data_9IQG
# 
_entry.id   9IQG 
# 
_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   9IQG         pdb_00009iqg 10.2210/pdb9iqg/pdb 
WWPDB D_1300049237 ?            ?                   
EMDB  EMD-60791    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IQG 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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        
'Cryo-EM structure of MsRv1273c/72c from Mycobacterium smegmatis in the ATP|ADP+Vi-bound Occ (Vi) state' 
_pdbx_database_related.db_id          EMD-60791 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              lijun1@shanghaitech.edu.cn 
_pdbx_contact_author.name_first         Jun 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3165-3699 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lan, Y.' 1 ? 
'Yu, J.'  2 ? 
'Li, J.'  3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3969 
_citation.page_last                 3969 
_citation.title                     
'Structure and mechanism of a mycobacterial isoniazid efflux pump MsRv1273c/72c with a degenerate nucleotide-binding site.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-59300-5 
_citation.pdbx_database_id_PubMed   40295516 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yu, J.'       1  ?                   
primary 'Lan, Y.'      2  ?                   
primary 'Zhu, C.'      3  ?                   
primary 'Chen, Z.'     4  ?                   
primary 'Pan, J.'      5  ?                   
primary 'Shi, Y.'      6  ?                   
primary 'Yang, L.'     7  ?                   
primary 'Hu, T.'       8  ?                   
primary 'Gao, Y.'      9  0000-0002-0364-6427 
primary 'Zhao, Y.'     10 0000-0002-2932-2164 
primary 'Chen, X.'     11 ?                   
primary 'Yang, X.'     12 0000-0003-3443-9815 
primary 'Lu, S.'       13 ?                   
primary 'Guddat, L.W.' 14 0000-0002-8204-8408 
primary 'Yang, H.'     15 0000-0002-1875-3268 
primary 'Rao, Z.'      16 0000-0001-9866-2384 
primary 'Li, J.'       17 0000-0003-3165-3699 
# 
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 'ABC transporter, ATP-binding protein' 63623.227 1 ? ? ? ? 
2 polymer     man 'ABC transporter transmembrane region' 70310.273 1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"            507.181   1 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                        24.305    2 ? ? ? ? 
5 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"             427.201   1 ? ? ? ? 
6 non-polymer syn 'VANADATE ION'                         114.939   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 
;MPEVVGSYFQSNMLWALLRQYVRPYRWLLAVVAVLQVISNMASLYLPTVNAAIIDDGVAKGDTARIVELGAVMLGVTALQ
VVCAVGAVFFGARAATGFGHDLRAAVFTHVTTFSAEEAGRFGAASLLTRTTNDVGHIQQLVQLTVTMLITAPIMSIGGIF
MALHQDAGLSWLLLVSVPVLGLANYWIIRHLMPVFTRMQSLIDGINRVLRDQLSGIRVIRAFAREPLERVRFAEANQTLS
DSALEAGRWQALMLPVTTLVINVSSVALIWFGGLRIDAGQMQVGSLIAFLAYFMQILMAVLMATFMLVIFPRAAVCADRI
GEVLSTQTAITNPADPVRPAAIAGDIGVHDATFCYPGADRPVLQDVSFTVPRGTTTAVVGSTGSGKSTLISLICRLYDVT
SGSLRIDGVDVRDLDIEQLWSAIGLVPQRGYLFSGTVAENLRYGRADATDDEMWEALRVAAAADFVRAHPQGLDMPVAQG
GINFSGGQRQRLAIARAVIRRPAIYLFDDAFSALDVHTDARVRDALREVAADATVVIVSQRISTVIEADQVVVIDDGRVV
GIGTHDTLLADCPIYAEFAESQALTAGEPR
;
;MPEVVGSYFQSNMLWALLRQYVRPYRWLLAVVAVLQVISNMASLYLPTVNAAIIDDGVAKGDTARIVELGAVMLGVTALQ
VVCAVGAVFFGARAATGFGHDLRAAVFTHVTTFSAEEAGRFGAASLLTRTTNDVGHIQQLVQLTVTMLITAPIMSIGGIF
MALHQDAGLSWLLLVSVPVLGLANYWIIRHLMPVFTRMQSLIDGINRVLRDQLSGIRVIRAFAREPLERVRFAEANQTLS
DSALEAGRWQALMLPVTTLVINVSSVALIWFGGLRIDAGQMQVGSLIAFLAYFMQILMAVLMATFMLVIFPRAAVCADRI
GEVLSTQTAITNPADPVRPAAIAGDIGVHDATFCYPGADRPVLQDVSFTVPRGTTTAVVGSTGSGKSTLISLICRLYDVT
SGSLRIDGVDVRDLDIEQLWSAIGLVPQRGYLFSGTVAENLRYGRADATDDEMWEALRVAAAADFVRAHPQGLDMPVAQG
GINFSGGQRQRLAIARAVIRRPAIYLFDDAFSALDVHTDARVRDALREVAADATVVIVSQRISTVIEADQVVVIDDGRVV
GIGTHDTLLADCPIYAEFAESQALTAGEPR
;
A ? 
2 'polypeptide(L)' no no 
;MRRGALPQAPLERTRDFKGSAIRLARRLLPQRALTLAVILLGVGGIAIGVIGPRILGHATDLLFNGVIGRELPAGLTKEQ
AVEAARARGDGTFADLLSGMDIVPGQGVDFGAVGRTLALALGLYLVAALLVWVQARLLNVTVQRTMVALRAEVQEKIHRL
PLSYFDSRQRGEVLSRVTNDVDNIQNSVSMTISQLLTSVLTVFAVLVMMLTISPLLTLFTVVTVPASLWVTRWITRRSQP
LFVAQWRNTGRLAAHLEETYSGFTIVKTFGHREAAAGKFAELNSETQQSSFGAQFFSGLVSPATMFIGNLSYVAVAVVGG
LQVATGQITLGSIQAFIQYVRQFNQPLTQVAGMYNTLQSGIASAERVFDLLDTEEESADSPRRADVRTGRVEFEHVSFSY
VPGTPVIEDLSLVAEPGSTVAIVGPTGAGKTTLVNLLMRFYDVDSGRITIDGVDIASVSRESLRASIGMVLQDTWLFAGT
IYDNIAYGRPDADEDEVIEAATAAYVDRFVHTLPNGYDTRVDDDGGAISAGEKQLITIARAVLARPKLLVLDEATSSVDT
RTELLIAHAMAELRRDRTSFIIAHRLSTIRDADLILVMDSGRIIERGTHEELLARHGRYWEMTRVHLGGIKAFHHHHHHH
HHH
;
;MRRGALPQAPLERTRDFKGSAIRLARRLLPQRALTLAVILLGVGGIAIGVIGPRILGHATDLLFNGVIGRELPAGLTKEQ
AVEAARARGDGTFADLLSGMDIVPGQGVDFGAVGRTLALALGLYLVAALLVWVQARLLNVTVQRTMVALRAEVQEKIHRL
PLSYFDSRQRGEVLSRVTNDVDNIQNSVSMTISQLLTSVLTVFAVLVMMLTISPLLTLFTVVTVPASLWVTRWITRRSQP
LFVAQWRNTGRLAAHLEETYSGFTIVKTFGHREAAAGKFAELNSETQQSSFGAQFFSGLVSPATMFIGNLSYVAVAVVGG
LQVATGQITLGSIQAFIQYVRQFNQPLTQVAGMYNTLQSGIASAERVFDLLDTEEESADSPRRADVRTGRVEFEHVSFSY
VPGTPVIEDLSLVAEPGSTVAIVGPTGAGKTTLVNLLMRFYDVDSGRITIDGVDIASVSRESLRASIGMVLQDTWLFAGT
IYDNIAYGRPDADEDEVIEAATAAYVDRFVHTLPNGYDTRVDDDGGAISAGEKQLITIARAVLARPKLLVLDEATSSVDT
RTELLIAHAMAELRRDRTSFIIAHRLSTIRDADLILVMDSGRIIERGTHEELLARHGRYWEMTRVHLGGIKAFHHHHHHH
HHH
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
5 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
6 'VANADATE ION'              VO4 
# 
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   PRO n 
1 3   GLU n 
1 4   VAL n 
1 5   VAL n 
1 6   GLY n 
1 7   SER n 
1 8   TYR n 
1 9   PHE n 
1 10  GLN n 
1 11  SER n 
1 12  ASN n 
1 13  MET n 
1 14  LEU n 
1 15  TRP n 
1 16  ALA n 
1 17  LEU n 
1 18  LEU n 
1 19  ARG n 
1 20  GLN n 
1 21  TYR n 
1 22  VAL n 
1 23  ARG n 
1 24  PRO n 
1 25  TYR n 
1 26  ARG n 
1 27  TRP n 
1 28  LEU n 
1 29  LEU n 
1 30  ALA n 
1 31  VAL n 
1 32  VAL n 
1 33  ALA n 
1 34  VAL n 
1 35  LEU n 
1 36  GLN n 
1 37  VAL n 
1 38  ILE n 
1 39  SER n 
1 40  ASN n 
1 41  MET n 
1 42  ALA n 
1 43  SER n 
1 44  LEU n 
1 45  TYR n 
1 46  LEU n 
1 47  PRO n 
1 48  THR n 
1 49  VAL n 
1 50  ASN n 
1 51  ALA n 
1 52  ALA n 
1 53  ILE n 
1 54  ILE n 
1 55  ASP n 
1 56  ASP n 
1 57  GLY n 
1 58  VAL n 
1 59  ALA n 
1 60  LYS n 
1 61  GLY n 
1 62  ASP n 
1 63  THR n 
1 64  ALA n 
1 65  ARG n 
1 66  ILE n 
1 67  VAL n 
1 68  GLU n 
1 69  LEU n 
1 70  GLY n 
1 71  ALA n 
1 72  VAL n 
1 73  MET n 
1 74  LEU n 
1 75  GLY n 
1 76  VAL n 
1 77  THR n 
1 78  ALA n 
1 79  LEU n 
1 80  GLN n 
1 81  VAL n 
1 82  VAL n 
1 83  CYS n 
1 84  ALA n 
1 85  VAL n 
1 86  GLY n 
1 87  ALA n 
1 88  VAL n 
1 89  PHE n 
1 90  PHE n 
1 91  GLY n 
1 92  ALA n 
1 93  ARG n 
1 94  ALA n 
1 95  ALA n 
1 96  THR n 
1 97  GLY n 
1 98  PHE n 
1 99  GLY n 
1 100 HIS n 
1 101 ASP n 
1 102 LEU n 
1 103 ARG n 
1 104 ALA n 
1 105 ALA n 
1 106 VAL n 
1 107 PHE n 
1 108 THR n 
1 109 HIS n 
1 110 VAL n 
1 111 THR n 
1 112 THR n 
1 113 PHE n 
1 114 SER n 
1 115 ALA n 
1 116 GLU n 
1 117 GLU n 
1 118 ALA n 
1 119 GLY n 
1 120 ARG n 
1 121 PHE n 
1 122 GLY n 
1 123 ALA n 
1 124 ALA n 
1 125 SER n 
1 126 LEU n 
1 127 LEU n 
1 128 THR n 
1 129 ARG n 
1 130 THR n 
1 131 THR n 
1 132 ASN n 
1 133 ASP n 
1 134 VAL n 
1 135 GLY n 
1 136 HIS n 
1 137 ILE n 
1 138 GLN n 
1 139 GLN n 
1 140 LEU n 
1 141 VAL n 
1 142 GLN n 
1 143 LEU n 
1 144 THR n 
1 145 VAL n 
1 146 THR n 
1 147 MET n 
1 148 LEU n 
1 149 ILE n 
1 150 THR n 
1 151 ALA n 
1 152 PRO n 
1 153 ILE n 
1 154 MET n 
1 155 SER n 
1 156 ILE n 
1 157 GLY n 
1 158 GLY n 
1 159 ILE n 
1 160 PHE n 
1 161 MET n 
1 162 ALA n 
1 163 LEU n 
1 164 HIS n 
1 165 GLN n 
1 166 ASP n 
1 167 ALA n 
1 168 GLY n 
1 169 LEU n 
1 170 SER n 
1 171 TRP n 
1 172 LEU n 
1 173 LEU n 
1 174 LEU n 
1 175 VAL n 
1 176 SER n 
1 177 VAL n 
1 178 PRO n 
1 179 VAL n 
1 180 LEU n 
1 181 GLY n 
1 182 LEU n 
1 183 ALA n 
1 184 ASN n 
1 185 TYR n 
1 186 TRP n 
1 187 ILE n 
1 188 ILE n 
1 189 ARG n 
1 190 HIS n 
1 191 LEU n 
1 192 MET n 
1 193 PRO n 
1 194 VAL n 
1 195 PHE n 
1 196 THR n 
1 197 ARG n 
1 198 MET n 
1 199 GLN n 
1 200 SER n 
1 201 LEU n 
1 202 ILE n 
1 203 ASP n 
1 204 GLY n 
1 205 ILE n 
1 206 ASN n 
1 207 ARG n 
1 208 VAL n 
1 209 LEU n 
1 210 ARG n 
1 211 ASP n 
1 212 GLN n 
1 213 LEU n 
1 214 SER n 
1 215 GLY n 
1 216 ILE n 
1 217 ARG n 
1 218 VAL n 
1 219 ILE n 
1 220 ARG n 
1 221 ALA n 
1 222 PHE n 
1 223 ALA n 
1 224 ARG n 
1 225 GLU n 
1 226 PRO n 
1 227 LEU n 
1 228 GLU n 
1 229 ARG n 
1 230 VAL n 
1 231 ARG n 
1 232 PHE n 
1 233 ALA n 
1 234 GLU n 
1 235 ALA n 
1 236 ASN n 
1 237 GLN n 
1 238 THR n 
1 239 LEU n 
1 240 SER n 
1 241 ASP n 
1 242 SER n 
1 243 ALA n 
1 244 LEU n 
1 245 GLU n 
1 246 ALA n 
1 247 GLY n 
1 248 ARG n 
1 249 TRP n 
1 250 GLN n 
1 251 ALA n 
1 252 LEU n 
1 253 MET n 
1 254 LEU n 
1 255 PRO n 
1 256 VAL n 
1 257 THR n 
1 258 THR n 
1 259 LEU n 
1 260 VAL n 
1 261 ILE n 
1 262 ASN n 
1 263 VAL n 
1 264 SER n 
1 265 SER n 
1 266 VAL n 
1 267 ALA n 
1 268 LEU n 
1 269 ILE n 
1 270 TRP n 
1 271 PHE n 
1 272 GLY n 
1 273 GLY n 
1 274 LEU n 
1 275 ARG n 
1 276 ILE n 
1 277 ASP n 
1 278 ALA n 
1 279 GLY n 
1 280 GLN n 
1 281 MET n 
1 282 GLN n 
1 283 VAL n 
1 284 GLY n 
1 285 SER n 
1 286 LEU n 
1 287 ILE n 
1 288 ALA n 
1 289 PHE n 
1 290 LEU n 
1 291 ALA n 
1 292 TYR n 
1 293 PHE n 
1 294 MET n 
1 295 GLN n 
1 296 ILE n 
1 297 LEU n 
1 298 MET n 
1 299 ALA n 
1 300 VAL n 
1 301 LEU n 
1 302 MET n 
1 303 ALA n 
1 304 THR n 
1 305 PHE n 
1 306 MET n 
1 307 LEU n 
1 308 VAL n 
1 309 ILE n 
1 310 PHE n 
1 311 PRO n 
1 312 ARG n 
1 313 ALA n 
1 314 ALA n 
1 315 VAL n 
1 316 CYS n 
1 317 ALA n 
1 318 ASP n 
1 319 ARG n 
1 320 ILE n 
1 321 GLY n 
1 322 GLU n 
1 323 VAL n 
1 324 LEU n 
1 325 SER n 
1 326 THR n 
1 327 GLN n 
1 328 THR n 
1 329 ALA n 
1 330 ILE n 
1 331 THR n 
1 332 ASN n 
1 333 PRO n 
1 334 ALA n 
1 335 ASP n 
1 336 PRO n 
1 337 VAL n 
1 338 ARG n 
1 339 PRO n 
1 340 ALA n 
1 341 ALA n 
1 342 ILE n 
1 343 ALA n 
1 344 GLY n 
1 345 ASP n 
1 346 ILE n 
1 347 GLY n 
1 348 VAL n 
1 349 HIS n 
1 350 ASP n 
1 351 ALA n 
1 352 THR n 
1 353 PHE n 
1 354 CYS n 
1 355 TYR n 
1 356 PRO n 
1 357 GLY n 
1 358 ALA n 
1 359 ASP n 
1 360 ARG n 
1 361 PRO n 
1 362 VAL n 
1 363 LEU n 
1 364 GLN n 
1 365 ASP n 
1 366 VAL n 
1 367 SER n 
1 368 PHE n 
1 369 THR n 
1 370 VAL n 
1 371 PRO n 
1 372 ARG n 
1 373 GLY n 
1 374 THR n 
1 375 THR n 
1 376 THR n 
1 377 ALA n 
1 378 VAL n 
1 379 VAL n 
1 380 GLY n 
1 381 SER n 
1 382 THR n 
1 383 GLY n 
1 384 SER n 
1 385 GLY n 
1 386 LYS n 
1 387 SER n 
1 388 THR n 
1 389 LEU n 
1 390 ILE n 
1 391 SER n 
1 392 LEU n 
1 393 ILE n 
1 394 CYS n 
1 395 ARG n 
1 396 LEU n 
1 397 TYR n 
1 398 ASP n 
1 399 VAL n 
1 400 THR n 
1 401 SER n 
1 402 GLY n 
1 403 SER n 
1 404 LEU n 
1 405 ARG n 
1 406 ILE n 
1 407 ASP n 
1 408 GLY n 
1 409 VAL n 
1 410 ASP n 
1 411 VAL n 
1 412 ARG n 
1 413 ASP n 
1 414 LEU n 
1 415 ASP n 
1 416 ILE n 
1 417 GLU n 
1 418 GLN n 
1 419 LEU n 
1 420 TRP n 
1 421 SER n 
1 422 ALA n 
1 423 ILE n 
1 424 GLY n 
1 425 LEU n 
1 426 VAL n 
1 427 PRO n 
1 428 GLN n 
1 429 ARG n 
1 430 GLY n 
1 431 TYR n 
1 432 LEU n 
1 433 PHE n 
1 434 SER n 
1 435 GLY n 
1 436 THR n 
1 437 VAL n 
1 438 ALA n 
1 439 GLU n 
1 440 ASN n 
1 441 LEU n 
1 442 ARG n 
1 443 TYR n 
1 444 GLY n 
1 445 ARG n 
1 446 ALA n 
1 447 ASP n 
1 448 ALA n 
1 449 THR n 
1 450 ASP n 
1 451 ASP n 
1 452 GLU n 
1 453 MET n 
1 454 TRP n 
1 455 GLU n 
1 456 ALA n 
1 457 LEU n 
1 458 ARG n 
1 459 VAL n 
1 460 ALA n 
1 461 ALA n 
1 462 ALA n 
1 463 ALA n 
1 464 ASP n 
1 465 PHE n 
1 466 VAL n 
1 467 ARG n 
1 468 ALA n 
1 469 HIS n 
1 470 PRO n 
1 471 GLN n 
1 472 GLY n 
1 473 LEU n 
1 474 ASP n 
1 475 MET n 
1 476 PRO n 
1 477 VAL n 
1 478 ALA n 
1 479 GLN n 
1 480 GLY n 
1 481 GLY n 
1 482 ILE n 
1 483 ASN n 
1 484 PHE n 
1 485 SER n 
1 486 GLY n 
1 487 GLY n 
1 488 GLN n 
1 489 ARG n 
1 490 GLN n 
1 491 ARG n 
1 492 LEU n 
1 493 ALA n 
1 494 ILE n 
1 495 ALA n 
1 496 ARG n 
1 497 ALA n 
1 498 VAL n 
1 499 ILE n 
1 500 ARG n 
1 501 ARG n 
1 502 PRO n 
1 503 ALA n 
1 504 ILE n 
1 505 TYR n 
1 506 LEU n 
1 507 PHE n 
1 508 ASP n 
1 509 ASP n 
1 510 ALA n 
1 511 PHE n 
1 512 SER n 
1 513 ALA n 
1 514 LEU n 
1 515 ASP n 
1 516 VAL n 
1 517 HIS n 
1 518 THR n 
1 519 ASP n 
1 520 ALA n 
1 521 ARG n 
1 522 VAL n 
1 523 ARG n 
1 524 ASP n 
1 525 ALA n 
1 526 LEU n 
1 527 ARG n 
1 528 GLU n 
1 529 VAL n 
1 530 ALA n 
1 531 ALA n 
1 532 ASP n 
1 533 ALA n 
1 534 THR n 
1 535 VAL n 
1 536 VAL n 
1 537 ILE n 
1 538 VAL n 
1 539 SER n 
1 540 GLN n 
1 541 ARG n 
1 542 ILE n 
1 543 SER n 
1 544 THR n 
1 545 VAL n 
1 546 ILE n 
1 547 GLU n 
1 548 ALA n 
1 549 ASP n 
1 550 GLN n 
1 551 VAL n 
1 552 VAL n 
1 553 VAL n 
1 554 ILE n 
1 555 ASP n 
1 556 ASP n 
1 557 GLY n 
1 558 ARG n 
1 559 VAL n 
1 560 VAL n 
1 561 GLY n 
1 562 ILE n 
1 563 GLY n 
1 564 THR n 
1 565 HIS n 
1 566 ASP n 
1 567 THR n 
1 568 LEU n 
1 569 LEU n 
1 570 ALA n 
1 571 ASP n 
1 572 CYS n 
1 573 PRO n 
1 574 ILE n 
1 575 TYR n 
1 576 ALA n 
1 577 GLU n 
1 578 PHE n 
1 579 ALA n 
1 580 GLU n 
1 581 SER n 
1 582 GLN n 
1 583 ALA n 
1 584 LEU n 
1 585 THR n 
1 586 ALA n 
1 587 GLY n 
1 588 GLU n 
1 589 PRO n 
1 590 ARG n 
2 1   MET n 
2 2   ARG n 
2 3   ARG n 
2 4   GLY n 
2 5   ALA n 
2 6   LEU n 
2 7   PRO n 
2 8   GLN n 
2 9   ALA n 
2 10  PRO n 
2 11  LEU n 
2 12  GLU n 
2 13  ARG n 
2 14  THR n 
2 15  ARG n 
2 16  ASP n 
2 17  PHE n 
2 18  LYS n 
2 19  GLY n 
2 20  SER n 
2 21  ALA n 
2 22  ILE n 
2 23  ARG n 
2 24  LEU n 
2 25  ALA n 
2 26  ARG n 
2 27  ARG n 
2 28  LEU n 
2 29  LEU n 
2 30  PRO n 
2 31  GLN n 
2 32  ARG n 
2 33  ALA n 
2 34  LEU n 
2 35  THR n 
2 36  LEU n 
2 37  ALA n 
2 38  VAL n 
2 39  ILE n 
2 40  LEU n 
2 41  LEU n 
2 42  GLY n 
2 43  VAL n 
2 44  GLY n 
2 45  GLY n 
2 46  ILE n 
2 47  ALA n 
2 48  ILE n 
2 49  GLY n 
2 50  VAL n 
2 51  ILE n 
2 52  GLY n 
2 53  PRO n 
2 54  ARG n 
2 55  ILE n 
2 56  LEU n 
2 57  GLY n 
2 58  HIS n 
2 59  ALA n 
2 60  THR n 
2 61  ASP n 
2 62  LEU n 
2 63  LEU n 
2 64  PHE n 
2 65  ASN n 
2 66  GLY n 
2 67  VAL n 
2 68  ILE n 
2 69  GLY n 
2 70  ARG n 
2 71  GLU n 
2 72  LEU n 
2 73  PRO n 
2 74  ALA n 
2 75  GLY n 
2 76  LEU n 
2 77  THR n 
2 78  LYS n 
2 79  GLU n 
2 80  GLN n 
2 81  ALA n 
2 82  VAL n 
2 83  GLU n 
2 84  ALA n 
2 85  ALA n 
2 86  ARG n 
2 87  ALA n 
2 88  ARG n 
2 89  GLY n 
2 90  ASP n 
2 91  GLY n 
2 92  THR n 
2 93  PHE n 
2 94  ALA n 
2 95  ASP n 
2 96  LEU n 
2 97  LEU n 
2 98  SER n 
2 99  GLY n 
2 100 MET n 
2 101 ASP n 
2 102 ILE n 
2 103 VAL n 
2 104 PRO n 
2 105 GLY n 
2 106 GLN n 
2 107 GLY n 
2 108 VAL n 
2 109 ASP n 
2 110 PHE n 
2 111 GLY n 
2 112 ALA n 
2 113 VAL n 
2 114 GLY n 
2 115 ARG n 
2 116 THR n 
2 117 LEU n 
2 118 ALA n 
2 119 LEU n 
2 120 ALA n 
2 121 LEU n 
2 122 GLY n 
2 123 LEU n 
2 124 TYR n 
2 125 LEU n 
2 126 VAL n 
2 127 ALA n 
2 128 ALA n 
2 129 LEU n 
2 130 LEU n 
2 131 VAL n 
2 132 TRP n 
2 133 VAL n 
2 134 GLN n 
2 135 ALA n 
2 136 ARG n 
2 137 LEU n 
2 138 LEU n 
2 139 ASN n 
2 140 VAL n 
2 141 THR n 
2 142 VAL n 
2 143 GLN n 
2 144 ARG n 
2 145 THR n 
2 146 MET n 
2 147 VAL n 
2 148 ALA n 
2 149 LEU n 
2 150 ARG n 
2 151 ALA n 
2 152 GLU n 
2 153 VAL n 
2 154 GLN n 
2 155 GLU n 
2 156 LYS n 
2 157 ILE n 
2 158 HIS n 
2 159 ARG n 
2 160 LEU n 
2 161 PRO n 
2 162 LEU n 
2 163 SER n 
2 164 TYR n 
2 165 PHE n 
2 166 ASP n 
2 167 SER n 
2 168 ARG n 
2 169 GLN n 
2 170 ARG n 
2 171 GLY n 
2 172 GLU n 
2 173 VAL n 
2 174 LEU n 
2 175 SER n 
2 176 ARG n 
2 177 VAL n 
2 178 THR n 
2 179 ASN n 
2 180 ASP n 
2 181 VAL n 
2 182 ASP n 
2 183 ASN n 
2 184 ILE n 
2 185 GLN n 
2 186 ASN n 
2 187 SER n 
2 188 VAL n 
2 189 SER n 
2 190 MET n 
2 191 THR n 
2 192 ILE n 
2 193 SER n 
2 194 GLN n 
2 195 LEU n 
2 196 LEU n 
2 197 THR n 
2 198 SER n 
2 199 VAL n 
2 200 LEU n 
2 201 THR n 
2 202 VAL n 
2 203 PHE n 
2 204 ALA n 
2 205 VAL n 
2 206 LEU n 
2 207 VAL n 
2 208 MET n 
2 209 MET n 
2 210 LEU n 
2 211 THR n 
2 212 ILE n 
2 213 SER n 
2 214 PRO n 
2 215 LEU n 
2 216 LEU n 
2 217 THR n 
2 218 LEU n 
2 219 PHE n 
2 220 THR n 
2 221 VAL n 
2 222 VAL n 
2 223 THR n 
2 224 VAL n 
2 225 PRO n 
2 226 ALA n 
2 227 SER n 
2 228 LEU n 
2 229 TRP n 
2 230 VAL n 
2 231 THR n 
2 232 ARG n 
2 233 TRP n 
2 234 ILE n 
2 235 THR n 
2 236 ARG n 
2 237 ARG n 
2 238 SER n 
2 239 GLN n 
2 240 PRO n 
2 241 LEU n 
2 242 PHE n 
2 243 VAL n 
2 244 ALA n 
2 245 GLN n 
2 246 TRP n 
2 247 ARG n 
2 248 ASN n 
2 249 THR n 
2 250 GLY n 
2 251 ARG n 
2 252 LEU n 
2 253 ALA n 
2 254 ALA n 
2 255 HIS n 
2 256 LEU n 
2 257 GLU n 
2 258 GLU n 
2 259 THR n 
2 260 TYR n 
2 261 SER n 
2 262 GLY n 
2 263 PHE n 
2 264 THR n 
2 265 ILE n 
2 266 VAL n 
2 267 LYS n 
2 268 THR n 
2 269 PHE n 
2 270 GLY n 
2 271 HIS n 
2 272 ARG n 
2 273 GLU n 
2 274 ALA n 
2 275 ALA n 
2 276 ALA n 
2 277 GLY n 
2 278 LYS n 
2 279 PHE n 
2 280 ALA n 
2 281 GLU n 
2 282 LEU n 
2 283 ASN n 
2 284 SER n 
2 285 GLU n 
2 286 THR n 
2 287 GLN n 
2 288 GLN n 
2 289 SER n 
2 290 SER n 
2 291 PHE n 
2 292 GLY n 
2 293 ALA n 
2 294 GLN n 
2 295 PHE n 
2 296 PHE n 
2 297 SER n 
2 298 GLY n 
2 299 LEU n 
2 300 VAL n 
2 301 SER n 
2 302 PRO n 
2 303 ALA n 
2 304 THR n 
2 305 MET n 
2 306 PHE n 
2 307 ILE n 
2 308 GLY n 
2 309 ASN n 
2 310 LEU n 
2 311 SER n 
2 312 TYR n 
2 313 VAL n 
2 314 ALA n 
2 315 VAL n 
2 316 ALA n 
2 317 VAL n 
2 318 VAL n 
2 319 GLY n 
2 320 GLY n 
2 321 LEU n 
2 322 GLN n 
2 323 VAL n 
2 324 ALA n 
2 325 THR n 
2 326 GLY n 
2 327 GLN n 
2 328 ILE n 
2 329 THR n 
2 330 LEU n 
2 331 GLY n 
2 332 SER n 
2 333 ILE n 
2 334 GLN n 
2 335 ALA n 
2 336 PHE n 
2 337 ILE n 
2 338 GLN n 
2 339 TYR n 
2 340 VAL n 
2 341 ARG n 
2 342 GLN n 
2 343 PHE n 
2 344 ASN n 
2 345 GLN n 
2 346 PRO n 
2 347 LEU n 
2 348 THR n 
2 349 GLN n 
2 350 VAL n 
2 351 ALA n 
2 352 GLY n 
2 353 MET n 
2 354 TYR n 
2 355 ASN n 
2 356 THR n 
2 357 LEU n 
2 358 GLN n 
2 359 SER n 
2 360 GLY n 
2 361 ILE n 
2 362 ALA n 
2 363 SER n 
2 364 ALA n 
2 365 GLU n 
2 366 ARG n 
2 367 VAL n 
2 368 PHE n 
2 369 ASP n 
2 370 LEU n 
2 371 LEU n 
2 372 ASP n 
2 373 THR n 
2 374 GLU n 
2 375 GLU n 
2 376 GLU n 
2 377 SER n 
2 378 ALA n 
2 379 ASP n 
2 380 SER n 
2 381 PRO n 
2 382 ARG n 
2 383 ARG n 
2 384 ALA n 
2 385 ASP n 
2 386 VAL n 
2 387 ARG n 
2 388 THR n 
2 389 GLY n 
2 390 ARG n 
2 391 VAL n 
2 392 GLU n 
2 393 PHE n 
2 394 GLU n 
2 395 HIS n 
2 396 VAL n 
2 397 SER n 
2 398 PHE n 
2 399 SER n 
2 400 TYR n 
2 401 VAL n 
2 402 PRO n 
2 403 GLY n 
2 404 THR n 
2 405 PRO n 
2 406 VAL n 
2 407 ILE n 
2 408 GLU n 
2 409 ASP n 
2 410 LEU n 
2 411 SER n 
2 412 LEU n 
2 413 VAL n 
2 414 ALA n 
2 415 GLU n 
2 416 PRO n 
2 417 GLY n 
2 418 SER n 
2 419 THR n 
2 420 VAL n 
2 421 ALA n 
2 422 ILE n 
2 423 VAL n 
2 424 GLY n 
2 425 PRO n 
2 426 THR n 
2 427 GLY n 
2 428 ALA n 
2 429 GLY n 
2 430 LYS n 
2 431 THR n 
2 432 THR n 
2 433 LEU n 
2 434 VAL n 
2 435 ASN n 
2 436 LEU n 
2 437 LEU n 
2 438 MET n 
2 439 ARG n 
2 440 PHE n 
2 441 TYR n 
2 442 ASP n 
2 443 VAL n 
2 444 ASP n 
2 445 SER n 
2 446 GLY n 
2 447 ARG n 
2 448 ILE n 
2 449 THR n 
2 450 ILE n 
2 451 ASP n 
2 452 GLY n 
2 453 VAL n 
2 454 ASP n 
2 455 ILE n 
2 456 ALA n 
2 457 SER n 
2 458 VAL n 
2 459 SER n 
2 460 ARG n 
2 461 GLU n 
2 462 SER n 
2 463 LEU n 
2 464 ARG n 
2 465 ALA n 
2 466 SER n 
2 467 ILE n 
2 468 GLY n 
2 469 MET n 
2 470 VAL n 
2 471 LEU n 
2 472 GLN n 
2 473 ASP n 
2 474 THR n 
2 475 TRP n 
2 476 LEU n 
2 477 PHE n 
2 478 ALA n 
2 479 GLY n 
2 480 THR n 
2 481 ILE n 
2 482 TYR n 
2 483 ASP n 
2 484 ASN n 
2 485 ILE n 
2 486 ALA n 
2 487 TYR n 
2 488 GLY n 
2 489 ARG n 
2 490 PRO n 
2 491 ASP n 
2 492 ALA n 
2 493 ASP n 
2 494 GLU n 
2 495 ASP n 
2 496 GLU n 
2 497 VAL n 
2 498 ILE n 
2 499 GLU n 
2 500 ALA n 
2 501 ALA n 
2 502 THR n 
2 503 ALA n 
2 504 ALA n 
2 505 TYR n 
2 506 VAL n 
2 507 ASP n 
2 508 ARG n 
2 509 PHE n 
2 510 VAL n 
2 511 HIS n 
2 512 THR n 
2 513 LEU n 
2 514 PRO n 
2 515 ASN n 
2 516 GLY n 
2 517 TYR n 
2 518 ASP n 
2 519 THR n 
2 520 ARG n 
2 521 VAL n 
2 522 ASP n 
2 523 ASP n 
2 524 ASP n 
2 525 GLY n 
2 526 GLY n 
2 527 ALA n 
2 528 ILE n 
2 529 SER n 
2 530 ALA n 
2 531 GLY n 
2 532 GLU n 
2 533 LYS n 
2 534 GLN n 
2 535 LEU n 
2 536 ILE n 
2 537 THR n 
2 538 ILE n 
2 539 ALA n 
2 540 ARG n 
2 541 ALA n 
2 542 VAL n 
2 543 LEU n 
2 544 ALA n 
2 545 ARG n 
2 546 PRO n 
2 547 LYS n 
2 548 LEU n 
2 549 LEU n 
2 550 VAL n 
2 551 LEU n 
2 552 ASP n 
2 553 GLU n 
2 554 ALA n 
2 555 THR n 
2 556 SER n 
2 557 SER n 
2 558 VAL n 
2 559 ASP n 
2 560 THR n 
2 561 ARG n 
2 562 THR n 
2 563 GLU n 
2 564 LEU n 
2 565 LEU n 
2 566 ILE n 
2 567 ALA n 
2 568 HIS n 
2 569 ALA n 
2 570 MET n 
2 571 ALA n 
2 572 GLU n 
2 573 LEU n 
2 574 ARG n 
2 575 ARG n 
2 576 ASP n 
2 577 ARG n 
2 578 THR n 
2 579 SER n 
2 580 PHE n 
2 581 ILE n 
2 582 ILE n 
2 583 ALA n 
2 584 HIS n 
2 585 ARG n 
2 586 LEU n 
2 587 SER n 
2 588 THR n 
2 589 ILE n 
2 590 ARG n 
2 591 ASP n 
2 592 ALA n 
2 593 ASP n 
2 594 LEU n 
2 595 ILE n 
2 596 LEU n 
2 597 VAL n 
2 598 MET n 
2 599 ASP n 
2 600 SER n 
2 601 GLY n 
2 602 ARG n 
2 603 ILE n 
2 604 ILE n 
2 605 GLU n 
2 606 ARG n 
2 607 GLY n 
2 608 THR n 
2 609 HIS n 
2 610 GLU n 
2 611 GLU n 
2 612 LEU n 
2 613 LEU n 
2 614 ALA n 
2 615 ARG n 
2 616 HIS n 
2 617 GLY n 
2 618 ARG n 
2 619 TYR n 
2 620 TRP n 
2 621 GLU n 
2 622 MET n 
2 623 THR n 
2 624 ARG n 
2 625 VAL n 
2 626 HIS n 
2 627 LEU n 
2 628 GLY n 
2 629 GLY n 
2 630 ILE n 
2 631 LYS n 
2 632 ALA n 
2 633 PHE n 
2 634 HIS n 
2 635 HIS n 
2 636 HIS n 
2 637 HIS n 
2 638 HIS n 
2 639 HIS n 
2 640 HIS n 
2 641 HIS n 
2 642 HIS n 
2 643 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 590 ? ? MSMEG_5008               ? ? ? ? ? ? 'Mycolicibacterium smegmatis MC2 155' 246196 ? ? ? 
? ? ? ? ? 'Mycolicibacterium smegmatis MC2 155' 246196 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 643 ? ? 'MSMEI_4882, MSMEG_5009' ? ? ? ? ? ? 'Mycolicibacterium smegmatis MC2 155' 246196 ? ? ? 
? ? ? ? ? 'Mycolicibacterium smegmatis MC2 155' 246196 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
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 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
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  
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 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
VO4 non-polymer         . 'VANADATE ION'              ? 'O4 V -3'           114.939 
# 
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   -11 ?   ?   ?   A . n 
A 1 2   PRO 2   -10 ?   ?   ?   A . n 
A 1 3   GLU 3   -9  ?   ?   ?   A . n 
A 1 4   VAL 4   -8  ?   ?   ?   A . n 
A 1 5   VAL 5   -7  ?   ?   ?   A . n 
A 1 6   GLY 6   -6  ?   ?   ?   A . n 
A 1 7   SER 7   -5  ?   ?   ?   A . n 
A 1 8   TYR 8   -4  ?   ?   ?   A . n 
A 1 9   PHE 9   -3  ?   ?   ?   A . n 
A 1 10  GLN 10  -2  -2  GLN GLN A . n 
A 1 11  SER 11  -1  -1  SER SER A . n 
A 1 12  ASN 12  0   0   ASN ASN A . n 
A 1 13  MET 13  1   1   MET MET A . n 
A 1 14  LEU 14  2   2   LEU LEU A . n 
A 1 15  TRP 15  3   3   TRP TRP A . n 
A 1 16  ALA 16  4   4   ALA ALA A . n 
A 1 17  LEU 17  5   5   LEU LEU A . n 
A 1 18  LEU 18  6   6   LEU LEU A . n 
A 1 19  ARG 19  7   7   ARG ARG A . n 
A 1 20  GLN 20  8   8   GLN GLN A . n 
A 1 21  TYR 21  9   9   TYR TYR A . n 
A 1 22  VAL 22  10  10  VAL VAL A . n 
A 1 23  ARG 23  11  11  ARG ARG A . n 
A 1 24  PRO 24  12  12  PRO PRO A . n 
A 1 25  TYR 25  13  13  TYR TYR A . n 
A 1 26  ARG 26  14  14  ARG ARG A . n 
A 1 27  TRP 27  15  15  TRP TRP A . n 
A 1 28  LEU 28  16  16  LEU LEU A . n 
A 1 29  LEU 29  17  17  LEU LEU A . n 
A 1 30  ALA 30  18  18  ALA ALA A . n 
A 1 31  VAL 31  19  19  VAL VAL A . n 
A 1 32  VAL 32  20  20  VAL VAL A . n 
A 1 33  ALA 33  21  21  ALA ALA A . n 
A 1 34  VAL 34  22  22  VAL VAL A . n 
A 1 35  LEU 35  23  23  LEU LEU A . n 
A 1 36  GLN 36  24  24  GLN GLN A . n 
A 1 37  VAL 37  25  25  VAL VAL A . n 
A 1 38  ILE 38  26  26  ILE ILE A . n 
A 1 39  SER 39  27  27  SER SER A . n 
A 1 40  ASN 40  28  28  ASN ASN A . n 
A 1 41  MET 41  29  29  MET MET A . n 
A 1 42  ALA 42  30  30  ALA ALA A . n 
A 1 43  SER 43  31  31  SER SER A . n 
A 1 44  LEU 44  32  32  LEU LEU A . n 
A 1 45  TYR 45  33  33  TYR TYR A . n 
A 1 46  LEU 46  34  34  LEU LEU A . n 
A 1 47  PRO 47  35  35  PRO PRO A . n 
A 1 48  THR 48  36  36  THR THR A . n 
A 1 49  VAL 49  37  37  VAL VAL A . n 
A 1 50  ASN 50  38  38  ASN ASN A . n 
A 1 51  ALA 51  39  39  ALA ALA A . n 
A 1 52  ALA 52  40  40  ALA ALA A . n 
A 1 53  ILE 53  41  41  ILE ILE A . n 
A 1 54  ILE 54  42  42  ILE ILE A . n 
A 1 55  ASP 55  43  43  ASP ASP A . n 
A 1 56  ASP 56  44  44  ASP ASP A . n 
A 1 57  GLY 57  45  45  GLY GLY A . n 
A 1 58  VAL 58  46  46  VAL VAL A . n 
A 1 59  ALA 59  47  47  ALA ALA A . n 
A 1 60  LYS 60  48  48  LYS LYS A . n 
A 1 61  GLY 61  49  49  GLY GLY A . n 
A 1 62  ASP 62  50  50  ASP ASP A . n 
A 1 63  THR 63  51  51  THR THR A . n 
A 1 64  ALA 64  52  52  ALA ALA A . n 
A 1 65  ARG 65  53  53  ARG ARG A . n 
A 1 66  ILE 66  54  54  ILE ILE A . n 
A 1 67  VAL 67  55  55  VAL VAL A . n 
A 1 68  GLU 68  56  56  GLU GLU A . n 
A 1 69  LEU 69  57  57  LEU LEU A . n 
A 1 70  GLY 70  58  58  GLY GLY A . n 
A 1 71  ALA 71  59  59  ALA ALA A . n 
A 1 72  VAL 72  60  60  VAL VAL A . n 
A 1 73  MET 73  61  61  MET MET A . n 
A 1 74  LEU 74  62  62  LEU LEU A . n 
A 1 75  GLY 75  63  63  GLY GLY A . n 
A 1 76  VAL 76  64  64  VAL VAL A . n 
A 1 77  THR 77  65  65  THR THR A . n 
A 1 78  ALA 78  66  66  ALA ALA A . n 
A 1 79  LEU 79  67  67  LEU LEU A . n 
A 1 80  GLN 80  68  68  GLN GLN A . n 
A 1 81  VAL 81  69  69  VAL VAL A . n 
A 1 82  VAL 82  70  70  VAL VAL A . n 
A 1 83  CYS 83  71  71  CYS CYS A . n 
A 1 84  ALA 84  72  72  ALA ALA A . n 
A 1 85  VAL 85  73  73  VAL VAL A . n 
A 1 86  GLY 86  74  74  GLY GLY A . n 
A 1 87  ALA 87  75  75  ALA ALA A . n 
A 1 88  VAL 88  76  76  VAL VAL A . n 
A 1 89  PHE 89  77  77  PHE PHE A . n 
A 1 90  PHE 90  78  78  PHE PHE A . n 
A 1 91  GLY 91  79  79  GLY GLY A . n 
A 1 92  ALA 92  80  80  ALA ALA A . n 
A 1 93  ARG 93  81  81  ARG ARG A . n 
A 1 94  ALA 94  82  82  ALA ALA A . n 
A 1 95  ALA 95  83  83  ALA ALA A . n 
A 1 96  THR 96  84  84  THR THR A . n 
A 1 97  GLY 97  85  85  GLY GLY A . n 
A 1 98  PHE 98  86  86  PHE PHE A . n 
A 1 99  GLY 99  87  87  GLY GLY A . n 
A 1 100 HIS 100 88  88  HIS HIS A . n 
A 1 101 ASP 101 89  89  ASP ASP A . n 
A 1 102 LEU 102 90  90  LEU LEU A . n 
A 1 103 ARG 103 91  91  ARG ARG A . n 
A 1 104 ALA 104 92  92  ALA ALA A . n 
A 1 105 ALA 105 93  93  ALA ALA A . n 
A 1 106 VAL 106 94  94  VAL VAL A . n 
A 1 107 PHE 107 95  95  PHE PHE A . n 
A 1 108 THR 108 96  96  THR THR A . n 
A 1 109 HIS 109 97  97  HIS HIS A . n 
A 1 110 VAL 110 98  98  VAL VAL A . n 
A 1 111 THR 111 99  99  THR THR A . n 
A 1 112 THR 112 100 100 THR THR A . n 
A 1 113 PHE 113 101 101 PHE PHE A . n 
A 1 114 SER 114 102 102 SER SER A . n 
A 1 115 ALA 115 103 103 ALA ALA A . n 
A 1 116 GLU 116 104 104 GLU GLU A . n 
A 1 117 GLU 117 105 105 GLU GLU A . n 
A 1 118 ALA 118 106 106 ALA ALA A . n 
A 1 119 GLY 119 107 107 GLY GLY A . n 
A 1 120 ARG 120 108 108 ARG ARG A . n 
A 1 121 PHE 121 109 109 PHE PHE A . n 
A 1 122 GLY 122 110 110 GLY GLY A . n 
A 1 123 ALA 123 111 111 ALA ALA A . n 
A 1 124 ALA 124 112 112 ALA ALA A . n 
A 1 125 SER 125 113 113 SER SER A . n 
A 1 126 LEU 126 114 114 LEU LEU A . n 
A 1 127 LEU 127 115 115 LEU LEU A . n 
A 1 128 THR 128 116 116 THR THR A . n 
A 1 129 ARG 129 117 117 ARG ARG A . n 
A 1 130 THR 130 118 118 THR THR A . n 
A 1 131 THR 131 119 119 THR THR A . n 
A 1 132 ASN 132 120 120 ASN ASN A . n 
A 1 133 ASP 133 121 121 ASP ASP A . n 
A 1 134 VAL 134 122 122 VAL VAL A . n 
A 1 135 GLY 135 123 123 GLY GLY A . n 
A 1 136 HIS 136 124 124 HIS HIS A . n 
A 1 137 ILE 137 125 125 ILE ILE A . n 
A 1 138 GLN 138 126 126 GLN GLN A . n 
A 1 139 GLN 139 127 127 GLN GLN A . n 
A 1 140 LEU 140 128 128 LEU LEU A . n 
A 1 141 VAL 141 129 129 VAL VAL A . n 
A 1 142 GLN 142 130 130 GLN GLN A . n 
A 1 143 LEU 143 131 131 LEU LEU A . n 
A 1 144 THR 144 132 132 THR THR A . n 
A 1 145 VAL 145 133 133 VAL VAL A . n 
A 1 146 THR 146 134 134 THR THR A . n 
A 1 147 MET 147 135 135 MET MET A . n 
A 1 148 LEU 148 136 136 LEU LEU A . n 
A 1 149 ILE 149 137 137 ILE ILE A . n 
A 1 150 THR 150 138 138 THR THR A . n 
A 1 151 ALA 151 139 139 ALA ALA A . n 
A 1 152 PRO 152 140 140 PRO PRO A . n 
A 1 153 ILE 153 141 141 ILE ILE A . n 
A 1 154 MET 154 142 142 MET MET A . n 
A 1 155 SER 155 143 143 SER SER A . n 
A 1 156 ILE 156 144 144 ILE ILE A . n 
A 1 157 GLY 157 145 145 GLY GLY A . n 
A 1 158 GLY 158 146 146 GLY GLY A . n 
A 1 159 ILE 159 147 147 ILE ILE A . n 
A 1 160 PHE 160 148 148 PHE PHE A . n 
A 1 161 MET 161 149 149 MET MET A . n 
A 1 162 ALA 162 150 150 ALA ALA A . n 
A 1 163 LEU 163 151 151 LEU LEU A . n 
A 1 164 HIS 164 152 152 HIS HIS A . n 
A 1 165 GLN 165 153 153 GLN GLN A . n 
A 1 166 ASP 166 154 154 ASP ASP A . n 
A 1 167 ALA 167 155 155 ALA ALA A . n 
A 1 168 GLY 168 156 156 GLY GLY A . n 
A 1 169 LEU 169 157 157 LEU LEU A . n 
A 1 170 SER 170 158 158 SER SER A . n 
A 1 171 TRP 171 159 159 TRP TRP A . n 
A 1 172 LEU 172 160 160 LEU LEU A . n 
A 1 173 LEU 173 161 161 LEU LEU A . n 
A 1 174 LEU 174 162 162 LEU LEU A . n 
A 1 175 VAL 175 163 163 VAL VAL A . n 
A 1 176 SER 176 164 164 SER SER A . n 
A 1 177 VAL 177 165 165 VAL VAL A . n 
A 1 178 PRO 178 166 166 PRO PRO A . n 
A 1 179 VAL 179 167 167 VAL VAL A . n 
A 1 180 LEU 180 168 168 LEU LEU A . n 
A 1 181 GLY 181 169 169 GLY GLY A . n 
A 1 182 LEU 182 170 170 LEU LEU A . n 
A 1 183 ALA 183 171 171 ALA ALA A . n 
A 1 184 ASN 184 172 172 ASN ASN A . n 
A 1 185 TYR 185 173 173 TYR TYR A . n 
A 1 186 TRP 186 174 174 TRP TRP A . n 
A 1 187 ILE 187 175 175 ILE ILE A . n 
A 1 188 ILE 188 176 176 ILE ILE A . n 
A 1 189 ARG 189 177 177 ARG ARG A . n 
A 1 190 HIS 190 178 178 HIS HIS A . n 
A 1 191 LEU 191 179 179 LEU LEU A . n 
A 1 192 MET 192 180 180 MET MET A . n 
A 1 193 PRO 193 181 181 PRO PRO A . n 
A 1 194 VAL 194 182 182 VAL VAL A . n 
A 1 195 PHE 195 183 183 PHE PHE A . n 
A 1 196 THR 196 184 184 THR THR A . n 
A 1 197 ARG 197 185 185 ARG ARG A . n 
A 1 198 MET 198 186 186 MET MET A . n 
A 1 199 GLN 199 187 187 GLN GLN A . n 
A 1 200 SER 200 188 188 SER SER A . n 
A 1 201 LEU 201 189 189 LEU LEU A . n 
A 1 202 ILE 202 190 190 ILE ILE A . n 
A 1 203 ASP 203 191 191 ASP ASP A . n 
A 1 204 GLY 204 192 192 GLY GLY A . n 
A 1 205 ILE 205 193 193 ILE ILE A . n 
A 1 206 ASN 206 194 194 ASN ASN A . n 
A 1 207 ARG 207 195 195 ARG ARG A . n 
A 1 208 VAL 208 196 196 VAL VAL A . n 
A 1 209 LEU 209 197 197 LEU LEU A . n 
A 1 210 ARG 210 198 198 ARG ARG A . n 
A 1 211 ASP 211 199 199 ASP ASP A . n 
A 1 212 GLN 212 200 200 GLN GLN A . n 
A 1 213 LEU 213 201 201 LEU LEU A . n 
A 1 214 SER 214 202 202 SER SER A . n 
A 1 215 GLY 215 203 203 GLY GLY A . n 
A 1 216 ILE 216 204 204 ILE ILE A . n 
A 1 217 ARG 217 205 205 ARG ARG A . n 
A 1 218 VAL 218 206 206 VAL VAL A . n 
A 1 219 ILE 219 207 207 ILE ILE A . n 
A 1 220 ARG 220 208 208 ARG ARG A . n 
A 1 221 ALA 221 209 209 ALA ALA A . n 
A 1 222 PHE 222 210 210 PHE PHE A . n 
A 1 223 ALA 223 211 211 ALA ALA A . n 
A 1 224 ARG 224 212 212 ARG ARG A . n 
A 1 225 GLU 225 213 213 GLU GLU A . n 
A 1 226 PRO 226 214 214 PRO PRO A . n 
A 1 227 LEU 227 215 215 LEU LEU A . n 
A 1 228 GLU 228 216 216 GLU GLU A . n 
A 1 229 ARG 229 217 217 ARG ARG A . n 
A 1 230 VAL 230 218 218 VAL VAL A . n 
A 1 231 ARG 231 219 219 ARG ARG A . n 
A 1 232 PHE 232 220 220 PHE PHE A . n 
A 1 233 ALA 233 221 221 ALA ALA A . n 
A 1 234 GLU 234 222 222 GLU GLU A . n 
A 1 235 ALA 235 223 223 ALA ALA A . n 
A 1 236 ASN 236 224 224 ASN ASN A . n 
A 1 237 GLN 237 225 225 GLN GLN A . n 
A 1 238 THR 238 226 226 THR THR A . n 
A 1 239 LEU 239 227 227 LEU LEU A . n 
A 1 240 SER 240 228 228 SER SER A . n 
A 1 241 ASP 241 229 229 ASP ASP A . n 
A 1 242 SER 242 230 230 SER SER A . n 
A 1 243 ALA 243 231 231 ALA ALA A . n 
A 1 244 LEU 244 232 232 LEU LEU A . n 
A 1 245 GLU 245 233 233 GLU GLU A . n 
A 1 246 ALA 246 234 234 ALA ALA A . n 
A 1 247 GLY 247 235 235 GLY GLY A . n 
A 1 248 ARG 248 236 236 ARG ARG A . n 
A 1 249 TRP 249 237 237 TRP TRP A . n 
A 1 250 GLN 250 238 238 GLN GLN A . n 
A 1 251 ALA 251 239 239 ALA ALA A . n 
A 1 252 LEU 252 240 240 LEU LEU A . n 
A 1 253 MET 253 241 241 MET MET A . n 
A 1 254 LEU 254 242 242 LEU LEU A . n 
A 1 255 PRO 255 243 243 PRO PRO A . n 
A 1 256 VAL 256 244 244 VAL VAL A . n 
A 1 257 THR 257 245 245 THR THR A . n 
A 1 258 THR 258 246 246 THR THR A . n 
A 1 259 LEU 259 247 247 LEU LEU A . n 
A 1 260 VAL 260 248 248 VAL VAL A . n 
A 1 261 ILE 261 249 249 ILE ILE A . n 
A 1 262 ASN 262 250 250 ASN ASN A . n 
A 1 263 VAL 263 251 251 VAL VAL A . n 
A 1 264 SER 264 252 252 SER SER A . n 
A 1 265 SER 265 253 253 SER SER A . n 
A 1 266 VAL 266 254 254 VAL VAL A . n 
A 1 267 ALA 267 255 255 ALA ALA A . n 
A 1 268 LEU 268 256 256 LEU LEU A . n 
A 1 269 ILE 269 257 257 ILE ILE A . n 
A 1 270 TRP 270 258 258 TRP TRP A . n 
A 1 271 PHE 271 259 259 PHE PHE A . n 
A 1 272 GLY 272 260 260 GLY GLY A . n 
A 1 273 GLY 273 261 261 GLY GLY A . n 
A 1 274 LEU 274 262 262 LEU LEU A . n 
A 1 275 ARG 275 263 263 ARG ARG A . n 
A 1 276 ILE 276 264 264 ILE ILE A . n 
A 1 277 ASP 277 265 265 ASP ASP A . n 
A 1 278 ALA 278 266 266 ALA ALA A . n 
A 1 279 GLY 279 267 267 GLY GLY A . n 
A 1 280 GLN 280 268 268 GLN GLN A . n 
A 1 281 MET 281 269 269 MET MET A . n 
A 1 282 GLN 282 270 270 GLN GLN A . n 
A 1 283 VAL 283 271 271 VAL VAL A . n 
A 1 284 GLY 284 272 272 GLY GLY A . n 
A 1 285 SER 285 273 273 SER SER A . n 
A 1 286 LEU 286 274 274 LEU LEU A . n 
A 1 287 ILE 287 275 275 ILE ILE A . n 
A 1 288 ALA 288 276 276 ALA ALA A . n 
A 1 289 PHE 289 277 277 PHE PHE A . n 
A 1 290 LEU 290 278 278 LEU LEU A . n 
A 1 291 ALA 291 279 279 ALA ALA A . n 
A 1 292 TYR 292 280 280 TYR TYR A . n 
A 1 293 PHE 293 281 281 PHE PHE A . n 
A 1 294 MET 294 282 282 MET MET A . n 
A 1 295 GLN 295 283 283 GLN GLN A . n 
A 1 296 ILE 296 284 284 ILE ILE A . n 
A 1 297 LEU 297 285 285 LEU LEU A . n 
A 1 298 MET 298 286 286 MET MET A . n 
A 1 299 ALA 299 287 287 ALA ALA A . n 
A 1 300 VAL 300 288 288 VAL VAL A . n 
A 1 301 LEU 301 289 289 LEU LEU A . n 
A 1 302 MET 302 290 290 MET MET A . n 
A 1 303 ALA 303 291 291 ALA ALA A . n 
A 1 304 THR 304 292 292 THR THR A . n 
A 1 305 PHE 305 293 293 PHE PHE A . n 
A 1 306 MET 306 294 294 MET MET A . n 
A 1 307 LEU 307 295 295 LEU LEU A . n 
A 1 308 VAL 308 296 296 VAL VAL A . n 
A 1 309 ILE 309 297 297 ILE ILE A . n 
A 1 310 PHE 310 298 298 PHE PHE A . n 
A 1 311 PRO 311 299 299 PRO PRO A . n 
A 1 312 ARG 312 300 300 ARG ARG A . n 
A 1 313 ALA 313 301 301 ALA ALA A . n 
A 1 314 ALA 314 302 302 ALA ALA A . n 
A 1 315 VAL 315 303 303 VAL VAL A . n 
A 1 316 CYS 316 304 304 CYS CYS A . n 
A 1 317 ALA 317 305 305 ALA ALA A . n 
A 1 318 ASP 318 306 306 ASP ASP A . n 
A 1 319 ARG 319 307 307 ARG ARG A . n 
A 1 320 ILE 320 308 308 ILE ILE A . n 
A 1 321 GLY 321 309 309 GLY GLY A . n 
A 1 322 GLU 322 310 310 GLU GLU A . n 
A 1 323 VAL 323 311 311 VAL VAL A . n 
A 1 324 LEU 324 312 312 LEU LEU A . n 
A 1 325 SER 325 313 313 SER SER A . n 
A 1 326 THR 326 314 314 THR THR A . n 
A 1 327 GLN 327 315 315 GLN GLN A . n 
A 1 328 THR 328 316 316 THR THR A . n 
A 1 329 ALA 329 317 317 ALA ALA A . n 
A 1 330 ILE 330 318 318 ILE ILE A . n 
A 1 331 THR 331 319 319 THR THR A . n 
A 1 332 ASN 332 320 320 ASN ASN A . n 
A 1 333 PRO 333 321 321 PRO PRO A . n 
A 1 334 ALA 334 322 322 ALA ALA A . n 
A 1 335 ASP 335 323 323 ASP ASP A . n 
A 1 336 PRO 336 324 324 PRO PRO A . n 
A 1 337 VAL 337 325 325 VAL VAL A . n 
A 1 338 ARG 338 326 326 ARG ARG A . n 
A 1 339 PRO 339 327 327 PRO PRO A . n 
A 1 340 ALA 340 328 328 ALA ALA A . n 
A 1 341 ALA 341 329 329 ALA ALA A . n 
A 1 342 ILE 342 330 330 ILE ILE A . n 
A 1 343 ALA 343 331 331 ALA ALA A . n 
A 1 344 GLY 344 332 332 GLY GLY A . n 
A 1 345 ASP 345 333 333 ASP ASP A . n 
A 1 346 ILE 346 334 334 ILE ILE A . n 
A 1 347 GLY 347 335 335 GLY GLY A . n 
A 1 348 VAL 348 336 336 VAL VAL A . n 
A 1 349 HIS 349 337 337 HIS HIS A . n 
A 1 350 ASP 350 338 338 ASP ASP A . n 
A 1 351 ALA 351 339 339 ALA ALA A . n 
A 1 352 THR 352 340 340 THR THR A . n 
A 1 353 PHE 353 341 341 PHE PHE A . n 
A 1 354 CYS 354 342 342 CYS CYS A . n 
A 1 355 TYR 355 343 343 TYR TYR A . n 
A 1 356 PRO 356 344 344 PRO PRO A . n 
A 1 357 GLY 357 345 345 GLY GLY A . n 
A 1 358 ALA 358 346 346 ALA ALA A . n 
A 1 359 ASP 359 347 347 ASP ASP A . n 
A 1 360 ARG 360 348 348 ARG ARG A . n 
A 1 361 PRO 361 349 349 PRO PRO A . n 
A 1 362 VAL 362 350 350 VAL VAL A . n 
A 1 363 LEU 363 351 351 LEU LEU A . n 
A 1 364 GLN 364 352 352 GLN GLN A . n 
A 1 365 ASP 365 353 353 ASP ASP A . n 
A 1 366 VAL 366 354 354 VAL VAL A . n 
A 1 367 SER 367 355 355 SER SER A . n 
A 1 368 PHE 368 356 356 PHE PHE A . n 
A 1 369 THR 369 357 357 THR THR A . n 
A 1 370 VAL 370 358 358 VAL VAL A . n 
A 1 371 PRO 371 359 359 PRO PRO A . n 
A 1 372 ARG 372 360 360 ARG ARG A . n 
A 1 373 GLY 373 361 361 GLY GLY A . n 
A 1 374 THR 374 362 362 THR THR A . n 
A 1 375 THR 375 363 363 THR THR A . n 
A 1 376 THR 376 364 364 THR THR A . n 
A 1 377 ALA 377 365 365 ALA ALA A . n 
A 1 378 VAL 378 366 366 VAL VAL A . n 
A 1 379 VAL 379 367 367 VAL VAL A . n 
A 1 380 GLY 380 368 368 GLY GLY A . n 
A 1 381 SER 381 369 369 SER SER A . n 
A 1 382 THR 382 370 370 THR THR A . n 
A 1 383 GLY 383 371 371 GLY GLY A . n 
A 1 384 SER 384 372 372 SER SER A . n 
A 1 385 GLY 385 373 373 GLY GLY A . n 
A 1 386 LYS 386 374 374 LYS LYS A . n 
A 1 387 SER 387 375 375 SER SER A . n 
A 1 388 THR 388 376 376 THR THR A . n 
A 1 389 LEU 389 377 377 LEU LEU A . n 
A 1 390 ILE 390 378 378 ILE ILE A . n 
A 1 391 SER 391 379 379 SER SER A . n 
A 1 392 LEU 392 380 380 LEU LEU A . n 
A 1 393 ILE 393 381 381 ILE ILE A . n 
A 1 394 CYS 394 382 382 CYS CYS A . n 
A 1 395 ARG 395 383 383 ARG ARG A . n 
A 1 396 LEU 396 384 384 LEU LEU A . n 
A 1 397 TYR 397 385 385 TYR TYR A . n 
A 1 398 ASP 398 386 386 ASP ASP A . n 
A 1 399 VAL 399 387 387 VAL VAL A . n 
A 1 400 THR 400 388 388 THR THR A . n 
A 1 401 SER 401 389 389 SER SER A . n 
A 1 402 GLY 402 390 390 GLY GLY A . n 
A 1 403 SER 403 391 391 SER SER A . n 
A 1 404 LEU 404 392 392 LEU LEU A . n 
A 1 405 ARG 405 393 393 ARG ARG A . n 
A 1 406 ILE 406 394 394 ILE ILE A . n 
A 1 407 ASP 407 395 395 ASP ASP A . n 
A 1 408 GLY 408 396 396 GLY GLY A . n 
A 1 409 VAL 409 397 397 VAL VAL A . n 
A 1 410 ASP 410 398 398 ASP ASP A . n 
A 1 411 VAL 411 399 399 VAL VAL A . n 
A 1 412 ARG 412 400 400 ARG ARG A . n 
A 1 413 ASP 413 401 401 ASP ASP A . n 
A 1 414 LEU 414 402 402 LEU LEU A . n 
A 1 415 ASP 415 403 403 ASP ASP A . n 
A 1 416 ILE 416 404 404 ILE ILE A . n 
A 1 417 GLU 417 405 405 GLU GLU A . n 
A 1 418 GLN 418 406 406 GLN GLN A . n 
A 1 419 LEU 419 407 407 LEU LEU A . n 
A 1 420 TRP 420 408 408 TRP TRP A . n 
A 1 421 SER 421 409 409 SER SER A . n 
A 1 422 ALA 422 410 410 ALA ALA A . n 
A 1 423 ILE 423 411 411 ILE ILE A . n 
A 1 424 GLY 424 412 412 GLY GLY A . n 
A 1 425 LEU 425 413 413 LEU LEU A . n 
A 1 426 VAL 426 414 414 VAL VAL A . n 
A 1 427 PRO 427 415 415 PRO PRO A . n 
A 1 428 GLN 428 416 416 GLN GLN A . n 
A 1 429 ARG 429 417 417 ARG ARG A . n 
A 1 430 GLY 430 418 418 GLY GLY A . n 
A 1 431 TYR 431 419 419 TYR TYR A . n 
A 1 432 LEU 432 420 420 LEU LEU A . n 
A 1 433 PHE 433 421 421 PHE PHE A . n 
A 1 434 SER 434 422 422 SER SER A . n 
A 1 435 GLY 435 423 423 GLY GLY A . n 
A 1 436 THR 436 424 424 THR THR A . n 
A 1 437 VAL 437 425 425 VAL VAL A . n 
A 1 438 ALA 438 426 426 ALA ALA A . n 
A 1 439 GLU 439 427 427 GLU GLU A . n 
A 1 440 ASN 440 428 428 ASN ASN A . n 
A 1 441 LEU 441 429 429 LEU LEU A . n 
A 1 442 ARG 442 430 430 ARG ARG A . n 
A 1 443 TYR 443 431 431 TYR TYR A . n 
A 1 444 GLY 444 432 432 GLY GLY A . n 
A 1 445 ARG 445 433 433 ARG ARG A . n 
A 1 446 ALA 446 434 434 ALA ALA A . n 
A 1 447 ASP 447 435 435 ASP ASP A . n 
A 1 448 ALA 448 436 436 ALA ALA A . n 
A 1 449 THR 449 437 437 THR THR A . n 
A 1 450 ASP 450 438 438 ASP ASP A . n 
A 1 451 ASP 451 439 439 ASP ASP A . n 
A 1 452 GLU 452 440 440 GLU GLU A . n 
A 1 453 MET 453 441 441 MET MET A . n 
A 1 454 TRP 454 442 442 TRP TRP A . n 
A 1 455 GLU 455 443 443 GLU GLU A . n 
A 1 456 ALA 456 444 444 ALA ALA A . n 
A 1 457 LEU 457 445 445 LEU LEU A . n 
A 1 458 ARG 458 446 446 ARG ARG A . n 
A 1 459 VAL 459 447 447 VAL VAL A . n 
A 1 460 ALA 460 448 448 ALA ALA A . n 
A 1 461 ALA 461 449 449 ALA ALA A . n 
A 1 462 ALA 462 450 450 ALA ALA A . n 
A 1 463 ALA 463 451 451 ALA ALA A . n 
A 1 464 ASP 464 452 452 ASP ASP A . n 
A 1 465 PHE 465 453 453 PHE PHE A . n 
A 1 466 VAL 466 454 454 VAL VAL A . n 
A 1 467 ARG 467 455 455 ARG ARG A . n 
A 1 468 ALA 468 456 456 ALA ALA A . n 
A 1 469 HIS 469 457 457 HIS HIS A . n 
A 1 470 PRO 470 458 458 PRO PRO A . n 
A 1 471 GLN 471 459 459 GLN GLN A . n 
A 1 472 GLY 472 460 460 GLY GLY A . n 
A 1 473 LEU 473 461 461 LEU LEU A . n 
A 1 474 ASP 474 462 462 ASP ASP A . n 
A 1 475 MET 475 463 463 MET MET A . n 
A 1 476 PRO 476 464 464 PRO PRO A . n 
A 1 477 VAL 477 465 465 VAL VAL A . n 
A 1 478 ALA 478 466 466 ALA ALA A . n 
A 1 479 GLN 479 467 467 GLN GLN A . n 
A 1 480 GLY 480 468 468 GLY GLY A . n 
A 1 481 GLY 481 469 469 GLY GLY A . n 
A 1 482 ILE 482 470 470 ILE ILE A . n 
A 1 483 ASN 483 471 471 ASN ASN A . n 
A 1 484 PHE 484 472 472 PHE PHE A . n 
A 1 485 SER 485 473 473 SER SER A . n 
A 1 486 GLY 486 474 474 GLY GLY A . n 
A 1 487 GLY 487 475 475 GLY GLY A . n 
A 1 488 GLN 488 476 476 GLN GLN A . n 
A 1 489 ARG 489 477 477 ARG ARG A . n 
A 1 490 GLN 490 478 478 GLN GLN A . n 
A 1 491 ARG 491 479 479 ARG ARG A . n 
A 1 492 LEU 492 480 480 LEU LEU A . n 
A 1 493 ALA 493 481 481 ALA ALA A . n 
A 1 494 ILE 494 482 482 ILE ILE A . n 
A 1 495 ALA 495 483 483 ALA ALA A . n 
A 1 496 ARG 496 484 484 ARG ARG A . n 
A 1 497 ALA 497 485 485 ALA ALA A . n 
A 1 498 VAL 498 486 486 VAL VAL A . n 
A 1 499 ILE 499 487 487 ILE ILE A . n 
A 1 500 ARG 500 488 488 ARG ARG A . n 
A 1 501 ARG 501 489 489 ARG ARG A . n 
A 1 502 PRO 502 490 490 PRO PRO A . n 
A 1 503 ALA 503 491 491 ALA ALA A . n 
A 1 504 ILE 504 492 492 ILE ILE A . n 
A 1 505 TYR 505 493 493 TYR TYR A . n 
A 1 506 LEU 506 494 494 LEU LEU A . n 
A 1 507 PHE 507 495 495 PHE PHE A . n 
A 1 508 ASP 508 496 496 ASP ASP A . n 
A 1 509 ASP 509 497 497 ASP ASP A . n 
A 1 510 ALA 510 498 498 ALA ALA A . n 
A 1 511 PHE 511 499 499 PHE PHE A . n 
A 1 512 SER 512 500 500 SER SER A . n 
A 1 513 ALA 513 501 501 ALA ALA A . n 
A 1 514 LEU 514 502 502 LEU LEU A . n 
A 1 515 ASP 515 503 503 ASP ASP A . n 
A 1 516 VAL 516 504 504 VAL VAL A . n 
A 1 517 HIS 517 505 505 HIS HIS A . n 
A 1 518 THR 518 506 506 THR THR A . n 
A 1 519 ASP 519 507 507 ASP ASP A . n 
A 1 520 ALA 520 508 508 ALA ALA A . n 
A 1 521 ARG 521 509 509 ARG ARG A . n 
A 1 522 VAL 522 510 510 VAL VAL A . n 
A 1 523 ARG 523 511 511 ARG ARG A . n 
A 1 524 ASP 524 512 512 ASP ASP A . n 
A 1 525 ALA 525 513 513 ALA ALA A . n 
A 1 526 LEU 526 514 514 LEU LEU A . n 
A 1 527 ARG 527 515 515 ARG ARG A . n 
A 1 528 GLU 528 516 516 GLU GLU A . n 
A 1 529 VAL 529 517 517 VAL VAL A . n 
A 1 530 ALA 530 518 518 ALA ALA A . n 
A 1 531 ALA 531 519 519 ALA ALA A . n 
A 1 532 ASP 532 520 520 ASP ASP A . n 
A 1 533 ALA 533 521 521 ALA ALA A . n 
A 1 534 THR 534 522 522 THR THR A . n 
A 1 535 VAL 535 523 523 VAL VAL A . n 
A 1 536 VAL 536 524 524 VAL VAL A . n 
A 1 537 ILE 537 525 525 ILE ILE A . n 
A 1 538 VAL 538 526 526 VAL VAL A . n 
A 1 539 SER 539 527 527 SER SER A . n 
A 1 540 GLN 540 528 528 GLN GLN A . n 
A 1 541 ARG 541 529 529 ARG ARG A . n 
A 1 542 ILE 542 530 530 ILE ILE A . n 
A 1 543 SER 543 531 531 SER SER A . n 
A 1 544 THR 544 532 532 THR THR A . n 
A 1 545 VAL 545 533 533 VAL VAL A . n 
A 1 546 ILE 546 534 534 ILE ILE A . n 
A 1 547 GLU 547 535 535 GLU GLU A . n 
A 1 548 ALA 548 536 536 ALA ALA A . n 
A 1 549 ASP 549 537 537 ASP ASP A . n 
A 1 550 GLN 550 538 538 GLN GLN A . n 
A 1 551 VAL 551 539 539 VAL VAL A . n 
A 1 552 VAL 552 540 540 VAL VAL A . n 
A 1 553 VAL 553 541 541 VAL VAL A . n 
A 1 554 ILE 554 542 542 ILE ILE A . n 
A 1 555 ASP 555 543 543 ASP ASP A . n 
A 1 556 ASP 556 544 544 ASP ASP A . n 
A 1 557 GLY 557 545 545 GLY GLY A . n 
A 1 558 ARG 558 546 546 ARG ARG A . n 
A 1 559 VAL 559 547 547 VAL VAL A . n 
A 1 560 VAL 560 548 548 VAL VAL A . n 
A 1 561 GLY 561 549 549 GLY GLY A . n 
A 1 562 ILE 562 550 550 ILE ILE A . n 
A 1 563 GLY 563 551 551 GLY GLY A . n 
A 1 564 THR 564 552 552 THR THR A . n 
A 1 565 HIS 565 553 553 HIS HIS A . n 
A 1 566 ASP 566 554 554 ASP ASP A . n 
A 1 567 THR 567 555 555 THR THR A . n 
A 1 568 LEU 568 556 556 LEU LEU A . n 
A 1 569 LEU 569 557 557 LEU LEU A . n 
A 1 570 ALA 570 558 558 ALA ALA A . n 
A 1 571 ASP 571 559 559 ASP ASP A . n 
A 1 572 CYS 572 560 560 CYS CYS A . n 
A 1 573 PRO 573 561 561 PRO PRO A . n 
A 1 574 ILE 574 562 562 ILE ILE A . n 
A 1 575 TYR 575 563 563 TYR TYR A . n 
A 1 576 ALA 576 564 564 ALA ALA A . n 
A 1 577 GLU 577 565 565 GLU GLU A . n 
A 1 578 PHE 578 566 566 PHE PHE A . n 
A 1 579 ALA 579 567 567 ALA ALA A . n 
A 1 580 GLU 580 568 568 GLU GLU A . n 
A 1 581 SER 581 569 569 SER SER A . n 
A 1 582 GLN 582 570 570 GLN GLN A . n 
A 1 583 ALA 583 571 571 ALA ALA A . n 
A 1 584 LEU 584 572 572 LEU LEU A . n 
A 1 585 THR 585 573 ?   ?   ?   A . n 
A 1 586 ALA 586 574 ?   ?   ?   A . n 
A 1 587 GLY 587 575 ?   ?   ?   A . n 
A 1 588 GLU 588 576 ?   ?   ?   A . n 
A 1 589 PRO 589 577 ?   ?   ?   A . n 
A 1 590 ARG 590 578 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ARG 2   2   ?   ?   ?   B . n 
B 2 3   ARG 3   3   ?   ?   ?   B . n 
B 2 4   GLY 4   4   ?   ?   ?   B . n 
B 2 5   ALA 5   5   ?   ?   ?   B . n 
B 2 6   LEU 6   6   ?   ?   ?   B . n 
B 2 7   PRO 7   7   ?   ?   ?   B . n 
B 2 8   GLN 8   8   ?   ?   ?   B . n 
B 2 9   ALA 9   9   ?   ?   ?   B . n 
B 2 10  PRO 10  10  ?   ?   ?   B . n 
B 2 11  LEU 11  11  ?   ?   ?   B . n 
B 2 12  GLU 12  12  ?   ?   ?   B . n 
B 2 13  ARG 13  13  ?   ?   ?   B . n 
B 2 14  THR 14  14  14  THR THR B . n 
B 2 15  ARG 15  15  15  ARG ARG B . n 
B 2 16  ASP 16  16  16  ASP ASP B . n 
B 2 17  PHE 17  17  17  PHE PHE B . n 
B 2 18  LYS 18  18  18  LYS LYS B . n 
B 2 19  GLY 19  19  19  GLY GLY B . n 
B 2 20  SER 20  20  20  SER SER B . n 
B 2 21  ALA 21  21  21  ALA ALA B . n 
B 2 22  ILE 22  22  22  ILE ILE B . n 
B 2 23  ARG 23  23  23  ARG ARG B . n 
B 2 24  LEU 24  24  24  LEU LEU B . n 
B 2 25  ALA 25  25  25  ALA ALA B . n 
B 2 26  ARG 26  26  26  ARG ARG B . n 
B 2 27  ARG 27  27  27  ARG ARG B . n 
B 2 28  LEU 28  28  28  LEU LEU B . n 
B 2 29  LEU 29  29  29  LEU LEU B . n 
B 2 30  PRO 30  30  30  PRO PRO B . n 
B 2 31  GLN 31  31  31  GLN GLN B . n 
B 2 32  ARG 32  32  32  ARG ARG B . n 
B 2 33  ALA 33  33  33  ALA ALA B . n 
B 2 34  LEU 34  34  34  LEU LEU B . n 
B 2 35  THR 35  35  35  THR THR B . n 
B 2 36  LEU 36  36  36  LEU LEU B . n 
B 2 37  ALA 37  37  37  ALA ALA B . n 
B 2 38  VAL 38  38  38  VAL VAL B . n 
B 2 39  ILE 39  39  39  ILE ILE B . n 
B 2 40  LEU 40  40  40  LEU LEU B . n 
B 2 41  LEU 41  41  41  LEU LEU B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  VAL 43  43  43  VAL VAL B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  GLY 45  45  45  GLY GLY B . n 
B 2 46  ILE 46  46  46  ILE ILE B . n 
B 2 47  ALA 47  47  47  ALA ALA B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  GLY 49  49  49  GLY GLY B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  GLY 52  52  52  GLY GLY B . n 
B 2 53  PRO 53  53  53  PRO PRO B . n 
B 2 54  ARG 54  54  54  ARG ARG B . n 
B 2 55  ILE 55  55  55  ILE ILE B . n 
B 2 56  LEU 56  56  56  LEU LEU B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  HIS 58  58  58  HIS HIS B . n 
B 2 59  ALA 59  59  59  ALA ALA B . n 
B 2 60  THR 60  60  60  THR THR B . n 
B 2 61  ASP 61  61  61  ASP ASP B . n 
B 2 62  LEU 62  62  62  LEU LEU B . n 
B 2 63  LEU 63  63  63  LEU LEU B . n 
B 2 64  PHE 64  64  64  PHE PHE B . n 
B 2 65  ASN 65  65  65  ASN ASN B . n 
B 2 66  GLY 66  66  66  GLY GLY B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  ILE 68  68  68  ILE ILE B . n 
B 2 69  GLY 69  69  69  GLY GLY B . n 
B 2 70  ARG 70  70  70  ARG ARG B . n 
B 2 71  GLU 71  71  71  GLU GLU B . n 
B 2 72  LEU 72  72  72  LEU LEU B . n 
B 2 73  PRO 73  73  73  PRO PRO B . n 
B 2 74  ALA 74  74  74  ALA ALA B . n 
B 2 75  GLY 75  75  75  GLY GLY B . n 
B 2 76  LEU 76  76  76  LEU LEU B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  LYS 78  78  78  LYS LYS B . n 
B 2 79  GLU 79  79  79  GLU GLU B . n 
B 2 80  GLN 80  80  80  GLN GLN B . n 
B 2 81  ALA 81  81  81  ALA ALA B . n 
B 2 82  VAL 82  82  82  VAL VAL B . n 
B 2 83  GLU 83  83  83  GLU GLU B . n 
B 2 84  ALA 84  84  84  ALA ALA B . n 
B 2 85  ALA 85  85  85  ALA ALA B . n 
B 2 86  ARG 86  86  86  ARG ARG B . n 
B 2 87  ALA 87  87  87  ALA ALA B . n 
B 2 88  ARG 88  88  88  ARG ARG B . n 
B 2 89  GLY 89  89  89  GLY GLY B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  GLY 91  91  91  GLY GLY B . n 
B 2 92  THR 92  92  92  THR THR B . n 
B 2 93  PHE 93  93  93  PHE PHE B . n 
B 2 94  ALA 94  94  94  ALA ALA B . n 
B 2 95  ASP 95  95  95  ASP ASP B . n 
B 2 96  LEU 96  96  96  LEU LEU B . n 
B 2 97  LEU 97  97  97  LEU LEU B . n 
B 2 98  SER 98  98  98  SER SER B . n 
B 2 99  GLY 99  99  99  GLY GLY B . n 
B 2 100 MET 100 100 100 MET MET B . n 
B 2 101 ASP 101 101 101 ASP ASP B . n 
B 2 102 ILE 102 102 102 ILE ILE B . n 
B 2 103 VAL 103 103 103 VAL VAL B . n 
B 2 104 PRO 104 104 104 PRO PRO B . n 
B 2 105 GLY 105 105 105 GLY GLY B . n 
B 2 106 GLN 106 106 106 GLN GLN B . n 
B 2 107 GLY 107 107 107 GLY GLY B . n 
B 2 108 VAL 108 108 108 VAL VAL B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 PHE 110 110 110 PHE PHE B . n 
B 2 111 GLY 111 111 111 GLY GLY B . n 
B 2 112 ALA 112 112 112 ALA ALA B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 GLY 114 114 114 GLY GLY B . n 
B 2 115 ARG 115 115 115 ARG ARG B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 LEU 117 117 117 LEU LEU B . n 
B 2 118 ALA 118 118 118 ALA ALA B . n 
B 2 119 LEU 119 119 119 LEU LEU B . n 
B 2 120 ALA 120 120 120 ALA ALA B . n 
B 2 121 LEU 121 121 121 LEU LEU B . n 
B 2 122 GLY 122 122 122 GLY GLY B . n 
B 2 123 LEU 123 123 123 LEU LEU B . n 
B 2 124 TYR 124 124 124 TYR TYR B . n 
B 2 125 LEU 125 125 125 LEU LEU B . n 
B 2 126 VAL 126 126 126 VAL VAL B . n 
B 2 127 ALA 127 127 127 ALA ALA B . n 
B 2 128 ALA 128 128 128 ALA ALA B . n 
B 2 129 LEU 129 129 129 LEU LEU B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 VAL 131 131 131 VAL VAL B . n 
B 2 132 TRP 132 132 132 TRP TRP B . n 
B 2 133 VAL 133 133 133 VAL VAL B . n 
B 2 134 GLN 134 134 134 GLN GLN B . n 
B 2 135 ALA 135 135 135 ALA ALA B . n 
B 2 136 ARG 136 136 136 ARG ARG B . n 
B 2 137 LEU 137 137 137 LEU LEU B . n 
B 2 138 LEU 138 138 138 LEU LEU B . n 
B 2 139 ASN 139 139 139 ASN ASN B . n 
B 2 140 VAL 140 140 140 VAL VAL B . n 
B 2 141 THR 141 141 141 THR THR B . n 
B 2 142 VAL 142 142 142 VAL VAL B . n 
B 2 143 GLN 143 143 143 GLN GLN B . n 
B 2 144 ARG 144 144 144 ARG ARG B . n 
B 2 145 THR 145 145 145 THR THR B . n 
B 2 146 MET 146 146 146 MET MET B . n 
B 2 147 VAL 147 147 147 VAL VAL B . n 
B 2 148 ALA 148 148 148 ALA ALA B . n 
B 2 149 LEU 149 149 149 LEU LEU B . n 
B 2 150 ARG 150 150 150 ARG ARG B . n 
B 2 151 ALA 151 151 151 ALA ALA B . n 
B 2 152 GLU 152 152 152 GLU GLU B . n 
B 2 153 VAL 153 153 153 VAL VAL B . n 
B 2 154 GLN 154 154 154 GLN GLN B . n 
B 2 155 GLU 155 155 155 GLU GLU B . n 
B 2 156 LYS 156 156 156 LYS LYS B . n 
B 2 157 ILE 157 157 157 ILE ILE B . n 
B 2 158 HIS 158 158 158 HIS HIS B . n 
B 2 159 ARG 159 159 159 ARG ARG B . n 
B 2 160 LEU 160 160 160 LEU LEU B . n 
B 2 161 PRO 161 161 161 PRO PRO B . n 
B 2 162 LEU 162 162 162 LEU LEU B . n 
B 2 163 SER 163 163 163 SER SER B . n 
B 2 164 TYR 164 164 164 TYR TYR B . n 
B 2 165 PHE 165 165 165 PHE PHE B . n 
B 2 166 ASP 166 166 166 ASP ASP B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 ARG 168 168 168 ARG ARG B . n 
B 2 169 GLN 169 169 169 GLN GLN B . n 
B 2 170 ARG 170 170 170 ARG ARG B . n 
B 2 171 GLY 171 171 171 GLY GLY B . n 
B 2 172 GLU 172 172 172 GLU GLU B . n 
B 2 173 VAL 173 173 173 VAL VAL 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 ARG 176 176 176 ARG ARG B . n 
B 2 177 VAL 177 177 177 VAL VAL B . n 
B 2 178 THR 178 178 178 THR THR B . n 
B 2 179 ASN 179 179 179 ASN ASN B . n 
B 2 180 ASP 180 180 180 ASP ASP B . n 
B 2 181 VAL 181 181 181 VAL VAL B . n 
B 2 182 ASP 182 182 182 ASP ASP B . n 
B 2 183 ASN 183 183 183 ASN ASN B . n 
B 2 184 ILE 184 184 184 ILE ILE B . n 
B 2 185 GLN 185 185 185 GLN GLN B . n 
B 2 186 ASN 186 186 186 ASN ASN B . n 
B 2 187 SER 187 187 187 SER SER B . n 
B 2 188 VAL 188 188 188 VAL VAL B . n 
B 2 189 SER 189 189 189 SER SER B . n 
B 2 190 MET 190 190 190 MET MET B . n 
B 2 191 THR 191 191 191 THR THR B . n 
B 2 192 ILE 192 192 192 ILE ILE B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 GLN 194 194 194 GLN GLN B . n 
B 2 195 LEU 195 195 195 LEU LEU B . n 
B 2 196 LEU 196 196 196 LEU LEU B . n 
B 2 197 THR 197 197 197 THR THR B . n 
B 2 198 SER 198 198 198 SER SER B . n 
B 2 199 VAL 199 199 199 VAL VAL B . n 
B 2 200 LEU 200 200 200 LEU LEU B . n 
B 2 201 THR 201 201 201 THR THR B . n 
B 2 202 VAL 202 202 202 VAL VAL B . n 
B 2 203 PHE 203 203 203 PHE PHE B . n 
B 2 204 ALA 204 204 204 ALA ALA B . n 
B 2 205 VAL 205 205 205 VAL VAL B . n 
B 2 206 LEU 206 206 206 LEU LEU B . n 
B 2 207 VAL 207 207 207 VAL VAL B . n 
B 2 208 MET 208 208 208 MET MET B . n 
B 2 209 MET 209 209 209 MET MET B . n 
B 2 210 LEU 210 210 210 LEU LEU B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 ILE 212 212 212 ILE ILE B . n 
B 2 213 SER 213 213 213 SER SER B . n 
B 2 214 PRO 214 214 214 PRO PRO B . n 
B 2 215 LEU 215 215 215 LEU LEU B . n 
B 2 216 LEU 216 216 216 LEU LEU B . n 
B 2 217 THR 217 217 217 THR THR B . n 
B 2 218 LEU 218 218 218 LEU LEU B . n 
B 2 219 PHE 219 219 219 PHE PHE B . n 
B 2 220 THR 220 220 220 THR THR B . n 
B 2 221 VAL 221 221 221 VAL VAL B . n 
B 2 222 VAL 222 222 222 VAL VAL B . n 
B 2 223 THR 223 223 223 THR THR B . n 
B 2 224 VAL 224 224 224 VAL VAL B . n 
B 2 225 PRO 225 225 225 PRO PRO B . n 
B 2 226 ALA 226 226 226 ALA ALA B . n 
B 2 227 SER 227 227 227 SER SER B . n 
B 2 228 LEU 228 228 228 LEU LEU B . n 
B 2 229 TRP 229 229 229 TRP TRP B . n 
B 2 230 VAL 230 230 230 VAL VAL B . n 
B 2 231 THR 231 231 231 THR THR B . n 
B 2 232 ARG 232 232 232 ARG ARG B . n 
B 2 233 TRP 233 233 233 TRP TRP B . n 
B 2 234 ILE 234 234 234 ILE ILE B . n 
B 2 235 THR 235 235 235 THR THR B . n 
B 2 236 ARG 236 236 236 ARG ARG B . n 
B 2 237 ARG 237 237 237 ARG ARG B . n 
B 2 238 SER 238 238 238 SER SER B . n 
B 2 239 GLN 239 239 239 GLN GLN B . n 
B 2 240 PRO 240 240 240 PRO PRO B . n 
B 2 241 LEU 241 241 241 LEU LEU B . n 
B 2 242 PHE 242 242 242 PHE PHE B . n 
B 2 243 VAL 243 243 243 VAL VAL B . n 
B 2 244 ALA 244 244 244 ALA ALA B . n 
B 2 245 GLN 245 245 245 GLN GLN B . n 
B 2 246 TRP 246 246 246 TRP TRP B . n 
B 2 247 ARG 247 247 247 ARG ARG B . n 
B 2 248 ASN 248 248 248 ASN ASN B . n 
B 2 249 THR 249 249 249 THR THR B . n 
B 2 250 GLY 250 250 250 GLY GLY B . n 
B 2 251 ARG 251 251 251 ARG ARG B . n 
B 2 252 LEU 252 252 252 LEU LEU B . n 
B 2 253 ALA 253 253 253 ALA ALA B . n 
B 2 254 ALA 254 254 254 ALA ALA B . n 
B 2 255 HIS 255 255 255 HIS HIS B . n 
B 2 256 LEU 256 256 256 LEU LEU B . n 
B 2 257 GLU 257 257 257 GLU GLU B . n 
B 2 258 GLU 258 258 258 GLU GLU B . n 
B 2 259 THR 259 259 259 THR THR B . n 
B 2 260 TYR 260 260 260 TYR TYR B . n 
B 2 261 SER 261 261 261 SER SER B . n 
B 2 262 GLY 262 262 262 GLY GLY B . n 
B 2 263 PHE 263 263 263 PHE PHE B . n 
B 2 264 THR 264 264 264 THR THR B . n 
B 2 265 ILE 265 265 265 ILE ILE B . n 
B 2 266 VAL 266 266 266 VAL VAL B . n 
B 2 267 LYS 267 267 267 LYS LYS B . n 
B 2 268 THR 268 268 268 THR THR B . n 
B 2 269 PHE 269 269 269 PHE PHE B . n 
B 2 270 GLY 270 270 270 GLY GLY B . n 
B 2 271 HIS 271 271 271 HIS HIS B . n 
B 2 272 ARG 272 272 272 ARG ARG B . n 
B 2 273 GLU 273 273 273 GLU GLU B . n 
B 2 274 ALA 274 274 274 ALA ALA B . n 
B 2 275 ALA 275 275 275 ALA ALA B . n 
B 2 276 ALA 276 276 276 ALA ALA B . n 
B 2 277 GLY 277 277 277 GLY GLY B . n 
B 2 278 LYS 278 278 278 LYS LYS B . n 
B 2 279 PHE 279 279 279 PHE PHE B . n 
B 2 280 ALA 280 280 280 ALA ALA B . n 
B 2 281 GLU 281 281 281 GLU GLU B . n 
B 2 282 LEU 282 282 282 LEU LEU B . n 
B 2 283 ASN 283 283 283 ASN ASN B . n 
B 2 284 SER 284 284 284 SER SER B . n 
B 2 285 GLU 285 285 285 GLU GLU B . n 
B 2 286 THR 286 286 286 THR THR B . n 
B 2 287 GLN 287 287 287 GLN GLN B . n 
B 2 288 GLN 288 288 288 GLN GLN B . n 
B 2 289 SER 289 289 289 SER SER B . n 
B 2 290 SER 290 290 290 SER SER B . n 
B 2 291 PHE 291 291 291 PHE PHE B . n 
B 2 292 GLY 292 292 292 GLY GLY B . n 
B 2 293 ALA 293 293 293 ALA ALA B . n 
B 2 294 GLN 294 294 294 GLN GLN B . n 
B 2 295 PHE 295 295 295 PHE PHE B . n 
B 2 296 PHE 296 296 296 PHE PHE B . n 
B 2 297 SER 297 297 297 SER SER B . n 
B 2 298 GLY 298 298 298 GLY GLY B . n 
B 2 299 LEU 299 299 299 LEU LEU B . n 
B 2 300 VAL 300 300 300 VAL VAL B . n 
B 2 301 SER 301 301 301 SER SER B . n 
B 2 302 PRO 302 302 302 PRO PRO B . n 
B 2 303 ALA 303 303 303 ALA ALA B . n 
B 2 304 THR 304 304 304 THR THR B . n 
B 2 305 MET 305 305 305 MET MET B . n 
B 2 306 PHE 306 306 306 PHE PHE B . n 
B 2 307 ILE 307 307 307 ILE ILE B . n 
B 2 308 GLY 308 308 308 GLY GLY B . n 
B 2 309 ASN 309 309 309 ASN ASN B . n 
B 2 310 LEU 310 310 310 LEU LEU B . n 
B 2 311 SER 311 311 311 SER SER B . n 
B 2 312 TYR 312 312 312 TYR TYR B . n 
B 2 313 VAL 313 313 313 VAL VAL B . n 
B 2 314 ALA 314 314 314 ALA ALA B . n 
B 2 315 VAL 315 315 315 VAL VAL B . n 
B 2 316 ALA 316 316 316 ALA ALA B . n 
B 2 317 VAL 317 317 317 VAL VAL B . n 
B 2 318 VAL 318 318 318 VAL VAL B . n 
B 2 319 GLY 319 319 319 GLY GLY B . n 
B 2 320 GLY 320 320 320 GLY GLY B . n 
B 2 321 LEU 321 321 321 LEU LEU B . n 
B 2 322 GLN 322 322 322 GLN GLN B . n 
B 2 323 VAL 323 323 323 VAL VAL B . n 
B 2 324 ALA 324 324 324 ALA ALA B . n 
B 2 325 THR 325 325 325 THR THR B . n 
B 2 326 GLY 326 326 326 GLY GLY B . n 
B 2 327 GLN 327 327 327 GLN GLN B . n 
B 2 328 ILE 328 328 328 ILE ILE B . n 
B 2 329 THR 329 329 329 THR THR B . n 
B 2 330 LEU 330 330 330 LEU LEU B . n 
B 2 331 GLY 331 331 331 GLY GLY B . n 
B 2 332 SER 332 332 332 SER SER B . n 
B 2 333 ILE 333 333 333 ILE ILE B . n 
B 2 334 GLN 334 334 334 GLN GLN B . n 
B 2 335 ALA 335 335 335 ALA ALA B . n 
B 2 336 PHE 336 336 336 PHE PHE B . n 
B 2 337 ILE 337 337 337 ILE ILE B . n 
B 2 338 GLN 338 338 338 GLN GLN B . n 
B 2 339 TYR 339 339 339 TYR TYR B . n 
B 2 340 VAL 340 340 340 VAL VAL B . n 
B 2 341 ARG 341 341 341 ARG ARG B . n 
B 2 342 GLN 342 342 342 GLN GLN B . n 
B 2 343 PHE 343 343 343 PHE PHE B . n 
B 2 344 ASN 344 344 344 ASN ASN B . n 
B 2 345 GLN 345 345 345 GLN GLN B . n 
B 2 346 PRO 346 346 346 PRO PRO B . n 
B 2 347 LEU 347 347 347 LEU LEU B . n 
B 2 348 THR 348 348 348 THR THR B . n 
B 2 349 GLN 349 349 349 GLN GLN B . n 
B 2 350 VAL 350 350 350 VAL VAL B . n 
B 2 351 ALA 351 351 351 ALA ALA B . n 
B 2 352 GLY 352 352 352 GLY GLY B . n 
B 2 353 MET 353 353 353 MET MET B . n 
B 2 354 TYR 354 354 354 TYR TYR B . n 
B 2 355 ASN 355 355 355 ASN ASN B . n 
B 2 356 THR 356 356 356 THR THR B . n 
B 2 357 LEU 357 357 357 LEU LEU B . n 
B 2 358 GLN 358 358 358 GLN GLN B . n 
B 2 359 SER 359 359 359 SER SER B . n 
B 2 360 GLY 360 360 360 GLY GLY B . n 
B 2 361 ILE 361 361 361 ILE ILE B . n 
B 2 362 ALA 362 362 362 ALA ALA 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 GLU 365 365 365 GLU GLU B . n 
B 2 366 ARG 366 366 366 ARG ARG B . n 
B 2 367 VAL 367 367 367 VAL VAL B . n 
B 2 368 PHE 368 368 368 PHE PHE B . n 
B 2 369 ASP 369 369 369 ASP ASP B . n 
B 2 370 LEU 370 370 370 LEU LEU B . n 
B 2 371 LEU 371 371 371 LEU LEU B . n 
B 2 372 ASP 372 372 372 ASP ASP B . n 
B 2 373 THR 373 373 373 THR THR B . n 
B 2 374 GLU 374 374 374 GLU GLU B . n 
B 2 375 GLU 375 375 375 GLU GLU B . n 
B 2 376 GLU 376 376 376 GLU GLU B . n 
B 2 377 SER 377 377 377 SER SER B . n 
B 2 378 ALA 378 378 378 ALA ALA B . n 
B 2 379 ASP 379 379 379 ASP ASP B . n 
B 2 380 SER 380 380 380 SER SER B . n 
B 2 381 PRO 381 381 381 PRO PRO B . n 
B 2 382 ARG 382 382 382 ARG ARG B . n 
B 2 383 ARG 383 383 383 ARG ARG B . n 
B 2 384 ALA 384 384 384 ALA ALA B . n 
B 2 385 ASP 385 385 385 ASP ASP B . n 
B 2 386 VAL 386 386 386 VAL VAL B . n 
B 2 387 ARG 387 387 387 ARG ARG B . n 
B 2 388 THR 388 388 388 THR THR B . n 
B 2 389 GLY 389 389 389 GLY GLY B . n 
B 2 390 ARG 390 390 390 ARG ARG B . n 
B 2 391 VAL 391 391 391 VAL VAL B . n 
B 2 392 GLU 392 392 392 GLU GLU B . n 
B 2 393 PHE 393 393 393 PHE PHE B . n 
B 2 394 GLU 394 394 394 GLU GLU B . n 
B 2 395 HIS 395 395 395 HIS HIS B . n 
B 2 396 VAL 396 396 396 VAL VAL B . n 
B 2 397 SER 397 397 397 SER SER B . n 
B 2 398 PHE 398 398 398 PHE PHE B . n 
B 2 399 SER 399 399 399 SER SER B . n 
B 2 400 TYR 400 400 400 TYR TYR B . n 
B 2 401 VAL 401 401 401 VAL VAL B . n 
B 2 402 PRO 402 402 402 PRO PRO B . n 
B 2 403 GLY 403 403 403 GLY GLY B . n 
B 2 404 THR 404 404 404 THR THR B . n 
B 2 405 PRO 405 405 405 PRO PRO B . n 
B 2 406 VAL 406 406 406 VAL VAL B . n 
B 2 407 ILE 407 407 407 ILE ILE B . n 
B 2 408 GLU 408 408 408 GLU GLU B . n 
B 2 409 ASP 409 409 409 ASP ASP B . n 
B 2 410 LEU 410 410 410 LEU LEU B . n 
B 2 411 SER 411 411 411 SER SER B . n 
B 2 412 LEU 412 412 412 LEU LEU B . n 
B 2 413 VAL 413 413 413 VAL VAL B . n 
B 2 414 ALA 414 414 414 ALA ALA B . n 
B 2 415 GLU 415 415 415 GLU GLU B . n 
B 2 416 PRO 416 416 416 PRO PRO B . n 
B 2 417 GLY 417 417 417 GLY GLY B . n 
B 2 418 SER 418 418 418 SER SER B . n 
B 2 419 THR 419 419 419 THR THR B . n 
B 2 420 VAL 420 420 420 VAL VAL B . n 
B 2 421 ALA 421 421 421 ALA ALA B . n 
B 2 422 ILE 422 422 422 ILE ILE B . n 
B 2 423 VAL 423 423 423 VAL VAL B . n 
B 2 424 GLY 424 424 424 GLY GLY B . n 
B 2 425 PRO 425 425 425 PRO PRO B . n 
B 2 426 THR 426 426 426 THR THR B . n 
B 2 427 GLY 427 427 427 GLY GLY B . n 
B 2 428 ALA 428 428 428 ALA ALA B . n 
B 2 429 GLY 429 429 429 GLY GLY B . n 
B 2 430 LYS 430 430 430 LYS LYS B . n 
B 2 431 THR 431 431 431 THR THR B . n 
B 2 432 THR 432 432 432 THR THR B . n 
B 2 433 LEU 433 433 433 LEU LEU B . n 
B 2 434 VAL 434 434 434 VAL VAL B . n 
B 2 435 ASN 435 435 435 ASN ASN B . n 
B 2 436 LEU 436 436 436 LEU LEU B . n 
B 2 437 LEU 437 437 437 LEU LEU B . n 
B 2 438 MET 438 438 438 MET MET B . n 
B 2 439 ARG 439 439 439 ARG ARG B . n 
B 2 440 PHE 440 440 440 PHE PHE B . n 
B 2 441 TYR 441 441 441 TYR TYR B . n 
B 2 442 ASP 442 442 442 ASP ASP B . n 
B 2 443 VAL 443 443 443 VAL VAL B . n 
B 2 444 ASP 444 444 444 ASP ASP B . n 
B 2 445 SER 445 445 445 SER SER B . n 
B 2 446 GLY 446 446 446 GLY GLY B . n 
B 2 447 ARG 447 447 447 ARG ARG B . n 
B 2 448 ILE 448 448 448 ILE ILE B . n 
B 2 449 THR 449 449 449 THR THR B . n 
B 2 450 ILE 450 450 450 ILE ILE B . n 
B 2 451 ASP 451 451 451 ASP ASP B . n 
B 2 452 GLY 452 452 452 GLY GLY B . n 
B 2 453 VAL 453 453 453 VAL VAL B . n 
B 2 454 ASP 454 454 454 ASP ASP B . n 
B 2 455 ILE 455 455 455 ILE ILE B . n 
B 2 456 ALA 456 456 456 ALA ALA B . n 
B 2 457 SER 457 457 457 SER SER B . n 
B 2 458 VAL 458 458 458 VAL VAL B . n 
B 2 459 SER 459 459 459 SER SER B . n 
B 2 460 ARG 460 460 460 ARG ARG B . n 
B 2 461 GLU 461 461 461 GLU GLU B . n 
B 2 462 SER 462 462 462 SER SER B . n 
B 2 463 LEU 463 463 463 LEU LEU B . n 
B 2 464 ARG 464 464 464 ARG ARG B . n 
B 2 465 ALA 465 465 465 ALA ALA B . n 
B 2 466 SER 466 466 466 SER SER B . n 
B 2 467 ILE 467 467 467 ILE ILE B . n 
B 2 468 GLY 468 468 468 GLY GLY B . n 
B 2 469 MET 469 469 469 MET MET B . n 
B 2 470 VAL 470 470 470 VAL VAL B . n 
B 2 471 LEU 471 471 471 LEU LEU B . n 
B 2 472 GLN 472 472 472 GLN GLN B . n 
B 2 473 ASP 473 473 473 ASP ASP B . n 
B 2 474 THR 474 474 474 THR THR B . n 
B 2 475 TRP 475 475 475 TRP TRP B . n 
B 2 476 LEU 476 476 476 LEU LEU B . n 
B 2 477 PHE 477 477 477 PHE PHE B . n 
B 2 478 ALA 478 478 478 ALA ALA B . n 
B 2 479 GLY 479 479 479 GLY GLY B . n 
B 2 480 THR 480 480 480 THR THR B . n 
B 2 481 ILE 481 481 481 ILE ILE B . n 
B 2 482 TYR 482 482 482 TYR TYR B . n 
B 2 483 ASP 483 483 483 ASP ASP B . n 
B 2 484 ASN 484 484 484 ASN ASN B . n 
B 2 485 ILE 485 485 485 ILE ILE B . n 
B 2 486 ALA 486 486 486 ALA ALA B . n 
B 2 487 TYR 487 487 487 TYR TYR B . n 
B 2 488 GLY 488 488 488 GLY GLY B . n 
B 2 489 ARG 489 489 489 ARG ARG B . n 
B 2 490 PRO 490 490 490 PRO PRO B . n 
B 2 491 ASP 491 491 491 ASP ASP B . n 
B 2 492 ALA 492 492 492 ALA ALA B . n 
B 2 493 ASP 493 493 493 ASP ASP B . n 
B 2 494 GLU 494 494 494 GLU GLU B . n 
B 2 495 ASP 495 495 495 ASP ASP B . n 
B 2 496 GLU 496 496 496 GLU GLU B . n 
B 2 497 VAL 497 497 497 VAL VAL B . n 
B 2 498 ILE 498 498 498 ILE ILE B . n 
B 2 499 GLU 499 499 499 GLU GLU B . n 
B 2 500 ALA 500 500 500 ALA ALA B . n 
B 2 501 ALA 501 501 501 ALA ALA B . n 
B 2 502 THR 502 502 502 THR THR B . n 
B 2 503 ALA 503 503 503 ALA ALA B . n 
B 2 504 ALA 504 504 504 ALA ALA B . n 
B 2 505 TYR 505 505 505 TYR TYR B . n 
B 2 506 VAL 506 506 506 VAL VAL B . n 
B 2 507 ASP 507 507 507 ASP ASP B . n 
B 2 508 ARG 508 508 508 ARG ARG B . n 
B 2 509 PHE 509 509 509 PHE PHE B . n 
B 2 510 VAL 510 510 510 VAL VAL B . n 
B 2 511 HIS 511 511 511 HIS HIS B . n 
B 2 512 THR 512 512 512 THR THR B . n 
B 2 513 LEU 513 513 513 LEU LEU B . n 
B 2 514 PRO 514 514 514 PRO PRO B . n 
B 2 515 ASN 515 515 515 ASN ASN B . n 
B 2 516 GLY 516 516 516 GLY GLY B . n 
B 2 517 TYR 517 517 517 TYR TYR B . n 
B 2 518 ASP 518 518 518 ASP ASP B . n 
B 2 519 THR 519 519 519 THR THR B . n 
B 2 520 ARG 520 520 520 ARG ARG B . n 
B 2 521 VAL 521 521 521 VAL VAL B . n 
B 2 522 ASP 522 522 522 ASP ASP B . n 
B 2 523 ASP 523 523 523 ASP ASP B . n 
B 2 524 ASP 524 524 524 ASP ASP B . n 
B 2 525 GLY 525 525 525 GLY GLY B . n 
B 2 526 GLY 526 526 526 GLY GLY B . n 
B 2 527 ALA 527 527 527 ALA ALA B . n 
B 2 528 ILE 528 528 528 ILE ILE B . n 
B 2 529 SER 529 529 529 SER SER B . n 
B 2 530 ALA 530 530 530 ALA ALA B . n 
B 2 531 GLY 531 531 531 GLY GLY B . n 
B 2 532 GLU 532 532 532 GLU GLU B . n 
B 2 533 LYS 533 533 533 LYS LYS B . n 
B 2 534 GLN 534 534 534 GLN GLN B . n 
B 2 535 LEU 535 535 535 LEU LEU B . n 
B 2 536 ILE 536 536 536 ILE ILE B . n 
B 2 537 THR 537 537 537 THR THR B . n 
B 2 538 ILE 538 538 538 ILE ILE B . n 
B 2 539 ALA 539 539 539 ALA ALA B . n 
B 2 540 ARG 540 540 540 ARG ARG B . n 
B 2 541 ALA 541 541 541 ALA ALA B . n 
B 2 542 VAL 542 542 542 VAL VAL B . n 
B 2 543 LEU 543 543 543 LEU LEU B . n 
B 2 544 ALA 544 544 544 ALA ALA B . n 
B 2 545 ARG 545 545 545 ARG ARG B . n 
B 2 546 PRO 546 546 546 PRO PRO B . n 
B 2 547 LYS 547 547 547 LYS LYS B . n 
B 2 548 LEU 548 548 548 LEU LEU B . n 
B 2 549 LEU 549 549 549 LEU LEU B . n 
B 2 550 VAL 550 550 550 VAL VAL B . n 
B 2 551 LEU 551 551 551 LEU LEU B . n 
B 2 552 ASP 552 552 552 ASP ASP B . n 
B 2 553 GLU 553 553 553 GLU GLU B . n 
B 2 554 ALA 554 554 554 ALA ALA B . n 
B 2 555 THR 555 555 555 THR THR B . n 
B 2 556 SER 556 556 556 SER SER B . n 
B 2 557 SER 557 557 557 SER SER B . n 
B 2 558 VAL 558 558 558 VAL VAL B . n 
B 2 559 ASP 559 559 559 ASP ASP B . n 
B 2 560 THR 560 560 560 THR THR B . n 
B 2 561 ARG 561 561 561 ARG ARG B . n 
B 2 562 THR 562 562 562 THR THR B . n 
B 2 563 GLU 563 563 563 GLU GLU B . n 
B 2 564 LEU 564 564 564 LEU LEU B . n 
B 2 565 LEU 565 565 565 LEU LEU B . n 
B 2 566 ILE 566 566 566 ILE ILE B . n 
B 2 567 ALA 567 567 567 ALA ALA B . n 
B 2 568 HIS 568 568 568 HIS HIS B . n 
B 2 569 ALA 569 569 569 ALA ALA B . n 
B 2 570 MET 570 570 570 MET MET B . n 
B 2 571 ALA 571 571 571 ALA ALA B . n 
B 2 572 GLU 572 572 572 GLU GLU B . n 
B 2 573 LEU 573 573 573 LEU LEU B . n 
B 2 574 ARG 574 574 574 ARG ARG B . n 
B 2 575 ARG 575 575 575 ARG ARG B . n 
B 2 576 ASP 576 576 576 ASP ASP B . n 
B 2 577 ARG 577 577 577 ARG ARG B . n 
B 2 578 THR 578 578 578 THR THR B . n 
B 2 579 SER 579 579 579 SER SER B . n 
B 2 580 PHE 580 580 580 PHE PHE B . n 
B 2 581 ILE 581 581 581 ILE ILE B . n 
B 2 582 ILE 582 582 582 ILE ILE B . n 
B 2 583 ALA 583 583 583 ALA ALA B . n 
B 2 584 HIS 584 584 584 HIS HIS B . n 
B 2 585 ARG 585 585 585 ARG ARG B . n 
B 2 586 LEU 586 586 586 LEU LEU B . n 
B 2 587 SER 587 587 587 SER SER B . n 
B 2 588 THR 588 588 588 THR THR B . n 
B 2 589 ILE 589 589 589 ILE ILE B . n 
B 2 590 ARG 590 590 590 ARG ARG B . n 
B 2 591 ASP 591 591 591 ASP ASP B . n 
B 2 592 ALA 592 592 592 ALA ALA B . n 
B 2 593 ASP 593 593 593 ASP ASP B . n 
B 2 594 LEU 594 594 594 LEU LEU B . n 
B 2 595 ILE 595 595 595 ILE ILE B . n 
B 2 596 LEU 596 596 596 LEU LEU B . n 
B 2 597 VAL 597 597 597 VAL VAL B . n 
B 2 598 MET 598 598 598 MET MET B . n 
B 2 599 ASP 599 599 599 ASP ASP B . n 
B 2 600 SER 600 600 600 SER SER B . n 
B 2 601 GLY 601 601 601 GLY GLY B . n 
B 2 602 ARG 602 602 602 ARG ARG B . n 
B 2 603 ILE 603 603 603 ILE ILE B . n 
B 2 604 ILE 604 604 604 ILE ILE B . n 
B 2 605 GLU 605 605 605 GLU GLU B . n 
B 2 606 ARG 606 606 606 ARG ARG B . n 
B 2 607 GLY 607 607 607 GLY GLY B . n 
B 2 608 THR 608 608 608 THR THR B . n 
B 2 609 HIS 609 609 609 HIS HIS B . n 
B 2 610 GLU 610 610 610 GLU GLU B . n 
B 2 611 GLU 611 611 611 GLU GLU B . n 
B 2 612 LEU 612 612 612 LEU LEU B . n 
B 2 613 LEU 613 613 613 LEU LEU B . n 
B 2 614 ALA 614 614 614 ALA ALA B . n 
B 2 615 ARG 615 615 615 ARG ARG B . n 
B 2 616 HIS 616 616 616 HIS HIS B . n 
B 2 617 GLY 617 617 617 GLY GLY B . n 
B 2 618 ARG 618 618 618 ARG ARG B . n 
B 2 619 TYR 619 619 619 TYR TYR B . n 
B 2 620 TRP 620 620 620 TRP TRP B . n 
B 2 621 GLU 621 621 621 GLU GLU B . n 
B 2 622 MET 622 622 622 MET MET B . n 
B 2 623 THR 623 623 623 THR THR B . n 
B 2 624 ARG 624 624 624 ARG ARG B . n 
B 2 625 VAL 625 625 625 VAL VAL B . n 
B 2 626 HIS 626 626 626 HIS HIS B . n 
B 2 627 LEU 627 627 627 LEU LEU B . n 
B 2 628 GLY 628 628 628 GLY GLY B . n 
B 2 629 GLY 629 629 629 GLY GLY B . n 
B 2 630 ILE 630 630 ?   ?   ?   B . n 
B 2 631 LYS 631 631 ?   ?   ?   B . n 
B 2 632 ALA 632 632 ?   ?   ?   B . n 
B 2 633 PHE 633 633 ?   ?   ?   B . n 
B 2 634 HIS 634 634 ?   ?   ?   B . n 
B 2 635 HIS 635 635 ?   ?   ?   B . n 
B 2 636 HIS 636 636 ?   ?   ?   B . n 
B 2 637 HIS 637 637 ?   ?   ?   B . n 
B 2 638 HIS 638 638 ?   ?   ?   B . n 
B 2 639 HIS 639 639 ?   ?   ?   B . n 
B 2 640 HIS 640 640 ?   ?   ?   B . n 
B 2 641 HIS 641 641 ?   ?   ?   B . n 
B 2 642 HIS 642 642 ?   ?   ?   B . n 
B 2 643 HIS 643 643 ?   ?   ?   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 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 VO4 ? ? VO4 ? ? '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 ATP 1 601 1 ATP ATP A . 
