A C     1 
ATOM   2660 O O     . LYS A 1 353 ? 92.226  80.843  109.017 1.00 77.27  ? 353 LYS A O     1 
ATOM   2661 C CB    . LYS A 1 353 ? 94.789  79.216  110.249 1.00 115.90 ? 353 LYS A CB    1 
ATOM   2662 C CG    . LYS A 1 353 ? 96.270  79.082  110.379 1.00 115.90 ? 353 LYS A CG    1 
ATOM   2663 C CD    . LYS A 1 353 ? 96.671  78.347  111.641 1.00 115.90 ? 353 LYS A CD    1 
ATOM   2664 C CE    . LYS A 1 353 ? 98.191  78.280  111.785 1.00 115.90 ? 353 LYS A CE    1 
ATOM   2665 N NZ    . LYS A 1 353 ? 98.846  77.449  110.731 1.00 115.90 ? 353 LYS A NZ    1 
ATOM   2666 N N     . ASP A 1 354 ? 92.441  78.811  108.108 1.00 81.40  ? 354 ASP A N     1 
ATOM   2667 C CA    . ASP A 1 354 ? 91.051  78.545  107.770 1.00 81.40  ? 354 ASP A CA    1 
ATOM   2668 C C     . ASP A 1 354 ? 90.500  79.260  106.535 1.00 81.40  ? 354 ASP A C     1 
ATOM   2669 O O     . ASP A 1 354 ? 89.327  79.071  106.220 1.00 81.40  ? 354 ASP A O     1 
ATOM   2670 C CB    . ASP A 1 354 ? 90.121  78.850  108.939 1.00 104.66 ? 354 ASP A CB    1 
ATOM   2671 C CG    . ASP A 1 354 ? 90.422  78.023  110.170 1.00 104.66 ? 354 ASP A CG    1 
ATOM   2672 O OD1   . ASP A 1 354 ? 90.748  76.835  110.060 1.00 104.66 ? 354 ASP A OD1   1 
ATOM   2673 O OD2   . ASP A 1 354 ? 90.303  78.558  111.274 1.00 104.66 ? 354 ASP A OD2   1 
ATOM   2674 N N     . SER A 1 355 ? 91.281  80.024  105.784 1.00 80.92  ? 355 SER A N     1 
ATOM   2675 C CA    . SER A 1 355 ? 90.706  80.520  104.531 1.00 80.92  ? 355 SER A CA    1 
ATOM   2676 C C     . SER A 1 355 ? 91.804  80.927  103.554 1.00 80.92  ? 355 SER A C     1 
ATOM   2677 O O     . SER A 1 355 ? 92.953  81.119  103.943 1.00 80.92  ? 355 SER A O     1 
ATOM   2678 C CB    . SER A 1 355 ? 89.753  81.689  104.782 1.00 108.99 ? 355 SER A CB    1 
ATOM   2679 O OG    . SER A 1 355 ? 90.444  82.853  105.169 1.00 108.99 ? 355 SER A OG    1 
ATOM   2680 N N     . ALA A 1 356 ? 91.459  81.055  102.271 1.00 78.52  ? 356 ALA A N     1 
ATOM   2681 C CA    . ALA A 1 356 ? 92.485  81.498  101.328 1.00 78.52  ? 356 ALA A CA    1 
ATOM   2682 C C     . ALA A 1 356 ? 92.804  82.970  101.486 1.00 78.52  ? 356 ALA A C     1 
ATOM   2683 O O     . ALA A 1 356 ? 93.935  83.396  101.242 1.00 78.52  ? 356 ALA A O     1 
ATOM   2684 C CB    . ALA A 1 356 ? 92.068  81.246  99.889  1.00 107.07 ? 356 ALA A CB    1 
ATOM   2685 N N     . LEU A 1 357 ? 91.809  83.766  101.814 1.00 72.21  ? 357 LEU A N     1 
ATOM   2686 C CA    . LEU A 1 357 ? 92.002  85.191  101.881 1.00 72.21  ? 357 LEU A CA    1 
ATOM   2687 C C     . LEU A 1 357 ? 91.272  85.770  103.037 1.00 72.21  ? 357 LEU A C     1 
ATOM   2688 O O     . LEU A 1 357 ? 90.081  85.558  103.184 1.00 72.21  ? 357 LEU A O     1 
ATOM   2689 C CB    . LEU A 1 357 ? 91.443  85.895  100.677 1.00 106.91 ? 357 LEU A CB    1 
ATOM   2690 C CG    . LEU A 1 357 ? 92.065  85.635  99.334  1.00 106.91 ? 357 LEU A CG    1 
ATOM   2691 C CD1   . LEU A 1 357 ? 91.200  86.290  98.259  1.00 106.91 ? 357 LEU A CD1   1 
ATOM   2692 C CD2   . LEU A 1 357 ? 93.475  86.186  99.330  1.00 106.91 ? 357 LEU A CD2   1 
ATOM   2693 N N     . GLY A 1 358 ? 91.946  86.567  103.826 1.00 68.41  ? 358 GLY A N     1 
ATOM   2694 C CA    . GLY A 1 358 ? 91.258  87.304  104.846 1.00 68.41  ? 358 GLY A CA    1 
ATOM   2695 C C     . GLY A 1 358 ? 91.089  88.707  104.307 1.00 68.41  ? 358 GLY A C     1 
ATOM   2696 O O     . GLY A 1 358 ? 92.007  89.240  103.699 1.00 68.41  ? 358 GLY A O     1 
ATOM   2697 N N     . VAL A 1 359 ? 89.940  89.321  104.545 1.00 68.65  ? 359 VAL A N     1 
ATOM   2698 C CA    . VAL A 1 359 ? 89.814  90.691  104.121 1.00 68.65  ? 359 VAL A CA    1 
ATOM   2699 C C     . VAL A 1 359 ? 89.437  91.536  105.300 1.00 68.65  ? 359 VAL A C     1 
ATOM   2700 O O     . VAL A 1 359 ? 88.447  91.261  105.973 1.00 68.65  ? 359 VAL A O     1 
ATOM   2701 C CB    . VAL A 1 359 ? 88.828  90.840  102.979 1.00 99.85  ? 359 VAL A CB    1 
ATOM   2702 C CG1   . VAL A 1 359 ? 88.775  92.293  102.527 1.00 99.85  ? 359 VAL A CG1   1 
ATOM   2703 C CG2   . VAL A 1 359 ? 89.313  89.972  101.858 1.00 99.85  ? 359 VAL A CG2   1 
ATOM   2704 N N     . ILE A 1 360 ? 90.211  92.558  105.556 1.00 66.42  ? 360 ILE A N     1 
ATOM   2705 C CA    . ILE A 1 360 ? 90.019  93.390  106.727 1.00 66.42  ? 360 ILE A CA    1 
ATOM   2706 C C     . ILE A 1 360 ? 89.827  94.823  106.359 1.00 66.42  ? 360 ILE A C     1 
ATOM   2707 O O     . ILE A 1 360 ? 90.694  95.423  105.715 1.00 66.42  ? 360 ILE A O     1 
ATOM   2708 C CB    . ILE A 1 360 ? 91.236  93.338  107.624 1.00 98.34  ? 360 ILE A CB    1 
ATOM   2709 C CG1   . ILE A 1 360 ? 91.501  91.914  107.989 1.00 98.34  ? 360 ILE A CG1   1 
ATOM   2710 C CG2   . ILE A 1 360 ? 91.046  94.164  108.799 1.00 98.34  ? 360 ILE A CG2   1 
ATOM   2711 C CD1   . ILE A 1 360 ? 92.587  91.216  107.130 1.00 98.34  ? 360 ILE A CD1   1 
ATOM   2712 N N     . MET A 1 361 ? 88.781  95.422  106.861 1.00 67.57  ? 361 MET A N     1 
ATOM   2713 C CA    . MET A 1 361 ? 88.605  96.836  106.602 1.00 67.57  ? 361 MET A CA    1 
ATOM   2714 C C     . MET A 1 361 ? 88.475  97.621  107.875 1.00 67.57  ? 361 MET A C     1 
ATOM   2715 O O     . MET A 1 361 ? 87.784  97.221  108.816 1.00 67.57  ? 361 MET A O     1 
ATOM   2716 C CB    . MET A 1 361 ? 87.419  97.091  105.748 1.00 97.07  ? 361 MET A CB    1 
ATOM   2717 C CG    . MET A 1 361 ? 87.128  98.537  105.446 1.00 97.07  ? 361 MET A CG    1 
ATOM   2718 S SD    . MET A 1 361 ? 86.139  99.347  106.676 1.00 97.07  ? 361 MET A SD    1 
ATOM   2719 C CE    . MET A 1 361 ? 84.500  98.736  106.246 1.00 97.07  ? 361 MET A CE    1 
ATOM   2720 N N     . LEU A 1 362 ? 89.150  98.728  107.879 1.00 59.17  ? 362 LEU A N     1 
ATOM   2721 C CA    . LEU A 1 362 ? 89.097  99.665  108.949 1.00 59.17  ? 362 LEU A CA    1 
ATOM   2722 C C     . LEU A 1 362 ? 88.609  100.931 108.344 1.00 59.17  ? 362 LEU A C     1 
ATOM   2723 O O     . LEU A 1 362 ? 88.949  101.256 107.208 1.00 59.17  ? 362 LEU A O     1 
ATOM   2724 C CB    . LEU A 1 362 ? 90.433  99.930  109.552 1.00 87.60  ? 362 LEU A CB    1 
ATOM   2725 C CG    . LEU A 1 362 ? 91.168  98.777  110.163 1.00 87.60  ? 362 LEU A CG    1 
ATOM   2726 C CD1   . LEU A 1 362 ? 92.536  99.251  110.583 1.00 87.60  ? 362 LEU A CD1   1 
ATOM   2727 C CD2   . LEU A 1 362 ? 90.403  98.257  111.337 1.00 87.60  ? 362 LEU A CD2   1 
ATOM   2728 N N     . GLY A 1 363 ? 87.905  101.707 109.125 1.00 57.60  ? 363 GLY A N     1 
ATOM   2729 C CA    . GLY A 1 363 ? 87.565  102.995 108.591 1.00 57.60  ? 363 GLY A CA    1 
ATOM   2730 C C     . GLY A 1 363 ? 86.992  103.950 109.595 1.00 57.60  ? 363 GLY A C     1 
ATOM   2731 O O     . GLY A 1 363 ? 86.477  103.579 110.650 1.00 57.60  ? 363 GLY A O     1 
ATOM   2732 N N     . ASN A 1 364 ? 87.063  105.171 109.228 1.00 62.52  ? 364 ASN A N     1 
ATOM   2733 C CA    . ASN A 1 364 ? 86.598  106.251 110.035 1.00 62.52  ? 364 ASN A CA    1 
ATOM   2734 C C     . ASN A 1 364 ? 85.399  106.760 109.270 1.00 62.52  ? 364 ASN A C     1 
ATOM   2735 O O     . ASN A 1 364 ? 85.546  107.323 108.185 1.00 62.52  ? 364 ASN A O     1 
ATOM   2736 C CB    . ASN A 1 364 ? 87.726  107.245 110.166 1.00 84.70  ? 364 ASN A CB    1 
ATOM   2737 C CG    . ASN A 1 364 ? 87.498  108.217 111.195 1.00 84.70  ? 364 ASN A CG    1 
ATOM   2738 O OD1   . ASN A 1 364 ? 86.363  108.486 111.586 1.00 84.70  ? 364 ASN A OD1   1 
ATOM   2739 N ND2   . ASN A 1 364 ? 88.578  108.780 111.680 1.00 84.70  ? 364 ASN A ND2   1 
ATOM   2740 N N     . ASN A 1 365 ? 84.225  106.500 109.782 1.00 65.43  ? 365 ASN A N     1 
ATOM   2741 C CA    . ASN A 1 365 ? 83.015  106.802 109.063 1.00 65.43  ? 365 ASN A CA    1 
ATOM   2742 C C     . ASN A 1 365 ? 82.035  107.496 109.976 1.00 65.43  ? 365 ASN A C     1 
ATOM   2743 O O     . ASN A 1 365 ? 81.929  107.190 111.160 1.00 65.43  ? 365 ASN A O     1 
ATOM   2744 C CB    . ASN A 1 365 ? 82.449  105.546 108.466 1.00 88.65  ? 365 ASN A CB    1 
ATOM   2745 C CG    . ASN A 1 365 ? 81.174  105.749 107.662 1.00 88.65  ? 365 ASN A CG    1 
ATOM   2746 O OD1   . ASN A 1 365 ? 80.116  106.126 108.180 1.00 88.65  ? 365 ASN A OD1   1 
ATOM   2747 N ND2   . ASN A 1 365 ? 81.251  105.417 106.389 1.00 88.65  ? 365 ASN A ND2   1 
ATOM   2748 N N     . SER A 1 366 ? 81.335  108.448 109.408 1.00 67.99  ? 366 SER A N     1 
ATOM   2749 C CA    . SER A 1 366 ? 80.448  109.324 110.150 1.00 67.99  ? 366 SER A CA    1 
ATOM   2750 C C     . SER A 1 366 ? 79.245  108.636 110.784 1.00 67.99  ? 366 SER A C     1 
ATOM   2751 O O     . SER A 1 366 ? 78.641  109.206 111.697 1.00 67.99  ? 366 SER A O     1 
ATOM   2752 C CB    . SER A 1 366 ? 79.954  110.408 109.216 1.00 91.58  ? 366 SER A CB    1 
ATOM   2753 O OG    . SER A 1 366 ? 79.205  109.857 108.146 1.00 91.58  ? 366 SER A OG    1 
ATOM   2754 N N     . GLU A 1 367 ? 78.876  107.441 110.366 1.00 68.56  ? 367 GLU A N     1 
ATOM   2755 C CA    . GLU A 1 367 ? 77.732  106.838 111.020 1.00 68.56  ? 367 GLU A CA    1 
ATOM   2756 C C     . GLU A 1 367 ? 78.097  106.293 112.347 1.00 68.56  ? 367 GLU A C     1 
ATOM   2757 O O     . GLU A 1 367 ? 77.224  105.841 113.069 1.00 68.56  ? 367 GLU A O     1 
ATOM   2758 C CB    . GLU A 1 367 ? 77.123  105.738 110.201 1.00 92.10  ? 367 GLU A CB    1 
ATOM   2759 C CG    . GLU A 1 367 ? 76.566  106.179 108.920 1.00 92.10  ? 367 GLU A CG    1 
ATOM   2760 C CD    . GLU A 1 367 ? 75.371  107.075 109.055 1.00 92.10  ? 367 GLU A CD    1 
ATOM   2761 O OE1   . GLU A 1 367 ? 74.834  107.213 110.154 1.00 92.10  ? 367 GLU A OE1   1 
ATOM   2762 O OE2   . GLU A 1 367 ? 74.942  107.621 108.034 1.00 92.10  ? 367 GLU A OE2   1 
ATOM   2763 N N     . ILE A 1 368 ? 79.375  106.350 112.694 1.00 65.99  ? 368 ILE A N     1 
ATOM   2764 C CA    . ILE A 1 368 ? 79.820  105.837 113.958 1.00 65.99  ? 368 ILE A CA    1 
ATOM   2765 C C     . ILE A 1 368 ? 79.221  106.637 115.065 1.00 65.99  ? 368 ILE A C     1 
ATOM   2766 O O     . ILE A 1 368 ? 79.204  106.195 116.214 1.00 65.99  ? 368 ILE A O     1 
ATOM   2767 C CB    . ILE A 1 368 ? 81.338  105.853 114.102 1.00 97.70  ? 368 ILE A CB    1 
ATOM   2768 C CG1   . ILE A 1 368 ? 81.736  104.849 115.187 1.00 97.70  ? 368 ILE A CG1   1 
ATOM   2769 C CG2   . ILE A 1 368 ? 81.833  107.252 114.424 1.00 97.70  ? 368 ILE A CG2   1 
ATOM   2770 C CD1   . ILE A 1 368 ? 83.178  104.467 115.172 1.00 97.70  ? 368 ILE A CD1   1 
ATOM   2771 N N     . VAL A 1 369 ? 78.697  107.812 114.751 1.00 65.92  ? 369 VAL A N     1 
ATOM   2772 C CA    . VAL A 1 369 ? 78.116  108.601 115.804 1.00 65.92  ? 369 VAL A CA    1 
ATOM   2773 C C     . VAL A 1 369 ? 76.976  107.877 116.444 1.00 65.92  ? 369 VAL A C     1 
ATOM   2774 O O     . VAL A 1 369 ? 76.734  108.073 117.635 1.00 65.92  ? 369 VAL A O     1 
ATOM   2775 C CB    . VAL A 1 369 ? 77.636  109.967 115.310 1.00 95.88  ? 369 VAL A CB    1 
ATOM   2776 C CG1   . VAL A 1 369 ? 78.789  110.736 114.771 1.00 95.88  ? 369 VAL A CG1   1 
ATOM   2777 C CG2   . VAL A 1 369 ? 76.502  109.816 114.282 1.00 95.88  ? 369 VAL A CG2   1 
ATOM   2778 N N     . SER A 1 370 ? 76.272  107.009 115.720 1.00 67.98  ? 370 SER A N     1 
ATOM   2779 C CA    . SER A 1 370 ? 75.134  106.386 116.365 1.00 67.98  ? 370 SER A CA    1 
ATOM   2780 C C     . SER A 1 370 ? 75.547  105.583 117.586 1.00 67.98  ? 370 SER A C     1 
ATOM   2781 O O     . SER A 1 370 ? 74.734  105.390 118.486 1.00 67.98  ? 370 SER A O     1 
ATOM   2782 C CB    . SER A 1 370 ? 74.388  105.515 115.405 1.00 91.56  ? 370 SER A CB    1 
ATOM   2783 O OG    . SER A 1 370 ? 75.151  104.387 115.095 1.00 91.56  ? 370 SER A OG    1 
ATOM   2784 N N     . VAL A 1 371 ? 76.811  105.187 117.678 1.00 65.18  ? 371 VAL A N     1 
ATOM   2785 C CA    . VAL A 1 371 ? 77.289  104.460 118.842 1.00 65.18  ? 371 VAL A CA    1 
ATOM   2786 C C     . VAL A 1 371 ? 77.292  105.352 120.026 1.00 65.18  ? 371 VAL A C     1 
ATOM   2787 O O     . VAL A 1 371 ? 76.953  104.944 121.144 1.00 65.18  ? 371 VAL A O     1 
ATOM   2788 C CB    . VAL A 1 371 ? 78.718  103.954 118.644 1.00 94.81  ? 371 VAL A CB    1 
ATOM   2789 C CG1   . VAL A 1 371 ? 79.238  103.321 119.966 1.00 94.81  ? 371 VAL A CG1   1 
ATOM   2790 C CG2   . VAL A 1 371 ? 78.786  102.997 117.487 1.00 94.81  ? 371 VAL A CG2   1 
ATOM   2791 N N     . PHE A 1 372 ? 77.764  106.550 119.820 1.00 64.34  ? 372 PHE A N     1 
ATOM   2792 C CA    . PHE A 1 372 ? 77.912  107.440 120.925 1.00 64.34  ? 372 PHE A CA    1 
ATOM   2793 C C     . PHE A 1 372 ? 76.602  108.084 121.250 1.00 64.34  ? 372 PHE A C     1 
ATOM   2794 O O     . PHE A 1 372 ? 76.349  108.440 122.404 1.00 64.34  ? 372 PHE A O     1 
ATOM   2795 C CB    . PHE A 1 372 ? 78.991  108.392 120.554 1.00 89.78  ? 372 PHE A CB    1 
ATOM   2796 C CG    . PHE A 1 372 ? 80.170  107.665 120.142 1.00 89.78  ? 372 PHE A CG    1 
ATOM   2797 C CD1   . PHE A 1 372 ? 80.723  106.717 120.981 1.00 89.78  ? 372 PHE A CD1   1 
ATOM   2798 C CD2   . PHE A 1 372 ? 80.673  107.804 118.891 1.00 89.78  ? 372 PHE A CD2   1 
ATOM   2799 C CE1   . PHE A 1 372 ? 81.793  105.969 120.585 1.00 89.78  ? 372 PHE A CE1   1 
ATOM   2800 C CE2   . PHE A 1 372 ? 81.748  107.056 118.491 1.00 89.78  ? 372 PHE A CE2   1 
ATOM   2801 C CZ    . PHE A 1 372 ? 82.303  106.138 119.340 1.00 89.78  ? 372 PHE A CZ    1 
ATOM   2802 N N     . GLU A 1 373 ? 75.754  108.194 120.257 1.00 64.04  ? 373 GLU A N     1 
ATOM   2803 C CA    . GLU A 1 373 ? 74.457  108.740 120.516 1.00 64.04  ? 373 GLU A CA    1 
ATOM   2804 C C     . GLU A 1 373 ? 73.679  107.799 121.400 1.00 64.04  ? 373 GLU A C     1 
ATOM   2805 O O     . GLU A 1 373 ? 72.982  108.248 122.315 1.00 64.04  ? 373 GLU A O     1 
ATOM   2806 C CB    . GLU A 1 373 ? 73.735  109.018 119.206 1.00 86.02  ? 373 GLU A CB    1 
ATOM   2807 C CG    . GLU A 1 373 ? 74.326  110.187 118.409 1.00 86.02  ? 373 GLU A CG    1 
ATOM   2808 C CD    . GLU A 1 373 ? 73.706  110.318 117.059 1.00 86.02  ? 373 GLU A CD    1 
ATOM   2809 O OE1   . GLU A 1 373 ? 72.981  109.402 116.674 1.00 86.02  ? 373 GLU A OE1   1 
ATOM   2810 O OE2   . GLU A 1 373 ? 73.931  111.326 116.385 1.00 86.02  ? 373 GLU A OE2   1 
ATOM   2811 N N     . ARG A 1 374 ? 73.809  106.489 121.172 1.00 62.92  ? 374 ARG A N     1 
ATOM   2812 C CA    . ARG A 1 374 ? 73.115  105.531 122.026 1.00 62.92  ? 374 ARG A CA    1 
ATOM   2813 C C     . ARG A 1 374 ? 73.599  105.654 123.454 1.00 62.92  ? 374 ARG A C     1 
ATOM   2814 O O     . ARG A 1 374 ? 72.789  105.661 124.391 1.00 62.92  ? 374 ARG A O     1 
ATOM   2815 C CB    . ARG A 1 374 ? 73.305  104.105 121.523 1.00 92.45  ? 374 ARG A CB    1 
ATOM   2816 C CG    . ARG A 1 374 ? 72.522  103.744 120.245 1.00 92.45  ? 374 ARG A CG    1 
ATOM   2817 C CD    . ARG A 1 374 ? 72.528  102.228 119.913 1.00 92.45  ? 374 ARG A CD    1 
ATOM   2818 N NE    . ARG A 1 374 ? 73.845  101.646 119.554 1.00 92.45  ? 374 ARG A NE    1 
ATOM   2819 C CZ    . ARG A 1 374 ? 74.380  101.578 118.323 1.00 92.45  ? 374 ARG A CZ    1 
ATOM   2820 N NH1   . ARG A 1 374 ? 73.773  102.103 117.271 1.00 92.45  ? 374 ARG A NH1   1 
ATOM   2821 N NH2   . ARG A 1 374 ? 75.553  100.959 118.144 1.00 92.45  ? 374 ARG A NH2   1 
ATOM   2822 N N     . ILE A 1 375 ? 74.898  105.814 123.641 1.00 61.87  ? 375 ILE A N     1 
ATOM   2823 C CA    . ILE A 1 375 ? 75.403  105.962 124.992 1.00 61.87  ? 375 ILE A CA    1 
ATOM   2824 C C     . ILE A 1 375 ? 74.842  107.195 125.619 1.00 61.87  ? 375 ILE A C     1 
ATOM   2825 O O     . ILE A 1 375 ? 74.418  107.183 126.778 1.00 61.87  ? 375 ILE A O     1 
ATOM   2826 C CB    . ILE A 1 375 ? 76.931  106.030 125.020 1.00 91.60  ? 375 ILE A CB    1 
ATOM   2827 C CG1   . ILE A 1 375 ? 77.487  104.690 124.575 1.00 91.60  ? 375 ILE A CG1   1 
ATOM   2828 C CG2   . ILE A 1 375 ? 77.432  106.452 126.450 1.00 91.60  ? 375 ILE A CG2   1 
ATOM   2829 C CD1   . ILE A 1 375 ? 78.945  104.705 124.250 1.00 91.60  ? 375 ILE A CD1   1 
ATOM   2830 N N     . GLY A 1 376 ? 74.865  108.283 124.886 1.00 59.27  ? 376 GLY A N     1 
ATOM   2831 C CA    . GLY A 1 376 ? 74.368  109.509 125.447 1.00 59.27  ? 376 GLY A CA    1 
ATOM   2832 C C     . GLY A 1 376 ? 72.926  109.359 125.849 1.00 59.27  ? 376 GLY A C     1 
ATOM   2833 O O     . GLY A 1 376 ? 72.535  109.757 126.939 1.00 59.27  ? 376 GLY A O     1 
ATOM   2834 N N     . ALA A 1 377 ? 72.130  108.734 125.006 1.00 60.01  ? 377 ALA A N     1 
ATOM   2835 C CA    . ALA A 1 377 ? 70.718  108.633 125.333 1.00 60.01  ? 377 ALA A CA    1 
ATOM   2836 C C     . ALA A 1 377 ? 70.509  107.890 126.628 1.00 60.01  ? 377 ALA A C     1 
ATOM   2837 O O     . ALA A 1 377 ? 69.698  108.294 127.462 1.00 60.01  ? 377 ALA A O     1 
ATOM   2838 C CB    . ALA A 1 377 ? 69.979  107.935 124.209 1.00 81.83  ? 377 ALA A CB    1 
ATOM   2839 N N     . ASN A 1 378 ? 71.242  106.809 126.815 1.00 55.66  ? 378 ASN A N     1 
ATOM   2840 C CA    . ASN A 1 378 ? 71.053  106.070 128.037 1.00 55.66  ? 378 ASN A CA    1 
ATOM   2841 C C     . ASN A 1 378 ? 71.433  106.934 129.201 1.00 55.66  ? 378 ASN A C     1 
ATOM   2842 O O     . ASN A 1 378 ? 70.731  106.974 130.220 1.00 55.66  ? 378 ASN A O     1 
ATOM   2843 C CB    . ASN A 1 378 ? 71.908  104.830 128.047 1.00 75.41  ? 378 ASN A CB    1 
ATOM   2844 C CG    . ASN A 1 378 ? 71.452  103.821 127.099 1.00 75.41  ? 378 ASN A CG    1 
ATOM   2845 O OD1   . ASN A 1 378 ? 70.289  103.780 126.710 1.00 75.41  ? 378 ASN A OD1   1 
ATOM   2846 N ND2   . ASN A 1 378 ? 72.360  102.964 126.701 1.00 75.41  ? 378 ASN A ND2   1 
ATOM   2847 N N     . PHE A 1 379 ? 72.528  107.664 129.041 1.00 56.37  ? 379 PHE A N     1 
ATOM   2848 C CA    . PHE A 1 379 ? 73.013  108.514 130.108 1.00 56.37  ? 379 PHE A CA    1 
ATOM   2849 C C     . PHE A 1 379 ? 71.994  109.548 130.470 1.00 56.37  ? 379 PHE A C     1 
ATOM   2850 O O     . PHE A 1 379 ? 71.705  109.760 131.647 1.00 56.37  ? 379 PHE A O     1 
ATOM   2851 C CB    . PHE A 1 379 ? 74.291  109.191 129.690 1.00 78.66  ? 379 PHE A CB    1 
ATOM   2852 C CG    . PHE A 1 379 ? 74.814  110.126 130.689 1.00 78.66  ? 379 PHE A CG    1 
ATOM   2853 C CD1   . PHE A 1 379 ? 75.598  109.685 131.727 1.00 78.66  ? 379 PHE A CD1   1 
ATOM   2854 C CD2   . PHE A 1 379 ? 74.552  111.461 130.576 1.00 78.66  ? 379 PHE A CD2   1 
ATOM   2855 C CE1   . PHE A 1 379 ? 76.109  110.580 132.642 1.00 78.66  ? 379 PHE A CE1   1 
ATOM   2856 C CE2   . PHE A 1 379 ? 75.057  112.353 131.478 1.00 78.66  ? 379 PHE A CE2   1 
ATOM   2857 C CZ    . PHE A 1 379 ? 75.838  111.915 132.513 1.00 78.66  ? 379 PHE A CZ    1 
ATOM   2858 N N     . ASP A 1 380 ? 71.430  110.200 129.471 1.00 58.36  ? 380 ASP A N     1 
ATOM   2859 C CA    . ASP A 1 380 ? 70.497  111.275 129.741 1.00 58.36  ? 380 ASP A CA    1 
ATOM   2860 C C     . ASP A 1 380 ? 69.293  110.757 130.489 1.00 58.36  ? 380 ASP A C     1 
ATOM   2861 O O     . ASP A 1 380 ? 68.880  111.333 131.502 1.00 58.36  ? 380 ASP A O     1 
ATOM   2862 C CB    . ASP A 1 380 ? 70.048  111.907 128.437 1.00 75.03  ? 380 ASP A CB    1 
ATOM   2863 C CG    . ASP A 1 380 ? 71.142  112.690 127.740 1.00 75.03  ? 380 ASP A CG    1 
ATOM   2864 O OD1   . ASP A 1 380 ? 72.160  113.014 128.355 1.00 75.03  ? 380 ASP A OD1   1 
ATOM   2865 O OD2   . ASP A 1 380 ? 70.967  112.992 126.557 1.00 75.03  ? 380 ASP A OD2   1 
ATOM   2866 N N     . ARG A 1 381 ? 68.779  109.613 130.059 1.00 58.34  ? 381 ARG A N     1 
ATOM   2867 C CA    . ARG A 1 381 ? 67.602  109.082 130.722 1.00 58.34  ? 381 ARG A CA    1 
ATOM   2868 C C     . ARG A 1 381 ? 67.872  108.791 132.175 1.00 58.34  ? 381 ARG A C     1 
ATOM   2869 O O     . ARG A 1 381 ? 66.973  108.930 133.005 1.00 58.34  ? 381 ARG A O     1 
ATOM   2870 C CB    . ARG A 1 381 ? 67.100  107.825 130.037 1.00 85.72  ? 381 ARG A CB    1 
ATOM   2871 C CG    . ARG A 1 381 ? 66.406  108.094 128.716 1.00 85.72  ? 381 ARG A CG    1 
ATOM   2872 C CD    . ARG A 1 381 ? 65.633  106.893 128.230 1.00 85.72  ? 381 ARG A CD    1 
ATOM   2873 N NE    . ARG A 1 381 ? 66.500  105.774 127.871 1.00 85.72  ? 381 ARG A NE    1 
ATOM   2874 C CZ    . ARG A 1 381 ? 67.004  105.549 126.659 1.00 85.72  ? 381 ARG A CZ    1 
ATOM   2875 N NH1   . ARG A 1 381 ? 66.753  106.353 125.638 1.00 85.72  ? 381 ARG A NH1   1 
ATOM   2876 N NH2   . ARG A 1 381 ? 67.776  104.485 126.467 1.00 85.72  ? 381 ARG A NH2   1 
ATOM   2877 N N     . LEU A 1 382 ? 69.084  108.397 132.510 1.00 58.28  ? 382 LEU A N     1 
ATOM   2878 C CA    . LEU A 1 382 ? 69.444  108.109 133.884 1.00 58.28  ? 382 LEU A CA    1 
ATOM   2879 C C     . LEU A 1 382 ? 70.042  109.293 134.610 1.00 58.28  ? 382 LEU A C     1 
ATOM   2880 O O     . LEU A 1 382 ? 70.487  109.129 135.747 1.00 58.28  ? 382 LEU A O     1 
ATOM   2881 C CB    . LEU A 1 382 ? 70.462  106.982 133.944 1.00 86.28  ? 382 LEU A CB    1 
ATOM   2882 C CG    . LEU A 1 382 ? 70.096  105.604 133.401 1.00 86.28  ? 382 LEU A CG    1 
ATOM   2883 C CD1   . LEU A 1 382 ? 71.329  104.703 133.503 1.00 86.28  ? 382 LEU A CD1   1 
ATOM   2884 C CD2   . LEU A 1 382 ? 68.914  105.006 134.170 1.00 86.28  ? 382 LEU A CD2   1 
ATOM   2885 N N     . TRP A 1 383 ? 70.164  110.442 133.958 1.00 59.61  ? 383 TRP A N     1 
ATOM   2886 C CA    . TRP A 1 383 ? 70.849  111.560 134.593 1.00 59.61  ? 383 TRP A CA    1 
ATOM   2887 C C     . TRP A 1 383 ? 70.128  112.885 134.561 1.00 59.61  ? 383 TRP A C     1 
ATOM   2888 O O     . TRP A 1 383 ? 70.085  113.610 135.555 1.00 59.61  ? 383 TRP A O     1 
ATOM   2889 C CB    . TRP A 1 383 ? 72.183  111.749 133.945 1.00 82.54  ? 383 TRP A CB    1 
ATOM   2890 C CG    . TRP A 1 383 ? 72.933  112.816 134.536 1.00 82.54  ? 383 TRP A CG    1 
ATOM   2891 C CD1   . TRP A 1 383 ? 73.333  113.949 133.927 1.00 82.54  ? 383 TRP A CD1   1 
ATOM   2892 C CD2   . TRP A 1 383 ? 73.410  112.878 135.872 1.00 82.54  ? 383 TRP A CD2   1 
ATOM   2893 N NE1   . TRP A 1 383 ? 74.053  114.718 134.795 1.00 82.54  ? 383 TRP A NE1   1 
ATOM   2894 C CE2   . TRP A 1 383 ? 74.109  114.074 136.002 1.00 82.54  ? 383 TRP A CE2   1 
ATOM   2895 C CE3   . TRP A 1 383 ? 73.322  112.025 136.974 1.00 82.54  ? 383 TRP A CE3   1 
ATOM   2896 C CZ2   . TRP A 1 383 ? 74.708  114.444 137.182 1.00 82.54  ? 383 TRP A CZ2   1 
ATOM   2897 C CZ3   . TRP A 1 383 ? 73.911  112.395 138.146 1.00 82.54  ? 383 TRP A CZ3   1 
ATOM   2898 C CH2   . TRP A 1 383 ? 74.590  113.584 138.248 1.00 82.54  ? 383 TRP A CH2   1 
ATOM   2899 N N     . SER A 1 384 ? 69.676  113.265 133.377 1.00 61.05  ? 384 SER A N     1 
ATOM   2900 C CA    . SER A 1 384 ? 69.012  114.543 133.259 1.00 61.05  ? 384 SER A CA    1 
ATOM   2901 C C     . SER A 1 384 ? 67.609  114.392 133.761 1.00 61.05  ? 384 SER A C     1 
ATOM   2902 O O     . SER A 1 384 ? 67.024  115.338 134.293 1.00 61.05  ? 384 SER A O     1 
ATOM   2903 C CB    . SER A 1 384 ? 69.010  115.011 131.811 1.00 82.23  ? 384 SER A CB    1 
ATOM   2904 O OG    . SER A 1 384 ? 68.156  114.193 131.041 1.00 82.23  ? 384 SER A OG    1 
ATOM   2905 N N     . ARG A 1 385 ? 67.086  113.180 133.630 1.00 57.74  ? 385 ARG A N     1 
ATOM   2906 C CA    . ARG A 1 385 ? 65.757  112.905 134.141 1.00 57.74  ? 385 ARG A CA    1 
ATOM   2907 C C     . ARG A 1 385 ? 65.784  112.888 135.642 1.00 57.74  ? 385 ARG A C     1 
ATOM   2908 O O     . ARG A 1 385 ? 64.847  113.349 136.303 1.00 57.74  ? 385 ARG A O     1 
ATOM   2909 C CB    . ARG A 1 385 ? 65.253  111.561 133.643 1.00 84.84  ? 385 ARG A CB    1 
ATOM   2910 C CG    . ARG A 1 385 ? 63.830  111.251 134.069 1.00 84.84  ? 385 ARG A CG    1 
ATOM   2911 C CD    . ARG A 1 385 ? 63.347  109.971 133.471 1.00 84.84  ? 385 ARG A CD    1 
ATOM   2912 N NE    . ARG A 1 385 ? 62.004  109.645 133.930 1.00 84.84  ? 385 ARG A NE    1 
ATOM   2913 C CZ    . ARG A 1 385 ? 61.356  108.521 133.640 1.00 84.84  ? 385 ARG A CZ    1 
ATOM   2914 N NH1   . ARG A 1 385 ? 61.904  107.582 132.890 1.00 84.84  ? 385 ARG A NH1   1 
ATOM   2915 N NH2   . ARG A 1 385 ? 60.128  108.336 134.118 1.00 84.84  ? 385 ARG A NH2   1 
ATOM   2916 N N     . LYS A 1 386 ? 66.846  112.325 136.184 1.00 60.90  ? 386 LYS A N     1 
ATOM   2917 C CA    . LYS A 1 386 ? 66.996  112.168 137.606 1.00 60.90  ? 386 LYS A CA    1 
ATOM   2918 C C     . LYS A 1 386 ? 68.411  111.749 137.870 1.00 60.90  ? 386 LYS A C     1 
ATOM   2919 O O     . LYS A 1 386 ? 69.033  111.110 137.038 1.00 60.90  ? 386 LYS A O     1 
ATOM   2920 C CB    . LYS A 1 386 ? 66.046  111.113 138.146 1.00 91.35  ? 386 LYS A CB    1 
ATOM   2921 C CG    . LYS A 1 386 ? 66.267  109.736 137.555 1.00 91.35  ? 386 LYS A CG    1 
ATOM   2922 C CD    . LYS A 1 386 ? 65.231  108.754 138.077 1.00 91.35  ? 386 LYS A CD    1 
ATOM   2923 C CE    . LYS A 1 386 ? 65.389  107.382 137.444 1.00 91.35  ? 386 LYS A CE    1 
ATOM   2924 N NZ    . LYS A 1 386 ? 64.369  106.414 137.951 1.00 91.35  ? 386 LYS A NZ    1 
ATOM   2925 N N     . ALA A 1 387 ? 68.887  112.017 139.066 1.00 56.66  ? 387 ALA A N     1 
ATOM   2926 C CA    . ALA A 1 387 ? 70.218  111.553 139.404 1.00 56.66  ? 387 ALA A CA    1 
ATOM   2927 C C     . ALA A 1 387 ? 70.162  110.091 139.827 1.00 56.66  ? 387 ALA A C     1 
ATOM   2928 O O     . ALA A 1 387 ? 70.194  109.756 141.005 1.00 56.66  ? 387 ALA A O     1 
ATOM   2929 C CB    . ALA A 1 387 ? 70.811  112.412 140.501 1.00 77.26  ? 387 ALA A CB    1 
ATOM   2930 N N     . PHE A 1 388 ? 70.090  109.213 138.839 1.00 56.87  ? 388 PHE A N     1 
ATOM   2931 C CA    . PHE A 1 388 ? 69.983  107.784 139.082 1.00 56.87  ? 388 PHE A CA    1 
ATOM   2932 C C     . PHE A 1 388 ? 71.198  107.215 139.760 1.00 56.87  ? 388 PHE A C     1 
ATOM   2933 O O     . PHE A 1 388 ? 71.084  106.306 140.576 1.00 56.87  ? 388 PHE A O     1 
ATOM   2934 C CB    . PHE A 1 388 ? 69.813  107.056 137.770 1.00 79.35  ? 388 PHE A CB    1 
ATOM   2935 C CG    . PHE A 1 388 ? 69.766  105.585 137.899 1.00 79.35  ? 388 PHE A CG    1 
ATOM   2936 C CD1   . PHE A 1 388 ? 68.637  104.960 138.365 1.00 79.35  ? 388 PHE A CD1   1 
ATOM   2937 C CD2   . PHE A 1 388 ? 70.841  104.811 137.506 1.00 79.35  ? 388 PHE A CD2   1 
ATOM   2938 C CE1   . PHE A 1 388 ? 68.587  103.587 138.450 1.00 79.35  ? 388 PHE A CE1   1 
ATOM   2939 C CE2   . PHE A 1 388 ? 70.790  103.446 137.587 1.00 79.35  ? 388 PHE A CE2   1 
ATOM   2940 C CZ    . PHE A 1 388 ? 69.667  102.831 138.059 1.00 79.35  ? 388 PHE A CZ    1 
ATOM   2941 N N     . ALA A 1 389 ? 72.371  107.655 139.356 1.00 53.10  ? 389 ALA A N     1 
ATOM   2942 C CA    . ALA A 1 389 ? 73.589  107.043 139.840 1.00 53.10  ? 389 ALA A CA    1 
ATOM   2943 C C     . ALA A 1 389 ? 73.562  106.970 141.345 1.00 53.10  ? 389 ALA A C     1 
ATOM   2944 O O     . ALA A 1 389 ? 73.297  107.955 142.027 1.00 53.10  ? 389 ALA A O     1 
ATOM   2945 C CB    . ALA A 1 389 ? 74.810  107.834 139.387 1.00 72.41  ? 389 ALA A CB    1 
ATOM   2946 N N     . HIS A 1 390 ? 73.927  105.816 141.850 1.00 56.33  ? 390 HIS A N     1 
ATOM   2947 C CA    . HIS A 1 390 ? 73.794  105.489 143.253 1.00 56.33  ? 390 HIS A CA    1 
ATOM   2948 C C     . HIS A 1 390 ? 74.792  106.191 144.139 1.00 56.33  ? 390 HIS A C     1 
ATOM   2949 O O     . HIS A 1 390 ? 75.668  105.549 144.724 1.00 56.33  ? 390 HIS A O     1 
ATOM   2950 C CB    . HIS A 1 390 ? 73.957  103.986 143.411 1.00 76.61  ? 390 HIS A CB    1 
ATOM   2951 C CG    . HIS A 1 390 ? 73.008  103.186 142.574 1.00 76.61  ? 390 HIS A CG    1 
ATOM   2952 N ND1   . HIS A 1 390 ? 73.299  101.908 142.144 1.00 76.61  ? 390 HIS A ND1   1 
ATOM   2953 C CD2   . HIS A 1 390 ? 71.777  103.476 142.088 1.00 76.61  ? 390 HIS A CD2   1 
ATOM   2954 C CE1   . HIS A 1 390 ? 72.287  101.447 141.433 1.00 76.61  ? 390 HIS A CE1   1 
ATOM   2955 N NE2   . HIS A 1 390 ? 71.351  102.377 141.384 1.00 76.61  ? 390 HIS A NE2   1 
ATOM   2956 N N     . TRP A 1 391 ? 74.655  107.496 144.252 1.00 54.45  ? 391 TRP A N     1 
ATOM   2957 C CA    . TRP A 1 391 ? 75.467  108.276 145.150 1.00 54.45  ? 391 TRP A CA    1 
ATOM   2958 C C     . TRP A 1 391 ? 76.937  108.092 144.906 1.00 54.45  ? 391 TRP A C     1 
ATOM   2959 O O     . TRP A 1 391 ? 77.726  107.939 145.831 1.00 54.45  ? 391 TRP A O     1 
ATOM   2960 C CB    . TRP A 1 391 ? 75.167  107.909 146.575 1.00 75.39  ? 391 TRP A CB    1 
ATOM   2961 C CG    . TRP A 1 391 ? 73.831  108.103 146.849 1.00 75.39  ? 391 TRP A CG    1 
ATOM   2962 C CD1   . TRP A 1 391 ? 72.876  107.161 146.958 1.00 75.39  ? 391 TRP A CD1   1 
ATOM   2963 C CD2   . TRP A 1 391 ? 73.210  109.355 147.048 1.00 75.39  ? 391 TRP A CD2   1 
ATOM   2964 N NE1   . TRP A 1 391 ? 71.675  107.749 147.231 1.00 75.39  ? 391 TRP A NE1   1 
ATOM   2965 C CE2   . TRP A 1 391 ? 71.858  109.105 147.287 1.00 75.39  ? 391 TRP A CE2   1 
ATOM   2966 C CE3   . TRP A 1 391 ? 73.671  110.679 147.048 1.00 75.39  ? 391 TRP A CE3   1 
ATOM   2967 C CZ2   . TRP A 1 391 ? 70.953  110.124 147.527 1.00 75.39  ? 391 TRP A CZ2   1 
ATOM   2968 C CZ3   . TRP A 1 391 ? 72.774  111.694 147.284 1.00 75.39  ? 391 TRP A CZ3   1 
ATOM   2969 C CH2   . TRP A 1 391 ? 71.434  111.416 147.522 1.00 75.39  ? 391 TRP A CH2   1 
ATOM   2970 N N     . PHE A 1 392 ? 77.321  108.135 143.660 1.00 56.15  ? 392 PHE A N     1 
ATOM   2971 C CA    . PHE A 1 392 ? 78.718  107.951 143.359 1.00 56.15  ? 392 PHE A CA    1 
ATOM   2972 C C     . PHE A 1 392 ? 79.426  109.250 143.636 1.00 56.15  ? 392 PHE A C     1 
ATOM   2973 O O     . PHE A 1 392 ? 79.809  109.955 142.706 1.00 56.15  ? 392 PHE A O     1 
ATOM   2974 C CB    . PHE A 1 392 ? 78.928  107.620 141.905 1.00 78.35  ? 392 PHE A CB    1 
ATOM   2975 C CG    . PHE A 1 392 ? 78.307  106.370 141.472 1.00 78.35  ? 392 PHE A CG    1 
ATOM   2976 C CD1   . PHE A 1 392 ? 77.903  105.409 142.377 1.00 78.35  ? 392 PHE A CD1   1 
ATOM   2977 C CD2   . PHE A 1 392 ? 78.130  106.138 140.123 1.00 78.35  ? 392 PHE A CD2   1 
ATOM   2978 C CE1   . PHE A 1 392 ? 77.350  104.242 141.937 1.00 78.35  ? 392 PHE A CE1   1 
ATOM   2979 C CE2   . PHE A 1 392 ? 77.574  104.969 139.685 1.00 78.35  ? 392 PHE A CE2   1 
ATOM   2980 C CZ    . PHE A 1 392 ? 77.185  104.020 140.595 1.00 78.35  ? 392 PHE A CZ    1 
ATOM   2981 N N     . THR A 1 393 ? 79.579  109.561 144.920 1.00 56.85  ? 393 THR A N     1 
ATOM   2982 C CA    . THR A 1 393 ? 80.163  110.824 145.338 1.00 56.85  ? 393 THR A CA    1 
ATOM   2983 C C     . THR A 1 393 ? 81.369  110.711 146.269 1.00 56.85  ? 393 THR A C     1 
ATOM   2984 O O     . THR A 1 393 ? 82.160  111.651 146.339 1.00 56.85  ? 393 THR A O     1 
ATOM   2985 C CB    . THR A 1 393 ? 79.091  111.675 146.032 1.00 79.59  ? 393 THR A CB    1 
ATOM   2986 O OG1   . THR A 1 393 ? 78.657  111.012 147.227 1.00 79.59  ? 393 THR A OG1   1 
ATOM   2987 C CG2   . THR A 1 393 ? 77.890  111.845 145.112 1.00 79.59  ? 393 THR A CG2   1 
ATOM   2988 N N     . ASP A 1 394 ? 81.546  109.601 146.977 1.00 59.13  ? 394 ASP A N     1 
ATOM   2989 C CA    . ASP A 1 394 ? 82.597  109.554 147.998 1.00 59.13  ? 394 ASP A CA    1 
ATOM   2990 C C     . ASP A 1 394 ? 83.975  109.491 147.376 1.00 59.13  ? 394 ASP A C     1 
ATOM   2991 O O     . ASP A 1 394 ? 84.943  110.072 147.880 1.00 59.13  ? 394 ASP A O     1 
ATOM   2992 C CB    . ASP A 1 394 ? 82.425  108.334 148.895 1.00 76.02  ? 394 ASP A CB    1 
ATOM   2993 C CG    . ASP A 1 394 ? 81.223  108.418 149.786 1.00 76.02  ? 394 ASP A CG    1 
ATOM   2994 O OD1   . ASP A 1 394 ? 80.682  109.505 149.998 1.00 76.02  ? 394 ASP A OD1   1 
ATOM   2995 O OD2   . ASP A 1 394 ? 80.818  107.370 150.278 1.00 76.02  ? 394 ASP A OD2   1 
ATOM   2996 N N     . SER A 1 395 ? 84.074  108.723 146.324 1.00 60.15  ? 395 SER A N     1 
ATOM   2997 C CA    . SER A 1 395 ? 85.227  108.522 145.487 1.00 60.15  ? 395 SER A CA    1 
ATOM   2998 C C     . SER A 1 395 ? 84.667  108.589 144.112 1.00 60.15  ? 395 SER A C     1 
ATOM   2999 O O     . SER A 1 395 ? 84.903  107.734 143.256 1.00 60.15  ? 395 SER A O     1 
ATOM   3000 C CB    . SER A 1 395 ? 85.904  107.183 145.761 1.00 81.02  ? 395 SER A CB    1 
ATOM   3001 O OG    . SER A 1 395 ? 85.002  106.115 145.545 1.00 81.02  ? 395 SER A OG    1 
ATOM   3002 N N     . GLY A 1 396 ? 83.748  109.517 143.973 1.00 60.88  ? 396 GLY A N     1 
ATOM   3003 C CA    . GLY A 1 396 ? 82.944  109.573 142.803 1.00 60.88  ? 396 GLY A CA    1 
ATOM   3004 C C     . GLY A 1 396 ? 83.110  110.851 142.062 1.00 60.88  ? 396 GLY A C     1 
ATOM   3005 O O     . GLY A 1 396 ? 84.189  111.436 142.002 1.00 60.88  ? 396 GLY A O     1 
ATOM   3006 N N     . PHE A 1 397 ? 82.018  111.279 141.482 1.00 63.41  ? 397 PHE A N     1 
ATOM   3007 C CA    . PHE A 1 397 ? 82.038  112.400 140.580 1.00 63.41  ? 397 PHE A CA    1 
ATOM   3008 C C     . PHE A 1 397 ? 81.039  113.447 141.002 1.00 63.41  ? 397 PHE A C     1 
ATOM   3009 O O     . PHE A 1 397 ? 79.957  113.136 141.493 1.00 63.41  ? 397 PHE A O     1 
ATOM   3010 C CB    . PHE A 1 397 ? 81.707  111.964 139.156 1.00 88.48  ? 397 PHE A CB    1 
ATOM   3011 C CG    . PHE A 1 397 ? 82.684  111.014 138.583 1.00 88.48  ? 397 PHE A CG    1 
ATOM   3012 C CD1   . PHE A 1 397 ? 83.933  111.441 138.197 1.00 88.48  ? 397 PHE A CD1   1 
ATOM   3013 C CD2   . PHE A 1 397 ? 82.373  109.683 138.453 1.00 88.48  ? 397 PHE A CD2   1 
ATOM   3014 C CE1   . PHE A 1 397 ? 84.850  110.551 137.681 1.00 88.48  ? 397 PHE A CE1   1 
ATOM   3015 C CE2   . PHE A 1 397 ? 83.274  108.791 137.934 1.00 88.48  ? 397 PHE A CE2   1 
ATOM   3016 C CZ    . PHE A 1 397 ? 84.516  109.224 137.547 1.00 88.48  ? 397 PHE A CZ    1 
ATOM   3017 N N     . GLU A 1 398 ? 81.398  114.690 140.758 1.00 65.91  ? 398 GLU A N     1 
ATOM   3018 C CA    . GLU A 1 398 ? 80.442  115.741 140.970 1.00 65.91  ? 398 GLU A CA    1 
ATOM   3019 C C     . GLU A 1 398 ? 79.585  115.801 139.748 1.00 65.91  ? 398 GLU A C     1 
ATOM   3020 O O     . GLU A 1 398 ? 79.948  115.294 138.692 1.00 65.91  ? 398 GLU A O     1 
ATOM   3021 C CB    . GLU A 1 398 ? 81.128  117.074 141.244 1.00 88.54  ? 398 GLU A CB    1 
ATOM   3022 C CG    . GLU A 1 398 ? 81.917  117.088 142.554 1.00 88.54  ? 398 GLU A CG    1 
ATOM   3023 C CD    . GLU A 1 398 ? 82.467  118.451 142.896 1.00 88.54  ? 398 GLU A CD    1 
ATOM   3024 O OE1   . GLU A 1 398 ? 81.965  119.442 142.363 1.00 88.54  ? 398 GLU A OE1   1 
ATOM   3025 O OE2   . GLU A 1 398 ? 83.402  118.530 143.696 1.00 88.54  ? 398 GLU A OE2   1 
ATOM   3026 N N     . GLU A 1 399 ? 78.432  116.399 139.888 1.00 61.53  ? 399 GLU A N     1 
ATOM   3027 C CA    . GLU A 1 399 ? 77.583  116.476 138.734 1.00 61.53  ? 399 GLU A CA    1 
ATOM   3028 C C     . GLU A 1 399 ? 78.348  117.079 137.583 1.00 61.53  ? 399 GLU A C     1 
ATOM   3029 O O     . GLU A 1 399 ? 78.257  116.605 136.458 1.00 61.53  ? 399 GLU A O     1 
ATOM   3030 C CB    . GLU A 1 399 ? 76.360  117.310 139.061 1.00 82.65  ? 399 GLU A CB    1 
ATOM   3031 C CG    . GLU A 1 399 ? 75.481  116.722 140.143 1.00 82.65  ? 399 GLU A CG    1 
ATOM   3032 C CD    . GLU A 1 399 ? 75.984  117.006 141.525 1.00 82.65  ? 399 GLU A CD    1 
ATOM   3033 O OE1   . GLU A 1 399 ? 76.998  117.694 141.652 1.00 82.65  ? 399 GLU A OE1   1 
ATOM   3034 O OE2   . GLU A 1 399 ? 75.374  116.532 142.481 1.00 82.65  ? 399 GLU A OE2   1 
ATOM   3035 N N     . LYS A 1 400 ? 79.183  118.063 137.864 1.00 62.95  ? 400 LYS A N     1 
ATOM   3036 C CA    . LYS A 1 400 ? 79.903  118.720 136.798 1.00 62.95  ? 400 LYS A CA    1 
ATOM   3037 C C     . LYS A 1 400 ? 80.814  117.776 136.046 1.00 62.95  ? 400 LYS A C     1 
ATOM   3038 O O     . LYS A 1 400 ? 81.130  118.032 134.887 1.00 62.95  ? 400 LYS A O     1 
ATOM   3039 C CB    . LYS A 1 400 ? 80.754  119.860 137.355 1.00 94.42  ? 400 LYS A CB    1 
ATOM   3040 C CG    . LYS A 1 400 ? 81.995  119.392 138.137 1.00 94.42  ? 400 LYS A CG    1 
ATOM   3041 C CD    . LYS A 1 400 ? 82.827  120.546 138.687 1.00 94.42  ? 400 LYS A CD    1 
ATOM   3042 C CE    . LYS A 1 400 ? 84.015  120.051 139.558 1.00 94.42  ? 400 LYS A CE    1 
ATOM   3043 N NZ    . LYS A 1 400 ? 85.104  119.324 138.793 1.00 94.42  ? 400 LYS A NZ    1 
ATOM   3044 N N     . ASP A 1 401 ? 81.255  116.700 136.676 1.00 64.94  ? 401 ASP A N     1 
ATOM   3045 C CA    . ASP A 1 401 ? 82.192  115.817 136.026 1.00 64.94  ? 401 ASP A CA    1 
ATOM   3046 C C     . ASP A 1 401 ? 81.446  114.890 135.143 1.00 64.94  ? 401 ASP A C     1 
ATOM   3047 O O     . ASP A 1 401 ? 81.931  114.467 134.087 1.00 64.94  ? 401 ASP A O     1 
ATOM   3048 C CB    . ASP A 1 401 ? 82.960  115.033 137.064 1.00 83.49  ? 401 ASP A CB    1 
ATOM   3049 C CG    . ASP A 1 401 ? 83.784  115.928 137.972 1.00 83.49  ? 401 ASP A CG    1 
ATOM   3050 O OD1   . ASP A 1 401 ? 84.489  116.828 137.483 1.00 83.49  ? 401 ASP A OD1   1 
ATOM   3051 O OD2   . ASP A 1 401 ? 83.716  115.736 139.192 1.00 83.49  ? 401 ASP A OD2   1 
ATOM   3052 N N     . LEU A 1 402 ? 80.260  114.587 135.564 1.00 60.46  ? 402 LEU A N     1 
ATOM   3053 C CA    . LEU A 1 402 ? 79.438  113.747 134.760 1.00 60.46  ? 402 LEU A CA    1 
ATOM   3054 C C     . LEU A 1 402 ? 78.957  114.552 133.579 1.00 60.46  ? 402 LEU A C     1 
ATOM   3055 O O     . LEU A 1 402 ? 78.858  114.043 132.452 1.00 60.46  ? 402 LEU A O     1 
ATOM   3056 C CB    . LEU A 1 402 ? 78.315  113.202 135.635 1.00 89.51  ? 402 LEU A CB    1 
ATOM   3057 C CG    . LEU A 1 402 ? 78.780  112.342 136.832 1.00 89.51  ? 402 LEU A CG    1 
ATOM   3058 C CD1   . LEU A 1 402 ? 77.607  112.023 137.712 1.00 89.51  ? 402 LEU A CD1   1 
ATOM   3059 C CD2   . LEU A 1 402 ? 79.445  111.059 136.359 1.00 89.51  ? 402 LEU A CD2   1 
ATOM   3060 N N     . ASP A 1 403 ? 78.749  115.835 133.813 1.00 64.05  ? 403 ASP A N     1 
ATOM   3061 C CA    . ASP A 1 403 ? 78.311  116.717 132.756 1.00 64.05  ? 403 ASP A CA    1 
ATOM   3062 C C     . ASP A 1 403 ? 79.455  116.989 131.814 1.00 64.05  ? 403 ASP A C     1 
ATOM   3063 O O     . ASP A 1 403 ? 79.243  117.123 130.612 1.00 64.05  ? 403 ASP A O     1 
ATOM   3064 C CB    . ASP A 1 403 ? 77.775  118.029 133.324 1.00 82.35  ? 403 ASP A CB    1 
ATOM   3065 C CG    . ASP A 1 403 ? 76.439  117.874 134.072 1.00 82.35  ? 403 ASP A CG    1 
ATOM   3066 O OD1   . ASP A 1 403 ? 75.711  116.889 133.874 1.00 82.35  ? 403 ASP A OD1   1 
ATOM   3067 O OD2   . ASP A 1 403 ? 76.125  118.767 134.864 1.00 82.35  ? 403 ASP A OD2   1 
ATOM   3068 N N     . ASP A 1 404 ? 80.674  117.043 132.334 1.00 62.02  ? 404 ASP A N     1 
ATOM   3069 C CA    . ASP A 1 404 ? 81.822  117.235 131.473 1.00 62.02  ? 404 ASP A CA    1 
ATOM   3070 C C     . ASP A 1 404 ? 81.916  116.094 130.512 1.00 62.02  ? 404 ASP A C     1 
ATOM   3071 O O     . ASP A 1 404 ? 82.103  116.298 129.311 1.00 62.02  ? 404 ASP A O     1 
ATOM   3072 C CB    . ASP A 1 404 ? 83.097  117.325 132.318 1.00 79.74  ? 404 ASP A CB    1 
ATOM   3073 C CG    . ASP A 1 404 ? 84.399  117.561 131.495 1.00 79.74  ? 404 ASP A CG    1 
ATOM   3074 O OD1   . ASP A 1 404 ? 84.594  118.656 130.955 1.00 79.74  ? 404 ASP A OD1   1 
ATOM   3075 O OD2   . ASP A 1 404 ? 85.240  116.641 131.431 1.00 79.74  ? 404 ASP A OD2   1 
ATOM   3076 N N     . ALA A 1 405 ? 81.782  114.875 131.018 1.00 57.12  ? 405 ALA A N     1 
ATOM   3077 C CA    . ALA A 1 405 ? 81.878  113.758 130.107 1.00 57.12  ? 405 ALA A CA    1 
ATOM   3078 C C     . ALA A 1 405 ? 80.810  113.856 129.055 1.00 57.12  ? 405 ALA A C     1 
ATOM   3079 O O     . ALA A 1 405 ? 81.069  113.621 127.870 1.00 57.12  ? 405 ALA A O     1 
ATOM   3080 C CB    . ALA A 1 405 ? 81.748  112.448 130.854 1.00 77.89  ? 405 ALA A CB    1 
ATOM   3081 N N     . ARG A 1 406 ? 79.607  114.210 129.461 1.00 57.36  ? 406 ARG A N     1 
ATOM   3082 C CA    . ARG A 1 406 ? 78.558  114.252 128.476 1.00 57.36  ? 406 ARG A CA    1 
ATOM   3083 C C     . ARG A 1 406 ? 78.865  115.299 127.458 1.00 57.36  ? 406 ARG A C     1 
ATOM   3084 O O     . ARG A 1 406 ? 78.617  115.108 126.271 1.00 57.36  ? 406 ARG A O     1 
ATOM   3085 C CB    . ARG A 1 406 ? 77.239  114.527 129.141 1.00 84.28  ? 406 ARG A CB    1 
ATOM   3086 C CG    . ARG A 1 406 ? 76.041  114.621 128.216 1.00 84.28  ? 406 ARG A CG    1 
ATOM   3087 C CD    . ARG A 1 406 ? 75.725  113.318 127.544 1.00 84.28  ? 406 ARG A CD    1 
ATOM   3088 N NE    . ARG A 1 406 ? 74.500  113.410 126.759 1.00 84.28  ? 406 ARG A NE    1 
ATOM   3089 C CZ    . ARG A 1 406 ? 74.428  113.791 125.491 1.00 84.28  ? 406 ARG A CZ    1 
ATOM   3090 N NH1   . ARG A 1 406 ? 75.507  114.110 124.806 1.00 84.28  ? 406 ARG A NH1   1 
ATOM   3091 N NH2   . ARG A 1 406 ? 73.240  113.862 124.900 1.00 84.28  ? 406 ARG A NH2   1 
ATOM   3092 N N     . ALA A 1 407 ? 79.418  116.410 127.911 1.00 57.93  ? 407 ALA A N     1 
ATOM   3093 C CA    . ALA A 1 407 ? 79.725  117.504 127.021 1.00 57.93  ? 407 ALA A CA    1 
ATOM   3094 C C     . ALA A 1 407 ? 80.777  117.103 126.027 1.00 57.93  ? 407 ALA A C     1 
ATOM   3095 O O     . ALA A 1 407 ? 80.684  117.451 124.845 1.00 57.93  ? 407 ALA A O     1 
ATOM   3096 C CB    . ALA A 1 407 ? 80.191  118.707 127.822 1.00 79.00  ? 407 ALA A CB    1 
ATOM   3097 N N     . LEU A 1 408 ? 81.780  116.366 126.475 1.00 57.09  ? 408 LEU A N     1 
ATOM   3098 C CA    . LEU A 1 408 ? 82.819  115.988 125.543 1.00 57.09  ? 408 LEU A CA    1 
ATOM   3099 C C     . LEU A 1 408 ? 82.264  115.054 124.516 1.00 57.09  ? 408 LEU A C     1 
ATOM   3100 O O     . LEU A 1 408 ? 82.592  115.135 123.325 1.00 57.09  ? 408 LEU A O     1 
ATOM   3101 C CB    . LEU A 1 408 ? 83.976  115.349 126.250 1.00 84.52  ? 408 LEU A CB    1 
ATOM   3102 C CG    . LEU A 1 408 ? 85.149  114.954 125.353 1.00 84.52  ? 408 LEU A CG    1 
ATOM   3103 C CD1   . LEU A 1 408 ? 85.707  116.147 124.587 1.00 84.52  ? 408 LEU A CD1   1 
ATOM   3104 C CD2   . LEU A 1 408 ? 86.230  114.354 126.206 1.00 84.52  ? 408 LEU A CD2   1 
ATOM   3105 N N     . VAL A 1 409 ? 81.416  114.166 124.956 1.00 57.87  ? 409 VAL A N     1 
ATOM   3106 C CA    . VAL A 1 409 ? 80.824  113.249 124.021 1.00 57.87  ? 409 VAL A CA    1 
ATOM   3107 C C     . VAL A 1 409 ? 79.942  113.996 123.051 1.00 57.87  ? 409 VAL A C     1 
ATOM   3108 O O     . VAL A 1 409 ? 79.928  113.690 121.855 1.00 57.87  ? 409 VAL A O     1 
ATOM   3109 C CB    . VAL A 1 409 ? 80.090  112.140 124.778 1.00 84.17  ? 409 VAL A CB    1 
ATOM   3110 C CG1   . VAL A 1 409 ? 79.303  111.255 123.807 1.00 84.17  ? 409 VAL A CG1   1 
ATOM   3111 C CG2   . VAL A 1 409 ? 81.130  111.334 125.551 1.00 84.17  ? 409 VAL A CG2   1 
ATOM   3112 N N     . GLN A 1 410 ? 79.195  114.982 123.514 1.00 60.38  ? 410 GLN A N     1 
ATOM   3113 C CA    . GLN A 1 410 ? 78.369  115.671 122.552 1.00 60.38  ? 410 GLN A CA    1 
ATOM   3114 C C     . GLN A 1 410 ? 79.239  116.374 121.551 1.00 60.38  ? 410 GLN A C     1 
ATOM   3115 O O     . GLN A 1 410 ? 78.922  116.397 120.367 1.00 60.38  ? 410 GLN A O     1 
ATOM   3116 C CB    . GLN A 1 410 ? 77.427  116.656 123.197 1.00 84.37  ? 410 GLN A CB    1 
ATOM   3117 C CG    . GLN A 1 410 ? 76.436  117.217 122.200 1.00 84.37  ? 410 GLN A CG    1 
ATOM   3118 C CD    . GLN A 1 410 ? 75.534  116.159 121.586 1.00 84.37  ? 410 GLN A CD    1 
ATOM   3119 O OE1   . GLN A 1 410 ? 75.073  115.248 122.260 1.00 84.37  ? 410 GLN A OE1   1 
ATOM   3120 N NE2   . GLN A 1 410 ? 75.272  116.286 120.293 1.00 84.37  ? 410 GLN A NE2   1 
ATOM   3121 N N     . LYS A 1 411 ? 80.359  116.907 121.989 1.00 63.15  ? 411 LYS A N     1 
ATOM   3122 C CA    . LYS A 1 411 ? 81.219  117.560 121.030 1.00 63.15  ? 411 LYS A CA    1 
ATOM   3123 C C     . LYS A 1 411 ? 81.674  116.599 119.958 1.00 63.15  ? 411 LYS A C     1 
ATOM   3124 O O     . LYS A 1 411 ? 81.640  116.942 118.784 1.00 63.15  ? 411 LYS A O     1 
ATOM   3125 C CB    . LYS A 1 411 ? 82.427  118.162 121.726 1.00 94.72  ? 411 LYS A CB    1 
ATOM   3126 C CG    . LYS A 1 411 ? 83.405  118.912 120.820 1.00 94.72  ? 411 LYS A CG    1 
ATOM   3127 C CD    . LYS A 1 411 ? 82.796  120.187 120.251 1.00 94.72  ? 411 LYS A CD    1 
ATOM   3128 C CE    . LYS A 1 411 ? 83.864  121.148 119.690 1.00 94.72  ? 411 LYS A CE    1 
ATOM   3129 N NZ    . LYS A 1 411 ? 84.480  120.688 118.400 1.00 94.72  ? 411 LYS A NZ    1 
ATOM   3130 N N     . VAL A 1 412 ? 82.081  115.384 120.324 1.00 62.51  ? 412 VAL A N     1 
ATOM   3131 C CA    . VAL A 1 412 ? 82.573  114.515 119.268 1.00 62.51  ? 412 VAL A CA    1 
ATOM   3132 C C     . VAL A 1 412 ? 81.452  114.179 118.314 1.00 62.51  ? 412 VAL A C     1 
ATOM   3133 O O     . VAL A 1 412 ? 81.661  114.104 117.092 1.00 62.51  ? 412 VAL A O     1 
ATOM   3134 C CB    . VAL A 1 412 ? 83.266  113.242 119.783 1.00 90.92  ? 412 VAL A CB    1 
ATOM   3135 C CG1   . VAL A 1 412 ? 82.300  112.198 120.326 1.00 90.92  ? 412 VAL A CG1   1 
ATOM   3136 C CG2   . VAL A 1 412 ? 84.032  112.646 118.661 1.00 90.92  ? 412 VAL A CG2   1 
ATOM   3137 N N     . ILE A 1 413 ? 80.245  114.011 118.837 1.00 63.20  ? 413 ILE A N     1 
ATOM   3138 C CA    . ILE A 1 413 ? 79.117  113.715 117.969 1.00 63.20  ? 413 ILE A CA    1 
ATOM   3139 C C     . ILE A 1 413 ? 78.878  114.869 117.004 1.00 63.20  ? 413 ILE A C     1 
ATOM   3140 O O     . ILE A 1 413 ? 78.696  114.675 115.788 1.00 63.20  ? 413 ILE A O     1 
ATOM   3141 C CB    . ILE A 1 413 ? 77.863  113.422 118.802 1.00 93.57  ? 413 ILE A CB    1 
ATOM   3142 C CG1   . ILE A 1 413 ? 78.062  112.123 119.589 1.00 93.57  ? 413 ILE A CG1   1 
ATOM   3143 C CG2   . ILE A 1 413 ? 76.631  113.345 117.882 1.00 93.57  ? 413 ILE A CG2   1 
ATOM   3144 C CD1   . ILE A 1 413 ? 77.033  111.871 120.678 1.00 93.57  ? 413 ILE A CD1   1 
ATOM   3145 N N     . ASP A 1 414 ? 78.896  116.094 117.535 1.00 66.41  ? 414 ASP A N     1 
ATOM   3146 C CA    . ASP A 1 414 ? 78.667  117.281 116.721 1.00 66.41  ? 414 ASP A CA    1 
ATOM   3147 C C     . ASP A 1 414 ? 79.741  117.436 115.653 1.00 66.41  ? 414 ASP A C     1 
ATOM   3148 O O     . ASP A 1 414 ? 79.440  117.828 114.527 1.00 66.41  ? 414 ASP A O     1 