D 4 MG  1 602 5 MG  MG  A . 
E 5 ADP 1 701 1 ADP ADP B . 
F 6 VO4 1 702 2 VO4 VO4 B . 
G 4 MG  1 703 5 MG  MG  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                     9IQG 
_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                         9IQG 
_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                   9IQG 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9IQG 
_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' ? 0.003 ? 9292  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.515 ? 12662 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 8.476 ? 1358  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 1522  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 1616  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9IQG 
_struct.title                        
'Cryo-EM structure of MsRv1273c/72c from Mycobacterium smegmatis in the ATP|ADP+Vi-bound Occ (Vi) state' 
_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        9IQG 
_struct_keywords.text            'ABC Transporter, exporter, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT 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 ? 
E N N 5 ? 
F N N 6 ? 
G 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 UNP A0R271_MYCS2 A0R271 ? 1 
;MLWALLRQYVRPYRWLLAVVAVLQVISNMASLYLPTVNAAIIDDGVAKGDTARIVELGAVMLGVTALQVVCAVGAVFFGA
RAATGFGHDLRAAVFTHVTTFSAEEAGRFGAASLLTRTTNDVGHIQQLVQLTVTMLITAPIMSIGGIFMALHQDAGLSWL
LLVSVPVLGLANYWIIRHLMPVFTRMQSLIDGINRVLRDQLSGIRVIRAFAREPLERVRFAEANQTLSDSALEAGRWQAL
MLPVTTLVINVSSVALIWFGGLRIDAGQMQVGSLIAFLAYFMQILMAVLMATFMLVIFPRAAVCADRIGEVLSTQTAITN
PADPVRPAAIAGDIGVHDATFCYPGADRPVLQDVSFTVPRGTTTAVVGSTGSGKSTLISLICRLYDVTSGSLRIDGVDVR
DLDIEQLWSAIGLVPQRGYLFSGTVAENLRYGRADATDDEMWEALRVAAAADFVRAHPQGLDMPVAQGGINFSGGQRQRL
AIARAVIRRPAIYLFDDAFSALDVHTDARVRDALREVAADATVVIVSQRISTVIEADQVVVIDDGRVVGIGTHDTLLADC
PIYAEFAESQALTAGEPR
;
1 
2 UNP I7GDB1_MYCS2 I7GDB1 ? 2 
;MRRGALPQAPLERTRDFKGSAIRLARRLLPQRALTLAVILLGVGGIAIGVIGPRILGHATDLLFNGVIGRELPAGLTKEQ
AVEAARARGDGTFADLLSGMDIVPGQGVDFGAVGRTLALALGLYLVAALLVWVQARLLNVTVQRTMVALRAEVQEKIHRL
PLSYFDSRQRGEVLSRVTNDVDNIQNSVSMTISQLLTSVLTVFAVLVMMLTISPLLTLFTVVTVPASLWVTRWITRRSQP
LFVAQWRNTGRLAAHLEETYSGFTIVKTFGHREAAAGKFAELNSETQQSSFGAQFFSGLVSPATMFIGNLSYVAVAVVGG
LQVATGQITLGSIQAFIQYVRQFNQPLTQVAGMYNTLQSGIASAERVFDLLDTEEESADSPRRADVRTGRVEFEHVSFSY
VPGTPVIEDLSLVAEPGSTVAIVGPTGAGKTTLVNLLMRFYDVDSGRITIDGVDIASVSRESLRASIGMVLQDTWLFAGT
IYDNIAYGRPDADEDEVIEAATAAYVDRFVHTLPNGYDTRVDDDGGAISAGEKQLITIARAVLARPKLLVLDEATSSVDT
RTELLIAHAMAELRRDRTSFIIAHRLSTIRDADLILVMDSGRIIERGTHEELLARHGRYWEMTRV
;
6 
# 
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 9IQG A 13 ? 590 ? A0R271 1 ? 578 ? 1 578 
2 2 9IQG B 1  ? 625 ? I7GDB1 6 ? 630 ? 1 625 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9IQG MET A 1   ? UNP A0R271 ? ? 'initiating methionine' -11 1  
1 9IQG PRO A 2   ? UNP A0R271 ? ? 'expression tag'        -10 2  
1 9IQG GLU A 3   ? UNP A0R271 ? ? 'expression tag'        -9  3  
1 9IQG VAL A 4   ? UNP A0R271 ? ? 'expression tag'        -8  4  
1 9IQG VAL A 5   ? UNP A0R271 ? ? 'expression tag'        -7  5  
1 9IQG GLY A 6   ? UNP A0R271 ? ? 'expression tag'        -6  6  
1 9IQG SER A 7   ? UNP A0R271 ? ? 'expression tag'        -5  7  
1 9IQG TYR A 8   ? UNP A0R271 ? ? 'expression tag'        -4  8  
1 9IQG PHE A 9   ? UNP A0R271 ? ? 'expression tag'        -3  9  
1 9IQG GLN A 10  ? UNP A0R271 ? ? 'expression tag'        -2  10 
1 9IQG SER A 11  ? UNP A0R271 ? ? 'expression tag'        -1  11 
1 9IQG ASN A 12  ? UNP A0R271 ? ? 'expression tag'        0   12 
2 9IQG HIS B 626 ? UNP I7GDB1 ? ? 'expression tag'        626 13 
2 9IQG LEU B 627 ? UNP I7GDB1 ? ? 'expression tag'        627 14 
2 9IQG GLY B 628 ? UNP I7GDB1 ? ? 'expression tag'        628 15 
2 9IQG GLY B 629 ? UNP I7GDB1 ? ? 'expression tag'        629 16 
2 9IQG ILE B 630 ? UNP I7GDB1 ? ? 'expression tag'        630 17 
2 9IQG LYS B 631 ? UNP I7GDB1 ? ? 'expression tag'        631 18 
2 9IQG ALA B 632 ? UNP I7GDB1 ? ? 'expression tag'        632 19 
2 9IQG PHE B 633 ? UNP I7GDB1 ? ? 'expression tag'        633 20 
2 9IQG HIS B 634 ? UNP I7GDB1 ? ? 'expression tag'        634 21 
2 9IQG HIS B 635 ? UNP I7GDB1 ? ? 'expression tag'        635 22 
2 9IQG HIS B 636 ? UNP I7GDB1 ? ? 'expression tag'        636 23 
2 9IQG HIS B 637 ? UNP I7GDB1 ? ? 'expression tag'        637 24 
2 9IQG HIS B 638 ? UNP I7GDB1 ? ? 'expression tag'        638 25 
2 9IQG HIS B 639 ? UNP I7GDB1 ? ? 'expression tag'        639 26 
2 9IQG HIS B 640 ? UNP I7GDB1 ? ? 'expression tag'        640 27 
2 9IQG HIS B 641 ? UNP I7GDB1 ? ? 'expression tag'        641 28 
2 9IQG HIS B 642 ? UNP I7GDB1 ? ? 'expression tag'        642 29 
2 9IQG HIS B 643 ? UNP I7GDB1 ? ? 'expression tag'        643 30 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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,E,F,G 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 11  ? VAL A 22  ? SER A -1  VAL A 10  1 ? 12 
HELX_P HELX_P2  AA2 TYR A 25  ? GLY A 57  ? TYR A 13  GLY A 45  1 ? 33 
HELX_P HELX_P3  AA3 ASP A 62  ? THR A 111 ? ASP A 50  THR A 99  1 ? 50 
HELX_P HELX_P4  AA4 SER A 114 ? ARG A 120 ? SER A 102 ARG A 108 1 ? 7  
HELX_P HELX_P5  AA5 GLY A 122 ? MET A 147 ? GLY A 110 MET A 135 1 ? 26 
HELX_P HELX_P6  AA6 ILE A 149 ? ASP A 166 ? ILE A 137 ASP A 154 1 ? 18 
HELX_P HELX_P7  AA7 LEU A 169 ? GLY A 215 ? LEU A 157 GLY A 203 1 ? 47 
HELX_P HELX_P8  AA8 GLY A 215 ? ALA A 223 ? GLY A 203 ALA A 211 1 ? 9  
HELX_P HELX_P9  AA9 ARG A 224 ? ALA A 251 ? ARG A 212 ALA A 239 1 ? 28 
HELX_P HELX_P10 AB1 LEU A 252 ? ALA A 278 ? LEU A 240 ALA A 266 1 ? 27 
HELX_P HELX_P11 AB2 VAL A 283 ? MET A 306 ? VAL A 271 MET A 294 1 ? 24 
HELX_P HELX_P12 AB3 VAL A 308 ? SER A 325 ? VAL A 296 SER A 313 1 ? 18 
HELX_P HELX_P13 AB4 GLY A 385 ? CYS A 394 ? GLY A 373 CYS A 382 1 ? 10 
HELX_P HELX_P14 AB5 ARG A 405 ? VAL A 409 ? ARG A 393 VAL A 397 5 ? 5  
HELX_P HELX_P15 AB6 GLU A 417 ? ALA A 422 ? GLU A 405 ALA A 410 1 ? 6  
HELX_P HELX_P16 AB7 VAL A 437 ? TYR A 443 ? VAL A 425 TYR A 431 1 ? 7  
HELX_P HELX_P17 AB8 THR A 449 ? ALA A 460 ? THR A 437 ALA A 448 1 ? 12 
HELX_P HELX_P18 AB9 ALA A 462 ? ALA A 468 ? ALA A 450 ALA A 456 1 ? 7  
HELX_P HELX_P19 AC1 GLN A 471 ? ASP A 474 ? GLN A 459 ASP A 462 5 ? 4  
HELX_P HELX_P20 AC2 SER A 485 ? ARG A 501 ? SER A 473 ARG A 489 1 ? 17 
HELX_P HELX_P21 AC3 ASP A 515 ? ALA A 530 ? ASP A 503 ALA A 518 1 ? 16 
HELX_P HELX_P22 AC4 ALA A 531 ? ALA A 533 ? ALA A 519 ALA A 521 5 ? 3  
HELX_P HELX_P23 AC5 ARG A 541 ? ILE A 546 ? ARG A 529 ILE A 534 1 ? 6  
HELX_P HELX_P24 AC6 THR A 564 ? CYS A 572 ? THR A 552 CYS A 560 1 ? 9  
HELX_P HELX_P25 AC7 CYS A 572 ? ALA A 583 ? CYS A 560 ALA A 571 1 ? 12 
HELX_P HELX_P26 AC8 ASP B 16  ? LEU B 29  ? ASP B 16  LEU B 29  1 ? 14 
HELX_P HELX_P27 AC9 LEU B 34  ? GLU B 71  ? LEU B 34  GLU B 71  1 ? 38 
HELX_P HELX_P28 AD1 THR B 77  ? ARG B 88  ? THR B 77  ARG B 88  1 ? 12 
HELX_P HELX_P29 AD2 GLY B 91  ? GLY B 99  ? GLY B 91  GLY B 99  1 ? 9  
HELX_P HELX_P30 AD3 ASP B 109 ? LEU B 160 ? ASP B 109 LEU B 160 1 ? 52 
HELX_P HELX_P31 AD4 PRO B 161 ? SER B 167 ? PRO B 161 SER B 167 1 ? 7  
HELX_P HELX_P32 AD5 GLN B 169 ? THR B 178 ? GLN B 169 THR B 178 1 ? 10 
HELX_P HELX_P33 AD6 THR B 178 ? SER B 213 ? THR B 178 SER B 213 1 ? 36 
HELX_P HELX_P34 AD7 SER B 213 ? VAL B 222 ? SER B 213 VAL B 222 1 ? 10 
HELX_P HELX_P35 AD8 VAL B 222 ? GLY B 262 ? VAL B 222 GLY B 262 1 ? 41 
HELX_P HELX_P36 AD9 GLY B 262 ? PHE B 269 ? GLY B 262 PHE B 269 1 ? 8  
HELX_P HELX_P37 AE1 HIS B 271 ? LEU B 299 ? HIS B 271 LEU B 299 1 ? 29 
HELX_P HELX_P38 AE2 LEU B 299 ? GLY B 326 ? LEU B 299 GLY B 326 1 ? 28 
HELX_P HELX_P39 AE3 THR B 329 ? MET B 353 ? THR B 329 MET B 353 1 ? 25 
HELX_P HELX_P40 AE4 MET B 353 ? ASP B 372 ? MET B 353 ASP B 372 1 ? 20 
HELX_P HELX_P41 AE5 GLY B 429 ? MET B 438 ? GLY B 429 MET B 438 1 ? 10 
HELX_P HELX_P42 AE6 ALA B 456 ? VAL B 458 ? ALA B 456 VAL B 458 5 ? 3  
HELX_P HELX_P43 AE7 SER B 459 ? SER B 466 ? SER B 459 SER B 466 1 ? 8  
HELX_P HELX_P44 AE8 ILE B 481 ? TYR B 487 ? ILE B 481 TYR B 487 1 ? 7  
HELX_P HELX_P45 AE9 ASP B 493 ? ALA B 504 ? ASP B 493 ALA B 504 1 ? 12 
HELX_P HELX_P46 AF1 TYR B 505 ? HIS B 511 ? TYR B 505 HIS B 511 1 ? 7  
HELX_P HELX_P47 AF2 SER B 529 ? ALA B 544 ? SER B 529 ALA B 544 1 ? 16 
HELX_P HELX_P48 AF3 ASP B 559 ? ARG B 575 ? ASP B 559 ARG B 575 1 ? 17 
HELX_P HELX_P49 AF4 THR B 608 ? HIS B 616 ? THR B 608 HIS B 616 1 ? 9  
HELX_P HELX_P50 AF5 HIS B 616 ? GLY B 628 ? HIS B 616 GLY B 628 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A SER 387 OG  ? ? ? 1_555 D MG . MG ? ? A SER 375 A MG 602 1_555 ? ? ? ? ? ? ? 1.936 ? ? 
metalc2 metalc ? ? A GLN 428 OE1 ? ? ? 1_555 D MG . MG ? ? A GLN 416 A MG 602 1_555 ? ? ? ? ? ? ? 1.913 ? ? 
metalc3 metalc ? ? C ATP .   O3G ? ? ? 1_555 D MG . MG ? ? A ATP 601 A MG 602 1_555 ? ? ? ? ? ? ? 2.779 ? ? 
metalc4 metalc ? ? C ATP .   O2B ? ? ? 1_555 D MG . MG ? ? A ATP 601 A MG 602 1_555 ? ? ? ? ? ? ? 2.972 ? ? 
metalc5 metalc ? ? C ATP .   O3B ? ? ? 1_555 D MG . MG ? ? A ATP 601 A MG 602 1_555 ? ? ? ? ? ? ? 2.628 ? ? 
metalc6 metalc ? ? B THR 431 OG1 ? ? ? 1_555 G MG . MG ? ? B THR 431 B MG 703 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc7 metalc ? ? B GLN 472 OE1 ? ? ? 1_555 G MG . MG ? ? B GLN 472 B MG 703 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc8 metalc ? ? F VO4 .   O4  ? ? ? 1_555 G MG . MG ? ? B VO4 702 B MG 703 1_555 ? ? ? ? ? ? ? 1.952 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 387 ? A SER 375 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 OE1 ? A GLN 428 ? A GLN 416 ? 1_555 99.7  ? 
2  OG  ? A SER 387 ? A SER 375 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O3G ? C ATP .   ? A ATP 601 ? 1_555 174.2 ? 
3  OE1 ? A GLN 428 ? A GLN 416 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O3G ? C ATP .   ? A ATP 601 ? 1_555 76.9  ? 
4  OG  ? A SER 387 ? A SER 375 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C ATP .   ? A ATP 601 ? 1_555 80.9  ? 
5  OE1 ? A GLN 428 ? A GLN 416 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C ATP .   ? A ATP 601 ? 1_555 167.4 ? 
6  O3G ? C ATP .   ? A ATP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C ATP .   ? A ATP 601 ? 1_555 101.3 ? 
7  OG  ? A SER 387 ? A SER 375 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O3B ? C ATP .   ? A ATP 601 ? 1_555 130.0 ? 
8  OE1 ? A GLN 428 ? A GLN 416 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O3B ? C ATP .   ? A ATP 601 ? 1_555 129.8 ? 
9  O3G ? C ATP .   ? A ATP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O3B ? C ATP .   ? A ATP 601 ? 1_555 54.2  ? 
10 O2B ? C ATP .   ? A ATP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O3B ? C ATP .   ? A ATP 601 ? 1_555 52.7  ? 
11 OG1 ? B THR 431 ? B THR 431 ? 1_555 MG ? G MG . ? B MG 703 ? 1_555 OE1 ? B GLN 472 ? B GLN 472 ? 1_555 113.1 ? 
12 OG1 ? B THR 431 ? B THR 431 ? 1_555 MG ? G MG . ? B MG 703 ? 1_555 O4  ? F VO4 .   ? B VO4 702 ? 1_555 105.2 ? 
13 OE1 ? B GLN 472 ? B GLN 472 ? 1_555 MG ? G MG . ? B MG 703 ? 1_555 O4  ? F VO4 .   ? B VO4 702 ? 1_555 108.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 363 ? VAL A 366 ? LEU A 351 VAL A 354 
AA1 2 HIS A 349 ? PHE A 353 ? HIS A 337 PHE A 341 
AA1 3 SER A 401 ? SER A 403 ? SER A 389 SER A 391 
AA2 1 ILE A 423 ? VAL A 426 ? ILE A 411 VAL A 414 
AA2 2 ILE A 504 ? ASP A 508 ? ILE A 492 ASP A 496 
AA2 3 THR A 534 ? VAL A 538 ? THR A 522 VAL A 526 
AA2 4 THR A 375 ? GLY A 380 ? THR A 363 GLY A 368 
AA2 5 GLN A 550 ? ASP A 555 ? GLN A 538 ASP A 543 
AA2 6 ARG A 558 ? GLY A 563 ? ARG A 546 GLY A 551 
AA3 1 GLY A 435 ? THR A 436 ? GLY A 423 THR A 424 
AA3 2 PRO A 476 ? VAL A 477 ? PRO A 464 VAL A 465 
AA4 1 ILE B 407 ? ALA B 414 ? ILE B 407 ALA B 414 
AA4 2 VAL B 391 ? PHE B 398 ? VAL B 391 PHE B 398 
AA4 3 SER B 445 ? ILE B 450 ? SER B 445 ILE B 450 
AA4 4 VAL B 453 ? ASP B 454 ? VAL B 453 ASP B 454 
AA5 1 ILE B 467 ? VAL B 470 ? ILE B 467 VAL B 470 
AA5 2 LEU B 548 ? ASP B 552 ? LEU B 548 ASP B 552 
AA5 3 PHE B 580 ? ILE B 582 ? PHE B 580 ILE B 582 
AA5 4 VAL B 420 ? VAL B 423 ? VAL B 420 VAL B 423 
AA5 5 LEU B 594 ? MET B 598 ? LEU B 594 MET B 598 
AA5 6 ILE B 603 ? GLY B 607 ? ILE B 603 GLY B 607 
AA6 1 GLY B 479 ? THR B 480 ? GLY B 479 THR B 480 
AA6 2 ARG B 520 ? VAL B 521 ? ARG B 520 VAL B 521 
# 
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 366 ? O VAL A 354 N ALA A 351 ? N ALA A 339 
AA1 2 3 N THR A 352 ? N THR A 340 O SER A 401 ? O SER A 389 
AA2 1 2 N GLY A 424 ? N GLY A 412 O ILE A 504 ? O ILE A 492 
AA2 2 3 N PHE A 507 ? N PHE A 495 O VAL A 538 ? O VAL A 526 
AA2 3 4 O VAL A 535 ? O VAL A 523 N THR A 376 ? N THR A 364 
AA2 4 5 N ALA A 377 ? N ALA A 365 O VAL A 552 ? O VAL A 540 
AA2 5 6 N VAL A 553 ? N VAL A 541 O VAL A 560 ? O VAL A 548 
AA3 1 2 N GLY A 435 ? N GLY A 423 O VAL A 477 ? O VAL A 465 
AA4 1 2 O ALA B 414 ? O ALA B 414 N VAL B 391 ? N VAL B 391 
AA4 2 3 N SER B 397 ? N SER B 397 O SER B 445 ? O SER B 445 
AA4 3 4 N ILE B 450 ? N ILE B 450 O VAL B 453 ? O VAL B 453 
AA5 1 2 N GLY B 468 ? N GLY B 468 O LEU B 548 ? O LEU B 548 
AA5 2 3 N LEU B 549 ? N LEU B 549 O PHE B 580 ? O PHE B 580 
AA5 3 4 O ILE B 581 ? O ILE B 581 N ILE B 422 ? N ILE B 422 
AA5 4 5 N ALA B 421 ? N ALA B 421 O LEU B 596 ? O LEU B 596 
AA5 5 6 N VAL B 597 ? N VAL B 597 O GLU B 605 ? O GLU B 605 
AA6 1 2 N GLY B 479 ? N GLY B 479 O VAL B 521 ? O VAL B 521 
# 
_pdbx_entry_details.entry_id                   9IQG 
_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_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 119 ? ? -109.31 -60.48  
2  1 MET A 294 ? ? -96.88  33.90   
3  1 ALA A 322 ? ? -136.50 -40.37  
4  1 ASP A 323 ? ? -160.80 88.05   
5  1 ALA A 331 ? ? -144.13 21.45   
6  1 VAL A 336 ? ? 45.00   77.58   
7  1 GLU A 405 ? ? -134.23 -39.88  
8  1 ALA A 434 ? ? 73.13   -6.17   
9  1 ASP A 544 ? ? 68.88   -2.85   
10 1 PRO B 30  ? ? -72.96  -169.86 
11 1 ASP B 90  ? ? 73.74   -11.82  
12 1 VAL B 401 ? ? 45.21   76.83   
13 1 ARG B 489 ? ? -150.85 89.32   
14 1 TYR B 517 ? ? 71.89   -7.35   
15 1 ALA B 527 ? ? -91.96  34.33   
16 1 ARG B 545 ? ? 36.23   58.95   
17 1 ASP B 591 ? ? 56.50   14.03   
18 1 HIS B 616 ? ? 64.99   -125.08 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9IQG 
_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                    9IQG 
_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                  2.70 
_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               406431 
_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            8.0 
# 
_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                 MsRv1273c/72c,MSMEG_5008-MSMEG_5009 
_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                        9IQG 
_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             1800 
_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_vitrification.entry_id              9IQG 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_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                9IQG 
_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 -11 ? A MET 1   
2  1 Y 1 A PRO -10 ? A PRO 2   
3  1 Y 1 A GLU -9  ? A GLU 3   
4  1 Y 1 A VAL -8  ? A VAL 4   
5  1 Y 1 A VAL -7  ? A VAL 5   
6  1 Y 1 A GLY -6  ? A GLY 6   
7  1 Y 1 A SER -5  ? A SER 7   
8  1 Y 1 A TYR -4  ? A TYR 8   
9  1 Y 1 A PHE -3  ? A PHE 9   
10 1 Y 1 A THR 573 ? A THR 585 
11 1 Y 1 A ALA 574 ? A ALA 586 
12 1 Y 1 A GLY 575 ? A GLY 587 
13 1 Y 1 A GLU 576 ? A GLU 588 
14 1 Y 1 A PRO 577 ? A PRO 589 
15 1 Y 1 A ARG 578 ? A ARG 590 
16 1 Y 1 B MET 1   ? B MET 1   
17 1 Y 1 B ARG 2   ? B ARG 2   
18 1 Y 1 B ARG 3   ? B ARG 3   
19 1 Y 1 B GLY 4   ? B GLY 4   
20 1 Y 1 B ALA 5   ? B ALA 5   
21 1 Y 1 B LEU 6   ? B LEU 6   
22 1 Y 1 B PRO 7   ? B PRO 7   
23 1 Y 1 B GLN 8   ? B GLN 8   
24 1 Y 1 B ALA 9   ? B ALA 9   
25 1 Y 1 B PRO 10  ? B PRO 10  
26 1 Y 1 B LEU 11  ? B LEU 11  
27 1 Y 1 B GLU 12  ? B GLU 12  
28 1 Y 1 B ARG 13  ? B ARG 13  
29 1 Y 1 B ILE 630 ? B ILE 630 
30 1 Y 1 B LYS 631 ? B LYS 631 
31 1 Y 1 B ALA 632 ? B ALA 632 
32 1 Y 1 B PHE 633 ? B PHE 633 
33 1 Y 1 B HIS 634 ? B HIS 634 
34 1 Y 1 B HIS 635 ? B HIS 635 
35 1 Y 1 B HIS 636 ? B HIS 636 
36 1 Y 1 B HIS 637 ? B HIS 637 
37 1 Y 1 B HIS 638 ? B HIS 638 
38 1 Y 1 B HIS 639 ? B HIS 639 
39 1 Y 1 B HIS 640 ? B HIS 640 
40 1 Y 1 B HIS 641 ? B HIS 641 
41 1 Y 1 B HIS 642 ? B HIS 642 
42 1 Y 1 B HIS 643 ? B HIS 643 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
ATP PG     P  N N 116 
ATP O1G    O  N N 117 
ATP O2G    O  N N 118 
ATP O3G    O  N N 119 
ATP PB     P  N R 120 
ATP O1B    O  N N 121 
ATP O2B    O  N N 122 
ATP O3B    O  N N 123 
ATP PA     P  N R 124 
ATP O1A    O  N N 125 
ATP O2A    O  N N 126 
ATP O3A    O  N N 127 
ATP "O5'"  O  N N 128 
ATP "C5'"  C  N N 129 
ATP "C4'"  C  N R 130 
ATP "O4'"  O  N N 131 
ATP "C3'"  C  N S 132 
ATP "O3'"  O  N N 133 
ATP "C2'"  C  N R 134 
ATP "O2'"  O  N N 135 
ATP "C1'"  C  N R 136 
ATP N9     N  Y N 137 
ATP C8     C  Y N 138 
ATP N7     N  Y N 139 
ATP C5     C  Y N 140 
ATP C6     C  Y N 141 
ATP N6     N  N N 142 
ATP N1     N  Y N 143 
ATP C2     C  Y N 144 
ATP N3     N  Y N 145 
ATP C4     C  Y N 146 
ATP HOG2   H  N N 147 
ATP HOG3   H  N N 148 
ATP HOB2   H  N N 149 
ATP HOA2   H  N N 150 
ATP "H5'1" H  N N 151 
ATP "H5'2" H  N N 152 
ATP "H4'"  H  N N 153 
ATP "H3'"  H  N N 154 
ATP "HO3'" H  N N 155 
ATP "H2'"  H  N N 156 
ATP "HO2'" H  N N 157 
ATP "H1'"  H  N N 158 
ATP H8     H  N N 159 
ATP HN61   H  N N 160 
ATP HN62   H  N N 161 
ATP H2     H  N N 162 
CYS N      N  N N 163 
CYS CA     C  N R 164 
CYS C      C  N N 165 
CYS O      O  N N 166 
CYS CB     C  N N 167 
CYS SG     S  N N 168 
CYS OXT    O  N N 169 
CYS H      H  N N 170 
CYS H2     H  N N 171 
CYS HA     H  N N 172 
CYS HB2    H  N N 173 
CYS HB3    H  N N 174 
CYS HG     H  N N 175 
CYS HXT    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
VO4 V      V  N N 478 
VO4 O1     O  N N 479 
VO4 O2     O  N N 480 
VO4 O3     O  N N 481 
VO4 O4     O  N N 482 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
VO4 V     O1     doub N N 467 
VO4 V     O2     sing N N 468 
VO4 V     O3     sing N N 469 
VO4 V     O4     sing N N 470 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-12 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9IQG 
_em_admin.last_update        2025-05-14 
_em_admin.map_release_date   2025-05-14 
_em_admin.title              
'Cryo-EM structure of MsRv1273c/72c from Mycobacterium smegmatis in the ATP|ADP+Vi-bound Occ (Vi) state' 
# 
_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          246196 
_em_entity_assembly_naturalsource.organism             'Mycolicibacterium smegmatis MC2 155' 
_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          246196 
_em_entity_assembly_recombinant.organism             'Mycolicibacterium smegmatis MC2 155' 
_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              'FEI FALCON IV (4k 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 ? ? ?      ?            
'MODEL REFINEMENT'         ? 2  ? ? ? PHENIX 1.21.1_5286: 
'IMAGE ACQUISITION'        ? 3  1 1 1 ?      ?            
MASKING                    ? 4  1 1 1 ?      ?            
'CTF CORRECTION'           ? 5  1 ? ? ?      ?            
'LAYERLINE INDEXING'       ? 6  1 1 1 ?      ?            
'DIFFRACTION INDEXING'     ? 7  1 1 1 ?      ?            
'MODEL FITTING'            ? 8  1 1 1 ?      ?            
OTHER                      ? 9  1 1 1 ?      ?            
'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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Science and Technology (MoST, China)' China 2021YFA1300900 1 
'Ministry of Science and Technology (MoST, China)' China 2022YFC230900  2 
'Other government'                                 ?     22ZR1441600    3 
# 
_atom_sites.entry_id                    9IQG 
_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  
MG 
N  
O  
P  
S  
V  
# 
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     . GLN A 1 10  ? 96.096  118.299 104.479 1.00 89.56  ? -2  GLN A N     1 
ATOM   2    C  CA    . GLN A 1 10  ? 96.012  117.172 103.559 1.00 98.86  ? -2  GLN A CA    1 
ATOM   3    C  C     . GLN A 1 10  ? 97.236  116.267 103.688 1.00 98.30  ? -2  GLN A C     1 
ATOM   4    O  O     . GLN A 1 10  ? 98.337  116.625 103.267 1.00 93.24  ? -2  GLN A O     1 
ATOM   5    C  CB    . GLN A 1 10  ? 95.867  117.667 102.117 1.00 101.58 ? -2  GLN A CB    1 
ATOM   6    C  CG    . GLN A 1 10  ? 96.038  116.591 101.048 1.00 95.86  ? -2  GLN A CG    1 
ATOM   7    C  CD    . GLN A 1 10  ? 94.847  115.655 100.942 1.00 103.58 ? -2  GLN A CD    1 
ATOM   8    O  OE1   . GLN A 1 10  ? 94.487  114.971 101.900 1.00 99.08  ? -2  GLN A OE1   1 
ATOM   9    N  NE2   . GLN A 1 10  ? 94.229  115.621 99.767  1.00 107.68 ? -2  GLN A NE2   1 
ATOM   10   N  N     . SER A 1 11  ? 97.033  115.092 104.288 1.00 91.71  ? -1  SER A N     1 
ATOM   11   C  CA    . SER A 1 11  ? 98.090  114.100 104.436 1.00 75.66  ? -1  SER A CA    1 
ATOM   12   C  C     . SER A 1 11  ? 97.564  112.693 104.187 1.00 70.09  ? -1  SER A C     1 
ATOM   13   O  O     . SER A 1 11  ? 98.096  111.723 104.734 1.00 66.77  ? -1  SER A O     1 
ATOM   14   C  CB    . SER A 1 11  ? 98.731  114.177 105.823 1.00 69.39  ? -1  SER A CB    1 
ATOM   15   O  OG    . SER A 1 11  ? 99.006  115.519 106.182 1.00 75.31  ? -1  SER A OG    1 
ATOM   16   N  N     . ASN A 1 12  ? 96.518  112.566 103.367 1.00 74.27  ? 0   ASN A N     1 
ATOM   17   C  CA    . ASN A 1 12  ? 95.910  111.261 103.130 1.00 69.61  ? 0   ASN A CA    1 
ATOM   18   C  C     . ASN A 1 12  ? 96.875  110.315 102.426 1.00 61.59  ? 0   ASN A C     1 
ATOM   19   O  O     . ASN A 1 12  ? 96.910  109.117 102.726 1.00 61.52  ? 0   ASN A O     1 
ATOM   20   C  CB    . ASN A 1 12  ? 94.627  111.423 102.317 1.00 74.73  ? 0   ASN A CB    1 
ATOM   21   C  CG    . ASN A 1 12  ? 93.397  111.558 103.192 1.00 88.65  ? 0   ASN A CG    1 
ATOM   22   O  OD1   . ASN A 1 12  ? 93.389  112.320 104.158 1.00 91.27  ? 0   ASN A OD1   1 
ATOM   23   N  ND2   . ASN A 1 12  ? 92.348  110.816 102.856 1.00 85.92  ? 0   ASN A ND2   1 
ATOM   24   N  N     . MET A 1 13  ? 97.659  110.832 101.477 1.00 59.09  ? 1   MET A N     1 
ATOM   25   C  CA    . MET A 1 13  ? 98.586  109.979 100.743 1.00 52.74  ? 1   MET A CA    1 
ATOM   26   C  C     . MET A 1 13  ? 99.764  109.544 101.605 1.00 47.91  ? 1   MET A C     1 
ATOM   27   O  O     . MET A 1 13  ? 100.290 108.442 101.418 1.00 47.87  ? 1   MET A O     1 
ATOM   28   C  CB    . MET A 1 13  ? 99.081  110.697 99.489  1.00 51.99  ? 1   MET A CB    1 
ATOM   29   C  CG    . MET A 1 13  ? 99.833  109.802 98.522  1.00 49.87  ? 1   MET A CG    1 
ATOM   30   S  SD    . MET A 1 13  ? 98.971  108.259 98.177  1.00 62.25  ? 1   MET A SD    1 
ATOM   31   C  CE    . MET A 1 13  ? 97.669  108.839 97.094  1.00 53.27  ? 1   MET A CE    1 
ATOM   32   N  N     . LEU A 1 14  ? 100.195 110.388 102.544 1.00 46.17  ? 2   LEU A N     1 
ATOM   33   C  CA    . LEU A 1 14  ? 101.308 110.023 103.416 1.00 42.93  ? 2   LEU A CA    1 
ATOM   34   C  C     . LEU A 1 14  ? 100.968 108.801 104.258 1.00 43.33  ? 2   LEU A C     1 
ATOM   35   O  O     . LEU A 1 14  ? 101.767 107.863 104.367 1.00 46.04  ? 2   LEU A O     1 
ATOM   36   C  CB    . LEU A 1 14  ? 101.681 111.208 104.307 1.00 40.79  ? 2   LEU A CB    1 
ATOM   37   C  CG    . LEU A 1 14  ? 102.756 110.972 105.368 1.00 37.90  ? 2   LEU A CG    1 
ATOM   38   C  CD1   . LEU A 1 14  ? 104.052 110.510 104.732 1.00 36.98  ? 2   LEU A CD1   1 
ATOM   39   C  CD2   . LEU A 1 14  ? 102.983 112.232 106.181 1.00 41.86  ? 2   LEU A CD2   1 
ATOM   40   N  N     . TRP A 1 15  ? 99.775  108.791 104.852 1.00 45.09  ? 3   TRP A N     1 
ATOM   41   C  CA    . TRP A 1 15  ? 99.368  107.652 105.663 1.00 45.85  ? 3   TRP A CA    1 
ATOM   42   C  C     . TRP A 1 15  ? 99.202  106.395 104.824 1.00 45.35  ? 3   TRP A C     1 
ATOM   43   O  O     . TRP A 1 15  ? 99.539  105.302 105.285 1.00 45.93  ? 3   TRP A O     1 
ATOM   44   C  CB    . TRP A 1 15  ? 98.079  107.976 106.415 1.00 54.36  ? 3   TRP A CB    1 
ATOM   45   C  CG    . TRP A 1 15  ? 98.203  109.184 107.289 1.00 60.41  ? 3   TRP A CG    1 
ATOM   46   C  CD1   . TRP A 1 15  ? 97.429  110.304 107.252 1.00 64.08  ? 3   TRP A CD1   1 
ATOM   47   C  CD2   . TRP A 1 15  ? 99.163  109.395 108.332 1.00 62.30  ? 3   TRP A CD2   1 
ATOM   48   N  NE1   . TRP A 1 15  ? 97.846  111.201 108.204 1.00 65.29  ? 3   TRP A NE1   1 
ATOM   49   C  CE2   . TRP A 1 15  ? 98.909  110.666 108.881 1.00 64.28  ? 3   TRP A CE2   1 
ATOM   50   C  CE3   . TRP A 1 15  ? 100.211 108.631 108.857 1.00 59.08  ? 3   TRP A CE3   1 
ATOM   51   C  CZ2   . TRP A 1 15  ? 99.661  111.189 109.928 1.00 64.34  ? 3   TRP A CZ2   1 
ATOM   52   C  CZ3   . TRP A 1 15  ? 100.958 109.155 109.894 1.00 63.11  ? 3   TRP A CZ3   1 
ATOM   53   C  CH2   . TRP A 1 15  ? 100.681 110.421 110.418 1.00 65.56  ? 3   TRP A CH2   1 
ATOM   54   N  N     . ALA A 1 16  ? 98.688  106.525 103.599 1.00 48.20  ? 4   ALA A N     1 
ATOM   55   C  CA    . ALA A 1 16  ? 98.567  105.363 102.724 1.00 43.83  ? 4   ALA A CA    1 
ATOM   56   C  C     . ALA A 1 16  ? 99.933  104.780 102.387 1.00 39.43  ? 4   ALA A C     1 
ATOM   57   O  O     . ALA A 1 16  ? 100.122 103.558 102.427 1.00 40.90  ? 4   ALA A O     1 
ATOM   58   C  CB    . ALA A 1 16  ? 97.816  105.742 101.450 1.00 39.63  ? 4   ALA A CB    1 
ATOM   59   N  N     . LEU A 1 17  ? 100.903 105.639 102.065 1.00 39.02  ? 5   LEU A N     1 
ATOM   60   C  CA    . LEU A 1 17  ? 102.247 105.159 101.762 1.00 36.29  ? 5   LEU A CA    1 
ATOM   61   C  C     . LEU A 1 17  ? 102.879 104.485 102.971 1.00 36.32  ? 5   LEU A C     1 
ATOM   62   O  O     . LEU A 1 17  ? 103.508 103.428 102.842 1.00 38.90  ? 5   LEU A O     1 
ATOM   63   C  CB    . LEU A 1 17  ? 103.125 106.311 101.277 1.00 33.60  ? 5   LEU A CB    1 
ATOM   64   C  CG    . LEU A 1 17  ? 102.880 106.813 99.856  1.00 35.79  ? 5   LEU A CG    1 
ATOM   65   C  CD1   . LEU A 1 17  ? 103.927 107.836 99.481  1.00 32.96  ? 5   LEU A CD1   1 
ATOM   66   C  CD2   . LEU A 1 17  ? 102.881 105.659 98.876  1.00 38.70  ? 5   LEU A CD2   1 
ATOM   67   N  N     . LEU A 1 18  ? 102.731 105.084 104.155 1.00 36.50  ? 6   LEU A N     1 
ATOM   68   C  CA    . LEU A 1 18  ? 103.283 104.474 105.359 1.00 30.79  ? 6   LEU A CA    1 
ATOM   69   C  C     . LEU A 1 18  ? 102.637 103.122 105.631 1.00 32.18  ? 6   LEU A C     1 
ATOM   70   O  O     . LEU A 1 18  ? 103.329 102.127 105.872 1.00 38.13  ? 6   LEU A O     1 
ATOM   71   C  CB    . LEU A 1 18  ? 103.102 105.412 106.550 1.00 29.25  ? 6   LEU A CB    1 
ATOM   72   C  CG    . LEU A 1 18  ? 103.909 106.707 106.496 1.00 32.21  ? 6   LEU A CG    1 
ATOM   73   C  CD1   . LEU A 1 18  ? 103.493 107.645 107.610 1.00 43.23  ? 6   LEU A CD1   1 
ATOM   74   C  CD2   . LEU A 1 18  ? 105.389 106.410 106.572 1.00 35.00  ? 6   LEU A CD2   1 
ATOM   75   N  N     . ARG A 1 19  ? 101.308 103.057 105.552 1.00 31.85  ? 7   ARG A N     1 
ATOM   76   C  CA    . ARG A 1 19  ? 100.604 101.805 105.798 1.00 37.80  ? 7   ARG A CA    1 
ATOM   77   C  C     . ARG A 1 19  ? 101.029 100.728 104.808 1.00 43.24  ? 7   ARG A C     1 
ATOM   78   O  O     . ARG A 1 19  ? 101.165 99.555  105.177 1.00 45.99  ? 7   ARG A O     1 
ATOM   79   C  CB    . ARG A 1 19  ? 99.096  102.042 105.728 1.00 39.61  ? 7   ARG A CB    1 
ATOM   80   C  CG    . ARG A 1 19  ? 98.251  100.784 105.758 1.00 44.14  ? 7   ARG A CG    1 
ATOM   81   C  CD    . ARG A 1 19  ? 96.788  101.107 105.506 1.00 50.25  ? 7   ARG A CD    1 
ATOM   82   N  NE    . ARG A 1 19  ? 96.462  102.477 105.884 1.00 61.13  ? 7   ARG A NE    1 
ATOM   83   C  CZ    . ARG A 1 19  ? 95.852  103.349 105.092 1.00 66.90  ? 7   ARG A CZ    1 
ATOM   84   N  NH1   . ARG A 1 19  ? 95.488  103.029 103.861 1.00 60.24  ? 7   ARG A NH1   1 
ATOM   85   N  NH2   . ARG A 1 19  ? 95.602  104.574 105.547 1.00 61.63  ? 7   ARG A NH2   1 
ATOM   86   N  N     . GLN A 1 20  ? 101.253 101.105 103.549 1.00 40.28  ? 8   GLN A N     1 
ATOM   87   C  CA    . GLN A 1 20  ? 101.606 100.108 102.546 1.00 35.46  ? 8   GLN A CA    1 
ATOM   88   C  C     . GLN A 1 20  ? 103.045 99.631  102.700 1.00 35.87  ? 8   GLN A C     1 
ATOM   89   O  O     . GLN A 1 20  ? 103.318 98.431  102.580 1.00 39.12  ? 8   GLN A O     1 
ATOM   90   C  CB    . GLN A 1 20  ? 101.381 100.667 101.144 1.00 35.78  ? 8   GLN A CB    1 
ATOM   91   C  CG    . GLN A 1 20  ? 101.751 99.694  100.043 1.00 37.14  ? 8   GLN A CG    1 
ATOM   92   C  CD    . GLN A 1 20  ? 101.106 100.035 98.722  1.00 48.14  ? 8   GLN A CD    1 
ATOM   93   O  OE1   . GLN A 1 20  ? 100.452 101.067 98.586  1.00 52.62  ? 8   GLN A OE1   1 
ATOM   94   N  NE2   . GLN A 1 20  ? 101.288 99.167  97.735  1.00 51.92  ? 8   GLN A NE2   1 
ATOM   95   N  N     . TYR A 1 21  ? 103.985 100.540 102.958 1.00 32.64  ? 9   TYR A N     1 
ATOM   96   C  CA    . TYR A 1 21  ? 105.396 100.200 102.839 1.00 33.56  ? 9   TYR A CA    1 
ATOM   97   C  C     . TYR A 1 21  ? 106.114 100.056 104.174 1.00 38.48  ? 9   TYR A C     1 
ATOM   98   O  O     . TYR A 1 21  ? 107.330 99.841  104.185 1.00 43.34  ? 9   TYR A O     1 
ATOM   99   C  CB    . TYR A 1 21  ? 106.107 101.226 101.954 1.00 31.58  ? 9   TYR A CB    1 
ATOM   100  C  CG    . TYR A 1 21  ? 105.684 101.110 100.512 1.00 32.33  ? 9   TYR A CG    1 
ATOM   101  C  CD1   . TYR A 1 21  ? 106.112 100.049 99.731  1.00 27.16  ? 9   TYR A CD1   1 
ATOM   102  C  CD2   . TYR A 1 21  ? 104.828 102.038 99.942  1.00 33.62  ? 9   TYR A CD2   1 
ATOM   103  C  CE1   . TYR A 1 21  ? 105.715 99.924  98.423  1.00 27.46  ? 9   TYR A CE1   1 
ATOM   104  C  CE2   . TYR A 1 21  ? 104.426 101.922 98.632  1.00 37.06  ? 9   TYR A CE2   1 
ATOM   105  C  CZ    . TYR A 1 21  ? 104.873 100.863 97.876  1.00 38.27  ? 9   TYR A CZ    1 
ATOM   106  O  OH    . TYR A 1 21  ? 104.474 100.744 96.566  1.00 41.73  ? 9   TYR A OH    1 
ATOM   107  N  N     . VAL A 1 22  ? 105.403 100.142 105.301 1.00 36.51  ? 10  VAL A N     1 
ATOM   108  C  CA    . VAL A 1 22  ? 105.992 99.771  106.582 1.00 34.08  ? 10  VAL A CA    1 
ATOM   109  C  C     . VAL A 1 22  ? 105.420 98.457  107.101 1.00 40.37  ? 10  VAL A C     1 
ATOM   110  O  O     . VAL A 1 22  ? 105.913 97.930  108.111 1.00 46.07  ? 10  VAL A O     1 
ATOM   111  C  CB    . VAL A 1 22  ? 105.813 100.904 107.618 1.00 30.49  ? 10  VAL A CB    1 
ATOM   112  C  CG1   . VAL A 1 22  ? 106.674 100.672 108.832 1.00 33.21  ? 10  VAL A CG1   1 
ATOM   113  C  CG2   . VAL A 1 22  ? 106.183 102.237 107.007 1.00 30.71  ? 10  VAL A CG2   1 
ATOM   114  N  N     . ARG A 1 23  ? 104.427 97.892  106.419 1.00 41.39  ? 11  ARG A N     1 
ATOM   115  C  CA    . ARG A 1 23  ? 103.823 96.635  106.853 1.00 43.20  ? 11  ARG A CA    1 
ATOM   116  C  C     . ARG A 1 23  ? 104.816 95.490  107.035 1.00 42.37  ? 11  ARG A C     1 
ATOM   117  O  O     . ARG A 1 23  ? 104.676 94.749  108.022 1.00 49.78  ? 11  ARG A O     1 
ATOM   118  C  CB    . ARG A 1 23  ? 102.713 96.242  105.867 1.00 45.62  ? 11  ARG A CB    1 
ATOM   119  C  CG    . ARG A 1 23  ? 101.817 95.124  106.360 1.00 54.84  ? 11  ARG A CG    1 
ATOM   120  C  CD    . ARG A 1 23  ? 100.563 95.015  105.516 1.00 63.48  ? 11  ARG A CD    1 
ATOM   121  N  NE    . ARG A 1 23  ? 99.674  96.152  105.719 1.00 75.08  ? 11  ARG A NE    1 
ATOM   122  C  CZ    . ARG A 1 23  ? 98.558  96.110  106.434 1.00 83.27  ? 11  ARG A CZ    1 
ATOM   123  N  NH1   . ARG A 1 23  ? 98.163  94.999  107.034 1.00 81.46  ? 11  ARG A NH1   1 
ATOM   124  N  NH2   . ARG A 1 23  ? 97.819  97.210  106.550 1.00 77.92  ? 11  ARG A NH2   1 
ATOM   125  N  N     . PRO A 1 24  ? 105.801 95.264  106.158 1.00 38.90  ? 12  PRO A N     1 
ATOM   126  C  CA    . PRO A 1 24  ? 106.785 94.205  106.440 1.00 36.63  ? 12  PRO A CA    1 
ATOM   127  C  C     . PRO A 1 24  ? 107.621 94.451  107.685 1.00 37.40  ? 12  PRO A C     1 
ATOM   128  O  O     . PRO A 1 24  ? 108.228 93.503  108.196 1.00 40.52  ? 12  PRO A O     1 
ATOM   129  C  CB    . PRO A 1 24  ? 107.657 94.183  105.177 1.00 35.38  ? 12  PRO A CB    1 
ATOM   130  C  CG    . PRO A 1 24  ? 107.412 95.481  104.509 1.00 38.65  ? 12  PRO A CG    1 
ATOM   131  C  CD    . PRO A 1 24  ? 105.995 95.824  104.810 1.00 39.80  ? 12  PRO A CD    1 
ATOM   132  N  N     . TYR A 1 25  ? 107.681 95.685  108.188 1.00 33.25  ? 13  TYR A N     1 
ATOM   133  C  CA    . TYR A 1 25  ? 108.513 96.028  109.335 1.00 31.24  ? 13  TYR A CA    1 
ATOM   134  C  C     . TYR A 1 25  ? 107.694 96.409  110.565 1.00 39.38  ? 13  TYR A C     1 
ATOM   135  O  O     . TYR A 1 25  ? 108.219 97.044  111.485 1.00 44.18  ? 13  TYR A O     1 
ATOM   136  C  CB    . TYR A 1 25  ? 109.476 97.153  108.959 1.00 33.64  ? 13  TYR A CB    1 
ATOM   137  C  CG    . TYR A 1 25  ? 110.286 96.838  107.726 1.00 31.42  ? 13  TYR A CG    1 
ATOM   138  C  CD1   . TYR A 1 25  ? 111.394 96.007  107.798 1.00 31.66  ? 13  TYR A CD1   1 
ATOM   139  C  CD2   . TYR A 1 25  ? 109.928 97.345  106.487 1.00 30.90  ? 13  TYR A CD2   1 
ATOM   140  C  CE1   . TYR A 1 25  ? 112.131 95.704  106.677 1.00 29.39  ? 13  TYR A CE1   1 
ATOM   141  C  CE2   . TYR A 1 25  ? 110.659 97.045  105.359 1.00 32.22  ? 13  TYR A CE2   1 
ATOM   142  C  CZ    . TYR A 1 25  ? 111.759 96.224  105.461 1.00 34.44  ? 13  TYR A CZ    1 
ATOM   143  O  OH    . TYR A 1 25  ? 112.495 95.919  104.342 1.00 37.10  ? 13  TYR A OH    1 
ATOM   144  N  N     . ARG A 1 26  ? 106.417 96.022  110.607 1.00 41.93  ? 14  ARG A N     1 
ATOM   145  C  CA    . ARG A 1 26  ? 105.594 96.343  111.766 1.00 37.55  ? 14  ARG A CA    1 
ATOM   146  C  C     . ARG A 1 26  ? 106.055 95.596  113.012 1.00 41.38  ? 14  ARG A C     1 
ATOM   147  O  O     . ARG A 1 26  ? 105.939 96.122  114.123 1.00 46.13  ? 14  ARG A O     1 
ATOM   148  C  CB    . ARG A 1 26  ? 104.126 96.044  111.470 1.00 35.04  ? 14  ARG A CB    1 
ATOM   149  C  CG    . ARG A 1 26  ? 103.848 94.613  111.080 1.00 46.70  ? 14  ARG A CG    1 
ATOM   150  C  CD    . ARG A 1 26  ? 102.492 94.479  110.416 1.00 54.18  ? 14  ARG A CD    1 
ATOM   151  N  NE    . ARG A 1 26  ? 102.413 93.270  109.607 1.00 62.39  ? 14  ARG A NE    1 
ATOM   152  C  CZ    . ARG A 1 26  ? 101.977 92.099  110.050 1.00 71.25  ? 14  ARG A CZ    1 
ATOM   153  N  NH1   . ARG A 1 26  ? 101.558 91.944  111.295 1.00 75.68  ? 14  ARG A NH1   1 
ATOM   154  N  NH2   . ARG A 1 26  ? 101.964 91.057  109.225 1.00 68.14  ? 14  ARG A NH2   1 
ATOM   155  N  N     . TRP A 1 27  ? 106.584 94.381  112.859 1.00 42.55  ? 15  TRP A N     1 
ATOM   156  C  CA    . TRP A 1 27  ? 107.104 93.665  114.019 1.00 39.39  ? 15  TRP A CA    1 
ATOM   157  C  C     . TRP A 1 27  ? 108.364 94.329  114.559 1.00 40.68  ? 15  TRP A C     1 
ATOM   158  O  O     . TRP A 1 27  ? 108.560 94.404  115.779 1.00 46.85  ? 15  TRP A O     1 
ATOM   159  C  CB    . TRP A 1 27  ? 107.364 92.204  113.661 1.00 46.09  ? 15  TRP A CB    1 
ATOM   160  C  CG    . TRP A 1 27  ? 106.117 91.451  113.295 1.00 62.32  ? 15  TRP A CG    1 
ATOM   161  C  CD1   . TRP A 1 27  ? 105.872 90.795  112.126 1.00 65.46  ? 15  TRP A CD1   1 
ATOM   162  C  CD2   . TRP A 1 27  ? 104.947 91.276  114.105 1.00 68.02  ? 15  TRP A CD2   1 
ATOM   163  N  NE1   . TRP A 1 27  ? 104.624 90.224  112.155 1.00 67.99  ? 15  TRP A NE1   1 
ATOM   164  C  CE2   . TRP A 1 27  ? 104.036 90.505  113.360 1.00 70.99  ? 15  TRP A CE2   1 
ATOM   165  C  CE3   . TRP A 1 27  ? 104.583 91.697  115.388 1.00 65.22  ? 15  TRP A CE3   1 
ATOM   166  C  CZ2   . TRP A 1 27  ? 102.784 90.145  113.853 1.00 73.80  ? 15  TRP A CZ2   1 
ATOM   167  C  CZ3   . TRP A 1 27  ? 103.340 91.340  115.876 1.00 66.19  ? 15  TRP A CZ3   1 
ATOM   168  C  CH2   . TRP A 1 27  ? 102.456 90.572  115.110 1.00 73.87  ? 15  TRP A CH2   1 
ATOM   169  N  N     . LEU A 1 28  ? 109.229 94.821  113.669 1.00 39.38  ? 16  LEU A N     1 
ATOM   170  C  CA    . LEU A 1 28  ? 110.375 95.604  114.118 1.00 29.75  ? 16  LEU A CA    1 
ATOM   171  C  C     . LEU A 1 28  ? 109.922 96.874  114.820 1.00 28.77  ? 16  LEU A C     1 
ATOM   172  O  O     . LEU A 1 28  ? 110.530 97.293  115.809 1.00 35.78  ? 16  LEU A O     1 
ATOM   173  C  CB    . LEU A 1 28  ? 111.285 95.942  112.939 1.00 31.46  ? 16  LEU A CB    1 
ATOM   174  C  CG    . LEU A 1 28  ? 112.056 94.797  112.289 1.00 29.63  ? 16  LEU A CG    1 
ATOM   175  C  CD1   . LEU A 1 28  ? 113.032 95.340  111.266 1.00 24.72  ? 16  LEU A CD1   1 
ATOM   176  C  CD2   . LEU A 1 28  ? 112.781 93.982  113.340 1.00 28.81  ? 16  LEU A CD2   1 
ATOM   177  N  N     . LEU A 1 29  ? 108.858 97.503  114.319 1.00 28.37  ? 17  LEU A N     1 
ATOM   178  C  CA    . LEU A 1 29  ? 108.315 98.679  114.995 1.00 31.49  ? 17  LEU A CA    1 
ATOM   179  C  C     . LEU A 1 29  ? 107.795 98.335  116.386 1.00 34.27  ? 17  LEU A C     1 
ATOM   180  O  O     . LEU A 1 29  ? 107.974 99.110  117.331 1.00 32.66  ? 17  LEU A O     1 
ATOM   181  C  CB    . LEU A 1 29  ? 107.208 99.310  114.159 1.00 34.99  ? 17  LEU A CB    1 
ATOM   182  C  CG    . LEU A 1 29  ? 107.606 99.906  112.815 1.00 36.59  ? 17  LEU A CG    1 
ATOM   183  C  CD1   . LEU A 1 29  ? 106.458 100.740 112.297 1.00 41.51  ? 17  LEU A CD1   1 
ATOM   184  C  CD2   . LEU A 1 29  ? 108.864 100.740 112.952 1.00 27.47  ? 17  LEU A CD2   1 
ATOM   185  N  N     . ALA A 1 30  ? 107.126 97.191  116.525 1.00 34.20  ? 18  ALA A N     1 
ATOM   186  C  CA    . ALA A 1 30  ? 106.639 96.772  117.837 1.00 30.48  ? 18  ALA A CA    1 
ATOM   187  C  C     . ALA A 1 30  ? 107.794 96.511  118.796 1.00 33.60  ? 18  ALA A C     1 
ATOM   188  O  O     . ALA A 1 30  ? 107.733 96.886  119.975 1.00 40.00  ? 18  ALA A O     1 
ATOM   189  C  CB    . ALA A 1 30  ? 105.763 95.530  117.698 1.00 28.50  ? 18  ALA A CB    1 
ATOM   190  N  N     . VAL A 1 31  ? 108.856 95.867  118.309 1.00 31.66  ? 19  VAL A N     1 
ATOM   191  C  CA    . VAL A 1 31  ? 110.034 95.638  119.143 1.00 29.90  ? 19  VAL A CA    1 
ATOM   192  C  C     . VAL A 1 31  ? 110.656 96.964  119.561 1.00 31.26  ? 19  VAL A C     1 
ATOM   193  O  O     . VAL A 1 31  ? 111.059 97.143  120.717 1.00 34.44  ? 19  VAL A O     1 
ATOM   194  C  CB    . VAL A 1 31  ? 111.047 94.744  118.405 1.00 28.53  ? 19  VAL A CB    1 
ATOM   195  C  CG1   . VAL A 1 31  ? 112.357 94.688  119.164 1.00 22.92  ? 19  VAL A CG1   1 
ATOM   196  C  CG2   . VAL A 1 31  ? 110.482 93.351  118.221 1.00 29.46  ? 19  VAL A CG2   1 
ATOM   197  N  N     . VAL A 1 32  ? 110.748 97.911  118.626 1.00 29.54  ? 20  VAL A N     1 
ATOM   198  C  CA    . VAL A 1 32  ? 111.300 99.225  118.940 1.00 28.19  ? 20  VAL A CA    1 
ATOM   199  C  C     . VAL A 1 32  ? 110.454 99.916  119.996 1.00 30.79  ? 20  VAL A C     1 
ATOM   200  O  O     . VAL A 1 32  ? 110.982 100.526 120.929 1.00 38.64  ? 20  VAL A O     1 
ATOM   201  C  CB    . VAL A 1 32  ? 111.414 100.078 117.664 1.00 28.50  ? 20  VAL A CB    1 
ATOM   202  C  CG1   . VAL A 1 32  ? 111.527 101.551 118.017 1.00 29.81  ? 20  VAL A CG1   1 
ATOM   203  C  CG2   . VAL A 1 32  ? 112.602 99.644  116.852 1.00 27.08  ? 20  VAL A CG2   1 
ATOM   204  N  N     . ALA A 1 33  ? 109.129 99.840  119.864 1.00 30.31  ? 21  ALA A N     1 
ATOM   205  C  CA    . ALA A 1 33  ? 108.248 100.470 120.840 1.00 30.90  ? 21  ALA A CA    1 
ATOM   206  C  C     . ALA A 1 33  ? 108.423 99.856  122.222 1.00 32.40  ? 21  ALA A C     1 
ATOM   207  O  O     . ALA A 1 33  ? 108.480 100.576 123.225 1.00 33.14  ? 21  ALA A O     1 
ATOM   208  C  CB    . ALA A 1 33  ? 106.794 100.357 120.384 1.00 24.89  ? 21  ALA A CB    1 
ATOM   209  N  N     . VAL A 1 34  ? 108.515 98.528  122.294 1.00 31.14  ? 22  VAL A N     1 
ATOM   210  C  CA    . VAL A 1 34  ? 108.684 97.865  123.585 1.00 26.32  ? 22  VAL A CA    1 
ATOM   211  C  C     . VAL A 1 34  ? 110.013 98.262  124.220 1.00 27.47  ? 22  VAL A C     1 
ATOM   212  O  O     . VAL A 1 34  ? 110.079 98.600  125.408 1.00 29.97  ? 22  VAL A O     1 
ATOM   213  C  CB    . VAL A 1 34  ? 108.564 96.340  123.424 1.00 31.86  ? 22  VAL A CB    1 
ATOM   214  C  CG1   . VAL A 1 34  ? 109.066 95.631  124.669 1.00 34.14  ? 22  VAL A CG1   1 
ATOM   215  C  CG2   . VAL A 1 34  ? 107.124 95.957  123.136 1.00 29.02  ? 22  VAL A CG2   1 
ATOM   216  N  N     . LEU A 1 35  ? 111.092 98.236  123.436 1.00 30.82  ? 23  LEU A N     1 
ATOM   217  C  CA    . LEU A 1 35  ? 112.396 98.602  123.982 1.00 29.92  ? 23  LEU A CA    1 
ATOM   218  C  C     . LEU A 1 35  ? 112.428 100.065 124.402 1.00 27.79  ? 23  LEU A C     1 
ATOM   219  O  O     . LEU A 1 35  ? 113.042 100.415 125.417 1.00 32.73  ? 23  LEU A O     1 
ATOM   220  C  CB    . LEU A 1 35  ? 113.496 98.302  122.967 1.00 27.32  ? 23  LEU A CB    1 
ATOM   221  C  CG    . LEU A 1 35  ? 113.755 96.815  122.718 1.00 25.10  ? 23  LEU A CG    1 
ATOM   222  C  CD1   . LEU A 1 35  ? 114.816 96.621  121.657 1.00 21.90  ? 23  LEU A CD1   1 
ATOM   223  C  CD2   . LEU A 1 35  ? 114.157 96.124  124.005 1.00 24.67  ? 23  LEU A CD2   1 
ATOM   224  N  N     . GLN A 1 36  ? 111.767 100.936 123.640 1.00 28.33  ? 24  GLN A N     1 
ATOM   225  C  CA    . GLN A 1 36  ? 111.728 102.349 123.990 1.00 30.02  ? 24  GLN A CA    1 
ATOM   226  C  C     . GLN A 1 36  ? 110.956 102.584 125.279 1.00 31.06  ? 24  GLN A C     1 
ATOM   227  O  O     . GLN A 1 36  ? 111.386 103.379 126.122 1.00 33.95  ? 24  GLN A O     1 
ATOM   228  C  CB    . GLN A 1 36  ? 111.124 103.160 122.846 1.00 33.15  ? 24  GLN A CB    1 
ATOM   229  C  CG    . GLN A 1 36  ? 112.092 103.428 121.713 1.00 38.28  ? 24  GLN A CG    1 
ATOM   230  C  CD    . GLN A 1 36  ? 112.917 104.675 121.933 1.00 43.88  ? 24  GLN A CD    1 
ATOM   231  O  OE1   . GLN A 1 36  ? 113.366 104.949 123.045 1.00 49.81  ? 24  GLN A OE1   1 
ATOM   232  N  NE2   . GLN A 1 36  ? 113.127 105.439 120.870 1.00 46.82  ? 24  GLN A NE2   1 
ATOM   233  N  N     . VAL A 1 37  ? 109.819 101.907 125.462 1.00 30.66  ? 25  VAL A N     1 
ATOM   234  C  CA    . VAL A 1 37  ? 109.091 102.100 126.711 1.00 31.27  ? 25  VAL A CA    1 
ATOM   235  C  C     . VAL A 1 37  ? 109.894 101.547 127.881 1.00 30.00  ? 25  VAL A C     1 
ATOM   236  O  O     . VAL A 1 37  ? 109.915 102.145 128.959 1.00 37.56  ? 25  VAL A O     1 
ATOM   237  C  CB    . VAL A 1 37  ? 107.667 101.503 126.657 1.00 30.41  ? 25  VAL A CB    1 
ATOM   238  C  CG1   . VAL A 1 37  ? 106.892 102.050 125.473 1.00 30.46  ? 25  VAL A CG1   1 
ATOM   239  C  CG2   . VAL A 1 37  ? 107.676 99.990  126.661 1.00 31.15  ? 25  VAL A CG2   1 
ATOM   240  N  N     . ILE A 1 38  ? 110.600 100.429 127.688 1.00 28.52  ? 26  ILE A N     1 
ATOM   241  C  CA    . ILE A 1 38  ? 111.392 99.882  128.790 1.00 26.57  ? 26  ILE A CA    1 
ATOM   242  C  C     . ILE A 1 38  ? 112.512 100.843 129.171 1.00 28.66  ? 26  ILE A C     1 
ATOM   243  O  O     . ILE A 1 38  ? 112.750 101.106 130.355 1.00 36.08  ? 26  ILE A O     1 
ATOM   244  C  CB    . ILE A 1 38  ? 111.941 98.489  128.439 1.00 29.16  ? 26  ILE A CB    1 
ATOM   245  C  CG1   . ILE A 1 38  ? 110.801 97.496  128.240 1.00 26.82  ? 26  ILE A CG1   1 
ATOM   246  C  CG2   . ILE A 1 38  ? 112.831 97.990  129.555 1.00 29.96  ? 26  ILE A CG2   1 
ATOM   247  C  CD1   . ILE A 1 38  ? 111.253 96.183  127.664 1.00 30.00  ? 26  ILE A CD1   1 
ATOM   248  N  N     . SER A 1 39  ? 113.215 101.387 128.174 1.00 28.56  ? 27  SER A N     1 
ATOM   249  C  CA    . SER A 1 39  ? 114.307 102.311 128.472 1.00 24.88  ? 27  SER A CA    1 
ATOM   250  C  C     . SER A 1 39  ? 113.792 103.595 129.112 1.00 26.42  ? 27  SER A C     1 
ATOM   251  O  O     . SER A 1 39  ? 114.418 104.129 130.036 1.00 31.75  ? 27  SER A O     1 
ATOM   252  C  CB    . SER A 1 39  ? 115.100 102.619 127.204 1.00 23.77  ? 27  SER A CB    1 
ATOM   253  O  OG    . SER A 1 39  ? 114.269 103.163 126.198 1.00 30.65  ? 27  SER A OG    1 
ATOM   254  N  N     . ASN A 1 40  ? 112.651 104.104 128.643 1.00 27.66  ? 28  ASN A N     1 
ATOM   255  C  CA    . ASN A 1 40  ? 112.101 105.327 129.215 1.00 28.22  ? 28  ASN A CA    1 
ATOM   256  C  C     . ASN A 1 40  ? 111.618 105.112 130.644 1.00 29.28  ? 28  ASN A C     1 
ATOM   257  O  O     . ASN A 1 40  ? 111.818 105.975 131.505 1.00 33.32  ? 28  ASN A O     1 
ATOM   258  C  CB    . ASN A 1 40  ? 110.978 105.855 128.328 1.00 30.05  ? 28  ASN A CB    1 
ATOM   259  C  CG    . ASN A 1 40  ? 111.489 106.383 127.004 1.00 36.67  ? 28  ASN A CG    1 
ATOM   260  O  OD1   . ASN A 1 40  ? 112.639 106.799 126.895 1.00 38.11  ? 28  ASN A OD1   1 
ATOM   261  N  ND2   . ASN A 1 40  ? 110.639 106.361 125.990 1.00 43.30  ? 28  ASN A ND2   1 
ATOM   262  N  N     . MET A 1 41  ? 110.996 103.965 130.929 1.00 28.08  ? 29  MET A N     1 
ATOM   263  C  CA    . MET A 1 41  ? 110.615 103.684 132.308 1.00 28.05  ? 29  MET A CA    1 
ATOM   264  C  C     . MET A 1 41  ? 111.827 103.442 133.198 1.00 27.93  ? 29  MET A C     1 
ATOM   265  O  O     . MET A 1 41  ? 111.784 103.773 134.381 1.00 34.38  ? 29  MET A O     1 
ATOM   266  C  CB    . MET A 1 41  ? 109.648 102.499 132.385 1.00 28.88  ? 29  MET A CB    1 
ATOM   267  C  CG    . MET A 1 41  ? 108.433 102.609 131.481 1.00 36.42  ? 29  MET A CG    1 
ATOM   268  S  SD    . MET A 1 41  ? 107.330 103.990 131.844 1.00 48.78  ? 29  MET A SD    1 
ATOM   269  C  CE    . MET A 1 41  ? 107.337 103.998 133.634 1.00 41.27  ? 29  MET A CE    1 
ATOM   270  N  N     . ALA A 1 42  ? 112.913 102.880 132.665 1.00 24.32  ? 30  ALA A N     1 
ATOM   271  C  CA    . ALA A 1 42  ? 114.129 102.759 133.468 1.00 26.72  ? 30  ALA A CA    1 
ATOM   272  C  C     . ALA A 1 42  ? 114.711 104.129 133.806 1.00 29.40  ? 30  ALA A C     1 
ATOM   273  O  O     . ALA A 1 42  ? 115.116 104.383 134.953 1.00 34.88  ? 30  ALA A O     1 
ATOM   274  C  CB    . ALA A 1 42  ? 115.158 101.905 132.731 1.00 21.71  ? 30  ALA A CB    1 
ATOM   275  N  N     . SER A 1 43  ? 114.757 105.024 132.817 1.00 25.20  ? 31  SER A N     1 
ATOM   276  C  CA    . SER A 1 43  ? 115.256 106.372 133.057 1.00 28.42  ? 31  SER A CA    1 
ATOM   277  C  C     . SER A 1 43  ? 114.348 107.151 134.001 1.00 30.21  ? 31  SER A C     1 
ATOM   278  O  O     . SER A 1 43  ? 114.825 108.025 134.730 1.00 32.36  ? 31  SER A O     1 
ATOM   279  C  CB    . SER A 1 43  ? 115.415 107.115 131.733 1.00 27.89  ? 31  SER A CB    1 
ATOM   280  O  OG    . SER A 1 43  ? 114.171 107.605 131.277 1.00 35.51  ? 31  SER A OG    1 
ATOM   281  N  N     . LEU A 1 44  ? 113.045 106.865 133.988 1.00 27.75  ? 32  LEU A N     1 
ATOM   282  C  CA    . LEU A 1 44  ? 112.138 107.472 134.956 1.00 24.49  ? 32  LEU A CA    1 
ATOM   283  C  C     . LEU A 1 44  ? 112.243 106.827 136.331 1.00 27.46  ? 32  LEU A C     1 
ATOM   284  O  O     . LEU A 1 44  ? 111.945 107.476 137.338 1.00 34.63  ? 32  LEU A O     1 
ATOM   285  C  CB    . LEU A 1 44  ? 110.695 107.387 134.459 1.00 25.68  ? 32  LEU A CB    1 
ATOM   286  C  CG    . LEU A 1 44  ? 110.274 108.369 133.368 1.00 29.30  ? 32  LEU A CG    1 
ATOM   287  C  CD1   . LEU A 1 44  ? 108.963 107.931 132.750 1.00 34.32  ? 32  LEU A CD1   1 
ATOM   288  C  CD2   . LEU A 1 44  ? 110.161 109.777 133.924 1.00 27.60  ? 32  LEU A CD2   1 
ATOM   289  N  N     . TYR A 1 45  ? 112.642 105.559 136.393 1.00 28.26  ? 33  TYR A N     1 
ATOM   290  C  CA    . TYR A 1 45  ? 112.713 104.850 137.662 1.00 28.06  ? 33  TYR A CA    1 
ATOM   291  C  C     . TYR A 1 45  ? 113.978 105.181 138.434 1.00 30.16  ? 33  TYR A C     1 
ATOM   292  O  O     . TYR A 1 45  ? 113.987 105.068 139.663 1.00 35.06  ? 33  TYR A O     1 
ATOM   293  C  CB    . TYR A 1 45  ? 112.625 103.342 137.428 1.00 27.46  ? 33  TYR A CB    1 
ATOM   294  C  CG    . TYR A 1 45  ? 112.473 102.539 138.695 1.00 27.87  ? 33  TYR A CG    1 
ATOM   295  C  CD1   . TYR A 1 45  ? 111.301 102.589 139.433 1.00 31.83  ? 33  TYR A CD1   1 
ATOM   296  C  CD2   . TYR A 1 45  ? 113.502 101.733 139.156 1.00 30.75  ? 33  TYR A CD2   1 
ATOM   297  C  CE1   . TYR A 1 45  ? 111.158 101.859 140.593 1.00 33.53  ? 33  TYR A CE1   1 
ATOM   298  C  CE2   . TYR A 1 45  ? 113.367 101.000 140.313 1.00 33.79  ? 33  TYR A CE2   1 
ATOM   299  C  CZ    . TYR A 1 45  ? 112.195 101.068 141.029 1.00 37.35  ? 33  TYR A CZ    1 
ATOM   300  O  OH    . TYR A 1 45  ? 112.057 100.337 142.185 1.00 40.77  ? 33  TYR A OH    1 
ATOM   301  N  N     . LEU A 1 46  ? 115.051 105.564 137.745 1.00 31.11  ? 34  LEU A N     1 
ATOM   302  C  CA    . LEU A 1 46  ? 116.251 106.001 138.463 1.00 29.46  ? 34  LEU A CA    1 
ATOM   303  C  C     . LEU A 1 46  ? 115.975 107.112 139.475 1.00 31.88  ? 34  LEU A C     1 
ATOM   304  O  O     . LEU A 1 46  ? 116.445 107.003 140.621 1.00 36.74  ? 34  LEU A O     1 
ATOM   305  C  CB    . LEU A 1 46  ? 117.334 106.426 137.462 1.00 31.50  ? 34  LEU A CB    1 
ATOM   306  C  CG    . LEU A 1 46  ? 118.100 105.312 136.755 1.00 30.71  ? 34  LEU A CG    1 
ATOM   307  C  CD1   . LEU A 1 46  ? 118.952 105.888 135.645 1.00 30.39  ? 34  LEU A CD1   1 
ATOM   308  C  CD2   . LEU A 1 46  ? 118.950 104.550 137.747 1.00 36.32  ? 34  LEU A CD2   1 
ATOM   309  N  N     . PRO A 1 47  ? 115.239 108.181 139.144 1.00 33.60  ? 35  PRO A N     1 
ATOM   310  C  CA    . PRO A 1 47  ? 114.856 109.149 140.185 1.00 32.36  ? 35  PRO A CA    1 
ATOM   311  C  C     . PRO A 1 47  ? 114.008 108.559 141.296 1.00 32.93  ? 35  PRO A C     1 
ATOM   312  O  O     . PRO A 1 47  ? 114.070 109.048 142.428 1.00 37.99  ? 35  PRO A O     1 
ATOM   313  C  CB    . PRO A 1 47  ? 114.081 110.212 139.401 1.00 29.67  ? 35  PRO A CB    1 
ATOM   314  C  CG    . PRO A 1 47  ? 114.580 110.094 138.026 1.00 27.98  ? 35  PRO A CG    1 
ATOM   315  C  CD    . PRO A 1 47  ? 114.848 108.657 137.807 1.00 31.20  ? 35  PRO A CD    1 
ATOM   316  N  N     . THR A 1 48  ? 113.196 107.541 141.011 1.00 30.00  ? 36  THR A N     1 
ATOM   317  C  CA    . THR A 1 48  ? 112.440 106.890 142.076 1.00 32.61  ? 36  THR A CA    1 
ATOM   318  C  C     . THR A 1 48  ? 113.370 106.200 143.068 1.00 36.30  ? 36  THR A C     1 
ATOM   319  O  O     . THR A 1 48  ? 113.149 106.256 144.284 1.00 37.78  ? 36  THR A O     1 
ATOM   320  C  CB    . THR A 1 48  ? 111.445 105.896 141.479 1.00 36.53  ? 36  THR A CB    1 
ATOM   321  O  OG1   . THR A 1 48  ? 110.659 106.555 140.480 1.00 36.12  ? 36  THR A OG1   1 
ATOM   322  C  CG2   . THR A 1 48  ? 110.525 105.353 142.551 1.00 42.09  ? 36  THR A CG2   1 
ATOM   323  N  N     . VAL A 1 49  ? 114.425 105.551 142.571 1.00 36.24  ? 37  VAL A N     1 
ATOM   324  C  CA    . VAL A 1 49  ? 115.405 104.957 143.472 1.00 35.64  ? 37  VAL A CA    1 
ATOM   325  C  C     . VAL A 1 49  ? 116.165 106.036 144.228 1.00 39.24  ? 37  VAL A C     1 
ATOM   326  O  O     . VAL A 1 49  ? 116.540 105.841 145.387 1.00 43.94  ? 37  VAL A O     1 
ATOM   327  C  CB    . VAL A 1 49  ? 116.364 104.029 142.708 1.00 34.33  ? 37  VAL A CB    1 
ATOM   328  C  CG1   . VAL A 1 49  ? 117.105 103.130 143.678 1.00 36.15  ? 37  VAL A CG1   1 
ATOM   329  C  CG2   . VAL A 1 49  ? 115.608 103.201 141.704 1.00 33.91  ? 37  VAL A CG2   1 
ATOM   330  N  N     . ASN A 1 50  ? 116.424 107.181 143.592 1.00 37.26  ? 38  ASN A N     1 
ATOM   331  C  CA    . ASN A 1 50  ? 117.044 108.291 144.312 1.00 35.98  ? 38  ASN A CA    1 
ATOM   332  C  C     . ASN A 1 50  ? 116.148 108.790 145.443 1.00 40.50  ? 38  ASN A C     1 
ATOM   333  O  O     . ASN A 1 50  ? 116.622 109.082 146.550 1.00 45.63  ? 38  ASN A O     1 
ATOM   334  C  CB    . ASN A 1 50  ? 117.359 109.420 143.336 1.00 38.64  ? 38  ASN A CB    1 
ATOM   335  C  CG    . ASN A 1 50  ? 118.476 110.308 143.818 1.00 42.86  ? 38  ASN A CG    1 
ATOM   336  O  OD1   . ASN A 1 50  ? 118.953 110.174 144.942 1.00 48.80  ? 38  ASN A OD1   1 
ATOM   337  N  ND2   . ASN A 1 50  ? 118.907 111.222 142.963 1.00 40.29  ? 38  ASN A ND2   1 
ATOM   338  N  N     . ALA A 1 51  ? 114.846 108.890 145.178 1.00 39.41  ? 39  ALA A N     1 
ATOM   339  C  CA    . ALA A 1 51  ? 113.893 109.267 146.214 1.00 38.28  ? 39  ALA A CA    1 
ATOM   340  C  C     . ALA A 1 51  ? 113.875 108.244 147.339 1.00 41.05  ? 39  ALA A C     1 
ATOM   341  O  O     . ALA A 1 51  ? 113.754 108.605 148.514 1.00 46.45  ? 39  ALA A O     1 
ATOM   342  C  CB    . ALA A 1 51  ? 112.500 109.422 145.609 1.00 35.88  ? 39  ALA A CB    1 
ATOM   343  N  N     . ALA A 1 52  ? 113.973 106.959 146.996 1.00 41.57  ? 40  ALA A N     1 
ATOM   344  C  CA    . ALA A 1 52  ? 114.048 105.922 148.019 1.00 44.10  ? 40  ALA A CA    1 
ATOM   345  C  C     . ALA A 1 52  ? 115.323 106.051 148.843 1.00 43.53  ? 40  ALA A C     1 
ATOM   346  O  O     . ALA A 1 52  ? 115.316 105.809 150.054 1.00 48.45  ? 40  ALA A O     1 
ATOM   347  C  CB    . ALA A 1 52  ? 113.961 104.541 147.374 1.00 46.17  ? 40  ALA A CB    1 
ATOM   348  N  N     . ILE A 1 53  ? 116.431 106.420 148.197 1.00 44.16  ? 41  ILE A N     1 
ATOM   349  C  CA    . ILE A 1 53  ? 117.677 106.674 148.917 1.00 44.76  ? 41  ILE A CA    1 
ATOM   350  C  C     . ILE A 1 53  ? 117.476 107.790 149.932 1.00 50.19  ? 41  ILE A C     1 
ATOM   351  O  O     . ILE A 1 53  ? 117.918 107.699 151.083 1.00 51.99  ? 41  ILE A O     1 
ATOM   352  C  CB    . ILE A 1 53  ? 118.810 107.015 147.931 1.00 42.25  ? 41  ILE A CB    1 
ATOM   353  C  CG1   . ILE A 1 53  ? 119.432 105.747 147.353 1.00 43.46  ? 41  ILE A CG1   1 
ATOM   354  C  CG2   . ILE A 1 53  ? 119.881 107.855 148.604 1.00 43.98  ? 41  ILE A CG2   1 
ATOM   355  C  CD1   . ILE A 1 53  ? 120.418 106.011 146.240 1.00 36.99  ? 41  ILE A CD1   1 
ATOM   356  N  N     . ILE A 1 54  ? 116.810 108.865 149.514 1.00 50.50  ? 42  ILE A N     1 
ATOM   357  C  CA    . ILE A 1 54  ? 116.589 109.993 150.415 1.00 49.23  ? 42  ILE A CA    1 
ATOM   358  C  C     . ILE A 1 54  ? 115.673 109.594 151.570 1.00 52.76  ? 42  ILE A C     1 
ATOM   359  O  O     . ILE A 1 54  ? 115.965 109.872 152.738 1.00 55.06  ? 42  ILE A O     1 
ATOM   360  C  CB    . ILE A 1 54  ? 116.029 111.198 149.640 1.00 51.12  ? 42  ILE A CB    1 
ATOM   361  C  CG1   . ILE A 1 54  ? 117.044 111.682 148.604 1.00 54.08  ? 42  ILE A CG1   1 
ATOM   362  C  CG2   . ILE A 1 54  ? 115.664 112.320 150.594 1.00 43.38  ? 42  ILE A CG2   1 
ATOM   363  C  CD1   . ILE A 1 54  ? 118.417 111.949 149.173 1.00 53.81  ? 42  ILE A CD1   1 
ATOM   364  N  N     . ASP A 1 55  ? 114.555 108.932 151.263 1.00 50.79  ? 43  ASP A N     1 
ATOM   365  C  CA    . ASP A 1 55  ? 113.566 108.623 152.293 1.00 53.51  ? 43  ASP A CA    1 
ATOM   366  C  C     . ASP A 1 55  ? 114.044 107.516 153.224 1.00 58.77  ? 43  ASP A C     1 
ATOM   367  O  O     . ASP A 1 55  ? 113.913 107.624 154.449 1.00 63.74  ? 43  ASP A O     1 
ATOM   368  C  CB    . ASP A 1 55  ? 112.236 108.234 151.647 1.00 56.02  ? 43  ASP A CB    1 
ATOM   369  C  CG    . ASP A 1 55  ? 111.701 109.303 150.721 1.00 59.65  ? 43  ASP A CG    1 
ATOM   370  O  OD1   . ASP A 1 55  ? 110.792 108.999 149.920 1.00 58.65  ? 43  ASP A OD1   1 
ATOM   371  O  OD2   . ASP A 1 55  ? 112.184 110.451 150.800 1.00 61.20  ? 43  ASP A OD2   1 
ATOM   372  N  N     . ASP A 1 56  ? 114.595 106.440 152.666 1.00 59.35  ? 44  ASP A N     1 
ATOM   373  C  CA    . ASP A 1 56  ? 114.935 105.268 153.465 1.00 60.67  ? 44  ASP A CA    1 
ATOM   374  C  C     . ASP A 1 56  ? 116.336 105.342 154.057 1.00 60.83  ? 44  ASP A C     1 
ATOM   375  O  O     . ASP A 1 56  ? 116.541 104.942 155.207 1.00 67.90  ? 44  ASP A O     1 
ATOM   376  C  CB    . ASP A 1 56  ? 114.798 103.998 152.623 1.00 62.86  ? 44  ASP A CB    1 
ATOM   377  C  CG    . ASP A 1 56  ? 113.357 103.682 152.277 1.00 72.71  ? 44  ASP A CG    1 
ATOM   378  O  OD1   . ASP A 1 56  ? 112.452 104.317 152.858 1.00 73.58  ? 44  ASP A OD1   1 
ATOM   379  O  OD2   . ASP A 1 56  ? 113.129 102.800 151.423 1.00 72.82  ? 44  ASP A OD2   1 
ATOM   380  N  N     . GLY A 1 57  ? 117.307 105.831 153.297 1.00 57.14  ? 45  GLY A N     1 
ATOM   381  C  CA    . GLY A 1 57  ? 118.667 105.892 153.790 1.00 62.26  ? 45  GLY A CA    1 
ATOM   382  C  C     . GLY A 1 57  ? 119.000 107.158 154.549 1.00 65.17  ? 45  GLY A C     1 
ATOM   383  O  O     . GLY A 1 57  ? 119.425 107.103 155.706 1.00 66.27  ? 45  GLY A O     1 
ATOM   384  N  N     . VAL A 1 58  ? 118.815 108.309 153.903 1.00 64.40  ? 46  VAL A N     1 
ATOM   385  C  CA    . VAL A 1 58  ? 119.248 109.573 154.492 1.00 60.62  ? 46  VAL A CA    1 
ATOM   386  C  C     . VAL A 1 58  ? 118.396 109.924 155.704 1.00 66.50  ? 46  VAL A C     1 
ATOM   387  O  O     . VAL A 1 58  ? 118.917 110.291 156.764 1.00 69.37  ? 46  VAL A O     1 
ATOM   388  C  CB    . VAL A 1 58  ? 119.217 110.690 153.435 1.00 55.46  ? 46  VAL A CB    1 
ATOM   389  C  CG1   . VAL A 1 58  ? 119.225 112.048 154.103 1.00 54.22  ? 46  VAL A CG1   1 
ATOM   390  C  CG2   . VAL A 1 58  ? 120.397 110.551 152.491 1.00 53.62  ? 46  VAL A CG2   1 
ATOM   391  N  N     . ALA A 1 59  ? 117.073 109.811 155.572 1.00 68.62  ? 47  ALA A N     1 
ATOM   392  C  CA    . ALA A 1 59  ? 116.178 110.227 156.645 1.00 69.32  ? 47  ALA A CA    1 
ATOM   393  C  C     . ALA A 1 59  ? 116.266 109.324 157.866 1.00 76.45  ? 47  ALA A C     1 
ATOM   394  O  O     . ALA A 1 59  ? 115.806 109.717 158.943 1.00 78.43  ? 47  ALA A O     1 
ATOM   395  C  CB    . ALA A 1 59  ? 114.737 110.276 156.138 1.00 65.70  ? 47  ALA A CB    1 
ATOM   396  N  N     . LYS A 1 60  ? 116.837 108.128 157.729 1.00 77.82  ? 48  LYS A N     1 
ATOM   397  C  CA    . LYS A 1 60  ? 116.974 107.199 158.844 1.00 76.18  ? 48  LYS A CA    1 
ATOM   398  C  C     . LYS A 1 60  ? 118.426 106.840 159.133 1.00 75.67  ? 48  LYS A C     1 
ATOM   399  O  O     . LYS A 1 60  ? 118.681 105.981 159.985 1.00 76.20  ? 48  LYS A O     1 
ATOM   400  C  CB    . LYS A 1 60  ? 116.162 105.928 158.579 1.00 71.63  ? 48  LYS A CB    1 
ATOM   401  C  CG    . LYS A 1 60  ? 114.714 106.190 158.199 1.00 70.68  ? 48  LYS A CG    1 
ATOM   402  C  CD    . LYS A 1 60  ? 114.157 105.081 157.325 1.00 75.44  ? 48  LYS A CD    1 
ATOM   403  C  CE    . LYS A 1 60  ? 112.745 104.709 157.741 1.00 76.57  ? 48  LYS A CE    1 
ATOM   404  N  NZ    . LYS A 1 60  ? 111.760 105.750 157.340 1.00 75.90  ? 48  LYS A NZ    1 
ATOM   405  N  N     . GLY A 1 61  ? 119.379 107.472 158.454 1.00 72.17  ? 49  GLY A N     1 
ATOM   406  C  CA    . GLY A 1 61  ? 120.782 107.181 158.684 1.00 79.25  ? 49  GLY A CA    1 
ATOM   407  C  C     . GLY A 1 61  ? 121.198 105.773 158.324 1.00 82.40  ? 49  GLY A C     1 
ATOM   408  O  O     . GLY A 1 61  ? 122.078 105.209 158.979 1.00 84.98  ? 49  GLY A O     1 
ATOM   409  N  N     . ASP A 1 62  ? 120.591 105.189 157.294 1.00 75.35  ? 50  ASP A N     1 
ATOM   410  C  CA    . ASP A 1 62  ? 120.868 103.811 156.891 1.00 70.60  ? 50  ASP A CA    1 
ATOM   411  C  C     . ASP A 1 62  ? 121.738 103.850 155.639 1.00 71.06  ? 50  ASP A C     1 
ATOM   412  O  O     . ASP A 1 62  ? 121.240 103.908 154.514 1.00 74.60  ? 50  ASP A O     1 
ATOM   413  C  CB    . ASP A 1 62  ? 119.569 103.049 156.659 1.00 71.12  ? 50  ASP A CB    1 
ATOM   414  C  CG    . ASP A 1 62  ? 119.743 101.551 156.782 1.00 81.57  ? 50  ASP A CG    1 
ATOM   415  O  OD1   . ASP A 1 62  ? 120.871 101.104 157.075 1.00 82.37  ? 50  ASP A OD1   1 
ATOM   416  O  OD2   . ASP A 1 62  ? 118.751 100.819 156.586 1.00 80.34  ? 50  ASP A OD2   1 
ATOM   417  N  N     . THR A 1 63  ? 123.057 103.814 155.841 1.00 68.42  ? 51  THR A N     1 
ATOM   418  C  CA    . THR A 1 63  ? 123.984 103.861 154.715 1.00 69.63  ? 51  THR A CA    1 
ATOM   419  C  C     . THR A 1 63  ? 123.975 102.562 153.917 1.00 67.41  ? 51  THR A C     1 
ATOM   420  O  O     . THR A 1 63  ? 124.204 102.580 152.700 1.00 67.16  ? 51  THR A O     1 
ATOM   421  C  CB    . THR A 1 63  ? 125.395 104.167 155.213 1.00 73.72  ? 51  THR A CB    1 
ATOM   422  O  OG1   . THR A 1 63  ? 125.750 103.237 156.243 1.00 79.58  ? 51  THR A OG1   1 
ATOM   423  C  CG2   . THR A 1 63  ? 125.464 105.579 155.770 1.00 69.54  ? 51  THR A CG2   1 
ATOM   424  N  N     . ALA A 1 64  ? 123.718 101.433 154.581 1.00 65.47  ? 52  ALA A N     1 
ATOM   425  C  CA    . ALA A 1 64  ? 123.624 100.164 153.868 1.00 69.56  ? 52  ALA A CA    1 
ATOM   426  C  C     . ALA A 1 64  ? 122.493 100.195 152.850 1.00 67.11  ? 52  ALA A C     1 
ATOM   427  O  O     . ALA A 1 64  ? 122.638 99.683  151.732 1.00 68.43  ? 52  ALA A O     1 
ATOM   428  C  CB    . ALA A 1 64  ? 123.428 99.018  154.859 1.00 72.19  ? 52  ALA A CB    1 
ATOM   429  N  N     . ARG A 1 65  ? 121.358 100.793 153.217 1.00 63.63  ? 53  ARG A N     1 
ATOM   430  C  CA    . ARG A 1 65  ? 120.265 100.944 152.264 1.00 64.65  ? 53  ARG A CA    1 
ATOM   431  C  C     . ARG A 1 65  ? 120.669 101.839 151.102 1.00 61.07  ? 53  ARG A C     1 
ATOM   432  O  O     . ARG A 1 65  ? 120.267 101.601 149.959 1.00 64.22  ? 53  ARG A O     1 
ATOM   433  C  CB    . ARG A 1 65  ? 119.024 101.497 152.961 1.00 61.30  ? 53  ARG A CB    1 
ATOM   434  C  CG    . ARG A 1 65  ? 118.071 100.420 153.426 1.00 67.88  ? 53  ARG A CG    1 
ATOM   435  C  CD    . ARG A 1 65  ? 117.587 99.584  152.257 1.00 65.37  ? 53  ARG A CD    1 
ATOM   436  N  NE    . ARG A 1 65  ? 116.462 100.195 151.562 1.00 65.06  ? 53  ARG A NE    1 
ATOM   437  C  CZ    . ARG A 1 65  ? 115.893 99.688  150.477 1.00 67.77  ? 53  ARG A CZ    1 
ATOM   438  N  NH1   . ARG A 1 65  ? 116.334 98.571  149.924 1.00 67.42  ? 53  ARG A NH1   1 
ATOM   439  N  NH2   . ARG A 1 65  ? 114.856 100.318 149.934 1.00 69.41  ? 53  ARG A NH2   1 
ATOM   440  N  N     . ILE A 1 66  ? 121.464 102.876 151.373 1.00 56.02  ? 54  ILE A N     1 
ATOM   441  C  CA    . ILE A 1 66  ? 121.930 103.754 150.303 1.00 55.21  ? 54  ILE A CA    1 
ATOM   442  C  C     . ILE A 1 66  ? 122.788 102.975 149.314 1.00 60.20  ? 54  ILE A C     1 
ATOM   443  O  O     . ILE A 1 66  ? 122.632 103.104 148.094 1.00 58.36  ? 54  ILE A O     1 
ATOM   444  C  CB    . ILE A 1 66  ? 122.691 104.958 150.886 1.00 50.70  ? 54  ILE A CB    1 
ATOM   445  C  CG1   . ILE A 1 66  ? 121.774 105.774 151.795 1.00 52.68  ? 54  ILE A CG1   1 
ATOM   446  C  CG2   . ILE A 1 66  ? 123.244 105.823 149.772 1.00 47.10  ? 54  ILE A CG2   1 
ATOM   447  C  CD1   . ILE A 1 66  ? 122.454 106.955 152.440 1.00 53.26  ? 54  ILE A CD1   1 
ATOM   448  N  N     . VAL A 1 67  ? 123.698 102.143 149.825 1.00 58.24  ? 55  VAL A N     1 
ATOM   449  C  CA    . VAL A 1 67  ? 124.551 101.347 148.943 1.00 56.10  ? 55  VAL A CA    1 
ATOM   450  C  C     . VAL A 1 67  ? 123.721 100.341 148.150 1.00 55.00  ? 55  VAL A C     1 
ATOM   451  O  O     . VAL A 1 67  ? 123.939 100.139 146.946 1.00 55.56  ? 55  VAL A O     1 
ATOM   452  C  CB    . VAL A 1 67  ? 125.659 100.656 149.758 1.00 56.74  ? 55  VAL A CB    1 
ATOM   453  C  CG1   . VAL A 1 67  ? 126.545 99.824  148.850 1.00 55.60  ? 55  VAL A CG1   1 
ATOM   454  C  CG2   . VAL A 1 67  ? 126.482 101.688 150.501 1.00 56.61  ? 55  VAL A CG2   1 
ATOM   455  N  N     . GLU A 1 68  ? 122.759 99.692  148.809 1.00 51.76  ? 56  GLU A N     1 
ATOM   456  C  CA    . GLU A 1 68  ? 121.911 98.720  148.125 1.00 54.38  ? 56  GLU A CA    1 
ATOM   457  C  C     . GLU A 1 68  ? 121.108 99.376  147.007 1.00 54.57  ? 56  GLU A C     1 
ATOM   458  O  O     . GLU A 1 68  ? 121.015 98.848  145.890 1.00 60.46  ? 56  GLU A O     1 
ATOM   459  C  CB    . GLU A 1 68  ? 120.979 98.053  149.132 1.00 58.04  ? 56  GLU A CB    1 
ATOM   460  C  CG    . GLU A 1 68  ? 119.981 97.099  148.515 1.00 68.14  ? 56  GLU A CG    1 
ATOM   461  C  CD    . GLU A 1 68  ? 118.944 96.627  149.510 1.00 78.18  ? 56  GLU A CD    1 
ATOM   462  O  OE1   . GLU A 1 68  ? 119.333 96.165  150.602 1.00 80.66  ? 56  GLU A OE1   1 
ATOM   463  O  OE2   . GLU A 1 68  ? 117.739 96.720  149.198 1.00 79.48  ? 56  GLU A OE2   1 
ATOM   464  N  N     . LEU A 1 69  ? 120.518 100.537 147.289 1.00 48.98  ? 57  LEU A N     1 
ATOM   465  C  CA    . LEU A 1 69  ? 119.740 101.224 146.270 1.00 44.79  ? 57  LEU A CA    1 
ATOM   466  C  C     . LEU A 1 69  ? 120.633 101.781 145.171 1.00 46.37  ? 57  LEU A C     1 
ATOM   467  O  O     . LEU A 1 69  ? 120.190 101.918 144.028 1.00 47.86  ? 57  LEU A O     1 
ATOM   468  C  CB    . LEU A 1 69  ? 118.900 102.326 146.909 1.00 47.19  ? 57  LEU A CB    1 
ATOM   469  C  CG    . LEU A 1 69  ? 117.801 101.835 147.853 1.00 48.55  ? 57  LEU A CG    1 
ATOM   470  C  CD1   . LEU A 1 69  ? 117.229 102.985 148.657 1.00 48.73  ? 57  LEU A CD1   1 
ATOM   471  C  CD2   . LEU A 1 69  ? 116.708 101.118 147.084 1.00 47.88  ? 57  LEU A CD2   1 
ATOM   472  N  N     . GLY A 1 70  ? 121.893 102.088 145.484 1.00 45.78  ? 58  GLY A N     1 
ATOM   473  C  CA    . GLY A 1 70  ? 122.834 102.439 144.433 1.00 42.43  ? 58  GLY A CA    1 
ATOM   474  C  C     . GLY A 1 70  ? 123.125 101.275 143.507 1.00 44.79  ? 58  GLY A C     1 
ATOM   475  O  O     . GLY A 1 70  ? 123.255 101.451 142.293 1.00 47.47  ? 58  GLY A O     1 
ATOM   476  N  N     . ALA A 1 71  ? 123.233 100.069 144.066 1.00 44.01  ? 59  ALA A N     1 
ATOM   477  C  CA    . ALA A 1 71  ? 123.372 98.881  143.226 1.00 44.53  ? 59  ALA A CA    1 
ATOM   478  C  C     . ALA A 1 71  ? 122.139 98.683  142.349 1.00 43.07  ? 59  ALA A C     1 
ATOM   479  O  O     . ALA A 1 71  ? 122.249 98.313  141.169 1.00 46.28  ? 59  ALA A O     1 
ATOM   480  C  CB    . ALA A 1 71  ? 123.620 97.649  144.095 1.00 38.25  ? 59  ALA A CB    1 
ATOM   481  N  N     . VAL A 1 72  ? 120.954 98.921  142.913 1.00 39.06  ? 60  VAL A N     1 
ATOM   482  C  CA    . VAL A 1 72  ? 119.724 98.850  142.125 1.00 36.68  ? 60  VAL A CA    1 
ATOM   483  C  C     . VAL A 1 72  ? 119.758 99.866  140.986 1.00 39.07  ? 60  VAL A C     1 
ATOM   484  O  O     . VAL A 1 72  ? 119.372 99.563  139.848 1.00 43.50  ? 60  VAL A O     1 
ATOM   485  C  CB    . VAL A 1 72  ? 118.496 99.057  143.029 1.00 37.18  ? 60  VAL A CB    1 
ATOM   486  C  CG1   . VAL A 1 72  ? 117.226 99.080  142.201 1.00 32.07  ? 60  VAL A CG1   1 
ATOM   487  C  CG2   . VAL A 1 72  ? 118.426 97.970  144.084 1.00 39.77  ? 60  VAL A CG2   1 
ATOM   488  N  N     . MET A 1 73  ? 120.218 101.085 141.274 1.00 37.17  ? 61  MET A N     1 
ATOM   489  C  CA    . MET A 1 73  ? 120.339 102.106 140.238 1.00 36.10  ? 61  MET A CA    1 
ATOM   490  C  C     . MET A 1 73  ? 121.308 101.674 139.146 1.00 36.42  ? 61  MET A C     1 
ATOM   491  O  O     . MET A 1 73  ? 121.065 101.914 137.959 1.00 40.21  ? 61  MET A O     1 
ATOM   492  C  CB    . MET A 1 73  ? 120.792 103.430 140.852 1.00 35.52  ? 61  MET A CB    1 
ATOM   493  C  CG    . MET A 1 73  ? 119.672 104.275 141.415 1.00 35.89  ? 61  MET A CG    1 
ATOM   494  S  SD    . MET A 1 73  ? 120.249 105.749 142.273 1.00 54.48  ? 61  MET A SD    1 
ATOM   495  C  CE    . MET A 1 73  ? 120.633 106.818 140.893 1.00 37.99  ? 61  MET A CE    1 
ATOM   496  N  N     . LEU A 1 74  ? 122.423 101.054 139.532 1.00 36.10  ? 62  LEU A N     1 
ATOM   497  C  CA    . LEU A 1 74  ? 123.390 100.577 138.548 1.00 34.49  ? 62  LEU A CA    1 
ATOM   498  C  C     . LEU A 1 74  ? 122.769 99.535  137.624 1.00 38.03  ? 62  LEU A C     1 
ATOM   499  O  O     . LEU A 1 74  ? 122.951 99.583  136.396 1.00 39.77  ? 62  LEU A O     1 
ATOM   500  C  CB    . LEU A 1 74  ? 124.608 100.003 139.268 1.00 36.19  ? 62  LEU A CB    1 
ATOM   501  C  CG    . LEU A 1 74  ? 125.916 99.931  138.490 1.00 41.11  ? 62  LEU A CG    1 
ATOM   502  C  CD1   . LEU A 1 74  ? 126.530 101.311 138.393 1.00 39.60  ? 62  LEU A CD1   1 
ATOM   503  C  CD2   . LEU A 1 74  ? 126.867 98.963  139.162 1.00 41.08  ? 62  LEU A CD2   1 
ATOM   504  N  N     . GLY A 1 75  ? 122.026 98.587  138.197 1.00 35.87  ? 63  GLY A N     1 
ATOM   505  C  CA    . GLY A 1 75  ? 121.332 97.612  137.369 1.00 30.06  ? 63  GLY A CA    1 
ATOM   506  C  C     . GLY A 1 75  ? 120.325 98.254  136.433 1.00 31.85  ? 63  GLY A C     1 
ATOM   507  O  O     . GLY A 1 75  ? 120.199 97.859  135.268 1.00 39.80  ? 63  GLY A O     1 
ATOM   508  N  N     . VAL A 1 76  ? 119.597 99.256  136.928 1.00 31.50  ? 64  VAL A N     1 
ATOM   509  C  CA    . VAL A 1 76  ? 118.615 99.946  136.095 1.00 29.38  ? 64  VAL A CA    1 
ATOM   510  C  C     . VAL A 1 76  ? 119.301 100.662 134.936 1.00 27.41  ? 64  VAL A C     1 
ATOM   511  O  O     . VAL A 1 76  ? 118.794 100.673 133.809 1.00 31.25  ? 64  VAL A O     1 
ATOM   512  C  CB    . VAL A 1 76  ? 117.773 100.910 136.951 1.00 30.17  ? 64  VAL A CB    1 
ATOM   513  C  CG1   . VAL A 1 76  ? 116.920 101.803 136.075 1.00 31.10  ? 64  VAL A CG1   1 
ATOM   514  C  CG2   . VAL A 1 76  ? 116.895 100.126 137.909 1.00 27.54  ? 64  VAL A CG2   1 
ATOM   515  N  N     . THR A 1 77  ? 120.465 101.267 135.190 1.00 27.71  ? 65  THR A N     1 
ATOM   516  C  CA    . THR A 1 77  ? 121.202 101.933 134.116 1.00 28.78  ? 65  THR A CA    1 
ATOM   517  C  C     . THR A 1 77  ? 121.676 100.938 133.063 1.00 30.55  ? 65  THR A C     1 
ATOM   518  O  O     . THR A 1 77  ? 121.637 101.228 131.858 1.00 31.02  ? 65  THR A O     1 
ATOM   519  C  CB    . THR A 1 77  ? 122.393 102.705 134.681 1.00 32.31  ? 65  THR A CB    1 
ATOM   520  O  OG1   . THR A 1 77  ? 123.280 101.801 135.349 1.00 41.44  ? 65  THR A OG1   1 
ATOM   521  C  CG2   . THR A 1 77  ? 121.930 103.766 135.653 1.00 33.02  ? 65  THR A CG2   1 
ATOM   522  N  N     . ALA A 1 78  ? 122.147 99.765  133.498 1.00 32.99  ? 66  ALA A N     1 
ATOM   523  C  CA    . ALA A 1 78  ? 122.543 98.738  132.535 1.00 30.31  ? 66  ALA A CA    1 
ATOM   524  C  C     . ALA A 1 78  ? 121.363 98.305  131.670 1.00 28.37  ? 66  ALA A C     1 
ATOM   525  O  O     . ALA A 1 78  ? 121.488 98.176  130.441 1.00 28.78  ? 66  ALA A O     1 
ATOM   526  C  CB    . ALA A 1 78  ? 123.143 97.538  133.266 1.00 26.30  ? 66  ALA A CB    1 
ATOM   527  N  N     . LEU A 1 79  ? 120.203 98.088  132.292 1.00 27.18  ? 67  LEU A N     1 
ATOM   528  C  CA    . LEU A 1 79  ? 119.014 97.737  131.521 1.00 27.80  ? 67  LEU A CA    1 
ATOM   529  C  C     . LEU A 1 79  ? 118.648 98.844  130.539 1.00 29.17  ? 67  LEU A C     1 
ATOM   530  O  O     . LEU A 1 79  ? 118.278 98.573  129.387 1.00 37.08  ? 67  LEU A O     1 
ATOM   531  C  CB    . LEU A 1 79  ? 117.849 97.447  132.467 1.00 27.71  ? 67  LEU A CB    1 
ATOM   532  C  CG    . LEU A 1 79  ? 116.460 97.352  131.840 1.00 30.06  ? 67  LEU A CG    1 
ATOM   533  C  CD1   . LEU A 1 79  ? 116.351 96.114  130.971 1.00 33.07  ? 67  LEU A CD1   1 
ATOM   534  C  CD2   . LEU A 1 79  ? 115.394 97.355  132.917 1.00 28.58  ? 67  LEU A CD2   1 
ATOM   535  N  N     . GLN A 1 80  ? 118.757 100.100 130.977 1.00 26.66  ? 68  GLN A N     1 
ATOM   536  C  CA    . GLN A 1 80  ? 118.425 101.230 130.119 1.00 25.05  ? 68  GLN A CA    1 
ATOM   537  C  C     . GLN A 1 80  ? 119.313 101.265 128.883 1.00 27.76  ? 68  GLN A C     1 
ATOM   538  O  O     . GLN A 1 80  ? 118.827 101.455 127.762 1.00 33.42  ? 68  GLN A O     1 
ATOM   539  C  CB    . GLN A 1 80  ? 118.558 102.533 130.906 1.00 21.39  ? 68  GLN A CB    1 
ATOM   540  C  CG    . GLN A 1 80  ? 117.612 103.626 130.468 1.00 26.52  ? 68  GLN A CG    1 
ATOM   541  C  CD    . GLN A 1 80  ? 118.284 104.662 129.600 1.00 33.68  ? 68  GLN A CD    1 
ATOM   542  O  OE1   . GLN A 1 80  ? 119.132 104.338 128.772 1.00 29.08  ? 68  GLN A OE1   1 
ATOM   543  N  NE2   . GLN A 1 80  ? 117.909 105.919 129.783 1.00 40.61  ? 68  GLN A NE2   1 
ATOM   544  N  N     . VAL A 1 81  ? 120.623 101.089 129.067 1.00 29.75  ? 69  VAL A N     1 
ATOM   545  C  CA    . VAL A 1 81  ? 121.522 101.187 127.921 1.00 26.65  ? 69  VAL A CA    1 
ATOM   546  C  C     . VAL A 1 81  ? 121.305 100.017 126.970 1.00 25.39  ? 69  VAL A C     1 
ATOM   547  O  O     . VAL A 1 81  ? 121.339 100.185 125.743 1.00 27.70  ? 69  VAL A O     1 
ATOM   548  C  CB    . VAL A 1 81  ? 122.993 101.304 128.370 1.00 28.53  ? 69  VAL A CB    1 
ATOM   549  C  CG1   . VAL A 1 81  ? 123.458 100.061 129.094 1.00 24.41  ? 69  VAL A CG1   1 
ATOM   550  C  CG2   . VAL A 1 81  ? 123.887 101.584 127.172 1.00 28.03  ? 69  VAL A CG2   1 
ATOM   551  N  N     . VAL A 1 82  ? 121.047 98.821  127.510 1.00 29.56  ? 70  VAL A N     1 
ATOM   552  C  CA    . VAL A 1 82  ? 120.788 97.669  126.648 1.00 28.79  ? 70  VAL A CA    1 
ATOM   553  C  C     . VAL A 1 82  ? 119.549 97.915  125.791 1.00 27.14  ? 70  VAL A C     1 
ATOM   554  O  O     . VAL A 1 82  ? 119.554 97.692  124.569 1.00 28.05  ? 70  VAL A O     1 
ATOM   555  C  CB    . VAL A 1 82  ? 120.650 96.391  127.495 1.00 28.62  ? 70  VAL A CB    1 
ATOM   556  C  CG1   . VAL A 1 82  ? 119.844 95.342  126.755 1.00 30.36  ? 70  VAL A CG1   1 
ATOM   557  C  CG2   . VAL A 1 82  ? 122.021 95.853  127.865 1.00 27.26  ? 70  VAL A CG2   1 
ATOM   558  N  N     . CYS A 1 83  ? 118.474 98.402  126.415 1.00 26.32  ? 71  CYS A N     1 
ATOM   559  C  CA    . CYS A 1 83  ? 117.240 98.632  125.672 1.00 23.30  ? 71  CYS A CA    1 
ATOM   560  C  C     . CYS A 1 83  ? 117.396 99.751  124.648 1.00 28.40  ? 71  CYS A C     1 
ATOM   561  O  O     . CYS A 1 83  ? 116.846 99.664  123.545 1.00 31.84  ? 71  CYS A O     1 
ATOM   562  C  CB    . CYS A 1 83  ? 116.098 98.929  126.637 1.00 24.71  ? 71  CYS A CB    1 
ATOM   563  S  SG    . CYS A 1 83  ? 115.592 97.479  127.570 1.00 53.94  ? 71  CYS A SG    1 
ATOM   564  N  N     . ALA A 1 84  ? 118.140 100.807 124.987 1.00 27.85  ? 72  ALA A N     1 