ATOM   3149 C CB    . ASP A 1 414 ? 78.646  118.547 117.587 1.00 85.38  ? 414 ASP A CB    1 
ATOM   3150 C CG    . ASP A 1 414 ? 77.395  118.696 118.465 1.00 85.38  ? 414 ASP A CG    1 
ATOM   3151 O OD1   . ASP A 1 414 ? 76.383  118.023 118.254 1.00 85.38  ? 414 ASP A OD1   1 
ATOM   3152 O OD2   . ASP A 1 414 ? 77.440  119.532 119.373 1.00 85.38  ? 414 ASP A OD2   1 
ATOM   3153 N N     . ASP A 1 415 ? 80.999  117.151 115.988 1.00 66.11  ? 415 ASP A N     1 
ATOM   3154 C CA    . ASP A 1 415 ? 82.056  117.322 115.004 1.00 66.11  ? 415 ASP A CA    1 
ATOM   3155 C C     . ASP A 1 415 ? 81.904  116.351 113.859 1.00 66.11  ? 415 ASP A C     1 
ATOM   3156 O O     . ASP A 1 415 ? 82.123  116.726 112.709 1.00 66.11  ? 415 ASP A O     1 
ATOM   3157 C CB    . ASP A 1 415 ? 83.432  117.174 115.650 1.00 85.00  ? 415 ASP A CB    1 
ATOM   3158 C CG    . ASP A 1 415 ? 83.837  118.385 116.494 1.00 85.00  ? 415 ASP A CG    1 
ATOM   3159 O OD1   . ASP A 1 415 ? 83.217  119.448 116.387 1.00 85.00  ? 415 ASP A OD1   1 
ATOM   3160 O OD2   . ASP A 1 415 ? 84.797  118.279 117.272 1.00 85.00  ? 415 ASP A OD2   1 
ATOM   3161 N N     . TYR A 1 416 ? 81.543  115.100 114.127 1.00 66.87  ? 416 TYR A N     1 
ATOM   3162 C CA    . TYR A 1 416 ? 81.341  114.232 112.975 1.00 66.87  ? 416 TYR A CA    1 
ATOM   3163 C C     . TYR A 1 416 ? 80.196  114.738 112.156 1.00 66.87  ? 416 TYR A C     1 
ATOM   3164 O O     . TYR A 1 416 ? 80.265  114.747 110.924 1.00 66.87  ? 416 TYR A O     1 
ATOM   3165 C CB    . TYR A 1 416 ? 81.057  112.792 113.338 1.00 92.59  ? 416 TYR A CB    1 
ATOM   3166 C CG    . TYR A 1 416 ? 82.239  111.911 113.519 1.00 92.59  ? 416 TYR A CG    1 
ATOM   3167 C CD1   . TYR A 1 416 ? 82.992  111.548 112.455 1.00 92.59  ? 416 TYR A CD1   1 
ATOM   3168 C CD2   . TYR A 1 416 ? 82.563  111.422 114.769 1.00 92.59  ? 416 TYR A CD2   1 
ATOM   3169 C CE1   . TYR A 1 416 ? 84.049  110.744 112.602 1.00 92.59  ? 416 TYR A CE1   1 
ATOM   3170 C CE2   . TYR A 1 416 ? 83.635  110.602 114.930 1.00 92.59  ? 416 TYR A CE2   1 
ATOM   3171 C CZ    . TYR A 1 416 ? 84.380  110.266 113.830 1.00 92.59  ? 416 TYR A CZ    1 
ATOM   3172 O OH    . TYR A 1 416 ? 85.463  109.435 113.980 1.00 92.59  ? 416 TYR A OH    1 
ATOM   3173 N N     . ARG A 1 417 ? 79.149  115.200 112.821 1.00 69.19  ? 417 ARG A N     1 
ATOM   3174 C CA    . ARG A 1 417 ? 78.011  115.687 112.070 1.00 69.19  ? 417 ARG A CA    1 
ATOM   3175 C C     . ARG A 1 417 ? 78.360  116.915 111.234 1.00 69.19  ? 417 ARG A C     1 
ATOM   3176 O O     . ARG A 1 417 ? 77.881  117.047 110.106 1.00 69.19  ? 417 ARG A O     1 
ATOM   3177 C CB    . ARG A 1 417 ? 76.856  115.948 113.014 1.00 101.67 ? 417 ARG A CB    1 
ATOM   3178 C CG    . ARG A 1 417 ? 76.189  114.677 113.426 1.00 101.67 ? 417 ARG A CG    1 
ATOM   3179 C CD    . ARG A 1 417 ? 75.013  114.912 114.296 1.00 101.67 ? 417 ARG A CD    1 
ATOM   3180 N NE    . ARG A 1 417 ? 74.271  113.680 114.509 1.00 101.67 ? 417 ARG A NE    1 
ATOM   3181 C CZ    . ARG A 1 417 ? 73.347  113.212 113.686 1.00 101.67 ? 417 ARG A CZ    1 
ATOM   3182 N NH1   . ARG A 1 417 ? 73.018  113.850 112.581 1.00 101.67 ? 417 ARG A NH1   1 
ATOM   3183 N NH2   . ARG A 1 417 ? 72.745  112.071 113.977 1.00 101.67 ? 417 ARG A NH2   1 
ATOM   3184 N N     . LYS A 1 418 ? 79.211  117.803 111.753 1.00 70.33  ? 418 LYS A N     1 
ATOM   3185 C CA    . LYS A 1 418 ? 79.597  118.998 111.006 1.00 70.33  ? 418 LYS A CA    1 
ATOM   3186 C C     . LYS A 1 418 ? 80.508  118.668 109.840 1.00 70.33  ? 418 LYS A C     1 
ATOM   3187 O O     . LYS A 1 418 ? 80.398  119.282 108.781 1.00 70.33  ? 418 LYS A O     1 
ATOM   3188 C CB    . LYS A 1 418 ? 80.277  120.027 111.911 1.00 105.49 ? 418 LYS A CB    1 
ATOM   3189 C CG    . LYS A 1 418 ? 80.704  121.317 111.196 1.00 105.49 ? 418 LYS A CG    1 
ATOM   3190 C CD    . LYS A 1 418 ? 79.508  122.045 110.599 1.00 105.49 ? 418 LYS A CD    1 
ATOM   3191 C CE    . LYS A 1 418 ? 79.865  123.368 109.941 1.00 105.49 ? 418 LYS A CE    1 
ATOM   3192 N NZ    . LYS A 1 418 ? 78.677  123.961 109.228 1.00 105.49 ? 418 LYS A NZ    1 
ATOM   3193 N N     . LEU A 1 419 ? 81.439  117.740 109.999 1.00 68.95  ? 419 LEU A N     1 
ATOM   3194 C CA    . LEU A 1 419 ? 82.276  117.457 108.850 1.00 68.95  ? 419 LEU A CA    1 
ATOM   3195 C C     . LEU A 1 419 ? 81.464  116.876 107.714 1.00 68.95  ? 419 LEU A C     1 
ATOM   3196 O O     . LEU A 1 419 ? 81.731  117.173 106.550 1.00 68.95  ? 419 LEU A O     1 
ATOM   3197 C CB    . LEU A 1 419 ? 83.403  116.504 109.185 1.00 102.08 ? 419 LEU A CB    1 
ATOM   3198 C CG    . LEU A 1 419 ? 84.538  117.000 110.061 1.00 102.08 ? 419 LEU A CG    1 
ATOM   3199 C CD1   . LEU A 1 419 ? 85.420  115.845 110.309 1.00 102.08 ? 419 LEU A CD1   1 
ATOM   3200 C CD2   . LEU A 1 419 ? 85.332  118.090 109.406 1.00 102.08 ? 419 LEU A CD2   1 
ATOM   3201 N N     . THR A 1 420 ? 80.502  116.020 107.999 1.00 72.66  ? 420 THR A N     1 
ATOM   3202 C CA    . THR A 1 420 ? 79.752  115.396 106.920 1.00 72.66  ? 420 THR A CA    1 
ATOM   3203 C C     . THR A 1 420 ? 78.336  115.927 106.799 1.00 72.66  ? 420 THR A C     1 
ATOM   3204 O O     . THR A 1 420 ? 77.378  115.217 107.108 1.00 72.66  ? 420 THR A O     1 
ATOM   3205 C CB    . THR A 1 420 ? 79.684  113.923 107.086 1.00 101.72 ? 420 THR A CB    1 
ATOM   3206 O OG1   . THR A 1 420 ? 79.026  113.603 108.314 1.00 101.72 ? 420 THR A OG1   1 
ATOM   3207 C CG2   . THR A 1 420 ? 81.039  113.393 107.111 1.00 101.72 ? 420 THR A CG2   1 
ATOM   3208 N N     . GLU A 1 421 ? 78.199  117.146 106.288 1.00 75.68  ? 421 GLU A N     1 
ATOM   3209 C CA    . GLU A 1 421 ? 76.896  117.732 105.997 1.00 75.68  ? 421 GLU A CA    1 
ATOM   3210 C C     . GLU A 1 421 ? 76.554  117.549 104.541 1.00 75.68  ? 421 GLU A C     1 
ATOM   3211 O O     . GLU A 1 421 ? 75.563  118.102 104.057 1.00 75.68  ? 421 GLU A O     1 
ATOM   3212 C CB    . GLU A 1 421 ? 76.861  119.224 106.347 1.00 101.66 ? 421 GLU A CB    1 
ATOM   3213 C CG    . GLU A 1 421 ? 76.968  119.536 107.830 1.00 101.66 ? 421 GLU A CG    1 
ATOM   3214 C CD    . GLU A 1 421 ? 76.904  121.030 108.151 1.00 101.66 ? 421 GLU A CD    1 
ATOM   3215 O OE1   . GLU A 1 421 ? 77.573  121.831 107.485 1.00 101.66 ? 421 GLU A OE1   1 
ATOM   3216 O OE2   . GLU A 1 421 ? 76.184  121.400 109.084 1.00 101.66 ? 421 GLU A OE2   1 
ATOM   3217 N N     . ASP A 1 422 ? 77.411  116.831 103.834 1.00 79.77  ? 422 ASP A N     1 
ATOM   3218 C CA    . ASP A 1 422 ? 77.270  116.525 102.418 1.00 79.77  ? 422 ASP A CA    1 
ATOM   3219 C C     . ASP A 1 422 ? 77.062  117.756 101.531 1.00 79.77  ? 422 ASP A C     1 
ATOM   3220 O O     . ASP A 1 422 ? 76.203  117.771 100.650 1.00 79.77  ? 422 ASP A O     1 
ATOM   3221 C CB    . ASP A 1 422 ? 76.168  115.499 102.251 1.00 102.56 ? 422 ASP A CB    1 
ATOM   3222 C CG    . ASP A 1 422 ? 76.521  114.226 102.973 1.00 102.56 ? 422 ASP A CG    1 
ATOM   3223 O OD1   . ASP A 1 422 ? 77.725  114.008 103.192 1.00 102.56 ? 422 ASP A OD1   1 
ATOM   3224 O OD2   . ASP A 1 422 ? 75.629  113.451 103.315 1.00 102.56 ? 422 ASP A OD2   1 
ATOM   3225 N N     . ALA A 1 423 ? 77.896  118.774 101.758 1.00 79.09  ? 423 ALA A N     1 
ATOM   3226 C CA    . ALA A 1 423 ? 77.920  120.036 101.039 1.00 79.09  ? 423 ALA A CA    1 
ATOM   3227 C C     . ALA A 1 423 ? 79.372  120.514 100.987 1.00 79.09  ? 423 ALA A C     1 
ATOM   3228 O O     . ALA A 1 423 ? 80.174  120.189 101.864 1.00 79.09  ? 423 ALA A O     1 
ATOM   3229 C CB    . ALA A 1 423 ? 77.000  121.072 101.710 1.00 102.60 ? 423 ALA A CB    1 
ATOM   3230 O OXT   . ALA A 1 423 ? 79.794  121.128 100.004 1.00 110.30 ? 423 ALA A OXT   1 
ATOM   3231 N N     . GLY B 2 2   ? 140.276 116.031 92.887  1.00 30.00  ? 2   GLY B N     1 
ATOM   3232 C CA    . GLY B 2 2   ? 139.661 114.882 93.528  1.00 30.00  ? 2   GLY B CA    1 
ATOM   3233 C C     . GLY B 2 2   ? 138.499 114.305 92.726  1.00 30.00  ? 2   GLY B C     1 
ATOM   3234 O O     . GLY B 2 2   ? 138.498 113.118 92.419  1.00 30.00  ? 2   GLY B O     1 
ATOM   3235 N N     . ARG B 2 3   ? 137.538 115.171 92.390  1.00 61.92  ? 3   ARG B N     1 
ATOM   3236 C CA    . ARG B 2 3   ? 136.314 114.845 91.650  1.00 61.92  ? 3   ARG B CA    1 
ATOM   3237 C C     . ARG B 2 3   ? 135.452 113.866 92.407  1.00 61.92  ? 3   ARG B C     1 
ATOM   3238 O O     . ARG B 2 3   ? 134.805 113.010 91.814  1.00 61.92  ? 3   ARG B O     1 
ATOM   3239 C CB    . ARG B 2 3   ? 136.611 114.251 90.277  1.00 90.98  ? 3   ARG B CB    1 
ATOM   3240 C CG    . ARG B 2 3   ? 137.546 115.034 89.432  1.00 90.98  ? 3   ARG B CG    1 
ATOM   3241 C CD    . ARG B 2 3   ? 137.822 114.357 88.130  1.00 90.98  ? 3   ARG B CD    1 
ATOM   3242 N NE    . ARG B 2 3   ? 138.221 112.962 88.308  1.00 90.98  ? 3   ARG B NE    1 
ATOM   3243 C CZ    . ARG B 2 3   ? 139.411 112.524 88.713  1.00 90.98  ? 3   ARG B CZ    1 
ATOM   3244 N NH1   . ARG B 2 3   ? 140.375 113.353 89.067  1.00 90.98  ? 3   ARG B NH1   1 
ATOM   3245 N NH2   . ARG B 2 3   ? 139.631 111.213 88.773  1.00 90.98  ? 3   ARG B NH2   1 
ATOM   3246 N N     . GLU B 2 4   ? 135.454 113.956 93.708  1.00 60.93  ? 4   GLU B N     1 
ATOM   3247 C CA    . GLU B 2 4   ? 134.757 112.959 94.474  1.00 60.93  ? 4   GLU B CA    1 
ATOM   3248 C C     . GLU B 2 4   ? 133.300 113.321 94.704  1.00 60.93  ? 4   GLU B C     1 
ATOM   3249 O O     . GLU B 2 4   ? 132.945 114.489 94.887  1.00 60.93  ? 4   GLU B O     1 
ATOM   3250 C CB    . GLU B 2 4   ? 135.488 112.741 95.783  1.00 81.85  ? 4   GLU B CB    1 
ATOM   3251 C CG    . GLU B 2 4   ? 136.941 112.329 95.552  1.00 81.85  ? 4   GLU B CG    1 
ATOM   3252 C CD    . GLU B 2 4   ? 137.624 111.793 96.775  1.00 81.85  ? 4   GLU B CD    1 
ATOM   3253 O OE1   . GLU B 2 4   ? 136.914 111.401 97.690  1.00 81.85  ? 4   GLU B OE1   1 
ATOM   3254 O OE2   . GLU B 2 4   ? 138.863 111.776 96.835  1.00 81.85  ? 4   GLU B OE2   1 
ATOM   3255 N N     . VAL B 2 5   ? 132.446 112.315 94.699  1.00 56.64  ? 5   VAL B N     1 
ATOM   3256 C CA    . VAL B 2 5   ? 131.033 112.516 94.952  1.00 56.64  ? 5   VAL B CA    1 
ATOM   3257 C C     . VAL B 2 5   ? 130.577 111.639 96.106  1.00 56.64  ? 5   VAL B C     1 
ATOM   3258 O O     . VAL B 2 5   ? 130.862 110.438 96.126  1.00 56.64  ? 5   VAL B O     1 
ATOM   3259 C CB    . VAL B 2 5   ? 130.220 112.232 93.689  1.00 82.38  ? 5   VAL B CB    1 
ATOM   3260 C CG1   . VAL B 2 5   ? 128.765 112.373 93.978  1.00 82.38  ? 5   VAL B CG1   1 
ATOM   3261 C CG2   . VAL B 2 5   ? 130.628 113.224 92.627  1.00 82.38  ? 5   VAL B CG2   1 
ATOM   3262 N N     . ILE B 2 6   ? 129.874 112.216 97.073  1.00 54.34  ? 6   ILE B N     1 
ATOM   3263 C CA    . ILE B 2 6   ? 129.381 111.435 98.198  1.00 54.34  ? 6   ILE B CA    1 
ATOM   3264 C C     . ILE B 2 6   ? 127.902 111.289 98.098  1.00 54.34  ? 6   ILE B C     1 
ATOM   3265 O O     . ILE B 2 6   ? 127.191 112.278 97.973  1.00 54.34  ? 6   ILE B O     1 
ATOM   3266 C CB    . ILE B 2 6   ? 129.709 112.042 99.550  1.00 80.45  ? 6   ILE B CB    1 
ATOM   3267 C CG1   . ILE B 2 6   ? 131.191 112.104 99.732  1.00 80.45  ? 6   ILE B CG1   1 
ATOM   3268 C CG2   . ILE B 2 6   ? 129.047 111.206 100.651 1.00 80.45  ? 6   ILE B CG2   1 
ATOM   3269 C CD1   . ILE B 2 6   ? 131.604 112.918 100.893 1.00 80.45  ? 6   ILE B CD1   1 
ATOM   3270 N N     . MET B 2 7   ? 127.430 110.072 98.194  1.00 61.05  ? 7   MET B N     1 
ATOM   3271 C CA    . MET B 2 7   ? 125.996 109.871 98.174  1.00 61.05  ? 7   MET B CA    1 
ATOM   3272 C C     . MET B 2 7   ? 125.401 109.785 99.572  1.00 61.05  ? 7   MET B C     1 
ATOM   3273 O O     . MET B 2 7   ? 125.991 109.232 100.502 1.00 61.05  ? 7   MET B O     1 
ATOM   3274 C CB    . MET B 2 7   ? 125.595 108.641 97.362  1.00 87.71  ? 7   MET B CB    1 
ATOM   3275 C CG    . MET B 2 7   ? 125.691 108.845 95.862  1.00 87.71  ? 7   MET B CG    1 
ATOM   3276 S SD    . MET B 2 7   ? 125.075 107.448 94.907  1.00 87.71  ? 7   MET B SD    1 
ATOM   3277 C CE    . MET B 2 7   ? 124.753 108.224 93.319  1.00 87.71  ? 7   MET B CE    1 
ATOM   3278 N N     . LEU B 2 8   ? 124.210 110.336 99.711  1.00 59.38  ? 8   LEU B N     1 
ATOM   3279 C CA    . LEU B 2 8   ? 123.495 110.268 100.963 1.00 59.38  ? 8   LEU B CA    1 
ATOM   3280 C C     . LEU B 2 8   ? 122.187 109.599 100.665 1.00 59.38  ? 8   LEU B C     1 
ATOM   3281 O O     . LEU B 2 8   ? 121.350 110.163 99.961  1.00 59.38  ? 8   LEU B O     1 
ATOM   3282 C CB    . LEU B 2 8   ? 123.279 111.654 101.536 1.00 87.91  ? 8   LEU B CB    1 
ATOM   3283 C CG    . LEU B 2 8   ? 124.517 112.355 102.112 1.00 87.91  ? 8   LEU B CG    1 
ATOM   3284 C CD1   . LEU B 2 8   ? 125.225 113.197 101.060 1.00 87.91  ? 8   LEU B CD1   1 
ATOM   3285 C CD2   . LEU B 2 8   ? 124.121 113.206 103.273 1.00 87.91  ? 8   LEU B CD2   1 
ATOM   3286 N N     . HIS B 2 9   ? 121.992 108.420 101.190 1.00 66.07  ? 9   HIS B N     1 
ATOM   3287 C CA    . HIS B 2 9   ? 120.755 107.722 100.926 1.00 66.07  ? 9   HIS B CA    1 
ATOM   3288 C C     . HIS B 2 9   ? 119.856 107.864 102.137 1.00 66.07  ? 9   HIS B C     1 
ATOM   3289 O O     . HIS B 2 9   ? 120.229 107.424 103.227 1.00 66.07  ? 9   HIS B O     1 
ATOM   3290 C CB    . HIS B 2 9   ? 121.048 106.274 100.628 1.00 89.85  ? 9   HIS B CB    1 
ATOM   3291 C CG    . HIS B 2 9   ? 121.975 106.106 99.492  1.00 89.85  ? 9   HIS B CG    1 
ATOM   3292 N ND1   . HIS B 2 9   ? 121.627 106.436 98.207  1.00 89.85  ? 9   HIS B ND1   1 
ATOM   3293 C CD2   . HIS B 2 9   ? 123.240 105.648 99.439  1.00 89.85  ? 9   HIS B CD2   1 
ATOM   3294 C CE1   . HIS B 2 9   ? 122.641 106.183 97.404  1.00 89.85  ? 9   HIS B CE1   1 
ATOM   3295 N NE2   . HIS B 2 9   ? 123.632 105.698 98.127  1.00 89.85  ? 9   HIS B NE2   1 
ATOM   3296 N N     . VAL B 2 10  ? 118.693 108.498 101.978 1.00 65.77  ? 10  VAL B N     1 
ATOM   3297 C CA    . VAL B 2 10  ? 117.879 108.834 103.135 1.00 65.77  ? 10  VAL B CA    1 
ATOM   3298 C C     . VAL B 2 10  ? 116.503 108.218 103.061 1.00 65.77  ? 10  VAL B C     1 
ATOM   3299 O O     . VAL B 2 10  ? 115.759 108.463 102.118 1.00 65.77  ? 10  VAL B O     1 
ATOM   3300 C CB    . VAL B 2 10  ? 117.771 110.343 103.297 1.00 95.66  ? 10  VAL B CB    1 
ATOM   3301 C CG1   . VAL B 2 10  ? 116.941 110.673 104.530 1.00 95.66  ? 10  VAL B CG1   1 
ATOM   3302 C CG2   . VAL B 2 10  ? 119.177 110.968 103.386 1.00 95.66  ? 10  VAL B CG2   1 
ATOM   3303 N N     . GLY B 2 11  ? 116.152 107.473 104.097 1.00 70.99  ? 11  GLY B N     1 
ATOM   3304 C CA    . GLY B 2 11  ? 114.838 106.863 104.241 1.00 70.99  ? 11  GLY B CA    1 
ATOM   3305 C C     . GLY B 2 11  ? 114.737 105.562 103.477 1.00 70.99  ? 11  GLY B C     1 
ATOM   3306 O O     . GLY B 2 11  ? 115.658 105.178 102.784 1.00 70.99  ? 11  GLY B O     1 
ATOM   3307 N N     . GLN B 2 12  ? 113.596 104.886 103.565 1.00 74.42  ? 12  GLN B N     1 
ATOM   3308 C CA    . GLN B 2 12  ? 113.495 103.580 102.927 1.00 74.42  ? 12  GLN B CA    1 
ATOM   3309 C C     . GLN B 2 12  ? 113.631 103.658 101.432 1.00 74.42  ? 12  GLN B C     1 
ATOM   3310 O O     . GLN B 2 12  ? 114.351 102.855 100.839 1.00 74.42  ? 12  GLN B O     1 
ATOM   3311 C CB    . GLN B 2 12  ? 112.174 102.902 103.264 1.00 103.98 ? 12  GLN B CB    1 
ATOM   3312 C CG    . GLN B 2 12  ? 111.891 101.504 102.615 1.00 103.98 ? 12  GLN B CG    1 
ATOM   3313 C CD    . GLN B 2 12  ? 112.718 100.327 103.141 1.00 103.98 ? 12  GLN B CD    1 
ATOM   3314 O OE1   . GLN B 2 12  ? 112.812 100.094 104.347 1.00 103.98 ? 12  GLN B OE1   1 
ATOM   3315 N NE2   . GLN B 2 12  ? 113.291 99.560  102.220 1.00 103.98 ? 12  GLN B NE2   1 
ATOM   3316 N N     . ALA B 2 13  ? 112.961 104.584 100.785 1.00 78.36  ? 13  ALA B N     1 
ATOM   3317 C CA    . ALA B 2 13  ? 113.092 104.587 99.334  1.00 78.36  ? 13  ALA B CA    1 
ATOM   3318 C C     . ALA B 2 13  ? 114.513 104.907 98.950  1.00 78.36  ? 13  ALA B C     1 
ATOM   3319 O O     . ALA B 2 13  ? 115.075 104.306 98.033  1.00 78.36  ? 13  ALA B O     1 
ATOM   3320 C CB    . ALA B 2 13  ? 112.155 105.594 98.703  1.00 106.85 ? 13  ALA B CB    1 
ATOM   3321 N N     . GLY B 2 14  ? 115.115 105.828 99.698  1.00 74.49  ? 14  GLY B N     1 
ATOM   3322 C CA    . GLY B 2 14  ? 116.466 106.272 99.409  1.00 74.49  ? 14  GLY B CA    1 
ATOM   3323 C C     . GLY B 2 14  ? 117.483 105.160 99.547  1.00 74.49  ? 14  GLY B C     1 
ATOM   3324 O O     . GLY B 2 14  ? 118.288 104.921 98.641  1.00 74.49  ? 14  GLY B O     1 
ATOM   3325 N N     . ILE B 2 15  ? 117.447 104.462 100.674 1.00 75.31  ? 15  ILE B N     1 
ATOM   3326 C CA    . ILE B 2 15  ? 118.415 103.428 100.908 1.00 75.31  ? 15  ILE B CA    1 
ATOM   3327 C C     . ILE B 2 15  ? 118.143 102.256 100.028 1.00 75.31  ? 15  ILE B C     1 
ATOM   3328 O O     . ILE B 2 15  ? 119.078 101.643 99.535  1.00 75.31  ? 15  ILE B O     1 
ATOM   3329 C CB    . ILE B 2 15  ? 118.459 103.050 102.367 1.00 111.50 ? 15  ILE B CB    1 
ATOM   3330 C CG1   . ILE B 2 15  ? 119.064 104.222 103.092 1.00 111.50 ? 15  ILE B CG1   1 
ATOM   3331 C CG2   . ILE B 2 15  ? 119.296 101.814 102.561 1.00 111.50 ? 15  ILE B CG2   1 
ATOM   3332 C CD1   . ILE B 2 15  ? 118.891 104.190 104.572 1.00 111.50 ? 15  ILE B CD1   1 
ATOM   3333 N N     . GLN B 2 16  ? 116.889 101.911 99.796  1.00 74.12  ? 16  GLN B N     1 
ATOM   3334 C CA    . GLN B 2 16  ? 116.632 100.760 98.947  1.00 74.12  ? 16  GLN B CA    1 
ATOM   3335 C C     . GLN B 2 16  ? 117.078 101.001 97.513  1.00 74.12  ? 16  GLN B C     1 
ATOM   3336 O O     . GLN B 2 16  ? 117.695 100.118 96.887  1.00 74.12  ? 16  GLN B O     1 
ATOM   3337 C CB    . GLN B 2 16  ? 115.163 100.408 98.973  1.00 103.56 ? 16  GLN B CB    1 
ATOM   3338 C CG    . GLN B 2 16  ? 114.842 99.130  98.300  1.00 103.56 ? 16  GLN B CG    1 
ATOM   3339 C CD    . GLN B 2 16  ? 115.473 97.980  99.003  1.00 103.56 ? 16  GLN B CD    1 
ATOM   3340 O OE1   . GLN B 2 16  ? 115.267 97.801  100.195 1.00 103.56 ? 16  GLN B OE1   1 
ATOM   3341 N NE2   . GLN B 2 16  ? 116.256 97.189  98.282  1.00 103.56 ? 16  GLN B NE2   1 
ATOM   3342 N N     . VAL B 2 17  ? 116.813 102.190 96.969  1.00 75.38  ? 17  VAL B N     1 
ATOM   3343 C CA    . VAL B 2 17  ? 117.254 102.448 95.607  1.00 75.38  ? 17  VAL B CA    1 
ATOM   3344 C C     . VAL B 2 17  ? 118.752 102.503 95.562  1.00 75.38  ? 17  VAL B C     1 
ATOM   3345 O O     . VAL B 2 17  ? 119.364 101.992 94.621  1.00 75.38  ? 17  VAL B O     1 
ATOM   3346 C CB    . VAL B 2 17  ? 116.650 103.727 95.022  1.00 109.64 ? 17  VAL B CB    1 
ATOM   3347 C CG1   . VAL B 2 17  ? 117.305 104.057 93.695  1.00 109.64 ? 17  VAL B CG1   1 
ATOM   3348 C CG2   . VAL B 2 17  ? 115.147 103.519 94.814  1.00 109.64 ? 17  VAL B CG2   1 
ATOM   3349 N N     . GLY B 2 18  ? 119.364 103.140 96.556  1.00 75.40  ? 18  GLY B N     1 
ATOM   3350 C CA    . GLY B 2 18  ? 120.806 103.201 96.604  1.00 75.40  ? 18  GLY B CA    1 
ATOM   3351 C C     . GLY B 2 18  ? 121.414 101.820 96.664  1.00 75.40  ? 18  GLY B C     1 
ATOM   3352 O O     . GLY B 2 18  ? 122.369 101.525 95.964  1.00 75.40  ? 18  GLY B O     1 
ATOM   3353 N N     . ALA B 2 19  ? 120.835 100.940 97.451  1.00 75.49  ? 19  ALA B N     1 
ATOM   3354 C CA    . ALA B 2 19  ? 121.373 99.607  97.520  1.00 75.49  ? 19  ALA B CA    1 
ATOM   3355 C C     . ALA B 2 19  ? 121.423 99.006  96.140  1.00 75.49  ? 19  ALA B C     1 
ATOM   3356 O O     . ALA B 2 19  ? 122.461 98.471  95.722  1.00 75.49  ? 19  ALA B O     1 
ATOM   3357 C CB    . ALA B 2 19  ? 120.518 98.761  98.452  1.00 102.94 ? 19  ALA B CB    1 
ATOM   3358 N N     . MET B 2 20  ? 120.362 99.176  95.378  1.00 76.95  ? 20  MET B N     1 
ATOM   3359 C CA    . MET B 2 20  ? 120.419 98.657  94.023  1.00 76.95  ? 20  MET B CA    1 
ATOM   3360 C C     . MET B 2 20  ? 121.457 99.389  93.151  1.00 76.95  ? 20  MET B C     1 
ATOM   3361 O O     . MET B 2 20  ? 122.165 98.758  92.345  1.00 76.95  ? 20  MET B O     1 
ATOM   3362 C CB    . MET B 2 20  ? 119.039 98.709  93.418  1.00 110.55 ? 20  MET B CB    1 
ATOM   3363 C CG    . MET B 2 20  ? 118.157 97.756  94.081  1.00 110.55 ? 20  MET B CG    1 
ATOM   3364 S SD    . MET B 2 20  ? 116.495 97.852  93.488  1.00 110.55 ? 20  MET B SD    1 
ATOM   3365 C CE    . MET B 2 20  ? 116.638 97.087  91.906  1.00 110.55 ? 20  MET B CE    1 
ATOM   3366 N N     . TYR B 2 21  ? 121.563 100.708 93.303  1.00 68.68  ? 21  TYR B N     1 
ATOM   3367 C CA    . TYR B 2 21  ? 122.525 101.482 92.540  1.00 68.68  ? 21  TYR B CA    1 
ATOM   3368 C C     . TYR B 2 21  ? 123.900 100.954 92.757  1.00 68.68  ? 21  TYR B C     1 
ATOM   3369 O O     . TYR B 2 21  ? 124.668 100.775 91.814  1.00 68.68  ? 21  TYR B O     1 
ATOM   3370 C CB    . TYR B 2 21  ? 122.520 102.918 92.983  1.00 95.09  ? 21  TYR B CB    1 
ATOM   3371 C CG    . TYR B 2 21  ? 123.579 103.748 92.362  1.00 95.09  ? 21  TYR B CG    1 
ATOM   3372 C CD1   . TYR B 2 21  ? 123.357 104.346 91.162  1.00 95.09  ? 21  TYR B CD1   1 
ATOM   3373 C CD2   . TYR B 2 21  ? 124.787 103.966 92.999  1.00 95.09  ? 21  TYR B CD2   1 
ATOM   3374 C CE1   . TYR B 2 21  ? 124.294 105.140 90.594  1.00 95.09  ? 21  TYR B CE1   1 
ATOM   3375 C CE2   . TYR B 2 21  ? 125.743 104.759 92.434  1.00 95.09  ? 21  TYR B CE2   1 
ATOM   3376 C CZ    . TYR B 2 21  ? 125.488 105.350 91.221  1.00 95.09  ? 21  TYR B CZ    1 
ATOM   3377 O OH    . TYR B 2 21  ? 126.420 106.169 90.620  1.00 95.09  ? 21  TYR B OH    1 
ATOM   3378 N N     . TRP B 2 22  ? 124.238 100.750 93.998  1.00 69.53  ? 22  TRP B N     1 
ATOM   3379 C CA    . TRP B 2 22  ? 125.555 100.290 94.332  1.00 69.53  ? 22  TRP B CA    1 
ATOM   3380 C C     . TRP B 2 22  ? 125.804 98.896  93.800  1.00 69.53  ? 22  TRP B C     1 
ATOM   3381 O O     . TRP B 2 22  ? 126.897 98.614  93.306  1.00 69.53  ? 22  TRP B O     1 
ATOM   3382 C CB    . TRP B 2 22  ? 125.754 100.361 95.822  1.00 96.27  ? 22  TRP B CB    1 
ATOM   3383 C CG    . TRP B 2 22  ? 125.932 101.744 96.236  1.00 96.27  ? 22  TRP B CG    1 
ATOM   3384 C CD1   . TRP B 2 22  ? 125.046 102.484 96.883  1.00 96.27  ? 22  TRP B CD1   1 
ATOM   3385 C CD2   . TRP B 2 22  ? 127.065 102.559 96.044  1.00 96.27  ? 22  TRP B CD2   1 
ATOM   3386 N NE1   . TRP B 2 22  ? 125.528 103.717 97.089  1.00 96.27  ? 22  TRP B NE1   1 
ATOM   3387 C CE2   . TRP B 2 22  ? 126.778 103.781 96.570  1.00 96.27  ? 22  TRP B CE2   1 
ATOM   3388 C CE3   . TRP B 2 22  ? 128.283 102.366 95.466  1.00 96.27  ? 22  TRP B CE3   1 
ATOM   3389 C CZ2   . TRP B 2 22  ? 127.645 104.806 96.548  1.00 96.27  ? 22  TRP B CZ2   1 
ATOM   3390 C CZ3   . TRP B 2 22  ? 129.151 103.393 95.433  1.00 96.27  ? 22  TRP B CZ3   1 
ATOM   3391 C CH2   . TRP B 2 22  ? 128.836 104.594 95.971  1.00 96.27  ? 22  TRP B CH2   1 
ATOM   3392 N N     . LYS B 2 23  ? 124.815 98.022  93.829  1.00 68.88  ? 23  LYS B N     1 
ATOM   3393 C CA    . LYS B 2 23  ? 125.085 96.712  93.260  1.00 68.88  ? 23  LYS B CA    1 
ATOM   3394 C C     . LYS B 2 23  ? 125.482 96.840  91.794  1.00 68.88  ? 23  LYS B C     1 
ATOM   3395 O O     . LYS B 2 23  ? 126.377 96.129  91.297  1.00 68.88  ? 23  LYS B O     1 
ATOM   3396 C CB    . LYS B 2 23  ? 123.866 95.791  93.380  1.00 103.32 ? 23  LYS B CB    1 
ATOM   3397 C CG    . LYS B 2 23  ? 123.469 95.296  94.782  1.00 103.32 ? 23  LYS B CG    1 
ATOM   3398 C CD    . LYS B 2 23  ? 122.212 94.373  94.718  1.00 103.32 ? 23  LYS B CD    1 
ATOM   3399 C CE    . LYS B 2 23  ? 121.686 93.959  96.094  1.00 103.32 ? 23  LYS B CE    1 
ATOM   3400 N NZ    . LYS B 2 23  ? 120.486 93.090  96.008  1.00 103.32 ? 23  LYS B NZ    1 
ATOM   3401 N N     . GLN B 2 24  ? 124.814 97.739  91.079  1.00 67.29  ? 24  GLN B N     1 
ATOM   3402 C CA    . GLN B 2 24  ? 125.052 97.854  89.644  1.00 67.29  ? 24  GLN B CA    1 
ATOM   3403 C C     . GLN B 2 24  ? 126.325 98.613  89.306  1.00 67.29  ? 24  GLN B C     1 
ATOM   3404 O O     . GLN B 2 24  ? 127.002 98.276  88.332  1.00 67.29  ? 24  GLN B O     1 
ATOM   3405 C CB    . GLN B 2 24  ? 123.860 98.502  88.966  1.00 94.02  ? 24  GLN B CB    1 
ATOM   3406 C CG    . GLN B 2 24  ? 123.948 98.520  87.479  1.00 94.02  ? 24  GLN B CG    1 
ATOM   3407 C CD    . GLN B 2 24  ? 122.643 98.878  86.867  1.00 94.02  ? 24  GLN B CD    1 
ATOM   3408 O OE1   . GLN B 2 24  ? 122.067 99.910  87.170  1.00 94.02  ? 24  GLN B OE1   1 
ATOM   3409 N NE2   . GLN B 2 24  ? 122.157 98.025  85.994  1.00 94.02  ? 24  GLN B NE2   1 
ATOM   3410 N N     . ILE B 2 25  ? 126.668 99.631  90.070  1.00 65.82  ? 25  ILE B N     1 
ATOM   3411 C CA    . ILE B 2 25  ? 127.895 100.330 89.779  1.00 65.82  ? 25  ILE B CA    1 
ATOM   3412 C C     . ILE B 2 25  ? 129.018 99.379  89.993  1.00 65.82  ? 25  ILE B C     1 
ATOM   3413 O O     . ILE B 2 25  ? 130.032 99.436  89.296  1.00 65.82  ? 25  ILE B O     1 
ATOM   3414 C CB    . ILE B 2 25  ? 128.066 101.576 90.659  1.00 97.45  ? 25  ILE B CB    1 
ATOM   3415 C CG1   . ILE B 2 25  ? 129.142 102.476 90.120  1.00 97.45  ? 25  ILE B CG1   1 
ATOM   3416 C CG2   . ILE B 2 25  ? 128.451 101.212 92.034  1.00 97.45  ? 25  ILE B CG2   1 
ATOM   3417 C CD1   . ILE B 2 25  ? 129.227 103.825 90.820  1.00 97.45  ? 25  ILE B CD1   1 
ATOM   3418 N N     . CYS B 2 26  ? 128.879 98.490  90.967  1.00 72.86  ? 26  CYS B N     1 
ATOM   3419 C CA    . CYS B 2 26  ? 129.958 97.567  91.193  1.00 72.86  ? 26  CYS B CA    1 
ATOM   3420 C C     . CYS B 2 26  ? 130.139 96.712  89.985  1.00 72.86  ? 26  CYS B C     1 
ATOM   3421 O O     . CYS B 2 26  ? 131.260 96.519  89.512  1.00 72.86  ? 26  CYS B O     1 
ATOM   3422 C CB    . CYS B 2 26  ? 129.667 96.710  92.402  1.00 98.14  ? 26  CYS B CB    1 
ATOM   3423 S SG    . CYS B 2 26  ? 129.750 97.614  93.915  1.00 98.14  ? 26  CYS B SG    1 
ATOM   3424 N N     . ALA B 2 27  ? 129.039 96.241  89.431  1.00 69.70  ? 27  ALA B N     1 
ATOM   3425 C CA    . ALA B 2 27  ? 129.195 95.411  88.256  1.00 69.70  ? 27  ALA B CA    1 
ATOM   3426 C C     . ALA B 2 27  ? 129.927 96.160  87.158  1.00 69.70  ? 27  ALA B C     1 
ATOM   3427 O O     . ALA B 2 27  ? 130.854 95.627  86.536  1.00 69.70  ? 27  ALA B O     1 
ATOM   3428 C CB    . ALA B 2 27  ? 127.840 94.944  87.772  1.00 95.05  ? 27  ALA B CB    1 
ATOM   3429 N N     . GLU B 2 28  ? 129.581 97.422  86.962  1.00 68.59  ? 28  GLU B N     1 
ATOM   3430 C CA    . GLU B 2 28  ? 130.232 98.195  85.918  1.00 68.59  ? 28  GLU B CA    1 
ATOM   3431 C C     . GLU B 2 28  ? 131.730 98.257  86.113  1.00 68.59  ? 28  GLU B C     1 
ATOM   3432 O O     . GLU B 2 28  ? 132.488 98.191  85.150  1.00 68.59  ? 28  GLU B O     1 
ATOM   3433 C CB    . GLU B 2 28  ? 129.669 99.599  85.906  1.00 92.14  ? 28  GLU B CB    1 
ATOM   3434 C CG    . GLU B 2 28  ? 130.202 100.451 84.805  1.00 92.14  ? 28  GLU B CG    1 
ATOM   3435 C CD    . GLU B 2 28  ? 129.636 101.811 84.865  1.00 92.14  ? 28  GLU B CD    1 
ATOM   3436 O OE1   . GLU B 2 28  ? 128.467 102.008 84.522  1.00 92.14  ? 28  GLU B OE1   1 
ATOM   3437 O OE2   . GLU B 2 28  ? 130.373 102.697 85.271  1.00 92.14  ? 28  GLU B OE2   1 
ATOM   3438 N N     . HIS B 2 29  ? 132.173 98.382  87.346  1.00 67.79  ? 29  HIS B N     1 
ATOM   3439 C CA    . HIS B 2 29  ? 133.581 98.476  87.662  1.00 67.79  ? 29  HIS B CA    1 
ATOM   3440 C C     . HIS B 2 29  ? 134.211 97.128  87.973  1.00 67.79  ? 29  HIS B C     1 
ATOM   3441 O O     . HIS B 2 29  ? 135.336 97.109  88.481  1.00 67.79  ? 29  HIS B O     1 
ATOM   3442 C CB    . HIS B 2 29  ? 133.859 99.314  88.910  1.00 92.19  ? 29  HIS B CB    1 
ATOM   3443 C CG    . HIS B 2 29  ? 133.642 100.796 88.833  1.00 92.19  ? 29  HIS B CG    1 
ATOM   3444 N ND1   . HIS B 2 29  ? 134.281 101.627 87.941  1.00 92.19  ? 29  HIS B ND1   1 
ATOM   3445 C CD2   . HIS B 2 29  ? 132.963 101.611 89.673  1.00 92.19  ? 29  HIS B CD2   1 
ATOM   3446 C CE1   . HIS B 2 29  ? 133.958 102.884 88.196  1.00 92.19  ? 29  HIS B CE1   1 
ATOM   3447 N NE2   . HIS B 2 29  ? 133.169 102.902 89.252  1.00 92.19  ? 29  HIS B NE2   1 
ATOM   3448 N N     . ASN B 2 30  ? 133.508 96.014  87.756  1.00 73.15  ? 30  ASN B N     1 
ATOM   3449 C CA    . ASN B 2 30  ? 134.060 94.679  88.027  1.00 73.15  ? 30  ASN B CA    1 
ATOM   3450 C C     . ASN B 2 30  ? 134.333 94.443  89.513  1.00 73.15  ? 30  ASN B C     1 
ATOM   3451 O O     . ASN B 2 30  ? 135.236 93.686  89.886  1.00 73.15  ? 30  ASN B O     1 
ATOM   3452 C CB    . ASN B 2 30  ? 135.334 94.476  87.194  1.00 99.11  ? 30  ASN B CB    1 
ATOM   3453 C CG    . ASN B 2 30  ? 135.837 93.046  87.143  1.00 99.11  ? 30  ASN B CG    1 
ATOM   3454 O OD1   . ASN B 2 30  ? 135.085 92.076  87.269  1.00 99.11  ? 30  ASN B OD1   1 
ATOM   3455 N ND2   . ASN B 2 30  ? 137.143 92.917  86.922  1.00 99.11  ? 30  ASN B ND2   1 
ATOM   3456 N N     . LEU B 2 31  ? 133.519 95.028  90.369  1.00 74.69  ? 31  LEU B N     1 
ATOM   3457 C CA    . LEU B 2 31  ? 133.727 94.854  91.789  1.00 74.69  ? 31  LEU B CA    1 
ATOM   3458 C C     . LEU B 2 31  ? 132.791 93.805  92.336  1.00 74.69  ? 31  LEU B C     1 
ATOM   3459 O O     . LEU B 2 31  ? 131.666 93.627  91.855  1.00 74.69  ? 31  LEU B O     1 
ATOM   3460 C CB    . LEU B 2 31  ? 133.513 96.163  92.528  1.00 110.58 ? 31  LEU B CB    1 
ATOM   3461 C CG    . LEU B 2 31  ? 134.443 97.312  92.131  1.00 110.58 ? 31  LEU B CG    1 
ATOM   3462 C CD1   . LEU B 2 31  ? 134.015 98.605  92.823  1.00 110.58 ? 31  LEU B CD1   1 
ATOM   3463 C CD2   . LEU B 2 31  ? 135.866 96.965  92.501  1.00 110.58 ? 31  LEU B CD2   1 
ATOM   3464 N N     . ASP B 2 32  ? 133.284 93.118  93.352  1.00 82.88  ? 32  ASP B N     1 
ATOM   3465 C CA    . ASP B 2 32  ? 132.534 92.095  94.052  1.00 82.88  ? 32  ASP B CA    1 
ATOM   3466 C C     . ASP B 2 32  ? 131.691 92.689  95.170  1.00 82.88  ? 32  ASP B C     1 
ATOM   3467 O O     . ASP B 2 32  ? 132.184 93.403  96.028  1.00 82.88  ? 32  ASP B O     1 
ATOM   3468 C CB    . ASP B 2 32  ? 133.488 91.050  94.591  1.00 106.56 ? 32  ASP B CB    1 
ATOM   3469 C CG    . ASP B 2 32  ? 132.779 89.943  95.303  1.00 106.56 ? 32  ASP B CG    1 
ATOM   3470 O OD1   . ASP B 2 32  ? 131.566 90.045  95.497  1.00 106.56 ? 32  ASP B OD1   1 
ATOM   3471 O OD2   . ASP B 2 32  ? 133.428 88.967  95.689  1.00 106.56 ? 32  ASP B OD2   1 
ATOM   3472 N N     . HIS B 2 33  ? 130.414 92.373  95.182  1.00 83.44  ? 33  HIS B N     1 
ATOM   3473 C CA    . HIS B 2 33  ? 129.568 92.956  96.189  1.00 83.44  ? 33  HIS B CA    1 
ATOM   3474 C C     . HIS B 2 33  ? 130.099 92.690  97.572  1.00 83.44  ? 33  HIS B C     1 
ATOM   3475 O O     . HIS B 2 33  ? 129.820 93.448  98.504  1.00 83.44  ? 33  HIS B O     1 
ATOM   3476 C CB    . HIS B 2 33  ? 128.181 92.373  96.088  1.00 113.48 ? 33  HIS B CB    1 
ATOM   3477 C CG    . HIS B 2 33  ? 127.459 92.745  94.850  1.00 113.48 ? 33  HIS B CG    1 
ATOM   3478 N ND1   . HIS B 2 33  ? 126.301 92.120  94.456  1.00 113.48 ? 33  HIS B ND1   1 
ATOM   3479 C CD2   . HIS B 2 33  ? 127.717 93.681  93.909  1.00 113.48 ? 33  HIS B CD2   1 
ATOM   3480 C CE1   . HIS B 2 33  ? 125.879 92.643  93.318  1.00 113.48 ? 33  HIS B CE1   1 
ATOM   3481 N NE2   . HIS B 2 33  ? 126.719 93.595  92.965  1.00 113.48 ? 33  HIS B NE2   1 
ATOM   3482 N N     . ASN B 2 34  ? 130.870 91.630  97.735  1.00 85.05  ? 34  ASN B N     1 
ATOM   3483 C CA    . ASN B 2 34  ? 131.353 91.238  99.054  1.00 85.05  ? 34  ASN B CA    1 
ATOM   3484 C C     . ASN B 2 34  ? 132.576 92.056  99.459  1.00 85.05  ? 34  ASN B C     1 
ATOM   3485 O O     . ASN B 2 34  ? 133.698 91.559  99.550  1.00 85.05  ? 34  ASN B O     1 
ATOM   3486 C CB    . ASN B 2 34  ? 131.666 89.756  99.075  1.00 115.23 ? 34  ASN B CB    1 
ATOM   3487 C CG    . ASN B 2 34  ? 131.962 89.253  100.462 1.00 115.23 ? 34  ASN B CG    1 
ATOM   3488 O OD1   . ASN B 2 34  ? 131.731 89.946  101.458 1.00 115.23 ? 34  ASN B OD1   1 
ATOM   3489 N ND2   . ASN B 2 34  ? 132.468 88.037  100.541 1.00 115.23 ? 34  ASN B ND2   1 
ATOM   3490 N N     . GLY B 2 35  ? 132.318 93.321  99.770  1.00 84.51  ? 35  GLY B N     1 
ATOM   3491 C CA    . GLY B 2 35  ? 133.334 94.263  100.214 1.00 84.51  ? 35  GLY B CA    1 
ATOM   3492 C C     . GLY B 2 35  ? 134.041 94.983  99.090  1.00 84.51  ? 35  GLY B C     1 
ATOM   3493 O O     . GLY B 2 35  ? 135.028 95.684  99.333  1.00 84.51  ? 35  GLY B O     1 
ATOM   3494 N N     . ALA B 2 36  ? 133.583 94.808  97.873  1.00 83.26  ? 36  ALA B N     1 
ATOM   3495 C CA    . ALA B 2 36  ? 134.156 95.432  96.690  1.00 83.26  ? 36  ALA B CA    1 
ATOM   3496 C C     . ALA B 2 36  ? 135.637 95.172  96.447  1.00 83.26  ? 36  ALA B C     1 
ATOM   3497 O O     . ALA B 2 36  ? 136.386 96.127  96.210  1.00 83.26  ? 36  ALA B O     1 
ATOM   3498 C CB    . ALA B 2 36  ? 133.941 96.933  96.755  1.00 113.54 ? 36  ALA B CB    1 
ATOM   3499 N N     . PRO B 2 37  ? 136.110 93.934  96.537  1.00 82.19  ? 37  PRO B N     1 
ATOM   3500 C CA    . PRO B 2 37  ? 137.422 93.598  95.994  1.00 82.19  ? 37  PRO B CA    1 
ATOM   3501 C C     . PRO B 2 37  ? 137.204 93.542  94.502  1.00 82.19  ? 37  PRO B C     1 
ATOM   3502 O O     . PRO B 2 37  ? 136.062 93.455  94.043  1.00 82.19  ? 37  PRO B O     1 
ATOM   3503 C CB    . PRO B 2 37  ? 137.727 92.227  96.617  1.00 542.67 ? 37  PRO B CB    1 
ATOM   3504 C CG    . PRO B 2 37  ? 136.376 91.621  96.849  1.00 542.67 ? 37  PRO B CG    1 
ATOM   3505 C CD    . PRO B 2 37  ? 135.465 92.790  97.193  1.00 542.67 ? 37  PRO B CD    1 
ATOM   3506 N N     . ILE B 2 38  ? 138.261 93.598  93.725  1.00 81.09  ? 38  ILE B N     1 
ATOM   3507 C CA    . ILE B 2 38  ? 138.044 93.611  92.292  1.00 81.09  ? 38  ILE B CA    1 
ATOM   3508 C C     . ILE B 2 38  ? 138.487 92.349  91.578  1.00 81.09  ? 38  ILE B C     1 
ATOM   3509 O O     . ILE B 2 38  ? 139.566 91.813  91.830  1.00 81.09  ? 38  ILE B O     1 
ATOM   3510 C CB    . ILE B 2 38  ? 138.714 94.808  91.662  1.00 120.05 ? 38  ILE B CB    1 
ATOM   3511 C CG1   . ILE B 2 38  ? 138.293 94.765  90.246  1.00 120.05 ? 38  ILE B CG1   1 
ATOM   3512 C CG2   . ILE B 2 38  ? 140.218 94.751  91.823  1.00 120.05 ? 38  ILE B CG2   1 
ATOM   3513 C CD1   . ILE B 2 38  ? 138.478 95.940  89.602  1.00 120.05 ? 38  ILE B CD1   1 
ATOM   3514 N N     . GLY B 2 39  ? 137.664 91.907  90.645  1.00 79.29  ? 39  GLY B N     1 
ATOM   3515 C CA    . GLY B 2 39  ? 137.978 90.743  89.852  1.00 79.29  ? 39  GLY B CA    1 
ATOM   3516 C C     . GLY B 2 39  ? 139.041 90.994  88.800  1.00 79.29  ? 39  GLY B C     1 
ATOM   3517 O O     . GLY B 2 39  ? 138.799 90.826  87.603  1.00 79.29  ? 39  GLY B O     1 
ATOM   3518 N N     . GLY B 2 40  ? 140.230 91.365  89.230  1.00 81.27  ? 40  GLY B N     1 
ATOM   3519 C CA    . GLY B 2 40  ? 141.297 91.700  88.303  1.00 81.27  ? 40  GLY B CA    1 
ATOM   3520 C C     . GLY B 2 40  ? 141.398 93.200  88.038  1.00 81.27  ? 40  GLY B C     1 
ATOM   3521 O O     . GLY B 2 40  ? 141.455 93.993  88.966  1.00 81.27  ? 40  GLY B O     1 
ATOM   3522 N N     . ASP B 2 41  ? 141.501 93.574  86.769  1.00 79.02  ? 41  ASP B N     1 
ATOM   3523 C CA    . ASP B 2 41  ? 141.668 94.977  86.397  1.00 79.02  ? 41  ASP B CA    1 
ATOM   3524 C C     . ASP B 2 41  ? 140.381 95.757  86.596  1.00 79.02  ? 41  ASP B C     1 
ATOM   3525 O O     . ASP B 2 41  ? 139.283 95.199  86.520  1.00 79.02  ? 41  ASP B O     1 
ATOM   3526 C CB    . ASP B 2 41  ? 142.061 95.108  84.938  1.00 101.60 ? 41  ASP B CB    1 
ATOM   3527 C CG    . ASP B 2 41  ? 143.455 94.657  84.666  1.00 101.60 ? 41  ASP B CG    1 
ATOM   3528 O OD1   . ASP B 2 41  ? 144.249 94.530  85.594  1.00 101.60 ? 41  ASP B OD1   1 
ATOM   3529 O OD2   . ASP B 2 41  ? 143.760 94.431  83.500  1.00 101.60 ? 41  ASP B OD2   1 
ATOM   3530 N N     . ILE B 2 42  ? 140.504 97.075  86.791  1.00 72.59  ? 42  ILE B N     1 
ATOM   3531 C CA    . ILE B 2 42  ? 139.318 97.891  87.001  1.00 72.59  ? 42  ILE B CA    1 
ATOM   3532 C C     . ILE B 2 42  ? 138.977 98.686  85.775  1.00 72.59  ? 42  ILE B C     1 
ATOM   3533 O O     . ILE B 2 42  ? 139.840 99.254  85.110  1.00 72.59  ? 42  ILE B O     1 
ATOM   3534 C CB    . ILE B 2 42  ? 139.441 98.820  88.207  1.00 107.47 ? 42  ILE B CB    1 
ATOM   3535 C CG1   . ILE B 2 42  ? 138.080 99.502  88.436  1.00 107.47 ? 42  ILE B CG1   1 
ATOM   3536 C CG2   . ILE B 2 42  ? 140.536 99.815  88.012  1.00 107.47 ? 42  ILE B CG2   1 
ATOM   3537 C CD1   . ILE B 2 42  ? 137.874 100.076 89.814  1.00 107.47 ? 42  ILE B CD1   1 
ATOM   3538 N N     . LYS B 2 43  ? 137.711 98.686  85.461  1.00 74.93  ? 43  LYS B N     1 
ATOM   3539 C CA    . LYS B 2 43  ? 137.180 99.415  84.348  1.00 74.93  ? 43  LYS B CA    1 
ATOM   3540 C C     . LYS B 2 43  ? 136.442 100.613 84.901  1.00 74.93  ? 43  LYS B C     1 
ATOM   3541 O O     . LYS B 2 43  ? 135.780 100.506 85.933  1.00 74.93  ? 43  LYS B O     1 
ATOM   3542 C CB    . LYS B 2 43  ? 136.238 98.530  83.557  1.00 112.39 ? 43  LYS B CB    1 
ATOM   3543 C CG    . LYS B 2 43  ? 136.841 97.214  83.145  1.00 112.39 ? 43  LYS B CG    1 
ATOM   3544 C CD    . LYS B 2 43  ? 138.001 97.402  82.166  1.00 112.39 ? 43  LYS B CD    1 
ATOM   3545 C CE    . LYS B 2 43  ? 138.538 96.064  81.662  1.00 112.39 ? 43  LYS B CE    1 
ATOM   3546 N NZ    . LYS B 2 43  ? 139.692 96.233  80.725  1.00 112.39 ? 43  LYS B NZ    1 
ATOM   3547 N N     . GLY B 2 44  ? 136.524 101.744 84.205  1.00 67.19  ? 44  GLY B N     1 
ATOM   3548 C CA    . GLY B 2 44  ? 135.849 102.961 84.630  1.00 67.19  ? 44  GLY B CA    1 
ATOM   3549 C C     . GLY B 2 44  ? 136.724 103.691 85.617  1.00 67.19  ? 44  GLY B C     1 
ATOM   3550 O O     . GLY B 2 44  ? 137.796 103.216 85.979  1.00 67.19  ? 44  GLY B O     1 
ATOM   3551 N N     . ASP B 2 45  ? 136.275 104.863 86.071  1.00 67.26  ? 45  ASP B N     1 
ATOM   3552 C CA    . ASP B 2 45  ? 137.074 105.632 87.010  1.00 67.26  ? 45  ASP B CA    1 
ATOM   3553 C C     . ASP B 2 45  ? 136.546 105.527 88.433  1.00 67.26  ? 45  ASP B C     1 
ATOM   3554 O O     . ASP B 2 45  ? 135.617 106.256 88.792  1.00 67.26  ? 45  ASP B O     1 
ATOM   3555 C CB    . ASP B 2 45  ? 137.118 107.092 86.596  1.00 86.48  ? 45  ASP B CB    1 
ATOM   3556 C CG    . ASP B 2 45  ? 138.013 107.887 87.497  1.00 86.48  ? 45  ASP B CG    1 
ATOM   3557 O OD1   . ASP B 2 45  ? 138.638 107.267 88.365  1.00 86.48  ? 45  ASP B OD1   1 
ATOM   3558 O OD2   . ASP B 2 45  ? 138.091 109.115 87.358  1.00 86.48  ? 45  ASP B OD2   1 
ATOM   3559 N N     . PRO B 2 46  ? 137.196 104.750 89.299  1.00 66.43  ? 46  PRO B N     1 
ATOM   3560 C CA    . PRO B 2 46  ? 136.759 104.564 90.680  1.00 66.43  ? 46  PRO B CA    1 
ATOM   3561 C C     . PRO B 2 46  ? 136.868 105.817 91.495  1.00 66.43  ? 46  PRO B C     1 
ATOM   3562 O O     . PRO B 2 46  ? 136.253 105.926 92.558  1.00 66.43  ? 46  PRO B O     1 
ATOM   3563 C CB    . PRO B 2 46  ? 137.734 103.506 91.197  1.00 438.60 ? 46  PRO B CB    1 
ATOM   3564 C CG    . PRO B 2 46  ? 138.957 103.720 90.373  1.00 438.60 ? 46  PRO B CG    1 
ATOM   3565 C CD    . PRO B 2 46  ? 138.468 104.097 89.017  1.00 438.60 ? 46  PRO B CD    1 
ATOM   3566 N N     . ASP B 2 47  ? 137.624 106.786 91.021  1.00 70.72  ? 47  ASP B N     1 
ATOM   3567 C CA    . ASP B 2 47  ? 137.827 107.973 91.816  1.00 70.72  ? 47  ASP B CA    1 
ATOM   3568 C C     . ASP B 2 47  ? 136.532 108.694 92.109  1.00 70.72  ? 47  ASP B C     1 
ATOM   3569 O O     . ASP B 2 47  ? 136.499 109.499 93.035  1.00 70.72  ? 47  ASP B O     1 
ATOM   3570 C CB    . ASP B 2 47  ? 138.762 108.965 91.106  1.00 90.93  ? 47  ASP B CB    1 
ATOM   3571 C CG    . ASP B 2 47  ? 140.248 108.543 91.086  1.00 90.93  ? 47  ASP B CG    1 
ATOM   3572 O OD1   . ASP B 2 47  ? 140.637 107.603 91.779  1.00 90.93  ? 47  ASP B OD1   1 
ATOM   3573 O OD2   . ASP B 2 47  ? 141.033 109.191 90.371  1.00 90.93  ? 47  ASP B OD2   1 
ATOM   3574 N N     . CYS B 2 48  ? 135.492 108.507 91.309  1.00 66.50  ? 48  CYS B N     1 
ATOM   3575 C CA    . CYS B 2 48  ? 134.294 109.283 91.584  1.00 66.50  ? 48  CYS B CA    1 
ATOM   3576 C C     . CYS B 2 48  ? 133.537 108.729 92.777  1.00 66.50  ? 48  CYS B C     1 
ATOM   3577 O O     . CYS B 2 48  ? 133.179 109.474 93.692  1.00 66.50  ? 48  CYS B O     1 
ATOM   3578 C CB    . CYS B 2 48  ? 133.368 109.344 90.369  1.00 89.57  ? 48  CYS B CB    1 
ATOM   3579 S SG    . CYS B 2 48  ? 131.908 110.396 90.648  1.00 89.57  ? 48  CYS B SG    1 
ATOM   3580 N N     . PHE B 2 49  ? 133.280 107.445 92.801  1.00 63.29  ? 49  PHE B N     1 
ATOM   3581 C CA    . PHE B 2 49  ? 132.423 106.932 93.836  1.00 63.29  ? 49  PHE B CA    1 
ATOM   3582 C C     . PHE B 2 49  ? 133.080 106.056 94.891  1.00 63.29  ? 49  PHE B C     1 
ATOM   3583 O O     . PHE B 2 49  ? 132.408 105.713 95.868  1.00 63.29  ? 49  PHE B O     1 
ATOM   3584 C CB    . PHE B 2 49  ? 131.261 106.181 93.190  1.00 88.31  ? 49  PHE B CB    1 
ATOM   3585 C CG    . PHE B 2 49  ? 130.335 107.073 92.439  1.00 88.31  ? 49  PHE B CG    1 
ATOM   3586 C CD1   . PHE B 2 49  ? 129.431 107.829 93.105  1.00 88.31  ? 49  PHE B CD1   1 
ATOM   3587 C CD2   . PHE B 2 49  ? 130.385 107.171 91.101  1.00 88.31  ? 49  PHE B CD2   1 
ATOM   3588 C CE1   . PHE B 2 49  ? 128.596 108.640 92.449  1.00 88.31  ? 49  PHE B CE1   1 
ATOM   3589 C CE2   . PHE B 2 49  ? 129.548 107.971 90.449  1.00 88.31  ? 49  PHE B CE2   1 
ATOM   3590 C CZ    . PHE B 2 49  ? 128.656 108.708 91.109  1.00 88.31  ? 49  PHE B CZ    1 
ATOM   3591 N N     . PHE B 2 50  ? 134.328 105.672 94.758  1.00 66.58  ? 50  PHE B N     1 
ATOM   3592 C CA    . PHE B 2 50  ? 134.876 104.740 95.728  1.00 66.58  ? 50  PHE B CA    1 
ATOM   3593 C C     . PHE B 2 50  ? 136.171 105.203 96.359  1.00 66.58  ? 50  PHE B C     1 
ATOM   3594 O O     . PHE B 2 50  ? 137.016 105.815 95.717  1.00 66.58  ? 50  PHE B O     1 
ATOM   3595 C CB    . PHE B 2 50  ? 135.110 103.398 95.096  1.00 92.90  ? 50  PHE B CB    1 
ATOM   3596 C CG    . PHE B 2 50  ? 133.858 102.650 94.745  1.00 92.90  ? 50  PHE B CG    1 
ATOM   3597 C CD1   . PHE B 2 50  ? 133.192 102.855 93.557  1.00 92.90  ? 50  PHE B CD1   1 
ATOM   3598 C CD2   . PHE B 2 50  ? 133.376 101.693 95.594  1.00 92.90  ? 50  PHE B CD2   1 
ATOM   3599 C CE1   . PHE B 2 50  ? 132.056 102.127 93.264  1.00 92.90  ? 50  PHE B CE1   1 
ATOM   3600 C CE2   . PHE B 2 50  ? 132.259 100.970 95.310  1.00 92.90  ? 50  PHE B CE2   1 
ATOM   3601 C CZ    . PHE B 2 50  ? 131.596 101.180 94.148  1.00 92.90  ? 50  PHE B CZ    1 
ATOM   3602 N N     . MET B 2 51  ? 136.370 104.827 97.601  1.00 69.88  ? 51  MET B N     1 
ATOM   3603 C CA    . MET B 2 51  ? 137.658 105.062 98.201  1.00 69.88  ? 51  MET B CA    1 
ATOM   3604 C C     . MET B 2 51  ? 138.540 103.935 97.779  1.00 69.88  ? 51  MET B C     1 
ATOM   3605 O O     . MET B 2 51  ? 138.218 102.774 97.998  1.00 69.88  ? 51  MET B O     1 
ATOM   3606 C CB    . MET B 2 51  ? 137.591 105.123 99.707  1.00 100.39 ? 51  MET B CB    1 
ATOM   3607 C CG    . MET B 2 51  ? 138.807 105.782 100.348 1.00 100.39 ? 51  MET B CG    1 
ATOM   3608 S SD    . MET B 2 51  ? 140.279 104.742 100.416 1.00 100.39 ? 51  MET B SD    1 
ATOM   3609 C CE    . MET B 2 51  ? 139.859 103.565 101.695 1.00 100.39 ? 51  MET B CE    1 
ATOM   3610 N N     . LYS B 2 52  ? 139.651 104.266 97.185  1.00 74.98  ? 52  LYS B N     1 
ATOM   3611 C CA    . LYS B 2 52  ? 140.520 103.246 96.634  1.00 74.98  ? 52  LYS B CA    1 
ATOM   3612 C C     . LYS B 2 52  ? 141.451 102.775 97.710  1.00 74.98  ? 52  LYS B C     1 
ATOM   3613 O O     . LYS B 2 52  ? 142.564 103.268 97.837  1.00 74.98  ? 52  LYS B O     1 
ATOM   3614 C CB    . LYS B 2 52  ? 141.337 103.794 95.482  1.00 112.47 ? 52  LYS B CB    1 
ATOM   3615 C CG    . LYS B 2 52  ? 140.532 104.324 94.337  1.00 112.47 ? 52  LYS B CG    1 
ATOM   3616 C CD    . LYS B 2 52  ? 141.432 104.742 93.182  1.00 112.47 ? 52  LYS B CD    1 
ATOM   3617 C CE    . LYS B 2 52  ? 142.434 105.828 93.595  1.00 112.47 ? 52  LYS B CE    1 
ATOM   3618 N NZ    . LYS B 2 52  ? 143.026 106.503 92.414  1.00 112.47 ? 52  LYS B NZ    1 
ATOM   3619 N N     . ALA B 2 53  ? 141.010 101.818 98.482  1.00 77.30  ? 53  ALA B N     1 
ATOM   3620 C CA    . ALA B 2 53  ? 141.892 101.364 99.515  1.00 77.30  ? 53  ALA B CA    1 
ATOM   3621 C C     . ALA B 2 53  ? 143.118 100.731 98.892  1.00 77.30  ? 53  ALA B C     1 
ATOM   3622 O O     . ALA B 2 53  ? 143.046 100.078 97.853  1.00 77.30  ? 53  ALA B O     1 
ATOM   3623 C CB    . ALA B 2 53  ? 141.211 100.354 100.417 1.00 105.41 ? 53  ALA B CB    1 
ATOM   3624 N N     . SER B 2 54  ? 144.250 100.902 99.561  1.00 83.13  ? 54  SER B N     1 
ATOM   3625 C CA    . SER B 2 54  ? 145.474 100.265 99.124  1.00 83.13  ? 54  SER B CA    1 
ATOM   3626 C C     . SER B 2 54  ? 145.369 98.764  99.262  1.00 83.13  ? 54  SER B C     1 
ATOM   3627 O O     . SER B 2 54  ? 146.142 98.021  98.646  1.00 83.13  ? 54  SER B O     1 
ATOM   3628 C CB    . SER B 2 54  ? 146.633 100.786 99.956  1.00 111.97 ? 54  SER B CB    1 
ATOM   3629 O OG    . SER B 2 54  ? 146.483 100.371 101.296 1.00 111.97 ? 54  SER B OG    1 
ATOM   3630 N N     . GLY B 2 55  ? 144.415 98.319  100.054 1.00 79.84  ? 55  GLY B N     1 
ATOM   3631 C CA    . GLY B 2 55  ? 144.139 96.928  100.282 1.00 79.84  ? 55  GLY B CA    1 
ATOM   3632 C C     . GLY B 2 55  ? 143.309 96.334  99.189  1.00 79.84  ? 55  GLY B C     1 
ATOM   3633 O O     . GLY B 2 55  ? 142.978 95.150  99.235  1.00 79.84  ? 55  GLY B O     1 
ATOM   3634 N N     . GLY B 2 56  ? 142.952 97.138  98.194  1.00 78.97  ? 56  GLY B N     1 
ATOM   3635 C CA    . GLY B 2 56  ? 142.167 96.654  97.087  1.00 78.97  ? 56  GLY B CA    1 
ATOM   3636 C C     . GLY B 2 56  ? 140.701 96.727  97.354  1.00 78.97  ? 56  GLY B C     1 
ATOM   3637 O O     . GLY B 2 56  ? 139.898 96.249  96.544  1.00 78.97  ? 56  GLY B O     1 