ATOM   565  C  CA    . ALA A 1 84  ? 118.359 101.886 124.028 1.00 21.59  ? 72  ALA A CA    1 
ATOM   566  C  C     . ALA A 1 84  ? 119.149 101.405 122.814 1.00 26.90  ? 72  ALA A C     1 
ATOM   567  O  O     . ALA A 1 84  ? 118.838 101.775 121.672 1.00 27.71  ? 72  ALA A O     1 
ATOM   568  C  CB    . ALA A 1 84  ? 119.072 103.052 124.709 1.00 21.75  ? 72  ALA A CB    1 
ATOM   569  N  N     . VAL A 1 85  ? 120.175 100.580 123.037 1.00 26.88  ? 73  VAL A N     1 
ATOM   570  C  CA    . VAL A 1 85  ? 120.954 100.052 121.917 1.00 25.96  ? 73  VAL A CA    1 
ATOM   571  C  C     . VAL A 1 85  ? 120.080 99.181  121.023 1.00 28.94  ? 73  VAL A C     1 
ATOM   572  O  O     . VAL A 1 85  ? 120.107 99.295  119.788 1.00 34.19  ? 73  VAL A O     1 
ATOM   573  C  CB    . VAL A 1 85  ? 122.182 99.281  122.433 1.00 25.88  ? 73  VAL A CB    1 
ATOM   574  C  CG1   . VAL A 1 85  ? 122.814 98.478  121.313 1.00 23.53  ? 73  VAL A CG1   1 
ATOM   575  C  CG2   . VAL A 1 85  ? 123.189 100.241 123.033 1.00 30.48  ? 73  VAL A CG2   1 
ATOM   576  N  N     . GLY A 1 86  ? 119.288 98.294  121.631 1.00 26.96  ? 74  GLY A N     1 
ATOM   577  C  CA    . GLY A 1 86  ? 118.392 97.472  120.834 1.00 22.90  ? 74  GLY A CA    1 
ATOM   578  C  C     . GLY A 1 86  ? 117.404 98.302  120.038 1.00 25.47  ? 74  GLY A C     1 
ATOM   579  O  O     . GLY A 1 86  ? 117.126 98.011  118.868 1.00 27.79  ? 74  GLY A O     1 
ATOM   580  N  N     . ALA A 1 87  ? 116.869 99.356  120.659 1.00 25.34  ? 75  ALA A N     1 
ATOM   581  C  CA    . ALA A 1 87  ? 115.900 100.209 119.985 1.00 23.76  ? 75  ALA A CA    1 
ATOM   582  C  C     . ALA A 1 87  ? 116.516 100.895 118.775 1.00 22.35  ? 75  ALA A C     1 
ATOM   583  O  O     . ALA A 1 87  ? 115.912 100.927 117.699 1.00 24.27  ? 75  ALA A O     1 
ATOM   584  C  CB    . ALA A 1 87  ? 115.341 101.240 120.964 1.00 27.56  ? 75  ALA A CB    1 
ATOM   585  N  N     . VAL A 1 88  ? 117.723 101.446 118.926 1.00 26.88  ? 76  VAL A N     1 
ATOM   586  C  CA    . VAL A 1 88  ? 118.323 102.148 117.793 1.00 26.60  ? 76  VAL A CA    1 
ATOM   587  C  C     . VAL A 1 88  ? 118.662 101.168 116.673 1.00 26.90  ? 76  VAL A C     1 
ATOM   588  O  O     . VAL A 1 88  ? 118.475 101.476 115.489 1.00 30.41  ? 76  VAL A O     1 
ATOM   589  C  CB    . VAL A 1 88  ? 119.548 102.982 118.225 1.00 26.25  ? 76  VAL A CB    1 
ATOM   590  C  CG1   . VAL A 1 88  ? 119.153 103.994 119.287 1.00 34.53  ? 76  VAL A CG1   1 
ATOM   591  C  CG2   . VAL A 1 88  ? 120.687 102.112 118.710 1.00 30.03  ? 76  VAL A CG2   1 
ATOM   592  N  N     . PHE A 1 89  ? 119.119 99.961  117.022 1.00 27.90  ? 77  PHE A N     1 
ATOM   593  C  CA    . PHE A 1 89  ? 119.426 98.970  115.992 1.00 28.60  ? 77  PHE A CA    1 
ATOM   594  C  C     . PHE A 1 89  ? 118.182 98.601  115.188 1.00 29.78  ? 77  PHE A C     1 
ATOM   595  O  O     . PHE A 1 89  ? 118.182 98.658  113.948 1.00 33.69  ? 77  PHE A O     1 
ATOM   596  C  CB    . PHE A 1 89  ? 120.043 97.730  116.639 1.00 24.00  ? 77  PHE A CB    1 
ATOM   597  C  CG    . PHE A 1 89  ? 120.207 96.568  115.704 1.00 24.25  ? 77  PHE A CG    1 
ATOM   598  C  CD1   . PHE A 1 89  ? 121.335 96.454  114.914 1.00 27.73  ? 77  PHE A CD1   1 
ATOM   599  C  CD2   . PHE A 1 89  ? 119.244 95.579  115.629 1.00 28.09  ? 77  PHE A CD2   1 
ATOM   600  C  CE1   . PHE A 1 89  ? 121.492 95.383  114.062 1.00 28.16  ? 77  PHE A CE1   1 
ATOM   601  C  CE2   . PHE A 1 89  ? 119.396 94.509  114.775 1.00 27.33  ? 77  PHE A CE2   1 
ATOM   602  C  CZ    . PHE A 1 89  ? 120.521 94.411  113.991 1.00 26.41  ? 77  PHE A CZ    1 
ATOM   603  N  N     . PHE A 1 90  ? 117.103 98.225  115.879 1.00 30.23  ? 78  PHE A N     1 
ATOM   604  C  CA    . PHE A 1 90  ? 115.909 97.787  115.163 1.00 24.04  ? 78  PHE A CA    1 
ATOM   605  C  C     . PHE A 1 90  ? 115.234 98.940  114.429 1.00 26.48  ? 78  PHE A C     1 
ATOM   606  O  O     . PHE A 1 90  ? 114.662 98.735  113.350 1.00 31.72  ? 78  PHE A O     1 
ATOM   607  C  CB    . PHE A 1 90  ? 114.945 97.104  116.128 1.00 23.73  ? 78  PHE A CB    1 
ATOM   608  C  CG    . PHE A 1 90  ? 115.393 95.739  116.553 1.00 26.50  ? 78  PHE A CG    1 
ATOM   609  C  CD1   . PHE A 1 90  ? 115.520 94.721  115.628 1.00 30.62  ? 78  PHE A CD1   1 
ATOM   610  C  CD2   . PHE A 1 90  ? 115.706 95.476  117.873 1.00 28.40  ? 78  PHE A CD2   1 
ATOM   611  C  CE1   . PHE A 1 90  ? 115.940 93.467  116.012 1.00 30.65  ? 78  PHE A CE1   1 
ATOM   612  C  CE2   . PHE A 1 90  ? 116.128 94.224  118.262 1.00 25.97  ? 78  PHE A CE2   1 
ATOM   613  C  CZ    . PHE A 1 90  ? 116.244 93.218  117.331 1.00 27.32  ? 78  PHE A CZ    1 
ATOM   614  N  N     . GLY A 1 91  ? 115.302 100.155 114.976 1.00 27.61  ? 79  GLY A N     1 
ATOM   615  C  CA    . GLY A 1 91  ? 114.764 101.300 114.265 1.00 27.87  ? 79  GLY A CA    1 
ATOM   616  C  C     . GLY A 1 91  ? 115.517 101.598 112.985 1.00 31.33  ? 79  GLY A C     1 
ATOM   617  O  O     . GLY A 1 91  ? 114.909 101.918 111.960 1.00 30.81  ? 79  GLY A O     1 
ATOM   618  N  N     . ALA A 1 92  ? 116.850 101.504 113.025 1.00 33.54  ? 80  ALA A N     1 
ATOM   619  C  CA    . ALA A 1 92  ? 117.629 101.675 111.805 1.00 25.73  ? 80  ALA A CA    1 
ATOM   620  C  C     . ALA A 1 92  ? 117.266 100.618 110.776 1.00 26.68  ? 80  ALA A C     1 
ATOM   621  O  O     . ALA A 1 92  ? 117.088 100.929 109.590 1.00 30.39  ? 80  ALA A O     1 
ATOM   622  C  CB    . ALA A 1 92  ? 119.122 101.624 112.124 1.00 27.98  ? 80  ALA A CB    1 
ATOM   623  N  N     . ARG A 1 93  ? 117.133 99.363  111.215 1.00 28.58  ? 81  ARG A N     1 
ATOM   624  C  CA    . ARG A 1 93  ? 116.731 98.299  110.297 1.00 28.92  ? 81  ARG A CA    1 
ATOM   625  C  C     . ARG A 1 93  ? 115.407 98.632  109.622 1.00 27.90  ? 81  ARG A C     1 
ATOM   626  O  O     . ARG A 1 93  ? 115.293 98.583  108.390 1.00 29.00  ? 81  ARG A O     1 
ATOM   627  C  CB    . ARG A 1 93  ? 116.623 96.969  111.045 1.00 32.18  ? 81  ARG A CB    1 
ATOM   628  C  CG    . ARG A 1 93  ? 117.898 96.143  111.089 1.00 36.36  ? 81  ARG A CG    1 
ATOM   629  C  CD    . ARG A 1 93  ? 118.379 95.685  109.716 1.00 45.34  ? 81  ARG A CD    1 
ATOM   630  N  NE    . ARG A 1 93  ? 117.311 95.587  108.729 1.00 56.70  ? 81  ARG A NE    1 
ATOM   631  C  CZ    . ARG A 1 93  ? 117.507 95.576  107.417 1.00 61.72  ? 81  ARG A CZ    1 
ATOM   632  N  NH1   . ARG A 1 93  ? 118.723 95.653  106.900 1.00 54.43  ? 81  ARG A NH1   1 
ATOM   633  N  NH2   . ARG A 1 93  ? 116.458 95.486  106.604 1.00 50.13  ? 81  ARG A NH2   1 
ATOM   634  N  N     . ALA A 1 94  ? 114.397 98.994  110.418 1.00 29.77  ? 82  ALA A N     1 
ATOM   635  C  CA    . ALA A 1 94  ? 113.068 99.246  109.868 1.00 25.69  ? 82  ALA A CA    1 
ATOM   636  C  C     . ALA A 1 94  ? 113.063 100.442 108.924 1.00 27.64  ? 82  ALA A C     1 
ATOM   637  O  O     . ALA A 1 94  ? 112.469 100.382 107.841 1.00 35.28  ? 82  ALA A O     1 
ATOM   638  C  CB    . ALA A 1 94  ? 112.064 99.454  110.999 1.00 24.35  ? 82  ALA A CB    1 
ATOM   639  N  N     . ALA A 1 95  ? 113.718 101.540 109.312 1.00 23.99  ? 83  ALA A N     1 
ATOM   640  C  CA    . ALA A 1 95  ? 113.702 102.736 108.475 1.00 18.39  ? 83  ALA A CA    1 
ATOM   641  C  C     . ALA A 1 95  ? 114.429 102.508 107.156 1.00 25.79  ? 83  ALA A C     1 
ATOM   642  O  O     . ALA A 1 95  ? 113.931 102.903 106.091 1.00 29.47  ? 83  ALA A O     1 
ATOM   643  C  CB    . ALA A 1 95  ? 114.314 103.912 109.230 1.00 20.33  ? 83  ALA A CB    1 
ATOM   644  N  N     . THR A 1 96  ? 115.606 101.877 107.196 1.00 24.41  ? 84  THR A N     1 
ATOM   645  C  CA    . THR A 1 96  ? 116.336 101.654 105.954 1.00 19.86  ? 84  THR A CA    1 
ATOM   646  C  C     . THR A 1 96  ? 115.612 100.658 105.059 1.00 24.69  ? 84  THR A C     1 
ATOM   647  O  O     . THR A 1 96  ? 115.609 100.813 103.832 1.00 25.98  ? 84  THR A O     1 
ATOM   648  C  CB    . THR A 1 96  ? 117.761 101.194 106.249 1.00 23.14  ? 84  THR A CB    1 
ATOM   649  O  OG1   . THR A 1 96  ? 117.732 100.024 107.074 1.00 33.47  ? 84  THR A OG1   1 
ATOM   650  C  CG2   . THR A 1 96  ? 118.523 102.296 106.957 1.00 22.21  ? 84  THR A CG2   1 
ATOM   651  N  N     . GLY A 1 97  ? 114.980 99.637  105.647 1.00 24.05  ? 85  GLY A N     1 
ATOM   652  C  CA    . GLY A 1 97  ? 114.183 98.728  104.844 1.00 22.76  ? 85  GLY A CA    1 
ATOM   653  C  C     . GLY A 1 97  ? 113.005 99.415  104.184 1.00 22.60  ? 85  GLY A C     1 
ATOM   654  O  O     . GLY A 1 97  ? 112.698 99.158  103.018 1.00 24.69  ? 85  GLY A O     1 
ATOM   655  N  N     . PHE A 1 98  ? 112.332 100.303 104.920 1.00 25.47  ? 86  PHE A N     1 
ATOM   656  C  CA    . PHE A 1 98  ? 111.219 101.051 104.347 1.00 23.62  ? 86  PHE A CA    1 
ATOM   657  C  C     . PHE A 1 98  ? 111.680 101.910 103.177 1.00 22.98  ? 86  PHE A C     1 
ATOM   658  O  O     . PHE A 1 98  ? 111.035 101.942 102.123 1.00 23.53  ? 86  PHE A O     1 
ATOM   659  C  CB    . PHE A 1 98  ? 110.562 101.917 105.422 1.00 21.74  ? 86  PHE A CB    1 
ATOM   660  C  CG    . PHE A 1 98  ? 109.714 103.025 104.869 1.00 25.93  ? 86  PHE A CG    1 
ATOM   661  C  CD1   . PHE A 1 98  ? 108.440 102.769 104.402 1.00 27.85  ? 86  PHE A CD1   1 
ATOM   662  C  CD2   . PHE A 1 98  ? 110.192 104.322 104.812 1.00 25.56  ? 86  PHE A CD2   1 
ATOM   663  C  CE1   . PHE A 1 98  ? 107.659 103.781 103.893 1.00 22.82  ? 86  PHE A CE1   1 
ATOM   664  C  CE2   . PHE A 1 98  ? 109.416 105.334 104.298 1.00 24.16  ? 86  PHE A CE2   1 
ATOM   665  C  CZ    . PHE A 1 98  ? 108.147 105.061 103.840 1.00 22.53  ? 86  PHE A CZ    1 
ATOM   666  N  N     . GLY A 1 99  ? 112.797 102.618 103.348 1.00 24.01  ? 87  GLY A N     1 
ATOM   667  C  CA    . GLY A 1 99  ? 113.303 103.449 102.265 1.00 18.59  ? 87  GLY A CA    1 
ATOM   668  C  C     . GLY A 1 99  ? 113.705 102.642 101.046 1.00 20.00  ? 87  GLY A C     1 
ATOM   669  O  O     . GLY A 1 99  ? 113.405 103.020 99.909  1.00 22.68  ? 87  GLY A O     1 
ATOM   670  N  N     . HIS A 1 100 ? 114.384 101.516 101.266 1.00 21.64  ? 88  HIS A N     1 
ATOM   671  C  CA    . HIS A 1 100 ? 114.774 100.637 100.169 1.00 21.11  ? 88  HIS A CA    1 
ATOM   672  C  C     . HIS A 1 100 ? 113.551 100.138 99.406  1.00 21.33  ? 88  HIS A C     1 
ATOM   673  O  O     . HIS A 1 100 ? 113.510 100.185 98.168  1.00 24.58  ? 88  HIS A O     1 
ATOM   674  C  CB    . HIS A 1 100 ? 115.595 99.478  100.740 1.00 21.73  ? 88  HIS A CB    1 
ATOM   675  C  CG    . HIS A 1 100 ? 115.804 98.337  99.796  1.00 22.66  ? 88  HIS A CG    1 
ATOM   676  N  ND1   . HIS A 1 100 ? 114.853 97.365  99.580  1.00 24.29  ? 88  HIS A ND1   1 
ATOM   677  C  CD2   . HIS A 1 100 ? 116.873 97.990  99.043  1.00 27.77  ? 88  HIS A CD2   1 
ATOM   678  C  CE1   . HIS A 1 100 ? 115.317 96.481  98.716  1.00 25.46  ? 88  HIS A CE1   1 
ATOM   679  N  NE2   . HIS A 1 100 ? 116.542 96.836  98.376  1.00 29.53  ? 88  HIS A NE2   1 
ATOM   680  N  N     . ASP A 1 101 ? 112.530 99.676  100.133 1.00 21.71  ? 89  ASP A N     1 
ATOM   681  C  CA    . ASP A 1 101 ? 111.336 99.148  99.484  1.00 19.56  ? 89  ASP A CA    1 
ATOM   682  C  C     . ASP A 1 101 ? 110.577 100.233 98.731  1.00 20.42  ? 89  ASP A C     1 
ATOM   683  O  O     . ASP A 1 101 ? 110.056 99.985  97.638  1.00 22.91  ? 89  ASP A O     1 
ATOM   684  C  CB    . ASP A 1 101 ? 110.433 98.479  100.517 1.00 26.09  ? 89  ASP A CB    1 
ATOM   685  C  CG    . ASP A 1 101 ? 111.013 97.185  101.043 1.00 31.92  ? 89  ASP A CG    1 
ATOM   686  O  OD1   . ASP A 1 101 ? 112.026 96.715  100.488 1.00 30.36  ? 89  ASP A OD1   1 
ATOM   687  O  OD2   . ASP A 1 101 ? 110.451 96.632  102.009 1.00 38.20  ? 89  ASP A OD2   1 
ATOM   688  N  N     . LEU A 1 102 ? 110.490 101.438 99.299  1.00 20.37  ? 90  LEU A N     1 
ATOM   689  C  CA    . LEU A 1 102 ? 109.789 102.520 98.613  1.00 18.42  ? 90  LEU A CA    1 
ATOM   690  C  C     . LEU A 1 102 ? 110.520 102.939 97.343  1.00 20.96  ? 90  LEU A C     1 
ATOM   691  O  O     . LEU A 1 102 ? 109.886 103.176 96.307  1.00 23.10  ? 90  LEU A O     1 
ATOM   692  C  CB    . LEU A 1 102 ? 109.603 103.709 99.555  1.00 20.43  ? 90  LEU A CB    1 
ATOM   693  C  CG    . LEU A 1 102 ? 108.662 104.821 99.082  1.00 24.78  ? 90  LEU A CG    1 
ATOM   694  C  CD1   . LEU A 1 102 ? 107.298 104.270 98.723  1.00 25.14  ? 90  LEU A CD1   1 
ATOM   695  C  CD2   . LEU A 1 102 ? 108.532 105.901 100.136 1.00 21.78  ? 90  LEU A CD2   1 
ATOM   696  N  N     . ARG A 1 103 ? 111.854 103.028 97.397  1.00 21.99  ? 91  ARG A N     1 
ATOM   697  C  CA    . ARG A 1 103 ? 112.619 103.324 96.190  1.00 16.44  ? 91  ARG A CA    1 
ATOM   698  C  C     . ARG A 1 103 ? 112.396 102.260 95.126  1.00 17.91  ? 91  ARG A C     1 
ATOM   699  O  O     . ARG A 1 103 ? 112.211 102.580 93.944  1.00 23.39  ? 91  ARG A O     1 
ATOM   700  C  CB    . ARG A 1 103 ? 114.108 103.427 96.515  1.00 18.90  ? 91  ARG A CB    1 
ATOM   701  C  CG    . ARG A 1 103 ? 114.538 104.726 97.150  1.00 22.53  ? 91  ARG A CG    1 
ATOM   702  C  CD    . ARG A 1 103 ? 116.042 104.892 97.071  1.00 24.26  ? 91  ARG A CD    1 
ATOM   703  N  NE    . ARG A 1 103 ? 116.747 103.766 97.671  1.00 30.50  ? 91  ARG A NE    1 
ATOM   704  C  CZ    . ARG A 1 103 ? 117.129 103.707 98.938  1.00 28.40  ? 91  ARG A CZ    1 
ATOM   705  N  NH1   . ARG A 1 103 ? 116.893 104.701 99.778  1.00 26.62  ? 91  ARG A NH1   1 
ATOM   706  N  NH2   . ARG A 1 103 ? 117.763 102.624 99.375  1.00 21.93  ? 91  ARG A NH2   1 
ATOM   707  N  N     . ALA A 1 104 ? 112.419 100.986 95.525  1.00 19.99  ? 92  ALA A N     1 
ATOM   708  C  CA    . ALA A 1 104 ? 112.214 99.910  94.563  1.00 19.52  ? 92  ALA A CA    1 
ATOM   709  C  C     . ALA A 1 104 ? 110.831 99.989  93.931  1.00 26.61  ? 92  ALA A C     1 
ATOM   710  O  O     . ALA A 1 104 ? 110.686 99.816  92.716  1.00 28.09  ? 92  ALA A O     1 
ATOM   711  C  CB    . ALA A 1 104 ? 112.422 98.557  95.239  1.00 17.64  ? 92  ALA A CB    1 
ATOM   712  N  N     . ALA A 1 105 ? 109.802 100.258 94.739  1.00 25.94  ? 93  ALA A N     1 
ATOM   713  C  CA    . ALA A 1 105 ? 108.447 100.361 94.207  1.00 22.65  ? 93  ALA A CA    1 
ATOM   714  C  C     . ALA A 1 105 ? 108.315 101.520 93.230  1.00 25.32  ? 93  ALA A C     1 
ATOM   715  O  O     . ALA A 1 105 ? 107.704 101.376 92.162  1.00 31.08  ? 93  ALA A O     1 
ATOM   716  C  CB    . ALA A 1 105 ? 107.447 100.515 95.349  1.00 26.12  ? 93  ALA A CB    1 
ATOM   717  N  N     . VAL A 1 106 ? 108.883 102.679 93.574  1.00 23.56  ? 94  VAL A N     1 
ATOM   718  C  CA    . VAL A 1 106 ? 108.785 103.839 92.692  1.00 21.34  ? 94  VAL A CA    1 
ATOM   719  C  C     . VAL A 1 106 ? 109.493 103.564 91.372  1.00 24.02  ? 94  VAL A C     1 
ATOM   720  O  O     . VAL A 1 106 ? 108.958 103.841 90.292  1.00 31.55  ? 94  VAL A O     1 
ATOM   721  C  CB    . VAL A 1 106 ? 109.346 105.094 93.383  1.00 21.68  ? 94  VAL A CB    1 
ATOM   722  C  CG1   . VAL A 1 106 ? 109.468 106.231 92.390  1.00 23.38  ? 94  VAL A CG1   1 
ATOM   723  C  CG2   . VAL A 1 106 ? 108.460 105.500 94.542  1.00 23.80  ? 94  VAL A CG2   1 
ATOM   724  N  N     . PHE A 1 107 ? 110.703 103.001 91.439  1.00 23.97  ? 95  PHE A N     1 
ATOM   725  C  CA    . PHE A 1 107 ? 111.444 102.707 90.217  1.00 21.09  ? 95  PHE A CA    1 
ATOM   726  C  C     . PHE A 1 107 ? 110.705 101.695 89.353  1.00 24.66  ? 95  PHE A C     1 
ATOM   727  O  O     . PHE A 1 107 ? 110.624 101.855 88.128  1.00 28.21  ? 95  PHE A O     1 
ATOM   728  C  CB    . PHE A 1 107 ? 112.840 102.194 90.565  1.00 21.76  ? 95  PHE A CB    1 
ATOM   729  C  CG    . PHE A 1 107 ? 113.609 101.669 89.385  1.00 23.99  ? 95  PHE A CG    1 
ATOM   730  C  CD1   . PHE A 1 107 ? 114.237 102.535 88.513  1.00 22.74  ? 95  PHE A CD1   1 
ATOM   731  C  CD2   . PHE A 1 107 ? 113.709 100.310 89.153  1.00 26.01  ? 95  PHE A CD2   1 
ATOM   732  C  CE1   . PHE A 1 107 ? 114.948 102.060 87.437  1.00 23.71  ? 95  PHE A CE1   1 
ATOM   733  C  CE2   . PHE A 1 107 ? 114.417 99.831  88.076  1.00 28.24  ? 95  PHE A CE2   1 
ATOM   734  C  CZ    . PHE A 1 107 ? 115.037 100.707 87.217  1.00 24.76  ? 95  PHE A CZ    1 
ATOM   735  N  N     . THR A 1 108 ? 110.164 100.645 89.971  1.00 26.40  ? 96  THR A N     1 
ATOM   736  C  CA    . THR A 1 108 ? 109.476 99.612  89.209  1.00 25.49  ? 96  THR A CA    1 
ATOM   737  C  C     . THR A 1 108 ? 108.231 100.163 88.533  1.00 27.76  ? 96  THR A C     1 
ATOM   738  O  O     . THR A 1 108 ? 107.940 99.820  87.382  1.00 30.75  ? 96  THR A O     1 
ATOM   739  C  CB    . THR A 1 108 ? 109.121 98.441  90.122  1.00 27.43  ? 96  THR A CB    1 
ATOM   740  O  OG1   . THR A 1 108 ? 110.298 98.001  90.807  1.00 32.41  ? 96  THR A OG1   1 
ATOM   741  C  CG2   . THR A 1 108 ? 108.559 97.289  89.314  1.00 31.23  ? 96  THR A CG2   1 
ATOM   742  N  N     . HIS A 1 109 ? 107.476 101.017 89.228  1.00 29.51  ? 97  HIS A N     1 
ATOM   743  C  CA    . HIS A 1 109 ? 106.301 101.601 88.595  1.00 32.03  ? 97  HIS A CA    1 
ATOM   744  C  C     . HIS A 1 109 ? 106.686 102.553 87.469  1.00 36.03  ? 97  HIS A C     1 
ATOM   745  O  O     . HIS A 1 109 ? 106.029 102.577 86.422  1.00 36.07  ? 97  HIS A O     1 
ATOM   746  C  CB    . HIS A 1 109 ? 105.432 102.320 89.622  1.00 31.99  ? 97  HIS A CB    1 
ATOM   747  C  CG    . HIS A 1 109 ? 104.057 102.626 89.120  1.00 36.26  ? 97  HIS A CG    1 
ATOM   748  N  ND1   . HIS A 1 109 ? 103.168 101.643 88.745  1.00 37.61  ? 97  HIS A ND1   1 
ATOM   749  C  CD2   . HIS A 1 109 ? 103.427 103.804 88.905  1.00 39.70  ? 97  HIS A CD2   1 
ATOM   750  C  CE1   . HIS A 1 109 ? 102.046 102.202 88.331  1.00 41.69  ? 97  HIS A CE1   1 
ATOM   751  N  NE2   . HIS A 1 109 ? 102.177 103.513 88.419  1.00 44.70  ? 97  HIS A NE2   1 
ATOM   752  N  N     . VAL A 1 110 ? 107.742 103.346 87.659  1.00 33.66  ? 98  VAL A N     1 
ATOM   753  C  CA    . VAL A 1 110 ? 108.136 104.298 86.625  1.00 25.78  ? 98  VAL A CA    1 
ATOM   754  C  C     . VAL A 1 110 ? 108.627 103.568 85.380  1.00 32.22  ? 98  VAL A C     1 
ATOM   755  O  O     . VAL A 1 110 ? 108.359 103.993 84.251  1.00 39.44  ? 98  VAL A O     1 
ATOM   756  C  CB    . VAL A 1 110 ? 109.194 105.274 87.169  1.00 21.60  ? 98  VAL A CB    1 
ATOM   757  C  CG1   . VAL A 1 110 ? 109.824 106.061 86.038  1.00 22.24  ? 98  VAL A CG1   1 
ATOM   758  C  CG2   . VAL A 1 110 ? 108.569 106.215 88.174  1.00 23.87  ? 98  VAL A CG2   1 
ATOM   759  N  N     . THR A 1 111 ? 109.337 102.453 85.557  1.00 35.20  ? 99  THR A N     1 
ATOM   760  C  CA    . THR A 1 111 ? 109.862 101.733 84.401  1.00 36.75  ? 99  THR A CA    1 
ATOM   761  C  C     . THR A 1 111 ? 108.779 101.060 83.568  1.00 41.95  ? 99  THR A C     1 
ATOM   762  O  O     . THR A 1 111 ? 109.087 100.562 82.481  1.00 49.74  ? 99  THR A O     1 
ATOM   763  C  CB    . THR A 1 111 ? 110.890 100.693 84.843  1.00 36.79  ? 99  THR A CB    1 
ATOM   764  O  OG1   . THR A 1 111 ? 110.359 99.916  85.921  1.00 41.92  ? 99  THR A OG1   1 
ATOM   765  C  CG2   . THR A 1 111 ? 112.161 101.378 85.295  1.00 31.87  ? 99  THR A CG2   1 
ATOM   766  N  N     . THR A 1 112 ? 107.538 101.015 84.042  1.00 40.47  ? 100 THR A N     1 
ATOM   767  C  CA    . THR A 1 112 ? 106.420 100.517 83.254  1.00 39.78  ? 100 THR A CA    1 
ATOM   768  C  C     . THR A 1 112 ? 105.716 101.616 82.472  1.00 42.57  ? 100 THR A C     1 
ATOM   769  O  O     . THR A 1 112 ? 104.795 101.319 81.708  1.00 51.30  ? 100 THR A O     1 
ATOM   770  C  CB    . THR A 1 112 ? 105.407 99.807  84.156  1.00 44.17  ? 100 THR A CB    1 
ATOM   771  O  OG1   . THR A 1 112 ? 104.865 100.742 85.096  1.00 48.62  ? 100 THR A OG1   1 
ATOM   772  C  CG2   . THR A 1 112 ? 106.066 98.665  84.907  1.00 41.88  ? 100 THR A CG2   1 
ATOM   773  N  N     . PHE A 1 113 ? 106.129 102.869 82.642  1.00 43.42  ? 101 PHE A N     1 
ATOM   774  C  CA    . PHE A 1 113 ? 105.474 103.981 81.970  1.00 44.49  ? 101 PHE A CA    1 
ATOM   775  C  C     . PHE A 1 113 ? 105.712 103.930 80.466  1.00 49.69  ? 101 PHE A C     1 
ATOM   776  O  O     . PHE A 1 113 ? 106.744 103.450 79.991  1.00 51.14  ? 101 PHE A O     1 
ATOM   777  C  CB    . PHE A 1 113 ? 105.984 105.316 82.513  1.00 38.25  ? 101 PHE A CB    1 
ATOM   778  C  CG    . PHE A 1 113 ? 105.378 105.716 83.825  1.00 37.49  ? 101 PHE A CG    1 
ATOM   779  C  CD1   . PHE A 1 113 ? 104.310 105.019 84.357  1.00 42.77  ? 101 PHE A CD1   1 
ATOM   780  C  CD2   . PHE A 1 113 ? 105.878 106.798 84.526  1.00 31.58  ? 101 PHE A CD2   1 
ATOM   781  C  CE1   . PHE A 1 113 ? 103.759 105.391 85.563  1.00 39.40  ? 101 PHE A CE1   1 
ATOM   782  C  CE2   . PHE A 1 113 ? 105.330 107.173 85.730  1.00 35.69  ? 101 PHE A CE2   1 
ATOM   783  C  CZ    . PHE A 1 113 ? 104.270 106.469 86.250  1.00 35.88  ? 101 PHE A CZ    1 
ATOM   784  N  N     . SER A 1 114 ? 104.738 104.434 79.717  1.00 53.84  ? 102 SER A N     1 
ATOM   785  C  CA    . SER A 1 114 ? 104.909 104.663 78.290  1.00 55.97  ? 102 SER A CA    1 
ATOM   786  C  C     . SER A 1 114 ? 105.583 106.018 78.097  1.00 60.17  ? 102 SER A C     1 
ATOM   787  O  O     . SER A 1 114 ? 106.024 106.661 79.053  1.00 64.45  ? 102 SER A O     1 
ATOM   788  C  CB    . SER A 1 114 ? 103.565 104.574 77.572  1.00 59.16  ? 102 SER A CB    1 
ATOM   789  O  OG    . SER A 1 114 ? 102.735 103.589 78.161  1.00 70.64  ? 102 SER A OG    1 
ATOM   790  N  N     . ALA A 1 115 ? 105.686 106.468 76.846  1.00 63.02  ? 103 ALA A N     1 
ATOM   791  C  CA    . ALA A 1 115 ? 106.255 107.786 76.586  1.00 67.23  ? 103 ALA A CA    1 
ATOM   792  C  C     . ALA A 1 115 ? 105.374 108.893 77.154  1.00 68.87  ? 103 ALA A C     1 
ATOM   793  O  O     . ALA A 1 115 ? 105.881 109.865 77.724  1.00 64.66  ? 103 ALA A O     1 
ATOM   794  C  CB    . ALA A 1 115 ? 106.462 107.978 75.085  1.00 64.96  ? 103 ALA A CB    1 
ATOM   795  N  N     . GLU A 1 116 ? 104.054 108.759 77.012  1.00 66.01  ? 104 GLU A N     1 
ATOM   796  C  CA    . GLU A 1 116 ? 103.138 109.810 77.444  1.00 63.63  ? 104 GLU A CA    1 
ATOM   797  C  C     . GLU A 1 116 ? 103.135 109.946 78.965  1.00 64.41  ? 104 GLU A C     1 
ATOM   798  O  O     . GLU A 1 116 ? 103.249 111.056 79.502  1.00 65.07  ? 104 GLU A O     1 
ATOM   799  C  CB    . GLU A 1 116 ? 101.734 109.508 76.901  1.00 63.81  ? 104 GLU A CB    1 
ATOM   800  C  CG    . GLU A 1 116 ? 100.522 109.829 77.791  1.00 70.22  ? 104 GLU A CG    1 
ATOM   801  C  CD    . GLU A 1 116 ? 100.393 111.293 78.201  1.00 75.02  ? 104 GLU A CD    1 
ATOM   802  O  OE1   . GLU A 1 116 ? 101.280 112.110 77.878  1.00 72.93  ? 104 GLU A OE1   1 
ATOM   803  O  OE2   . GLU A 1 116 ? 99.380  111.630 78.848  1.00 74.74  ? 104 GLU A OE2   1 
ATOM   804  N  N     . GLU A 1 117 ? 103.020 108.822 79.677  1.00 59.06  ? 105 GLU A N     1 
ATOM   805  C  CA    . GLU A 1 117 ? 103.008 108.868 81.136  1.00 53.41  ? 105 GLU A CA    1 
ATOM   806  C  C     . GLU A 1 117 ? 104.336 109.372 81.685  1.00 53.09  ? 105 GLU A C     1 
ATOM   807  O  O     . GLU A 1 117 ? 104.363 110.143 82.649  1.00 54.21  ? 105 GLU A O     1 
ATOM   808  C  CB    . GLU A 1 117 ? 102.683 107.487 81.699  1.00 51.51  ? 105 GLU A CB    1 
ATOM   809  C  CG    . GLU A 1 117 ? 101.375 106.909 81.201  1.00 58.42  ? 105 GLU A CG    1 
ATOM   810  C  CD    . GLU A 1 117 ? 101.520 105.483 80.718  1.00 64.91  ? 105 GLU A CD    1 
ATOM   811  O  OE1   . GLU A 1 117 ? 102.153 104.676 81.428  1.00 59.99  ? 105 GLU A OE1   1 
ATOM   812  O  OE2   . GLU A 1 117 ? 101.005 105.171 79.624  1.00 72.16  ? 105 GLU A OE2   1 
ATOM   813  N  N     . ALA A 1 118 ? 105.449 108.938 81.091  1.00 53.52  ? 106 ALA A N     1 
ATOM   814  C  CA    . ALA A 1 118 ? 106.755 109.399 81.548  1.00 52.20  ? 106 ALA A CA    1 
ATOM   815  C  C     . ALA A 1 118 ? 106.942 110.886 81.277  1.00 58.53  ? 106 ALA A C     1 
ATOM   816  O  O     . ALA A 1 118 ? 107.524 111.603 82.099  1.00 59.48  ? 106 ALA A O     1 
ATOM   817  C  CB    . ALA A 1 118 ? 107.864 108.585 80.885  1.00 47.05  ? 106 ALA A CB    1 
ATOM   818  N  N     . GLY A 1 119 ? 106.461 111.367 80.129  1.00 59.16  ? 107 GLY A N     1 
ATOM   819  C  CA    . GLY A 1 119 ? 106.543 112.782 79.821  1.00 55.66  ? 107 GLY A CA    1 
ATOM   820  C  C     . GLY A 1 119 ? 105.626 113.645 80.657  1.00 57.70  ? 107 GLY A C     1 
ATOM   821  O  O     . GLY A 1 119 ? 105.882 114.845 80.800  1.00 57.48  ? 107 GLY A O     1 
ATOM   822  N  N     . ARG A 1 120 ? 104.558 113.063 81.207  1.00 57.34  ? 108 ARG A N     1 
ATOM   823  C  CA    . ARG A 1 120 ? 103.707 113.806 82.130  1.00 54.06  ? 108 ARG A CA    1 
ATOM   824  C  C     . ARG A 1 120 ? 104.463 114.274 83.367  1.00 52.93  ? 108 ARG A C     1 
ATOM   825  O  O     . ARG A 1 120 ? 104.029 115.227 84.021  1.00 52.28  ? 108 ARG A O     1 
ATOM   826  C  CB    . ARG A 1 120 ? 102.514 112.954 82.556  1.00 53.20  ? 108 ARG A CB    1 
ATOM   827  C  CG    . ARG A 1 120 ? 101.349 112.994 81.596  1.00 55.00  ? 108 ARG A CG    1 
ATOM   828  C  CD    . ARG A 1 120 ? 100.467 111.778 81.776  1.00 58.91  ? 108 ARG A CD    1 
ATOM   829  N  NE    . ARG A 1 120 ? 100.140 111.545 83.176  1.00 72.22  ? 108 ARG A NE    1 
ATOM   830  C  CZ    . ARG A 1 120 ? 99.405  110.532 83.612  1.00 73.93  ? 108 ARG A CZ    1 
ATOM   831  N  NH1   . ARG A 1 120 ? 98.906  109.632 82.780  1.00 64.18  ? 108 ARG A NH1   1 
ATOM   832  N  NH2   . ARG A 1 120 ? 99.165  110.419 84.915  1.00 72.63  ? 108 ARG A NH2   1 
ATOM   833  N  N     . PHE A 1 121 ? 105.575 113.625 83.707  1.00 51.66  ? 109 PHE A N     1 
ATOM   834  C  CA    . PHE A 1 121 ? 106.381 113.980 84.868  1.00 50.19  ? 109 PHE A CA    1 
ATOM   835  C  C     . PHE A 1 121 ? 107.750 114.533 84.511  1.00 51.29  ? 109 PHE A C     1 
ATOM   836  O  O     . PHE A 1 121 ? 108.184 115.521 85.106  1.00 56.35  ? 109 PHE A O     1 
ATOM   837  C  CB    . PHE A 1 121 ? 106.565 112.761 85.778  1.00 47.54  ? 109 PHE A CB    1 
ATOM   838  C  CG    . PHE A 1 121 ? 105.290 112.249 86.372  1.00 47.82  ? 109 PHE A CG    1 
ATOM   839  C  CD1   . PHE A 1 121 ? 104.724 112.871 87.468  1.00 46.01  ? 109 PHE A CD1   1 
ATOM   840  C  CD2   . PHE A 1 121 ? 104.657 111.144 85.835  1.00 49.57  ? 109 PHE A CD2   1 
ATOM   841  C  CE1   . PHE A 1 121 ? 103.552 112.402 88.017  1.00 46.41  ? 109 PHE A CE1   1 
ATOM   842  C  CE2   . PHE A 1 121 ? 103.483 110.671 86.381  1.00 49.20  ? 109 PHE A CE2   1 
ATOM   843  C  CZ    . PHE A 1 121 ? 102.931 111.302 87.472  1.00 48.27  ? 109 PHE A CZ    1 
ATOM   844  N  N     . GLY A 1 122 ? 108.440 113.924 83.560  1.00 48.56  ? 110 GLY A N     1 
ATOM   845  C  CA    . GLY A 1 122 ? 109.795 114.333 83.226  1.00 49.75  ? 110 GLY A CA    1 
ATOM   846  C  C     . GLY A 1 122 ? 110.835 113.541 83.991  1.00 49.17  ? 110 GLY A C     1 
ATOM   847  O  O     . GLY A 1 122 ? 110.628 113.112 85.124  1.00 52.40  ? 110 GLY A O     1 
ATOM   848  N  N     . ALA A 1 123 ? 111.990 113.353 83.350  1.00 46.44  ? 111 ALA A N     1 
ATOM   849  C  CA    . ALA A 1 123 ? 113.038 112.524 83.937  1.00 40.93  ? 111 ALA A CA    1 
ATOM   850  C  C     . ALA A 1 123 ? 113.574 113.127 85.230  1.00 44.39  ? 111 ALA A C     1 
ATOM   851  O  O     . ALA A 1 123 ? 113.836 112.403 86.198  1.00 43.14  ? 111 ALA A O     1 
ATOM   852  C  CB    . ALA A 1 123 ? 114.168 112.320 82.931  1.00 37.37  ? 111 ALA A CB    1 
ATOM   853  N  N     . ALA A 1 124 ? 113.757 114.448 85.262  1.00 45.58  ? 112 ALA A N     1 
ATOM   854  C  CA    . ALA A 1 124 ? 114.297 115.096 86.454  1.00 46.15  ? 112 ALA A CA    1 
ATOM   855  C  C     . ALA A 1 124 ? 113.356 114.940 87.642  1.00 44.02  ? 112 ALA A C     1 
ATOM   856  O  O     . ALA A 1 124 ? 113.788 114.621 88.757  1.00 43.54  ? 112 ALA A O     1 
ATOM   857  C  CB    . ALA A 1 124 ? 114.565 116.573 86.166  1.00 44.15  ? 112 ALA A CB    1 
ATOM   858  N  N     . SER A 1 125 ? 112.060 115.164 87.420  1.00 42.25  ? 113 SER A N     1 
ATOM   859  C  CA    . SER A 1 125 ? 111.087 115.016 88.494  1.00 44.51  ? 113 SER A CA    1 
ATOM   860  C  C     . SER A 1 125 ? 111.014 113.573 88.975  1.00 43.94  ? 113 SER A C     1 
ATOM   861  O  O     . SER A 1 125 ? 110.922 113.318 90.182  1.00 45.36  ? 113 SER A O     1 
ATOM   862  C  CB    . SER A 1 125 ? 109.716 115.498 88.026  1.00 46.12  ? 113 SER A CB    1 
ATOM   863  O  OG    . SER A 1 125 ? 108.827 115.646 89.116  1.00 54.22  ? 113 SER A OG    1 
ATOM   864  N  N     . LEU A 1 126 ? 111.056 112.618 88.044  1.00 40.11  ? 114 LEU A N     1 
ATOM   865  C  CA    . LEU A 1 126 ? 111.025 111.211 88.423  1.00 34.26  ? 114 LEU A CA    1 
ATOM   866  C  C     . LEU A 1 126 ? 112.244 110.834 89.253  1.00 37.18  ? 114 LEU A C     1 
ATOM   867  O  O     . LEU A 1 126 ? 112.125 110.110 90.244  1.00 45.14  ? 114 LEU A O     1 
ATOM   868  C  CB    . LEU A 1 126 ? 110.929 110.335 87.177  1.00 34.19  ? 114 LEU A CB    1 
ATOM   869  C  CG    . LEU A 1 126 ? 109.599 110.405 86.429  1.00 37.27  ? 114 LEU A CG    1 
ATOM   870  C  CD1   . LEU A 1 126 ? 109.693 109.672 85.106  1.00 32.40  ? 114 LEU A CD1   1 
ATOM   871  C  CD2   . LEU A 1 126 ? 108.469 109.853 87.278  1.00 36.57  ? 114 LEU A CD2   1 
ATOM   872  N  N     . LEU A 1 127 ? 113.426 111.318 88.870  1.00 36.04  ? 115 LEU A N     1 
ATOM   873  C  CA    . LEU A 1 127 ? 114.625 111.036 89.654  1.00 35.69  ? 115 LEU A CA    1 
ATOM   874  C  C     . LEU A 1 127 ? 114.524 111.641 91.050  1.00 36.02  ? 115 LEU A C     1 
ATOM   875  O  O     . LEU A 1 127 ? 114.843 110.987 92.055  1.00 42.03  ? 115 LEU A O     1 
ATOM   876  C  CB    . LEU A 1 127 ? 115.859 111.562 88.921  1.00 37.08  ? 115 LEU A CB    1 
ATOM   877  C  CG    . LEU A 1 127 ? 117.140 111.747 89.736  1.00 38.53  ? 115 LEU A CG    1 
ATOM   878  C  CD1   . LEU A 1 127 ? 117.744 110.409 90.108  1.00 39.13  ? 115 LEU A CD1   1 
ATOM   879  C  CD2   . LEU A 1 127 ? 118.138 112.593 88.971  1.00 40.70  ? 115 LEU A CD2   1 
ATOM   880  N  N     . THR A 1 128 ? 114.074 112.896 91.131  1.00 38.20  ? 116 THR A N     1 
ATOM   881  C  CA    . THR A 1 128 ? 113.983 113.557 92.428  1.00 37.31  ? 116 THR A CA    1 
ATOM   882  C  C     . THR A 1 128 ? 112.994 112.850 93.341  1.00 39.00  ? 116 THR A C     1 
ATOM   883  O  O     . THR A 1 128 ? 113.273 112.651 94.525  1.00 43.68  ? 116 THR A O     1 
ATOM   884  C  CB    . THR A 1 128 ? 113.594 115.024 92.260  1.00 42.07  ? 116 THR A CB    1 
ATOM   885  O  OG1   . THR A 1 128 ? 112.418 115.119 91.450  1.00 49.61  ? 116 THR A OG1   1 
ATOM   886  C  CG2   . THR A 1 128 ? 114.723 115.800 91.610  1.00 48.00  ? 116 THR A CG2   1 
ATOM   887  N  N     . ARG A 1 129 ? 111.845 112.444 92.817  1.00 38.54  ? 117 ARG A N     1 
ATOM   888  C  CA    . ARG A 1 129 ? 110.864 111.775 93.658  1.00 39.13  ? 117 ARG A CA    1 
ATOM   889  C  C     . ARG A 1 129 ? 111.077 110.269 93.739  1.00 38.64  ? 117 ARG A C     1 
ATOM   890  O  O     . ARG A 1 129 ? 110.288 109.580 94.392  1.00 47.39  ? 117 ARG A O     1 
ATOM   891  C  CB    . ARG A 1 129 ? 109.448 112.103 93.181  1.00 37.53  ? 117 ARG A CB    1 
ATOM   892  C  CG    . ARG A 1 129 ? 109.021 111.456 91.901  1.00 33.55  ? 117 ARG A CG    1 
ATOM   893  C  CD    . ARG A 1 129 ? 107.650 111.966 91.527  1.00 39.21  ? 117 ARG A CD    1 
ATOM   894  N  NE    . ARG A 1 129 ? 107.673 113.344 91.052  1.00 49.26  ? 117 ARG A NE    1 
ATOM   895  C  CZ    . ARG A 1 129 ? 106.593 114.045 90.736  1.00 48.79  ? 117 ARG A CZ    1 
ATOM   896  N  NH1   . ARG A 1 129 ? 105.379 113.530 90.839  1.00 45.44  ? 117 ARG A NH1   1 
ATOM   897  N  NH2   . ARG A 1 129 ? 106.733 115.295 90.308  1.00 50.17  ? 117 ARG A NH2   1 
ATOM   898  N  N     . THR A 1 130 ? 112.112 109.744 93.089  1.00 35.97  ? 118 THR A N     1 
ATOM   899  C  CA    . THR A 1 130 ? 112.575 108.393 93.367  1.00 30.51  ? 118 THR A CA    1 
ATOM   900  C  C     . THR A 1 130 ? 113.658 108.365 94.433  1.00 34.94  ? 118 THR A C     1 
ATOM   901  O  O     . THR A 1 130 ? 113.819 107.348 95.115  1.00 42.88  ? 118 THR A O     1 
ATOM   902  C  CB    . THR A 1 130 ? 113.106 107.735 92.089  1.00 26.21  ? 118 THR A CB    1 
ATOM   903  O  OG1   . THR A 1 130 ? 112.197 107.981 91.012  1.00 34.33  ? 118 THR A OG1   1 
ATOM   904  C  CG2   . THR A 1 130 ? 113.252 106.235 92.276  1.00 22.11  ? 118 THR A CG2   1 
ATOM   905  N  N     . THR A 1 131 ? 114.403 109.456 94.605  1.00 33.81  ? 119 THR A N     1 
ATOM   906  C  CA    . THR A 1 131 ? 115.471 109.471 95.597  1.00 32.74  ? 119 THR A CA    1 
ATOM   907  C  C     . THR A 1 131 ? 115.161 110.352 96.801  1.00 36.08  ? 119 THR A C     1 
ATOM   908  O  O     . THR A 1 131 ? 115.065 109.852 97.926  1.00 37.95  ? 119 THR A O     1 
ATOM   909  C  CB    . THR A 1 131 ? 116.781 109.925 94.938  1.00 38.00  ? 119 THR A CB    1 
ATOM   910  O  OG1   . THR A 1 131 ? 116.531 111.058 94.098  1.00 37.06  ? 119 THR A OG1   1 
ATOM   911  C  CG2   . THR A 1 131 ? 117.373 108.808 94.106  1.00 34.29  ? 119 THR A CG2   1 
ATOM   912  N  N     . ASN A 1 132 ? 114.949 111.652 96.596  1.00 35.72  ? 120 ASN A N     1 
ATOM   913  C  CA    . ASN A 1 132 ? 114.907 112.579 97.720  1.00 35.13  ? 120 ASN A CA    1 
ATOM   914  C  C     . ASN A 1 132 ? 113.568 112.555 98.446  1.00 38.44  ? 120 ASN A C     1 
ATOM   915  O  O     . ASN A 1 132 ? 113.530 112.695 99.671  1.00 42.26  ? 120 ASN A O     1 
ATOM   916  C  CB    . ASN A 1 132 ? 115.230 113.989 97.234  1.00 40.70  ? 120 ASN A CB    1 
ATOM   917  C  CG    . ASN A 1 132 ? 116.606 114.082 96.621  1.00 51.08  ? 120 ASN A CG    1 
ATOM   918  O  OD1   . ASN A 1 132 ? 116.749 114.211 95.407  1.00 56.76  ? 120 ASN A OD1   1 
ATOM   919  N  ND2   . ASN A 1 132 ? 117.632 114.003 97.458  1.00 52.13  ? 120 ASN A ND2   1 
ATOM   920  N  N     . ASP A 1 133 ? 112.461 112.395 97.721  1.00 33.18  ? 121 ASP A N     1 
ATOM   921  C  CA    . ASP A 1 133 ? 111.168 112.283 98.389  1.00 32.92  ? 121 ASP A CA    1 
ATOM   922  C  C     . ASP A 1 133 ? 111.102 111.023 99.243  1.00 34.46  ? 121 ASP A C     1 
ATOM   923  O  O     . ASP A 1 133 ? 110.609 111.051 100.382 1.00 40.46  ? 121 ASP A O     1 
ATOM   924  C  CB    . ASP A 1 133 ? 110.044 112.298 97.356  1.00 36.02  ? 121 ASP A CB    1 
ATOM   925  C  CG    . ASP A 1 133 ? 110.050 113.550 96.508  1.00 42.58  ? 121 ASP A CG    1 
ATOM   926  O  OD1   . ASP A 1 133 ? 111.067 114.274 96.520  1.00 46.35  ? 121 ASP A OD1   1 
ATOM   927  O  OD2   . ASP A 1 133 ? 109.037 113.818 95.835  1.00 44.55  ? 121 ASP A OD2   1 
ATOM   928  N  N     . VAL A 1 134 ? 111.606 109.910 98.709  1.00 31.99  ? 122 VAL A N     1 
ATOM   929  C  CA    . VAL A 1 134 ? 111.688 108.682 99.487  1.00 28.96  ? 122 VAL A CA    1 
ATOM   930  C  C     . VAL A 1 134 ? 112.592 108.881 100.693 1.00 29.45  ? 122 VAL A C     1 
ATOM   931  O  O     . VAL A 1 134 ? 112.297 108.396 101.790 1.00 33.29  ? 122 VAL A O     1 
ATOM   932  C  CB    . VAL A 1 134 ? 112.170 107.518 98.602  1.00 25.80  ? 122 VAL A CB    1 
ATOM   933  C  CG1   . VAL A 1 134 ? 112.265 106.247 99.417  1.00 24.63  ? 122 VAL A CG1   1 
ATOM   934  C  CG2   . VAL A 1 134 ? 111.233 107.329 97.425  1.00 23.52  ? 122 VAL A CG2   1 
ATOM   935  N  N     . GLY A 1 135 ? 113.706 109.592 100.512 1.00 30.65  ? 123 GLY A N     1 
ATOM   936  C  CA    . GLY A 1 135 ? 114.579 109.870 101.639 1.00 28.76  ? 123 GLY A CA    1 
ATOM   937  C  C     . GLY A 1 135 ? 113.901 110.698 102.713 1.00 31.62  ? 123 GLY A C     1 
ATOM   938  O  O     . GLY A 1 135 ? 114.120 110.483 103.904 1.00 35.15  ? 123 GLY A O     1 
ATOM   939  N  N     . HIS A 1 136 ? 113.068 111.655 102.305 1.00 32.95  ? 124 HIS A N     1 
ATOM   940  C  CA    . HIS A 1 136 ? 112.338 112.473 103.269 1.00 34.49  ? 124 HIS A CA    1 
ATOM   941  C  C     . HIS A 1 136 ? 111.343 111.641 104.066 1.00 31.08  ? 124 HIS A C     1 
ATOM   942  O  O     . HIS A 1 136 ? 111.245 111.781 105.292 1.00 38.11  ? 124 HIS A O     1 
ATOM   943  C  CB    . HIS A 1 136 ? 111.624 113.615 102.552 1.00 37.78  ? 124 HIS A CB    1 
ATOM   944  C  CG    . HIS A 1 136 ? 112.545 114.681 102.051 1.00 42.65  ? 124 HIS A CG    1 
ATOM   945  N  ND1   . HIS A 1 136 ? 112.151 115.636 101.141 1.00 42.99  ? 124 HIS A ND1   1 
ATOM   946  C  CD2   . HIS A 1 136 ? 113.841 114.943 102.336 1.00 47.40  ? 124 HIS A CD2   1 
ATOM   947  C  CE1   . HIS A 1 136 ? 113.167 116.440 100.884 1.00 49.01  ? 124 HIS A CE1   1 
ATOM   948  N  NE2   . HIS A 1 136 ? 114.204 116.041 101.597 1.00 52.91  ? 124 HIS A NE2   1 
ATOM   949  N  N     . ILE A 1 137 ? 110.594 110.768 103.393 1.00 29.47  ? 125 ILE A N     1 
ATOM   950  C  CA    . ILE A 1 137 ? 109.639 109.937 104.124 1.00 29.30  ? 125 ILE A CA    1 
ATOM   951  C  C     . ILE A 1 137 ? 110.369 108.942 105.025 1.00 31.09  ? 125 ILE A C     1 
ATOM   952  O  O     . ILE A 1 137 ? 109.928 108.656 106.148 1.00 35.31  ? 125 ILE A O     1 
ATOM   953  C  CB    . ILE A 1 137 ? 108.677 109.237 103.151 1.00 28.90  ? 125 ILE A CB    1 
ATOM   954  C  CG1   . ILE A 1 137 ? 108.038 110.264 102.221 1.00 28.56  ? 125 ILE A CG1   1 
ATOM   955  C  CG2   . ILE A 1 137 ? 107.594 108.509 103.916 1.00 26.39  ? 125 ILE A CG2   1 
ATOM   956  C  CD1   . ILE A 1 137 ? 107.048 109.676 101.265 1.00 29.63  ? 125 ILE A CD1   1 
ATOM   957  N  N     . GLN A 1 138 ? 111.500 108.408 104.559 1.00 29.61  ? 126 GLN A N     1 
ATOM   958  C  CA    . GLN A 1 138 ? 112.302 107.520 105.393 1.00 27.17  ? 126 GLN A CA    1 
ATOM   959  C  C     . GLN A 1 138 ? 112.846 108.250 106.613 1.00 33.55  ? 126 GLN A C     1 
ATOM   960  O  O     . GLN A 1 138 ? 112.921 107.678 107.704 1.00 36.99  ? 126 GLN A O     1 
ATOM   961  C  CB    . GLN A 1 138 ? 113.444 106.922 104.573 1.00 27.23  ? 126 GLN A CB    1 
ATOM   962  C  CG    . GLN A 1 138 ? 114.450 106.139 105.393 1.00 24.51  ? 126 GLN A CG    1 
ATOM   963  C  CD    . GLN A 1 138 ? 115.616 105.653 104.569 1.00 27.58  ? 126 GLN A CD    1 
ATOM   964  O  OE1   . GLN A 1 138 ? 115.559 105.639 103.343 1.00 30.56  ? 126 GLN A OE1   1 
ATOM   965  N  NE2   . GLN A 1 138 ? 116.688 105.255 105.239 1.00 31.84  ? 126 GLN A NE2   1 
ATOM   966  N  N     . GLN A 1 139 ? 113.249 109.510 106.442 1.00 32.92  ? 127 GLN A N     1 
ATOM   967  C  CA    . GLN A 1 139 ? 113.706 110.306 107.574 1.00 32.32  ? 127 GLN A CA    1 
ATOM   968  C  C     . GLN A 1 139 ? 112.576 110.548 108.562 1.00 34.53  ? 127 GLN A C     1 
ATOM   969  O  O     . GLN A 1 139 ? 112.793 110.543 109.778 1.00 41.41  ? 127 GLN A O     1 
ATOM   970  C  CB    . GLN A 1 139 ? 114.286 111.632 107.083 1.00 34.01  ? 127 GLN A CB    1 
ATOM   971  C  CG    . GLN A 1 139 ? 114.737 112.558 108.196 1.00 45.14  ? 127 GLN A CG    1 
ATOM   972  C  CD    . GLN A 1 139 ? 115.245 113.886 107.681 1.00 56.95  ? 127 GLN A CD    1 
ATOM   973  O  OE1   . GLN A 1 139 ? 114.790 114.379 106.650 1.00 62.38  ? 127 GLN A OE1   1 
ATOM   974  N  NE2   . GLN A 1 139 ? 116.188 114.478 108.402 1.00 53.74  ? 127 GLN A NE2   1 
ATOM   975  N  N     . LEU A 1 140 ? 111.362 110.769 108.056 1.00 33.62  ? 128 LEU A N     1 
ATOM   976  C  CA    . LEU A 1 140 ? 110.208 110.881 108.944 1.00 34.15  ? 128 LEU A CA    1 
ATOM   977  C  C     . LEU A 1 140 ? 110.028 109.611 109.763 1.00 35.98  ? 128 LEU A C     1 
ATOM   978  O  O     . LEU A 1 140 ? 109.830 109.667 110.981 1.00 40.62  ? 128 LEU A O     1 
ATOM   979  C  CB    . LEU A 1 140 ? 108.944 111.177 108.138 1.00 37.76  ? 128 LEU A CB    1 
ATOM   980  C  CG    . LEU A 1 140 ? 107.639 111.055 108.930 1.00 36.32  ? 128 LEU A CG    1 
ATOM   981  C  CD1   . LEU A 1 140 ? 107.433 112.268 109.819 1.00 38.70  ? 128 LEU A CD1   1 
ATOM   982  C  CD2   . LEU A 1 140 ? 106.451 110.850 108.012 1.00 36.44  ? 128 LEU A CD2   1 
ATOM   983  N  N     . VAL A 1 141 ? 110.104 108.451 109.108 1.00 36.69  ? 129 VAL A N     1 
ATOM   984  C  CA    . VAL A 1 141 ? 109.950 107.181 109.819 1.00 34.37  ? 129 VAL A CA    1 
ATOM   985  C  C     . VAL A 1 141 ? 111.052 107.008 110.859 1.00 37.20  ? 129 VAL A C     1 
ATOM   986  O  O     . VAL A 1 141 ? 110.795 106.607 112.002 1.00 42.95  ? 129 VAL A O     1 
ATOM   987  C  CB    . VAL A 1 141 ? 109.928 106.008 108.821 1.00 30.30  ? 129 VAL A CB    1 
ATOM   988  C  CG1   . VAL A 1 141 ? 109.906 104.679 109.556 1.00 23.79  ? 129 VAL A CG1   1 
ATOM   989  C  CG2   . VAL A 1 141 ? 108.735 106.121 107.900 1.00 28.74  ? 129 VAL A CG2   1 
ATOM   990  N  N     . GLN A 1 142 ? 112.295 107.311 110.479 1.00 36.54  ? 130 GLN A N     1 
ATOM   991  C  CA    . GLN A 1 142 ? 113.425 107.139 111.386 1.00 35.94  ? 130 GLN A CA    1 
ATOM   992  C  C     . GLN A 1 142 ? 113.309 108.046 112.604 1.00 41.71  ? 130 GLN A C     1 
ATOM   993  O  O     . GLN A 1 142 ? 113.546 107.609 113.735 1.00 46.80  ? 130 GLN A O     1 
ATOM   994  C  CB    . GLN A 1 142 ? 114.731 107.413 110.642 1.00 35.81  ? 130 GLN A CB    1 
ATOM   995  C  CG    . GLN A 1 142 ? 115.971 107.393 111.518 1.00 40.82  ? 130 GLN A CG    1 
ATOM   996  C  CD    . GLN A 1 142 ? 116.434 105.989 111.845 1.00 44.81  ? 130 GLN A CD    1 
ATOM   997  O  OE1   . GLN A 1 142 ? 116.752 105.206 110.954 1.00 44.84  ? 130 GLN A OE1   1 
ATOM   998  N  NE2   . GLN A 1 142 ? 116.474 105.664 113.129 1.00 43.85  ? 130 GLN A NE2   1 
ATOM   999  N  N     . LEU A 1 143 ? 112.945 109.313 112.395 1.00 42.28  ? 131 LEU A N     1 
ATOM   1000 C  CA    . LEU A 1 143 ? 112.850 110.239 113.516 1.00 44.42  ? 131 LEU A CA    1 
ATOM   1001 C  C     . LEU A 1 143 ? 111.627 109.956 114.376 1.00 44.83  ? 131 LEU A C     1 
ATOM   1002 O  O     . LEU A 1 143 ? 111.652 110.214 115.583 1.00 52.18  ? 131 LEU A O     1 
ATOM   1003 C  CB    . LEU A 1 143 ? 112.837 111.679 113.007 1.00 44.48  ? 131 LEU A CB    1 
ATOM   1004 C  CG    . LEU A 1 143 ? 114.167 112.155 112.414 1.00 47.68  ? 131 LEU A CG    1 
ATOM   1005 C  CD1   . LEU A 1 143 ? 114.088 113.606 111.977 1.00 46.68  ? 131 LEU A CD1   1 
ATOM   1006 C  CD2   . LEU A 1 143 ? 115.300 111.957 113.406 1.00 48.08  ? 131 LEU A CD2   1 
ATOM   1007 N  N     . THR A 1 144 ? 110.551 109.434 113.782 1.00 43.29  ? 132 THR A N     1 
ATOM   1008 C  CA    . THR A 1 144 ? 109.416 108.990 114.583 1.00 42.75  ? 132 THR A CA    1 
ATOM   1009 C  C     . THR A 1 144 ? 109.807 107.825 115.477 1.00 45.13  ? 132 THR A C     1 
ATOM   1010 O  O     . THR A 1 144 ? 109.450 107.789 116.659 1.00 51.60  ? 132 THR A O     1 
ATOM   1011 C  CB    . THR A 1 144 ? 108.255 108.596 113.673 1.00 42.45  ? 132 THR A CB    1 
ATOM   1012 O  OG1   . THR A 1 144 ? 107.808 109.743 112.943 1.00 51.21  ? 132 THR A OG1   1 
ATOM   1013 C  CG2   . THR A 1 144 ? 107.103 108.041 114.488 1.00 39.92  ? 132 THR A CG2   1 
ATOM   1014 N  N     . VAL A 1 145 ? 110.550 106.865 114.928 1.00 46.62  ? 133 VAL A N     1 
ATOM   1015 C  CA    . VAL A 1 145 ? 110.995 105.724 115.720 1.00 45.07  ? 133 VAL A CA    1 
ATOM   1016 C  C     . VAL A 1 145 ? 111.954 106.169 116.819 1.00 47.90  ? 133 VAL A C     1 
ATOM   1017 O  O     . VAL A 1 145 ? 111.880 105.691 117.957 1.00 51.23  ? 133 VAL A O     1 
ATOM   1018 C  CB    . VAL A 1 145 ? 111.631 104.669 114.796 1.00 42.00  ? 133 VAL A CB    1 
ATOM   1019 C  CG1   . VAL A 1 145 ? 112.679 103.869 115.533 1.00 42.38  ? 133 VAL A CG1   1 
ATOM   1020 C  CG2   . VAL A 1 145 ? 110.562 103.755 114.230 1.00 36.93  ? 133 VAL A CG2   1 
ATOM   1021 N  N     . THR A 1 146 ? 112.856 107.099 116.506 1.00 48.84  ? 134 THR A N     1 
ATOM   1022 C  CA    . THR A 1 146 ? 113.942 107.422 117.423 1.00 50.18  ? 134 THR A CA    1 
ATOM   1023 C  C     . THR A 1 146 ? 113.506 108.393 118.517 1.00 55.18  ? 134 THR A C     1 
ATOM   1024 O  O     . THR A 1 146 ? 113.723 108.134 119.705 1.00 63.47  ? 134 THR A O     1 
ATOM   1025 C  CB    . THR A 1 146 ? 115.127 108.000 116.647 1.00 58.28  ? 134 THR A CB    1 
ATOM   1026 O  OG1   . THR A 1 146 ? 115.267 107.309 115.401 1.00 60.29  ? 134 THR A OG1   1 
ATOM   1027 C  CG2   . THR A 1 146 ? 116.407 107.844 117.443 1.00 55.87  ? 134 THR A CG2   1 
ATOM   1028 N  N     . MET A 1 147 ? 112.900 109.518 118.142 1.00 55.55  ? 135 MET A N     1 
ATOM   1029 C  CA    . MET A 1 147 ? 112.679 110.607 119.084 1.00 57.82  ? 135 MET A CA    1 
ATOM   1030 C  C     . MET A 1 147 ? 111.224 111.007 119.271 1.00 54.74  ? 135 MET A C     1 
ATOM   1031 O  O     . MET A 1 147 ? 110.866 111.455 120.361 1.00 61.88  ? 135 MET A O     1 
ATOM   1032 C  CB    . MET A 1 147 ? 113.467 111.854 118.652 1.00 66.34  ? 135 MET A CB    1 
ATOM   1033 C  CG    . MET A 1 147 ? 114.826 111.556 118.042 1.00 70.71  ? 135 MET A CG    1 
ATOM   1034 S  SD    . MET A 1 147 ? 116.067 112.784 118.490 1.00 94.47  ? 135 MET A SD    1 
ATOM   1035 C  CE    . MET A 1 147 ? 117.354 112.416 117.302 1.00 71.13  ? 135 MET A CE    1 
ATOM   1036 N  N     . LEU A 1 148 ? 110.379 110.876 118.249 1.00 50.75  ? 136 LEU A N     1 
ATOM   1037 C  CA    . LEU A 1 148 ? 109.025 111.410 118.358 1.00 52.69  ? 136 LEU A CA    1 
ATOM   1038 C  C     . LEU A 1 148 ? 108.171 110.589 119.318 1.00 54.67  ? 136 LEU A C     1 
ATOM   1039 O  O     . LEU A 1 148 ? 107.332 111.145 120.034 1.00 58.70  ? 136 LEU A O     1 
ATOM   1040 C  CB    . LEU A 1 148 ? 108.370 111.482 116.980 1.00 54.34  ? 136 LEU A CB    1 
ATOM   1041 C  CG    . LEU A 1 148 ? 109.017 112.449 115.984 1.00 55.41  ? 136 LEU A CG    1 
ATOM   1042 C  CD1   . LEU A 1 148 ? 108.196 112.544 114.710 1.00 51.87  ? 136 LEU A CD1   1 
ATOM   1043 C  CD2   . LEU A 1 148 ? 109.212 113.821 116.602 1.00 54.98  ? 136 LEU A CD2   1 
ATOM   1044 N  N     . ILE A 1 149 ? 108.362 109.268 119.347 1.00 51.31  ? 137 ILE A N     1 
ATOM   1045 C  CA    . ILE A 1 149 ? 107.558 108.432 120.233 1.00 50.66  ? 137 ILE A CA    1 
ATOM   1046 C  C     . ILE A 1 149 ? 107.981 108.566 121.689 1.00 51.04  ? 137 ILE A C     1 
ATOM   1047 O  O     . ILE A 1 149 ? 107.243 108.138 122.582 1.00 51.15  ? 137 ILE A O     1 
ATOM   1048 C  CB    . ILE A 1 149 ? 107.619 106.955 119.807 1.00 46.29  ? 137 ILE A CB    1 
ATOM   1049 C  CG1   . ILE A 1 149 ? 109.063 106.456 119.812 1.00 46.51  ? 137 ILE A CG1   1 
ATOM   1050 C  CG2   . ILE A 1 149 ? 106.975 106.766 118.446 1.00 52.44  ? 137 ILE A CG2   1 
ATOM   1051 C  CD1   . ILE A 1 149 ? 109.182 104.953 119.810 1.00 48.27  ? 137 ILE A CD1   1 
ATOM   1052 N  N     . THR A 1 150 ? 109.156 109.138 121.955 1.00 50.67  ? 138 THR A N     1 
ATOM   1053 C  CA    . THR A 1 150 ? 109.611 109.278 123.334 1.00 43.99  ? 138 THR A CA    1 
ATOM   1054 C  C     . THR A 1 150 ? 108.690 110.191 124.133 1.00 46.37  ? 138 THR A C     1 
ATOM   1055 O  O     . THR A 1 150 ? 108.381 109.905 125.295 1.00 47.13  ? 138 THR A O     1 
ATOM   1056 C  CB    . THR A 1 150 ? 111.045 109.806 123.363 1.00 48.41  ? 138 THR A CB    1 
ATOM   1057 O  OG1   . THR A 1 150 ? 111.895 108.921 122.624 1.00 55.50  ? 138 THR A OG1   1 
ATOM   1058 C  CG2   . THR A 1 150 ? 111.551 109.904 124.790 1.00 46.87  ? 138 THR A CG2   1 
ATOM   1059 N  N     . ALA A 1 151 ? 108.237 111.288 123.526 1.00 51.70  ? 139 ALA A N     1 
ATOM   1060 C  CA    . ALA A 1 151 ? 107.424 112.261 124.255 1.00 50.58  ? 139 ALA A CA    1 
ATOM   1061 C  C     . ALA A 1 151 ? 106.114 111.682 124.780 1.00 46.76  ? 139 ALA A C     1 
ATOM   1062 O  O     . ALA A 1 151 ? 105.814 111.884 125.969 1.00 50.45  ? 139 ALA A O     1 
ATOM   1063 C  CB    . ALA A 1 151 ? 107.187 113.491 123.373 1.00 49.29  ? 139 ALA A CB    1 
ATOM   1064 N  N     . PRO A 1 152 ? 105.293 110.979 123.988 1.00 44.99  ? 140 PRO A N     1 
ATOM   1065 C  CA    . PRO A 1 152 ? 104.096 110.360 124.584 1.00 47.31  ? 140 PRO A CA    1 
ATOM   1066 C  C     . PRO A 1 152 ? 104.427 109.297 125.614 1.00 47.18  ? 140 PRO A C     1 
ATOM   1067 O  O     . PRO A 1 152 ? 103.774 109.220 126.665 1.00 48.58  ? 140 PRO A O     1 
ATOM   1068 C  CB    . PRO A 1 152 ? 103.365 109.767 123.371 1.00 44.95  ? 140 PRO A CB    1 
ATOM   1069 C  CG    . PRO A 1 152 ? 103.914 110.488 122.198 1.00 48.29  ? 140 PRO A CG    1 
ATOM   1070 C  CD    . PRO A 1 152 ? 105.337 110.756 122.533 1.00 46.78  ? 140 PRO A CD    1 
ATOM   1071 N  N     . ILE A 1 153 ? 105.434 108.467 125.333 1.00 48.89  ? 141 ILE A N     1 
ATOM   1072 C  CA    . ILE A 1 153 ? 105.836 107.432 126.279 1.00 45.15  ? 141 ILE A CA    1 
ATOM   1073 C  C     . ILE A 1 153 ? 106.327 108.066 127.570 1.00 46.90  ? 141 ILE A C     1 
ATOM   1074 O  O     . ILE A 1 153 ? 105.963 107.636 128.669 1.00 50.56  ? 141 ILE A O     1 
ATOM   1075 C  CB    . ILE A 1 153 ? 106.907 106.518 125.657 1.00 43.52  ? 141 ILE A CB    1 
ATOM   1076 C  CG1   . ILE A 1 153 ? 106.318 105.711 124.501 1.00 45.08  ? 141 ILE A CG1   1 
ATOM   1077 C  CG2   . ILE A 1 153 ? 107.487 105.588 126.707 1.00 37.44  ? 141 ILE A CG2   1 
ATOM   1078 C  CD1   . ILE A 1 153 ? 107.361 105.085 123.606 1.00 41.63  ? 141 ILE A CD1   1 
ATOM   1079 N  N     . MET A 1 154 ? 107.158 109.105 127.456 1.00 43.32  ? 142 MET A N     1 
ATOM   1080 C  CA    . MET A 1 154 ? 107.658 109.773 128.652 1.00 41.34  ? 142 MET A CA    1 
ATOM   1081 C  C     . MET A 1 154 ? 106.529 110.425 129.435 1.00 43.19  ? 142 MET A C     1 
ATOM   1082 O  O     . MET A 1 154 ? 106.508 110.355 130.664 1.00 48.95  ? 142 MET A O     1 
ATOM   1083 C  CB    . MET A 1 154 ? 108.723 110.805 128.287 1.00 43.02  ? 142 MET A CB    1 
ATOM   1084 C  CG    . MET A 1 154 ? 110.124 110.230 128.241 1.00 40.87  ? 142 MET A CG    1 
ATOM   1085 S  SD    . MET A 1 154 ? 110.752 109.828 129.878 1.00 46.85  ? 142 MET A SD    1 
ATOM   1086 C  CE    . MET A 1 154 ? 112.511 109.796 129.563 1.00 39.15  ? 142 MET A CE    1 
ATOM   1087 N  N     . SER A 1 155 ? 105.572 111.048 128.745 1.00 43.14  ? 143 SER A N     1 
ATOM   1088 C  CA    . SER A 1 155 ? 104.461 111.691 129.442 1.00 41.45  ? 143 SER A CA    1 
ATOM   1089 C  C     . SER A 1 155 ? 103.620 110.675 130.208 1.00 45.90  ? 143 SER A C     1 
ATOM   1090 O  O     . SER A 1 155 ? 103.332 110.859 131.397 1.00 49.01  ? 143 SER A O     1 
ATOM   1091 C  CB    . SER A 1 155 ? 103.598 112.464 128.446 1.00 40.17  ? 143 SER A CB    1 
ATOM   1092 O  OG    . SER A 1 155 ? 104.362 113.444 127.769 1.00 44.08  ? 143 SER A OG    1 
ATOM   1093 N  N     . ILE A 1 156 ? 103.223 109.586 129.546 1.00 47.07  ? 144 ILE A N     1 
ATOM   1094 C  CA    . ILE A 1 156 ? 102.374 108.597 130.206 1.00 48.52  ? 144 ILE A CA    1 
ATOM   1095 C  C     . ILE A 1 156 ? 103.136 107.895 131.327 1.00 46.86  ? 144 ILE A C     1 
ATOM   1096 O  O     . ILE A 1 156 ? 102.603 107.689 132.428 1.00 49.36  ? 144 ILE A O     1 
ATOM   1097 C  CB    . ILE A 1 156 ? 101.812 107.599 129.175 1.00 51.75  ? 144 ILE A CB    1 
ATOM   1098 C  CG1   . ILE A 1 156 ? 100.451 108.069 128.659 1.00 49.92  ? 144 ILE A CG1   1 
ATOM   1099 C  CG2   . ILE A 1 156 ? 101.677 106.210 129.776 1.00 43.77  ? 144 ILE A CG2   1 
ATOM   1100 C  CD1   . ILE A 1 156 ? 100.500 109.346 127.854 1.00 44.01  ? 144 ILE A CD1   1 
ATOM   1101 N  N     . GLY A 1 157 ? 104.393 107.523 131.074 1.00 42.86  ? 145 GLY A N     1 
ATOM   1102 C  CA    . GLY A 1 157 ? 105.180 106.869 132.101 1.00 43.76  ? 145 GLY A CA    1 
ATOM   1103 C  C     . GLY A 1 157 ? 105.456 107.770 133.285 1.00 46.32  ? 145 GLY A C     1 
ATOM   1104 O  O     . GLY A 1 157 ? 105.485 107.310 134.425 1.00 51.50  ? 145 GLY A O     1 
ATOM   1105 N  N     . GLY A 1 158 ? 105.664 109.063 133.037 1.00 41.75  ? 146 GLY A N     1 
ATOM   1106 C  CA    . GLY A 1 158 ? 105.851 109.995 134.131 1.00 41.12  ? 146 GLY A CA    1 
ATOM   1107 C  C     . GLY A 1 158 ? 104.590 110.203 134.941 1.00 48.59  ? 146 GLY A C     1 
ATOM   1108 O  O     . GLY A 1 158 ? 104.648 110.337 136.163 1.00 54.20  ? 146 GLY A O     1 
ATOM   1109 N  N     . ILE A 1 159 ? 103.433 110.235 134.276 1.00 44.55  ? 147 ILE A N     1 
ATOM   1110 C  CA    . ILE A 1 159 ? 102.175 110.322 135.012 1.00 44.24  ? 147 ILE A CA    1 
ATOM   1111 C  C     . ILE A 1 159 ? 102.002 109.101 135.907 1.00 47.90  ? 147 ILE A C     1 
ATOM   1112 O  O     . ILE A 1 159 ? 101.630 109.218 137.083 1.00 53.65  ? 147 ILE A O     1 
ATOM   1113 C  CB    . ILE A 1 159 ? 100.993 110.493 134.040 1.00 43.77  ? 147 ILE A CB    1 
ATOM   1114 C  CG1   . ILE A 1 159 ? 100.889 111.948 133.582 1.00 45.39  ? 147 ILE A CG1   1 
ATOM   1115 C  CG2   . ILE A 1 159 ? 99.694  110.052 134.691 1.00 40.16  ? 147 ILE A CG2   1 
ATOM   1116 C  CD1   . ILE A 1 159 ? 99.942  112.159 132.428 1.00 45.69  ? 147 ILE A CD1   1 
ATOM   1117 N  N     . PHE A 1 160 ? 102.291 107.912 135.375 1.00 42.05  ? 148 PHE A N     1 
ATOM   1118 C  CA    . PHE A 1 160 ? 102.141 106.703 136.181 1.00 42.07  ? 148 PHE A CA    1 
ATOM   1119 C  C     . PHE A 1 160 ? 103.183 106.638 137.296 1.00 42.91  ? 148 PHE A C     1 
ATOM   1120 O  O     . PHE A 1 160 ? 102.885 106.174 138.402 1.00 48.97  ? 148 PHE A O     1 
ATOM   1121 C  CB    . PHE A 1 160 ? 102.209 105.469 135.285 1.00 49.08  ? 148 PHE A CB    1 
ATOM   1122 C  CG    . PHE A 1 160 ? 100.926 105.189 134.557 1.00 59.12  ? 148 PHE A CG    1 
ATOM   1123 C  CD1   . PHE A 1 160 ? 99.747  104.999 135.256 1.00 58.23  ? 148 PHE A CD1   1 
ATOM   1124 C  CD2   . PHE A 1 160 ? 100.895 105.129 133.175 1.00 57.43  ? 148 PHE A CD2   1 
ATOM   1125 C  CE1   . PHE A 1 160 ? 98.564  104.749 134.592 1.00 57.52  ? 148 PHE A CE1   1 
ATOM   1126 C  CE2   . PHE A 1 160 ? 99.714  104.878 132.506 1.00 53.49  ? 148 PHE A CE2   1 
ATOM   1127 C  CZ    . PHE A 1 160 ? 98.548  104.688 133.216 1.00 54.74  ? 148 PHE A CZ    1 
ATOM   1128 N  N     . MET A 1 161 ? 104.403 107.109 137.032 1.00 42.90  ? 149 MET A N     1 
ATOM   1129 C  CA    . MET A 1 161 ? 105.430 107.160 138.067 1.00 42.03  ? 149 MET A CA    1 
ATOM   1130 C  C     . MET A 1 161 ? 105.054 108.137 139.172 1.00 45.69  ? 149 MET A C     1 
ATOM   1131 O  O     . MET A 1 161 ? 105.324 107.882 140.349 1.00 48.70  ? 149 MET A O     1 
ATOM   1132 C  CB    . MET A 1 161 ? 106.776 107.544 137.454 1.00 41.03  ? 149 MET A CB    1 
ATOM   1133 C  CG    . MET A 1 161 ? 107.546 106.386 136.853 1.00 45.44  ? 149 MET A CG    1 
ATOM   1134 S  SD    . MET A 1 161 ? 108.177 105.243 138.093 1.00 53.37  ? 149 MET A SD    1 
ATOM   1135 C  CE    . MET A 1 161 ? 109.006 104.056 137.045 1.00 37.03  ? 149 MET A CE    1 
ATOM   1136 N  N     . ALA A 1 162 ? 104.455 109.272 138.810 1.00 43.29  ? 150 ALA A N     1 
ATOM   1137 C  CA    . ALA A 1 162 ? 103.974 110.216 139.810 1.00 43.81  ? 150 ALA A CA    1 
ATOM   1138 C  C     . ALA A 1 162 ? 102.843 109.616 140.633 1.00 48.19  ? 150 ALA A C     1 
ATOM   1139 O  O     . ALA A 1 162 ? 102.765 109.840 141.846 1.00 51.31  ? 150 ALA A O     1 
ATOM   1140 C  CB    . ALA A 1 162 ? 103.518 111.505 139.135 1.00 42.48  ? 150 ALA A CB    1 
ATOM   1141 N  N     . LEU A 1 163 ? 101.949 108.863 139.990 1.00 48.92  ? 151 LEU A N     1 
ATOM   1142 C  CA    . LEU A 1 163 ? 100.901 108.174 140.736 1.00 48.92  ? 151 LEU A CA    1 
ATOM   1143 C  C     . LEU A 1 163 ? 101.496 107.165 141.710 1.00 49.45  ? 151 LEU A C     1 
ATOM   1144 O  O     . LEU A 1 163 ? 101.025 107.032 142.846 1.00 50.69  ? 151 LEU A O     1 
ATOM   1145 C  CB    . LEU A 1 163 ? 99.937  107.481 139.775 1.00 45.03  ? 151 LEU A CB    1 
ATOM   1146 C  CG    . LEU A 1 163 ? 98.851  108.352 139.149 1.00 48.54  ? 151 LEU A CG    1 
ATOM   1147 C  CD1   . LEU A 1 163 ? 98.326  107.710 137.878 1.00 52.47  ? 151 LEU A CD1   1 
ATOM   1148 C  CD2   . LEU A 1 163 ? 97.727  108.584 140.138 1.00 51.20  ? 151 LEU A CD2   1 
ATOM   1149 N  N     . HIS A 1 164 ? 102.526 106.438 141.277 1.00 49.25  ? 152 HIS A N     1 
ATOM   1150 C  CA    . HIS A 1 164 ? 103.169 105.457 142.146 1.00 52.71  ? 152 HIS A CA    1 
ATOM   1151 C  C     . HIS A 1 164 ? 103.901 106.126 143.305 1.00 54.83  ? 152 HIS A C     1 
ATOM   1152 O  O     . HIS A 1 164 ? 103.865 105.631 144.437 1.00 56.91  ? 152 HIS A O     1 
ATOM   1153 C  CB    . HIS A 1 164 ? 104.124 104.591 141.326 1.00 51.47  ? 152 HIS A CB    1 
ATOM   1154 C  CG    . HIS A 1 164 ? 105.018 103.721 142.153 1.00 61.69  ? 152 HIS A CG    1 
ATOM   1155 N  ND1   . HIS A 1 164 ? 106.379 103.921 142.240 1.00 68.99  ? 152 HIS A ND1   1 
ATOM   1156 C  CD2   . HIS A 1 164 ? 104.747 102.642 142.924 1.00 61.83  ? 152 HIS A CD2   1 
ATOM   1157 C  CE1   . HIS A 1 164 ? 106.907 103.006 143.032 1.00 65.07  ? 152 HIS A CE1   1 
ATOM   1158 N  NE2   . HIS A 1 164 ? 105.938 102.217 143.460 1.00 65.30  ? 152 HIS A NE2   1 
ATOM   1159 N  N     . GLN A 1 165 ? 104.572 107.249 143.044 1.00 51.16  ? 153 GLN A N     1 
ATOM   1160 C  CA    . GLN A 1 165 ? 105.340 107.928 144.084 1.00 50.17  ? 153 GLN A CA    1 
ATOM   1161 C  C     . GLN A 1 165 ? 104.423 108.577 145.112 1.00 54.30  ? 153 GLN A C     1 
ATOM   1162 O  O     . GLN A 1 165 ? 104.462 108.240 146.300 1.00 58.55  ? 153 GLN A O     1 
ATOM   1163 C  CB    . GLN A 1 165 ? 106.264 108.971 143.453 1.00 46.38  ? 153 GLN A CB    1 
ATOM   1164 C  CG    . GLN A 1 165 ? 107.711 108.534 143.331 1.00 46.74  ? 153 GLN A CG    1 
ATOM   1165 C  CD    . GLN A 1 165 ? 108.423 108.517 144.665 1.00 49.44  ? 153 GLN A CD    1 
ATOM   1166 O  OE1   . GLN A 1 165 ? 108.241 109.411 145.488 1.00 52.47  ? 153 GLN A OE1   1 
ATOM   1167 N  NE2   . GLN A 1 165 ? 109.241 107.497 144.887 1.00 47.28  ? 153 GLN A NE2   1 
ATOM   1168 N  N     . ASP A 1 166 ? 103.591 109.519 144.672 1.00 54.85  ? 154 ASP A N     1 
ATOM   1169 C  CA    . ASP A 1 166 ? 102.656 110.196 145.568 1.00 58.20  ? 154 ASP A CA    1 
ATOM   1170 C  C     . ASP A 1 166 ? 101.393 110.499 144.768 1.00 57.03  ? 154 ASP A C     1 
ATOM   1171 O  O     . ASP A 1 166 ? 101.373 111.443 143.974 1.00 58.37  ? 154 ASP A O     1 
ATOM   1172 C  CB    . ASP A 1 166 ? 103.264 111.465 146.148 1.00 55.72  ? 154 ASP A CB    1 
ATOM   1173 C  CG    . ASP A 1 166 ? 102.452 112.023 147.298 1.00 66.08  ? 154 ASP A CG    1 
ATOM   1174 O  OD1   . ASP A 1 166 ? 101.747 111.239 147.967 1.00 65.93  ? 154 ASP A OD1   1 
ATOM   1175 O  OD2   . ASP A 1 166 ? 102.504 113.247 147.524 1.00 65.96  ? 154 ASP A OD2   1 
ATOM   1176 N  N     . ALA A 1 167 ? 100.350 109.697 144.984 1.00 55.40  ? 155 ALA A N     1 
ATOM   1177 C  CA    . ALA A 1 167 ? 99.092  109.904 144.278 1.00 55.98  ? 155 ALA A CA    1 
ATOM   1178 C  C     . ALA A 1 167 ? 98.431  111.223 144.646 1.00 57.05  ? 155 ALA A C     1 
ATOM   1179 O  O     . ALA A 1 167 ? 97.656  111.757 143.845 1.00 61.23  ? 155 ALA A O     1 
ATOM   1180 C  CB    . ALA A 1 167 ? 98.134  108.747 144.559 1.00 62.83  ? 155 ALA A CB    1 
ATOM   1181 N  N     . GLY A 1 168 ? 98.718  111.763 145.829 1.00 56.11  ? 156 GLY A N     1 
ATOM   1182 C  CA    . GLY A 1 168 ? 98.137  113.028 146.236 1.00 60.33  ? 156 GLY A CA    1 
ATOM   1183 C  C     . GLY A 1 168 ? 98.738  114.242 145.562 1.00 60.40  ? 156 GLY A C     1 
ATOM   1184 O  O     . GLY A 1 168 ? 98.184  115.338 145.695 1.00 63.08  ? 156 GLY A O     1 
ATOM   1185 N  N     . LEU A 1 169 ? 99.849  114.077 144.847 1.00 57.48  ? 157 LEU A N     1 
ATOM   1186 C  CA    . LEU A 1 169 ? 100.483 115.171 144.130 1.00 53.48  ? 157 LEU A CA    1 
ATOM   1187 C  C     . LEU A 1 169 ? 100.587 114.919 142.633 1.00 55.15  ? 157 LEU A C     1 
ATOM   1188 O  O     . LEU A 1 169 ? 101.091 115.784 141.909 1.00 55.47  ? 157 LEU A O     1 
ATOM   1189 C  CB    . LEU A 1 169 ? 101.880 115.442 144.704 1.00 54.26  ? 157 LEU A CB    1 
ATOM   1190 C  CG    . LEU A 1 169 ? 102.353 116.894 144.708 1.00 51.16  ? 157 LEU A CG    1 
ATOM   1191 C  CD1   . LEU A 1 169 ? 101.377 117.772 145.465 1.00 52.27  ? 157 LEU A CD1   1 
ATOM   1192 C  CD2   . LEU A 1 169 ? 103.732 116.983 145.322 1.00 43.92  ? 157 LEU A CD2   1 
ATOM   1193 N  N     . SER A 1 170 ? 100.125 113.764 142.148 1.00 54.58  ? 158 SER A N     1 
ATOM   1194 C  CA    . SER A 1 170 ? 100.155 113.477 140.719 1.00 51.86  ? 158 SER A CA    1 
ATOM   1195 C  C     . SER A 1 170 ? 99.184  114.347 139.933 1.00 56.33  ? 158 SER A C     1 
ATOM   1196 O  O     . SER A 1 170 ? 99.308  114.442 138.705 1.00 56.83  ? 158 SER A O     1 
ATOM   1197 C  CB    . SER A 1 170 ? 99.847  112.001 140.479 1.00 52.69  ? 158 SER A CB    1 
ATOM   1198 O  OG    . SER A 1 170 ? 98.491  111.716 140.765 1.00 56.62  ? 158 SER A OG    1 
ATOM   1199 N  N     . TRP A 1 171 ? 98.222  114.982 140.609 1.00 55.86  ? 159 TRP A N     1 
ATOM   1200 C  CA    . TRP A 1 171 ? 97.335  115.916 139.927 1.00 53.84  ? 159 TRP A CA    1 
ATOM   1201 C  C     . TRP A 1 171 ? 98.116  117.060 139.303 1.00 52.41  ? 159 TRP A C     1 
ATOM   1202 O  O     . TRP A 1 171 ? 97.686  117.631 138.295 1.00 53.60  ? 159 TRP A O     1 
ATOM   1203 C  CB    . TRP A 1 171 ? 96.286  116.458 140.897 1.00 51.86  ? 159 TRP A CB    1 
ATOM   1204 C  CG    . TRP A 1 171 ? 96.850  117.320 141.988 1.00 52.61  ? 159 TRP A CG    1 
ATOM   1205 C  CD1   . TRP A 1 171 ? 97.205  116.921 143.241 1.00 56.58  ? 159 TRP A CD1   1 
ATOM   1206 C  CD2   . TRP A 1 171 ? 97.119  118.726 141.925 1.00 54.49  ? 159 TRP A CD2   1 
ATOM   1207 N  NE1   . TRP A 1 171 ? 97.680  117.988 143.962 1.00 58.38  ? 159 TRP A NE1   1 
ATOM   1208 C  CE2   . TRP A 1 171 ? 97.638  119.108 143.176 1.00 56.77  ? 159 TRP A CE2   1 
ATOM   1209 C  CE3   . TRP A 1 171 ? 96.972  119.699 140.932 1.00 54.51  ? 159 TRP A CE3   1 
ATOM   1210 C  CZ2   . TRP A 1 171 ? 98.010  120.418 143.461 1.00 54.58  ? 159 TRP A CZ2   1 
ATOM   1211 C  CZ3   . TRP A 1 171 ? 97.344  120.999 141.217 1.00 53.23  ? 159 TRP A CZ3   1 
ATOM   1212 C  CH2   . TRP A 1 171 ? 97.855  121.347 142.469 1.00 51.53  ? 159 TRP A CH2   1 
ATOM   1213 N  N     . LEU A 1 172 ? 99.267  117.406 139.879 1.00 50.23  ? 160 LEU A N     1 
ATOM   1214 C  CA    . LEU A 1 172 ? 100.079 118.466 139.298 1.00 49.03  ? 160 LEU A CA    1 
ATOM   1215 C  C     . LEU A 1 172 ? 100.565 118.085 137.906 1.00 48.30  ? 160 LEU A C     1 
ATOM   1216 O  O     . LEU A 1 172 ? 100.508 118.900 136.981 1.00 55.57  ? 160 LEU A O     1 
ATOM   1217 C  CB    . LEU A 1 172 ? 101.255 118.789 140.212 1.00 45.67  ? 160 LEU A CB    1 
ATOM   1218 C  CG    . LEU A 1 172 ? 101.913 120.120 139.870 1.00 43.22  ? 160 LEU A CG    1 
ATOM   1219 C  CD1   . LEU A 1 172 ? 101.003 121.268 140.259 1.00 44.71  ? 160 LEU A CD1   1 
ATOM   1220 C  CD2   . LEU A 1 172 ? 103.237 120.231 140.565 1.00 42.39  ? 160 LEU A CD2   1 
ATOM   1221 N  N     . LEU A 1 173 ? 101.036 116.848 137.730 1.00 45.66  ? 161 LEU A N     1 
ATOM   1222 C  CA    . LEU A 1 173 ? 101.373 116.383 136.389 1.00 45.96  ? 161 LEU A CA    1 
ATOM   1223 C  C     . LEU A 1 173 ? 100.129 116.264 135.517 1.00 47.69  ? 161 LEU A C     1 
ATOM   1224 O  O     . LEU A 1 173 ? 100.154 116.638 134.338 1.00 46.87  ? 161 LEU A O     1 
ATOM   1225 C  CB    . LEU A 1 173 ? 102.106 115.044 136.453 1.00 42.28  ? 161 LEU A CB    1 
ATOM   1226 C  CG    . LEU A 1 173 ? 103.629 115.090 136.323 1.00 43.08  ? 161 LEU A CG    1 
ATOM   1227 C  CD1   . LEU A 1 173 ? 104.221 113.710 136.473 1.00 37.39  ? 161 LEU A CD1   1 
ATOM   1228 C  CD2   . LEU A 1 173 ? 104.030 115.688 134.988 1.00 44.86  ? 161 LEU A CD2   1 
ATOM   1229 N  N     . LEU A 1 174 ? 99.031  115.752 136.081 1.00 50.88  ? 162 LEU A N     1 
ATOM   1230 C  CA    . LEU A 1 174 ? 97.796  115.602 135.317 1.00 49.48  ? 162 LEU A CA    1 
ATOM   1231 C  C     . LEU A 1 174 ? 97.249  116.935 134.827 1.00 50.66  ? 162 LEU A C     1 
ATOM   1232 O  O     . LEU A 1 174 ? 96.403  116.950 133.928 1.00 54.80  ? 162 LEU A O     1 
ATOM   1233 C  CB    . LEU A 1 174 ? 96.733  114.895 136.157 1.00 49.91  ? 162 LEU A CB    1 
ATOM   1234 C  CG    . LEU A 1 174 ? 96.915  113.396 136.378 1.00 56.10  ? 162 LEU A CG    1 
ATOM   1235 C  CD1   . LEU A 1 174 ? 95.868  112.879 137.347 1.00 59.26  ? 162 LEU A CD1   1 
ATOM   1236 C  CD2   . LEU A 1 174 ? 96.843  112.654 135.056 1.00 50.78  ? 162 LEU A CD2   1 
ATOM   1237 N  N     . VAL A 1 175 ? 97.673  118.040 135.428 1.00 47.65  ? 163 VAL A N     1 
ATOM   1238 C  CA    . VAL A 1 175 ? 97.313  119.372 134.964 1.00 45.04  ? 163 VAL A CA    1 
ATOM   1239 C  C     . VAL A 1 175 ? 98.384  119.958 134.050 1.00 50.15  ? 163 VAL A C     1 
ATOM   1240 O  O     . VAL A 1 175 ? 98.067  120.616 133.059 1.00 55.45  ? 163 VAL A O     1 
ATOM   1241 C  CB    . VAL A 1 175 ? 97.045  120.297 136.171 1.00 45.32  ? 163 VAL A CB    1 
ATOM   1242 C  CG1   . VAL A 1 175 ? 96.957  121.748 135.733 1.00 45.23  ? 163 VAL A CG1   1 
ATOM   1243 C  CG2   . VAL A 1 175 ? 95.772  119.877 136.886 1.00 51.18  ? 163 VAL A CG2   1 
ATOM   1244 N  N     . SER A 1 176 ? 99.658  119.717 134.364 1.00 51.10  ? 164 SER A N     1 
ATOM   1245 C  CA    . SER A 1 176 ? 100.746 120.359 133.635 1.00 45.14  ? 164 SER A CA    1 
ATOM   1246 C  C     . SER A 1 176 ? 100.934 119.757 132.248 1.00 46.03  ? 164 SER A C     1 
ATOM   1247 O  O     . SER A 1 176 ? 101.218 120.484 131.289 1.00 47.39  ? 164 SER A O     1 
ATOM   1248 C  CB    . SER A 1 176 ? 102.036 120.257 134.446 1.00 44.14  ? 164 SER A CB    1 
ATOM   1249 O  OG    . SER A 1 176 ? 103.115 120.863 133.766 1.00 53.21  ? 164 SER A OG    1 
ATOM   1250 N  N     . VAL A 1 177 ? 100.810 118.434 132.118 1.00 45.87  ? 165 VAL A N     1 
ATOM   1251 C  CA    . VAL A 1 177 ? 100.980 117.802 130.807 1.00 43.49  ? 165 VAL A CA    1 
ATOM   1252 C  C     . VAL A 1 177 ? 99.928  118.263 129.802 1.00 46.93  ? 165 VAL A C     1 
ATOM   1253 O  O     . VAL A 1 177 ? 100.303 118.648 128.683 1.00 49.60  ? 165 VAL A O     1 
ATOM   1254 C  CB    . VAL A 1 177 ? 101.031 116.271 130.958 1.00 42.90  ? 165 VAL A CB    1 
ATOM   1255 C  CG1   . VAL A 1 177 ? 100.836 115.599 129.612 1.00 37.36  ? 165 VAL A CG1   1 
ATOM   1256 C  CG2   . VAL A 1 177 ? 102.352 115.846 131.572 1.00 44.43  ? 165 VAL A CG2   1 
ATOM   1257 N  N     . PRO A 1 178 ? 98.623  118.245 130.109 1.00 46.87  ? 166 PRO A N     1 
ATOM   1258 C  CA    . PRO A 1 178 ? 97.655  118.749 129.125 1.00 46.08  ? 166 PRO A CA    1 
ATOM   1259 C  C     . PRO A 1 178 ? 97.817  120.223 128.809 1.00 46.49  ? 166 PRO A C     1 
ATOM   1260 O  O     . PRO A 1 178 ? 97.513  120.628 127.684 1.00 53.89  ? 166 PRO A O     1 
ATOM   1261 C  CB    . PRO A 1 178 ? 96.299  118.458 129.780 1.00 45.96  ? 166 PRO A CB    1 
ATOM   1262 C  CG    . PRO A 1 178 ? 96.586  118.392 131.210 1.00 44.87  ? 166 PRO A CG    1 
ATOM   1263 C  CD    . PRO A 1 178 ? 97.937  117.757 131.316 1.00 44.92  ? 166 PRO A CD    1 
ATOM   1264 N  N     . VAL A 1 179 ? 98.273  121.043 129.755 1.00 44.39  ? 167 VAL A N     1 
ATOM   1265 C  CA    . VAL A 1 179 ? 98.449  122.467 129.476 1.00 43.50  ? 167 VAL A CA    1 
ATOM   1266 C  C     . VAL A 1 179 ? 99.534  122.674 128.427 1.00 44.74  ? 167 VAL A C     1 
ATOM   1267 O  O     . VAL A 1 179 ? 99.350  123.412 127.448 1.00 50.20  ? 167 VAL A O     1 
ATOM   1268 C  CB    . VAL A 1 179 ? 98.762  123.229 130.776 1.00 43.88  ? 167 VAL A CB    1 
ATOM   1269 C  CG1   . VAL A 1 179 ? 99.511  124.515 130.475 1.00 44.59  ? 167 VAL A CG1   1 
ATOM   1270 C  CG2   . VAL A 1 179 ? 97.481  123.522 131.534 1.00 44.30  ? 167 VAL A CG2   1 
ATOM   1271 N  N     . LEU A 1 180 ? 100.679 122.016 128.610 1.00 44.51  ? 168 LEU A N     1 
ATOM   1272 C  CA    . LEU A 1 180 ? 101.745 122.103 127.621 1.00 45.50  ? 168 LEU A CA    1 
ATOM   1273 C  C     . LEU A 1 180 ? 101.318 121.480 126.300 1.00 48.18  ? 168 LEU A C     1 
ATOM   1274 O  O     . LEU A 1 180 ? 101.662 121.989 125.228 1.00 50.00  ? 168 LEU A O     1 
ATOM   1275 C  CB    . LEU A 1 180 ? 103.010 121.432 128.149 1.00 46.91  ? 168 LEU A CB    1 
ATOM   1276 C  CG    . LEU A 1 180 ? 104.227 121.598 127.242 1.00 54.92  ? 168 LEU A CG    1 
ATOM   1277 C  CD1   . LEU A 1 180 ? 104.407 123.058 126.882 1.00 50.98  ? 168 LEU A CD1   1 
ATOM   1278 C  CD2   . LEU A 1 180 ? 105.468 121.060 127.910 1.00 53.80  ? 168 LEU A CD2   1 
ATOM   1279 N  N     . GLY A 1 181 ? 100.565 120.380 126.356 1.00 47.21  ? 169 GLY A N     1 
ATOM   1280 C  CA    . GLY A 1 181 ? 100.051 119.789 125.134 1.00 41.92  ? 169 GLY A CA    1 
ATOM   1281 C  C     . GLY A 1 181 ? 99.144  120.730 124.366 1.00 43.60  ? 169 GLY A C     1 
ATOM   1282 O  O     . GLY A 1 181 ? 99.230  120.826 123.144 1.00 50.50  ? 169 GLY A O     1 
ATOM   1283 N  N     . LEU A 1 182 ? 98.267  121.443 125.074 1.00 42.51  ? 170 LEU A N     1 
ATOM   1284 C  CA    . LEU A 1 182 ? 97.370  122.391 124.424 1.00 45.39  ? 170 LEU A CA    1 
ATOM   1285 C  C     . LEU A 1 182 ? 98.136  123.563 123.826 1.00 48.48  ? 170 LEU A C     1 
ATOM   1286 O  O     . LEU A 1 182 ? 97.849  123.989 122.699 1.00 57.34  ? 170 LEU A O     1 
ATOM   1287 C  CB    . LEU A 1 182 ? 96.326  122.891 125.421 1.00 48.72  ? 170 LEU A CB    1 
ATOM   1288 C  CG    . LEU A 1 182 ? 95.428  124.031 124.937 1.00 62.21  ? 170 LEU A CG    1 
ATOM   1289 C  CD1   . LEU A 1 182 ? 94.447  123.538 123.884 1.00 61.61  ? 170 LEU A CD1   1 
ATOM   1290 C  CD2   . LEU A 1 182 ? 94.697  124.680 126.101 1.00 61.81  ? 170 LEU A CD2   1 
ATOM   1291 N  N     . ALA A 1 183 ? 99.109  124.103 124.563 1.00 43.27  ? 171 ALA A N     1 
ATOM   1292 C  CA    . ALA A 1 183 ? 99.900  125.209 124.029 1.00 40.71  ? 171 ALA A CA    1 
ATOM   1293 C  C     . ALA A 1 183 ? 100.668 124.780 122.784 1.00 45.56  ? 171 ALA A C     1 
ATOM   1294 O  O     . ALA A 1 183 ? 100.685 125.489 121.766 1.00 49.74  ? 171 ALA A O     1 
ATOM   1295 C  CB    . ALA A 1 183 ? 100.854 125.733 125.101 1.00 35.60  ? 171 ALA A CB    1 
ATOM   1296 N  N     . ASN A 1 184 ? 101.294 123.604 122.842 1.00 42.05  ? 172 ASN A N     1 
ATOM   1297 C  CA    . ASN A 1 184 ? 102.035 123.104 121.693 1.00 37.20  ? 172 ASN A CA    1 
ATOM   1298 C  C     . ASN A 1 184 ? 101.106 122.810 120.525 1.00 42.88  ? 172 ASN A C     1 
ATOM   1299 O  O     . ASN A 1 184 ? 101.472 123.038 119.372 1.00 46.67  ? 172 ASN A O     1 
ATOM   1300 C  CB    . ASN A 1 184 ? 102.828 121.861 122.084 1.00 42.60  ? 172 ASN A CB    1 
ATOM   1301 C  CG    . ASN A 1 184 ? 104.151 122.200 122.736 1.00 53.43  ? 172 ASN A CG    1 
ATOM   1302 O  OD1   . ASN A 1 184 ? 104.826 123.147 122.340 1.00 58.11  ? 172 ASN A OD1   1 
ATOM   1303 N  ND2   . ASN A 1 184 ? 104.528 121.425 123.743 1.00 53.71  ? 172 ASN A ND2   1 
ATOM   1304 N  N     . TYR A 1 185 ? 99.902  122.302 120.800 1.00 46.35  ? 173 TYR A N     1 
ATOM   1305 C  CA    . TYR A 1 185 ? 98.944  122.048 119.730 1.00 43.20  ? 173 TYR A CA    1 
ATOM   1306 C  C     . TYR A 1 185 ? 98.521  123.342 119.054 1.00 45.43  ? 173 TYR A C     1 
ATOM   1307 O  O     . TYR A 1 185 ? 98.371  123.386 117.831 1.00 50.85  ? 173 TYR A O     1 
ATOM   1308 C  CB    . TYR A 1 185 ? 97.721  121.312 120.273 1.00 45.69  ? 173 TYR A CB    1 
ATOM   1309 C  CG    . TYR A 1 185 ? 96.508  121.422 119.375 1.00 54.21  ? 173 TYR A CG    1 
ATOM   1310 C  CD1   . TYR A 1 185 ? 96.423  120.692 118.198 1.00 51.12  ? 173 TYR A CD1   1 
ATOM   1311 C  CD2   . TYR A 1 185 ? 95.453  122.266 119.700 1.00 53.21  ? 173 TYR A CD2   1 
ATOM   1312 C  CE1   . TYR A 1 185 ? 95.321  120.792 117.373 1.00 50.67  ? 173 TYR A CE1   1 
ATOM   1313 C  CE2   . TYR A 1 185 ? 94.348  122.374 118.880 1.00 51.33  ? 173 TYR A CE2   1 
ATOM   1314 C  CZ    . TYR A 1 185 ? 94.287  121.635 117.719 1.00 56.31  ? 173 TYR A CZ    1 
ATOM   1315 O  OH    . TYR A 1 185 ? 93.187  121.739 116.900 1.00 67.09  ? 173 TYR A OH    1 
ATOM   1316 N  N     . TRP A 1 186 ? 98.306  124.401 119.834 1.00 41.81  ? 174 TRP A N     1 
ATOM   1317 C  CA    . TRP A 1 186 ? 97.973  125.693 119.244 1.00 45.62  ? 174 TRP A CA    1 
ATOM   1318 C  C     . TRP A 1 186 ? 99.108  126.200 118.359 1.00 49.61  ? 174 TRP A C     1 
ATOM   1319 O  O     . TRP A 1 186 ? 98.876  126.658 117.228 1.00 54.40  ? 174 TRP A O     1 
ATOM   1320 C  CB    . TRP A 1 186 ? 97.651  126.694 120.354 1.00 48.21  ? 174 TRP A CB    1 
ATOM   1321 C  CG    . TRP A 1 186 ? 97.329  128.073 119.878 1.00 56.04  ? 174 TRP A CG    1 
ATOM   1322 C  CD1   . TRP A 1 186 ? 96.197  128.474 119.236 1.00 54.86  ? 174 TRP A CD1   1 
ATOM   1323 C  CD2   . TRP A 1 186 ? 98.143  129.242 120.025 1.00 58.19  ? 174 TRP A CD2   1 
ATOM   1324 N  NE1   . TRP A 1 186 ? 96.257  129.818 118.966 1.00 56.57  ? 174 TRP A NE1   1 
ATOM   1325 C  CE2   . TRP A 1 186 ? 97.443  130.313 119.440 1.00 59.96  ? 174 TRP A CE2   1 
ATOM   1326 C  CE3   . TRP A 1 186 ? 99.397  129.485 120.592 1.00 51.55  ? 174 TRP A CE3   1 
ATOM   1327 C  CZ2   . TRP A 1 186 ? 97.955  131.608 119.404 1.00 56.99  ? 174 TRP A CZ2   1 
ATOM   1328 C  CZ3   . TRP A 1 186 ? 99.903  130.770 120.555 1.00 52.26  ? 174 TRP A CZ3   1 
ATOM   1329 C  CH2   . TRP A 1 186 ? 99.183  131.815 119.965 1.00 52.75  ? 174 TRP A CH2   1 
ATOM   1330 N  N     . ILE A 1 187 ? 100.348 126.095 118.845 1.00 47.43  ? 175 ILE A N     1 
ATOM   1331 C  CA    . ILE A 1 187 ? 101.492 126.531 118.046 1.00 44.29  ? 175 ILE A CA    1 
ATOM   1332 C  C     . ILE A 1 187 ? 101.603 125.707 116.766 1.00 42.97  ? 175 ILE A C     1 
ATOM   1333 O  O     . ILE A 1 187 ? 101.853 126.249 115.685 1.00 44.13  ? 175 ILE A O     1 
ATOM   1334 C  CB    . ILE A 1 187 ? 102.787 126.466 118.876 1.00 42.35  ? 175 ILE A CB    1 
ATOM   1335 C  CG1   . ILE A 1 187 ? 102.767 127.524 119.977 1.00 37.84  ? 175 ILE A CG1   1 
ATOM   1336 C  CG2   . ILE A 1 187 ? 104.001 126.658 117.990 1.00 40.60  ? 175 ILE A CG2   1 
ATOM   1337 C  CD1   . ILE A 1 187 ? 103.799 127.297 121.051 1.00 40.28  ? 175 ILE A CD1   1 
ATOM   1338 N  N     . ILE A 1 188 ? 101.415 124.390 116.865 1.00 41.37  ? 176 ILE A N     1 
ATOM   1339 C  CA    . ILE A 1 188 ? 101.529 123.519 115.699 1.00 41.94  ? 176 ILE A CA    1 
ATOM   1340 C  C     . ILE A 1 188 ? 100.416 123.807 114.701 1.00 43.10  ? 176 ILE A C     1 
ATOM   1341 O  O     . ILE A 1 188 ? 100.631 123.778 113.484 1.00 46.97  ? 176 ILE A O     1 