ATOM   3638 N N     . LYS B 2 57  ? 140.337 97.292  98.474  1.00 74.37  ? 57  LYS B N     1 
ATOM   3639 C CA    . LYS B 2 57  ? 138.954 97.438  98.817  1.00 74.37  ? 57  LYS B CA    1 
ATOM   3640 C C     . LYS B 2 57  ? 138.457 98.744  98.260  1.00 74.37  ? 57  LYS B C     1 
ATOM   3641 O O     . LYS B 2 57  ? 138.972 99.797  98.598  1.00 74.37  ? 57  LYS B O     1 
ATOM   3642 C CB    . LYS B 2 57  ? 138.802 97.412  100.326 1.00 111.55 ? 57  LYS B CB    1 
ATOM   3643 C CG    . LYS B 2 57  ? 137.363 97.447  100.797 1.00 111.55 ? 57  LYS B CG    1 
ATOM   3644 C CD    . LYS B 2 57  ? 137.259 97.402  102.321 1.00 111.55 ? 57  LYS B CD    1 
ATOM   3645 C CE    . LYS B 2 57  ? 135.796 97.410  102.789 1.00 111.55 ? 57  LYS B CE    1 
ATOM   3646 N NZ    . LYS B 2 57  ? 135.676 97.388  104.282 1.00 111.55 ? 57  LYS B NZ    1 
ATOM   3647 N N     . TYR B 2 58  ? 137.456 98.701  97.464  1.00 72.43  ? 58  TYR B N     1 
ATOM   3648 C CA    . TYR B 2 58  ? 136.914 99.937  96.971  1.00 72.43  ? 58  TYR B CA    1 
ATOM   3649 C C     . TYR B 2 58  ? 135.729 100.265 97.836  1.00 72.43  ? 58  TYR B C     1 
ATOM   3650 O O     . TYR B 2 58  ? 134.694 99.606  97.775  1.00 72.43  ? 58  TYR B O     1 
ATOM   3651 C CB    . TYR B 2 58  ? 136.535 99.801  95.516  1.00 100.29 ? 58  TYR B CB    1 
ATOM   3652 C CG    . TYR B 2 58  ? 137.727 99.682  94.651  1.00 100.29 ? 58  TYR B CG    1 
ATOM   3653 C CD1   . TYR B 2 58  ? 138.336 98.452  94.443  1.00 100.29 ? 58  TYR B CD1   1 
ATOM   3654 C CD2   . TYR B 2 58  ? 138.245 100.802 94.031  1.00 100.29 ? 58  TYR B CD2   1 
ATOM   3655 C CE1   . TYR B 2 58  ? 139.432 98.343  93.630  1.00 100.29 ? 58  TYR B CE1   1 
ATOM   3656 C CE2   . TYR B 2 58  ? 139.342 100.707 93.214  1.00 100.29 ? 58  TYR B CE2   1 
ATOM   3657 C CZ    . TYR B 2 58  ? 139.934 99.476  93.016  1.00 100.29 ? 58  TYR B CZ    1 
ATOM   3658 O OH    . TYR B 2 58  ? 141.034 99.376  92.200  1.00 100.29 ? 58  TYR B OH    1 
ATOM   3659 N N     . VAL B 2 59  ? 135.836 101.285 98.647  1.00 67.11  ? 59  VAL B N     1 
ATOM   3660 C CA    . VAL B 2 59  ? 134.795 101.569 99.617  1.00 67.11  ? 59  VAL B CA    1 
ATOM   3661 C C     . VAL B 2 59  ? 133.789 102.520 98.990  1.00 67.11  ? 59  VAL B C     1 
ATOM   3662 O O     . VAL B 2 59  ? 134.152 103.639 98.671  1.00 67.11  ? 59  VAL B O     1 
ATOM   3663 C CB    . VAL B 2 59  ? 135.405 102.183 100.854 1.00 97.61  ? 59  VAL B CB    1 
ATOM   3664 C CG1   . VAL B 2 59  ? 134.336 102.459 101.858 1.00 97.61  ? 59  VAL B CG1   1 
ATOM   3665 C CG2   . VAL B 2 59  ? 136.474 101.266 101.356 1.00 97.61  ? 59  VAL B CG2   1 
ATOM   3666 N N     . PRO B 2 60  ? 132.552 102.124 98.806  1.00 67.22  ? 60  PRO B N     1 
ATOM   3667 C CA    . PRO B 2 60  ? 131.554 103.008 98.240  1.00 67.22  ? 60  PRO B CA    1 
ATOM   3668 C C     . PRO B 2 60  ? 131.448 104.173 99.170  1.00 67.22  ? 60  PRO B C     1 
ATOM   3669 O O     . PRO B 2 60  ? 131.336 103.975 100.373 1.00 67.22  ? 60  PRO B O     1 
ATOM   3670 C CB    . PRO B 2 60  ? 130.301 102.172 98.286  1.00 443.82 ? 60  PRO B CB    1 
ATOM   3671 C CG    . PRO B 2 60  ? 130.564 101.272 99.452  1.00 443.82 ? 60  PRO B CG    1 
ATOM   3672 C CD    . PRO B 2 60  ? 131.988 100.940 99.394  1.00 443.82 ? 60  PRO B CD    1 
ATOM   3673 N N     . ARG B 2 61  ? 131.458 105.382 98.651  1.00 63.39  ? 61  ARG B N     1 
ATOM   3674 C CA    . ARG B 2 61  ? 131.397 106.527 99.543  1.00 63.39  ? 61  ARG B CA    1 
ATOM   3675 C C     . ARG B 2 61  ? 129.978 107.001 99.627  1.00 63.39  ? 61  ARG B C     1 
ATOM   3676 O O     . ARG B 2 61  ? 129.484 107.710 98.753  1.00 63.39  ? 61  ARG B O     1 
ATOM   3677 C CB    . ARG B 2 61  ? 132.343 107.608 99.088  1.00 93.14  ? 61  ARG B CB    1 
ATOM   3678 C CG    . ARG B 2 61  ? 133.748 107.088 99.169  1.00 93.14  ? 61  ARG B CG    1 
ATOM   3679 C CD    . ARG B 2 61  ? 134.778 108.032 98.697  1.00 93.14  ? 61  ARG B CD    1 
ATOM   3680 N NE    . ARG B 2 61  ? 134.579 108.350 97.298  1.00 93.14  ? 61  ARG B NE    1 
ATOM   3681 C CZ    . ARG B 2 61  ? 135.545 108.683 96.462  1.00 93.14  ? 61  ARG B CZ    1 
ATOM   3682 N NH1   . ARG B 2 61  ? 136.811 108.684 96.824  1.00 93.14  ? 61  ARG B NH1   1 
ATOM   3683 N NH2   . ARG B 2 61  ? 135.231 109.032 95.236  1.00 93.14  ? 61  ARG B NH2   1 
ATOM   3684 N N     . ALA B 2 62  ? 129.334 106.597 100.705 1.00 62.53  ? 62  ALA B N     1 
ATOM   3685 C CA    . ALA B 2 62  ? 127.943 106.907 100.912 1.00 62.53  ? 62  ALA B CA    1 
ATOM   3686 C C     . ALA B 2 62  ? 127.580 106.748 102.371 1.00 62.53  ? 62  ALA B C     1 
ATOM   3687 O O     . ALA B 2 62  ? 128.222 106.022 103.118 1.00 62.53  ? 62  ALA B O     1 
ATOM   3688 C CB    . ALA B 2 62  ? 127.051 106.014 100.064 1.00 85.27  ? 62  ALA B CB    1 
ATOM   3689 N N     . LEU B 2 63  ? 126.529 107.425 102.752 1.00 66.42  ? 63  LEU B N     1 
ATOM   3690 C CA    . LEU B 2 63  ? 125.956 107.250 104.057 1.00 66.42  ? 63  LEU B CA    1 
ATOM   3691 C C     . LEU B 2 63  ? 124.603 106.589 103.905 1.00 66.42  ? 63  LEU B C     1 
ATOM   3692 O O     . LEU B 2 63  ? 123.862 106.900 102.974 1.00 66.42  ? 63  LEU B O     1 
ATOM   3693 C CB    . LEU B 2 63  ? 125.794 108.597 104.750 1.00 98.34  ? 63  LEU B CB    1 
ATOM   3694 C CG    . LEU B 2 63  ? 127.007 109.543 104.863 1.00 98.34  ? 63  LEU B CG    1 
ATOM   3695 C CD1   . LEU B 2 63  ? 126.602 110.824 105.571 1.00 98.34  ? 63  LEU B CD1   1 
ATOM   3696 C CD2   . LEU B 2 63  ? 128.142 108.888 105.590 1.00 98.34  ? 63  LEU B CD2   1 
ATOM   3697 N N     . LEU B 2 64  ? 124.253 105.698 104.801 1.00 74.05  ? 64  LEU B N     1 
ATOM   3698 C CA    . LEU B 2 64  ? 122.887 105.191 104.826 1.00 74.05  ? 64  LEU B CA    1 
ATOM   3699 C C     . LEU B 2 64  ? 122.210 105.778 106.056 1.00 74.05  ? 64  LEU B C     1 
ATOM   3700 O O     . LEU B 2 64  ? 122.572 105.439 107.186 1.00 74.05  ? 64  LEU B O     1 
ATOM   3701 C CB    . LEU B 2 64  ? 122.813 103.669 104.868 1.00 109.63 ? 64  LEU B CB    1 
ATOM   3702 C CG    . LEU B 2 64  ? 123.555 102.863 103.820 1.00 109.63 ? 64  LEU B CG    1 
ATOM   3703 C CD1   . LEU B 2 64  ? 123.255 101.379 104.027 1.00 109.63 ? 64  LEU B CD1   1 
ATOM   3704 C CD2   . LEU B 2 64  ? 123.178 103.308 102.423 1.00 109.63 ? 64  LEU B CD2   1 
ATOM   3705 N N     . ILE B 2 65  ? 121.221 106.639 105.856 1.00 81.56  ? 65  ILE B N     1 
ATOM   3706 C CA    . ILE B 2 65  ? 120.621 107.388 106.944 1.00 81.56  ? 65  ILE B CA    1 
ATOM   3707 C C     . ILE B 2 65  ? 119.155 107.073 107.095 1.00 81.56  ? 65  ILE B C     1 
ATOM   3708 O O     . ILE B 2 65  ? 118.385 107.236 106.152 1.00 81.56  ? 65  ILE B O     1 
ATOM   3709 C CB    . ILE B 2 65  ? 120.792 108.868 106.687 1.00 120.75 ? 65  ILE B CB    1 
ATOM   3710 C CG1   . ILE B 2 65  ? 122.275 109.187 106.614 1.00 120.75 ? 65  ILE B CG1   1 
ATOM   3711 C CG2   . ILE B 2 65  ? 120.122 109.635 107.765 1.00 120.75 ? 65  ILE B CG2   1 
ATOM   3712 C CD1   . ILE B 2 65  ? 122.582 110.559 106.077 1.00 120.75 ? 65  ILE B CD1   1 
ATOM   3713 N N     . ASP B 2 66  ? 118.754 106.689 108.292 1.00 98.70  ? 66  ASP B N     1 
ATOM   3714 C CA    . ASP B 2 66  ? 117.341 106.477 108.534 1.00 98.70  ? 66  ASP B CA    1 
ATOM   3715 C C     . ASP B 2 66  ? 116.967 106.685 109.994 1.00 98.70  ? 66  ASP B C     1 
ATOM   3716 O O     . ASP B 2 66  ? 117.787 106.551 110.891 1.00 98.70  ? 66  ASP B O     1 
ATOM   3717 C CB    . ASP B 2 66  ? 116.942 105.080 108.103 1.00 126.90 ? 66  ASP B CB    1 
ATOM   3718 C CG    . ASP B 2 66  ? 115.451 104.915 107.942 1.00 126.90 ? 66  ASP B CG    1 
ATOM   3719 O OD1   . ASP B 2 66  ? 114.685 105.725 108.468 1.00 126.90 ? 66  ASP B OD1   1 
ATOM   3720 O OD2   . ASP B 2 66  ? 115.045 103.965 107.279 1.00 126.90 ? 66  ASP B OD2   1 
ATOM   3721 N N     . LEU B 2 67  ? 115.708 107.014 110.228 1.00 101.33 ? 67  LEU B N     1 
ATOM   3722 C CA    . LEU B 2 67  ? 115.258 107.156 111.589 1.00 101.33 ? 67  LEU B CA    1 
ATOM   3723 C C     . LEU B 2 67  ? 114.893 105.806 112.140 1.00 101.33 ? 67  LEU B C     1 
ATOM   3724 O O     . LEU B 2 67  ? 115.038 105.569 113.338 1.00 101.33 ? 67  LEU B O     1 
ATOM   3725 C CB    . LEU B 2 67  ? 114.070 108.090 111.657 1.00 150.02 ? 67  LEU B CB    1 
ATOM   3726 C CG    . LEU B 2 67  ? 114.270 109.531 111.261 1.00 150.02 ? 67  LEU B CG    1 
ATOM   3727 C CD1   . LEU B 2 67  ? 112.921 110.234 111.272 1.00 150.02 ? 67  LEU B CD1   1 
ATOM   3728 C CD2   . LEU B 2 67  ? 115.189 110.211 112.233 1.00 150.02 ? 67  LEU B CD2   1 
ATOM   3729 N N     . GLU B 2 68  ? 114.439 104.920 111.298 1.00 110.40 ? 68  GLU B N     1 
ATOM   3730 C CA    . GLU B 2 68  ? 114.098 103.573 111.750 1.00 110.40 ? 68  GLU B CA    1 
ATOM   3731 C C     . GLU B 2 68  ? 115.292 102.655 111.586 1.00 110.40 ? 68  GLU B C     1 
ATOM   3732 O O     . GLU B 2 68  ? 115.805 102.529 110.480 1.00 110.40 ? 68  GLU B O     1 
ATOM   3733 C CB    . GLU B 2 68  ? 112.937 102.993 110.960 1.00 148.30 ? 68  GLU B CB    1 
ATOM   3734 C CG    . GLU B 2 68  ? 112.516 101.644 111.493 1.00 148.30 ? 68  GLU B CG    1 
ATOM   3735 C CD    . GLU B 2 68  ? 111.399 100.990 110.733 1.00 148.30 ? 68  GLU B CD    1 
ATOM   3736 O OE1   . GLU B 2 68  ? 110.955 101.528 109.721 1.00 148.30 ? 68  GLU B OE1   1 
ATOM   3737 O OE2   . GLU B 2 68  ? 110.971 99.917  111.159 1.00 148.30 ? 68  GLU B OE2   1 
ATOM   3738 N N     . PRO B 2 69  ? 115.734 101.994 112.606 1.00 114.19 ? 69  PRO B N     1 
ATOM   3739 C CA    . PRO B 2 69  ? 116.891 101.119 112.554 1.00 114.19 ? 69  PRO B CA    1 
ATOM   3740 C C     . PRO B 2 69  ? 116.521 99.803  111.908 1.00 114.19 ? 69  PRO B C     1 
ATOM   3741 O O     . PRO B 2 69  ? 116.526 98.756  112.550 1.00 114.19 ? 69  PRO B O     1 
ATOM   3742 C CB    . PRO B 2 69  ? 117.218 100.940 114.023 1.00 753.97 ? 69  PRO B CB    1 
ATOM   3743 C CG    . PRO B 2 69  ? 115.902 100.978 114.660 1.00 753.97 ? 69  PRO B CG    1 
ATOM   3744 C CD    . PRO B 2 69  ? 115.133 102.020 113.925 1.00 753.97 ? 69  PRO B CD    1 
ATOM   3745 N N     . LYS B 2 70  ? 116.079 99.873  110.662 1.00 112.14 ? 70  LYS B N     1 
ATOM   3746 C CA    . LYS B 2 70  ? 115.670 98.674  109.956 1.00 112.14 ? 70  LYS B CA    1 
ATOM   3747 C C     . LYS B 2 70  ? 116.327 98.510  108.592 1.00 112.14 ? 70  LYS B C     1 
ATOM   3748 O O     . LYS B 2 70  ? 117.137 97.599  108.404 1.00 112.14 ? 70  LYS B O     1 
ATOM   3749 C CB    . LYS B 2 70  ? 114.176 98.694  109.801 1.00 168.21 ? 70  LYS B CB    1 
ATOM   3750 C CG    . LYS B 2 70  ? 113.603 97.488  109.137 1.00 168.21 ? 70  LYS B CG    1 
ATOM   3751 C CD    . LYS B 2 70  ? 112.100 97.638  109.057 1.00 168.21 ? 70  LYS B CD    1 
ATOM   3752 C CE    . LYS B 2 70  ? 111.424 96.458  108.398 1.00 168.21 ? 70  LYS B CE    1 
ATOM   3753 N NZ    . LYS B 2 70  ? 109.960 96.690  108.272 1.00 168.21 ? 70  LYS B NZ    1 
ATOM   3754 N N     . VAL B 2 71  ? 116.062 99.432  107.658 1.00 111.90 ? 71  VAL B N     1 
ATOM   3755 C CA    . VAL B 2 71  ? 116.603 99.296  106.316 1.00 111.90 ? 71  VAL B CA    1 
ATOM   3756 C C     . VAL B 2 71  ? 118.100 99.369  106.359 1.00 111.90 ? 71  VAL B C     1 
ATOM   3757 O O     . VAL B 2 71  ? 118.782 98.755  105.538 1.00 111.90 ? 71  VAL B O     1 
ATOM   3758 C CB    . VAL B 2 71  ? 116.026 100.350 105.369 1.00 162.76 ? 71  VAL B CB    1 
ATOM   3759 C CG1   . VAL B 2 71  ? 116.581 101.707 105.680 1.00 162.76 ? 71  VAL B CG1   1 
ATOM   3760 C CG2   . VAL B 2 71  ? 116.340 99.999  103.942 1.00 162.76 ? 71  VAL B CG2   1 
ATOM   3761 N N     . VAL B 2 72  ? 118.638 100.100 107.311 1.00 110.13 ? 72  VAL B N     1 
ATOM   3762 C CA    . VAL B 2 72  ? 120.076 100.190 107.432 1.00 110.13 ? 72  VAL B CA    1 
ATOM   3763 C C     . VAL B 2 72  ? 120.674 98.865  107.851 1.00 110.13 ? 72  VAL B C     1 
ATOM   3764 O O     . VAL B 2 72  ? 121.791 98.528  107.434 1.00 110.13 ? 72  VAL B O     1 
ATOM   3765 C CB    . VAL B 2 72  ? 120.467 101.305 108.410 1.00 160.19 ? 72  VAL B CB    1 
ATOM   3766 C CG1   . VAL B 2 72  ? 120.087 102.675 107.842 1.00 160.19 ? 72  VAL B CG1   1 
ATOM   3767 C CG2   . VAL B 2 72  ? 119.772 101.089 109.744 1.00 160.19 ? 72  VAL B CG2   1 
ATOM   3768 N N     . ARG B 2 73  ? 119.966 98.092  108.677 1.00 112.58 ? 73  ARG B N     1 
ATOM   3769 C CA    . ARG B 2 73  ? 120.492 96.807  109.103 1.00 112.58 ? 73  ARG B CA    1 
ATOM   3770 C C     . ARG B 2 73  ? 120.274 95.784  108.013 1.00 112.58 ? 73  ARG B C     1 
ATOM   3771 O O     . ARG B 2 73  ? 121.154 94.974  107.735 1.00 112.58 ? 73  ARG B O     1 
ATOM   3772 C CB    . ARG B 2 73  ? 119.849 96.380  110.416 1.00 165.42 ? 73  ARG B CB    1 
ATOM   3773 C CG    . ARG B 2 73  ? 120.287 97.223  111.649 1.00 165.42 ? 73  ARG B CG    1 
ATOM   3774 C CD    . ARG B 2 73  ? 119.516 96.857  112.919 1.00 165.42 ? 73  ARG B CD    1 
ATOM   3775 N NE    . ARG B 2 73  ? 119.976 97.598  114.099 1.00 165.42 ? 73  ARG B NE    1 
ATOM   3776 C CZ    . ARG B 2 73  ? 119.302 97.743  115.243 1.00 165.42 ? 73  ARG B CZ    1 
ATOM   3777 N NH1   . ARG B 2 73  ? 118.097 97.228  115.413 1.00 165.42 ? 73  ARG B NH1   1 
ATOM   3778 N NH2   . ARG B 2 73  ? 119.840 98.445  116.236 1.00 165.42 ? 73  ARG B NH2   1 
ATOM   3779 N N     . GLN B 2 74  ? 119.153 95.855  107.322 1.00 110.13 ? 74  GLN B N     1 
ATOM   3780 C CA    . GLN B 2 74  ? 118.955 94.918  106.238 1.00 110.13 ? 74  GLN B CA    1 
ATOM   3781 C C     . GLN B 2 74  ? 120.006 95.103  105.176 1.00 110.13 ? 74  GLN B C     1 
ATOM   3782 O O     . GLN B 2 74  ? 120.572 94.137  104.682 1.00 110.13 ? 74  GLN B O     1 
ATOM   3783 C CB    . GLN B 2 74  ? 117.588 95.083  105.616 1.00 153.88 ? 74  GLN B CB    1 
ATOM   3784 C CG    . GLN B 2 74  ? 117.348 94.106  104.532 1.00 153.88 ? 74  GLN B CG    1 
ATOM   3785 C CD    . GLN B 2 74  ? 115.996 94.224  103.957 1.00 153.88 ? 74  GLN B CD    1 
ATOM   3786 O OE1   . GLN B 2 74  ? 115.266 95.147  104.274 1.00 153.88 ? 74  GLN B OE1   1 
ATOM   3787 N NE2   . GLN B 2 74  ? 115.635 93.288  103.097 1.00 153.88 ? 74  GLN B NE2   1 
ATOM   3788 N N     . VAL B 2 75  ? 120.323 96.330  104.825 1.00 109.26 ? 75  VAL B N     1 
ATOM   3789 C CA    . VAL B 2 75  ? 121.313 96.482  103.787 1.00 109.26 ? 75  VAL B CA    1 
ATOM   3790 C C     . VAL B 2 75  ? 122.706 96.190  104.312 1.00 109.26 ? 75  VAL B C     1 
ATOM   3791 O O     . VAL B 2 75  ? 123.468 95.467  103.665 1.00 109.26 ? 75  VAL B O     1 
ATOM   3792 C CB    . VAL B 2 75  ? 121.204 97.860  103.139 1.00 158.92 ? 75  VAL B CB    1 
ATOM   3793 C CG1   . VAL B 2 75  ? 122.351 98.079  102.171 1.00 158.92 ? 75  VAL B CG1   1 
ATOM   3794 C CG2   . VAL B 2 75  ? 119.887 97.926  102.393 1.00 158.92 ? 75  VAL B CG2   1 
ATOM   3795 N N     . GLY B 2 76  ? 123.064 96.711  105.480 1.00 110.33 ? 76  GLY B N     1 
ATOM   3796 C CA    . GLY B 2 76  ? 124.392 96.485  106.010 1.00 110.33 ? 76  GLY B CA    1 
ATOM   3797 C C     . GLY B 2 76  ? 124.700 95.038  106.316 1.00 110.33 ? 76  GLY B C     1 
ATOM   3798 O O     . GLY B 2 76  ? 125.846 94.606  106.181 1.00 110.33 ? 76  GLY B O     1 
ATOM   3799 N N     . ASN B 2 77  ? 123.692 94.263  106.697 1.00 110.02 ? 77  ASN B N     1 
ATOM   3800 C CA    . ASN B 2 77  ? 123.910 92.871  107.040 1.00 110.02 ? 77  ASN B CA    1 
ATOM   3801 C C     . ASN B 2 77  ? 123.446 91.854  106.019 1.00 110.02 ? 77  ASN B C     1 
ATOM   3802 O O     . ASN B 2 77  ? 123.975 90.740  106.033 1.00 110.02 ? 77  ASN B O     1 
ATOM   3803 C CB    . ASN B 2 77  ? 123.229 92.541  108.344 1.00 149.06 ? 77  ASN B CB    1 
ATOM   3804 C CG    . ASN B 2 77  ? 123.821 93.289  109.494 1.00 149.06 ? 77  ASN B CG    1 
ATOM   3805 O OD1   . ASN B 2 77  ? 125.033 93.516  109.568 1.00 149.06 ? 77  ASN B OD1   1 
ATOM   3806 N ND2   . ASN B 2 77  ? 122.969 93.685  110.413 1.00 149.06 ? 77  ASN B ND2   1 
ATOM   3807 N N     . GLU B 2 78  ? 122.483 92.152  105.145 1.00 108.17 ? 78  GLU B N     1 
ATOM   3808 C CA    . GLU B 2 78  ? 121.983 91.116  104.243 1.00 108.17 ? 78  GLU B CA    1 
ATOM   3809 C C     . GLU B 2 78  ? 122.135 91.414  102.755 1.00 108.17 ? 78  GLU B C     1 
ATOM   3810 O O     . GLU B 2 78  ? 122.576 90.542  102.000 1.00 108.17 ? 78  GLU B O     1 
ATOM   3811 C CB    . GLU B 2 78  ? 120.503 90.841  104.527 1.00 145.30 ? 78  GLU B CB    1 
ATOM   3812 C CG    . GLU B 2 78  ? 120.208 90.311  105.922 1.00 145.30 ? 78  GLU B CG    1 
ATOM   3813 C CD    . GLU B 2 78  ? 118.728 90.088  106.159 1.00 145.30 ? 78  GLU B CD    1 
ATOM   3814 O OE1   . GLU B 2 78  ? 117.933 90.370  105.258 1.00 145.30 ? 78  GLU B OE1   1 
ATOM   3815 O OE2   . GLU B 2 78  ? 118.364 89.632  107.245 1.00 145.30 ? 78  GLU B OE2   1 
ATOM   3816 N N     . GLN B 2 79  ? 121.744 92.596  102.286 1.00 100.83 ? 79  GLN B N     1 
ATOM   3817 C CA    . GLN B 2 79  ? 121.730 92.800  100.839 1.00 100.83 ? 79  GLN B CA    1 
ATOM   3818 C C     . GLN B 2 79  ? 123.087 93.160  100.280 1.00 100.83 ? 79  GLN B C     1 
ATOM   3819 O O     . GLN B 2 79  ? 123.456 92.691  99.209  1.00 100.83 ? 79  GLN B O     1 
ATOM   3820 C CB    . GLN B 2 79  ? 120.725 93.875  100.453 1.00 140.89 ? 79  GLN B CB    1 
ATOM   3821 C CG    . GLN B 2 79  ? 119.309 93.430  100.627 1.00 140.89 ? 79  GLN B CG    1 
ATOM   3822 C CD    . GLN B 2 79  ? 118.975 92.285  99.712  1.00 140.89 ? 79  GLN B CD    1 
ATOM   3823 O OE1   . GLN B 2 79  ? 119.231 92.332  98.500  1.00 140.89 ? 79  GLN B OE1   1 
ATOM   3824 N NE2   . GLN B 2 79  ? 118.418 91.232  100.286 1.00 140.89 ? 79  GLN B NE2   1 
ATOM   3825 N N     . LEU B 2 80  ? 123.838 93.974  100.958 1.00 93.40  ? 80  LEU B N     1 
ATOM   3826 C CA    . LEU B 2 80  ? 125.173 94.300  100.502 1.00 93.40  ? 80  LEU B CA    1 
ATOM   3827 C C     . LEU B 2 80  ? 126.067 94.128  101.695 1.00 93.40  ? 80  LEU B C     1 
ATOM   3828 O O     . LEU B 2 80  ? 126.651 95.086  102.196 1.00 93.40  ? 80  LEU B O     1 
ATOM   3829 C CB    . LEU B 2 80  ? 125.255 95.713  99.935  1.00 138.28 ? 80  LEU B CB    1 
ATOM   3830 C CG    . LEU B 2 80  ? 124.604 95.974  98.575  1.00 138.28 ? 80  LEU B CG    1 
ATOM   3831 C CD1   . LEU B 2 80  ? 123.187 96.411  98.752  1.00 138.28 ? 80  LEU B CD1   1 
ATOM   3832 C CD2   . LEU B 2 80  ? 125.363 97.037  97.799  1.00 138.28 ? 80  LEU B CD2   1 
ATOM   3833 N N     . PRO B 2 81  ? 126.154 92.931  102.197 1.00 93.45  ? 81  PRO B N     1 
ATOM   3834 C CA    . PRO B 2 81  ? 126.791 92.703  103.465 1.00 93.45  ? 81  PRO B CA    1 
ATOM   3835 C C     . PRO B 2 81  ? 128.209 93.119  103.362 1.00 93.45  ? 81  PRO B C     1 
ATOM   3836 O O     . PRO B 2 81  ? 128.873 92.807  102.392 1.00 93.45  ? 81  PRO B O     1 
ATOM   3837 C CB    . PRO B 2 81  ? 126.675 91.205  103.637 1.00 617.02 ? 81  PRO B CB    1 
ATOM   3838 C CG    . PRO B 2 81  ? 126.583 90.695  102.257 1.00 617.02 ? 81  PRO B CG    1 
ATOM   3839 C CD    . PRO B 2 81  ? 125.851 91.716  101.482 1.00 617.02 ? 81  PRO B CD    1 
ATOM   3840 N N     . SER B 2 82  ? 128.669 93.821  104.362 1.00 87.61  ? 82  SER B N     1 
ATOM   3841 C CA    . SER B 2 82  ? 130.059 94.235  104.495 1.00 87.61  ? 82  SER B CA    1 
ATOM   3842 C C     . SER B 2 82  ? 130.537 95.177  103.403 1.00 87.61  ? 82  SER B C     1 
ATOM   3843 O O     . SER B 2 82  ? 131.736 95.452  103.308 1.00 87.61  ? 82  SER B O     1 
ATOM   3844 C CB    . SER B 2 82  ? 130.980 93.037  104.535 1.00 118.01 ? 82  SER B CB    1 
ATOM   3845 O OG    . SER B 2 82  ? 130.640 92.177  105.591 1.00 118.01 ? 82  SER B OG    1 
ATOM   3846 N N     . PHE B 2 83  ? 129.637 95.689  102.590 1.00 84.79  ? 83  PHE B N     1 
ATOM   3847 C CA    . PHE B 2 83  ? 130.000 96.584  101.511 1.00 84.79  ? 83  PHE B CA    1 
ATOM   3848 C C     . PHE B 2 83  ? 130.160 97.993  102.004 1.00 84.79  ? 83  PHE B C     1 
ATOM   3849 O O     . PHE B 2 83  ? 131.188 98.623  101.778 1.00 84.79  ? 83  PHE B O     1 
ATOM   3850 C CB    . PHE B 2 83  ? 128.912 96.493  100.472 1.00 118.31 ? 83  PHE B CB    1 
ATOM   3851 C CG    . PHE B 2 83  ? 129.063 97.367  99.341  1.00 118.31 ? 83  PHE B CG    1 
ATOM   3852 C CD1   . PHE B 2 83  ? 130.015 97.145  98.383  1.00 118.31 ? 83  PHE B CD1   1 
ATOM   3853 C CD2   . PHE B 2 83  ? 128.183 98.371  99.179  1.00 118.31 ? 83  PHE B CD2   1 
ATOM   3854 C CE1   . PHE B 2 83  ? 130.093 97.967  97.298  1.00 118.31 ? 83  PHE B CE1   1 
ATOM   3855 C CE2   . PHE B 2 83  ? 128.241 99.191  98.107  1.00 118.31 ? 83  PHE B CE2   1 
ATOM   3856 C CZ    . PHE B 2 83  ? 129.198 98.993  97.157  1.00 118.31 ? 83  PHE B CZ    1 
ATOM   3857 N N     . PHE B 2 84  ? 129.158 98.508  102.683 1.00 84.22  ? 84  PHE B N     1 
ATOM   3858 C CA    . PHE B 2 84  ? 129.201 99.863  103.173 1.00 84.22  ? 84  PHE B CA    1 
ATOM   3859 C C     . PHE B 2 84  ? 129.956 99.859  104.485 1.00 84.22  ? 84  PHE B C     1 
ATOM   3860 O O     . PHE B 2 84  ? 129.789 98.941  105.290 1.00 84.22  ? 84  PHE B O     1 
ATOM   3861 C CB    . PHE B 2 84  ? 127.813 100.367 103.404 1.00 117.52 ? 84  PHE B CB    1 
ATOM   3862 C CG    . PHE B 2 84  ? 127.018 100.483 102.224 1.00 117.52 ? 84  PHE B CG    1 
ATOM   3863 C CD1   . PHE B 2 84  ? 127.138 101.542 101.420 1.00 117.52 ? 84  PHE B CD1   1 
ATOM   3864 C CD2   . PHE B 2 84  ? 126.085 99.586  101.948 1.00 117.52 ? 84  PHE B CD2   1 
ATOM   3865 C CE1   . PHE B 2 84  ? 126.349 101.667 100.339 1.00 117.52 ? 84  PHE B CE1   1 
ATOM   3866 C CE2   . PHE B 2 84  ? 125.295 99.703  100.881 1.00 117.52 ? 84  PHE B CE2   1 
ATOM   3867 C CZ    . PHE B 2 84  ? 125.415 100.726 100.071 1.00 117.52 ? 84  PHE B CZ    1 
ATOM   3868 N N     . ASP B 2 85  ? 130.764 100.883 104.715 1.00 87.63  ? 85  ASP B N     1 
ATOM   3869 C CA    . ASP B 2 85  ? 131.529 101.014 105.966 1.00 87.63  ? 85  ASP B CA    1 
ATOM   3870 C C     . ASP B 2 85  ? 130.604 101.317 107.139 1.00 87.63  ? 85  ASP B C     1 
ATOM   3871 O O     . ASP B 2 85  ? 129.944 102.357 107.126 1.00 87.63  ? 85  ASP B O     1 
ATOM   3872 C CB    . ASP B 2 85  ? 132.570 102.117 105.815 1.00 112.67 ? 85  ASP B CB    1 
ATOM   3873 C CG    . ASP B 2 85  ? 133.486 102.277 107.039 1.00 112.67 ? 85  ASP B CG    1 
ATOM   3874 O OD1   . ASP B 2 85  ? 133.104 101.948 108.178 1.00 112.67 ? 85  ASP B OD1   1 
ATOM   3875 O OD2   . ASP B 2 85  ? 134.612 102.773 106.856 1.00 112.67 ? 85  ASP B OD2   1 
ATOM   3876 N N     . PRO B 2 86  ? 130.572 100.468 108.177 1.00 88.54  ? 86  PRO B N     1 
ATOM   3877 C CA    . PRO B 2 86  ? 129.648 100.582 109.310 1.00 88.54  ? 86  PRO B CA    1 
ATOM   3878 C C     . PRO B 2 86  ? 129.597 101.926 109.962 1.00 88.54  ? 86  PRO B C     1 
ATOM   3879 O O     . PRO B 2 86  ? 128.552 102.327 110.467 1.00 88.54  ? 86  PRO B O     1 
ATOM   3880 C CB    . PRO B 2 86  ? 130.224 99.563  110.282 1.00 584.62 ? 86  PRO B CB    1 
ATOM   3881 C CG    . PRO B 2 86  ? 130.842 98.554  109.416 1.00 584.62 ? 86  PRO B CG    1 
ATOM   3882 C CD    . PRO B 2 86  ? 131.419 99.294  108.276 1.00 584.62 ? 86  PRO B CD    1 
ATOM   3883 N N     . LYS B 2 87  ? 130.697 102.653 109.990 1.00 84.87  ? 87  LYS B N     1 
ATOM   3884 C CA    . LYS B 2 87  ? 130.631 103.939 110.656 1.00 84.87  ? 87  LYS B CA    1 
ATOM   3885 C C     . LYS B 2 87  ? 129.723 104.893 109.929 1.00 84.87  ? 87  LYS B C     1 
ATOM   3886 O O     . LYS B 2 87  ? 129.280 105.875 110.510 1.00 84.87  ? 87  LYS B O     1 
ATOM   3887 C CB    . LYS B 2 87  ? 132.019 104.534 110.796 1.00 127.30 ? 87  LYS B CB    1 
ATOM   3888 C CG    . LYS B 2 87  ? 132.669 104.893 109.481 1.00 127.30 ? 87  LYS B CG    1 
ATOM   3889 C CD    . LYS B 2 87  ? 134.098 105.464 109.631 1.00 127.30 ? 87  LYS B CD    1 
ATOM   3890 C CE    . LYS B 2 87  ? 135.136 104.442 110.178 1.00 127.30 ? 87  LYS B CE    1 
ATOM   3891 N NZ    . LYS B 2 87  ? 135.301 103.216 109.326 1.00 127.30 ? 87  LYS B NZ    1 
ATOM   3892 N N     . ASN B 2 88  ? 129.412 104.605 108.690 1.00 84.21  ? 88  ASN B N     1 
ATOM   3893 C CA    . ASN B 2 88  ? 128.576 105.459 107.889 1.00 84.21  ? 88  ASN B CA    1 
ATOM   3894 C C     . ASN B 2 88  ? 127.150 104.987 107.864 1.00 84.21  ? 88  ASN B C     1 
ATOM   3895 O O     . ASN B 2 88  ? 126.342 105.506 107.091 1.00 84.21  ? 88  ASN B O     1 
ATOM   3896 C CB    . ASN B 2 88  ? 129.128 105.559 106.474 1.00 114.09 ? 88  ASN B CB    1 
ATOM   3897 C CG    . ASN B 2 88  ? 130.372 106.408 106.395 1.00 114.09 ? 88  ASN B CG    1 
ATOM   3898 O OD1   . ASN B 2 88  ? 130.596 107.289 107.230 1.00 114.09 ? 88  ASN B OD1   1 
ATOM   3899 N ND2   . ASN B 2 88  ? 131.176 106.171 105.379 1.00 114.09 ? 88  ASN B ND2   1 
ATOM   3900 N N     . LEU B 2 89  ? 126.815 104.029 108.666 1.00 90.27  ? 89  LEU B N     1 
ATOM   3901 C CA    . LEU B 2 89  ? 125.440 103.629 108.765 1.00 90.27  ? 89  LEU B CA    1 
ATOM   3902 C C     . LEU B 2 89  ? 124.900 104.343 109.982 1.00 90.27  ? 89  LEU B C     1 
ATOM   3903 O O     . LEU B 2 89  ? 125.318 104.091 111.115 1.00 90.27  ? 89  LEU B O     1 
ATOM   3904 C CB    . LEU B 2 89  ? 125.305 102.121 108.853 1.00 133.65 ? 89  LEU B CB    1 
ATOM   3905 C CG    . LEU B 2 89  ? 125.284 101.393 107.508 1.00 133.65 ? 89  LEU B CG    1 
ATOM   3906 C CD1   . LEU B 2 89  ? 126.587 101.545 106.738 1.00 133.65 ? 89  LEU B CD1   1 
ATOM   3907 C CD2   . LEU B 2 89  ? 124.985 99.927  107.731 1.00 133.65 ? 89  LEU B CD2   1 
ATOM   3908 N N     . ILE B 2 90  ? 124.004 105.269 109.744 1.00 92.91  ? 90  ILE B N     1 
ATOM   3909 C CA    . ILE B 2 90  ? 123.570 106.203 110.751 1.00 92.91  ? 90  ILE B CA    1 
ATOM   3910 C C     . ILE B 2 90  ? 122.090 106.020 110.976 1.00 92.91  ? 90  ILE B C     1 
ATOM   3911 O O     . ILE B 2 90  ? 121.308 106.150 110.035 1.00 92.91  ? 90  ILE B O     1 
ATOM   3912 C CB    . ILE B 2 90  ? 123.849 107.618 110.278 1.00 137.55 ? 90  ILE B CB    1 
ATOM   3913 C CG1   . ILE B 2 90  ? 125.332 107.763 109.916 1.00 137.55 ? 90  ILE B CG1   1 
ATOM   3914 C CG2   . ILE B 2 90  ? 123.438 108.605 111.338 1.00 137.55 ? 90  ILE B CG2   1 
ATOM   3915 C CD1   . ILE B 2 90  ? 125.648 108.996 109.079 1.00 137.55 ? 90  ILE B CD1   1 
ATOM   3916 N N     . HIS B 2 91  ? 121.681 105.765 112.211 1.00 106.35 ? 91  HIS B N     1 
ATOM   3917 C CA    . HIS B 2 91  ? 120.251 105.643 112.374 1.00 106.35 ? 91  HIS B CA    1 
ATOM   3918 C C     . HIS B 2 91  ? 119.731 106.082 113.724 1.00 106.35 ? 91  HIS B C     1 
ATOM   3919 O O     . HIS B 2 91  ? 120.442 106.125 114.728 1.00 106.35 ? 91  HIS B O     1 
ATOM   3920 C CB    . HIS B 2 91  ? 119.789 104.242 112.117 1.00 144.64 ? 91  HIS B CB    1 
ATOM   3921 C CG    . HIS B 2 91  ? 120.336 103.259 113.061 1.00 144.64 ? 91  HIS B CG    1 
ATOM   3922 N ND1   . HIS B 2 91  ? 119.835 103.105 114.318 1.00 144.64 ? 91  HIS B ND1   1 
ATOM   3923 C CD2   . HIS B 2 91  ? 121.328 102.360 112.932 1.00 144.64 ? 91  HIS B CD2   1 
ATOM   3924 C CE1   . HIS B 2 91  ? 120.496 102.151 114.935 1.00 144.64 ? 91  HIS B CE1   1 
ATOM   3925 N NE2   . HIS B 2 91  ? 121.406 101.677 114.114 1.00 144.64 ? 91  HIS B NE2   1 
ATOM   3926 N N     . GLY B 2 92  ? 118.445 106.380 113.711 1.00 111.61 ? 92  GLY B N     1 
ATOM   3927 C CA    . GLY B 2 92  ? 117.682 106.732 114.890 1.00 111.61 ? 92  GLY B CA    1 
ATOM   3928 C C     . GLY B 2 92  ? 117.009 105.526 115.527 1.00 111.61 ? 92  GLY B C     1 
ATOM   3929 O O     . GLY B 2 92  ? 117.421 104.379 115.335 1.00 111.61 ? 92  GLY B O     1 
ATOM   3930 N N     . LEU B 2 93  ? 115.988 105.796 116.344 1.00 115.52 ? 93  LEU B N     1 
ATOM   3931 C CA    . LEU B 2 93  ? 115.297 104.748 117.061 1.00 115.52 ? 93  LEU B CA    1 
ATOM   3932 C C     . LEU B 2 93  ? 113.846 104.592 116.691 1.00 115.52 ? 93  LEU B C     1 
ATOM   3933 O O     . LEU B 2 93  ? 113.311 103.489 116.765 1.00 115.52 ? 93  LEU B O     1 
ATOM   3934 C CB    . LEU B 2 93  ? 115.397 105.016 118.546 1.00 171.03 ? 93  LEU B CB    1 
ATOM   3935 C CG    . LEU B 2 93  ? 116.818 105.080 119.096 1.00 171.03 ? 93  LEU B CG    1 
ATOM   3936 C CD1   . LEU B 2 93  ? 116.715 105.440 120.558 1.00 171.03 ? 93  LEU B CD1   1 
ATOM   3937 C CD2   . LEU B 2 93  ? 117.541 103.764 118.916 1.00 171.03 ? 93  LEU B CD2   1 
ATOM   3938 N N     . TYR B 2 94  ? 113.211 105.649 116.285 1.00 116.08 ? 94  TYR B N     1 
ATOM   3939 C CA    . TYR B 2 94  ? 111.800 105.666 115.998 1.00 116.08 ? 94  TYR B CA    1 
ATOM   3940 C C     . TYR B 2 94  ? 111.636 106.256 114.630 1.00 116.08 ? 94  TYR B C     1 
ATOM   3941 O O     . TYR B 2 94  ? 112.370 107.163 114.284 1.00 116.08 ? 94  TYR B O     1 
ATOM   3942 C CB    . TYR B 2 94  ? 111.058 106.591 116.936 1.00 160.73 ? 94  TYR B CB    1 
ATOM   3943 C CG    . TYR B 2 94  ? 111.273 106.382 118.396 1.00 160.73 ? 94  TYR B CG    1 
ATOM   3944 C CD1   . TYR B 2 94  ? 112.340 106.963 119.029 1.00 160.73 ? 94  TYR B CD1   1 
ATOM   3945 C CD2   . TYR B 2 94  ? 110.394 105.641 119.136 1.00 160.73 ? 94  TYR B CD2   1 
ATOM   3946 C CE1   . TYR B 2 94  ? 112.547 106.805 120.352 1.00 160.73 ? 94  TYR B CE1   1 
ATOM   3947 C CE2   . TYR B 2 94  ? 110.593 105.475 120.472 1.00 160.73 ? 94  TYR B CE2   1 
ATOM   3948 C CZ    . TYR B 2 94  ? 111.679 106.066 121.074 1.00 160.73 ? 94  TYR B CZ    1 
ATOM   3949 O OH    . TYR B 2 94  ? 111.889 105.902 122.419 1.00 160.73 ? 94  TYR B OH    1 
ATOM   3950 N N     . GLY B 2 95  ? 110.670 105.797 113.860 1.00 105.70 ? 95  GLY B N     1 
ATOM   3951 C CA    . GLY B 2 95  ? 110.423 106.418 112.575 1.00 105.70 ? 95  GLY B CA    1 
ATOM   3952 C C     . GLY B 2 95  ? 109.350 107.464 112.716 1.00 105.70 ? 95  GLY B C     1 
ATOM   3953 O O     . GLY B 2 95  ? 108.784 107.639 113.776 1.00 105.70 ? 95  GLY B O     1 
ATOM   3954 N N     . GLY B 2 96  ? 109.047 108.154 111.647 1.00 99.66  ? 96  GLY B N     1 
ATOM   3955 C CA    . GLY B 2 96  ? 107.988 109.125 111.684 1.00 99.66  ? 96  GLY B CA    1 
ATOM   3956 C C     . GLY B 2 96  ? 106.748 108.454 111.158 1.00 99.66  ? 96  GLY B C     1 
ATOM   3957 O O     . GLY B 2 96  ? 106.818 107.602 110.309 1.00 99.66  ? 96  GLY B O     1 
ATOM   3958 N N     . ALA B 2 97  ? 105.600 108.867 111.642 1.00 96.16  ? 97  ALA B N     1 
ATOM   3959 C CA    . ALA B 2 97  ? 104.363 108.257 111.173 1.00 96.16  ? 97  ALA B CA    1 
ATOM   3960 C C     . ALA B 2 97  ? 103.902 108.969 109.914 1.00 96.16  ? 97  ALA B C     1 
ATOM   3961 O O     . ALA B 2 97  ? 102.870 109.630 109.897 1.00 96.16  ? 97  ALA B O     1 
ATOM   3962 C CB    . ALA B 2 97  ? 103.289 108.321 112.243 1.00 131.13 ? 97  ALA B CB    1 
ATOM   3963 N N     . ASN B 2 98  ? 104.695 108.835 108.874 1.00 91.90  ? 98  ASN B N     1 
ATOM   3964 C CA    . ASN B 2 98  ? 104.416 109.490 107.631 1.00 91.90  ? 98  ASN B CA    1 
ATOM   3965 C C     . ASN B 2 98  ? 104.277 110.980 107.816 1.00 91.90  ? 98  ASN B C     1 
ATOM   3966 O O     . ASN B 2 98  ? 103.485 111.617 107.126 1.00 91.90  ? 98  ASN B O     1 
ATOM   3967 C CB    . ASN B 2 98  ? 103.161 108.988 106.983 1.00 124.51 ? 98  ASN B CB    1 
ATOM   3968 C CG    . ASN B 2 98  ? 103.259 107.621 106.585 1.00 124.51 ? 98  ASN B CG    1 
ATOM   3969 O OD1   . ASN B 2 98  ? 104.249 107.202 105.993 1.00 124.51 ? 98  ASN B OD1   1 
ATOM   3970 N ND2   . ASN B 2 98  ? 102.234 106.868 106.883 1.00 124.51 ? 98  ASN B ND2   1 
ATOM   3971 N N     . SER B 2 99  ? 105.068 111.571 108.705 1.00 97.83  ? 99  SER B N     1 
ATOM   3972 C CA    . SER B 2 99  ? 104.895 112.994 108.981 1.00 97.83  ? 99  SER B CA    1 
ATOM   3973 C C     . SER B 2 99  ? 106.180 113.784 108.857 1.00 97.83  ? 99  SER B C     1 
ATOM   3974 O O     . SER B 2 99  ? 107.120 113.579 109.628 1.00 97.83  ? 99  SER B O     1 
ATOM   3975 C CB    . SER B 2 99  ? 104.313 113.205 110.361 1.00 131.77 ? 99  SER B CB    1 
ATOM   3976 O OG    . SER B 2 99  ? 104.251 114.583 110.647 1.00 131.77 ? 99  SER B OG    1 
ATOM   3977 N N     . PHE B 2 100 ? 106.181 114.708 107.901 1.00 96.19  ? 100 PHE B N     1 
ATOM   3978 C CA    . PHE B 2 100 ? 107.328 115.551 107.671 1.00 96.19  ? 100 PHE B CA    1 
ATOM   3979 C C     . PHE B 2 100 ? 107.681 116.197 108.958 1.00 96.19  ? 100 PHE B C     1 
ATOM   3980 O O     . PHE B 2 100 ? 108.843 116.267 109.337 1.00 96.19  ? 100 PHE B O     1 
ATOM   3981 C CB    . PHE B 2 100 ? 107.015 116.623 106.636 1.00 134.22 ? 100 PHE B CB    1 
ATOM   3982 C CG    . PHE B 2 100 ? 108.192 117.492 106.229 1.00 134.22 ? 100 PHE B CG    1 
ATOM   3983 C CD1   . PHE B 2 100 ? 108.662 118.535 107.014 1.00 134.22 ? 100 PHE B CD1   1 
ATOM   3984 C CD2   . PHE B 2 100 ? 108.804 117.279 105.020 1.00 134.22 ? 100 PHE B CD2   1 
ATOM   3985 C CE1   . PHE B 2 100 ? 109.697 119.326 106.600 1.00 134.22 ? 100 PHE B CE1   1 
ATOM   3986 C CE2   . PHE B 2 100 ? 109.849 118.067 104.620 1.00 134.22 ? 100 PHE B CE2   1 
ATOM   3987 C CZ    . PHE B 2 100 ? 110.284 119.090 105.415 1.00 134.22 ? 100 PHE B CZ    1 
ATOM   3988 N N     . ALA B 2 101 ? 106.683 116.684 109.651 1.00 104.46 ? 101 ALA B N     1 
ATOM   3989 C CA    . ALA B 2 101 ? 107.005 117.403 110.848 1.00 104.46 ? 101 ALA B CA    1 
ATOM   3990 C C     . ALA B 2 101 ? 107.785 116.540 111.791 1.00 104.46 ? 101 ALA B C     1 
ATOM   3991 O O     . ALA B 2 101 ? 108.641 117.038 112.503 1.00 104.46 ? 101 ALA B O     1 
ATOM   3992 C CB    . ALA B 2 101 ? 105.762 117.907 111.536 1.00 142.45 ? 101 ALA B CB    1 
ATOM   3993 N N     . LYS B 2 102 ? 107.506 115.258 111.850 1.00 102.65 ? 102 LYS B N     1 
ATOM   3994 C CA    . LYS B 2 102 ? 108.291 114.533 112.818 1.00 102.65 ? 102 LYS B CA    1 
ATOM   3995 C C     . LYS B 2 102 ? 109.682 114.377 112.298 1.00 102.65 ? 102 LYS B C     1 
ATOM   3996 O O     . LYS B 2 102 ? 110.641 114.589 113.028 1.00 102.65 ? 102 LYS B O     1 
ATOM   3997 C CB    . LYS B 2 102 ? 107.654 113.199 113.190 1.00 153.97 ? 102 LYS B CB    1 
ATOM   3998 C CG    . LYS B 2 102 ? 106.438 113.389 114.091 1.00 153.97 ? 102 LYS B CG    1 
ATOM   3999 C CD    . LYS B 2 102 ? 105.790 112.095 114.558 1.00 153.97 ? 102 LYS B CD    1 
ATOM   4000 C CE    . LYS B 2 102 ? 104.621 112.418 115.506 1.00 153.97 ? 102 LYS B CE    1 
ATOM   4001 N NZ    . LYS B 2 102 ? 103.964 111.202 116.070 1.00 153.97 ? 102 LYS B NZ    1 
ATOM   4002 N N     . GLY B 2 103 ? 109.807 114.101 111.020 1.00 109.84 ? 103 GLY B N     1 
ATOM   4003 C CA    . GLY B 2 103 ? 111.119 113.897 110.444 1.00 109.84 ? 103 GLY B CA    1 
ATOM   4004 C C     . GLY B 2 103 ? 111.995 115.127 110.504 1.00 109.84 ? 103 GLY B C     1 
ATOM   4005 O O     . GLY B 2 103 ? 113.216 115.021 110.609 1.00 109.84 ? 103 GLY B O     1 
ATOM   4006 N N     . TYR B 2 104 ? 111.393 116.300 110.450 1.00 110.71 ? 104 TYR B N     1 
ATOM   4007 C CA    . TYR B 2 104 ? 112.105 117.569 110.431 1.00 110.71 ? 104 TYR B CA    1 
ATOM   4008 C C     . TYR B 2 104 ? 112.203 118.284 111.776 1.00 110.71 ? 104 TYR B C     1 
ATOM   4009 O O     . TYR B 2 104 ? 113.238 118.886 112.072 1.00 110.71 ? 104 TYR B O     1 
ATOM   4010 C CB    . TYR B 2 104 ? 111.445 118.480 109.427 1.00 153.29 ? 104 TYR B CB    1 
ATOM   4011 C CG    . TYR B 2 104 ? 112.023 119.812 109.406 1.00 153.29 ? 104 TYR B CG    1 
ATOM   4012 C CD1   . TYR B 2 104 ? 113.278 120.023 108.919 1.00 153.29 ? 104 TYR B CD1   1 
ATOM   4013 C CD2   . TYR B 2 104 ? 111.317 120.859 109.854 1.00 153.29 ? 104 TYR B CD2   1 
ATOM   4014 C CE1   . TYR B 2 104 ? 113.803 121.264 108.904 1.00 153.29 ? 104 TYR B CE1   1 
ATOM   4015 C CE2   . TYR B 2 104 ? 111.823 122.093 109.836 1.00 153.29 ? 104 TYR B CE2   1 
ATOM   4016 C CZ    . TYR B 2 104 ? 113.065 122.300 109.367 1.00 153.29 ? 104 TYR B CZ    1 
ATOM   4017 O OH    . TYR B 2 104 ? 113.568 123.570 109.369 1.00 153.29 ? 104 TYR B OH    1 
ATOM   4018 N N     . LEU B 2 105 ? 111.152 118.272 112.587 1.00 115.67 ? 105 LEU B N     1 
ATOM   4019 C CA    . LEU B 2 105 ? 111.123 118.993 113.853 1.00 115.67 ? 105 LEU B CA    1 
ATOM   4020 C C     . LEU B 2 105 ? 111.383 118.133 115.088 1.00 115.67 ? 105 LEU B C     1 
ATOM   4021 O O     . LEU B 2 105 ? 111.746 118.679 116.133 1.00 115.67 ? 105 LEU B O     1 
ATOM   4022 C CB    . LEU B 2 105 ? 109.760 119.664 114.045 1.00 171.25 ? 105 LEU B CB    1 
ATOM   4023 C CG    . LEU B 2 105 ? 109.307 120.678 113.007 1.00 171.25 ? 105 LEU B CG    1 
ATOM   4024 C CD1   . LEU B 2 105 ? 107.907 121.136 113.352 1.00 171.25 ? 105 LEU B CD1   1 
ATOM   4025 C CD2   . LEU B 2 105 ? 110.250 121.853 112.974 1.00 171.25 ? 105 LEU B CD2   1 
ATOM   4026 N N     . GLY B 2 106 ? 111.144 116.826 115.022 1.00 115.63 ? 106 GLY B N     1 
ATOM   4027 C CA    . GLY B 2 106 ? 111.218 115.980 116.195 1.00 115.63 ? 106 GLY B CA    1 
ATOM   4028 C C     . GLY B 2 106 ? 112.414 115.070 116.159 1.00 115.63 ? 106 GLY B C     1 
ATOM   4029 O O     . GLY B 2 106 ? 113.536 115.482 116.467 1.00 115.63 ? 106 GLY B O     1 
ATOM   4030 N N     . GLU B 2 107 ? 112.180 113.816 115.823 1.00 113.85 ? 107 GLU B N     1 
ATOM   4031 C CA    . GLU B 2 107 ? 113.289 112.906 115.750 1.00 113.85 ? 107 GLU B CA    1 
ATOM   4032 C C     . GLU B 2 107 ? 114.184 113.458 114.682 1.00 113.85 ? 107 GLU B C     1 
ATOM   4033 O O     . GLU B 2 107 ? 113.706 114.003 113.697 1.00 113.85 ? 107 GLU B O     1 
ATOM   4034 C CB    . GLU B 2 107 ? 112.832 111.502 115.392 1.00 152.93 ? 107 GLU B CB    1 
ATOM   4035 C CG    . GLU B 2 107 ? 111.921 110.860 116.402 1.00 152.93 ? 107 GLU B CG    1 
ATOM   4036 C CD    . GLU B 2 107 ? 112.625 110.549 117.681 1.00 152.93 ? 107 GLU B CD    1 
ATOM   4037 O OE1   . GLU B 2 107 ? 113.656 109.879 117.645 1.00 152.93 ? 107 GLU B OE1   1 
ATOM   4038 O OE2   . GLU B 2 107 ? 112.154 110.988 118.725 1.00 152.93 ? 107 GLU B OE2   1 
ATOM   4039 N N     . GLY B 2 108 ? 115.469 113.362 114.882 1.00 109.27 ? 108 GLY B N     1 
ATOM   4040 C CA    . GLY B 2 108 ? 116.392 113.874 113.923 1.00 109.27 ? 108 GLY B CA    1 
ATOM   4041 C C     . GLY B 2 108 ? 117.000 115.183 114.333 1.00 109.27 ? 108 GLY B C     1 
ATOM   4042 O O     . GLY B 2 108 ? 118.067 115.536 113.837 1.00 109.27 ? 108 GLY B O     1 
ATOM   4043 N N     . ARG B 2 109 ? 116.390 115.893 115.268 1.00 108.75 ? 109 ARG B N     1 
ATOM   4044 C CA    . ARG B 2 109 ? 117.004 117.148 115.656 1.00 108.75 ? 109 ARG B CA    1 
ATOM   4045 C C     . ARG B 2 109 ? 118.266 116.903 116.429 1.00 108.75 ? 109 ARG B C     1 
ATOM   4046 O O     . ARG B 2 109 ? 119.153 117.749 116.452 1.00 108.75 ? 109 ARG B O     1 
ATOM   4047 C CB    . ARG B 2 109 ? 116.097 118.011 116.512 1.00 159.80 ? 109 ARG B CB    1 
ATOM   4048 C CG    . ARG B 2 109 ? 114.821 118.506 115.881 1.00 159.80 ? 109 ARG B CG    1 
ATOM   4049 C CD    . ARG B 2 109 ? 114.979 119.237 114.578 1.00 159.80 ? 109 ARG B CD    1 
ATOM   4050 N NE    . ARG B 2 109 ? 115.758 120.457 114.648 1.00 159.80 ? 109 ARG B NE    1 
ATOM   4051 C CZ    . ARG B 2 109 ? 115.882 121.293 113.631 1.00 159.80 ? 109 ARG B CZ    1 
ATOM   4052 N NH1   . ARG B 2 109 ? 115.253 121.082 112.496 1.00 159.80 ? 109 ARG B NH1   1 
ATOM   4053 N NH2   . ARG B 2 109 ? 116.659 122.361 113.759 1.00 159.80 ? 109 ARG B NH2   1 
ATOM   4054 N N     . ASP B 2 110 ? 118.325 115.796 117.123 1.00 99.35  ? 110 ASP B N     1 
ATOM   4055 C CA    . ASP B 2 110 ? 119.531 115.450 117.831 1.00 99.35  ? 110 ASP B CA    1 
ATOM   4056 C C     . ASP B 2 110 ? 120.486 114.739 116.887 1.00 99.35  ? 110 ASP B C     1 
ATOM   4057 O O     . ASP B 2 110 ? 121.654 115.112 116.751 1.00 99.35  ? 110 ASP B O     1 
ATOM   4058 C CB    . ASP B 2 110 ? 119.147 114.589 119.024 1.00 127.74 ? 110 ASP B CB    1 
ATOM   4059 C CG    . ASP B 2 110 ? 118.216 113.449 118.641 1.00 127.74 ? 110 ASP B CG    1 
ATOM   4060 O OD1   . ASP B 2 110 ? 117.764 113.406 117.484 1.00 127.74 ? 110 ASP B OD1   1 
ATOM   4061 O OD2   . ASP B 2 110 ? 117.944 112.598 119.489 1.00 127.74 ? 110 ASP B OD2   1 
ATOM   4062 N N     . MET B 2 111 ? 119.945 113.783 116.157 1.00 99.03  ? 111 MET B N     1 
ATOM   4063 C CA    . MET B 2 111 ? 120.677 112.944 115.238 1.00 99.03  ? 111 MET B CA    1 
ATOM   4064 C C     . MET B 2 111 ? 121.462 113.738 114.226 1.00 99.03  ? 111 MET B C     1 
ATOM   4065 O O     . MET B 2 111 ? 122.568 113.338 113.858 1.00 99.03  ? 111 MET B O     1 
ATOM   4066 C CB    . MET B 2 111 ? 119.674 112.082 114.507 1.00 142.27 ? 111 MET B CB    1 
ATOM   4067 C CG    . MET B 2 111 ? 120.215 111.024 113.630 1.00 142.27 ? 111 MET B CG    1 
ATOM   4068 S SD    . MET B 2 111 ? 118.836 110.206 112.840 1.00 142.27 ? 111 MET B SD    1 
ATOM   4069 C CE    . MET B 2 111 ? 119.661 109.155 111.682 1.00 142.27 ? 111 MET B CE    1 
ATOM   4070 N N     . ILE B 2 112 ? 120.928 114.875 113.781 1.00 95.29  ? 112 ILE B N     1 
ATOM   4071 C CA    . ILE B 2 112 ? 121.574 115.654 112.735 1.00 95.29  ? 112 ILE B CA    1 
ATOM   4072 C C     . ILE B 2 112 ? 122.990 116.031 113.099 1.00 95.29  ? 112 ILE B C     1 
ATOM   4073 O O     . ILE B 2 112 ? 123.812 116.221 112.213 1.00 95.29  ? 112 ILE B O     1 
ATOM   4074 C CB    . ILE B 2 112 ? 120.746 116.900 112.397 1.00 141.08 ? 112 ILE B CB    1 
ATOM   4075 C CG1   . ILE B 2 112 ? 121.236 117.596 111.135 1.00 141.08 ? 112 ILE B CG1   1 
ATOM   4076 C CG2   . ILE B 2 112 ? 120.801 117.865 113.539 1.00 141.08 ? 112 ILE B CG2   1 
ATOM   4077 C CD1   . ILE B 2 112 ? 121.092 116.812 109.829 1.00 141.08 ? 112 ILE B CD1   1 
ATOM   4078 N N     . ASP B 2 113 ? 123.322 116.155 114.364 1.00 95.14  ? 113 ASP B N     1 
ATOM   4079 C CA    . ASP B 2 113 ? 124.706 116.486 114.609 1.00 95.14  ? 113 ASP B CA    1 
ATOM   4080 C C     . ASP B 2 113 ? 125.590 115.309 114.294 1.00 95.14  ? 113 ASP B C     1 
ATOM   4081 O O     . ASP B 2 113 ? 126.724 115.483 113.849 1.00 95.14  ? 113 ASP B O     1 
ATOM   4082 C CB    . ASP B 2 113 ? 124.939 116.923 116.046 1.00 122.32 ? 113 ASP B CB    1 
ATOM   4083 C CG    . ASP B 2 113 ? 124.432 118.325 116.339 1.00 122.32 ? 113 ASP B CG    1 
ATOM   4084 O OD1   . ASP B 2 113 ? 124.170 119.106 115.417 1.00 122.32 ? 113 ASP B OD1   1 
ATOM   4085 O OD2   . ASP B 2 113 ? 124.317 118.648 117.521 1.00 122.32 ? 113 ASP B OD2   1 
ATOM   4086 N N     . ASN B 2 114 ? 125.093 114.108 114.504 1.00 88.49  ? 114 ASN B N     1 
ATOM   4087 C CA    . ASN B 2 114 ? 125.889 112.950 114.191 1.00 88.49  ? 114 ASN B CA    1 
ATOM   4088 C C     . ASN B 2 114 ? 125.908 112.741 112.710 1.00 88.49  ? 114 ASN B C     1 
ATOM   4089 O O     . ASN B 2 114 ? 126.918 112.295 112.165 1.00 88.49  ? 114 ASN B O     1 
ATOM   4090 C CB    . ASN B 2 114 ? 125.332 111.729 114.870 1.00 119.89 ? 114 ASN B CB    1 
ATOM   4091 C CG    . ASN B 2 114 ? 125.502 111.800 116.330 1.00 119.89 ? 114 ASN B CG    1 
ATOM   4092 O OD1   . ASN B 2 114 ? 126.427 112.442 116.830 1.00 119.89 ? 114 ASN B OD1   1 
ATOM   4093 N ND2   . ASN B 2 114 ? 124.609 111.160 117.049 1.00 119.89 ? 114 ASN B ND2   1 
ATOM   4094 N N     . ILE B 2 115 ? 124.815 113.083 112.037 1.00 86.12  ? 115 ILE B N     1 
ATOM   4095 C CA    . ILE B 2 115 ? 124.818 112.916 110.599 1.00 86.12  ? 115 ILE B CA    1 
ATOM   4096 C C     . ILE B 2 115 ? 125.841 113.821 110.001 1.00 86.12  ? 115 ILE B C     1 
ATOM   4097 O O     . ILE B 2 115 ? 126.621 113.418 109.137 1.00 86.12  ? 115 ILE B O     1 
ATOM   4098 C CB    . ILE B 2 115 ? 123.465 113.212 109.956 1.00 127.50 ? 115 ILE B CB    1 
ATOM   4099 C CG1   . ILE B 2 115 ? 122.426 112.207 110.384 1.00 127.50 ? 115 ILE B CG1   1 
ATOM   4100 C CG2   . ILE B 2 115 ? 123.627 113.185 108.439 1.00 127.50 ? 115 ILE B CG2   1 
ATOM   4101 C CD1   . ILE B 2 115 ? 121.007 112.611 110.040 1.00 127.50 ? 115 ILE B CD1   1 
ATOM   4102 N N     . MET B 2 116 ? 125.829 115.067 110.416 1.00 81.40  ? 116 MET B N     1 
ATOM   4103 C CA    . MET B 2 116 ? 126.738 115.990 109.800 1.00 81.40  ? 116 MET B CA    1 
ATOM   4104 C C     . MET B 2 116 ? 128.145 115.742 110.270 1.00 81.40  ? 116 MET B C     1 
ATOM   4105 O O     . MET B 2 116 ? 129.086 115.949 109.504 1.00 81.40  ? 116 MET B O     1 
ATOM   4106 C CB    . MET B 2 116 ? 126.295 117.417 110.059 1.00 116.94 ? 116 MET B CB    1 
ATOM   4107 C CG    . MET B 2 116 ? 124.993 117.784 109.353 1.00 116.94 ? 116 MET B CG    1 
ATOM   4108 S SD    . MET B 2 116 ? 124.949 117.479 107.554 1.00 116.94 ? 116 MET B SD    1 
ATOM   4109 C CE    . MET B 2 116 ? 126.185 118.605 106.916 1.00 116.94 ? 116 MET B CE    1 
ATOM   4110 N N     . GLU B 2 117 ? 128.332 115.273 111.486 1.00 76.68  ? 117 GLU B N     1 
ATOM   4111 C CA    . GLU B 2 117 ? 129.698 115.025 111.872 1.00 76.68  ? 117 GLU B CA    1 
ATOM   4112 C C     . GLU B 2 117 ? 130.243 113.868 111.086 1.00 76.68  ? 117 GLU B C     1 
ATOM   4113 O O     . GLU B 2 117 ? 131.392 113.897 110.635 1.00 76.68  ? 117 GLU B O     1 
ATOM   4114 C CB    . GLU B 2 117 ? 129.793 114.749 113.351 1.00 103.00 ? 117 GLU B CB    1 
ATOM   4115 C CG    . GLU B 2 117 ? 131.202 114.561 113.835 1.00 103.00 ? 117 GLU B CG    1 
ATOM   4116 C CD    . GLU B 2 117 ? 132.043 115.792 113.692 1.00 103.00 ? 117 GLU B CD    1 
ATOM   4117 O OE1   . GLU B 2 117 ? 131.492 116.882 113.583 1.00 103.00 ? 117 GLU B OE1   1 
ATOM   4118 O OE2   . GLU B 2 117 ? 133.270 115.672 113.703 1.00 103.00 ? 117 GLU B OE2   1 
ATOM   4119 N N     . GLN B 2 118 ? 129.431 112.845 110.879 1.00 75.07  ? 118 GLN B N     1 
ATOM   4120 C CA    . GLN B 2 118 ? 129.922 111.709 110.131 1.00 75.07  ? 118 GLN B CA    1 
ATOM   4121 C C     . GLN B 2 118 ? 130.121 112.074 108.676 1.00 75.07  ? 118 GLN B C     1 
ATOM   4122 O O     . GLN B 2 118 ? 131.058 111.576 108.037 1.00 75.07  ? 118 GLN B O     1 
ATOM   4123 C CB    . GLN B 2 118 ? 128.969 110.533 110.279 1.00 104.89 ? 118 GLN B CB    1 
ATOM   4124 C CG    . GLN B 2 118 ? 129.495 109.241 109.709 1.00 104.89 ? 118 GLN B CG    1 
ATOM   4125 C CD    . GLN B 2 118 ? 130.771 108.809 110.393 1.00 104.89 ? 118 GLN B CD    1 
ATOM   4126 O OE1   . GLN B 2 118 ? 130.907 108.911 111.614 1.00 104.89 ? 118 GLN B OE1   1 
ATOM   4127 N NE2   . GLN B 2 118 ? 131.718 108.330 109.609 1.00 104.89 ? 118 GLN B NE2   1 
ATOM   4128 N N     . LEU B 2 119 ? 129.282 112.951 108.128 1.00 68.85  ? 119 LEU B N     1 
ATOM   4129 C CA    . LEU B 2 119 ? 129.537 113.369 106.766 1.00 68.85  ? 119 LEU B CA    1 
ATOM   4130 C C     . LEU B 2 119 ? 130.863 114.082 106.719 1.00 68.85  ? 119 LEU B C     1 
ATOM   4131 O O     . LEU B 2 119 ? 131.703 113.776 105.883 1.00 68.85  ? 119 LEU B O     1 
ATOM   4132 C CB    . LEU B 2 119 ? 128.434 114.272 106.229 1.00 101.93 ? 119 LEU B CB    1 
ATOM   4133 C CG    . LEU B 2 119 ? 128.542 114.742 104.770 1.00 101.93 ? 119 LEU B CG    1 
ATOM   4134 C CD1   . LEU B 2 119 ? 128.514 113.569 103.795 1.00 101.93 ? 119 LEU B CD1   1 
ATOM   4135 C CD2   . LEU B 2 119 ? 127.408 115.724 104.448 1.00 101.93 ? 119 LEU B CD2   1 
ATOM   4136 N N     . LYS B 2 120 ? 131.120 114.951 107.682 1.00 67.83  ? 120 LYS B N     1 
ATOM   4137 C CA    . LYS B 2 120 ? 132.390 115.653 107.683 1.00 67.83  ? 120 LYS B CA    1 
ATOM   4138 C C     . LYS B 2 120 ? 133.531 114.681 107.651 1.00 67.83  ? 120 LYS B C     1 
ATOM   4139 O O     . LYS B 2 120 ? 134.490 114.868 106.903 1.00 67.83  ? 120 LYS B O     1 
ATOM   4140 C CB    . LYS B 2 120 ? 132.538 116.535 108.905 1.00 101.74 ? 120 LYS B CB    1 
ATOM   4141 C CG    . LYS B 2 120 ? 133.854 117.287 108.953 1.00 101.74 ? 120 LYS B CG    1 
ATOM   4142 C CD    . LYS B 2 120 ? 133.904 118.178 110.164 1.00 101.74 ? 120 LYS B CD    1 
ATOM   4143 C CE    . LYS B 2 120 ? 135.219 118.898 110.262 1.00 101.74 ? 120 LYS B CE    1 
ATOM   4144 N NZ    . LYS B 2 120 ? 135.288 119.756 111.475 1.00 101.74 ? 120 LYS B NZ    1 
ATOM   4145 N N     . LYS B 2 121 ? 133.443 113.629 108.445 1.00 63.97  ? 121 LYS B N     1 
ATOM   4146 C CA    . LYS B 2 121 ? 134.527 112.667 108.471 1.00 63.97  ? 121 LYS B CA    1 
ATOM   4147 C C     . LYS B 2 121 ? 134.748 112.068 107.105 1.00 63.97  ? 121 LYS B C     1 
ATOM   4148 O O     . LYS B 2 121 ? 135.885 111.765 106.736 1.00 63.97  ? 121 LYS B O     1 
ATOM   4149 C CB    . LYS B 2 121 ? 134.239 111.562 109.473 1.00 95.95  ? 121 LYS B CB    1 
ATOM   4150 C CG    . LYS B 2 121 ? 134.319 111.989 110.919 1.00 95.95  ? 121 LYS B CG    1 
ATOM   4151 C CD    . LYS B 2 121 ? 133.950 110.840 111.843 1.00 95.95  ? 121 LYS B CD    1 
ATOM   4152 C CE    . LYS B 2 121 ? 134.006 111.253 113.303 1.00 95.95  ? 121 LYS B CE    1 
ATOM   4153 N NZ    . LYS B 2 121 ? 133.553 110.155 114.203 1.00 95.95  ? 121 LYS B NZ    1 
ATOM   4154 N N     . GLU B 2 122 ? 133.671 111.848 106.361 1.00 63.09  ? 122 GLU B N     1 
ATOM   4155 C CA    . GLU B 2 122 ? 133.818 111.279 105.022 1.00 63.09  ? 122 GLU B CA    1 
ATOM   4156 C C     . GLU B 2 122 ? 134.406 112.316 104.071 1.00 63.09  ? 122 GLU B C     1 
ATOM   4157 O O     . GLU B 2 122 ? 135.327 112.034 103.298 1.00 63.09  ? 122 GLU B O     1 
ATOM   4158 C CB    . GLU B 2 122 ? 132.450 110.785 104.523 1.00 84.75  ? 122 GLU B CB    1 
ATOM   4159 C CG    . GLU B 2 122 ? 132.447 109.973 103.223 1.00 84.75  ? 122 GLU B CG    1 
ATOM   4160 C CD    . GLU B 2 122 ? 133.111 108.614 103.368 1.00 84.75  ? 122 GLU B CD    1 
ATOM   4161 O OE1   . GLU B 2 122 ? 133.212 108.095 104.482 1.00 84.75  ? 122 GLU B OE1   1 
ATOM   4162 O OE2   . GLU B 2 122 ? 133.563 108.081 102.362 1.00 84.75  ? 122 GLU B OE2   1 
ATOM   4163 N N     . VAL B 2 123 ? 133.919 113.540 104.165 1.00 61.79  ? 123 VAL B N     1 
ATOM   4164 C CA    . VAL B 2 123 ? 134.385 114.595 103.280 1.00 61.79  ? 123 VAL B CA    1 
ATOM   4165 C C     . VAL B 2 123 ? 135.851 114.828 103.512 1.00 61.79  ? 123 VAL B C     1 
ATOM   4166 O O     . VAL B 2 123 ? 136.615 115.118 102.595 1.00 61.79  ? 123 VAL B O     1 
ATOM   4167 C CB    . VAL B 2 123 ? 133.588 115.887 103.530 1.00 89.88  ? 123 VAL B CB    1 
ATOM   4168 C CG1   . VAL B 2 123 ? 134.191 117.030 102.734 1.00 89.88  ? 123 VAL B CG1   1 
ATOM   4169 C CG2   . VAL B 2 123 ? 132.120 115.692 103.180 1.00 89.88  ? 123 VAL B CG2   1 
ATOM   4170 N N     . ALA B 2 124 ? 136.246 114.742 104.763 1.00 60.99  ? 124 ALA B N     1 
ATOM   4171 C CA    . ALA B 2 124 ? 137.591 115.027 105.197 1.00 60.99  ? 124 ALA B CA    1 
ATOM   4172 C C     . ALA B 2 124 ? 138.625 114.123 104.571 1.00 60.99  ? 124 ALA B C     1 
ATOM   4173 O O     . ALA B 2 124 ? 139.806 114.475 104.567 1.00 60.99  ? 124 ALA B O     1 
ATOM   4174 C CB    . ALA B 2 124 ? 137.657 114.891 106.708 1.00 83.17  ? 124 ALA B CB    1 
ATOM   4175 N N     . LYS B 2 125 ? 138.254 112.943 104.114 1.00 63.34  ? 125 LYS B N     1 
ATOM   4176 C CA    . LYS B 2 125 ? 139.259 112.071 103.534 1.00 63.34  ? 125 LYS B CA    1 
ATOM   4177 C C     . LYS B 2 125 ? 139.198 112.099 102.032 1.00 63.34  ? 125 LYS B C     1 
ATOM   4178 O O     . LYS B 2 125 ? 139.881 111.316 101.372 1.00 63.34  ? 125 LYS B O     1 
ATOM   4179 C CB    . LYS B 2 125 ? 139.126 110.642 104.055 1.00 95.01  ? 125 LYS B CB    1 
ATOM   4180 C CG    . LYS B 2 125 ? 137.895 109.908 103.622 1.00 95.01  ? 125 LYS B CG    1 
ATOM   4181 C CD    . LYS B 2 125 ? 137.827 108.538 104.251 1.00 95.01  ? 125 LYS B CD    1 
ATOM   4182 C CE    . LYS B 2 125 ? 136.547 107.857 103.857 1.00 95.01  ? 125 LYS B CE    1 
ATOM   4183 N NZ    . LYS B 2 125 ? 136.358 106.551 104.531 1.00 95.01  ? 125 LYS B NZ    1 
ATOM   4184 N N     . CYS B 2 126 ? 138.378 112.975 101.485 1.00 61.87  ? 126 CYS B N     1 
ATOM   4185 C CA    . CYS B 2 126 ? 138.237 113.126 100.055 1.00 61.87  ? 126 CYS B CA    1 
ATOM   4186 C C     . CYS B 2 126 ? 139.276 114.131 99.592  1.00 61.87  ? 126 CYS B C     1 
ATOM   4187 O O     . CYS B 2 126 ? 139.514 115.122 100.273 1.00 61.87  ? 126 CYS B O     1 
ATOM   4188 C CB    . CYS B 2 126 ? 136.825 113.621 99.727  1.00 83.33  ? 126 CYS B CB    1 
ATOM   4189 S SG    . CYS B 2 126 ? 135.481 112.488 100.249 1.00 83.33  ? 126 CYS B SG    1 
ATOM   4190 N N     . GLU B 2 127 ? 139.902 113.900 98.443  1.00 61.39  ? 127 GLU B N     1 
ATOM   4191 C CA    . GLU B 2 127 ? 140.885 114.879 97.998  1.00 61.39  ? 127 GLU B CA    1 
ATOM   4192 C C     . GLU B 2 127 ? 140.228 116.215 97.734  1.00 61.39  ? 127 GLU B C     1 
ATOM   4193 O O     . GLU B 2 127 ? 140.738 117.266 98.126  1.00 61.39  ? 127 GLU B O     1 
ATOM   4194 C CB    . GLU B 2 127 ? 141.601 114.404 96.750  1.00 82.46  ? 127 GLU B CB    1 
ATOM   4195 C CG    . GLU B 2 127 ? 142.629 115.392 96.249  1.00 82.46  ? 127 GLU B CG    1 
ATOM   4196 C CD    . GLU B 2 127 ? 143.363 114.894 95.043  1.00 82.46  ? 127 GLU B CD    1 
ATOM   4197 O OE1   . GLU B 2 127 ? 143.027 113.818 94.554  1.00 82.46  ? 127 GLU B OE1   1 
ATOM   4198 O OE2   . GLU B 2 127 ? 144.272 115.579 94.579  1.00 82.46  ? 127 GLU B OE2   1 
ATOM   4199 N N     . SER B 2 128 ? 139.096 116.184 97.059  1.00 58.04  ? 128 SER B N     1 
ATOM   4200 C CA    . SER B 2 128 ? 138.309 117.367 96.786  1.00 58.04  ? 128 SER B CA    1 
ATOM   4201 C C     . SER B 2 128 ? 136.958 116.956 96.261  1.00 58.04  ? 128 SER B C     1 
ATOM   4202 O O     . SER B 2 128 ? 136.881 116.183 95.305  1.00 58.04  ? 128 SER B O     1 
ATOM   4203 C CB    . SER B 2 128 ? 138.985 118.254 95.769  1.00 78.18  ? 128 SER B CB    1 
ATOM   4204 O OG    . SER B 2 128 ? 138.183 119.384 95.529  1.00 78.18  ? 128 SER B OG    1 
ATOM   4205 N N     . LEU B 2 129 ? 135.893 117.462 96.862  1.00 54.56  ? 129 LEU B N     1 
ATOM   4206 C CA    . LEU B 2 129 ? 134.577 117.072 96.393  1.00 54.56  ? 129 LEU B CA    1 
ATOM   4207 C C     . LEU B 2 129 ? 134.163 117.867 95.204  1.00 54.56  ? 129 LEU B C     1 
ATOM   4208 O O     . LEU B 2 129 ? 134.459 119.053 95.084  1.00 54.56  ? 129 LEU B O     1 
ATOM   4209 C CB    . LEU B 2 129 ? 133.478 117.304 97.399  1.00 80.78  ? 129 LEU B CB    1 
ATOM   4210 C CG    . LEU B 2 129 ? 133.477 116.571 98.705  1.00 80.78  ? 129 LEU B CG    1 
ATOM   4211 C CD1   . LEU B 2 129 ? 132.282 117.076 99.448  1.00 80.78  ? 129 LEU B CD1   1 
ATOM   4212 C CD2   . LEU B 2 129 ? 133.389 115.077 98.488  1.00 80.78  ? 129 LEU B CD2   1 
ATOM   4213 N N     . GLN B 2 130 ? 133.432 117.203 94.347  1.00 58.50  ? 130 GLN B N     1 
ATOM   4214 C CA    . GLN B 2 130 ? 132.760 117.861 93.273  1.00 58.50  ? 130 GLN B CA    1 
ATOM   4215 C C     . GLN B 2 130 ? 131.412 118.236 93.770  1.00 58.50  ? 130 GLN B C     1 
ATOM   4216 O O     . GLN B 2 130 ? 130.924 119.333 93.509  1.00 58.50  ? 130 GLN B O     1 
ATOM   4217 C CB    . GLN B 2 130 ? 132.655 116.916 92.102  1.00 81.74  ? 130 GLN B CB    1 
ATOM   4218 C CG    . GLN B 2 130 ? 132.225 117.561 90.852  1.00 81.74  ? 130 GLN B CG    1 
ATOM   4219 C CD    . GLN B 2 130 ? 132.283 116.616 89.685  1.00 81.74  ? 130 GLN B CD    1 
ATOM   4220 O OE1   . GLN B 2 130 ? 131.269 116.076 89.262  1.00 81.74  ? 130 GLN B OE1   1 
ATOM   4221 N NE2   . GLN B 2 130 ? 133.473 116.411 89.152  1.00 81.74  ? 130 GLN B NE2   1 
ATOM   4222 N N     . GLY B 2 131 ? 130.841 117.348 94.570  1.00 55.12  ? 131 GLY B N     1 
ATOM   4223 C CA    . GLY B 2 131 ? 129.535 117.612 95.133  1.00 55.12  ? 131 GLY B CA    1 
ATOM   4224 C C     . GLY B 2 131 ? 128.939 116.420 95.856  1.00 55.12  ? 131 GLY B C     1 
ATOM   4225 O O     . GLY B 2 131 ? 129.589 115.394 96.075  1.00 55.12  ? 131 GLY B O     1 
ATOM   4226 N N     . PHE B 2 132 ? 127.673 116.587 96.220  1.00 51.16  ? 132 PHE B N     1 
ATOM   4227 C CA    . PHE B 2 132 ? 126.919 115.600 96.959  1.00 51.16  ? 132 PHE B CA    1 
ATOM   4228 C C     . PHE B 2 132 ? 125.708 115.183 96.172  1.00 51.16  ? 132 PHE B C     1 
ATOM   4229 O O     . PHE B 2 132 ? 125.097 116.005 95.503  1.00 51.16  ? 132 PHE B O     1 
ATOM   4230 C CB    . PHE B 2 132 ? 126.418 116.150 98.245  1.00 71.39  ? 132 PHE B CB    1 
ATOM   4231 C CG    . PHE B 2 132 ? 127.459 116.639 99.145  1.00 71.39  ? 132 PHE B CG    1 
ATOM   4232 C CD1   . PHE B 2 132 ? 128.061 115.802 100.036 1.00 71.39  ? 132 PHE B CD1   1 
ATOM   4233 C CD2   . PHE B 2 132 ? 127.805 117.937 99.143  1.00 71.39  ? 132 PHE B CD2   1 
ATOM   4234 C CE1   . PHE B 2 132 ? 129.003 116.264 100.894 1.00 71.39  ? 132 PHE B CE1   1 
ATOM   4235 C CE2   . PHE B 2 132 ? 128.743 118.411 100.001 1.00 71.39  ? 132 PHE B CE2   1 
ATOM   4236 C CZ    . PHE B 2 132 ? 129.340 117.574 100.878 1.00 71.39  ? 132 PHE B CZ    1 
ATOM   4237 N N     . ILE B 2 133 ? 125.331 113.922 96.276  1.00 56.58  ? 133 ILE B N     1 
ATOM   4238 C CA    . ILE B 2 133 ? 124.094 113.453 95.686  1.00 56.58  ? 133 ILE B CA    1 
ATOM   4239 C C     . ILE B 2 133 ? 123.219 112.778 96.729  1.00 56.58  ? 133 ILE B C     1 
ATOM   4240 O O     . ILE B 2 133 ? 123.573 111.719 97.252  1.00 56.58  ? 133 ILE B O     1 
ATOM   4241 C CB    . ILE B 2 133 ? 124.339 112.485 94.532  1.00 83.77  ? 133 ILE B CB    1 
ATOM   4242 C CG1   . ILE B 2 133 ? 125.116 113.181 93.403  1.00 83.77  ? 133 ILE B CG1   1 
ATOM   4243 C CG2   . ILE B 2 133 ? 123.005 111.946 94.061  1.00 83.77  ? 133 ILE B CG2   1 
ATOM   4244 C CD1   . ILE B 2 133 ? 125.519 112.270 92.236  1.00 83.77  ? 133 ILE B CD1   1 
ATOM   4245 N N     . MET B 2 134 ? 122.032 113.312 96.964  1.00 61.80  ? 134 MET B N     1 
ATOM   4246 C CA    . MET B 2 134 ? 121.144 112.698 97.936  1.00 61.80  ? 134 MET B CA    1 
ATOM   4247 C C     . MET B 2 134 ? 119.999 112.012 97.229  1.00 61.80  ? 134 MET B C     1 
ATOM   4248 O O     . MET B 2 134 ? 119.476 112.538 96.249  1.00 61.80  ? 134 MET B O     1 
ATOM   4249 C CB    . MET B 2 134 ? 120.620 113.741 98.889  1.00 88.78  ? 134 MET B CB    1 
ATOM   4250 C CG    . MET B 2 134 ? 119.792 113.181 100.013 1.00 88.78  ? 134 MET B CG    1 
ATOM   4251 S SD    . MET B 2 134 ? 119.169 114.439 101.128 1.00 88.78  ? 134 MET B SD    1 
ATOM   4252 C CE    . MET B 2 134 ? 120.656 115.018 101.924 1.00 88.78  ? 134 MET B CE    1 
ATOM   4253 N N     . THR B 2 135 ? 119.584 110.855 97.717  1.00 62.51  ? 135 THR B N     1 
ATOM   4254 C CA    . THR B 2 135 ? 118.437 110.152 97.150  1.00 62.51  ? 135 THR B CA    1 
ATOM   4255 C C     . THR B 2 135 ? 117.344 109.899 98.189  1.00 62.51  ? 135 THR B C     1 
ATOM   4256 O O     . THR B 2 135 ? 117.641 109.381 99.269  1.00 62.51  ? 135 THR B O     1 
ATOM   4257 C CB    . THR B 2 135 ? 118.875 108.823 96.567  1.00 87.51  ? 135 THR B CB    1 
ATOM   4258 O OG1   . THR B 2 135 ? 119.354 108.004 97.626  1.00 87.51  ? 135 THR B OG1   1 
ATOM   4259 C CG2   . THR B 2 135 ? 120.014 109.021 95.546  1.00 87.51  ? 135 THR B CG2   1 
ATOM   4260 N N     . HIS B 2 136 ? 116.071 110.219 97.867  1.00 68.99  ? 136 HIS B N     1 
ATOM   4261 C CA    . HIS B 2 136 ? 114.971 109.985 98.818  1.00 68.99  ? 136 HIS B CA    1 
ATOM   4262 C C     . HIS B 2 136 ? 113.571 110.068 98.200  1.00 68.99  ? 136 HIS B C     1 
ATOM   4263 O O     . HIS B 2 136 ? 113.385 110.575 97.101  1.00 68.99  ? 136 HIS B O     1 
ATOM   4264 C CB    . HIS B 2 136 ? 115.055 110.968 99.959  1.00 93.83  ? 136 HIS B CB    1 
ATOM   4265 C CG    . HIS B 2 136 ? 114.867 112.380 99.539  1.00 93.83  ? 136 HIS B CG    1 
ATOM   4266 N ND1   . HIS B 2 136 ? 113.640 113.002 99.569  1.00 93.83  ? 136 HIS B ND1   1 
ATOM   4267 C CD2   . HIS B 2 136 ? 115.745 113.292 99.072  1.00 93.83  ? 136 HIS B CD2   1 
ATOM   4268 C CE1   . HIS B 2 136 ? 113.774 114.245 99.149  1.00 93.83  ? 136 HIS B CE1   1 
ATOM   4269 N NE2   . HIS B 2 136 ? 115.044 114.445 98.841  1.00 93.83  ? 136 HIS B NE2   1 
ATOM   4270 N N     . ALA B 2 137 ? 112.565 109.567 98.920  1.00 77.24  ? 137 ALA B N     1 
ATOM   4271 C CA    . ALA B 2 137 ? 111.184 109.840 98.514  1.00 77.24  ? 137 ALA B CA    1 
ATOM   4272 C C     . ALA B 2 137 ? 110.839 111.274 98.897  1.00 77.24  ? 137 ALA B C     1 
ATOM   4273 O O     . ALA B 2 137 ? 111.121 111.703 100.016 1.00 77.24  ? 137 ALA B O     1 
ATOM   4274 C CB    . ALA B 2 137 ? 110.192 108.877 99.175  1.00 105.33 ? 137 ALA B CB    1 
ATOM   4275 N N     . VAL B 2 138 ? 110.185 112.008 97.995  1.00 78.44  ? 138 VAL B N     1 
ATOM   4276 C CA    . VAL B 2 138 ? 109.934 113.429 98.239  1.00 78.44  ? 138 VAL B CA    1 
ATOM   4277 C C     . VAL B 2 138 ? 109.021 113.619 99.407  1.00 78.44  ? 138 VAL B C     1 
ATOM   4278 O O     . VAL B 2 138 ? 109.216 114.526 100.225 1.00 78.44  ? 138 VAL B O     1 
ATOM   4279 C CB    . VAL B 2 138 ? 109.328 114.111 97.003  1.00 114.09 ? 138 VAL B CB    1 
ATOM   4280 C CG1   . VAL B 2 138 ? 108.880 115.553 97.326  1.00 114.09 ? 138 VAL B CG1   1 
ATOM   4281 C CG2   . VAL B 2 138 ? 110.321 114.141 95.912  1.00 114.09 ? 138 VAL B CG2   1 
ATOM   4282 N N     . GLY B 2 139 ? 107.964 112.832 99.440  1.00 79.28  ? 139 GLY B N     1 
ATOM   4283 C CA    . GLY B 2 139 ? 106.917 112.925 100.426 1.00 79.28  ? 139 GLY B CA    1 
ATOM   4284 C C     . GLY B 2 139 ? 107.086 111.950 101.558 1.00 79.28  ? 139 GLY B C     1 
ATOM   4285 O O     . GLY B 2 139 ? 106.135 111.690 102.302 1.00 79.28  ? 139 GLY B O     1 
ATOM   4286 N N     . GLY B 2 140 ? 108.246 111.343 101.684 1.00 83.01  ? 140 GLY B N     1 
ATOM   4287 C CA    . GLY B 2 140 ? 108.424 110.416 102.772 1.00 83.01  ? 140 GLY B CA    1 
ATOM   4288 C C     . GLY B 2 140 ? 108.517 111.196 104.065 1.00 83.01  ? 140 GLY B C     1 
ATOM   4289 O O     . GLY B 2 140 ? 109.032 112.307 104.088 1.00 83.01  ? 140 GLY B O     1 
ATOM   4290 N N     . GLY B 2 141 ? 108.062 110.608 105.155 1.00 88.44  ? 141 GLY B N     1 
ATOM   4291 C CA    . GLY B 2 141 ? 108.203 111.294 106.417 1.00 88.44  ? 141 GLY B CA    1 
ATOM   4292 C C     . GLY B 2 141 ? 109.652 111.622 106.687 1.00 88.44  ? 141 GLY B C     1 
ATOM   4293 O O     . GLY B 2 141 ? 110.020 112.801 106.787 1.00 88.44  ? 141 GLY B O     1 
ATOM   4294 N N     . SER B 2 142 ? 110.506 110.603 106.763 1.00 87.67  ? 142 SER B N     1 
ATOM   4295 C CA    . SER B 2 142 ? 111.908 110.897 106.996 1.00 87.67  ? 142 SER B CA    1 
ATOM   4296 C C     . SER B 2 142 ? 112.596 111.361 105.733 1.00 87.67  ? 142 SER B C     1 
ATOM   4297 O O     . SER B 2 142 ? 113.550 112.137 105.791 1.00 87.67  ? 142 SER B O     1 
ATOM   4298 C CB    . SER B 2 142 ? 112.620 109.679 107.512 1.00 118.09 ? 142 SER B CB    1 
ATOM   4299 O OG    . SER B 2 142 ? 112.738 108.752 106.467 1.00 118.09 ? 142 SER B OG    1 
ATOM   4300 N N     . GLY B 2 143 ? 112.071 110.941 104.596 1.00 83.56  ? 143 GLY B N     1 
ATOM   4301 C CA    . GLY B 2 143 ? 112.633 111.262 103.305 1.00 83.56  ? 143 GLY B CA    1 
ATOM   4302 C C     . GLY B 2 143 ? 112.660 112.752 103.104 1.00 83.56  ? 143 GLY B C     1 
ATOM   4303 O O     . GLY B 2 143 ? 113.725 113.342 102.934 1.00 83.56  ? 143 GLY B O     1 
ATOM   4304 N N     . GLY B 2 144 ? 111.500 113.378 103.186 1.00 84.08  ? 144 GLY B N     1 
ATOM   4305 C CA    . GLY B 2 144 ? 111.474 114.805 103.105 1.00 84.08  ? 144 GLY B CA    1 
ATOM   4306 C C     . GLY B 2 144 ? 112.024 115.423 104.362 1.00 84.08  ? 144 GLY B C     1 
ATOM   4307 O O     . GLY B 2 144 ? 112.645 116.480 104.306 1.00 84.08  ? 144 GLY B O     1 
ATOM   4308 N N     . GLY B 2 145 ? 111.886 114.738 105.493 1.00 83.96  ? 145 GLY B N     1 
ATOM   4309 C CA    . GLY B 2 145 ? 112.292 115.270 106.778 1.00 83.96  ? 145 GLY B CA    1 
ATOM   4310 C C     . GLY B 2 145 ? 113.782 115.352 107.003 1.00 83.96  ? 145 GLY B C     1 
ATOM   4311 O O     . GLY B 2 145 ? 114.345 116.453 107.010 1.00 83.96  ? 145 GLY B O     1 
ATOM   4312 N N     . LEU B 2 146 ? 114.441 114.225 107.208 1.00 77.68  ? 146 LEU B N     1 
ATOM   4313 C CA    . LEU B 2 146 ? 115.867 114.299 107.378 1.00 77.68  ? 146 LEU B CA    1 
ATOM   4314 C C     . LEU B 2 146 ? 116.456 114.765 106.104 1.00 77.68  ? 146 LEU B C     1 
ATOM   4315 O O     . LEU B 2 146 ? 117.408 115.532 106.108 1.00 77.68  ? 146 LEU B O     1 
ATOM   4316 C CB    . LEU B 2 146 ? 116.504 112.971 107.731 1.00 115.01 ? 146 LEU B CB    1 
ATOM   4317 C CG    . LEU B 2 146 ? 116.343 112.370 109.104 1.00 115.01 ? 146 LEU B CG    1 
ATOM   4318 C CD1   . LEU B 2 146 ? 116.951 110.980 109.089 1.00 115.01 ? 146 LEU B CD1   1 
ATOM   4319 C CD2   . LEU B 2 146 ? 117.040 113.231 110.145 1.00 115.01 ? 146 LEU B CD2   1 
ATOM   4320 N N     . GLY B 2 147 ? 115.905 114.322 104.976 1.00 76.40  ? 147 GLY B N     1 
ATOM   4321 C CA    . GLY B 2 147 ? 116.468 114.760 103.726 1.00 76.40  ? 147 GLY B CA    1 
ATOM   4322 C C     . GLY B 2 147 ? 116.617 116.263 103.685 1.00 76.40  ? 147 GLY B C     1 
ATOM   4323 O O     . GLY B 2 147 ? 117.715 116.779 103.472 1.00 76.40  ? 147 GLY B O     1 
ATOM   4324 N N     . CYS B 2 148 ? 115.539 116.989 103.943 1.00 73.74  ? 148 CYS B N     1 
ATOM   4325 C CA    . CYS B 2 148 ? 115.658 118.413 103.860 1.00 73.74  ? 148 CYS B CA    1 
ATOM   4326 C C     . CYS B 2 148 ? 116.527 118.972 104.951 1.00 73.74  ? 148 CYS B C     1 
ATOM   4327 O O     . CYS B 2 148 ? 117.248 119.949 104.720 1.00 73.74  ? 148 CYS B O     1 
ATOM   4328 C CB    . CYS B 2 148 ? 114.301 119.038 103.893 1.00 99.32  ? 148 CYS B CB    1 
ATOM   4329 S SG    . CYS B 2 148 ? 113.399 118.704 102.413 1.00 99.32  ? 148 CYS B SG    1 
ATOM   4330 N N     . LEU B 2 149 ? 116.478 118.397 106.144 1.00 71.46  ? 149 LEU B N     1 
ATOM   4331 C CA    . LEU B 2 149 ? 117.286 118.944 107.228 1.00 71.46  ? 149 LEU B CA    1 
ATOM   4332 C C     . LEU B 2 149 ? 118.761 118.815 106.917 1.00 71.46  ? 149 LEU B C     1 
ATOM   4333 O O     . LEU B 2 149 ? 119.559 119.730 107.170 1.00 71.46  ? 149 LEU B O     1 
ATOM   4334 C CB    . LEU B 2 149 ? 116.981 118.227 108.525 1.00 105.80 ? 149 LEU B CB    1 
ATOM   4335 C CG    . LEU B 2 149 ? 117.750 118.659 109.772 1.00 105.80 ? 149 LEU B CG    1 
ATOM   4336 C CD1   . LEU B 2 149 ? 117.530 120.132 110.050 1.00 105.80 ? 149 LEU B CD1   1 
ATOM   4337 C CD2   . LEU B 2 149 ? 117.278 117.817 110.976 1.00 105.80 ? 149 LEU B CD2   1 
ATOM   4338 N N     . ILE B 2 150 ? 119.132 117.674 106.355 1.00 69.34  ? 150 ILE B N     1 
ATOM   4339 C CA    . ILE B 2 150 ? 120.499 117.423 105.979 1.00 69.34  ? 150 ILE B CA    1 
ATOM   4340 C C     . ILE B 2 150 ? 120.901 118.389 104.916 1.00 69.34  ? 150 ILE B C     1 
ATOM   4341 O O     . ILE B 2 150 ? 121.950 119.009 105.015 1.00 69.34  ? 150 ILE B O     1 
ATOM   4342 C CB    . ILE B 2 150 ? 120.663 115.989 105.494 1.00 102.66 ? 150 ILE B CB    1 
ATOM   4343 C CG1   . ILE B 2 150 ? 120.382 115.011 106.628 1.00 102.66 ? 150 ILE B CG1   1 
ATOM   4344 C CG2   . ILE B 2 150 ? 122.077 115.816 105.023 1.00 102.66 ? 150 ILE B CG2   1 
ATOM   4345 C CD1   . ILE B 2 150 ? 120.152 113.594 106.143 1.00 102.66 ? 150 ILE B CD1   1 
ATOM   4346 N N     . MET B 2 151 ? 120.058 118.569 103.907 1.00 65.48  ? 151 MET B N     1 
ATOM   4347 C CA    . MET B 2 151 ? 120.402 119.508 102.856 1.00 65.48  ? 151 MET B CA    1 
ATOM   4348 C C     . MET B 2 151 ? 120.683 120.876 103.414 1.00 65.48  ? 151 MET B C     1 
ATOM   4349 O O     . MET B 2 151 ? 121.623 121.542 102.980 1.00 65.48  ? 151 MET B O     1 
ATOM   4350 C CB    . MET B 2 151 ? 119.293 119.617 101.846 1.00 94.07  ? 151 MET B CB    1 
ATOM   4351 C CG    . MET B 2 151 ? 119.125 118.423 101.012 1.00 94.07  ? 151 MET B CG    1 
ATOM   4352 S SD    . MET B 2 151 ? 117.803 118.669 99.861  1.00 94.07  ? 151 MET B SD    1 
ATOM   4353 C CE    . MET B 2 151 ? 117.626 117.023 99.211  1.00 94.07  ? 151 MET B CE    1 
ATOM   4354 N N     . GLU B 2 152 ? 119.859 121.332 104.339 1.00 64.91  ? 152 GLU B N     1 
ATOM   4355 C CA    . GLU B 2 152 ? 120.110 122.644 104.891 1.00 64.91  ? 152 GLU B CA    1 
ATOM   4356 C C     . GLU B 2 152 ? 121.459 122.686 105.529 1.00 64.91  ? 152 GLU B C     1 
ATOM   4357 O O     . GLU B 2 152 ? 122.242 123.632 105.315 1.00 64.91  ? 152 GLU B O     1 
ATOM   4358 C CB    . GLU B 2 152 ? 119.074 123.031 105.934 1.00 87.19  ? 152 GLU B CB    1 
ATOM   4359 C CG    . GLU B 2 152 ? 119.340 124.426 106.532 1.00 87.19  ? 152 GLU B CG    1 
ATOM   4360 C CD    . GLU B 2 152 ? 118.249 124.899 107.441 1.00 87.19  ? 152 GLU B CD    1 
ATOM   4361 O OE1   . GLU B 2 152 ? 117.932 124.195 108.399 1.00 87.19  ? 152 GLU B OE1   1 
ATOM   4362 O OE2   . GLU B 2 152 ? 117.691 125.969 107.179 1.00 87.19  ? 152 GLU B OE2   1 
ATOM   4363 N N     . LYS B 2 153 ? 121.768 121.670 106.303 1.00 61.61  ? 153 LYS B N     1 
ATOM   4364 C CA    . LYS B 2 153 ? 123.041 121.736 106.965 1.00 61.61  ? 153 LYS B CA    1 
ATOM   4365 C C     . LYS B 2 153 ? 124.198 121.593 105.974 1.00 61.61  ? 153 LYS B C     1 
ATOM   4366 O O     . LYS B 2 153 ? 125.256 122.201 106.174 1.00 61.61  ? 153 LYS B O     1 
ATOM   4367 C CB    . LYS B 2 153 ? 123.084 120.703 108.069 1.00 92.41  ? 153 LYS B CB    1 
ATOM   4368 C CG    . LYS B 2 153 ? 122.036 120.935 109.178 1.00 92.41  ? 153 LYS B CG    1 
ATOM   4369 C CD    . LYS B 2 153 ? 122.106 122.303 109.867 1.00 92.41  ? 153 LYS B CD    1 
ATOM   4370 C CE    . LYS B 2 153 ? 123.301 122.443 110.790 1.00 92.41  ? 153 LYS B CE    1 
ATOM   4371 N NZ    . LYS B 2 153 ? 123.340 123.783 111.450 1.00 92.41  ? 153 LYS B NZ    1 
ATOM   4372 N N     . ILE B 2 154 ? 124.014 120.841 104.888 1.00 61.12  ? 154 ILE B N     1 
ATOM   4373 C CA    . ILE B 2 154 ? 125.074 120.734 103.896 1.00 61.12  ? 154 ILE B CA    1 
ATOM   4374 C C     . ILE B 2 154 ? 125.342 122.088 103.317 1.00 61.12  ? 154 ILE B C     1 
ATOM   4375 O O     . ILE B 2 154 ? 126.499 122.486 103.160 1.00 61.12  ? 154 ILE B O     1 
ATOM   4376 C CB    . ILE B 2 154 ? 124.751 119.739 102.758 1.00 90.49  ? 154 ILE B CB    1 
ATOM   4377 C CG1   . ILE B 2 154 ? 124.751 118.286 103.260 1.00 90.49  ? 154 ILE B CG1   1 
ATOM   4378 C CG2   . ILE B 2 154 ? 125.754 119.910 101.578 1.00 90.49  ? 154 ILE B CG2   1 
ATOM   4379 C CD1   . ILE B 2 154 ? 124.190 117.255 102.267 1.00 90.49  ? 154 ILE B CD1   1 
ATOM   4380 N N     . LYS B 2 155 ? 124.291 122.816 102.971 1.00 55.80  ? 155 LYS B N     1 
ATOM   4381 C CA    . LYS B 2 155 ? 124.524 124.115 102.366 1.00 55.80  ? 155 LYS B CA    1 
ATOM   4382 C C     . LYS B 2 155 ? 125.285 125.010 103.312 1.00 55.80  ? 155 LYS B C     1 
ATOM   4383 O O     . LYS B 2 155 ? 126.150 125.772 102.881 1.00 55.80  ? 155 LYS B O     1 
ATOM   4384 C CB    . LYS B 2 155 ? 123.221 124.775 101.944 1.00 83.70  ? 155 LYS B CB    1 
ATOM   4385 C CG    . LYS B 2 155 ? 122.517 124.117 100.765 1.00 83.70  ? 155 LYS B CG    1 
ATOM   4386 C CD    . LYS B 2 155 ? 123.226 124.307 99.445  1.00 83.70  ? 155 LYS B CD    1 
ATOM   4387 C CE    . LYS B 2 155 ? 122.945 125.655 98.833  1.00 83.70  ? 155 LYS B CE    1 
ATOM   4388 N NZ    . LYS B 2 155 ? 123.522 125.765 97.459  1.00 83.70  ? 155 LYS B NZ    1 
ATOM   4389 N N     . GLU B 2 156 ? 124.996 124.933 104.596 1.00 62.57  ? 156 GLU B N     1 
ATOM   4390 C CA    . GLU B 2 156 ? 125.759 125.770 105.517 1.00 62.57  ? 156 GLU B CA    1 
ATOM   4391 C C     . GLU B 2 156 ? 127.231 125.351 105.621 1.00 62.57  ? 156 GLU B C     1 
ATOM   4392 O O     . GLU B 2 156 ? 128.117 126.213 105.677 1.00 62.57  ? 156 GLU B O     1 
ATOM   4393 C CB    . GLU B 2 156 ? 125.141 125.746 106.903 1.00 84.05  ? 156 GLU B CB    1 
ATOM   4394 C CG    . GLU B 2 156 ? 123.817 126.430 107.051 1.00 84.05  ? 156 GLU B CG    1 
ATOM   4395 C CD    . GLU B 2 156 ? 123.303 126.303 108.460 1.00 84.05  ? 156 GLU B CD    1 
ATOM   4396 O OE1   . GLU B 2 156 ? 123.839 125.477 109.207 1.00 84.05  ? 156 GLU B OE1   1 
ATOM   4397 O OE2   . GLU B 2 156 ? 122.385 127.028 108.835 1.00 84.05  ? 156 GLU B OE2   1 
ATOM   4398 N N     . GLU B 2 157 ? 127.516 124.042 105.669 1.00 63.26  ? 157 GLU B N     1 
ATOM   4399 C CA    . GLU B 2 157 ? 128.895 123.594 105.883 1.00 63.26  ? 157 GLU B CA    1 
ATOM   4400 C C     . GLU B 2 157 ? 129.747 123.555 104.623 1.00 63.26  ? 157 GLU B C     1 
ATOM   4401 O O     . GLU B 2 157 ? 130.976 123.691 104.700 1.00 63.26  ? 157 GLU B O     1 
ATOM   4402 C CB    . GLU B 2 157 ? 128.919 122.211 106.508 1.00 84.98  ? 157 GLU B CB    1 
ATOM   4403 C CG    . GLU B 2 157 ? 128.496 122.157 107.962 1.00 84.98  ? 157 GLU B CG    1 
ATOM   4404 C CD    . GLU B 2 157 ? 128.712 120.791 108.560 1.00 84.98  ? 157 GLU B CD    1 
ATOM   4405 O OE1   . GLU B 2 157 ? 128.891 119.847 107.792 1.00 84.98  ? 157 GLU B OE1   1 
ATOM   4406 O OE2   . GLU B 2 157 ? 128.720 120.666 109.786 1.00 84.98  ? 157 GLU B OE2   1 
ATOM   4407 N N     . TYR B 2 158 ? 129.137 123.368 103.464 1.00 59.51  ? 158 TYR B N     1 
ATOM   4408 C CA    . TYR B 2 158 ? 129.869 123.226 102.211 1.00 59.51  ? 158 TYR B CA    1 
ATOM   4409 C C     . TYR B 2 158 ? 129.349 124.214 101.167 1.00 59.51  ? 158 TYR B C     1 
ATOM   4410 O O     . TYR B 2 158 ? 128.765 123.814 100.156 1.00 59.51  ? 158 TYR B O     1 
ATOM   4411 C CB    . TYR B 2 158 ? 129.751 121.782 101.738 1.00 82.40  ? 158 TYR B CB    1 
ATOM   4412 C CG    . TYR B 2 158 ? 130.202 120.857 102.810 1.00 82.40  ? 158 TYR B CG    1 
ATOM   4413 C CD1   . TYR B 2 158 ? 131.545 120.716 103.077 1.00 82.40  ? 158 TYR B CD1   1 
ATOM   4414 C CD2   . TYR B 2 158 ? 129.288 120.166 103.580 1.00 82.40  ? 158 TYR B CD2   1 
ATOM   4415 C CE1   . TYR B 2 158 ? 131.969 119.902 104.061 1.00 82.40  ? 158 TYR B CE1   1 
ATOM   4416 C CE2   . TYR B 2 158 ? 129.705 119.340 104.569 1.00 82.40  ? 158 TYR B CE2   1 
ATOM   4417 C CZ    . TYR B 2 158 ? 131.050 119.211 104.811 1.00 82.40  ? 158 TYR B CZ    1 
ATOM   4418 O OH    . TYR B 2 158 ? 131.486 118.391 105.814 1.00 82.40  ? 158 TYR B OH    1 
ATOM   4419 N N     . PRO B 2 159 ? 129.639 125.506 101.358 1.00 57.85  ? 159 PRO B N     1 
ATOM   4420 C CA    . PRO B 2 159 ? 129.025 126.603 100.591 1.00 57.85  ? 159 PRO B CA    1 
ATOM   4421 C C     . PRO B 2 159 ? 129.338 126.634 99.120  1.00 57.85  ? 159 PRO B C     1 
ATOM   4422 O O     . PRO B 2 159 ? 128.640 127.319 98.361  1.00 57.85  ? 159 PRO B O     1 
ATOM   4423 C CB    . PRO B 2 159 ? 129.619 127.839 101.272 1.00 381.96 ? 159 PRO B CB    1 
ATOM   4424 C CG    . PRO B 2 159 ? 130.893 127.346 101.897 1.00 381.96 ? 159 PRO B CG    1 
ATOM   4425 C CD    . PRO B 2 159 ? 130.605 125.976 102.349 1.00 381.96 ? 159 PRO B CD    1 
ATOM   4426 N N     . LYS B 2 160 ? 130.397 125.981 98.689  1.00 60.14  ? 160 LYS B N     1 
ATOM   4427 C CA    . LYS B 2 160 ? 130.755 126.017 97.288  1.00 60.14  ? 160 LYS B CA    1 
ATOM   4428 C C     . LYS B 2 160 ? 130.626 124.670 96.594  1.00 60.14  ? 160 LYS B C     1 
ATOM   4429 O O     . LYS B 2 160 ? 131.118 124.516 95.475  1.00 60.14  ? 160 LYS B O     1 
ATOM   4430 C CB    . LYS B 2 160 ? 132.169 126.540 97.142  1.00 90.21  ? 160 LYS B CB    1 
ATOM   4431 C CG    . LYS B 2 160 ? 132.366 127.956 97.668  1.00 90.21  ? 160 LYS B CG    1 
ATOM   4432 C CD    . LYS B 2 160 ? 131.569 128.989 96.868  1.00 90.21  ? 160 LYS B CD    1 
ATOM   4433 C CE    . LYS B 2 160 ? 131.889 130.405 97.326  1.00 90.21  ? 160 LYS B CE    1 
ATOM   4434 N NZ    . LYS B 2 160 ? 131.102 131.429 96.578  1.00 90.21  ? 160 LYS B NZ    1 
ATOM   4435 N N     . LYS B 2 161 ? 130.004 123.682 97.216  1.00 56.07  ? 161 LYS B N     1 
ATOM   4436 C CA    . LYS B 2 161 ? 129.894 122.389 96.563  1.00 56.07  ? 161 LYS B CA    1 
ATOM   4437 C C     . LYS B 2 161 ? 128.534 122.281 95.917  1.00 56.07  ? 161 LYS B C     1 
ATOM   4438 O O     . LYS B 2 161 ? 127.595 122.955 96.317  1.00 56.07  ? 161 LYS B O     1 
ATOM   4439 C CB    . LYS B 2 161 ? 130.136 121.276 97.560  1.00 84.10  ? 161 LYS B CB    1 
ATOM   4440 C CG    . LYS B 2 161 ? 131.517 121.364 98.232  1.00 84.10  ? 161 LYS B CG    1 
ATOM   4441 C CD    . LYS B 2 161 ? 132.652 121.316 97.201  1.00 84.10  ? 161 LYS B CD    1 
ATOM   4442 C CE    . LYS B 2 161 ? 134.045 121.254 97.825  1.00 84.10  ? 161 LYS B CE    1 
ATOM   4443 N NZ    . LYS B 2 161 ? 135.095 121.302 96.772  1.00 84.10  ? 161 LYS B NZ    1 
ATOM   4444 N N     . ILE B 2 162 ? 128.416 121.487 94.901  1.00 58.18  ? 162 ILE B N     1 
ATOM   4445 C CA    . ILE B 2 162 ? 127.135 121.394 94.224  1.00 58.18  ? 162 ILE B CA    1 
ATOM   4446 C C     . ILE B 2 162 ? 126.252 120.358 94.874  1.00 58.18  ? 162 ILE B C     1 
ATOM   4447 O O     . ILE B 2 162 ? 126.681 119.224 95.129  1.00 58.18  ? 162 ILE B O     1 
ATOM   4448 C CB    . ILE B 2 162 ? 127.329 121.058 92.766  1.00 86.14  ? 162 ILE B CB    1 
ATOM   4449 C CG1   . ILE B 2 162 ? 128.093 122.201 92.158  1.00 86.14  ? 162 ILE B CG1   1 
ATOM   4450 C CG2   . ILE B 2 162 ? 125.986 120.823 92.114  1.00 86.14  ? 162 ILE B CG2   1 
ATOM   4451 C CD1   . ILE B 2 162 ? 128.608 121.908 90.813  1.00 86.14  ? 162 ILE B CD1   1 
ATOM   4452 N N     . LEU B 2 163 ? 125.013 120.733 95.142  1.00 56.27  ? 163 LEU B N     1 
ATOM   4453 C CA    . LEU B 2 163 ? 124.079 119.816 95.781  1.00 56.27  ? 163 LEU B CA    1 
ATOM   4454 C C     . LEU B 2 163 ? 123.016 119.347 94.807  1.00 56.27  ? 163 LEU B C     1 
ATOM   4455 O O     . LEU B 2 163 ? 122.145 120.113 94.377  1.00 56.27  ? 163 LEU B O     1 
ATOM   4456 C CB    . LEU B 2 163 ? 123.451 120.446 97.017  1.00 83.31  ? 163 LEU B CB    1 
ATOM   4457 C CG    . LEU B 2 163 ? 122.390 119.639 97.781  1.00 83.31  ? 163 LEU B CG    1 
ATOM   4458 C CD1   . LEU B 2 163 ? 122.957 118.335 98.335  1.00 83.31  ? 163 LEU B CD1   1 
ATOM   4459 C CD2   . LEU B 2 163 ? 121.824 120.504 98.905  1.00 83.31  ? 163 LEU B CD2   1 
ATOM   4460 N N     . TRP B 2 164 ? 123.067 118.074 94.517  1.00 59.97  ? 164 TRP B N     1 
ATOM   4461 C CA    . TRP B 2 164 ? 122.125 117.424 93.646  1.00 59.97  ? 164 TRP B CA    1 
ATOM   4462 C C     . TRP B 2 164 ? 121.233 116.515 94.427  1.00 59.97  ? 164 TRP B C     1 
ATOM   4463 O O     . TRP B 2 164 ? 121.657 115.889 95.404  1.00 59.97  ? 164 TRP B O     1 
ATOM   4464 C CB    . TRP B 2 164 ? 122.792 116.520 92.668  1.00 83.03  ? 164 TRP B CB    1 
ATOM   4465 C CG    . TRP B 2 164 ? 123.421 117.124 91.557  1.00 83.03  ? 164 TRP B CG    1 
ATOM   4466 C CD1   . TRP B 2 164 ? 123.599 118.436 91.304  1.00 83.03  ? 164 TRP B CD1   1 
ATOM   4467 C CD2   . TRP B 2 164 ? 123.968 116.415 90.470  1.00 83.03  ? 164 TRP B CD2   1 
ATOM   4468 N NE1   . TRP B 2 164 ? 124.240 118.581 90.110  1.00 83.03  ? 164 TRP B NE1   1 
ATOM   4469 C CE2   . TRP B 2 164 ? 124.472 117.339 89.591  1.00 83.03  ? 164 TRP B CE2   1 
ATOM   4470 C CE3   . TRP B 2 164 ? 124.067 115.066 90.162  1.00 83.03  ? 164 TRP B CE3   1 
ATOM   4471 C CZ2   . TRP B 2 164 ? 125.055 116.977 88.431  1.00 83.03  ? 164 TRP B CZ2   1 
ATOM   4472 C CZ3   . TRP B 2 164 ? 124.659 114.701 89.012  1.00 83.03  ? 164 TRP B CZ3   1 
ATOM   4473 C CH2   . TRP B 2 164 ? 125.145 115.640 88.155  1.00 83.03  ? 164 TRP B CH2   1 
ATOM   4474 N N     . SER B 2 165 ? 120.038 116.337 93.918  1.00 58.62  ? 165 SER B N     1 
ATOM   4475 C CA    . SER B 2 165 ? 119.200 115.338 94.527  1.00 58.62  ? 165 SER B CA    1 
ATOM   4476 C C     . SER B 2 165 ? 118.379 114.626 93.498  1.00 58.62  ? 165 SER B C     1 
ATOM   4477 O O     . SER B 2 165 ? 118.022 115.187 92.469  1.00 58.62  ? 165 SER B O     1 
ATOM   4478 C CB    . SER B 2 165 ? 118.265 115.938 95.544  1.00 78.96  ? 165 SER B CB    1 
ATOM   4479 O OG    . SER B 2 165 ? 117.354 116.811 94.917  1.00 78.96  ? 165 SER B OG    1 
ATOM   4480 N N     . TYR B 2 166 ? 118.076 113.392 93.802  1.00 63.67  ? 166 TYR B N     1 
ATOM   4481 C CA    . TYR B 2 166 ? 117.182 112.591 93.016  1.00 63.67  ? 166 TYR B CA    1 
ATOM   4482 C C     . TYR B 2 166 ? 116.076 112.205 93.939  1.00 63.67  ? 166 TYR B C     1 
ATOM   4483 O O     . TYR B 2 166 ? 116.332 111.688 95.022  1.00 63.67  ? 166 TYR B O     1 
ATOM   4484 C CB    . TYR B 2 166 ? 117.866 111.346 92.472  1.00 88.16  ? 166 TYR B CB    1 
ATOM   4485 C CG    . TYR B 2 166 ? 118.965 111.646 91.495  1.00 88.16  ? 166 TYR B CG    1 
ATOM   4486 C CD1   . TYR B 2 166 ? 120.208 112.055 91.940  1.00 88.16  ? 166 TYR B CD1   1 
ATOM   4487 C CD2   . TYR B 2 166 ? 118.764 111.510 90.127  1.00 88.16  ? 166 TYR B CD2   1 
ATOM   4488 C CE1   . TYR B 2 166 ? 121.225 112.335 91.053  1.00 88.16  ? 166 TYR B CE1   1 
ATOM   4489 C CE2   . TYR B 2 166 ? 119.781 111.786 89.228  1.00 88.16  ? 166 TYR B CE2   1 
ATOM   4490 C CZ    . TYR B 2 166 ? 121.010 112.200 89.702  1.00 88.16  ? 166 TYR B CZ    1 
ATOM   4491 O OH    . TYR B 2 166 ? 122.037 112.481 88.837  1.00 88.16  ? 166 TYR B OH    1 
ATOM   4492 N N     . SER B 2 167 ? 114.851 112.418 93.521  1.00 67.64  ? 167 SER B N     1 
ATOM   4493 C CA    . SER B 2 167 ? 113.809 112.092 94.465  1.00 67.64  ? 167 SER B CA    1 
ATOM   4494 C C     . SER B 2 167 ? 112.546 111.587 93.795  1.00 67.64  ? 167 SER B C     1 
ATOM   4495 O O     . SER B 2 167 ? 112.283 111.840 92.618  1.00 67.64  ? 167 SER B O     1 
ATOM   4496 C CB    . SER B 2 167 ? 113.534 113.299 95.331  1.00 91.11  ? 167 SER B CB    1 
ATOM   4497 O OG    . SER B 2 167 ? 113.053 114.367 94.550  1.00 91.11  ? 167 SER B OG    1 
ATOM   4498 N N     . ILE B 2 168 ? 111.766 110.854 94.570  1.00 71.82  ? 168 ILE B N     1 
ATOM   4499 C CA    . ILE B 2 168 ? 110.602 110.182 94.036  1.00 71.82  ? 168 ILE B CA    1 
ATOM   4500 C C     . ILE B 2 168 ? 109.306 110.762 94.560  1.00 71.82  ? 168 ILE B C     1 
ATOM   4501 O O     . ILE B 2 168 ? 109.087 110.821 95.772  1.00 71.82  ? 168 ILE B O     1 
ATOM   4502 C CB    . ILE B 2 168 ? 110.655 108.706 94.376  1.00 106.33 ? 168 ILE B CB    1 
ATOM   4503 C CG1   . ILE B 2 168 ? 112.023 108.111 93.983  1.00 106.33 ? 168 ILE B CG1   1 
ATOM   4504 C CG2   . ILE B 2 168 ? 109.530 108.027 93.696  1.00 106.33 ? 168 ILE B CG2   1 
ATOM   4505 C CD1   . ILE B 2 168 ? 112.409 108.218 92.523  1.00 106.33 ? 168 ILE B CD1   1 
ATOM   4506 N N     . LEU B 2 169 ? 108.419 111.117 93.653  1.00 75.87  ? 169 LEU B N     1 
ATOM   4507 C CA    . LEU B 2 169 ? 107.132 111.669 94.037  1.00 75.87  ? 169 LEU B CA    1 
ATOM   4508 C C     . LEU B 2 169 ? 106.078 110.593 94.232  1.00 75.87  ? 169 LEU B C     1 
ATOM   4509 O O     . LEU B 2 169 ? 106.019 109.625 93.470  1.00 75.87  ? 169 LEU B O     1 
ATOM   4510 C CB    . LEU B 2 169 ? 106.605 112.591 92.972  1.00 112.33 ? 169 LEU B CB    1 
ATOM   4511 C CG    . LEU B 2 169 ? 107.395 113.808 92.676  1.00 112.33 ? 169 LEU B CG    1 
ATOM   4512 C CD1   . LEU B 2 169 ? 106.803 114.397 91.476  1.00 112.33 ? 169 LEU B CD1   1 
ATOM   4513 C CD2   . LEU B 2 169 ? 107.316 114.777 93.825  1.00 112.33 ? 169 LEU B CD2   1 
ATOM   4514 N N     . PRO B 2 170 ? 105.181 110.852 95.171  1.00 81.15  ? 170 PRO B N     1 
ATOM   4515 C CA    . PRO B 2 170 ? 104.029 110.000 95.420  1.00 81.15  ? 170 PRO B CA    1 
ATOM   4516 C C     . PRO B 2 170 ? 103.021 110.141 94.312  1.00 81.15  ? 170 PRO B C     1 
ATOM   4517 O O     . PRO B 2 170 ? 102.976 111.162 93.639  1.00 81.15  ? 170 PRO B O     1 
ATOM   4518 C CB    . PRO B 2 170 ? 103.487 110.574 96.716  1.00 535.80 ? 170 PRO B CB    1 
ATOM   4519 C CG    . PRO B 2 170 ? 103.910 111.999 96.658  1.00 535.80 ? 170 PRO B CG    1 
ATOM   4520 C CD    . PRO B 2 170 ? 105.222 112.017 96.038  1.00 535.80 ? 170 PRO B CD    1 
ATOM   4521 N N     . SER B 2 171 ? 102.174 109.133 94.162  1.00 86.94  ? 171 SER B N     1 
ATOM   4522 C CA    . SER B 2 171 ? 101.158 109.127 93.125  1.00 86.94  ? 171 SER B CA    1 
ATOM   4523 C C     . SER B 2 171 ? 99.822  108.678 93.692  1.00 86.94  ? 171 SER B C     1 
ATOM   4524 O O     . SER B 2 171 ? 99.771  108.122 94.789  1.00 86.94  ? 171 SER B O     1 
ATOM   4525 C CB    . SER B 2 171 ? 101.584 108.184 91.997  1.00 117.10 ? 171 SER B CB    1 
ATOM   4526 O OG    . SER B 2 171 ? 101.526 106.836 92.415  1.00 117.10 ? 171 SER B OG    1 
ATOM   4527 N N     . PRO B 2 172 ? 98.729  108.899 92.967  1.00 87.90  ? 172 PRO B N     1 
ATOM   4528 C CA    . PRO B 2 172 ? 97.400  108.410 93.367  1.00 87.90  ? 172 PRO B CA    1 
ATOM   4529 C C     . PRO B 2 172 ? 97.298  106.925 93.628  1.00 87.90  ? 172 PRO B C     1 
ATOM   4530 O O     . PRO B 2 172 ? 96.485  106.501 94.456  1.00 87.90  ? 172 PRO B O     1 
ATOM   4531 C CB    . PRO B 2 172 ? 96.544  108.791 92.155  1.00 580.37 ? 172 PRO B CB    1 
ATOM   4532 C CG    . PRO B 2 172 ? 97.240  109.981 91.569  1.00 580.37 ? 172 PRO B CG    1 
ATOM   4533 C CD    . PRO B 2 172 ? 98.689  109.702 91.744  1.00 580.37 ? 172 PRO B CD    1 
ATOM   4534 N N     . LEU B 2 173 ? 98.071  106.104 92.941  1.00 93.38  ? 173 LEU B N     1 
ATOM   4535 C CA    . LEU B 2 173 ? 97.984  104.677 93.174  1.00 93.38  ? 173 LEU B CA    1 
ATOM   4536 C C     . LEU B 2 173 ? 99.064  104.155 94.088  1.00 93.38  ? 173 LEU B C     1 
ATOM   4537 O O     . LEU B 2 173 ? 98.850  103.169 94.796  1.00 93.38  ? 173 LEU B O     1 
ATOM   4538 C CB    . LEU B 2 173 ? 98.065  103.948 91.853  1.00 138.25 ? 173 LEU B CB    1 
ATOM   4539 C CG    . LEU B 2 173 ? 97.000  104.338 90.842  1.00 138.25 ? 173 LEU B CG    1 
ATOM   4540 C CD1   . LEU B 2 173 ? 97.272  103.589 89.559  1.00 138.25 ? 173 LEU B CD1   1 
ATOM   4541 C CD2   . LEU B 2 173 ? 95.615  104.029 91.370  1.00 138.25 ? 173 LEU B CD2   1 
ATOM   4542 N N     . LEU B 2 174 ? 100.222 104.765 94.087  1.00 96.04  ? 174 LEU B N     1 
ATOM   4543 C CA    . LEU B 2 174 ? 101.271 104.276 94.956  1.00 96.04  ? 174 LEU B CA    1 
ATOM   4544 C C     . LEU B 2 174 ? 101.579 105.327 96.000  1.00 96.04  ? 174 LEU B C     1 
ATOM   4545 O O     . LEU B 2 174 ? 102.025 106.431 95.689  1.00 96.04  ? 174 LEU B O     1 
ATOM   4546 C CB    . LEU B 2 174 ? 102.511 103.828 94.184  1.00 142.19 ? 174 LEU B CB    1 
ATOM   4547 C CG    . LEU B 2 174 ? 102.482 102.373 93.714  1.00 142.19 ? 174 LEU B CG    1 
ATOM   4548 C CD1   . LEU B 2 174 ? 102.367 101.434 94.890  1.00 142.19 ? 174 LEU B CD1   1 
ATOM   4549 C CD2   . LEU B 2 174 ? 101.320 102.162 92.784  1.00 142.19 ? 174 LEU B CD2   1 
ATOM   4550 N N     . SER B 2 175 ? 101.291 104.975 97.230  1.00 98.46  ? 175 SER B N     1 
ATOM   4551 C CA    . SER B 2 175 ? 101.534 105.810 98.383  1.00 98.46  ? 175 SER B CA    1 
ATOM   4552 C C     . SER B 2 175 ? 101.198 105.051 99.654  1.00 98.46  ? 175 SER B C     1 
ATOM   4553 O O     . SER B 2 175 ? 100.195 104.340 99.713  1.00 98.46  ? 175 SER B O     1 
ATOM   4554 C CB    . SER B 2 175 ? 100.715 107.087 98.288  1.00 132.62 ? 175 SER B CB    1 
ATOM   4555 O OG    . SER B 2 175 ? 100.832 107.837 99.469  1.00 132.62 ? 175 SER B OG    1 
ATOM   4556 N N     . ASP B 2 176 ? 102.022 105.213 100.677 1.00 104.65 ? 176 ASP B N     1 
ATOM   4557 C CA    . ASP B 2 176 ? 101.795 104.587 101.966 1.00 104.65 ? 176 ASP B CA    1 
ATOM   4558 C C     . ASP B 2 176 ? 101.194 105.572 102.952 1.00 104.65 ? 176 ASP B C     1 
ATOM   4559 O O     . ASP B 2 176 ? 101.108 105.275 104.149 1.00 104.65 ? 176 ASP B O     1 
ATOM   4560 C CB    . ASP B 2 176 ? 103.098 104.040 102.584 1.00 134.55 ? 176 ASP B CB    1 
ATOM   4561 C CG    . ASP B 2 176 ? 103.763 102.901 101.798 1.00 134.55 ? 176 ASP B CG    1 
ATOM   4562 O OD1   . ASP B 2 176 ? 103.202 102.384 100.852 1.00 134.55 ? 176 ASP B OD1   1 
ATOM   4563 O OD2   . ASP B 2 176 ? 104.867 102.493 102.181 1.00 134.55 ? 176 ASP B OD2   1 
ATOM   4564 N N     . ALA B 2 177 ? 100.795 106.743 102.484 1.00 103.17 ? 177 ALA B N     1 
ATOM   4565 C CA    . ALA B 2 177 ? 100.347 107.771 103.388 1.00 103.17 ? 177 ALA B CA    1 
ATOM   4566 C C     . ALA B 2 177 ? 99.217  108.549 102.783 1.00 103.17 ? 177 ALA B C     1 
ATOM   4567 O O     . ALA B 2 177 ? 99.080  108.658 101.576 1.00 103.17 ? 177 ALA B O     1 
ATOM   4568 C CB    . ALA B 2 177 ? 101.469 108.723 103.724 1.00 140.69 ? 177 ALA B CB    1 
ATOM   4569 N N     . VAL B 2 178 ? 98.434  109.144 103.649 1.00 101.93 ? 178 VAL B N     1 
ATOM   4570 C CA    . VAL B 2 178 ? 97.359  109.969 103.183 1.00 101.93 ? 178 VAL B CA    1 
ATOM   4571 C C     . VAL B 2 178 ? 97.744  111.418 103.277 1.00 101.93 ? 178 VAL B C     1 
ATOM   4572 O O     . VAL B 2 178 ? 97.012  112.288 102.790 1.00 101.93 ? 178 VAL B O     1 
ATOM   4573 C CB    . VAL B 2 178 ? 96.105  109.685 104.016 1.00 148.26 ? 178 VAL B CB    1 
ATOM   4574 C CG1   . VAL B 2 178 ? 95.803  108.194 104.022 1.00 148.26 ? 178 VAL B CG1   1 
ATOM   4575 C CG2   . VAL B 2 178 ? 96.331  110.176 105.391 1.00 148.26 ? 178 VAL B CG2   1 
ATOM   4576 N N     . VAL B 2 179 ? 98.860  111.709 103.915 1.00 99.27  ? 179 VAL B N     1 
ATOM   4577 C CA    . VAL B 2 179 ? 99.284  113.065 104.155 1.00 99.27  ? 179 VAL B CA    1 
ATOM   4578 C C     . VAL B 2 179 ? 100.440 113.452 103.296 1.00 99.27  ? 179 VAL B C     1 
ATOM   4579 O O     . VAL B 2 179 ? 100.961 114.568 103.425 1.00 99.27  ? 179 VAL B O     1 
ATOM   4580 C CB    . VAL B 2 179 ? 99.677  113.280 105.604 1.00 144.39 ? 179 VAL B CB    1 
ATOM   4581 C CG1   . VAL B 2 179 ? 98.519  113.046 106.490 1.00 144.39 ? 179 VAL B CG1   1 
ATOM   4582 C CG2   . VAL B 2 179 ? 100.816 112.382 105.953 1.00 144.39 ? 179 VAL B CG2   1 
ATOM   4583 N N     . GLU B 2 180 ? 100.779 112.629 102.374 1.00 92.99  ? 180 GLU B N     1 
ATOM   4584 C CA    . GLU B 2 180 ? 101.838 112.906 101.444 1.00 92.99  ? 180 GLU B CA    1 
ATOM   4585 C C     . GLU B 2 180 ? 101.848 114.323 100.995 1.00 92.99  ? 180 GLU B C     1 
ATOM   4586 O O     . GLU B 2 180 ? 102.700 115.138 101.379 1.00 92.99  ? 180 GLU B O     1 
ATOM   4587 C CB    . GLU B 2 180 ? 101.601 112.108 100.170 1.00 124.91 ? 180 GLU B CB    1 
ATOM   4588 C CG    . GLU B 2 180 ? 101.379 110.696 100.376 1.00 124.91 ? 180 GLU B CG    1 
ATOM   4589 C CD    . GLU B 2 180 ? 102.676 109.968 100.374 1.00 124.91 ? 180 GLU B CD    1 
ATOM   4590 O OE1   . GLU B 2 180 ? 103.639 110.544 99.863  1.00 124.91 ? 180 GLU B OE1   1 
ATOM   4591 O OE2   . GLU B 2 180 ? 102.744 108.827 100.880 1.00 124.91 ? 180 GLU B OE2   1 
ATOM   4592 N N     . PRO B 2 181 ? 100.835 114.641 100.290 1.00 94.03  ? 181 PRO B N     1 
ATOM   4593 C CA    . PRO B 2 181 ? 100.857 115.845 99.515  1.00 94.03  ? 181 PRO B CA    1 
ATOM   4594 C C     . PRO B 2 181 ? 101.400 116.995 100.327 1.00 94.03  ? 181 PRO B C     1 
ATOM   4595 O O     . PRO B 2 181 ? 102.002 117.916 99.767  1.00 94.03  ? 181 PRO B O     1 
ATOM   4596 C CB    . PRO B 2 181 ? 99.395  116.028 99.130  1.00 620.85 ? 181 PRO B CB    1 
ATOM   4597 C CG    . PRO B 2 181 ? 98.851  114.701 99.181  1.00 620.85 ? 181 PRO B CG    1 
ATOM   4598 C CD    . PRO B 2 181 ? 99.493  114.058 100.322 1.00 620.85 ? 181 PRO B CD    1 
ATOM   4599 N N     . TYR B 2 182 ? 101.298 116.927 101.636 1.00 93.47  ? 182 TYR B N     1 
ATOM   4600 C CA    . TYR B 2 182 ? 101.846 118.033 102.377 1.00 93.47  ? 182 TYR B CA    1 
ATOM   4601 C C     . TYR B 2 182 ? 103.285 117.773 102.675 1.00 93.47  ? 182 TYR B C     1 
ATOM   4602 O O     . TYR B 2 182 ? 104.102 118.708 102.645 1.00 93.47  ? 182 TYR B O     1 
ATOM   4603 C CB    . TYR B 2 182 ? 101.096 118.316 103.671 1.00 129.42 ? 182 TYR B CB    1 
ATOM   4604 C CG    . TYR B 2 182 ? 101.727 119.446 104.448 1.00 129.42 ? 182 TYR B CG    1 
ATOM   4605 C CD1   . TYR B 2 182 ? 101.967 120.672 103.853 1.00 129.42 ? 182 TYR B CD1   1 
ATOM   4606 C CD2   . TYR B 2 182 ? 102.066 119.282 105.761 1.00 129.42 ? 182 TYR B CD2   1 
ATOM   4607 C CE1   . TYR B 2 182 ? 102.523 121.698 104.544 1.00 129.42 ? 182 TYR B CE1   1 
ATOM   4608 C CE2   . TYR B 2 182 ? 102.630 120.303 106.468 1.00 129.42 ? 182 TYR B CE2   1 
ATOM   4609 C CZ    . TYR B 2 182 ? 102.850 121.518 105.859 1.00 129.42 ? 182 TYR B CZ    1 
ATOM   4610 O OH    . TYR B 2 182 ? 103.403 122.549 106.570 1.00 129.42 ? 182 TYR B OH    1 
ATOM   4611 N N     . ASN B 2 183 ? 103.629 116.523 102.939 1.00 88.62  ? 183 ASN B N     1 
ATOM   4612 C CA    . ASN B 2 183 ? 105.032 116.297 103.161 1.00 88.62  ? 183 ASN B CA    1 
ATOM   4613 C C     . ASN B 2 183 ? 105.767 116.733 101.917 1.00 88.62  ? 183 ASN B C     1 
ATOM   4614 O O     . ASN B 2 183 ? 106.850 117.318 101.982 1.00 88.62  ? 183 ASN B O     1 