ATOM   1342 C  CB    . ILE A 1 188 ? 101.528 122.045 116.139 1.00 41.47  ? 176 ILE A CB    1 
ATOM   1343 C  CG1   . ILE A 1 188 ? 102.800 121.720 116.919 1.00 45.29  ? 176 ILE A CG1   1 
ATOM   1344 C  CG2   . ILE A 1 188 ? 101.401 121.123 114.941 1.00 41.90  ? 176 ILE A CG2   1 
ATOM   1345 C  CD1   . ILE A 1 188 ? 102.669 120.502 117.806 1.00 43.16  ? 176 ILE A CD1   1 
ATOM   1346 N  N     . ARG A 1 189 ? 99.208  124.078 115.195 1.00 42.85  ? 177 ARG A N     1 
ATOM   1347 C  CA    . ARG A 1 189 ? 98.105  124.423 114.309 1.00 44.81  ? 177 ARG A CA    1 
ATOM   1348 C  C     . ARG A 1 189 ? 98.403  125.705 113.548 1.00 48.86  ? 177 ARG A C     1 
ATOM   1349 O  O     . ARG A 1 189 ? 98.096  125.812 112.356 1.00 53.10  ? 177 ARG A O     1 
ATOM   1350 C  CB    . ARG A 1 189 ? 96.812  124.554 115.116 1.00 47.92  ? 177 ARG A CB    1 
ATOM   1351 C  CG    . ARG A 1 189 ? 95.933  125.729 114.722 1.00 58.73  ? 177 ARG A CG    1 
ATOM   1352 C  CD    . ARG A 1 189 ? 94.485  125.493 115.110 1.00 69.48  ? 177 ARG A CD    1 
ATOM   1353 N  NE    . ARG A 1 189 ? 93.720  126.734 115.150 1.00 80.75  ? 177 ARG A NE    1 
ATOM   1354 C  CZ    . ARG A 1 189 ? 92.909  127.147 114.185 1.00 83.18  ? 177 ARG A CZ    1 
ATOM   1355 N  NH1   . ARG A 1 189 ? 92.740  126.445 113.077 1.00 79.17  ? 177 ARG A NH1   1 
ATOM   1356 N  NH2   . ARG A 1 189 ? 92.252  128.293 114.336 1.00 81.00  ? 177 ARG A NH2   1 
ATOM   1357 N  N     . HIS A 1 190 ? 99.009  126.687 114.215 1.00 47.53  ? 178 HIS A N     1 
ATOM   1358 C  CA    . HIS A 1 190 ? 99.366  127.913 113.511 1.00 44.20  ? 178 HIS A CA    1 
ATOM   1359 C  C     . HIS A 1 190 ? 100.606 127.760 112.635 1.00 41.66  ? 178 HIS A C     1 
ATOM   1360 O  O     . HIS A 1 190 ? 100.799 128.561 111.716 1.00 47.44  ? 178 HIS A O     1 
ATOM   1361 C  CB    . HIS A 1 190 ? 99.574  129.048 114.512 1.00 46.66  ? 178 HIS A CB    1 
ATOM   1362 C  CG    . HIS A 1 190 ? 98.309  129.753 114.886 1.00 53.48  ? 178 HIS A CG    1 
ATOM   1363 N  ND1   . HIS A 1 190 ? 97.320  129.157 115.638 1.00 58.31  ? 178 HIS A ND1   1 
ATOM   1364 C  CD2   . HIS A 1 190 ? 97.866  131.001 114.605 1.00 54.16  ? 178 HIS A CD2   1 
ATOM   1365 C  CE1   . HIS A 1 190 ? 96.324  130.008 115.806 1.00 62.07  ? 178 HIS A CE1   1 
ATOM   1366 N  NE2   . HIS A 1 190 ? 96.631  131.135 115.190 1.00 63.54  ? 178 HIS A NE2   1 
ATOM   1367 N  N     . LEU A 1 191 ? 101.436 126.749 112.887 1.00 39.68  ? 179 LEU A N     1 
ATOM   1368 C  CA    . LEU A 1 191 ? 102.723 126.601 112.219 1.00 40.52  ? 179 LEU A CA    1 
ATOM   1369 C  C     . LEU A 1 191 ? 102.697 125.676 111.008 1.00 45.15  ? 179 LEU A C     1 
ATOM   1370 O  O     . LEU A 1 191 ? 103.480 125.881 110.076 1.00 42.78  ? 179 LEU A O     1 
ATOM   1371 C  CB    . LEU A 1 191 ? 103.761 126.088 113.224 1.00 40.34  ? 179 LEU A CB    1 
ATOM   1372 C  CG    . LEU A 1 191 ? 105.193 125.788 112.783 1.00 43.07  ? 179 LEU A CG    1 
ATOM   1373 C  CD1   . LEU A 1 191 ? 105.800 126.971 112.065 1.00 41.39  ? 179 LEU A CD1   1 
ATOM   1374 C  CD2   . LEU A 1 191 ? 106.036 125.403 113.984 1.00 37.65  ? 179 LEU A CD2   1 
ATOM   1375 N  N     . MET A 1 192 ? 101.832 124.661 110.997 1.00 46.73  ? 180 MET A N     1 
ATOM   1376 C  CA    . MET A 1 192 ? 101.833 123.699 109.895 1.00 41.90  ? 180 MET A CA    1 
ATOM   1377 C  C     . MET A 1 192 ? 101.519 124.326 108.539 1.00 43.79  ? 180 MET A C     1 
ATOM   1378 O  O     . MET A 1 192 ? 102.232 124.018 107.567 1.00 44.91  ? 180 MET A O     1 
ATOM   1379 C  CB    . MET A 1 192 ? 100.870 122.551 110.214 1.00 42.52  ? 180 MET A CB    1 
ATOM   1380 C  CG    . MET A 1 192 ? 101.388 121.547 111.231 1.00 48.55  ? 180 MET A CG    1 
ATOM   1381 S  SD    . MET A 1 192 ? 102.816 120.602 110.670 1.00 76.49  ? 180 MET A SD    1 
ATOM   1382 C  CE    . MET A 1 192 ? 104.146 121.444 111.526 1.00 57.56  ? 180 MET A CE    1 
ATOM   1383 N  N     . PRO A 1 193 ? 100.486 125.166 108.380 1.00 42.68  ? 181 PRO A N     1 
ATOM   1384 C  CA    . PRO A 1 193 ? 100.281 125.807 107.069 1.00 41.49  ? 181 PRO A CA    1 
ATOM   1385 C  C     . PRO A 1 193 ? 101.454 126.662 106.619 1.00 41.78  ? 181 PRO A C     1 
ATOM   1386 O  O     . PRO A 1 193 ? 101.747 126.715 105.416 1.00 46.47  ? 181 PRO A O     1 
ATOM   1387 C  CB    . PRO A 1 193 ? 99.011  126.646 107.281 1.00 36.23  ? 181 PRO A CB    1 
ATOM   1388 C  CG    . PRO A 1 193 ? 98.845  126.752 108.750 1.00 34.86  ? 181 PRO A CG    1 
ATOM   1389 C  CD    . PRO A 1 193 ? 99.389  125.489 109.309 1.00 37.02  ? 181 PRO A CD    1 
ATOM   1390 N  N     . VAL A 1 194 ? 102.141 127.329 107.548 1.00 38.26  ? 182 VAL A N     1 
ATOM   1391 C  CA    . VAL A 1 194 ? 103.334 128.087 107.186 1.00 37.24  ? 182 VAL A CA    1 
ATOM   1392 C  C     . VAL A 1 194 ? 104.404 127.156 106.638 1.00 41.97  ? 182 VAL A C     1 
ATOM   1393 O  O     . VAL A 1 194 ? 105.088 127.479 105.661 1.00 49.84  ? 182 VAL A O     1 
ATOM   1394 C  CB    . VAL A 1 194 ? 103.848 128.890 108.394 1.00 37.38  ? 182 VAL A CB    1 
ATOM   1395 C  CG1   . VAL A 1 194 ? 104.985 129.796 107.974 1.00 38.59  ? 182 VAL A CG1   1 
ATOM   1396 C  CG2   . VAL A 1 194 ? 102.724 129.699 109.005 1.00 44.02  ? 182 VAL A CG2   1 
ATOM   1397 N  N     . PHE A 1 195 ? 104.567 125.987 107.258 1.00 39.76  ? 183 PHE A N     1 
ATOM   1398 C  CA    . PHE A 1 195 ? 105.548 125.022 106.775 1.00 36.31  ? 183 PHE A CA    1 
ATOM   1399 C  C     . PHE A 1 195 ? 105.180 124.497 105.392 1.00 38.31  ? 183 PHE A C     1 
ATOM   1400 O  O     . PHE A 1 195 ? 106.057 124.304 104.543 1.00 43.44  ? 183 PHE A O     1 
ATOM   1401 C  CB    . PHE A 1 195 ? 105.679 123.874 107.772 1.00 38.99  ? 183 PHE A CB    1 
ATOM   1402 C  CG    . PHE A 1 195 ? 106.755 124.081 108.797 1.00 43.81  ? 183 PHE A CG    1 
ATOM   1403 C  CD1   . PHE A 1 195 ? 107.899 124.790 108.486 1.00 42.09  ? 183 PHE A CD1   1 
ATOM   1404 C  CD2   . PHE A 1 195 ? 106.619 123.568 110.073 1.00 50.74  ? 183 PHE A CD2   1 
ATOM   1405 C  CE1   . PHE A 1 195 ? 108.885 124.981 109.426 1.00 43.56  ? 183 PHE A CE1   1 
ATOM   1406 C  CE2   . PHE A 1 195 ? 107.604 123.757 111.017 1.00 52.65  ? 183 PHE A CE2   1 
ATOM   1407 C  CZ    . PHE A 1 195 ? 108.737 124.464 110.693 1.00 48.13  ? 183 PHE A CZ    1 
ATOM   1408 N  N     . THR A 1 196 ? 103.891 124.245 105.148 1.00 38.67  ? 184 THR A N     1 
ATOM   1409 C  CA    . THR A 1 196 ? 103.478 123.787 103.823 1.00 39.19  ? 184 THR A CA    1 
ATOM   1410 C  C     . THR A 1 196 ? 103.726 124.856 102.765 1.00 43.04  ? 184 THR A C     1 
ATOM   1411 O  O     . THR A 1 196 ? 104.164 124.548 101.649 1.00 47.66  ? 184 THR A O     1 
ATOM   1412 C  CB    . THR A 1 196 ? 102.007 123.372 103.830 1.00 42.47  ? 184 THR A CB    1 
ATOM   1413 O  OG1   . THR A 1 196 ? 101.180 124.521 104.047 1.00 45.75  ? 184 THR A OG1   1 
ATOM   1414 C  CG2   . THR A 1 196 ? 101.746 122.343 104.914 1.00 42.07  ? 184 THR A CG2   1 
ATOM   1415 N  N     . ARG A 1 197 ? 103.452 126.119 103.096 1.00 43.36  ? 185 ARG A N     1 
ATOM   1416 C  CA    . ARG A 1 197 ? 103.754 127.206 102.169 1.00 44.42  ? 185 ARG A CA    1 
ATOM   1417 C  C     . ARG A 1 197 ? 105.254 127.309 101.910 1.00 42.88  ? 185 ARG A C     1 
ATOM   1418 O  O     . ARG A 1 197 ? 105.685 127.553 100.776 1.00 47.43  ? 185 ARG A O     1 
ATOM   1419 C  CB    . ARG A 1 197 ? 103.209 128.520 102.720 1.00 44.47  ? 185 ARG A CB    1 
ATOM   1420 C  CG    . ARG A 1 197 ? 103.033 129.612 101.687 1.00 47.98  ? 185 ARG A CG    1 
ATOM   1421 C  CD    . ARG A 1 197 ? 103.170 130.992 102.314 1.00 55.61  ? 185 ARG A CD    1 
ATOM   1422 N  NE    . ARG A 1 197 ? 102.921 130.985 103.752 1.00 63.94  ? 185 ARG A NE    1 
ATOM   1423 C  CZ    . ARG A 1 197 ? 101.718 131.045 104.308 1.00 65.39  ? 185 ARG A CZ    1 
ATOM   1424 N  NH1   . ARG A 1 197 ? 100.619 131.096 103.574 1.00 66.36  ? 185 ARG A NH1   1 
ATOM   1425 N  NH2   . ARG A 1 197 ? 101.615 131.052 105.634 1.00 56.89  ? 185 ARG A NH2   1 
ATOM   1426 N  N     . MET A 1 198 ? 106.063 127.129 102.956 1.00 41.16  ? 186 MET A N     1 
ATOM   1427 C  CA    . MET A 1 198 ? 107.512 127.135 102.795 1.00 41.40  ? 186 MET A CA    1 
ATOM   1428 C  C     . MET A 1 198 ? 107.969 126.017 101.866 1.00 42.96  ? 186 MET A C     1 
ATOM   1429 O  O     . MET A 1 198 ? 108.853 126.219 101.029 1.00 44.06  ? 186 MET A O     1 
ATOM   1430 C  CB    . MET A 1 198 ? 108.182 127.005 104.162 1.00 42.50  ? 186 MET A CB    1 
ATOM   1431 C  CG    . MET A 1 198 ? 109.621 127.469 104.207 1.00 49.26  ? 186 MET A CG    1 
ATOM   1432 S  SD    . MET A 1 198 ? 110.397 127.118 105.793 1.00 66.73  ? 186 MET A SD    1 
ATOM   1433 C  CE    . MET A 1 198 ? 110.653 125.352 105.662 1.00 57.75  ? 186 MET A CE    1 
ATOM   1434 N  N     . GLN A 1 199 ? 107.384 124.827 102.006 1.00 43.12  ? 187 GLN A N     1 
ATOM   1435 C  CA    . GLN A 1 199 ? 107.738 123.722 101.120 1.00 42.56  ? 187 GLN A CA    1 
ATOM   1436 C  C     . GLN A 1 199 ? 107.325 124.010 99.681  1.00 42.52  ? 187 GLN A C     1 
ATOM   1437 O  O     . GLN A 1 199 ? 108.050 123.667 98.739  1.00 45.92  ? 187 GLN A O     1 
ATOM   1438 C  CB    . GLN A 1 199 ? 107.103 122.424 101.613 1.00 42.62  ? 187 GLN A CB    1 
ATOM   1439 C  CG    . GLN A 1 199 ? 107.613 121.967 102.966 1.00 47.65  ? 187 GLN A CG    1 
ATOM   1440 C  CD    . GLN A 1 199 ? 109.123 121.847 103.013 1.00 59.01  ? 187 GLN A CD    1 
ATOM   1441 O  OE1   . GLN A 1 199 ? 109.752 121.382 102.062 1.00 59.07  ? 187 GLN A OE1   1 
ATOM   1442 N  NE2   . GLN A 1 199 ? 109.715 122.267 104.124 1.00 56.49  ? 187 GLN A NE2   1 
ATOM   1443 N  N     . SER A 1 200 ? 106.159 124.632 99.492  1.00 41.66  ? 188 SER A N     1 
ATOM   1444 C  CA    . SER A 1 200 ? 105.737 125.013 98.147  1.00 40.72  ? 188 SER A CA    1 
ATOM   1445 C  C     . SER A 1 200 ? 106.721 125.992 97.518  1.00 41.59  ? 188 SER A C     1 
ATOM   1446 O  O     . SER A 1 200 ? 107.085 125.858 96.342  1.00 41.43  ? 188 SER A O     1 
ATOM   1447 C  CB    . SER A 1 200 ? 104.334 125.617 98.196  1.00 38.84  ? 188 SER A CB    1 
ATOM   1448 O  OG    . SER A 1 200 ? 103.896 125.999 96.906  1.00 46.47  ? 188 SER A OG    1 
ATOM   1449 N  N     . LEU A 1 201 ? 107.172 126.978 98.292  1.00 41.73  ? 189 LEU A N     1 
ATOM   1450 C  CA    . LEU A 1 201 ? 108.130 127.943 97.765  1.00 35.19  ? 189 LEU A CA    1 
ATOM   1451 C  C     . LEU A 1 201 ? 109.493 127.309 97.516  1.00 36.96  ? 189 LEU A C     1 
ATOM   1452 O  O     . LEU A 1 201 ? 110.203 127.713 96.587  1.00 41.87  ? 189 LEU A O     1 
ATOM   1453 C  CB    . LEU A 1 201 ? 108.251 129.125 98.718  1.00 37.60  ? 189 LEU A CB    1 
ATOM   1454 C  CG    . LEU A 1 201 ? 106.943 129.883 98.923  1.00 36.07  ? 189 LEU A CG    1 
ATOM   1455 C  CD1   . LEU A 1 201 ? 107.109 130.893 100.021 1.00 36.55  ? 189 LEU A CD1   1 
ATOM   1456 C  CD2   . LEU A 1 201 ? 106.496 130.554 97.642  1.00 33.75  ? 189 LEU A CD2   1 
ATOM   1457 N  N     . ILE A 1 202 ? 109.877 126.323 98.329  1.00 40.19  ? 190 ILE A N     1 
ATOM   1458 C  CA    . ILE A 1 202 ? 111.108 125.580 98.076  1.00 43.83  ? 190 ILE A CA    1 
ATOM   1459 C  C     . ILE A 1 202 ? 111.010 124.830 96.754  1.00 40.66  ? 190 ILE A C     1 
ATOM   1460 O  O     . ILE A 1 202 ? 111.955 124.816 95.957  1.00 41.01  ? 190 ILE A O     1 
ATOM   1461 C  CB    . ILE A 1 202 ? 111.410 124.628 99.249  1.00 46.27  ? 190 ILE A CB    1 
ATOM   1462 C  CG1   . ILE A 1 202 ? 111.940 125.410 100.449 1.00 44.40  ? 190 ILE A CG1   1 
ATOM   1463 C  CG2   . ILE A 1 202 ? 112.414 123.565 98.838  1.00 43.25  ? 190 ILE A CG2   1 
ATOM   1464 C  CD1   . ILE A 1 202 ? 111.923 124.632 101.742 1.00 45.57  ? 190 ILE A CD1   1 
ATOM   1465 N  N     . ASP A 1 203 ? 109.863 124.200 96.499  1.00 42.48  ? 191 ASP A N     1 
ATOM   1466 C  CA    . ASP A 1 203 ? 109.658 123.535 95.216  1.00 44.32  ? 191 ASP A CA    1 
ATOM   1467 C  C     . ASP A 1 203 ? 109.735 124.528 94.062  1.00 44.90  ? 191 ASP A C     1 
ATOM   1468 O  O     . ASP A 1 203 ? 110.310 124.226 93.011  1.00 46.58  ? 191 ASP A O     1 
ATOM   1469 C  CB    . ASP A 1 203 ? 108.313 122.809 95.208  1.00 50.77  ? 191 ASP A CB    1 
ATOM   1470 C  CG    . ASP A 1 203 ? 108.208 121.769 96.303  1.00 60.33  ? 191 ASP A CG    1 
ATOM   1471 O  OD1   . ASP A 1 203 ? 109.260 121.267 96.749  1.00 60.06  ? 191 ASP A OD1   1 
ATOM   1472 O  OD2   . ASP A 1 203 ? 107.073 121.457 96.721  1.00 59.08  ? 191 ASP A OD2   1 
ATOM   1473 N  N     . GLY A 1 204 ? 109.159 125.718 94.240  1.00 44.80  ? 192 GLY A N     1 
ATOM   1474 C  CA    . GLY A 1 204 ? 109.226 126.723 93.188  1.00 42.88  ? 192 GLY A CA    1 
ATOM   1475 C  C     . GLY A 1 204 ? 110.644 127.180 92.893  1.00 39.89  ? 192 GLY A C     1 
ATOM   1476 O  O     . GLY A 1 204 ? 111.048 127.297 91.731  1.00 43.59  ? 192 GLY A O     1 
ATOM   1477 N  N     . ILE A 1 205 ? 111.423 127.445 93.944  1.00 38.42  ? 193 ILE A N     1 
ATOM   1478 C  CA    . ILE A 1 205 ? 112.801 127.886 93.745  1.00 36.33  ? 193 ILE A CA    1 
ATOM   1479 C  C     . ILE A 1 205 ? 113.637 126.766 93.132  1.00 39.92  ? 193 ILE A C     1 
ATOM   1480 O  O     . ILE A 1 205 ? 114.525 127.016 92.305  1.00 42.37  ? 193 ILE A O     1 
ATOM   1481 C  CB    . ILE A 1 205 ? 113.398 128.411 95.067  1.00 35.53  ? 193 ILE A CB    1 
ATOM   1482 C  CG1   . ILE A 1 205 ? 114.548 129.374 94.790  1.00 36.07  ? 193 ILE A CG1   1 
ATOM   1483 C  CG2   . ILE A 1 205 ? 113.883 127.286 95.965  1.00 38.84  ? 193 ILE A CG2   1 
ATOM   1484 C  CD1   . ILE A 1 205 ? 114.918 130.224 95.977  1.00 40.11  ? 193 ILE A CD1   1 
ATOM   1485 N  N     . ASN A 1 206 ? 113.354 125.514 93.503  1.00 37.50  ? 194 ASN A N     1 
ATOM   1486 C  CA    . ASN A 1 206 ? 114.061 124.391 92.900  1.00 34.95  ? 194 ASN A CA    1 
ATOM   1487 C  C     . ASN A 1 206 ? 113.716 124.253 91.426  1.00 37.65  ? 194 ASN A C     1 
ATOM   1488 O  O     . ASN A 1 206 ? 114.582 123.921 90.611  1.00 41.81  ? 194 ASN A O     1 
ATOM   1489 C  CB    . ASN A 1 206 ? 113.740 123.100 93.652  1.00 35.48  ? 194 ASN A CB    1 
ATOM   1490 C  CG    . ASN A 1 206 ? 114.453 123.010 94.983  1.00 40.98  ? 194 ASN A CG    1 
ATOM   1491 O  OD1   . ASN A 1 206 ? 115.273 123.861 95.321  1.00 36.45  ? 194 ASN A OD1   1 
ATOM   1492 N  ND2   . ASN A 1 206 ? 114.147 121.970 95.746  1.00 40.63  ? 194 ASN A ND2   1 
ATOM   1493 N  N     . ARG A 1 207 ? 112.453 124.491 91.066  1.00 38.98  ? 195 ARG A N     1 
ATOM   1494 C  CA    . ARG A 1 207 ? 112.069 124.465 89.659  1.00 37.49  ? 195 ARG A CA    1 
ATOM   1495 C  C     . ARG A 1 207 ? 112.780 125.560 88.878  1.00 37.71  ? 195 ARG A C     1 
ATOM   1496 O  O     . ARG A 1 207 ? 113.225 125.338 87.745  1.00 42.67  ? 195 ARG A O     1 
ATOM   1497 C  CB    . ARG A 1 207 ? 110.553 124.605 89.526  1.00 43.77  ? 195 ARG A CB    1 
ATOM   1498 C  CG    . ARG A 1 207 ? 109.812 123.280 89.524  1.00 52.62  ? 195 ARG A CG    1 
ATOM   1499 C  CD    . ARG A 1 207 ? 108.350 123.457 89.152  1.00 62.22  ? 195 ARG A CD    1 
ATOM   1500 N  NE    . ARG A 1 207 ? 107.755 124.620 89.800  1.00 66.11  ? 195 ARG A NE    1 
ATOM   1501 C  CZ    . ARG A 1 207 ? 106.992 124.563 90.883  1.00 63.99  ? 195 ARG A CZ    1 
ATOM   1502 N  NH1   . ARG A 1 207 ? 106.717 123.413 91.476  1.00 64.80  ? 195 ARG A NH1   1 
ATOM   1503 N  NH2   . ARG A 1 207 ? 106.492 125.689 91.384  1.00 56.91  ? 195 ARG A NH2   1 
ATOM   1504 N  N     . VAL A 1 208 ? 112.898 126.749 89.471  1.00 38.02  ? 196 VAL A N     1 
ATOM   1505 C  CA    . VAL A 1 208 ? 113.620 127.840 88.815  1.00 37.25  ? 196 VAL A CA    1 
ATOM   1506 C  C     . VAL A 1 208 ? 115.076 127.449 88.582  1.00 37.23  ? 196 VAL A C     1 
ATOM   1507 O  O     . VAL A 1 208 ? 115.629 127.653 87.493  1.00 38.81  ? 196 VAL A O     1 
ATOM   1508 C  CB    . VAL A 1 208 ? 113.506 129.132 89.644  1.00 43.32  ? 196 VAL A CB    1 
ATOM   1509 C  CG1   . VAL A 1 208 ? 114.464 130.189 89.126  1.00 40.27  ? 196 VAL A CG1   1 
ATOM   1510 C  CG2   . VAL A 1 208 ? 112.081 129.649 89.622  1.00 45.55  ? 196 VAL A CG2   1 
ATOM   1511 N  N     . LEU A 1 209 ? 115.718 126.871 89.601  1.00 39.75  ? 197 LEU A N     1 
ATOM   1512 C  CA    . LEU A 1 209 ? 117.116 126.467 89.462  1.00 38.51  ? 197 LEU A CA    1 
ATOM   1513 C  C     . LEU A 1 209 ? 117.283 125.364 88.423  1.00 39.07  ? 197 LEU A C     1 
ATOM   1514 O  O     . LEU A 1 209 ? 118.252 125.368 87.655  1.00 38.29  ? 197 LEU A O     1 
ATOM   1515 C  CB    . LEU A 1 209 ? 117.673 126.017 90.810  1.00 36.57  ? 197 LEU A CB    1 
ATOM   1516 C  CG    . LEU A 1 209 ? 118.127 127.133 91.746  1.00 36.10  ? 197 LEU A CG    1 
ATOM   1517 C  CD1   . LEU A 1 209 ? 118.231 126.621 93.170  1.00 36.88  ? 197 LEU A CD1   1 
ATOM   1518 C  CD2   . LEU A 1 209 ? 119.449 127.703 91.277  1.00 36.75  ? 197 LEU A CD2   1 
ATOM   1519 N  N     . ARG A 1 210 ? 116.363 124.397 88.400  1.00 37.31  ? 198 ARG A N     1 
ATOM   1520 C  CA    . ARG A 1 210 ? 116.434 123.331 87.408  1.00 36.12  ? 198 ARG A CA    1 
ATOM   1521 C  C     . ARG A 1 210 ? 116.287 123.880 85.997  1.00 41.12  ? 198 ARG A C     1 
ATOM   1522 O  O     . ARG A 1 210 ? 117.006 123.463 85.082  1.00 43.90  ? 198 ARG A O     1 
ATOM   1523 C  CB    . ARG A 1 210 ? 115.360 122.281 87.686  1.00 39.76  ? 198 ARG A CB    1 
ATOM   1524 C  CG    . ARG A 1 210 ? 115.360 121.129 86.702  1.00 45.73  ? 198 ARG A CG    1 
ATOM   1525 C  CD    . ARG A 1 210 ? 113.967 120.566 86.511  1.00 49.87  ? 198 ARG A CD    1 
ATOM   1526 N  NE    . ARG A 1 210 ? 113.465 119.927 87.721  1.00 62.87  ? 198 ARG A NE    1 
ATOM   1527 C  CZ    . ARG A 1 210 ? 112.197 119.598 87.923  1.00 62.84  ? 198 ARG A CZ    1 
ATOM   1528 N  NH1   . ARG A 1 210 ? 111.266 119.843 87.016  1.00 54.54  ? 198 ARG A NH1   1 
ATOM   1529 N  NH2   . ARG A 1 210 ? 111.854 119.007 89.063  1.00 61.48  ? 198 ARG A NH2   1 
ATOM   1530 N  N     . ASP A 1 211 ? 115.355 124.815 85.801  1.00 45.52  ? 199 ASP A N     1 
ATOM   1531 C  CA    . ASP A 1 211 ? 115.200 125.438 84.492  1.00 42.55  ? 199 ASP A CA    1 
ATOM   1532 C  C     . ASP A 1 211 ? 116.460 126.191 84.091  1.00 44.18  ? 199 ASP A C     1 
ATOM   1533 O  O     . ASP A 1 211 ? 116.878 126.143 82.929  1.00 42.08  ? 199 ASP A O     1 
ATOM   1534 C  CB    . ASP A 1 211 ? 113.994 126.376 84.500  1.00 48.74  ? 199 ASP A CB    1 
ATOM   1535 C  CG    . ASP A 1 211 ? 113.439 126.621 83.113  1.00 67.71  ? 199 ASP A CG    1 
ATOM   1536 O  OD1   . ASP A 1 211 ? 113.165 127.794 82.782  1.00 73.62  ? 199 ASP A OD1   1 
ATOM   1537 O  OD2   . ASP A 1 211 ? 113.274 125.643 82.355  1.00 69.74  ? 199 ASP A OD2   1 
ATOM   1538 N  N     . GLN A 1 212 ? 117.076 126.897 85.041  1.00 47.82  ? 200 GLN A N     1 
ATOM   1539 C  CA    . GLN A 1 212 ? 118.294 127.637 84.730  1.00 38.70  ? 200 GLN A CA    1 
ATOM   1540 C  C     . GLN A 1 212 ? 119.440 126.704 84.361  1.00 40.16  ? 200 GLN A C     1 
ATOM   1541 O  O     . GLN A 1 212 ? 120.202 126.987 83.430  1.00 41.11  ? 200 GLN A O     1 
ATOM   1542 C  CB    . GLN A 1 212 ? 118.684 128.526 85.908  1.00 37.83  ? 200 GLN A CB    1 
ATOM   1543 C  CG    . GLN A 1 212 ? 117.900 129.818 85.970  1.00 43.59  ? 200 GLN A CG    1 
ATOM   1544 C  CD    . GLN A 1 212 ? 118.111 130.570 87.262  1.00 50.81  ? 200 GLN A CD    1 
ATOM   1545 O  OE1   . GLN A 1 212 ? 119.061 130.312 87.998  1.00 55.98  ? 200 GLN A OE1   1 
ATOM   1546 N  NE2   . GLN A 1 212 ? 117.215 131.505 87.552  1.00 51.84  ? 200 GLN A NE2   1 
ATOM   1547 N  N     . LEU A 1 213 ? 119.584 125.591 85.080  1.00 44.63  ? 201 LEU A N     1 
ATOM   1548 C  CA    . LEU A 1 213 ? 120.702 124.689 84.823  1.00 40.29  ? 201 LEU A CA    1 
ATOM   1549 C  C     . LEU A 1 213 ? 120.504 123.905 83.531  1.00 40.12  ? 201 LEU A C     1 
ATOM   1550 O  O     . LEU A 1 213 ? 121.466 123.664 82.794  1.00 41.84  ? 201 LEU A O     1 
ATOM   1551 C  CB    . LEU A 1 213 ? 120.889 123.739 86.004  1.00 34.70  ? 201 LEU A CB    1 
ATOM   1552 C  CG    . LEU A 1 213 ? 121.580 124.329 87.232  1.00 35.02  ? 201 LEU A CG    1 
ATOM   1553 C  CD1   . LEU A 1 213 ? 121.455 123.390 88.417  1.00 38.54  ? 201 LEU A CD1   1 
ATOM   1554 C  CD2   . LEU A 1 213 ? 123.032 124.618 86.929  1.00 31.82  ? 201 LEU A CD2   1 
ATOM   1555 N  N     . SER A 1 214 ? 119.269 123.488 83.247  1.00 42.66  ? 202 SER A N     1 
ATOM   1556 C  CA    . SER A 1 214 ? 119.009 122.697 82.048  1.00 43.75  ? 202 SER A CA    1 
ATOM   1557 C  C     . SER A 1 214 ? 119.261 123.502 80.778  1.00 48.32  ? 202 SER A C     1 
ATOM   1558 O  O     . SER A 1 214 ? 119.808 122.976 79.802  1.00 47.95  ? 202 SER A O     1 
ATOM   1559 C  CB    . SER A 1 214 ? 117.577 122.169 82.073  1.00 49.06  ? 202 SER A CB    1 
ATOM   1560 O  OG    . SER A 1 214 ? 117.294 121.415 80.910  1.00 59.41  ? 202 SER A OG    1 
ATOM   1561 N  N     . GLY A 1 215 ? 118.865 124.771 80.766  1.00 48.05  ? 203 GLY A N     1 
ATOM   1562 C  CA    . GLY A 1 215 ? 119.034 125.605 79.594  1.00 44.34  ? 203 GLY A CA    1 
ATOM   1563 C  C     . GLY A 1 215 ? 120.094 126.673 79.759  1.00 41.31  ? 203 GLY A C     1 
ATOM   1564 O  O     . GLY A 1 215 ? 119.888 127.822 79.357  1.00 40.61  ? 203 GLY A O     1 
ATOM   1565 N  N     . ILE A 1 216 ? 121.231 126.307 80.354  1.00 39.97  ? 204 ILE A N     1 
ATOM   1566 C  CA    . ILE A 1 216 ? 122.280 127.285 80.632  1.00 36.09  ? 204 ILE A CA    1 
ATOM   1567 C  C     . ILE A 1 216 ? 122.866 127.834 79.335  1.00 38.65  ? 204 ILE A C     1 
ATOM   1568 O  O     . ILE A 1 216 ? 123.213 129.018 79.248  1.00 41.94  ? 204 ILE A O     1 
ATOM   1569 C  CB    . ILE A 1 216 ? 123.360 126.664 81.541  1.00 37.57  ? 204 ILE A CB    1 
ATOM   1570 C  CG1   . ILE A 1 216 ? 124.366 127.724 81.990  1.00 39.90  ? 204 ILE A CG1   1 
ATOM   1571 C  CG2   . ILE A 1 216 ? 124.060 125.502 80.857  1.00 40.14  ? 204 ILE A CG2   1 
ATOM   1572 C  CD1   . ILE A 1 216 ? 123.752 128.834 82.814  1.00 43.18  ? 204 ILE A CD1   1 
ATOM   1573 N  N     . ARG A 1 217 ? 122.982 126.991 78.307  1.00 39.30  ? 205 ARG A N     1 
ATOM   1574 C  CA    . ARG A 1 217 ? 123.508 127.456 77.028  1.00 37.62  ? 205 ARG A CA    1 
ATOM   1575 C  C     . ARG A 1 217 ? 122.555 128.440 76.362  1.00 39.96  ? 205 ARG A C     1 
ATOM   1576 O  O     . ARG A 1 217 ? 122.992 129.442 75.789  1.00 39.68  ? 205 ARG A O     1 
ATOM   1577 C  CB    . ARG A 1 217 ? 123.785 126.266 76.112  1.00 39.55  ? 205 ARG A CB    1 
ATOM   1578 C  CG    . ARG A 1 217 ? 125.126 125.606 76.362  1.00 40.78  ? 205 ARG A CG    1 
ATOM   1579 C  CD    . ARG A 1 217 ? 125.323 124.388 75.484  1.00 44.41  ? 205 ARG A CD    1 
ATOM   1580 N  NE    . ARG A 1 217 ? 126.719 123.970 75.438  1.00 55.45  ? 205 ARG A NE    1 
ATOM   1581 C  CZ    . ARG A 1 217 ? 127.304 123.212 76.355  1.00 54.95  ? 205 ARG A CZ    1 
ATOM   1582 N  NH1   . ARG A 1 217 ? 126.644 122.770 77.412  1.00 57.92  ? 205 ARG A NH1   1 
ATOM   1583 N  NH2   . ARG A 1 217 ? 128.585 122.889 76.207  1.00 47.61  ? 205 ARG A NH2   1 
ATOM   1584 N  N     . VAL A 1 218 ? 121.251 128.170 76.424  1.00 44.25  ? 206 VAL A N     1 
ATOM   1585 C  CA    . VAL A 1 218 ? 120.272 129.101 75.871  1.00 42.94  ? 206 VAL A CA    1 
ATOM   1586 C  C     . VAL A 1 218 ? 120.219 130.376 76.702  1.00 42.81  ? 206 VAL A C     1 
ATOM   1587 O  O     . VAL A 1 218 ? 119.994 131.470 76.171  1.00 50.02  ? 206 VAL A O     1 
ATOM   1588 C  CB    . VAL A 1 218 ? 118.893 128.428 75.769  1.00 45.88  ? 206 VAL A CB    1 
ATOM   1589 C  CG1   . VAL A 1 218 ? 117.903 129.349 75.079  1.00 47.00  ? 206 VAL A CG1   1 
ATOM   1590 C  CG2   . VAL A 1 218 ? 119.006 127.117 75.020  1.00 48.19  ? 206 VAL A CG2   1 
ATOM   1591 N  N     . ILE A 1 219 ? 120.408 130.258 78.017  1.00 39.38  ? 207 ILE A N     1 
ATOM   1592 C  CA    . ILE A 1 219 ? 120.438 131.439 78.876  1.00 39.37  ? 207 ILE A CA    1 
ATOM   1593 C  C     . ILE A 1 219 ? 121.603 132.342 78.493  1.00 42.45  ? 207 ILE A C     1 
ATOM   1594 O  O     . ILE A 1 219 ? 121.448 133.559 78.347  1.00 49.14  ? 207 ILE A O     1 
ATOM   1595 C  CB    . ILE A 1 219 ? 120.508 131.026 80.356  1.00 35.24  ? 207 ILE A CB    1 
ATOM   1596 C  CG1   . ILE A 1 219 ? 119.123 130.644 80.863  1.00 38.62  ? 207 ILE A CG1   1 
ATOM   1597 C  CG2   . ILE A 1 219 ? 121.087 132.143 81.205  1.00 35.80  ? 207 ILE A CG2   1 
ATOM   1598 C  CD1   . ILE A 1 219 ? 119.148 129.855 82.127  1.00 37.28  ? 207 ILE A CD1   1 
ATOM   1599 N  N     . ARG A 1 220 ? 122.788 131.756 78.315  1.00 40.26  ? 208 ARG A N     1 
ATOM   1600 C  CA    . ARG A 1 220 ? 123.946 132.559 77.941  1.00 39.41  ? 208 ARG A CA    1 
ATOM   1601 C  C     . ARG A 1 220 ? 123.843 133.065 76.509  1.00 42.11  ? 208 ARG A C     1 
ATOM   1602 O  O     . ARG A 1 220 ? 124.354 134.145 76.201  1.00 49.40  ? 208 ARG A O     1 
ATOM   1603 C  CB    . ARG A 1 220 ? 125.229 131.754 78.139  1.00 42.12  ? 208 ARG A CB    1 
ATOM   1604 C  CG    . ARG A 1 220 ? 125.542 131.467 79.595  1.00 38.94  ? 208 ARG A CG    1 
ATOM   1605 C  CD    . ARG A 1 220 ? 126.752 130.569 79.749  1.00 36.30  ? 208 ARG A CD    1 
ATOM   1606 N  NE    . ARG A 1 220 ? 126.928 130.139 81.130  1.00 37.12  ? 208 ARG A NE    1 
ATOM   1607 C  CZ    . ARG A 1 220 ? 128.089 129.792 81.667  1.00 40.97  ? 208 ARG A CZ    1 
ATOM   1608 N  NH1   . ARG A 1 220 ? 129.209 129.807 80.964  1.00 42.97  ? 208 ARG A NH1   1 
ATOM   1609 N  NH2   . ARG A 1 220 ? 128.127 129.416 82.940  1.00 37.68  ? 208 ARG A NH2   1 
ATOM   1610 N  N     . ALA A 1 221 ? 123.188 132.311 75.624  1.00 42.53  ? 209 ALA A N     1 
ATOM   1611 C  CA    . ALA A 1 221 ? 123.046 132.748 74.239  1.00 42.37  ? 209 ALA A CA    1 
ATOM   1612 C  C     . ALA A 1 221 ? 122.205 134.014 74.139  1.00 48.70  ? 209 ALA A C     1 
ATOM   1613 O  O     . ALA A 1 221 ? 122.543 134.936 73.388  1.00 54.19  ? 209 ALA A O     1 
ATOM   1614 C  CB    . ALA A 1 221 ? 122.433 131.631 73.397  1.00 43.64  ? 209 ALA A CB    1 
ATOM   1615 N  N     . PHE A 1 222 ? 121.107 134.077 74.883  1.00 48.00  ? 210 PHE A N     1 
ATOM   1616 C  CA    . PHE A 1 222 ? 120.217 135.226 74.851  1.00 46.20  ? 210 PHE A CA    1 
ATOM   1617 C  C     . PHE A 1 222 ? 120.548 136.259 75.916  1.00 50.50  ? 210 PHE A C     1 
ATOM   1618 O  O     . PHE A 1 222 ? 119.834 137.260 76.026  1.00 58.14  ? 210 PHE A O     1 
ATOM   1619 C  CB    . PHE A 1 222 ? 118.763 134.770 75.005  1.00 49.84  ? 210 PHE A CB    1 
ATOM   1620 C  CG    . PHE A 1 222 ? 118.190 134.160 73.761  1.00 56.96  ? 210 PHE A CG    1 
ATOM   1621 C  CD1   . PHE A 1 222 ? 118.268 132.798 73.544  1.00 53.23  ? 210 PHE A CD1   1 
ATOM   1622 C  CD2   . PHE A 1 222 ? 117.589 134.951 72.800  1.00 56.68  ? 210 PHE A CD2   1 
ATOM   1623 C  CE1   . PHE A 1 222 ? 117.751 132.236 72.400  1.00 51.31  ? 210 PHE A CE1   1 
ATOM   1624 C  CE2   . PHE A 1 222 ? 117.070 134.394 71.653  1.00 51.59  ? 210 PHE A CE2   1 
ATOM   1625 C  CZ    . PHE A 1 222 ? 117.151 133.035 71.454  1.00 51.77  ? 210 PHE A CZ    1 
ATOM   1626 N  N     . ALA A 1 223 ? 121.611 136.040 76.691  1.00 49.50  ? 211 ALA A N     1 
ATOM   1627 C  CA    . ALA A 1 223 ? 122.023 136.950 77.758  1.00 51.48  ? 211 ALA A CA    1 
ATOM   1628 C  C     . ALA A 1 223 ? 120.880 137.203 78.739  1.00 53.89  ? 211 ALA A C     1 
ATOM   1629 O  O     . ALA A 1 223 ? 120.563 138.343 79.083  1.00 57.45  ? 211 ALA A O     1 
ATOM   1630 C  CB    . ALA A 1 223 ? 122.561 138.262 77.187  1.00 51.87  ? 211 ALA A CB    1 
ATOM   1631 N  N     . ARG A 1 224 ? 120.255 136.116 79.188  1.00 50.01  ? 212 ARG A N     1 
ATOM   1632 C  CA    . ARG A 1 224 ? 119.144 136.183 80.126  1.00 49.14  ? 212 ARG A CA    1 
ATOM   1633 C  C     . ARG A 1 224 ? 119.596 136.137 81.579  1.00 51.86  ? 212 ARG A C     1 
ATOM   1634 O  O     . ARG A 1 224 ? 118.789 135.813 82.455  1.00 58.72  ? 212 ARG A O     1 
ATOM   1635 C  CB    . ARG A 1 224 ? 118.154 135.049 79.855  1.00 48.11  ? 212 ARG A CB    1 
ATOM   1636 C  CG    . ARG A 1 224 ? 117.349 135.226 78.586  1.00 57.24  ? 212 ARG A CG    1 
ATOM   1637 C  CD    . ARG A 1 224 ? 116.364 136.373 78.715  1.00 61.14  ? 212 ARG A CD    1 
ATOM   1638 N  NE    . ARG A 1 224 ? 116.105 137.013 77.431  1.00 64.88  ? 212 ARG A NE    1 
ATOM   1639 C  CZ    . ARG A 1 224 ? 116.712 138.113 77.007  1.00 65.08  ? 212 ARG A CZ    1 
ATOM   1640 N  NH1   . ARG A 1 224 ? 117.621 138.728 77.744  1.00 59.38  ? 212 ARG A NH1   1 
ATOM   1641 N  NH2   . ARG A 1 224 ? 116.398 138.607 75.814  1.00 72.03  ? 212 ARG A NH2   1 
ATOM   1642 N  N     . GLU A 1 225 ? 120.863 136.440 81.852  1.00 51.45  ? 213 GLU A N     1 
ATOM   1643 C  CA    . GLU A 1 225 ? 121.346 136.403 83.231  1.00 55.31  ? 213 GLU A CA    1 
ATOM   1644 C  C     . GLU A 1 225 ? 120.627 137.384 84.149  1.00 58.88  ? 213 GLU A C     1 
ATOM   1645 O  O     . GLU A 1 225 ? 120.239 136.976 85.257  1.00 60.99  ? 213 GLU A O     1 
ATOM   1646 C  CB    . GLU A 1 225 ? 122.862 136.623 83.255  1.00 59.30  ? 213 GLU A CB    1 
ATOM   1647 C  CG    . GLU A 1 225 ? 123.669 135.404 82.847  1.00 62.33  ? 213 GLU A CG    1 
ATOM   1648 C  CD    . GLU A 1 225 ? 124.121 135.453 81.403  1.00 64.26  ? 213 GLU A CD    1 
ATOM   1649 O  OE1   . GLU A 1 225 ? 123.373 135.990 80.562  1.00 58.72  ? 213 GLU A OE1   1 
ATOM   1650 O  OE2   . GLU A 1 225 ? 125.228 134.955 81.111  1.00 68.88  ? 213 GLU A OE2   1 
ATOM   1651 N  N     . PRO A 1 226 ? 120.436 138.663 83.794  1.00 54.99  ? 214 PRO A N     1 
ATOM   1652 C  CA    . PRO A 1 226 ? 119.722 139.556 84.723  1.00 50.21  ? 214 PRO A CA    1 
ATOM   1653 C  C     . PRO A 1 226 ? 118.300 139.117 85.021  1.00 53.97  ? 214 PRO A C     1 
ATOM   1654 O  O     . PRO A 1 226 ? 117.851 139.235 86.167  1.00 58.55  ? 214 PRO A O     1 
ATOM   1655 C  CB    . PRO A 1 226 ? 119.760 140.913 84.005  1.00 50.57  ? 214 PRO A CB    1 
ATOM   1656 C  CG    . PRO A 1 226 ? 120.008 140.594 82.585  1.00 53.70  ? 214 PRO A CG    1 
ATOM   1657 C  CD    . PRO A 1 226 ? 120.887 139.391 82.596  1.00 56.13  ? 214 PRO A CD    1 
ATOM   1658 N  N     . LEU A 1 227 ? 117.579 138.601 84.025  1.00 53.30  ? 215 LEU A N     1 
ATOM   1659 C  CA    . LEU A 1 227 ? 116.201 138.177 84.256  1.00 50.91  ? 215 LEU A CA    1 
ATOM   1660 C  C     . LEU A 1 227 ? 116.145 136.989 85.206  1.00 49.81  ? 215 LEU A C     1 
ATOM   1661 O  O     . LEU A 1 227 ? 115.328 136.960 86.133  1.00 55.09  ? 215 LEU A O     1 
ATOM   1662 C  CB    . LEU A 1 227 ? 115.525 137.834 82.929  1.00 54.40  ? 215 LEU A CB    1 
ATOM   1663 C  CG    . LEU A 1 227 ? 114.877 138.986 82.161  1.00 61.58  ? 215 LEU A CG    1 
ATOM   1664 C  CD1   . LEU A 1 227 ? 114.019 139.835 83.085  1.00 57.79  ? 215 LEU A CD1   1 
ATOM   1665 C  CD2   . LEU A 1 227 ? 115.931 139.831 81.466  1.00 60.70  ? 215 LEU A CD2   1 
ATOM   1666 N  N     . GLU A 1 228 ? 117.008 135.998 84.986  1.00 51.09  ? 216 GLU A N     1 
ATOM   1667 C  CA    . GLU A 1 228 ? 117.058 134.845 85.877  1.00 53.96  ? 216 GLU A CA    1 
ATOM   1668 C  C     . GLU A 1 228 ? 117.485 135.255 87.279  1.00 52.26  ? 216 GLU A C     1 
ATOM   1669 O  O     . GLU A 1 228 ? 116.970 134.732 88.273  1.00 51.91  ? 216 GLU A O     1 
ATOM   1670 C  CB    . GLU A 1 228 ? 118.007 133.789 85.313  1.00 54.25  ? 216 GLU A CB    1 
ATOM   1671 C  CG    . GLU A 1 228 ? 117.632 133.285 83.934  1.00 53.18  ? 216 GLU A CG    1 
ATOM   1672 C  CD    . GLU A 1 228 ? 116.280 132.606 83.904  1.00 65.11  ? 216 GLU A CD    1 
ATOM   1673 O  OE1   . GLU A 1 228 ? 115.876 132.029 84.934  1.00 64.44  ? 216 GLU A OE1   1 
ATOM   1674 O  OE2   . GLU A 1 228 ? 115.619 132.648 82.846  1.00 66.82  ? 216 GLU A OE2   1 
ATOM   1675 N  N     . ARG A 1 229 ? 118.430 136.191 87.376  1.00 53.88  ? 217 ARG A N     1 
ATOM   1676 C  CA    . ARG A 1 229 ? 118.879 136.670 88.678  1.00 54.98  ? 217 ARG A CA    1 
ATOM   1677 C  C     . ARG A 1 229 ? 117.749 137.361 89.432  1.00 54.28  ? 217 ARG A C     1 
ATOM   1678 O  O     . ARG A 1 229 ? 117.561 137.129 90.631  1.00 55.38  ? 217 ARG A O     1 
ATOM   1679 C  CB    . ARG A 1 229 ? 120.064 137.613 88.490  1.00 55.58  ? 217 ARG A CB    1 
ATOM   1680 C  CG    . ARG A 1 229 ? 120.739 138.047 89.769  1.00 59.20  ? 217 ARG A CG    1 
ATOM   1681 C  CD    . ARG A 1 229 ? 121.968 138.879 89.460  1.00 61.94  ? 217 ARG A CD    1 
ATOM   1682 N  NE    . ARG A 1 229 ? 122.982 138.106 88.753  1.00 69.98  ? 217 ARG A NE    1 
ATOM   1683 C  CZ    . ARG A 1 229 ? 123.412 138.380 87.528  1.00 74.67  ? 217 ARG A CZ    1 
ATOM   1684 N  NH1   . ARG A 1 229 ? 122.938 139.408 86.843  1.00 71.90  ? 217 ARG A NH1   1 
ATOM   1685 N  NH2   . ARG A 1 229 ? 124.341 137.604 86.978  1.00 68.68  ? 217 ARG A NH2   1 
ATOM   1686 N  N     . VAL A 1 230 ? 116.975 138.202 88.742  1.00 51.94  ? 218 VAL A N     1 
ATOM   1687 C  CA    . VAL A 1 230 ? 115.847 138.877 89.378  1.00 47.26  ? 218 VAL A CA    1 
ATOM   1688 C  C     . VAL A 1 230 ? 114.778 137.871 89.792  1.00 50.78  ? 218 VAL A C     1 
ATOM   1689 O  O     . VAL A 1 230 ? 114.218 137.955 90.894  1.00 54.95  ? 218 VAL A O     1 
ATOM   1690 C  CB    . VAL A 1 230 ? 115.280 139.958 88.438  1.00 47.19  ? 218 VAL A CB    1 
ATOM   1691 C  CG1   . VAL A 1 230 ? 113.954 140.481 88.957  1.00 52.44  ? 218 VAL A CG1   1 
ATOM   1692 C  CG2   . VAL A 1 230 ? 116.273 141.094 88.286  1.00 49.26  ? 218 VAL A CG2   1 
ATOM   1693 N  N     . ARG A 1 231 ? 114.473 136.909 88.921  1.00 50.68  ? 219 ARG A N     1 
ATOM   1694 C  CA    . ARG A 1 231 ? 113.475 135.901 89.261  1.00 48.45  ? 219 ARG A CA    1 
ATOM   1695 C  C     . ARG A 1 231 ? 113.896 135.120 90.498  1.00 49.74  ? 219 ARG A C     1 
ATOM   1696 O  O     . ARG A 1 231 ? 113.096 134.906 91.420  1.00 58.28  ? 219 ARG A O     1 
ATOM   1697 C  CB    . ARG A 1 231 ? 113.258 134.963 88.074  1.00 48.68  ? 219 ARG A CB    1 
ATOM   1698 C  CG    . ARG A 1 231 ? 112.362 133.780 88.380  1.00 55.80  ? 219 ARG A CG    1 
ATOM   1699 C  CD    . ARG A 1 231 ? 111.882 133.104 87.110  1.00 63.16  ? 219 ARG A CD    1 
ATOM   1700 N  NE    . ARG A 1 231 ? 112.932 132.323 86.470  1.00 68.91  ? 219 ARG A NE    1 
ATOM   1701 C  CZ    . ARG A 1 231 ? 112.724 131.188 85.818  1.00 67.10  ? 219 ARG A CZ    1 
ATOM   1702 N  NH1   . ARG A 1 231 ? 111.510 130.678 85.691  1.00 62.18  ? 219 ARG A NH1   1 
ATOM   1703 N  NH2   . ARG A 1 231 ? 113.759 130.546 85.283  1.00 63.27  ? 219 ARG A NH2   1 
ATOM   1704 N  N     . PHE A 1 232 ? 115.165 134.709 90.547  1.00 47.06  ? 220 PHE A N     1 
ATOM   1705 C  CA    . PHE A 1 232 ? 115.647 133.966 91.702  1.00 44.13  ? 220 PHE A CA    1 
ATOM   1706 C  C     . PHE A 1 232 ? 115.641 134.830 92.953  1.00 44.33  ? 220 PHE A C     1 
ATOM   1707 O  O     . PHE A 1 232 ? 115.364 134.331 94.044  1.00 47.80  ? 220 PHE A O     1 
ATOM   1708 C  CB    . PHE A 1 232 ? 117.046 133.416 91.442  1.00 44.81  ? 220 PHE A CB    1 
ATOM   1709 C  CG    . PHE A 1 232 ? 117.533 132.490 92.517  1.00 45.62  ? 220 PHE A CG    1 
ATOM   1710 C  CD1   . PHE A 1 232 ? 117.215 131.144 92.482  1.00 44.54  ? 220 PHE A CD1   1 
ATOM   1711 C  CD2   . PHE A 1 232 ? 118.292 132.966 93.571  1.00 38.67  ? 220 PHE A CD2   1 
ATOM   1712 C  CE1   . PHE A 1 232 ? 117.653 130.292 93.472  1.00 41.35  ? 220 PHE A CE1   1 
ATOM   1713 C  CE2   . PHE A 1 232 ? 118.730 132.118 94.560  1.00 38.73  ? 220 PHE A CE2   1 
ATOM   1714 C  CZ    . PHE A 1 232 ? 118.409 130.780 94.511  1.00 39.44  ? 220 PHE A CZ    1 
ATOM   1715 N  N     . ALA A 1 233 ? 115.952 136.121 92.823  1.00 46.76  ? 221 ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 233 ? 115.964 136.995 93.992  1.00 46.28  ? 221 ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 233 ? 114.571 137.134 94.592  1.00 50.62  ? 221 ALA A C     1 
ATOM   1718 O  O     . ALA A 1 233 ? 114.398 137.057 95.813  1.00 53.31  ? 221 ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 233 ? 116.531 138.362 93.618  1.00 41.75  ? 221 ALA A CB    1 
ATOM   1720 N  N     . GLU A 1 234 ? 113.559 137.333 93.744  1.00 51.80  ? 222 GLU A N     1 
ATOM   1721 C  CA    . GLU A 1 234 ? 112.187 137.413 94.248  1.00 54.96  ? 222 GLU A CA    1 
ATOM   1722 C  C     . GLU A 1 234 ? 111.727 136.094 94.865  1.00 52.72  ? 222 GLU A C     1 
ATOM   1723 O  O     . GLU A 1 234 ? 111.107 136.087 95.939  1.00 55.06  ? 222 GLU A O     1 
ATOM   1724 C  CB    . GLU A 1 234 ? 111.241 137.864 93.133  1.00 57.40  ? 222 GLU A CB    1 
ATOM   1725 C  CG    . GLU A 1 234 ? 111.095 139.392 92.942  1.00 63.51  ? 222 GLU A CG    1 
ATOM   1726 C  CD    . GLU A 1 234 ? 112.396 140.166 92.709  1.00 65.49  ? 222 GLU A CD    1 
ATOM   1727 O  OE1   . GLU A 1 234 ? 112.310 141.398 92.522  1.00 69.64  ? 222 GLU A OE1   1 
ATOM   1728 O  OE2   . GLU A 1 234 ? 113.495 139.583 92.728  1.00 62.80  ? 222 GLU A OE2   1 
ATOM   1729 N  N     . ALA A 1 235 ? 112.019 134.966 94.210  1.00 47.53  ? 223 ALA A N     1 
ATOM   1730 C  CA    . ALA A 1 235 ? 111.640 133.678 94.788  1.00 45.75  ? 223 ALA A CA    1 
ATOM   1731 C  C     . ALA A 1 235 ? 112.342 133.444 96.121  1.00 48.42  ? 223 ALA A C     1 
ATOM   1732 O  O     . ALA A 1 235 ? 111.733 132.950 97.081  1.00 50.50  ? 223 ALA A O     1 
ATOM   1733 C  CB    . ALA A 1 235 ? 111.953 132.547 93.810  1.00 39.43  ? 223 ALA A CB    1 
ATOM   1734 N  N     . ASN A 1 236 ? 113.626 133.802 96.198  1.00 46.24  ? 224 ASN A N     1 
ATOM   1735 C  CA    . ASN A 1 236 ? 114.398 133.645 97.423  1.00 44.75  ? 224 ASN A CA    1 
ATOM   1736 C  C     . ASN A 1 236 ? 113.835 134.506 98.543  1.00 45.21  ? 224 ASN A C     1 
ATOM   1737 O  O     . ASN A 1 236 ? 113.730 134.055 99.687  1.00 45.06  ? 224 ASN A O     1 
ATOM   1738 C  CB    . ASN A 1 236 ? 115.860 134.001 97.145  1.00 39.69  ? 224 ASN A CB    1 
ATOM   1739 C  CG    . ASN A 1 236 ? 116.822 133.334 98.099  1.00 40.98  ? 224 ASN A CG    1 
ATOM   1740 O  OD1   . ASN A 1 236 ? 116.487 132.348 98.752  1.00 50.17  ? 224 ASN A OD1   1 
ATOM   1741 N  ND2   . ASN A 1 236 ? 118.035 133.863 98.176  1.00 35.41  ? 224 ASN A ND2   1 
ATOM   1742 N  N     . GLN A 1 237 ? 113.464 135.750 98.232  1.00 43.70  ? 225 GLN A N     1 
ATOM   1743 C  CA    . GLN A 1 237 ? 112.896 136.627 99.250  1.00 43.14  ? 225 GLN A CA    1 
ATOM   1744 C  C     . GLN A 1 237 ? 111.563 136.096 99.759  1.00 47.05  ? 225 GLN A C     1 
ATOM   1745 O  O     . GLN A 1 237 ? 111.295 136.131 100.965 1.00 52.96  ? 225 GLN A O     1 
ATOM   1746 C  CB    . GLN A 1 237 ? 112.733 138.040 98.695  1.00 52.22  ? 225 GLN A CB    1 
ATOM   1747 C  CG    . GLN A 1 237 ? 113.913 138.958 98.977  1.00 64.73  ? 225 GLN A CG    1 
ATOM   1748 C  CD    . GLN A 1 237 ? 114.398 138.867 100.411 1.00 66.78  ? 225 GLN A CD    1 
ATOM   1749 O  OE1   . GLN A 1 237 ? 115.488 138.363 100.681 1.00 59.30  ? 225 GLN A OE1   1 
ATOM   1750 N  NE2   . GLN A 1 237 ? 113.587 139.360 101.341 1.00 60.41  ? 225 GLN A NE2   1 
ATOM   1751 N  N     . THR A 1 238 ? 110.709 135.607 98.856  1.00 48.81  ? 226 THR A N     1 
ATOM   1752 C  CA    . THR A 1 238 ? 109.424 135.062 99.290  1.00 45.74  ? 226 THR A CA    1 
ATOM   1753 C  C     . THR A 1 238 ? 109.614 133.836 100.178 1.00 40.77  ? 226 THR A C     1 
ATOM   1754 O  O     . THR A 1 238 ? 108.967 133.705 101.231 1.00 45.35  ? 226 THR A O     1 
ATOM   1755 C  CB    . THR A 1 238 ? 108.566 134.720 98.072  1.00 47.55  ? 226 THR A CB    1 
ATOM   1756 O  OG1   . THR A 1 238 ? 108.347 135.903 97.296  1.00 53.17  ? 226 THR A OG1   1 
ATOM   1757 C  CG2   . THR A 1 238 ? 107.228 134.173 98.503  1.00 49.81  ? 226 THR A CG2   1 
ATOM   1758 N  N     . LEU A 1 239 ? 110.511 132.932 99.777  1.00 36.71  ? 227 LEU A N     1 
ATOM   1759 C  CA    . LEU A 1 239 ? 110.789 131.755 100.592 1.00 37.92  ? 227 LEU A CA    1 
ATOM   1760 C  C     . LEU A 1 239 ? 111.365 132.146 101.948 1.00 42.17  ? 227 LEU A C     1 
ATOM   1761 O  O     . LEU A 1 239 ? 111.036 131.535 102.970 1.00 42.81  ? 227 LEU A O     1 
ATOM   1762 C  CB    . LEU A 1 239 ? 111.742 130.824 99.847  1.00 35.79  ? 227 LEU A CB    1 
ATOM   1763 C  CG    . LEU A 1 239 ? 112.264 129.620 100.627 1.00 37.01  ? 227 LEU A CG    1 
ATOM   1764 C  CD1   . LEU A 1 239 ? 111.111 128.798 101.169 1.00 40.00  ? 227 LEU A CD1   1 
ATOM   1765 C  CD2   . LEU A 1 239 ? 113.162 128.779 99.746  1.00 38.67  ? 227 LEU A CD2   1 
ATOM   1766 N  N     . SER A 1 240 ? 112.231 133.162 101.976 1.00 40.89  ? 228 SER A N     1 
ATOM   1767 C  CA    . SER A 1 240 ? 112.788 133.629 103.239 1.00 35.61  ? 228 SER A CA    1 
ATOM   1768 C  C     . SER A 1 240 ? 111.712 134.217 104.139 1.00 40.22  ? 228 SER A C     1 
ATOM   1769 O  O     . SER A 1 240 ? 111.755 134.036 105.358 1.00 43.55  ? 228 SER A O     1 
ATOM   1770 C  CB    . SER A 1 240 ? 113.876 134.663 102.983 1.00 43.46  ? 228 SER A CB    1 
ATOM   1771 O  OG    . SER A 1 240 ? 114.475 135.073 104.197 1.00 49.55  ? 228 SER A OG    1 
ATOM   1772 N  N     . ASP A 1 241 ? 110.753 134.943 103.564 1.00 41.97  ? 229 ASP A N     1 
ATOM   1773 C  CA    . ASP A 1 241 ? 109.655 135.478 104.364 1.00 40.37  ? 229 ASP A CA    1 
ATOM   1774 C  C     . ASP A 1 241 ? 108.840 134.354 104.992 1.00 39.56  ? 229 ASP A C     1 
ATOM   1775 O  O     . ASP A 1 241 ? 108.493 134.404 106.182 1.00 43.97  ? 229 ASP A O     1 
ATOM   1776 C  CB    . ASP A 1 241 ? 108.765 136.369 103.499 1.00 41.50  ? 229 ASP A CB    1 
ATOM   1777 C  CG    . ASP A 1 241 ? 109.462 137.636 103.063 1.00 54.28  ? 229 ASP A CG    1 
ATOM   1778 O  OD1   . ASP A 1 241 ? 110.515 137.963 103.647 1.00 55.79  ? 229 ASP A OD1   1 
ATOM   1779 O  OD2   . ASP A 1 241 ? 108.958 138.305 102.138 1.00 57.72  ? 229 ASP A OD2   1 
ATOM   1780 N  N     . SER A 1 242 ? 108.526 133.324 104.205 1.00 37.05  ? 230 SER A N     1 
ATOM   1781 C  CA    . SER A 1 242 ? 107.773 132.202 104.759 1.00 34.32  ? 230 SER A CA    1 
ATOM   1782 C  C     . SER A 1 242 ? 108.570 131.470 105.832 1.00 35.29  ? 230 SER A C     1 
ATOM   1783 O  O     . SER A 1 242 ? 108.017 131.075 106.866 1.00 45.11  ? 230 SER A O     1 
ATOM   1784 C  CB    . SER A 1 242 ? 107.354 131.246 103.647 1.00 40.29  ? 230 SER A CB    1 
ATOM   1785 O  OG    . SER A 1 242 ? 106.332 131.827 102.860 1.00 52.12  ? 230 SER A OG    1 
ATOM   1786 N  N     . ALA A 1 243 ? 109.871 131.285 105.608 1.00 37.89  ? 231 ALA A N     1 
ATOM   1787 C  CA    . ALA A 1 243 ? 110.702 130.617 106.602 1.00 36.31  ? 231 ALA A CA    1 
ATOM   1788 C  C     . ALA A 1 243 ? 110.822 131.451 107.869 1.00 35.08  ? 231 ALA A C     1 
ATOM   1789 O  O     . ALA A 1 243 ? 110.898 130.904 108.972 1.00 40.09  ? 231 ALA A O     1 
ATOM   1790 C  CB    . ALA A 1 243 ? 112.079 130.319 106.017 1.00 33.73  ? 231 ALA A CB    1 
ATOM   1791 N  N     . LEU A 1 244 ? 110.845 132.776 107.730 1.00 37.06  ? 232 LEU A N     1 
ATOM   1792 C  CA    . LEU A 1 244 ? 110.871 133.653 108.893 1.00 34.91  ? 232 LEU A CA    1 
ATOM   1793 C  C     . LEU A 1 244 ? 109.583 133.541 109.696 1.00 36.65  ? 232 LEU A C     1 
ATOM   1794 O  O     . LEU A 1 244 ? 109.615 133.537 110.929 1.00 38.28  ? 232 LEU A O     1 
ATOM   1795 C  CB    . LEU A 1 244 ? 111.101 135.097 108.452 1.00 39.57  ? 232 LEU A CB    1 
ATOM   1796 C  CG    . LEU A 1 244 ? 112.498 135.687 108.637 1.00 37.22  ? 232 LEU A CG    1 
ATOM   1797 C  CD1   . LEU A 1 244 ? 112.411 137.193 108.765 1.00 43.36  ? 232 LEU A CD1   1 
ATOM   1798 C  CD2   . LEU A 1 244 ? 113.183 135.096 109.845 1.00 36.60  ? 232 LEU A CD2   1 
ATOM   1799 N  N     . GLU A 1 245 ? 108.437 133.463 109.017 1.00 38.43  ? 233 GLU A N     1 
ATOM   1800 C  CA    . GLU A 1 245 ? 107.179 133.254 109.736 1.00 39.02  ? 233 GLU A CA    1 
ATOM   1801 C  C     . GLU A 1 245 ? 107.174 131.911 110.461 1.00 39.07  ? 233 GLU A C     1 
ATOM   1802 O  O     . GLU A 1 245 ? 106.737 131.812 111.620 1.00 41.71  ? 233 GLU A O     1 
ATOM   1803 C  CB    . GLU A 1 245 ? 106.000 133.346 108.770 1.00 41.10  ? 233 GLU A CB    1 
ATOM   1804 C  CG    . GLU A 1 245 ? 104.750 133.954 109.374 1.00 49.89  ? 233 GLU A CG    1 
ATOM   1805 C  CD    . GLU A 1 245 ? 103.883 134.648 108.342 1.00 68.23  ? 233 GLU A CD    1 
ATOM   1806 O  OE1   . GLU A 1 245 ? 103.214 135.643 108.692 1.00 67.77  ? 233 GLU A OE1   1 
ATOM   1807 O  OE2   . GLU A 1 245 ? 103.870 134.197 107.177 1.00 70.22  ? 233 GLU A OE2   1 
ATOM   1808 N  N     . ALA A 1 246 ? 107.663 130.864 109.793 1.00 38.34  ? 234 ALA A N     1 
ATOM   1809 C  CA    . ALA A 1 246 ? 107.745 129.555 110.430 1.00 36.02  ? 234 ALA A CA    1 
ATOM   1810 C  C     . ALA A 1 246 ? 108.666 129.587 111.643 1.00 37.14  ? 234 ALA A C     1 
ATOM   1811 O  O     . ALA A 1 246 ? 108.365 128.981 112.675 1.00 39.46  ? 234 ALA A O     1 
ATOM   1812 C  CB    . ALA A 1 246 ? 108.218 128.510 109.421 1.00 37.09  ? 234 ALA A CB    1 
ATOM   1813 N  N     . GLY A 1 247 ? 109.795 130.287 111.538 1.00 35.70  ? 235 GLY A N     1 
ATOM   1814 C  CA    . GLY A 1 247 ? 110.680 130.434 112.680 1.00 31.45  ? 235 GLY A CA    1 
ATOM   1815 C  C     . GLY A 1 247 ? 110.075 131.253 113.801 1.00 37.03  ? 235 GLY A C     1 
ATOM   1816 O  O     . GLY A 1 247 ? 110.335 130.988 114.975 1.00 42.75  ? 235 GLY A O     1 
ATOM   1817 N  N     . ARG A 1 248 ? 109.272 132.261 113.459 1.00 37.92  ? 236 ARG A N     1 
ATOM   1818 C  CA    . ARG A 1 248 ? 108.562 133.025 114.478 1.00 33.75  ? 236 ARG A CA    1 
ATOM   1819 C  C     . ARG A 1 248 ? 107.633 132.126 115.274 1.00 35.84  ? 236 ARG A C     1 
ATOM   1820 O  O     . ARG A 1 248 ? 107.552 132.231 116.503 1.00 36.23  ? 236 ARG A O     1 
ATOM   1821 C  CB    . ARG A 1 248 ? 107.765 134.155 113.831 1.00 31.80  ? 236 ARG A CB    1 
ATOM   1822 C  CG    . ARG A 1 248 ? 108.575 135.382 113.491 1.00 39.73  ? 236 ARG A CG    1 
ATOM   1823 C  CD    . ARG A 1 248 ? 107.672 136.527 113.080 1.00 39.60  ? 236 ARG A CD    1 
ATOM   1824 N  NE    . ARG A 1 248 ? 107.350 136.493 111.660 1.00 43.77  ? 236 ARG A NE    1 
ATOM   1825 C  CZ    . ARG A 1 248 ? 108.118 137.006 110.709 1.00 45.86  ? 236 ARG A CZ    1 
ATOM   1826 N  NH1   . ARG A 1 248 ? 109.275 137.580 110.991 1.00 39.99  ? 236 ARG A NH1   1 
ATOM   1827 N  NH2   . ARG A 1 248 ? 107.715 136.939 109.444 1.00 46.66  ? 236 ARG A NH2   1 
ATOM   1828 N  N     . TRP A 1 249 ? 106.915 131.241 114.587 1.00 37.97  ? 237 TRP A N     1 
ATOM   1829 C  CA    . TRP A 1 249 ? 106.039 130.322 115.304 1.00 32.77  ? 237 TRP A CA    1 
ATOM   1830 C  C     . TRP A 1 249 ? 106.818 129.239 116.041 1.00 33.05  ? 237 TRP A C     1 
ATOM   1831 O  O     . TRP A 1 249 ? 106.372 128.770 117.092 1.00 39.21  ? 237 TRP A O     1 
ATOM   1832 C  CB    . TRP A 1 249 ? 105.033 129.695 114.343 1.00 37.40  ? 237 TRP A CB    1 
ATOM   1833 C  CG    . TRP A 1 249 ? 103.868 130.583 114.062 1.00 37.34  ? 237 TRP A CG    1 
ATOM   1834 C  CD1   . TRP A 1 249 ? 103.530 131.135 112.865 1.00 40.57  ? 237 TRP A CD1   1 
ATOM   1835 C  CD2   . TRP A 1 249 ? 102.888 131.034 115.004 1.00 38.27  ? 237 TRP A CD2   1 
ATOM   1836 N  NE1   . TRP A 1 249 ? 102.398 131.899 112.999 1.00 47.89  ? 237 TRP A NE1   1 
ATOM   1837 C  CE2   . TRP A 1 249 ? 101.984 131.853 114.304 1.00 44.19  ? 237 TRP A CE2   1 
ATOM   1838 C  CE3   . TRP A 1 249 ? 102.687 130.821 116.371 1.00 38.90  ? 237 TRP A CE3   1 
ATOM   1839 C  CZ2   . TRP A 1 249 ? 100.895 132.461 114.922 1.00 44.84  ? 237 TRP A CZ2   1 
ATOM   1840 C  CZ3   . TRP A 1 249 ? 101.606 131.425 116.982 1.00 40.94  ? 237 TRP A CZ3   1 
ATOM   1841 C  CH2   . TRP A 1 249 ? 100.724 132.234 116.259 1.00 44.93  ? 237 TRP A CH2   1 
ATOM   1842 N  N     . GLN A 1 250 ? 107.975 128.835 115.516 1.00 36.38  ? 238 GLN A N     1 
ATOM   1843 C  CA    . GLN A 1 250 ? 108.758 127.778 116.149 1.00 36.53  ? 238 GLN A CA    1 
ATOM   1844 C  C     . GLN A 1 250 ? 109.512 128.277 117.374 1.00 32.75  ? 238 GLN A C     1 
ATOM   1845 O  O     . GLN A 1 250 ? 109.824 127.487 118.271 1.00 36.42  ? 238 GLN A O     1 
ATOM   1846 C  CB    . GLN A 1 250 ? 109.736 127.183 115.137 1.00 38.40  ? 238 GLN A CB    1 
ATOM   1847 C  CG    . GLN A 1 250 ? 110.329 125.853 115.549 1.00 46.82  ? 238 GLN A CG    1 
ATOM   1848 C  CD    . GLN A 1 250 ? 110.381 124.866 114.405 1.00 62.37  ? 238 GLN A CD    1 
ATOM   1849 O  OE1   . GLN A 1 250 ? 110.653 125.238 113.264 1.00 67.88  ? 238 GLN A OE1   1 
ATOM   1850 N  NE2   . GLN A 1 250 ? 110.121 123.598 114.703 1.00 63.08  ? 238 GLN A NE2   1 
ATOM   1851 N  N     . ALA A 1 251 ? 109.816 129.572 117.432 1.00 35.28  ? 239 ALA A N     1 
ATOM   1852 C  CA    . ALA A 1 251 ? 110.560 130.126 118.555 1.00 30.83  ? 239 ALA A CA    1 
ATOM   1853 C  C     . ALA A 1 251 ? 109.751 130.166 119.841 1.00 39.81  ? 239 ALA A C     1 
ATOM   1854 O  O     . ALA A 1 251 ? 110.316 130.474 120.893 1.00 37.47  ? 239 ALA A O     1 
ATOM   1855 C  CB    . ALA A 1 251 ? 111.048 131.532 118.212 1.00 31.30  ? 239 ALA A CB    1 
ATOM   1856 N  N     . LEU A 1 252 ? 108.449 129.889 119.781 1.00 43.35  ? 240 LEU A N     1 
ATOM   1857 C  CA    . LEU A 1 252 ? 107.607 129.849 120.967 1.00 38.59  ? 240 LEU A CA    1 
ATOM   1858 C  C     . LEU A 1 252 ? 107.615 128.498 121.667 1.00 41.11  ? 240 LEU A C     1 
ATOM   1859 O  O     . LEU A 1 252 ? 107.149 128.407 122.806 1.00 46.60  ? 240 LEU A O     1 
ATOM   1860 C  CB    . LEU A 1 252 ? 106.161 130.194 120.600 1.00 33.51  ? 240 LEU A CB    1 
ATOM   1861 C  CG    . LEU A 1 252 ? 105.777 131.661 120.444 1.00 34.25  ? 240 LEU A CG    1 
ATOM   1862 C  CD1   . LEU A 1 252 ? 104.462 131.769 119.704 1.00 34.45  ? 240 LEU A CD1   1 
ATOM   1863 C  CD2   . LEU A 1 252 ? 105.677 132.321 121.802 1.00 32.85  ? 240 LEU A CD2   1 
ATOM   1864 N  N     . MET A 1 253 ? 108.117 127.450 121.015 1.00 40.21  ? 241 MET A N     1 
ATOM   1865 C  CA    . MET A 1 253 ? 107.940 126.106 121.553 1.00 42.34  ? 241 MET A CA    1 
ATOM   1866 C  C     . MET A 1 253 ? 108.862 125.849 122.740 1.00 44.80  ? 241 MET A C     1 
ATOM   1867 O  O     . MET A 1 253 ? 108.436 125.269 123.744 1.00 49.98  ? 241 MET A O     1 
ATOM   1868 C  CB    . MET A 1 253 ? 108.161 125.075 120.448 1.00 45.95  ? 241 MET A CB    1 
ATOM   1869 C  CG    . MET A 1 253 ? 107.453 125.441 119.154 1.00 51.78  ? 241 MET A CG    1 
ATOM   1870 S  SD    . MET A 1 253 ? 107.064 124.060 118.069 1.00 62.82  ? 241 MET A SD    1 
ATOM   1871 C  CE    . MET A 1 253 ? 105.623 123.401 118.900 1.00 46.86  ? 241 MET A CE    1 
ATOM   1872 N  N     . LEU A 1 254 ? 110.132 126.256 122.641 1.00 43.83  ? 242 LEU A N     1 
ATOM   1873 C  CA    . LEU A 1 254 ? 111.041 126.074 123.773 1.00 41.95  ? 242 LEU A CA    1 
ATOM   1874 C  C     . LEU A 1 254 ? 110.663 126.935 124.972 1.00 44.07  ? 242 LEU A C     1 
ATOM   1875 O  O     . LEU A 1 254 ? 110.598 126.397 126.092 1.00 47.64  ? 242 LEU A O     1 
ATOM   1876 C  CB    . LEU A 1 254 ? 112.488 126.322 123.333 1.00 44.96  ? 242 LEU A CB    1 
ATOM   1877 C  CG    . LEU A 1 254 ? 113.579 125.639 124.165 1.00 45.85  ? 242 LEU A CG    1 
ATOM   1878 C  CD1   . LEU A 1 254 ? 114.812 125.365 123.327 1.00 51.36  ? 242 LEU A CD1   1 
ATOM   1879 C  CD2   . LEU A 1 254 ? 113.950 126.459 125.387 1.00 43.77  ? 242 LEU A CD2   1 
ATOM   1880 N  N     . PRO A 1 255 ? 110.440 128.251 124.840 1.00 46.05  ? 243 PRO A N     1 
ATOM   1881 C  CA    . PRO A 1 255 ? 110.094 129.037 126.035 1.00 43.25  ? 243 PRO A CA    1 
ATOM   1882 C  C     . PRO A 1 255 ? 108.836 128.561 126.731 1.00 43.10  ? 243 PRO A C     1 
ATOM   1883 O  O     . PRO A 1 255 ? 108.800 128.540 127.963 1.00 49.81  ? 243 PRO A O     1 
ATOM   1884 C  CB    . PRO A 1 255 ? 109.933 130.462 125.484 1.00 41.03  ? 243 PRO A CB    1 
ATOM   1885 C  CG    . PRO A 1 255 ? 109.692 130.288 124.040 1.00 45.53  ? 243 PRO A CG    1 
ATOM   1886 C  CD    . PRO A 1 255 ? 110.522 129.113 123.651 1.00 45.98  ? 243 PRO A CD    1 
ATOM   1887 N  N     . VAL A 1 256 ? 107.809 128.159 125.983 1.00 40.29  ? 244 VAL A N     1 
ATOM   1888 C  CA    . VAL A 1 256 ? 106.570 127.707 126.609 1.00 39.64  ? 244 VAL A CA    1 
ATOM   1889 C  C     . VAL A 1 256 ? 106.793 126.400 127.361 1.00 43.26  ? 244 VAL A C     1 
ATOM   1890 O  O     . VAL A 1 256 ? 106.323 126.232 128.493 1.00 48.53  ? 244 VAL A O     1 
ATOM   1891 C  CB    . VAL A 1 256 ? 105.459 127.580 125.553 1.00 41.60  ? 244 VAL A CB    1 
ATOM   1892 C  CG1   . VAL A 1 256 ? 104.303 126.761 126.088 1.00 46.73  ? 244 VAL A CG1   1 
ATOM   1893 C  CG2   . VAL A 1 256 ? 104.979 128.956 125.134 1.00 41.57  ? 244 VAL A CG2   1 
ATOM   1894 N  N     . THR A 1 257 ? 107.521 125.461 126.753 1.00 40.26  ? 245 THR A N     1 
ATOM   1895 C  CA    . THR A 1 257 ? 107.799 124.189 127.413 1.00 41.75  ? 245 THR A CA    1 
ATOM   1896 C  C     . THR A 1 257 ? 108.620 124.393 128.680 1.00 42.33  ? 245 THR A C     1 
ATOM   1897 O  O     . THR A 1 257 ? 108.317 123.816 129.731 1.00 49.07  ? 245 THR A O     1 
ATOM   1898 C  CB    . THR A 1 257 ? 108.521 123.250 126.447 1.00 46.67  ? 245 THR A CB    1 
ATOM   1899 O  OG1   . THR A 1 257 ? 107.642 122.903 125.371 1.00 48.97  ? 245 THR A OG1   1 
ATOM   1900 C  CG2   . THR A 1 257 ? 108.967 121.983 127.160 1.00 43.89  ? 245 THR A CG2   1 
ATOM   1901 N  N     . THR A 1 258 ? 109.661 125.222 128.604 1.00 39.73  ? 246 THR A N     1 
ATOM   1902 C  CA    . THR A 1 258 ? 110.487 125.468 129.781 1.00 36.71  ? 246 THR A CA    1 
ATOM   1903 C  C     . THR A 1 258 ? 109.712 126.222 130.854 1.00 38.55  ? 246 THR A C     1 
ATOM   1904 O  O     . THR A 1 258 ? 109.886 125.964 132.050 1.00 43.00  ? 246 THR A O     1 
ATOM   1905 C  CB    . THR A 1 258 ? 111.750 126.230 129.387 1.00 41.02  ? 246 THR A CB    1 
ATOM   1906 O  OG1   . THR A 1 258 ? 112.391 125.554 128.300 1.00 47.53  ? 246 THR A OG1   1 
ATOM   1907 C  CG2   . THR A 1 258 ? 112.713 126.305 130.555 1.00 37.77  ? 246 THR A CG2   1 
ATOM   1908 N  N     . LEU A 1 259 ? 108.847 127.155 130.452 1.00 37.15  ? 247 LEU A N     1 
ATOM   1909 C  CA    . LEU A 1 259 ? 108.030 127.874 131.419 1.00 39.43  ? 247 LEU A CA    1 
ATOM   1910 C  C     . LEU A 1 259 ? 107.077 126.931 132.134 1.00 41.44  ? 247 LEU A C     1 
ATOM   1911 O  O     . LEU A 1 259 ? 106.859 127.056 133.343 1.00 48.77  ? 247 LEU A O     1 
ATOM   1912 C  CB    . LEU A 1 259 ? 107.261 128.993 130.720 1.00 38.41  ? 247 LEU A CB    1 
ATOM   1913 C  CG    . LEU A 1 259 ? 106.690 130.083 131.621 1.00 39.25  ? 247 LEU A CG    1 
ATOM   1914 C  CD1   . LEU A 1 259 ? 107.802 130.728 132.416 1.00 43.92  ? 247 LEU A CD1   1 
ATOM   1915 C  CD2   . LEU A 1 259 ? 105.953 131.119 130.797 1.00 32.09  ? 247 LEU A CD2   1 
ATOM   1916 N  N     . VAL A 1 260 ? 106.492 125.983 131.401 1.00 39.20  ? 248 VAL A N     1 
ATOM   1917 C  CA    . VAL A 1 260 ? 105.655 124.974 132.042 1.00 36.62  ? 248 VAL A CA    1 
ATOM   1918 C  C     . VAL A 1 260 ? 106.485 124.128 133.000 1.00 39.00  ? 248 VAL A C     1 
ATOM   1919 O  O     . VAL A 1 260 ? 106.062 123.858 134.130 1.00 42.73  ? 248 VAL A O     1 
ATOM   1920 C  CB    . VAL A 1 260 ? 104.942 124.116 130.982 1.00 40.81  ? 248 VAL A CB    1 
ATOM   1921 C  CG1   . VAL A 1 260 ? 104.275 122.921 131.628 1.00 41.71  ? 248 VAL A CG1   1 
ATOM   1922 C  CG2   . VAL A 1 260 ? 103.914 124.948 130.238 1.00 38.08  ? 248 VAL A CG2   1 
ATOM   1923 N  N     . ILE A 1 261 ? 107.693 123.730 132.579 1.00 40.41  ? 249 ILE A N     1 
ATOM   1924 C  CA    . ILE A 1 261 ? 108.589 122.970 133.456 1.00 39.66  ? 249 ILE A CA    1 
ATOM   1925 C  C     . ILE A 1 261 ? 108.777 123.707 134.772 1.00 39.18  ? 249 ILE A C     1 
ATOM   1926 O  O     . ILE A 1 261 ? 108.611 123.145 135.859 1.00 38.61  ? 249 ILE A O     1 
ATOM   1927 C  CB    . ILE A 1 261 ? 109.954 122.744 132.775 1.00 44.04  ? 249 ILE A CB    1 
ATOM   1928 C  CG1   . ILE A 1 261 ? 109.983 121.472 131.948 1.00 41.62  ? 249 ILE A CG1   1 
ATOM   1929 C  CG2   . ILE A 1 261 ? 111.066 122.639 133.808 1.00 42.67  ? 249 ILE A CG2   1 
ATOM   1930 C  CD1   . ILE A 1 261 ? 111.111 121.439 130.925 1.00 41.92  ? 249 ILE A CD1   1 
ATOM   1931 N  N     . ASN A 1 262 ? 109.103 124.992 134.680 1.00 35.05  ? 250 ASN A N     1 
ATOM   1932 C  CA    . ASN A 1 262 ? 109.524 125.757 135.843 1.00 36.12  ? 250 ASN A CA    1 
ATOM   1933 C  C     . ASN A 1 262 ? 108.354 126.121 136.749 1.00 39.85  ? 250 ASN A C     1 
ATOM   1934 O  O     . ASN A 1 262 ? 108.475 126.058 137.978 1.00 42.73  ? 250 ASN A O     1 
ATOM   1935 C  CB    . ASN A 1 262 ? 110.262 127.001 135.375 1.00 41.80  ? 250 ASN A CB    1 
ATOM   1936 C  CG    . ASN A 1 262 ? 111.458 126.673 134.509 1.00 45.11  ? 250 ASN A CG    1 
ATOM   1937 O  OD1   . ASN A 1 262 ? 111.748 127.372 133.541 1.00 53.00  ? 250 ASN A OD1   1 
ATOM   1938 N  ND2   . ASN A 1 262 ? 112.157 125.600 134.851 1.00 41.12  ? 250 ASN A ND2   1 
ATOM   1939 N  N     . VAL A 1 263 ? 107.217 126.506 136.168 1.00 37.18  ? 251 VAL A N     1 
ATOM   1940 C  CA    . VAL A 1 263 ? 106.034 126.780 136.976 1.00 38.59  ? 251 VAL A CA    1 
ATOM   1941 C  C     . VAL A 1 263 ? 105.564 125.508 137.667 1.00 38.48  ? 251 VAL A C     1 
ATOM   1942 O  O     . VAL A 1 263 ? 105.162 125.533 138.837 1.00 40.01  ? 251 VAL A O     1 
ATOM   1943 C  CB    . VAL A 1 263 ? 104.926 127.408 136.112 1.00 38.57  ? 251 VAL A CB    1 
ATOM   1944 C  CG1   . VAL A 1 263 ? 103.636 127.527 136.903 1.00 34.21  ? 251 VAL A CG1   1 
ATOM   1945 C  CG2   . VAL A 1 263 ? 105.363 128.768 135.611 1.00 41.80  ? 251 VAL A CG2   1 
ATOM   1946 N  N     . SER A 1 264 ? 105.613 124.373 136.962 1.00 35.61  ? 252 SER A N     1 
ATOM   1947 C  CA    . SER A 1 264 ? 105.259 123.106 137.585 1.00 31.79  ? 252 SER A CA    1 
ATOM   1948 C  C     . SER A 1 264 ? 106.219 122.759 138.713 1.00 34.68  ? 252 SER A C     1 
ATOM   1949 O  O     . SER A 1 264 ? 105.800 122.236 139.745 1.00 40.92  ? 252 SER A O     1 
ATOM   1950 C  CB    . SER A 1 264 ? 105.236 121.995 136.538 1.00 38.82  ? 252 SER A CB    1 
ATOM   1951 O  OG    . SER A 1 264 ? 104.431 122.359 135.433 1.00 48.08  ? 252 SER A OG    1 
ATOM   1952 N  N     . SER A 1 265 ? 107.512 123.041 138.537 1.00 31.09  ? 253 SER A N     1 
ATOM   1953 C  CA    . SER A 1 265 ? 108.476 122.770 139.600 1.00 29.12  ? 253 SER A CA    1 
ATOM   1954 C  C     . SER A 1 265 ? 108.205 123.626 140.832 1.00 34.46  ? 253 SER A C     1 
ATOM   1955 O  O     . SER A 1 265 ? 108.262 123.135 141.966 1.00 36.15  ? 253 SER A O     1 
ATOM   1956 C  CB    . SER A 1 265 ? 109.895 123.005 139.091 1.00 28.57  ? 253 SER A CB    1 
ATOM   1957 O  OG    . SER A 1 265 ? 110.182 122.169 137.987 1.00 35.21  ? 253 SER A OG    1 
ATOM   1958 N  N     . VAL A 1 266 ? 107.916 124.913 140.630 1.00 36.32  ? 254 VAL A N     1 
ATOM   1959 C  CA    . VAL A 1 266 ? 107.640 125.795 141.761 1.00 31.06  ? 254 VAL A CA    1 
ATOM   1960 C  C     . VAL A 1 266 ? 106.361 125.372 142.475 1.00 33.69  ? 254 VAL A C     1 
ATOM   1961 O  O     . VAL A 1 266 ? 106.312 125.309 143.712 1.00 38.44  ? 254 VAL A O     1 
ATOM   1962 C  CB    . VAL A 1 266 ? 107.573 127.257 141.288 1.00 32.35  ? 254 VAL A CB    1 
ATOM   1963 C  CG1   . VAL A 1 266 ? 107.123 128.164 142.418 1.00 35.09  ? 254 VAL A CG1   1 
ATOM   1964 C  CG2   . VAL A 1 266 ? 108.922 127.696 140.757 1.00 36.48  ? 254 VAL A CG2   1 
ATOM   1965 N  N     . ALA A 1 267 ? 105.306 125.072 141.712 1.00 32.41  ? 255 ALA A N     1 
ATOM   1966 C  CA    . ALA A 1 267 ? 104.069 124.594 142.318 1.00 37.31  ? 255 ALA A CA    1 
ATOM   1967 C  C     . ALA A 1 267 ? 104.276 123.263 143.021 1.00 36.30  ? 255 ALA A C     1 
ATOM   1968 O  O     . ALA A 1 267 ? 103.655 123.004 144.056 1.00 41.98  ? 255 ALA A O     1 
ATOM   1969 C  CB    . ALA A 1 267 ? 102.975 124.474 141.259 1.00 37.24  ? 255 ALA A CB    1 
ATOM   1970 N  N     . LEU A 1 268 ? 105.138 122.407 142.473 1.00 35.29  ? 256 LEU A N     1 
ATOM   1971 C  CA    . LEU A 1 268 ? 105.467 121.150 143.126 1.00 33.23  ? 256 LEU A CA    1 
ATOM   1972 C  C     . LEU A 1 268 ? 106.117 121.393 144.474 1.00 33.26  ? 256 LEU A C     1 
ATOM   1973 O  O     . LEU A 1 268 ? 105.740 120.778 145.470 1.00 39.21  ? 256 LEU A O     1 
ATOM   1974 C  CB    . LEU A 1 268 ? 106.383 120.319 142.232 1.00 31.33  ? 256 LEU A CB    1 
ATOM   1975 C  CG    . LEU A 1 268 ? 107.308 119.353 142.967 1.00 33.14  ? 256 LEU A CG    1 
ATOM   1976 C  CD1   . LEU A 1 268 ? 106.539 118.140 143.433 1.00 39.60  ? 256 LEU A CD1   1 
ATOM   1977 C  CD2   . LEU A 1 268 ? 108.451 118.952 142.068 1.00 36.68  ? 256 LEU A CD2   1 
ATOM   1978 N  N     . ILE A 1 269 ? 107.091 122.299 144.528 1.00 31.76  ? 257 ILE A N     1 
ATOM   1979 C  CA    . ILE A 1 269 ? 107.728 122.583 145.809 1.00 33.64  ? 257 ILE A CA    1 
ATOM   1980 C  C     . ILE A 1 269 ? 106.703 123.117 146.800 1.00 37.22  ? 257 ILE A C     1 
ATOM   1981 O  O     . ILE A 1 269 ? 106.644 122.668 147.948 1.00 42.00  ? 257 ILE A O     1 
ATOM   1982 C  CB    . ILE A 1 269 ? 108.912 123.550 145.633 1.00 36.91  ? 257 ILE A CB    1 
ATOM   1983 C  CG1   . ILE A 1 269 ? 109.955 122.945 144.697 1.00 34.54  ? 257 ILE A CG1   1 
ATOM   1984 C  CG2   . ILE A 1 269 ? 109.547 123.849 146.978 1.00 32.78  ? 257 ILE A CG2   1 
ATOM   1985 C  CD1   . ILE A 1 269 ? 110.518 121.634 145.177 1.00 35.77  ? 257 ILE A CD1   1 
ATOM   1986 N  N     . TRP A 1 270 ? 105.842 124.037 146.358 1.00 36.75  ? 258 TRP A N     1 
ATOM   1987 C  CA    . TRP A 1 270 ? 104.866 124.638 147.267 1.00 36.26  ? 258 TRP A CA    1 
ATOM   1988 C  C     . TRP A 1 270 ? 103.885 123.600 147.811 1.00 37.33  ? 258 TRP A C     1 
ATOM   1989 O  O     . TRP A 1 270 ? 103.717 123.455 149.030 1.00 39.61  ? 258 TRP A O     1 
ATOM   1990 C  CB    . TRP A 1 270 ? 104.120 125.764 146.550 1.00 37.55  ? 258 TRP A CB    1 
ATOM   1991 C  CG    . TRP A 1 270 ? 103.076 126.436 147.388 1.00 42.28  ? 258 TRP A CG    1 
ATOM   1992 C  CD1   . TRP A 1 270 ? 101.732 126.441 147.171 1.00 40.59  ? 258 TRP A CD1   1 
ATOM   1993 C  CD2   . TRP A 1 270 ? 103.293 127.203 148.578 1.00 40.56  ? 258 TRP A CD2   1 
ATOM   1994 N  NE1   . TRP A 1 270 ? 101.097 127.162 148.150 1.00 37.54  ? 258 TRP A NE1   1 
ATOM   1995 C  CE2   . TRP A 1 270 ? 102.034 127.640 149.027 1.00 36.56  ? 258 TRP A CE2   1 
ATOM   1996 C  CE3   . TRP A 1 270 ? 104.430 127.560 149.307 1.00 40.43  ? 258 TRP A CE3   1 
ATOM   1997 C  CZ2   . TRP A 1 270 ? 101.879 128.415 150.171 1.00 33.18  ? 258 TRP A CZ2   1 
ATOM   1998 C  CZ3   . TRP A 1 270 ? 104.273 128.329 150.442 1.00 42.53  ? 258 TRP A CZ3   1 
ATOM   1999 C  CH2   . TRP A 1 270 ? 103.008 128.749 150.862 1.00 36.83  ? 258 TRP A CH2   1 
ATOM   2000 N  N     . PHE A 1 271 ? 103.241 122.846 146.919 1.00 34.97  ? 259 PHE A N     1 
ATOM   2001 C  CA    . PHE A 1 271 ? 102.197 121.927 147.360 1.00 37.96  ? 259 PHE A CA    1 
ATOM   2002 C  C     . PHE A 1 271 ? 102.786 120.692 148.032 1.00 46.54  ? 259 PHE A C     1 
ATOM   2003 O  O     . PHE A 1 271 ? 102.195 120.152 148.975 1.00 53.52  ? 259 PHE A O     1 
ATOM   2004 C  CB    . PHE A 1 271 ? 101.307 121.545 146.179 1.00 38.31  ? 259 PHE A CB    1 
ATOM   2005 C  CG    . PHE A 1 271 ? 100.428 122.667 145.702 1.00 43.27  ? 259 PHE A CG    1 
ATOM   2006 C  CD1   . PHE A 1 271 ? 99.419  123.165 146.509 1.00 43.33  ? 259 PHE A CD1   1 
ATOM   2007 C  CD2   . PHE A 1 271 ? 100.614 123.232 144.453 1.00 41.27  ? 259 PHE A CD2   1 
ATOM   2008 C  CE1   . PHE A 1 271 ? 98.613  124.199 146.078 1.00 32.17  ? 259 PHE A CE1   1 
ATOM   2009 C  CE2   . PHE A 1 271 ? 99.811  124.266 144.018 1.00 38.09  ? 259 PHE A CE2   1 
ATOM   2010 C  CZ    . PHE A 1 271 ? 98.809  124.749 144.832 1.00 34.50  ? 259 PHE A CZ    1 
ATOM   2011 N  N     . GLY A 1 272 ? 103.954 120.236 147.580 1.00 43.18  ? 260 GLY A N     1 
ATOM   2012 C  CA    . GLY A 1 272 ? 104.633 119.161 148.272 1.00 40.76  ? 260 GLY A CA    1 
ATOM   2013 C  C     . GLY A 1 272 ? 105.086 119.563 149.658 1.00 44.02  ? 260 GLY A C     1 
ATOM   2014 O  O     . GLY A 1 272 ? 105.061 118.753 150.578 1.00 54.09  ? 260 GLY A O     1 
ATOM   2015 N  N     . GLY A 1 273 ? 105.501 120.818 149.832 1.00 43.51  ? 261 GLY A N     1 
ATOM   2016 C  CA    . GLY A 1 273 ? 105.806 121.296 151.168 1.00 45.26  ? 261 GLY A CA    1 
ATOM   2017 C  C     . GLY A 1 273 ? 104.574 121.373 152.046 1.00 46.70  ? 261 GLY A C     1 
ATOM   2018 O  O     . GLY A 1 273 ? 104.631 121.068 153.240 1.00 53.10  ? 261 GLY A O     1 
ATOM   2019 N  N     . LEU A 1 274 ? 103.444 121.782 151.467 1.00 46.40  ? 262 LEU A N     1 
ATOM   2020 C  CA    . LEU A 1 274 ? 102.194 121.766 152.221 1.00 48.71  ? 262 LEU A CA    1 
ATOM   2021 C  C     . LEU A 1 274 ? 101.835 120.351 152.661 1.00 52.98  ? 262 LEU A C     1 
ATOM   2022 O  O     . LEU A 1 274 ? 101.361 120.143 153.783 1.00 58.04  ? 262 LEU A O     1 
ATOM   2023 C  CB    . LEU A 1 274 ? 101.066 122.372 151.387 1.00 44.22  ? 262 LEU A CB    1 
ATOM   2024 C  CG    . LEU A 1 274 ? 101.020 123.899 151.320 1.00 42.63  ? 262 LEU A CG    1 
ATOM   2025 C  CD1   . LEU A 1 274 ? 100.027 124.356 150.272 1.00 37.08  ? 262 LEU A CD1   1 
ATOM   2026 C  CD2   . LEU A 1 274 ? 100.673 124.480 152.677 1.00 45.87  ? 262 LEU A CD2   1 
ATOM   2027 N  N     . ARG A 1 275 ? 102.051 119.366 151.788 1.00 50.01  ? 263 ARG A N     1 
ATOM   2028 C  CA    . ARG A 1 275 ? 101.755 117.979 152.138 1.00 48.43  ? 263 ARG A CA    1 
ATOM   2029 C  C     . ARG A 1 275 ? 102.793 117.378 153.082 1.00 56.33  ? 263 ARG A C     1 
ATOM   2030 O  O     . ARG A 1 275 ? 102.469 116.464 153.846 1.00 63.41  ? 263 ARG A O     1 
ATOM   2031 C  CB    . ARG A 1 275 ? 101.652 117.129 150.872 1.00 51.30  ? 263 ARG A CB    1 
ATOM   2032 C  CG    . ARG A 1 275 ? 100.366 117.336 150.101 1.00 55.38  ? 263 ARG A CG    1 
ATOM   2033 C  CD    . ARG A 1 275 ? 100.325 116.480 148.851 1.00 59.98  ? 263 ARG A CD    1 
ATOM   2034 N  NE    . ARG A 1 275 ? 100.341 115.056 149.160 1.00 66.29  ? 263 ARG A NE    1 
ATOM   2035 C  CZ    . ARG A 1 275 ? 99.288  114.371 149.584 1.00 68.93  ? 263 ARG A CZ    1 
ATOM   2036 N  NH1   . ARG A 1 275 ? 98.114  114.951 149.767 1.00 66.96  ? 263 ARG A NH1   1 
ATOM   2037 N  NH2   . ARG A 1 275 ? 99.415  113.070 149.825 1.00 66.32  ? 263 ARG A NH2   1 
ATOM   2038 N  N     . ILE A 1 276 ? 104.034 117.862 153.033 1.00 54.25  ? 264 ILE A N     1 
ATOM   2039 C  CA    . ILE A 1 276 ? 105.099 117.342 153.884 1.00 50.82  ? 264 ILE A CA    1 
ATOM   2040 C  C     . ILE A 1 276 ? 104.998 117.923 155.288 1.00 54.99  ? 264 ILE A C     1 
ATOM   2041 O  O     . ILE A 1 276 ? 105.380 117.267 156.265 1.00 59.84  ? 264 ILE A O     1 
ATOM   2042 C  CB    . ILE A 1 276 ? 106.467 117.632 153.236 1.00 46.01  ? 264 ILE A CB    1 
ATOM   2043 C  CG1   . ILE A 1 276 ? 106.744 116.650 152.100 1.00 50.47  ? 264 ILE A CG1   1 
ATOM   2044 C  CG2   . ILE A 1 276 ? 107.595 117.546 154.242 1.00 44.60  ? 264 ILE A CG2   1 
ATOM   2045 C  CD1   . ILE A 1 276 ? 107.847 117.105 151.175 1.00 52.03  ? 264 ILE A CD1   1 
ATOM   2046 N  N     . ASP A 1 277 ? 104.478 119.146 155.418 1.00 56.90  ? 265 ASP A N     1 
ATOM   2047 C  CA    . ASP A 1 277 ? 104.202 119.690 156.742 1.00 62.12  ? 265 ASP A CA    1 
ATOM   2048 C  C     . ASP A 1 277 ? 103.267 118.770 157.517 1.00 64.62  ? 265 ASP A C     1 
ATOM   2049 O  O     . ASP A 1 277 ? 103.429 118.580 158.728 1.00 65.81  ? 265 ASP A O     1 
ATOM   2050 C  CB    . ASP A 1 277 ? 103.606 121.092 156.619 1.00 62.79  ? 265 ASP A CB    1 
ATOM   2051 C  CG    . ASP A 1 277 ? 103.418 121.765 157.962 1.00 71.78  ? 265 ASP A CG    1 
ATOM   2052 O  OD1   . ASP A 1 277 ? 104.401 121.850 158.728 1.00 73.59  ? 265 ASP A OD1   1 
ATOM   2053 O  OD2   . ASP A 1 277 ? 102.288 122.209 158.254 1.00 71.32  ? 265 ASP A OD2   1 
ATOM   2054 N  N     . ALA A 1 278 ? 102.288 118.187 156.832 1.00 62.91  ? 266 ALA A N     1 
ATOM   2055 C  CA    . ALA A 1 278 ? 101.499 117.105 157.390 1.00 65.85  ? 266 ALA A CA    1 
ATOM   2056 C  C     . ALA A 1 278 ? 102.189 115.766 157.132 1.00 69.66  ? 266 ALA A C     1 
ATOM   2057 O  O     . ALA A 1 278 ? 103.188 115.677 156.415 1.00 72.02  ? 266 ALA A O     1 
ATOM   2058 C  CB    . ALA A 1 278 ? 100.092 117.108 156.796 1.00 61.54  ? 266 ALA A CB    1 
ATOM   2059 N  N     . GLY A 1 279 ? 101.647 114.710 157.725 1.00 67.07  ? 267 GLY A N     1 
ATOM   2060 C  CA    . GLY A 1 279 ? 102.219 113.392 157.530 1.00 68.32  ? 267 GLY A CA    1 
ATOM   2061 C  C     . GLY A 1 279 ? 101.717 112.713 156.274 1.00 71.82  ? 267 GLY A C     1 
ATOM   2062 O  O     . GLY A 1 279 ? 101.283 111.558 156.317 1.00 81.12  ? 267 GLY A O     1 
ATOM   2063 N  N     . GLN A 1 280 ? 101.772 113.418 155.143 1.00 63.78  ? 268 GLN A N     1 
ATOM   2064 C  CA    . GLN A 1 280 ? 101.200 112.924 153.901 1.00 66.88  ? 268 GLN A CA    1 
ATOM   2065 C  C     . GLN A 1 280 ? 102.221 112.692 152.797 1.00 65.88  ? 268 GLN A C     1 
ATOM   2066 O  O     . GLN A 1 280 ? 101.884 112.052 151.796 1.00 67.36  ? 268 GLN A O     1 
ATOM   2067 C  CB    . GLN A 1 280 ? 100.125 113.896 153.392 1.00 66.20  ? 268 GLN A CB    1 
ATOM   2068 C  CG    . GLN A 1 280 ? 98.942  114.053 154.331 1.00 74.76  ? 268 GLN A CG    1 
ATOM   2069 C  CD    . GLN A 1 280 ? 98.021  115.187 153.927 1.00 82.62  ? 268 GLN A CD    1 
ATOM   2070 O  OE1   . GLN A 1 280 ? 98.174  115.777 152.859 1.00 77.40  ? 268 GLN A OE1   1 
ATOM   2071 N  NE2   . GLN A 1 280 ? 97.056  115.499 154.784 1.00 88.62  ? 268 GLN A NE2   1 
ATOM   2072 N  N     . MET A 1 281 ? 103.448 113.185 152.943 1.00 62.16  ? 269 MET A N     1 
ATOM   2073 C  CA    . MET A 1 281 ? 104.424 113.081 151.871 1.00 55.89  ? 269 MET A CA    1 
ATOM   2074 C  C     . MET A 1 281 ? 105.827 113.081 152.457 1.00 55.57  ? 269 MET A C     1 
ATOM   2075 O  O     . MET A 1 281 ? 106.057 113.592 153.556 1.00 56.83  ? 269 MET A O     1 
ATOM   2076 C  CB    . MET A 1 281 ? 104.255 114.227 150.867 1.00 56.81  ? 269 MET A CB    1 
ATOM   2077 C  CG    . MET A 1 281 ? 104.847 113.963 149.499 1.00 55.58  ? 269 MET A CG    1 
ATOM   2078 S  SD    . MET A 1 281 ? 104.757 115.416 148.442 1.00 63.88  ? 269 MET A SD    1 
ATOM   2079 C  CE    . MET A 1 281 ? 106.480 115.648 148.038 1.00 45.50  ? 269 MET A CE    1 
ATOM   2080 N  N     . GLN A 1 282 ? 106.760 112.500 151.710 1.00 54.90  ? 270 GLN A N     1 
ATOM   2081 C  CA    . GLN A 1 282 ? 108.161 112.436 152.089 1.00 53.93  ? 270 GLN A CA    1 
ATOM   2082 C  C     . GLN A 1 282 ? 108.974 113.394 151.228 1.00 50.55  ? 270 GLN A C     1 
ATOM   2083 O  O     . GLN A 1 282 ? 108.540 113.820 150.155 1.00 55.20  ? 270 GLN A O     1 
ATOM   2084 C  CB    . GLN A 1 282 ? 108.702 111.010 151.953 1.00 61.12  ? 270 GLN A CB    1 
ATOM   2085 C  CG    . GLN A 1 282 ? 107.880 109.969 152.690 1.00 62.76  ? 270 GLN A CG    1 
ATOM   2086 C  CD    . GLN A 1 282 ? 108.438 109.649 154.061 1.00 68.28  ? 270 GLN A CD    1 
ATOM   2087 O  OE1   . GLN A 1 282 ? 108.152 110.342 155.037 1.00 69.23  ? 270 GLN A OE1   1 
ATOM   2088 N  NE2   . GLN A 1 282 ? 109.234 108.591 154.142 1.00 67.70  ? 270 GLN A NE2   1 
ATOM   2089 N  N     . VAL A 1 283 ? 110.169 113.731 151.714 1.00 48.04  ? 271 VAL A N     1 
ATOM   2090 C  CA    . VAL A 1 283 ? 110.963 114.771 151.069 1.00 47.75  ? 271 VAL A CA    1 
ATOM   2091 C  C     . VAL A 1 283 ? 111.503 114.296 149.724 1.00 50.00  ? 271 VAL A C     1 
ATOM   2092 O  O     . VAL A 1 283 ? 111.565 115.070 148.762 1.00 59.75  ? 271 VAL A O     1 
ATOM   2093 C  CB    . VAL A 1 283 ? 112.090 115.239 152.003 1.00 52.00  ? 271 VAL A CB    1 
ATOM   2094 C  CG1   . VAL A 1 283 ? 112.603 116.596 151.560 1.00 48.92  ? 271 VAL A CG1   1 
ATOM   2095 C  CG2   . VAL A 1 283 ? 111.594 115.296 153.434 1.00 46.34  ? 271 VAL A CG2   1 
ATOM   2096 N  N     . GLY A 1 284 ? 111.912 113.028 149.631 1.00 48.16  ? 272 GLY A N     1 
ATOM   2097 C  CA    . GLY A 1 284 ? 112.482 112.518 148.393 1.00 43.91  ? 272 GLY A CA    1 
ATOM   2098 C  C     . GLY A 1 284 ? 111.520 112.521 147.224 1.00 43.69  ? 272 GLY A C     1 
ATOM   2099 O  O     . GLY A 1 284 ? 111.957 112.502 146.064 1.00 46.70  ? 272 GLY A O     1 
ATOM   2100 N  N     . SER A 1 285 ? 110.216 112.543 147.500 1.00 42.42  ? 273 SER A N     1 
ATOM   2101 C  CA    . SER A 1 285 ? 109.243 112.647 146.422 1.00 41.93  ? 273 SER A CA    1 
ATOM   2102 C  C     . SER A 1 285 ? 109.399 113.955 145.661 1.00 43.90  ? 273 SER A C     1 
ATOM   2103 O  O     . SER A 1 285 ? 109.079 114.018 144.472 1.00 47.57  ? 273 SER A O     1 
ATOM   2104 C  CB    . SER A 1 285 ? 107.829 112.509 146.980 1.00 47.65  ? 273 SER A CB    1 
ATOM   2105 O  OG    . SER A 1 285 ? 107.639 111.234 147.562 1.00 48.67  ? 273 SER A OG    1 
ATOM   2106 N  N     . LEU A 1 286 ? 109.900 115.002 146.318 1.00 43.68  ? 274 LEU A N     1 
ATOM   2107 C  CA    . LEU A 1 286 ? 110.179 116.249 145.614 1.00 41.09  ? 274 LEU A CA    1 
ATOM   2108 C  C     . LEU A 1 286 ? 111.263 116.053 144.561 1.00 41.23  ? 274 LEU A C     1 
ATOM   2109 O  O     . LEU A 1 286 ? 111.134 116.524 143.426 1.00 46.75  ? 274 LEU A O     1 
ATOM   2110 C  CB    . LEU A 1 286 ? 110.581 117.338 146.607 1.00 40.20  ? 274 LEU A CB    1 
ATOM   2111 C  CG    . LEU A 1 286 ? 109.473 117.865 147.519 1.00 38.97  ? 274 LEU A CG    1 
ATOM   2112 C  CD1   . LEU A 1 286 ? 110.029 118.880 148.498 1.00 38.37  ? 274 LEU A CD1   1 
ATOM   2113 C  CD2   . LEU A 1 286 ? 108.358 118.471 146.696 1.00 42.30  ? 274 LEU A CD2   1 
ATOM   2114 N  N     . ILE A 1 287 ? 112.340 115.352 144.921 1.00 36.04  ? 275 ILE A N     1 
ATOM   2115 C  CA    . ILE A 1 287 ? 113.399 115.049 143.961 1.00 37.15  ? 275 ILE A CA    1 
ATOM   2116 C  C     . ILE A 1 287 ? 112.848 114.207 142.818 1.00 38.17  ? 275 ILE A C     1 
ATOM   2117 O  O     . ILE A 1 287 ? 113.121 114.464 141.635 1.00 42.16  ? 275 ILE A O     1 
ATOM   2118 C  CB    . ILE A 1 287 ? 114.569 114.341 144.669 1.00 39.92  ? 275 ILE A CB    1 