ATOM   4615 C CB    . ASN B 2 183 ? 105.325 114.845 103.423 1.00 120.07 ? 183 ASN B CB    1 
ATOM   4616 C CG    . ASN B 2 183 ? 104.765 114.316 104.714 1.00 120.07 ? 183 ASN B CG    1 
ATOM   4617 O OD1   . ASN B 2 183 ? 104.384 115.050 105.632 1.00 120.07 ? 183 ASN B OD1   1 
ATOM   4618 N ND2   . ASN B 2 183 ? 104.734 112.998 104.796 1.00 120.07 ? 183 ASN B ND2   1 
ATOM   4619 N N     . ALA B 2 184 ? 105.138 116.494 100.763 1.00 82.82  ? 184 ALA B N     1 
ATOM   4620 C CA    . ALA B 2 184 ? 105.710 116.839 99.471  1.00 82.82  ? 184 ALA B CA    1 
ATOM   4621 C C     . ALA B 2 184 ? 105.853 118.337 99.270  1.00 82.82  ? 184 ALA B C     1 
ATOM   4622 O O     . ALA B 2 184 ? 106.892 118.769 98.791  1.00 82.82  ? 184 ALA B O     1 
ATOM   4623 C CB    . ALA B 2 184 ? 104.878 116.252 98.343  1.00 112.94 ? 184 ALA B CB    1 
ATOM   4624 N N     . ILE B 2 185 ? 104.865 119.159 99.618  1.00 78.40  ? 185 ILE B N     1 
ATOM   4625 C CA    . ILE B 2 185 ? 105.183 120.542 99.338  1.00 78.40  ? 185 ILE B CA    1 
ATOM   4626 C C     . ILE B 2 185 ? 106.186 121.075 100.299 1.00 78.40  ? 185 ILE B C     1 
ATOM   4627 O O     . ILE B 2 185 ? 106.971 121.944 99.925  1.00 78.40  ? 185 ILE B O     1 
ATOM   4628 C CB    . ILE B 2 185 ? 103.990 121.465 99.265  1.00 116.07 ? 185 ILE B CB    1 
ATOM   4629 C CG1   . ILE B 2 185 ? 103.366 121.685 100.627 1.00 116.07 ? 185 ILE B CG1   1 
ATOM   4630 C CG2   . ILE B 2 185 ? 103.037 120.936 98.249  1.00 116.07 ? 185 ILE B CG2   1 
ATOM   4631 C CD1   . ILE B 2 185 ? 102.405 122.849 100.645 1.00 116.07 ? 185 ILE B CD1   1 
ATOM   4632 N N     . LEU B 2 186 ? 106.220 120.613 101.530 1.00 77.59  ? 186 LEU B N     1 
ATOM   4633 C CA    . LEU B 2 186 ? 107.284 121.103 102.387 1.00 77.59  ? 186 LEU B CA    1 
ATOM   4634 C C     . LEU B 2 186 ? 108.634 120.705 101.852 1.00 77.59  ? 186 LEU B C     1 
ATOM   4635 O O     . LEU B 2 186 ? 109.591 121.499 101.858 1.00 77.59  ? 186 LEU B O     1 
ATOM   4636 C CB    . LEU B 2 186 ? 107.177 120.561 103.784 1.00 114.87 ? 186 LEU B CB    1 
ATOM   4637 C CG    . LEU B 2 186 ? 106.070 121.089 104.630 1.00 114.87 ? 186 LEU B CG    1 
ATOM   4638 C CD1   . LEU B 2 186 ? 106.044 120.267 105.881 1.00 114.87 ? 186 LEU B CD1   1 
ATOM   4639 C CD2   . LEU B 2 186 ? 106.339 122.545 104.985 1.00 114.87 ? 186 LEU B CD2   1 
ATOM   4640 N N     . SER B 2 187 ? 108.715 119.472 101.388 1.00 73.80  ? 187 SER B N     1 
ATOM   4641 C CA    . SER B 2 187 ? 109.948 118.938 100.876 1.00 73.80  ? 187 SER B CA    1 
ATOM   4642 C C     . SER B 2 187 ? 110.376 119.700 99.651  1.00 73.80  ? 187 SER B C     1 
ATOM   4643 O O     . SER B 2 187 ? 111.528 120.117 99.533  1.00 73.80  ? 187 SER B O     1 
ATOM   4644 C CB    . SER B 2 187 ? 109.689 117.474 100.591 1.00 99.40  ? 187 SER B CB    1 
ATOM   4645 O OG    . SER B 2 187 ? 110.809 116.797 100.114 1.00 99.40  ? 187 SER B OG    1 
ATOM   4646 N N     . LEU B 2 188 ? 109.436 119.960 98.764  1.00 65.81  ? 188 LEU B N     1 
ATOM   4647 C CA    . LEU B 2 188 ? 109.756 120.690 97.562  1.00 65.81  ? 188 LEU B CA    1 
ATOM   4648 C C     . LEU B 2 188 ? 110.201 122.085 97.901  1.00 65.81  ? 188 LEU B C     1 
ATOM   4649 O O     . LEU B 2 188 ? 111.165 122.575 97.326  1.00 65.81  ? 188 LEU B O     1 
ATOM   4650 C CB    . LEU B 2 188 ? 108.556 120.706 96.613  1.00 97.43  ? 188 LEU B CB    1 
ATOM   4651 C CG    . LEU B 2 188 ? 108.138 119.372 95.946  1.00 97.43  ? 188 LEU B CG    1 
ATOM   4652 C CD1   . LEU B 2 188 ? 106.770 119.520 95.307  1.00 97.43  ? 188 LEU B CD1   1 
ATOM   4653 C CD2   . LEU B 2 188 ? 109.164 118.914 94.907  1.00 97.43  ? 188 LEU B CD2   1 
ATOM   4654 N N     . ASP B 2 189 ? 109.535 122.727 98.839  1.00 66.14  ? 189 ASP B N     1 
ATOM   4655 C CA    . ASP B 2 189 ? 109.881 124.090 99.174  1.00 66.14  ? 189 ASP B CA    1 
ATOM   4656 C C     . ASP B 2 189 ? 111.302 124.181 99.653  1.00 66.14  ? 189 ASP B C     1 
ATOM   4657 O O     . ASP B 2 189 ? 112.081 125.054 99.229  1.00 66.14  ? 189 ASP B O     1 
ATOM   4658 C CB    . ASP B 2 189 ? 108.949 124.618 100.262 1.00 85.04  ? 189 ASP B CB    1 
ATOM   4659 C CG    . ASP B 2 189 ? 109.245 126.065 100.649 1.00 85.04  ? 189 ASP B CG    1 
ATOM   4660 O OD1   . ASP B 2 189 ? 109.777 126.809 99.822  1.00 85.04  ? 189 ASP B OD1   1 
ATOM   4661 O OD2   . ASP B 2 189 ? 108.957 126.462 101.783 1.00 85.04  ? 189 ASP B OD2   1 
ATOM   4662 N N     . LYS B 2 190 ? 111.665 123.320 100.568 1.00 63.24  ? 190 LYS B N     1 
ATOM   4663 C CA    . LYS B 2 190 ? 113.014 123.437 101.045 1.00 63.24  ? 190 LYS B CA    1 
ATOM   4664 C C     . LYS B 2 190 ? 113.995 123.146 99.934  1.00 63.24  ? 190 LYS B C     1 
ATOM   4665 O O     . LYS B 2 190 ? 114.959 123.879 99.757  1.00 63.24  ? 190 LYS B O     1 
ATOM   4666 C CB    . LYS B 2 190 ? 113.192 122.549 102.241 1.00 94.86  ? 190 LYS B CB    1 
ATOM   4667 C CG    . LYS B 2 190 ? 112.517 123.150 103.434 1.00 94.86  ? 190 LYS B CG    1 
ATOM   4668 C CD    . LYS B 2 190 ? 112.719 122.318 104.665 1.00 94.86  ? 190 LYS B CD    1 
ATOM   4669 C CE    . LYS B 2 190 ? 112.011 122.920 105.856 1.00 94.86  ? 190 LYS B CE    1 
ATOM   4670 N NZ    . LYS B 2 190 ? 112.656 124.188 106.302 1.00 94.86  ? 190 LYS B NZ    1 
ATOM   4671 N N     . MET B 2 191 ? 113.709 122.166 99.094  1.00 60.91  ? 191 MET B N     1 
ATOM   4672 C CA    . MET B 2 191 ? 114.651 121.919 98.027  1.00 60.91  ? 191 MET B CA    1 
ATOM   4673 C C     . MET B 2 191 ? 114.786 123.138 97.121  1.00 60.91  ? 191 MET B C     1 
ATOM   4674 O O     . MET B 2 191 ? 115.902 123.481 96.730  1.00 60.91  ? 191 MET B O     1 
ATOM   4675 C CB    . MET B 2 191 ? 114.260 120.658 97.260  1.00 87.50  ? 191 MET B CB    1 
ATOM   4676 C CG    . MET B 2 191 ? 114.496 119.404 98.059  1.00 87.50  ? 191 MET B CG    1 
ATOM   4677 S SD    . MET B 2 191 ? 114.268 117.878 97.151  1.00 87.50  ? 191 MET B SD    1 
ATOM   4678 C CE    . MET B 2 191 ? 112.485 117.724 97.140  1.00 87.50  ? 191 MET B CE    1 
ATOM   4679 N N     . ILE B 2 192 ? 113.703 123.865 96.855  1.00 57.72  ? 192 ILE B N     1 
ATOM   4680 C CA    . ILE B 2 192 ? 113.843 125.038 96.002  1.00 57.72  ? 192 ILE B CA    1 
ATOM   4681 C C     . ILE B 2 192 ? 114.869 125.935 96.599  1.00 57.72  ? 192 ILE B C     1 
ATOM   4682 O O     . ILE B 2 192 ? 115.706 126.513 95.906  1.00 57.72  ? 192 ILE B O     1 
ATOM   4683 C CB    . ILE B 2 192 ? 112.557 125.851 95.867  1.00 85.45  ? 192 ILE B CB    1 
ATOM   4684 C CG1   . ILE B 2 192 ? 111.452 125.089 95.178  1.00 85.45  ? 192 ILE B CG1   1 
ATOM   4685 C CG2   . ILE B 2 192 ? 112.845 127.077 95.049  1.00 85.45  ? 192 ILE B CG2   1 
ATOM   4686 C CD1   . ILE B 2 192 ? 110.040 125.732 95.375  1.00 85.45  ? 192 ILE B CD1   1 
ATOM   4687 N N     . GLN B 2 193 ? 114.801 126.076 97.904  1.00 57.64  ? 193 GLN B N     1 
ATOM   4688 C CA    . GLN B 2 193 ? 115.699 126.960 98.619  1.00 57.64  ? 193 GLN B CA    1 
ATOM   4689 C C     . GLN B 2 193 ? 117.103 126.401 98.800  1.00 57.64  ? 193 GLN B C     1 
ATOM   4690 O O     . GLN B 2 193 ? 118.037 127.184 98.939  1.00 57.64  ? 193 GLN B O     1 
ATOM   4691 C CB    . GLN B 2 193 ? 115.094 127.283 99.978  1.00 80.54  ? 193 GLN B CB    1 
ATOM   4692 C CG    . GLN B 2 193 ? 113.806 128.075 99.901  1.00 80.54  ? 193 GLN B CG    1 
ATOM   4693 C CD    . GLN B 2 193 ? 113.219 128.351 101.253 1.00 80.54  ? 193 GLN B CD    1 
ATOM   4694 O OE1   . GLN B 2 193 ? 113.942 128.720 102.164 1.00 80.54  ? 193 GLN B OE1   1 
ATOM   4695 N NE2   . GLN B 2 193 ? 111.915 128.168 101.400 1.00 80.54  ? 193 GLN B NE2   1 
ATOM   4696 N N     . TYR B 2 194 ? 117.305 125.093 98.806  1.00 56.85  ? 194 TYR B N     1 
ATOM   4697 C CA    . TYR B 2 194 ? 118.650 124.576 99.104  1.00 56.85  ? 194 TYR B CA    1 
ATOM   4698 C C     . TYR B 2 194 ? 119.408 123.913 97.967  1.00 56.85  ? 194 TYR B C     1 
ATOM   4699 O O     . TYR B 2 194 ? 120.628 123.863 98.038  1.00 56.85  ? 194 TYR B O     1 
ATOM   4700 C CB    . TYR B 2 194 ? 118.627 123.533 100.225 1.00 78.71  ? 194 TYR B CB    1 
ATOM   4701 C CG    . TYR B 2 194 ? 118.084 124.030 101.507 1.00 78.71  ? 194 TYR B CG    1 
ATOM   4702 C CD1   . TYR B 2 194 ? 118.663 125.101 102.163 1.00 78.71  ? 194 TYR B CD1   1 
ATOM   4703 C CD2   . TYR B 2 194 ? 116.972 123.439 102.048 1.00 78.71  ? 194 TYR B CD2   1 
ATOM   4704 C CE1   . TYR B 2 194 ? 118.129 125.566 103.329 1.00 78.71  ? 194 TYR B CE1   1 
ATOM   4705 C CE2   . TYR B 2 194 ? 116.436 123.895 103.202 1.00 78.71  ? 194 TYR B CE2   1 
ATOM   4706 C CZ    . TYR B 2 194 ? 117.005 124.956 103.844 1.00 78.71  ? 194 TYR B CZ    1 
ATOM   4707 O OH    . TYR B 2 194 ? 116.417 125.381 105.014 1.00 78.71  ? 194 TYR B OH    1 
ATOM   4708 N N     . THR B 2 195 ? 118.744 123.332 96.978  1.00 58.63  ? 195 THR B N     1 
ATOM   4709 C CA    . THR B 2 195 ? 119.446 122.545 95.972  1.00 58.63  ? 195 THR B CA    1 
ATOM   4710 C C     . THR B 2 195 ? 119.863 123.369 94.757  1.00 58.63  ? 195 THR B C     1 
ATOM   4711 O O     . THR B 2 195 ? 119.320 124.432 94.471  1.00 58.63  ? 195 THR B O     1 
ATOM   4712 C CB    . THR B 2 195 ? 118.597 121.347 95.507  1.00 82.08  ? 195 THR B CB    1 
ATOM   4713 O OG1   . THR B 2 195 ? 117.338 121.787 94.975  1.00 82.08  ? 195 THR B OG1   1 
ATOM   4714 C CG2   . THR B 2 195 ? 118.354 120.393 96.675  1.00 82.08  ? 195 THR B CG2   1 
ATOM   4715 N N     . ASP B 2 196 ? 120.847 122.852 94.040  1.00 57.75  ? 196 ASP B N     1 
ATOM   4716 C CA    . ASP B 2 196 ? 121.279 123.442 92.799  1.00 57.75  ? 196 ASP B CA    1 
ATOM   4717 C C     . ASP B 2 196 ? 120.598 122.789 91.636  1.00 57.75  ? 196 ASP B C     1 
ATOM   4718 O O     . ASP B 2 196 ? 120.260 123.452 90.660  1.00 57.75  ? 196 ASP B O     1 
ATOM   4719 C CB    . ASP B 2 196 ? 122.788 123.273 92.639  1.00 74.25  ? 196 ASP B CB    1 
ATOM   4720 C CG    . ASP B 2 196 ? 123.598 124.031 93.683  1.00 74.25  ? 196 ASP B CG    1 
ATOM   4721 O OD1   . ASP B 2 196 ? 123.551 125.264 93.683  1.00 74.25  ? 196 ASP B OD1   1 
ATOM   4722 O OD2   . ASP B 2 196 ? 124.279 123.400 94.509  1.00 74.25  ? 196 ASP B OD2   1 
ATOM   4723 N N     . GLU B 2 197 ? 120.394 121.490 91.722  1.00 59.26  ? 197 GLU B N     1 
ATOM   4724 C CA    . GLU B 2 197 ? 119.763 120.767 90.637  1.00 59.26  ? 197 GLU B CA    1 
ATOM   4725 C C     . GLU B 2 197 ? 119.077 119.524 91.163  1.00 59.26  ? 197 GLU B C     1 
ATOM   4726 O O     . GLU B 2 197 ? 119.599 118.844 92.046  1.00 59.26  ? 197 GLU B O     1 
ATOM   4727 C CB    . GLU B 2 197 ? 120.796 120.401 89.576  1.00 79.60  ? 197 GLU B CB    1 
ATOM   4728 C CG    . GLU B 2 197 ? 120.268 119.664 88.365  1.00 79.60  ? 197 GLU B CG    1 
ATOM   4729 C CD    . GLU B 2 197 ? 121.338 119.459 87.325  1.00 79.60  ? 197 GLU B CD    1 
ATOM   4730 O OE1   . GLU B 2 197 ? 121.781 120.442 86.730  1.00 79.60  ? 197 GLU B OE1   1 
ATOM   4731 O OE2   . GLU B 2 197 ? 121.737 118.318 87.104  1.00 79.60  ? 197 GLU B OE2   1 
ATOM   4732 N N     . THR B 2 198 ? 117.915 119.213 90.623  1.00 58.92  ? 198 THR B N     1 
ATOM   4733 C CA    . THR B 2 198 ? 117.278 118.002 91.082  1.00 58.92  ? 198 THR B CA    1 
ATOM   4734 C C     . THR B 2 198 ? 116.565 117.287 89.963  1.00 58.92  ? 198 THR B C     1 
ATOM   4735 O O     . THR B 2 198 ? 116.037 117.898 89.031  1.00 58.92  ? 198 THR B O     1 
ATOM   4736 C CB    . THR B 2 198 ? 116.297 118.278 92.205  1.00 82.49  ? 198 THR B CB    1 
ATOM   4737 O OG1   . THR B 2 198 ? 115.822 117.033 92.715  1.00 82.49  ? 198 THR B OG1   1 
ATOM   4738 C CG2   . THR B 2 198 ? 115.116 119.088 91.714  1.00 82.49  ? 198 THR B CG2   1 
ATOM   4739 N N     . VAL B 2 199 ? 116.532 115.979 90.082  1.00 58.77  ? 199 VAL B N     1 
ATOM   4740 C CA    . VAL B 2 199 ? 115.859 115.151 89.117  1.00 58.77  ? 199 VAL B CA    1 
ATOM   4741 C C     . VAL B 2 199 ? 114.704 114.524 89.823  1.00 58.77  ? 199 VAL B C     1 
ATOM   4742 O O     . VAL B 2 199 ? 114.870 113.883 90.861  1.00 58.77  ? 199 VAL B O     1 
ATOM   4743 C CB    . VAL B 2 199 ? 116.791 114.087 88.532  1.00 85.48  ? 199 VAL B CB    1 
ATOM   4744 C CG1   . VAL B 2 199 ? 116.033 113.194 87.552  1.00 85.48  ? 199 VAL B CG1   1 
ATOM   4745 C CG2   . VAL B 2 199 ? 117.969 114.758 87.845  1.00 85.48  ? 199 VAL B CG2   1 
ATOM   4746 N N     . VAL B 2 200 ? 113.539 114.706 89.280  1.00 63.81  ? 200 VAL B N     1 
ATOM   4747 C CA    . VAL B 2 200 ? 112.371 114.223 89.945  1.00 63.81  ? 200 VAL B CA    1 
ATOM   4748 C C     . VAL B 2 200 ? 111.685 113.187 89.094  1.00 63.81  ? 200 VAL B C     1 
ATOM   4749 O O     . VAL B 2 200 ? 111.390 113.420 87.914  1.00 63.81  ? 200 VAL B O     1 
ATOM   4750 C CB    . VAL B 2 200 ? 111.449 115.380 90.307  1.00 92.81  ? 200 VAL B CB    1 
ATOM   4751 C CG1   . VAL B 2 200 ? 110.238 114.852 90.976  1.00 92.81  ? 200 VAL B CG1   1 
ATOM   4752 C CG2   . VAL B 2 200 ? 112.192 116.320 91.249  1.00 92.81  ? 200 VAL B CG2   1 
ATOM   4753 N N     . ILE B 2 201 ? 111.432 112.047 89.710  1.00 70.47  ? 201 ILE B N     1 
ATOM   4754 C CA    . ILE B 2 201 ? 110.777 110.910 89.096  1.00 70.47  ? 201 ILE B CA    1 
ATOM   4755 C C     . ILE B 2 201 ? 109.441 110.696 89.767  1.00 70.47  ? 201 ILE B C     1 
ATOM   4756 O O     . ILE B 2 201 ? 109.341 110.737 90.995  1.00 70.47  ? 201 ILE B O     1 
ATOM   4757 C CB    . ILE B 2 201 ? 111.667 109.681 89.216  1.00 104.33 ? 201 ILE B CB    1 
ATOM   4758 C CG1   . ILE B 2 201 ? 112.917 109.892 88.356  1.00 104.33 ? 201 ILE B CG1   1 
ATOM   4759 C CG2   . ILE B 2 201 ? 110.891 108.418 88.883  1.00 104.33 ? 201 ILE B CG2   1 
ATOM   4760 C CD1   . ILE B 2 201 ? 114.053 108.915 88.633  1.00 104.33 ? 201 ILE B CD1   1 
ATOM   4761 N N     . ASP B 2 202 ? 108.408 110.538 88.958  1.00 77.58  ? 202 ASP B N     1 
ATOM   4762 C CA    . ASP B 2 202 ? 107.038 110.398 89.432  1.00 77.58  ? 202 ASP B CA    1 
ATOM   4763 C C     . ASP B 2 202 ? 106.632 108.930 89.445  1.00 77.58  ? 202 ASP B C     1 
ATOM   4764 O O     . ASP B 2 202 ? 106.594 108.296 88.391  1.00 77.58  ? 202 ASP B O     1 
ATOM   4765 C CB    . ASP B 2 202 ? 106.097 111.220 88.550  1.00 99.75  ? 202 ASP B CB    1 
ATOM   4766 C CG    . ASP B 2 202 ? 104.682 111.252 89.091  1.00 99.75  ? 202 ASP B CG    1 
ATOM   4767 O OD1   . ASP B 2 202 ? 104.330 110.322 89.815  1.00 99.75  ? 202 ASP B OD1   1 
ATOM   4768 O OD2   . ASP B 2 202 ? 103.921 112.187 88.807  1.00 99.75  ? 202 ASP B OD2   1 
ATOM   4769 N N     . ASN B 2 203 ? 106.300 108.377 90.615  1.00 74.72  ? 203 ASN B N     1 
ATOM   4770 C CA    . ASN B 2 203 ? 105.948 106.962 90.614  1.00 74.72  ? 203 ASN B CA    1 
ATOM   4771 C C     . ASN B 2 203 ? 104.725 106.678 89.761  1.00 74.72  ? 203 ASN B C     1 
ATOM   4772 O O     . ASN B 2 203 ? 104.519 105.532 89.355  1.00 74.72  ? 203 ASN B O     1 
ATOM   4773 C CB    . ASN B 2 203 ? 105.721 106.430 92.007  1.00 101.23 ? 203 ASN B CB    1 
ATOM   4774 C CG    . ASN B 2 203 ? 106.974 106.030 92.693  1.00 101.23 ? 203 ASN B CG    1 
ATOM   4775 O OD1   . ASN B 2 203 ? 108.010 105.796 92.075  1.00 101.23 ? 203 ASN B OD1   1 
ATOM   4776 N ND2   . ASN B 2 203 ? 106.895 105.922 94.002  1.00 101.23 ? 203 ASN B ND2   1 
ATOM   4777 N N     . HIS B 2 204 ? 103.931 107.691 89.466  1.00 78.87  ? 204 HIS B N     1 
ATOM   4778 C CA    . HIS B 2 204 ? 102.792 107.519 88.577  1.00 78.87  ? 204 HIS B CA    1 
ATOM   4779 C C     . HIS B 2 204 ? 103.274 107.079 87.225  1.00 78.87  ? 204 HIS B C     1 
ATOM   4780 O O     . HIS B 2 204 ? 102.707 106.184 86.587  1.00 78.87  ? 204 HIS B O     1 
ATOM   4781 C CB    . HIS B 2 204 ? 102.074 108.849 88.451  1.00 107.26 ? 204 HIS B CB    1 
ATOM   4782 C CG    . HIS B 2 204 ? 100.782 108.818 87.715  1.00 107.26 ? 204 HIS B CG    1 
ATOM   4783 N ND1   . HIS B 2 204 ? 99.659  108.208 88.213  1.00 107.26 ? 204 HIS B ND1   1 
ATOM   4784 C CD2   . HIS B 2 204 ? 100.412 109.398 86.557  1.00 107.26 ? 204 HIS B CD2   1 
ATOM   4785 C CE1   . HIS B 2 204 ? 98.658  108.395 87.379  1.00 107.26 ? 204 HIS B CE1   1 
ATOM   4786 N NE2   . HIS B 2 204 ? 99.090  109.116 86.368  1.00 107.26 ? 204 HIS B NE2   1 
ATOM   4787 N N     . ALA B 2 205 ? 104.331 107.720 86.774  1.00 77.78  ? 205 ALA B N     1 
ATOM   4788 C CA    . ALA B 2 205 ? 104.887 107.431 85.478  1.00 77.78  ? 205 ALA B CA    1 
ATOM   4789 C C     . ALA B 2 205 ? 105.427 106.050 85.436  1.00 77.78  ? 205 ALA B C     1 
ATOM   4790 O O     . ALA B 2 205 ? 105.251 105.320 84.461  1.00 77.78  ? 205 ALA B O     1 
ATOM   4791 C CB    . ALA B 2 205 ? 106.030 108.377 85.188  1.00 106.06 ? 205 ALA B CB    1 
ATOM   4792 N N     . LEU B 2 206 ? 106.131 105.700 86.467  1.00 77.74  ? 206 LEU B N     1 
ATOM   4793 C CA    . LEU B 2 206 ? 106.799 104.452 86.414  1.00 77.74  ? 206 LEU B CA    1 
ATOM   4794 C C     . LEU B 2 206 ? 105.806 103.368 86.442  1.00 77.74  ? 206 LEU B C     1 
ATOM   4795 O O     . LEU B 2 206 ? 105.994 102.333 85.815  1.00 77.74  ? 206 LEU B O     1 
ATOM   4796 C CB    . LEU B 2 206 ? 107.699 104.298 87.585  1.00 115.09 ? 206 LEU B CB    1 
ATOM   4797 C CG    . LEU B 2 206 ? 108.761 105.317 87.730  1.00 115.09 ? 206 LEU B CG    1 
ATOM   4798 C CD1   . LEU B 2 206 ? 109.511 104.947 88.943  1.00 115.09 ? 206 LEU B CD1   1 
ATOM   4799 C CD2   . LEU B 2 206 ? 109.624 105.367 86.505  1.00 115.09 ? 206 LEU B CD2   1 
ATOM   4800 N N     . PHE B 2 207 ? 104.753 103.573 87.176  1.00 78.47  ? 207 PHE B N     1 
ATOM   4801 C CA    . PHE B 2 207 ? 103.786 102.544 87.167  1.00 78.47  ? 207 PHE B CA    1 
ATOM   4802 C C     . PHE B 2 207 ? 103.418 102.367 85.759  1.00 78.47  ? 207 PHE B C     1 
ATOM   4803 O O     . PHE B 2 207 ? 103.722 101.353 85.140  1.00 78.47  ? 207 PHE B O     1 
ATOM   4804 C CB    . PHE B 2 207 ? 102.572 102.980 87.925  1.00 109.49 ? 207 PHE B CB    1 
ATOM   4805 C CG    . PHE B 2 207 ? 101.735 101.867 88.430  1.00 109.49 ? 207 PHE B CG    1 
ATOM   4806 C CD1   . PHE B 2 207 ? 101.992 101.321 89.663  1.00 109.49 ? 207 PHE B CD1   1 
ATOM   4807 C CD2   . PHE B 2 207 ? 100.659 101.396 87.702  1.00 109.49 ? 207 PHE B CD2   1 
ATOM   4808 C CE1   . PHE B 2 207 ? 101.211 100.303 90.156  1.00 109.49 ? 207 PHE B CE1   1 
ATOM   4809 C CE2   . PHE B 2 207 ? 99.867  100.376 88.191  1.00 109.49 ? 207 PHE B CE2   1 
ATOM   4810 C CZ    . PHE B 2 207 ? 100.144 99.828  89.423  1.00 109.49 ? 207 PHE B CZ    1 
ATOM   4811 N N     . GLN B 2 208 ? 102.849 103.401 85.211  1.00 79.34  ? 208 GLN B N     1 
ATOM   4812 C CA    . GLN B 2 208 ? 102.299 103.264 83.891  1.00 79.34  ? 208 GLN B CA    1 
ATOM   4813 C C     . GLN B 2 208 ? 103.243 102.540 82.954  1.00 79.34  ? 208 GLN B C     1 
ATOM   4814 O O     . GLN B 2 208 ? 102.821 101.699 82.156  1.00 79.34  ? 208 GLN B O     1 
ATOM   4815 C CB    . GLN B 2 208 ? 102.006 104.632 83.326  1.00 110.86 ? 208 GLN B CB    1 
ATOM   4816 C CG    . GLN B 2 208 ? 100.877 105.375 83.992  1.00 110.86 ? 208 GLN B CG    1 
ATOM   4817 C CD    . GLN B 2 208 ? 100.793 106.805 83.492  1.00 110.86 ? 208 GLN B CD    1 
ATOM   4818 O OE1   . GLN B 2 208 ? 101.748 107.328 82.913  1.00 110.86 ? 208 GLN B OE1   1 
ATOM   4819 N NE2   . GLN B 2 208 ? 99.651  107.440 83.700  1.00 110.86 ? 208 GLN B NE2   1 
ATOM   4820 N N     . ILE B 2 209 ? 104.528 102.841 83.062  1.00 78.98  ? 209 ILE B N     1 
ATOM   4821 C CA    . ILE B 2 209 ? 105.493 102.198 82.187  1.00 78.98  ? 209 ILE B CA    1 
ATOM   4822 C C     . ILE B 2 209 ? 105.566 100.708 82.493  1.00 78.98  ? 209 ILE B C     1 
ATOM   4823 O O     . ILE B 2 209 ? 105.488 99.868  81.597  1.00 78.98  ? 209 ILE B O     1 
ATOM   4824 C CB    . ILE B 2 209 ? 106.869 102.875 82.322  1.00 116.93 ? 209 ILE B CB    1 
ATOM   4825 C CG1   . ILE B 2 209 ? 106.791 104.337 81.816  1.00 116.93 ? 209 ILE B CG1   1 
ATOM   4826 C CG2   . ILE B 2 209 ? 107.922 102.080 81.533  1.00 116.93 ? 209 ILE B CG2   1 
ATOM   4827 C CD1   . ILE B 2 209 ? 107.977 105.247 82.195  1.00 116.93 ? 209 ILE B CD1   1 
ATOM   4828 N N     . VAL B 2 210 ? 105.665 100.358 83.768  1.00 80.94  ? 210 VAL B N     1 
ATOM   4829 C CA    . VAL B 2 210 ? 105.754 98.956  84.136  1.00 80.94  ? 210 VAL B CA    1 
ATOM   4830 C C     . VAL B 2 210 ? 104.528 98.233  83.675  1.00 80.94  ? 210 VAL B C     1 
ATOM   4831 O O     . VAL B 2 210 ? 104.601 97.147  83.102  1.00 80.94  ? 210 VAL B O     1 
ATOM   4832 C CB    . VAL B 2 210 ? 105.912 98.812  85.650  1.00 117.73 ? 210 VAL B CB    1 
ATOM   4833 C CG1   . VAL B 2 210 ? 105.784 97.362  86.068  1.00 117.73 ? 210 VAL B CG1   1 
ATOM   4834 C CG2   . VAL B 2 210 ? 107.251 99.332  86.093  1.00 117.73 ? 210 VAL B CG2   1 
ATOM   4835 N N     . THR B 2 211 ? 103.387 98.838  83.905  1.00 81.02  ? 211 THR B N     1 
ATOM   4836 C CA    . THR B 2 211 ? 102.117 98.216  83.606  1.00 81.02  ? 211 THR B CA    1 
ATOM   4837 C C     . THR B 2 211 ? 101.938 97.947  82.126  1.00 81.02  ? 211 THR B C     1 
ATOM   4838 O O     . THR B 2 211 ? 101.495 96.863  81.741  1.00 81.02  ? 211 THR B O     1 
ATOM   4839 C CB    . THR B 2 211 ? 100.975 99.092  84.108  1.00 113.43 ? 211 THR B CB    1 
ATOM   4840 O OG1   . THR B 2 211 ? 101.085 99.266  85.527  1.00 113.43 ? 211 THR B OG1   1 
ATOM   4841 C CG2   . THR B 2 211 ? 99.640  98.439  83.807  1.00 113.43 ? 211 THR B CG2   1 
ATOM   4842 N N     . LYS B 2 212 ? 102.249 98.912  81.272  1.00 79.73  ? 212 LYS B N     1 
ATOM   4843 C CA    . LYS B 2 212 ? 101.935 98.717  79.863  1.00 79.73  ? 212 LYS B CA    1 
ATOM   4844 C C     . LYS B 2 212 ? 103.117 98.522  78.943  1.00 79.73  ? 212 LYS B C     1 
ATOM   4845 O O     . LYS B 2 212 ? 102.980 97.838  77.934  1.00 79.73  ? 212 LYS B O     1 
ATOM   4846 C CB    . LYS B 2 212 ? 101.125 99.894  79.334  1.00 119.59 ? 212 LYS B CB    1 
ATOM   4847 C CG    . LYS B 2 212 ? 99.769  100.102 80.018  1.00 119.59 ? 212 LYS B CG    1 
ATOM   4848 C CD    . LYS B 2 212 ? 98.803  98.933  79.782  1.00 119.59 ? 212 LYS B CD    1 
ATOM   4849 C CE    . LYS B 2 212 ? 97.421  99.223  80.359  1.00 119.59 ? 212 LYS B CE    1 
ATOM   4850 N NZ    . LYS B 2 212 ? 96.479  98.080  80.164  1.00 119.59 ? 212 LYS B NZ    1 
ATOM   4851 N N     . ASN B 2 213 ? 104.253 99.114  79.225  1.00 77.10  ? 213 ASN B N     1 
ATOM   4852 C CA    . ASN B 2 213 ? 105.351 98.987  78.298  1.00 77.10  ? 213 ASN B CA    1 
ATOM   4853 C C     . ASN B 2 213 ? 106.236 97.830  78.668  1.00 77.10  ? 213 ASN B C     1 
ATOM   4854 O O     . ASN B 2 213 ? 106.761 97.148  77.786  1.00 77.10  ? 213 ASN B O     1 
ATOM   4855 C CB    . ASN B 2 213 ? 106.132 100.289 78.253  1.00 104.46 ? 213 ASN B CB    1 
ATOM   4856 C CG    . ASN B 2 213 ? 105.285 101.425 77.740  1.00 104.46 ? 213 ASN B CG    1 
ATOM   4857 O OD1   . ASN B 2 213 ? 104.355 101.221 76.957  1.00 104.46 ? 213 ASN B OD1   1 
ATOM   4858 N ND2   . ASN B 2 213 ? 105.579 102.622 78.188  1.00 104.46 ? 213 ASN B ND2   1 
ATOM   4859 N N     . MET B 2 214 ? 106.384 97.569  79.952  1.00 81.72  ? 214 MET B N     1 
ATOM   4860 C CA    . MET B 2 214 ? 107.185 96.427  80.333  1.00 81.72  ? 214 MET B CA    1 
ATOM   4861 C C     . MET B 2 214 ? 106.373 95.144  80.333  1.00 81.72  ? 214 MET B C     1 
ATOM   4862 O O     . MET B 2 214 ? 106.955 94.056  80.287  1.00 81.72  ? 214 MET B O     1 
ATOM   4863 C CB    . MET B 2 214 ? 107.820 96.624  81.707  1.00 117.40 ? 214 MET B CB    1 
ATOM   4864 C CG    . MET B 2 214 ? 108.761 97.811  81.819  1.00 117.40 ? 214 MET B CG    1 
ATOM   4865 S SD    . MET B 2 214 ? 109.538 97.863  83.445  1.00 117.40 ? 214 MET B SD    1 
ATOM   4866 C CE    . MET B 2 214 ? 110.048 99.571  83.598  1.00 117.40 ? 214 MET B CE    1 
ATOM   4867 N N     . GLY B 2 215 ? 105.045 95.255  80.383  1.00 79.23  ? 215 GLY B N     1 
ATOM   4868 C CA    . GLY B 2 215 ? 104.168 94.098  80.389  1.00 79.23  ? 215 GLY B CA    1 
ATOM   4869 C C     . GLY B 2 215 ? 104.120 93.351  81.703  1.00 79.23  ? 215 GLY B C     1 
ATOM   4870 O O     . GLY B 2 215 ? 103.879 92.143  81.719  1.00 79.23  ? 215 GLY B O     1 
ATOM   4871 N N     . ILE B 2 216 ? 104.356 94.022  82.811  1.00 81.33  ? 216 ILE B N     1 
ATOM   4872 C CA    . ILE B 2 216 ? 104.403 93.365  84.100  1.00 81.33  ? 216 ILE B CA    1 
ATOM   4873 C C     . ILE B 2 216 ? 103.146 93.688  84.876  1.00 81.33  ? 216 ILE B C     1 
ATOM   4874 O O     . ILE B 2 216 ? 102.912 94.842  85.241  1.00 81.33  ? 216 ILE B O     1 
ATOM   4875 C CB    . ILE B 2 216 ? 105.636 93.811  84.873  1.00 120.41 ? 216 ILE B CB    1 
ATOM   4876 C CG1   . ILE B 2 216 ? 106.883 93.435  84.067  1.00 120.41 ? 216 ILE B CG1   1 
ATOM   4877 C CG2   . ILE B 2 216 ? 105.613 93.264  86.291  1.00 120.41 ? 216 ILE B CG2   1 
ATOM   4878 C CD1   . ILE B 2 216 ? 108.172 94.060  84.574  1.00 120.41 ? 216 ILE B CD1   1 
ATOM   4879 N N     . ASP B 2 217 ? 102.344 92.680  85.152  1.00 84.86  ? 217 ASP B N     1 
ATOM   4880 C CA    . ASP B 2 217 ? 101.130 92.919  85.900  1.00 84.86  ? 217 ASP B CA    1 
ATOM   4881 C C     . ASP B 2 217 ? 101.504 92.906  87.364  1.00 84.86  ? 217 ASP B C     1 
ATOM   4882 O O     . ASP B 2 217 ? 102.658 92.668  87.712  1.00 84.86  ? 217 ASP B O     1 
ATOM   4883 C CB    . ASP B 2 217 ? 100.095 91.854  85.573  1.00 109.11 ? 217 ASP B CB    1 
ATOM   4884 C CG    . ASP B 2 217 ? 98.673  92.303  85.837  1.00 109.11 ? 217 ASP B CG    1 
ATOM   4885 O OD1   . ASP B 2 217 ? 98.467  93.235  86.618  1.00 109.11 ? 217 ASP B OD1   1 
ATOM   4886 O OD2   . ASP B 2 217 ? 97.754  91.700  85.277  1.00 109.11 ? 217 ASP B OD2   1 
ATOM   4887 N N     . ASP B 2 218 ? 100.543 93.132  88.247  1.00 84.51  ? 218 ASP B N     1 
ATOM   4888 C CA    . ASP B 2 218 ? 100.796 93.152  89.686  1.00 84.51  ? 218 ASP B CA    1 
ATOM   4889 C C     . ASP B 2 218 ? 102.066 93.963  90.001  1.00 84.51  ? 218 ASP B C     1 
ATOM   4890 O O     . ASP B 2 218 ? 102.969 93.419  90.637  1.00 84.51  ? 218 ASP B O     1 
ATOM   4891 C CB    . ASP B 2 218 ? 100.967 91.734  90.244  1.00 108.66 ? 218 ASP B CB    1 
ATOM   4892 C CG    . ASP B 2 218 ? 99.727  90.796  90.212  1.00 108.66 ? 218 ASP B CG    1 
ATOM   4893 O OD1   . ASP B 2 218 ? 98.615  91.168  90.626  1.00 108.66 ? 218 ASP B OD1   1 
ATOM   4894 O OD2   . ASP B 2 218 ? 99.928  89.619  89.835  1.00 108.66 ? 218 ASP B OD2   1 
ATOM   4895 N N     . PRO B 2 219 ? 102.181 95.212  89.575  1.00 80.88  ? 219 PRO B N     1 
ATOM   4896 C CA    . PRO B 2 219 ? 103.426 95.938  89.786  1.00 80.88  ? 219 PRO B CA    1 
ATOM   4897 C C     . PRO B 2 219 ? 103.739 96.027  91.254  1.00 80.88  ? 219 PRO B C     1 
ATOM   4898 O O     . PRO B 2 219 ? 102.847 96.250  92.060  1.00 80.88  ? 219 PRO B O     1 
ATOM   4899 C CB    . PRO B 2 219 ? 103.115 97.313  89.221  1.00 534.02 ? 219 PRO B CB    1 
ATOM   4900 C CG    . PRO B 2 219 ? 102.017 97.075  88.298  1.00 534.02 ? 219 PRO B CG    1 
ATOM   4901 C CD    . PRO B 2 219 ? 101.184 96.051  88.942  1.00 534.02 ? 219 PRO B CD    1 
ATOM   4902 N N     . ILE B 2 220 ? 105.012 95.890  91.600  1.00 77.86  ? 220 ILE B N     1 
ATOM   4903 C CA    . ILE B 2 220 ? 105.467 95.987  92.974  1.00 77.86  ? 220 ILE B CA    1 
ATOM   4904 C C     . ILE B 2 220 ? 106.648 96.926  93.061  1.00 77.86  ? 220 ILE B C     1 
ATOM   4905 O O     . ILE B 2 220 ? 107.278 97.249  92.056  1.00 77.86  ? 220 ILE B O     1 
ATOM   4906 C CB    . ILE B 2 220 ? 105.837 94.624  93.532  1.00 115.27 ? 220 ILE B CB    1 
ATOM   4907 C CG1   . ILE B 2 220 ? 106.935 93.991  92.673  1.00 115.27 ? 220 ILE B CG1   1 
ATOM   4908 C CG2   . ILE B 2 220 ? 104.594 93.772  93.606  1.00 115.27 ? 220 ILE B CG2   1 
ATOM   4909 C CD1   . ILE B 2 220 ? 107.490 92.680  93.213  1.00 115.27 ? 220 ILE B CD1   1 
ATOM   4910 N N     . TYR B 2 221 ? 106.964 97.354  94.276  1.00 81.41  ? 221 TYR B N     1 
ATOM   4911 C CA    . TYR B 2 221 ? 108.054 98.299  94.418  1.00 81.41  ? 221 TYR B CA    1 
ATOM   4912 C C     . TYR B 2 221 ? 109.374 97.679  94.032  1.00 81.41  ? 221 TYR B C     1 
ATOM   4913 O O     . TYR B 2 221 ? 110.241 98.361  93.477  1.00 81.41  ? 221 TYR B O     1 
ATOM   4914 C CB    . TYR B 2 221 ? 108.117 98.861  95.822  1.00 112.72 ? 221 TYR B CB    1 
ATOM   4915 C CG    . TYR B 2 221 ? 107.091 99.918  96.069  1.00 112.72 ? 221 TYR B CG    1 
ATOM   4916 C CD1   . TYR B 2 221 ? 107.186 101.154 95.467  1.00 112.72 ? 221 TYR B CD1   1 
ATOM   4917 C CD2   . TYR B 2 221 ? 106.044 99.676  96.892  1.00 112.72 ? 221 TYR B CD2   1 
ATOM   4918 C CE1   . TYR B 2 221 ? 106.247 102.116 95.691  1.00 112.72 ? 221 TYR B CE1   1 
ATOM   4919 C CE2   . TYR B 2 221 ? 105.107 100.628 97.126  1.00 112.72 ? 221 TYR B CE2   1 
ATOM   4920 C CZ    . TYR B 2 221 ? 105.210 101.846 96.525  1.00 112.72 ? 221 TYR B CZ    1 
ATOM   4921 O OH    . TYR B 2 221 ? 104.258 102.803 96.779  1.00 112.72 ? 221 TYR B OH    1 
ATOM   4922 N N     . ASP B 2 222 ? 109.506 96.374  94.193  1.00 77.64  ? 222 ASP B N     1 
ATOM   4923 C CA    . ASP B 2 222 ? 110.761 95.752  93.799  1.00 77.64  ? 222 ASP B CA    1 
ATOM   4924 C C     . ASP B 2 222 ? 111.093 95.970  92.323  1.00 77.64  ? 222 ASP B C     1 
ATOM   4925 O O     . ASP B 2 222 ? 112.268 95.966  91.960  1.00 77.64  ? 222 ASP B O     1 
ATOM   4926 C CB    . ASP B 2 222 ? 110.725 94.257  94.060  1.00 99.82  ? 222 ASP B CB    1 
ATOM   4927 C CG    . ASP B 2 222 ? 110.701 93.898  95.528  1.00 99.82  ? 222 ASP B CG    1 
ATOM   4928 O OD1   . ASP B 2 222 ? 110.949 94.748  96.385  1.00 99.82  ? 222 ASP B OD1   1 
ATOM   4929 O OD2   . ASP B 2 222 ? 110.428 92.733  95.817  1.00 99.82  ? 222 ASP B OD2   1 
ATOM   4930 N N     . ASP B 2 223 ? 110.106 96.122  91.451  1.00 78.79  ? 223 ASP B N     1 
ATOM   4931 C CA    . ASP B 2 223 ? 110.431 96.363  90.050  1.00 78.79  ? 223 ASP B CA    1 
ATOM   4932 C C     . ASP B 2 223 ? 110.609 97.856  89.762  1.00 78.79  ? 223 ASP B C     1 
ATOM   4933 O O     . ASP B 2 223 ? 111.498 98.272  88.998  1.00 78.79  ? 223 ASP B O     1 
ATOM   4934 C CB    . ASP B 2 223 ? 109.327 95.821  89.139  1.00 101.30 ? 223 ASP B CB    1 
ATOM   4935 C CG    . ASP B 2 223 ? 109.106 94.343  89.285  1.00 101.30 ? 223 ASP B CG    1 
ATOM   4936 O OD1   . ASP B 2 223 ? 110.051 93.566  89.146  1.00 101.30 ? 223 ASP B OD1   1 
ATOM   4937 O OD2   . ASP B 2 223 ? 107.960 93.963  89.516  1.00 101.30 ? 223 ASP B OD2   1 
ATOM   4938 N N     . LEU B 2 224 ? 109.800 98.669  90.410  1.00 77.29  ? 224 LEU B N     1 
ATOM   4939 C CA    . LEU B 2 224 ? 109.895 100.096 90.217  1.00 77.29  ? 224 LEU B CA    1 
ATOM   4940 C C     . LEU B 2 224 ? 111.258 100.569 90.638  1.00 77.29  ? 224 LEU B C     1 
ATOM   4941 O O     . LEU B 2 224 ? 111.854 101.444 89.999  1.00 77.29  ? 224 LEU B O     1 
ATOM   4942 C CB    . LEU B 2 224 ? 108.811 100.789 91.030  1.00 114.43 ? 224 LEU B CB    1 
ATOM   4943 C CG    . LEU B 2 224 ? 107.375 100.525 90.589  1.00 114.43 ? 224 LEU B CG    1 
ATOM   4944 C CD1   . LEU B 2 224 ? 106.407 100.994 91.640  1.00 114.43 ? 224 LEU B CD1   1 
ATOM   4945 C CD2   . LEU B 2 224 ? 107.096 101.265 89.310  1.00 114.43 ? 224 LEU B CD2   1 
ATOM   4946 N N     . ASN B 2 225 ? 111.783 99.992  91.695  1.00 78.54  ? 225 ASN B N     1 
ATOM   4947 C CA    . ASN B 2 225 ? 113.073 100.418 92.151  1.00 78.54  ? 225 ASN B CA    1 
ATOM   4948 C C     . ASN B 2 225 ? 114.111 100.106 91.128  1.00 78.54  ? 225 ASN B C     1 
ATOM   4949 O O     . ASN B 2 225 ? 115.177 100.740 91.124  1.00 78.54  ? 225 ASN B O     1 
ATOM   4950 C CB    . ASN B 2 225 ? 113.407 99.771  93.459  1.00 106.41 ? 225 ASN B CB    1 
ATOM   4951 C CG    . ASN B 2 225 ? 112.665 100.354 94.541  1.00 106.41 ? 225 ASN B CG    1 
ATOM   4952 O OD1   . ASN B 2 225 ? 112.318 101.513 94.473  1.00 106.41 ? 225 ASN B OD1   1 
ATOM   4953 N ND2   . ASN B 2 225 ? 112.366 99.583  95.548  1.00 106.41 ? 225 ASN B ND2   1 
ATOM   4954 N N     . HIS B 2 226 ? 113.791 99.189  90.224  1.00 77.55  ? 226 HIS B N     1 
ATOM   4955 C CA    . HIS B 2 226 ? 114.766 98.870  89.221  1.00 77.55  ? 226 HIS B CA    1 
ATOM   4956 C C     . HIS B 2 226 ? 114.861 100.045 88.379  1.00 77.55  ? 226 HIS B C     1 
ATOM   4957 O O     . HIS B 2 226 ? 115.838 100.789 88.363  1.00 77.55  ? 226 HIS B O     1 
ATOM   4958 C CB    . HIS B 2 226 ? 114.287 97.813  88.272  1.00 105.47 ? 226 HIS B CB    1 
ATOM   4959 C CG    . HIS B 2 226 ? 114.290 96.443  88.812  1.00 105.47 ? 226 HIS B CG    1 
ATOM   4960 N ND1   . HIS B 2 226 ? 113.202 95.611  88.704  1.00 105.47 ? 226 HIS B ND1   1 
ATOM   4961 C CD2   . HIS B 2 226 ? 115.251 95.736  89.439  1.00 105.47 ? 226 HIS B CD2   1 
ATOM   4962 C CE1   . HIS B 2 226 ? 113.485 94.453  89.267  1.00 105.47 ? 226 HIS B CE1   1 
ATOM   4963 N NE2   . HIS B 2 226 ? 114.723 94.503  89.720  1.00 105.47 ? 226 HIS B NE2   1 
ATOM   4964 N N     . VAL B 2 227 ? 113.754 100.274 87.748  1.00 74.15  ? 227 VAL B N     1 
ATOM   4965 C CA    . VAL B 2 227 ? 113.859 101.255 86.706  1.00 74.15  ? 227 VAL B CA    1 
ATOM   4966 C C     . VAL B 2 227 ? 114.443 102.535 87.258  1.00 74.15  ? 227 VAL B C     1 
ATOM   4967 O O     . VAL B 2 227 ? 115.173 103.243 86.556  1.00 74.15  ? 227 VAL B O     1 
ATOM   4968 C CB    . VAL B 2 227 ? 112.512 101.459 86.006  1.00 107.85 ? 227 VAL B CB    1 
ATOM   4969 C CG1   . VAL B 2 227 ? 111.478 102.065 86.913  1.00 107.85 ? 227 VAL B CG1   1 
ATOM   4970 C CG2   . VAL B 2 227 ? 112.720 102.327 84.836  1.00 107.85 ? 227 VAL B CG2   1 
ATOM   4971 N N     . ILE B 2 228 ? 114.207 102.817 88.531  1.00 73.54  ? 228 ILE B N     1 
ATOM   4972 C CA    . ILE B 2 228 ? 114.803 104.006 89.108  1.00 73.54  ? 228 ILE B CA    1 
ATOM   4973 C C     . ILE B 2 228 ? 116.313 103.856 89.182  1.00 73.54  ? 228 ILE B C     1 
ATOM   4974 O O     . ILE B 2 228 ? 117.054 104.765 88.783  1.00 73.54  ? 228 ILE B O     1 
ATOM   4975 C CB    . ILE B 2 228 ? 114.220 104.313 90.489  1.00 108.88 ? 228 ILE B CB    1 
ATOM   4976 C CG1   . ILE B 2 228 ? 112.753 104.671 90.351  1.00 108.88 ? 228 ILE B CG1   1 
ATOM   4977 C CG2   . ILE B 2 228 ? 114.956 105.483 91.087  1.00 108.88 ? 228 ILE B CG2   1 
ATOM   4978 C CD1   . ILE B 2 228 ? 111.982 104.661 91.658  1.00 108.88 ? 228 ILE B CD1   1 
ATOM   4979 N N     . SER B 2 229 ? 116.803 102.727 89.696  1.00 71.53  ? 229 SER B N     1 
ATOM   4980 C CA    . SER B 2 229 ? 118.242 102.605 89.840  1.00 71.53  ? 229 SER B CA    1 
ATOM   4981 C C     . SER B 2 229 ? 118.915 102.527 88.507  1.00 71.53  ? 229 SER B C     1 
ATOM   4982 O O     . SER B 2 229 ? 120.054 102.969 88.366  1.00 71.53  ? 229 SER B O     1 
ATOM   4983 C CB    . SER B 2 229 ? 118.611 101.361 90.614  1.00 96.35  ? 229 SER B CB    1 
ATOM   4984 O OG    . SER B 2 229 ? 118.344 100.227 89.832  1.00 96.35  ? 229 SER B OG    1 
ATOM   4985 N N     . GLN B 2 230 ? 118.230 101.963 87.530  1.00 70.71  ? 230 GLN B N     1 
ATOM   4986 C CA    . GLN B 2 230 ? 118.775 101.825 86.186  1.00 70.71  ? 230 GLN B CA    1 
ATOM   4987 C C     . GLN B 2 230 ? 118.961 103.199 85.550  1.00 70.71  ? 230 GLN B C     1 
ATOM   4988 O O     . GLN B 2 230 ? 120.005 103.502 84.945  1.00 70.71  ? 230 GLN B O     1 
ATOM   4989 C CB    . GLN B 2 230 ? 117.831 100.935 85.366  1.00 98.80  ? 230 GLN B CB    1 
ATOM   4990 C CG    . GLN B 2 230 ? 118.299 100.478 84.026  1.00 98.80  ? 230 GLN B CG    1 
ATOM   4991 C CD    . GLN B 2 230 ? 119.517 99.597  84.067  1.00 98.80  ? 230 GLN B CD    1 
ATOM   4992 O OE1   . GLN B 2 230 ? 119.580 98.571  84.757  1.00 98.80  ? 230 GLN B OE1   1 
ATOM   4993 N NE2   . GLN B 2 230 ? 120.519 100.002 83.300  1.00 98.80  ? 230 GLN B NE2   1 
ATOM   4994 N N     . ALA B 2 231 ? 117.978 104.068 85.726  1.00 65.85  ? 231 ALA B N     1 
ATOM   4995 C CA    . ALA B 2 231 ? 118.146 105.400 85.196  1.00 65.85  ? 231 ALA B CA    1 
ATOM   4996 C C     . ALA B 2 231 ? 119.253 106.122 85.920  1.00 65.85  ? 231 ALA B C     1 
ATOM   4997 O O     . ALA B 2 231 ? 120.021 106.841 85.297  1.00 65.85  ? 231 ALA B O     1 
ATOM   4998 C CB    . ALA B 2 231 ? 116.842 106.169 85.302  1.00 89.80  ? 231 ALA B CB    1 
ATOM   4999 N N     . LEU B 2 232 ? 119.355 105.933 87.228  1.00 65.56  ? 232 LEU B N     1 
ATOM   5000 C CA    . LEU B 2 232 ? 120.352 106.648 88.003  1.00 65.56  ? 232 LEU B CA    1 
ATOM   5001 C C     . LEU B 2 232 ? 121.740 106.232 87.622  1.00 65.56  ? 232 LEU B C     1 
ATOM   5002 O O     . LEU B 2 232 ? 122.647 107.068 87.550  1.00 65.56  ? 232 LEU B O     1 
ATOM   5003 C CB    . LEU B 2 232 ? 120.174 106.417 89.503  1.00 97.06  ? 232 LEU B CB    1 
ATOM   5004 C CG    . LEU B 2 232 ? 121.142 107.151 90.483  1.00 97.06  ? 232 LEU B CG    1 
ATOM   5005 C CD1   . LEU B 2 232 ? 121.054 108.658 90.324  1.00 97.06  ? 232 LEU B CD1   1 
ATOM   5006 C CD2   . LEU B 2 232 ? 120.837 106.776 91.941  1.00 97.06  ? 232 LEU B CD2   1 
ATOM   5007 N N     . SER B 2 233 ? 121.939 104.951 87.408  1.00 63.75  ? 233 SER B N     1 
ATOM   5008 C CA    . SER B 2 233 ? 123.260 104.507 87.025  1.00 63.75  ? 233 SER B CA    1 
ATOM   5009 C C     . SER B 2 233 ? 123.611 105.000 85.632  1.00 63.75  ? 233 SER B C     1 
ATOM   5010 O O     . SER B 2 233 ? 124.788 105.210 85.336  1.00 63.75  ? 233 SER B O     1 
ATOM   5011 C CB    . SER B 2 233 ? 123.351 102.991 87.114  1.00 85.87  ? 233 SER B CB    1 
ATOM   5012 O OG    . SER B 2 233 ? 122.586 102.368 86.110  1.00 85.87  ? 233 SER B OG    1 
ATOM   5013 N N     . ASP B 2 234 ? 122.615 105.240 84.781  1.00 64.16  ? 234 ASP B N     1 
ATOM   5014 C CA    . ASP B 2 234 ? 122.942 105.818 83.486  1.00 64.16  ? 234 ASP B CA    1 
ATOM   5015 C C     . ASP B 2 234 ? 123.219 107.316 83.599  1.00 64.16  ? 234 ASP B C     1 
ATOM   5016 O O     . ASP B 2 234 ? 124.211 107.817 83.086  1.00 64.16  ? 234 ASP B O     1 
ATOM   5017 C CB    . ASP B 2 234 ? 121.809 105.543 82.515  1.00 82.49  ? 234 ASP B CB    1 
ATOM   5018 C CG    . ASP B 2 234 ? 122.245 105.666 81.086  1.00 82.49  ? 234 ASP B CG    1 
ATOM   5019 O OD1   . ASP B 2 234 ? 123.017 104.816 80.640  1.00 82.49  ? 234 ASP B OD1   1 
ATOM   5020 O OD2   . ASP B 2 234 ? 121.854 106.621 80.413  1.00 82.49  ? 234 ASP B OD2   1 
ATOM   5021 N N     . ILE B 2 235 ? 122.405 108.037 84.348  1.00 61.09  ? 235 ILE B N     1 
ATOM   5022 C CA    . ILE B 2 235 ? 122.559 109.477 84.422  1.00 61.09  ? 235 ILE B CA    1 
ATOM   5023 C C     . ILE B 2 235 ? 123.905 109.839 84.976  1.00 61.09  ? 235 ILE B C     1 
ATOM   5024 O O     . ILE B 2 235 ? 124.558 110.754 84.486  1.00 61.09  ? 235 ILE B O     1 
ATOM   5025 C CB    . ILE B 2 235 ? 121.439 110.109 85.263  1.00 90.44  ? 235 ILE B CB    1 
ATOM   5026 C CG1   . ILE B 2 235 ? 120.084 109.976 84.537  1.00 90.44  ? 235 ILE B CG1   1 
ATOM   5027 C CG2   . ILE B 2 235 ? 121.770 111.580 85.557  1.00 90.44  ? 235 ILE B CG2   1 
ATOM   5028 C CD1   . ILE B 2 235 ? 118.842 110.256 85.405  1.00 90.44  ? 235 ILE B CD1   1 
ATOM   5029 N N     . THR B 2 236 ? 124.333 109.156 86.010  1.00 61.17  ? 236 THR B N     1 
ATOM   5030 C CA    . THR B 2 236 ? 125.576 109.476 86.665  1.00 61.17  ? 236 THR B CA    1 
ATOM   5031 C C     . THR B 2 236 ? 126.777 108.881 85.956  1.00 61.17  ? 236 THR B C     1 
ATOM   5032 O O     . THR B 2 236 ? 127.914 109.118 86.367  1.00 61.17  ? 236 THR B O     1 
ATOM   5033 C CB    . THR B 2 236 ? 125.553 109.013 88.116  1.00 85.64  ? 236 THR B CB    1 
ATOM   5034 O OG1   . THR B 2 236 ? 125.304 107.601 88.186  1.00 85.64  ? 236 THR B OG1   1 
ATOM   5035 C CG2   . THR B 2 236 ? 124.497 109.761 88.935  1.00 85.64  ? 236 THR B CG2   1 
ATOM   5036 N N     . ALA B 2 237 ? 126.548 108.146 84.871  1.00 62.48  ? 237 ALA B N     1 
ATOM   5037 C CA    . ALA B 2 237 ? 127.612 107.445 84.157  1.00 62.48  ? 237 ALA B CA    1 
ATOM   5038 C C     . ALA B 2 237 ? 128.680 108.369 83.601  1.00 62.48  ? 237 ALA B C     1 
ATOM   5039 O O     . ALA B 2 237 ? 129.841 107.968 83.507  1.00 62.48  ? 237 ALA B O     1 
ATOM   5040 C CB    . ALA B 2 237 ? 127.027 106.631 83.009  1.00 85.20  ? 237 ALA B CB    1 
ATOM   5041 N N     . SER B 2 238 ? 128.330 109.579 83.186  1.00 58.36  ? 238 SER B N     1 
ATOM   5042 C CA    . SER B 2 238 ? 129.360 110.401 82.597  1.00 58.36  ? 238 SER B CA    1 
ATOM   5043 C C     . SER B 2 238 ? 130.424 110.723 83.604  1.00 58.36  ? 238 SER B C     1 
ATOM   5044 O O     . SER B 2 238 ? 131.566 111.007 83.234  1.00 58.36  ? 238 SER B O     1 
ATOM   5045 C CB    . SER B 2 238 ? 128.795 111.684 82.094  1.00 78.61  ? 238 SER B CB    1 
ATOM   5046 O OG    . SER B 2 238 ? 128.530 112.508 83.201  1.00 78.61  ? 238 SER B OG    1 
ATOM   5047 N N     . LEU B 2 239 ? 130.095 110.644 84.863  1.00 60.85  ? 239 LEU B N     1 
ATOM   5048 C CA    . LEU B 2 239 ? 131.047 111.020 85.879  1.00 60.85  ? 239 LEU B CA    1 
ATOM   5049 C C     . LEU B 2 239 ? 132.056 109.922 86.105  1.00 60.85  ? 239 LEU B C     1 
ATOM   5050 O O     . LEU B 2 239 ? 133.014 110.118 86.859  1.00 60.85  ? 239 LEU B O     1 
ATOM   5051 C CB    . LEU B 2 239 ? 130.313 111.327 87.189  1.00 90.09  ? 239 LEU B CB    1 
ATOM   5052 C CG    . LEU B 2 239 ? 129.292 112.483 87.233  1.00 90.09  ? 239 LEU B CG    1 
ATOM   5053 C CD1   . LEU B 2 239 ? 128.523 112.458 88.575  1.00 90.09  ? 239 LEU B CD1   1 
ATOM   5054 C CD2   . LEU B 2 239 ? 130.001 113.829 87.050  1.00 90.09  ? 239 LEU B CD2   1 
ATOM   5055 N N     . ARG B 2 240 ? 131.848 108.761 85.489  1.00 63.17  ? 240 ARG B N     1 
ATOM   5056 C CA    . ARG B 2 240 ? 132.719 107.619 85.704  1.00 63.17  ? 240 ARG B CA    1 
ATOM   5057 C C     . ARG B 2 240 ? 133.637 107.287 84.539  1.00 63.17  ? 240 ARG B C     1 
ATOM   5058 O O     . ARG B 2 240 ? 134.414 106.336 84.636  1.00 63.17  ? 240 ARG B O     1 
ATOM   5059 C CB    . ARG B 2 240 ? 131.873 106.401 86.022  1.00 92.82  ? 240 ARG B CB    1 
ATOM   5060 C CG    . ARG B 2 240 ? 131.077 106.590 87.267  1.00 92.82  ? 240 ARG B CG    1 
ATOM   5061 C CD    . ARG B 2 240 ? 130.472 105.325 87.759  1.00 92.82  ? 240 ARG B CD    1 
ATOM   5062 N NE    . ARG B 2 240 ? 129.457 104.764 86.880  1.00 92.82  ? 240 ARG B NE    1 
ATOM   5063 C CZ    . ARG B 2 240 ? 128.169 105.087 86.903  1.00 92.82  ? 240 ARG B CZ    1 
ATOM   5064 N NH1   . ARG B 2 240 ? 127.705 106.023 87.716  1.00 92.82  ? 240 ARG B NH1   1 
ATOM   5065 N NH2   . ARG B 2 240 ? 127.330 104.456 86.084  1.00 92.82  ? 240 ARG B NH2   1 
ATOM   5066 N N     . PHE B 2 241 ? 133.572 108.021 83.438  1.00 63.12  ? 241 PHE B N     1 
ATOM   5067 C CA    . PHE B 2 241 ? 134.363 107.632 82.279  1.00 63.12  ? 241 PHE B CA    1 
ATOM   5068 C C     . PHE B 2 241 ? 134.982 108.799 81.540  1.00 63.12  ? 241 PHE B C     1 
ATOM   5069 O O     . PHE B 2 241 ? 134.498 109.929 81.581  1.00 63.12  ? 241 PHE B O     1 
ATOM   5070 C CB    . PHE B 2 241 ? 133.525 106.865 81.277  1.00 88.07  ? 241 PHE B CB    1 
ATOM   5071 C CG    . PHE B 2 241 ? 133.079 105.539 81.761  1.00 88.07  ? 241 PHE B CG    1 
ATOM   5072 C CD1   . PHE B 2 241 ? 131.900 105.407 82.441  1.00 88.07  ? 241 PHE B CD1   1 
ATOM   5073 C CD2   . PHE B 2 241 ? 133.832 104.414 81.515  1.00 88.07  ? 241 PHE B CD2   1 
ATOM   5074 C CE1   . PHE B 2 241 ? 131.490 104.187 82.875  1.00 88.07  ? 241 PHE B CE1   1 
ATOM   5075 C CE2   . PHE B 2 241 ? 133.416 103.188 81.953  1.00 88.07  ? 241 PHE B CE2   1 
ATOM   5076 C CZ    . PHE B 2 241 ? 132.247 103.079 82.636  1.00 88.07  ? 241 PHE B CZ    1 
ATOM   5077 N N     . LYS B 2 242 ? 136.048 108.499 80.822  1.00 65.98  ? 242 LYS B N     1 
ATOM   5078 C CA    . LYS B 2 242 ? 136.555 109.474 79.887  1.00 65.98  ? 242 LYS B CA    1 
ATOM   5079 C C     . LYS B 2 242 ? 135.437 109.789 78.913  1.00 65.98  ? 242 LYS B C     1 
ATOM   5080 O O     . LYS B 2 242 ? 134.817 108.884 78.355  1.00 65.98  ? 242 LYS B O     1 
ATOM   5081 C CB    . LYS B 2 242 ? 137.767 108.931 79.144  1.00 98.97  ? 242 LYS B CB    1 
ATOM   5082 C CG    . LYS B 2 242 ? 138.390 109.909 78.190  1.00 98.97  ? 242 LYS B CG    1 
ATOM   5083 C CD    . LYS B 2 242 ? 139.630 109.315 77.529  1.00 98.97  ? 242 LYS B CD    1 
ATOM   5084 C CE    . LYS B 2 242 ? 140.270 110.293 76.551  1.00 98.97  ? 242 LYS B CE    1 
ATOM   5085 N NZ    . LYS B 2 242 ? 141.476 109.715 75.890  1.00 98.97  ? 242 LYS B NZ    1 
ATOM   5086 N N     . GLY B 2 243 ? 135.170 111.066 78.707  1.00 64.33  ? 243 GLY B N     1 
ATOM   5087 C CA    . GLY B 2 243 ? 134.091 111.444 77.824  1.00 64.33  ? 243 GLY B CA    1 
ATOM   5088 C C     . GLY B 2 243 ? 134.021 112.948 77.730  1.00 64.33  ? 243 GLY B C     1 
ATOM   5089 O O     . GLY B 2 243 ? 134.940 113.653 78.137  1.00 64.33  ? 243 GLY B O     1 
ATOM   5090 N N     . SER B 2 244 ? 132.915 113.431 77.184  1.00 64.13  ? 244 SER B N     1 
ATOM   5091 C CA    . SER B 2 244 ? 132.686 114.856 76.992  1.00 64.13  ? 244 SER B CA    1 
ATOM   5092 C C     . SER B 2 244 ? 131.309 115.203 77.540  1.00 64.13  ? 244 SER B C     1 
ATOM   5093 O O     . SER B 2 244 ? 130.717 114.456 78.322  1.00 64.13  ? 244 SER B O     1 
ATOM   5094 C CB    . SER B 2 244 ? 132.778 115.248 75.528  1.00 86.38  ? 244 SER B CB    1 
ATOM   5095 O OG    . SER B 2 244 ? 132.745 116.646 75.389  1.00 86.38  ? 244 SER B OG    1 
ATOM   5096 N N     . LEU B 2 245 ? 130.802 116.352 77.131  1.00 63.03  ? 245 LEU B N     1 
ATOM   5097 C CA    . LEU B 2 245 ? 129.541 116.867 77.613  1.00 63.03  ? 245 LEU B CA    1 
ATOM   5098 C C     . LEU B 2 245 ? 129.670 117.139 79.086  1.00 63.03  ? 245 LEU B C     1 
ATOM   5099 O O     . LEU B 2 245 ? 130.667 117.694 79.554  1.00 63.03  ? 245 LEU B O     1 
ATOM   5100 C CB    . LEU B 2 245 ? 128.412 115.927 77.400  1.00 93.32  ? 245 LEU B CB    1 
ATOM   5101 C CG    . LEU B 2 245 ? 128.139 115.354 76.089  1.00 93.32  ? 245 LEU B CG    1 
ATOM   5102 C CD1   . LEU B 2 245 ? 126.990 114.378 76.298  1.00 93.32  ? 245 LEU B CD1   1 
ATOM   5103 C CD2   . LEU B 2 245 ? 127.784 116.465 75.136  1.00 93.32  ? 245 LEU B CD2   1 
ATOM   5104 N N     . ASN B 2 246 ? 128.690 116.747 79.845  1.00 59.80  ? 246 ASN B N     1 
ATOM   5105 C CA    . ASN B 2 246 ? 128.673 117.049 81.238  1.00 59.80  ? 246 ASN B CA    1 
ATOM   5106 C C     . ASN B 2 246 ? 129.422 115.978 81.963  1.00 59.80  ? 246 ASN B C     1 
ATOM   5107 O O     . ASN B 2 246 ? 128.854 114.977 82.365  1.00 59.80  ? 246 ASN B O     1 
ATOM   5108 C CB    . ASN B 2 246 ? 127.261 117.135 81.736  1.00 81.02  ? 246 ASN B CB    1 
ATOM   5109 C CG    . ASN B 2 246 ? 126.528 118.270 81.148  1.00 81.02  ? 246 ASN B CG    1 
ATOM   5110 O OD1   . ASN B 2 246 ? 127.117 119.290 80.793  1.00 81.02  ? 246 ASN B OD1   1 
ATOM   5111 N ND2   . ASN B 2 246 ? 125.224 118.130 81.055  1.00 81.02  ? 246 ASN B ND2   1 
ATOM   5112 N N     . THR B 2 247 ? 130.702 116.225 82.152  1.00 56.09  ? 247 THR B N     1 
ATOM   5113 C CA    . THR B 2 247 ? 131.620 115.328 82.809  1.00 56.09  ? 247 THR B CA    1 
ATOM   5114 C C     . THR B 2 247 ? 131.874 115.720 84.240  1.00 56.09  ? 247 THR B C     1 
ATOM   5115 O O     . THR B 2 247 ? 132.661 115.069 84.936  1.00 56.09  ? 247 THR B O     1 
ATOM   5116 C CB    . THR B 2 247 ? 132.931 115.327 82.073  1.00 78.53  ? 247 THR B CB    1 
ATOM   5117 O OG1   . THR B 2 247 ? 133.491 116.634 82.147  1.00 78.53  ? 247 THR B OG1   1 
ATOM   5118 C CG2   . THR B 2 247 ? 132.709 114.987 80.646  1.00 78.53  ? 247 THR B CG2   1 
ATOM   5119 N N     . ASP B 2 248 ? 131.219 116.781 84.686  1.00 60.58  ? 248 ASP B N     1 
ATOM   5120 C CA    . ASP B 2 248 ? 131.378 117.369 86.008  1.00 60.58  ? 248 ASP B CA    1 
ATOM   5121 C C     . ASP B 2 248 ? 130.063 117.985 86.426  1.00 60.58  ? 248 ASP B C     1 
ATOM   5122 O O     . ASP B 2 248 ? 129.421 118.676 85.630  1.00 60.58  ? 248 ASP B O     1 
ATOM   5123 C CB    . ASP B 2 248 ? 132.445 118.465 85.979  1.00 77.89  ? 248 ASP B CB    1 
ATOM   5124 C CG    . ASP B 2 248 ? 132.831 118.985 87.362  1.00 77.89  ? 248 ASP B CG    1 
ATOM   5125 O OD1   . ASP B 2 248 ? 132.063 119.729 87.995  1.00 77.89  ? 248 ASP B OD1   1 
ATOM   5126 O OD2   . ASP B 2 248 ? 133.941 118.666 87.801  1.00 77.89  ? 248 ASP B OD2   1 
ATOM   5127 N N     . MET B 2 249 ? 129.717 117.818 87.688  1.00 59.37  ? 249 MET B N     1 
ATOM   5128 C CA    . MET B 2 249 ? 128.466 118.367 88.173  1.00 59.37  ? 249 MET B CA    1 
ATOM   5129 C C     . MET B 2 249 ? 128.308 119.849 87.795  1.00 59.37  ? 249 MET B C     1 
ATOM   5130 O O     . MET B 2 249 ? 127.195 120.312 87.505  1.00 59.37  ? 249 MET B O     1 
ATOM   5131 C CB    . MET B 2 249 ? 128.394 118.159 89.684  1.00 85.29  ? 249 MET B CB    1 
ATOM   5132 C CG    . MET B 2 249 ? 128.268 116.712 90.115  1.00 85.29  ? 249 MET B CG    1 
ATOM   5133 S SD    . MET B 2 249 ? 128.458 116.455 91.879  1.00 85.29  ? 249 MET B SD    1 
ATOM   5134 C CE    . MET B 2 249 ? 126.874 116.943 92.517  1.00 85.29  ? 249 MET B CE    1 
ATOM   5135 N N     . LYS B 2 250 ? 129.408 120.609 87.779  1.00 59.10  ? 250 LYS B N     1 
ATOM   5136 C CA    . LYS B 2 250 ? 129.312 122.030 87.462  1.00 59.10  ? 250 LYS B CA    1 
ATOM   5137 C C     . LYS B 2 250 ? 128.861 122.250 86.036  1.00 59.10  ? 250 LYS B C     1 
ATOM   5138 O O     . LYS B 2 250 ? 128.118 123.198 85.743  1.00 59.10  ? 250 LYS B O     1 
ATOM   5139 C CB    . LYS B 2 250 ? 130.641 122.725 87.695  1.00 88.65  ? 250 LYS B CB    1 
ATOM   5140 C CG    . LYS B 2 250 ? 130.568 124.216 87.475  1.00 88.65  ? 250 LYS B CG    1 
ATOM   5141 C CD    . LYS B 2 250 ? 131.833 124.881 87.860  1.00 88.65  ? 250 LYS B CD    1 
ATOM   5142 C CE    . LYS B 2 250 ? 131.748 126.365 87.633  1.00 88.65  ? 250 LYS B CE    1 
ATOM   5143 N NZ    . LYS B 2 250 ? 133.012 127.058 88.009  1.00 88.65  ? 250 LYS B NZ    1 
ATOM   5144 N N     . GLU B 2 251 ? 129.334 121.417 85.131  1.00 58.72  ? 251 GLU B N     1 
ATOM   5145 C CA    . GLU B 2 251 ? 128.977 121.597 83.743  1.00 58.72  ? 251 GLU B CA    1 
ATOM   5146 C C     . GLU B 2 251 ? 127.523 121.269 83.553  1.00 58.72  ? 251 GLU B C     1 
ATOM   5147 O O     . GLU B 2 251 ? 126.837 121.899 82.737  1.00 58.72  ? 251 GLU B O     1 
ATOM   5148 C CB    . GLU B 2 251 ? 129.853 120.722 82.856  1.00 78.88  ? 251 GLU B CB    1 
ATOM   5149 C CG    . GLU B 2 251 ? 131.323 121.122 82.865  1.00 78.88  ? 251 GLU B CG    1 
ATOM   5150 C CD    . GLU B 2 251 ? 131.562 122.516 82.338  1.00 78.88  ? 251 GLU B CD    1 
ATOM   5151 O OE1   . GLU B 2 251 ? 131.087 122.841 81.250  1.00 78.88  ? 251 GLU B OE1   1 
ATOM   5152 O OE2   . GLU B 2 251 ? 132.230 123.288 83.023  1.00 78.88  ? 251 GLU B OE2   1 
ATOM   5153 N N     . PHE B 2 252 ? 127.035 120.310 84.334  1.00 57.57  ? 252 PHE B N     1 
ATOM   5154 C CA    . PHE B 2 252 ? 125.625 119.998 84.268  1.00 57.57  ? 252 PHE B CA    1 
ATOM   5155 C C     . PHE B 2 252 ? 124.845 121.235 84.615  1.00 57.57  ? 252 PHE B C     1 
ATOM   5156 O O     . PHE B 2 252 ? 123.972 121.643 83.853  1.00 57.57  ? 252 PHE B O     1 
ATOM   5157 C CB    . PHE B 2 252 ? 125.218 118.900 85.259  1.00 80.33  ? 252 PHE B CB    1 
ATOM   5158 C CG    . PHE B 2 252 ? 125.546 117.473 84.881  1.00 80.33  ? 252 PHE B CG    1 
ATOM   5159 C CD1   . PHE B 2 252 ? 126.752 116.933 85.225  1.00 80.33  ? 252 PHE B CD1   1 
ATOM   5160 C CD2   . PHE B 2 252 ? 124.601 116.653 84.309  1.00 80.33  ? 252 PHE B CD2   1 
ATOM   5161 C CE1   . PHE B 2 252 ? 127.052 115.626 84.957  1.00 80.33  ? 252 PHE B CE1   1 
ATOM   5162 C CE2   . PHE B 2 252 ? 124.886 115.342 84.035  1.00 80.33  ? 252 PHE B CE2   1 
ATOM   5163 C CZ    . PHE B 2 252 ? 126.119 114.827 84.360  1.00 80.33  ? 252 PHE B CZ    1 
ATOM   5164 N N     . LEU B 2 253 ? 125.225 121.912 85.707  1.00 56.21  ? 253 LEU B N     1 
ATOM   5165 C CA    . LEU B 2 253 ? 124.448 123.080 86.107  1.00 56.21  ? 253 LEU B CA    1 
ATOM   5166 C C     . LEU B 2 253 ? 124.425 124.118 85.007  1.00 56.21  ? 253 LEU B C     1 
ATOM   5167 O O     . LEU B 2 253 ? 123.381 124.716 84.715  1.00 56.21  ? 253 LEU B O     1 
ATOM   5168 C CB    . LEU B 2 253 ? 125.027 123.736 87.340  1.00 83.22  ? 253 LEU B CB    1 
ATOM   5169 C CG    . LEU B 2 253 ? 125.031 122.964 88.646  1.00 83.22  ? 253 LEU B CG    1 
ATOM   5170 C CD1   . LEU B 2 253 ? 125.719 123.820 89.688  1.00 83.22  ? 253 LEU B CD1   1 
ATOM   5171 C CD2   . LEU B 2 253 ? 123.633 122.593 89.076  1.00 83.22  ? 253 LEU B CD2   1 
ATOM   5172 N N     . VAL B 2 254 ? 125.569 124.324 84.364  1.00 54.64  ? 254 VAL B N     1 
ATOM   5173 C CA    . VAL B 2 254 ? 125.621 125.325 83.310  1.00 54.64  ? 254 VAL B CA    1 
ATOM   5174 C C     . VAL B 2 254 ? 124.668 124.986 82.196  1.00 54.64  ? 254 VAL B C     1 
ATOM   5175 O O     . VAL B 2 254 ? 123.955 125.847 81.687  1.00 54.64  ? 254 VAL B O     1 
ATOM   5176 C CB    . VAL B 2 254 ? 127.038 125.451 82.761  1.00 79.48  ? 254 VAL B CB    1 
ATOM   5177 C CG1   . VAL B 2 254 ? 127.036 126.338 81.521  1.00 79.48  ? 254 VAL B CG1   1 
ATOM   5178 C CG2   . VAL B 2 254 ? 127.937 126.022 83.829  1.00 79.48  ? 254 VAL B CG2   1 
ATOM   5179 N N     . ASN B 2 255 ? 124.644 123.744 81.807  1.00 56.17  ? 255 ASN B N     1 
ATOM   5180 C CA    . ASN B 2 255 ? 123.814 123.363 80.695  1.00 56.17  ? 255 ASN B CA    1 
ATOM   5181 C C     . ASN B 2 255 ? 122.359 123.168 81.044  1.00 56.17  ? 255 ASN B C     1 
ATOM   5182 O O     . ASN B 2 255 ? 121.497 123.376 80.194  1.00 56.17  ? 255 ASN B O     1 
ATOM   5183 C CB    . ASN B 2 255 ? 124.411 122.128 80.103  1.00 76.10  ? 255 ASN B CB    1 
ATOM   5184 C CG    . ASN B 2 255 ? 125.651 122.462 79.352  1.00 76.10  ? 255 ASN B CG    1 
ATOM   5185 O OD1   . ASN B 2 255 ? 125.756 123.546 78.770  1.00 76.10  ? 255 ASN B OD1   1 
ATOM   5186 N ND2   . ASN B 2 255 ? 126.611 121.577 79.371  1.00 76.10  ? 255 ASN B ND2   1 
ATOM   5187 N N     . LEU B 2 256 ? 122.055 122.787 82.255  1.00 54.89  ? 256 LEU B N     1 
ATOM   5188 C CA    . LEU B 2 256 ? 120.700 122.425 82.575  1.00 54.89  ? 256 LEU B CA    1 
ATOM   5189 C C     . LEU B 2 256 ? 119.866 123.458 83.341  1.00 54.89  ? 256 LEU B C     1 
ATOM   5190 O O     . LEU B 2 256 ? 118.640 123.317 83.361  1.00 54.89  ? 256 LEU B O     1 
ATOM   5191 C CB    . LEU B 2 256 ? 120.731 121.116 83.334  1.00 81.27  ? 256 LEU B CB    1 
ATOM   5192 C CG    . LEU B 2 256 ? 121.231 119.946 82.479  1.00 81.27  ? 256 LEU B CG    1 
ATOM   5193 C CD1   . LEU B 2 256 ? 121.424 118.756 83.352  1.00 81.27  ? 256 LEU B CD1   1 
ATOM   5194 C CD2   . LEU B 2 256 ? 120.217 119.586 81.363  1.00 81.27  ? 256 LEU B CD2   1 
ATOM   5195 N N     . VAL B 2 257 ? 120.443 124.470 83.980  1.00 56.06  ? 257 VAL B N     1 
ATOM   5196 C CA    . VAL B 2 257 ? 119.610 125.399 84.739  1.00 56.06  ? 257 VAL B CA    1 
ATOM   5197 C C     . VAL B 2 257 ? 119.854 126.852 84.369  1.00 56.06  ? 257 VAL B C     1 
ATOM   5198 O O     . VAL B 2 257 ? 120.570 127.561 85.093  1.00 56.06  ? 257 VAL B O     1 
ATOM   5199 C CB    . VAL B 2 257 ? 119.849 125.260 86.243  1.00 81.54  ? 257 VAL B CB    1 
ATOM   5200 C CG1   . VAL B 2 257 ? 118.847 126.157 87.011  1.00 81.54  ? 257 VAL B CG1   1 
ATOM   5201 C CG2   . VAL B 2 257 ? 119.768 123.792 86.677  1.00 81.54  ? 257 VAL B CG2   1 
ATOM   5202 N N     . PRO B 2 258 ? 119.308 127.336 83.265  1.00 56.59  ? 258 PRO B N     1 
ATOM   5203 C CA    . PRO B 2 258 ? 119.394 128.767 83.001  1.00 56.59  ? 258 PRO B CA    1 
ATOM   5204 C C     . PRO B 2 258 ? 118.365 129.440 83.877  1.00 56.59  ? 258 PRO B C     1 
ATOM   5205 O O     . PRO B 2 258 ? 117.289 128.881 84.081  1.00 56.59  ? 258 PRO B O     1 
ATOM   5206 C CB    . PRO B 2 258 ? 119.008 128.885 81.521  1.00 373.65 ? 258 PRO B CB    1 
ATOM   5207 C CG    . PRO B 2 258 ? 118.878 127.484 81.015  1.00 373.65 ? 258 PRO B CG    1 
ATOM   5208 C CD    . PRO B 2 258 ? 118.574 126.642 82.201  1.00 373.65 ? 258 PRO B CD    1 
ATOM   5209 N N     . TYR B 2 259 ? 118.687 130.625 84.413  1.00 60.13  ? 259 TYR B N     1 
ATOM   5210 C CA    . TYR B 2 259 ? 117.778 131.307 85.339  1.00 60.13  ? 259 TYR B CA    1 
ATOM   5211 C C     . TYR B 2 259 ? 117.735 130.548 86.653  1.00 60.13  ? 259 TYR B C     1 
ATOM   5212 O O     . TYR B 2 259 ? 118.151 129.393 86.715  1.00 60.13  ? 259 TYR B O     1 
ATOM   5213 C CB    . TYR B 2 259 ? 116.372 131.449 84.751  1.00 83.26  ? 259 TYR B CB    1 
ATOM   5214 C CG    . TYR B 2 259 ? 116.350 131.908 83.311  1.00 83.26  ? 259 TYR B CG    1 
ATOM   5215 C CD1   . TYR B 2 259 ? 116.674 133.214 82.975  1.00 83.26  ? 259 TYR B CD1   1 
ATOM   5216 C CD2   . TYR B 2 259 ? 116.004 131.037 82.284  1.00 83.26  ? 259 TYR B CD2   1 
ATOM   5217 C CE1   . TYR B 2 259 ? 116.657 133.641 81.657  1.00 83.26  ? 259 TYR B CE1   1 
ATOM   5218 C CE2   . TYR B 2 259 ? 115.987 131.452 80.966  1.00 83.26  ? 259 TYR B CE2   1 
ATOM   5219 C CZ    . TYR B 2 259 ? 116.313 132.756 80.658  1.00 83.26  ? 259 TYR B CZ    1 
ATOM   5220 O OH    . TYR B 2 259 ? 116.295 133.178 79.348  1.00 83.26  ? 259 TYR B OH    1 
ATOM   5221 N N     . PRO B 2 260 ? 117.279 131.166 87.727  1.00 61.29  ? 260 PRO B N     1 
ATOM   5222 C CA    . PRO B 2 260 ? 117.312 130.509 89.035  1.00 61.29  ? 260 PRO B CA    1 
ATOM   5223 C C     . PRO B 2 260 ? 116.016 129.760 89.320  1.00 61.29  ? 260 PRO B C     1 
ATOM   5224 O O     . PRO B 2 260 ? 115.033 129.915 88.613  1.00 61.29  ? 260 PRO B O     1 
ATOM   5225 C CB    . PRO B 2 260 ? 117.473 131.690 89.996  1.00 404.68 ? 260 PRO B CB    1 
ATOM   5226 C CG    . PRO B 2 260 ? 116.741 132.813 89.319  1.00 404.68 ? 260 PRO B CG    1 
ATOM   5227 C CD    . PRO B 2 260 ? 116.845 132.576 87.831  1.00 404.68 ? 260 PRO B CD    1 
ATOM   5228 N N     . ARG B 2 261 ? 116.043 128.931 90.349  1.00 60.75  ? 261 ARG B N     1 
ATOM   5229 C CA    . ARG B 2 261 ? 114.867 128.224 90.835  1.00 60.75  ? 261 ARG B CA    1 
ATOM   5230 C C     . ARG B 2 261 ? 114.309 127.165 89.901  1.00 60.75  ? 261 ARG B C     1 
ATOM   5231 O O     . ARG B 2 261 ? 113.952 126.074 90.359  1.00 60.75  ? 261 ARG B O     1 
ATOM   5232 C CB    . ARG B 2 261 ? 113.707 129.210 91.102  1.00 89.26  ? 261 ARG B CB    1 
ATOM   5233 C CG    . ARG B 2 261 ? 113.827 130.067 92.346  1.00 89.26  ? 261 ARG B CG    1 
ATOM   5234 C CD    . ARG B 2 261 ? 112.530 130.800 92.625  1.00 89.26  ? 261 ARG B CD    1 
ATOM   5235 N NE    . ARG B 2 261 ? 111.415 129.875 92.807  1.00 89.26  ? 261 ARG B NE    1 
ATOM   5236 C CZ    . ARG B 2 261 ? 110.157 130.253 92.969  1.00 89.26  ? 261 ARG B CZ    1 
ATOM   5237 N NH1   . ARG B 2 261 ? 109.825 131.529 92.973  1.00 89.26  ? 261 ARG B NH1   1 
ATOM   5238 N NH2   . ARG B 2 261 ? 109.209 129.332 93.129  1.00 89.26  ? 261 ARG B NH2   1 
ATOM   5239 N N     . SER B 2 262 ? 114.337 127.392 88.598  1.00 58.98  ? 262 SER B N     1 
ATOM   5240 C CA    . SER B 2 262 ? 113.679 126.437 87.711  1.00 58.98  ? 262 SER B CA    1 
ATOM   5241 C C     . SER B 2 262 ? 114.643 125.312 87.394  1.00 58.98  ? 262 SER B C     1 
ATOM   5242 O O     . SER B 2 262 ? 115.098 125.174 86.259  1.00 58.98  ? 262 SER B O     1 
ATOM   5243 C CB    . SER B 2 262 ? 113.246 127.091 86.415  1.00 79.44  ? 262 SER B CB    1 
ATOM   5244 O OG    . SER B 2 262 ? 112.247 128.057 86.615  1.00 79.44  ? 262 SER B OG    1 
ATOM   5245 N N     . HIS B 2 263 ? 114.954 124.514 88.402  1.00 57.93  ? 263 HIS B N     1 
ATOM   5246 C CA    . HIS B 2 263 ? 115.985 123.517 88.230  1.00 57.93  ? 263 HIS B CA    1 
ATOM   5247 C C     . HIS B 2 263 ? 115.468 122.120 88.424  1.00 57.93  ? 263 HIS B C     1 
ATOM   5248 O O     . HIS B 2 263 ? 116.201 121.230 88.859  1.00 57.93  ? 263 HIS B O     1 
ATOM   5249 C CB    . HIS B 2 263 ? 117.172 123.771 89.138  1.00 78.78  ? 263 HIS B CB    1 
ATOM   5250 C CG    . HIS B 2 263 ? 116.873 123.778 90.581  1.00 78.78  ? 263 HIS B CG    1 
ATOM   5251 N ND1   . HIS B 2 263 ? 116.636 124.937 91.277  1.00 78.78  ? 263 HIS B ND1   1 
ATOM   5252 C CD2   . HIS B 2 263 ? 116.850 122.776 91.489  1.00 78.78  ? 263 HIS B CD2   1 
ATOM   5253 C CE1   . HIS B 2 263 ? 116.457 124.646 92.555  1.00 78.78  ? 263 HIS B CE1   1 
ATOM   5254 N NE2   . HIS B 2 263 ? 116.580 123.339 92.708  1.00 78.78  ? 263 HIS B NE2   1 
ATOM   5255 N N     . PHE B 2 264 ? 114.242 121.912 88.077  1.00 57.65  ? 264 PHE B N     1 
ATOM   5256 C CA    . PHE B 2 264 ? 113.624 120.616 88.223  1.00 57.65  ? 264 PHE B CA    1 
ATOM   5257 C C     . PHE B 2 264 ? 113.653 119.896 86.893  1.00 57.65  ? 264 PHE B C     1 
ATOM   5258 O O     . PHE B 2 264 ? 112.988 120.314 85.944  1.00 57.65  ? 264 PHE B O     1 
ATOM   5259 C CB    . PHE B 2 264 ? 112.202 120.789 88.740  1.00 80.44  ? 264 PHE B CB    1 
ATOM   5260 C CG    . PHE B 2 264 ? 112.165 121.311 90.134  1.00 80.44  ? 264 PHE B CG    1 
ATOM   5261 C CD1   . PHE B 2 264 ? 112.290 122.658 90.382  1.00 80.44  ? 264 PHE B CD1   1 
ATOM   5262 C CD2   . PHE B 2 264 ? 112.049 120.457 91.191  1.00 80.44  ? 264 PHE B CD2   1 
ATOM   5263 C CE1   . PHE B 2 264 ? 112.290 123.126 91.660  1.00 80.44  ? 264 PHE B CE1   1 
ATOM   5264 C CE2   . PHE B 2 264 ? 112.044 120.918 92.467  1.00 80.44  ? 264 PHE B CE2   1 
ATOM   5265 C CZ    . PHE B 2 264 ? 112.165 122.254 92.705  1.00 80.44  ? 264 PHE B CZ    1 
ATOM   5266 N N     . LEU B 2 265 ? 114.387 118.800 86.834  1.00 54.45  ? 265 LEU B N     1 
ATOM   5267 C CA    . LEU B 2 265 ? 114.580 118.061 85.607  1.00 54.45  ? 265 LEU B CA    1 
ATOM   5268 C C     . LEU B 2 265 ? 113.800 116.769 85.564  1.00 54.45  ? 265 LEU B C     1 
ATOM   5269 O O     . LEU B 2 265 ? 113.656 116.074 86.561  1.00 54.45  ? 265 LEU B O     1 
ATOM   5270 C CB    . LEU B 2 265 ? 116.031 117.711 85.465  1.00 80.61  ? 265 LEU B CB    1 
ATOM   5271 C CG    . LEU B 2 265 ? 116.993 118.861 85.557  1.00 80.61  ? 265 LEU B CG    1 
ATOM   5272 C CD1   . LEU B 2 265 ? 118.366 118.290 85.545  1.00 80.61  ? 265 LEU B CD1   1 
ATOM   5273 C CD2   . LEU B 2 265 ? 116.794 119.770 84.405  1.00 80.61  ? 265 LEU B CD2   1 
ATOM   5274 N N     . MET B 2 266 ? 113.354 116.426 84.379  1.00 56.90  ? 266 MET B N     1 
ATOM   5275 C CA    . MET B 2 266 ? 112.708 115.157 84.142  1.00 56.90  ? 266 MET B CA    1 
ATOM   5276 C C     . MET B 2 266 ? 113.705 114.118 83.681  1.00 56.90  ? 266 MET B C     1 
ATOM   5277 O O     . MET B 2 266 ? 114.609 114.416 82.899  1.00 56.90  ? 266 MET B O     1 
ATOM   5278 C CB    . MET B 2 266 ? 111.653 115.301 83.066  1.00 81.74  ? 266 MET B CB    1 
ATOM   5279 C CG    . MET B 2 266 ? 110.601 116.226 83.441  1.00 81.74  ? 266 MET B CG    1 
ATOM   5280 S SD    . MET B 2 266 ? 109.333 116.301 82.213  1.00 81.74  ? 266 MET B SD    1 
ATOM   5281 C CE    . MET B 2 266 ? 108.471 117.602 83.007  1.00 81.74  ? 266 MET B CE    1 
ATOM   5282 N N     . ALA B 2 267 ? 113.513 112.884 84.114  1.00 58.15  ? 267 ALA B N     1 
ATOM   5283 C CA    . ALA B 2 267 ? 114.372 111.811 83.651  1.00 58.15  ? 267 ALA B CA    1 
ATOM   5284 C C     . ALA B 2 267 ? 113.749 111.085 82.476  1.00 58.15  ? 267 ALA B C     1 
ATOM   5285 O O     . ALA B 2 267 ? 112.568 110.727 82.497  1.00 58.15  ? 267 ALA B O     1 
ATOM   5286 C CB    . ALA B 2 267 ? 114.660 110.811 84.771  1.00 79.30  ? 267 ALA B CB    1 
ATOM   5287 N N     . SER B 2 268 ? 114.587 110.786 81.499  1.00 59.31  ? 268 SER B N     1 
ATOM   5288 C CA    . SER B 2 268 ? 114.218 109.997 80.336  1.00 59.31  ? 268 SER B CA    1 
ATOM   5289 C C     . SER B 2 268 ? 115.237 108.882 80.165  1.00 59.31  ? 268 SER B C     1 
ATOM   5290 O O     . SER B 2 268 ? 116.437 109.152 80.119  1.00 59.31  ? 268 SER B O     1 
ATOM   5291 C CB    . SER B 2 268 ? 114.177 110.874 79.097  1.00 79.89  ? 268 SER B CB    1 
ATOM   5292 O OG    . SER B 2 268 ? 113.968 110.087 77.954  1.00 79.89  ? 268 SER B OG    1 
ATOM   5293 N N     . PHE B 2 269 ? 114.776 107.626 80.096  1.00 65.71  ? 269 PHE B N     1 
ATOM   5294 C CA    . PHE B 2 269 ? 115.726 106.520 80.009  1.00 65.71  ? 269 PHE B CA    1 
ATOM   5295 C C     . PHE B 2 269 ? 115.292 105.341 79.149  1.00 65.71  ? 269 PHE B C     1 
ATOM   5296 O O     . PHE B 2 269 ? 114.170 104.863 79.274  1.00 65.71  ? 269 PHE B O     1 
ATOM   5297 C CB    . PHE B 2 269 ? 116.044 105.974 81.365  1.00 91.69  ? 269 PHE B CB    1 
ATOM   5298 C CG    . PHE B 2 269 ? 116.814 104.763 81.273  1.00 91.69  ? 269 PHE B CG    1 
ATOM   5299 C CD1   . PHE B 2 269 ? 118.150 104.811 81.034  1.00 91.69  ? 269 PHE B CD1   1 
ATOM   5300 C CD2   . PHE B 2 269 ? 116.191 103.551 81.348  1.00 91.69  ? 269 PHE B CD2   1 
ATOM   5301 C CE1   . PHE B 2 269 ? 118.866 103.668 80.883  1.00 91.69  ? 269 PHE B CE1   1 
ATOM   5302 C CE2   . PHE B 2 269 ? 116.886 102.407 81.193  1.00 91.69  ? 269 PHE B CE2   1 
ATOM   5303 C CZ    . PHE B 2 269 ? 118.234 102.459 80.958  1.00 91.69  ? 269 PHE B CZ    1 
ATOM   5304 N N     . ALA B 2 270 ? 116.220 104.801 78.356  1.00 63.54  ? 270 ALA B N     1 
ATOM   5305 C CA    . ALA B 2 270 ? 115.887 103.653 77.521  1.00 63.54  ? 270 ALA B CA    1 
ATOM   5306 C C     . ALA B 2 270 ? 117.124 102.810 77.185  1.00 63.54  ? 270 ALA B C     1 
ATOM   5307 O O     . ALA B 2 270 ? 118.244 103.326 77.117  1.00 63.54  ? 270 ALA B O     1 
ATOM   5308 C CB    . ALA B 2 270 ? 115.203 104.128 76.235  1.00 86.65  ? 270 ALA B CB    1 
ATOM   5309 N N     . PRO B 2 271 ? 116.946 101.519 76.893  1.00 68.40  ? 271 PRO B N     1 
ATOM   5310 C CA    . PRO B 2 271 ? 115.767 100.659 76.900  1.00 68.40  ? 271 PRO B CA    1 
ATOM   5311 C C     . PRO B 2 271 ? 115.427 100.211 78.268  1.00 68.40  ? 271 PRO B C     1 
ATOM   5312 O O     . PRO B 2 271 ? 116.282 100.063 79.107  1.00 68.40  ? 271 PRO B O     1 
ATOM   5313 C CB    . PRO B 2 271 ? 116.214 99.458  76.090  1.00 451.62 ? 271 PRO B CB    1 
ATOM   5314 C CG    . PRO B 2 271 ? 117.656 99.372  76.382  1.00 451.62 ? 271 PRO B CG    1 
ATOM   5315 C CD    . PRO B 2 271 ? 118.138 100.781 76.499  1.00 451.62 ? 271 PRO B CD    1 
ATOM   5316 N N     . MET B 2 272 ? 114.198 99.814  78.466  1.00 74.86  ? 272 MET B N     1 
ATOM   5317 C CA    . MET B 2 272 ? 113.811 99.292  79.736  1.00 74.86  ? 272 MET B CA    1 
ATOM   5318 C C     . MET B 2 272 ? 113.857 97.803  79.597  1.00 74.86  ? 272 MET B C     1 
ATOM   5319 O O     . MET B 2 272 ? 112.856 97.127  79.578  1.00 74.86  ? 272 MET B O     1 
ATOM   5320 C CB    . MET B 2 272 ? 112.407 99.730  80.096  1.00 107.54 ? 272 MET B CB    1 
ATOM   5321 C CG    . MET B 2 272 ? 112.172 101.216 80.044  1.00 107.54 ? 272 MET B CG    1 
ATOM   5322 S SD    . MET B 2 272 ? 113.084 102.114 81.309  1.00 107.54 ? 272 MET B SD    1 
ATOM   5323 C CE    . MET B 2 272 ? 112.223 103.684 81.288  1.00 107.54 ? 272 MET B CE    1 
ATOM   5324 N N     . ALA B 2 273 ? 115.053 97.316  79.476  1.00 84.77  ? 273 ALA B N     1 
ATOM   5325 C CA    . ALA B 2 273 ? 115.186 95.887  79.414  1.00 84.77  ? 273 ALA B CA    1 
ATOM   5326 C C     . ALA B 2 273 ? 114.649 95.232  80.662  1.00 84.77  ? 273 ALA B C     1 
ATOM   5327 O O     . ALA B 2 273 ? 114.160 94.104  80.596  1.00 84.77  ? 273 ALA B O     1 
ATOM   5328 C CB    . ALA B 2 273 ? 116.645 95.511  79.235  1.00 115.60 ? 273 ALA B CB    1 
ATOM   5329 N N     . THR B 2 274 ? 114.740 95.907  81.806  1.00 94.34  ? 274 THR B N     1 
ATOM   5330 C CA    . THR B 2 274 ? 114.375 95.312  83.092  1.00 94.34  ? 274 THR B CA    1 
ATOM   5331 C C     . THR B 2 274 ? 114.864 93.875  83.146  1.00 94.34  ? 274 THR B C     1 
ATOM   5332 O O     . THR B 2 274 ? 116.069 93.638  83.106  1.00 94.34  ? 274 THR B O     1 
ATOM   5333 C CB    . THR B 2 274 ? 112.859 95.400  83.398  1.00 132.08 ? 274 THR B CB    1 
ATOM   5334 O OG1   . THR B 2 274 ? 112.560 94.618  84.562  1.00 132.08 ? 274 THR B OG1   1 
ATOM   5335 C CG2   . THR B 2 274 ? 111.967 94.936  82.242  1.00 132.08 ? 274 THR B CG2   1 
ATOM   5336 N N     . ALA B 2 275 ? 113.967 92.916  83.253  1.00 100.19 ? 275 ALA B N     1 
ATOM   5337 C CA    . ALA B 2 275 ? 114.371 91.534  83.376  1.00 100.19 ? 275 ALA B CA    1 
ATOM   5338 C C     . ALA B 2 275 ? 113.842 90.681  82.246  1.00 100.19 ? 275 ALA B C     1 
ATOM   5339 O O     . ALA B 2 275 ? 114.235 89.515  82.119  1.00 100.19 ? 275 ALA B O     1 
ATOM   5340 C CB    . ALA B 2 275 ? 113.906 90.965  84.720  1.00 136.62 ? 275 ALA B CB    1 
ATOM   5341 N N     . GLU B 2 276 ? 112.966 91.234  81.421  1.00 102.97 ? 276 GLU B N     1 
ATOM   5342 C CA    . GLU B 2 276 ? 112.456 90.496  80.283  1.00 102.97 ? 276 GLU B CA    1 
ATOM   5343 C C     . GLU B 2 276 ? 113.618 90.098  79.397  1.00 102.97 ? 276 GLU B C     1 
ATOM   5344 O O     . GLU B 2 276 ? 114.657 90.758  79.386  1.00 102.97 ? 276 GLU B O     1 
ATOM   5345 C CB    . GLU B 2 276 ? 111.451 91.345  79.509  1.00 138.32 ? 276 GLU B CB    1 
ATOM   5346 C CG    . GLU B 2 276 ? 111.091 90.808  78.136  1.00 138.32 ? 276 GLU B CG    1 
ATOM   5347 C CD    . GLU B 2 276 ? 110.541 89.400  78.185  1.00 138.32 ? 276 GLU B CD    1 
ATOM   5348 O OE1   . GLU B 2 276 ? 109.921 89.037  79.204  1.00 138.32 ? 276 GLU B OE1   1 
ATOM   5349 O OE2   . GLU B 2 276 ? 110.724 88.656  77.199  1.00 138.32 ? 276 GLU B OE2   1 
ATOM   5350 N N     . ASP B 2 277 ? 113.453 88.989  78.670  1.00 109.11 ? 277 ASP B N     1 
ATOM   5351 C CA    . ASP B 2 277 ? 114.495 88.575  77.745  1.00 109.11 ? 277 ASP B CA    1 
ATOM   5352 C C     . ASP B 2 277 ? 114.906 89.751  76.895  1.00 109.11 ? 277 ASP B C     1 
ATOM   5353 O O     . ASP B 2 277 ? 116.085 89.920  76.578  1.00 109.11 ? 277 ASP B O     1 
ATOM   5354 C CB    . ASP B 2 277 ? 114.008 87.439  76.862  1.00 140.28 ? 277 ASP B CB    1 
ATOM   5355 C CG    . ASP B 2 277 ? 113.422 86.288  77.654  1.00 140.28 ? 277 ASP B CG    1 
ATOM   5356 O OD1   . ASP B 2 277 ? 113.401 86.368  78.900  1.00 140.28 ? 277 ASP B OD1   1 
ATOM   5357 O OD2   . ASP B 2 277 ? 112.977 85.303  77.027  1.00 140.28 ? 277 ASP B OD2   1 
ATOM   5358 N N     . ARG B 2 278 ? 113.947 90.595  76.548  1.00 104.52 ? 278 ARG B N     1 
ATOM   5359 C CA    . ARG B 2 278 ? 114.234 91.820  75.825  1.00 104.52 ? 278 ARG B CA    1 
ATOM   5360 C C     . ARG B 2 278 ? 115.170 91.569  74.667  1.00 104.52 ? 278 ARG B C     1 
ATOM   5361 O O     . ARG B 2 278 ? 116.141 92.297  74.475  1.00 104.52 ? 278 ARG B O     1 
ATOM   5362 C CB    . ARG B 2 278 ? 114.842 92.874  76.747  1.00 153.58 ? 278 ARG B CB    1 
ATOM   5363 C CG    . ARG B 2 278 ? 113.966 93.266  77.884  1.00 153.58 ? 278 ARG B CG    1 
ATOM   5364 C CD    . ARG B 2 278 ? 112.737 94.030  77.432  1.00 153.58 ? 278 ARG B CD    1 
ATOM   5365 N NE    . ARG B 2 278 ? 111.973 94.546  78.563  1.00 153.58 ? 278 ARG B NE    1 
ATOM   5366 C CZ    . ARG B 2 278 ? 110.839 95.224  78.447  1.00 153.58 ? 278 ARG B CZ    1 
ATOM   5367 N NH1   . ARG B 2 278 ? 110.315 95.484  77.261  1.00 153.58 ? 278 ARG B NH1   1 
ATOM   5368 N NH2   . ARG B 2 278 ? 110.220 95.655  79.543  1.00 153.58 ? 278 ARG B NH2   1 
ATOM   5369 N N     . GLN B 2 279 ? 114.917 90.501  73.922  1.00 97.95  ? 279 GLN B N     1 
ATOM   5370 C CA    . GLN B 2 279 ? 115.690 90.329  72.725  1.00 97.95  ? 279 GLN B CA    1 
ATOM   5371 C C     . GLN B 2 279 ? 115.376 91.581  71.973  1.00 97.95  ? 279 GLN B C     1 
ATOM   5372 O O     . GLN B 2 279 ? 114.280 92.108  72.118  1.00 97.95  ? 279 GLN B O     1 
ATOM   5373 C CB    . GLN B 2 279 ? 115.253 89.106  71.935  1.00 136.86 ? 279 GLN B CB    1 
ATOM   5374 C CG    . GLN B 2 279 ? 115.351 87.820  72.670  1.00 136.86 ? 279 GLN B CG    1 
ATOM   5375 C CD    . GLN B 2 279 ? 114.136 87.553  73.507  1.00 136.86 ? 279 GLN B CD    1 
ATOM   5376 O OE1   . GLN B 2 279 ? 113.350 88.466  73.787  1.00 136.86 ? 279 GLN B OE1   1 
ATOM   5377 N NE2   . GLN B 2 279 ? 113.976 86.302  73.938  1.00 136.86 ? 279 GLN B NE2   1 
ATOM   5378 N N     . TYR B 2 280 ? 116.336 92.111  71.242  1.00 106.31 ? 280 TYR B N     1 
ATOM   5379 C CA    . TYR B 2 280 ? 116.140 93.380  70.555  1.00 106.31 ? 280 TYR B CA    1 
ATOM   5380 C C     . TYR B 2 280 ? 116.343 93.214  69.065  1.00 106.31 ? 280 TYR B C     1 
ATOM   5381 O O     . TYR B 2 280 ? 117.463 92.967  68.611  1.00 106.31 ? 280 TYR B O     1 
ATOM   5382 C CB    . TYR B 2 280 ? 117.095 94.434  71.085  1.00 147.20 ? 280 TYR B CB    1 
ATOM   5383 C CG    . TYR B 2 280 ? 116.864 94.823  72.528  1.00 147.20 ? 280 TYR B CG    1 
ATOM   5384 C CD1   . TYR B 2 280 ? 115.745 95.552  72.896  1.00 147.20 ? 280 TYR B CD1   1 
ATOM   5385 C CD2   . TYR B 2 280 ? 117.776 94.487  73.517  1.00 147.20 ? 280 TYR B CD2   1 
ATOM   5386 C CE1   . TYR B 2 280 ? 115.533 95.915  74.205  1.00 147.20 ? 280 TYR B CE1   1 
ATOM   5387 C CE2   . TYR B 2 280 ? 117.572 94.849  74.824  1.00 147.20 ? 280 TYR B CE2   1 
ATOM   5388 C CZ    . TYR B 2 280 ? 116.452 95.560  75.162  1.00 147.20 ? 280 TYR B CZ    1 
ATOM   5389 O OH    . TYR B 2 280 ? 116.241 95.932  76.462  1.00 147.20 ? 280 TYR B OH    1 
ATOM   5390 N N     . ALA B 2 281 ? 115.274 93.362  68.299  1.00 96.36  ? 281 ALA B N     1 
ATOM   5391 C CA    . ALA B 2 281 ? 115.392 93.298  66.852  1.00 96.36  ? 281 ALA B CA    1 
ATOM   5392 C C     . ALA B 2 281 ? 115.772 94.650  66.278  1.00 96.36  ? 281 ALA B C     1 
ATOM   5393 O O     . ALA B 2 281 ? 116.014 94.761  65.070  1.00 96.36  ? 281 ALA B O     1 
ATOM   5394 C CB    . ALA B 2 281 ? 114.084 92.795  66.235  1.00 131.40 ? 281 ALA B CB    1 
ATOM   5395 N N     . LYS B 2 282 ? 115.781 95.685  67.120  1.00 86.79  ? 282 LYS B N     1 
ATOM   5396 C CA    . LYS B 2 282 ? 116.095 97.011  66.626  1.00 86.79  ? 282 LYS B CA    1 
ATOM   5397 C C     . LYS B 2 282 ? 117.229 97.695  67.366  1.00 86.79  ? 282 LYS B C     1 
ATOM   5398 O O     . LYS B 2 282 ? 118.357 97.722  66.869  1.00 86.79  ? 282 LYS B O     1 
ATOM   5399 C CB    . LYS B 2 282 ? 114.841 97.889  66.712  1.00 130.18 ? 282 LYS B CB    1 
ATOM   5400 C CG    . LYS B 2 282 ? 113.641 97.326  65.969  1.00 130.18 ? 282 LYS B CG    1 
ATOM   5401 C CD    . LYS B 2 282 ? 113.959 97.129  64.497  1.00 130.18 ? 282 LYS B CD    1 
ATOM   5402 C CE    . LYS B 2 282 ? 112.822 96.427  63.776  1.00 130.18 ? 282 LYS B CE    1 
ATOM   5403 N NZ    . LYS B 2 282 ? 113.131 96.213  62.335  1.00 130.18 ? 282 LYS B NZ    1 
ATOM   5404 N N     . LEU B 2 283 ? 116.959 98.215  68.564  1.00 85.04  ? 283 LEU B N     1 
ATOM   5405 C CA    . LEU B 2 283 ? 117.960 98.967  69.298  1.00 85.04  ? 283 LEU B CA    1 
ATOM   5406 C C     . LEU B 2 283 ? 118.582 100.013 68.397  1.00 85.04  ? 283 LEU B C     1 
ATOM   5407 O O     . LEU B 2 283 ? 119.601 100.612 68.748  1.00 85.04  ? 283 LEU B O     1 
ATOM   5408 C CB    . LEU B 2 283 ? 119.037 98.050  69.852  1.00 125.90 ? 283 LEU B CB    1 
ATOM   5409 C CG    . LEU B 2 283 ? 118.752 97.380  71.190  1.00 125.90 ? 283 LEU B CG    1 
ATOM   5410 C CD1   . LEU B 2 283 ? 119.969 96.589  71.662  1.00 125.90 ? 283 LEU B CD1   1 
ATOM   5411 C CD2   . LEU B 2 283 ? 118.353 98.411  72.227  1.00 125.90 ? 283 LEU B CD2   1 
ATOM   5412 N N     . THR B 2 284 ? 117.975 100.243 67.232  1.00 75.07  ? 284 THR B N     1 
ATOM   5413 C CA    . THR B 2 284 ? 118.554 101.176 66.301  1.00 75.07  ? 284 THR B CA    1 
ATOM   5414 C C     . THR B 2 284 ? 118.502 102.572 66.870  1.00 75.07  ? 284 THR B C     1 
ATOM   5415 O O     . THR B 2 284 ? 117.588 102.944 67.611  1.00 75.07  ? 284 THR B O     1 
ATOM   5416 C CB    . THR B 2 284 ? 117.860 101.152 64.961  1.00 105.10 ? 284 THR B CB    1 
ATOM   5417 O OG1   . THR B 2 284 ? 118.406 102.207 64.156  1.00 105.10 ? 284 THR B OG1   1 
ATOM   5418 C CG2   . THR B 2 284 ? 116.385 101.343 65.116  1.00 105.10 ? 284 THR B CG2   1 
ATOM   5419 N N     . THR B 2 285 ? 119.510 103.348 66.507  1.00 72.54  ? 285 THR B N     1 
ATOM   5420 C CA    . THR B 2 285 ? 119.605 104.725 66.937  1.00 72.54  ? 285 THR B CA    1 
ATOM   5421 C C     . THR B 2 285 ? 118.533 105.553 66.299  1.00 72.54  ? 285 THR B C     1 
ATOM   5422 O O     . THR B 2 285 ? 118.134 106.568 66.871  1.00 72.54  ? 285 THR B O     1 
ATOM   5423 C CB    . THR B 2 285 ? 120.978 105.282 66.584  1.00 101.56 ? 285 THR B CB    1 
ATOM   5424 O OG1   . THR B 2 285 ? 121.197 105.168 65.171  1.00 101.56 ? 285 THR B OG1   1 
ATOM   5425 C CG2   . THR B 2 285 ? 122.043 104.511 67.316  1.00 101.56 ? 285 THR B CG2   1 
ATOM   5426 N N     . SER B 2 286 ? 118.022 105.097 65.159  1.00 70.30  ? 286 SER B N     1 
ATOM   5427 C CA    . SER B 2 286 ? 116.934 105.777 64.485  1.00 70.30  ? 286 SER B CA    1 
ATOM   5428 C C     . SER B 2 286 ? 115.683 105.725 65.325  1.00 70.30  ? 286 SER B C     1 
ATOM   5429 O O     . SER B 2 286 ? 114.717 106.449 65.062  1.00 70.30  ? 286 SER B O     1 
ATOM   5430 C CB    . SER B 2 286 ? 116.676 105.163 63.129  1.00 94.69  ? 286 SER B CB    1 
ATOM   5431 O OG    . SER B 2 286 ? 116.144 103.881 63.253  1.00 94.69  ? 286 SER B OG    1 
ATOM   5432 N N     . ASN B 2 287 ? 115.689 104.856 66.321  1.00 72.99  ? 287 ASN B N     1 
ATOM   5433 C CA    . ASN B 2 287 ? 114.626 104.800 67.277  1.00 72.99  ? 287 ASN B CA    1 
ATOM   5434 C C     . ASN B 2 287 ? 115.104 105.342 68.599  1.00 72.99  ? 287 ASN B C     1 
ATOM   5435 O O     . ASN B 2 287 ? 114.474 106.257 69.116  1.00 72.99  ? 287 ASN B O     1 
ATOM   5436 C CB    . ASN B 2 287 ? 114.093 103.378 67.431  1.00 98.89  ? 287 ASN B CB    1 
ATOM   5437 C CG    . ASN B 2 287 ? 113.321 102.903 66.211  1.00 98.89  ? 287 ASN B CG    1 
ATOM   5438 O OD1   . ASN B 2 287 ? 112.827 103.693 65.402  1.00 98.89  ? 287 ASN B OD1   1 
ATOM   5439 N ND2   . ASN B 2 287 ? 113.195 101.598 66.088  1.00 98.89  ? 287 ASN B ND2   1 
ATOM   5440 N N     . LEU B 2 288 ? 116.252 104.878 69.097  1.00 70.08  ? 288 LEU B N     1 
ATOM   5441 C CA    . LEU B 2 288 ? 116.704 105.272 70.428  1.00 70.08  ? 288 LEU B CA    1 
ATOM   5442 C C     . LEU B 2 288 ? 116.755 106.775 70.597  1.00 70.08  ? 288 LEU B C     1 
ATOM   5443 O O     . LEU B 2 288 ? 116.314 107.318 71.617  1.00 70.08  ? 288 LEU B O     1 
ATOM   5444 C CB    . LEU B 2 288 ? 118.084 104.711 70.713  1.00 103.75 ? 288 LEU B CB    1 
ATOM   5445 C CG    . LEU B 2 288 ? 118.747 105.073 72.065  1.00 103.75 ? 288 LEU B CG    1 
ATOM   5446 C CD1   . LEU B 2 288 ? 117.954 104.545 73.282  1.00 103.75 ? 288 LEU B CD1   1 
ATOM   5447 C CD2   . LEU B 2 288 ? 120.185 104.528 72.080  1.00 103.75 ? 288 LEU B CD2   1 
ATOM   5448 N N     . ALA B 2 289 ? 117.298 107.467 69.612  1.00 69.00  ? 289 ALA B N     1 
ATOM   5449 C CA    . ALA B 2 289 ? 117.395 108.899 69.762  1.00 69.00  ? 289 ALA B CA    1 
ATOM   5450 C C     . ALA B 2 289 ? 116.028 109.508 69.900  1.00 69.00  ? 289 ALA B C     1 
ATOM   5451 O O     . ALA B 2 289 ? 115.872 110.522 70.584  1.00 69.00  ? 289 ALA B O     1 
ATOM   5452 C CB    . ALA B 2 289 ? 118.127 109.493 68.574  1.00 94.09  ? 289 ALA B CB    1 
ATOM   5453 N N     . ASN B 2 290 ? 115.047 108.936 69.242  1.00 66.78  ? 290 ASN B N     1 
ATOM   5454 C CA    . ASN B 2 290 ? 113.717 109.474 69.328  1.00 66.78  ? 290 ASN B CA    1 
ATOM   5455 C C     . ASN B 2 290 ? 113.025 108.971 70.567  1.00 66.78  ? 290 ASN B C     1 
ATOM   5456 O O     . ASN B 2 290 ? 112.229 109.683 71.179  1.00 66.78  ? 290 ASN B O     1 
ATOM   5457 C CB    . ASN B 2 290 ? 112.944 109.097 68.083  1.00 90.48  ? 290 ASN B CB    1 
ATOM   5458 C CG    . ASN B 2 290 ? 113.430 109.829 66.870  1.00 90.48  ? 290 ASN B CG    1 
ATOM   5459 O OD1   . ASN B 2 290 ? 113.232 111.042 66.736  1.00 90.48  ? 290 ASN B OD1   1 
ATOM   5460 N ND2   . ASN B 2 290 ? 114.059 109.108 65.961  1.00 90.48  ? 290 ASN B ND2   1 
ATOM   5461 N N     . ALA B 2 291 ? 113.384 107.773 70.966  1.00 63.63  ? 291 ALA B N     1 
ATOM   5462 C CA    . ALA B 2 291 ? 112.746 107.136 72.081  1.00 63.63  ? 291 ALA B CA    1 
ATOM   5463 C C     . ALA B 2 291 ? 112.902 107.974 73.300  1.00 63.63  ? 291 ALA B C     1 
ATOM   5464 O O     . ALA B 2 291 ? 111.991 108.062 74.123  1.00 63.63  ? 291 ALA B O     1 
ATOM   5465 C CB    . ALA B 2 291 ? 113.368 105.770 72.322  1.00 86.77  ? 291 ALA B CB    1 
ATOM   5466 N N     . LEU B 2 292 ? 114.030 108.648 73.412  1.00 61.72  ? 292 LEU B N     1 
ATOM   5467 C CA    . LEU B 2 292 ? 114.266 109.429 74.614  1.00 61.72  ? 292 LEU B CA    1 
ATOM   5468 C C     . LEU B 2 292 ? 113.409 110.690 74.670  1.00 61.72  ? 292 LEU B C     1 
ATOM   5469 O O     . LEU B 2 292 ? 113.404 111.376 75.693  1.00 61.72  ? 292 LEU B O     1 
ATOM   5470 C CB    . LEU B 2 292 ? 115.762 109.718 74.733  1.00 91.38  ? 292 LEU B CB    1 
ATOM   5471 C CG    . LEU B 2 292 ? 116.624 108.476 75.058  1.00 91.38  ? 292 LEU B CG    1 
ATOM   5472 C CD1   . LEU B 2 292 ? 118.091 108.788 74.950  1.00 91.38  ? 292 LEU B CD1   1 
ATOM   5473 C CD2   . LEU B 2 292 ? 116.328 107.977 76.456  1.00 91.38  ? 292 LEU B CD2   1 
ATOM   5474 N N     . PHE B 2 293 ? 112.667 110.987 73.611  1.00 62.11  ? 293 PHE B N     1 
ATOM   5475 C CA    . PHE B 2 293 ? 111.697 112.057 73.607  1.00 62.11  ? 293 PHE B CA    1 
ATOM   5476 C C     . PHE B 2 293 ? 110.293 111.521 73.542  1.00 62.11  ? 293 PHE B C     1 
ATOM   5477 O O     . PHE B 2 293 ? 109.352 112.294 73.359  1.00 62.11  ? 293 PHE B O     1 
ATOM   5478 C CB    . PHE B 2 293 ? 111.991 113.002 72.473  1.00 86.66  ? 293 PHE B CB    1 
ATOM   5479 C CG    . PHE B 2 293 ? 113.270 113.627 72.669  1.00 86.66  ? 293 PHE B CG    1 
ATOM   5480 C CD1   . PHE B 2 293 ? 113.387 114.711 73.504  1.00 86.66  ? 293 PHE B CD1   1 
ATOM   5481 C CD2   . PHE B 2 293 ? 114.396 113.090 72.115  1.00 86.66  ? 293 PHE B CD2   1 
ATOM   5482 C CE1   . PHE B 2 293 ? 114.613 115.278 73.749  1.00 86.66  ? 293 PHE B CE1   1 
ATOM   5483 C CE2   . PHE B 2 293 ? 115.627 113.647 72.355  1.00 86.66  ? 293 PHE B CE2   1 
ATOM   5484 C CZ    . PHE B 2 293 ? 115.736 114.745 73.175  1.00 86.66  ? 293 PHE B CZ    1 
ATOM   5485 N N     . GLU B 2 294 ? 110.126 110.215 73.715  1.00 67.10  ? 294 GLU B N     1 
ATOM   5486 C CA    . GLU B 2 294 ? 108.808 109.598 73.717  1.00 67.10  ? 294 GLU B CA    1 
ATOM   5487 C C     . GLU B 2 294 ? 108.302 109.406 75.140  1.00 67.10  ? 294 GLU B C     1 
ATOM   5488 O O     . GLU B 2 294 ? 109.066 109.109 76.059  1.00 67.10  ? 294 GLU B O     1 
ATOM   5489 C CB    . GLU B 2 294 ? 108.807 108.238 73.013  1.00 90.13  ? 294 GLU B CB    1 
ATOM   5490 C CG    . GLU B 2 294 ? 109.042 108.255 71.507  1.00 90.13  ? 294 GLU B CG    1 
ATOM   5491 C CD    . GLU B 2 294 ? 109.007 106.860 70.932  1.00 90.13  ? 294 GLU B CD    1 
ATOM   5492 O OE1   . GLU B 2 294 ? 109.031 105.918 71.724  1.00 90.13  ? 294 GLU B OE1   1 
ATOM   5493 O OE2   . GLU B 2 294 ? 108.951 106.702 69.711  1.00 90.13  ? 294 GLU B OE2   1 
ATOM   5494 N N     . GLU B 2 295 ? 106.983 109.479 75.288  1.00 68.14  ? 295 GLU B N     1 
ATOM   5495 C CA    . GLU B 2 295 ? 106.349 109.370 76.590  1.00 68.14  ? 295 GLU B CA    1 
ATOM   5496 C C     . GLU B 2 295 ? 106.609 108.044 77.243  1.00 68.14  ? 295 GLU B C     1 
ATOM   5497 O O     . GLU B 2 295 ? 106.535 107.932 78.466  1.00 68.14  ? 295 GLU B O     1 
ATOM   5498 C CB    . GLU B 2 295 ? 104.851 109.572 76.420  1.00 91.53  ? 295 GLU B CB    1 
ATOM   5499 C CG    . GLU B 2 295 ? 104.152 108.487 75.606  1.00 91.53  ? 295 GLU B CG    1 
ATOM   5500 C CD    . GLU B 2 295 ? 104.279 108.684 74.131  1.00 91.53  ? 295 GLU B CD    1 
ATOM   5501 O OE1   . GLU B 2 295 ? 104.920 109.647 73.712  1.00 91.53  ? 295 GLU B OE1   1 
ATOM   5502 O OE2   . GLU B 2 295 ? 103.746 107.864 73.385  1.00 91.53  ? 295 GLU B OE2   1 
ATOM   5503 N N     . ASN B 2 296 ? 106.952 107.052 76.450  1.00 68.84  ? 296 ASN B N     1 
ATOM   5504 C CA    . ASN B 2 296 ? 107.148 105.700 76.922  1.00 68.84  ? 296 ASN B CA    1 
ATOM   5505 C C     . ASN B 2 296 ? 108.344 105.570 77.821  1.00 68.84  ? 296 ASN B C     1 
ATOM   5506 O O     . ASN B 2 296 ? 108.469 104.583 78.549  1.00 68.84  ? 296 ASN B O     1 
ATOM   5507 C CB    . ASN B 2 296 ? 107.296 104.797 75.725  1.00 93.27  ? 296 ASN B CB    1 
ATOM   5508 C CG    . ASN B 2 296 ? 106.006 104.650 74.993  1.00 93.27  ? 296 ASN B CG    1 
ATOM   5509 O OD1   . ASN B 2 296 ? 104.932 104.811 75.572  1.00 93.27  ? 296 ASN B OD1   1 
ATOM   5510 N ND2   . ASN B 2 296 ? 106.087 104.356 73.715  1.00 93.27  ? 296 ASN B ND2   1 
ATOM   5511 N N     . TYR B 2 297 ? 109.231 106.525 77.764  1.00 66.39  ? 297 TYR B N     1 
ATOM   5512 C CA    . TYR B 2 297 ? 110.411 106.459 78.569  1.00 66.39  ? 297 TYR B CA    1 
ATOM   5513 C C     . TYR B 2 297 ? 110.470 107.635 79.500  1.00 66.39  ? 297 TYR B C     1 
ATOM   5514 O O     . TYR B 2 297 ? 111.522 107.915 80.077  1.00 66.39  ? 297 TYR B O     1 
ATOM   5515 C CB    . TYR B 2 297 ? 111.595 106.365 77.643  1.00 91.92  ? 297 TYR B CB    1 
ATOM   5516 C CG    . TYR B 2 297 ? 111.433 105.161 76.796  1.00 91.92  ? 297 TYR B CG    1 
ATOM   5517 C CD1   . TYR B 2 297 ? 111.716 103.934 77.288  1.00 91.92  ? 297 TYR B CD1   1 
ATOM   5518 C CD2   . TYR B 2 297 ? 110.961 105.258 75.524  1.00 91.92  ? 297 TYR B CD2   1 
ATOM   5519 C CE1   . TYR B 2 297 ? 111.549 102.830 76.537  1.00 91.92  ? 297 TYR B CE1   1 
ATOM   5520 C CE2   . TYR B 2 297 ? 110.800 104.152 74.759  1.00 91.92  ? 297 TYR B CE2   1 
ATOM   5521 C CZ    . TYR B 2 297 ? 111.096 102.936 75.276  1.00 91.92  ? 297 TYR B CZ    1 
ATOM   5522 O OH    . TYR B 2 297 ? 110.932 101.818 74.516  1.00 91.92  ? 297 TYR B OH    1 
ATOM   5523 N N     . MET B 2 298 ? 109.359 108.339 79.665  1.00 71.22  ? 298 MET B N     1 
ATOM   5524 C CA    . MET B 2 298 ? 109.349 109.512 80.515  1.00 71.22  ? 298 MET B CA    1 
ATOM   5525 C C     . MET B 2 298 ? 108.964 109.155 81.926  1.00 71.22  ? 298 MET B C     1 
ATOM   5526 O O     . MET B 2 298 ? 107.799 108.897 82.220  1.00 71.22  ? 298 MET B O     1 
ATOM   5527 C CB    . MET B 2 298 ? 108.401 110.566 79.992  1.00 102.32 ? 298 MET B CB    1 
ATOM   5528 C CG    . MET B 2 298 ? 108.821 111.128 78.704  1.00 102.32 ? 298 MET B CG    1 
ATOM   5529 S SD    . MET B 2 298 ? 110.335 112.067 78.799  1.00 102.32 ? 298 MET B SD    1 
ATOM   5530 C CE    . MET B 2 298 ? 110.691 112.137 77.060  1.00 102.32 ? 298 MET B CE    1 
ATOM   5531 N N     . MET B 2 299 ? 109.911 109.275 82.810  1.00 68.61  ? 299 MET B N     1 
ATOM   5532 C CA    . MET B 2 299 ? 109.718 108.910 84.192  1.00 68.61  ? 299 MET B CA    1 
ATOM   5533 C C     . MET B 2 299 ? 109.017 110.010 84.978  1.00 68.61  ? 299 MET B C     1 
ATOM   5534 O O     . MET B 2 299 ? 108.804 109.887 86.190  1.00 68.61  ? 299 MET B O     1 
ATOM   5535 C CB    . MET B 2 299 ? 111.085 108.569 84.767  1.00 98.57  ? 299 MET B CB    1 
ATOM   5536 C CG    . MET B 2 299 ? 111.728 107.403 84.050  1.00 98.57  ? 299 MET B CG    1 
ATOM   5537 S SD    . MET B 2 299 ? 113.398 107.057 84.597  1.00 98.57  ? 299 MET B SD    1 
ATOM   5538 C CE    . MET B 2 299 ? 113.147 106.226 86.163  1.00 98.57  ? 299 MET B CE    1 
ATOM   5539 N N     . ALA B 2 300 ? 108.673 111.084 84.292  1.00 71.01  ? 300 ALA B N     1 
ATOM   5540 C CA    . ALA B 2 300 ? 107.991 112.228 84.848  1.00 71.01  ? 300 ALA B CA    1 
ATOM   5541 C C     . ALA B 2 300 ? 106.492 112.242 84.582  1.00 71.01  ? 300 ALA B C     1 
ATOM   5542 O O     . ALA B 2 300 ? 105.798 113.064 85.169  1.00 71.01  ? 300 ALA B O     1 
ATOM   5543 C CB    . ALA B 2 300 ? 108.608 113.493 84.264  1.00 96.83  ? 300 ALA B CB    1 
ATOM   5544 N N     . ALA B 2 301 ? 105.977 111.407 83.691  1.00 68.92  ? 301 ALA B N     1 
ATOM   5545 C CA    . ALA B 2 301 ? 104.556 111.444 83.300  1.00 68.92  ? 301 ALA B CA    1 
ATOM   5546 C C     . ALA B 2 301 ? 104.122 112.777 82.693  1.00 68.92  ? 301 ALA B C     1 
ATOM   5547 O O     . ALA B 2 301 ? 103.019 113.240 82.936  1.00 68.92  ? 301 ALA B O     1 
ATOM   5548 C CB    . ALA B 2 301 ? 103.637 111.124 84.481  1.00 93.98  ? 301 ALA B CB    1 
ATOM   5549 N N     . VAL B 2 302 ? 104.975 113.381 81.884  1.00 64.96  ? 302 VAL B N     1 
ATOM   5550 C CA    . VAL B 2 302 ? 104.675 114.636 81.207  1.00 64.96  ? 302 VAL B CA    1 
ATOM   5551 C C     . VAL B 2 302 ? 104.969 114.517 79.722  1.00 64.96  ? 302 VAL B C     1 
ATOM   5552 O O     . VAL B 2 302 ? 106.006 113.976 79.327  1.00 64.96  ? 302 VAL B O     1 
ATOM   5553 C CB    . VAL B 2 302 ? 105.484 115.797 81.787  1.00 94.49  ? 302 VAL B CB    1 
ATOM   5554 C CG1   . VAL B 2 302 ? 105.178 117.070 81.014  1.00 94.49  ? 302 VAL B CG1   1 
ATOM   5555 C CG2   . VAL B 2 302 ? 105.134 115.976 83.244  1.00 94.49  ? 302 VAL B CG2   1 
ATOM   5556 N N     . ASP B 2 303 ? 104.077 115.037 78.892  1.00 62.03  ? 303 ASP B N     1 
ATOM   5557 C CA    . ASP B 2 303 ? 104.299 114.977 77.446  1.00 62.03  ? 303 ASP B CA    1 
ATOM   5558 C C     . ASP B 2 303 ? 105.203 116.120 76.964  1.00 62.03  ? 303 ASP B C     1 
ATOM   5559 O O     . ASP B 2 303 ? 104.751 117.265 76.870  1.00 62.03  ? 303 ASP B O     1 
ATOM   5560 C CB    . ASP B 2 303 ? 102.973 115.029 76.703  1.00 79.75  ? 303 ASP B CB    1 
ATOM   5561 C CG    . ASP B 2 303 ? 103.164 114.858 75.234  1.00 79.75  ? 303 ASP B CG    1 
ATOM   5562 O OD1   . ASP B 2 303 ? 104.320 114.672 74.815  1.00 79.75  ? 303 ASP B OD1   1 
ATOM   5563 O OD2   . ASP B 2 303 ? 102.185 114.890 74.499  1.00 79.75  ? 303 ASP B OD2   1 
ATOM   5564 N N     . VAL B 2 304 ? 106.456 115.806 76.589  1.00 59.93  ? 304 VAL B N     1 
ATOM   5565 C CA    . VAL B 2 304 ? 107.441 116.805 76.155  1.00 59.93  ? 304 VAL B CA    1 
ATOM   5566 C C     . VAL B 2 304 ? 107.077 117.420 74.827  1.00 59.93  ? 304 VAL B C     1 
ATOM   5567 O O     . VAL B 2 304 ? 107.718 118.371 74.384  1.00 59.93  ? 304 VAL B O     1 
ATOM   5568 C CB    . VAL B 2 304 ? 108.857 116.205 76.043  1.00 87.17  ? 304 VAL B CB    1 
ATOM   5569 C CG1   . VAL B 2 304 ? 109.309 115.646 77.372  1.00 87.17  ? 304 VAL B CG1   1 
ATOM   5570 C CG2   . VAL B 2 304 ? 108.915 115.120 74.959  1.00 87.17  ? 304 VAL B CG2   1 
ATOM   5571 N N     . THR B 2 305 ? 106.069 116.863 74.183  1.00 61.61  ? 305 THR B N     1 
ATOM   5572 C CA    . THR B 2 305 ? 105.577 117.366 72.917  1.00 61.61  ? 305 THR B CA    1 
ATOM   5573 C C     . THR B 2 305 ? 105.022 118.755 73.066  1.00 61.61  ? 305 THR B C     1 
ATOM   5574 O O     . THR B 2 305 ? 105.122 119.570 72.147  1.00 61.61  ? 305 THR B O     1 
ATOM   5575 C CB    . THR B 2 305 ? 104.454 116.483 72.373  1.00 86.25  ? 305 THR B CB    1 
ATOM   5576 O OG1   . THR B 2 305 ? 104.917 115.140 72.219  1.00 86.25  ? 305 THR B OG1   1 
ATOM   5577 C CG2   . THR B 2 305 ? 103.992 116.992 71.025  1.00 86.25  ? 305 THR B CG2   1 
ATOM   5578 N N     . LYS B 2 306 ? 104.341 119.023 74.165  1.00 62.49  ? 306 LYS B N     1 
ATOM   5579 C CA    . LYS B 2 306 ? 103.665 120.301 74.300  1.00 62.49  ? 306 LYS B CA    1 
ATOM   5580 C C     . LYS B 2 306 ? 104.244 121.065 75.466  1.00 62.49  ? 306 LYS B C     1 
ATOM   5581 O O     . LYS B 2 306 ? 103.814 120.894 76.605  1.00 62.49  ? 306 LYS B O     1 
ATOM   5582 C CB    . LYS B 2 306 ? 102.182 120.094 74.479  1.00 93.73  ? 306 LYS B CB    1 
ATOM   5583 C CG    . LYS B 2 306 ? 101.517 119.305 73.365  1.00 93.73  ? 306 LYS B CG    1 
ATOM   5584 C CD    . LYS B 2 306 ? 101.506 120.056 72.048  1.00 93.73  ? 306 LYS B CD    1 
ATOM   5585 C CE    . LYS B 2 306 ? 100.705 119.301 70.991  1.00 93.73  ? 306 LYS B CE    1 
ATOM   5586 N NZ    . LYS B 2 306 ? 100.702 119.999 69.670  1.00 93.73  ? 306 LYS B NZ    1 
ATOM   5587 N N     . GLY B 2 307 ? 105.194 121.931 75.177  1.00 60.44  ? 307 GLY B N     1 
ATOM   5588 C CA    . GLY B 2 307 ? 105.900 122.682 76.201  1.00 60.44  ? 307 GLY B CA    1 
ATOM   5589 C C     . GLY B 2 307 ? 107.159 123.265 75.608  1.00 60.44  ? 307 GLY B C     1 
ATOM   5590 O O     . GLY B 2 307 ? 107.507 122.998 74.463  1.00 60.44  ? 307 GLY B O     1 
ATOM   5591 N N     . THR B 2 308 ? 107.858 124.072 76.392  1.00 61.16  ? 308 THR B N     1 
ATOM   5592 C CA    . THR B 2 308 ? 109.062 124.703 75.879  1.00 61.16  ? 308 THR B CA    1 