ATOM   2119 C  CG1   . ILE A 1 287 ? 115.370 115.334 145.508 1.00 43.30  ? 275 ILE A CG1   1 
ATOM   2120 C  CG2   . ILE A 1 287 ? 115.464 113.631 143.667 1.00 37.86  ? 275 ILE A CG2   1 
ATOM   2121 C  CD1   . ILE A 1 287 ? 116.198 114.686 146.586 1.00 41.82  ? 275 ILE A CD1   1 
ATOM   2122 N  N     . ALA A 1 288 ? 112.053 113.192 143.162 1.00 37.19  ? 276 ALA A N     1 
ATOM   2123 C  CA    . ALA A 1 288 ? 111.476 112.323 142.142 1.00 30.13  ? 276 ALA A CA    1 
ATOM   2124 C  C     . ALA A 1 288 ? 110.618 113.116 141.162 1.00 31.87  ? 276 ALA A C     1 
ATOM   2125 O  O     . ALA A 1 288 ? 110.738 112.956 139.944 1.00 35.66  ? 276 ALA A O     1 
ATOM   2126 C  CB    . ALA A 1 288 ? 110.657 111.216 142.802 1.00 31.66  ? 276 ALA A CB    1 
ATOM   2127 N  N     . PHE A 1 289 ? 109.762 113.999 141.678 1.00 34.93  ? 277 PHE A N     1 
ATOM   2128 C  CA    . PHE A 1 289 ? 108.857 114.751 140.817 1.00 29.68  ? 277 PHE A CA    1 
ATOM   2129 C  C     . PHE A 1 289 ? 109.601 115.790 139.989 1.00 29.71  ? 277 PHE A C     1 
ATOM   2130 O  O     . PHE A 1 289 ? 109.240 116.043 138.833 1.00 33.41  ? 277 PHE A O     1 
ATOM   2131 C  CB    . PHE A 1 289 ? 107.772 115.417 141.656 1.00 30.89  ? 277 PHE A CB    1 
ATOM   2132 C  CG    . PHE A 1 289 ? 106.561 114.563 141.873 1.00 36.06  ? 277 PHE A CG    1 
ATOM   2133 C  CD1   . PHE A 1 289 ? 106.616 113.453 142.692 1.00 39.13  ? 277 PHE A CD1   1 
ATOM   2134 C  CD2   . PHE A 1 289 ? 105.364 114.875 141.259 1.00 39.39  ? 277 PHE A CD2   1 
ATOM   2135 C  CE1   . PHE A 1 289 ? 105.503 112.670 142.893 1.00 45.96  ? 277 PHE A CE1   1 
ATOM   2136 C  CE2   . PHE A 1 289 ? 104.248 114.095 141.455 1.00 43.75  ? 277 PHE A CE2   1 
ATOM   2137 C  CZ    . PHE A 1 289 ? 104.318 112.991 142.274 1.00 46.10  ? 277 PHE A CZ    1 
ATOM   2138 N  N     . LEU A 1 290 ? 110.630 116.416 140.565 1.00 29.07  ? 278 LEU A N     1 
ATOM   2139 C  CA    . LEU A 1 290 ? 111.439 117.349 139.792 1.00 27.55  ? 278 LEU A CA    1 
ATOM   2140 C  C     . LEU A 1 290 ? 112.083 116.647 138.608 1.00 32.14  ? 278 LEU A C     1 
ATOM   2141 O  O     . LEU A 1 290 ? 112.078 117.166 137.484 1.00 34.48  ? 278 LEU A O     1 
ATOM   2142 C  CB    . LEU A 1 290 ? 112.507 117.983 140.681 1.00 25.91  ? 278 LEU A CB    1 
ATOM   2143 C  CG    . LEU A 1 290 ? 112.054 119.068 141.657 1.00 30.38  ? 278 LEU A CG    1 
ATOM   2144 C  CD1   . LEU A 1 290 ? 113.129 119.334 142.691 1.00 32.92  ? 278 LEU A CD1   1 
ATOM   2145 C  CD2   . LEU A 1 290 ? 111.690 120.341 140.922 1.00 31.86  ? 278 LEU A CD2   1 
ATOM   2146 N  N     . ALA A 1 291 ? 112.624 115.450 138.838 1.00 32.99  ? 279 ALA A N     1 
ATOM   2147 C  CA    . ALA A 1 291 ? 113.195 114.695 137.733 1.00 27.10  ? 279 ALA A CA    1 
ATOM   2148 C  C     . ALA A 1 291 ? 112.130 114.251 136.739 1.00 29.73  ? 279 ALA A C     1 
ATOM   2149 O  O     . ALA A 1 291 ? 112.394 114.208 135.533 1.00 34.78  ? 279 ALA A O     1 
ATOM   2150 C  CB    . ALA A 1 291 ? 113.965 113.497 138.267 1.00 27.86  ? 279 ALA A CB    1 
ATOM   2151 N  N     . TYR A 1 292 ? 110.926 113.927 137.216 1.00 30.28  ? 280 TYR A N     1 
ATOM   2152 C  CA    . TYR A 1 292 ? 109.844 113.559 136.305 1.00 25.06  ? 280 TYR A CA    1 
ATOM   2153 C  C     . TYR A 1 292 ? 109.508 114.707 135.363 1.00 27.80  ? 280 TYR A C     1 
ATOM   2154 O  O     . TYR A 1 292 ? 109.345 114.505 134.157 1.00 34.26  ? 280 TYR A O     1 
ATOM   2155 C  CB    . TYR A 1 292 ? 108.603 113.138 137.092 1.00 24.91  ? 280 TYR A CB    1 
ATOM   2156 C  CG    . TYR A 1 292 ? 108.783 111.887 137.916 1.00 30.26  ? 280 TYR A CG    1 
ATOM   2157 C  CD1   . TYR A 1 292 ? 109.767 110.964 137.606 1.00 27.48  ? 280 TYR A CD1   1 
ATOM   2158 C  CD2   . TYR A 1 292 ? 107.971 111.635 139.012 1.00 32.36  ? 280 TYR A CD2   1 
ATOM   2159 C  CE1   . TYR A 1 292 ? 109.937 109.825 138.360 1.00 28.38  ? 280 TYR A CE1   1 
ATOM   2160 C  CE2   . TYR A 1 292 ? 108.136 110.500 139.774 1.00 32.75  ? 280 TYR A CE2   1 
ATOM   2161 C  CZ    . TYR A 1 292 ? 109.119 109.598 139.442 1.00 35.12  ? 280 TYR A CZ    1 
ATOM   2162 O  OH    . TYR A 1 292 ? 109.287 108.462 140.195 1.00 42.06  ? 280 TYR A OH    1 
ATOM   2163 N  N     . PHE A 1 293 ? 109.394 115.923 135.901 1.00 28.69  ? 281 PHE A N     1 
ATOM   2164 C  CA    . PHE A 1 293 ? 109.150 117.089 135.053 1.00 27.62  ? 281 PHE A CA    1 
ATOM   2165 C  C     . PHE A 1 293 ? 110.292 117.285 134.064 1.00 32.22  ? 281 PHE A C     1 
ATOM   2166 O  O     . PHE A 1 293 ? 110.074 117.420 132.849 1.00 38.25  ? 281 PHE A O     1 
ATOM   2167 C  CB    . PHE A 1 293 ? 108.988 118.346 135.909 1.00 26.80  ? 281 PHE A CB    1 
ATOM   2168 C  CG    . PHE A 1 293 ? 107.697 118.416 136.666 1.00 29.48  ? 281 PHE A CG    1 
ATOM   2169 C  CD1   . PHE A 1 293 ? 106.484 118.314 136.016 1.00 34.74  ? 281 PHE A CD1   1 
ATOM   2170 C  CD2   . PHE A 1 293 ? 107.701 118.617 138.034 1.00 30.21  ? 281 PHE A CD2   1 
ATOM   2171 C  CE1   . PHE A 1 293 ? 105.300 118.393 136.722 1.00 37.47  ? 281 PHE A CE1   1 
ATOM   2172 C  CE2   . PHE A 1 293 ? 106.522 118.692 138.742 1.00 31.11  ? 281 PHE A CE2   1 
ATOM   2173 C  CZ    . PHE A 1 293 ? 105.321 118.578 138.085 1.00 33.96  ? 281 PHE A CZ    1 
ATOM   2174 N  N     . MET A 1 294 ? 111.528 117.292 134.578 1.00 33.14  ? 282 MET A N     1 
ATOM   2175 C  CA    . MET A 1 294 ? 112.704 117.546 133.757 1.00 34.05  ? 282 MET A CA    1 
ATOM   2176 C  C     . MET A 1 294 ? 112.896 116.498 132.676 1.00 38.41  ? 282 MET A C     1 
ATOM   2177 O  O     . MET A 1 294 ? 113.590 116.763 131.692 1.00 47.98  ? 282 MET A O     1 
ATOM   2178 C  CB    . MET A 1 294 ? 113.950 117.600 134.637 1.00 39.66  ? 282 MET A CB    1 
ATOM   2179 C  CG    . MET A 1 294 ? 114.567 118.977 134.776 1.00 54.13  ? 282 MET A CG    1 
ATOM   2180 S  SD    . MET A 1 294 ? 116.141 118.920 135.652 1.00 75.97  ? 282 MET A SD    1 
ATOM   2181 C  CE    . MET A 1 294 ? 115.677 117.993 137.113 1.00 40.91  ? 282 MET A CE    1 
ATOM   2182 N  N     . GLN A 1 295 ? 112.326 115.309 132.844 1.00 36.97  ? 283 GLN A N     1 
ATOM   2183 C  CA    . GLN A 1 295 ? 112.421 114.289 131.811 1.00 32.45  ? 283 GLN A CA    1 
ATOM   2184 C  C     . GLN A 1 295 ? 111.261 114.365 130.829 1.00 35.71  ? 283 GLN A C     1 
ATOM   2185 O  O     . GLN A 1 295 ? 111.477 114.359 129.613 1.00 41.74  ? 283 GLN A O     1 
ATOM   2186 C  CB    . GLN A 1 295 ? 112.484 112.903 132.450 1.00 31.81  ? 283 GLN A CB    1 
ATOM   2187 C  CG    . GLN A 1 295 ? 113.808 112.596 133.108 1.00 31.05  ? 283 GLN A CG    1 
ATOM   2188 C  CD    . GLN A 1 295 ? 113.964 111.132 133.425 1.00 33.03  ? 283 GLN A CD    1 
ATOM   2189 O  OE1   . GLN A 1 295 ? 113.673 110.692 134.535 1.00 32.53  ? 283 GLN A OE1   1 
ATOM   2190 N  NE2   . GLN A 1 295 ? 114.426 110.363 132.449 1.00 33.49  ? 283 GLN A NE2   1 
ATOM   2191 N  N     . ILE A 1 296 ? 110.029 114.448 131.340 1.00 36.48  ? 284 ILE A N     1 
ATOM   2192 C  CA    . ILE A 1 296 ? 108.856 114.451 130.472 1.00 39.58  ? 284 ILE A CA    1 
ATOM   2193 C  C     . ILE A 1 296 ? 108.915 115.623 129.508 1.00 45.53  ? 284 ILE A C     1 
ATOM   2194 O  O     . ILE A 1 296 ? 108.812 115.459 128.283 1.00 54.07  ? 284 ILE A O     1 
ATOM   2195 C  CB    . ILE A 1 296 ? 107.566 114.499 131.310 1.00 39.09  ? 284 ILE A CB    1 
ATOM   2196 C  CG1   . ILE A 1 296 ? 107.351 113.199 132.076 1.00 41.19  ? 284 ILE A CG1   1 
ATOM   2197 C  CG2   . ILE A 1 296 ? 106.371 114.777 130.427 1.00 43.96  ? 284 ILE A CG2   1 
ATOM   2198 C  CD1   . ILE A 1 296 ? 106.310 113.327 133.155 1.00 38.98  ? 284 ILE A CD1   1 
ATOM   2199 N  N     . LEU A 1 297 ? 109.103 116.827 130.036 1.00 44.48  ? 285 LEU A N     1 
ATOM   2200 C  CA    . LEU A 1 297 ? 108.991 117.962 129.140 1.00 48.86  ? 285 LEU A CA    1 
ATOM   2201 C  C     . LEU A 1 297 ? 110.269 118.204 128.347 1.00 48.49  ? 285 LEU A C     1 
ATOM   2202 O  O     . LEU A 1 297 ? 110.207 118.820 127.280 1.00 58.26  ? 285 LEU A O     1 
ATOM   2203 C  CB    . LEU A 1 297 ? 108.551 119.195 129.926 1.00 56.77  ? 285 LEU A CB    1 
ATOM   2204 C  CG    . LEU A 1 297 ? 107.332 118.921 130.824 1.00 56.86  ? 285 LEU A CG    1 
ATOM   2205 C  CD1   . LEU A 1 297 ? 106.846 120.161 131.558 1.00 47.21  ? 285 LEU A CD1   1 
ATOM   2206 C  CD2   . LEU A 1 297 ? 106.195 118.306 130.023 1.00 53.74  ? 285 LEU A CD2   1 
ATOM   2207 N  N     . MET A 1 298 ? 111.412 117.681 128.796 1.00 44.82  ? 286 MET A N     1 
ATOM   2208 C  CA    . MET A 1 298 ? 112.592 117.674 127.935 1.00 48.08  ? 286 MET A CA    1 
ATOM   2209 C  C     . MET A 1 298 ? 112.403 116.738 126.746 1.00 52.69  ? 286 MET A C     1 
ATOM   2210 O  O     . MET A 1 298 ? 112.825 117.053 125.628 1.00 52.66  ? 286 MET A O     1 
ATOM   2211 C  CB    . MET A 1 298 ? 113.834 117.280 128.730 1.00 51.26  ? 286 MET A CB    1 
ATOM   2212 C  CG    . MET A 1 298 ? 115.021 116.873 127.876 1.00 55.33  ? 286 MET A CG    1 
ATOM   2213 S  SD    . MET A 1 298 ? 115.397 115.116 127.993 1.00 73.66  ? 286 MET A SD    1 
ATOM   2214 C  CE    . MET A 1 298 ? 116.928 115.036 127.067 1.00 72.00  ? 286 MET A CE    1 
ATOM   2215 N  N     . ALA A 1 299 ? 111.774 115.580 126.964 1.00 53.65  ? 287 ALA A N     1 
ATOM   2216 C  CA    . ALA A 1 299 ? 111.444 114.705 125.844 1.00 45.52  ? 287 ALA A CA    1 
ATOM   2217 C  C     . ALA A 1 299 ? 110.469 115.382 124.892 1.00 51.96  ? 287 ALA A C     1 
ATOM   2218 O  O     . ALA A 1 299 ? 110.598 115.265 123.667 1.00 63.08  ? 287 ALA A O     1 
ATOM   2219 C  CB    . ALA A 1 299 ? 110.865 113.389 126.358 1.00 46.82  ? 287 ALA A CB    1 
ATOM   2220 N  N     . VAL A 1 300 ? 109.482 116.093 125.441 1.00 54.40  ? 288 VAL A N     1 
ATOM   2221 C  CA    . VAL A 1 300 ? 108.551 116.843 124.599 1.00 56.54  ? 288 VAL A CA    1 
ATOM   2222 C  C     . VAL A 1 300 ? 109.295 117.896 123.783 1.00 54.69  ? 288 VAL A C     1 
ATOM   2223 O  O     . VAL A 1 300 ? 109.032 118.081 122.587 1.00 56.06  ? 288 VAL A O     1 
ATOM   2224 C  CB    . VAL A 1 300 ? 107.440 117.470 125.461 1.00 53.88  ? 288 VAL A CB    1 
ATOM   2225 C  CG1   . VAL A 1 300 ? 106.683 118.522 124.674 1.00 51.46  ? 288 VAL A CG1   1 
ATOM   2226 C  CG2   . VAL A 1 300 ? 106.493 116.393 125.957 1.00 53.56  ? 288 VAL A CG2   1 
ATOM   2227 N  N     . LEU A 1 301 ? 110.236 118.597 124.416 1.00 54.35  ? 289 LEU A N     1 
ATOM   2228 C  CA    . LEU A 1 301 ? 111.024 119.606 123.717 1.00 53.59  ? 289 LEU A CA    1 
ATOM   2229 C  C     . LEU A 1 301 ? 111.858 118.986 122.604 1.00 61.99  ? 289 LEU A C     1 
ATOM   2230 O  O     . LEU A 1 301 ? 111.992 119.563 121.519 1.00 68.90  ? 289 LEU A O     1 
ATOM   2231 C  CB    . LEU A 1 301 ? 111.919 120.334 124.716 1.00 48.86  ? 289 LEU A CB    1 
ATOM   2232 C  CG    . LEU A 1 301 ? 112.632 121.585 124.227 1.00 51.13  ? 289 LEU A CG    1 
ATOM   2233 C  CD1   . LEU A 1 301 ? 111.618 122.533 123.630 1.00 53.10  ? 289 LEU A CD1   1 
ATOM   2234 C  CD2   . LEU A 1 301 ? 113.374 122.236 125.377 1.00 49.39  ? 289 LEU A CD2   1 
ATOM   2235 N  N     . MET A 1 302 ? 112.446 117.818 122.864 1.00 64.64  ? 290 MET A N     1 
ATOM   2236 C  CA    . MET A 1 302 ? 113.209 117.122 121.833 1.00 65.17  ? 290 MET A CA    1 
ATOM   2237 C  C     . MET A 1 302 ? 112.324 116.740 120.656 1.00 63.12  ? 290 MET A C     1 
ATOM   2238 O  O     . MET A 1 302 ? 112.697 116.941 119.495 1.00 65.78  ? 290 MET A O     1 
ATOM   2239 C  CB    . MET A 1 302 ? 113.870 115.880 122.429 1.00 69.31  ? 290 MET A CB    1 
ATOM   2240 C  CG    . MET A 1 302 ? 114.400 114.899 121.404 1.00 74.76  ? 290 MET A CG    1 
ATOM   2241 S  SD    . MET A 1 302 ? 114.392 113.203 122.015 1.00 100.95 ? 290 MET A SD    1 
ATOM   2242 C  CE    . MET A 1 302 ? 115.248 113.394 123.577 1.00 89.74  ? 290 MET A CE    1 
ATOM   2243 N  N     . ALA A 1 303 ? 111.139 116.198 120.936 1.00 63.91  ? 291 ALA A N     1 
ATOM   2244 C  CA    . ALA A 1 303 ? 110.245 115.781 119.864 1.00 62.61  ? 291 ALA A CA    1 
ATOM   2245 C  C     . ALA A 1 303 ? 109.654 116.959 119.103 1.00 65.18  ? 291 ALA A C     1 
ATOM   2246 O  O     . ALA A 1 303 ? 109.249 116.791 117.949 1.00 72.80  ? 291 ALA A O     1 
ATOM   2247 C  CB    . ALA A 1 303 ? 109.116 114.917 120.424 1.00 58.21  ? 291 ALA A CB    1 
ATOM   2248 N  N     . THR A 1 304 ? 109.579 118.137 119.721 1.00 64.79  ? 292 THR A N     1 
ATOM   2249 C  CA    . THR A 1 304 ? 108.919 119.259 119.064 1.00 61.30  ? 292 THR A CA    1 
ATOM   2250 C  C     . THR A 1 304 ? 109.838 119.997 118.098 1.00 61.11  ? 292 THR A C     1 
ATOM   2251 O  O     . THR A 1 304 ? 109.358 120.786 117.278 1.00 63.25  ? 292 THR A O     1 
ATOM   2252 C  CB    . THR A 1 304 ? 108.370 120.228 120.113 1.00 61.10  ? 292 THR A CB    1 
ATOM   2253 O  OG1   . THR A 1 304 ? 107.156 120.811 119.629 1.00 64.53  ? 292 THR A OG1   1 
ATOM   2254 C  CG2   . THR A 1 304 ? 109.381 121.338 120.437 1.00 57.70  ? 292 THR A CG2   1 
ATOM   2255 N  N     . PHE A 1 305 ? 111.148 119.756 118.169 1.00 68.97  ? 293 PHE A N     1 
ATOM   2256 C  CA    . PHE A 1 305 ? 112.078 120.542 117.363 1.00 70.41  ? 293 PHE A CA    1 
ATOM   2257 C  C     . PHE A 1 305 ? 112.124 120.063 115.918 1.00 71.51  ? 293 PHE A C     1 
ATOM   2258 O  O     . PHE A 1 305 ? 112.371 120.861 115.006 1.00 75.08  ? 293 PHE A O     1 
ATOM   2259 C  CB    . PHE A 1 305 ? 113.473 120.510 117.978 1.00 71.19  ? 293 PHE A CB    1 
ATOM   2260 C  CG    . PHE A 1 305 ? 113.830 121.765 118.713 1.00 76.05  ? 293 PHE A CG    1 
ATOM   2261 C  CD1   . PHE A 1 305 ? 114.205 121.722 120.046 1.00 71.08  ? 293 PHE A CD1   1 
ATOM   2262 C  CD2   . PHE A 1 305 ? 113.769 122.996 118.078 1.00 76.96  ? 293 PHE A CD2   1 
ATOM   2263 C  CE1   . PHE A 1 305 ? 114.526 122.880 120.723 1.00 67.29  ? 293 PHE A CE1   1 
ATOM   2264 C  CE2   . PHE A 1 305 ? 114.081 124.157 118.753 1.00 79.57  ? 293 PHE A CE2   1 
ATOM   2265 C  CZ    . PHE A 1 305 ? 114.460 124.099 120.075 1.00 72.12  ? 293 PHE A CZ    1 
ATOM   2266 N  N     . MET A 1 306 ? 111.913 118.771 115.684 1.00 68.66  ? 294 MET A N     1 
ATOM   2267 C  CA    . MET A 1 306 ? 112.006 118.205 114.338 1.00 65.12  ? 294 MET A CA    1 
ATOM   2268 C  C     . MET A 1 306 ? 110.648 118.086 113.662 1.00 62.89  ? 294 MET A C     1 
ATOM   2269 O  O     . MET A 1 306 ? 110.410 117.154 112.893 1.00 63.32  ? 294 MET A O     1 
ATOM   2270 C  CB    . MET A 1 306 ? 112.705 116.850 114.394 1.00 63.52  ? 294 MET A CB    1 
ATOM   2271 C  CG    . MET A 1 306 ? 112.479 116.078 115.682 1.00 67.13  ? 294 MET A CG    1 
ATOM   2272 S  SD    . MET A 1 306 ? 113.846 114.954 116.032 1.00 91.81  ? 294 MET A SD    1 
ATOM   2273 C  CE    . MET A 1 306 ? 114.797 115.923 117.201 1.00 78.91  ? 294 MET A CE    1 
ATOM   2274 N  N     . LEU A 1 307 ? 109.736 119.018 113.930 1.00 64.21  ? 295 LEU A N     1 
ATOM   2275 C  CA    . LEU A 1 307 ? 108.388 118.957 113.378 1.00 62.96  ? 295 LEU A CA    1 
ATOM   2276 C  C     . LEU A 1 307 ? 108.297 119.478 111.950 1.00 55.44  ? 295 LEU A C     1 
ATOM   2277 O  O     . LEU A 1 307 ? 107.236 119.352 111.331 1.00 53.79  ? 295 LEU A O     1 
ATOM   2278 C  CB    . LEU A 1 307 ? 107.429 119.738 114.275 1.00 68.84  ? 295 LEU A CB    1 
ATOM   2279 C  CG    . LEU A 1 307 ? 106.645 118.879 115.266 1.00 65.72  ? 295 LEU A CG    1 
ATOM   2280 C  CD1   . LEU A 1 307 ? 105.665 119.736 116.025 1.00 57.08  ? 295 LEU A CD1   1 
ATOM   2281 C  CD2   . LEU A 1 307 ? 105.926 117.745 114.552 1.00 59.00  ? 295 LEU A CD2   1 
ATOM   2282 N  N     . VAL A 1 308 ? 109.370 120.065 111.415 1.00 56.93  ? 296 VAL A N     1 
ATOM   2283 C  CA    . VAL A 1 308 ? 109.371 120.488 110.021 1.00 53.73  ? 296 VAL A CA    1 
ATOM   2284 C  C     . VAL A 1 308 ? 109.307 119.295 109.076 1.00 54.04  ? 296 VAL A C     1 
ATOM   2285 O  O     . VAL A 1 308 ? 108.857 119.435 107.933 1.00 57.06  ? 296 VAL A O     1 
ATOM   2286 C  CB    . VAL A 1 308 ? 110.613 121.356 109.734 1.00 59.40  ? 296 VAL A CB    1 
ATOM   2287 C  CG1   . VAL A 1 308 ? 111.885 120.527 109.829 1.00 57.21  ? 296 VAL A CG1   1 
ATOM   2288 C  CG2   . VAL A 1 308 ? 110.506 122.026 108.373 1.00 55.73  ? 296 VAL A CG2   1 
ATOM   2289 N  N     . ILE A 1 309 ? 109.731 118.113 109.530 1.00 50.85  ? 297 ILE A N     1 
ATOM   2290 C  CA    . ILE A 1 309 ? 109.803 116.956 108.650 1.00 50.64  ? 297 ILE A CA    1 
ATOM   2291 C  C     . ILE A 1 309 ? 108.430 116.411 108.289 1.00 47.27  ? 297 ILE A C     1 
ATOM   2292 O  O     . ILE A 1 309 ? 108.324 115.585 107.377 1.00 52.81  ? 297 ILE A O     1 
ATOM   2293 C  CB    . ILE A 1 309 ? 110.655 115.845 109.290 1.00 49.04  ? 297 ILE A CB    1 
ATOM   2294 C  CG1   . ILE A 1 309 ? 109.854 115.131 110.380 1.00 47.14  ? 297 ILE A CG1   1 
ATOM   2295 C  CG2   . ILE A 1 309 ? 111.948 116.418 109.844 1.00 45.28  ? 297 ILE A CG2   1 
ATOM   2296 C  CD1   . ILE A 1 309 ? 110.638 114.099 111.142 1.00 45.79  ? 297 ILE A CD1   1 
ATOM   2297 N  N     . PHE A 1 310 ? 107.375 116.829 108.979 1.00 46.46  ? 298 PHE A N     1 
ATOM   2298 C  CA    . PHE A 1 310 ? 106.066 116.247 108.705 1.00 44.87  ? 298 PHE A CA    1 
ATOM   2299 C  C     . PHE A 1 310 ? 105.405 116.825 107.453 1.00 45.27  ? 298 PHE A C     1 
ATOM   2300 O  O     . PHE A 1 310 ? 104.988 116.048 106.587 1.00 47.50  ? 298 PHE A O     1 
ATOM   2301 C  CB    . PHE A 1 310 ? 105.144 116.390 109.918 1.00 46.28  ? 298 PHE A CB    1 
ATOM   2302 C  CG    . PHE A 1 310 ? 103.997 115.429 109.907 1.00 49.66  ? 298 PHE A CG    1 
ATOM   2303 C  CD1   . PHE A 1 310 ? 104.075 114.232 110.596 1.00 46.22  ? 298 PHE A CD1   1 
ATOM   2304 C  CD2   . PHE A 1 310 ? 102.843 115.718 109.199 1.00 50.41  ? 298 PHE A CD2   1 
ATOM   2305 C  CE1   . PHE A 1 310 ? 103.024 113.344 110.578 1.00 52.92  ? 298 PHE A CE1   1 
ATOM   2306 C  CE2   . PHE A 1 310 ? 101.791 114.835 109.179 1.00 50.58  ? 298 PHE A CE2   1 
ATOM   2307 C  CZ    . PHE A 1 310 ? 101.880 113.647 109.870 1.00 58.60  ? 298 PHE A CZ    1 
ATOM   2308 N  N     . PRO A 1 311 ? 105.249 118.148 107.311 1.00 45.79  ? 299 PRO A N     1 
ATOM   2309 C  CA    . PRO A 1 311 ? 104.681 118.665 106.053 1.00 43.65  ? 299 PRO A CA    1 
ATOM   2310 C  C     . PRO A 1 311 ? 105.539 118.365 104.836 1.00 45.57  ? 299 PRO A C     1 
ATOM   2311 O  O     . PRO A 1 311 ? 105.001 118.143 103.740 1.00 44.80  ? 299 PRO A O     1 
ATOM   2312 C  CB    . PRO A 1 311 ? 104.570 120.172 106.314 1.00 47.86  ? 299 PRO A CB    1 
ATOM   2313 C  CG    . PRO A 1 311 ? 105.590 120.442 107.341 1.00 45.78  ? 299 PRO A CG    1 
ATOM   2314 C  CD    . PRO A 1 311 ? 105.596 119.249 108.229 1.00 48.02  ? 299 PRO A CD    1 
ATOM   2315 N  N     . ARG A 1 312 ? 106.863 118.355 104.997 1.00 47.85  ? 300 ARG A N     1 
ATOM   2316 C  CA    . ARG A 1 312 ? 107.744 117.962 103.904 1.00 47.24  ? 300 ARG A CA    1 
ATOM   2317 C  C     . ARG A 1 312 ? 107.475 116.524 103.482 1.00 44.16  ? 300 ARG A C     1 
ATOM   2318 O  O     . ARG A 1 312 ? 107.369 116.221 102.288 1.00 46.57  ? 300 ARG A O     1 
ATOM   2319 C  CB    . ARG A 1 312 ? 109.202 118.145 104.327 1.00 43.05  ? 300 ARG A CB    1 
ATOM   2320 C  CG    . ARG A 1 312 ? 110.213 117.577 103.359 1.00 48.45  ? 300 ARG A CG    1 
ATOM   2321 C  CD    . ARG A 1 312 ? 111.515 118.349 103.423 1.00 55.57  ? 300 ARG A CD    1 
ATOM   2322 N  NE    . ARG A 1 312 ? 111.958 118.575 104.794 1.00 62.99  ? 300 ARG A NE    1 
ATOM   2323 C  CZ    . ARG A 1 312 ? 112.718 117.737 105.487 1.00 66.25  ? 300 ARG A CZ    1 
ATOM   2324 N  NH1   . ARG A 1 312 ? 113.149 116.602 104.966 1.00 58.98  ? 300 ARG A NH1   1 
ATOM   2325 N  NH2   . ARG A 1 312 ? 113.057 118.050 106.734 1.00 64.50  ? 300 ARG A NH2   1 
ATOM   2326 N  N     . ALA A 1 313 ? 107.342 115.625 104.458 1.00 38.78  ? 301 ALA A N     1 
ATOM   2327 C  CA    . ALA A 1 313 ? 107.017 114.241 104.143 1.00 36.62  ? 301 ALA A CA    1 
ATOM   2328 C  C     . ALA A 1 313 ? 105.643 114.134 103.501 1.00 40.31  ? 301 ALA A C     1 
ATOM   2329 O  O     . ALA A 1 313 ? 105.433 113.305 102.614 1.00 46.14  ? 301 ALA A O     1 
ATOM   2330 C  CB    . ALA A 1 313 ? 107.093 113.379 105.402 1.00 37.68  ? 301 ALA A CB    1 
ATOM   2331 N  N     . ALA A 1 314 ? 104.695 114.969 103.929 1.00 40.98  ? 302 ALA A N     1 
ATOM   2332 C  CA    . ALA A 1 314 ? 103.352 114.922 103.356 1.00 38.04  ? 302 ALA A CA    1 
ATOM   2333 C  C     . ALA A 1 314 ? 103.352 115.332 101.888 1.00 41.25  ? 302 ALA A C     1 
ATOM   2334 O  O     . ALA A 1 314 ? 102.715 114.675 101.057 1.00 45.01  ? 302 ALA A O     1 
ATOM   2335 C  CB    . ALA A 1 314 ? 102.406 115.808 104.163 1.00 37.40  ? 302 ALA A CB    1 
ATOM   2336 N  N     . VAL A 1 315 ? 104.062 116.408 101.541 1.00 41.07  ? 303 VAL A N     1 
ATOM   2337 C  CA    . VAL A 1 315 ? 104.092 116.830 100.141 1.00 43.53  ? 303 VAL A CA    1 
ATOM   2338 C  C     . VAL A 1 315 ? 104.894 115.843 99.294  1.00 44.09  ? 303 VAL A C     1 
ATOM   2339 O  O     . VAL A 1 315 ? 104.521 115.536 98.149  1.00 44.20  ? 303 VAL A O     1 
ATOM   2340 C  CB    . VAL A 1 315 ? 104.621 118.272 100.009 1.00 49.47  ? 303 VAL A CB    1 
ATOM   2341 C  CG1   . VAL A 1 315 ? 103.698 119.239 100.729 1.00 49.86  ? 303 VAL A CG1   1 
ATOM   2342 C  CG2   . VAL A 1 315 ? 106.040 118.398 100.534 1.00 48.89  ? 303 VAL A CG2   1 
ATOM   2343 N  N     . CYS A 1 316 ? 105.998 115.319 99.837  1.00 41.72  ? 304 CYS A N     1 
ATOM   2344 C  CA    . CYS A 1 316 ? 106.767 114.316 99.110  1.00 36.85  ? 304 CYS A CA    1 
ATOM   2345 C  C     . CYS A 1 316 ? 105.941 113.058 98.879  1.00 38.69  ? 304 CYS A C     1 
ATOM   2346 O  O     . CYS A 1 316 ? 106.021 112.437 97.814  1.00 48.08  ? 304 CYS A O     1 
ATOM   2347 C  CB    . CYS A 1 316 ? 108.051 113.992 99.870  1.00 40.03  ? 304 CYS A CB    1 
ATOM   2348 S  SG    . CYS A 1 316 ? 109.305 115.293 99.816  1.00 39.89  ? 304 CYS A SG    1 
ATOM   2349 N  N     . ALA A 1 317 ? 105.136 112.669 99.867  1.00 34.94  ? 305 ALA A N     1 
ATOM   2350 C  CA    . ALA A 1 317 ? 104.252 111.526 99.709  1.00 34.90  ? 305 ALA A CA    1 
ATOM   2351 C  C     . ALA A 1 317 ? 103.149 111.807 98.705  1.00 39.36  ? 305 ALA A C     1 
ATOM   2352 O  O     . ALA A 1 317 ? 102.736 110.900 97.982  1.00 42.23  ? 305 ALA A O     1 
ATOM   2353 C  CB    . ALA A 1 317 ? 103.656 111.139 101.057 1.00 37.49  ? 305 ALA A CB    1 
ATOM   2354 N  N     . ASP A 1 318 ? 102.656 113.044 98.648  1.00 44.20  ? 306 ASP A N     1 
ATOM   2355 C  CA    . ASP A 1 318 ? 101.705 113.399 97.601  1.00 43.91  ? 306 ASP A CA    1 
ATOM   2356 C  C     . ASP A 1 318 ? 102.316 113.201 96.221  1.00 46.92  ? 306 ASP A C     1 
ATOM   2357 O  O     . ASP A 1 318 ? 101.677 112.636 95.328  1.00 52.52  ? 306 ASP A O     1 
ATOM   2358 C  CB    . ASP A 1 318 ? 101.236 114.843 97.776  1.00 50.05  ? 306 ASP A CB    1 
ATOM   2359 C  CG    . ASP A 1 318 ? 100.060 114.964 98.722  1.00 61.98  ? 306 ASP A CG    1 
ATOM   2360 O  OD1   . ASP A 1 318 ? 99.349  113.958 98.919  1.00 61.98  ? 306 ASP A OD1   1 
ATOM   2361 O  OD2   . ASP A 1 318 ? 99.844  116.066 99.267  1.00 66.67  ? 306 ASP A OD2   1 
ATOM   2362 N  N     . ARG A 1 319 ? 103.562 113.641 96.035  1.00 46.05  ? 307 ARG A N     1 
ATOM   2363 C  CA    . ARG A 1 319 ? 104.225 113.447 94.744  1.00 43.45  ? 307 ARG A CA    1 
ATOM   2364 C  C     . ARG A 1 319 ? 104.442 111.965 94.435  1.00 44.62  ? 307 ARG A C     1 
ATOM   2365 O  O     . ARG A 1 319 ? 104.180 111.504 93.311  1.00 47.31  ? 307 ARG A O     1 
ATOM   2366 C  CB    . ARG A 1 319 ? 105.553 114.201 94.727  1.00 40.39  ? 307 ARG A CB    1 
ATOM   2367 C  CG    . ARG A 1 319 ? 105.386 115.704 94.768  1.00 40.27  ? 307 ARG A CG    1 
ATOM   2368 C  CD    . ARG A 1 319 ? 106.633 116.421 94.302  1.00 42.04  ? 307 ARG A CD    1 
ATOM   2369 N  NE    . ARG A 1 319 ? 107.717 116.333 95.271  1.00 52.25  ? 307 ARG A NE    1 
ATOM   2370 C  CZ    . ARG A 1 319 ? 108.169 117.359 95.978  1.00 53.73  ? 307 ARG A CZ    1 
ATOM   2371 N  NH1   . ARG A 1 319 ? 107.636 118.564 95.866  1.00 49.06  ? 307 ARG A NH1   1 
ATOM   2372 N  NH2   . ARG A 1 319 ? 109.182 117.172 96.818  1.00 52.31  ? 307 ARG A NH2   1 
ATOM   2373 N  N     . ILE A 1 320 ? 104.909 111.200 95.424  1.00 40.29  ? 308 ILE A N     1 
ATOM   2374 C  CA    . ILE A 1 320 ? 105.174 109.780 95.210  1.00 32.88  ? 308 ILE A CA    1 
ATOM   2375 C  C     . ILE A 1 320 ? 103.885 109.036 94.892  1.00 38.40  ? 308 ILE A C     1 
ATOM   2376 O  O     . ILE A 1 320 ? 103.855 108.170 94.013  1.00 44.62  ? 308 ILE A O     1 
ATOM   2377 C  CB    . ILE A 1 320 ? 105.894 109.178 96.430  1.00 31.75  ? 308 ILE A CB    1 
ATOM   2378 C  CG1   . ILE A 1 320 ? 107.344 109.648 96.476  1.00 30.80  ? 308 ILE A CG1   1 
ATOM   2379 C  CG2   . ILE A 1 320 ? 105.849 107.664 96.388  1.00 35.21  ? 308 ILE A CG2   1 
ATOM   2380 C  CD1   . ILE A 1 320 ? 108.024 109.359 97.781  1.00 34.11  ? 308 ILE A CD1   1 
ATOM   2381 N  N     . GLY A 1 321 ? 102.800 109.356 95.600  1.00 37.61  ? 309 GLY A N     1 
ATOM   2382 C  CA    . GLY A 1 321 ? 101.525 108.723 95.321  1.00 37.46  ? 309 GLY A CA    1 
ATOM   2383 C  C     . GLY A 1 321 ? 100.915 109.169 94.011  1.00 40.37  ? 309 GLY A C     1 
ATOM   2384 O  O     . GLY A 1 321 ? 100.161 108.418 93.390  1.00 42.20  ? 309 GLY A O     1 
ATOM   2385 N  N     . GLU A 1 322 ? 101.223 110.392 93.574  1.00 43.54  ? 310 GLU A N     1 
ATOM   2386 C  CA    . GLU A 1 322 ? 100.822 110.817 92.239  1.00 43.38  ? 310 GLU A CA    1 
ATOM   2387 C  C     . GLU A 1 322 ? 101.494 109.964 91.176  1.00 44.38  ? 310 GLU A C     1 
ATOM   2388 O  O     . GLU A 1 322 ? 100.860 109.574 90.189  1.00 47.58  ? 310 GLU A O     1 
ATOM   2389 C  CB    . GLU A 1 322 ? 101.158 112.293 92.036  1.00 47.38  ? 310 GLU A CB    1 
ATOM   2390 C  CG    . GLU A 1 322 ? 100.761 112.835 90.678  1.00 58.21  ? 310 GLU A CG    1 
ATOM   2391 C  CD    . GLU A 1 322 ? 101.226 114.259 90.460  1.00 67.75  ? 310 GLU A CD    1 
ATOM   2392 O  OE1   . GLU A 1 322 ? 102.307 114.619 90.972  1.00 65.22  ? 310 GLU A OE1   1 
ATOM   2393 O  OE2   . GLU A 1 322 ? 100.513 115.018 89.771  1.00 70.25  ? 310 GLU A OE2   1 
ATOM   2394 N  N     . VAL A 1 323 ? 102.782 109.669 91.356  1.00 45.41  ? 311 VAL A N     1 
ATOM   2395 C  CA    . VAL A 1 323 ? 103.454 108.768 90.420  1.00 40.25  ? 311 VAL A CA    1 
ATOM   2396 C  C     . VAL A 1 323 ? 102.892 107.354 90.524  1.00 37.46  ? 311 VAL A C     1 
ATOM   2397 O  O     . VAL A 1 323 ? 102.608 106.709 89.508  1.00 46.40  ? 311 VAL A O     1 
ATOM   2398 C  CB    . VAL A 1 323 ? 104.977 108.793 90.635  1.00 38.73  ? 311 VAL A CB    1 
ATOM   2399 C  CG1   . VAL A 1 323 ? 105.600 107.483 90.188  1.00 35.87  ? 311 VAL A CG1   1 
ATOM   2400 C  CG2   . VAL A 1 323 ? 105.572 109.912 89.835  1.00 38.34  ? 311 VAL A CG2   1 
ATOM   2401 N  N     . LEU A 1 324 ? 102.708 106.853 91.745  1.00 33.82  ? 312 LEU A N     1 
ATOM   2402 C  CA    . LEU A 1 324 ? 102.291 105.468 91.935  1.00 37.28  ? 312 LEU A CA    1 
ATOM   2403 C  C     . LEU A 1 324 ? 100.832 105.234 91.568  1.00 41.93  ? 312 LEU A C     1 
ATOM   2404 O  O     . LEU A 1 324 ? 100.427 104.079 91.407  1.00 42.21  ? 312 LEU A O     1 
ATOM   2405 C  CB    . LEU A 1 324 ? 102.537 105.041 93.382  1.00 33.01  ? 312 LEU A CB    1 
ATOM   2406 C  CG    . LEU A 1 324 ? 103.994 104.861 93.810  1.00 32.02  ? 312 LEU A CG    1 
ATOM   2407 C  CD1   . LEU A 1 324 ? 104.077 104.590 95.297  1.00 30.42  ? 312 LEU A CD1   1 
ATOM   2408 C  CD2   . LEU A 1 324 ? 104.651 103.741 93.029  1.00 30.90  ? 312 LEU A CD2   1 
ATOM   2409 N  N     . SER A 1 325 ? 100.035 106.291 91.444  1.00 45.57  ? 313 SER A N     1 
ATOM   2410 C  CA    . SER A 1 325 ? 98.639  106.173 91.050  1.00 44.62  ? 313 SER A CA    1 
ATOM   2411 C  C     . SER A 1 325 ? 98.440  106.246 89.544  1.00 49.51  ? 313 SER A C     1 
ATOM   2412 O  O     . SER A 1 325 ? 97.303  106.125 89.078  1.00 56.55  ? 313 SER A O     1 
ATOM   2413 C  CB    . SER A 1 325 ? 97.807  107.265 91.728  1.00 44.67  ? 313 SER A CB    1 
ATOM   2414 O  OG    . SER A 1 325 ? 97.912  107.184 93.138  1.00 50.37  ? 313 SER A OG    1 
ATOM   2415 N  N     . THR A 1 326 ? 99.508  106.439 88.776  1.00 46.76  ? 314 THR A N     1 
ATOM   2416 C  CA    . THR A 1 326 ? 99.408  106.521 87.325  1.00 49.11  ? 314 THR A CA    1 
ATOM   2417 C  C     . THR A 1 326 ? 99.255  105.120 86.746  1.00 51.95  ? 314 THR A C     1 
ATOM   2418 O  O     . THR A 1 326 ? 100.041 104.222 87.062  1.00 53.46  ? 314 THR A O     1 
ATOM   2419 C  CB    . THR A 1 326 ? 100.639 107.210 86.745  1.00 46.03  ? 314 THR A CB    1 
ATOM   2420 O  OG1   . THR A 1 326 ? 100.702 108.557 87.226  1.00 50.02  ? 314 THR A OG1   1 
ATOM   2421 C  CG2   . THR A 1 326 ? 100.573 107.226 85.230  1.00 50.97  ? 314 THR A CG2   1 
ATOM   2422 N  N     . GLN A 1 327 ? 98.242  104.933 85.907  1.00 55.17  ? 315 GLN A N     1 
ATOM   2423 C  CA    . GLN A 1 327 ? 97.996  103.650 85.268  1.00 63.11  ? 315 GLN A CA    1 
ATOM   2424 C  C     . GLN A 1 327 ? 98.585  103.640 83.865  1.00 63.81  ? 315 GLN A C     1 
ATOM   2425 O  O     . GLN A 1 327 ? 98.376  104.572 83.084  1.00 64.65  ? 315 GLN A O     1 
ATOM   2426 C  CB    . GLN A 1 327 ? 96.497  103.355 85.209  1.00 70.25  ? 315 GLN A CB    1 
ATOM   2427 C  CG    . GLN A 1 327 ? 95.851  103.152 86.568  1.00 75.47  ? 315 GLN A CG    1 
ATOM   2428 C  CD    . GLN A 1 327 ? 94.544  102.390 86.482  1.00 89.26  ? 315 GLN A CD    1 
ATOM   2429 O  OE1   . GLN A 1 327 ? 94.373  101.523 85.626  1.00 95.87  ? 315 GLN A OE1   1 
ATOM   2430 N  NE2   . GLN A 1 327 ? 93.612  102.713 87.370  1.00 85.90  ? 315 GLN A NE2   1 
ATOM   2431 N  N     . THR A 1 328 ? 99.324  102.581 83.551  1.00 64.05  ? 316 THR A N     1 
ATOM   2432 C  CA    . THR A 1 328 ? 99.928  102.446 82.236  1.00 63.26  ? 316 THR A CA    1 
ATOM   2433 C  C     . THR A 1 328 ? 98.878  102.050 81.207  1.00 65.89  ? 316 THR A C     1 
ATOM   2434 O  O     . THR A 1 328 ? 97.887  101.386 81.521  1.00 68.16  ? 316 THR A O     1 
ATOM   2435 C  CB    . THR A 1 328 ? 101.051 101.409 82.258  1.00 65.97  ? 316 THR A CB    1 
ATOM   2436 O  OG1   . THR A 1 328 ? 100.491 100.097 82.380  1.00 71.66  ? 316 THR A OG1   1 
ATOM   2437 C  CG2   . THR A 1 328 ? 101.977 101.660 83.434  1.00 61.01  ? 316 THR A CG2   1 
ATOM   2438 N  N     . ALA A 1 329 ? 99.104  102.470 79.963  1.00 67.27  ? 317 ALA A N     1 
ATOM   2439 C  CA    . ALA A 1 329 ? 98.174  102.191 78.878  1.00 67.06  ? 317 ALA A CA    1 
ATOM   2440 C  C     . ALA A 1 329 ? 98.666  101.126 77.909  1.00 71.10  ? 317 ALA A C     1 
ATOM   2441 O  O     . ALA A 1 329 ? 97.868  100.629 77.108  1.00 65.97  ? 317 ALA A O     1 
ATOM   2442 C  CB    . ALA A 1 329 ? 97.873  103.474 78.096  1.00 61.75  ? 317 ALA A CB    1 
ATOM   2443 N  N     . ILE A 1 330 ? 99.946  100.766 77.955  1.00 73.61  ? 318 ILE A N     1 
ATOM   2444 C  CA    . ILE A 1 330 ? 100.534 99.808  77.025  1.00 75.49  ? 318 ILE A CA    1 
ATOM   2445 C  C     . ILE A 1 330 ? 101.052 98.626  77.832  1.00 80.13  ? 318 ILE A C     1 
ATOM   2446 O  O     . ILE A 1 330 ? 102.019 98.760  78.593  1.00 80.49  ? 318 ILE A O     1 
ATOM   2447 C  CB    . ILE A 1 330 ? 101.654 100.437 76.187  1.00 70.02  ? 318 ILE A CB    1 
ATOM   2448 C  CG1   . ILE A 1 330 ? 101.134 101.676 75.457  1.00 64.56  ? 318 ILE A CG1   1 
ATOM   2449 C  CG2   . ILE A 1 330 ? 102.215 99.429  75.201  1.00 70.31  ? 318 ILE A CG2   1 
ATOM   2450 C  CD1   . ILE A 1 330 ? 102.133 102.287 74.518  1.00 65.25  ? 318 ILE A CD1   1 
ATOM   2451 N  N     . THR A 1 331 ? 100.418 97.467  77.658  1.00 84.36  ? 319 THR A N     1 
ATOM   2452 C  CA    . THR A 1 331 ? 100.786 96.241  78.354  1.00 87.07  ? 319 THR A CA    1 
ATOM   2453 C  C     . THR A 1 331 ? 100.564 95.056  77.424  1.00 90.10  ? 319 THR A C     1 
ATOM   2454 O  O     . THR A 1 331 ? 99.868  95.159  76.412  1.00 96.60  ? 319 THR A O     1 
ATOM   2455 C  CB    . THR A 1 331 ? 99.970  96.034  79.643  1.00 89.26  ? 319 THR A CB    1 
ATOM   2456 O  OG1   . THR A 1 331 ? 98.570  96.059  79.336  1.00 92.54  ? 319 THR A OG1   1 
ATOM   2457 C  CG2   . THR A 1 331 ? 100.280 97.103  80.683  1.00 79.57  ? 319 THR A CG2   1 
ATOM   2458 N  N     . ASN A 1 332 ? 101.164 93.927  77.776  1.00 85.22  ? 320 ASN A N     1 
ATOM   2459 C  CA    . ASN A 1 332 ? 100.885 92.680  77.069  1.00 96.04  ? 320 ASN A CA    1 
ATOM   2460 C  C     . ASN A 1 332 ? 99.504  92.185  77.481  1.00 102.95 ? 320 ASN A C     1 
ATOM   2461 O  O     . ASN A 1 332 ? 99.281  91.932  78.672  1.00 103.72 ? 320 ASN A O     1 
ATOM   2462 C  CB    . ASN A 1 332 ? 101.953 91.642  77.388  1.00 99.21  ? 320 ASN A CB    1 
ATOM   2463 C  CG    . ASN A 1 332 ? 103.359 92.171  77.179  1.00 94.57  ? 320 ASN A CG    1 
ATOM   2464 O  OD1   . ASN A 1 332 ? 103.568 93.127  76.434  1.00 93.96  ? 320 ASN A OD1   1 
ATOM   2465 N  ND2   . ASN A 1 332 ? 104.330 91.550  77.836  1.00 90.74  ? 320 ASN A ND2   1 
ATOM   2466 N  N     . PRO A 1 333 ? 98.549  92.041  76.548  1.00 106.95 ? 321 PRO A N     1 
ATOM   2467 C  CA    . PRO A 1 333 ? 97.134  91.949  76.949  1.00 110.17 ? 321 PRO A CA    1 
ATOM   2468 C  C     . PRO A 1 333 ? 96.768  90.774  77.847  1.00 112.08 ? 321 PRO A C     1 
ATOM   2469 O  O     . PRO A 1 333 ? 96.381  90.983  79.002  1.00 109.49 ? 321 PRO A O     1 
ATOM   2470 C  CB    . PRO A 1 333 ? 96.404  91.847  75.602  1.00 106.92 ? 321 PRO A CB    1 
ATOM   2471 C  CG    . PRO A 1 333 ? 97.426  91.304  74.651  1.00 102.13 ? 321 PRO A CG    1 
ATOM   2472 C  CD    . PRO A 1 333 ? 98.736  91.874  75.097  1.00 100.41 ? 321 PRO A CD    1 
ATOM   2473 N  N     . ALA A 1 334 ? 96.877  89.543  77.348  1.00 112.41 ? 322 ALA A N     1 
ATOM   2474 C  CA    . ALA A 1 334 ? 96.656  88.374  78.192  1.00 112.31 ? 322 ALA A CA    1 
ATOM   2475 C  C     . ALA A 1 334 ? 97.706  87.298  77.951  1.00 111.90 ? 322 ALA A C     1 
ATOM   2476 O  O     . ALA A 1 334 ? 98.191  86.661  78.891  1.00 107.15 ? 322 ALA A O     1 
ATOM   2477 C  CB    . ALA A 1 334 ? 95.256  87.804  77.955  1.00 112.34 ? 322 ALA A CB    1 
ATOM   2478 N  N     . ASP A 1 335 ? 98.059  87.104  76.685  1.00 112.93 ? 323 ASP A N     1 
ATOM   2479 C  CA    . ASP A 1 335 ? 98.937  86.035  76.231  1.00 109.21 ? 323 ASP A CA    1 
ATOM   2480 C  C     . ASP A 1 335 ? 99.500  86.378  74.855  1.00 107.47 ? 323 ASP A C     1 
ATOM   2481 O  O     . ASP A 1 335 ? 98.921  86.017  73.824  1.00 101.56 ? 323 ASP A O     1 
ATOM   2482 C  CB    . ASP A 1 335 ? 98.192  84.692  76.247  1.00 110.89 ? 323 ASP A CB    1 
ATOM   2483 C  CG    . ASP A 1 335 ? 96.982  84.667  75.324  1.00 114.23 ? 323 ASP A CG    1 
ATOM   2484 O  OD1   . ASP A 1 335 ? 96.491  83.560  75.019  1.00 111.82 ? 323 ASP A OD1   1 
ATOM   2485 O  OD2   . ASP A 1 335 ? 96.499  85.752  74.934  1.00 109.69 ? 323 ASP A OD2   1 
ATOM   2486 N  N     . PRO A 1 336 ? 100.624 87.088  74.805  1.00 105.28 ? 324 PRO A N     1 
ATOM   2487 C  CA    . PRO A 1 336 ? 101.127 87.583  73.519  1.00 99.01  ? 324 PRO A CA    1 
ATOM   2488 C  C     . PRO A 1 336 ? 101.454 86.453  72.553  1.00 94.83  ? 324 PRO A C     1 
ATOM   2489 O  O     . PRO A 1 336 ? 101.987 85.411  72.939  1.00 93.04  ? 324 PRO A O     1 
ATOM   2490 C  CB    . PRO A 1 336 ? 102.386 88.363  73.910  1.00 94.68  ? 324 PRO A CB    1 
ATOM   2491 C  CG    . PRO A 1 336 ? 102.233 88.646  75.369  1.00 94.32  ? 324 PRO A CG    1 
ATOM   2492 C  CD    . PRO A 1 336 ? 101.488 87.484  75.927  1.00 99.96  ? 324 PRO A CD    1 
ATOM   2493 N  N     . VAL A 1 337 ? 101.129 86.678  71.281  1.00 91.85  ? 325 VAL A N     1 
ATOM   2494 C  CA    . VAL A 1 337 ? 101.562 85.776  70.223  1.00 94.01  ? 325 VAL A CA    1 
ATOM   2495 C  C     . VAL A 1 337 ? 103.058 85.954  70.014  1.00 97.06  ? 325 VAL A C     1 
ATOM   2496 O  O     . VAL A 1 337 ? 103.565 87.083  69.985  1.00 100.42 ? 325 VAL A O     1 
ATOM   2497 C  CB    . VAL A 1 337 ? 100.778 86.045  68.930  1.00 90.80  ? 325 VAL A CB    1 
ATOM   2498 C  CG1   . VAL A 1 337 ? 101.212 85.088  67.832  1.00 85.40  ? 325 VAL A CG1   1 
ATOM   2499 C  CG2   . VAL A 1 337 ? 99.284  85.935  69.183  1.00 83.57  ? 325 VAL A CG2   1 
ATOM   2500 N  N     . ARG A 1 338 ? 103.777 84.842  69.871  1.00 92.60  ? 326 ARG A N     1 
ATOM   2501 C  CA    . ARG A 1 338 ? 105.234 84.855  69.753  1.00 94.61  ? 326 ARG A CA    1 
ATOM   2502 C  C     . ARG A 1 338 ? 105.643 84.206  68.439  1.00 95.03  ? 326 ARG A C     1 
ATOM   2503 O  O     . ARG A 1 338 ? 105.927 82.999  68.391  1.00 95.19  ? 326 ARG A O     1 
ATOM   2504 C  CB    . ARG A 1 338 ? 105.882 84.152  70.943  1.00 91.94  ? 326 ARG A CB    1 
ATOM   2505 C  CG    . ARG A 1 338 ? 105.593 84.830  72.268  1.00 98.05  ? 326 ARG A CG    1 
ATOM   2506 C  CD    . ARG A 1 338 ? 106.185 84.065  73.441  1.00 97.45  ? 326 ARG A CD    1 
ATOM   2507 N  NE    . ARG A 1 338 ? 106.073 84.798  74.698  1.00 97.73  ? 326 ARG A NE    1 
ATOM   2508 C  CZ    . ARG A 1 338 ? 104.932 85.133  75.286  1.00 100.34 ? 326 ARG A CZ    1 
ATOM   2509 N  NH1   . ARG A 1 338 ? 103.760 84.775  74.785  1.00 99.37  ? 326 ARG A NH1   1 
ATOM   2510 N  NH2   . ARG A 1 338 ? 104.967 85.836  76.415  1.00 94.38  ? 326 ARG A NH2   1 
ATOM   2511 N  N     . PRO A 1 339 ? 105.686 84.967  67.348  1.00 95.35  ? 327 PRO A N     1 
ATOM   2512 C  CA    . PRO A 1 339 ? 106.172 84.416  66.082  1.00 96.51  ? 327 PRO A CA    1 
ATOM   2513 C  C     . PRO A 1 339 ? 107.651 84.080  66.164  1.00 97.25  ? 327 PRO A C     1 
ATOM   2514 O  O     . PRO A 1 339 ? 108.415 84.675  66.927  1.00 97.35  ? 327 PRO A O     1 
ATOM   2515 C  CB    . PRO A 1 339 ? 105.914 85.544  65.075  1.00 97.55  ? 327 PRO A CB    1 
ATOM   2516 C  CG    . PRO A 1 339 ? 104.939 86.461  65.752  1.00 94.23  ? 327 PRO A CG    1 
ATOM   2517 C  CD    . PRO A 1 339 ? 105.257 86.367  67.208  1.00 94.03  ? 327 PRO A CD    1 
ATOM   2518 N  N     . ALA A 1 340 ? 108.051 83.102  65.358  1.00 100.99 ? 328 ALA A N     1 
ATOM   2519 C  CA    . ALA A 1 340 ? 109.441 82.663  65.319  1.00 103.95 ? 328 ALA A CA    1 
ATOM   2520 C  C     . ALA A 1 340 ? 110.227 83.585  64.396  1.00 110.09 ? 328 ALA A C     1 
ATOM   2521 O  O     . ALA A 1 340 ? 109.975 83.626  63.187  1.00 111.14 ? 328 ALA A O     1 
ATOM   2522 C  CB    . ALA A 1 340 ? 109.530 81.213  64.855  1.00 100.48 ? 328 ALA A CB    1 
ATOM   2523 N  N     . ALA A 1 341 ? 111.173 84.333  64.968  1.00 109.81 ? 329 ALA A N     1 
ATOM   2524 C  CA    . ALA A 1 341 ? 112.098 85.182  64.217  1.00 103.81 ? 329 ALA A CA    1 
ATOM   2525 C  C     . ALA A 1 341 ? 111.339 86.200  63.359  1.00 103.11 ? 329 ALA A C     1 
ATOM   2526 O  O     . ALA A 1 341 ? 111.364 86.169  62.128  1.00 103.19 ? 329 ALA A O     1 
ATOM   2527 C  CB    . ALA A 1 341 ? 113.046 84.333  63.362  1.00 98.47  ? 329 ALA A CB    1 
ATOM   2528 N  N     . ILE A 1 342 ? 110.642 87.096  64.056  1.00 100.04 ? 330 ILE A N     1 
ATOM   2529 C  CA    . ILE A 1 342 ? 109.897 88.170  63.405  1.00 99.37  ? 330 ILE A CA    1 
ATOM   2530 C  C     . ILE A 1 342 ? 110.849 89.013  62.561  1.00 94.09  ? 330 ILE A C     1 
ATOM   2531 O  O     . ILE A 1 342 ? 111.751 89.677  63.083  1.00 93.47  ? 330 ILE A O     1 
ATOM   2532 C  CB    . ILE A 1 342 ? 109.138 89.015  64.451  1.00 98.69  ? 330 ILE A CB    1 
ATOM   2533 C  CG1   . ILE A 1 342 ? 108.298 90.107  63.787  1.00 92.32  ? 330 ILE A CG1   1 
ATOM   2534 C  CG2   . ILE A 1 342 ? 110.065 89.552  65.536  1.00 92.66  ? 330 ILE A CG2   1 
ATOM   2535 C  CD1   . ILE A 1 342 ? 106.905 90.216  64.361  1.00 95.89  ? 330 ILE A CD1   1 
ATOM   2536 N  N     . ALA A 1 343 ? 110.672 88.963  61.237  1.00 97.92  ? 331 ALA A N     1 
ATOM   2537 C  CA    . ALA A 1 343 ? 111.588 89.653  60.336  1.00 100.18 ? 331 ALA A CA    1 
ATOM   2538 C  C     . ALA A 1 343 ? 110.893 90.240  59.111  1.00 99.65  ? 331 ALA A C     1 
ATOM   2539 O  O     . ALA A 1 343 ? 111.558 90.491  58.099  1.00 95.10  ? 331 ALA A O     1 
ATOM   2540 C  CB    . ALA A 1 343 ? 112.709 88.712  59.883  1.00 95.70  ? 331 ALA A CB    1 
ATOM   2541 N  N     . GLY A 1 344 ? 109.586 90.470  59.166  1.00 98.91  ? 332 GLY A N     1 
ATOM   2542 C  CA    . GLY A 1 344 ? 108.852 90.764  57.953  1.00 99.20  ? 332 GLY A CA    1 
ATOM   2543 C  C     . GLY A 1 344 ? 108.345 92.178  57.769  1.00 96.02  ? 332 GLY A C     1 
ATOM   2544 O  O     . GLY A 1 344 ? 109.072 93.152  57.984  1.00 91.74  ? 332 GLY A O     1 
ATOM   2545 N  N     . ASP A 1 345 ? 107.081 92.290  57.373  1.00 95.35  ? 333 ASP A N     1 
ATOM   2546 C  CA    . ASP A 1 345 ? 106.520 93.514  56.826  1.00 95.37  ? 333 ASP A CA    1 
ATOM   2547 C  C     . ASP A 1 345 ? 105.720 94.290  57.870  1.00 88.66  ? 333 ASP A C     1 
ATOM   2548 O  O     . ASP A 1 345 ? 105.464 93.822  58.980  1.00 86.77  ? 333 ASP A O     1 
ATOM   2549 C  CB    . ASP A 1 345 ? 105.640 93.184  55.622  1.00 99.95  ? 333 ASP A CB    1 
ATOM   2550 C  CG    . ASP A 1 345 ? 104.826 91.925  55.825  1.00 103.80 ? 333 ASP A CG    1 
ATOM   2551 O  OD1   . ASP A 1 345 ? 105.364 90.961  56.408  1.00 105.44 ? 333 ASP A OD1   1 
ATOM   2552 O  OD2   . ASP A 1 345 ? 103.651 91.900  55.404  1.00 101.20 ? 333 ASP A OD2   1 
ATOM   2553 N  N     . ILE A 1 346 ? 105.322 95.502  57.485  1.00 90.44  ? 334 ILE A N     1 
ATOM   2554 C  CA    . ILE A 1 346 ? 104.502 96.384  58.306  1.00 90.97  ? 334 ILE A CA    1 
ATOM   2555 C  C     . ILE A 1 346 ? 103.142 96.528  57.638  1.00 89.84  ? 334 ILE A C     1 
ATOM   2556 O  O     . ILE A 1 346 ? 103.057 96.803  56.436  1.00 90.42  ? 334 ILE A O     1 
ATOM   2557 C  CB    . ILE A 1 346 ? 105.158 97.765  58.499  1.00 84.90  ? 334 ILE A CB    1 
ATOM   2558 C  CG1   . ILE A 1 346 ? 106.685 97.657  58.476  1.00 79.54  ? 334 ILE A CG1   1 
ATOM   2559 C  CG2   . ILE A 1 346 ? 104.693 98.396  59.798  1.00 76.93  ? 334 ILE A CG2   1 
ATOM   2560 C  CD1   . ILE A 1 346 ? 107.276 96.991  59.692  1.00 77.00  ? 334 ILE A CD1   1 
ATOM   2561 N  N     . GLY A 1 347 ? 102.079 96.342  58.415  1.00 85.65  ? 335 GLY A N     1 
ATOM   2562 C  CA    . GLY A 1 347 ? 100.739 96.380  57.862  1.00 87.58  ? 335 GLY A CA    1 
ATOM   2563 C  C     . GLY A 1 347 ? 100.122 97.760  57.782  1.00 87.43  ? 335 GLY A C     1 
ATOM   2564 O  O     . GLY A 1 347 ? 99.769  98.213  56.691  1.00 93.10  ? 335 GLY A O     1 
ATOM   2565 N  N     . VAL A 1 348 ? 99.997  98.436  58.927  1.00 86.24  ? 336 VAL A N     1 
ATOM   2566 C  CA    . VAL A 1 348 ? 99.382  99.759  59.035  1.00 90.29  ? 336 VAL A CA    1 
ATOM   2567 C  C     . VAL A 1 348 ? 98.083  99.823  58.239  1.00 90.87  ? 336 VAL A C     1 
ATOM   2568 O  O     . VAL A 1 348 ? 98.044  100.387 57.140  1.00 88.18  ? 336 VAL A O     1 
ATOM   2569 C  CB    . VAL A 1 348 ? 100.352 100.865 58.578  1.00 86.73  ? 336 VAL A CB    1 
ATOM   2570 C  CG1   . VAL A 1 348 ? 99.900  102.215 59.110  1.00 79.59  ? 336 VAL A CG1   1 
ATOM   2571 C  CG2   . VAL A 1 348 ? 101.763 100.559 59.043  1.00 89.69  ? 336 VAL A CG2   1 
ATOM   2572 N  N     . HIS A 1 349 ? 97.011  99.255  58.787  1.00 91.65  ? 337 HIS A N     1 
ATOM   2573 C  CA    . HIS A 1 349 ? 95.723  99.176  58.107  1.00 90.06  ? 337 HIS A CA    1 
ATOM   2574 C  C     . HIS A 1 349 ? 94.748  100.152 58.755  1.00 89.22  ? 337 HIS A C     1 
ATOM   2575 O  O     . HIS A 1 349 ? 94.283  99.920  59.876  1.00 88.52  ? 337 HIS A O     1 
ATOM   2576 C  CB    . HIS A 1 349 ? 95.173  97.752  58.146  1.00 91.30  ? 337 HIS A CB    1 
ATOM   2577 C  CG    . HIS A 1 349 ? 96.076  96.738  57.519  1.00 93.82  ? 337 HIS A CG    1 
ATOM   2578 N  ND1   . HIS A 1 349 ? 96.647  95.706  58.232  1.00 95.69  ? 337 HIS A ND1   1 
ATOM   2579 C  CD2   . HIS A 1 349 ? 96.502  96.593  56.242  1.00 90.40  ? 337 HIS A CD2   1 
ATOM   2580 C  CE1   . HIS A 1 349 ? 97.389  94.972  57.423  1.00 94.15  ? 337 HIS A CE1   1 
ATOM   2581 N  NE2   . HIS A 1 349 ? 97.318  95.488  56.209  1.00 93.43  ? 337 HIS A NE2   1 
ATOM   2582 N  N     . ASP A 1 350 ? 94.435  101.233 58.036  1.00 89.74  ? 338 ASP A N     1 
ATOM   2583 C  CA    . ASP A 1 350 ? 93.431  102.213 58.457  1.00 89.36  ? 338 ASP A CA    1 
ATOM   2584 C  C     . ASP A 1 350 ? 93.720  102.743 59.859  1.00 90.41  ? 338 ASP A C     1 
ATOM   2585 O  O     . ASP A 1 350 ? 92.822  102.895 60.689  1.00 89.24  ? 338 ASP A O     1 
ATOM   2586 C  CB    . ASP A 1 350 ? 92.025  101.618 58.376  1.00 91.34  ? 338 ASP A CB    1 
ATOM   2587 C  CG    . ASP A 1 350 ? 90.965  102.662 58.088  1.00 97.39  ? 338 ASP A CG    1 
ATOM   2588 O  OD1   . ASP A 1 350 ? 90.697  103.501 58.973  1.00 97.98  ? 338 ASP A OD1   1 
ATOM   2589 O  OD2   . ASP A 1 350 ? 90.399  102.643 56.975  1.00 96.14  ? 338 ASP A OD2   1 
ATOM   2590 N  N     . ALA A 1 351 ? 94.991  103.028 60.124  1.00 90.06  ? 339 ALA A N     1 
ATOM   2591 C  CA    . ALA A 1 351 ? 95.410  103.476 61.444  1.00 85.63  ? 339 ALA A CA    1 
ATOM   2592 C  C     . ALA A 1 351 ? 94.986  104.919 61.677  1.00 84.69  ? 339 ALA A C     1 
ATOM   2593 O  O     . ALA A 1 351 ? 95.191  105.784 60.821  1.00 83.82  ? 339 ALA A O     1 
ATOM   2594 C  CB    . ALA A 1 351 ? 96.924  103.339 61.597  1.00 87.85  ? 339 ALA A CB    1 
ATOM   2595 N  N     . THR A 1 352 ? 94.387  105.171 62.838  1.00 80.50  ? 340 THR A N     1 
ATOM   2596 C  CA    . THR A 1 352 ? 94.017  106.512 63.269  1.00 79.07  ? 340 THR A CA    1 
ATOM   2597 C  C     . THR A 1 352 ? 94.527  106.717 64.685  1.00 75.33  ? 340 THR A C     1 
ATOM   2598 O  O     . THR A 1 352 ? 94.253  105.897 65.567  1.00 81.07  ? 340 THR A O     1 
ATOM   2599 C  CB    . THR A 1 352 ? 92.500  106.720 63.215  1.00 82.93  ? 340 THR A CB    1 
ATOM   2600 O  OG1   . THR A 1 352 ? 92.053  106.653 61.856  1.00 87.53  ? 340 THR A OG1   1 
ATOM   2601 C  CG2   . THR A 1 352 ? 92.123  108.068 63.802  1.00 75.40  ? 340 THR A CG2   1 
ATOM   2602 N  N     . PHE A 1 353 ? 95.268  107.798 64.904  1.00 68.31  ? 341 PHE A N     1 
ATOM   2603 C  CA    . PHE A 1 353 ? 95.843  108.081 66.209  1.00 68.18  ? 341 PHE A CA    1 
ATOM   2604 C  C     . PHE A 1 353 ? 95.544  109.515 66.612  1.00 70.04  ? 341 PHE A C     1 
ATOM   2605 O  O     . PHE A 1 353 ? 95.679  110.439 65.806  1.00 74.76  ? 341 PHE A O     1 
ATOM   2606 C  CB    . PHE A 1 353 ? 97.356  107.851 66.222  1.00 68.71  ? 341 PHE A CB    1 
ATOM   2607 C  CG    . PHE A 1 353 ? 98.009  108.198 67.529  1.00 65.76  ? 341 PHE A CG    1 
ATOM   2608 C  CD1   . PHE A 1 353 ? 97.941  107.330 68.603  1.00 62.64  ? 341 PHE A CD1   1 
ATOM   2609 C  CD2   . PHE A 1 353 ? 98.686  109.394 67.686  1.00 60.38  ? 341 PHE A CD2   1 
ATOM   2610 C  CE1   . PHE A 1 353 ? 98.536  107.647 69.804  1.00 56.77  ? 341 PHE A CE1   1 
ATOM   2611 C  CE2   . PHE A 1 353 ? 99.283  109.714 68.884  1.00 58.22  ? 341 PHE A CE2   1 
ATOM   2612 C  CZ    . PHE A 1 353 ? 99.208  108.840 69.944  1.00 55.43  ? 341 PHE A CZ    1 
ATOM   2613 N  N     . CYS A 1 354 ? 95.141  109.688 67.867  1.00 66.47  ? 342 CYS A N     1 
ATOM   2614 C  CA    . CYS A 1 354 ? 94.931  110.999 68.463  1.00 68.74  ? 342 CYS A CA    1 
ATOM   2615 C  C     . CYS A 1 354 ? 95.680  111.046 69.784  1.00 72.38  ? 342 CYS A C     1 
ATOM   2616 O  O     . CYS A 1 354 ? 95.533  110.142 70.613  1.00 75.29  ? 342 CYS A O     1 
ATOM   2617 C  CB    . CYS A 1 354 ? 93.440  111.278 68.681  1.00 73.86  ? 342 CYS A CB    1 
ATOM   2618 S  SG    . CYS A 1 354 ? 93.070  112.913 69.349  1.00 93.87  ? 342 CYS A SG    1 
ATOM   2619 N  N     . TYR A 1 355 ? 96.488  112.082 69.974  1.00 69.89  ? 343 TYR A N     1 
ATOM   2620 C  CA    . TYR A 1 355 ? 97.236  112.206 71.214  1.00 68.42  ? 343 TYR A CA    1 
ATOM   2621 C  C     . TYR A 1 355 ? 96.277  112.453 72.376  1.00 77.22  ? 343 TYR A C     1 
ATOM   2622 O  O     . TYR A 1 355 ? 95.264  113.138 72.209  1.00 83.99  ? 343 TYR A O     1 
ATOM   2623 C  CB    . TYR A 1 355 ? 98.250  113.345 71.120  1.00 62.01  ? 343 TYR A CB    1 
ATOM   2624 C  CG    . TYR A 1 355 ? 99.510  112.983 70.369  1.00 64.63  ? 343 TYR A CG    1 
ATOM   2625 C  CD1   . TYR A 1 355 ? 100.545 112.305 70.996  1.00 61.58  ? 343 TYR A CD1   1 
ATOM   2626 C  CD2   . TYR A 1 355 ? 99.665  113.319 69.033  1.00 63.56  ? 343 TYR A CD2   1 
ATOM   2627 C  CE1   . TYR A 1 355 ? 101.696 111.973 70.313  1.00 58.00  ? 343 TYR A CE1   1 
ATOM   2628 C  CE2   . TYR A 1 355 ? 100.812 112.992 68.344  1.00 58.76  ? 343 TYR A CE2   1 
ATOM   2629 C  CZ    . TYR A 1 355 ? 101.824 112.320 68.987  1.00 56.53  ? 343 TYR A CZ    1 
ATOM   2630 O  OH    . TYR A 1 355 ? 102.968 111.994 68.300  1.00 56.51  ? 343 TYR A OH    1 
ATOM   2631 N  N     . PRO A 1 356 ? 96.553  111.893 73.553  1.00 77.69  ? 344 PRO A N     1 
ATOM   2632 C  CA    . PRO A 1 356 ? 95.692  112.163 74.710  1.00 82.90  ? 344 PRO A CA    1 
ATOM   2633 C  C     . PRO A 1 356 ? 95.674  113.646 75.046  1.00 86.12  ? 344 PRO A C     1 
ATOM   2634 O  O     . PRO A 1 356 ? 96.701  114.327 74.998  1.00 84.19  ? 344 PRO A O     1 
ATOM   2635 C  CB    . PRO A 1 356 ? 96.329  111.334 75.831  1.00 80.45  ? 344 PRO A CB    1 
ATOM   2636 C  CG    . PRO A 1 356 ? 97.727  111.072 75.376  1.00 71.19  ? 344 PRO A CG    1 
ATOM   2637 C  CD    . PRO A 1 356 ? 97.660  110.983 73.886  1.00 74.29  ? 344 PRO A CD    1 
ATOM   2638 N  N     . GLY A 1 357 ? 94.489  114.144 75.389  1.00 86.63  ? 345 GLY A N     1 
ATOM   2639 C  CA    . GLY A 1 357 ? 94.314  115.550 75.679  1.00 91.11  ? 345 GLY A CA    1 
ATOM   2640 C  C     . GLY A 1 357 ? 94.183  116.446 74.468  1.00 98.36  ? 345 GLY A C     1 
ATOM   2641 O  O     . GLY A 1 357 ? 94.095  117.669 74.633  1.00 100.10 ? 345 GLY A O     1 
ATOM   2642 N  N     . ALA A 1 358 ? 94.168  115.888 73.262  1.00 97.62  ? 346 ALA A N     1 
ATOM   2643 C  CA    . ALA A 1 358 ? 94.051  116.667 72.039  1.00 97.23  ? 346 ALA A CA    1 
ATOM   2644 C  C     . ALA A 1 358 ? 92.612  116.663 71.539  1.00 100.70 ? 346 ALA A C     1 
ATOM   2645 O  O     . ALA A 1 358 ? 91.852  115.721 71.778  1.00 101.30 ? 346 ALA A O     1 
ATOM   2646 C  CB    . ALA A 1 358 ? 94.981  116.125 70.953  1.00 93.50  ? 346 ALA A CB    1 
ATOM   2647 N  N     . ASP A 1 359 ? 92.246  117.733 70.835  1.00 98.83  ? 347 ASP A N     1 
ATOM   2648 C  CA    . ASP A 1 359 ? 90.894  117.886 70.317  1.00 105.80 ? 347 ASP A CA    1 
ATOM   2649 C  C     . ASP A 1 359 ? 90.686  117.215 68.968  1.00 103.13 ? 347 ASP A C     1 
ATOM   2650 O  O     . ASP A 1 359 ? 89.556  116.820 68.656  1.00 101.41 ? 347 ASP A O     1 
ATOM   2651 C  CB    . ASP A 1 359 ? 90.542  119.373 70.197  1.00 109.18 ? 347 ASP A CB    1 
ATOM   2652 C  CG    . ASP A 1 359 ? 89.080  119.602 69.863  1.00 114.52 ? 347 ASP A CG    1 
ATOM   2653 O  OD1   . ASP A 1 359 ? 88.213  119.049 70.572  1.00 114.89 ? 347 ASP A OD1   1 
ATOM   2654 O  OD2   . ASP A 1 359 ? 88.799  120.331 68.889  1.00 112.95 ? 347 ASP A OD2   1 
ATOM   2655 N  N     . ARG A 1 360 ? 91.735  117.070 68.168  1.00 100.63 ? 348 ARG A N     1 
ATOM   2656 C  CA    . ARG A 1 360 ? 91.631  116.502 66.835  1.00 95.66  ? 348 ARG A CA    1 
ATOM   2657 C  C     . ARG A 1 360 ? 92.673  115.408 66.665  1.00 92.18  ? 348 ARG A C     1 
ATOM   2658 O  O     . ARG A 1 360 ? 93.751  115.474 67.267  1.00 89.84  ? 348 ARG A O     1 
ATOM   2659 C  CB    . ARG A 1 360 ? 91.831  117.573 65.750  1.00 94.12  ? 348 ARG A CB    1 
ATOM   2660 C  CG    . ARG A 1 360 ? 92.727  118.721 66.181  1.00 98.71  ? 348 ARG A CG    1 
ATOM   2661 C  CD    . ARG A 1 360 ? 93.273  119.488 64.985  1.00 99.58  ? 348 ARG A CD    1 
ATOM   2662 N  NE    . ARG A 1 360 ? 94.525  118.918 64.498  1.00 103.10 ? 348 ARG A NE    1 
ATOM   2663 C  CZ    . ARG A 1 360 ? 95.680  118.967 65.149  1.00 105.12 ? 348 ARG A CZ    1 
ATOM   2664 N  NH1   . ARG A 1 360 ? 95.792  119.583 66.315  1.00 101.33 ? 348 ARG A NH1   1 
ATOM   2665 N  NH2   . ARG A 1 360 ? 96.752  118.388 64.614  1.00 98.62  ? 348 ARG A NH2   1 
ATOM   2666 N  N     . PRO A 1 361 ? 92.377  114.389 65.858  1.00 88.91  ? 349 PRO A N     1 
ATOM   2667 C  CA    . PRO A 1 361 ? 93.378  113.348 65.593  1.00 83.36  ? 349 PRO A CA    1 
ATOM   2668 C  C     . PRO A 1 361 ? 94.518  113.892 64.744  1.00 82.13  ? 349 PRO A C     1 
ATOM   2669 O  O     . PRO A 1 361 ? 94.313  114.734 63.869  1.00 83.27  ? 349 PRO A O     1 
ATOM   2670 C  CB    . PRO A 1 361 ? 92.582  112.270 64.848  1.00 82.00  ? 349 PRO A CB    1 
ATOM   2671 C  CG    . PRO A 1 361 ? 91.433  113.000 64.245  1.00 85.72  ? 349 PRO A CG    1 
ATOM   2672 C  CD    . PRO A 1 361 ? 91.096  114.116 65.186  1.00 90.47  ? 349 PRO A CD    1 
ATOM   2673 N  N     . VAL A 1 362 ? 95.729  113.398 65.012  1.00 82.29  ? 350 VAL A N     1 
ATOM   2674 C  CA    . VAL A 1 362 ? 96.890  113.808 64.230  1.00 73.73  ? 350 VAL A CA    1 
ATOM   2675 C  C     . VAL A 1 362 ? 97.123  112.895 63.035  1.00 72.50  ? 350 VAL A C     1 
ATOM   2676 O  O     . VAL A 1 362 ? 97.805  113.295 62.085  1.00 70.53  ? 350 VAL A O     1 
ATOM   2677 C  CB    . VAL A 1 362 ? 98.148  113.857 65.112  1.00 67.42  ? 350 VAL A CB    1 
ATOM   2678 C  CG1   . VAL A 1 362 ? 97.967  114.869 66.226  1.00 70.47  ? 350 VAL A CG1   1 
ATOM   2679 C  CG2   . VAL A 1 362 ? 98.446  112.485 65.685  1.00 65.65  ? 350 VAL A CG2   1 
ATOM   2680 N  N     . LEU A 1 363 ? 96.582  111.680 63.061  1.00 76.15  ? 351 LEU A N     1 
ATOM   2681 C  CA    . LEU A 1 363 ? 96.664  110.745 61.948  1.00 74.64  ? 351 LEU A CA    1 
ATOM   2682 C  C     . LEU A 1 363 ? 95.271  110.204 61.674  1.00 79.49  ? 351 LEU A C     1 
ATOM   2683 O  O     . LEU A 1 363 ? 94.579  109.778 62.603  1.00 81.80  ? 351 LEU A O     1 
ATOM   2684 C  CB    . LEU A 1 363 ? 97.632  109.598 62.256  1.00 72.86  ? 351 LEU A CB    1 
ATOM   2685 C  CG    . LEU A 1 363 ? 99.125  109.921 62.211  1.00 68.37  ? 351 LEU A CG    1 
ATOM   2686 C  CD1   . LEU A 1 363 ? 99.932  108.742 62.709  1.00 60.81  ? 351 LEU A CD1   1 
ATOM   2687 C  CD2   . LEU A 1 363 ? 99.548  110.299 60.803  1.00 71.40  ? 351 LEU A CD2   1 
ATOM   2688 N  N     . GLN A 1 364 ? 94.858  110.223 60.408  1.00 83.72  ? 352 GLN A N     1 
ATOM   2689 C  CA    . GLN A 1 364 ? 93.519  109.785 60.031  1.00 88.03  ? 352 GLN A CA    1 
ATOM   2690 C  C     . GLN A 1 364 ? 93.600  108.895 58.802  1.00 89.19  ? 352 GLN A C     1 
ATOM   2691 O  O     . GLN A 1 364 ? 94.130  109.313 57.769  1.00 91.00  ? 352 GLN A O     1 
ATOM   2692 C  CB    . GLN A 1 364 ? 92.601  110.980 59.758  1.00 89.59  ? 352 GLN A CB    1 
ATOM   2693 C  CG    . GLN A 1 364 ? 92.337  111.847 60.971  1.00 89.01  ? 352 GLN A CG    1 
ATOM   2694 C  CD    . GLN A 1 364 ? 91.552  113.097 60.634  1.00 96.76  ? 352 GLN A CD    1 
ATOM   2695 O  OE1   . GLN A 1 364 ? 92.080  114.208 60.683  1.00 93.97  ? 352 GLN A OE1   1 
ATOM   2696 N  NE2   . GLN A 1 364 ? 90.283  112.922 60.288  1.00 102.07 ? 352 GLN A NE2   1 
ATOM   2697 N  N     . ASP A 1 365 ? 93.063  107.679 58.918  1.00 90.35  ? 353 ASP A N     1 
ATOM   2698 C  CA    . ASP A 1 365 ? 92.906  106.761 57.788  1.00 95.23  ? 353 ASP A CA    1 
ATOM   2699 C  C     . ASP A 1 365 ? 94.230  106.504 57.074  1.00 93.11  ? 353 ASP A C     1 
ATOM   2700 O  O     . ASP A 1 365 ? 94.294  106.462 55.844  1.00 90.52  ? 353 ASP A O     1 
ATOM   2701 C  CB    . ASP A 1 365 ? 91.853  107.278 56.805  1.00 96.58  ? 353 ASP A CB    1 
ATOM   2702 C  CG    . ASP A 1 365 ? 90.549  107.639 57.485  1.00 100.38 ? 353 ASP A CG    1 
ATOM   2703 O  OD1   . ASP A 1 365 ? 90.159  106.935 58.438  1.00 101.64 ? 353 ASP A OD1   1 
ATOM   2704 O  OD2   . ASP A 1 365 ? 89.915  108.632 57.069  1.00 96.71  ? 353 ASP A OD2   1 
ATOM   2705 N  N     . VAL A 1 366 ? 95.296  106.331 57.846  1.00 91.28  ? 354 VAL A N     1 
ATOM   2706 C  CA    . VAL A 1 366 ? 96.602  106.017 57.277  1.00 90.11  ? 354 VAL A CA    1 
ATOM   2707 C  C     . VAL A 1 366 ? 96.644  104.526 56.968  1.00 84.15  ? 354 VAL A C     1 
ATOM   2708 O  O     . VAL A 1 366 ? 96.493  103.691 57.865  1.00 83.79  ? 354 VAL A O     1 
ATOM   2709 C  CB    . VAL A 1 366 ? 97.736  106.418 58.231  1.00 88.14  ? 354 VAL A CB    1 
ATOM   2710 C  CG1   . VAL A 1 366 ? 99.079  106.030 57.643  1.00 82.56  ? 354 VAL A CG1   1 
ATOM   2711 C  CG2   . VAL A 1 366 ? 97.687  107.910 58.510  1.00 85.10  ? 354 VAL A CG2   1 
ATOM   2712 N  N     . SER A 1 367 ? 96.849  104.189 55.697  1.00 84.49  ? 355 SER A N     1 
ATOM   2713 C  CA    . SER A 1 367 ? 96.838  102.798 55.252  1.00 87.36  ? 355 SER A CA    1 
ATOM   2714 C  C     . SER A 1 367 ? 97.904  102.621 54.181  1.00 87.03  ? 355 SER A C     1 
ATOM   2715 O  O     . SER A 1 367 ? 97.770  103.154 53.075  1.00 85.92  ? 355 SER A O     1 
ATOM   2716 C  CB    . SER A 1 367 ? 95.460  102.399 54.724  1.00 87.58  ? 355 SER A CB    1 
ATOM   2717 O  OG    . SER A 1 367 ? 95.262  101.000 54.829  1.00 84.84  ? 355 SER A OG    1 
ATOM   2718 N  N     . PHE A 1 368 ? 98.957  101.879 54.512  1.00 88.61  ? 356 PHE A N     1 
ATOM   2719 C  CA    . PHE A 1 368 ? 100.019 101.557 53.570  1.00 88.67  ? 356 PHE A CA    1 
ATOM   2720 C  C     . PHE A 1 368 ? 100.794 100.369 54.115  1.00 90.52  ? 356 PHE A C     1 
ATOM   2721 O  O     . PHE A 1 368 ? 100.948 100.220 55.328  1.00 93.16  ? 356 PHE A O     1 
ATOM   2722 C  CB    . PHE A 1 368 ? 100.954 102.750 53.335  1.00 85.40  ? 356 PHE A CB    1 
ATOM   2723 C  CG    . PHE A 1 368 ? 101.801 103.101 54.524  1.00 84.96  ? 356 PHE A CG    1 
ATOM   2724 C  CD1   . PHE A 1 368 ? 101.291 103.880 55.546  1.00 82.42  ? 356 PHE A CD1   1 
ATOM   2725 C  CD2   . PHE A 1 368 ? 103.106 102.655 54.617  1.00 88.04  ? 356 PHE A CD2   1 
ATOM   2726 C  CE1   . PHE A 1 368 ? 102.067 104.204 56.638  1.00 81.93  ? 356 PHE A CE1   1 
ATOM   2727 C  CE2   . PHE A 1 368 ? 103.885 102.976 55.709  1.00 85.54  ? 356 PHE A CE2   1 
ATOM   2728 C  CZ    . PHE A 1 368 ? 103.365 103.750 56.719  1.00 81.73  ? 356 PHE A CZ    1 
ATOM   2729 N  N     . THR A 1 369 ? 101.291 99.534  53.206  1.00 89.84  ? 357 THR A N     1 
ATOM   2730 C  CA    . THR A 1 369 ? 102.004 98.315  53.563  1.00 89.57  ? 357 THR A CA    1 
ATOM   2731 C  C     . THR A 1 369 ? 103.457 98.435  53.129  1.00 91.26  ? 357 THR A C     1 
ATOM   2732 O  O     . THR A 1 369 ? 103.737 98.808  51.985  1.00 93.76  ? 357 THR A O     1 
ATOM   2733 C  CB    . THR A 1 369 ? 101.352 97.087  52.916  1.00 93.65  ? 357 THR A CB    1 
ATOM   2734 O  OG1   . THR A 1 369 ? 100.208 96.692  53.683  1.00 93.40  ? 357 THR A OG1   1 
ATOM   2735 C  CG2   . THR A 1 369 ? 102.331 95.924  52.846  1.00 92.13  ? 357 THR A CG2   1 
ATOM   2736 N  N     . VAL A 1 370 ? 104.373 98.123  54.041  1.00 89.61  ? 358 VAL A N     1 
ATOM   2737 C  CA    . VAL A 1 370 ? 105.806 98.147  53.767  1.00 89.13  ? 358 VAL A CA    1 
ATOM   2738 C  C     . VAL A 1 370 ? 106.264 96.702  53.580  1.00 89.69  ? 358 VAL A C     1 
ATOM   2739 O  O     . VAL A 1 370 ? 106.340 95.959  54.570  1.00 88.20  ? 358 VAL A O     1 
ATOM   2740 C  CB    . VAL A 1 370 ? 106.586 98.827  54.899  1.00 85.43  ? 358 VAL A CB    1 
ATOM   2741 C  CG1   . VAL A 1 370 ? 108.071 98.849  54.580  1.00 79.17  ? 358 VAL A CG1   1 
ATOM   2742 C  CG2   . VAL A 1 370 ? 106.063 100.231 55.138  1.00 84.79  ? 358 VAL A CG2   1 
ATOM   2743 N  N     . PRO A 1 371 ? 106.582 96.269  52.360  1.00 92.61  ? 359 PRO A N     1 
ATOM   2744 C  CA    . PRO A 1 371 ? 107.006 94.879  52.160  1.00 90.88  ? 359 PRO A CA    1 
ATOM   2745 C  C     . PRO A 1 371 ? 108.313 94.584  52.879  1.00 93.60  ? 359 PRO A C     1 
ATOM   2746 O  O     . PRO A 1 371 ? 109.148 95.466  53.085  1.00 96.12  ? 359 PRO A O     1 
ATOM   2747 C  CB    . PRO A 1 371 ? 107.169 94.771  50.639  1.00 86.01  ? 359 PRO A CB    1 
ATOM   2748 C  CG    . PRO A 1 371 ? 106.394 95.922  50.081  1.00 89.95  ? 359 PRO A CG    1 
ATOM   2749 C  CD    . PRO A 1 371 ? 106.510 97.013  51.093  1.00 90.78  ? 359 PRO A CD    1 
ATOM   2750 N  N     . ARG A 1 372 ? 108.479 93.322  53.268  1.00 89.98  ? 360 ARG A N     1 
ATOM   2751 C  CA    . ARG A 1 372 ? 109.690 92.909  53.960  1.00 90.31  ? 360 ARG A CA    1 
ATOM   2752 C  C     . ARG A 1 372 ? 110.899 93.044  53.043  1.00 92.69  ? 360 ARG A C     1 
ATOM   2753 O  O     . ARG A 1 372 ? 110.812 92.824  51.831  1.00 93.18  ? 360 ARG A O     1 
ATOM   2754 C  CB    . ARG A 1 372 ? 109.553 91.470  54.463  1.00 94.82  ? 360 ARG A CB    1 
ATOM   2755 C  CG    . ARG A 1 372 ? 110.305 90.426  53.651  1.00 97.56  ? 360 ARG A CG    1 
ATOM   2756 C  CD    . ARG A 1 372 ? 110.027 89.019  54.152  1.00 98.40  ? 360 ARG A CD    1 
ATOM   2757 N  NE    . ARG A 1 372 ? 108.600 88.719  54.176  1.00 107.78 ? 360 ARG A NE    1 
ATOM   2758 C  CZ    . ARG A 1 372 ? 108.025 87.881  55.027  1.00 108.43 ? 360 ARG A CZ    1 
ATOM   2759 N  NH1   . ARG A 1 372 ? 108.729 87.233  55.941  1.00 104.72 ? 360 ARG A NH1   1 
ATOM   2760 N  NH2   . ARG A 1 372 ? 106.711 87.687  54.959  1.00 102.72 ? 360 ARG A NH2   1 
ATOM   2761 N  N     . GLY A 1 373 ? 112.028 93.444  53.624  1.00 91.17  ? 361 GLY A N     1 
ATOM   2762 C  CA    . GLY A 1 373 ? 113.258 93.589  52.879  1.00 87.11  ? 361 GLY A CA    1 
ATOM   2763 C  C     . GLY A 1 373 ? 113.325 94.798  51.974  1.00 89.87  ? 361 GLY A C     1 
ATOM   2764 O  O     . GLY A 1 373 ? 114.282 94.915  51.199  1.00 88.34  ? 361 GLY A O     1 
ATOM   2765 N  N     . THR A 1 374 ? 112.350 95.696  52.043  1.00 91.18  ? 362 THR A N     1 
ATOM   2766 C  CA    . THR A 1 374 ? 112.299 96.873  51.191  1.00 90.75  ? 362 THR A CA    1 
ATOM   2767 C  C     . THR A 1 374 ? 112.450 98.137  52.027  1.00 83.44  ? 362 THR A C     1 
ATOM   2768 O  O     . THR A 1 374 ? 112.251 98.135  53.244  1.00 81.66  ? 362 THR A O     1 
ATOM   2769 C  CB    . THR A 1 374 ? 110.986 96.926  50.401  1.00 91.02  ? 362 THR A CB    1 
ATOM   2770 O  OG1   . THR A 1 374 ? 109.896 97.184  51.294  1.00 89.06  ? 362 THR A OG1   1 
ATOM   2771 C  CG2   . THR A 1 374 ? 110.744 95.610  49.683  1.00 87.97  ? 362 THR A CG2   1 
ATOM   2772 N  N     . THR A 1 375 ? 112.810 99.223  51.352  1.00 84.06  ? 363 THR A N     1 
ATOM   2773 C  CA    . THR A 1 375 ? 112.967 100.529 51.976  1.00 81.50  ? 363 THR A CA    1 
ATOM   2774 C  C     . THR A 1 375 ? 111.788 101.404 51.578  1.00 79.16  ? 363 THR A C     1 
ATOM   2775 O  O     . THR A 1 375 ? 111.535 101.606 50.386  1.00 80.50  ? 363 THR A O     1 
ATOM   2776 C  CB    . THR A 1 375 ? 114.285 101.185 51.565  1.00 83.30  ? 363 THR A CB    1 
ATOM   2777 O  OG1   . THR A 1 375 ? 115.383 100.402 52.049  1.00 84.96  ? 363 THR A OG1   1 
ATOM   2778 C  CG2   . THR A 1 375 ? 114.381 102.589 52.137  1.00 77.15  ? 363 THR A CG2   1 
ATOM   2779 N  N     . THR A 1 376 ? 111.071 101.916 52.572  1.00 77.88  ? 364 THR A N     1 
ATOM   2780 C  CA    . THR A 1 376 ? 109.932 102.797 52.355  1.00 79.62  ? 364 THR A CA    1 
ATOM   2781 C  C     . THR A 1 376 ? 110.252 104.174 52.918  1.00 76.64  ? 364 THR A C     1 
ATOM   2782 O  O     . THR A 1 376 ? 110.652 104.296 54.080  1.00 74.44  ? 364 THR A O     1 
ATOM   2783 C  CB    . THR A 1 376 ? 108.667 102.232 53.006  1.00 80.52  ? 364 THR A CB    1 
ATOM   2784 O  OG1   . THR A 1 376 ? 108.182 101.133 52.227  1.00 87.35  ? 364 THR A OG1   1 
ATOM   2785 C  CG2   . THR A 1 376 ? 107.585 103.294 53.092  1.00 77.21  ? 364 THR A CG2   1 
ATOM   2786 N  N     . ALA A 1 377 ? 110.083 105.201 52.093  1.00 74.52  ? 365 ALA A N     1 
ATOM   2787 C  CA    . ALA A 1 377 ? 110.372 106.574 52.478  1.00 73.42  ? 365 ALA A CA    1 
ATOM   2788 C  C     . ALA A 1 377 ? 109.081 107.283 52.858  1.00 72.09  ? 365 ALA A C     1 
ATOM   2789 O  O     . ALA A 1 377 ? 108.092 107.221 52.121  1.00 74.10  ? 365 ALA A O     1 
ATOM   2790 C  CB    . ALA A 1 377 ? 111.074 107.324 51.347  1.00 75.70  ? 365 ALA A CB    1 
ATOM   2791 N  N     . VAL A 1 378 ? 109.095 107.953 54.005  1.00 70.17  ? 366 VAL A N     1 
ATOM   2792 C  CA    . VAL A 1 378 ? 107.957 108.724 54.488  1.00 68.32  ? 366 VAL A CA    1 
ATOM   2793 C  C     . VAL A 1 378 ? 108.330 110.196 54.406  1.00 70.02  ? 366 VAL A C     1 
ATOM   2794 O  O     . VAL A 1 378 ? 109.283 110.640 55.058  1.00 68.08  ? 366 VAL A O     1 
ATOM   2795 C  CB    . VAL A 1 378 ? 107.571 108.329 55.921  1.00 65.24  ? 366 VAL A CB    1 
ATOM   2796 C  CG1   . VAL A 1 378 ? 106.346 109.104 56.371  1.00 67.72  ? 366 VAL A CG1   1 
ATOM   2797 C  CG2   . VAL A 1 378 ? 107.327 106.833 56.008  1.00 64.86  ? 366 VAL A CG2   1 
ATOM   2798 N  N     . VAL A 1 379 ? 107.582 110.953 53.606  1.00 72.20  ? 367 VAL A N     1 
ATOM   2799 C  CA    . VAL A 1 379 ? 107.843 112.370 53.414  1.00 73.65  ? 367 VAL A CA    1 
ATOM   2800 C  C     . VAL A 1 379 ? 106.612 113.157 53.842  1.00 72.93  ? 367 VAL A C     1 
ATOM   2801 O  O     . VAL A 1 379 ? 105.491 112.645 53.872  1.00 76.47  ? 367 VAL A O     1 
ATOM   2802 C  CB    . VAL A 1 379 ? 108.227 112.706 51.957  1.00 70.17  ? 367 VAL A CB    1 
ATOM   2803 C  CG1   . VAL A 1 379 ? 109.356 111.807 51.484  1.00 73.71  ? 367 VAL A CG1   1 
ATOM   2804 C  CG2   . VAL A 1 379 ? 107.025 112.574 51.046  1.00 74.66  ? 367 VAL A CG2   1 
ATOM   2805 N  N     . GLY A 1 380 ? 106.840 114.416 54.187  1.00 69.97  ? 368 GLY A N     1 
ATOM   2806 C  CA    . GLY A 1 380 ? 105.762 115.279 54.624  1.00 67.43  ? 368 GLY A CA    1 
ATOM   2807 C  C     . GLY A 1 380 ? 106.315 116.575 55.163  1.00 72.34  ? 368 GLY A C     1 
ATOM   2808 O  O     . GLY A 1 380 ? 107.526 116.754 55.313  1.00 73.58  ? 368 GLY A O     1 
ATOM   2809 N  N     . SER A 1 381 ? 105.395 117.487 55.456  1.00 73.70  ? 369 SER A N     1 
ATOM   2810 C  CA    . SER A 1 381 ? 105.767 118.784 55.992  1.00 73.21  ? 369 SER A CA    1 
ATOM   2811 C  C     . SER A 1 381 ? 106.056 118.683 57.487  1.00 67.20  ? 369 SER A C     1 
ATOM   2812 O  O     . SER A 1 381 ? 105.903 117.630 58.112  1.00 63.59  ? 369 SER A O     1 
ATOM   2813 C  CB    . SER A 1 381 ? 104.663 119.807 55.730  1.00 73.08  ? 369 SER A CB    1 
ATOM   2814 O  OG    . SER A 1 381 ? 104.910 120.527 54.535  1.00 80.48  ? 369 SER A OG    1 
ATOM   2815 N  N     . THR A 1 382 ? 106.494 119.800 58.059  1.00 63.69  ? 370 THR A N     1 
ATOM   2816 C  CA    . THR A 1 382 ? 106.725 119.863 59.495  1.00 57.32  ? 370 THR A CA    1 
ATOM   2817 C  C     . THR A 1 382 ? 105.410 119.688 60.244  1.00 59.36  ? 370 THR A C     1 
ATOM   2818 O  O     . THR A 1 382 ? 104.399 120.309 59.904  1.00 65.25  ? 370 THR A O     1 
ATOM   2819 C  CB    . THR A 1 382 ? 107.379 121.196 59.861  1.00 60.03  ? 370 THR A CB    1 
ATOM   2820 O  OG1   . THR A 1 382 ? 108.745 121.189 59.432  1.00 64.60  ? 370 THR A OG1   1 
ATOM   2821 C  CG2   . THR A 1 382 ? 107.326 121.431 61.357  1.00 54.60  ? 370 THR A CG2   1 
ATOM   2822 N  N     . GLY A 1 383 ? 105.423 118.831 61.261  1.00 56.83  ? 371 GLY A N     1 
ATOM   2823 C  CA    . GLY A 1 383 ? 104.218 118.545 62.011  1.00 56.29  ? 371 GLY A CA    1 
ATOM   2824 C  C     . GLY A 1 383 ? 103.205 117.698 61.282  1.00 57.81  ? 371 GLY A C     1 
ATOM   2825 O  O     . GLY A 1 383 ? 102.028 117.708 61.650  1.00 63.96  ? 371 GLY A O     1 
ATOM   2826 N  N     . SER A 1 384 ? 103.625 116.961 60.252  1.00 56.86  ? 372 SER A N     1 
ATOM   2827 C  CA    . SER A 1 384 ? 102.690 116.157 59.474  1.00 58.43  ? 372 SER A CA    1 
ATOM   2828 C  C     . SER A 1 384 ? 102.278 114.889 60.212  1.00 65.41  ? 372 SER A C     1 
ATOM   2829 O  O     . SER A 1 384 ? 101.127 114.455 60.107  1.00 73.24  ? 372 SER A O     1 
ATOM   2830 C  CB    . SER A 1 384 ? 103.303 115.807 58.120  1.00 61.42  ? 372 SER A CB    1 
ATOM   2831 O  OG    . SER A 1 384 ? 102.324 115.299 57.235  1.00 74.46  ? 372 SER A OG    1 
ATOM   2832 N  N     . GLY A 1 385 ? 103.199 114.279 60.953  1.00 61.06  ? 373 GLY A N     1 
ATOM   2833 C  CA    . GLY A 1 385 ? 102.891 113.066 61.684  1.00 53.36  ? 373 GLY A CA    1 
ATOM   2834 C  C     . GLY A 1 385 ? 103.814 111.909 61.366  1.00 55.87  ? 373 GLY A C     1 
ATOM   2835 O  O     . GLY A 1 385 ? 103.475 110.751 61.624  1.00 58.70  ? 373 GLY A O     1 
ATOM   2836 N  N     . LYS A 1 386 ? 104.985 112.206 60.801  1.00 56.01  ? 374 LYS A N     1 
ATOM   2837 C  CA    . LYS A 1 386 ? 105.946 111.154 60.486  1.00 51.80  ? 374 LYS A CA    1 
ATOM   2838 C  C     . LYS A 1 386 ? 106.522 110.535 61.755  1.00 49.93  ? 374 LYS A C     1 
ATOM   2839 O  O     . LYS A 1 386 ? 106.610 109.307 61.874  1.00 49.82  ? 374 LYS A O     1 
ATOM   2840 C  CB    . LYS A 1 386 ? 107.060 111.714 59.603  1.00 53.90  ? 374 LYS A CB    1 
ATOM   2841 C  CG    . LYS A 1 386 ? 106.568 112.340 58.310  1.00 58.32  ? 374 LYS A CG    1 
ATOM   2842 C  CD    . LYS A 1 386 ? 107.697 113.024 57.559  1.00 62.73  ? 374 LYS A CD    1 
ATOM   2843 C  CE    . LYS A 1 386 ? 108.275 114.181 58.352  1.00 57.08  ? 374 LYS A CE    1 
ATOM   2844 N  NZ    . LYS A 1 386 ? 107.300 115.287 58.522  1.00 54.65  ? 374 LYS A NZ    1 
ATOM   2845 N  N     . SER A 1 387 ? 106.922 111.372 62.715  1.00 47.65  ? 375 SER A N     1 
ATOM   2846 C  CA    . SER A 1 387 ? 107.435 110.856 63.979  1.00 44.91  ? 375 SER A CA    1 
ATOM   2847 C  C     . SER A 1 387 ? 106.361 110.107 64.751  1.00 47.83  ? 375 SER A C     1 
ATOM   2848 O  O     . SER A 1 387 ? 106.656 109.096 65.398  1.00 52.77  ? 375 SER A O     1 
ATOM   2849 C  CB    . SER A 1 387 ? 107.998 111.995 64.826  1.00 46.23  ? 375 SER A CB    1 
ATOM   2850 O  OG    . SER A 1 387 ? 109.199 112.498 64.272  1.00 51.50  ? 375 SER A OG    1 
ATOM   2851 N  N     . THR A 1 388 ? 105.118 110.587 64.700  1.00 48.85  ? 376 THR A N     1 
ATOM   2852 C  CA    . THR A 1 388 ? 104.018 109.866 65.328  1.00 49.86  ? 376 THR A CA    1 
ATOM   2853 C  C     . THR A 1 388 ? 103.838 108.488 64.704  1.00 51.57  ? 376 THR A C     1 
ATOM   2854 O  O     . THR A 1 388 ? 103.624 107.501 65.414  1.00 51.13  ? 376 THR A O     1 
ATOM   2855 C  CB    . THR A 1 388 ? 102.729 110.678 65.214  1.00 52.64  ? 376 THR A CB    1 
ATOM   2856 O  OG1   . THR A 1 388 ? 102.908 111.950 65.847  1.00 57.15  ? 376 THR A OG1   1 
ATOM   2857 C  CG2   . THR A 1 388 ? 101.580 109.947 65.873  1.00 52.08  ? 376 THR A CG2   1 
ATOM   2858 N  N     . LEU A 1 389 ? 103.923 108.403 63.376  1.00 51.52  ? 377 LEU A N     1 
ATOM   2859 C  CA    . LEU A 1 389 ? 103.810 107.113 62.704  1.00 49.90  ? 377 LEU A CA    1 
ATOM   2860 C  C     . LEU A 1 389 ? 104.953 106.183 63.095  1.00 47.66  ? 377 LEU A C     1 
ATOM   2861 O  O     . LEU A 1 389 ? 104.742 104.986 63.328  1.00 51.06  ? 377 LEU A O     1 
ATOM   2862 C  CB    . LEU A 1 389 ? 103.774 107.329 61.192  1.00 54.19  ? 377 LEU A CB    1 
ATOM   2863 C  CG    . LEU A 1 389 ? 103.522 106.130 60.284  1.00 61.57  ? 377 LEU A CG    1 
ATOM   2864 C  CD1   . LEU A 1 389 ? 102.121 105.592 60.493  1.00 64.07  ? 377 LEU A CD1   1 
ATOM   2865 C  CD2   . LEU A 1 389 ? 103.728 106.535 58.840  1.00 61.83  ? 377 LEU A CD2   1 
ATOM   2866 N  N     . ILE A 1 390 ? 106.172 106.721 63.177  1.00 51.52  ? 378 ILE A N     1 
ATOM   2867 C  CA    . ILE A 1 390 ? 107.319 105.916 63.591  1.00 48.58  ? 378 ILE A CA    1 
ATOM   2868 C  C     . ILE A 1 390 ? 107.115 105.385 65.004  1.00 46.44  ? 378 ILE A C     1 
ATOM   2869 O  O     . ILE A 1 390 ? 107.384 104.212 65.287  1.00 49.32  ? 378 ILE A O     1 
ATOM   2870 C  CB    . ILE A 1 390 ? 108.616 106.738 63.473  1.00 44.43  ? 378 ILE A CB    1 
ATOM   2871 C  CG1   . ILE A 1 390 ? 108.943 107.010 62.005  1.00 46.11  ? 378 ILE A CG1   1 
ATOM   2872 C  CG2   . ILE A 1 390 ? 109.772 106.022 64.146  1.00 46.64  ? 378 ILE A CG2   1 
ATOM   2873 C  CD1   . ILE A 1 390 ? 109.318 105.776 61.222  1.00 46.07  ? 378 ILE A CD1   1 
ATOM   2874 N  N     . SER A 1 391 ? 106.633 106.237 65.912  1.00 44.19  ? 379 SER A N     1 
ATOM   2875 C  CA    . SER A 1 391 ? 106.371 105.794 67.277  1.00 46.83  ? 379 SER A CA    1 
ATOM   2876 C  C     . SER A 1 391 ? 105.240 104.777 67.335  1.00 50.78  ? 379 SER A C     1 
ATOM   2877 O  O     . SER A 1 391 ? 105.245 103.897 68.203  1.00 57.10  ? 379 SER A O     1 
ATOM   2878 C  CB    . SER A 1 391 ? 106.054 106.993 68.168  1.00 50.35  ? 379 SER A CB    1 
ATOM   2879 O  OG    . SER A 1 391 ? 107.139 107.903 68.197  1.00 49.76  ? 379 SER A OG    1 
ATOM   2880 N  N     . LEU A 1 392 ? 104.256 104.888 66.441  1.00 48.43  ? 380 LEU A N     1 
ATOM   2881 C  CA    . LEU A 1 392 ? 103.204 103.879 66.376  1.00 51.54  ? 380 LEU A CA    1 
ATOM   2882 C  C     . LEU A 1 392 ? 103.763 102.532 65.938  1.00 50.90  ? 380 LEU A C     1 
ATOM   2883 O  O     . LEU A 1 392 ? 103.355 101.486 66.455  1.00 52.36  ? 380 LEU A O     1 
ATOM   2884 C  CB    . LEU A 1 392 ? 102.089 104.327 65.431  1.00 51.21  ? 380 LEU A CB    1 
ATOM   2885 C  CG    . LEU A 1 392 ? 101.192 105.471 65.905  1.00 54.04  ? 380 LEU A CG    1 
ATOM   2886 C  CD1   . LEU A 1 392 ? 100.144 105.787 64.857  1.00 54.81  ? 380 LEU A CD1   1 
ATOM   2887 C  CD2   . LEU A 1 392 ? 100.544 105.141 67.233  1.00 54.40  ? 380 LEU A CD2   1 
ATOM   2888 N  N     . ILE A 1 393 ? 104.697 102.536 64.984  1.00 51.21  ? 381 ILE A N     1 
ATOM   2889 C  CA    . ILE A 1 393 ? 105.328 101.283 64.571  1.00 48.30  ? 381 ILE A CA    1 
ATOM   2890 C  C     . ILE A 1 393 ? 106.075 100.651 65.741  1.00 49.42  ? 381 ILE A C     1 
ATOM   2891 O  O     . ILE A 1 393 ? 106.008 99.435  65.954  1.00 49.42  ? 381 ILE A O     1 
ATOM   2892 C  CB    . ILE A 1 393 ? 106.253 101.514 63.362  1.00 49.61  ? 381 ILE A CB    1 
ATOM   2893 C  CG1   . ILE A 1 393 ? 105.442 101.981 62.154  1.00 53.18  ? 381 ILE A CG1   1 
ATOM   2894 C  CG2   . ILE A 1 393 ? 107.006 100.242 63.016  1.00 47.15  ? 381 ILE A CG2   1 