ATOM   5593 C C     . THR B 2 308 ? 110.289 124.248 76.643  1.00 61.16  ? 308 THR B C     1 
ATOM   5594 O O     . THR B 2 308 ? 110.318 124.278 77.866  1.00 61.16  ? 308 THR B O     1 
ATOM   5595 C CB    . THR B 2 308 ? 108.933 126.215 75.921  1.00 85.62  ? 308 THR B CB    1 
ATOM   5596 O OG1   . THR B 2 308 ? 107.861 126.614 75.063  1.00 85.62  ? 308 THR B OG1   1 
ATOM   5597 C CG2   . THR B 2 308 ? 110.180 126.847 75.443  1.00 85.62  ? 308 THR B CG2   1 
ATOM   5598 N N     . PHE B 2 309 ? 111.290 123.818 75.927  1.00 57.18  ? 309 PHE B N     1 
ATOM   5599 C CA    . PHE B 2 309 ? 112.461 123.369 76.603  1.00 57.18  ? 309 PHE B CA    1 
ATOM   5600 C C     . PHE B 2 309 ? 113.287 124.522 77.014  1.00 57.18  ? 309 PHE B C     1 
ATOM   5601 O O     . PHE B 2 309 ? 113.501 125.478 76.272  1.00 57.18  ? 309 PHE B O     1 
ATOM   5602 C CB    . PHE B 2 309 ? 113.298 122.502 75.728  1.00 79.79  ? 309 PHE B CB    1 
ATOM   5603 C CG    . PHE B 2 309 ? 112.843 121.118 75.613  1.00 79.79  ? 309 PHE B CG    1 
ATOM   5604 C CD1   . PHE B 2 309 ? 111.508 120.735 75.684  1.00 79.79  ? 309 PHE B CD1   1 
ATOM   5605 C CD2   . PHE B 2 309 ? 113.789 120.146 75.422  1.00 79.79  ? 309 PHE B CD2   1 
ATOM   5606 C CE1   . PHE B 2 309 ? 111.157 119.395 75.565  1.00 79.79  ? 309 PHE B CE1   1 
ATOM   5607 C CE2   . PHE B 2 309 ? 113.453 118.827 75.305  1.00 79.79  ? 309 PHE B CE2   1 
ATOM   5608 C CZ    . PHE B 2 309 ? 112.138 118.442 75.375  1.00 79.79  ? 309 PHE B CZ    1 
ATOM   5609 N N     . LEU B 2 310 ? 113.790 124.407 78.196  1.00 55.57  ? 310 LEU B N     1 
ATOM   5610 C CA    . LEU B 2 310 ? 114.739 125.353 78.688  1.00 55.57  ? 310 LEU B CA    1 
ATOM   5611 C C     . LEU B 2 310 ? 116.124 124.786 78.525  1.00 55.57  ? 310 LEU B C     1 
ATOM   5612 O O     . LEU B 2 310 ? 117.089 125.524 78.307  1.00 55.57  ? 310 LEU B O     1 
ATOM   5613 C CB    . LEU B 2 310 ? 114.427 125.655 80.152  1.00 82.27  ? 310 LEU B CB    1 
ATOM   5614 C CG    . LEU B 2 310 ? 112.986 126.117 80.417  1.00 82.27  ? 310 LEU B CG    1 
ATOM   5615 C CD1   . LEU B 2 310 ? 112.783 126.275 81.910  1.00 82.27  ? 310 LEU B CD1   1 
ATOM   5616 C CD2   . LEU B 2 310 ? 112.662 127.426 79.670  1.00 82.27  ? 310 LEU B CD2   1 
ATOM   5617 N N     . ALA B 2 311 ? 116.212 123.462 78.584  1.00 51.69  ? 311 ALA B N     1 
ATOM   5618 C CA    . ALA B 2 311 ? 117.486 122.780 78.439  1.00 51.69  ? 311 ALA B CA    1 
ATOM   5619 C C     . ALA B 2 311 ? 117.269 121.320 78.099  1.00 51.69  ? 311 ALA B C     1 
ATOM   5620 O O     . ALA B 2 311 ? 116.245 120.732 78.442  1.00 51.69  ? 311 ALA B O     1 
ATOM   5621 C CB    . ALA B 2 311 ? 118.310 122.887 79.711  1.00 70.49  ? 311 ALA B CB    1 
ATOM   5622 N N     . CYS B 2 312 ? 118.271 120.725 77.457  1.00 50.97  ? 312 CYS B N     1 
ATOM   5623 C CA    . CYS B 2 312 ? 118.246 119.290 77.226  1.00 50.97  ? 312 CYS B CA    1 
ATOM   5624 C C     . CYS B 2 312 ? 119.628 118.747 77.011  1.00 50.97  ? 312 CYS B C     1 
ATOM   5625 O O     . CYS B 2 312 ? 120.368 119.237 76.166  1.00 50.97  ? 312 CYS B O     1 
ATOM   5626 C CB    . CYS B 2 312 ? 117.426 118.902 76.030  1.00 68.65  ? 312 CYS B CB    1 
ATOM   5627 S SG    . CYS B 2 312 ? 117.391 117.121 75.794  1.00 68.65  ? 312 CYS B SG    1 
ATOM   5628 N N     . SER B 2 313 ? 119.945 117.718 77.751  1.00 54.56  ? 313 SER B N     1 
ATOM   5629 C CA    . SER B 2 313 ? 121.205 117.025 77.625  1.00 54.56  ? 313 SER B CA    1 
ATOM   5630 C C     . SER B 2 313 ? 120.900 115.578 77.313  1.00 54.56  ? 313 SER B C     1 
ATOM   5631 O O     . SER B 2 313 ? 120.344 114.848 78.143  1.00 54.56  ? 313 SER B O     1 
ATOM   5632 C CB    . SER B 2 313 ? 122.031 117.148 78.882  1.00 73.49  ? 313 SER B CB    1 
ATOM   5633 O OG    . SER B 2 313 ? 123.215 116.406 78.770  1.00 73.49  ? 313 SER B OG    1 
ATOM   5634 N N     . LEU B 2 314 ? 121.251 115.179 76.118  1.00 53.03  ? 314 LEU B N     1 
ATOM   5635 C CA    . LEU B 2 314 ? 120.950 113.868 75.588  1.00 53.03  ? 314 LEU B CA    1 
ATOM   5636 C C     . LEU B 2 314 ? 122.234 113.036 75.509  1.00 53.03  ? 314 LEU B C     1 
ATOM   5637 O O     . LEU B 2 314 ? 123.135 113.330 74.718  1.00 53.03  ? 314 LEU B O     1 
ATOM   5638 C CB    . LEU B 2 314 ? 120.286 114.101 74.257  1.00 78.51  ? 314 LEU B CB    1 
ATOM   5639 C CG    . LEU B 2 314 ? 119.950 112.931 73.430  1.00 78.51  ? 314 LEU B CG    1 
ATOM   5640 C CD1   . LEU B 2 314 ? 118.914 112.139 74.114  1.00 78.51  ? 314 LEU B CD1   1 
ATOM   5641 C CD2   . LEU B 2 314 ? 119.469 113.439 72.086  1.00 78.51  ? 314 LEU B CD2   1 
ATOM   5642 N N     . LEU B 2 315 ? 122.335 112.005 76.344  1.00 57.41  ? 315 LEU B N     1 
ATOM   5643 C CA    . LEU B 2 315 ? 123.553 111.217 76.466  1.00 57.41  ? 315 LEU B CA    1 
ATOM   5644 C C     . LEU B 2 315 ? 123.387 109.826 75.900  1.00 57.41  ? 315 LEU B C     1 
ATOM   5645 O O     . LEU B 2 315 ? 122.456 109.102 76.263  1.00 57.41  ? 315 LEU B O     1 
ATOM   5646 C CB    . LEU B 2 315 ? 123.998 111.091 77.915  1.00 85.00  ? 315 LEU B CB    1 
ATOM   5647 C CG    . LEU B 2 315 ? 125.199 110.167 78.208  1.00 85.00  ? 315 LEU B CG    1 
ATOM   5648 C CD1   . LEU B 2 315 ? 126.487 110.712 77.592  1.00 85.00  ? 315 LEU B CD1   1 
ATOM   5649 C CD2   . LEU B 2 315 ? 125.375 109.970 79.720  1.00 85.00  ? 315 LEU B CD2   1 
ATOM   5650 N N     . PHE B 2 316 ? 124.327 109.425 75.062  1.00 60.26  ? 316 PHE B N     1 
ATOM   5651 C CA    . PHE B 2 316 ? 124.303 108.077 74.553  1.00 60.26  ? 316 PHE B CA    1 
ATOM   5652 C C     . PHE B 2 316 ? 125.513 107.322 75.044  1.00 60.26  ? 316 PHE B C     1 
ATOM   5653 O O     . PHE B 2 316 ? 126.532 107.905 75.400  1.00 60.26  ? 316 PHE B O     1 
ATOM   5654 C CB    . PHE B 2 316 ? 124.227 108.056 73.070  1.00 84.08  ? 316 PHE B CB    1 
ATOM   5655 C CG    . PHE B 2 316 ? 123.036 108.679 72.574  1.00 84.08  ? 316 PHE B CG    1 
ATOM   5656 C CD1   . PHE B 2 316 ? 121.859 108.001 72.517  1.00 84.08  ? 316 PHE B CD1   1 
ATOM   5657 C CD2   . PHE B 2 316 ? 123.080 109.959 72.170  1.00 84.08  ? 316 PHE B CD2   1 
ATOM   5658 C CE1   . PHE B 2 316 ? 120.734 108.605 72.043  1.00 84.08  ? 316 PHE B CE1   1 
ATOM   5659 C CE2   . PHE B 2 316 ? 121.973 110.574 71.695  1.00 84.08  ? 316 PHE B CE2   1 
ATOM   5660 C CZ    . PHE B 2 316 ? 120.792 109.895 71.629  1.00 84.08  ? 316 PHE B CZ    1 
ATOM   5661 N N     . ARG B 2 317 ? 125.357 106.015 75.110  1.00 63.29  ? 317 ARG B N     1 
ATOM   5662 C CA    . ARG B 2 317 ? 126.424 105.152 75.544  1.00 63.29  ? 317 ARG B CA    1 
ATOM   5663 C C     . ARG B 2 317 ? 126.624 103.994 74.585  1.00 63.29  ? 317 ARG B C     1 
ATOM   5664 O O     . ARG B 2 317 ? 125.672 103.491 73.981  1.00 63.29  ? 317 ARG B O     1 
ATOM   5665 C CB    . ARG B 2 317 ? 126.136 104.587 76.923  1.00 93.00  ? 317 ARG B CB    1 
ATOM   5666 C CG    . ARG B 2 317 ? 125.980 105.619 78.013  1.00 93.00  ? 317 ARG B CG    1 
ATOM   5667 C CD    . ARG B 2 317 ? 125.657 104.976 79.344  1.00 93.00  ? 317 ARG B CD    1 
ATOM   5668 N NE    . ARG B 2 317 ? 126.791 104.301 79.968  1.00 93.00  ? 317 ARG B NE    1 
ATOM   5669 C CZ    . ARG B 2 317 ? 126.717 103.613 81.098  1.00 93.00  ? 317 ARG B CZ    1 
ATOM   5670 N NH1   . ARG B 2 317 ? 125.570 103.453 81.724  1.00 93.00  ? 317 ARG B NH1   1 
ATOM   5671 N NH2   . ARG B 2 317 ? 127.824 103.079 81.612  1.00 93.00  ? 317 ARG B NH2   1 
ATOM   5672 N N     . GLY B 2 318 ? 127.879 103.543 74.509  1.00 68.50  ? 318 GLY B N     1 
ATOM   5673 C CA    . GLY B 2 318 ? 128.252 102.339 73.791  1.00 68.50  ? 318 GLY B CA    1 
ATOM   5674 C C     . GLY B 2 318 ? 128.660 102.493 72.338  1.00 68.50  ? 318 GLY B C     1 
ATOM   5675 O O     . GLY B 2 318 ? 129.433 103.377 71.959  1.00 68.50  ? 318 GLY B O     1 
ATOM   5676 N N     . GLU B 2 319 ? 128.116 101.600 71.518  1.00 71.53  ? 319 GLU B N     1 
ATOM   5677 C CA    . GLU B 2 319 ? 128.484 101.395 70.121  1.00 71.53  ? 319 GLU B CA    1 
ATOM   5678 C C     . GLU B 2 319 ? 127.860 102.386 69.143  1.00 71.53  ? 319 GLU B C     1 
ATOM   5679 O O     . GLU B 2 319 ? 128.070 102.251 67.932  1.00 71.53  ? 319 GLU B O     1 
ATOM   5680 C CB    . GLU B 2 319 ? 128.075 99.992  69.685  1.00 96.08  ? 319 GLU B CB    1 
ATOM   5681 C CG    . GLU B 2 319 ? 128.798 98.857  70.349  1.00 96.08  ? 319 GLU B CG    1 
ATOM   5682 C CD    . GLU B 2 319 ? 128.298 97.530  69.852  1.00 96.08  ? 319 GLU B CD    1 
ATOM   5683 O OE1   . GLU B 2 319 ? 127.412 97.518  68.991  1.00 96.08  ? 319 GLU B OE1   1 
ATOM   5684 O OE2   . GLU B 2 319 ? 128.779 96.502  70.324  1.00 96.08  ? 319 GLU B OE2   1 
ATOM   5685 N N     . ASN B 2 320 ? 127.076 103.340 69.611  1.00 71.46  ? 320 ASN B N     1 
ATOM   5686 C CA    . ASN B 2 320 ? 126.462 104.288 68.702  1.00 71.46  ? 320 ASN B CA    1 
ATOM   5687 C C     . ASN B 2 320 ? 127.481 105.122 67.938  1.00 71.46  ? 320 ASN B C     1 
ATOM   5688 O O     . ASN B 2 320 ? 128.463 105.617 68.490  1.00 71.46  ? 320 ASN B O     1 
ATOM   5689 C CB    . ASN B 2 320 ? 125.557 105.197 69.466  1.00 96.82  ? 320 ASN B CB    1 
ATOM   5690 C CG    . ASN B 2 320 ? 124.412 104.491 69.947  1.00 96.82  ? 320 ASN B CG    1 
ATOM   5691 O OD1   . ASN B 2 320 ? 124.015 103.500 69.357  1.00 96.82  ? 320 ASN B OD1   1 
ATOM   5692 N ND2   . ASN B 2 320 ? 123.852 104.954 71.032  1.00 96.82  ? 320 ASN B ND2   1 
ATOM   5693 N N     . THR B 2 321 ? 127.210 105.277 66.655  1.00 72.21  ? 321 THR B N     1 
ATOM   5694 C CA    . THR B 2 321 ? 127.998 106.077 65.739  1.00 72.21  ? 321 THR B CA    1 
ATOM   5695 C C     . THR B 2 321 ? 127.747 107.538 66.027  1.00 72.21  ? 321 THR B C     1 
ATOM   5696 O O     . THR B 2 321 ? 126.596 107.951 66.112  1.00 72.21  ? 321 THR B O     1 
ATOM   5697 C CB    . THR B 2 321 ? 127.541 105.805 64.303  1.00 101.09 ? 321 THR B CB    1 
ATOM   5698 O OG1   . THR B 2 321 ? 127.551 104.410 64.001  1.00 101.09 ? 321 THR B OG1   1 
ATOM   5699 C CG2   . THR B 2 321 ? 128.393 106.515 63.297  1.00 101.09 ? 321 THR B CG2   1 
ATOM   5700 N N     . ALA B 2 322 ? 128.800 108.339 66.093  1.00 67.22  ? 322 ALA B N     1 
ATOM   5701 C CA    . ALA B 2 322 ? 128.614 109.764 66.347  1.00 67.22  ? 322 ALA B CA    1 
ATOM   5702 C C     . ALA B 2 322 ? 127.802 110.438 65.251  1.00 67.22  ? 322 ALA B C     1 
ATOM   5703 O O     . ALA B 2 322 ? 126.990 111.339 65.512  1.00 67.22  ? 322 ALA B O     1 
ATOM   5704 C CB    . ALA B 2 322 ? 129.968 110.442 66.473  1.00 91.66  ? 322 ALA B CB    1 
ATOM   5705 N N     . GLN B 2 323 ? 128.015 110.010 64.025  1.00 69.76  ? 323 GLN B N     1 
ATOM   5706 C CA    . GLN B 2 323 ? 127.355 110.587 62.882  1.00 69.76  ? 323 GLN B CA    1 
ATOM   5707 C C     . GLN B 2 323 ? 125.917 110.137 62.771  1.00 69.76  ? 323 GLN B C     1 
ATOM   5708 O O     . GLN B 2 323 ? 125.058 110.898 62.325  1.00 69.76  ? 323 GLN B O     1 
ATOM   5709 C CB    . GLN B 2 323 ? 128.127 110.200 61.636  1.00 97.47  ? 323 GLN B CB    1 
ATOM   5710 C CG    . GLN B 2 323 ? 129.507 110.821 61.566  1.00 97.47  ? 323 GLN B CG    1 
ATOM   5711 C CD    . GLN B 2 323 ? 130.510 110.181 62.516  1.00 97.47  ? 323 GLN B CD    1 
ATOM   5712 O OE1   . GLN B 2 323 ? 130.254 109.129 63.115  1.00 97.47  ? 323 GLN B OE1   1 
ATOM   5713 N NE2   . GLN B 2 323 ? 131.661 110.822 62.662  1.00 97.47  ? 323 GLN B NE2   1 
ATOM   5714 N N     . ASP B 2 324 ? 125.634 108.914 63.161  1.00 69.47  ? 324 ASP B N     1 
ATOM   5715 C CA    . ASP B 2 324 ? 124.269 108.468 63.044  1.00 69.47  ? 324 ASP B CA    1 
ATOM   5716 C C     . ASP B 2 324 ? 123.421 109.212 64.048  1.00 69.47  ? 324 ASP B C     1 
ATOM   5717 O O     . ASP B 2 324 ? 122.290 109.600 63.741  1.00 69.47  ? 324 ASP B O     1 
ATOM   5718 C CB    . ASP B 2 324 ? 124.153 106.963 63.284  1.00 89.32  ? 324 ASP B CB    1 
ATOM   5719 C CG    . ASP B 2 324 ? 124.888 106.114 62.245  1.00 89.32  ? 324 ASP B CG    1 
ATOM   5720 O OD1   . ASP B 2 324 ? 125.146 106.581 61.138  1.00 89.32  ? 324 ASP B OD1   1 
ATOM   5721 O OD2   . ASP B 2 324 ? 125.222 104.962 62.565  1.00 89.32  ? 324 ASP B OD2   1 
ATOM   5722 N N     . ILE B 2 325 ? 123.962 109.433 65.254  1.00 67.66  ? 325 ILE B N     1 
ATOM   5723 C CA    . ILE B 2 325 ? 123.223 110.195 66.250  1.00 67.66  ? 325 ILE B CA    1 
ATOM   5724 C C     . ILE B 2 325 ? 123.053 111.601 65.755  1.00 67.66  ? 325 ILE B C     1 
ATOM   5725 O O     . ILE B 2 325 ? 121.943 112.150 65.767  1.00 67.66  ? 325 ILE B O     1 
ATOM   5726 C CB    . ILE B 2 325 ? 123.911 110.185 67.629  1.00 100.17 ? 325 ILE B CB    1 
ATOM   5727 C CG1   . ILE B 2 325 ? 123.928 108.757 68.251  1.00 100.17 ? 325 ILE B CG1   1 
ATOM   5728 C CG2   . ILE B 2 325 ? 123.233 111.201 68.550  1.00 100.17 ? 325 ILE B CG2   1 
ATOM   5729 C CD1   . ILE B 2 325 ? 122.567 108.114 68.525  1.00 100.17 ? 325 ILE B CD1   1 
ATOM   5730 N N     . THR B 2 326 ? 124.130 112.173 65.235  1.00 66.50  ? 326 THR B N     1 
ATOM   5731 C CA    . THR B 2 326 ? 124.018 113.511 64.712  1.00 66.50  ? 326 THR B CA    1 
ATOM   5732 C C     . THR B 2 326 ? 122.902 113.582 63.690  1.00 66.50  ? 326 THR B C     1 
ATOM   5733 O O     . THR B 2 326 ? 122.092 114.513 63.715  1.00 66.50  ? 326 THR B O     1 
ATOM   5734 C CB    . THR B 2 326 ? 125.344 113.951 64.115  1.00 93.10  ? 326 THR B CB    1 
ATOM   5735 O OG1   . THR B 2 326 ? 126.337 113.976 65.149  1.00 93.10  ? 326 THR B OG1   1 
ATOM   5736 C CG2   . THR B 2 326 ? 125.211 115.336 63.501  1.00 93.10  ? 326 THR B CG2   1 
ATOM   5737 N N     . ASN B 2 327 ? 122.813 112.590 62.811  1.00 68.49  ? 327 ASN B N     1 
ATOM   5738 C CA    . ASN B 2 327 ? 121.733 112.596 61.847  1.00 68.49  ? 327 ASN B CA    1 
ATOM   5739 C C     . ASN B 2 327 ? 120.402 112.350 62.505  1.00 68.49  ? 327 ASN B C     1 
ATOM   5740 O O     . ASN B 2 327 ? 119.395 112.916 62.091  1.00 68.49  ? 327 ASN B O     1 
ATOM   5741 C CB    . ASN B 2 327 ? 121.996 111.555 60.790  1.00 92.79  ? 327 ASN B CB    1 
ATOM   5742 C CG    . ASN B 2 327 ? 123.123 111.942 59.905  1.00 92.79  ? 327 ASN B CG    1 
ATOM   5743 O OD1   . ASN B 2 327 ? 123.473 113.121 59.794  1.00 92.79  ? 327 ASN B OD1   1 
ATOM   5744 N ND2   . ASN B 2 327 ? 123.709 110.966 59.263  1.00 92.79  ? 327 ASN B ND2   1 
ATOM   5745 N N     . ALA B 2 328 ? 120.380 111.545 63.552  1.00 66.49  ? 328 ALA B N     1 
ATOM   5746 C CA    . ALA B 2 328 ? 119.119 111.247 64.215  1.00 66.49  ? 328 ALA B CA    1 
ATOM   5747 C C     . ALA B 2 328 ? 118.482 112.503 64.779  1.00 66.49  ? 328 ALA B C     1 
ATOM   5748 O O     . ALA B 2 328 ? 117.257 112.670 64.724  1.00 66.49  ? 328 ALA B O     1 
ATOM   5749 C CB    . ALA B 2 328 ? 119.334 110.228 65.322  1.00 90.67  ? 328 ALA B CB    1 
ATOM   5750 N N     . LEU B 2 329 ? 119.299 113.413 65.285  1.00 65.85  ? 329 LEU B N     1 
ATOM   5751 C CA    . LEU B 2 329 ? 118.779 114.632 65.883  1.00 65.85  ? 329 LEU B CA    1 
ATOM   5752 C C     . LEU B 2 329 ? 118.043 115.491 64.882  1.00 65.85  ? 329 LEU B C     1 
ATOM   5753 O O     . LEU B 2 329 ? 117.213 116.311 65.266  1.00 65.85  ? 329 LEU B O     1 
ATOM   5754 C CB    . LEU B 2 329 ? 119.916 115.445 66.490  1.00 97.49  ? 329 LEU B CB    1 
ATOM   5755 C CG    . LEU B 2 329 ? 120.228 115.268 67.987  1.00 97.49  ? 329 LEU B CG    1 
ATOM   5756 C CD1   . LEU B 2 329 ? 119.060 115.768 68.848  1.00 97.49  ? 329 LEU B CD1   1 
ATOM   5757 C CD2   . LEU B 2 329 ? 120.567 113.821 68.300  1.00 97.49  ? 329 LEU B CD2   1 
ATOM   5758 N N     . LEU B 2 330 ? 118.313 115.316 63.603  1.00 65.26  ? 330 LEU B N     1 
ATOM   5759 C CA    . LEU B 2 330 ? 117.670 116.143 62.605  1.00 65.26  ? 330 LEU B CA    1 
ATOM   5760 C C     . LEU B 2 330 ? 116.174 115.947 62.612  1.00 65.26  ? 330 LEU B C     1 
ATOM   5761 O O     . LEU B 2 330 ? 115.430 116.861 62.278  1.00 65.26  ? 330 LEU B O     1 
ATOM   5762 C CB    . LEU B 2 330 ? 118.221 115.797 61.237  1.00 96.62  ? 330 LEU B CB    1 
ATOM   5763 C CG    . LEU B 2 330 ? 119.708 116.086 61.001  1.00 96.62  ? 330 LEU B CG    1 
ATOM   5764 C CD1   . LEU B 2 330 ? 120.134 115.460 59.680  1.00 96.62  ? 330 LEU B CD1   1 
ATOM   5765 C CD2   . LEU B 2 330 ? 119.973 117.593 61.002  1.00 96.62  ? 330 LEU B CD2   1 
ATOM   5766 N N     . ASP B 2 331 ? 115.713 114.777 62.998  1.00 66.86  ? 331 ASP B N     1 
ATOM   5767 C CA    . ASP B 2 331 ? 114.291 114.507 63.026  1.00 66.86  ? 331 ASP B CA    1 
ATOM   5768 C C     . ASP B 2 331 ? 113.692 114.715 64.409  1.00 66.86  ? 331 ASP B C     1 
ATOM   5769 O O     . ASP B 2 331 ? 112.529 114.362 64.637  1.00 66.86  ? 331 ASP B O     1 
ATOM   5770 C CB    . ASP B 2 331 ? 114.021 113.078 62.556  1.00 85.96  ? 331 ASP B CB    1 
ATOM   5771 C CG    . ASP B 2 331 ? 114.367 112.848 61.091  1.00 85.96  ? 331 ASP B CG    1 
ATOM   5772 O OD1   . ASP B 2 331 ? 114.318 113.782 60.289  1.00 85.96  ? 331 ASP B OD1   1 
ATOM   5773 O OD2   . ASP B 2 331 ? 114.665 111.703 60.744  1.00 85.96  ? 331 ASP B OD2   1 
ATOM   5774 N N     . ILE B 2 332 ? 114.479 115.213 65.348  1.00 65.62  ? 332 ILE B N     1 
ATOM   5775 C CA    . ILE B 2 332 ? 114.006 115.521 66.673  1.00 65.62  ? 332 ILE B CA    1 
ATOM   5776 C C     . ILE B 2 332 ? 113.819 117.002 66.808  1.00 65.62  ? 332 ILE B C     1 
ATOM   5777 O O     . ILE B 2 332 ? 112.778 117.481 67.264  1.00 65.62  ? 332 ILE B O     1 
ATOM   5778 C CB    . ILE B 2 332 ? 114.991 115.002 67.739  1.00 97.15  ? 332 ILE B CB    1 
ATOM   5779 C CG1   . ILE B 2 332 ? 115.112 113.489 67.612  1.00 97.15  ? 332 ILE B CG1   1 
ATOM   5780 C CG2   . ILE B 2 332 ? 114.514 115.423 69.137  1.00 97.15  ? 332 ILE B CG2   1 
ATOM   5781 C CD1   . ILE B 2 332 ? 116.203 112.832 68.422  1.00 97.15  ? 332 ILE B CD1   1 
ATOM   5782 N N     . LYS B 2 333 ? 114.844 117.735 66.410  1.00 61.75  ? 333 LYS B N     1 
ATOM   5783 C CA    . LYS B 2 333 ? 114.766 119.173 66.448  1.00 61.75  ? 333 LYS B CA    1 
ATOM   5784 C C     . LYS B 2 333 ? 113.606 119.589 65.558  1.00 61.75  ? 333 LYS B C     1 
ATOM   5785 O O     . LYS B 2 333 ? 113.491 119.123 64.429  1.00 61.75  ? 333 LYS B O     1 
ATOM   5786 C CB    . LYS B 2 333 ? 116.077 119.774 65.955  1.00 92.62  ? 333 LYS B CB    1 
ATOM   5787 C CG    . LYS B 2 333 ? 117.282 119.491 66.831  1.00 92.62  ? 333 LYS B CG    1 
ATOM   5788 C CD    . LYS B 2 333 ? 118.539 120.113 66.223  1.00 92.62  ? 333 LYS B CD    1 
ATOM   5789 C CE    . LYS B 2 333 ? 119.789 119.846 67.057  1.00 92.62  ? 333 LYS B CE    1 
ATOM   5790 N NZ    . LYS B 2 333 ? 121.013 120.446 66.432  1.00 92.62  ? 333 LYS B NZ    1 
ATOM   5791 N N     . GLY B 2 334 ? 112.745 120.457 66.052  1.00 60.75  ? 334 GLY B N     1 
ATOM   5792 C CA    . GLY B 2 334 ? 111.578 120.838 65.296  1.00 60.75  ? 334 GLY B CA    1 
ATOM   5793 C C     . GLY B 2 334 ? 110.336 120.132 65.768  1.00 60.75  ? 334 GLY B C     1 
ATOM   5794 O O     . GLY B 2 334 ? 109.223 120.547 65.443  1.00 60.75  ? 334 GLY B O     1 
ATOM   5795 N N     . ARG B 2 335 ? 110.494 119.061 66.505  1.00 64.23  ? 335 ARG B N     1 
ATOM   5796 C CA    . ARG B 2 335 ? 109.382 118.487 67.203  1.00 64.23  ? 335 ARG B CA    1 
ATOM   5797 C C     . ARG B 2 335 ? 109.531 118.995 68.589  1.00 64.23  ? 335 ARG B C     1 
ATOM   5798 O O     . ARG B 2 335 ? 108.568 119.361 69.252  1.00 64.23  ? 335 ARG B O     1 
ATOM   5799 C CB    . ARG B 2 335 ? 109.444 116.956 67.167  1.00 94.38  ? 335 ARG B CB    1 
ATOM   5800 C CG    . ARG B 2 335 ? 109.459 116.362 65.774  1.00 94.38  ? 335 ARG B CG    1 
ATOM   5801 C CD    . ARG B 2 335 ? 109.267 114.854 65.803  1.00 94.38  ? 335 ARG B CD    1 
ATOM   5802 N NE    . ARG B 2 335 ? 110.354 114.095 66.441  1.00 94.38  ? 335 ARG B NE    1 
ATOM   5803 C CZ    . ARG B 2 335 ? 110.275 113.515 67.645  1.00 94.38  ? 335 ARG B CZ    1 
ATOM   5804 N NH1   . ARG B 2 335 ? 109.200 113.647 68.401  1.00 94.38  ? 335 ARG B NH1   1 
ATOM   5805 N NH2   . ARG B 2 335 ? 111.288 112.768 68.097  1.00 94.38  ? 335 ARG B NH2   1 
ATOM   5806 N N     . ILE B 2 336 ? 110.791 119.203 68.901  1.00 61.67  ? 336 ILE B N     1 
ATOM   5807 C CA    . ILE B 2 336 ? 111.247 119.763 70.145  1.00 61.67  ? 336 ILE B CA    1 
ATOM   5808 C C     . ILE B 2 336 ? 111.602 121.216 69.907  1.00 61.67  ? 336 ILE B C     1 
ATOM   5809 O O     . ILE B 2 336 ? 112.330 121.550 68.964  1.00 61.67  ? 336 ILE B O     1 
ATOM   5810 C CB    . ILE B 2 336 ? 112.455 118.988 70.690  1.00 91.30  ? 336 ILE B CB    1 
ATOM   5811 C CG1   . ILE B 2 336 ? 112.108 117.491 70.904  1.00 91.30  ? 336 ILE B CG1   1 
ATOM   5812 C CG2   . ILE B 2 336 ? 112.988 119.653 71.956  1.00 91.30  ? 336 ILE B CG2   1 
ATOM   5813 C CD1   . ILE B 2 336 ? 110.933 117.195 71.851  1.00 91.30  ? 336 ILE B CD1   1 
ATOM   5814 N N     . LYS B 2 337 ? 111.059 122.085 70.750  1.00 61.34  ? 337 LYS B N     1 
ATOM   5815 C CA    . LYS B 2 337 ? 111.275 123.522 70.671  1.00 61.34  ? 337 LYS B CA    1 
ATOM   5816 C C     . LYS B 2 337 ? 111.794 124.064 72.000  1.00 61.34  ? 337 LYS B C     1 
ATOM   5817 O O     . LYS B 2 337 ? 111.435 123.579 73.072  1.00 61.34  ? 337 LYS B O     1 
ATOM   5818 C CB    . LYS B 2 337 ? 109.995 124.249 70.280  1.00 92.01  ? 337 LYS B CB    1 
ATOM   5819 C CG    . LYS B 2 337 ? 109.627 124.170 68.781  1.00 92.01  ? 337 LYS B CG    1 
ATOM   5820 C CD    . LYS B 2 337 ? 108.893 122.861 68.349  1.00 92.01  ? 337 LYS B CD    1 
ATOM   5821 C CE    . LYS B 2 337 ? 107.491 122.706 68.956  1.00 92.01  ? 337 LYS B CE    1 
ATOM   5822 N NZ    . LYS B 2 337 ? 106.800 121.479 68.468  1.00 92.01  ? 337 LYS B NZ    1 
ATOM   5823 N N     . PHE B 2 338 ? 112.648 125.064 71.905  1.00 59.42  ? 338 PHE B N     1 
ATOM   5824 C CA    . PHE B 2 338 ? 113.284 125.710 73.029  1.00 59.42  ? 338 PHE B CA    1 
ATOM   5825 C C     . PHE B 2 338 ? 112.893 127.164 73.117  1.00 59.42  ? 338 PHE B C     1 
ATOM   5826 O O     . PHE B 2 338 ? 112.533 127.797 72.125  1.00 59.42  ? 338 PHE B O     1 
ATOM   5827 C CB    . PHE B 2 338 ? 114.784 125.693 72.919  1.00 82.91  ? 338 PHE B CB    1 
ATOM   5828 C CG    . PHE B 2 338 ? 115.396 124.400 73.152  1.00 82.91  ? 338 PHE B CG    1 
ATOM   5829 C CD1   . PHE B 2 338 ? 115.378 123.424 72.182  1.00 82.91  ? 338 PHE B CD1   1 
ATOM   5830 C CD2   . PHE B 2 338 ? 116.063 124.167 74.328  1.00 82.91  ? 338 PHE B CD2   1 
ATOM   5831 C CE1   . PHE B 2 338 ? 115.984 122.219 72.401  1.00 82.91  ? 338 PHE B CE1   1 
ATOM   5832 C CE2   . PHE B 2 338 ? 116.677 122.968 74.553  1.00 82.91  ? 338 PHE B CE2   1 
ATOM   5833 C CZ    . PHE B 2 338 ? 116.635 121.987 73.590  1.00 82.91  ? 338 PHE B CZ    1 
ATOM   5834 N N     . SER B 2 339 ? 113.045 127.708 74.312  1.00 54.02  ? 339 SER B N     1 
ATOM   5835 C CA    . SER B 2 339 ? 112.736 129.108 74.537  1.00 54.02  ? 339 SER B CA    1 
ATOM   5836 C C     . SER B 2 339 ? 113.582 130.041 73.690  1.00 54.02  ? 339 SER B C     1 
ATOM   5837 O O     . SER B 2 339 ? 114.786 129.860 73.508  1.00 54.02  ? 339 SER B O     1 
ATOM   5838 C CB    . SER B 2 339 ? 112.919 129.470 76.000  1.00 72.76  ? 339 SER B CB    1 
ATOM   5839 O OG    . SER B 2 339 ? 112.802 130.869 76.162  1.00 72.76  ? 339 SER B OG    1 
ATOM   5840 N N     . SER B 2 340 ? 112.935 131.089 73.227  1.00 50.63  ? 340 SER B N     1 
ATOM   5841 C CA    . SER B 2 340 ? 113.547 132.107 72.402  1.00 50.63  ? 340 SER B CA    1 
ATOM   5842 C C     . SER B 2 340 ? 114.517 132.977 73.162  1.00 50.63  ? 340 SER B C     1 
ATOM   5843 O O     . SER B 2 340 ? 115.243 133.765 72.552  1.00 50.63  ? 340 SER B O     1 
ATOM   5844 C CB    . SER B 2 340 ? 112.460 132.984 71.824  1.00 68.20  ? 340 SER B CB    1 
ATOM   5845 O OG    . SER B 2 340 ? 111.870 133.727 72.859  1.00 68.20  ? 340 SER B OG    1 
ATOM   5846 N N     . PHE B 2 341 ? 114.541 132.868 74.470  1.00 53.19  ? 341 PHE B N     1 
ATOM   5847 C CA    . PHE B 2 341 ? 115.381 133.724 75.276  1.00 53.19  ? 341 PHE B CA    1 
ATOM   5848 C C     . PHE B 2 341 ? 116.676 133.070 75.693  1.00 53.19  ? 341 PHE B C     1 
ATOM   5849 O O     . PHE B 2 341 ? 117.413 133.628 76.510  1.00 53.19  ? 341 PHE B O     1 
ATOM   5850 C CB    . PHE B 2 341 ? 114.613 134.161 76.497  1.00 74.22  ? 341 PHE B CB    1 
ATOM   5851 C CG    . PHE B 2 341 ? 113.428 134.953 76.157  1.00 74.22  ? 341 PHE B CG    1 
ATOM   5852 C CD1   . PHE B 2 341 ? 113.558 136.264 75.762  1.00 74.22  ? 341 PHE B CD1   1 
ATOM   5853 C CD2   . PHE B 2 341 ? 112.181 134.388 76.197  1.00 74.22  ? 341 PHE B CD2   1 
ATOM   5854 C CE1   . PHE B 2 341 ? 112.464 137.005 75.430  1.00 74.22  ? 341 PHE B CE1   1 
ATOM   5855 C CE2   . PHE B 2 341 ? 111.072 135.125 75.865  1.00 74.22  ? 341 PHE B CE2   1 
ATOM   5856 C CZ    . PHE B 2 341 ? 111.215 136.439 75.482  1.00 74.22  ? 341 PHE B CZ    1 
ATOM   5857 N N     . ILE B 2 342 ? 116.976 131.905 75.152  1.00 53.39  ? 342 ILE B N     1 
ATOM   5858 C CA    . ILE B 2 342 ? 118.182 131.184 75.532  1.00 53.39  ? 342 ILE B CA    1 
ATOM   5859 C C     . ILE B 2 342 ? 118.909 130.739 74.266  1.00 53.39  ? 342 ILE B C     1 
ATOM   5860 O O     . ILE B 2 342 ? 118.381 130.892 73.157  1.00 53.39  ? 342 ILE B O     1 
ATOM   5861 C CB    . ILE B 2 342 ? 117.830 129.993 76.442  1.00 79.04  ? 342 ILE B CB    1 
ATOM   5862 C CG1   . ILE B 2 342 ? 116.862 129.091 75.681  1.00 79.04  ? 342 ILE B CG1   1 
ATOM   5863 C CG2   . ILE B 2 342 ? 117.215 130.503 77.752  1.00 79.04  ? 342 ILE B CG2   1 
ATOM   5864 C CD1   . ILE B 2 342 ? 116.564 127.782 76.318  1.00 79.04  ? 342 ILE B CD1   1 
ATOM   5865 N N     . PRO B 2 343 ? 120.183 130.351 74.380  1.00 54.89  ? 343 PRO B N     1 
ATOM   5866 C CA    . PRO B 2 343 ? 120.857 129.592 73.317  1.00 54.89  ? 343 PRO B CA    1 
ATOM   5867 C C     . PRO B 2 343 ? 120.083 128.306 73.164  1.00 54.89  ? 343 PRO B C     1 
ATOM   5868 O O     . PRO B 2 343 ? 119.667 127.731 74.166  1.00 54.89  ? 343 PRO B O     1 
ATOM   5869 C CB    . PRO B 2 343 ? 122.250 129.344 73.901  1.00 362.41 ? 343 PRO B CB    1 
ATOM   5870 C CG    . PRO B 2 343 ? 122.420 130.445 74.927  1.00 362.41 ? 343 PRO B CG    1 
ATOM   5871 C CD    . PRO B 2 343 ? 121.059 130.682 75.499  1.00 362.41 ? 343 PRO B CD    1 
ATOM   5872 N N     . THR B 2 344 ? 119.886 127.831 71.939  1.00 55.51  ? 344 THR B N     1 
ATOM   5873 C CA    . THR B 2 344 ? 119.012 126.674 71.780  1.00 55.51  ? 344 THR B CA    1 
ATOM   5874 C C     . THR B 2 344 ? 119.685 125.481 71.127  1.00 55.51  ? 344 THR B C     1 
ATOM   5875 O O     . THR B 2 344 ? 120.804 125.555 70.618  1.00 55.51  ? 344 THR B O     1 
ATOM   5876 C CB    . THR B 2 344 ? 117.764 127.024 70.968  1.00 77.71  ? 344 THR B CB    1 
ATOM   5877 O OG1   . THR B 2 344 ? 118.150 127.427 69.652  1.00 77.71  ? 344 THR B OG1   1 
ATOM   5878 C CG2   . THR B 2 344 ? 116.995 128.144 71.652  1.00 77.71  ? 344 THR B CG2   1 
ATOM   5879 N N     . GLY B 2 345 ? 118.960 124.373 71.158  1.00 55.81  ? 345 GLY B N     1 
ATOM   5880 C CA    . GLY B 2 345 ? 119.339 123.115 70.558  1.00 55.81  ? 345 GLY B CA    1 
ATOM   5881 C C     . GLY B 2 345 ? 119.616 122.070 71.613  1.00 55.81  ? 345 GLY B C     1 
ATOM   5882 O O     . GLY B 2 345 ? 119.949 122.383 72.763  1.00 55.81  ? 345 GLY B O     1 
ATOM   5883 N N     . ILE B 2 346 ? 119.453 120.820 71.230  1.00 57.92  ? 346 ILE B N     1 
ATOM   5884 C CA    . ILE B 2 346 ? 119.713 119.728 72.132  1.00 57.92  ? 346 ILE B CA    1 
ATOM   5885 C C     . ILE B 2 346 ? 121.194 119.541 72.172  1.00 57.92  ? 346 ILE B C     1 
ATOM   5886 O O     . ILE B 2 346 ? 121.837 119.505 71.129  1.00 57.92  ? 346 ILE B O     1 
ATOM   5887 C CB    . ILE B 2 346 ? 119.012 118.460 71.664  1.00 85.75  ? 346 ILE B CB    1 
ATOM   5888 C CG1   . ILE B 2 346 ? 117.492 118.689 71.705  1.00 85.75  ? 346 ILE B CG1   1 
ATOM   5889 C CG2   . ILE B 2 346 ? 119.449 117.272 72.546  1.00 85.75  ? 346 ILE B CG2   1 
ATOM   5890 C CD1   . ILE B 2 346 ? 116.652 117.637 70.998  1.00 85.75  ? 346 ILE B CD1   1 
ATOM   5891 N N     . LYS B 2 347 ? 121.749 119.454 73.345  1.00 58.44  ? 347 LYS B N     1 
ATOM   5892 C CA    . LYS B 2 347 ? 123.159 119.196 73.438  1.00 58.44  ? 347 LYS B CA    1 
ATOM   5893 C C     . LYS B 2 347 ? 123.297 117.705 73.612  1.00 58.44  ? 347 LYS B C     1 
ATOM   5894 O O     . LYS B 2 347 ? 122.565 117.122 74.405  1.00 58.44  ? 347 LYS B O     1 
ATOM   5895 C CB    . LYS B 2 347 ? 123.751 119.964 74.593  1.00 87.66  ? 347 LYS B CB    1 
ATOM   5896 C CG    . LYS B 2 347 ? 123.349 121.441 74.564  1.00 87.66  ? 347 LYS B CG    1 
ATOM   5897 C CD    . LYS B 2 347 ? 123.805 122.170 73.294  1.00 87.66  ? 347 LYS B CD    1 
ATOM   5898 C CE    . LYS B 2 347 ? 123.397 123.646 73.325  1.00 87.66  ? 347 LYS B CE    1 
ATOM   5899 N NZ    . LYS B 2 347 ? 123.771 124.368 72.073  1.00 87.66  ? 347 LYS B NZ    1 
ATOM   5900 N N     . TYR B 2 348 ? 124.165 117.072 72.830  1.00 62.61  ? 348 TYR B N     1 
ATOM   5901 C CA    . TYR B 2 348 ? 124.266 115.627 72.911  1.00 62.61  ? 348 TYR B CA    1 
ATOM   5902 C C     . TYR B 2 348 ? 125.659 115.169 72.606  1.00 62.61  ? 348 TYR B C     1 
ATOM   5903 O O     . TYR B 2 348 ? 126.447 115.866 71.974  1.00 62.61  ? 348 TYR B O     1 
ATOM   5904 C CB    . TYR B 2 348 ? 123.358 114.920 71.939  1.00 86.69  ? 348 TYR B CB    1 
ATOM   5905 C CG    . TYR B 2 348 ? 123.832 115.127 70.581  1.00 86.69  ? 348 TYR B CG    1 
ATOM   5906 C CD1   . TYR B 2 348 ? 123.470 116.256 69.916  1.00 86.69  ? 348 TYR B CD1   1 
ATOM   5907 C CD2   . TYR B 2 348 ? 124.657 114.213 69.960  1.00 86.69  ? 348 TYR B CD2   1 
ATOM   5908 C CE1   . TYR B 2 348 ? 123.912 116.499 68.664  1.00 86.69  ? 348 TYR B CE1   1 
ATOM   5909 C CE2   . TYR B 2 348 ? 125.117 114.439 68.687  1.00 86.69  ? 348 TYR B CE2   1 
ATOM   5910 C CZ    . TYR B 2 348 ? 124.737 115.597 68.044  1.00 86.69  ? 348 TYR B CZ    1 
ATOM   5911 O OH    . TYR B 2 348 ? 125.172 115.884 66.776  1.00 86.69  ? 348 TYR B OH    1 
ATOM   5912 N N     . GLY B 2 349 ? 125.919 113.946 73.013  1.00 61.07  ? 349 GLY B N     1 
ATOM   5913 C CA    . GLY B 2 349 ? 127.205 113.320 72.790  1.00 61.07  ? 349 GLY B CA    1 
ATOM   5914 C C     . GLY B 2 349 ? 127.180 111.930 73.382  1.00 61.07  ? 349 GLY B C     1 
ATOM   5915 O O     . GLY B 2 349 ? 126.125 111.457 73.816  1.00 61.07  ? 349 GLY B O     1 
ATOM   5916 N N     . MET B 2 350 ? 128.343 111.269 73.419  1.00 65.22  ? 350 MET B N     1 
ATOM   5917 C CA    . MET B 2 350 ? 128.324 109.895 73.884  1.00 65.22  ? 350 MET B CA    1 
ATOM   5918 C C     . MET B 2 350 ? 129.644 109.417 74.459  1.00 65.22  ? 350 MET B C     1 
ATOM   5919 O O     . MET B 2 350 ? 130.713 109.933 74.135  1.00 65.22  ? 350 MET B O     1 
ATOM   5920 C CB    . MET B 2 350 ? 127.909 109.003 72.735  1.00 93.70  ? 350 MET B CB    1 
ATOM   5921 C CG    . MET B 2 350 ? 128.838 109.066 71.574  1.00 93.70  ? 350 MET B CG    1 
ATOM   5922 S SD    . MET B 2 350 ? 128.051 108.482 70.086  1.00 93.70  ? 350 MET B SD    1 
ATOM   5923 C CE    . MET B 2 350 ? 127.003 109.885 69.711  1.00 93.70  ? 350 MET B CE    1 
ATOM   5924 N N     . THR B 2 351 ? 129.546 108.380 75.299  1.00 64.38  ? 351 THR B N     1 
ATOM   5925 C CA    . THR B 2 351 ? 130.699 107.666 75.854  1.00 64.38  ? 351 THR B CA    1 
ATOM   5926 C C     . THR B 2 351 ? 130.642 106.200 75.436  1.00 64.38  ? 351 THR B C     1 
ATOM   5927 O O     . THR B 2 351 ? 129.683 105.500 75.763  1.00 64.38  ? 351 THR B O     1 
ATOM   5928 C CB    . THR B 2 351 ? 130.735 107.755 77.380  1.00 90.13  ? 351 THR B CB    1 
ATOM   5929 O OG1   . THR B 2 351 ? 130.817 109.125 77.783  1.00 90.13  ? 351 THR B OG1   1 
ATOM   5930 C CG2   . THR B 2 351 ? 131.938 107.017 77.913  1.00 90.13  ? 351 THR B CG2   1 
ATOM   5931 N N     . GLY B 2 352 ? 131.701 105.709 74.797  1.00 62.87  ? 352 GLY B N     1 
ATOM   5932 C CA    . GLY B 2 352 ? 131.713 104.357 74.239  1.00 62.87  ? 352 GLY B CA    1 
ATOM   5933 C C     . GLY B 2 352 ? 131.896 103.194 75.201  1.00 62.87  ? 352 GLY B C     1 
ATOM   5934 O O     . GLY B 2 352 ? 132.748 102.323 74.997  1.00 62.87  ? 352 GLY B O     1 
ATOM   5935 N N     . THR B 2 353 ? 131.087 103.167 76.243  1.00 63.25  ? 353 THR B N     1 
ATOM   5936 C CA    . THR B 2 353 ? 131.085 102.111 77.238  1.00 63.25  ? 353 THR B CA    1 
ATOM   5937 C C     . THR B 2 353 ? 129.674 101.619 77.354  1.00 63.25  ? 353 THR B C     1 
ATOM   5938 O O     . THR B 2 353 ? 128.767 102.230 76.807  1.00 63.25  ? 353 THR B O     1 
ATOM   5939 C CB    . THR B 2 353 ? 131.541 102.612 78.604  1.00 88.55  ? 353 THR B CB    1 
ATOM   5940 O OG1   . THR B 2 353 ? 131.694 101.494 79.483  1.00 88.55  ? 353 THR B OG1   1 
ATOM   5941 C CG2   . THR B 2 353 ? 130.491 103.576 79.176  1.00 88.55  ? 353 THR B CG2   1 
ATOM   5942 N N     . ALA B 2 354 ? 129.451 100.557 78.106  1.00 64.58  ? 354 ALA B N     1 
ATOM   5943 C CA    . ALA B 2 354 ? 128.069 100.136 78.199  1.00 64.58  ? 354 ALA B CA    1 
ATOM   5944 C C     . ALA B 2 354 ? 127.842 99.254  79.404  1.00 64.58  ? 354 ALA B C     1 
ATOM   5945 O O     . ALA B 2 354 ? 128.772 98.606  79.877  1.00 64.58  ? 354 ALA B O     1 
ATOM   5946 C CB    . ALA B 2 354 ? 127.658 99.401  76.929  1.00 88.06  ? 354 ALA B CB    1 
ATOM   5947 N N     . PRO B 2 355 ? 126.622 99.240  79.928  1.00 68.16  ? 355 PRO B N     1 
ATOM   5948 C CA    . PRO B 2 355 ? 126.206 98.307  80.969  1.00 68.16  ? 355 PRO B CA    1 
ATOM   5949 C C     . PRO B 2 355 ? 126.013 96.910  80.400  1.00 68.16  ? 355 PRO B C     1 
ATOM   5950 O O     . PRO B 2 355 ? 125.759 96.734  79.209  1.00 68.16  ? 355 PRO B O     1 
ATOM   5951 C CB    . PRO B 2 355 ? 124.873 98.906  81.428  1.00 450.04 ? 355 PRO B CB    1 
ATOM   5952 C CG    . PRO B 2 355 ? 124.365 99.634  80.230  1.00 450.04 ? 355 PRO B CG    1 
ATOM   5953 C CD    . PRO B 2 355 ? 125.566 100.176 79.547  1.00 450.04 ? 355 PRO B CD    1 
ATOM   5954 N N     . GLU B 2 356 ? 126.097 95.912  81.280  1.00 68.05  ? 356 GLU B N     1 
ATOM   5955 C CA    . GLU B 2 356 ? 125.937 94.524  80.868  1.00 68.05  ? 356 GLU B CA    1 
ATOM   5956 C C     . GLU B 2 356 ? 124.613 94.277  80.176  1.00 68.05  ? 356 GLU B C     1 
ATOM   5957 O O     . GLU B 2 356 ? 123.548 94.612  80.697  1.00 68.05  ? 356 GLU B O     1 
ATOM   5958 C CB    . GLU B 2 356 ? 126.039 93.603  82.071  1.00 91.41  ? 356 GLU B CB    1 
ATOM   5959 C CG    . GLU B 2 356 ? 125.829 92.136  81.741  1.00 91.41  ? 356 GLU B CG    1 
ATOM   5960 C CD    . GLU B 2 356 ? 126.881 91.614  80.817  1.00 91.41  ? 356 GLU B CD    1 
ATOM   5961 O OE1   . GLU B 2 356 ? 128.051 91.927  81.021  1.00 91.41  ? 356 GLU B OE1   1 
ATOM   5962 O OE2   . GLU B 2 356 ? 126.536 90.908  79.872  1.00 91.41  ? 356 GLU B OE2   1 
ATOM   5963 N N     . GLY B 2 357 ? 124.695 93.641  79.019  1.00 71.94  ? 357 GLY B N     1 
ATOM   5964 C CA    . GLY B 2 357 ? 123.537 93.265  78.244  1.00 71.94  ? 357 GLY B CA    1 
ATOM   5965 C C     . GLY B 2 357 ? 123.192 94.208  77.113  1.00 71.94  ? 357 GLY B C     1 
ATOM   5966 O O     . GLY B 2 357 ? 122.409 93.840  76.234  1.00 71.94  ? 357 GLY B O     1 
ATOM   5967 N N     . LEU B 2 358 ? 123.757 95.393  77.082  1.00 76.98  ? 358 LEU B N     1 
ATOM   5968 C CA    . LEU B 2 358 ? 123.377 96.328  76.044  1.00 76.98  ? 358 LEU B CA    1 
ATOM   5969 C C     . LEU B 2 358 ? 124.565 96.843  75.251  1.00 76.98  ? 358 LEU B C     1 
ATOM   5970 O O     . LEU B 2 358 ? 125.517 97.383  75.809  1.00 76.98  ? 358 LEU B O     1 
ATOM   5971 C CB    . LEU B 2 358 ? 122.621 97.488  76.677  1.00 113.97 ? 358 LEU B CB    1 
ATOM   5972 C CG    . LEU B 2 358 ? 121.335 97.132  77.444  1.00 113.97 ? 358 LEU B CG    1 
ATOM   5973 C CD1   . LEU B 2 358 ? 120.822 98.356  78.179  1.00 113.97 ? 358 LEU B CD1   1 
ATOM   5974 C CD2   . LEU B 2 358 ? 120.259 96.629  76.480  1.00 113.97 ? 358 LEU B CD2   1 
ATOM   5975 N N     . GLU B 2 359 ? 124.462 96.731  73.947  1.00 76.83  ? 359 GLU B N     1 
ATOM   5976 C CA    . GLU B 2 359 ? 125.452 97.289  73.046  1.00 76.83  ? 359 GLU B CA    1 
ATOM   5977 C C     . GLU B 2 359 ? 125.361 98.805  72.989  1.00 76.83  ? 359 GLU B C     1 
ATOM   5978 O O     . GLU B 2 359 ? 126.377 99.502  72.878  1.00 76.83  ? 359 GLU B O     1 
ATOM   5979 C CB    . GLU B 2 359 ? 125.224 96.701  71.669  1.00 103.20 ? 359 GLU B CB    1 
ATOM   5980 C CG    . GLU B 2 359 ? 125.467 95.217  71.599  1.00 103.20 ? 359 GLU B CG    1 
ATOM   5981 C CD    . GLU B 2 359 ? 124.341 94.409  72.183  1.00 103.20 ? 359 GLU B CD    1 
ATOM   5982 O OE1   . GLU B 2 359 ? 123.302 94.988  72.508  1.00 103.20 ? 359 GLU B OE1   1 
ATOM   5983 O OE2   . GLU B 2 359 ? 124.497 93.199  72.322  1.00 103.20 ? 359 GLU B OE2   1 
ATOM   5984 N N     . ARG B 2 360 ? 124.141 99.320  73.040  1.00 72.07  ? 360 ARG B N     1 
ATOM   5985 C CA    . ARG B 2 360 ? 123.865 100.742 72.966  1.00 72.07  ? 360 ARG B CA    1 
ATOM   5986 C C     . ARG B 2 360 ? 122.633 101.088 73.791  1.00 72.07  ? 360 ARG B C     1 
ATOM   5987 O O     . ARG B 2 360 ? 121.669 100.328 73.837  1.00 72.07  ? 360 ARG B O     1 
ATOM   5988 C CB    . ARG B 2 360 ? 123.678 101.153 71.522  1.00 105.90 ? 360 ARG B CB    1 
ATOM   5989 C CG    . ARG B 2 360 ? 122.622 100.371 70.800  1.00 105.90 ? 360 ARG B CG    1 
ATOM   5990 C CD    . ARG B 2 360 ? 122.772 100.552 69.342  1.00 105.90 ? 360 ARG B CD    1 
ATOM   5991 N NE    . ARG B 2 360 ? 124.047 100.013 68.871  1.00 105.90 ? 360 ARG B NE    1 
ATOM   5992 C CZ    . ARG B 2 360 ? 124.671 100.391 67.756  1.00 105.90 ? 360 ARG B CZ    1 
ATOM   5993 N NH1   . ARG B 2 360 ? 124.187 101.346 66.984  1.00 105.90 ? 360 ARG B NH1   1 
ATOM   5994 N NH2   . ARG B 2 360 ? 125.811 99.797  67.407  1.00 105.90 ? 360 ARG B NH2   1 
ATOM   5995 N N     . SER B 2 361 ? 122.672 102.244 74.434  1.00 64.60  ? 361 SER B N     1 
ATOM   5996 C CA    . SER B 2 361 ? 121.586 102.715 75.285  1.00 64.60  ? 361 SER B CA    1 
ATOM   5997 C C     . SER B 2 361 ? 121.753 104.200 75.529  1.00 64.60  ? 361 SER B C     1 
ATOM   5998 O O     . SER B 2 361 ? 122.752 104.793 75.129  1.00 64.60  ? 361 SER B O     1 
ATOM   5999 C CB    . SER B 2 361 ? 121.588 102.002 76.614  1.00 87.01  ? 361 SER B CB    1 
ATOM   6000 O OG    . SER B 2 361 ? 122.717 102.388 77.374  1.00 87.01  ? 361 SER B OG    1 
ATOM   6001 N N     . GLY B 2 362 ? 120.784 104.805 76.213  1.00 55.13  ? 362 GLY B N     1 
ATOM   6002 C CA    . GLY B 2 362 ? 120.950 106.220 76.531  1.00 55.13  ? 362 GLY B CA    1 
ATOM   6003 C C     . GLY B 2 362 ? 119.883 106.808 77.443  1.00 55.13  ? 362 GLY B C     1 
ATOM   6004 O O     . GLY B 2 362 ? 118.945 106.126 77.872  1.00 55.13  ? 362 GLY B O     1 
ATOM   6005 N N     . SER B 2 363 ? 120.048 108.100 77.733  1.00 53.46  ? 363 SER B N     1 
ATOM   6006 C CA    . SER B 2 363 ? 119.157 108.808 78.633  1.00 53.46  ? 363 SER B CA    1 
ATOM   6007 C C     . SER B 2 363 ? 119.173 110.287 78.348  1.00 53.46  ? 363 SER B C     1 
ATOM   6008 O O     . SER B 2 363 ? 120.041 110.797 77.639  1.00 53.46  ? 363 SER B O     1 
ATOM   6009 C CB    . SER B 2 363 ? 119.538 108.593 80.084  1.00 72.01  ? 363 SER B CB    1 
ATOM   6010 O OG    . SER B 2 363 ? 120.806 109.127 80.359  1.00 72.01  ? 363 SER B OG    1 
ATOM   6011 N N     . ALA B 2 364 ? 118.210 110.985 78.934  1.00 55.80  ? 364 ALA B N     1 
ATOM   6012 C CA    . ALA B 2 364 ? 118.208 112.422 78.768  1.00 55.80  ? 364 ALA B CA    1 
ATOM   6013 C C     . ALA B 2 364 ? 117.701 113.132 80.009  1.00 55.80  ? 364 ALA B C     1 
ATOM   6014 O O     . ALA B 2 364 ? 116.832 112.639 80.734  1.00 55.80  ? 364 ALA B O     1 
ATOM   6015 C CB    . ALA B 2 364 ? 117.375 112.831 77.566  1.00 76.09  ? 364 ALA B CB    1 
ATOM   6016 N N     . LEU B 2 365 ? 118.262 114.310 80.234  1.00 52.17  ? 365 LEU B N     1 
ATOM   6017 C CA    . LEU B 2 365 ? 117.807 115.206 81.271  1.00 52.17  ? 365 LEU B CA    1 
ATOM   6018 C C     . LEU B 2 365 ? 117.115 116.370 80.600  1.00 52.17  ? 365 LEU B C     1 
ATOM   6019 O O     . LEU B 2 365 ? 117.732 117.122 79.842  1.00 52.17  ? 365 LEU B O     1 
ATOM   6020 C CB    . LEU B 2 365 ? 118.968 115.668 82.137  1.00 77.24  ? 365 LEU B CB    1 
ATOM   6021 C CG    . LEU B 2 365 ? 119.692 114.581 82.941  1.00 77.24  ? 365 LEU B CG    1 
ATOM   6022 C CD1   . LEU B 2 365 ? 120.887 115.187 83.632  1.00 77.24  ? 365 LEU B CD1   1 
ATOM   6023 C CD2   . LEU B 2 365 ? 118.755 113.968 83.981  1.00 77.24  ? 365 LEU B CD2   1 
ATOM   6024 N N     . ILE B 2 366 ? 115.839 116.516 80.862  1.00 57.15  ? 366 ILE B N     1 
ATOM   6025 C CA    . ILE B 2 366 ? 115.064 117.525 80.183  1.00 57.15  ? 366 ILE B CA    1 
ATOM   6026 C C     . ILE B 2 366 ? 114.483 118.535 81.167  1.00 57.15  ? 366 ILE B C     1 
ATOM   6027 O O     . ILE B 2 366 ? 113.812 118.177 82.138  1.00 57.15  ? 366 ILE B O     1 
ATOM   6028 C CB    . ILE B 2 366 ? 113.962 116.890 79.341  1.00 84.61  ? 366 ILE B CB    1 
ATOM   6029 C CG1   . ILE B 2 366 ? 114.589 115.982 78.290  1.00 84.61  ? 366 ILE B CG1   1 
ATOM   6030 C CG2   . ILE B 2 366 ? 113.151 117.973 78.717  1.00 84.61  ? 366 ILE B CG2   1 
ATOM   6031 C CD1   . ILE B 2 366 ? 113.609 115.100 77.527  1.00 84.61  ? 366 ILE B CD1   1 
ATOM   6032 N N     . ASN B 2 367 ? 114.727 119.796 80.904  1.00 55.23  ? 367 ASN B N     1 
ATOM   6033 C CA    . ASN B 2 367 ? 114.182 120.874 81.706  1.00 55.23  ? 367 ASN B CA    1 
ATOM   6034 C C     . ASN B 2 367 ? 113.152 121.552 80.838  1.00 55.23  ? 367 ASN B C     1 
ATOM   6035 O O     . ASN B 2 367 ? 113.515 122.236 79.881  1.00 55.23  ? 367 ASN B O     1 
ATOM   6036 C CB    . ASN B 2 367 ? 115.262 121.863 82.095  1.00 74.83  ? 367 ASN B CB    1 
ATOM   6037 C CG    . ASN B 2 367 ? 114.794 122.830 83.130  1.00 74.83  ? 367 ASN B CG    1 
ATOM   6038 O OD1   . ASN B 2 367 ? 113.593 123.003 83.313  1.00 74.83  ? 367 ASN B OD1   1 
ATOM   6039 N ND2   . ASN B 2 367 ? 115.730 123.463 83.836  1.00 74.83  ? 367 ASN B ND2   1 
ATOM   6040 N N     . HIS B 2 368 ? 111.879 121.352 81.112  1.00 61.58  ? 368 HIS B N     1 
ATOM   6041 C CA    . HIS B 2 368 ? 110.935 122.032 80.256  1.00 61.58  ? 368 HIS B CA    1 
ATOM   6042 C C     . HIS B 2 368 ? 109.716 122.412 81.051  1.00 61.58  ? 368 HIS B C     1 
ATOM   6043 O O     . HIS B 2 368 ? 109.505 121.934 82.164  1.00 61.58  ? 368 HIS B O     1 
ATOM   6044 C CB    . HIS B 2 368 ? 110.572 121.224 79.038  1.00 83.75  ? 368 HIS B CB    1 
ATOM   6045 C CG    . HIS B 2 368 ? 109.583 120.190 79.259  1.00 83.75  ? 368 HIS B CG    1 
ATOM   6046 N ND1   . HIS B 2 368 ? 108.262 120.381 78.966  1.00 83.75  ? 368 HIS B ND1   1 
ATOM   6047 C CD2   . HIS B 2 368 ? 109.708 118.912 79.671  1.00 83.75  ? 368 HIS B CD2   1 
ATOM   6048 C CE1   . HIS B 2 368 ? 107.604 119.259 79.194  1.00 83.75  ? 368 HIS B CE1   1 
ATOM   6049 N NE2   . HIS B 2 368 ? 108.458 118.355 79.632  1.00 83.75  ? 368 HIS B NE2   1 
ATOM   6050 N N     . THR B 2 369 ? 108.913 123.290 80.459  1.00 62.58  ? 369 THR B N     1 
ATOM   6051 C CA    . THR B 2 369 ? 107.810 123.933 81.156  1.00 62.58  ? 369 THR B CA    1 
ATOM   6052 C C     . THR B 2 369 ? 106.746 122.966 81.638  1.00 62.58  ? 369 THR B C     1 
ATOM   6053 O O     . THR B 2 369 ? 106.024 123.289 82.587  1.00 62.58  ? 369 THR B O     1 
ATOM   6054 C CB    . THR B 2 369 ? 107.147 124.968 80.250  1.00 87.61  ? 369 THR B CB    1 
ATOM   6055 O OG1   . THR B 2 369 ? 106.688 124.329 79.045  1.00 87.61  ? 369 THR B OG1   1 
ATOM   6056 C CG2   . THR B 2 369 ? 108.133 126.075 79.910  1.00 87.61  ? 369 THR B CG2   1 
ATOM   6057 N N     . GLY B 2 370 ? 106.643 121.786 81.045  1.00 60.64  ? 370 GLY B N     1 
ATOM   6058 C CA    . GLY B 2 370 ? 105.616 120.864 81.478  1.00 60.64  ? 370 GLY B CA    1 
ATOM   6059 C C     . GLY B 2 370 ? 105.837 120.312 82.865  1.00 60.64  ? 370 GLY B C     1 
ATOM   6060 O O     . GLY B 2 370 ? 104.946 119.649 83.401  1.00 60.64  ? 370 GLY B O     1 
ATOM   6061 N N     . VAL B 2 371 ? 106.983 120.594 83.479  1.00 63.94  ? 371 VAL B N     1 
ATOM   6062 C CA    . VAL B 2 371 ? 107.209 120.140 84.838  1.00 63.94  ? 371 VAL B CA    1 
ATOM   6063 C C     . VAL B 2 371 ? 106.200 120.781 85.745  1.00 63.94  ? 371 VAL B C     1 
ATOM   6064 O O     . VAL B 2 371 ? 105.896 120.260 86.821  1.00 63.94  ? 371 VAL B O     1 
ATOM   6065 C CB    . VAL B 2 371 ? 108.634 120.454 85.302  1.00 93.00  ? 371 VAL B CB    1 
ATOM   6066 C CG1   . VAL B 2 371 ? 108.770 121.860 85.583  1.00 93.00  ? 371 VAL B CG1   1 
ATOM   6067 C CG2   . VAL B 2 371 ? 108.987 119.667 86.518  1.00 93.00  ? 371 VAL B CG2   1 
ATOM   6068 N N     . ALA B 2 372 ? 105.645 121.901 85.305  1.00 66.57  ? 372 ALA B N     1 
ATOM   6069 C CA    . ALA B 2 372 ? 104.647 122.615 86.066  1.00 66.57  ? 372 ALA B CA    1 
ATOM   6070 C C     . ALA B 2 372 ? 103.468 121.737 86.366  1.00 66.57  ? 372 ALA B C     1 
ATOM   6071 O O     . ALA B 2 372 ? 102.852 121.880 87.422  1.00 66.57  ? 372 ALA B O     1 
ATOM   6072 C CB    . ALA B 2 372 ? 104.194 123.848 85.298  1.00 90.78  ? 372 ALA B CB    1 
ATOM   6073 N N     . GLU B 2 373 ? 103.154 120.817 85.479  1.00 70.48  ? 373 GLU B N     1 
ATOM   6074 C CA    . GLU B 2 373 ? 101.986 120.004 85.693  1.00 70.48  ? 373 GLU B CA    1 
ATOM   6075 C C     . GLU B 2 373 ? 102.179 119.051 86.838  1.00 70.48  ? 373 GLU B C     1 
ATOM   6076 O O     . GLU B 2 373 ? 101.209 118.652 87.483  1.00 70.48  ? 373 GLU B O     1 
ATOM   6077 C CB    . GLU B 2 373 ? 101.644 119.253 84.436  1.00 94.67  ? 373 GLU B CB    1 
ATOM   6078 C CG    . GLU B 2 373 ? 101.294 120.162 83.299  1.00 94.67  ? 373 GLU B CG    1 
ATOM   6079 C CD    . GLU B 2 373 ? 100.196 121.144 83.633  1.00 94.67  ? 373 GLU B CD    1 
ATOM   6080 O OE1   . GLU B 2 373 ? 99.354  120.862 84.493  1.00 94.67  ? 373 GLU B OE1   1 
ATOM   6081 O OE2   . GLU B 2 373 ? 100.178 122.219 83.032  1.00 94.67  ? 373 GLU B OE2   1 