ATOM   2895 C  CD1   . ILE A 1 393 ? 106.290 102.403 60.979  1.00 51.81  ? 381 ILE A CD1   1 
ATOM   2896 N  N     . CYS A 1 394 ? 106.793 101.464 66.520  1.00 53.80  ? 382 CYS A N     1 
ATOM   2897 C  CA    . CYS A 1 394 ? 107.475 100.973 67.712  1.00 52.86  ? 382 CYS A CA    1 
ATOM   2898 C  C     . CYS A 1 394 ? 106.515 100.607 68.835  1.00 54.42  ? 382 CYS A C     1 
ATOM   2899 O  O     . CYS A 1 394 ? 106.952 100.017 69.828  1.00 59.58  ? 382 CYS A O     1 
ATOM   2900 C  CB    . CYS A 1 394 ? 108.460 102.020 68.234  1.00 49.40  ? 382 CYS A CB    1 
ATOM   2901 S  SG    . CYS A 1 394 ? 109.757 102.497 67.090  1.00 64.08  ? 382 CYS A SG    1 
ATOM   2902 N  N     . ARG A 1 395 ? 105.233 100.945 68.701  1.00 53.02  ? 383 ARG A N     1 
ATOM   2903 C  CA    . ARG A 1 395 ? 104.246 100.797 69.771  1.00 56.26  ? 383 ARG A CA    1 
ATOM   2904 C  C     . ARG A 1 395 ? 104.660 101.573 71.018  1.00 54.32  ? 383 ARG A C     1 
ATOM   2905 O  O     . ARG A 1 395 ? 104.424 101.145 72.148  1.00 59.44  ? 383 ARG A O     1 
ATOM   2906 C  CB    . ARG A 1 395 ? 103.978 99.328  70.103  1.00 62.22  ? 383 ARG A CB    1 
ATOM   2907 C  CG    . ARG A 1 395 ? 102.564 99.088  70.601  1.00 67.07  ? 383 ARG A CG    1 
ATOM   2908 C  CD    . ARG A 1 395 ? 102.424 97.785  71.358  1.00 71.71  ? 383 ARG A CD    1 
ATOM   2909 N  NE    . ARG A 1 395 ? 101.133 97.708  72.031  1.00 74.10  ? 383 ARG A NE    1 
ATOM   2910 C  CZ    . ARG A 1 395 ? 100.897 96.997  73.124  1.00 75.44  ? 383 ARG A CZ    1 
ATOM   2911 N  NH1   . ARG A 1 395 ? 101.833 96.242  73.674  1.00 74.76  ? 383 ARG A NH1   1 
ATOM   2912 N  NH2   . ARG A 1 395 ? 99.689  97.041  73.677  1.00 73.93  ? 383 ARG A NH2   1 
ATOM   2913 N  N     . LEU A 1 396 ? 105.295 102.727 70.810  1.00 51.91  ? 384 LEU A N     1 
ATOM   2914 C  CA    . LEU A 1 396 ? 105.442 103.686 71.897  1.00 51.40  ? 384 LEU A CA    1 
ATOM   2915 C  C     . LEU A 1 396 ? 104.116 104.371 72.192  1.00 56.88  ? 384 LEU A C     1 
ATOM   2916 O  O     . LEU A 1 396 ? 103.885 104.823 73.319  1.00 62.19  ? 384 LEU A O     1 
ATOM   2917 C  CB    . LEU A 1 396 ? 106.515 104.715 71.552  1.00 51.68  ? 384 LEU A CB    1 
ATOM   2918 C  CG    . LEU A 1 396 ? 107.911 104.157 71.276  1.00 53.72  ? 384 LEU A CG    1 
ATOM   2919 C  CD1   . LEU A 1 396 ? 108.830 105.250 70.770  1.00 50.51  ? 384 LEU A CD1   1 
ATOM   2920 C  CD2   . LEU A 1 396 ? 108.485 103.507 72.522  1.00 57.43  ? 384 LEU A CD2   1 
ATOM   2921 N  N     . TYR A 1 397 ? 103.246 104.460 71.191  1.00 56.69  ? 385 TYR A N     1 
ATOM   2922 C  CA    . TYR A 1 397 ? 101.878 104.925 71.345  1.00 55.99  ? 385 TYR A CA    1 
ATOM   2923 C  C     . TYR A 1 397 ? 100.946 103.900 70.721  1.00 62.30  ? 385 TYR A C     1 
ATOM   2924 O  O     . TYR A 1 397 ? 101.329 103.173 69.801  1.00 62.31  ? 385 TYR A O     1 
ATOM   2925 C  CB    . TYR A 1 397 ? 101.662 106.295 70.688  1.00 58.15  ? 385 TYR A CB    1 
ATOM   2926 C  CG    . TYR A 1 397 ? 102.462 107.418 71.306  1.00 58.42  ? 385 TYR A CG    1 
ATOM   2927 C  CD1   . TYR A 1 397 ? 102.043 108.029 72.478  1.00 61.22  ? 385 TYR A CD1   1 
ATOM   2928 C  CD2   . TYR A 1 397 ? 103.631 107.872 70.713  1.00 54.88  ? 385 TYR A CD2   1 
ATOM   2929 C  CE1   . TYR A 1 397 ? 102.768 109.055 73.044  1.00 64.97  ? 385 TYR A CE1   1 
ATOM   2930 C  CE2   . TYR A 1 397 ? 104.362 108.897 71.272  1.00 57.31  ? 385 TYR A CE2   1 
ATOM   2931 C  CZ    . TYR A 1 397 ? 103.927 109.485 72.438  1.00 67.58  ? 385 TYR A CZ    1 
ATOM   2932 O  OH    . TYR A 1 397 ? 104.652 110.509 73.002  1.00 71.39  ? 385 TYR A OH    1 
ATOM   2933 N  N     . ASP A 1 398 ? 99.720  103.843 71.228  1.00 63.16  ? 386 ASP A N     1 
ATOM   2934 C  CA    . ASP A 1 398 ? 98.724  102.892 70.755  1.00 63.76  ? 386 ASP A CA    1 
ATOM   2935 C  C     . ASP A 1 398 ? 97.732  103.600 69.843  1.00 67.94  ? 386 ASP A C     1 
ATOM   2936 O  O     . ASP A 1 398 ? 97.247  104.687 70.174  1.00 71.69  ? 386 ASP A O     1 
ATOM   2937 C  CB    . ASP A 1 398 ? 97.993  102.239 71.928  1.00 69.91  ? 386 ASP A CB    1 
ATOM   2938 C  CG    . ASP A 1 398 ? 98.504  100.846 72.230  1.00 77.08  ? 386 ASP A CG    1 
ATOM   2939 O  OD1   . ASP A 1 398 ? 99.010  100.182 71.302  1.00 76.28  ? 386 ASP A OD1   1 
ATOM   2940 O  OD2   . ASP A 1 398 ? 98.398  100.414 73.397  1.00 78.62  ? 386 ASP A OD2   1 
ATOM   2941 N  N     . VAL A 1 399 ? 97.435  102.982 68.698  1.00 70.06  ? 387 VAL A N     1 
ATOM   2942 C  CA    . VAL A 1 399 ? 96.517  103.589 67.744  1.00 72.53  ? 387 VAL A CA    1 
ATOM   2943 C  C     . VAL A 1 399 ? 95.127  103.695 68.353  1.00 70.55  ? 387 VAL A C     1 
ATOM   2944 O  O     . VAL A 1 399 ? 94.625  102.755 68.983  1.00 73.20  ? 387 VAL A O     1 
ATOM   2945 C  CB    . VAL A 1 399 ? 96.480  102.782 66.435  1.00 70.30  ? 387 VAL A CB    1 
ATOM   2946 C  CG1   . VAL A 1 399 ? 97.650  103.157 65.547  1.00 71.41  ? 387 VAL A CG1   1 
ATOM   2947 C  CG2   . VAL A 1 399 ? 96.488  101.294 66.729  1.00 72.27  ? 387 VAL A CG2   1 
ATOM   2948 N  N     . THR A 1 400 ? 94.504  104.862 68.179  1.00 71.91  ? 388 THR A N     1 
ATOM   2949 C  CA    . THR A 1 400 ? 93.126  105.038 68.622  1.00 74.10  ? 388 THR A CA    1 
ATOM   2950 C  C     . THR A 1 400 ? 92.184  104.114 67.860  1.00 76.42  ? 388 THR A C     1 
ATOM   2951 O  O     . THR A 1 400 ? 91.302  103.482 68.454  1.00 78.87  ? 388 THR A O     1 
ATOM   2952 C  CB    . THR A 1 400 ? 92.708  106.499 68.451  1.00 73.43  ? 388 THR A CB    1 
ATOM   2953 O  OG1   . THR A 1 400 ? 93.263  107.282 69.515  1.00 70.91  ? 388 THR A OG1   1 
ATOM   2954 C  CG2   . THR A 1 400 ? 91.195  106.636 68.467  1.00 78.85  ? 388 THR A CG2   1 
ATOM   2955 N  N     . SER A 1 401 ? 92.370  104.006 66.547  1.00 73.97  ? 389 SER A N     1 
ATOM   2956 C  CA    . SER A 1 401 ? 91.542  103.157 65.707  1.00 75.10  ? 389 SER A CA    1 
ATOM   2957 C  C     . SER A 1 401 ? 92.431  102.437 64.704  1.00 82.02  ? 389 SER A C     1 
ATOM   2958 O  O     . SER A 1 401 ? 93.571  102.837 64.455  1.00 85.17  ? 389 SER A O     1 
ATOM   2959 C  CB    . SER A 1 401 ? 90.459  103.962 64.980  1.00 74.38  ? 389 SER A CB    1 
ATOM   2960 O  OG    . SER A 1 401 ? 89.659  103.121 64.169  1.00 81.05  ? 389 SER A OG    1 
ATOM   2961 N  N     . GLY A 1 402 ? 91.897  101.362 64.133  1.00 81.18  ? 390 GLY A N     1 
ATOM   2962 C  CA    . GLY A 1 402 ? 92.657  100.576 63.185  1.00 81.71  ? 390 GLY A CA    1 
ATOM   2963 C  C     . GLY A 1 402 ? 93.693  99.702  63.871  1.00 85.31  ? 390 GLY A C     1 
ATOM   2964 O  O     . GLY A 1 402 ? 93.569  99.331  65.043  1.00 83.91  ? 390 GLY A O     1 
ATOM   2965 N  N     . SER A 1 403 ? 94.735  99.369  63.115  1.00 84.48  ? 391 SER A N     1 
ATOM   2966 C  CA    . SER A 1 403 ? 95.808  98.522  63.617  1.00 83.84  ? 391 SER A CA    1 
ATOM   2967 C  C     . SER A 1 403 ? 97.058  98.769  62.785  1.00 87.39  ? 391 SER A C     1 
ATOM   2968 O  O     . SER A 1 403 ? 97.008  99.392  61.723  1.00 87.25  ? 391 SER A O     1 
ATOM   2969 C  CB    . SER A 1 403 ? 95.407  97.044  63.587  1.00 87.98  ? 391 SER A CB    1 
ATOM   2970 O  OG    . SER A 1 403 ? 94.974  96.664  62.294  1.00 95.00  ? 391 SER A OG    1 
ATOM   2971 N  N     . LEU A 1 404 ? 98.187  98.275  63.290  1.00 86.64  ? 392 LEU A N     1 
ATOM   2972 C  CA    . LEU A 1 404 ? 99.471  98.389  62.607  1.00 88.01  ? 392 LEU A CA    1 
ATOM   2973 C  C     . LEU A 1 404 ? 99.930  97.094  61.961  1.00 92.29  ? 392 LEU A C     1 
ATOM   2974 O  O     . LEU A 1 404 ? 100.487 97.129  60.864  1.00 93.63  ? 392 LEU A O     1 
ATOM   2975 C  CB    . LEU A 1 404 ? 100.544 98.885  63.581  1.00 80.38  ? 392 LEU A CB    1 
ATOM   2976 C  CG    . LEU A 1 404 ? 100.429 100.378 63.887  1.00 74.59  ? 392 LEU A CG    1 
ATOM   2977 C  CD1   . LEU A 1 404 ? 100.510 100.629 65.378  1.00 77.58  ? 392 LEU A CD1   1 
ATOM   2978 C  CD2   . LEU A 1 404 ? 101.503 101.155 63.148  1.00 64.10  ? 392 LEU A CD2   1 
ATOM   2979 N  N     . ARG A 1 405 ? 99.718  95.952  62.618  1.00 88.89  ? 393 ARG A N     1 
ATOM   2980 C  CA    . ARG A 1 405 ? 99.856  94.629  62.008  1.00 89.23  ? 393 ARG A CA    1 
ATOM   2981 C  C     . ARG A 1 405 ? 101.264 94.404  61.446  1.00 87.46  ? 393 ARG A C     1 
ATOM   2982 O  O     . ARG A 1 405 ? 101.475 94.287  60.238  1.00 88.15  ? 393 ARG A O     1 
ATOM   2983 C  CB    . ARG A 1 405 ? 98.801  94.418  60.916  1.00 87.84  ? 393 ARG A CB    1 
ATOM   2984 C  CG    . ARG A 1 405 ? 97.411  94.884  61.290  1.00 89.47  ? 393 ARG A CG    1 
ATOM   2985 C  CD    . ARG A 1 405 ? 96.589  93.759  61.889  1.00 93.10  ? 393 ARG A CD    1 
ATOM   2986 N  NE    . ARG A 1 405 ? 95.175  93.896  61.564  1.00 99.64  ? 393 ARG A NE    1 
ATOM   2987 C  CZ    . ARG A 1 405 ? 94.648  93.610  60.382  1.00 100.14 ? 393 ARG A CZ    1 
ATOM   2988 N  NH1   . ARG A 1 405 ? 95.387  93.141  59.390  1.00 99.43  ? 393 ARG A NH1   1 
ATOM   2989 N  NH2   . ARG A 1 405 ? 93.345  93.796  60.190  1.00 96.11  ? 393 ARG A NH2   1 
ATOM   2990 N  N     . ILE A 1 406 ? 102.230 94.349  62.357  1.00 84.64  ? 394 ILE A N     1 
ATOM   2991 C  CA    . ILE A 1 406 ? 103.579 93.940  61.982  1.00 86.02  ? 394 ILE A CA    1 
ATOM   2992 C  C     . ILE A 1 406 ? 103.593 92.423  61.826  1.00 87.64  ? 394 ILE A C     1 
ATOM   2993 O  O     . ILE A 1 406 ? 102.973 91.700  62.615  1.00 89.40  ? 394 ILE A O     1 
ATOM   2994 C  CB    . ILE A 1 406 ? 104.612 94.434  63.011  1.00 85.29  ? 394 ILE A CB    1 
ATOM   2995 C  CG1   . ILE A 1 406 ? 105.872 94.924  62.300  1.00 80.16  ? 394 ILE A CG1   1 
ATOM   2996 C  CG2   . ILE A 1 406 ? 104.994 93.354  64.007  1.00 83.50  ? 394 ILE A CG2   1 
ATOM   2997 C  CD1   . ILE A 1 406 ? 106.816 95.674  63.201  1.00 70.21  ? 394 ILE A CD1   1 
ATOM   2998 N  N     . ASP A 1 407 ? 104.238 91.942  60.761  1.00 92.15  ? 395 ASP A N     1 
ATOM   2999 C  CA    . ASP A 1 407 ? 104.245 90.517  60.411  1.00 93.38  ? 395 ASP A CA    1 
ATOM   3000 C  C     . ASP A 1 407 ? 102.833 89.952  60.277  1.00 93.92  ? 395 ASP A C     1 
ATOM   3001 O  O     . ASP A 1 407 ? 102.620 88.747  60.431  1.00 92.75  ? 395 ASP A O     1 
ATOM   3002 C  CB    . ASP A 1 407 ? 105.044 89.696  61.425  1.00 93.99  ? 395 ASP A CB    1 
ATOM   3003 C  CG    . ASP A 1 407 ? 106.300 89.100  60.831  1.00 99.41  ? 395 ASP A CG    1 
ATOM   3004 O  OD1   . ASP A 1 407 ? 106.698 89.538  59.735  1.00 99.81  ? 395 ASP A OD1   1 
ATOM   3005 O  OD2   . ASP A 1 407 ? 106.890 88.196  61.458  1.00 100.98 ? 395 ASP A OD2   1 
ATOM   3006 N  N     . GLY A 1 408 ? 101.859 90.811  59.992  1.00 91.67  ? 396 GLY A N     1 
ATOM   3007 C  CA    . GLY A 1 408 ? 100.478 90.390  59.919  1.00 85.56  ? 396 GLY A CA    1 
ATOM   3008 C  C     . GLY A 1 408 ? 99.782  90.228  61.251  1.00 86.67  ? 396 GLY A C     1 
ATOM   3009 O  O     . GLY A 1 408 ? 98.609  89.838  61.271  1.00 88.70  ? 396 GLY A O     1 
ATOM   3010 N  N     . VAL A 1 409 ? 100.457 90.514  62.362  1.00 88.18  ? 397 VAL A N     1 
ATOM   3011 C  CA    . VAL A 1 409 ? 99.880  90.401  63.696  1.00 86.17  ? 397 VAL A CA    1 
ATOM   3012 C  C     . VAL A 1 409 ? 99.902  91.779  64.344  1.00 88.70  ? 397 VAL A C     1 
ATOM   3013 O  O     . VAL A 1 409 ? 100.842 92.557  64.139  1.00 89.97  ? 397 VAL A O     1 
ATOM   3014 C  CB    . VAL A 1 409 ? 100.622 89.358  64.554  1.00 86.87  ? 397 VAL A CB    1 
ATOM   3015 C  CG1   . VAL A 1 409 ? 100.917 88.110  63.737  1.00 85.99  ? 397 VAL A CG1   1 
ATOM   3016 C  CG2   . VAL A 1 409 ? 101.909 89.924  65.124  1.00 86.24  ? 397 VAL A CG2   1 
ATOM   3017 N  N     . ASP A 1 410 ? 98.849  92.093  65.094  1.00 87.07  ? 398 ASP A N     1 
ATOM   3018 C  CA    . ASP A 1 410 ? 98.741  93.400  65.726  1.00 83.58  ? 398 ASP A CA    1 
ATOM   3019 C  C     . ASP A 1 410 ? 99.879  93.611  66.716  1.00 83.91  ? 398 ASP A C     1 
ATOM   3020 O  O     . ASP A 1 410 ? 100.296 92.685  67.416  1.00 84.55  ? 398 ASP A O     1 
ATOM   3021 C  CB    . ASP A 1 410 ? 97.392  93.528  66.434  1.00 82.60  ? 398 ASP A CB    1 
ATOM   3022 C  CG    . ASP A 1 410 ? 97.001  94.968  66.695  1.00 86.25  ? 398 ASP A CG    1 
ATOM   3023 O  OD1   . ASP A 1 410 ? 97.874  95.764  67.097  1.00 87.94  ? 398 ASP A OD1   1 
ATOM   3024 O  OD2   . ASP A 1 410 ? 95.815  95.306  66.497  1.00 86.96  ? 398 ASP A OD2   1 
ATOM   3025 N  N     . VAL A 1 411 ? 100.391 94.844  66.762  1.00 81.34  ? 399 VAL A N     1 
ATOM   3026 C  CA    . VAL A 1 411 ? 101.441 95.171  67.723  1.00 79.68  ? 399 VAL A CA    1 
ATOM   3027 C  C     . VAL A 1 411 ? 100.913 95.077  69.147  1.00 79.86  ? 399 VAL A C     1 
ATOM   3028 O  O     . VAL A 1 411 ? 101.679 94.838  70.087  1.00 80.86  ? 399 VAL A O     1 
ATOM   3029 C  CB    . VAL A 1 411 ? 102.033 96.562  67.428  1.00 70.57  ? 399 VAL A CB    1 
ATOM   3030 C  CG1   . VAL A 1 411 ? 102.699 96.572  66.065  1.00 73.19  ? 399 VAL A CG1   1 
ATOM   3031 C  CG2   . VAL A 1 411 ? 100.958 97.626  67.502  1.00 75.29  ? 399 VAL A CG2   1 
ATOM   3032 N  N     . ARG A 1 412 ? 99.605  95.271  69.335  1.00 78.35  ? 400 ARG A N     1 
ATOM   3033 C  CA    . ARG A 1 412 ? 99.018  95.087  70.657  1.00 79.13  ? 400 ARG A CA    1 
ATOM   3034 C  C     . ARG A 1 412 ? 99.025  93.623  71.071  1.00 83.47  ? 400 ARG A C     1 
ATOM   3035 O  O     . ARG A 1 412 ? 99.159  93.318  72.260  1.00 85.28  ? 400 ARG A O     1 
ATOM   3036 C  CB    . ARG A 1 412 ? 97.594  95.640  70.683  1.00 79.65  ? 400 ARG A CB    1 
ATOM   3037 C  CG    . ARG A 1 412 ? 97.515  97.154  70.614  1.00 81.86  ? 400 ARG A CG    1 
ATOM   3038 C  CD    . ARG A 1 412 ? 96.113  97.622  70.262  1.00 79.52  ? 400 ARG A CD    1 
ATOM   3039 N  NE    . ARG A 1 412 ? 95.784  97.347  68.870  1.00 84.01  ? 400 ARG A NE    1 
ATOM   3040 C  CZ    . ARG A 1 412 ? 94.848  97.985  68.182  1.00 84.85  ? 400 ARG A CZ    1 
ATOM   3041 N  NH1   . ARG A 1 412 ? 94.122  98.945  68.730  1.00 77.78  ? 400 ARG A NH1   1 
ATOM   3042 N  NH2   . ARG A 1 412 ? 94.637  97.653  66.912  1.00 87.40  ? 400 ARG A NH2   1 
ATOM   3043 N  N     . ASP A 1 413 ? 98.881  92.709  70.111  1.00 86.41  ? 401 ASP A N     1 
ATOM   3044 C  CA    . ASP A 1 413 ? 98.882  91.284  70.413  1.00 83.85  ? 401 ASP A CA    1 
ATOM   3045 C  C     . ASP A 1 413 ? 100.277 90.738  70.679  1.00 83.97  ? 401 ASP A C     1 
ATOM   3046 O  O     . ASP A 1 413 ? 100.404 89.588  71.109  1.00 89.83  ? 401 ASP A O     1 
ATOM   3047 C  CB    . ASP A 1 413 ? 98.234  90.507  69.267  1.00 84.31  ? 401 ASP A CB    1 
ATOM   3048 C  CG    . ASP A 1 413 ? 96.790  90.904  69.041  1.00 84.89  ? 401 ASP A CG    1 
ATOM   3049 O  OD1   . ASP A 1 413 ? 96.257  91.690  69.851  1.00 78.00  ? 401 ASP A OD1   1 
ATOM   3050 O  OD2   . ASP A 1 413 ? 96.188  90.431  68.055  1.00 87.12  ? 401 ASP A OD2   1 
ATOM   3051 N  N     . LEU A 1 414 ? 101.318 91.521  70.420  1.00 83.32  ? 402 LEU A N     1 
ATOM   3052 C  CA    . LEU A 1 414 ? 102.674 91.102  70.728  1.00 87.01  ? 402 LEU A CA    1 
ATOM   3053 C  C     . LEU A 1 414 ? 103.074 91.563  72.124  1.00 88.47  ? 402 LEU A C     1 
ATOM   3054 O  O     . LEU A 1 414 ? 102.523 92.518  72.676  1.00 90.13  ? 402 LEU A O     1 
ATOM   3055 C  CB    . LEU A 1 414 ? 103.665 91.668  69.711  1.00 84.12  ? 402 LEU A CB    1 
ATOM   3056 C  CG    . LEU A 1 414 ? 103.544 91.234  68.254  1.00 82.87  ? 402 LEU A CG    1 
ATOM   3057 C  CD1   . LEU A 1 414 ? 104.502 92.035  67.397  1.00 72.56  ? 402 LEU A CD1   1 
ATOM   3058 C  CD2   . LEU A 1 414 ? 103.840 89.754  68.142  1.00 89.00  ? 402 LEU A CD2   1 
ATOM   3059 N  N     . ASP A 1 415 ? 104.048 90.865  72.695  1.00 85.37  ? 403 ASP A N     1 
ATOM   3060 C  CA    . ASP A 1 415 ? 104.743 91.359  73.872  1.00 86.12  ? 403 ASP A CA    1 
ATOM   3061 C  C     . ASP A 1 415 ? 105.826 92.320  73.416  1.00 82.27  ? 403 ASP A C     1 
ATOM   3062 O  O     . ASP A 1 415 ? 106.576 92.025  72.482  1.00 79.29  ? 403 ASP A O     1 
ATOM   3063 C  CB    . ASP A 1 415 ? 105.362 90.215  74.676  1.00 89.14  ? 403 ASP A CB    1 
ATOM   3064 C  CG    . ASP A 1 415 ? 106.228 89.308  73.828  1.00 93.01  ? 403 ASP A CG    1 
ATOM   3065 O  OD1   . ASP A 1 415 ? 105.945 89.179  72.619  1.00 94.80  ? 403 ASP A OD1   1 
ATOM   3066 O  OD2   . ASP A 1 415 ? 107.196 88.731  74.368  1.00 84.26  ? 403 ASP A OD2   1 
ATOM   3067 N  N     . ILE A 1 416 ? 105.908 93.476  74.067  1.00 79.47  ? 404 ILE A N     1 
ATOM   3068 C  CA    . ILE A 1 416 ? 106.923 94.427  73.642  1.00 69.78  ? 404 ILE A CA    1 
ATOM   3069 C  C     . ILE A 1 416 ? 108.247 94.135  74.336  1.00 70.68  ? 404 ILE A C     1 
ATOM   3070 O  O     . ILE A 1 416 ? 108.720 94.897  75.182  1.00 76.22  ? 404 ILE A O     1 
ATOM   3071 C  CB    . ILE A 1 416 ? 106.433 95.878  73.858  1.00 68.78  ? 404 ILE A CB    1 
ATOM   3072 C  CG1   . ILE A 1 416 ? 105.628 96.060  75.165  1.00 69.75  ? 404 ILE A CG1   1 
ATOM   3073 C  CG2   . ILE A 1 416 ? 105.619 96.352  72.664  1.00 69.76  ? 404 ILE A CG2   1 
ATOM   3074 C  CD1   . ILE A 1 416 ? 106.298 95.756  76.489  1.00 70.67  ? 404 ILE A CD1   1 
ATOM   3075 N  N     . GLU A 1 417 ? 108.869 93.050  73.932  1.00 69.64  ? 405 GLU A N     1 
ATOM   3076 C  CA    . GLU A 1 417 ? 110.300 92.806  73.997  1.00 68.07  ? 405 GLU A CA    1 
ATOM   3077 C  C     . GLU A 1 417 ? 110.825 92.232  72.694  1.00 67.69  ? 405 GLU A C     1 
ATOM   3078 O  O     . GLU A 1 417 ? 111.880 92.651  72.225  1.00 74.30  ? 405 GLU A O     1 
ATOM   3079 C  CB    . GLU A 1 417 ? 110.641 91.868  75.167  1.00 76.82  ? 405 GLU A CB    1 
ATOM   3080 C  CG    . GLU A 1 417 ? 110.641 92.508  76.566  1.00 79.94  ? 405 GLU A CG    1 
ATOM   3081 C  CD    . GLU A 1 417 ? 111.190 93.933  76.631  1.00 80.29  ? 405 GLU A CD    1 
ATOM   3082 O  OE1   . GLU A 1 417 ? 110.804 94.661  77.569  1.00 77.91  ? 405 GLU A OE1   1 
ATOM   3083 O  OE2   . GLU A 1 417 ? 112.053 94.312  75.810  1.00 74.10  ? 405 GLU A OE2   1 
ATOM   3084 N  N     . GLN A 1 418 ? 110.074 91.325  72.066  1.00 68.07  ? 406 GLN A N     1 
ATOM   3085 C  CA    . GLN A 1 418 ? 110.491 90.765  70.786  1.00 66.08  ? 406 GLN A CA    1 
ATOM   3086 C  C     . GLN A 1 418 ? 110.293 91.772  69.662  1.00 65.19  ? 406 GLN A C     1 
ATOM   3087 O  O     . GLN A 1 418 ? 111.122 91.865  68.746  1.00 64.98  ? 406 GLN A O     1 
ATOM   3088 C  CB    . GLN A 1 418 ? 109.717 89.475  70.515  1.00 70.72  ? 406 GLN A CB    1 
ATOM   3089 C  CG    . GLN A 1 418 ? 109.524 89.143  69.051  1.00 81.53  ? 406 GLN A CG    1 
ATOM   3090 C  CD    . GLN A 1 418 ? 109.011 87.734  68.839  1.00 88.73  ? 406 GLN A CD    1 
ATOM   3091 O  OE1   . GLN A 1 418 ? 107.874 87.417  69.184  1.00 88.92  ? 406 GLN A OE1   1 
ATOM   3092 N  NE2   . GLN A 1 418 ? 109.850 86.879  68.265  1.00 90.24  ? 406 GLN A NE2   1 
ATOM   3093 N  N     . LEU A 1 419 ? 109.209 92.547  69.729  1.00 64.88  ? 407 LEU A N     1 
ATOM   3094 C  CA    . LEU A 1 419 ? 108.995 93.621  68.766  1.00 60.85  ? 407 LEU A CA    1 
ATOM   3095 C  C     . LEU A 1 419 ? 110.142 94.619  68.799  1.00 60.24  ? 407 LEU A C     1 
ATOM   3096 O  O     . LEU A 1 419 ? 110.622 95.062  67.750  1.00 64.17  ? 407 LEU A O     1 
ATOM   3097 C  CB    . LEU A 1 419 ? 107.669 94.321  69.058  1.00 62.34  ? 407 LEU A CB    1 
ATOM   3098 C  CG    . LEU A 1 419 ? 107.357 95.599  68.280  1.00 59.65  ? 407 LEU A CG    1 
ATOM   3099 C  CD1   . LEU A 1 419 ? 107.132 95.291  66.813  1.00 63.83  ? 407 LEU A CD1   1 
ATOM   3100 C  CD2   . LEU A 1 419 ? 106.154 96.309  68.877  1.00 59.92  ? 407 LEU A CD2   1 
ATOM   3101 N  N     . TRP A 1 420 ? 110.602 94.978  69.996  1.00 58.24  ? 408 TRP A N     1 
ATOM   3102 C  CA    . TRP A 1 420 ? 111.713 95.911  70.120  1.00 54.91  ? 408 TRP A CA    1 
ATOM   3103 C  C     . TRP A 1 420 ? 113.052 95.267  69.784  1.00 57.93  ? 408 TRP A C     1 
ATOM   3104 O  O     . TRP A 1 420 ? 113.955 95.952  69.291  1.00 61.69  ? 408 TRP A O     1 
ATOM   3105 C  CB    . TRP A 1 420 ? 111.743 96.496  71.529  1.00 52.87  ? 408 TRP A CB    1 
ATOM   3106 C  CG    . TRP A 1 420 ? 110.584 97.383  71.813  1.00 53.69  ? 408 TRP A CG    1 
ATOM   3107 C  CD1   . TRP A 1 420 ? 109.827 98.054  70.901  1.00 56.03  ? 408 TRP A CD1   1 
ATOM   3108 C  CD2   . TRP A 1 420 ? 110.049 97.708  73.097  1.00 55.87  ? 408 TRP A CD2   1 
ATOM   3109 N  NE1   . TRP A 1 420 ? 108.848 98.773  71.537  1.00 57.55  ? 408 TRP A NE1   1 
ATOM   3110 C  CE2   . TRP A 1 420 ? 108.963 98.578  72.887  1.00 56.90  ? 408 TRP A CE2   1 
ATOM   3111 C  CE3   . TRP A 1 420 ? 110.380 97.346  74.403  1.00 56.39  ? 408 TRP A CE3   1 
ATOM   3112 C  CZ2   . TRP A 1 420 ? 108.208 99.091  73.935  1.00 55.42  ? 408 TRP A CZ2   1 
ATOM   3113 C  CZ3   . TRP A 1 420 ? 109.629 97.854  75.439  1.00 52.34  ? 408 TRP A CZ3   1 
ATOM   3114 C  CH2   . TRP A 1 420 ? 108.554 98.715  75.200  1.00 51.95  ? 408 TRP A CH2   1 
ATOM   3115 N  N     . SER A 1 421 ? 113.206 93.967  70.043  1.00 56.20  ? 409 SER A N     1 
ATOM   3116 C  CA    . SER A 1 421 ? 114.437 93.283  69.669  1.00 57.21  ? 409 SER A CA    1 
ATOM   3117 C  C     . SER A 1 421 ? 114.574 93.165  68.159  1.00 60.60  ? 409 SER A C     1 
ATOM   3118 O  O     . SER A 1 421 ? 115.696 93.138  67.640  1.00 62.55  ? 409 SER A O     1 
ATOM   3119 C  CB    . SER A 1 421 ? 114.487 91.902  70.319  1.00 56.34  ? 409 SER A CB    1 
ATOM   3120 O  OG    . SER A 1 421 ? 115.756 91.300  70.135  1.00 58.91  ? 409 SER A OG    1 
ATOM   3121 N  N     . ALA A 1 422 ? 113.455 93.088  67.440  1.00 60.68  ? 410 ALA A N     1 
ATOM   3122 C  CA    . ALA A 1 422 ? 113.504 93.024  65.986  1.00 63.84  ? 410 ALA A CA    1 
ATOM   3123 C  C     . ALA A 1 422 ? 113.658 94.389  65.331  1.00 63.46  ? 410 ALA A C     1 
ATOM   3124 O  O     . ALA A 1 422 ? 113.877 94.451  64.117  1.00 64.88  ? 410 ALA A O     1 
ATOM   3125 C  CB    . ALA A 1 422 ? 112.245 92.348  65.446  1.00 69.72  ? 410 ALA A CB    1 
ATOM   3126 N  N     . ILE A 1 423 ? 113.561 95.473  66.093  1.00 59.97  ? 411 ILE A N     1 
ATOM   3127 C  CA    . ILE A 1 423 ? 113.569 96.828  65.555  1.00 58.88  ? 411 ILE A CA    1 
ATOM   3128 C  C     . ILE A 1 423 ? 114.824 97.537  66.040  1.00 58.55  ? 411 ILE A C     1 
ATOM   3129 O  O     . ILE A 1 423 ? 115.103 97.566  67.244  1.00 59.42  ? 411 ILE A O     1 
ATOM   3130 C  CB    . ILE A 1 423 ? 112.310 97.607  65.972  1.00 57.09  ? 411 ILE A CB    1 
ATOM   3131 C  CG1   . ILE A 1 423 ? 111.088 97.110  65.202  1.00 58.45  ? 411 ILE A CG1   1 
ATOM   3132 C  CG2   . ILE A 1 423 ? 112.506 99.098  65.752  1.00 54.54  ? 411 ILE A CG2   1 
ATOM   3133 C  CD1   . ILE A 1 423 ? 109.785 97.668  65.718  1.00 53.28  ? 411 ILE A CD1   1 
ATOM   3134 N  N     . GLY A 1 424 ? 115.582 98.098  65.103  1.00 58.39  ? 412 GLY A N     1 
ATOM   3135 C  CA    . GLY A 1 424 ? 116.690 98.969  65.437  1.00 51.28  ? 412 GLY A CA    1 
ATOM   3136 C  C     . GLY A 1 424 ? 116.330 100.407 65.140  1.00 50.15  ? 412 GLY A C     1 
ATOM   3137 O  O     . GLY A 1 424 ? 116.309 100.823 63.979  1.00 51.79  ? 412 GLY A O     1 
ATOM   3138 N  N     . LEU A 1 425 ? 116.044 101.174 66.184  1.00 50.55  ? 413 LEU A N     1 
ATOM   3139 C  CA    . LEU A 1 425 ? 115.453 102.496 66.053  1.00 45.61  ? 413 LEU A CA    1 
ATOM   3140 C  C     . LEU A 1 425 ? 116.472 103.565 66.411  1.00 45.95  ? 413 LEU A C     1 
ATOM   3141 O  O     . LEU A 1 425 ? 117.109 103.494 67.467  1.00 52.59  ? 413 LEU A O     1 
ATOM   3142 C  CB    . LEU A 1 425 ? 114.222 102.625 66.952  1.00 45.58  ? 413 LEU A CB    1 
ATOM   3143 C  CG    . LEU A 1 425 ? 113.674 104.031 67.195  1.00 44.35  ? 413 LEU A CG    1 
ATOM   3144 C  CD1   . LEU A 1 425 ? 112.863 104.507 66.003  1.00 45.43  ? 413 LEU A CD1   1 
ATOM   3145 C  CD2   . LEU A 1 425 ? 112.848 104.068 68.465  1.00 38.21  ? 413 LEU A CD2   1 
ATOM   3146 N  N     . VAL A 1 426 ? 116.624 104.547 65.532  1.00 42.73  ? 414 VAL A N     1 
ATOM   3147 C  CA    . VAL A 1 426 ? 117.347 105.777 65.827  1.00 42.69  ? 414 VAL A CA    1 
ATOM   3148 C  C     . VAL A 1 426 ? 116.323 106.911 65.830  1.00 44.96  ? 414 VAL A C     1 
ATOM   3149 O  O     . VAL A 1 426 ? 115.854 107.332 64.763  1.00 47.22  ? 414 VAL A O     1 
ATOM   3150 C  CB    . VAL A 1 426 ? 118.485 106.027 64.827  1.00 41.55  ? 414 VAL A CB    1 
ATOM   3151 C  CG1   . VAL A 1 426 ? 118.062 105.650 63.428  1.00 44.00  ? 414 VAL A CG1   1 
ATOM   3152 C  CG2   . VAL A 1 426 ? 118.956 107.472 64.887  1.00 44.87  ? 414 VAL A CG2   1 
ATOM   3153 N  N     . PRO A 1 427 ? 115.913 107.400 66.994  1.00 44.25  ? 415 PRO A N     1 
ATOM   3154 C  CA    . PRO A 1 427 ? 114.816 108.368 67.055  1.00 46.19  ? 415 PRO A CA    1 
ATOM   3155 C  C     . PRO A 1 427 ? 115.259 109.760 66.622  1.00 47.61  ? 415 PRO A C     1 
ATOM   3156 O  O     . PRO A 1 427 ? 116.445 110.083 66.560  1.00 50.73  ? 415 PRO A O     1 
ATOM   3157 C  CB    . PRO A 1 427 ? 114.418 108.347 68.533  1.00 47.58  ? 415 PRO A CB    1 
ATOM   3158 C  CG    . PRO A 1 427 ? 115.662 107.966 69.239  1.00 45.02  ? 415 PRO A CG    1 
ATOM   3159 C  CD    . PRO A 1 427 ? 116.392 107.020 68.333  1.00 40.95  ? 415 PRO A CD    1 
ATOM   3160 N  N     . GLN A 1 428 ? 114.260 110.588 66.311  1.00 48.73  ? 416 GLN A N     1 
ATOM   3161 C  CA    . GLN A 1 428 ? 114.534 111.976 65.955  1.00 49.07  ? 416 GLN A CA    1 
ATOM   3162 C  C     . GLN A 1 428 ? 115.122 112.737 67.136  1.00 51.42  ? 416 GLN A C     1 
ATOM   3163 O  O     . GLN A 1 428 ? 116.046 113.541 66.967  1.00 53.75  ? 416 GLN A O     1 
ATOM   3164 C  CB    . GLN A 1 428 ? 113.259 112.647 65.449  1.00 42.75  ? 416 GLN A CB    1 
ATOM   3165 C  CG    . GLN A 1 428 ? 113.404 114.128 65.187  1.00 40.65  ? 416 GLN A CG    1 
ATOM   3166 C  CD    . GLN A 1 428 ? 112.521 114.607 64.060  1.00 47.45  ? 416 GLN A CD    1 
ATOM   3167 O  OE1   . GLN A 1 428 ? 111.296 114.559 64.152  1.00 53.70  ? 416 GLN A OE1   1 
ATOM   3168 N  NE2   . GLN A 1 428 ? 113.139 115.079 62.987  1.00 49.86  ? 416 GLN A NE2   1 
ATOM   3169 N  N     . ARG A 1 429 ? 114.602 112.501 68.335  1.00 51.50  ? 417 ARG A N     1 
ATOM   3170 C  CA    . ARG A 1 429 ? 115.181 113.019 69.571  1.00 54.00  ? 417 ARG A CA    1 
ATOM   3171 C  C     . ARG A 1 429 ? 115.872 111.844 70.255  1.00 58.72  ? 417 ARG A C     1 
ATOM   3172 O  O     . ARG A 1 429 ? 115.234 111.065 70.968  1.00 60.13  ? 417 ARG A O     1 
ATOM   3173 C  CB    . ARG A 1 429 ? 114.114 113.651 70.461  1.00 59.98  ? 417 ARG A CB    1 
ATOM   3174 C  CG    . ARG A 1 429 ? 114.612 114.052 71.843  1.00 67.30  ? 417 ARG A CG    1 
ATOM   3175 C  CD    . ARG A 1 429 ? 113.937 115.323 72.335  1.00 69.59  ? 417 ARG A CD    1 
ATOM   3176 N  NE    . ARG A 1 429 ? 114.084 115.495 73.775  1.00 79.78  ? 417 ARG A NE    1 
ATOM   3177 C  CZ    . ARG A 1 429 ? 114.835 116.427 74.347  1.00 79.29  ? 417 ARG A CZ    1 
ATOM   3178 N  NH1   . ARG A 1 429 ? 115.522 117.299 73.628  1.00 70.82  ? 417 ARG A NH1   1 
ATOM   3179 N  NH2   . ARG A 1 429 ? 114.900 116.483 75.674  1.00 81.63  ? 417 ARG A NH2   1 
ATOM   3180 N  N     . GLY A 1 430 ? 117.177 111.711 70.022  1.00 57.26  ? 418 GLY A N     1 
ATOM   3181 C  CA    . GLY A 1 430 ? 117.948 110.604 70.531  1.00 54.41  ? 418 GLY A CA    1 
ATOM   3182 C  C     . GLY A 1 430 ? 118.583 110.892 71.879  1.00 56.56  ? 418 GLY A C     1 
ATOM   3183 O  O     . GLY A 1 430 ? 118.378 111.940 72.493  1.00 59.15  ? 418 GLY A O     1 
ATOM   3184 N  N     . TYR A 1 431 ? 119.375 109.925 72.336  1.00 47.50  ? 419 TYR A N     1 
ATOM   3185 C  CA    . TYR A 1 431 ? 120.068 110.043 73.611  1.00 37.56  ? 419 TYR A CA    1 
ATOM   3186 C  C     . TYR A 1 431 ? 121.296 109.148 73.598  1.00 41.03  ? 419 TYR A C     1 
ATOM   3187 O  O     . TYR A 1 431 ? 121.212 107.983 73.202  1.00 42.12  ? 419 TYR A O     1 
ATOM   3188 C  CB    . TYR A 1 431 ? 119.149 109.664 74.776  1.00 34.57  ? 419 TYR A CB    1 
ATOM   3189 C  CG    . TYR A 1 431 ? 119.701 110.042 76.129  1.00 35.48  ? 419 TYR A CG    1 
ATOM   3190 C  CD1   . TYR A 1 431 ? 119.653 111.352 76.579  1.00 35.44  ? 419 TYR A CD1   1 
ATOM   3191 C  CD2   . TYR A 1 431 ? 120.280 109.089 76.951  1.00 35.38  ? 419 TYR A CD2   1 
ATOM   3192 C  CE1   . TYR A 1 431 ? 120.160 111.699 77.812  1.00 36.00  ? 419 TYR A CE1   1 
ATOM   3193 C  CE2   . TYR A 1 431 ? 120.788 109.426 78.185  1.00 38.41  ? 419 TYR A CE2   1 
ATOM   3194 C  CZ    . TYR A 1 431 ? 120.726 110.732 78.610  1.00 41.29  ? 419 TYR A CZ    1 
ATOM   3195 O  OH    . TYR A 1 431 ? 121.235 111.071 79.841  1.00 45.86  ? 419 TYR A OH    1 
ATOM   3196 N  N     . LEU A 1 432 ? 122.428 109.698 74.026  1.00 37.63  ? 420 LEU A N     1 
ATOM   3197 C  CA    . LEU A 1 432 ? 123.647 108.936 74.250  1.00 33.82  ? 420 LEU A CA    1 
ATOM   3198 C  C     . LEU A 1 432 ? 123.971 108.988 75.732  1.00 35.78  ? 420 LEU A C     1 
ATOM   3199 O  O     . LEU A 1 432 ? 123.965 110.066 76.330  1.00 40.08  ? 420 LEU A O     1 
ATOM   3200 C  CB    . LEU A 1 432 ? 124.813 109.488 73.429  1.00 34.56  ? 420 LEU A CB    1 
ATOM   3201 C  CG    . LEU A 1 432 ? 124.722 109.324 71.913  1.00 38.22  ? 420 LEU A CG    1 
ATOM   3202 C  CD1   . LEU A 1 432 ? 125.795 110.148 71.242  1.00 35.27  ? 420 LEU A CD1   1 
ATOM   3203 C  CD2   . LEU A 1 432 ? 124.837 107.865 71.516  1.00 34.25  ? 420 LEU A CD2   1 
ATOM   3204 N  N     . PHE A 1 433 ? 124.248 107.831 76.320  1.00 39.85  ? 421 PHE A N     1 
ATOM   3205 C  CA    . PHE A 1 433 ? 124.452 107.740 77.755  1.00 39.72  ? 421 PHE A CA    1 
ATOM   3206 C  C     . PHE A 1 433 ? 125.874 108.134 78.139  1.00 39.52  ? 421 PHE A C     1 
ATOM   3207 O  O     . PHE A 1 433 ? 126.812 108.048 77.343  1.00 38.36  ? 421 PHE A O     1 
ATOM   3208 C  CB    . PHE A 1 433 ? 124.154 106.325 78.247  1.00 43.41  ? 421 PHE A CB    1 
ATOM   3209 C  CG    . PHE A 1 433 ? 122.767 105.859 77.931  1.00 40.91  ? 421 PHE A CG    1 
ATOM   3210 C  CD1   . PHE A 1 433 ? 122.485 105.255 76.720  1.00 37.44  ? 421 PHE A CD1   1 
ATOM   3211 C  CD2   . PHE A 1 433 ? 121.744 106.029 78.843  1.00 37.03  ? 421 PHE A CD2   1 
ATOM   3212 C  CE1   . PHE A 1 433 ? 121.212 104.832 76.427  1.00 38.12  ? 421 PHE A CE1   1 
ATOM   3213 C  CE2   . PHE A 1 433 ? 120.470 105.606 78.555  1.00 40.17  ? 421 PHE A CE2   1 
ATOM   3214 C  CZ    . PHE A 1 433 ? 120.204 105.006 77.344  1.00 42.75  ? 421 PHE A CZ    1 
ATOM   3215 N  N     . SER A 1 434 ? 126.020 108.572 79.386  1.00 40.77  ? 422 SER A N     1 
ATOM   3216 C  CA    . SER A 1 434 ? 127.336 108.869 79.930  1.00 40.06  ? 422 SER A CA    1 
ATOM   3217 C  C     . SER A 1 434 ? 128.159 107.594 80.045  1.00 43.10  ? 422 SER A C     1 
ATOM   3218 O  O     . SER A 1 434 ? 127.645 106.533 80.409  1.00 48.76  ? 422 SER A O     1 
ATOM   3219 C  CB    . SER A 1 434 ? 127.206 109.536 81.297  1.00 43.24  ? 422 SER A CB    1 
ATOM   3220 O  OG    . SER A 1 434 ? 128.282 110.422 81.536  1.00 50.56  ? 422 SER A OG    1 
ATOM   3221 N  N     . GLY A 1 435 ? 129.444 107.700 79.731  1.00 41.16  ? 423 GLY A N     1 
ATOM   3222 C  CA    . GLY A 1 435 ? 130.321 106.549 79.766  1.00 43.54  ? 423 GLY A CA    1 
ATOM   3223 C  C     . GLY A 1 435 ? 131.305 106.547 78.618  1.00 46.85  ? 423 GLY A C     1 
ATOM   3224 O  O     . GLY A 1 435 ? 131.901 107.579 78.308  1.00 51.85  ? 423 GLY A O     1 
ATOM   3225 N  N     . THR A 1 436 ? 131.479 105.400 77.975  1.00 46.48  ? 424 THR A N     1 
ATOM   3226 C  CA    . THR A 1 436 ? 132.393 105.264 76.854  1.00 47.04  ? 424 THR A CA    1 
ATOM   3227 C  C     . THR A 1 436 ? 131.612 104.967 75.582  1.00 44.87  ? 424 THR A C     1 
ATOM   3228 O  O     . THR A 1 436 ? 130.422 104.644 75.612  1.00 44.94  ? 424 THR A O     1 
ATOM   3229 C  CB    . THR A 1 436 ? 133.431 104.163 77.112  1.00 53.49  ? 424 THR A CB    1 
ATOM   3230 O  OG1   . THR A 1 436 ? 132.783 102.887 77.149  1.00 54.02  ? 424 THR A OG1   1 
ATOM   3231 C  CG2   . THR A 1 436 ? 134.143 104.398 78.429  1.00 51.50  ? 424 THR A CG2   1 
ATOM   3232 N  N     . VAL A 1 437 ? 132.303 105.097 74.448  1.00 46.35  ? 425 VAL A N     1 
ATOM   3233 C  CA    . VAL A 1 437 ? 131.692 104.785 73.160  1.00 43.70  ? 425 VAL A CA    1 
ATOM   3234 C  C     . VAL A 1 437 ? 131.310 103.313 73.097  1.00 48.24  ? 425 VAL A C     1 
ATOM   3235 O  O     . VAL A 1 437 ? 130.233 102.957 72.605  1.00 50.53  ? 425 VAL A O     1 
ATOM   3236 C  CB    . VAL A 1 437 ? 132.639 105.180 72.011  1.00 45.34  ? 425 VAL A CB    1 
ATOM   3237 C  CG1   . VAL A 1 437 ? 132.234 104.496 70.719  1.00 43.08  ? 425 VAL A CG1   1 
ATOM   3238 C  CG2   . VAL A 1 437 ? 132.647 106.684 71.831  1.00 45.76  ? 425 VAL A CG2   1 
ATOM   3239 N  N     . ALA A 1 438 ? 132.187 102.435 73.588  1.00 51.34  ? 426 ALA A N     1 
ATOM   3240 C  CA    . ALA A 1 438 ? 131.889 101.006 73.590  1.00 45.88  ? 426 ALA A CA    1 
ATOM   3241 C  C     . ALA A 1 438 ? 130.681 100.691 74.464  1.00 45.91  ? 426 ALA A C     1 
ATOM   3242 O  O     . ALA A 1 438 ? 129.840 99.864  74.097  1.00 46.72  ? 426 ALA A O     1 
ATOM   3243 C  CB    . ALA A 1 438 ? 133.109 100.216 74.058  1.00 48.98  ? 426 ALA A CB    1 
ATOM   3244 N  N     . GLU A 1 439 ? 130.581 101.338 75.627  1.00 48.30  ? 427 GLU A N     1 
ATOM   3245 C  CA    . GLU A 1 439 ? 129.424 101.128 76.491  1.00 44.86  ? 427 GLU A CA    1 
ATOM   3246 C  C     . GLU A 1 439 ? 128.140 101.591 75.817  1.00 42.99  ? 427 GLU A C     1 
ATOM   3247 O  O     . GLU A 1 439 ? 127.099 100.935 75.931  1.00 45.99  ? 427 GLU A O     1 
ATOM   3248 C  CB    . GLU A 1 439 ? 129.623 101.854 77.820  1.00 45.55  ? 427 GLU A CB    1 
ATOM   3249 C  CG    . GLU A 1 439 ? 130.370 101.044 78.861  1.00 55.70  ? 427 GLU A CG    1 
ATOM   3250 C  CD    . GLU A 1 439 ? 130.953 101.904 79.962  1.00 64.66  ? 427 GLU A CD    1 
ATOM   3251 O  OE1   . GLU A 1 439 ? 130.191 102.671 80.585  1.00 61.37  ? 427 GLU A OE1   1 
ATOM   3252 O  OE2   . GLU A 1 439 ? 132.174 101.813 80.206  1.00 70.92  ? 427 GLU A OE2   1 
ATOM   3253 N  N     . ASN A 1 440 ? 128.191 102.729 75.122  1.00 45.26  ? 428 ASN A N     1 
ATOM   3254 C  CA    . ASN A 1 440 ? 127.015 103.219 74.411  1.00 40.44  ? 428 ASN A CA    1 
ATOM   3255 C  C     . ASN A 1 440 ? 126.621 102.284 73.276  1.00 42.28  ? 428 ASN A C     1 
ATOM   3256 O  O     . ASN A 1 440 ? 125.432 102.024 73.063  1.00 46.21  ? 428 ASN A O     1 
ATOM   3257 C  CB    . ASN A 1 440 ? 127.276 104.627 73.881  1.00 35.35  ? 428 ASN A CB    1 
ATOM   3258 C  CG    . ASN A 1 440 ? 126.794 105.699 74.827  1.00 38.96  ? 428 ASN A CG    1 
ATOM   3259 O  OD1   . ASN A 1 440 ? 125.651 106.136 74.751  1.00 44.25  ? 428 ASN A OD1   1 
ATOM   3260 N  ND2   . ASN A 1 440 ? 127.664 106.126 75.730  1.00 39.77  ? 428 ASN A ND2   1 
ATOM   3261 N  N     . LEU A 1 441 ? 127.604 101.773 72.534  1.00 39.68  ? 429 LEU A N     1 
ATOM   3262 C  CA    . LEU A 1 441 ? 127.322 100.826 71.464  1.00 39.00  ? 429 LEU A CA    1 
ATOM   3263 C  C     . LEU A 1 441 ? 126.827 99.490  71.994  1.00 46.67  ? 429 LEU A C     1 
ATOM   3264 O  O     . LEU A 1 441 ? 126.136 98.768  71.268  1.00 50.80  ? 429 LEU A O     1 
ATOM   3265 C  CB    . LEU A 1 441 ? 128.570 100.614 70.608  1.00 45.16  ? 429 LEU A CB    1 
ATOM   3266 C  CG    . LEU A 1 441 ? 128.600 101.287 69.238  1.00 46.07  ? 429 LEU A CG    1 
ATOM   3267 C  CD1   . LEU A 1 441 ? 128.416 102.788 69.364  1.00 43.22  ? 429 LEU A CD1   1 
ATOM   3268 C  CD2   . LEU A 1 441 ? 129.904 100.968 68.536  1.00 53.87  ? 429 LEU A CD2   1 
ATOM   3269 N  N     . ARG A 1 442 ? 127.166 99.143  73.237  1.00 47.96  ? 430 ARG A N     1 
ATOM   3270 C  CA    . ARG A 1 442 ? 126.672 97.904  73.824  1.00 46.57  ? 430 ARG A CA    1 
ATOM   3271 C  C     . ARG A 1 442 ? 125.169 97.933  74.057  1.00 47.98  ? 430 ARG A C     1 
ATOM   3272 O  O     . ARG A 1 442 ? 124.561 96.873  74.209  1.00 52.69  ? 430 ARG A O     1 
ATOM   3273 C  CB    . ARG A 1 442 ? 127.393 97.613  75.139  1.00 48.28  ? 430 ARG A CB    1 
ATOM   3274 C  CG    . ARG A 1 442 ? 128.636 96.763  74.975  1.00 50.73  ? 430 ARG A CG    1 
ATOM   3275 C  CD    . ARG A 1 442 ? 129.378 96.601  76.284  1.00 52.33  ? 430 ARG A CD    1 
ATOM   3276 N  NE    . ARG A 1 442 ? 130.775 96.251  76.066  1.00 54.23  ? 430 ARG A NE    1 
ATOM   3277 C  CZ    . ARG A 1 442 ? 131.800 96.918  76.576  1.00 59.42  ? 430 ARG A CZ    1 
ATOM   3278 N  NH1   . ARG A 1 442 ? 131.619 97.961  77.369  1.00 52.49  ? 430 ARG A NH1   1 
ATOM   3279 N  NH2   . ARG A 1 442 ? 133.037 96.527  76.287  1.00 64.98  ? 430 ARG A NH2   1 
ATOM   3280 N  N     . TYR A 1 443 ? 124.553 99.115  74.091  1.00 46.69  ? 431 TYR A N     1 
ATOM   3281 C  CA    . TYR A 1 443 ? 123.099 99.165  74.179  1.00 43.04  ? 431 TYR A CA    1 
ATOM   3282 C  C     . TYR A 1 443 ? 122.453 98.513  72.966  1.00 44.70  ? 431 TYR A C     1 
ATOM   3283 O  O     . TYR A 1 443 ? 121.332 98.001  73.059  1.00 47.22  ? 431 TYR A O     1 
ATOM   3284 C  CB    . TYR A 1 443 ? 122.627 100.609 74.330  1.00 38.79  ? 431 TYR A CB    1 
ATOM   3285 C  CG    . TYR A 1 443 ? 122.448 101.033 75.766  1.00 38.37  ? 431 TYR A CG    1 
ATOM   3286 C  CD1   . TYR A 1 443 ? 123.530 101.442 76.528  1.00 42.32  ? 431 TYR A CD1   1 
ATOM   3287 C  CD2   . TYR A 1 443 ? 121.196 101.018 76.362  1.00 36.86  ? 431 TYR A CD2   1 
ATOM   3288 C  CE1   . TYR A 1 443 ? 123.371 101.828 77.841  1.00 41.51  ? 431 TYR A CE1   1 
ATOM   3289 C  CE2   . TYR A 1 443 ? 121.029 101.402 77.675  1.00 39.69  ? 431 TYR A CE2   1 
ATOM   3290 C  CZ    . TYR A 1 443 ? 122.120 101.805 78.410  1.00 41.94  ? 431 TYR A CZ    1 
ATOM   3291 O  OH    . TYR A 1 443 ? 121.960 102.190 79.719  1.00 43.24  ? 431 TYR A OH    1 
ATOM   3292 N  N     . GLY A 1 444 ? 123.141 98.522  71.824  1.00 41.94  ? 432 GLY A N     1 
ATOM   3293 C  CA    . GLY A 1 444 ? 122.634 97.813  70.663  1.00 43.24  ? 432 GLY A CA    1 
ATOM   3294 C  C     . GLY A 1 444 ? 122.707 96.305  70.810  1.00 60.06  ? 432 GLY A C     1 
ATOM   3295 O  O     . GLY A 1 444 ? 121.754 95.596  70.475  1.00 67.77  ? 432 GLY A O     1 
ATOM   3296 N  N     . ARG A 1 445 ? 123.831 95.791  71.309  1.00 57.64  ? 433 ARG A N     1 
ATOM   3297 C  CA    . ARG A 1 445 ? 124.052 94.349  71.345  1.00 59.56  ? 433 ARG A CA    1 
ATOM   3298 C  C     . ARG A 1 445 ? 124.307 93.792  72.738  1.00 65.25  ? 433 ARG A C     1 
ATOM   3299 O  O     . ARG A 1 445 ? 123.769 92.732  73.070  1.00 70.91  ? 433 ARG A O     1 
ATOM   3300 C  CB    . ARG A 1 445 ? 125.221 93.982  70.419  1.00 61.43  ? 433 ARG A CB    1 
ATOM   3301 C  CG    . ARG A 1 445 ? 125.525 92.499  70.359  1.00 68.79  ? 433 ARG A CG    1 
ATOM   3302 C  CD    . ARG A 1 445 ? 126.192 92.137  69.046  1.00 71.29  ? 433 ARG A CD    1 
ATOM   3303 N  NE    . ARG A 1 445 ? 125.233 92.076  67.950  1.00 73.29  ? 433 ARG A NE    1 
ATOM   3304 C  CZ    . ARG A 1 445 ? 124.455 91.034  67.693  1.00 79.97  ? 433 ARG A CZ    1 
ATOM   3305 N  NH1   . ARG A 1 445 ? 124.507 89.935  68.427  1.00 84.76  ? 433 ARG A NH1   1 
ATOM   3306 N  NH2   . ARG A 1 445 ? 123.605 91.095  66.672  1.00 73.48  ? 433 ARG A NH2   1 
ATOM   3307 N  N     . ALA A 1 446 ? 125.130 94.465  73.550  1.00 61.54  ? 434 ALA A N     1 
ATOM   3308 C  CA    . ALA A 1 446 ? 125.451 94.090  74.931  1.00 60.91  ? 434 ALA A CA    1 
ATOM   3309 C  C     . ALA A 1 446 ? 126.372 92.879  75.021  1.00 64.73  ? 434 ALA A C     1 
ATOM   3310 O  O     . ALA A 1 446 ? 126.828 92.526  76.113  1.00 72.06  ? 434 ALA A O     1 
ATOM   3311 C  CB    . ALA A 1 446 ? 124.179 93.843  75.749  1.00 55.18  ? 434 ALA A CB    1 
ATOM   3312 N  N     . ASP A 1 447 ? 126.665 92.243  73.888  1.00 66.18  ? 435 ASP A N     1 
ATOM   3313 C  CA    . ASP A 1 447 ? 127.660 91.178  73.838  1.00 68.72  ? 435 ASP A CA    1 
ATOM   3314 C  C     . ASP A 1 447 ? 128.555 91.318  72.615  1.00 72.25  ? 435 ASP A C     1 
ATOM   3315 O  O     . ASP A 1 447 ? 129.137 90.329  72.160  1.00 76.11  ? 435 ASP A O     1 
ATOM   3316 C  CB    . ASP A 1 447 ? 127.000 89.796  73.855  1.00 73.51  ? 435 ASP A CB    1 
ATOM   3317 C  CG    . ASP A 1 447 ? 125.799 89.708  72.936  1.00 76.97  ? 435 ASP A CG    1 
ATOM   3318 O  OD1   . ASP A 1 447 ? 124.707 90.155  73.338  1.00 73.28  ? 435 ASP A OD1   1 
ATOM   3319 O  OD2   . ASP A 1 447 ? 125.948 89.188  71.811  1.00 77.76  ? 435 ASP A OD2   1 
ATOM   3320 N  N     . ALA A 1 448 ? 128.672 92.527  72.077  1.00 71.36  ? 436 ALA A N     1 
ATOM   3321 C  CA    . ALA A 1 448 ? 129.429 92.738  70.855  1.00 71.65  ? 436 ALA A CA    1 
ATOM   3322 C  C     . ALA A 1 448 ? 130.926 92.730  71.131  1.00 69.28  ? 436 ALA A C     1 
ATOM   3323 O  O     . ALA A 1 448 ? 131.392 93.251  72.147  1.00 66.47  ? 436 ALA A O     1 
ATOM   3324 C  CB    . ALA A 1 448 ? 129.028 94.060  70.207  1.00 72.56  ? 436 ALA A CB    1 
ATOM   3325 N  N     . THR A 1 449 ? 131.677 92.133  70.213  1.00 71.70  ? 437 THR A N     1 
ATOM   3326 C  CA    . THR A 1 449 ? 133.127 92.166  70.267  1.00 73.41  ? 437 THR A CA    1 
ATOM   3327 C  C     . THR A 1 449 ? 133.637 93.496  69.718  1.00 70.79  ? 437 THR A C     1 
ATOM   3328 O  O     . THR A 1 449 ? 132.901 94.267  69.098  1.00 72.07  ? 437 THR A O     1 
ATOM   3329 C  CB    . THR A 1 449 ? 133.716 90.999  69.477  1.00 76.94  ? 437 THR A CB    1 
ATOM   3330 O  OG1   . THR A 1 449 ? 132.778 89.916  69.455  1.00 76.11  ? 437 THR A OG1   1 
ATOM   3331 C  CG2   . THR A 1 449 ? 135.012 90.517  70.118  1.00 75.35  ? 437 THR A CG2   1 
ATOM   3332 N  N     . ASP A 1 450 ? 134.921 93.766  69.955  1.00 71.76  ? 438 ASP A N     1 
ATOM   3333 C  CA    . ASP A 1 450 ? 135.516 94.998  69.449  1.00 70.97  ? 438 ASP A CA    1 
ATOM   3334 C  C     . ASP A 1 450 ? 135.534 95.028  67.927  1.00 74.27  ? 438 ASP A C     1 
ATOM   3335 O  O     . ASP A 1 450 ? 135.425 96.104  67.328  1.00 75.35  ? 438 ASP A O     1 
ATOM   3336 C  CB    . ASP A 1 450 ? 136.931 95.165  70.000  1.00 73.94  ? 438 ASP A CB    1 
ATOM   3337 C  CG    . ASP A 1 450 ? 136.949 95.414  71.494  1.00 79.68  ? 438 ASP A CG    1 
ATOM   3338 O  OD1   . ASP A 1 450 ? 135.862 95.605  72.079  1.00 77.70  ? 438 ASP A OD1   1 
ATOM   3339 O  OD2   . ASP A 1 450 ? 138.049 95.421  72.083  1.00 82.62  ? 438 ASP A OD2   1 
ATOM   3340 N  N     . ASP A 1 451 ? 135.673 93.867  67.284  1.00 73.58  ? 439 ASP A N     1 
ATOM   3341 C  CA    . ASP A 1 451 ? 135.711 93.830  65.826  1.00 71.16  ? 439 ASP A CA    1 
ATOM   3342 C  C     . ASP A 1 451 ? 134.369 94.233  65.226  1.00 73.17  ? 439 ASP A C     1 
ATOM   3343 O  O     . ASP A 1 451 ? 134.314 95.041  64.292  1.00 77.57  ? 439 ASP A O     1 
ATOM   3344 C  CB    . ASP A 1 451 ? 136.127 92.440  65.348  1.00 79.22  ? 439 ASP A CB    1 
ATOM   3345 C  CG    . ASP A 1 451 ? 137.606 92.181  65.539  1.00 88.20  ? 439 ASP A CG    1 
ATOM   3346 O  OD1   . ASP A 1 451 ? 138.306 93.091  66.034  1.00 85.90  ? 439 ASP A OD1   1 
ATOM   3347 O  OD2   . ASP A 1 451 ? 138.072 91.075  65.192  1.00 91.94  ? 439 ASP A OD2   1 
ATOM   3348 N  N     . GLU A 1 452 ? 133.269 93.691  65.754  1.00 72.86  ? 440 GLU A N     1 
ATOM   3349 C  CA    . GLU A 1 452 ? 131.964 94.089  65.240  1.00 73.00  ? 440 GLU A CA    1 
ATOM   3350 C  C     . GLU A 1 452 ? 131.597 95.502  65.679  1.00 67.80  ? 440 GLU A C     1 
ATOM   3351 O  O     . GLU A 1 452 ? 130.852 96.191  64.976  1.00 67.76  ? 440 GLU A O     1 
ATOM   3352 C  CB    . GLU A 1 452 ? 130.891 93.085  65.662  1.00 69.79  ? 440 GLU A CB    1 
ATOM   3353 C  CG    . GLU A 1 452 ? 130.681 92.957  67.150  1.00 76.52  ? 440 GLU A CG    1 
ATOM   3354 C  CD    . GLU A 1 452 ? 129.989 91.662  67.523  1.00 83.11  ? 440 GLU A CD    1 
ATOM   3355 O  OE1   . GLU A 1 452 ? 128.893 91.397  66.988  1.00 84.20  ? 440 GLU A OE1   1 
ATOM   3356 O  OE2   . GLU A 1 452 ? 130.543 90.905  68.347  1.00 83.44  ? 440 GLU A OE2   1 
ATOM   3357 N  N     . MET A 1 453 ? 132.128 95.961  66.814  1.00 65.04  ? 441 MET A N     1 
ATOM   3358 C  CA    . MET A 1 453 ? 131.973 97.364  67.184  1.00 57.51  ? 441 MET A CA    1 
ATOM   3359 C  C     . MET A 1 453 ? 132.619 98.271  66.147  1.00 57.42  ? 441 MET A C     1 
ATOM   3360 O  O     . MET A 1 453 ? 132.026 99.265  65.713  1.00 62.53  ? 441 MET A O     1 
ATOM   3361 C  CB    . MET A 1 453 ? 132.582 97.615  68.562  1.00 56.56  ? 441 MET A CB    1 
ATOM   3362 C  CG    . MET A 1 453 ? 131.644 97.351  69.713  1.00 60.86  ? 441 MET A CG    1 
ATOM   3363 S  SD    . MET A 1 453 ? 132.353 97.833  71.291  1.00 79.65  ? 441 MET A SD    1 
ATOM   3364 C  CE    . MET A 1 453 ? 131.035 97.345  72.390  1.00 61.00  ? 441 MET A CE    1 
ATOM   3365 N  N     . TRP A 1 454 ? 133.842 97.937  65.734  1.00 58.89  ? 442 TRP A N     1 
ATOM   3366 C  CA    . TRP A 1 454 ? 134.517 98.723  64.709  1.00 57.53  ? 442 TRP A CA    1 
ATOM   3367 C  C     . TRP A 1 454 ? 133.814 98.610  63.365  1.00 59.84  ? 442 TRP A C     1 
ATOM   3368 O  O     . TRP A 1 454 ? 133.784 99.579  62.603  1.00 62.85  ? 442 TRP A O     1 
ATOM   3369 C  CB    . TRP A 1 454 ? 135.977 98.289  64.591  1.00 60.49  ? 442 TRP A CB    1 
ATOM   3370 C  CG    . TRP A 1 454 ? 136.853 98.863  65.660  1.00 63.79  ? 442 TRP A CG    1 
ATOM   3371 C  CD1   . TRP A 1 454 ? 137.530 98.173  66.619  1.00 63.68  ? 442 TRP A CD1   1 
ATOM   3372 C  CD2   . TRP A 1 454 ? 137.150 100.248 65.877  1.00 65.62  ? 442 TRP A CD2   1 
ATOM   3373 N  NE1   . TRP A 1 454 ? 138.229 99.040  67.421  1.00 67.51  ? 442 TRP A NE1   1 
ATOM   3374 C  CE2   . TRP A 1 454 ? 138.012 100.320 66.987  1.00 63.82  ? 442 TRP A CE2   1 
ATOM   3375 C  CE3   . TRP A 1 454 ? 136.770 101.433 65.240  1.00 61.72  ? 442 TRP A CE3   1 
ATOM   3376 C  CZ2   . TRP A 1 454 ? 138.500 101.528 67.474  1.00 58.92  ? 442 TRP A CZ2   1 
ATOM   3377 C  CZ3   . TRP A 1 454 ? 137.257 102.630 65.726  1.00 59.56  ? 442 TRP A CZ3   1 
ATOM   3378 C  CH2   . TRP A 1 454 ? 138.112 102.669 66.831  1.00 58.44  ? 442 TRP A CH2   1 
ATOM   3379 N  N     . GLU A 1 455 ? 133.243 97.444  63.059  1.00 58.71  ? 443 GLU A N     1 
ATOM   3380 C  CA    . GLU A 1 455 ? 132.469 97.307  61.829  1.00 62.28  ? 443 GLU A CA    1 
ATOM   3381 C  C     . GLU A 1 455 ? 131.240 98.210  61.846  1.00 62.22  ? 443 GLU A C     1 
ATOM   3382 O  O     . GLU A 1 455 ? 130.935 98.877  60.849  1.00 63.66  ? 443 GLU A O     1 
ATOM   3383 C  CB    . GLU A 1 455 ? 132.063 95.847  61.626  1.00 63.10  ? 443 GLU A CB    1 
ATOM   3384 C  CG    . GLU A 1 455 ? 130.983 95.622  60.573  1.00 70.97  ? 443 GLU A CG    1 
ATOM   3385 C  CD    . GLU A 1 455 ? 131.461 95.853  59.147  1.00 77.96  ? 443 GLU A CD    1 
ATOM   3386 O  OE1   . GLU A 1 455 ? 132.610 96.301  58.949  1.00 77.10  ? 443 GLU A OE1   1 
ATOM   3387 O  OE2   . GLU A 1 455 ? 130.674 95.585  58.215  1.00 79.99  ? 443 GLU A OE2   1 
ATOM   3388 N  N     . ALA A 1 456 ? 130.526 98.248  62.975  1.00 59.37  ? 444 ALA A N     1 
ATOM   3389 C  CA    . ALA A 1 456 ? 129.366 99.126  63.097  1.00 53.16  ? 444 ALA A CA    1 
ATOM   3390 C  C     . ALA A 1 456 ? 129.770 100.590 62.994  1.00 51.64  ? 444 ALA A C     1 
ATOM   3391 O  O     . ALA A 1 456 ? 129.066 101.393 62.373  1.00 51.45  ? 444 ALA A O     1 
ATOM   3392 C  CB    . ALA A 1 456 ? 128.645 98.862  64.417  1.00 47.01  ? 444 ALA A CB    1 
ATOM   3393 N  N     . LEU A 1 457 ? 130.895 100.957 63.609  1.00 54.54  ? 445 LEU A N     1 
ATOM   3394 C  CA    . LEU A 1 457 ? 131.389 102.325 63.492  1.00 50.21  ? 445 LEU A CA    1 
ATOM   3395 C  C     . LEU A 1 457 ? 131.748 102.662 62.051  1.00 49.91  ? 445 LEU A C     1 
ATOM   3396 O  O     . LEU A 1 457 ? 131.503 103.781 61.588  1.00 54.49  ? 445 LEU A O     1 
ATOM   3397 C  CB    . LEU A 1 457 ? 132.595 102.524 64.406  1.00 49.79  ? 445 LEU A CB    1 
ATOM   3398 C  CG    . LEU A 1 457 ? 132.308 102.507 65.906  1.00 49.32  ? 445 LEU A CG    1 
ATOM   3399 C  CD1   . LEU A 1 457 ? 133.604 102.497 66.686  1.00 52.50  ? 445 LEU A CD1   1 
ATOM   3400 C  CD2   . LEU A 1 457 ? 131.456 103.697 66.299  1.00 51.45  ? 445 LEU A CD2   1 
ATOM   3401 N  N     . ARG A 1 458 ? 132.343 101.710 61.331  1.00 51.74  ? 446 ARG A N     1 
ATOM   3402 C  CA    . ARG A 1 458 ? 132.693 101.941 59.934  1.00 55.12  ? 446 ARG A CA    1 
ATOM   3403 C  C     . ARG A 1 458 ? 131.451 102.118 59.071  1.00 57.27  ? 446 ARG A C     1 
ATOM   3404 O  O     . ARG A 1 458 ? 131.433 102.964 58.170  1.00 61.86  ? 446 ARG A O     1 
ATOM   3405 C  CB    . ARG A 1 458 ? 133.547 100.789 59.410  1.00 62.07  ? 446 ARG A CB    1 
ATOM   3406 C  CG    . ARG A 1 458 ? 134.047 100.994 57.995  1.00 66.90  ? 446 ARG A CG    1 
ATOM   3407 C  CD    . ARG A 1 458 ? 134.402 99.673  57.339  1.00 71.08  ? 446 ARG A CD    1 
ATOM   3408 N  NE    . ARG A 1 458 ? 133.265 98.762  57.300  1.00 75.51  ? 446 ARG A NE    1 
ATOM   3409 C  CZ    . ARG A 1 458 ? 132.232 98.882  56.476  1.00 72.79  ? 446 ARG A CZ    1 
ATOM   3410 N  NH1   . ARG A 1 458 ? 132.156 99.871  55.602  1.00 66.72  ? 446 ARG A NH1   1 
ATOM   3411 N  NH2   . ARG A 1 458 ? 131.252 97.985  56.530  1.00 71.38  ? 446 ARG A NH2   1 
ATOM   3412 N  N     . VAL A 1 459 ? 130.410 101.320 59.319  1.00 55.15  ? 447 VAL A N     1 
ATOM   3413 C  CA    . VAL A 1 459 ? 129.177 101.452 58.545  1.00 54.05  ? 447 VAL A CA    1 
ATOM   3414 C  C     . VAL A 1 459 ? 128.570 102.835 58.741  1.00 54.58  ? 447 VAL A C     1 
ATOM   3415 O  O     . VAL A 1 459 ? 128.150 103.489 57.779  1.00 57.32  ? 447 VAL A O     1 
ATOM   3416 C  CB    . VAL A 1 459 ? 128.182 100.340 58.924  1.00 55.09  ? 447 VAL A CB    1 
ATOM   3417 C  CG1   . VAL A 1 459 ? 126.820 100.617 58.310  1.00 55.23  ? 447 VAL A CG1   1 
ATOM   3418 C  CG2   . VAL A 1 459 ? 128.704 98.991  58.476  1.00 62.05  ? 447 VAL A CG2   1 
ATOM   3419 N  N     . ALA A 1 460 ? 128.526 103.306 59.982  1.00 53.32  ? 448 ALA A N     1 
ATOM   3420 C  CA    . ALA A 1 460 ? 127.991 104.623 60.291  1.00 45.88  ? 448 ALA A CA    1 
ATOM   3421 C  C     . ALA A 1 460 ? 128.970 105.746 59.989  1.00 50.21  ? 448 ALA A C     1 
ATOM   3422 O  O     . ALA A 1 460 ? 128.689 106.893 60.348  1.00 50.65  ? 448 ALA A O     1 
ATOM   3423 C  CB    . ALA A 1 460 ? 127.573 104.687 61.760  1.00 36.92  ? 448 ALA A CB    1 
ATOM   3424 N  N     . ALA A 1 461 ? 130.103 105.442 59.351  1.00 51.27  ? 449 ALA A N     1 
ATOM   3425 C  CA    . ALA A 1 461 ? 131.161 106.418 59.086  1.00 49.77  ? 449 ALA A CA    1 
ATOM   3426 C  C     . ALA A 1 461 ? 131.656 107.067 60.373  1.00 50.32  ? 449 ALA A C     1 
ATOM   3427 O  O     . ALA A 1 461 ? 132.102 108.216 60.373  1.00 53.36  ? 449 ALA A O     1 
ATOM   3428 C  CB    . ALA A 1 461 ? 130.708 107.484 58.085  1.00 48.15  ? 449 ALA A CB    1 
ATOM   3429 N  N     . ALA A 1 462 ? 131.574 106.332 61.479  1.00 50.43  ? 450 ALA A N     1 
ATOM   3430 C  CA    . ALA A 1 462 ? 131.988 106.818 62.785  1.00 48.54  ? 450 ALA A CA    1 
ATOM   3431 C  C     . ALA A 1 462 ? 133.323 106.246 63.234  1.00 58.22  ? 450 ALA A C     1 
ATOM   3432 O  O     . ALA A 1 462 ? 133.738 106.496 64.367  1.00 60.11  ? 450 ALA A O     1 
ATOM   3433 C  CB    . ALA A 1 462 ? 130.913 106.496 63.828  1.00 45.09  ? 450 ALA A CB    1 
ATOM   3434 N  N     . ALA A 1 463 ? 134.003 105.482 62.377  1.00 59.46  ? 451 ALA A N     1 
ATOM   3435 C  CA    . ALA A 1 463 ? 135.249 104.846 62.786  1.00 55.71  ? 451 ALA A CA    1 
ATOM   3436 C  C     . ALA A 1 463 ? 136.391 105.845 62.888  1.00 61.33  ? 451 ALA A C     1 
ATOM   3437 O  O     . ALA A 1 463 ? 137.292 105.665 63.713  1.00 64.67  ? 451 ALA A O     1 
ATOM   3438 C  CB    . ALA A 1 463 ? 135.616 103.729 61.811  1.00 57.43  ? 451 ALA A CB    1 
ATOM   3439 N  N     . ASP A 1 464 ? 136.374 106.897 62.066  1.00 61.62  ? 452 ASP A N     1 
ATOM   3440 C  CA    . ASP A 1 464 ? 137.512 107.810 62.011  1.00 60.00  ? 452 ASP A CA    1 
ATOM   3441 C  C     . ASP A 1 464 ? 137.678 108.588 63.314  1.00 62.00  ? 452 ASP A C     1 
ATOM   3442 O  O     . ASP A 1 464 ? 138.778 108.645 63.875  1.00 63.61  ? 452 ASP A O     1 
ATOM   3443 C  CB    . ASP A 1 464 ? 137.376 108.746 60.804  1.00 63.83  ? 452 ASP A CB    1 
ATOM   3444 C  CG    . ASP A 1 464 ? 136.096 109.578 60.824  1.00 72.09  ? 452 ASP A CG    1 
ATOM   3445 O  OD1   . ASP A 1 464 ? 135.661 110.024 61.905  1.00 69.18  ? 452 ASP A OD1   1 
ATOM   3446 O  OD2   . ASP A 1 464 ? 135.522 109.790 59.736  1.00 74.05  ? 452 ASP A OD2   1 
ATOM   3447 N  N     . PHE A 1 465 ? 136.598 109.183 63.824  1.00 56.43  ? 453 PHE A N     1 
ATOM   3448 C  CA    . PHE A 1 465 ? 136.725 109.996 65.026  1.00 54.03  ? 453 PHE A CA    1 
ATOM   3449 C  C     . PHE A 1 465 ? 136.787 109.167 66.301  1.00 58.84  ? 453 PHE A C     1 
ATOM   3450 O  O     . PHE A 1 465 ? 137.137 109.711 67.353  1.00 61.67  ? 453 PHE A O     1 
ATOM   3451 C  CB    . PHE A 1 465 ? 135.587 111.025 65.107  1.00 51.92  ? 453 PHE A CB    1 
ATOM   3452 C  CG    . PHE A 1 465 ? 134.255 110.455 65.517  1.00 51.57  ? 453 PHE A CG    1 
ATOM   3453 C  CD1   . PHE A 1 465 ? 133.908 110.346 66.855  1.00 48.33  ? 453 PHE A CD1   1 
ATOM   3454 C  CD2   . PHE A 1 465 ? 133.330 110.075 64.562  1.00 48.12  ? 453 PHE A CD2   1 
ATOM   3455 C  CE1   . PHE A 1 465 ? 132.684 109.836 67.227  1.00 44.34  ? 453 PHE A CE1   1 
ATOM   3456 C  CE2   . PHE A 1 465 ? 132.102 109.572 64.932  1.00 45.45  ? 453 PHE A CE2   1 
ATOM   3457 C  CZ    . PHE A 1 465 ? 131.780 109.450 66.264  1.00 41.70  ? 453 PHE A CZ    1 
ATOM   3458 N  N     . VAL A 1 466 ? 136.461 107.877 66.238  1.00 58.84  ? 454 VAL A N     1 
ATOM   3459 C  CA    . VAL A 1 466 ? 136.676 107.011 67.392  1.00 59.30  ? 454 VAL A CA    1 
ATOM   3460 C  C     . VAL A 1 466 ? 138.106 106.487 67.404  1.00 64.32  ? 454 VAL A C     1 
ATOM   3461 O  O     . VAL A 1 466 ? 138.749 106.428 68.457  1.00 68.52  ? 454 VAL A O     1 
ATOM   3462 C  CB    . VAL A 1 466 ? 135.645 105.869 67.404  1.00 54.32  ? 454 VAL A CB    1 
ATOM   3463 C  CG1   . VAL A 1 466 ? 135.914 104.922 68.556  1.00 56.48  ? 454 VAL A CG1   1 
ATOM   3464 C  CG2   . VAL A 1 466 ? 134.241 106.433 67.506  1.00 53.08  ? 454 VAL A CG2   1 
ATOM   3465 N  N     . ARG A 1 467 ? 138.628 106.111 66.235  1.00 64.34  ? 455 ARG A N     1 
ATOM   3466 C  CA    . ARG A 1 467 ? 140.025 105.707 66.137  1.00 64.18  ? 455 ARG A CA    1 
ATOM   3467 C  C     . ARG A 1 467 ? 140.964 106.862 66.448  1.00 68.14  ? 455 ARG A C     1 
ATOM   3468 O  O     . ARG A 1 467 ? 142.048 106.647 67.001  1.00 72.74  ? 455 ARG A O     1 
ATOM   3469 C  CB    . ARG A 1 467 ? 140.311 105.156 64.741  1.00 63.42  ? 455 ARG A CB    1 
ATOM   3470 C  CG    . ARG A 1 467 ? 141.581 104.336 64.638  1.00 64.85  ? 455 ARG A CG    1 
ATOM   3471 C  CD    . ARG A 1 467 ? 141.325 102.885 65.000  1.00 68.22  ? 455 ARG A CD    1 
ATOM   3472 N  NE    . ARG A 1 467 ? 140.471 102.224 64.020  1.00 67.35  ? 455 ARG A NE    1 
ATOM   3473 C  CZ    . ARG A 1 467 ? 140.149 100.939 64.053  1.00 66.47  ? 455 ARG A CZ    1 
ATOM   3474 N  NH1   . ARG A 1 467 ? 140.602 100.137 65.002  1.00 65.54  ? 455 ARG A NH1   1 
ATOM   3475 N  NH2   . ARG A 1 467 ? 139.353 100.446 63.109  1.00 59.91  ? 455 ARG A NH2   1 
ATOM   3476 N  N     . ALA A 1 468 ? 140.571 108.091 66.100  1.00 65.42  ? 456 ALA A N     1 
ATOM   3477 C  CA    . ALA A 1 468 ? 141.423 109.246 66.352  1.00 67.44  ? 456 ALA A CA    1 
ATOM   3478 C  C     . ALA A 1 468 ? 141.645 109.499 67.837  1.00 69.74  ? 456 ALA A C     1 
ATOM   3479 O  O     . ALA A 1 468 ? 142.681 110.061 68.206  1.00 72.28  ? 456 ALA A O     1 
ATOM   3480 C  CB    . ALA A 1 468 ? 140.826 110.493 65.700  1.00 63.93  ? 456 ALA A CB    1 
ATOM   3481 N  N     . HIS A 1 469 ? 140.706 109.108 68.690  1.00 66.12  ? 457 HIS A N     1 
ATOM   3482 C  CA    . HIS A 1 469 ? 140.882 109.308 70.119  1.00 67.45  ? 457 HIS A CA    1 
ATOM   3483 C  C     . HIS A 1 469 ? 141.953 108.360 70.653  1.00 71.14  ? 457 HIS A C     1 
ATOM   3484 O  O     . HIS A 1 469 ? 142.066 107.223 70.186  1.00 72.97  ? 457 HIS A O     1 
ATOM   3485 C  CB    . HIS A 1 469 ? 139.565 109.085 70.859  1.00 65.98  ? 457 HIS A CB    1 
ATOM   3486 C  CG    . HIS A 1 469 ? 139.533 109.688 72.229  1.00 69.92  ? 457 HIS A CG    1 
ATOM   3487 N  ND1   . HIS A 1 469 ? 139.934 109.000 73.353  1.00 69.45  ? 457 HIS A ND1   1 
ATOM   3488 C  CD2   . HIS A 1 469 ? 139.160 110.918 72.653  1.00 66.52  ? 457 HIS A CD2   1 
ATOM   3489 C  CE1   . HIS A 1 469 ? 139.802 109.778 74.413  1.00 66.25  ? 457 HIS A CE1   1 
ATOM   3490 N  NE2   . HIS A 1 469 ? 139.334 110.948 74.015  1.00 63.76  ? 457 HIS A NE2   1 
ATOM   3491 N  N     . PRO A 1 470 ? 142.762 108.802 71.619  1.00 71.12  ? 458 PRO A N     1 
ATOM   3492 C  CA    . PRO A 1 470 ? 143.790 107.908 72.178  1.00 68.62  ? 458 PRO A CA    1 
ATOM   3493 C  C     . PRO A 1 470 ? 143.230 106.646 72.807  1.00 73.11  ? 458 PRO A C     1 
ATOM   3494 O  O     . PRO A 1 470 ? 143.903 105.608 72.793  1.00 73.45  ? 458 PRO A O     1 
ATOM   3495 C  CB    . PRO A 1 470 ? 144.489 108.793 73.218  1.00 69.82  ? 458 PRO A CB    1 
ATOM   3496 C  CG    . PRO A 1 470 ? 144.251 110.185 72.747  1.00 68.58  ? 458 PRO A CG    1 
ATOM   3497 C  CD    . PRO A 1 470 ? 142.885 110.176 72.133  1.00 71.23  ? 458 PRO A CD    1 
ATOM   3498 N  N     . GLN A 1 471 ? 142.023 106.699 73.365  1.00 71.80  ? 459 GLN A N     1 
ATOM   3499 C  CA    . GLN A 1 471 ? 141.437 105.554 74.048  1.00 70.63  ? 459 GLN A CA    1 
ATOM   3500 C  C     . GLN A 1 471 ? 140.590 104.678 73.134  1.00 72.16  ? 459 GLN A C     1 
ATOM   3501 O  O     . GLN A 1 471 ? 140.049 103.670 73.599  1.00 72.29  ? 459 GLN A O     1 
ATOM   3502 C  CB    . GLN A 1 471 ? 140.598 106.029 75.237  1.00 69.13  ? 459 GLN A CB    1 
ATOM   3503 C  CG    . GLN A 1 471 ? 141.400 106.785 76.283  1.00 73.87  ? 459 GLN A CG    1 
ATOM   3504 C  CD    . GLN A 1 471 ? 140.546 107.278 77.430  1.00 78.06  ? 459 GLN A CD    1 
ATOM   3505 O  OE1   . GLN A 1 471 ? 140.231 108.464 77.519  1.00 75.18  ? 459 GLN A OE1   1 
ATOM   3506 N  NE2   . GLN A 1 471 ? 140.164 106.368 78.317  1.00 77.13  ? 459 GLN A NE2   1 
ATOM   3507 N  N     . GLY A 1 472 ? 140.466 105.032 71.858  1.00 73.14  ? 460 GLY A N     1 
ATOM   3508 C  CA    . GLY A 1 472 ? 139.743 104.184 70.922  1.00 66.83  ? 460 GLY A CA    1 
ATOM   3509 C  C     . GLY A 1 472 ? 138.286 104.029 71.308  1.00 65.74  ? 460 GLY A C     1 
ATOM   3510 O  O     . GLY A 1 472 ? 137.567 105.009 71.528  1.00 65.52  ? 460 GLY A O     1 
ATOM   3511 N  N     . LEU A 1 473 ? 137.840 102.773 71.393  1.00 61.64  ? 461 LEU A N     1 
ATOM   3512 C  CA    . LEU A 1 473 ? 136.456 102.486 71.748  1.00 58.54  ? 461 LEU A CA    1 
ATOM   3513 C  C     . LEU A 1 473 ? 136.117 102.930 73.162  1.00 58.21  ? 461 LEU A C     1 
ATOM   3514 O  O     . LEU A 1 473 ? 134.934 103.068 73.490  1.00 58.48  ? 461 LEU A O     1 
ATOM   3515 C  CB    . LEU A 1 473 ? 136.177 100.992 71.600  1.00 58.51  ? 461 LEU A CB    1 
ATOM   3516 C  CG    . LEU A 1 473 ? 136.142 100.431 70.181  1.00 58.37  ? 461 LEU A CG    1 
ATOM   3517 C  CD1   . LEU A 1 473 ? 136.452 98.947  70.198  1.00 61.08  ? 461 LEU A CD1   1 
ATOM   3518 C  CD2   . LEU A 1 473 ? 134.789 100.680 69.554  1.00 57.96  ? 461 LEU A CD2   1 
ATOM   3519 N  N     . ASP A 1 474 ? 137.122 103.152 74.008  1.00 59.74  ? 462 ASP A N     1 
ATOM   3520 C  CA    . ASP A 1 474 ? 136.904 103.588 75.380  1.00 65.11  ? 462 ASP A CA    1 
ATOM   3521 C  C     . ASP A 1 474 ? 136.993 105.101 75.537  1.00 66.00  ? 462 ASP A C     1 
ATOM   3522 O  O     . ASP A 1 474 ? 137.281 105.589 76.637  1.00 63.19  ? 462 ASP A O     1 
ATOM   3523 C  CB    . ASP A 1 474 ? 137.898 102.894 76.311  1.00 70.37  ? 462 ASP A CB    1 
ATOM   3524 C  CG    . ASP A 1 474 ? 137.456 101.495 76.693  1.00 74.39  ? 462 ASP A CG    1 
ATOM   3525 O  OD1   . ASP A 1 474 ? 136.234 101.266 76.808  1.00 73.47  ? 462 ASP A OD1   1 
ATOM   3526 O  OD2   . ASP A 1 474 ? 138.331 100.624 76.876  1.00 79.54  ? 462 ASP A OD2   1 
ATOM   3527 N  N     . MET A 1 475 ? 136.760 105.853 74.468  1.00 62.07  ? 463 MET A N     1 
ATOM   3528 C  CA    . MET A 1 475 ? 136.728 107.305 74.574  1.00 57.28  ? 463 MET A CA    1 
ATOM   3529 C  C     . MET A 1 475 ? 135.529 107.722 75.417  1.00 56.28  ? 463 MET A C     1 
ATOM   3530 O  O     . MET A 1 475 ? 134.428 107.194 75.222  1.00 60.59  ? 463 MET A O     1 
ATOM   3531 C  CB    . MET A 1 475 ? 136.654 107.948 73.191  1.00 54.54  ? 463 MET A CB    1 
ATOM   3532 C  CG    . MET A 1 475 ? 135.791 109.200 73.134  1.00 56.81  ? 463 MET A CG    1 
ATOM   3533 S  SD    . MET A 1 475 ? 135.776 109.990 71.516  1.00 72.98  ? 463 MET A SD    1 
ATOM   3534 C  CE    . MET A 1 475 ? 135.567 108.565 70.460  1.00 58.53  ? 463 MET A CE    1 
ATOM   3535 N  N     . PRO A 1 476 ? 135.695 108.644 76.359  1.00 52.55  ? 464 PRO A N     1 
ATOM   3536 C  CA    . PRO A 1 476 ? 134.579 109.013 77.235  1.00 48.93  ? 464 PRO A CA    1 
ATOM   3537 C  C     . PRO A 1 476 ? 133.453 109.692 76.473  1.00 51.27  ? 464 PRO A C     1 
ATOM   3538 O  O     . PRO A 1 476 ? 133.669 110.372 75.467  1.00 56.33  ? 464 PRO A O     1 
ATOM   3539 C  CB    . PRO A 1 476 ? 135.223 109.971 78.242  1.00 49.26  ? 464 PRO A CB    1 
ATOM   3540 C  CG    . PRO A 1 476 ? 136.408 110.522 77.525  1.00 58.42  ? 464 PRO A CG    1 
ATOM   3541 C  CD    . PRO A 1 476 ? 136.914 109.414 76.656  1.00 58.82  ? 464 PRO A CD    1 
ATOM   3542 N  N     . VAL A 1 477 ? 132.234 109.494 76.968  1.00 45.48  ? 465 VAL A N     1 
ATOM   3543 C  CA    . VAL A 1 477 ? 131.033 110.104 76.409  1.00 43.57  ? 465 VAL A CA    1 
ATOM   3544 C  C     . VAL A 1 477 ? 130.311 110.840 77.528  1.00 42.82  ? 465 VAL A C     1 
ATOM   3545 O  O     . VAL A 1 477 ? 130.139 110.296 78.623  1.00 44.96  ? 465 VAL A O     1 
ATOM   3546 C  CB    . VAL A 1 477 ? 130.106 109.058 75.759  1.00 42.86  ? 465 VAL A CB    1 
ATOM   3547 C  CG1   . VAL A 1 477 ? 128.820 109.707 75.281  1.00 38.91  ? 465 VAL A CG1   1 
ATOM   3548 C  CG2   . VAL A 1 477 ? 130.810 108.377 74.605  1.00 39.99  ? 465 VAL A CG2   1 
ATOM   3549 N  N     . ALA A 1 478 ? 129.894 112.073 77.256  1.00 39.58  ? 466 ALA A N     1 
ATOM   3550 C  CA    . ALA A 1 478 ? 129.217 112.881 78.256  1.00 37.88  ? 466 ALA A CA    1 
ATOM   3551 C  C     . ALA A 1 478 ? 127.778 112.403 78.445  1.00 40.19  ? 466 ALA A C     1 
ATOM   3552 O  O     . ALA A 1 478 ? 127.320 111.449 77.811  1.00 45.46  ? 466 ALA A O     1 
ATOM   3553 C  CB    . ALA A 1 478 ? 129.267 114.350 77.863  1.00 36.07  ? 466 ALA A CB    1 
ATOM   3554 N  N     . GLN A 1 479 ? 127.050 113.094 79.328  1.00 40.61  ? 467 GLN A N     1 
ATOM   3555 C  CA    . GLN A 1 479 ? 125.739 112.609 79.753  1.00 43.07  ? 467 GLN A CA    1 
ATOM   3556 C  C     . GLN A 1 479 ? 124.764 112.517 78.589  1.00 44.81  ? 467 GLN A C     1 
ATOM   3557 O  O     . GLN A 1 479 ? 123.992 111.557 78.494  1.00 49.79  ? 467 GLN A O     1 
ATOM   3558 C  CB    . GLN A 1 479 ? 125.164 113.508 80.843  1.00 41.29  ? 467 GLN A CB    1 
ATOM   3559 C  CG    . GLN A 1 479 ? 123.736 113.149 81.198  1.00 45.05  ? 467 GLN A CG    1 
ATOM   3560 C  CD    . GLN A 1 479 ? 123.191 113.966 82.337  1.00 52.76  ? 467 GLN A CD    1 
ATOM   3561 O  OE1   . GLN A 1 479 ? 123.544 115.131 82.504  1.00 60.88  ? 467 GLN A OE1   1 
ATOM   3562 N  NE2   . GLN A 1 479 ? 122.321 113.360 83.132  1.00 49.10  ? 467 GLN A NE2   1 
ATOM   3563 N  N     . GLY A 1 480 ? 124.760 113.514 77.709  1.00 36.56  ? 468 GLY A N     1 
ATOM   3564 C  CA    . GLY A 1 480 ? 123.964 113.458 76.502  1.00 33.14  ? 468 GLY A CA    1 
ATOM   3565 C  C     . GLY A 1 480 ? 124.766 113.377 75.226  1.00 39.02  ? 468 GLY A C     1 
ATOM   3566 O  O     . GLY A 1 480 ? 124.188 113.521 74.140  1.00 39.05  ? 468 GLY A O     1 
ATOM   3567 N  N     . GLY A 1 481 ? 126.072 113.141 75.304  1.00 40.74  ? 469 GLY A N     1 
ATOM   3568 C  CA    . GLY A 1 481 ? 126.901 113.177 74.121  1.00 36.00  ? 469 GLY A CA    1 
ATOM   3569 C  C     . GLY A 1 481 ? 127.251 114.566 73.649  1.00 38.11  ? 469 GLY A C     1 
ATOM   3570 O  O     . GLY A 1 481 ? 127.671 114.730 72.502  1.00 38.73  ? 469 GLY A O     1 
ATOM   3571 N  N     . ILE A 1 482 ? 127.088 115.581 74.505  1.00 39.20  ? 470 ILE A N     1 
ATOM   3572 C  CA    . ILE A 1 482 ? 127.363 116.962 74.110  1.00 41.53  ? 470 ILE A CA    1 
ATOM   3573 C  C     . ILE A 1 482 ? 128.844 117.255 73.951  1.00 41.87  ? 470 ILE A C     1 
ATOM   3574 O  O     . ILE A 1 482 ? 129.201 118.348 73.493  1.00 43.63  ? 470 ILE A O     1 
ATOM   3575 C  CB    . ILE A 1 482 ? 126.716 117.949 75.103  1.00 44.16  ? 470 ILE A CB    1 
ATOM   3576 C  CG1   . ILE A 1 482 ? 126.797 117.443 76.545  1.00 37.54  ? 470 ILE A CG1   1 
ATOM   3577 C  CG2   . ILE A 1 482 ? 125.278 118.236 74.716  1.00 49.14  ? 470 ILE A CG2   1 
ATOM   3578 C  CD1   . ILE A 1 482 ? 128.163 117.501 77.159  1.00 40.92  ? 470 ILE A CD1   1 
ATOM   3579 N  N     . ASN A 1 483 ? 129.717 116.322 74.321  1.00 38.80  ? 471 ASN A N     1 
ATOM   3580 C  CA    . ASN A 1 483 ? 131.128 116.410 73.973  1.00 36.20  ? 471 ASN A CA    1 
ATOM   3581 C  C     . ASN A 1 483 ? 131.398 115.934 72.553  1.00 37.06  ? 471 ASN A C     1 
ATOM   3582 O  O     . ASN A 1 483 ? 132.558 115.726 72.186  1.00 39.75  ? 471 ASN A O     1 
ATOM   3583 C  CB    . ASN A 1 483 ? 131.971 115.609 74.967  1.00 32.58  ? 471 ASN A CB    1 
ATOM   3584 C  CG    . ASN A 1 483 ? 131.708 114.122 74.891  1.00 39.79  ? 471 ASN A CG    1 
ATOM   3585 O  OD1   . ASN A 1 483 ? 130.561 113.682 74.859  1.00 46.68  ? 471 ASN A OD1   1 
ATOM   3586 N  ND2   . ASN A 1 483 ? 132.775 113.336 74.869  1.00 39.71  ? 471 ASN A ND2   1 
ATOM   3587 N  N     . PHE A 1 484 ? 130.346 115.745 71.764  1.00 34.62  ? 472 PHE A N     1 
ATOM   3588 C  CA    . PHE A 1 484 ? 130.431 115.397 70.358  1.00 37.31  ? 472 PHE A CA    1 
ATOM   3589 C  C     . PHE A 1 484 ? 129.677 116.433 69.540  1.00 38.02  ? 472 PHE A C     1 
ATOM   3590 O  O     . PHE A 1 484 ? 128.868 117.201 70.065  1.00 39.90  ? 472 PHE A O     1 
ATOM   3591 C  CB    . PHE A 1 484 ? 129.846 114.004 70.085  1.00 39.53  ? 472 PHE A CB    1 
ATOM   3592 C  CG    . PHE A 1 484 ? 130.657 112.878 70.651  1.00 43.74  ? 472 PHE A CG    1 
ATOM   3593 C  CD1   . PHE A 1 484 ? 131.909 112.587 70.141  1.00 47.39  ? 472 PHE A CD1   1 
ATOM   3594 C  CD2   . PHE A 1 484 ? 130.167 112.106 71.687  1.00 42.65  ? 472 PHE A CD2   1 
ATOM   3595 C  CE1   . PHE A 1 484 ? 132.656 111.551 70.656  1.00 48.19  ? 472 PHE A CE1   1 
ATOM   3596 C  CE2   . PHE A 1 484 ? 130.912 111.068 72.206  1.00 41.26  ? 472 PHE A CE2   1 
ATOM   3597 C  CZ    . PHE A 1 484 ? 132.157 110.791 71.690  1.00 43.70  ? 472 PHE A CZ    1 
ATOM   3598 N  N     . SER A 1 485 ? 129.956 116.455 68.244  1.00 36.92  ? 473 SER A N     1 
ATOM   3599 C  CA    . SER A 1 485 ? 129.156 117.259 67.339  1.00 34.21  ? 473 SER A CA    1 
ATOM   3600 C  C     . SER A 1 485 ? 127.813 116.578 67.092  1.00 35.29  ? 473 SER A C     1 
ATOM   3601 O  O     . SER A 1 485 ? 127.623 115.396 67.389  1.00 38.93  ? 473 SER A O     1 
ATOM   3602 C  CB    . SER A 1 485 ? 129.900 117.486 66.025  1.00 32.19  ? 473 SER A CB    1 
ATOM   3603 O  OG    . SER A 1 485 ? 129.875 116.329 65.215  1.00 38.16  ? 473 SER A OG    1 
ATOM   3604 N  N     . GLY A 1 486 ? 126.864 117.348 66.559  1.00 36.01  ? 474 GLY A N     1 
ATOM   3605 C  CA    . GLY A 1 486 ? 125.534 116.808 66.329  1.00 35.35  ? 474 GLY A CA    1 
ATOM   3606 C  C     . GLY A 1 486 ? 125.532 115.636 65.369  1.00 35.64  ? 474 GLY A C     1 
ATOM   3607 O  O     . GLY A 1 486 ? 124.863 114.626 65.604  1.00 39.61  ? 474 GLY A O     1 
ATOM   3608 N  N     . GLY A 1 487 ? 126.288 115.748 64.277  1.00 33.97  ? 475 GLY A N     1 
ATOM   3609 C  CA    . GLY A 1 487 ? 126.388 114.643 63.344  1.00 32.52  ? 475 GLY A CA    1 
ATOM   3610 C  C     . GLY A 1 487 ? 127.183 113.474 63.885  1.00 34.50  ? 475 GLY A C     1 
ATOM   3611 O  O     . GLY A 1 487 ? 126.935 112.329 63.507  1.00 41.20  ? 475 GLY A O     1 
ATOM   3612 N  N     . GLN A 1 488 ? 128.141 113.736 64.775  1.00 32.00  ? 476 GLN A N     1 
ATOM   3613 C  CA    . GLN A 1 488 ? 128.818 112.639 65.459  1.00 30.20  ? 476 GLN A CA    1 
ATOM   3614 C  C     . GLN A 1 488 ? 127.849 111.876 66.350  1.00 33.53  ? 476 GLN A C     1 
ATOM   3615 O  O     . GLN A 1 488 ? 127.888 110.644 66.410  1.00 40.85  ? 476 GLN A O     1 
ATOM   3616 C  CB    . GLN A 1 488 ? 129.998 113.166 66.275  1.00 34.36  ? 476 GLN A CB    1 
ATOM   3617 C  CG    . GLN A 1 488 ? 131.277 113.329 65.478  1.00 36.49  ? 476 GLN A CG    1 
ATOM   3618 C  CD    . GLN A 1 488 ? 132.382 113.984 66.274  1.00 37.86  ? 476 GLN A CD    1 
ATOM   3619 O  OE1   . GLN A 1 488 ? 132.157 114.490 67.372  1.00 37.91  ? 476 GLN A OE1   1 
ATOM   3620 N  NE2   . GLN A 1 488 ? 133.587 113.984 65.721  1.00 39.17  ? 476 GLN A NE2   1 
ATOM   3621 N  N     . ARG A 1 489 ? 126.963 112.594 67.045  1.00 33.66  ? 477 ARG A N     1 
ATOM   3622 C  CA    . ARG A 1 489 ? 125.919 111.935 67.822  1.00 34.26  ? 477 ARG A CA    1 
ATOM   3623 C  C     . ARG A 1 489 ? 124.988 111.136 66.922  1.00 34.79  ? 477 ARG A C     1 
ATOM   3624 O  O     . ARG A 1 489 ? 124.591 110.013 67.262  1.00 35.82  ? 477 ARG A O     1 
ATOM   3625 C  CB    . ARG A 1 489 ? 125.125 112.970 68.614  1.00 36.64  ? 477 ARG A CB    1 
ATOM   3626 C  CG    . ARG A 1 489 ? 125.808 113.460 69.864  1.00 36.97  ? 477 ARG A CG    1 
ATOM   3627 C  CD    . ARG A 1 489 ? 124.970 114.512 70.549  1.00 34.44  ? 477 ARG A CD    1 
ATOM   3628 N  NE    . ARG A 1 489 ? 125.711 115.748 70.754  1.00 43.27  ? 477 ARG A NE    1 
ATOM   3629 C  CZ    . ARG A 1 489 ? 125.262 116.949 70.422  1.00 48.65  ? 477 ARG A CZ    1 
ATOM   3630 N  NH1   . ARG A 1 489 ? 124.077 117.111 69.859  1.00 47.45  ? 477 ARG A NH1   1 
ATOM   3631 N  NH2   . ARG A 1 489 ? 126.022 118.014 70.661  1.00 50.46  ? 477 ARG A NH2   1 
ATOM   3632 N  N     . GLN A 1 490 ? 124.619 111.706 65.773  1.00 35.70  ? 478 GLN A N     1 
ATOM   3633 C  CA    . GLN A 1 490 ? 123.763 110.992 64.833  1.00 36.04  ? 478 GLN A CA    1 
ATOM   3634 C  C     . GLN A 1 490 ? 124.429 109.715 64.339  1.00 36.12  ? 478 GLN A C     1 
ATOM   3635 O  O     . GLN A 1 490 ? 123.781 108.668 64.236  1.00 40.25  ? 478 GLN A O     1 
ATOM   3636 C  CB    . GLN A 1 490 ? 123.410 111.897 63.656  1.00 36.23  ? 478 GLN A CB    1 
ATOM   3637 C  CG    . GLN A 1 490 ? 122.220 112.796 63.904  1.00 43.60  ? 478 GLN A CG    1 
ATOM   3638 C  CD    . GLN A 1 490 ? 121.675 113.386 62.627  1.00 48.22  ? 478 GLN A CD    1 
ATOM   3639 O  OE1   . GLN A 1 490 ? 122.289 113.273 61.569  1.00 50.51  ? 478 GLN A OE1   1 
ATOM   3640 N  NE2   . GLN A 1 490 ? 120.514 114.022 62.716  1.00 47.75  ? 478 GLN A NE2   1 
ATOM   3641 N  N     . ARG A 1 491 ? 125.723 109.783 64.029  1.00 36.32  ? 479 ARG A N     1 
ATOM   3642 C  CA    . ARG A 1 491 ? 126.434 108.603 63.556  1.00 34.35  ? 479 ARG A CA    1 
ATOM   3643 C  C     . ARG A 1 491 ? 126.619 107.576 64.664  1.00 33.27  ? 479 ARG A C     1 
ATOM   3644 O  O     . ARG A 1 491 ? 126.606 106.374 64.393  1.00 39.51  ? 479 ARG A O     1 
ATOM   3645 C  CB    . ARG A 1 491 ? 127.780 109.006 62.961  1.00 38.12  ? 479 ARG A CB    1 
ATOM   3646 C  CG    . ARG A 1 491 ? 127.666 109.657 61.596  1.00 41.44  ? 479 ARG A CG    1 
ATOM   3647 C  CD    . ARG A 1 491 ? 129.027 109.990 61.034  1.00 42.79  ? 479 ARG A CD    1 
ATOM   3648 N  NE    . ARG A 1 491 ? 129.606 111.159 61.680  1.00 43.35  ? 479 ARG A NE    1 
ATOM   3649 C  CZ    . ARG A 1 491 ? 130.881 111.508 61.589  1.00 49.04  ? 479 ARG A CZ    1 
ATOM   3650 N  NH1   . ARG A 1 491 ? 131.741 110.801 60.874  1.00 54.30  ? 479 ARG A NH1   1 
ATOM   3651 N  NH2   . ARG A 1 491 ? 131.306 112.589 62.235  1.00 45.84  ? 479 ARG A NH2   1 
ATOM   3652 N  N     . LEU A 1 492 ? 126.788 108.019 65.911  1.00 30.60  ? 480 LEU A N     1 
ATOM   3653 C  CA    . LEU A 1 492 ? 126.836 107.072 67.021  1.00 31.21  ? 480 LEU A CA    1 
ATOM   3654 C  C     . LEU A 1 492 ? 125.502 106.357 67.192  1.00 34.82  ? 480 LEU A C     1 
ATOM   3655 O  O     . LEU A 1 492 ? 125.465 105.149 67.446  1.00 35.87  ? 480 LEU A O     1 
ATOM   3656 C  CB    . LEU A 1 492 ? 127.232 107.785 68.312  1.00 32.31  ? 480 LEU A CB    1 
ATOM   3657 C  CG    . LEU A 1 492 ? 128.707 108.159 68.446  1.00 36.81  ? 480 LEU A CG    1 
ATOM   3658 C  CD1   . LEU A 1 492 ? 128.968 108.831 69.782  1.00 31.99  ? 480 LEU A CD1   1 
ATOM   3659 C  CD2   . LEU A 1 492 ? 129.591 106.936 68.270  1.00 39.03  ? 480 LEU A CD2   1 
ATOM   3660 N  N     . ALA A 1 493 ? 124.393 107.088 67.056  1.00 36.52  ? 481 ALA A N     1 
ATOM   3661 C  CA    . ALA A 1 493 ? 123.079 106.453 67.107  1.00 30.11  ? 481 ALA A CA    1 
ATOM   3662 C  C     . ALA A 1 493 ? 122.893 105.472 65.954  1.00 33.02  ? 481 ALA A C     1 
ATOM   3663 O  O     . ALA A 1 493 ? 122.340 104.379 66.136  1.00 41.01  ? 481 ALA A O     1 
ATOM   3664 C  CB    . ALA A 1 493 ? 121.983 107.514 67.093  1.00 31.97  ? 481 ALA A CB    1 
ATOM   3665 N  N     . ILE A 1 494 ? 123.351 105.847 64.759  1.00 29.11  ? 482 ILE A N     1 
ATOM   3666 C  CA    . ILE A 1 494 ? 123.266 104.950 63.610  1.00 29.44  ? 482 ILE A CA    1 
ATOM   3667 C  C     . ILE A 1 494 ? 124.085 103.690 63.856  1.00 35.23  ? 482 ILE A C     1 
ATOM   3668 O  O     . ILE A 1 494 ? 123.646 102.580 63.546  1.00 42.07  ? 482 ILE A O     1 
ATOM   3669 C  CB    . ILE A 1 494 ? 123.713 105.673 62.326  1.00 36.15  ? 482 ILE A CB    1 
ATOM   3670 C  CG1   . ILE A 1 494 ? 122.688 106.731 61.921  1.00 42.37  ? 482 ILE A CG1   1 
ATOM   3671 C  CG2   . ILE A 1 494 ? 123.911 104.683 61.192  1.00 34.95  ? 482 ILE A CG2   1 