ATOM   6082 N N     . ILE B 2 374 ? 103.394 118.640 87.085  1.00 69.39  ? 374 ILE B N     1 
ATOM   6083 C CA    . ILE B 2 374 ? 103.618 117.778 88.210  1.00 69.39  ? 374 ILE B CA    1 
ATOM   6084 C C     . ILE B 2 374 ? 103.305 118.540 89.456  1.00 69.39  ? 374 ILE B C     1 
ATOM   6085 O O     . ILE B 2 374 ? 102.604 118.066 90.367  1.00 69.39  ? 374 ILE B O     1 
ATOM   6086 C CB    . ILE B 2 374 ? 105.072 117.311 88.214  1.00 102.73 ? 374 ILE B CB    1 
ATOM   6087 C CG1   . ILE B 2 374 ? 105.317 116.430 86.995  1.00 102.73 ? 374 ILE B CG1   1 
ATOM   6088 C CG2   . ILE B 2 374 ? 105.398 116.635 89.508  1.00 102.73 ? 374 ILE B CG2   1 
ATOM   6089 C CD1   . ILE B 2 374 ? 106.764 116.153 86.707  1.00 102.73 ? 374 ILE B CD1   1 
ATOM   6090 N N     . PHE B 2 375 ? 103.819 119.749 89.505  1.00 71.07  ? 375 PHE B N     1 
ATOM   6091 C CA    . PHE B 2 375 ? 103.589 120.562 90.660  1.00 71.07  ? 375 PHE B CA    1 
ATOM   6092 C C     . PHE B 2 375 ? 102.126 120.868 90.804  1.00 71.07  ? 375 PHE B C     1 
ATOM   6093 O O     . PHE B 2 375 ? 101.614 120.909 91.919  1.00 71.07  ? 375 PHE B O     1 
ATOM   6094 C CB    . PHE B 2 375 ? 104.356 121.831 90.539  1.00 99.17  ? 375 PHE B CB    1 
ATOM   6095 C CG    . PHE B 2 375 ? 105.767 121.648 90.647  1.00 99.17  ? 375 PHE B CG    1 
ATOM   6096 C CD1   . PHE B 2 375 ? 106.320 121.373 91.846  1.00 99.17  ? 375 PHE B CD1   1 
ATOM   6097 C CD2   . PHE B 2 375 ? 106.567 121.776 89.548  1.00 99.17  ? 375 PHE B CD2   1 
ATOM   6098 C CE1   . PHE B 2 375 ? 107.663 121.223 91.961  1.00 99.17  ? 375 PHE B CE1   1 
ATOM   6099 C CE2   . PHE B 2 375 ? 107.911 121.619 89.647  1.00 99.17  ? 375 PHE B CE2   1 
ATOM   6100 C CZ    . PHE B 2 375 ? 108.463 121.341 90.859  1.00 99.17  ? 375 PHE B CZ    1 
ATOM   6101 N N     . ASN B 2 376 ? 101.436 121.083 89.698  1.00 75.46  ? 376 ASN B N     1 
ATOM   6102 C CA    . ASN B 2 376 ? 100.036 121.428 89.793  1.00 75.46  ? 376 ASN B CA    1 
ATOM   6103 C C     . ASN B 2 376 ? 99.240  120.309 90.423  1.00 75.46  ? 376 ASN B C     1 
ATOM   6104 O O     . ASN B 2 376 ? 98.340  120.560 91.228  1.00 75.46  ? 376 ASN B O     1 
ATOM   6105 C CB    . ASN B 2 376 ? 99.471  121.749 88.432  1.00 102.24 ? 376 ASN B CB    1 
ATOM   6106 C CG    . ASN B 2 376 ? 100.000 123.012 87.883  1.00 102.24 ? 376 ASN B CG    1 
ATOM   6107 O OD1   . ASN B 2 376 ? 100.476 123.891 88.610  1.00 102.24 ? 376 ASN B OD1   1 
ATOM   6108 N ND2   . ASN B 2 376 ? 99.926  123.134 86.574  1.00 102.24 ? 376 ASN B ND2   1 
ATOM   6109 N N     . ARG B 2 377 ? 99.552  119.070 90.087  1.00 77.56  ? 377 ARG B N     1 
ATOM   6110 C CA    . ARG B 2 377 ? 98.820  117.974 90.693  1.00 77.56  ? 377 ARG B CA    1 
ATOM   6111 C C     . ARG B 2 377 ? 99.043  117.936 92.180  1.00 77.56  ? 377 ARG B C     1 
ATOM   6112 O O     . ARG B 2 377 ? 98.090  117.790 92.962  1.00 77.56  ? 377 ARG B O     1 
ATOM   6113 C CB    . ARG B 2 377 ? 99.248  116.643 90.096  1.00 113.96 ? 377 ARG B CB    1 
ATOM   6114 C CG    . ARG B 2 377 ? 98.541  115.454 90.734  1.00 113.96 ? 377 ARG B CG    1 
ATOM   6115 C CD    . ARG B 2 377 ? 98.866  114.099 90.093  1.00 113.96 ? 377 ARG B CD    1 
ATOM   6116 N NE    . ARG B 2 377 ? 100.269 113.660 90.195  1.00 113.96 ? 377 ARG B NE    1 
ATOM   6117 C CZ    . ARG B 2 377 ? 100.850 113.158 91.288  1.00 113.96 ? 377 ARG B CZ    1 
ATOM   6118 N NH1   . ARG B 2 377 ? 100.215 113.096 92.446  1.00 113.96 ? 377 ARG B NH1   1 
ATOM   6119 N NH2   . ARG B 2 377 ? 102.099 112.711 91.220  1.00 113.96 ? 377 ARG B NH2   1 
ATOM   6120 N N     . ILE B 2 378 ? 100.286 118.090 92.598  1.00 80.73  ? 378 ILE B N     1 
ATOM   6121 C CA    . ILE B 2 378 ? 100.564 118.013 94.015  1.00 80.73  ? 378 ILE B CA    1 
ATOM   6122 C C     . ILE B 2 378 ? 99.923  119.146 94.763  1.00 80.73  ? 378 ILE B C     1 
ATOM   6123 O O     . ILE B 2 378 ? 99.331  118.943 95.829  1.00 80.73  ? 378 ILE B O     1 
ATOM   6124 C CB    . ILE B 2 378 ? 102.056 118.005 94.271  1.00 119.52 ? 378 ILE B CB    1 
ATOM   6125 C CG1   . ILE B 2 378 ? 102.600 116.717 93.723  1.00 119.52 ? 378 ILE B CG1   1 
ATOM   6126 C CG2   . ILE B 2 378 ? 102.344 118.156 95.768  1.00 119.52 ? 378 ILE B CG2   1 
ATOM   6127 C CD1   . ILE B 2 378 ? 104.088 116.685 93.583  1.00 119.52 ? 378 ILE B CD1   1 
ATOM   6128 N N     . LEU B 2 379 ? 100.042 120.349 94.247  1.00 80.50  ? 379 LEU B N     1 
ATOM   6129 C CA    . LEU B 2 379 ? 99.439  121.467 94.918  1.00 80.50  ? 379 LEU B CA    1 
ATOM   6130 C C     . LEU B 2 379 ? 97.954  121.308 95.011  1.00 80.50  ? 379 LEU B C     1 
ATOM   6131 O O     . LEU B 2 379 ? 97.376  121.598 96.045  1.00 80.50  ? 379 LEU B O     1 
ATOM   6132 C CB    . LEU B 2 379 ? 99.739  122.758 94.207  1.00 119.18 ? 379 LEU B CB    1 
ATOM   6133 C CG    . LEU B 2 379 ? 101.152 123.284 94.329  1.00 119.18 ? 379 LEU B CG    1 
ATOM   6134 C CD1   . LEU B 2 379 ? 101.322 124.407 93.325  1.00 119.18 ? 379 LEU B CD1   1 
ATOM   6135 C CD2   . LEU B 2 379 ? 101.397 123.803 95.750  1.00 119.18 ? 379 LEU B CD2   1 
ATOM   6136 N N     . ALA B 2 380 ? 97.297  120.869 93.965  1.00 86.30  ? 380 ALA B N     1 
ATOM   6137 C CA    . ALA B 2 380 ? 95.864  120.755 94.103  1.00 86.30  ? 380 ALA B CA    1 
ATOM   6138 C C     . ALA B 2 380 ? 95.492  119.866 95.281  1.00 86.30  ? 380 ALA B C     1 
ATOM   6139 O O     . ALA B 2 380 ? 94.591  120.205 96.072  1.00 86.30  ? 380 ALA B O     1 
ATOM   6140 C CB    . ALA B 2 380 ? 95.267  120.214 92.826  1.00 117.68 ? 380 ALA B CB    1 
ATOM   6141 N N     . GLN B 2 381 ? 96.190  118.747 95.446  1.00 90.29  ? 381 GLN B N     1 
ATOM   6142 C CA    . GLN B 2 381 ? 95.803  117.897 96.561  1.00 90.29  ? 381 GLN B CA    1 
ATOM   6143 C C     . GLN B 2 381 ? 96.074  118.607 97.857  1.00 90.29  ? 381 GLN B C     1 
ATOM   6144 O O     . GLN B 2 381 ? 95.274  118.541 98.807  1.00 90.29  ? 381 GLN B O     1 
ATOM   6145 C CB    . GLN B 2 381 ? 96.530  116.549 96.526  1.00 126.16 ? 381 GLN B CB    1 
ATOM   6146 C CG    . GLN B 2 381 ? 96.098  115.669 95.400  1.00 126.16 ? 381 GLN B CG    1 
ATOM   6147 C CD    . GLN B 2 381 ? 96.724  114.350 95.463  1.00 126.16 ? 381 GLN B CD    1 
ATOM   6148 O OE1   . GLN B 2 381 ? 97.720  114.164 96.130  1.00 126.16 ? 381 GLN B OE1   1 
ATOM   6149 N NE2   . GLN B 2 381 ? 96.145  113.401 94.772  1.00 126.16 ? 381 GLN B NE2   1 
ATOM   6150 N N     . PHE B 2 382 ? 97.181  119.310 97.904  1.00 89.55  ? 382 PHE B N     1 
ATOM   6151 C CA    . PHE B 2 382 ? 97.527  119.997 99.121  1.00 89.55  ? 382 PHE B CA    1 
ATOM   6152 C C     . PHE B 2 382 ? 96.522  121.048 99.470  1.00 89.55  ? 382 PHE B C     1 
ATOM   6153 O O     . PHE B 2 382 ? 96.123  121.182 100.626 1.00 89.55  ? 382 PHE B O     1 
ATOM   6154 C CB    . PHE B 2 382 ? 98.860  120.663 99.038  1.00 124.95 ? 382 PHE B CB    1 
ATOM   6155 C CG    . PHE B 2 382 ? 99.022  121.548 100.132 1.00 124.95 ? 382 PHE B CG    1 
ATOM   6156 C CD1   . PHE B 2 382 ? 99.235  121.048 101.367 1.00 124.95 ? 382 PHE B CD1   1 
ATOM   6157 C CD2   . PHE B 2 382 ? 98.881  122.874 99.967  1.00 124.95 ? 382 PHE B CD2   1 
ATOM   6158 C CE1   . PHE B 2 382 ? 99.333  121.871 102.413 1.00 124.95 ? 382 PHE B CE1   1 
ATOM   6159 C CE2   . PHE B 2 382 ? 98.991  123.712 101.009 1.00 124.95 ? 382 PHE B CE2   1 
ATOM   6160 C CZ    . PHE B 2 382 ? 99.219  123.212 102.242 1.00 124.95 ? 382 PHE B CZ    1 
ATOM   6161 N N     . ASN B 2 383 ? 96.151  121.846 98.508  1.00 92.19  ? 383 ASN B N     1 
ATOM   6162 C CA    . ASN B 2 383 ? 95.248  122.930 98.787  1.00 92.19  ? 383 ASN B CA    1 
ATOM   6163 C C     . ASN B 2 383 ? 93.974  122.413 99.409  1.00 92.19  ? 383 ASN B C     1 
ATOM   6164 O O     . ASN B 2 383 ? 93.481  122.981 100.390 1.00 92.19  ? 383 ASN B O     1 
ATOM   6165 C CB    . ASN B 2 383 ? 94.950  123.656 97.515  1.00 124.90 ? 383 ASN B CB    1 
ATOM   6166 C CG    . ASN B 2 383 ? 96.130  124.389 97.012  1.00 124.90 ? 383 ASN B CG    1 
ATOM   6167 O OD1   . ASN B 2 383 ? 97.044  124.742 97.754  1.00 124.90 ? 383 ASN B OD1   1 
ATOM   6168 N ND2   . ASN B 2 383 ? 96.133  124.633 95.727  1.00 124.90 ? 383 ASN B ND2   1 
ATOM   6169 N N     . LEU B 2 384 ? 93.461  121.297 98.908  1.00 92.64  ? 384 LEU B N     1 
ATOM   6170 C CA    . LEU B 2 384 ? 92.256  120.758 99.526  1.00 92.64  ? 384 LEU B CA    1 
ATOM   6171 C C     . LEU B 2 384 ? 92.500  120.316 100.968 1.00 92.64  ? 384 LEU B C     1 
ATOM   6172 O O     . LEU B 2 384 ? 91.731  120.665 101.869 1.00 92.64  ? 384 LEU B O     1 
ATOM   6173 C CB    . LEU B 2 384 ? 91.743  119.614 98.686  1.00 137.15 ? 384 LEU B CB    1 
ATOM   6174 C CG    . LEU B 2 384 ? 90.519  118.869 99.149  1.00 137.15 ? 384 LEU B CG    1 
ATOM   6175 C CD1   . LEU B 2 384 ? 89.328  119.783 99.245  1.00 137.15 ? 384 LEU B CD1   1 
ATOM   6176 C CD2   . LEU B 2 384 ? 90.258  117.732 98.163  1.00 137.15 ? 384 LEU B CD2   1 
ATOM   6177 N N     . MET B 2 385 ? 93.590  119.587 101.211 1.00 96.07  ? 385 MET B N     1 
ATOM   6178 C CA    . MET B 2 385 ? 93.911  119.119 102.559 1.00 96.07  ? 385 MET B CA    1 
ATOM   6179 C C     . MET B 2 385 ? 93.969  120.250 103.537 1.00 96.07  ? 385 MET B C     1 
ATOM   6180 O O     . MET B 2 385 ? 93.374  120.216 104.616 1.00 96.07  ? 385 MET B O     1 
ATOM   6181 C CB    . MET B 2 385 ? 95.278  118.443 102.583 1.00 138.02 ? 385 MET B CB    1 
ATOM   6182 C CG    . MET B 2 385 ? 95.856  118.209 103.980 1.00 138.02 ? 385 MET B CG    1 
ATOM   6183 S SD    . MET B 2 385 ? 97.490  117.489 103.945 1.00 138.02 ? 385 MET B SD    1 
ATOM   6184 C CE    . MET B 2 385 ? 98.095  117.954 105.543 1.00 138.02 ? 385 MET B CE    1 
ATOM   6185 N N     . PHE B 2 386 ? 94.735  121.244 103.186 1.00 95.28  ? 386 PHE B N     1 
ATOM   6186 C CA    . PHE B 2 386 ? 94.981  122.320 104.101 1.00 95.28  ? 386 PHE B CA    1 
ATOM   6187 C C     . PHE B 2 386 ? 93.764  123.155 104.334 1.00 95.28  ? 386 PHE B C     1 
ATOM   6188 O O     . PHE B 2 386 ? 93.426  123.448 105.478 1.00 95.28  ? 386 PHE B O     1 
ATOM   6189 C CB    . PHE B 2 386 ? 96.055  123.199 103.591 1.00 132.95 ? 386 PHE B CB    1 
ATOM   6190 C CG    . PHE B 2 386 ? 96.290  124.298 104.454 1.00 132.95 ? 386 PHE B CG    1 
ATOM   6191 C CD1   . PHE B 2 386 ? 96.925  124.093 105.622 1.00 132.95 ? 386 PHE B CD1   1 
ATOM   6192 C CD2   . PHE B 2 386 ? 95.881  125.535 104.133 1.00 132.95 ? 386 PHE B CD2   1 
ATOM   6193 C CE1   . PHE B 2 386 ? 97.177  125.113 106.474 1.00 132.95 ? 386 PHE B CE1   1 
ATOM   6194 C CE2   . PHE B 2 386 ? 96.130  126.570 104.983 1.00 132.95 ? 386 PHE B CE2   1 
ATOM   6195 C CZ    . PHE B 2 386 ? 96.779  126.353 106.160 1.00 132.95 ? 386 PHE B CZ    1 
ATOM   6196 N N     . ASP B 2 387 ? 93.085  123.543 103.285 1.00 95.99  ? 387 ASP B N     1 
ATOM   6197 C CA    . ASP B 2 387 ? 92.012  124.480 103.496 1.00 95.99  ? 387 ASP B CA    1 
ATOM   6198 C C     . ASP B 2 387 ? 90.948  123.934 104.431 1.00 95.99  ? 387 ASP B C     1 
ATOM   6199 O O     . ASP B 2 387 ? 90.378  124.700 105.200 1.00 95.99  ? 387 ASP B O     1 
ATOM   6200 C CB    . ASP B 2 387 ? 91.463  124.920 102.160 1.00 123.42 ? 387 ASP B CB    1 
ATOM   6201 C CG    . ASP B 2 387 ? 92.425  125.891 101.450 1.00 123.42 ? 387 ASP B CG    1 
ATOM   6202 O OD1   . ASP B 2 387 ? 93.338  126.405 102.110 1.00 123.42 ? 387 ASP B OD1   1 
ATOM   6203 O OD2   . ASP B 2 387 ? 92.285  126.145 100.250 1.00 123.42 ? 387 ASP B OD2   1 
ATOM   6204 N N     . LYS B 2 388 ? 90.683  122.637 104.446 1.00 95.25  ? 388 LYS B N     1 
ATOM   6205 C CA    . LYS B 2 388 ? 89.682  122.169 105.391 1.00 95.25  ? 388 LYS B CA    1 
ATOM   6206 C C     . LYS B 2 388 ? 90.290  121.583 106.630 1.00 95.25  ? 388 LYS B C     1 
ATOM   6207 O O     . LYS B 2 388 ? 89.581  121.007 107.445 1.00 95.25  ? 388 LYS B O     1 
ATOM   6208 C CB    . LYS B 2 388 ? 88.710  121.185 104.755 1.00 142.87 ? 388 LYS B CB    1 
ATOM   6209 C CG    . LYS B 2 388 ? 87.845  121.858 103.673 1.00 142.87 ? 388 LYS B CG    1 
ATOM   6210 C CD    . LYS B 2 388 ? 86.645  121.050 103.277 1.00 142.87 ? 388 LYS B CD    1 
ATOM   6211 C CE    . LYS B 2 388 ? 85.539  121.218 104.285 1.00 142.87 ? 388 LYS B CE    1 
ATOM   6212 N NZ    . LYS B 2 388 ? 84.308  120.444 103.932 1.00 142.87 ? 388 LYS B NZ    1 
ATOM   6213 N N     . GLY B 2 389 ? 91.582  121.722 106.787 1.00 98.25  ? 389 GLY B N     1 
ATOM   6214 C CA    . GLY B 2 389 ? 92.303  121.325 107.974 1.00 98.25  ? 389 GLY B CA    1 
ATOM   6215 C C     . GLY B 2 389 ? 92.566  119.856 108.180 1.00 98.25  ? 389 GLY B C     1 
ATOM   6216 O O     . GLY B 2 389 ? 92.831  119.431 109.306 1.00 98.25  ? 389 GLY B O     1 
ATOM   6217 N N     . ALA B 2 390 ? 92.501  119.044 107.156 1.00 101.05 ? 390 ALA B N     1 
ATOM   6218 C CA    . ALA B 2 390 ? 92.677  117.637 107.434 1.00 101.05 ? 390 ALA B CA    1 
ATOM   6219 C C     . ALA B 2 390 ? 94.102  117.347 107.856 1.00 101.05 ? 390 ALA B C     1 
ATOM   6220 O O     . ALA B 2 390 ? 95.044  117.867 107.284 1.00 101.05 ? 390 ALA B O     1 
ATOM   6221 C CB    . ALA B 2 390 ? 92.295  116.823 106.217 1.00 137.80 ? 390 ALA B CB    1 
ATOM   6222 N N     . PHE B 2 391 ? 94.253  116.521 108.853 1.00 103.76 ? 391 PHE B N     1 
ATOM   6223 C CA    . PHE B 2 391 ? 95.525  116.023 109.304 1.00 103.76 ? 391 PHE B CA    1 
ATOM   6224 C C     . PHE B 2 391 ? 96.434  117.099 109.785 1.00 103.76 ? 391 PHE B C     1 
ATOM   6225 O O     . PHE B 2 391 ? 97.603  116.831 110.027 1.00 103.76 ? 391 PHE B O     1 
ATOM   6226 C CB    . PHE B 2 391 ? 96.223  115.228 108.226 1.00 144.78 ? 391 PHE B CB    1 
ATOM   6227 C CG    . PHE B 2 391 ? 95.406  114.129 107.663 1.00 144.78 ? 391 PHE B CG    1 
ATOM   6228 C CD1   . PHE B 2 391 ? 95.331  112.922 108.275 1.00 144.78 ? 391 PHE B CD1   1 
ATOM   6229 C CD2   . PHE B 2 391 ? 94.744  114.295 106.479 1.00 144.78 ? 391 PHE B CD2   1 
ATOM   6230 C CE1   . PHE B 2 391 ? 94.581  111.928 107.742 1.00 144.78 ? 391 PHE B CE1   1 
ATOM   6231 C CE2   . PHE B 2 391 ? 93.988  113.301 105.949 1.00 144.78 ? 391 PHE B CE2   1 
ATOM   6232 C CZ    . PHE B 2 391 ? 93.901  112.134 106.574 1.00 144.78 ? 391 PHE B CZ    1 
ATOM   6233 N N     . LEU B 2 392 ? 95.946  118.300 110.017 1.00 103.74 ? 392 LEU B N     1 
ATOM   6234 C CA    . LEU B 2 392 ? 96.867  119.322 110.465 1.00 103.74 ? 392 LEU B CA    1 
ATOM   6235 C C     . LEU B 2 392 ? 97.482  118.961 111.778 1.00 103.74 ? 392 LEU B C     1 
ATOM   6236 O O     . LEU B 2 392 ? 98.637  119.287 112.030 1.00 103.74 ? 392 LEU B O     1 
ATOM   6237 C CB    . LEU B 2 392 ? 96.201  120.647 110.660 1.00 153.59 ? 392 LEU B CB    1 
ATOM   6238 C CG    . LEU B 2 392 ? 95.613  121.329 109.478 1.00 153.59 ? 392 LEU B CG    1 
ATOM   6239 C CD1   . LEU B 2 392 ? 94.998  122.616 109.984 1.00 153.59 ? 392 LEU B CD1   1 
ATOM   6240 C CD2   . LEU B 2 392 ? 96.634  121.603 108.429 1.00 153.59 ? 392 LEU B CD2   1 
ATOM   6241 N N     . ASN B 2 393 ? 96.733  118.279 112.626 1.00 106.43 ? 393 ASN B N     1 
ATOM   6242 C CA    . ASN B 2 393 ? 97.228  118.009 113.963 1.00 106.43 ? 393 ASN B CA    1 
ATOM   6243 C C     . ASN B 2 393 ? 98.465  117.162 113.941 1.00 106.43 ? 393 ASN B C     1 
ATOM   6244 O O     . ASN B 2 393 ? 99.314  117.303 114.804 1.00 106.43 ? 393 ASN B O     1 
ATOM   6245 C CB    . ASN B 2 393 ? 96.179  117.316 114.782 1.00 144.20 ? 393 ASN B CB    1 
ATOM   6246 C CG    . ASN B 2 393 ? 95.850  116.006 114.230 1.00 144.20 ? 393 ASN B CG    1 
ATOM   6247 O OD1   . ASN B 2 393 ? 95.499  115.892 113.057 1.00 144.20 ? 393 ASN B OD1   1 
ATOM   6248 N ND2   . ASN B 2 393 ? 95.970  114.987 115.041 1.00 144.20 ? 393 ASN B ND2   1 
ATOM   6249 N N     . TRP B 2 394 ? 98.645  116.348 112.934 1.00 105.81 ? 394 TRP B N     1 
ATOM   6250 C CA    . TRP B 2 394 ? 99.817  115.506 112.988 1.00 105.81 ? 394 TRP B CA    1 
ATOM   6251 C C     . TRP B 2 394 ? 101.068 116.303 112.728 1.00 105.81 ? 394 TRP B C     1 
ATOM   6252 O O     . TRP B 2 394 ? 102.182 115.776 112.845 1.00 105.81 ? 394 TRP B O     1 
ATOM   6253 C CB    . TRP B 2 394 ? 99.683  114.357 111.996 1.00 146.51 ? 394 TRP B CB    1 
ATOM   6254 C CG    . TRP B 2 394 ? 98.520  113.500 112.334 1.00 146.51 ? 394 TRP B CG    1 
ATOM   6255 C CD1   . TRP B 2 394 ? 97.393  113.356 111.609 1.00 146.51 ? 394 TRP B CD1   1 
ATOM   6256 C CD2   . TRP B 2 394 ? 98.337  112.712 113.515 1.00 146.51 ? 394 TRP B CD2   1 
ATOM   6257 N NE1   . TRP B 2 394 ? 96.529  112.518 112.249 1.00 146.51 ? 394 TRP B NE1   1 
ATOM   6258 C CE2   . TRP B 2 394 ? 97.092  112.112 113.420 1.00 146.51 ? 394 TRP B CE2   1 
ATOM   6259 C CE3   . TRP B 2 394 ? 99.102  112.470 114.632 1.00 146.51 ? 394 TRP B CE3   1 
ATOM   6260 C CZ2   . TRP B 2 394 ? 96.598  111.306 114.384 1.00 146.51 ? 394 TRP B CZ2   1 
ATOM   6261 C CZ3   . TRP B 2 394 ? 98.607  111.667 115.588 1.00 146.51 ? 394 TRP B CZ3   1 
ATOM   6262 C CH2   . TRP B 2 394 ? 97.372  111.095 115.465 1.00 146.51 ? 394 TRP B CH2   1 
ATOM   6263 N N     . TYR B 2 395 ? 100.896 117.550 112.353 1.00 103.32 ? 395 TYR B N     1 
ATOM   6264 C CA    . TYR B 2 395 ? 101.975 118.463 112.119 1.00 103.32 ? 395 TYR B CA    1 
ATOM   6265 C C     . TYR B 2 395 ? 102.028 119.498 113.224 1.00 103.32 ? 395 TYR B C     1 
ATOM   6266 O O     . TYR B 2 395 ? 103.094 119.754 113.790 1.00 103.32 ? 395 TYR B O     1 
ATOM   6267 C CB    . TYR B 2 395 ? 101.769 119.103 110.731 1.00 143.06 ? 395 TYR B CB    1 
ATOM   6268 C CG    . TYR B 2 395 ? 101.776 118.088 109.611 1.00 143.06 ? 395 TYR B CG    1 
ATOM   6269 C CD1   . TYR B 2 395 ? 102.965 117.643 109.101 1.00 143.06 ? 395 TYR B CD1   1 
ATOM   6270 C CD2   . TYR B 2 395 ? 100.606 117.576 109.096 1.00 143.06 ? 395 TYR B CD2   1 
ATOM   6271 C CE1   . TYR B 2 395 ? 103.007 116.732 108.122 1.00 143.06 ? 395 TYR B CE1   1 
ATOM   6272 C CE2   . TYR B 2 395 ? 100.640 116.648 108.099 1.00 143.06 ? 395 TYR B CE2   1 
ATOM   6273 C CZ    . TYR B 2 395 ? 101.853 116.232 107.621 1.00 143.06 ? 395 TYR B CZ    1 
ATOM   6274 O OH    . TYR B 2 395 ? 101.924 115.301 106.627 1.00 143.06 ? 395 TYR B OH    1 
ATOM   6275 N N     . GLU B 2 396 ? 100.858 120.013 113.604 1.00 103.45 ? 396 GLU B N     1 
ATOM   6276 C CA    . GLU B 2 396 ? 100.772 121.050 114.614 1.00 103.45 ? 396 GLU B CA    1 
ATOM   6277 C C     . GLU B 2 396 ? 101.311 120.568 115.924 1.00 103.45 ? 396 GLU B C     1 
ATOM   6278 O O     . GLU B 2 396 ? 101.963 121.323 116.649 1.00 103.45 ? 396 GLU B O     1 
ATOM   6279 C CB    . GLU B 2 396 ? 99.339  121.497 114.817 1.00 138.96 ? 396 GLU B CB    1 
ATOM   6280 C CG    . GLU B 2 396 ? 98.772  122.274 113.660 1.00 138.96 ? 396 GLU B CG    1 
ATOM   6281 C CD    . GLU B 2 396 ? 97.326  122.599 113.857 1.00 138.96 ? 396 GLU B CD    1 
ATOM   6282 O OE1   . GLU B 2 396 ? 96.718  122.018 114.756 1.00 138.96 ? 396 GLU B OE1   1 
ATOM   6283 O OE2   . GLU B 2 396 ? 96.798  123.436 113.123 1.00 138.96 ? 396 GLU B OE2   1 
ATOM   6284 N N     . ILE B 2 397 ? 101.100 119.294 116.217 1.00 103.41 ? 397 ILE B N     1 
ATOM   6285 C CA    . ILE B 2 397 ? 101.557 118.709 117.465 1.00 103.41 ? 397 ILE B CA    1 
ATOM   6286 C C     . ILE B 2 397 ? 103.065 118.854 117.651 1.00 103.41 ? 397 ILE B C     1 
ATOM   6287 O O     . ILE B 2 397 ? 103.541 118.934 118.786 1.00 103.41 ? 397 ILE B O     1 
ATOM   6288 C CB    . ILE B 2 397 ? 101.118 117.240 117.536 1.00 153.10 ? 397 ILE B CB    1 
ATOM   6289 C CG1   . ILE B 2 397 ? 99.593  117.162 117.736 1.00 153.10 ? 397 ILE B CG1   1 
ATOM   6290 C CG2   . ILE B 2 397 ? 101.869 116.513 118.637 1.00 153.10 ? 397 ILE B CG2   1 
ATOM   6291 C CD1   . ILE B 2 397 ? 98.966  115.757 117.495 1.00 153.10 ? 397 ILE B CD1   1 
ATOM   6292 N N     . GLU B 2 398 ? 103.841 118.861 116.573 1.00 101.77 ? 398 GLU B N     1 
ATOM   6293 C CA    . GLU B 2 398 ? 105.280 118.967 116.696 1.00 101.77 ? 398 GLU B CA    1 
ATOM   6294 C C     . GLU B 2 398 ? 105.776 120.380 116.520 1.00 101.77 ? 398 GLU B C     1 
ATOM   6295 O O     . GLU B 2 398 ? 106.980 120.602 116.492 1.00 101.77 ? 398 GLU B O     1 
ATOM   6296 C CB    . GLU B 2 398 ? 105.927 118.065 115.674 1.00 136.71 ? 398 GLU B CB    1 
ATOM   6297 C CG    . GLU B 2 398 ? 105.555 116.645 115.863 1.00 136.71 ? 398 GLU B CG    1 
ATOM   6298 C CD    . GLU B 2 398 ? 105.968 116.153 117.218 1.00 136.71 ? 398 GLU B CD    1 
ATOM   6299 O OE1   . GLU B 2 398 ? 107.051 116.528 117.666 1.00 136.71 ? 398 GLU B OE1   1 
ATOM   6300 O OE2   . GLU B 2 398 ? 105.204 115.422 117.856 1.00 136.71 ? 398 GLU B OE2   1 
ATOM   6301 N N     . GLY B 2 399 ? 104.878 121.336 116.358 1.00 100.38 ? 399 GLY B N     1 
ATOM   6302 C CA    . GLY B 2 399 ? 105.255 122.713 116.105 1.00 100.38 ? 399 GLY B CA    1 
ATOM   6303 C C     . GLY B 2 399 ? 105.214 123.142 114.654 1.00 100.38 ? 399 GLY B C     1 
ATOM   6304 O O     . GLY B 2 399 ? 105.664 124.236 114.329 1.00 100.38 ? 399 GLY B O     1 
ATOM   6305 N N     . MET B 2 400 ? 104.680 122.331 113.775 1.00 96.27  ? 400 MET B N     1 
ATOM   6306 C CA    . MET B 2 400 ? 104.659 122.721 112.379 1.00 96.27  ? 400 MET B CA    1 
ATOM   6307 C C     . MET B 2 400 ? 103.474 123.636 112.174 1.00 96.27  ? 400 MET B C     1 
ATOM   6308 O O     . MET B 2 400 ? 102.366 123.204 111.871 1.00 96.27  ? 400 MET B O     1 
ATOM   6309 C CB    . MET B 2 400 ? 104.583 121.497 111.491 1.00 138.30 ? 400 MET B CB    1 
ATOM   6310 C CG    . MET B 2 400 ? 104.609 121.754 110.013 1.00 138.30 ? 400 MET B CG    1 
ATOM   6311 S SD    . MET B 2 400 ? 106.160 122.370 109.415 1.00 138.30 ? 400 MET B SD    1 
ATOM   6312 C CE    . MET B 2 400 ? 107.177 120.909 109.500 1.00 138.30 ? 400 MET B CE    1 
ATOM   6313 N N     . SER B 2 401 ? 103.732 124.917 112.303 1.00 91.97  ? 401 SER B N     1 
ATOM   6314 C CA    . SER B 2 401 ? 102.700 125.934 112.264 1.00 91.97  ? 401 SER B CA    1 
ATOM   6315 C C     . SER B 2 401 ? 102.004 126.054 110.936 1.00 91.97  ? 401 SER B C     1 
ATOM   6316 O O     . SER B 2 401 ? 102.573 125.814 109.878 1.00 91.97  ? 401 SER B O     1 
ATOM   6317 C CB    . SER B 2 401 ? 103.284 127.294 112.580 1.00 123.88 ? 401 SER B CB    1 
ATOM   6318 O OG    . SER B 2 401 ? 102.307 128.281 112.324 1.00 123.88 ? 401 SER B OG    1 
ATOM   6319 N N     . LYS B 2 402 ? 100.783 126.528 111.015 1.00 86.19  ? 402 LYS B N     1 
ATOM   6320 C CA    . LYS B 2 402 ? 99.974  126.800 109.854 1.00 86.19  ? 402 LYS B CA    1 
ATOM   6321 C C     . LYS B 2 402 ? 100.651 127.788 108.923 1.00 86.19  ? 402 LYS B C     1 
ATOM   6322 O O     . LYS B 2 402 ? 100.364 127.822 107.712 1.00 86.19  ? 402 LYS B O     1 
ATOM   6323 C CB    . LYS B 2 402 ? 98.636  127.365 110.311 1.00 129.28 ? 402 LYS B CB    1 
ATOM   6324 C CG    . LYS B 2 402 ? 98.758  128.778 110.915 1.00 129.28 ? 402 LYS B CG    1 
ATOM   6325 C CD    . LYS B 2 402 ? 97.422  129.348 111.371 1.00 129.28 ? 402 LYS B CD    1 
ATOM   6326 C CE    . LYS B 2 402 ? 97.589  130.714 112.080 1.00 129.28 ? 402 LYS B CE    1 
ATOM   6327 N NZ    . LYS B 2 402 ? 98.101  131.822 111.187 1.00 129.28 ? 402 LYS B NZ    1 
ATOM   6328 N N     . ASP B 2 403 ? 101.547 128.590 109.467 1.00 85.39  ? 403 ASP B N     1 
ATOM   6329 C CA    . ASP B 2 403 ? 102.245 129.579 108.685 1.00 85.39  ? 403 ASP B CA    1 
ATOM   6330 C C     . ASP B 2 403 ? 103.284 128.951 107.792 1.00 85.39  ? 403 ASP B C     1 
ATOM   6331 O O     . ASP B 2 403 ? 103.633 129.517 106.753 1.00 85.39  ? 403 ASP B O     1 
ATOM   6332 C CB    . ASP B 2 403 ? 102.876 130.571 109.614 1.00 109.79 ? 403 ASP B CB    1 
ATOM   6333 C CG    . ASP B 2 403 ? 101.841 131.338 110.404 1.00 109.79 ? 403 ASP B CG    1 
ATOM   6334 O OD1   . ASP B 2 403 ? 100.686 131.445 109.966 1.00 109.79 ? 403 ASP B OD1   1 
ATOM   6335 O OD2   . ASP B 2 403 ? 102.173 131.820 111.480 1.00 109.79 ? 403 ASP B OD2   1 
ATOM   6336 N N     . ASP B 2 404 ? 103.778 127.776 108.160 1.00 86.16  ? 404 ASP B N     1 
ATOM   6337 C CA    . ASP B 2 404 ? 104.747 127.107 107.323 1.00 86.16  ? 404 ASP B CA    1 
ATOM   6338 C C     . ASP B 2 404 ? 104.022 126.393 106.226 1.00 86.16  ? 404 ASP B C     1 
ATOM   6339 O O     . ASP B 2 404 ? 104.542 126.265 105.109 1.00 86.16  ? 404 ASP B O     1 
ATOM   6340 C CB    . ASP B 2 404 ? 105.603 126.145 108.140 1.00 110.78 ? 404 ASP B CB    1 
ATOM   6341 C CG    . ASP B 2 404 ? 106.482 126.866 109.142 1.00 110.78 ? 404 ASP B CG    1 
ATOM   6342 O OD1   . ASP B 2 404 ? 107.224 127.759 108.752 1.00 110.78 ? 404 ASP B OD1   1 
ATOM   6343 O OD2   . ASP B 2 404 ? 106.427 126.540 110.320 1.00 110.78 ? 404 ASP B OD2   1 
ATOM   6344 N N     . PHE B 2 405 ? 102.804 125.967 106.510 1.00 83.32  ? 405 PHE B N     1 
ATOM   6345 C CA    . PHE B 2 405 ? 102.017 125.371 105.454 1.00 83.32  ? 405 PHE B CA    1 
ATOM   6346 C C     . PHE B 2 405 ? 101.816 126.403 104.380 1.00 83.32  ? 405 PHE B C     1 
ATOM   6347 O O     . PHE B 2 405 ? 102.010 126.142 103.188 1.00 83.32  ? 405 PHE B O     1 
ATOM   6348 C CB    . PHE B 2 405 ? 100.634 124.960 105.939 1.00 116.26 ? 405 PHE B CB    1 
ATOM   6349 C CG    . PHE B 2 405 ? 100.526 123.692 106.725 1.00 116.26 ? 405 PHE B CG    1 
ATOM   6350 C CD1   . PHE B 2 405 ? 100.935 123.611 108.034 1.00 116.26 ? 405 PHE B CD1   1 
ATOM   6351 C CD2   . PHE B 2 405 ? 99.846  122.634 106.193 1.00 116.26 ? 405 PHE B CD2   1 
ATOM   6352 C CE1   . PHE B 2 405 ? 100.741 122.456 108.763 1.00 116.26 ? 405 PHE B CE1   1 
ATOM   6353 C CE2   . PHE B 2 405 ? 99.644  121.495 106.903 1.00 116.26 ? 405 PHE B CE2   1 
ATOM   6354 C CZ    . PHE B 2 405 ? 100.090 121.397 108.194 1.00 116.26 ? 405 PHE B CZ    1 
ATOM   6355 N N     . ALA B 2 406 ? 101.447 127.602 104.800 1.00 78.61  ? 406 ALA B N     1 
ATOM   6356 C CA    . ALA B 2 406 ? 101.191 128.657 103.841 1.00 78.61  ? 406 ALA B CA    1 
ATOM   6357 C C     . ALA B 2 406 ? 102.439 129.030 103.082 1.00 78.61  ? 406 ALA B C     1 
ATOM   6358 O O     . ALA B 2 406 ? 102.383 129.291 101.876 1.00 78.61  ? 406 ALA B O     1 
ATOM   6359 C CB    . ALA B 2 406 ? 100.638 129.864 104.561 1.00 107.20 ? 406 ALA B CB    1 
ATOM   6360 N N     . GLY B 2 407 ? 103.584 129.054 103.772 1.00 71.36  ? 407 GLY B N     1 
ATOM   6361 C CA    . GLY B 2 407 ? 104.833 129.406 103.108 1.00 71.36  ? 407 GLY B CA    1 
ATOM   6362 C C     . GLY B 2 407 ? 105.179 128.457 101.985 1.00 71.36  ? 407 GLY B C     1 
ATOM   6363 O O     . GLY B 2 407 ? 105.469 128.878 100.862 1.00 71.36  ? 407 GLY B O     1 
ATOM   6364 N N     . ALA B 2 408 ? 105.133 127.168 102.270 1.00 70.72  ? 408 ALA B N     1 
ATOM   6365 C CA    . ALA B 2 408 ? 105.425 126.214 101.233 1.00 70.72  ? 408 ALA B CA    1 
ATOM   6366 C C     . ALA B 2 408 ? 104.419 126.342 100.124 1.00 70.72  ? 408 ALA B C     1 
ATOM   6367 O O     . ALA B 2 408 ? 104.773 126.228 98.948  1.00 70.72  ? 408 ALA B O     1 
ATOM   6368 C CB    . ALA B 2 408 ? 105.427 124.805 101.791 1.00 96.44  ? 408 ALA B CB    1 
ATOM   6369 N N     . ARG B 2 409 ? 103.168 126.595 100.473 1.00 68.14  ? 409 ARG B N     1 
ATOM   6370 C CA    . ARG B 2 409 ? 102.161 126.718 99.451  1.00 68.14  ? 409 ARG B CA    1 
ATOM   6371 C C     . ARG B 2 409 ? 102.569 127.776 98.470  1.00 68.14  ? 409 ARG B C     1 
ATOM   6372 O O     . ARG B 2 409 ? 102.554 127.557 97.249  1.00 68.14  ? 409 ARG B O     1 
ATOM   6373 C CB    . ARG B 2 409 ? 100.830 127.087 100.057 1.00 100.12 ? 409 ARG B CB    1 
ATOM   6374 C CG    . ARG B 2 409 ? 99.661  127.152 99.081  1.00 100.12 ? 409 ARG B CG    1 
ATOM   6375 C CD    . ARG B 2 409 ? 98.386  127.500 99.829  1.00 100.12 ? 409 ARG B CD    1 
ATOM   6376 N NE    . ARG B 2 409 ? 97.171  127.437 99.017  1.00 100.12 ? 409 ARG B NE    1 
ATOM   6377 C CZ    . ARG B 2 409 ? 95.954  127.347 99.539  1.00 100.12 ? 409 ARG B CZ    1 
ATOM   6378 N NH1   . ARG B 2 409 ? 95.778  127.300 100.838 1.00 100.12 ? 409 ARG B NH1   1 
ATOM   6379 N NH2   . ARG B 2 409 ? 94.891  127.273 98.742  1.00 100.12 ? 409 ARG B NH2   1 
ATOM   6380 N N     . ASP B 2 410 ? 103.027 128.908 98.989  1.00 68.39  ? 410 ASP B N     1 
ATOM   6381 C CA    . ASP B 2 410 ? 103.381 130.010 98.112  1.00 68.39  ? 410 ASP B CA    1 
ATOM   6382 C C     . ASP B 2 410 ? 104.596 129.718 97.250  1.00 68.39  ? 410 ASP B C     1 
ATOM   6383 O O     . ASP B 2 410 ? 104.604 130.013 96.055  1.00 68.39  ? 410 ASP B O     1 
ATOM   6384 C CB    . ASP B 2 410 ? 103.652 131.252 98.924  1.00 87.93  ? 410 ASP B CB    1 
ATOM   6385 C CG    . ASP B 2 410 ? 102.398 131.894 99.480  1.00 87.93  ? 410 ASP B CG    1 
ATOM   6386 O OD1   . ASP B 2 410 ? 101.283 131.568 99.063  1.00 87.93  ? 410 ASP B OD1   1 
ATOM   6387 O OD2   . ASP B 2 410 ? 102.548 132.754 100.348 1.00 87.93  ? 410 ASP B OD2   1 
ATOM   6388 N N     . ASN B 2 411 ? 105.628 129.133 97.808  1.00 62.42  ? 411 ASN B N     1 
ATOM   6389 C CA    . ASN B 2 411 ? 106.795 128.989 96.964  1.00 62.42  ? 411 ASN B CA    1 
ATOM   6390 C C     . ASN B 2 411 ? 106.600 127.961 95.883  1.00 62.42  ? 411 ASN B C     1 
ATOM   6391 O O     . ASN B 2 411 ? 107.099 128.123 94.761  1.00 62.42  ? 411 ASN B O     1 
ATOM   6392 C CB    . ASN B 2 411 ? 107.987 128.665 97.799  1.00 84.57  ? 411 ASN B CB    1 
ATOM   6393 C CG    . ASN B 2 411 ? 108.449 129.841 98.538  1.00 84.57  ? 411 ASN B CG    1 
ATOM   6394 O OD1   . ASN B 2 411 ? 108.161 130.981 98.158  1.00 84.57  ? 411 ASN B OD1   1 
ATOM   6395 N ND2   . ASN B 2 411 ? 109.165 129.609 99.604  1.00 84.57  ? 411 ASN B ND2   1 
ATOM   6396 N N     . VAL B 2 412 ? 105.909 126.881 96.190  1.00 63.96  ? 412 VAL B N     1 
ATOM   6397 C CA    . VAL B 2 412 ? 105.746 125.879 95.161  1.00 63.96  ? 412 VAL B CA    1 
ATOM   6398 C C     . VAL B 2 412 ? 104.827 126.421 94.082  1.00 63.96  ? 412 VAL B C     1 
ATOM   6399 O O     . VAL B 2 412 ? 105.051 126.194 92.884  1.00 63.96  ? 412 VAL B O     1 
ATOM   6400 C CB    . VAL B 2 412 ? 105.289 124.547 95.777  1.00 93.03  ? 412 VAL B CB    1 
ATOM   6401 C CG1   . VAL B 2 412 ? 105.016 123.529 94.702  1.00 93.03  ? 412 VAL B CG1   1 
ATOM   6402 C CG2   . VAL B 2 412 ? 106.382 124.018 96.732  1.00 93.03  ? 412 VAL B CG2   1 
ATOM   6403 N N     . GLN B 2 413 ? 103.810 127.182 94.473  1.00 63.79  ? 413 GLN B N     1 
ATOM   6404 C CA    . GLN B 2 413 ? 102.961 127.769 93.470  1.00 63.79  ? 413 GLN B CA    1 
ATOM   6405 C C     . GLN B 2 413 ? 103.764 128.684 92.612  1.00 63.79  ? 413 GLN B C     1 
ATOM   6406 O O     . GLN B 2 413 ? 103.569 128.719 91.390  1.00 63.79  ? 413 GLN B O     1 
ATOM   6407 C CB    . GLN B 2 413 ? 101.811 128.537 94.079  1.00 89.13  ? 413 GLN B CB    1 
ATOM   6408 C CG    . GLN B 2 413 ? 100.857 129.164 93.098  1.00 89.13  ? 413 GLN B CG    1 
ATOM   6409 C CD    . GLN B 2 413 ? 100.065 128.194 92.294  1.00 89.13  ? 413 GLN B CD    1 
ATOM   6410 O OE1   . GLN B 2 413 ? 99.466  127.283 92.825  1.00 89.13  ? 413 GLN B OE1   1 
ATOM   6411 N NE2   . GLN B 2 413 ? 100.030 128.399 90.987  1.00 89.13  ? 413 GLN B NE2   1 
ATOM   6412 N N     . LYS B 2 414 ? 104.702 129.412 93.204  1.00 60.30  ? 414 LYS B N     1 
ATOM   6413 C CA    . LYS B 2 414 ? 105.502 130.284 92.362  1.00 60.30  ? 414 LYS B CA    1 
ATOM   6414 C C     . LYS B 2 414 ? 106.271 129.485 91.324  1.00 60.30  ? 414 LYS B C     1 
ATOM   6415 O O     . LYS B 2 414 ? 106.340 129.904 90.169  1.00 60.30  ? 414 LYS B O     1 
ATOM   6416 C CB    . LYS B 2 414 ? 106.443 131.144 93.181  1.00 90.45  ? 414 LYS B CB    1 
ATOM   6417 C CG    . LYS B 2 414 ? 105.757 132.254 93.919  1.00 90.45  ? 414 LYS B CG    1 
ATOM   6418 C CD    . LYS B 2 414 ? 106.748 133.055 94.752  1.00 90.45  ? 414 LYS B CD    1 
ATOM   6419 C CE    . LYS B 2 414 ? 106.057 134.160 95.546  1.00 90.45  ? 414 LYS B CE    1 
ATOM   6420 N NZ    . LYS B 2 414 ? 107.016 134.942 96.388  1.00 90.45  ? 414 LYS B NZ    1 
ATOM   6421 N N     . LEU B 2 415 ? 106.824 128.316 91.679  1.00 59.86  ? 415 LEU B N     1 
ATOM   6422 C CA    . LEU B 2 415 ? 107.538 127.603 90.631  1.00 59.86  ? 415 LEU B CA    1 
ATOM   6423 C C     . LEU B 2 415 ? 106.644 127.369 89.473  1.00 59.86  ? 415 LEU B C     1 
ATOM   6424 O O     . LEU B 2 415 ? 107.048 127.523 88.312  1.00 59.86  ? 415 LEU B O     1 
ATOM   6425 C CB    . LEU B 2 415 ? 107.989 126.239 91.015  1.00 88.62  ? 415 LEU B CB    1 
ATOM   6426 C CG    . LEU B 2 415 ? 109.079 126.077 91.976  1.00 88.62  ? 415 LEU B CG    1 
ATOM   6427 C CD1   . LEU B 2 415 ? 109.151 124.585 92.180  1.00 88.62  ? 415 LEU B CD1   1 
ATOM   6428 C CD2   . LEU B 2 415 ? 110.389 126.645 91.445  1.00 88.62  ? 415 LEU B CD2   1 
ATOM   6429 N N     . SER B 2 416 ? 105.448 126.926 89.758  1.00 58.19  ? 416 SER B N     1 
ATOM   6430 C CA    . SER B 2 416 ? 104.595 126.592 88.643  1.00 58.19  ? 416 SER B CA    1 
ATOM   6431 C C     . SER B 2 416 ? 104.364 127.817 87.797  1.00 58.19  ? 416 SER B C     1 
ATOM   6432 O O     . SER B 2 416 ? 104.446 127.752 86.565  1.00 58.19  ? 416 SER B O     1 
ATOM   6433 C CB    . SER B 2 416 ? 103.270 126.006 89.114  1.00 78.38  ? 416 SER B CB    1 
ATOM   6434 O OG    . SER B 2 416 ? 102.455 125.694 87.999  1.00 78.38  ? 416 SER B OG    1 
ATOM   6435 N N     . ASP B 2 417 ? 104.122 128.952 88.442  1.00 62.30  ? 417 ASP B N     1 
ATOM   6436 C CA    . ASP B 2 417 ? 103.843 130.165 87.692  1.00 62.30  ? 417 ASP B CA    1 
ATOM   6437 C C     . ASP B 2 417 ? 105.025 130.541 86.814  1.00 62.30  ? 417 ASP B C     1 
ATOM   6438 O O     . ASP B 2 417 ? 104.863 130.997 85.677  1.00 62.30  ? 417 ASP B O     1 
ATOM   6439 C CB    . ASP B 2 417 ? 103.544 131.315 88.648  1.00 80.10  ? 417 ASP B CB    1 
ATOM   6440 C CG    . ASP B 2 417 ? 102.237 131.159 89.430  1.00 80.10  ? 417 ASP B CG    1 
ATOM   6441 O OD1   . ASP B 2 417 ? 101.392 130.312 89.117  1.00 80.10  ? 417 ASP B OD1   1 
ATOM   6442 O OD2   . ASP B 2 417 ? 102.063 131.925 90.381  1.00 80.10  ? 417 ASP B OD2   1 
ATOM   6443 N N     . GLU B 2 418 ? 106.221 130.349 87.334  1.00 61.49  ? 418 GLU B N     1 
ATOM   6444 C CA    . GLU B 2 418 ? 107.413 130.696 86.593  1.00 61.49  ? 418 GLU B CA    1 
ATOM   6445 C C     . GLU B 2 418 ? 107.558 129.854 85.348  1.00 61.49  ? 418 GLU B C     1 
ATOM   6446 O O     . GLU B 2 418 ? 108.073 130.336 84.339  1.00 61.49  ? 418 GLU B O     1 
ATOM   6447 C CB    . GLU B 2 418 ? 108.645 130.541 87.459  1.00 82.60  ? 418 GLU B CB    1 
ATOM   6448 C CG    . GLU B 2 418 ? 108.799 131.596 88.505  1.00 82.60  ? 418 GLU B CG    1 
ATOM   6449 C CD    . GLU B 2 418 ? 110.024 131.391 89.330  1.00 82.60  ? 418 GLU B CD    1 
ATOM   6450 O OE1   . GLU B 2 418 ? 110.551 130.282 89.315  1.00 82.60  ? 418 GLU B OE1   1 
ATOM   6451 O OE2   . GLU B 2 418 ? 110.471 132.331 89.993  1.00 82.60  ? 418 GLU B OE2   1 
ATOM   6452 N N     . TYR B 2 419 ? 107.172 128.578 85.402  1.00 61.70  ? 419 TYR B N     1 
ATOM   6453 C CA    . TYR B 2 419 ? 107.271 127.746 84.201  1.00 61.70  ? 419 TYR B CA    1 
ATOM   6454 C C     . TYR B 2 419 ? 106.148 128.024 83.226  1.00 61.70  ? 419 TYR B C     1 
ATOM   6455 O O     . TYR B 2 419 ? 106.343 127.987 82.018  1.00 61.70  ? 419 TYR B O     1 
ATOM   6456 C CB    . TYR B 2 419 ? 107.251 126.263 84.549  1.00 85.43  ? 419 TYR B CB    1 
ATOM   6457 C CG    . TYR B 2 419 ? 108.507 125.688 85.145  1.00 85.43  ? 419 TYR B CG    1 
ATOM   6458 C CD1   . TYR B 2 419 ? 109.589 125.414 84.356  1.00 85.43  ? 419 TYR B CD1   1 
ATOM   6459 C CD2   . TYR B 2 419 ? 108.581 125.374 86.492  1.00 85.43  ? 419 TYR B CD2   1 
ATOM   6460 C CE1   . TYR B 2 419 ? 110.724 124.863 84.883  1.00 85.43  ? 419 TYR B CE1   1 
ATOM   6461 C CE2   . TYR B 2 419 ? 109.718 124.821 87.027  1.00 85.43  ? 419 TYR B CE2   1 
ATOM   6462 C CZ    . TYR B 2 419 ? 110.793 124.569 86.208  1.00 85.43  ? 419 TYR B CZ    1 
ATOM   6463 O OH    . TYR B 2 419 ? 111.938 123.995 86.719  1.00 85.43  ? 419 TYR B OH    1 
ATOM   6464 N N     . LYS B 2 420 ? 104.973 128.321 83.735  1.00 64.31  ? 420 LYS B N     1 
ATOM   6465 C CA    . LYS B 2 420 ? 103.825 128.504 82.872  1.00 64.31  ? 420 LYS B CA    1 
ATOM   6466 C C     . LYS B 2 420 ? 104.011 129.699 81.978  1.00 64.31  ? 420 LYS B C     1 
ATOM   6467 O O     . LYS B 2 420 ? 103.641 129.680 80.807  1.00 64.31  ? 420 LYS B O     1 
ATOM   6468 C CB    . LYS B 2 420 ? 102.573 128.672 83.716  1.00 96.46  ? 420 LYS B CB    1 
ATOM   6469 C CG    . LYS B 2 420 ? 101.279 128.721 82.942  1.00 96.46  ? 420 LYS B CG    1 
ATOM   6470 C CD    . LYS B 2 420 ? 100.954 127.375 82.340  1.00 96.46  ? 420 LYS B CD    1 
ATOM   6471 C CE    . LYS B 2 420 ? 99.613  127.364 81.625  1.00 96.46  ? 420 LYS B CE    1 
ATOM   6472 N NZ    . LYS B 2 420 ? 99.340  126.027 81.012  1.00 96.46  ? 420 LYS B NZ    1 
ATOM   6473 N N     . ARG B 2 421 ? 104.621 130.743 82.504  1.00 66.45  ? 421 ARG B N     1 
ATOM   6474 C CA    . ARG B 2 421 ? 104.800 131.954 81.719  1.00 66.45  ? 421 ARG B CA    1 
ATOM   6475 C C     . ARG B 2 421 ? 105.754 131.765 80.559  1.00 66.45  ? 421 ARG B C     1 
ATOM   6476 O O     . ARG B 2 421 ? 105.832 132.646 79.705  1.00 66.45  ? 421 ARG B O     1 
ATOM   6477 C CB    . ARG B 2 421 ? 105.312 133.090 82.582  1.00 97.64  ? 421 ARG B CB    1 
ATOM   6478 C CG    . ARG B 2 421 ? 106.639 132.802 83.083  1.00 97.64  ? 421 ARG B CG    1 
ATOM   6479 C CD    . ARG B 2 421 ? 107.167 133.837 83.966  1.00 97.64  ? 421 ARG B CD    1 
ATOM   6480 N NE    . ARG B 2 421 ? 108.436 133.349 84.477  1.00 97.64  ? 421 ARG B NE    1 
ATOM   6481 C CZ    . ARG B 2 421 ? 109.293 134.039 85.219  1.00 97.64  ? 421 ARG B CZ    1 
ATOM   6482 N NH1   . ARG B 2 421 ? 109.062 135.298 85.555  1.00 97.64  ? 421 ARG B NH1   1 
ATOM   6483 N NH2   . ARG B 2 421 ? 110.408 133.447 85.636  1.00 97.64  ? 421 ARG B NH2   1 
ATOM   6484 N N     . ASP B 2 422 ? 106.494 130.665 80.509  1.00 63.09  ? 422 ASP B N     1 
ATOM   6485 C CA    . ASP B 2 422 ? 107.418 130.473 79.412  1.00 63.09  ? 422 ASP B CA    1 
ATOM   6486 C C     . ASP B 2 422 ? 106.798 129.730 78.256  1.00 63.09  ? 422 ASP B C     1 
ATOM   6487 O O     . ASP B 2 422 ? 107.489 129.457 77.284  1.00 63.09  ? 422 ASP B O     1 
ATOM   6488 C CB    . ASP B 2 422 ? 108.657 129.739 79.875  1.00 81.12  ? 422 ASP B CB    1 
ATOM   6489 C CG    . ASP B 2 422 ? 109.569 130.583 80.737  1.00 81.12  ? 422 ASP B CG    1 
ATOM   6490 O OD1   . ASP B 2 422 ? 109.631 131.803 80.570  1.00 81.12  ? 422 ASP B OD1   1 
ATOM   6491 O OD2   . ASP B 2 422 ? 110.253 130.003 81.581  1.00 81.12  ? 422 ASP B OD2   1 
ATOM   6492 N N     . GLU B 2 423 ? 105.515 129.419 78.308  1.00 64.47  ? 423 GLU B N     1 
ATOM   6493 C CA    . GLU B 2 423 ? 104.927 128.650 77.213  1.00 64.47  ? 423 GLU B CA    1 
ATOM   6494 C C     . GLU B 2 423 ? 104.908 129.376 75.866  1.00 64.47  ? 423 GLU B C     1 
ATOM   6495 O O     . GLU B 2 423 ? 104.990 128.708 74.828  1.00 64.47  ? 423 GLU B O     1 
ATOM   6496 C CB    . GLU B 2 423 ? 103.502 128.215 77.543  1.00 86.60  ? 423 GLU B CB    1 
ATOM   6497 C CG    . GLU B 2 423 ? 103.388 127.068 78.529  1.00 86.60  ? 423 GLU B CG    1 
ATOM   6498 C CD    . GLU B 2 423 ? 101.952 126.665 78.754  1.00 86.60  ? 423 GLU B CD    1 
ATOM   6499 O OE1   . GLU B 2 423 ? 101.061 127.371 78.281  1.00 86.60  ? 423 GLU B OE1   1 
ATOM   6500 O OE2   . GLU B 2 423 ? 101.706 125.646 79.401  1.00 86.60  ? 423 GLU B OE2   1 
ATOM   6501 N N     . GLU B 2 424 ? 104.724 130.697 75.844  1.00 66.92  ? 424 GLU B N     1 
ATOM   6502 C CA    . GLU B 2 424 ? 104.689 131.513 74.610  1.00 66.92  ? 424 GLU B CA    1 
ATOM   6503 C C     . GLU B 2 424 ? 105.064 132.926 75.033  1.00 66.92  ? 424 GLU B C     1 
ATOM   6504 O O     . GLU B 2 424 ? 105.833 133.613 74.362  1.00 0.00   ? 424 GLU B O     1 
ATOM   6505 C CB    . GLU B 2 424 ? 103.308 131.476 73.911  1.00 85.57  ? 424 GLU B CB    1 
ATOM   6506 C CG    . GLU B 2 424 ? 103.224 132.275 72.539  1.00 85.57  ? 424 GLU B CG    1 
ATOM   6507 C CD    . GLU B 2 424 ? 101.892 132.205 71.806  1.00 85.57  ? 424 GLU B CD    1 
ATOM   6508 O OE1   . GLU B 2 424 ? 100.959 131.550 72.273  1.00 85.57  ? 424 GLU B OE1   1 
ATOM   6509 O OE2   . GLU B 2 424 ? 101.789 132.815 70.742  1.00 85.57  ? 424 GLU B OE2   1 
ATOM   6510 O OXT   . GLU B 2 424 ? 104.697 133.349 76.134  1.00 90.84  ? 424 GLU B OXT   1 
HETATM 6511 P PB    . GDP C 3 .   ? 85.415  93.452  135.493 1.00 74.99  ? 501 GDP A PB    1 
HETATM 6512 O O1B   . GDP C 3 .   ? 85.550  94.866  135.017 1.00 74.99  ? 501 GDP A O1B   1 
HETATM 6513 O O2B   . GDP C 3 .   ? 85.039  93.487  137.001 1.00 74.99  ? 501 GDP A O2B   1 
HETATM 6514 O O3B   . GDP C 3 .   ? 86.750  92.709  135.236 1.00 74.99  ? 501 GDP A O3B   1 
HETATM 6515 O O3A   . GDP C 3 .   ? 84.206  92.777  134.690 1.00 74.99  ? 501 GDP A O3A   1 
HETATM 6516 P PA    . GDP C 3 .   ? 83.905  92.686  133.134 1.00 74.99  ? 501 GDP A PA    1 
HETATM 6517 O O1A   . GDP C 3 .   ? 85.162  92.995  132.378 1.00 74.99  ? 501 GDP A O1A   1 
HETATM 6518 O O2A   . GDP C 3 .   ? 83.395  91.274  132.854 1.00 74.99  ? 501 GDP A O2A   1 
HETATM 6519 O "O5'" . GDP C 3 .   ? 82.761  93.783  132.827 1.00 74.99  ? 501 GDP A "O5'" 1 
HETATM 6520 C "C5'" . GDP C 3 .   ? 81.404  93.536  132.426 1.00 74.99  ? 501 GDP A "C5'" 1 
HETATM 6521 C "C4'" . GDP C 3 .   ? 81.084  94.186  131.080 1.00 74.99  ? 501 GDP A "C4'" 1 
HETATM 6522 O "O4'" . GDP C 3 .   ? 82.007  93.678  130.140 1.00 74.99  ? 501 GDP A "O4'" 1 
HETATM 6523 C "C3'" . GDP C 3 .   ? 79.698  93.875  130.506 1.00 74.99  ? 501 GDP A "C3'" 1 
HETATM 6524 O "O3'" . GDP C 3 .   ? 79.172  94.984  129.738 1.00 74.99  ? 501 GDP A "O3'" 1 
HETATM 6525 C "C2'" . GDP C 3 .   ? 79.953  92.667  129.619 1.00 74.99  ? 501 GDP A "C2'" 1 
HETATM 6526 O "O2'" . GDP C 3 .   ? 79.015  92.532  128.548 1.00 74.99  ? 501 GDP A "O2'" 1 
HETATM 6527 C "C1'" . GDP C 3 .   ? 81.346  92.932  129.095 1.00 74.99  ? 501 GDP A "C1'" 1 
HETATM 6528 N N9    . GDP C 3 .   ? 82.113  91.676  128.807 1.00 74.99  ? 501 GDP A N9    1 
HETATM 6529 C C8    . GDP C 3 .   ? 82.639  90.904  129.787 1.00 74.99  ? 501 GDP A C8    1 
HETATM 6530 N N7    . GDP C 3 .   ? 83.323  89.880  129.289 1.00 74.99  ? 501 GDP A N7    1 
HETATM 6531 C C5    . GDP C 3 .   ? 83.252  89.963  127.965 1.00 74.99  ? 501 GDP A C5    1 
HETATM 6532 C C6    . GDP C 3 .   ? 83.779  89.151  126.888 1.00 74.99  ? 501 GDP A C6    1 
HETATM 6533 O O6    . GDP C 3 .   ? 84.441  88.129  127.151 1.00 74.99  ? 501 GDP A O6    1 
HETATM 6534 N N1    . GDP C 3 .   ? 83.529  89.512  125.613 1.00 74.99  ? 501 GDP A N1    1 
HETATM 6535 C C2    . GDP C 3 .   ? 82.785  90.605  125.301 1.00 74.99  ? 501 GDP A C2    1 
HETATM 6536 N N2    . GDP C 3 .   ? 82.571  90.891  123.984 1.00 74.99  ? 501 GDP A N2    1 
HETATM 6537 N N3    . GDP C 3 .   ? 82.266  91.398  126.273 1.00 74.99  ? 501 GDP A N3    1 
HETATM 6538 C C4    . GDP C 3 .   ? 82.468  91.128  127.606 1.00 74.99  ? 501 GDP A C4    1 
HETATM 6539 P PG    . GTP D 4 .   ? 109.690 106.840 106.432 1.00 0.00   ? 501 GTP B PG    1 
HETATM 6540 O O1G   . GTP D 4 .   ? 110.838 105.920 106.732 1.00 0.00   ? 501 GTP B O1G   1 
HETATM 6541 O O2G   . GTP D 4 .   ? 109.834 108.139 107.174 1.00 0.00   ? 501 GTP B O2G   1 
HETATM 6542 O O3G   . GTP D 4 .   ? 108.340 106.188 106.562 1.00 0.00   ? 501 GTP B O3G   1 
HETATM 6543 O O3B   . GTP D 4 .   ? 109.820 107.272 104.886 1.00 0.00   ? 501 GTP B O3B   1 
HETATM 6544 P PB    . GTP D 4 .   ? 109.709 106.369 103.579 1.00 0.00   ? 501 GTP B PB    1 
HETATM 6545 O O1B   . GTP D 4 .   ? 110.848 106.612 102.676 1.00 0.00   ? 501 GTP B O1B   1 
HETATM 6546 O O2B   . GTP D 4 .   ? 109.406 105.006 104.050 1.00 0.00   ? 501 GTP B O2B   1 
HETATM 6547 O O3A   . GTP D 4 .   ? 108.398 106.816 102.807 1.00 0.00   ? 501 GTP B O3A   1 
HETATM 6548 P PA    . GTP D 4 .   ? 107.857 106.228 101.456 1.00 0.00   ? 501 GTP B PA    1 
HETATM 6549 O O1A   . GTP D 4 .   ? 108.827 106.596 100.407 1.00 0.00   ? 501 GTP B O1A   1 
HETATM 6550 O O2A   . GTP D 4 .   ? 107.509 104.807 101.666 1.00 0.00   ? 501 GTP B O2A   1 
HETATM 6551 O "O5'" . GTP D 4 .   ? 106.518 107.066 101.306 1.00 0.00   ? 501 GTP B "O5'" 1 
HETATM 6552 C "C5'" . GTP D 4 .   ? 106.520 108.013 100.257 1.00 0.00   ? 501 GTP B "C5'" 1 
HETATM 6553 C "C4'" . GTP D 4 .   ? 106.061 107.292 99.026  1.00 0.00   ? 501 GTP B "C4'" 1 
HETATM 6554 O "O4'" . GTP D 4 .   ? 107.170 106.647 98.386  1.00 0.00   ? 501 GTP B "O4'" 1 
HETATM 6555 C "C3'" . GTP D 4 .   ? 105.146 106.110 99.290  1.00 0.00   ? 501 GTP B "C3'" 1 
HETATM 6556 O "O3'" . GTP D 4 .   ? 103.907 106.621 99.746  1.00 0.00   ? 501 GTP B "O3'" 1 
HETATM 6557 C "C2'" . GTP D 4 .   ? 105.141 105.522 97.887  1.00 0.00   ? 501 GTP B "C2'" 1 
HETATM 6558 O "O2'" . GTP D 4 .   ? 104.359 106.354 97.062  1.00 0.00   ? 501 GTP B "O2'" 1 
HETATM 6559 C "C1'" . GTP D 4 .   ? 106.619 105.661 97.516  1.00 0.00   ? 501 GTP B "C1'" 1 
HETATM 6560 N N9    . GTP D 4 .   ? 107.429 104.448 97.642  1.00 0.00   ? 501 GTP B N9    1 
HETATM 6561 C C8    . GTP D 4 .   ? 107.192 103.301 98.353  1.00 0.00   ? 501 GTP B C8    1 
HETATM 6562 N N7    . GTP D 4 .   ? 108.147 102.410 98.251  1.00 0.00   ? 501 GTP B N7    1 
HETATM 6563 C C5    . GTP D 4 .   ? 109.092 103.035 97.451  1.00 0.00   ? 501 GTP B C5    1 
HETATM 6564 C C6    . GTP D 4 .   ? 110.345 102.574 97.007  1.00 0.00   ? 501 GTP B C6    1 
HETATM 6565 O O6    . GTP D 4 .   ? 110.881 101.486 97.247  1.00 0.00   ? 501 GTP B O6    1 
HETATM 6566 N N1    . GTP D 4 .   ? 110.990 103.520 96.223  1.00 0.00   ? 501 GTP B N1    1 
HETATM 6567 C C2    . GTP D 4 .   ? 110.491 104.743 95.890  1.00 0.00   ? 501 GTP B C2    1 
HETATM 6568 N N2    . GTP D 4 .   ? 111.257 105.516 95.117  1.00 0.00   ? 501 GTP B N2    1 
HETATM 6569 N N3    . GTP D 4 .   ? 109.311 105.184 96.294  1.00 0.00   ? 501 GTP B N3    1 
HETATM 6570 C C4    . GTP D 4 .   ? 108.671 104.282 97.070  1.00 0.00   ? 501 GTP B C4    1 
# 