ATOM   3672 C  CD1   . ILE A 1 494 ? 123.254 107.815 61.036  1.00 39.30  ? 482 ILE A CD1   1 
ATOM   3673 N  N     . ALA A 1 495 ? 125.289 103.841 64.411  1.00 35.05  ? 483 ALA A N     1 
ATOM   3674 C  CA    . ALA A 1 495 ? 126.132 102.685 64.699  1.00 35.42  ? 483 ALA A CA    1 
ATOM   3675 C  C     . ALA A 1 495 ? 125.512 101.799 65.770  1.00 38.89  ? 483 ALA A C     1 
ATOM   3676 O  O     . ALA A 1 495 ? 125.632 100.571 65.711  1.00 49.89  ? 483 ALA A O     1 
ATOM   3677 C  CB    . ALA A 1 495 ? 127.524 103.144 65.127  1.00 39.60  ? 483 ALA A CB    1 
ATOM   3678 N  N     . ARG A 1 496 ? 124.865 102.404 66.767  1.00 36.36  ? 484 ARG A N     1 
ATOM   3679 C  CA    . ARG A 1 496 ? 124.164 101.620 67.777  1.00 33.83  ? 484 ARG A CA    1 
ATOM   3680 C  C     . ARG A 1 496 ? 123.032 100.815 67.155  1.00 38.27  ? 484 ARG A C     1 
ATOM   3681 O  O     . ARG A 1 496 ? 122.810 99.656  67.520  1.00 44.78  ? 484 ARG A O     1 
ATOM   3682 C  CB    . ARG A 1 496 ? 123.631 102.538 68.874  1.00 27.76  ? 484 ARG A CB    1 
ATOM   3683 C  CG    . ARG A 1 496 ? 122.899 101.815 69.980  1.00 30.38  ? 484 ARG A CG    1 
ATOM   3684 C  CD    . ARG A 1 496 ? 122.431 102.784 71.041  1.00 31.17  ? 484 ARG A CD    1 
ATOM   3685 N  NE    . ARG A 1 496 ? 121.562 103.811 70.484  1.00 38.11  ? 484 ARG A NE    1 
ATOM   3686 C  CZ    . ARG A 1 496 ? 121.472 105.049 70.949  1.00 36.89  ? 484 ARG A CZ    1 
ATOM   3687 N  NH1   . ARG A 1 496 ? 122.186 105.450 71.986  1.00 39.14  ? 484 ARG A NH1   1 
ATOM   3688 N  NH2   . ARG A 1 496 ? 120.642 105.903 70.360  1.00 32.39  ? 484 ARG A NH2   1 
ATOM   3689 N  N     . ALA A 1 497 ? 122.301 101.417 66.217  1.00 42.35  ? 485 ALA A N     1 
ATOM   3690 C  CA    . ALA A 1 497 ? 121.262 100.673 65.511  1.00 43.15  ? 485 ALA A CA    1 
ATOM   3691 C  C     . ALA A 1 497 ? 121.859 99.580  64.630  1.00 44.18  ? 485 ALA A C     1 
ATOM   3692 O  O     . ALA A 1 497 ? 121.272 98.502  64.486  1.00 52.45  ? 485 ALA A O     1 
ATOM   3693 C  CB    . ALA A 1 497 ? 120.408 101.628 64.679  1.00 43.96  ? 485 ALA A CB    1 
ATOM   3694 N  N     . VAL A 1 498 ? 123.017 99.846  64.023  1.00 43.59  ? 486 VAL A N     1 
ATOM   3695 C  CA    . VAL A 1 498 ? 123.624 98.896  63.094  1.00 51.33  ? 486 VAL A CA    1 
ATOM   3696 C  C     . VAL A 1 498 ? 124.160 97.677  63.835  1.00 52.87  ? 486 VAL A C     1 
ATOM   3697 O  O     . VAL A 1 498 ? 123.980 96.537  63.391  1.00 58.86  ? 486 VAL A O     1 
ATOM   3698 C  CB    . VAL A 1 498 ? 124.727 99.588  62.271  1.00 48.63  ? 486 VAL A CB    1 
ATOM   3699 C  CG1   . VAL A 1 498 ? 125.647 98.562  61.635  1.00 53.04  ? 486 VAL A CG1   1 
ATOM   3700 C  CG2   . VAL A 1 498 ? 124.115 100.472 61.206  1.00 45.26  ? 486 VAL A CG2   1 
ATOM   3701 N  N     . ILE A 1 499 ? 124.822 97.894  64.974  1.00 46.19  ? 487 ILE A N     1 
ATOM   3702 C  CA    . ILE A 1 499 ? 125.417 96.795  65.726  1.00 51.79  ? 487 ILE A CA    1 
ATOM   3703 C  C     . ILE A 1 499 ? 124.364 95.808  66.205  1.00 60.39  ? 487 ILE A C     1 
ATOM   3704 O  O     . ILE A 1 499 ? 124.684 94.652  66.498  1.00 67.23  ? 487 ILE A O     1 
ATOM   3705 C  CB    . ILE A 1 499 ? 126.243 97.344  66.908  1.00 49.54  ? 487 ILE A CB    1 
ATOM   3706 C  CG1   . ILE A 1 499 ? 127.383 96.388  67.253  1.00 51.87  ? 487 ILE A CG1   1 
ATOM   3707 C  CG2   . ILE A 1 499 ? 125.366 97.582  68.124  1.00 49.90  ? 487 ILE A CG2   1 
ATOM   3708 C  CD1   . ILE A 1 499 ? 128.384 96.974  68.204  1.00 54.87  ? 487 ILE A CD1   1 
ATOM   3709 N  N     . ARG A 1 500 ? 123.105 96.239  66.290  1.00 54.03  ? 488 ARG A N     1 
ATOM   3710 C  CA    . ARG A 1 500 ? 122.027 95.325  66.641  1.00 52.32  ? 488 ARG A CA    1 
ATOM   3711 C  C     . ARG A 1 500 ? 121.730 94.350  65.510  1.00 59.01  ? 488 ARG A C     1 
ATOM   3712 O  O     . ARG A 1 500 ? 121.306 93.218  65.766  1.00 68.06  ? 488 ARG A O     1 
ATOM   3713 C  CB    . ARG A 1 500 ? 120.782 96.130  67.012  1.00 50.84  ? 488 ARG A CB    1 
ATOM   3714 C  CG    . ARG A 1 500 ? 119.488 95.348  67.027  1.00 52.51  ? 488 ARG A CG    1 
ATOM   3715 C  CD    . ARG A 1 500 ? 118.420 96.101  67.788  1.00 53.92  ? 488 ARG A CD    1 
ATOM   3716 N  NE    . ARG A 1 500 ? 118.552 95.903  69.224  1.00 52.67  ? 488 ARG A NE    1 
ATOM   3717 C  CZ    . ARG A 1 500 ? 117.537 95.906  70.076  1.00 52.71  ? 488 ARG A CZ    1 
ATOM   3718 N  NH1   . ARG A 1 500 ? 116.298 96.124  69.671  1.00 56.25  ? 488 ARG A NH1   1 
ATOM   3719 N  NH2   . ARG A 1 500 ? 117.772 95.683  71.364  1.00 51.30  ? 488 ARG A NH2   1 
ATOM   3720 N  N     . ARG A 1 501 ? 121.976 94.757  64.268  1.00 57.68  ? 489 ARG A N     1 
ATOM   3721 C  CA    . ARG A 1 501 ? 121.588 93.998  63.085  1.00 59.76  ? 489 ARG A CA    1 
ATOM   3722 C  C     . ARG A 1 501 ? 120.110 93.599  63.142  1.00 61.23  ? 489 ARG A C     1 
ATOM   3723 O  O     . ARG A 1 501 ? 119.780 92.410  63.101  1.00 58.52  ? 489 ARG A O     1 
ATOM   3724 C  CB    . ARG A 1 501 ? 122.471 92.771  62.907  1.00 60.85  ? 489 ARG A CB    1 
ATOM   3725 C  CG    . ARG A 1 501 ? 123.946 93.087  62.739  1.00 65.65  ? 489 ARG A CG    1 
ATOM   3726 C  CD    . ARG A 1 501 ? 124.193 93.862  61.457  1.00 70.52  ? 489 ARG A CD    1 
ATOM   3727 N  NE    . ARG A 1 501 ? 125.363 94.727  61.553  1.00 74.16  ? 489 ARG A NE    1 
ATOM   3728 C  CZ    . ARG A 1 501 ? 126.407 94.669  60.738  1.00 79.65  ? 489 ARG A CZ    1 
ATOM   3729 N  NH1   . ARG A 1 501 ? 126.464 93.792  59.749  1.00 83.19  ? 489 ARG A NH1   1 
ATOM   3730 N  NH2   . ARG A 1 501 ? 127.418 95.513  60.918  1.00 77.01  ? 489 ARG A NH2   1 
ATOM   3731 N  N     . PRO A 1 502 ? 119.202 94.566  63.230  1.00 66.67  ? 490 PRO A N     1 
ATOM   3732 C  CA    . PRO A 1 502 ? 117.789 94.245  63.430  1.00 66.13  ? 490 PRO A CA    1 
ATOM   3733 C  C     . PRO A 1 502 ? 117.112 93.821  62.134  1.00 65.11  ? 490 PRO A C     1 
ATOM   3734 O  O     . PRO A 1 502 ? 117.654 93.948  61.036  1.00 63.13  ? 490 PRO A O     1 
ATOM   3735 C  CB    . PRO A 1 502 ? 117.216 95.565  63.940  1.00 62.22  ? 490 PRO A CB    1 
ATOM   3736 C  CG    . PRO A 1 502 ? 118.013 96.579  63.209  1.00 59.26  ? 490 PRO A CG    1 
ATOM   3737 C  CD    . PRO A 1 502 ? 119.410 96.020  63.110  1.00 61.66  ? 490 PRO A CD    1 
ATOM   3738 N  N     . ALA A 1 503 ? 115.894 93.306  62.290  1.00 64.15  ? 491 ALA A N     1 
ATOM   3739 C  CA    . ALA A 1 503 ? 115.073 92.968  61.136  1.00 67.50  ? 491 ALA A CA    1 
ATOM   3740 C  C     . ALA A 1 503 ? 114.457 94.202  60.495  1.00 67.17  ? 491 ALA A C     1 
ATOM   3741 O  O     . ALA A 1 503 ? 114.243 94.221  59.278  1.00 69.67  ? 491 ALA A O     1 
ATOM   3742 C  CB    . ALA A 1 503 ? 113.973 91.991  61.545  1.00 69.14  ? 491 ALA A CB    1 
ATOM   3743 N  N     . ILE A 1 504 ? 114.165 95.229  61.287  1.00 66.29  ? 492 ILE A N     1 
ATOM   3744 C  CA    . ILE A 1 504 ? 113.527 96.449  60.809  1.00 69.15  ? 492 ILE A CA    1 
ATOM   3745 C  C     . ILE A 1 504 ? 114.368 97.638  61.244  1.00 66.89  ? 492 ILE A C     1 
ATOM   3746 O  O     . ILE A 1 504 ? 114.723 97.756  62.422  1.00 64.52  ? 492 ILE A O     1 
ATOM   3747 C  CB    . ILE A 1 504 ? 112.085 96.582  61.336  1.00 65.55  ? 492 ILE A CB    1 
ATOM   3748 C  CG1   . ILE A 1 504 ? 111.184 95.536  60.680  1.00 68.06  ? 492 ILE A CG1   1 
ATOM   3749 C  CG2   . ILE A 1 504 ? 111.549 97.980  61.091  1.00 59.78  ? 492 ILE A CG2   1 
ATOM   3750 C  CD1   . ILE A 1 504 ? 110.024 95.112  61.539  1.00 64.16  ? 492 ILE A CD1   1 
ATOM   3751 N  N     . TYR A 1 505 ? 114.690 98.512  60.296  1.00 65.81  ? 493 TYR A N     1 
ATOM   3752 C  CA    . TYR A 1 505 ? 115.391 99.756  60.573  1.00 54.70  ? 493 TYR A CA    1 
ATOM   3753 C  C     . TYR A 1 505 ? 114.402 100.908 60.494  1.00 56.64  ? 493 TYR A C     1 
ATOM   3754 O  O     . TYR A 1 505 ? 113.695 101.054 59.492  1.00 58.10  ? 493 TYR A O     1 
ATOM   3755 C  CB    . TYR A 1 505 ? 116.527 99.981  59.577  1.00 57.23  ? 493 TYR A CB    1 
ATOM   3756 C  CG    . TYR A 1 505 ? 117.740 99.104  59.778  1.00 60.98  ? 493 TYR A CG    1 
ATOM   3757 C  CD1   . TYR A 1 505 ? 118.786 99.511  60.593  1.00 66.17  ? 493 TYR A CD1   1 
ATOM   3758 C  CD2   . TYR A 1 505 ? 117.850 97.882  59.132  1.00 63.69  ? 493 TYR A CD2   1 
ATOM   3759 C  CE1   . TYR A 1 505 ? 119.900 98.718  60.770  1.00 65.51  ? 493 TYR A CE1   1 
ATOM   3760 C  CE2   . TYR A 1 505 ? 118.959 97.083  59.305  1.00 66.43  ? 493 TYR A CE2   1 
ATOM   3761 C  CZ    . TYR A 1 505 ? 119.982 97.506  60.122  1.00 67.72  ? 493 TYR A CZ    1 
ATOM   3762 O  OH    . TYR A 1 505 ? 121.089 96.712  60.297  1.00 68.99  ? 493 TYR A OH    1 
ATOM   3763 N  N     . LEU A 1 506 ? 114.351 101.721 61.544  1.00 56.92  ? 494 LEU A N     1 
ATOM   3764 C  CA    . LEU A 1 506 ? 113.478 102.892 61.592  1.00 56.38  ? 494 LEU A CA    1 
ATOM   3765 C  C     . LEU A 1 506 ? 114.358 104.129 61.727  1.00 52.93  ? 494 LEU A C     1 
ATOM   3766 O  O     . LEU A 1 506 ? 114.853 104.433 62.816  1.00 51.35  ? 494 LEU A O     1 
ATOM   3767 C  CB    . LEU A 1 506 ? 112.476 102.790 62.738  1.00 51.45  ? 494 LEU A CB    1 
ATOM   3768 C  CG    . LEU A 1 506 ? 111.495 101.620 62.665  1.00 49.99  ? 494 LEU A CG    1 
ATOM   3769 C  CD1   . LEU A 1 506 ? 110.563 101.637 63.850  1.00 47.46  ? 494 LEU A CD1   1 
ATOM   3770 C  CD2   . LEU A 1 506 ? 110.706 101.667 61.377  1.00 47.76  ? 494 LEU A CD2   1 
ATOM   3771 N  N     . PHE A 1 507 ? 114.548 104.840 60.620  1.00 53.20  ? 495 PHE A N     1 
ATOM   3772 C  CA    . PHE A 1 507 ? 115.389 106.033 60.579  1.00 53.27  ? 495 PHE A CA    1 
ATOM   3773 C  C     . PHE A 1 507 ? 114.470 107.249 60.629  1.00 54.97  ? 495 PHE A C     1 
ATOM   3774 O  O     . PHE A 1 507 ? 113.984 107.725 59.604  1.00 59.01  ? 495 PHE A O     1 
ATOM   3775 C  CB    . PHE A 1 507 ? 116.263 106.038 59.331  1.00 58.90  ? 495 PHE A CB    1 
ATOM   3776 C  CG    . PHE A 1 507 ? 117.206 104.872 59.243  1.00 57.73  ? 495 PHE A CG    1 
ATOM   3777 C  CD1   . PHE A 1 507 ? 118.240 104.729 60.150  1.00 53.57  ? 495 PHE A CD1   1 
ATOM   3778 C  CD2   . PHE A 1 507 ? 117.066 103.927 58.244  1.00 56.66  ? 495 PHE A CD2   1 
ATOM   3779 C  CE1   . PHE A 1 507 ? 119.109 103.663 60.071  1.00 50.60  ? 495 PHE A CE1   1 
ATOM   3780 C  CE2   . PHE A 1 507 ? 117.934 102.860 58.157  1.00 58.74  ? 495 PHE A CE2   1 
ATOM   3781 C  CZ    . PHE A 1 507 ? 118.956 102.728 59.073  1.00 58.75  ? 495 PHE A CZ    1 
ATOM   3782 N  N     . ASP A 1 508 ? 114.229 107.753 61.839  1.00 51.76  ? 496 ASP A N     1 
ATOM   3783 C  CA    . ASP A 1 508 ? 113.370 108.920 62.035  1.00 55.33  ? 496 ASP A CA    1 
ATOM   3784 C  C     . ASP A 1 508 ? 114.224 110.178 61.905  1.00 57.69  ? 496 ASP A C     1 
ATOM   3785 O  O     . ASP A 1 508 ? 114.612 110.815 62.886  1.00 52.79  ? 496 ASP A O     1 
ATOM   3786 C  CB    . ASP A 1 508 ? 112.666 108.848 63.383  1.00 52.42  ? 496 ASP A CB    1 
ATOM   3787 C  CG    . ASP A 1 508 ? 111.514 109.826 63.492  1.00 51.85  ? 496 ASP A CG    1 
ATOM   3788 O  OD1   . ASP A 1 508 ? 111.060 110.334 62.446  1.00 49.96  ? 496 ASP A OD1   1 
ATOM   3789 O  OD2   . ASP A 1 508 ? 111.060 110.084 64.625  1.00 50.19  ? 496 ASP A OD2   1 
ATOM   3790 N  N     . ASP A 1 509 ? 114.515 110.534 60.652  1.00 61.61  ? 497 ASP A N     1 
ATOM   3791 C  CA    . ASP A 1 509 ? 115.360 111.680 60.314  1.00 60.04  ? 497 ASP A CA    1 
ATOM   3792 C  C     . ASP A 1 509 ? 116.721 111.574 61.006  1.00 62.02  ? 497 ASP A C     1 
ATOM   3793 O  O     . ASP A 1 509 ? 117.104 112.407 61.828  1.00 62.60  ? 497 ASP A O     1 
ATOM   3794 C  CB    . ASP A 1 509 ? 114.659 112.998 60.658  1.00 65.33  ? 497 ASP A CB    1 
ATOM   3795 C  CG    . ASP A 1 509 ? 115.006 114.111 59.688  1.00 81.88  ? 497 ASP A CG    1 
ATOM   3796 O  OD1   . ASP A 1 509 ? 115.587 113.813 58.623  1.00 81.39  ? 497 ASP A OD1   1 
ATOM   3797 O  OD2   . ASP A 1 509 ? 114.699 115.283 59.989  1.00 84.44  ? 497 ASP A OD2   1 
ATOM   3798 N  N     . ALA A 1 510 ? 117.449 110.519 60.650  1.00 61.63  ? 498 ALA A N     1 
ATOM   3799 C  CA    . ALA A 1 510 ? 118.727 110.198 61.267  1.00 55.36  ? 498 ALA A CA    1 
ATOM   3800 C  C     . ALA A 1 510 ? 119.921 110.769 60.516  1.00 56.20  ? 498 ALA A C     1 
ATOM   3801 O  O     . ALA A 1 510 ? 121.061 110.470 60.881  1.00 60.09  ? 498 ALA A O     1 
ATOM   3802 C  CB    . ALA A 1 510 ? 118.883 108.680 61.388  1.00 52.91  ? 498 ALA A CB    1 
ATOM   3803 N  N     . PHE A 1 511 ? 119.694 111.576 59.478  1.00 56.90  ? 499 PHE A N     1 
ATOM   3804 C  CA    . PHE A 1 511 ? 120.779 112.075 58.641  1.00 52.57  ? 499 PHE A CA    1 
ATOM   3805 C  C     . PHE A 1 511 ? 120.695 113.580 58.418  1.00 52.86  ? 499 PHE A C     1 
ATOM   3806 O  O     . PHE A 1 511 ? 121.311 114.093 57.480  1.00 58.71  ? 499 PHE A O     1 
ATOM   3807 C  CB    . PHE A 1 511 ? 120.792 111.345 57.298  1.00 55.12  ? 499 PHE A CB    1 
ATOM   3808 C  CG    . PHE A 1 511 ? 120.665 109.857 57.419  1.00 59.90  ? 499 PHE A CG    1 
ATOM   3809 C  CD1   . PHE A 1 511 ? 121.774 109.075 57.675  1.00 59.56  ? 499 PHE A CD1   1 
ATOM   3810 C  CD2   . PHE A 1 511 ? 119.435 109.241 57.288  1.00 62.42  ? 499 PHE A CD2   1 
ATOM   3811 C  CE1   . PHE A 1 511 ? 121.660 107.707 57.794  1.00 63.13  ? 499 PHE A CE1   1 
ATOM   3812 C  CE2   . PHE A 1 511 ? 119.318 107.874 57.408  1.00 60.00  ? 499 PHE A CE2   1 
ATOM   3813 C  CZ    . PHE A 1 511 ? 120.431 107.107 57.659  1.00 61.27  ? 499 PHE A CZ    1 
ATOM   3814 N  N     . SER A 1 512 ? 119.951 114.298 59.258  1.00 54.09  ? 500 SER A N     1 
ATOM   3815 C  CA    . SER A 1 512 ? 119.803 115.737 59.075  1.00 53.12  ? 500 SER A CA    1 
ATOM   3816 C  C     . SER A 1 512 ? 121.066 116.506 59.438  1.00 50.13  ? 500 SER A C     1 
ATOM   3817 O  O     . SER A 1 512 ? 121.270 117.610 58.926  1.00 47.86  ? 500 SER A O     1 
ATOM   3818 C  CB    . SER A 1 512 ? 118.627 116.253 59.904  1.00 53.42  ? 500 SER A CB    1 
ATOM   3819 O  OG    . SER A 1 512 ? 118.888 116.135 61.291  1.00 50.72  ? 500 SER A OG    1 
ATOM   3820 N  N     . ALA A 1 513 ? 121.916 115.954 60.301  1.00 50.30  ? 501 ALA A N     1 
ATOM   3821 C  CA    . ALA A 1 513 ? 123.121 116.635 60.755  1.00 49.99  ? 501 ALA A CA    1 
ATOM   3822 C  C     . ALA A 1 513 ? 124.376 116.157 60.040  1.00 47.25  ? 501 ALA A C     1 
ATOM   3823 O  O     . ALA A 1 513 ? 125.484 116.491 60.468  1.00 48.01  ? 501 ALA A O     1 
ATOM   3824 C  CB    . ALA A 1 513 ? 123.285 116.468 62.266  1.00 37.69  ? 501 ALA A CB    1 
ATOM   3825 N  N     . LEU A 1 514 ? 124.232 115.385 58.970  1.00 45.86  ? 502 LEU A N     1 
ATOM   3826 C  CA    . LEU A 1 514 ? 125.363 114.891 58.201  1.00 49.21  ? 502 LEU A CA    1 
ATOM   3827 C  C     . LEU A 1 514 ? 125.539 115.723 56.939  1.00 55.75  ? 502 LEU A C     1 
ATOM   3828 O  O     . LEU A 1 514 ? 124.559 116.166 56.334  1.00 58.06  ? 502 LEU A O     1 
ATOM   3829 C  CB    . LEU A 1 514 ? 125.174 113.420 57.824  1.00 53.63  ? 502 LEU A CB    1 
ATOM   3830 C  CG    . LEU A 1 514 ? 124.838 112.429 58.937  1.00 54.53  ? 502 LEU A CG    1 
ATOM   3831 C  CD1   . LEU A 1 514 ? 124.800 111.019 58.381  1.00 56.69  ? 502 LEU A CD1   1 
ATOM   3832 C  CD2   . LEU A 1 514 ? 125.837 112.532 60.072  1.00 46.80  ? 502 LEU A CD2   1 
ATOM   3833 N  N     . ASP A 1 515 ? 126.793 115.937 56.551  1.00 54.06  ? 503 ASP A N     1 
ATOM   3834 C  CA    . ASP A 1 515 ? 127.078 116.611 55.297  1.00 53.12  ? 503 ASP A CA    1 
ATOM   3835 C  C     . ASP A 1 515 ? 126.778 115.680 54.124  1.00 58.19  ? 503 ASP A C     1 
ATOM   3836 O  O     . ASP A 1 515 ? 126.481 114.497 54.296  1.00 60.89  ? 503 ASP A O     1 
ATOM   3837 C  CB    . ASP A 1 515 ? 128.530 117.087 55.263  1.00 54.26  ? 503 ASP A CB    1 
ATOM   3838 C  CG    . ASP A 1 515 ? 129.522 115.944 55.312  1.00 57.96  ? 503 ASP A CG    1 
ATOM   3839 O  OD1   . ASP A 1 515 ? 129.847 115.390 54.243  1.00 63.95  ? 503 ASP A OD1   1 
ATOM   3840 O  OD2   . ASP A 1 515 ? 129.977 115.596 56.421  1.00 54.63  ? 503 ASP A OD2   1 
ATOM   3841 N  N     . VAL A 1 516 ? 126.855 116.232 52.912  1.00 63.87  ? 504 VAL A N     1 
ATOM   3842 C  CA    . VAL A 1 516 ? 126.478 115.470 51.723  1.00 66.45  ? 504 VAL A CA    1 
ATOM   3843 C  C     . VAL A 1 516 ? 127.380 114.253 51.549  1.00 68.28  ? 504 VAL A C     1 
ATOM   3844 O  O     . VAL A 1 516 ? 126.904 113.152 51.246  1.00 68.03  ? 504 VAL A O     1 
ATOM   3845 C  CB    . VAL A 1 516 ? 126.495 116.375 50.477  1.00 72.60  ? 504 VAL A CB    1 
ATOM   3846 C  CG1   . VAL A 1 516 ? 125.232 117.212 50.422  1.00 77.77  ? 504 VAL A CG1   1 
ATOM   3847 C  CG2   . VAL A 1 516 ? 127.724 117.268 50.481  1.00 70.47  ? 504 VAL A CG2   1 
ATOM   3848 N  N     . HIS A 1 517 ? 128.690 114.424 51.739  1.00 67.45  ? 505 HIS A N     1 
ATOM   3849 C  CA    . HIS A 1 517 ? 129.611 113.303 51.576  1.00 67.41  ? 505 HIS A CA    1 
ATOM   3850 C  C     . HIS A 1 517 ? 129.394 112.243 52.650  1.00 65.96  ? 505 HIS A C     1 
ATOM   3851 O  O     . HIS A 1 517 ? 129.315 111.046 52.349  1.00 69.38  ? 505 HIS A O     1 
ATOM   3852 C  CB    . HIS A 1 517 ? 131.055 113.802 51.596  1.00 67.85  ? 505 HIS A CB    1 
ATOM   3853 C  CG    . HIS A 1 517 ? 131.454 114.549 50.363  1.00 76.37  ? 505 HIS A CG    1 
ATOM   3854 N  ND1   . HIS A 1 517 ? 131.418 113.983 49.107  1.00 78.92  ? 505 HIS A ND1   1 
ATOM   3855 C  CD2   . HIS A 1 517 ? 131.904 115.814 50.193  1.00 77.53  ? 505 HIS A CD2   1 
ATOM   3856 C  CE1   . HIS A 1 517 ? 131.825 114.869 48.216  1.00 81.18  ? 505 HIS A CE1   1 
ATOM   3857 N  NE2   . HIS A 1 517 ? 132.126 115.989 48.849  1.00 80.52  ? 505 HIS A NE2   1 
ATOM   3858 N  N     . THR A 1 518 ? 129.303 112.665 53.913  1.00 60.18  ? 506 THR A N     1 
ATOM   3859 C  CA    . THR A 1 518 ? 129.076 111.713 54.995  1.00 60.90  ? 506 THR A CA    1 
ATOM   3860 C  C     . THR A 1 518 ? 127.716 111.043 54.860  1.00 60.58  ? 506 THR A C     1 
ATOM   3861 O  O     . THR A 1 518 ? 127.587 109.835 55.090  1.00 64.24  ? 506 THR A O     1 
ATOM   3862 C  CB    . THR A 1 518 ? 129.198 112.411 56.349  1.00 61.05  ? 506 THR A CB    1 
ATOM   3863 O  OG1   . THR A 1 518 ? 130.466 113.072 56.434  1.00 61.64  ? 506 THR A OG1   1 
ATOM   3864 C  CG2   . THR A 1 518 ? 129.088 111.405 57.481  1.00 53.43  ? 506 THR A CG2   1 
ATOM   3865 N  N     . ASP A 1 519 ? 126.690 111.811 54.488  1.00 61.74  ? 507 ASP A N     1 
ATOM   3866 C  CA    . ASP A 1 519 ? 125.372 111.226 54.272  1.00 63.18  ? 507 ASP A CA    1 
ATOM   3867 C  C     . ASP A 1 519 ? 125.405 110.188 53.162  1.00 65.62  ? 507 ASP A C     1 
ATOM   3868 O  O     . ASP A 1 519 ? 124.820 109.109 53.298  1.00 66.46  ? 507 ASP A O     1 
ATOM   3869 C  CB    . ASP A 1 519 ? 124.354 112.319 53.954  1.00 70.38  ? 507 ASP A CB    1 
ATOM   3870 C  CG    . ASP A 1 519 ? 122.929 111.835 54.070  1.00 79.68  ? 507 ASP A CG    1 
ATOM   3871 O  OD1   . ASP A 1 519 ? 122.065 112.334 53.320  1.00 81.14  ? 507 ASP A OD1   1 
ATOM   3872 O  OD2   . ASP A 1 519 ? 122.677 110.934 54.894  1.00 80.16  ? 507 ASP A OD2   1 
ATOM   3873 N  N     . ALA A 1 520 ? 126.089 110.492 52.056  1.00 68.85  ? 508 ALA A N     1 
ATOM   3874 C  CA    . ALA A 1 520 ? 126.188 109.531 50.964  1.00 67.16  ? 508 ALA A CA    1 
ATOM   3875 C  C     . ALA A 1 520 ? 126.921 108.270 51.402  1.00 64.52  ? 508 ALA A C     1 
ATOM   3876 O  O     . ALA A 1 520 ? 126.482 107.154 51.104  1.00 65.27  ? 508 ALA A O     1 
ATOM   3877 C  CB    . ALA A 1 520 ? 126.886 110.169 49.765  1.00 64.80  ? 508 ALA A CB    1 
ATOM   3878 N  N     . ARG A 1 521 ? 128.038 108.426 52.116  1.00 62.68  ? 509 ARG A N     1 
ATOM   3879 C  CA    . ARG A 1 521 ? 128.791 107.261 52.568  1.00 61.05  ? 509 ARG A CA    1 
ATOM   3880 C  C     . ARG A 1 521 ? 127.950 106.390 53.492  1.00 63.79  ? 509 ARG A C     1 
ATOM   3881 O  O     . ARG A 1 521 ? 127.904 105.163 53.340  1.00 68.36  ? 509 ARG A O     1 
ATOM   3882 C  CB    . ARG A 1 521 ? 130.072 107.705 53.272  1.00 63.97  ? 509 ARG A CB    1 
ATOM   3883 C  CG    . ARG A 1 521 ? 131.199 108.096 52.335  1.00 66.50  ? 509 ARG A CG    1 
ATOM   3884 C  CD    . ARG A 1 521 ? 132.246 108.915 53.065  1.00 70.62  ? 509 ARG A CD    1 
ATOM   3885 N  NE    . ARG A 1 521 ? 132.862 108.166 54.152  1.00 76.86  ? 509 ARG A NE    1 
ATOM   3886 C  CZ    . ARG A 1 521 ? 133.342 108.714 55.260  1.00 76.20  ? 509 ARG A CZ    1 
ATOM   3887 N  NH1   . ARG A 1 521 ? 133.281 110.018 55.468  1.00 70.50  ? 509 ARG A NH1   1 
ATOM   3888 N  NH2   . ARG A 1 521 ? 133.895 107.933 56.184  1.00 70.66  ? 509 ARG A NH2   1 
ATOM   3889 N  N     . VAL A 1 522 ? 127.260 107.015 54.450  1.00 61.17  ? 510 VAL A N     1 
ATOM   3890 C  CA    . VAL A 1 522 ? 126.446 106.258 55.395  1.00 57.63  ? 510 VAL A CA    1 
ATOM   3891 C  C     . VAL A 1 522 ? 125.295 105.569 54.675  1.00 63.64  ? 510 VAL A C     1 
ATOM   3892 O  O     . VAL A 1 522 ? 124.959 104.419 54.974  1.00 69.55  ? 510 VAL A O     1 
ATOM   3893 C  CB    . VAL A 1 522 ? 125.945 107.174 56.527  1.00 56.32  ? 510 VAL A CB    1 
ATOM   3894 C  CG1   . VAL A 1 522 ? 124.935 106.446 57.395  1.00 54.12  ? 510 VAL A CG1   1 
ATOM   3895 C  CG2   . VAL A 1 522 ? 127.111 107.653 57.371  1.00 54.36  ? 510 VAL A CG2   1 
ATOM   3896 N  N     . ARG A 1 523 ? 124.670 106.257 53.716  1.00 66.60  ? 511 ARG A N     1 
ATOM   3897 C  CA    . ARG A 1 523 ? 123.544 105.663 53.005  1.00 66.61  ? 511 ARG A CA    1 
ATOM   3898 C  C     . ARG A 1 523 ? 123.981 104.476 52.156  1.00 70.13  ? 511 ARG A C     1 
ATOM   3899 O  O     . ARG A 1 523 ? 123.287 103.455 52.115  1.00 72.63  ? 511 ARG A O     1 
ATOM   3900 C  CB    . ARG A 1 523 ? 122.845 106.719 52.152  1.00 72.77  ? 511 ARG A CB    1 
ATOM   3901 C  CG    . ARG A 1 523 ? 121.949 107.648 52.955  1.00 74.38  ? 511 ARG A CG    1 
ATOM   3902 C  CD    . ARG A 1 523 ? 121.464 108.821 52.125  1.00 77.38  ? 511 ARG A CD    1 
ATOM   3903 N  NE    . ARG A 1 523 ? 121.482 108.524 50.698  1.00 84.58  ? 511 ARG A NE    1 
ATOM   3904 C  CZ    . ARG A 1 523 ? 121.883 109.374 49.763  1.00 90.19  ? 511 ARG A CZ    1 
ATOM   3905 N  NH1   . ARG A 1 523 ? 122.306 110.589 50.070  1.00 89.01  ? 511 ARG A NH1   1 
ATOM   3906 N  NH2   . ARG A 1 523 ? 121.856 108.995 48.488  1.00 90.15  ? 511 ARG A NH2   1 
ATOM   3907 N  N     . ASP A 1 524 ? 125.125 104.580 51.474  1.00 71.15  ? 512 ASP A N     1 
ATOM   3908 C  CA    . ASP A 1 524 ? 125.632 103.429 50.728  1.00 75.36  ? 512 ASP A CA    1 
ATOM   3909 C  C     . ASP A 1 524 ? 126.007 102.276 51.653  1.00 77.28  ? 512 ASP A C     1 
ATOM   3910 O  O     . ASP A 1 524 ? 125.731 101.110 51.340  1.00 83.55  ? 512 ASP A O     1 
ATOM   3911 C  CB    . ASP A 1 524 ? 126.819 103.835 49.856  1.00 74.04  ? 512 ASP A CB    1 
ATOM   3912 C  CG    . ASP A 1 524 ? 126.535 105.065 49.021  1.00 80.20  ? 512 ASP A CG    1 
ATOM   3913 O  OD1   . ASP A 1 524 ? 125.447 105.657 49.182  1.00 80.10  ? 512 ASP A OD1   1 
ATOM   3914 O  OD2   . ASP A 1 524 ? 127.401 105.446 48.206  1.00 81.58  ? 512 ASP A OD2   1 
ATOM   3915 N  N     . ALA A 1 525 ? 126.630 102.573 52.796  1.00 73.24  ? 513 ALA A N     1 
ATOM   3916 C  CA    . ALA A 1 525 ? 126.969 101.508 53.735  1.00 71.75  ? 513 ALA A CA    1 
ATOM   3917 C  C     . ALA A 1 525 ? 125.717 100.815 54.260  1.00 72.83  ? 513 ALA A C     1 
ATOM   3918 O  O     . ALA A 1 525 ? 125.685 99.586  54.391  1.00 75.64  ? 513 ALA A O     1 
ATOM   3919 C  CB    . ALA A 1 525 ? 127.799 102.069 54.889  1.00 66.04  ? 513 ALA A CB    1 
ATOM   3920 N  N     . LEU A 1 526 ? 124.671 101.587 54.560  1.00 72.49  ? 514 LEU A N     1 
ATOM   3921 C  CA    . LEU A 1 526 ? 123.426 101.002 55.044  1.00 71.63  ? 514 LEU A CA    1 
ATOM   3922 C  C     . LEU A 1 526 ? 122.721 100.212 53.950  1.00 75.06  ? 514 LEU A C     1 
ATOM   3923 O  O     . LEU A 1 526 ? 122.102 99.179  54.224  1.00 82.04  ? 514 LEU A O     1 
ATOM   3924 C  CB    . LEU A 1 526 ? 122.515 102.098 55.592  1.00 65.72  ? 514 LEU A CB    1 
ATOM   3925 C  CG    . LEU A 1 526 ? 122.940 102.663 56.947  1.00 62.23  ? 514 LEU A CG    1 
ATOM   3926 C  CD1   . LEU A 1 526 ? 122.168 103.927 57.269  1.00 64.50  ? 514 LEU A CD1   1 
ATOM   3927 C  CD2   . LEU A 1 526 ? 122.747 101.624 58.033  1.00 63.13  ? 514 LEU A CD2   1 
ATOM   3928 N  N     . ARG A 1 527 ? 122.796 100.687 52.706  1.00 75.88  ? 515 ARG A N     1 
ATOM   3929 C  CA    . ARG A 1 527 ? 122.236 99.935  51.590  1.00 82.63  ? 515 ARG A CA    1 
ATOM   3930 C  C     . ARG A 1 527 ? 122.943 98.597  51.428  1.00 85.42  ? 515 ARG A C     1 
ATOM   3931 O  O     . ARG A 1 527 ? 122.305 97.577  51.144  1.00 87.11  ? 515 ARG A O     1 
ATOM   3932 C  CB    . ARG A 1 527 ? 122.338 100.758 50.308  1.00 82.26  ? 515 ARG A CB    1 
ATOM   3933 C  CG    . ARG A 1 527 ? 121.369 100.349 49.215  1.00 89.76  ? 515 ARG A CG    1 
ATOM   3934 C  CD    . ARG A 1 527 ? 121.562 101.202 47.971  1.00 93.39  ? 515 ARG A CD    1 
ATOM   3935 N  NE    . ARG A 1 527 ? 121.599 102.625 48.286  1.00 96.02  ? 515 ARG A NE    1 
ATOM   3936 C  CZ    . ARG A 1 527 ? 122.672 103.395 48.164  1.00 93.13  ? 515 ARG A CZ    1 
ATOM   3937 N  NH1   . ARG A 1 527 ? 123.825 102.909 47.732  1.00 90.36  ? 515 ARG A NH1   1 
ATOM   3938 N  NH2   . ARG A 1 527 ? 122.587 104.683 48.484  1.00 86.88  ? 515 ARG A NH2   1 
ATOM   3939 N  N     . GLU A 1 528 ? 124.265 98.586  51.598  1.00 84.06  ? 516 GLU A N     1 
ATOM   3940 C  CA    . GLU A 1 528 ? 125.002 97.327  51.574  1.00 87.50  ? 516 GLU A CA    1 
ATOM   3941 C  C     . GLU A 1 528 ? 124.621 96.437  52.752  1.00 86.02  ? 516 GLU A C     1 
ATOM   3942 O  O     . GLU A 1 528 ? 124.529 95.213  52.607  1.00 88.96  ? 516 GLU A O     1 
ATOM   3943 C  CB    . GLU A 1 528 ? 126.506 97.601  51.567  1.00 91.24  ? 516 GLU A CB    1 
ATOM   3944 C  CG    . GLU A 1 528 ? 127.336 96.523  50.887  1.00 94.45  ? 516 GLU A CG    1 
ATOM   3945 C  CD    . GLU A 1 528 ? 127.938 95.534  51.868  1.00 99.28  ? 516 GLU A CD    1 
ATOM   3946 O  OE1   . GLU A 1 528 ? 127.404 95.399  52.989  1.00 94.85  ? 516 GLU A OE1   1 
ATOM   3947 O  OE2   . GLU A 1 528 ? 128.949 94.889  51.517  1.00 98.60  ? 516 GLU A OE2   1 
ATOM   3948 N  N     . VAL A 1 529 ? 124.398 97.030  53.925  1.00 82.52  ? 517 VAL A N     1 
ATOM   3949 C  CA    . VAL A 1 529 ? 124.182 96.240  55.135  1.00 82.32  ? 517 VAL A CA    1 
ATOM   3950 C  C     . VAL A 1 529 ? 122.712 95.864  55.290  1.00 81.13  ? 517 VAL A C     1 
ATOM   3951 O  O     . VAL A 1 529 ? 122.378 94.698  55.527  1.00 75.95  ? 517 VAL A O     1 
ATOM   3952 C  CB    . VAL A 1 529 ? 124.706 97.005  56.366  1.00 83.60  ? 517 VAL A CB    1 
ATOM   3953 C  CG1   . VAL A 1 529 ? 123.945 96.600  57.620  1.00 82.07  ? 517 VAL A CG1   1 
ATOM   3954 C  CG2   . VAL A 1 529 ? 126.194 96.761  56.543  1.00 82.96  ? 517 VAL A CG2   1 
ATOM   3955 N  N     . ALA A 1 530 ? 121.810 96.838  55.154  1.00 83.26  ? 518 ALA A N     1 
ATOM   3956 C  CA    . ALA A 1 530 ? 120.388 96.625  55.400  1.00 80.65  ? 518 ALA A CA    1 
ATOM   3957 C  C     . ALA A 1 530 ? 119.634 96.169  54.158  1.00 84.57  ? 518 ALA A C     1 
ATOM   3958 O  O     . ALA A 1 530 ? 118.424 96.406  54.052  1.00 86.58  ? 518 ALA A O     1 
ATOM   3959 C  CB    . ALA A 1 530 ? 119.755 97.897  55.965  1.00 79.53  ? 518 ALA A CB    1 
ATOM   3960 N  N     . ALA A 1 531 ? 120.319 95.526  53.210  1.00 85.42  ? 519 ALA A N     1 
ATOM   3961 C  CA    . ALA A 1 531 ? 119.641 95.031  52.017  1.00 84.68  ? 519 ALA A CA    1 
ATOM   3962 C  C     . ALA A 1 531 ? 118.623 93.952  52.367  1.00 85.47  ? 519 ALA A C     1 
ATOM   3963 O  O     . ALA A 1 531 ? 117.529 93.910  51.791  1.00 83.79  ? 519 ALA A O     1 
ATOM   3964 C  CB    . ALA A 1 531 ? 120.664 94.500  51.015  1.00 79.70  ? 519 ALA A CB    1 
ATOM   3965 N  N     . ASP A 1 532 ? 118.963 93.074  53.308  1.00 86.87  ? 520 ASP A N     1 
ATOM   3966 C  CA    . ASP A 1 532 ? 118.087 91.977  53.699  1.00 88.33  ? 520 ASP A CA    1 
ATOM   3967 C  C     . ASP A 1 532 ? 117.060 92.374  54.751  1.00 87.01  ? 520 ASP A C     1 
ATOM   3968 O  O     . ASP A 1 532 ? 116.226 91.540  55.120  1.00 88.41  ? 520 ASP A O     1 
ATOM   3969 C  CB    . ASP A 1 532 ? 118.919 90.804  54.223  1.00 86.70  ? 520 ASP A CB    1 
ATOM   3970 C  CG    . ASP A 1 532 ? 119.853 90.235  53.174  1.00 92.89  ? 520 ASP A CG    1 
ATOM   3971 O  OD1   . ASP A 1 532 ? 119.803 90.696  52.014  1.00 95.35  ? 520 ASP A OD1   1 
ATOM   3972 O  OD2   . ASP A 1 532 ? 120.640 89.326  53.511  1.00 92.31  ? 520 ASP A OD2   1 
ATOM   3973 N  N     . ALA A 1 533 ? 117.092 93.610  55.240  1.00 82.90  ? 521 ALA A N     1 
ATOM   3974 C  CA    . ALA A 1 533 ? 116.227 94.044  56.325  1.00 79.28  ? 521 ALA A CA    1 
ATOM   3975 C  C     . ALA A 1 533 ? 115.257 95.112  55.840  1.00 79.12  ? 521 ALA A C     1 
ATOM   3976 O  O     . ALA A 1 533 ? 115.577 95.912  54.957  1.00 81.61  ? 521 ALA A O     1 
ATOM   3977 C  CB    . ALA A 1 533 ? 117.045 94.584  57.501  1.00 73.40  ? 521 ALA A CB    1 
ATOM   3978 N  N     . THR A 1 534 ? 114.062 95.109  56.426  1.00 76.71  ? 522 THR A N     1 
ATOM   3979 C  CA    . THR A 1 534 ? 113.071 96.133  56.127  1.00 78.36  ? 522 THR A CA    1 
ATOM   3980 C  C     . THR A 1 534 ? 113.517 97.476  56.689  1.00 73.36  ? 522 THR A C     1 
ATOM   3981 O  O     . THR A 1 534 ? 113.984 97.567  57.827  1.00 70.21  ? 522 THR A O     1 
ATOM   3982 C  CB    . THR A 1 534 ? 111.714 95.744  56.713  1.00 78.21  ? 522 THR A CB    1 
ATOM   3983 O  OG1   . THR A 1 534 ? 111.392 94.404  56.327  1.00 84.89  ? 522 THR A OG1   1 
ATOM   3984 C  CG2   . THR A 1 534 ? 110.629 96.678  56.214  1.00 78.47  ? 522 THR A CG2   1 
ATOM   3985 N  N     . VAL A 1 535 ? 113.376 98.526  55.886  1.00 71.85  ? 523 VAL A N     1 
ATOM   3986 C  CA    . VAL A 1 535 ? 113.797 99.867  56.270  1.00 65.99  ? 523 VAL A CA    1 
ATOM   3987 C  C     . VAL A 1 535 ? 112.633 100.826 56.071  1.00 65.65  ? 523 VAL A C     1 
ATOM   3988 O  O     . VAL A 1 535 ? 112.049 100.884 54.984  1.00 67.32  ? 523 VAL A O     1 
ATOM   3989 C  CB    . VAL A 1 535 ? 115.022 100.336 55.462  1.00 66.93  ? 523 VAL A CB    1 
ATOM   3990 C  CG1   . VAL A 1 535 ? 115.353 101.780 55.793  1.00 64.15  ? 523 VAL A CG1   1 
ATOM   3991 C  CG2   . VAL A 1 535 ? 116.216 99.439  55.741  1.00 69.13  ? 523 VAL A CG2   1 
ATOM   3992 N  N     . VAL A 1 536 ? 112.295 101.569 57.120  1.00 65.90  ? 524 VAL A N     1 
ATOM   3993 C  CA    . VAL A 1 536 ? 111.366 102.689 57.034  1.00 64.29  ? 524 VAL A CA    1 
ATOM   3994 C  C     . VAL A 1 536 ? 112.148 103.941 57.394  1.00 61.88  ? 524 VAL A C     1 
ATOM   3995 O  O     . VAL A 1 536 ? 112.670 104.054 58.509  1.00 62.11  ? 524 VAL A O     1 
ATOM   3996 C  CB    . VAL A 1 536 ? 110.151 102.512 57.956  1.00 58.39  ? 524 VAL A CB    1 
ATOM   3997 C  CG1   . VAL A 1 536 ? 109.137 103.613 57.705  1.00 57.95  ? 524 VAL A CG1   1 
ATOM   3998 C  CG2   . VAL A 1 536 ? 109.522 101.149 57.745  1.00 66.07  ? 524 VAL A CG2   1 
ATOM   3999 N  N     . ILE A 1 537 ? 112.233 104.874 56.453  1.00 61.34  ? 525 ILE A N     1 
ATOM   4000 C  CA    . ILE A 1 537 ? 113.094 106.041 56.574  1.00 60.02  ? 525 ILE A CA    1 
ATOM   4001 C  C     . ILE A 1 537 ? 112.238 107.295 56.474  1.00 62.27  ? 525 ILE A C     1 
ATOM   4002 O  O     . ILE A 1 537 ? 111.387 107.408 55.584  1.00 66.10  ? 525 ILE A O     1 
ATOM   4003 C  CB    . ILE A 1 537 ? 114.206 106.029 55.507  1.00 63.87  ? 525 ILE A CB    1 
ATOM   4004 C  CG1   . ILE A 1 537 ? 115.201 107.163 55.741  1.00 64.16  ? 525 ILE A CG1   1 
ATOM   4005 C  CG2   . ILE A 1 537 ? 113.637 106.056 54.095  1.00 65.56  ? 525 ILE A CG2   1 
ATOM   4006 C  CD1   . ILE A 1 537 ? 116.629 106.717 55.654  1.00 61.59  ? 525 ILE A CD1   1 
ATOM   4007 N  N     . VAL A 1 538 ? 112.439 108.217 57.408  1.00 61.25  ? 526 VAL A N     1 
ATOM   4008 C  CA    . VAL A 1 538 ? 111.823 109.536 57.363  1.00 62.49  ? 526 VAL A CA    1 
ATOM   4009 C  C     . VAL A 1 538 ? 112.873 110.509 56.854  1.00 69.10  ? 526 VAL A C     1 
ATOM   4010 O  O     . VAL A 1 538 ? 113.878 110.760 57.530  1.00 69.39  ? 526 VAL A O     1 
ATOM   4011 C  CB    . VAL A 1 538 ? 111.291 109.960 58.740  1.00 59.51  ? 526 VAL A CB    1 
ATOM   4012 C  CG1   . VAL A 1 538 ? 110.874 111.416 58.716  1.00 60.94  ? 526 VAL A CG1   1 
ATOM   4013 C  CG2   . VAL A 1 538 ? 110.127 109.080 59.149  1.00 57.60  ? 526 VAL A CG2   1 
ATOM   4014 N  N     . SER A 1 539 ? 112.653 111.048 55.661  1.00 74.32  ? 527 SER A N     1 
ATOM   4015 C  CA    . SER A 1 539 ? 113.648 111.878 55.005  1.00 79.07  ? 527 SER A CA    1 
ATOM   4016 C  C     . SER A 1 539 ? 112.978 113.095 54.391  1.00 87.76  ? 527 SER A C     1 
ATOM   4017 O  O     . SER A 1 539 ? 111.796 113.066 54.042  1.00 82.74  ? 527 SER A O     1 
ATOM   4018 C  CB    . SER A 1 539 ? 114.402 111.095 53.926  1.00 78.79  ? 527 SER A CB    1 
ATOM   4019 O  OG    . SER A 1 539 ? 113.497 110.384 53.100  1.00 79.22  ? 527 SER A OG    1 
ATOM   4020 N  N     . GLN A 1 540 ? 113.753 114.170 54.265  1.00 92.88  ? 528 GLN A N     1 
ATOM   4021 C  CA    . GLN A 1 540 ? 113.290 115.393 53.629  1.00 89.37  ? 528 GLN A CA    1 
ATOM   4022 C  C     . GLN A 1 540 ? 113.843 115.591 52.229  1.00 90.30  ? 528 GLN A C     1 
ATOM   4023 O  O     . GLN A 1 540 ? 113.198 116.253 51.415  1.00 95.72  ? 528 GLN A O     1 
ATOM   4024 C  CB    . GLN A 1 540 ? 113.659 116.611 54.485  1.00 85.56  ? 528 GLN A CB    1 
ATOM   4025 C  CG    . GLN A 1 540 ? 113.510 116.382 55.980  1.00 91.02  ? 528 GLN A CG    1 
ATOM   4026 C  CD    . GLN A 1 540 ? 112.066 116.184 56.402  1.00 89.91  ? 528 GLN A CD    1 
ATOM   4027 O  OE1   . GLN A 1 540 ? 111.622 115.057 56.622  1.00 84.93  ? 528 GLN A OE1   1 
ATOM   4028 N  NE2   . GLN A 1 540 ? 111.327 117.280 56.519  1.00 81.77  ? 528 GLN A NE2   1 
ATOM   4029 N  N     . ARG A 1 541 ? 115.009 115.026 51.927  1.00 89.32  ? 529 ARG A N     1 
ATOM   4030 C  CA    . ARG A 1 541 ? 115.623 115.189 50.616  1.00 93.89  ? 529 ARG A CA    1 
ATOM   4031 C  C     . ARG A 1 541 ? 115.001 114.209 49.630  1.00 94.21  ? 529 ARG A C     1 
ATOM   4032 O  O     . ARG A 1 541 ? 115.028 112.994 49.852  1.00 95.08  ? 529 ARG A O     1 
ATOM   4033 C  CB    . ARG A 1 541 ? 117.133 114.983 50.708  1.00 95.61  ? 529 ARG A CB    1 
ATOM   4034 C  CG    . ARG A 1 541 ? 117.764 115.611 51.937  1.00 97.41  ? 529 ARG A CG    1 
ATOM   4035 C  CD    . ARG A 1 541 ? 119.127 115.011 52.233  1.00 102.90 ? 529 ARG A CD    1 
ATOM   4036 N  NE    . ARG A 1 541 ? 120.107 116.031 52.585  1.00 105.89 ? 529 ARG A NE    1 
ATOM   4037 C  CZ    . ARG A 1 541 ? 121.406 115.939 52.336  1.00 104.05 ? 529 ARG A CZ    1 
ATOM   4038 N  NH1   . ARG A 1 541 ? 121.920 114.885 51.724  1.00 97.22  ? 529 ARG A NH1   1 
ATOM   4039 N  NH2   . ARG A 1 541 ? 122.210 116.930 52.711  1.00 94.19  ? 529 ARG A NH2   1 
ATOM   4040 N  N     . ILE A 1 542 ? 114.438 114.739 48.542  1.00 96.39  ? 530 ILE A N     1 
ATOM   4041 C  CA    . ILE A 1 542 ? 113.826 113.892 47.523  1.00 96.99  ? 530 ILE A CA    1 
ATOM   4042 C  C     . ILE A 1 542 ? 114.880 113.045 46.819  1.00 98.56  ? 530 ILE A C     1 
ATOM   4043 O  O     . ILE A 1 542 ? 114.599 111.918 46.392  1.00 102.81 ? 530 ILE A O     1 
ATOM   4044 C  CB    . ILE A 1 542 ? 113.017 114.757 46.533  1.00 98.48  ? 530 ILE A CB    1 
ATOM   4045 C  CG1   . ILE A 1 542 ? 111.539 114.830 46.940  1.00 95.42  ? 530 ILE A CG1   1 
ATOM   4046 C  CG2   . ILE A 1 542 ? 113.149 114.249 45.102  1.00 95.14  ? 530 ILE A CG2   1 
ATOM   4047 C  CD1   . ILE A 1 542 ? 111.288 115.136 48.400  1.00 93.86  ? 530 ILE A CD1   1 
ATOM   4048 N  N     . SER A 1 543 ? 116.109 113.553 46.707  1.00 96.65  ? 531 SER A N     1 
ATOM   4049 C  CA    . SER A 1 543 ? 117.162 112.805 46.028  1.00 101.01 ? 531 SER A CA    1 
ATOM   4050 C  C     . SER A 1 543 ? 117.443 111.472 46.711  1.00 101.29 ? 531 SER A C     1 
ATOM   4051 O  O     . SER A 1 543 ? 117.803 110.497 46.042  1.00 99.63  ? 531 SER A O     1 
ATOM   4052 C  CB    . SER A 1 543 ? 118.437 113.647 45.960  1.00 100.27 ? 531 SER A CB    1 
ATOM   4053 O  OG    . SER A 1 543 ? 119.517 112.901 45.430  1.00 101.88 ? 531 SER A OG    1 
ATOM   4054 N  N     . THR A 1 544 ? 117.283 111.406 48.032  1.00 97.54  ? 532 THR A N     1 
ATOM   4055 C  CA    . THR A 1 544 ? 117.553 110.176 48.765  1.00 93.48  ? 532 THR A CA    1 
ATOM   4056 C  C     . THR A 1 544 ? 116.371 109.216 48.785  1.00 92.37  ? 532 THR A C     1 
ATOM   4057 O  O     . THR A 1 544 ? 116.554 108.047 49.141  1.00 94.70  ? 532 THR A O     1 
ATOM   4058 C  CB    . THR A 1 544 ? 117.966 110.498 50.202  1.00 91.71  ? 532 THR A CB    1 
ATOM   4059 O  OG1   . THR A 1 544 ? 116.800 110.788 50.981  1.00 89.90  ? 532 THR A OG1   1 
ATOM   4060 C  CG2   . THR A 1 544 ? 118.895 111.700 50.227  1.00 93.66  ? 532 THR A CG2   1 
ATOM   4061 N  N     . VAL A 1 545 ? 115.168 109.668 48.414  1.00 92.15  ? 533 VAL A N     1 
ATOM   4062 C  CA    . VAL A 1 545 ? 114.005 108.788 48.397  1.00 92.31  ? 533 VAL A CA    1 
ATOM   4063 C  C     . VAL A 1 545 ? 113.812 108.107 47.052  1.00 96.28  ? 533 VAL A C     1 
ATOM   4064 O  O     . VAL A 1 545 ? 112.908 107.273 46.914  1.00 99.98  ? 533 VAL A O     1 
ATOM   4065 C  CB    . VAL A 1 545 ? 112.717 109.548 48.780  1.00 91.61  ? 533 VAL A CB    1 
ATOM   4066 C  CG1   . VAL A 1 545 ? 112.975 110.470 49.953  1.00 89.26  ? 533 VAL A CG1   1 
ATOM   4067 C  CG2   . VAL A 1 545 ? 112.173 110.322 47.595  1.00 96.77  ? 533 VAL A CG2   1 
ATOM   4068 N  N     . ILE A 1 546 ? 114.631 108.439 46.051  1.00 94.40  ? 534 ILE A N     1 
ATOM   4069 C  CA    . ILE A 1 546 ? 114.552 107.749 44.767  1.00 98.05  ? 534 ILE A CA    1 
ATOM   4070 C  C     . ILE A 1 546 ? 114.895 106.275 44.935  1.00 102.50 ? 534 ILE A C     1 
ATOM   4071 O  O     . ILE A 1 546 ? 114.233 105.398 44.365  1.00 102.93 ? 534 ILE A O     1 
ATOM   4072 C  CB    . ILE A 1 546 ? 115.469 108.432 43.736  1.00 99.75  ? 534 ILE A CB    1 
ATOM   4073 C  CG1   . ILE A 1 546 ? 115.089 109.905 43.582  1.00 101.67 ? 534 ILE A CG1   1 
ATOM   4074 C  CG2   . ILE A 1 546 ? 115.394 107.716 42.397  1.00 96.79  ? 534 ILE A CG2   1 
ATOM   4075 C  CD1   . ILE A 1 546 ? 115.904 110.637 42.543  1.00 100.67 ? 534 ILE A CD1   1 
ATOM   4076 N  N     . GLU A 1 547 ? 115.932 105.977 45.721  1.00 101.06 ? 535 GLU A N     1 
ATOM   4077 C  CA    . GLU A 1 547 ? 116.313 104.592 45.968  1.00 99.62  ? 535 GLU A CA    1 
ATOM   4078 C  C     . GLU A 1 547 ? 115.250 103.823 46.741  1.00 98.55  ? 535 GLU A C     1 
ATOM   4079 O  O     . GLU A 1 547 ? 115.258 102.588 46.714  1.00 103.32 ? 535 GLU A O     1 
ATOM   4080 C  CB    . GLU A 1 547 ? 117.641 104.537 46.726  1.00 104.69 ? 535 GLU A CB    1 
ATOM   4081 C  CG    . GLU A 1 547 ? 118.859 104.873 45.881  1.00 107.39 ? 535 GLU A CG    1 
ATOM   4082 C  CD    . GLU A 1 547 ? 119.066 106.366 45.726  1.00 110.51 ? 535 GLU A CD    1 
ATOM   4083 O  OE1   . GLU A 1 547 ? 118.437 107.134 46.485  1.00 108.55 ? 535 GLU A OE1   1 
ATOM   4084 O  OE2   . GLU A 1 547 ? 119.856 106.771 44.848  1.00 111.80 ? 535 GLU A OE2   1 
ATOM   4085 N  N     . ALA A 1 548 ? 114.345 104.516 47.428  1.00 93.17  ? 536 ALA A N     1 
ATOM   4086 C  CA    . ALA A 1 548 ? 113.305 103.839 48.187  1.00 90.77  ? 536 ALA A CA    1 
ATOM   4087 C  C     . ALA A 1 548 ? 112.336 103.123 47.255  1.00 94.13  ? 536 ALA A C     1 
ATOM   4088 O  O     . ALA A 1 548 ? 111.953 103.647 46.205  1.00 91.39  ? 536 ALA A O     1 
ATOM   4089 C  CB    . ALA A 1 548 ? 112.550 104.836 49.064  1.00 88.51  ? 536 ALA A CB    1 
ATOM   4090 N  N     . ASP A 1 549 ? 111.940 101.912 47.648  1.00 95.30  ? 537 ASP A N     1 
ATOM   4091 C  CA    . ASP A 1 549 ? 111.022 101.128 46.829  1.00 93.16  ? 537 ASP A CA    1 
ATOM   4092 C  C     . ASP A 1 549 ? 109.617 101.714 46.835  1.00 91.48  ? 537 ASP A C     1 
ATOM   4093 O  O     . ASP A 1 549 ? 108.910 101.633 45.825  1.00 93.10  ? 537 ASP A O     1 
ATOM   4094 C  CB    . ASP A 1 549 ? 111.002 99.680  47.315  1.00 91.05  ? 537 ASP A CB    1 
ATOM   4095 C  CG    . ASP A 1 549 ? 112.388 99.068  47.373  1.00 91.92  ? 537 ASP A CG    1 
ATOM   4096 O  OD1   . ASP A 1 549 ? 113.003 98.886  46.302  1.00 94.02  ? 537 ASP A OD1   1 
ATOM   4097 O  OD2   . ASP A 1 549 ? 112.867 98.774  48.487  1.00 87.82  ? 537 ASP A OD2   1 
ATOM   4098 N  N     . GLN A 1 550 ? 109.195 102.300 47.952  1.00 88.37  ? 538 GLN A N     1 
ATOM   4099 C  CA    . GLN A 1 550 ? 107.890 102.932 48.063  1.00 85.02  ? 538 GLN A CA    1 
ATOM   4100 C  C     . GLN A 1 550 ? 108.037 104.239 48.824  1.00 85.08  ? 538 GLN A C     1 
ATOM   4101 O  O     . GLN A 1 550 ? 108.789 104.315 49.798  1.00 86.47  ? 538 GLN A O     1 
ATOM   4102 C  CB    . GLN A 1 550 ? 106.882 102.014 48.769  1.00 84.38  ? 538 GLN A CB    1 
ATOM   4103 C  CG    . GLN A 1 550 ? 105.540 102.663 49.060  1.00 90.07  ? 538 GLN A CG    1 
ATOM   4104 C  CD    . GLN A 1 550 ? 104.731 101.891 50.081  1.00 94.39  ? 538 GLN A CD    1 
ATOM   4105 O  OE1   . GLN A 1 550 ? 105.058 101.877 51.267  1.00 93.69  ? 538 GLN A OE1   1 
ATOM   4106 N  NE2   . GLN A 1 550 ? 103.665 101.246 49.625  1.00 89.09  ? 538 GLN A NE2   1 
ATOM   4107 N  N     . VAL A 1 551 ? 107.327 105.268 48.369  1.00 87.37  ? 539 VAL A N     1 
ATOM   4108 C  CA    . VAL A 1 551 ? 107.348 106.584 48.996  1.00 85.06  ? 539 VAL A CA    1 
ATOM   4109 C  C     . VAL A 1 551 ? 105.938 106.919 49.457  1.00 84.44  ? 539 VAL A C     1 
ATOM   4110 O  O     . VAL A 1 551 ? 104.986 106.836 48.673  1.00 87.74  ? 539 VAL A O     1 
ATOM   4111 C  CB    . VAL A 1 551 ? 107.882 107.666 48.040  1.00 83.48  ? 539 VAL A CB    1 
ATOM   4112 C  CG1   . VAL A 1 551 ? 108.038 108.986 48.773  1.00 80.96  ? 539 VAL A CG1   1 
ATOM   4113 C  CG2   . VAL A 1 551 ? 109.203 107.232 47.432  1.00 85.20  ? 539 VAL A CG2   1 
ATOM   4114 N  N     . VAL A 1 552 ? 105.807 107.301 50.724  1.00 81.48  ? 540 VAL A N     1 
ATOM   4115 C  CA    . VAL A 1 552 ? 104.528 107.659 51.325  1.00 83.81  ? 540 VAL A CA    1 
ATOM   4116 C  C     . VAL A 1 552 ? 104.551 109.146 51.636  1.00 84.33  ? 540 VAL A C     1 
ATOM   4117 O  O     . VAL A 1 552 ? 105.473 109.633 52.301  1.00 83.87  ? 540 VAL A O     1 
ATOM   4118 C  CB    . VAL A 1 552 ? 104.251 106.836 52.595  1.00 85.80  ? 540 VAL A CB    1 
ATOM   4119 C  CG1   . VAL A 1 552 ? 102.936 107.261 53.225  1.00 81.61  ? 540 VAL A CG1   1 
ATOM   4120 C  CG2   . VAL A 1 552 ? 104.240 105.352 52.274  1.00 87.73  ? 540 VAL A CG2   1 
ATOM   4121 N  N     . VAL A 1 553 ? 103.541 109.866 51.157  1.00 84.76  ? 541 VAL A N     1 
ATOM   4122 C  CA    . VAL A 1 553 ? 103.415 111.302 51.375  1.00 82.04  ? 541 VAL A CA    1 
ATOM   4123 C  C     . VAL A 1 553 ? 102.209 111.535 52.270  1.00 81.94  ? 541 VAL A C     1 
ATOM   4124 O  O     . VAL A 1 553 ? 101.095 111.107 51.944  1.00 86.60  ? 541 VAL A O     1 
ATOM   4125 C  CB    . VAL A 1 553 ? 103.272 112.070 50.052  1.00 83.93  ? 541 VAL A CB    1 
ATOM   4126 C  CG1   . VAL A 1 553 ? 103.580 113.544 50.259  1.00 89.18  ? 541 VAL A CG1   1 
ATOM   4127 C  CG2   . VAL A 1 553 ? 104.179 111.476 48.994  1.00 85.64  ? 541 VAL A CG2   1 
ATOM   4128 N  N     . ILE A 1 554 ? 102.425 112.213 53.392  1.00 75.95  ? 542 ILE A N     1 
ATOM   4129 C  CA    . ILE A 1 554 ? 101.359 112.535 54.331  1.00 76.75  ? 542 ILE A CA    1 
ATOM   4130 C  C     . ILE A 1 554 ? 101.307 114.046 54.502  1.00 81.17  ? 542 ILE A C     1 
ATOM   4131 O  O     . ILE A 1 554 ? 102.345 114.705 54.634  1.00 82.51  ? 542 ILE A O     1 
ATOM   4132 C  CB    . ILE A 1 554 ? 101.547 111.827 55.690  1.00 71.84  ? 542 ILE A CB    1 
ATOM   4133 C  CG1   . ILE A 1 554 ? 102.866 112.226 56.348  1.00 70.77  ? 542 ILE A CG1   1 
ATOM   4134 C  CG2   . ILE A 1 554 ? 101.498 110.319 55.516  1.00 74.77  ? 542 ILE A CG2   1 
ATOM   4135 C  CD1   . ILE A 1 554 ? 102.925 111.894 57.817  1.00 63.37  ? 542 ILE A CD1   1 
ATOM   4136 N  N     . ASP A 1 555 ? 100.098 114.596 54.465  1.00 86.38  ? 543 ASP A N     1 
ATOM   4137 C  CA    . ASP A 1 555 ? 99.889  116.022 54.654  1.00 86.32  ? 543 ASP A CA    1 
ATOM   4138 C  C     . ASP A 1 555 ? 98.640  116.227 55.493  1.00 88.26  ? 543 ASP A C     1 
ATOM   4139 O  O     . ASP A 1 555 ? 97.632  115.545 55.287  1.00 90.97  ? 543 ASP A O     1 
ATOM   4140 C  CB    . ASP A 1 555 ? 99.761  116.753 53.310  1.00 90.54  ? 543 ASP A CB    1 
ATOM   4141 C  CG    . ASP A 1 555 ? 99.056  118.089 53.436  1.00 96.77  ? 543 ASP A CG    1 
ATOM   4142 O  OD1   . ASP A 1 555 ? 99.734  119.094 53.739  1.00 96.34  ? 543 ASP A OD1   1 
ATOM   4143 O  OD2   . ASP A 1 555 ? 97.826  118.137 53.227  1.00 97.08  ? 543 ASP A OD2   1 
ATOM   4144 N  N     . ASP A 1 556 ? 98.730  117.142 56.461  1.00 84.81  ? 544 ASP A N     1 
ATOM   4145 C  CA    . ASP A 1 556 ? 97.623  117.509 57.341  1.00 89.47  ? 544 ASP A CA    1 
ATOM   4146 C  C     . ASP A 1 556 ? 97.284  116.356 58.284  1.00 90.06  ? 544 ASP A C     1 
ATOM   4147 O  O     . ASP A 1 556 ? 96.436  116.493 59.171  1.00 93.68  ? 544 ASP A O     1 
ATOM   4148 C  CB    . ASP A 1 556 ? 96.407  117.948 56.508  1.00 93.56  ? 544 ASP A CB    1 
ATOM   4149 C  CG    . ASP A 1 556 ? 95.169  118.206 57.347  1.00 99.57  ? 544 ASP A CG    1 
ATOM   4150 O  OD1   . ASP A 1 556 ? 95.268  118.957 58.341  1.00 98.39  ? 544 ASP A OD1   1 
ATOM   4151 O  OD2   . ASP A 1 556 ? 94.097  117.661 57.011  1.00 98.83  ? 544 ASP A OD2   1 
ATOM   4152 N  N     . GLY A 1 557 ? 97.971  115.226 58.130  1.00 82.84  ? 545 GLY A N     1 
ATOM   4153 C  CA    . GLY A 1 557 ? 97.760  114.095 59.007  1.00 77.88  ? 545 GLY A CA    1 
ATOM   4154 C  C     . GLY A 1 557 ? 97.160  112.883 58.326  1.00 83.00  ? 545 GLY A C     1 
ATOM   4155 O  O     . GLY A 1 557 ? 96.762  111.926 58.994  1.00 83.69  ? 545 GLY A O     1 
ATOM   4156 N  N     . ARG A 1 558 ? 97.085  112.909 56.999  1.00 87.97  ? 546 ARG A N     1 
ATOM   4157 C  CA    . ARG A 1 558 ? 96.557  111.785 56.242  1.00 87.00  ? 546 ARG A CA    1 
ATOM   4158 C  C     . ARG A 1 558 ? 97.395  111.585 54.989  1.00 86.44  ? 546 ARG A C     1 
ATOM   4159 O  O     . ARG A 1 558 ? 98.062  112.503 54.508  1.00 85.92  ? 546 ARG A O     1 
ATOM   4160 C  CB    . ARG A 1 558 ? 95.082  111.989 55.876  1.00 87.31  ? 546 ARG A CB    1 
ATOM   4161 C  CG    . ARG A 1 558 ? 94.769  113.335 55.256  1.00 91.52  ? 546 ARG A CG    1 
ATOM   4162 C  CD    . ARG A 1 558 ? 93.418  113.843 55.727  1.00 97.08  ? 546 ARG A CD    1 
ATOM   4163 N  NE    . ARG A 1 558 ? 92.470  112.754 55.928  1.00 101.00 ? 546 ARG A NE    1 
ATOM   4164 C  CZ    . ARG A 1 558 ? 91.283  112.890 56.503  1.00 99.13  ? 546 ARG A CZ    1 
ATOM   4165 N  NH1   . ARG A 1 558 ? 90.861  114.061 56.949  1.00 94.11  ? 546 ARG A NH1   1 
ATOM   4166 N  NH2   . ARG A 1 558 ? 90.500  111.823 56.634  1.00 96.09  ? 546 ARG A NH2   1 
ATOM   4167 N  N     . VAL A 1 559 ? 97.354  110.360 54.467  1.00 87.16  ? 547 VAL A N     1 
ATOM   4168 C  CA    . VAL A 1 559 ? 98.144  110.016 53.292  1.00 85.58  ? 547 VAL A CA    1 
ATOM   4169 C  C     . VAL A 1 559 ? 97.552  110.699 52.068  1.00 88.31  ? 547 VAL A C     1 
ATOM   4170 O  O     . VAL A 1 559 ? 96.351  110.586 51.792  1.00 88.47  ? 547 VAL A O     1 
ATOM   4171 C  CB    . VAL A 1 559 ? 98.199  108.493 53.110  1.00 81.39  ? 547 VAL A CB    1 
ATOM   4172 C  CG1   . VAL A 1 559 ? 98.829  108.140 51.774  1.00 78.10  ? 547 VAL A CG1   1 
ATOM   4173 C  CG2   . VAL A 1 559 ? 98.964  107.850 54.253  1.00 80.94  ? 547 VAL A CG2   1 
ATOM   4174 N  N     . VAL A 1 560 ? 98.396  111.414 51.326  1.00 86.45  ? 548 VAL A N     1 
ATOM   4175 C  CA    . VAL A 1 560 ? 97.978  112.118 50.120  1.00 86.08  ? 548 VAL A CA    1 
ATOM   4176 C  C     . VAL A 1 560 ? 98.514  111.471 48.857  1.00 91.55  ? 548 VAL A C     1 
ATOM   4177 O  O     . VAL A 1 560 ? 98.176  111.921 47.753  1.00 95.54  ? 548 VAL A O     1 
ATOM   4178 C  CB    . VAL A 1 560 ? 98.382  113.603 50.171  1.00 86.29  ? 548 VAL A CB    1 
ATOM   4179 C  CG1   . VAL A 1 560 ? 97.758  114.281 51.379  1.00 84.04  ? 548 VAL A CG1   1 
ATOM   4180 C  CG2   . VAL A 1 560 ? 99.893  113.740 50.199  1.00 87.52  ? 548 VAL A CG2   1 
ATOM   4181 N  N     . GLY A 1 561 ? 99.335  110.432 48.977  1.00 90.19  ? 549 GLY A N     1 
ATOM   4182 C  CA    . GLY A 1 561 ? 99.885  109.770 47.812  1.00 94.62  ? 549 GLY A CA    1 
ATOM   4183 C  C     . GLY A 1 561 ? 100.816 108.626 48.154  1.00 96.57  ? 549 GLY A C     1 
ATOM   4184 O  O     . GLY A 1 561 ? 101.627 108.730 49.079  1.00 96.96  ? 549 GLY A O     1 
ATOM   4185 N  N     . ILE A 1 562 ? 100.706 107.525 47.416  1.00 95.53  ? 550 ILE A N     1 
ATOM   4186 C  CA    . ILE A 1 562 ? 101.542 106.348 47.612  1.00 91.75  ? 550 ILE A CA    1 
ATOM   4187 C  C     . ILE A 1 562 ? 102.065 105.905 46.254  1.00 90.11  ? 550 ILE A C     1 
ATOM   4188 O  O     . ILE A 1 562 ? 101.287 105.750 45.306  1.00 86.15  ? 550 ILE A O     1 
ATOM   4189 C  CB    . ILE A 1 562 ? 100.768 105.205 48.295  1.00 89.63  ? 550 ILE A CB    1 
ATOM   4190 C  CG1   . ILE A 1 562 ? 100.515 105.537 49.765  1.00 91.11  ? 550 ILE A CG1   1 
ATOM   4191 C  CG2   . ILE A 1 562 ? 101.531 103.898 48.180  1.00 90.76  ? 550 ILE A CG2   1 
ATOM   4192 C  CD1   . ILE A 1 562 ? 99.570  104.579 50.450  1.00 91.41  ? 550 ILE A CD1   1 
ATOM   4193 N  N     . GLY A 1 563 ? 103.371 105.705 46.160  1.00 92.06  ? 551 GLY A N     1 
ATOM   4194 C  CA    . GLY A 1 563 ? 103.970 105.265 44.918  1.00 94.12  ? 551 GLY A CA    1 
ATOM   4195 C  C     . GLY A 1 563 ? 105.451 105.585 44.896  1.00 96.52  ? 551 GLY A C     1 
ATOM   4196 O  O     . GLY A 1 563 ? 106.028 106.024 45.890  1.00 97.94  ? 551 GLY A O     1 
ATOM   4197 N  N     . THR A 1 564 ? 106.050 105.352 43.733  1.00 101.68 ? 552 THR A N     1 
ATOM   4198 C  CA    . THR A 1 564 ? 107.464 105.622 43.544  1.00 105.64 ? 552 THR A CA    1 
ATOM   4199 C  C     . THR A 1 564 ? 107.692 107.106 43.265  1.00 102.14 ? 552 THR A C     1 
ATOM   4200 O  O     . THR A 1 564 ? 106.754 107.898 43.146  1.00 100.16 ? 552 THR A O     1 
ATOM   4201 C  CB    . THR A 1 564 ? 108.028 104.772 42.408  1.00 107.92 ? 552 THR A CB    1 
ATOM   4202 O  OG1   . THR A 1 564 ? 107.218 104.934 41.237  1.00 110.66 ? 552 THR A OG1   1 
ATOM   4203 C  CG2   . THR A 1 564 ? 108.052 103.303 42.805  1.00 103.02 ? 552 THR A CG2   1 
ATOM   4204 N  N     . HIS A 1 565 ? 108.970 107.478 43.168  1.00 100.73 ? 553 HIS A N     1 
ATOM   4205 C  CA    . HIS A 1 565 ? 109.328 108.877 42.954  1.00 102.75 ? 553 HIS A CA    1 
ATOM   4206 C  C     . HIS A 1 565 ? 108.789 109.389 41.623  1.00 105.74 ? 553 HIS A C     1 
ATOM   4207 O  O     . HIS A 1 565 ? 108.188 110.468 41.557  1.00 105.87 ? 553 HIS A O     1 
ATOM   4208 C  CB    . HIS A 1 565 ? 110.847 109.033 43.025  1.00 101.31 ? 553 HIS A CB    1 
ATOM   4209 C  CG    . HIS A 1 565 ? 111.359 110.297 42.410  1.00 104.24 ? 553 HIS A CG    1 
ATOM   4210 N  ND1   . HIS A 1 565 ? 111.123 111.540 42.956  1.00 105.74 ? 553 HIS A ND1   1 
ATOM   4211 C  CD2   . HIS A 1 565 ? 112.102 110.510 41.299  1.00 104.40 ? 553 HIS A CD2   1 
ATOM   4212 C  CE1   . HIS A 1 565 ? 111.695 112.465 42.206  1.00 105.53 ? 553 HIS A CE1   1 
ATOM   4213 N  NE2   . HIS A 1 565 ? 112.296 111.866 41.194  1.00 104.58 ? 553 HIS A NE2   1 
ATOM   4214 N  N     . ASP A 1 566 ? 108.988 108.619 40.550  1.00 107.16 ? 554 ASP A N     1 
ATOM   4215 C  CA    . ASP A 1 566 ? 108.512 109.040 39.236  1.00 106.83 ? 554 ASP A CA    1 
ATOM   4216 C  C     . ASP A 1 566 ? 106.990 109.100 39.190  1.00 107.26 ? 554 ASP A C     1 
ATOM   4217 O  O     . ASP A 1 566 ? 106.415 110.022 38.600  1.00 107.75 ? 554 ASP A O     1 
ATOM   4218 C  CB    . ASP A 1 566 ? 109.048 108.098 38.159  1.00 107.07 ? 554 ASP A CB    1 
ATOM   4219 C  CG    . ASP A 1 566 ? 110.488 107.696 38.405  1.00 108.78 ? 554 ASP A CG    1 
ATOM   4220 O  OD1   . ASP A 1 566 ? 110.714 106.686 39.104  1.00 108.97 ? 554 ASP A OD1   1 
ATOM   4221 O  OD2   . ASP A 1 566 ? 111.394 108.390 37.899  1.00 108.85 ? 554 ASP A OD2   1 
ATOM   4222 N  N     . THR A 1 567 ? 106.323 108.118 39.797  1.00 106.11 ? 555 THR A N     1 
ATOM   4223 C  CA    . THR A 1 567 ? 104.864 108.120 39.837  1.00 107.95 ? 555 THR A CA    1 
ATOM   4224 C  C     . THR A 1 567 ? 104.334 109.301 40.643  1.00 108.05 ? 555 THR A C     1 
ATOM   4225 O  O     . THR A 1 567 ? 103.366 109.959 40.238  1.00 107.88 ? 555 THR A O     1 
ATOM   4226 C  CB    . THR A 1 567 ? 104.367 106.799 40.425  1.00 107.88 ? 555 THR A CB    1 
ATOM   4227 O  OG1   . THR A 1 567 ? 104.952 105.706 39.707  1.00 107.24 ? 555 THR A OG1   1 
ATOM   4228 C  CG2   . THR A 1 567 ? 102.858 106.701 40.333  1.00 105.75 ? 555 THR A CG2   1 
ATOM   4229 N  N     . LEU A 1 568 ? 104.965 109.592 41.782  1.00 106.74 ? 556 LEU A N     1 
ATOM   4230 C  CA    . LEU A 1 568 ? 104.467 110.633 42.671  1.00 104.06 ? 556 LEU A CA    1 
ATOM   4231 C  C     . LEU A 1 568 ? 104.748 112.033 42.141  1.00 106.81 ? 556 LEU A C     1 
ATOM   4232 O  O     . LEU A 1 568 ? 103.941 112.942 42.365  1.00 107.46 ? 556 LEU A O     1 
ATOM   4233 C  CB    . LEU A 1 568 ? 105.071 110.461 44.063  1.00 101.17 ? 556 LEU A CB    1 
ATOM   4234 C  CG    . LEU A 1 568 ? 104.398 109.388 44.920  1.00 98.15  ? 556 LEU A CG    1 
ATOM   4235 C  CD1   . LEU A 1 568 ? 105.073 109.280 46.272  1.00 95.89  ? 556 LEU A CD1   1 
ATOM   4236 C  CD2   . LEU A 1 568 ? 102.917 109.682 45.078  1.00 95.35  ? 556 LEU A CD2   1 
ATOM   4237 N  N     . LEU A 1 569 ? 105.867 112.235 41.440  1.00 108.06 ? 557 LEU A N     1 
ATOM   4238 C  CA    . LEU A 1 569 ? 106.115 113.550 40.859  1.00 108.48 ? 557 LEU A CA    1 
ATOM   4239 C  C     . LEU A 1 569 ? 105.148 113.874 39.729  1.00 109.56 ? 557 LEU A C     1 
ATOM   4240 O  O     . LEU A 1 569 ? 105.111 115.024 39.279  1.00 104.20 ? 557 LEU A O     1 
ATOM   4241 C  CB    . LEU A 1 569 ? 107.562 113.663 40.364  1.00 107.50 ? 557 LEU A CB    1 
ATOM   4242 C  CG    . LEU A 1 569 ? 108.072 112.816 39.194  1.00 110.54 ? 557 LEU A CG    1 
ATOM   4243 C  CD1   . LEU A 1 569 ? 107.854 113.510 37.856  1.00 107.26 ? 557 LEU A CD1   1 
ATOM   4244 C  CD2   . LEU A 1 569 ? 109.547 112.506 39.385  1.00 108.74 ? 557 LEU A CD2   1 
ATOM   4245 N  N     . ALA A 1 570 ? 104.375 112.893 39.259  1.00 113.48 ? 558 ALA A N     1 
ATOM   4246 C  CA    . ALA A 1 570 ? 103.376 113.116 38.229  1.00 109.64 ? 558 ALA A CA    1 
ATOM   4247 C  C     . ALA A 1 570 ? 101.944 113.057 38.738  1.00 107.96 ? 558 ALA A C     1 
ATOM   4248 O  O     . ALA A 1 570 ? 101.066 113.664 38.118  1.00 107.97 ? 558 ALA A O     1 
ATOM   4249 C  CB    . ALA A 1 570 ? 103.539 112.092 37.096  1.00 101.33 ? 558 ALA A CB    1 
ATOM   4250 N  N     . ASP A 1 571 ? 101.679 112.347 39.839  1.00 108.41 ? 559 ASP A N     1 
ATOM   4251 C  CA    . ASP A 1 571 ? 100.318 112.238 40.349  1.00 109.21 ? 559 ASP A CA    1 
ATOM   4252 C  C     . ASP A 1 571 ? 100.085 112.905 41.698  1.00 109.78 ? 559 ASP A C     1 
ATOM   4253 O  O     . ASP A 1 571 ? 98.925  113.123 42.059  1.00 103.91 ? 559 ASP A O     1 
ATOM   4254 C  CB    . ASP A 1 571 ? 99.898  110.764 40.452  1.00 109.86 ? 559 ASP A CB    1 
ATOM   4255 C  CG    . ASP A 1 571 ? 100.395 109.933 39.289  1.00 112.54 ? 559 ASP A CG    1 
ATOM   4256 O  OD1   . ASP A 1 571 ? 100.658 108.731 39.488  1.00 112.85 ? 559 ASP A OD1   1 
ATOM   4257 O  OD2   . ASP A 1 571 ? 100.519 110.478 38.173  1.00 115.03 ? 559 ASP A OD2   1 
ATOM   4258 N  N     . CYS A 1 572 ? 101.135 113.233 42.449  1.00 110.21 ? 560 CYS A N     1 
ATOM   4259 C  CA    . CYS A 1 572 ? 100.967 113.848 43.761  1.00 108.17 ? 560 CYS A CA    1 
ATOM   4260 C  C     . CYS A 1 572 ? 101.347 115.318 43.701  1.00 109.68 ? 560 CYS A C     1 
ATOM   4261 O  O     . CYS A 1 572 ? 102.526 115.637 43.487  1.00 108.39 ? 560 CYS A O     1 
ATOM   4262 C  CB    . CYS A 1 572 ? 101.807 113.125 44.811  1.00 108.12 ? 560 CYS A CB    1 
ATOM   4263 S  SG    . CYS A 1 572 ? 101.638 113.791 46.485  1.00 104.69 ? 560 CYS A SG    1 
ATOM   4264 N  N     . PRO A 1 573 ? 100.395 116.241 43.870  1.00 115.19 ? 561 PRO A N     1 
ATOM   4265 C  CA    . PRO A 1 573 ? 100.758 117.669 43.872  1.00 112.69 ? 561 PRO A CA    1 
ATOM   4266 C  C     . PRO A 1 573 ? 101.722 118.047 44.982  1.00 109.74 ? 561 PRO A C     1 
ATOM   4267 O  O     . PRO A 1 573 ? 102.598 118.895 44.773  1.00 106.70 ? 561 PRO A O     1 
ATOM   4268 C  CB    . PRO A 1 573 ? 99.402  118.371 44.028  1.00 113.85 ? 561 PRO A CB    1 
ATOM   4269 C  CG    . PRO A 1 573 ? 98.520  117.354 44.675  1.00 115.57 ? 561 PRO A CG    1 
ATOM   4270 C  CD    . PRO A 1 573 ? 98.961  116.030 44.127  1.00 116.26 ? 561 PRO A CD    1 
ATOM   4271 N  N     . ILE A 1 574 ? 101.589 117.436 46.162  1.00 110.12 ? 562 ILE A N     1 
ATOM   4272 C  CA    . ILE A 1 574 ? 102.482 117.760 47.270  1.00 110.04 ? 562 ILE A CA    1 
ATOM   4273 C  C     . ILE A 1 574 ? 103.892 117.257 46.988  1.00 105.85 ? 562 ILE A C     1 
ATOM   4274 O  O     . ILE A 1 574 ? 104.881 117.961 47.234  1.00 103.40 ? 562 ILE A O     1 
ATOM   4275 C  CB    . ILE A 1 574 ? 101.925 117.186 48.585  1.00 107.01 ? 562 ILE A CB    1 
ATOM   4276 C  CG1   . ILE A 1 574 ? 100.546 117.782 48.883  1.00 102.89 ? 562 ILE A CG1   1 
ATOM   4277 C  CG2   . ILE A 1 574 ? 102.897 117.434 49.733  1.00 98.95  ? 562 ILE A CG2   1 
ATOM   4278 C  CD1   . ILE A 1 574 ? 100.571 118.976 49.813  1.00 98.68  ? 562 ILE A CD1   1 
ATOM   4279 N  N     . TYR A 1 575 ? 104.011 116.032 46.470  1.00 102.91 ? 563 TYR A N     1 
ATOM   4280 C  CA    . TYR A 1 575 ? 105.323 115.510 46.104  1.00 102.11 ? 563 TYR A CA    1 
ATOM   4281 C  C     . TYR A 1 575 ? 105.944 116.327 44.979  1.00 105.34 ? 563 TYR A C     1 
ATOM   4282 O  O     . TYR A 1 575 ? 107.157 116.568 44.972  1.00 108.46 ? 563 TYR A O     1 
ATOM   4283 C  CB    . TYR A 1 575 ? 105.211 114.041 45.703  1.00 101.15 ? 563 TYR A CB    1 
ATOM   4284 C  CG    . TYR A 1 575 ? 106.542 113.343 45.578  1.00 98.73  ? 563 TYR A CG    1 
ATOM   4285 C  CD1   . TYR A 1 575 ? 107.161 112.782 46.686  1.00 96.36  ? 563 TYR A CD1   1 
ATOM   4286 C  CD2   . TYR A 1 575 ? 107.183 113.249 44.351  1.00 99.59  ? 563 TYR A CD2   1 
ATOM   4287 C  CE1   . TYR A 1 575 ? 108.379 112.144 46.575  1.00 97.96  ? 563 TYR A CE1   1 
ATOM   4288 C  CE2   . TYR A 1 575 ? 108.400 112.614 44.231  1.00 103.30 ? 563 TYR A CE2   1 
ATOM   4289 C  CZ    . TYR A 1 575 ? 108.994 112.063 45.345  1.00 103.10 ? 563 TYR A CZ    1 
ATOM   4290 O  OH    . TYR A 1 575 ? 110.208 111.429 45.227  1.00 102.30 ? 563 TYR A OH    1 
ATOM   4291 N  N     . ALA A 1 576 ? 105.127 116.752 44.013  1.00 107.44 ? 564 ALA A N     1 
ATOM   4292 C  CA    . ALA A 1 576 ? 105.630 117.607 42.944  1.00 105.79 ? 564 ALA A CA    1 
ATOM   4293 C  C     . ALA A 1 576 ? 106.134 118.934 43.495  1.00 104.34 ? 564 ALA A C     1 
ATOM   4294 O  O     . ALA A 1 576 ? 107.172 119.440 43.059  1.00 100.78 ? 564 ALA A O     1 
ATOM   4295 C  CB    . ALA A 1 576 ? 104.541 117.836 41.898  1.00 103.03 ? 564 ALA A CB    1 
ATOM   4296 N  N     . GLU A 1 577 ? 105.409 119.513 44.455  1.00 104.46 ? 565 GLU A N     1 
ATOM   4297 C  CA    . GLU A 1 577 ? 105.862 120.753 45.077  1.00 105.08 ? 565 GLU A CA    1 
ATOM   4298 C  C     . GLU A 1 577 ? 107.173 120.549 45.827  1.00 105.40 ? 565 GLU A C     1 
ATOM   4299 O  O     . GLU A 1 577 ? 108.069 121.398 45.765  1.00 106.33 ? 565 GLU A O     1 
ATOM   4300 C  CB    . GLU A 1 577 ? 104.785 121.294 46.017  1.00 105.40 ? 565 GLU A CB    1 
ATOM   4301 C  CG    . GLU A 1 577 ? 105.064 122.695 46.532  1.00 104.67 ? 565 GLU A CG    1 
ATOM   4302 C  CD    . GLU A 1 577 ? 103.851 123.329 47.180  1.00 109.84 ? 565 GLU A CD    1 
ATOM   4303 O  OE1   . GLU A 1 577 ? 103.436 122.857 48.259  1.00 109.97 ? 565 GLU A OE1   1 
ATOM   4304 O  OE2   . GLU A 1 577 ? 103.312 124.300 46.610  1.00 113.89 ? 565 GLU A OE2   1 
ATOM   4305 N  N     . PHE A 1 578 ? 107.300 119.430 46.543  1.00 102.95 ? 566 PHE A N     1 
ATOM   4306 C  CA    . PHE A 1 578 ? 108.547 119.136 47.245  1.00 98.34  ? 566 PHE A CA    1 
ATOM   4307 C  C     . PHE A 1 578 ? 109.711 119.001 46.270  1.00 100.75 ? 566 PHE A C     1 
ATOM   4308 O  O     . PHE A 1 578 ? 110.799 119.548 46.503  1.00 100.09 ? 566 PHE A O     1 
ATOM   4309 C  CB    . PHE A 1 578 ? 108.394 117.858 48.071  1.00 95.35  ? 566 PHE A CB    1 
ATOM   4310 C  CG    . PHE A 1 578 ? 108.172 118.103 49.535  1.00 92.79  ? 566 PHE A CG    1 
ATOM   4311 C  CD1   . PHE A 1 578 ? 106.988 117.719 50.144  1.00 91.49  ? 566 PHE A CD1   1 
ATOM   4312 C  CD2   . PHE A 1 578 ? 109.146 118.715 50.304  1.00 95.77  ? 566 PHE A CD2   1 
ATOM   4313 C  CE1   . PHE A 1 578 ? 106.781 117.942 51.491  1.00 87.68  ? 566 PHE A CE1   1 
ATOM   4314 C  CE2   . PHE A 1 578 ? 108.944 118.941 51.653  1.00 90.72  ? 566 PHE A CE2   1 
ATOM   4315 C  CZ    . PHE A 1 578 ? 107.761 118.554 52.246  1.00 85.24  ? 566 PHE A CZ    1 
ATOM   4316 N  N     . ALA A 1 579 ? 109.497 118.279 45.167  1.00 104.04 ? 567 ALA A N     1 
ATOM   4317 C  CA    . ALA A 1 579 ? 110.550 118.108 44.172  1.00 103.75 ? 567 ALA A CA    1 
ATOM   4318 C  C     . ALA A 1 579 ? 110.919 119.435 43.522  1.00 104.77 ? 567 ALA A C     1 
ATOM   4319 O  O     . ALA A 1 579 ? 112.100 119.710 43.284  1.00 105.84 ? 567 ALA A O     1 
ATOM   4320 C  CB    . ALA A 1 579 ? 110.114 117.094 43.116  1.00 100.39 ? 567 ALA A CB    1 
ATOM   4321 N  N     . GLU A 1 580 ? 109.923 120.271 43.223  1.00 103.63 ? 568 GLU A N     1 
ATOM   4322 C  CA    . GLU A 1 580 ? 110.204 121.583 42.650  1.00 104.11 ? 568 GLU A CA    1 
ATOM   4323 C  C     . GLU A 1 580 ? 110.994 122.450 43.622  1.00 105.56 ? 568 GLU A C     1 
ATOM   4324 O  O     . GLU A 1 580 ? 111.920 123.164 43.219  1.00 104.09 ? 568 GLU A O     1 
ATOM   4325 C  CB    . GLU A 1 580 ? 108.897 122.269 42.250  1.00 105.75 ? 568 GLU A CB    1 
ATOM   4326 C  CG    . GLU A 1 580 ? 108.984 123.783 42.159  1.00 110.46 ? 568 GLU A CG    1 
ATOM   4327 C  CD    . GLU A 1 580 ? 107.788 124.392 41.458  1.00 114.69 ? 568 GLU A CD    1 
ATOM   4328 O  OE1   . GLU A 1 580 ? 107.053 123.645 40.779  1.00 111.42 ? 568 GLU A OE1   1 
ATOM   4329 O  OE2   . GLU A 1 580 ? 107.582 125.617 41.586  1.00 114.43 ? 568 GLU A OE2   1 
ATOM   4330 N  N     . SER A 1 581 ? 110.642 122.400 44.908  1.00 105.37 ? 569 SER A N     1 
ATOM   4331 C  CA    . SER A 1 581 ? 111.367 123.181 45.904  1.00 103.91 ? 569 SER A CA    1 
ATOM   4332 C  C     . SER A 1 581 ? 112.810 122.712 46.032  1.00 103.07 ? 569 SER A C     1 
ATOM   4333 O  O     . SER A 1 581 ? 113.725 123.530 46.183  1.00 102.54 ? 569 SER A O     1 
ATOM   4334 C  CB    . SER A 1 581 ? 110.655 123.100 47.254  1.00 96.16  ? 569 SER A CB    1 
ATOM   4335 O  OG    . SER A 1 581 ? 110.957 121.886 47.918  1.00 95.59  ? 569 SER A OG    1 
ATOM   4336 N  N     . GLN A 1 582 ? 113.035 121.402 45.976  1.00 103.20 ? 570 GLN A N     1 
ATOM   4337 C  CA    . GLN A 1 582 ? 114.376 120.858 46.146  1.00 104.60 ? 570 GLN A CA    1 
ATOM   4338 C  C     . GLN A 1 582 ? 115.183 120.817 44.854  1.00 108.85 ? 570 GLN A C     1 
ATOM   4339 O  O     . GLN A 1 582 ? 116.374 120.491 44.899  1.00 108.42 ? 570 GLN A O     1 
ATOM   4340 C  CB    . GLN A 1 582 ? 114.301 119.454 46.744  1.00 103.91 ? 570 GLN A CB    1 
ATOM   4341 C  CG    . GLN A 1 582 ? 113.745 119.425 48.149  1.00 101.26 ? 570 GLN A CG    1 
ATOM   4342 C  CD    . GLN A 1 582 ? 113.823 118.054 48.770  1.00 96.82  ? 570 GLN A CD    1 
ATOM   4343 O  OE1   . GLN A 1 582 ? 114.520 117.173 48.268  1.00 94.91  ? 570 GLN A OE1   1 
ATOM   4344 N  NE2   . GLN A 1 582 ? 113.104 117.859 49.866  1.00 96.01  ? 570 GLN A NE2   1 
ATOM   4345 N  N     . ALA A 1 583 ? 114.569 121.123 43.713  1.00 110.96 ? 571 ALA A N     1 
ATOM   4346 C  CA    . ALA A 1 583 ? 115.299 121.128 42.453  1.00 112.88 ? 571 ALA A CA    1 
ATOM   4347 C  C     . ALA A 1 583 ? 116.418 122.161 42.475  1.00 118.23 ? 571 ALA A C     1 
ATOM   4348 O  O     . ALA A 1 583 ? 116.270 123.254 43.028  1.00 118.99 ? 571 ALA A O     1 
ATOM   4349 C  CB    . ALA A 1 583 ? 114.345 121.410 41.292  1.00 106.84 ? 571 ALA A CB    1 
ATOM   4350 N  N     . LEU A 1 584 ? 117.545 121.805 41.868  1.00 117.35 ? 572 LEU A N     1 
ATOM   4351 C  CA    . LEU A 1 584 ? 118.711 122.680 41.834  1.00 116.20 ? 572 LEU A CA    1 
ATOM   4352 C  C     . LEU A 1 584 ? 118.901 123.288 40.448  1.00 114.52 ? 572 LEU A C     1 
ATOM   4353 O  O     . LEU A 1 584 ? 119.275 122.595 39.501  1.00 116.49 ? 572 LEU A O     1 
ATOM   4354 C  CB    . LEU A 1 584 ? 119.967 121.911 42.249  1.00 118.34 ? 572 LEU A CB    1 
ATOM   4355 C  CG    . LEU A 1 584 ? 121.292 122.671 42.177  1.00 117.81 ? 572 LEU A CG    1 
ATOM   4356 C  CD1   . LEU A 1 584 ? 121.259 123.889 43.086  1.00 110.00 ? 572 LEU A CD1   1 
ATOM   4357 C  CD2   . LEU A 1 584 ? 122.454 121.760 42.537  1.00 115.53 ? 572 LEU A CD2   1 
ATOM   4358 N  N     . THR B 2 14  ? 141.020 113.895 100.705 1.00 111.09 ? 14  THR B N     1 
ATOM   4359 C  CA    . THR B 2 14  ? 139.814 113.698 99.910  1.00 107.45 ? 14  THR B CA    1 
ATOM   4360 C  C     . THR B 2 14  ? 138.838 114.851 100.100 1.00 104.03 ? 14  THR B C     1 
ATOM   4361 O  O     . THR B 2 14  ? 138.746 115.746 99.260  1.00 99.23  ? 14  THR B O     1 
ATOM   4362 C  CB    . THR B 2 14  ? 139.103 112.378 100.272 1.00 103.78 ? 14  THR B CB    1 
ATOM   4363 O  OG1   . THR B 2 14  ? 138.882 112.323 101.687 1.00 98.03  ? 14  THR B OG1   1 
ATOM   4364 C  CG2   . THR B 2 14  ? 139.943 111.183 99.848  1.00 99.96  ? 14  THR B CG2   1 
ATOM   4365 N  N     . ARG B 2 15  ? 138.108 114.818 101.212 1.00 102.71 ? 15  ARG B N     1 
ATOM   4366 C  CA    . ARG B 2 15  ? 137.087 115.805 101.527 1.00 96.20  ? 15  ARG B CA    1 
ATOM   4367 C  C     . ARG B 2 15  ? 137.291 116.324 102.943 1.00 89.99  ? 15  ARG B C     1 
ATOM   4368 O  O     . ARG B 2 15  ? 137.641 115.561 103.849 1.00 88.99  ? 15  ARG B O     1 
ATOM   4369 C  CB    . ARG B 2 15  ? 135.689 115.203 101.367 1.00 86.99  ? 15  ARG B CB    1 
ATOM   4370 C  CG    . ARG B 2 15  ? 135.437 114.670 99.969  1.00 87.73  ? 15  ARG B CG    1 
ATOM   4371 C  CD    . ARG B 2 15  ? 133.963 114.530 99.667  1.00 88.01  ? 15  ARG B CD    1 
ATOM   4372 N  NE    . ARG B 2 15  ? 133.472 113.224 100.085 1.00 93.70  ? 15  ARG B NE    1 
ATOM   4373 C  CZ    . ARG B 2 15  ? 132.348 113.020 100.757 1.00 92.32  ? 15  ARG B CZ    1 
ATOM   4374 N  NH1   . ARG B 2 15  ? 131.549 114.021 101.090 1.00 86.95  ? 15  ARG B NH1   1 
ATOM   4375 N  NH2   . ARG B 2 15  ? 132.016 111.780 101.098 1.00 72.91  ? 15  ARG B NH2   1 
ATOM   4376 N  N     . ASP B 2 16  ? 137.073 117.623 103.126 1.00 80.49  ? 16  ASP B N     1 
ATOM   4377 C  CA    . ASP B 2 16  ? 137.340 118.311 104.387 1.00 77.72  ? 16  ASP B CA    1 
ATOM   4378 C  C     . ASP B 2 16  ? 136.009 118.607 105.070 1.00 72.76  ? 16  ASP B C     1 
ATOM   4379 O  O     . ASP B 2 16  ? 135.296 119.536 104.683 1.00 76.19  ? 16  ASP B O     1 
ATOM   4380 C  CB    . ASP B 2 16  ? 138.135 119.589 104.139 1.00 78.86  ? 16  ASP B CB    1 
ATOM   4381 C  CG    . ASP B 2 16  ? 138.552 120.276 105.422 1.00 79.36  ? 16  ASP B CG    1 
ATOM   4382 O  OD1   . ASP B 2 16  ? 138.577 119.609 106.477 1.00 77.84  ? 16  ASP B OD1   1 
ATOM   4383 O  OD2   . ASP B 2 16  ? 138.854 121.487 105.375 1.00 76.41  ? 16  ASP B OD2   1 
ATOM   4384 N  N     . PHE B 2 17  ? 135.680 117.819 106.094 1.00 69.07  ? 17  PHE B N     1 
ATOM   4385 C  CA    . PHE B 2 17  ? 134.438 118.010 106.834 1.00 67.69  ? 17  PHE B CA    1 
ATOM   4386 C  C     . PHE B 2 17  ? 134.603 118.952 108.020 1.00 63.96  ? 17  PHE B C     1 
ATOM   4387 O  O     . PHE B 2 17  ? 133.693 119.732 108.316 1.00 63.74  ? 17  PHE B O     1 
ATOM   4388 C  CB    . PHE B 2 17  ? 133.894 116.659 107.306 1.00 69.26  ? 17  PHE B CB    1 
ATOM   4389 C  CG    . PHE B 2 17  ? 133.549 115.723 106.186 1.00 70.79  ? 17  PHE B CG    1 
ATOM   4390 C  CD1   . PHE B 2 17  ? 132.342 115.837 105.519 1.00 64.27  ? 17  PHE B CD1   1 
ATOM   4391 C  CD2   . PHE B 2 17  ? 134.438 114.738 105.789 1.00 73.08  ? 17  PHE B CD2   1 
ATOM   4392 C  CE1   . PHE B 2 17  ? 132.024 114.981 104.485 1.00 71.81  ? 17  PHE B CE1   1 
ATOM   4393 C  CE2   . PHE B 2 17  ? 134.125 113.879 104.754 1.00 74.10  ? 17  PHE B CE2   1 
ATOM   4394 C  CZ    . PHE B 2 17  ? 132.917 114.001 104.101 1.00 78.27  ? 17  PHE B CZ    1 
ATOM   4395 N  N     . LYS B 2 18  ? 135.743 118.895 108.711 1.00 66.95  ? 18  LYS B N     1 
ATOM   4396 C  CA    . LYS B 2 18  ? 135.994 119.834 109.800 1.00 67.53  ? 18  LYS B CA    1 
ATOM   4397 C  C     . LYS B 2 18  ? 136.061 121.265 109.280 1.00 63.78  ? 18  LYS B C     1 
ATOM   4398 O  O     . LYS B 2 18  ? 135.473 122.183 109.866 1.00 61.18  ? 18  LYS B O     1 
ATOM   4399 C  CB    . LYS B 2 18  ? 137.287 119.456 110.523 1.00 70.90  ? 18  LYS B CB    1 
ATOM   4400 C  CG    . LYS B 2 18  ? 137.814 120.524 111.463 1.00 73.58  ? 18  LYS B CG    1 
ATOM   4401 C  CD    . LYS B 2 18  ? 138.944 119.987 112.323 1.00 75.86  ? 18  LYS B CD    1 
ATOM   4402 C  CE    . LYS B 2 18  ? 140.214 119.806 111.509 1.00 84.67  ? 18  LYS B CE    1 
ATOM   4403 N  NZ    . LYS B 2 18  ? 140.523 121.005 110.684 1.00 77.40  ? 18  LYS B NZ    1 
ATOM   4404 N  N     . GLY B 2 19  ? 136.765 121.468 108.166 1.00 61.81  ? 19  GLY B N     1 
ATOM   4405 C  CA    . GLY B 2 19  ? 136.834 122.794 107.578 1.00 58.89  ? 19  GLY B CA    1 
ATOM   4406 C  C     . GLY B 2 19  ? 135.488 123.285 107.087 1.00 55.94  ? 19  GLY B C     1 
ATOM   4407 O  O     . GLY B 2 19  ? 135.163 124.466 107.219 1.00 61.35  ? 19  GLY B O     1 
ATOM   4408 N  N     . SER B 2 20  ? 134.685 122.388 106.513 1.00 54.49  ? 20  SER B N     1 
ATOM   4409 C  CA    . SER B 2 20  ? 133.354 122.776 106.058 1.00 53.56  ? 20  SER B CA    1 
ATOM   4410 C  C     . SER B 2 20  ? 132.448 123.136 107.228 1.00 52.27  ? 20  SER B C     1 
ATOM   4411 O  O     . SER B 2 20  ? 131.661 124.084 107.139 1.00 49.75  ? 20  SER B O     1 
ATOM   4412 C  CB    . SER B 2 20  ? 132.740 121.658 105.220 1.00 53.92  ? 20  SER B CB    1 
ATOM   4413 O  OG    . SER B 2 20  ? 133.504 121.442 104.049 1.00 59.75  ? 20  SER B OG    1 
ATOM   4414 N  N     . ALA B 2 21  ? 132.539 122.390 108.331 1.00 53.21  ? 21  ALA B N     1 
ATOM   4415 C  CA    . ALA B 2 21  ? 131.772 122.739 109.522 1.00 44.88  ? 21  ALA B CA    1 
ATOM   4416 C  C     . ALA B 2 21  ? 132.204 124.090 110.074 1.00 48.37  ? 21  ALA B C     1 
ATOM   4417 O  O     . ALA B 2 21  ? 131.364 124.893 110.498 1.00 50.83  ? 21  ALA B O     1 
ATOM   4418 C  CB    . ALA B 2 21  ? 131.921 121.652 110.585 1.00 43.33  ? 21  ALA B CB    1 
ATOM   4419 N  N     . ILE B 2 22  ? 133.511 124.360 110.075 1.00 50.01  ? 22  ILE B N     1 
ATOM   4420 C  CA    . ILE B 2 22  ? 133.999 125.660 110.527 1.00 48.63  ? 22  ILE B CA    1 
ATOM   4421 C  C     . ILE B 2 22  ? 133.478 126.774 109.626 1.00 51.31  ? 22  ILE B C     1 
ATOM   4422 O  O     . ILE B 2 22  ? 133.059 127.834 110.105 1.00 55.53  ? 22  ILE B O     1 
ATOM   4423 C  CB    . ILE B 2 22  ? 135.537 125.658 110.599 1.00 48.86  ? 22  ILE B CB    1 
ATOM   4424 C  CG1   . ILE B 2 22  ? 136.013 124.846 111.803 1.00 53.28  ? 22  ILE B CG1   1 
ATOM   4425 C  CG2   . ILE B 2 22  ? 136.074 127.075 110.675 1.00 50.51  ? 22  ILE B CG2   1 
ATOM   4426 C  CD1   . ILE B 2 22  ? 137.506 124.607 111.821 1.00 58.78  ? 22  ILE B CD1   1 
ATOM   4427 N  N     . ARG B 2 23  ? 133.500 126.558 108.308 1.00 48.83  ? 23  ARG B N     1 
ATOM   4428 C  CA    . ARG B 2 23  ? 133.004 127.571 107.380 1.00 47.86  ? 23  ARG B CA    1 
ATOM   4429 C  C     . ARG B 2 23  ? 131.513 127.818 107.570 1.00 48.86  ? 23  ARG B C     1 
ATOM   4430 O  O     . ARG B 2 23  ? 131.055 128.966 107.531 1.00 51.57  ? 23  ARG B O     1 
ATOM   4431 C  CB    . ARG B 2 23  ? 133.286 127.156 105.938 1.00 48.61  ? 23  ARG B CB    1 
ATOM   4432 C  CG    . ARG B 2 23  ? 134.726 127.314 105.500 1.00 51.46  ? 23  ARG B CG    1 
ATOM   4433 C  CD    . ARG B 2 23  ? 134.918 126.764 104.098 1.00 49.31  ? 23  ARG B CD    1 
ATOM   4434 N  NE    . ARG B 2 23  ? 134.295 127.620 103.096 1.00 46.79  ? 23  ARG B NE    1 
ATOM   4435 C  CZ    . ARG B 2 23  ? 134.421 127.457 101.787 1.00 51.88  ? 23  ARG B CZ    1 
ATOM   4436 N  NH1   . ARG B 2 23  ? 135.132 126.464 101.280 1.00 50.53  ? 23  ARG B NH1   1 
ATOM   4437 N  NH2   . ARG B 2 23  ? 133.818 128.311 100.965 1.00 53.70  ? 23  ARG B NH2   1 
ATOM   4438 N  N     . LEU B 2 24  ? 130.738 126.749 107.765 1.00 45.71  ? 24  LEU B N     1 
ATOM   4439 C  CA    . LEU B 2 24  ? 129.306 126.902 107.992 1.00 45.86  ? 24  LEU B CA    1 
ATOM   4440 C  C     . LEU B 2 24  ? 129.030 127.647 109.291 1.00 47.97  ? 24  LEU B C     1 
ATOM   4441 O  O     . LEU B 2 24  ? 128.148 128.513 109.344 1.00 51.60  ? 24  LEU B O     1 
ATOM   4442 C  CB    . LEU B 2 24  ? 128.631 125.532 108.000 1.00 46.95  ? 24  LEU B CB    1 
ATOM   4443 C  CG    . LEU B 2 24  ? 127.111 125.513 108.160 1.00 48.91  ? 24  LEU B CG    1 
ATOM   4444 C  CD1   . LEU B 2 24  ? 126.450 126.319 107.057 1.00 44.03  ? 24  LEU B CD1   1 
ATOM   4445 C  CD2   . LEU B 2 24  ? 126.601 124.085 108.160 1.00 41.09  ? 24  LEU B CD2   1 
ATOM   4446 N  N     . ALA B 2 25  ? 129.777 127.328 110.350 1.00 50.38  ? 25  ALA B N     1 
ATOM   4447 C  CA    . ALA B 2 25  ? 129.614 128.041 111.612 1.00 48.48  ? 25  ALA B CA    1 
ATOM   4448 C  C     . ALA B 2 25  ? 129.978 129.512 111.464 1.00 49.73  ? 25  ALA B C     1 
ATOM   4449 O  O     . ALA B 2 25  ? 129.305 130.383 112.022 1.00 52.45  ? 25  ALA B O     1 
ATOM   4450 C  CB    . ALA B 2 25  ? 130.460 127.385 112.701 1.00 44.60  ? 25  ALA B CB    1 
ATOM   4451 N  N     . ARG B 2 26  ? 131.046 129.807 110.721 1.00 48.75  ? 26  ARG B N     1 
ATOM   4452 C  CA    . ARG B 2 26  ? 131.439 131.195 110.505 1.00 52.19  ? 26  ARG B CA    1 
ATOM   4453 C  C     . ARG B 2 26  ? 130.401 131.956 109.691 1.00 53.92  ? 26  ARG B C     1 
ATOM   4454 O  O     . ARG B 2 26  ? 130.177 133.146 109.934 1.00 50.45  ? 26  ARG B O     1 
ATOM   4455 C  CB    . ARG B 2 26  ? 132.803 131.252 109.820 1.00 50.71  ? 26  ARG B CB    1 
ATOM   4456 C  CG    . ARG B 2 26  ? 133.799 132.160 110.516 1.00 59.74  ? 26  ARG B CG    1 
ATOM   4457 C  CD    . ARG B 2 26  ? 135.153 132.141 109.832 1.00 66.41  ? 26  ARG B CD    1 
ATOM   4458 N  NE    . ARG B 2 26  ? 136.119 131.342 110.575 1.00 75.17  ? 26  ARG B NE    1 
ATOM   4459 C  CZ    . ARG B 2 26  ? 137.433 131.408 110.409 1.00 75.50  ? 26  ARG B CZ    1 
ATOM   4460 N  NH1   . ARG B 2 26  ? 137.979 132.237 109.534 1.00 74.84  ? 26  ARG B NH1   1 
ATOM   4461 N  NH2   . ARG B 2 26  ? 138.219 130.625 111.141 1.00 72.17  ? 26  ARG B NH2   1 
ATOM   4462 N  N     . ARG B 2 27  ? 129.775 131.299 108.713 1.00 57.86  ? 27  ARG B N     1 
ATOM   4463 C  CA    . ARG B 2 27  ? 128.699 131.943 107.966 1.00 52.20  ? 27  ARG B CA    1 
ATOM   4464 C  C     . ARG B 2 27  ? 127.481 132.184 108.848 1.00 52.12  ? 27  ARG B C     1 
ATOM   4465 O  O     . ARG B 2 27  ? 126.838 133.236 108.752 1.00 51.93  ? 27  ARG B O     1 
ATOM   4466 C  CB    . ARG B 2 27  ? 128.324 131.101 106.748 1.00 48.36  ? 27  ARG B CB    1 
ATOM   4467 C  CG    . ARG B 2 27  ? 129.357 131.140 105.639 1.00 51.40  ? 27  ARG B CG    1 
ATOM   4468 C  CD    . ARG B 2 27  ? 128.839 130.497 104.367 1.00 54.59  ? 27  ARG B CD    1 
ATOM   4469 N  NE    . ARG B 2 27  ? 128.049 131.429 103.573 1.00 59.90  ? 27  ARG B NE    1 
ATOM   4470 C  CZ    . ARG B 2 27  ? 128.444 131.952 102.421 1.00 56.27  ? 27  ARG B CZ    1 
ATOM   4471 N  NH1   . ARG B 2 27  ? 129.619 131.654 101.893 1.00 53.22  ? 27  ARG B NH1   1 
ATOM   4472 N  NH2   . ARG B 2 27  ? 127.639 132.797 101.782 1.00 51.15  ? 27  ARG B NH2   1 
ATOM   4473 N  N     . LEU B 2 28  ? 127.148 131.222 109.712 1.00 51.58  ? 28  LEU B N     1 
ATOM   4474 C  CA    . LEU B 2 28  ? 125.994 131.378 110.592 1.00 46.99  ? 28  LEU B CA    1 
ATOM   4475 C  C     . LEU B 2 28  ? 126.225 132.439 111.659 1.00 52.24  ? 28  LEU B C     1 
ATOM   4476 O  O     . LEU B 2 28  ? 125.277 133.118 112.067 1.00 54.54  ? 28  LEU B O     1 
ATOM   4477 C  CB    . LEU B 2 28  ? 125.647 130.047 111.254 1.00 43.49  ? 28  LEU B CB    1 
ATOM   4478 C  CG    . LEU B 2 28  ? 124.898 129.037 110.391 1.00 45.15  ? 28  LEU B CG    1 
ATOM   4479 C  CD1   . LEU B 2 28  ? 124.863 127.686 111.073 1.00 44.16  ? 28  LEU B CD1   1 
ATOM   4480 C  CD2   . LEU B 2 28  ? 123.499 129.541 110.118 1.00 43.21  ? 28  LEU B CD2   1 
ATOM   4481 N  N     . LEU B 2 29  ? 127.465 132.600 112.123 1.00 54.72  ? 29  LEU B N     1 
ATOM   4482 C  CA    . LEU B 2 29  ? 127.797 133.522 113.207 1.00 56.04  ? 29  LEU B CA    1 
ATOM   4483 C  C     . LEU B 2 29  ? 128.882 134.484 112.735 1.00 61.35  ? 29  LEU B C     1 
ATOM   4484 O  O     . LEU B 2 29  ? 130.067 134.309 113.055 1.00 63.36  ? 29  LEU B O     1 
ATOM   4485 C  CB    . LEU B 2 29  ? 128.241 132.764 114.456 1.00 55.04  ? 29  LEU B CB    1 
ATOM   4486 C  CG    . LEU B 2 29  ? 127.222 131.798 115.065 1.00 59.55  ? 29  LEU B CG    1 
ATOM   4487 C  CD1   . LEU B 2 29  ? 127.881 130.912 116.107 1.00 56.44  ? 29  LEU B CD1   1 
ATOM   4488 C  CD2   . LEU B 2 29  ? 126.053 132.559 115.672 1.00 56.44  ? 29  LEU B CD2   1 
ATOM   4489 N  N     . PRO B 2 30  ? 128.510 135.522 111.982 1.00 61.45  ? 30  PRO B N     1 
ATOM   4490 C  CA    . PRO B 2 30  ? 129.494 136.525 111.552 1.00 64.41  ? 30  PRO B CA    1 
ATOM   4491 C  C     . PRO B 2 30  ? 129.941 137.439 112.683 1.00 71.97  ? 30  PRO B C     1 
ATOM   4492 O  O     . PRO B 2 30  ? 129.652 137.176 113.854 1.00 71.48  ? 30  PRO B O     1 
ATOM   4493 C  CB    . PRO B 2 30  ? 128.747 137.309 110.463 1.00 65.82  ? 30  PRO B CB    1 
ATOM   4494 C  CG    . PRO B 2 30  ? 127.574 136.456 110.095 1.00 65.57  ? 30  PRO B CG    1 
ATOM   4495 C  CD    . PRO B 2 30  ? 127.204 135.736 111.342 1.00 59.58  ? 30  PRO B CD    1 
ATOM   4496 N  N     . GLN B 2 31  ? 130.669 138.503 112.336 1.00 81.27  ? 31  GLN B N     1 
ATOM   4497 C  CA    . GLN B 2 31  ? 131.229 139.438 113.307 1.00 82.93  ? 31  GLN B CA    1 
ATOM   4498 C  C     . GLN B 2 31  ? 130.170 139.984 114.258 1.00 85.93  ? 31  GLN B C     1 
ATOM   4499 O  O     . GLN B 2 31  ? 128.971 139.943 113.961 1.00 79.53  ? 31  GLN B O     1 
ATOM   4500 C  CB    . GLN B 2 31  ? 131.932 140.593 112.591 1.00 88.38  ? 31  GLN B CB    1 
ATOM   4501 C  CG    . GLN B 2 31  ? 130.993 141.558 111.884 1.00 94.13  ? 31  GLN B CG    1 
ATOM   4502 C  CD    . GLN B 2 31  ? 130.980 142.934 112.526 1.00 100.20 ? 31  GLN B CD    1 
ATOM   4503 O  OE1   . GLN B 2 31  ? 131.321 143.088 113.699 1.00 100.16 ? 31  GLN B OE1   1 
ATOM   4504 N  NE2   . GLN B 2 31  ? 130.594 143.944 111.754 1.00 96.15  ? 31  GLN B NE2   1 
ATOM   4505 N  N     . ARG B 2 32  ? 130.613 140.525 115.390 1.00 88.46  ? 32  ARG B N     1 
ATOM   4506 C  CA    . ARG B 2 32  ? 129.739 140.773 116.530 1.00 89.35  ? 32  ARG B CA    1 
ATOM   4507 C  C     . ARG B 2 32  ? 128.790 141.943 116.302 1.00 87.98  ? 32  ARG B C     1 
ATOM   4508 O  O     . ARG B 2 32  ? 128.969 143.019 116.881 1.00 85.74  ? 32  ARG B O     1 
ATOM   4509 C  CB    . ARG B 2 32  ? 130.578 141.018 117.788 1.00 87.05  ? 32  ARG B CB    1 
ATOM   4510 C  CG    . ARG B 2 32  ? 131.775 140.083 117.939 1.00 86.23  ? 32  ARG B CG    1 
ATOM   4511 C  CD    . ARG B 2 32  ? 131.351 138.622 117.968 1.00 82.92  ? 32  ARG B CD    1 
ATOM   4512 N  NE    . ARG B 2 32  ? 132.451 137.741 118.343 1.00 84.31  ? 32  ARG B NE    1 
ATOM   4513 C  CZ    . ARG B 2 32  ? 132.550 136.467 117.986 1.00 80.56  ? 32  ARG B CZ    1 
ATOM   4514 N  NH1   . ARG B 2 32  ? 131.629 135.887 117.234 1.00 74.72  ? 32  ARG B NH1   1 
ATOM   4515 N  NH2   . ARG B 2 32  ? 133.597 135.758 118.395 1.00 72.53  ? 32  ARG B NH2   1 
ATOM   4516 N  N     . ALA B 2 33  ? 127.778 141.742 115.455 1.00 83.59  ? 33  ALA B N     1 
ATOM   4517 C  CA    . ALA B 2 33  ? 126.696 142.706 115.287 1.00 80.91  ? 33  ALA B CA    1 
ATOM   4518 C  C     . ALA B 2 33  ? 125.392 142.189 115.886 1.00 70.04  ? 33  ALA B C     1 
ATOM   4519 O  O     . ALA B 2 33  ? 124.800 142.835 116.755 1.00 64.09  ? 33  ALA B O     1 
ATOM   4520 C  CB    . ALA B 2 33  ? 126.512 143.042 113.801 1.00 81.73  ? 33  ALA B CB    1 
ATOM   4521 N  N     . LEU B 2 34  ? 124.937 141.019 115.435 1.00 65.30  ? 34  LEU B N     1 
ATOM   4522 C  CA    . LEU B 2 34  ? 123.773 140.355 115.999 1.00 54.41  ? 34  LEU B CA    1 
ATOM   4523 C  C     . LEU B 2 34  ? 124.109 139.041 116.681 1.00 56.64  ? 34  LEU B C     1 
ATOM   4524 O  O     . LEU B 2 34  ? 123.387 138.637 117.601 1.00 60.94  ? 34  LEU B O     1 
ATOM   4525 C  CB    . LEU B 2 34  ? 122.722 140.094 114.906 1.00 50.18  ? 34  LEU B CB    1 
ATOM   4526 C  CG    . LEU B 2 34  ? 121.420 139.388 115.293 1.00 52.84  ? 34  LEU B CG    1 
ATOM   4527 C  CD1   . LEU B 2 34  ? 120.447 140.367 115.932 1.00 53.93  ? 34  LEU B CD1   1 
ATOM   4528 C  CD2   . LEU B 2 34  ? 120.790 138.708 114.090 1.00 46.17  ? 34  LEU B CD2   1 
ATOM   4529 N  N     . THR B 2 35  ? 125.189 138.373 116.271 1.00 59.87  ? 35  THR B N     1 
ATOM   4530 C  CA    . THR B 2 35  ? 125.598 137.144 116.940 1.00 58.75  ? 35  THR B CA    1 
ATOM   4531 C  C     . THR B 2 35  ? 126.016 137.419 118.376 1.00 57.24  ? 35  THR B C     1 
ATOM   4532 O  O     . THR B 2 35  ? 125.817 136.578 119.258 1.00 53.12  ? 35  THR B O     1 
ATOM   4533 C  CB    . THR B 2 35  ? 126.734 136.481 116.167 1.00 61.61  ? 35  THR B CB    1 
ATOM   4534 O  OG1   . THR B 2 35  ? 127.941 137.229 116.353 1.00 66.96  ? 35  THR B OG1   1 
ATOM   4535 C  CG2   . THR B 2 35  ? 126.400 136.453 114.698 1.00 59.19  ? 35  THR B CG2   1 
ATOM   4536 N  N     . LEU B 2 36  ? 126.605 138.589 118.628 1.00 61.82  ? 36  LEU B N     1 
ATOM   4537 C  CA    . LEU B 2 36  ? 126.936 138.965 119.996 1.00 58.41  ? 36  LEU B CA    1 
ATOM   4538 C  C     . LEU B 2 36  ? 125.681 139.085 120.851 1.00 55.35  ? 36  LEU B C     1 
ATOM   4539 O  O     . LEU B 2 36  ? 125.653 138.613 121.993 1.00 55.08  ? 36  LEU B O     1 
ATOM   4540 C  CB    . LEU B 2 36  ? 127.722 140.274 120.003 1.00 65.13  ? 36  LEU B CB    1 
ATOM   4541 C  CG    . LEU B 2 36  ? 128.117 140.831 121.370 1.00 63.11  ? 36  LEU B CG    1 
ATOM   4542 C  CD1   . LEU B 2 36  ? 129.612 141.082 121.423 1.00 66.48  ? 36  LEU B CD1   1 
ATOM   4543 C  CD2   . LEU B 2 36  ? 127.347 142.106 121.664 1.00 60.81  ? 36  LEU B CD2   1 
ATOM   4544 N  N     . ALA B 2 37  ? 124.630 139.706 120.312 1.00 55.29  ? 37  ALA B N     1 
ATOM   4545 C  CA    . ALA B 2 37  ? 123.368 139.796 121.041 1.00 53.38  ? 37  ALA B CA    1 
ATOM   4546 C  C     . ALA B 2 37  ? 122.772 138.416 121.281 1.00 51.89  ? 37  ALA B C     1 
ATOM   4547 O  O     . ALA B 2 37  ? 122.260 138.133 122.370 1.00 53.66  ? 37  ALA B O     1 
ATOM   4548 C  CB    . ALA B 2 37  ? 122.382 140.680 120.281 1.00 46.70  ? 37  ALA B CB    1 
ATOM   4549 N  N     . VAL B 2 38  ? 122.828 137.544 120.272 1.00 53.42  ? 38  VAL B N     1 
ATOM   4550 C  CA    . VAL B 2 38  ? 122.312 136.185 120.429 1.00 49.66  ? 38  VAL B CA    1 
ATOM   4551 C  C     . VAL B 2 38  ? 123.062 135.462 121.542 1.00 52.42  ? 38  VAL B C     1 
ATOM   4552 O  O     . VAL B 2 38  ? 122.458 134.833 122.421 1.00 49.92  ? 38  VAL B O     1 
ATOM   4553 C  CB    . VAL B 2 38  ? 122.411 135.416 119.098 1.00 47.94  ? 38  VAL B CB    1 
ATOM   4554 C  CG1   . VAL B 2 38  ? 122.169 133.932 119.315 1.00 38.86  ? 38  VAL B CG1   1 
ATOM   4555 C  CG2   . VAL B 2 38  ? 121.440 135.975 118.079 1.00 47.56  ? 38  VAL B CG2   1 
ATOM   4556 N  N     . ILE B 2 39  ? 124.393 135.557 121.526 1.00 52.65  ? 39  ILE B N     1 
ATOM   4557 C  CA    . ILE B 2 39  ? 125.214 134.864 122.516 1.00 48.55  ? 39  ILE B CA    1 
ATOM   4558 C  C     . ILE B 2 39  ? 124.932 135.406 123.911 1.00 51.97  ? 39  ILE B C     1 
ATOM   4559 O  O     . ILE B 2 39  ? 124.797 134.644 124.875 1.00 53.97  ? 39  ILE B O     1 
ATOM   4560 C  CB    . ILE B 2 39  ? 126.706 134.978 122.148 1.00 48.07  ? 39  ILE B CB    1 
ATOM   4561 C  CG1   . ILE B 2 39  ? 127.182 133.723 121.412 1.00 48.55  ? 39  ILE B CG1   1 
ATOM   4562 C  CG2   . ILE B 2 39  ? 127.565 135.194 123.383 1.00 48.39  ? 39  ILE B CG2   1 
ATOM   4563 C  CD1   . ILE B 2 39  ? 126.423 133.416 120.142 1.00 52.33  ? 39  ILE B CD1   1 
ATOM   4564 N  N     . LEU B 2 40  ? 124.834 136.732 124.042 1.00 51.36  ? 40  LEU B N     1 
ATOM   4565 C  CA    . LEU B 2 40  ? 124.611 137.325 125.356 1.00 47.77  ? 40  LEU B CA    1 
ATOM   4566 C  C     . LEU B 2 40  ? 123.236 136.972 125.902 1.00 48.35  ? 40  LEU B C     1 
ATOM   4567 O  O     . LEU B 2 40  ? 123.098 136.669 127.093 1.00 53.13  ? 40  LEU B O     1 
ATOM   4568 C  CB    . LEU B 2 40  ? 124.794 138.840 125.287 1.00 55.38  ? 40  LEU B CB    1 
ATOM   4569 C  CG    . LEU B 2 40  ? 126.225 139.347 125.086 1.00 60.64  ? 40  LEU B CG    1 
ATOM   4570 C  CD1   . LEU B 2 40  ? 126.369 140.755 125.630 1.00 60.11  ? 40  LEU B CD1   1 
ATOM   4571 C  CD2   . LEU B 2 40  ? 127.234 138.415 125.739 1.00 54.49  ? 40  LEU B CD2   1 
ATOM   4572 N  N     . LEU B 2 41  ? 122.203 137.007 125.055 1.00 51.34  ? 41  LEU B N     1 
ATOM   4573 C  CA    . LEU B 2 41  ? 120.871 136.620 125.509 1.00 51.84  ? 41  LEU B CA    1 
ATOM   4574 C  C     . LEU B 2 41  ? 120.834 135.154 125.915 1.00 47.53  ? 41  LEU B C     1 
ATOM   4575 O  O     . LEU B 2 41  ? 120.216 134.798 126.926 1.00 45.66  ? 41  LEU B O     1 
ATOM   4576 C  CB    . LEU B 2 41  ? 119.839 136.905 124.420 1.00 49.89  ? 41  LEU B CB    1 
ATOM   4577 C  CG    . LEU B 2 41  ? 119.379 138.357 124.311 1.00 48.45  ? 41  LEU B CG    1 
ATOM   4578 C  CD1   . LEU B 2 41  ? 118.566 138.563 123.052 1.00 43.17  ? 41  LEU B CD1   1 
ATOM   4579 C  CD2   . LEU B 2 41  ? 118.575 138.749 125.533 1.00 46.86  ? 41  LEU B CD2   1 
ATOM   4580 N  N     . GLY B 2 42  ? 121.498 134.288 125.147 1.00 50.09  ? 42  GLY B N     1 
ATOM   4581 C  CA    . GLY B 2 42  ? 121.563 132.888 125.527 1.00 52.37  ? 42  GLY B CA    1 
ATOM   4582 C  C     . GLY B 2 42  ? 122.275 132.672 126.847 1.00 51.49  ? 42  GLY B C     1 
ATOM   4583 O  O     . GLY B 2 42  ? 121.817 131.897 127.688 1.00 52.15  ? 42  GLY B O     1 
ATOM   4584 N  N     . VAL B 2 43  ? 123.399 133.362 127.051 1.00 50.88  ? 43  VAL B N     1 
ATOM   4585 C  CA    . VAL B 2 43  ? 124.148 133.226 128.299 1.00 51.40  ? 43  VAL B CA    1 
ATOM   4586 C  C     . VAL B 2 43  ? 123.309 133.707 129.476 1.00 50.35  ? 43  VAL B C     1 
ATOM   4587 O  O     . VAL B 2 43  ? 123.247 133.053 130.524 1.00 50.95  ? 43  VAL B O     1 
ATOM   4588 C  CB    . VAL B 2 43  ? 125.484 133.986 128.210 1.00 51.05  ? 43  VAL B CB    1 
ATOM   4589 C  CG1   . VAL B 2 43  ? 126.086 134.167 129.592 1.00 44.09  ? 43  VAL B CG1   1 
ATOM   4590 C  CG2   . VAL B 2 43  ? 126.450 133.252 127.306 1.00 51.11  ? 43  VAL B CG2   1 
ATOM   4591 N  N     . GLY B 2 44  ? 122.649 134.856 129.319 1.00 45.42  ? 44  GLY B N     1 
ATOM   4592 C  CA    . GLY B 2 44  ? 121.827 135.375 130.401 1.00 41.91  ? 44  GLY B CA    1 
ATOM   4593 C  C     . GLY B 2 44  ? 120.675 134.452 130.747 1.00 47.36  ? 44  GLY B C     1 
ATOM   4594 O  O     . GLY B 2 44  ? 120.428 134.159 131.921 1.00 50.83  ? 44  GLY B O     1 
ATOM   4595 N  N     . GLY B 2 45  ? 119.963 133.969 129.728 1.00 46.55  ? 45  GLY B N     1 
ATOM   4596 C  CA    . GLY B 2 45  ? 118.866 133.052 129.981 1.00 41.36  ? 45  GLY B CA    1 
ATOM   4597 C  C     . GLY B 2 45  ? 119.327 131.759 130.622 1.00 48.30  ? 45  GLY B C     1 
ATOM   4598 O  O     . GLY B 2 45  ? 118.693 131.258 131.554 1.00 54.03  ? 45  GLY B O     1 
ATOM   4599 N  N     . ILE B 2 46  ? 120.444 131.207 130.141 1.00 50.32  ? 46  ILE B N     1 
ATOM   4600 C  CA    . ILE B 2 46  ? 120.950 129.951 130.684 1.00 50.92  ? 46  ILE B CA    1 
ATOM   4601 C  C     . ILE B 2 46  ? 121.364 130.129 132.139 1.00 49.08  ? 46  ILE B C     1 
ATOM   4602 O  O     . ILE B 2 46  ? 121.037 129.299 132.994 1.00 49.60  ? 46  ILE B O     1 
ATOM   4603 C  CB    . ILE B 2 46  ? 122.107 129.421 129.812 1.00 53.10  ? 46  ILE B CB    1 
ATOM   4604 C  CG1   . ILE B 2 46  ? 121.595 128.392 128.801 1.00 53.58  ? 46  ILE B CG1   1 
ATOM   4605 C  CG2   . ILE B 2 46  ? 123.194 128.792 130.665 1.00 45.55  ? 46  ILE B CG2   1 
ATOM   4606 C  CD1   . ILE B 2 46  ? 120.543 128.915 127.851 1.00 49.13  ? 46  ILE B CD1   1 
ATOM   4607 N  N     . ALA B 2 47  ? 122.070 131.220 132.450 1.00 46.73  ? 47  ALA B N     1 
ATOM   4608 C  CA    . ALA B 2 47  ? 122.488 131.456 133.828 1.00 47.84  ? 47  ALA B CA    1 
ATOM   4609 C  C     . ALA B 2 47  ? 121.290 131.650 134.748 1.00 47.90  ? 47  ALA B C     1 
ATOM   4610 O  O     . ALA B 2 47  ? 121.250 131.099 135.857 1.00 51.78  ? 47  ALA B O     1 
ATOM   4611 C  CB    . ALA B 2 47  ? 123.416 132.668 133.894 1.00 39.72  ? 47  ALA B CB    1 
ATOM   4612 N  N     . ILE B 2 48  ? 120.296 132.421 134.302 1.00 48.42  ? 48  ILE B N     1 
ATOM   4613 C  CA    . ILE B 2 48  ? 119.145 132.694 135.154 1.00 49.81  ? 48  ILE B CA    1 
ATOM   4614 C  C     . ILE B 2 48  ? 118.334 131.424 135.389 1.00 47.53  ? 48  ILE B C     1 
ATOM   4615 O  O     . ILE B 2 48  ? 117.884 131.159 136.509 1.00 50.75  ? 48  ILE B O     1 
ATOM   4616 C  CB    . ILE B 2 48  ? 118.295 133.822 134.544 1.00 49.57  ? 48  ILE B CB    1 
ATOM   4617 C  CG1   . ILE B 2 48  ? 118.969 135.170 134.784 1.00 48.41  ? 48  ILE B CG1   1 
ATOM   4618 C  CG2   . ILE B 2 48  ? 116.921 133.839 135.159 1.00 47.62  ? 48  ILE B CG2   1 
ATOM   4619 C  CD1   . ILE B 2 48  ? 118.396 136.291 133.954 1.00 54.42  ? 48  ILE B CD1   1 
ATOM   4620 N  N     . GLY B 2 49  ? 118.147 130.609 134.348 1.00 45.86  ? 49  GLY B N     1 
ATOM   4621 C  CA    . GLY B 2 49  ? 117.426 129.360 134.518 1.00 44.10  ? 49  GLY B CA    1 
ATOM   4622 C  C     . GLY B 2 49  ? 118.216 128.281 135.228 1.00 46.05  ? 49  GLY B C     1 
ATOM   4623 O  O     . GLY B 2 49  ? 117.623 127.307 135.704 1.00 49.28  ? 49  GLY B O     1 
ATOM   4624 N  N     . VAL B 2 50  ? 119.538 128.420 135.293 1.00 46.54  ? 50  VAL B N     1 
ATOM   4625 C  CA    . VAL B 2 50  ? 120.360 127.480 136.044 1.00 46.15  ? 50  VAL B CA    1 
ATOM   4626 C  C     . VAL B 2 50  ? 120.415 127.849 137.525 1.00 43.26  ? 50  VAL B C     1 
ATOM   4627 O  O     . VAL B 2 50  ? 120.552 126.968 138.380 1.00 41.21  ? 50  VAL B O     1 
ATOM   4628 C  CB    . VAL B 2 50  ? 121.764 127.414 135.411 1.00 44.79  ? 50  VAL B CB    1 
ATOM   4629 C  CG1   . VAL B 2 50  ? 122.823 127.076 136.429 1.00 41.01  ? 50  VAL B CG1   1 
ATOM   4630 C  CG2   . VAL B 2 50  ? 121.784 126.392 134.284 1.00 51.55  ? 50  VAL B CG2   1 
ATOM   4631 N  N     . ILE B 2 51  ? 120.271 129.135 137.849 1.00 45.52  ? 51  ILE B N     1 
ATOM   4632 C  CA    . ILE B 2 51  ? 120.214 129.547 139.250 1.00 40.78  ? 51  ILE B CA    1 
ATOM   4633 C  C     . ILE B 2 51  ? 119.021 128.916 139.965 1.00 38.51  ? 51  ILE B C     1 
ATOM   4634 O  O     . ILE B 2 51  ? 119.083 128.644 141.170 1.00 39.77  ? 51  ILE B O     1 
ATOM   4635 C  CB    . ILE B 2 51  ? 120.192 131.088 139.333 1.00 45.11  ? 51  ILE B CB    1 
ATOM   4636 C  CG1   . ILE B 2 51  ? 121.611 131.642 139.206 1.00 47.88  ? 51  ILE B CG1   1 
ATOM   4637 C  CG2   . ILE B 2 51  ? 119.553 131.572 140.623 1.00 44.69  ? 51  ILE B CG2   1 
ATOM   4638 C  CD1   . ILE B 2 51  ? 122.477 131.375 140.414 1.00 45.75  ? 51  ILE B CD1   1 
ATOM   4639 N  N     . GLY B 2 52  ? 117.944 128.631 139.236 1.00 40.28  ? 52  GLY B N     1 
ATOM   4640 C  CA    . GLY B 2 52  ? 116.684 128.214 139.815 1.00 38.61  ? 52  GLY B CA    1 
ATOM   4641 C  C     . GLY B 2 52  ? 116.706 126.977 140.699 1.00 37.73  ? 52  GLY B C     1 
ATOM   4642 O  O     . GLY B 2 52  ? 116.113 126.968 141.785 1.00 41.17  ? 52  GLY B O     1 
ATOM   4643 N  N     . PRO B 2 53  ? 117.355 125.899 140.248 1.00 35.10  ? 53  PRO B N     1 
ATOM   4644 C  CA    . PRO B 2 53  ? 117.449 124.704 141.101 1.00 37.12  ? 53  PRO B CA    1 
ATOM   4645 C  C     . PRO B 2 53  ? 118.086 124.955 142.458 1.00 35.22  ? 53  PRO B C     1 
ATOM   4646 O  O     . PRO B 2 53  ? 117.707 124.295 143.429 1.00 38.96  ? 53  PRO B O     1 
ATOM   4647 C  CB    . PRO B 2 53  ? 118.288 123.745 140.250 1.00 33.79  ? 53  PRO B CB    1 
ATOM   4648 C  CG    . PRO B 2 53  ? 117.925 124.096 138.868 1.00 38.39  ? 53  PRO B CG    1 
ATOM   4649 C  CD    . PRO B 2 53  ? 117.695 125.586 138.849 1.00 38.36  ? 53  PRO B CD    1 
ATOM   4650 N  N     . ARG B 2 54  ? 119.036 125.885 142.563 1.00 35.17  ? 54  ARG B N     1 
ATOM   4651 C  CA    . ARG B 2 54  ? 119.585 126.237 143.871 1.00 34.15  ? 54  ARG B CA    1 
ATOM   4652 C  C     . ARG B 2 54  ? 118.517 126.847 144.774 1.00 35.25  ? 54  ARG B C     1 
ATOM   4653 O  O     . ARG B 2 54  ? 118.456 126.548 145.972 1.00 39.89  ? 54  ARG B O     1 
ATOM   4654 C  CB    . ARG B 2 54  ? 120.757 127.201 143.701 1.00 34.14  ? 54  ARG B CB    1 
ATOM   4655 C  CG    . ARG B 2 54  ? 121.757 127.177 144.835 1.00 36.11  ? 54  ARG B CG    1 
ATOM   4656 C  CD    . ARG B 2 54  ? 122.765 126.061 144.660 1.00 40.13  ? 54  ARG B CD    1 
ATOM   4657 N  NE    . ARG B 2 54  ? 123.887 126.198 145.580 1.00 49.60  ? 54  ARG B NE    1 
ATOM   4658 C  CZ    . ARG B 2 54  ? 123.955 125.617 146.769 1.00 46.54  ? 54  ARG B CZ    1 
ATOM   4659 N  NH1   . ARG B 2 54  ? 122.975 124.852 147.222 1.00 40.07  ? 54  ARG B NH1   1 
ATOM   4660 N  NH2   . ARG B 2 54  ? 125.031 125.810 147.525 1.00 45.00  ? 54  ARG B NH2   1 
ATOM   4661 N  N     . ILE B 2 55  ? 117.669 127.710 144.214 1.00 36.04  ? 55  ILE B N     1 
ATOM   4662 C  CA    . ILE B 2 55  ? 116.584 128.317 144.981 1.00 35.75  ? 55  ILE B CA    1 
ATOM   4663 C  C     . ILE B 2 55  ? 115.583 127.256 145.428 1.00 36.83  ? 55  ILE B C     1 
ATOM   4664 O  O     . ILE B 2 55  ? 115.119 127.253 146.579 1.00 41.17  ? 55  ILE B O     1 
ATOM   4665 C  CB    . ILE B 2 55  ? 115.916 129.419 144.139 1.00 36.90  ? 55  ILE B CB    1 
ATOM   4666 C  CG1   . ILE B 2 55  ? 116.922 130.524 143.823 1.00 37.46  ? 55  ILE B CG1   1 
ATOM   4667 C  CG2   . ILE B 2 55  ? 114.715 129.988 144.844 1.00 38.08  ? 55  ILE B CG2   1 
ATOM   4668 C  CD1   . ILE B 2 55  ? 116.468 131.456 142.734 1.00 45.61  ? 55  ILE B CD1   1 
ATOM   4669 N  N     . LEU B 2 56  ? 115.236 126.338 144.525 1.00 37.09  ? 56  LEU B N     1 
ATOM   4670 C  CA    . LEU B 2 56  ? 114.333 125.251 144.887 1.00 34.34  ? 56  LEU B CA    1 
ATOM   4671 C  C     . LEU B 2 56  ? 114.945 124.365 145.966 1.00 36.15  ? 56  LEU B C     1 
ATOM   4672 O  O     . LEU B 2 56  ? 114.243 123.891 146.866 1.00 40.72  ? 56  LEU B O     1 
ATOM   4673 C  CB    . LEU B 2 56  ? 113.981 124.434 143.645 1.00 34.80  ? 56  LEU B CB    1 
ATOM   4674 C  CG    . LEU B 2 56  ? 112.650 124.737 142.955 1.00 35.74  ? 56  LEU B CG    1 
ATOM   4675 C  CD1   . LEU B 2 56  ? 112.489 126.220 142.689 1.00 38.72  ? 56  LEU B CD1   1 
ATOM   4676 C  CD2   . LEU B 2 56  ? 112.544 123.956 141.661 1.00 35.94  ? 56  LEU B CD2   1 
ATOM   4677 N  N     . GLY B 2 57  ? 116.256 124.132 145.890 1.00 36.05  ? 57  GLY B N     1 
ATOM   4678 C  CA    . GLY B 2 57  ? 116.927 123.372 146.929 1.00 34.09  ? 57  GLY B CA    1 
ATOM   4679 C  C     . GLY B 2 57  ? 116.917 124.080 148.268 1.00 40.25  ? 57  GLY B C     1 
ATOM   4680 O  O     . GLY B 2 57  ? 116.806 123.441 149.313 1.00 45.22  ? 57  GLY B O     1 
ATOM   4681 N  N     . HIS B 2 58  ? 117.044 125.407 148.258 1.00 41.01  ? 58  HIS B N     1 
ATOM   4682 C  CA    . HIS B 2 58  ? 116.925 126.159 149.505 1.00 38.36  ? 58  HIS B CA    1 
ATOM   4683 C  C     . HIS B 2 58  ? 115.530 126.020 150.099 1.00 39.74  ? 58  HIS B C     1 
ATOM   4684 O  O     . HIS B 2 58  ? 115.374 125.881 151.319 1.00 43.19  ? 58  HIS B O     1 
ATOM   4685 C  CB    . HIS B 2 58  ? 117.260 127.630 149.276 1.00 41.44  ? 58  HIS B CB    1 
ATOM   4686 C  CG    . HIS B 2 58  ? 117.139 128.470 150.509 1.00 54.66  ? 58  HIS B CG    1 
ATOM   4687 N  ND1   . HIS B 2 58  ? 116.302 129.562 150.587 1.00 56.12  ? 58  HIS B ND1   1 
ATOM   4688 C  CD2   . HIS B 2 58  ? 117.742 128.372 151.717 1.00 55.23  ? 58  HIS B CD2   1 
ATOM   4689 C  CE1   . HIS B 2 58  ? 116.398 130.102 151.789 1.00 55.03  ? 58  HIS B CE1   1 
ATOM   4690 N  NE2   . HIS B 2 58  ? 117.265 129.399 152.494 1.00 55.57  ? 58  HIS B NE2   1 
ATOM   4691 N  N     . ALA B 2 59  ? 114.499 126.068 149.253 1.00 42.68  ? 59  ALA B N     1 
ATOM   4692 C  CA    . ALA B 2 59  ? 113.137 125.869 149.746 1.00 39.45  ? 59  ALA B CA    1 
ATOM   4693 C  C     . ALA B 2 59  ? 112.963 124.473 150.337 1.00 40.08  ? 59  ALA B C     1 
ATOM   4694 O  O     . ALA B 2 59  ? 112.335 124.304 151.392 1.00 44.71  ? 59  ALA B O     1 
ATOM   4695 C  CB    . ALA B 2 59  ? 112.131 126.105 148.622 1.00 38.98  ? 59  ALA B CB    1 
ATOM   4696 N  N     . THR B 2 60  ? 113.516 123.460 149.668 1.00 40.58  ? 60  THR B N     1 
ATOM   4697 C  CA    . THR B 2 60  ? 113.465 122.100 150.195 1.00 37.97  ? 60  THR B CA    1 
ATOM   4698 C  C     . THR B 2 60  ? 114.215 121.991 151.519 1.00 42.76  ? 60  THR B C     1 
ATOM   4699 O  O     . THR B 2 60  ? 113.786 121.271 152.425 1.00 46.82  ? 60  THR B O     1 
ATOM   4700 C  CB    . THR B 2 60  ? 114.037 121.121 149.171 1.00 32.77  ? 60  THR B CB    1 
ATOM   4701 O  OG1   . THR B 2 60  ? 113.246 121.163 147.979 1.00 38.10  ? 60  THR B OG1   1 
ATOM   4702 C  CG2   . THR B 2 60  ? 114.030 119.706 149.720 1.00 32.38  ? 60  THR B CG2   1 
ATOM   4703 N  N     . ASP B 2 61  ? 115.346 122.689 151.642 1.00 41.43  ? 61  ASP B N     1 
ATOM   4704 C  CA    . ASP B 2 61  ? 116.082 122.698 152.902 1.00 41.71  ? 61  ASP B CA    1 
ATOM   4705 C  C     . ASP B 2 61  ? 115.259 123.326 154.016 1.00 48.65  ? 61  ASP B C     1 
ATOM   4706 O  O     . ASP B 2 61  ? 115.270 122.839 155.150 1.00 56.07  ? 61  ASP B O     1 
ATOM   4707 C  CB    . ASP B 2 61  ? 117.406 123.443 152.741 1.00 48.09  ? 61  ASP B CB    1 
ATOM   4708 C  CG    . ASP B 2 61  ? 118.584 122.508 152.600 1.00 55.83  ? 61  ASP B CG    1 
ATOM   4709 O  OD1   . ASP B 2 61  ? 118.462 121.336 153.011 1.00 56.59  ? 61  ASP B OD1   1 
ATOM   4710 O  OD2   . ASP B 2 61  ? 119.635 122.944 152.087 1.00 55.34  ? 61  ASP B OD2   1 
ATOM   4711 N  N     . LEU B 2 62  ? 114.550 124.415 153.719 1.00 50.34  ? 62  LEU B N     1 
ATOM   4712 C  CA    . LEU B 2 62  ? 113.676 125.019 154.723 1.00 49.27  ? 62  LEU B CA    1 
ATOM   4713 C  C     . LEU B 2 62  ? 112.589 124.044 155.157 1.00 49.28  ? 62  LEU B C     1 
ATOM   4714 O  O     . LEU B 2 62  ? 112.319 123.885 156.355 1.00 52.86  ? 62  LEU B O     1 
ATOM   4715 C  CB    . LEU B 2 62  ? 113.054 126.305 154.180 1.00 46.54  ? 62  LEU B CB    1 
ATOM   4716 C  CG    . LEU B 2 62  ? 113.966 127.517 154.006 1.00 53.11  ? 62  LEU B CG    1 
ATOM   4717 C  CD1   . LEU B 2 62  ? 113.232 128.617 153.267 1.00 51.02  ? 62  LEU B CD1   1 
ATOM   4718 C  CD2   . LEU B 2 62  ? 114.464 128.014 155.349 1.00 53.33  ? 62  LEU B CD2   1 
ATOM   4719 N  N     . LEU B 2 63  ? 111.957 123.374 154.189 1.00 48.10  ? 63  LEU B N     1 
ATOM   4720 C  CA    . LEU B 2 63  ? 110.910 122.411 154.523 1.00 48.12  ? 63  LEU B CA    1 
ATOM   4721 C  C     . LEU B 2 63  ? 111.458 121.279 155.381 1.00 53.53  ? 63  LEU B C     1 
ATOM   4722 O  O     . LEU B 2 63  ? 110.859 120.907 156.398 1.00 61.51  ? 63  LEU B O     1 
ATOM   4723 C  CB    . LEU B 2 63  ? 110.280 121.851 153.249 1.00 42.26  ? 63  LEU B CB    1 
ATOM   4724 C  CG    . LEU B 2 63  ? 109.507 122.824 152.362 1.00 48.18  ? 63  LEU B CG    1 
ATOM   4725 C  CD1   . LEU B 2 63  ? 109.262 122.206 150.998 1.00 43.29  ? 63  LEU B CD1   1 
ATOM   4726 C  CD2   . LEU B 2 63  ? 108.200 123.220 153.022 1.00 45.82  ? 63  LEU B CD2   1 
ATOM   4727 N  N     . PHE B 2 64  ? 112.602 120.718 154.983 1.00 52.12  ? 64  PHE B N     1 
ATOM   4728 C  CA    . PHE B 2 64  ? 113.190 119.604 155.718 1.00 50.25  ? 64  PHE B CA    1 
ATOM   4729 C  C     . PHE B 2 64  ? 113.607 120.027 157.118 1.00 54.92  ? 64  PHE B C     1 
ATOM   4730 O  O     . PHE B 2 64  ? 113.390 119.288 158.086 1.00 58.64  ? 64  PHE B O     1 
ATOM   4731 C  CB    . PHE B 2 64  ? 114.384 119.049 154.945 1.00 47.40  ? 64  PHE B CB    1 
ATOM   4732 C  CG    . PHE B 2 64  ? 114.886 117.737 155.465 1.00 52.55  ? 64  PHE B CG    1 
ATOM   4733 C  CD1   . PHE B 2 64  ? 114.009 116.706 155.744 1.00 54.65  ? 64  PHE B CD1   1 
ATOM   4734 C  CD2   . PHE B 2 64  ? 116.238 117.532 155.670 1.00 52.60  ? 64  PHE B CD2   1 
ATOM   4735 C  CE1   . PHE B 2 64  ? 114.469 115.498 156.220 1.00 54.50  ? 64  PHE B CE1   1 
ATOM   4736 C  CE2   . PHE B 2 64  ? 116.703 116.326 156.146 1.00 54.53  ? 64  PHE B CE2   1 
ATOM   4737 C  CZ    . PHE B 2 64  ? 115.818 115.308 156.422 1.00 55.90  ? 64  PHE B CZ    1 
ATOM   4738 N  N     . ASN B 2 65  ? 114.203 121.214 157.246 1.00 56.04  ? 65  ASN B N     1 
ATOM   4739 C  CA    . ASN B 2 65  ? 114.603 121.714 158.553 1.00 60.68  ? 65  ASN B CA    1 
ATOM   4740 C  C     . ASN B 2 65  ? 113.400 121.868 159.466 1.00 66.72  ? 65  ASN B C     1 
ATOM   4741 O  O     . ASN B 2 65  ? 113.429 121.431 160.622 1.00 69.78  ? 65  ASN B O     1 
ATOM   4742 C  CB    . ASN B 2 65  ? 115.324 123.052 158.402 1.00 62.09  ? 65  ASN B CB    1 
ATOM   4743 C  CG    . ASN B 2 65  ? 116.746 122.896 157.921 1.00 67.46  ? 65  ASN B CG    1 
ATOM   4744 O  OD1   . ASN B 2 65  ? 117.361 121.852 158.106 1.00 69.37  ? 65  ASN B OD1   1 
ATOM   4745 N  ND2   . ASN B 2 65  ? 117.277 123.939 157.296 1.00 73.45  ? 65  ASN B ND2   1 
ATOM   4746 N  N     . GLY B 2 66  ? 112.326 122.478 158.962 1.00 67.37  ? 66  GLY B N     1 
ATOM   4747 C  CA    . GLY B 2 66  ? 111.136 122.636 159.780 1.00 68.42  ? 66  GLY B CA    1 
ATOM   4748 C  C     . GLY B 2 66  ? 110.536 121.307 160.193 1.00 67.73  ? 66  GLY B C     1 
ATOM   4749 O  O     . GLY B 2 66  ? 110.183 121.104 161.357 1.00 73.29  ? 66  GLY B O     1 
ATOM   4750 N  N     . VAL B 2 67  ? 110.431 120.374 159.244 1.00 67.31  ? 67  VAL B N     1 
ATOM   4751 C  CA    . VAL B 2 67  ? 109.798 119.090 159.529 1.00 68.56  ? 67  VAL B CA    1 
ATOM   4752 C  C     . VAL B 2 67  ? 110.610 118.303 160.550 1.00 71.32  ? 67  VAL B C     1 
ATOM   4753 O  O     . VAL B 2 67  ? 110.050 117.681 161.461 1.00 73.70  ? 67  VAL B O     1 
ATOM   4754 C  CB    . VAL B 2 67  ? 109.594 118.300 158.224 1.00 62.92  ? 67  VAL B CB    1 
ATOM   4755 C  CG1   . VAL B 2 67  ? 109.276 116.845 158.518 1.00 61.69  ? 67  VAL B CG1   1 
ATOM   4756 C  CG2   . VAL B 2 67  ? 108.484 118.932 157.412 1.00 63.31  ? 67  VAL B CG2   1 
ATOM   4757 N  N     . ILE B 2 68  ? 111.938 118.312 160.418 1.00 71.97  ? 68  ILE B N     1 
ATOM   4758 C  CA    . ILE B 2 68  ? 112.772 117.577 161.362 1.00 69.85  ? 68  ILE B CA    1 
ATOM   4759 C  C     . ILE B 2 68  ? 112.754 118.241 162.734 1.00 74.77  ? 68  ILE B C     1 
ATOM   4760 O  O     . ILE B 2 68  ? 112.633 117.563 163.762 1.00 78.93  ? 68  ILE B O     1 
ATOM   4761 C  CB    . ILE B 2 68  ? 114.204 117.440 160.817 1.00 68.09  ? 68  ILE B CB    1 
ATOM   4762 C  CG1   . ILE B 2 68  ? 114.223 116.507 159.607 1.00 62.80  ? 68  ILE B CG1   1 
ATOM   4763 C  CG2   . ILE B 2 68  ? 115.127 116.917 161.892 1.00 69.40  ? 68  ILE B CG2   1 
ATOM   4764 C  CD1   . ILE B 2 68  ? 113.971 115.060 159.949 1.00 61.38  ? 68  ILE B CD1   1 
ATOM   4765 N  N     . GLY B 2 69  ? 112.863 119.572 162.781 1.00 76.10  ? 69  GLY B N     1 
ATOM   4766 C  CA    . GLY B 2 69  ? 112.921 120.259 164.057 1.00 82.04  ? 69  GLY B CA    1 
ATOM   4767 C  C     . GLY B 2 69  ? 111.605 120.335 164.796 1.00 85.58  ? 69  GLY B C     1 
ATOM   4768 O  O     . GLY B 2 69  ? 111.603 120.582 166.005 1.00 90.53  ? 69  GLY B O     1 
ATOM   4769 N  N     . ARG B 2 70  ? 110.485 120.136 164.098 1.00 85.24  ? 70  ARG B N     1 
ATOM   4770 C  CA    . ARG B 2 70  ? 109.191 120.152 164.771 1.00 86.75  ? 70  ARG B CA    1 
ATOM   4771 C  C     . ARG B 2 70  ? 109.070 119.006 165.768 1.00 91.87  ? 70  ARG B C     1 
ATOM   4772 O  O     . ARG B 2 70  ? 108.518 119.179 166.861 1.00 94.75  ? 70  ARG B O     1 
ATOM   4773 C  CB    . ARG B 2 70  ? 108.068 120.086 163.738 1.00 81.40  ? 70  ARG B CB    1 
ATOM   4774 C  CG    . ARG B 2 70  ? 106.775 120.737 164.184 1.00 84.39  ? 70  ARG B CG    1 
ATOM   4775 C  CD    . ARG B 2 70  ? 105.632 120.371 163.255 1.00 82.86  ? 70  ARG B CD    1 
ATOM   4776 N  NE    . ARG B 2 70  ? 105.830 119.065 162.639 1.00 76.93  ? 70  ARG B NE    1 
ATOM   4777 C  CZ    . ARG B 2 70  ? 105.549 118.783 161.375 1.00 73.01  ? 70  ARG B CZ    1 
ATOM   4778 N  NH1   . ARG B 2 70  ? 105.048 119.695 160.559 1.00 70.34  ? 70  ARG B NH1   1 
ATOM   4779 N  NH2   . ARG B 2 70  ? 105.773 117.555 160.918 1.00 72.65  ? 70  ARG B NH2   1 
ATOM   4780 N  N     . GLU B 2 71  ? 109.583 117.828 165.413 1.00 94.39  ? 71  GLU B N     1 
ATOM   4781 C  CA    . GLU B 2 71  ? 109.426 116.643 166.246 1.00 97.91  ? 71  GLU B CA    1 
ATOM   4782 C  C     . GLU B 2 71  ? 110.384 116.602 167.430 1.00 98.75  ? 71  GLU B C     1 
ATOM   4783 O  O     . GLU B 2 71  ? 110.202 115.764 168.320 1.00 95.36  ? 71  GLU B O     1 
ATOM   4784 C  CB    . GLU B 2 71  ? 109.609 115.381 165.400 1.00 97.12  ? 71  GLU B CB    1 
ATOM   4785 C  CG    . GLU B 2 71  ? 108.342 114.919 164.700 1.00 96.52  ? 71  GLU B CG    1 
ATOM   4786 C  CD    . GLU B 2 71  ? 107.663 113.770 165.421 1.00 105.38 ? 71  GLU B CD    1 
ATOM   4787 O  OE1   . GLU B 2 71  ? 106.628 113.283 164.921 1.00 103.39 ? 71  GLU B OE1   1 
ATOM   4788 O  OE2   . GLU B 2 71  ? 108.164 113.357 166.488 1.00 106.55 ? 71  GLU B OE2   1 
ATOM   4789 N  N     . LEU B 2 72  ? 111.391 117.467 167.467 1.00 100.73 ? 72  LEU B N     1 
ATOM   4790 C  CA    . LEU B 2 72  ? 112.271 117.436 168.624 1.00 106.42 ? 72  LEU B CA    1 
ATOM   4791 C  C     . LEU B 2 72  ? 111.717 118.308 169.748 1.00 114.94 ? 72  LEU B C     1 
ATOM   4792 O  O     . LEU B 2 72  ? 110.976 119.262 169.491 1.00 114.39 ? 72  LEU B O     1 
ATOM   4793 C  CB    . LEU B 2 72  ? 113.669 117.915 168.243 1.00 99.28  ? 72  LEU B CB    1 
ATOM   4794 C  CG    . LEU B 2 72  ? 114.425 117.023 167.260 1.00 98.60  ? 72  LEU B CG    1 
ATOM   4795 C  CD1   . LEU B 2 72  ? 115.727 117.674 166.843 1.00 100.84 ? 72  LEU B CD1   1 
ATOM   4796 C  CD2   . LEU B 2 72  ? 114.677 115.653 167.865 1.00 99.23  ? 72  LEU B CD2   1 
ATOM   4797 N  N     . PRO B 2 73  ? 112.047 117.994 171.002 1.00 115.97 ? 73  PRO B N     1 
ATOM   4798 C  CA    . PRO B 2 73  ? 111.566 118.822 172.116 1.00 113.45 ? 73  PRO B CA    1 
ATOM   4799 C  C     . PRO B 2 73  ? 112.075 120.252 172.009 1.00 111.46 ? 73  PRO B C     1 
ATOM   4800 O  O     . PRO B 2 73  ? 113.219 120.498 171.621 1.00 112.01 ? 73  PRO B O     1 
ATOM   4801 C  CB    . PRO B 2 73  ? 112.128 118.114 173.355 1.00 114.19 ? 73  PRO B CB    1 
ATOM   4802 C  CG    . PRO B 2 73  ? 113.255 117.277 172.844 1.00 110.62 ? 73  PRO B CG    1 
ATOM   4803 C  CD    . PRO B 2 73  ? 112.842 116.849 171.474 1.00 108.29 ? 73  PRO B CD    1 
ATOM   4804 N  N     . ALA B 2 74  ? 111.210 121.200 172.371 1.00 111.93 ? 74  ALA B N     1 
ATOM   4805 C  CA    . ALA B 2 74  ? 111.532 122.614 172.232 1.00 116.67 ? 74  ALA B CA    1 
ATOM   4806 C  C     . ALA B 2 74  ? 112.511 123.107 173.288 1.00 117.99 ? 74  ALA B C     1 
ATOM   4807 O  O     . ALA B 2 74  ? 113.142 124.151 173.088 1.00 113.55 ? 74  ALA B O     1 
ATOM   4808 C  CB    . ALA B 2 74  ? 110.254 123.451 172.287 1.00 110.48 ? 74  ALA B CB    1 
ATOM   4809 N  N     . GLY B 2 75  ? 112.657 122.388 174.399 1.00 117.34 ? 75  GLY B N     1 
ATOM   4810 C  CA    . GLY B 2 75  ? 113.552 122.819 175.456 1.00 120.16 ? 75  GLY B CA    1 
ATOM   4811 C  C     . GLY B 2 75  ? 115.023 122.609 175.182 1.00 123.10 ? 75  GLY B C     1 
ATOM   4812 O  O     . GLY B 2 75  ? 115.857 123.084 175.959 1.00 120.15 ? 75  GLY B O     1 
ATOM   4813 N  N     . LEU B 2 76  ? 115.363 121.913 174.103 1.00 124.01 ? 76  LEU B N     1 
ATOM   4814 C  CA    . LEU B 2 76  ? 116.746 121.616 173.766 1.00 122.81 ? 76  LEU B CA    1 
ATOM   4815 C  C     . LEU B 2 76  ? 117.209 122.478 172.599 1.00 122.39 ? 76  LEU B C     1 
ATOM   4816 O  O     . LEU B 2 76  ? 116.424 122.840 171.719 1.00 121.92 ? 76  LEU B O     1 
ATOM   4817 C  CB    . LEU B 2 76  ? 116.913 120.138 173.412 1.00 120.68 ? 76  LEU B CB    1 
ATOM   4818 C  CG    . LEU B 2 76  ? 116.409 119.120 174.436 1.00 122.79 ? 76  LEU B CG    1 
ATOM   4819 C  CD1   . LEU B 2 76  ? 116.793 117.710 174.018 1.00 121.93 ? 76  LEU B CD1   1 
ATOM   4820 C  CD2   . LEU B 2 76  ? 116.945 119.438 175.823 1.00 119.66 ? 76  LEU B CD2   1 
ATOM   4821 N  N     . THR B 2 77  ? 118.497 122.811 172.605 1.00 121.73 ? 77  THR B N     1 
ATOM   4822 C  CA    . THR B 2 77  ? 119.116 123.506 171.490 1.00 121.90 ? 77  THR B CA    1 
ATOM   4823 C  C     . THR B 2 77  ? 119.614 122.484 170.469 1.00 121.68 ? 77  THR B C     1 
ATOM   4824 O  O     . THR B 2 77  ? 119.487 121.272 170.655 1.00 121.21 ? 77  THR B O     1 
ATOM   4825 C  CB    . THR B 2 77  ? 120.251 124.403 171.976 1.00 119.22 ? 77  THR B CB    1 
ATOM   4826 O  OG1   . THR B 2 77  ? 121.397 123.602 172.290 1.00 121.24 ? 77  THR B OG1   1 
ATOM   4827 C  CG2   . THR B 2 77  ? 119.824 125.173 173.215 1.00 116.26 ? 77  THR B CG2   1 
ATOM   4828 N  N     . LYS B 2 78  ? 120.185 122.978 169.367 1.00 118.04 ? 78  LYS B N     1 
ATOM   4829 C  CA    . LYS B 2 78  ? 120.673 122.074 168.331 1.00 117.22 ? 78  LYS B CA    1 
ATOM   4830 C  C     . LYS B 2 78  ? 121.806 121.197 168.850 1.00 118.48 ? 78  LYS B C     1 
ATOM   4831 O  O     . LYS B 2 78  ? 121.822 119.985 168.609 1.00 118.31 ? 78  LYS B O     1 
ATOM   4832 C  CB    . LYS B 2 78  ? 121.128 122.868 167.107 1.00 112.88 ? 78  LYS B CB    1 
ATOM   4833 C  CG    . LYS B 2 78  ? 121.597 121.992 165.960 1.00 103.74 ? 78  LYS B CG    1 
ATOM   4834 C  CD    . LYS B 2 78  ? 122.297 122.798 164.885 1.00 97.38  ? 78  LYS B CD    1 
ATOM   4835 C  CE    . LYS B 2 78  ? 122.928 121.881 163.854 1.00 91.29  ? 78  LYS B CE    1 
ATOM   4836 N  NZ    . LYS B 2 78  ? 123.884 122.599 162.969 1.00 89.30  ? 78  LYS B NZ    1 
ATOM   4837 N  N     . GLU B 2 79  ? 122.761 121.792 169.570 1.00 116.64 ? 79  GLU B N     1 
ATOM   4838 C  CA    . GLU B 2 79  ? 123.842 121.004 170.153 1.00 117.39 ? 79  GLU B CA    1 
ATOM   4839 C  C     . GLU B 2 79  ? 123.310 120.032 171.198 1.00 119.20 ? 79  GLU B C     1 
ATOM   4840 O  O     . GLU B 2 79  ? 123.751 118.879 171.267 1.00 118.36 ? 79  GLU B O     1 
ATOM   4841 C  CB    . GLU B 2 79  ? 124.894 121.928 170.764 1.00 124.83 ? 79  GLU B CB    1 
ATOM   4842 C  CG    . GLU B 2 79  ? 126.096 122.173 169.870 1.00 128.92 ? 79  GLU B CG    1 
ATOM   4843 C  CD    . GLU B 2 79  ? 125.998 123.478 169.104 1.00 131.47 ? 79  GLU B CD    1 
ATOM   4844 O  OE1   . GLU B 2 79  ? 124.865 123.922 168.825 1.00 127.48 ? 79  GLU B OE1   1 
ATOM   4845 O  OE2   . GLU B 2 79  ? 127.056 124.059 168.782 1.00 131.38 ? 79  GLU B OE2   1 
ATOM   4846 N  N     . GLN B 2 80  ? 122.360 120.481 172.021 1.00 121.21 ? 80  GLN B N     1 
ATOM   4847 C  CA    . GLN B 2 80  ? 121.757 119.592 173.008 1.00 121.72 ? 80  GLN B CA    1 
ATOM   4848 C  C     . GLN B 2 80  ? 120.979 118.469 172.335 1.00 118.93 ? 80  GLN B C     1 
ATOM   4849 O  O     . GLN B 2 80  ? 121.000 117.326 172.804 1.00 114.85 ? 80  GLN B O     1 
ATOM   4850 C  CB    . GLN B 2 80  ? 120.858 120.391 173.950 1.00 120.55 ? 80  GLN B CB    1 
ATOM   4851 C  CG    . GLN B 2 80  ? 121.617 121.373 174.828 1.00 119.10 ? 80  GLN B CG    1 
ATOM   4852 C  CD    . GLN B 2 80  ? 120.706 122.358 175.531 1.00 122.40 ? 80  GLN B CD    1 
ATOM   4853 O  OE1   . GLN B 2 80  ? 119.518 122.449 175.224 1.00 122.87 ? 80  GLN B OE1   1 
ATOM   4854 N  NE2   . GLN B 2 80  ? 121.261 123.105 176.477 1.00 122.25 ? 80  GLN B NE2   1 
ATOM   4855 N  N     . ALA B 2 81  ? 120.284 118.773 171.236 1.00 119.40 ? 81  ALA B N     1 
ATOM   4856 C  CA    . ALA B 2 81  ? 119.572 117.732 170.500 1.00 117.69 ? 81  ALA B CA    1 
ATOM   4857 C  C     . ALA B 2 81  ? 120.539 116.714 169.909 1.00 116.79 ? 81  ALA B C     1 
ATOM   4858 O  O     . ALA B 2 81  ? 120.276 115.506 169.939 1.00 114.78 ? 81  ALA B O     1 
ATOM   4859 C  CB    . ALA B 2 81  ? 118.713 118.359 169.404 1.00 114.24 ? 81  ALA B CB    1 
ATOM   4860 N  N     . VAL B 2 82  ? 121.665 117.183 169.364 1.00 117.54 ? 82  VAL B N     1 
ATOM   4861 C  CA    . VAL B 2 82  ? 122.667 116.268 168.823 1.00 114.93 ? 82  VAL B CA    1 
ATOM   4862 C  C     . VAL B 2 82  ? 123.246 115.396 169.930 1.00 117.65 ? 82  VAL B C     1 
ATOM   4863 O  O     . VAL B 2 82  ? 123.450 114.189 169.749 1.00 116.21 ? 82  VAL B O     1 
ATOM   4864 C  CB    . VAL B 2 82  ? 123.765 117.057 168.084 1.00 111.25 ? 82  VAL B CB    1 
ATOM   4865 C  CG1   . VAL B 2 82  ? 124.963 116.167 167.794 1.00 107.51 ? 82  VAL B CG1   1 
ATOM   4866 C  CG2   . VAL B 2 82  ? 123.215 117.645 166.795 1.00 101.27 ? 82  VAL B CG2   1 
ATOM   4867 N  N     . GLU B 2 83  ? 123.522 115.992 171.093 1.00 119.10 ? 83  GLU B N     1 
ATOM   4868 C  CA    . GLU B 2 83  ? 124.034 115.219 172.220 1.00 116.77 ? 83  GLU B CA    1 
ATOM   4869 C  C     . GLU B 2 83  ? 123.026 114.168 172.669 1.00 117.72 ? 83  GLU B C     1 
ATOM   4870 O  O     . GLU B 2 83  ? 123.395 113.022 172.951 1.00 119.44 ? 83  GLU B O     1 
ATOM   4871 C  CB    . GLU B 2 83  ? 124.390 116.159 173.374 1.00 118.82 ? 83  GLU B CB    1 
ATOM   4872 C  CG    . GLU B 2 83  ? 125.416 115.615 174.362 1.00 121.27 ? 83  GLU B CG    1 
ATOM   4873 C  CD    . GLU B 2 83  ? 124.890 114.454 175.185 1.00 121.23 ? 83  GLU B CD    1 
ATOM   4874 O  OE1   . GLU B 2 83  ? 123.984 114.676 176.016 1.00 120.08 ? 83  GLU B OE1   1 
ATOM   4875 O  OE2   . GLU B 2 83  ? 125.382 113.321 175.002 1.00 120.17 ? 83  GLU B OE2   1 
ATOM   4876 N  N     . ALA B 2 84  ? 121.745 114.540 172.738 1.00 117.65 ? 84  ALA B N     1 
ATOM   4877 C  CA    . ALA B 2 84  ? 120.714 113.582 173.122 1.00 119.85 ? 84  ALA B CA    1 
ATOM   4878 C  C     . ALA B 2 84  ? 120.609 112.449 172.110 1.00 121.32 ? 84  ALA B C     1 
ATOM   4879 O  O     . ALA B 2 84  ? 120.436 111.284 172.486 1.00 121.06 ? 84  ALA B O     1 
ATOM   4880 C  CB    . ALA B 2 84  ? 119.370 114.293 173.276 1.00 120.67 ? 84  ALA B CB    1 
ATOM   4881 N  N     . ALA B 2 85  ? 120.704 112.773 170.818 1.00 120.73 ? 85  ALA B N     1 
ATOM   4882 C  CA    . ALA B 2 85  ? 120.658 111.738 169.791 1.00 119.84 ? 85  ALA B CA    1 
ATOM   4883 C  C     . ALA B 2 85  ? 121.857 110.804 169.894 1.00 119.01 ? 85  ALA B C     1 
ATOM   4884 O  O     . ALA B 2 85  ? 121.729 109.592 169.687 1.00 119.17 ? 85  ALA B O     1 
ATOM   4885 C  CB    . ALA B 2 85  ? 120.586 112.376 168.405 1.00 114.35 ? 85  ALA B CB    1 
ATOM   4886 N  N     . ARG B 2 86  ? 123.036 111.351 170.203 1.00 117.55 ? 86  ARG B N     1 
ATOM   4887 C  CA    . ARG B 2 86  ? 124.206 110.504 170.416 1.00 115.72 ? 86  ARG B CA    1 
ATOM   4888 C  C     . ARG B 2 86  ? 124.014 109.600 171.626 1.00 118.79 ? 86  ARG B C     1 
ATOM   4889 O  O     . ARG B 2 86  ? 124.403 108.426 171.602 1.00 115.93 ? 86  ARG B O     1 
ATOM   4890 C  CB    . ARG B 2 86  ? 125.461 111.360 170.585 1.00 109.71 ? 86  ARG B CB    1 
ATOM   4891 C  CG    . ARG B 2 86  ? 125.900 112.061 169.320 1.00 107.80 ? 86  ARG B CG    1 
ATOM   4892 C  CD    . ARG B 2 86  ? 127.345 112.516 169.385 1.00 110.20 ? 86  ARG B CD    1 
ATOM   4893 N  NE    . ARG B 2 86  ? 127.667 113.446 168.309 1.00 111.59 ? 86  ARG B NE    1 
ATOM   4894 C  CZ    . ARG B 2 86  ? 127.791 113.110 167.032 1.00 107.49 ? 86  ARG B CZ    1 
ATOM   4895 N  NH1   . ARG B 2 86  ? 127.632 111.861 166.626 1.00 103.40 ? 86  ARG B NH1   1 
ATOM   4896 N  NH2   . ARG B 2 86  ? 128.083 114.051 166.139 1.00 101.69 ? 86  ARG B NH2   1 
ATOM   4897 N  N     . ALA B 2 87  ? 123.418 110.132 172.696 1.00 122.25 ? 87  ALA B N     1 
ATOM   4898 C  CA    . ALA B 2 87  ? 123.132 109.316 173.871 1.00 121.68 ? 87  ALA B CA    1 
ATOM   4899 C  C     . ALA B 2 87  ? 122.148 108.199 173.551 1.00 125.58 ? 87  ALA B C     1 
ATOM   4900 O  O     . ALA B 2 87  ? 122.149 107.160 174.220 1.00 124.93 ? 87  ALA B O     1 
ATOM   4901 C  CB    . ALA B 2 87  ? 122.595 110.192 175.002 1.00 116.56 ? 87  ALA B CB    1 
ATOM   4902 N  N     . ARG B 2 88  ? 121.305 108.392 172.541 1.00 126.71 ? 88  ARG B N     1 
ATOM   4903 C  CA    . ARG B 2 88  ? 120.398 107.349 172.083 1.00 124.85 ? 88  ARG B CA    1 
ATOM   4904 C  C     . ARG B 2 88  ? 121.159 106.385 171.174 1.00 127.28 ? 88  ARG B C     1 
ATOM   4905 O  O     . ARG B 2 88  ? 122.391 106.398 171.102 1.00 127.91 ? 88  ARG B O     1 
ATOM   4906 C  CB    . ARG B 2 88  ? 119.184 107.963 171.393 1.00 124.25 ? 88  ARG B CB    1 
ATOM   4907 C  CG    . ARG B 2 88  ? 118.152 108.532 172.354 1.00 128.22 ? 88  ARG B CG    1 
ATOM   4908 C  CD    . ARG B 2 88  ? 116.961 109.116 171.612 1.00 128.37 ? 88  ARG B CD    1 
ATOM   4909 N  NE    . ARG B 2 88  ? 117.288 110.370 170.944 1.00 126.51 ? 88  ARG B NE    1 
ATOM   4910 C  CZ    . ARG B 2 88  ? 116.635 110.850 169.895 1.00 124.44 ? 88  ARG B CZ    1 
ATOM   4911 N  NH1   . ARG B 2 88  ? 115.616 110.199 169.359 1.00 120.91 ? 88  ARG B NH1   1 
ATOM   4912 N  NH2   . ARG B 2 88  ? 117.013 112.012 169.371 1.00 121.36 ? 88  ARG B NH2   1 
ATOM   4913 N  N     . GLY B 2 89  ? 120.426 105.529 170.466 1.00 127.39 ? 89  GLY B N     1 
ATOM   4914 C  CA    . GLY B 2 89  ? 121.050 104.473 169.703 1.00 125.22 ? 89  GLY B CA    1 
ATOM   4915 C  C     . GLY B 2 89  ? 121.331 104.824 168.250 1.00 127.39 ? 89  GLY B C     1 
ATOM   4916 O  O     . GLY B 2 89  ? 120.840 105.818 167.715 1.00 126.33 ? 89  GLY B O     1 
ATOM   4917 N  N     . ASP B 2 90  ? 122.172 103.982 167.644 1.00 128.44 ? 90  ASP B N     1 
ATOM   4918 C  CA    . ASP B 2 90  ? 122.465 103.929 166.214 1.00 128.69 ? 90  ASP B CA    1 
ATOM   4919 C  C     . ASP B 2 90  ? 123.341 105.080 165.729 1.00 123.14 ? 90  ASP B C     1 
ATOM   4920 O  O     . ASP B 2 90  ? 123.844 105.040 164.601 1.00 120.75 ? 90  ASP B O     1 
ATOM   4921 C  CB    . ASP B 2 90  ? 121.165 103.890 165.404 1.00 128.08 ? 90  ASP B CB    1 
ATOM   4922 C  CG    . ASP B 2 90  ? 120.192 102.840 165.910 1.00 127.56 ? 90  ASP B CG    1 
ATOM   4923 O  OD1   . ASP B 2 90  ? 120.649 101.765 166.352 1.00 128.46 ? 90  ASP B OD1   1 
ATOM   4924 O  OD2   . ASP B 2 90  ? 118.969 103.092 165.869 1.00 124.66 ? 90  ASP B OD2   1 
ATOM   4925 N  N     . GLY B 2 91  ? 123.538 106.105 166.555 1.00 119.34 ? 91  GLY B N     1 
ATOM   4926 C  CA    . GLY B 2 91  ? 124.625 107.044 166.347 1.00 112.89 ? 91  GLY B CA    1 
ATOM   4927 C  C     . GLY B 2 91  ? 124.483 108.024 165.197 1.00 103.98 ? 91  GLY B C     1 
ATOM   4928 O  O     . GLY B 2 91  ? 124.990 109.147 165.270 1.00 99.24  ? 91  GLY B O     1 
ATOM   4929 N  N     . THR B 2 92  ? 123.801 107.612 164.127 1.00 103.99 ? 92  THR B N     1 
ATOM   4930 C  CA    . THR B 2 92  ? 123.852 108.329 162.858 1.00 97.86  ? 92  THR B CA    1 
ATOM   4931 C  C     . THR B 2 92  ? 122.820 109.442 162.737 1.00 97.03  ? 92  THR B C     1 
ATOM   4932 O  O     . THR B 2 92  ? 123.013 110.359 161.927 1.00 91.41  ? 92  THR B O     1 
ATOM   4933 C  CB    . THR B 2 92  ? 123.669 107.350 161.696 1.00 93.82  ? 92  THR B CB    1 
ATOM   4934 O  OG1   . THR B 2 92  ? 123.559 108.077 160.467 1.00 86.34  ? 92  THR B OG1   1 
ATOM   4935 C  CG2   . THR B 2 92  ? 122.419 106.510 161.907 1.00 90.96  ? 92  THR B CG2   1 
ATOM   4936 N  N     . PHE B 2 93  ? 121.732 109.385 163.506 1.00 99.42  ? 93  PHE B N     1 
ATOM   4937 C  CA    . PHE B 2 93  ? 120.763 110.473 163.470 1.00 94.76  ? 93  PHE B CA    1 
ATOM   4938 C  C     . PHE B 2 93  ? 121.387 111.779 163.937 1.00 94.20  ? 93  PHE B C     1 
ATOM   4939 O  O     . PHE B 2 93  ? 121.075 112.842 163.395 1.00 92.61  ? 93  PHE B O     1 
ATOM   4940 C  CB    . PHE B 2 93  ? 119.543 110.132 164.322 1.00 95.43  ? 93  PHE B CB    1 
ATOM   4941 C  CG    . PHE B 2 93  ? 118.389 111.073 164.125 1.00 97.07  ? 93  PHE B CG    1 
ATOM   4942 C  CD1   . PHE B 2 93  ? 117.960 111.406 162.852 1.00 88.61  ? 93  PHE B CD1   1 
ATOM   4943 C  CD2   . PHE B 2 93  ? 117.736 111.629 165.212 1.00 100.42 ? 93  PHE B CD2   1 
ATOM   4944 C  CE1   . PHE B 2 93  ? 116.901 112.271 162.667 1.00 87.62  ? 93  PHE B CE1   1 
ATOM   4945 C  CE2   . PHE B 2 93  ? 116.677 112.495 165.033 1.00 97.90  ? 93  PHE B CE2   1 
ATOM   4946 C  CZ    . PHE B 2 93  ? 116.259 112.816 163.758 1.00 92.42  ? 93  PHE B CZ    1 
ATOM   4947 N  N     . ALA B 2 94  ? 122.271 111.720 164.934 1.00 91.81  ? 94  ALA B N     1 
ATOM   4948 C  CA    . ALA B 2 94  ? 122.959 112.924 165.386 1.00 91.41  ? 94  ALA B CA    1 
ATOM   4949 C  C     . ALA B 2 94  ? 123.880 113.482 164.307 1.00 89.45  ? 94  ALA B C     1 
ATOM   4950 O  O     . ALA B 2 94  ? 123.961 114.702 164.124 1.00 87.44  ? 94  ALA B O     1 
ATOM   4951 C  CB    . ALA B 2 94  ? 123.747 112.628 166.657 1.00 100.19 ? 94  ALA B CB    1 
ATOM   4952 N  N     . ASP B 2 95  ? 124.597 112.608 163.597 1.00 92.68  ? 95  ASP B N     1 
ATOM   4953 C  CA    . ASP B 2 95  ? 125.453 113.072 162.510 1.00 90.63  ? 95  ASP B CA    1 
ATOM   4954 C  C     . ASP B 2 95  ? 124.627 113.714 161.405 1.00 85.30  ? 95  ASP B C     1 
ATOM   4955 O  O     . ASP B 2 95  ? 125.039 114.717 160.811 1.00 82.92  ? 95  ASP B O     1 
ATOM   4956 C  CB    . ASP B 2 95  ? 126.280 111.911 161.961 1.00 88.30  ? 95  ASP B CB    1 
ATOM   4957 C  CG    . ASP B 2 95  ? 127.448 111.556 162.856 1.00 96.42  ? 95  ASP B CG    1 
ATOM   4958 O  OD1   . ASP B 2 95  ? 127.742 112.337 163.785 1.00 96.87  ? 95  ASP B OD1   1 
ATOM   4959 O  OD2   . ASP B 2 95  ? 128.072 110.497 162.634 1.00 98.11  ? 95  ASP B OD2   1 
ATOM   4960 N  N     . LEU B 2 96  ? 123.459 113.142 161.112 1.00 82.69  ? 96  LEU B N     1 
ATOM   4961 C  CA    . LEU B 2 96  ? 122.544 113.763 160.160 1.00 76.61  ? 96  LEU B CA    1 
ATOM   4962 C  C     . LEU B 2 96  ? 122.064 115.122 160.661 1.00 77.18  ? 96  LEU B C     1 
ATOM   4963 O  O     . LEU B 2 96  ? 121.973 116.082 159.887 1.00 75.32  ? 96  LEU B O     1 
ATOM   4964 C  CB    . LEU B 2 96  ? 121.361 112.829 159.902 1.00 77.67  ? 96  LEU B CB    1 
ATOM   4965 C  CG    . LEU B 2 96  ? 120.203 113.339 159.046 1.00 69.87  ? 96  LEU B CG    1 
ATOM   4966 C  CD1   . LEU B 2 96  ? 120.561 113.346 157.572 1.00 63.49  ? 96  LEU B CD1   1 
ATOM   4967 C  CD2   . LEU B 2 96  ? 118.950 112.518 159.295 1.00 71.94  ? 96  LEU B CD2   1 
ATOM   4968 N  N     . LEU B 2 97  ? 121.758 115.221 161.957 1.00 81.02  ? 97  LEU B N     1 
ATOM   4969 C  CA    . LEU B 2 97  ? 121.252 116.465 162.529 1.00 82.64  ? 97  LEU B CA    1 
ATOM   4970 C  C     . LEU B 2 97  ? 122.317 117.551 162.576 1.00 88.27  ? 97  LEU B C     1 
ATOM   4971 O  O     . LEU B 2 97  ? 121.984 118.741 162.573 1.00 88.49  ? 97  LEU B O     1 
ATOM   4972 C  CB    . LEU B 2 97  ? 120.720 116.210 163.938 1.00 81.39  ? 97  LEU B CB    1 
ATOM   4973 C  CG    . LEU B 2 97  ? 119.346 115.560 164.068 1.00 82.94  ? 97  LEU B CG    1 
ATOM   4974 C  CD1   . LEU B 2 97  ? 118.912 115.526 165.523 1.00 89.56  ? 97  LEU B CD1   1 
ATOM   4975 C  CD2   . LEU B 2 97  ? 118.343 116.310 163.226 1.00 77.36  ? 97  LEU B CD2   1 
ATOM   4976 N  N     . SER B 2 98  ? 123.592 117.161 162.639 1.00 87.53  ? 98  SER B N     1 
ATOM   4977 C  CA    . SER B 2 98  ? 124.661 118.136 162.835 1.00 86.03  ? 98  SER B CA    1 
ATOM   4978 C  C     . SER B 2 98  ? 124.701 119.164 161.710 1.00 86.61  ? 98  SER B C     1 
ATOM   4979 O  O     . SER B 2 98  ? 124.935 120.353 161.956 1.00 85.81  ? 98  SER B O     1 
ATOM   4980 C  CB    . SER B 2 98  ? 126.004 117.418 162.954 1.00 85.16  ? 98  SER B CB    1 
ATOM   4981 O  OG    . SER B 2 98  ? 127.047 118.334 163.233 1.00 93.95  ? 98  SER B OG    1 
ATOM   4982 N  N     . GLY B 2 99  ? 124.489 118.730 160.473 1.00 83.74  ? 99  GLY B N     1 
ATOM   4983 C  CA    . GLY B 2 99  ? 124.500 119.638 159.347 1.00 82.10  ? 99  GLY B CA    1 
ATOM   4984 C  C     . GLY B 2 99  ? 123.176 120.271 158.993 1.00 81.59  ? 99  GLY B C     1 
ATOM   4985 O  O     . GLY B 2 99  ? 123.109 121.038 158.028 1.00 80.42  ? 99  GLY B O     1 
ATOM   4986 N  N     . MET B 2 100 ? 122.113 119.986 159.748 1.00 82.43  ? 100 MET B N     1 
ATOM   4987 C  CA    . MET B 2 100 ? 120.792 120.496 159.389 1.00 79.51  ? 100 MET B CA    1 
ATOM   4988 C  C     . MET B 2 100 ? 120.638 121.972 159.736 1.00 82.89  ? 100 MET B C     1 
ATOM   4989 O  O     . MET B 2 100 ? 119.968 122.715 159.009 1.00 83.62  ? 100 MET B O     1 
ATOM   4990 C  CB    . MET B 2 100 ? 119.706 119.672 160.078 1.00 76.05  ? 100 MET B CB    1 
ATOM   4991 C  CG    . MET B 2 100 ? 118.582 119.248 159.156 1.00 72.75  ? 100 MET B CG    1 
ATOM   4992 S  SD    . MET B 2 100 ? 117.813 117.699 159.631 1.00 86.08  ? 100 MET B SD    1 
ATOM   4993 C  CE    . MET B 2 100 ? 118.935 116.557 158.854 1.00 69.59  ? 100 MET B CE    1 
ATOM   4994 N  N     . ASP B 2 101 ? 121.244 122.412 160.840 1.00 88.06  ? 101 ASP B N     1 
ATOM   4995 C  CA    . ASP B 2 101 ? 121.047 123.763 161.371 1.00 96.03  ? 101 ASP B CA    1 
ATOM   4996 C  C     . ASP B 2 101 ? 119.564 124.026 161.637 1.00 88.40  ? 101 ASP B C     1 
ATOM   4997 O  O     . ASP B 2 101 ? 118.955 124.940 161.075 1.00 80.88  ? 101 ASP B O     1 
ATOM   4998 C  CB    . ASP B 2 101 ? 121.644 124.825 160.441 1.00 98.57  ? 101 ASP B CB    1 
ATOM   4999 C  CG    . ASP B 2 101 ? 121.936 126.131 161.159 1.00 101.95 ? 101 ASP B CG    1 
ATOM   5000 O  OD1   . ASP B 2 101 ? 121.802 126.172 162.400 1.00 97.94  ? 101 ASP B OD1   1 
ATOM   5001 O  OD2   . ASP B 2 101 ? 122.304 127.115 160.482 1.00 98.47  ? 101 ASP B OD2   1 
ATOM   5002 N  N     . ILE B 2 102 ? 118.983 123.200 162.503 1.00 88.84  ? 102 ILE B N     1 
ATOM   5003 C  CA    . ILE B 2 102 ? 117.569 123.279 162.831 1.00 85.08  ? 102 ILE B CA    1 
ATOM   5004 C  C     . ILE B 2 102 ? 117.391 123.965 164.179 1.00 91.96  ? 102 ILE B C     1 
ATOM   5005 O  O     . ILE B 2 102 ? 118.312 124.046 164.996 1.00 99.20  ? 102 ILE B O     1 
ATOM   5006 C  CB    . ILE B 2 102 ? 116.921 121.882 162.841 1.00 83.80  ? 102 ILE B CB    1 
ATOM   5007 C  CG1   . ILE B 2 102 ? 117.808 120.896 163.598 1.00 84.92  ? 102 ILE B CG1   1 
ATOM   5008 C  CG2   . ILE B 2 102 ? 116.685 121.395 161.432 1.00 80.69  ? 102 ILE B CG2   1 
ATOM   5009 C  CD1   . ILE B 2 102 ? 117.053 119.744 164.205 1.00 78.22  ? 102 ILE B CD1   1 
ATOM   5010 N  N     . VAL B 2 103 ? 116.183 124.467 164.412 1.00 91.73  ? 103 VAL B N     1 
ATOM   5011 C  CA    . VAL B 2 103 ? 115.801 125.026 165.706 1.00 99.38  ? 103 VAL B CA    1 
ATOM   5012 C  C     . VAL B 2 103 ? 114.659 124.178 166.254 1.00 100.46 ? 103 VAL B C     1 
ATOM   5013 O  O     . VAL B 2 103 ? 113.541 124.234 165.722 1.00 101.98 ? 103 VAL B O     1 
ATOM   5014 C  CB    . VAL B 2 103 ? 115.398 126.504 165.585 1.00 98.00  ? 103 VAL B CB    1 
ATOM   5015 C  CG1   . VAL B 2 103 ? 115.291 127.136 166.964 1.00 93.98  ? 103 VAL B CG1   1 
ATOM   5016 C  CG2   . VAL B 2 103 ? 116.392 127.258 164.720 1.00 95.16  ? 103 VAL B CG2   1 
ATOM   5017 N  N     . PRO B 2 104 ? 114.891 123.377 167.293 1.00 104.28 ? 104 PRO B N     1 
ATOM   5018 C  CA    . PRO B 2 104 ? 113.858 122.437 167.746 1.00 104.64 ? 104 PRO B CA    1 
ATOM   5019 C  C     . PRO B 2 104 ? 112.585 123.148 168.182 1.00 105.06 ? 104 PRO B C     1 
ATOM   5020 O  O     . PRO B 2 104 ? 112.623 124.219 168.792 1.00 104.91 ? 104 PRO B O     1 
ATOM   5021 C  CB    . PRO B 2 104 ? 114.529 121.717 168.921 1.00 106.58 ? 104 PRO B CB    1 
ATOM   5022 C  CG    . PRO B 2 104 ? 115.993 121.876 168.676 1.00 108.67 ? 104 PRO B CG    1 
ATOM   5023 C  CD    . PRO B 2 104 ? 116.142 123.230 168.053 1.00 105.91 ? 104 PRO B CD    1 
ATOM   5024 N  N     . GLY B 2 105 ? 111.448 122.535 167.858 1.00 103.64 ? 105 GLY B N     1 
ATOM   5025 C  CA    . GLY B 2 105 ? 110.156 123.074 168.227 1.00 99.41  ? 105 GLY B CA    1 
ATOM   5026 C  C     . GLY B 2 105 ? 109.677 124.245 167.400 1.00 99.47  ? 105 GLY B C     1 
ATOM   5027 O  O     . GLY B 2 105 ? 108.760 124.951 167.835 1.00 97.24  ? 105 GLY B O     1 
ATOM   5028 N  N     . GLN B 2 106 ? 110.264 124.483 166.228 1.00 94.97  ? 106 GLN B N     1 
ATOM   5029 C  CA    . GLN B 2 106 ? 109.873 125.625 165.410 1.00 93.27  ? 106 GLN B CA    1 
ATOM   5030 C  C     . GLN B 2 106 ? 108.869 125.250 164.326 1.00 90.58  ? 106 GLN B C     1 
ATOM   5031 O  O     . GLN B 2 106 ? 107.854 125.932 164.156 1.00 87.97  ? 106 GLN B O     1 
ATOM   5032 C  CB    . GLN B 2 106 ? 111.111 126.269 164.780 1.00 92.52  ? 106 GLN B CB    1 
ATOM   5033 C  CG    . GLN B 2 106 ? 111.874 127.178 165.723 1.00 98.55  ? 106 GLN B CG    1 
ATOM   5034 C  CD    . GLN B 2 106 ? 111.055 128.370 166.174 1.00 101.32 ? 106 GLN B CD    1 
ATOM   5035 O  OE1   . GLN B 2 106 ? 110.315 128.963 165.389 1.00 96.46  ? 106 GLN B OE1   1 
ATOM   5036 N  NE2   . GLN B 2 106 ? 111.182 128.728 167.446 1.00 101.07 ? 106 GLN B NE2   1 
ATOM   5037 N  N     . GLY B 2 107 ? 109.132 124.178 163.590 1.00 82.95  ? 107 GLY B N     1 
ATOM   5038 C  CA    . GLY B 2 107 ? 108.281 123.817 162.480 1.00 74.67  ? 107 GLY B CA    1 
ATOM   5039 C  C     . GLY B 2 107 ? 108.655 124.560 161.211 1.00 72.63  ? 107 GLY B C     1 
ATOM   5040 O  O     . GLY B 2 107 ? 109.639 125.301 161.144 1.00 72.65  ? 107 GLY B O     1 
ATOM   5041 N  N     . VAL B 2 108 ? 107.841 124.349 160.184 1.00 69.60  ? 108 VAL B N     1 
ATOM   5042 C  CA    . VAL B 2 108 ? 108.111 124.916 158.868 1.00 66.05  ? 108 VAL B CA    1 
ATOM   5043 C  C     . VAL B 2 108 ? 107.611 126.353 158.823 1.00 65.61  ? 108 VAL B C     1 
ATOM   5044 O  O     . VAL B 2 108 ? 106.448 126.631 159.140 1.00 66.25  ? 108 VAL B O     1 
ATOM   5045 C  CB    . VAL B 2 108 ? 107.459 124.069 157.765 1.00 64.75  ? 108 VAL B CB    1 
ATOM   5046 C  CG1   . VAL B 2 108 ? 107.706 124.695 156.405 1.00 59.63  ? 108 VAL B CG1   1 
ATOM   5047 C  CG2   . VAL B 2 108 ? 107.991 122.650 157.803 1.00 64.97  ? 108 VAL B CG2   1 
ATOM   5048 N  N     . ASP B 2 109 ? 108.491 127.270 158.427 1.00 66.59  ? 109 ASP B N     1 
ATOM   5049 C  CA    . ASP B 2 109 ? 108.126 128.667 158.198 1.00 66.86  ? 109 ASP B CA    1 
ATOM   5050 C  C     . ASP B 2 109 ? 107.715 128.799 156.737 1.00 63.92  ? 109 ASP B C     1 
ATOM   5051 O  O     . ASP B 2 109 ? 108.562 128.916 155.850 1.00 64.09  ? 109 ASP B O     1 
ATOM   5052 C  CB    . ASP B 2 109 ? 109.288 129.592 158.539 1.00 66.05  ? 109 ASP B CB    1 
ATOM   5053 C  CG    . ASP B 2 109 ? 108.908 131.059 158.468 1.00 72.11  ? 109 ASP B CG    1 
ATOM   5054 O  OD1   . ASP B 2 109 ? 107.709 131.363 158.296 1.00 69.66  ? 109 ASP B OD1   1 
ATOM   5055 O  OD2   . ASP B 2 109 ? 109.814 131.911 158.581 1.00 77.40  ? 109 ASP B OD2   1 
ATOM   5056 N  N     . PHE B 2 110 ? 106.405 128.781 156.485 1.00 60.58  ? 110 PHE B N     1 
ATOM   5057 C  CA    . PHE B 2 110 ? 105.922 128.797 155.110 1.00 56.84  ? 110 PHE B CA    1 
ATOM   5058 C  C     . PHE B 2 110 ? 106.077 130.160 154.450 1.00 57.36  ? 110 PHE B C     1 
ATOM   5059 O  O     . PHE B 2 110 ? 106.012 130.245 153.221 1.00 57.05  ? 110 PHE B O     1 
ATOM   5060 C  CB    . PHE B 2 110 ? 104.463 128.348 155.060 1.00 55.96  ? 110 PHE B CB    1 
ATOM   5061 C  CG    . PHE B 2 110 ? 104.298 126.868 154.888 1.00 56.23  ? 110 PHE B CG    1 
ATOM   5062 C  CD1   . PHE B 2 110 ? 104.468 126.280 153.648 1.00 52.06  ? 110 PHE B CD1   1 
ATOM   5063 C  CD2   . PHE B 2 110 ? 103.989 126.063 155.969 1.00 56.38  ? 110 PHE B CD2   1 
ATOM   5064 C  CE1   . PHE B 2 110 ? 104.324 124.919 153.488 1.00 53.79  ? 110 PHE B CE1   1 
ATOM   5065 C  CE2   . PHE B 2 110 ? 103.844 124.701 155.815 1.00 57.27  ? 110 PHE B CE2   1 
ATOM   5066 C  CZ    . PHE B 2 110 ? 104.011 124.128 154.573 1.00 58.65  ? 110 PHE B CZ    1 
ATOM   5067 N  N     . GLY B 2 111 ? 106.281 131.223 155.228 1.00 58.60  ? 111 GLY B N     1 
ATOM   5068 C  CA    . GLY B 2 111 ? 106.552 132.517 154.624 1.00 56.30  ? 111 GLY B CA    1 
ATOM   5069 C  C     . GLY B 2 111 ? 107.863 132.539 153.864 1.00 59.56  ? 111 GLY B C     1 
ATOM   5070 O  O     . GLY B 2 111 ? 107.935 133.047 152.741 1.00 61.02  ? 111 GLY B O     1 
ATOM   5071 N  N     . ALA B 2 112 ? 108.919 131.983 154.463 1.00 57.67  ? 112 ALA B N     1 
ATOM   5072 C  CA    . ALA B 2 112 ? 110.205 131.903 153.779 1.00 53.20  ? 112 ALA B CA    1 
ATOM   5073 C  C     . ALA B 2 112 ? 110.122 131.003 152.553 1.00 49.82  ? 112 ALA B C     1 
ATOM   5074 O  O     . ALA B 2 112 ? 110.707 131.309 151.507 1.00 47.61  ? 112 ALA B O     1 
ATOM   5075 C  CB    . ALA B 2 112 ? 111.281 131.408 154.742 1.00 49.68  ? 112 ALA B CB    1 
ATOM   5076 N  N     . VAL B 2 113 ? 109.391 129.890 152.660 1.00 47.65  ? 113 VAL B N     1 
ATOM   5077 C  CA    . VAL B 2 113 ? 109.202 129.003 151.515 1.00 47.14  ? 113 VAL B CA    1 
ATOM   5078 C  C     . VAL B 2 113 ? 108.493 129.741 150.386 1.00 47.64  ? 113 VAL B C     1 
ATOM   5079 O  O     . VAL B 2 113 ? 108.891 129.659 149.217 1.00 52.33  ? 113 VAL B O     1 
ATOM   5080 C  CB    . VAL B 2 113 ? 108.426 127.742 151.936 1.00 41.06  ? 113 VAL B CB    1 
ATOM   5081 C  CG1   . VAL B 2 113 ? 108.234 126.814 150.750 1.00 38.15  ? 113 VAL B CG1   1 
ATOM   5082 C  CG2   . VAL B 2 113 ? 109.143 127.029 153.065 1.00 46.91  ? 113 VAL B CG2   1 
ATOM   5083 N  N     . GLY B 2 114 ? 107.435 130.480 150.723 1.00 42.93  ? 114 GLY B N     1 
ATOM   5084 C  CA    . GLY B 2 114 ? 106.698 131.206 149.705 1.00 43.32  ? 114 GLY B CA    1 
ATOM   5085 C  C     . GLY B 2 114 ? 107.523 132.293 149.047 1.00 47.09  ? 114 GLY B C     1 
ATOM   5086 O  O     . GLY B 2 114 ? 107.457 132.482 147.831 1.00 50.88  ? 114 GLY B O     1 
ATOM   5087 N  N     . ARG B 2 115 ? 108.308 133.026 149.839 1.00 46.72  ? 115 ARG B N     1 
ATOM   5088 C  CA    . ARG B 2 115 ? 109.156 134.069 149.268 1.00 46.30  ? 115 ARG B CA    1 
ATOM   5089 C  C     . ARG B 2 115 ? 110.228 133.476 148.361 1.00 42.71  ? 115 ARG B C     1 
ATOM   5090 O  O     . ARG B 2 115 ? 110.495 134.004 147.272 1.00 46.23  ? 115 ARG B O     1 
ATOM   5091 C  CB    . ARG B 2 115 ? 109.785 134.896 150.387 1.00 51.03  ? 115 ARG B CB    1 
ATOM   5092 C  CG    . ARG B 2 115 ? 108.797 135.810 151.095 1.00 55.80  ? 115 ARG B CG    1 
ATOM   5093 C  CD    . ARG B 2 115 ? 109.269 136.168 152.492 1.00 65.00  ? 115 ARG B CD    1 
ATOM   5094 N  NE    . ARG B 2 115 ? 110.574 136.816 152.475 1.00 78.73  ? 115 ARG B NE    1 
ATOM   5095 C  CZ    . ARG B 2 115 ? 111.462 136.737 153.457 1.00 82.71  ? 115 ARG B CZ    1 
ATOM   5096 N  NH1   . ARG B 2 115 ? 111.217 136.043 154.556 1.00 71.91  ? 115 ARG B NH1   1 
ATOM   5097 N  NH2   . ARG B 2 115 ? 112.624 137.372 153.332 1.00 79.62  ? 115 ARG B NH2   1 
ATOM   5098 N  N     . THR B 2 116 ? 110.845 132.374 148.790 1.00 39.95  ? 116 THR B N     1 
ATOM   5099 C  CA    . THR B 2 116 ? 111.849 131.711 147.967 1.00 39.21  ? 116 THR B CA    1 
ATOM   5100 C  C     . THR B 2 116 ? 111.245 131.231 146.652 1.00 41.79  ? 116 THR B C     1 
ATOM   5101 O  O     . THR B 2 116 ? 111.844 131.398 145.581 1.00 46.46  ? 116 THR B O     1 
ATOM   5102 C  CB    . THR B 2 116 ? 112.451 130.544 148.749 1.00 39.47  ? 116 THR B CB    1 
ATOM   5103 O  OG1   . THR B 2 116 ? 112.653 130.943 150.110 1.00 45.01  ? 116 THR B OG1   1 
ATOM   5104 C  CG2   . THR B 2 116 ? 113.782 130.144 148.173 1.00 39.25  ? 116 THR B CG2   1 
ATOM   5105 N  N     . LEU B 2 117 ? 110.043 130.653 146.711 1.00 39.71  ? 117 LEU B N     1 
ATOM   5106 C  CA    . LEU B 2 117 ? 109.392 130.177 145.497 1.00 39.60  ? 117 LEU B CA    1 
ATOM   5107 C  C     . LEU B 2 117 ? 108.959 131.325 144.593 1.00 37.78  ? 117 LEU B C     1 
ATOM   5108 O  O     . LEU B 2 117 ? 108.992 131.186 143.368 1.00 42.12  ? 117 LEU B O     1 
ATOM   5109 C  CB    . LEU B 2 117 ? 108.203 129.294 145.859 1.00 38.72  ? 117 LEU B CB    1 
ATOM   5110 C  CG    . LEU B 2 117 ? 108.636 127.957 146.455 1.00 34.34  ? 117 LEU B CG    1 
ATOM   5111 C  CD1   . LEU B 2 117 ? 107.437 127.118 146.803 1.00 36.22  ? 117 LEU B CD1   1 
ATOM   5112 C  CD2   . LEU B 2 117 ? 109.539 127.227 145.483 1.00 37.22  ? 117 LEU B CD2   1 
ATOM   5113 N  N     . ALA B 2 118 ? 108.547 132.456 145.166 1.00 38.42  ? 118 ALA B N     1 
ATOM   5114 C  CA    . ALA B 2 118 ? 108.230 133.621 144.347 1.00 40.89  ? 118 ALA B CA    1 
ATOM   5115 C  C     . ALA B 2 118 ? 109.466 134.131 143.618 1.00 43.48  ? 118 ALA B C     1 
ATOM   5116 O  O     . ALA B 2 118 ? 109.397 134.496 142.436 1.00 43.73  ? 118 ALA B O     1 
ATOM   5117 C  CB    . ALA B 2 118 ? 107.622 134.722 145.213 1.00 36.74  ? 118 ALA B CB    1 
ATOM   5118 N  N     . LEU B 2 119 ? 110.609 134.164 144.309 1.00 40.00  ? 119 LEU B N     1 
ATOM   5119 C  CA    . LEU B 2 119 ? 111.854 134.549 143.651 1.00 40.18  ? 119 LEU B CA    1 
ATOM   5120 C  C     . LEU B 2 119 ? 112.195 133.590 142.516 1.00 42.74  ? 119 LEU B C     1 
ATOM   5121 O  O     . LEU B 2 119 ? 112.581 134.019 141.418 1.00 49.87  ? 119 LEU B O     1 
ATOM   5122 C  CB    . LEU B 2 119 ? 112.989 134.595 144.672 1.00 36.84  ? 119 LEU B CB    1 
ATOM   5123 C  CG    . LEU B 2 119 ? 114.406 134.696 144.113 1.00 39.20  ? 119 LEU B CG    1 
ATOM   5124 C  CD1   . LEU B 2 119 ? 114.647 136.069 143.513 1.00 49.00  ? 119 LEU B CD1   1 
ATOM   5125 C  CD2   . LEU B 2 119 ? 115.423 134.398 145.195 1.00 38.24  ? 119 LEU B CD2   1 
ATOM   5126 N  N     . ALA B 2 120 ? 112.043 132.286 142.762 1.00 40.97  ? 120 ALA B N     1 
ATOM   5127 C  CA    . ALA B 2 120 ? 112.300 131.302 141.716 1.00 39.97  ? 120 ALA B CA    1 
ATOM   5128 C  C     . ALA B 2 120 ? 111.377 131.509 140.523 1.00 42.91  ? 120 ALA B C     1 
ATOM   5129 O  O     . ALA B 2 120 ? 111.814 131.427 139.370 1.00 49.85  ? 120 ALA B O     1 
ATOM   5130 C  CB    . ALA B 2 120 ? 112.139 129.889 142.272 1.00 39.19  ? 120 ALA B CB    1 
ATOM   5131 N  N     . LEU B 2 121 ? 110.096 131.776 140.782 1.00 39.55  ? 121 LEU B N     1 
ATOM   5132 C  CA    . LEU B 2 121 ? 109.135 131.965 139.700 1.00 36.02  ? 121 LEU B CA    1 
ATOM   5133 C  C     . LEU B 2 121 ? 109.473 133.193 138.868 1.00 44.26  ? 121 LEU B C     1 
ATOM   5134 O  O     . LEU B 2 121 ? 109.386 133.161 137.633 1.00 50.61  ? 121 LEU B O     1 
ATOM   5135 C  CB    . LEU B 2 121 ? 107.726 132.076 140.277 1.00 38.03  ? 121 LEU B CB    1 
ATOM   5136 C  CG    . LEU B 2 121 ? 106.558 131.899 139.310 1.00 43.60  ? 121 LEU B CG    1 
ATOM   5137 C  CD1   . LEU B 2 121 ? 106.482 130.464 138.823 1.00 41.65  ? 121 LEU B CD1   1 
ATOM   5138 C  CD2   . LEU B 2 121 ? 105.259 132.308 139.979 1.00 34.46  ? 121 LEU B CD2   1 
ATOM   5139 N  N     . GLY B 2 122 ? 109.857 134.289 139.525 1.00 43.62  ? 122 GLY B N     1 
ATOM   5140 C  CA    . GLY B 2 122 ? 110.259 135.474 138.783 1.00 42.52  ? 122 GLY B CA    1 
ATOM   5141 C  C     . GLY B 2 122 ? 111.478 135.228 137.914 1.00 41.17  ? 122 GLY B C     1 
ATOM   5142 O  O     . GLY B 2 122 ? 111.515 135.631 136.743 1.00 41.48  ? 122 GLY B O     1 
ATOM   5143 N  N     . LEU B 2 123 ? 112.486 134.549 138.467 1.00 39.64  ? 123 LEU B N     1 
ATOM   5144 C  CA    . LEU B 2 123 ? 113.670 134.233 137.675 1.00 39.78  ? 123 LEU B CA    1 
ATOM   5145 C  C     . LEU B 2 123 ? 113.320 133.335 136.495 1.00 38.62  ? 123 LEU B C     1 
ATOM   5146 O  O     . LEU B 2 123 ? 113.856 133.506 135.395 1.00 45.20  ? 123 LEU B O     1 
ATOM   5147 C  CB    . LEU B 2 123 ? 114.735 133.579 138.553 1.00 43.11  ? 123 LEU B CB    1 
ATOM   5148 C  CG    . LEU B 2 123 ? 115.430 134.506 139.550 1.00 44.39  ? 123 LEU B CG    1 
ATOM   5149 C  CD1   . LEU B 2 123 ? 116.741 133.903 140.006 1.00 45.49  ? 123 LEU B CD1   1 
ATOM   5150 C  CD2   . LEU B 2 123 ? 115.654 135.879 138.944 1.00 43.79  ? 123 LEU B CD2   1 
ATOM   5151 N  N     . TYR B 2 124 ? 112.421 132.373 136.702 1.00 36.93  ? 124 TYR B N     1 
ATOM   5152 C  CA    . TYR B 2 124 ? 112.027 131.482 135.616 1.00 38.10  ? 124 TYR B CA    1 
ATOM   5153 C  C     . TYR B 2 124 ? 111.302 132.235 134.507 1.00 43.44  ? 124 TYR B C     1 
ATOM   5154 O  O     . TYR B 2 124 ? 111.527 131.974 133.318 1.00 46.56  ? 124 TYR B O     1 
ATOM   5155 C  CB    . TYR B 2 124 ? 111.159 130.356 136.168 1.00 35.59  ? 124 TYR B CB    1 
ATOM   5156 C  CG    . TYR B 2 124 ? 111.951 129.290 136.884 1.00 40.57  ? 124 TYR B CG    1 
ATOM   5157 C  CD1   . TYR B 2 124 ? 113.173 128.863 136.389 1.00 41.04  ? 124 TYR B CD1   1 
ATOM   5158 C  CD2   . TYR B 2 124 ? 111.472 128.700 138.043 1.00 42.46  ? 124 TYR B CD2   1 
ATOM   5159 C  CE1   . TYR B 2 124 ? 113.898 127.885 137.030 1.00 41.37  ? 124 TYR B CE1   1 
ATOM   5160 C  CE2   . TYR B 2 124 ? 112.191 127.719 138.691 1.00 42.97  ? 124 TYR B CE2   1 
ATOM   5161 C  CZ    . TYR B 2 124 ? 113.403 127.316 138.180 1.00 44.96  ? 124 TYR B CZ    1 
ATOM   5162 O  OH    . TYR B 2 124 ? 114.127 126.340 138.821 1.00 49.78  ? 124 TYR B OH    1 
ATOM   5163 N  N     . LEU B 2 125 ? 110.423 133.169 134.875 1.00 42.29  ? 125 LEU B N     1 
ATOM   5164 C  CA    . LEU B 2 125 ? 109.755 133.987 133.866 1.00 37.77  ? 125 LEU B CA    1 
ATOM   5165 C  C     . LEU B 2 125 ? 110.763 134.805 133.067 1.00 42.48  ? 125 LEU B C     1 
ATOM   5166 O  O     . LEU B 2 125 ? 110.681 134.882 131.830 1.00 44.27  ? 125 LEU B O     1 
ATOM   5167 C  CB    . LEU B 2 125 ? 108.730 134.906 134.531 1.00 36.61  ? 125 LEU B CB    1 
ATOM   5168 C  CG    . LEU B 2 125 ? 107.278 134.440 134.657 1.00 38.60  ? 125 LEU B CG    1 
ATOM   5169 C  CD1   . LEU B 2 125 ? 107.186 133.016 135.164 1.00 38.12  ? 125 LEU B CD1   1 
ATOM   5170 C  CD2   . LEU B 2 125 ? 106.506 135.376 135.569 1.00 38.35  ? 125 LEU B CD2   1 
ATOM   5171 N  N     . VAL B 2 126 ? 111.728 135.418 133.758 1.00 39.02  ? 126 VAL B N     1 
ATOM   5172 C  CA    . VAL B 2 126 ? 112.744 136.210 133.068 1.00 34.54  ? 126 VAL B CA    1 
ATOM   5173 C  C     . VAL B 2 126 ? 113.543 135.336 132.109 1.00 36.98  ? 126 VAL B C     1 
ATOM   5174 O  O     . VAL B 2 126 ? 113.822 135.730 130.966 1.00 46.26  ? 126 VAL B O     1 
ATOM   5175 C  CB    . VAL B 2 126 ? 113.655 136.912 134.092 1.00 37.23  ? 126 VAL B CB    1 
ATOM   5176 C  CG1   . VAL B 2 126 ? 114.903 137.448 133.421 1.00 38.86  ? 126 VAL B CG1   1 
ATOM   5177 C  CG2   . VAL B 2 126 ? 112.900 138.032 134.785 1.00 33.69  ? 126 VAL B CG2   1 
ATOM   5178 N  N     . ALA B 2 127 ? 113.921 134.137 132.557 1.00 37.18  ? 127 ALA B N     1 
ATOM   5179 C  CA    . ALA B 2 127 ? 114.691 133.233 131.711 1.00 35.10  ? 127 ALA B CA    1 
ATOM   5180 C  C     . ALA B 2 127 ? 113.902 132.822 130.477 1.00 35.94  ? 127 ALA B C     1 
ATOM   5181 O  O     . ALA B 2 127 ? 114.456 132.747 129.375 1.00 38.55  ? 127 ALA B O     1 
ATOM   5182 C  CB    . ALA B 2 127 ? 115.114 132.002 132.510 1.00 35.87  ? 127 ALA B CB    1 
ATOM   5183 N  N     . ALA B 2 128 ? 112.606 132.546 130.642 1.00 37.05  ? 128 ALA B N     1 
ATOM   5184 C  CA    . ALA B 2 128 ? 111.784 132.180 129.493 1.00 40.52  ? 128 ALA B CA    1 
ATOM   5185 C  C     . ALA B 2 128 ? 111.716 133.315 128.480 1.00 41.19  ? 128 ALA B C     1 
ATOM   5186 O  O     . ALA B 2 128 ? 111.827 133.086 127.268 1.00 40.71  ? 128 ALA B O     1 
ATOM   5187 C  CB    . ALA B 2 128 ? 110.382 131.786 129.951 1.00 35.37  ? 128 ALA B CB    1 
ATOM   5188 N  N     . LEU B 2 129 ? 111.542 134.550 128.957 1.00 40.83  ? 129 LEU B N     1 
ATOM   5189 C  CA    . LEU B 2 129 ? 111.490 135.686 128.038 1.00 37.86  ? 129 LEU B CA    1 
ATOM   5190 C  C     . LEU B 2 129 ? 112.808 135.848 127.281 1.00 39.51  ? 129 LEU B C     1 
ATOM   5191 O  O     . LEU B 2 129 ? 112.821 136.059 126.057 1.00 41.50  ? 129 LEU B O     1 
ATOM   5192 C  CB    . LEU B 2 129 ? 111.145 136.960 128.807 1.00 37.32  ? 129 LEU B CB    1 
ATOM   5193 C  CG    . LEU B 2 129 ? 111.101 138.245 127.982 1.00 43.90  ? 129 LEU B CG    1 
ATOM   5194 C  CD1   . LEU B 2 129 ? 109.798 138.338 127.210 1.00 37.00  ? 129 LEU B CD1   1 
ATOM   5195 C  CD2   . LEU B 2 129 ? 111.292 139.459 128.875 1.00 43.10  ? 129 LEU B CD2   1 
ATOM   5196 N  N     . LEU B 2 130 ? 113.933 135.746 127.995 1.00 36.04  ? 130 LEU B N     1 
ATOM   5197 C  CA    . LEU B 2 130 ? 115.231 135.889 127.342 1.00 32.21  ? 130 LEU B CA    1 
ATOM   5198 C  C     . LEU B 2 130 ? 115.458 134.788 126.313 1.00 37.70  ? 130 LEU B C     1 
ATOM   5199 O  O     . LEU B 2 130 ? 115.984 135.045 125.223 1.00 45.94  ? 130 LEU B O     1 
ATOM   5200 C  CB    . LEU B 2 130 ? 116.351 135.890 128.380 1.00 33.21  ? 130 LEU B CB    1 
ATOM   5201 C  CG    . LEU B 2 130 ? 116.383 137.071 129.349 1.00 34.69  ? 130 LEU B CG    1 
ATOM   5202 C  CD1   . LEU B 2 130 ? 117.674 137.070 130.143 1.00 38.84  ? 130 LEU B CD1   1 
ATOM   5203 C  CD2   . LEU B 2 130 ? 116.210 138.382 128.608 1.00 34.15  ? 130 LEU B CD2   1 
ATOM   5204 N  N     . VAL B 2 131 ? 115.069 133.555 126.642 1.00 36.58  ? 131 VAL B N     1 
ATOM   5205 C  CA    . VAL B 2 131 ? 115.246 132.445 125.711 1.00 35.65  ? 131 VAL B CA    1 
ATOM   5206 C  C     . VAL B 2 131 ? 114.395 132.650 124.465 1.00 36.26  ? 131 VAL B C     1 
ATOM   5207 O  O     . VAL B 2 131 ? 114.830 132.358 123.344 1.00 41.49  ? 131 VAL B O     1 
ATOM   5208 C  CB    . VAL B 2 131 ? 114.928 131.112 126.414 1.00 41.16  ? 131 VAL B CB    1 
ATOM   5209 C  CG1   . VAL B 2 131 ? 114.644 130.020 125.402 1.00 43.20  ? 131 VAL B CG1   1 
ATOM   5210 C  CG2   . VAL B 2 131 ? 116.084 130.709 127.314 1.00 36.15  ? 131 VAL B CG2   1 
ATOM   5211 N  N     . TRP B 2 132 ? 113.172 133.160 124.636 1.00 35.63  ? 132 TRP B N     1 
ATOM   5212 C  CA    . TRP B 2 132 ? 112.319 133.425 123.481 1.00 32.61  ? 132 TRP B CA    1 
ATOM   5213 C  C     . TRP B 2 132 ? 112.942 134.469 122.561 1.00 33.80  ? 132 TRP B C     1 
ATOM   5214 O  O     . TRP B 2 132 ? 112.968 134.296 121.332 1.00 37.50  ? 132 TRP B O     1 
ATOM   5215 C  CB    . TRP B 2 132 ? 110.937 133.874 123.951 1.00 33.46  ? 132 TRP B CB    1 
ATOM   5216 C  CG    . TRP B 2 132 ? 110.009 134.284 122.851 1.00 34.02  ? 132 TRP B CG    1 
ATOM   5217 C  CD1   . TRP B 2 132 ? 109.617 133.530 121.787 1.00 35.71  ? 132 TRP B CD1   1 
ATOM   5218 C  CD2   . TRP B 2 132 ? 109.339 135.541 122.719 1.00 33.90  ? 132 TRP B CD2   1 
ATOM   5219 N  NE1   . TRP B 2 132 ? 108.753 134.241 120.995 1.00 32.03  ? 132 TRP B NE1   1 
ATOM   5220 C  CE2   . TRP B 2 132 ? 108.565 135.480 121.546 1.00 32.94  ? 132 TRP B CE2   1 
ATOM   5221 C  CE3   . TRP B 2 132 ? 109.322 136.715 123.477 1.00 36.37  ? 132 TRP B CE3   1 
ATOM   5222 C  CZ2   . TRP B 2 132 ? 107.785 136.545 121.112 1.00 37.94  ? 132 TRP B CZ2   1 
ATOM   5223 C  CZ3   . TRP B 2 132 ? 108.547 137.771 123.044 1.00 35.52  ? 132 TRP B CZ3   1 
ATOM   5224 C  CH2   . TRP B 2 132 ? 107.789 137.679 121.874 1.00 41.57  ? 132 TRP B CH2   1 
ATOM   5225 N  N     . VAL B 2 133 ? 113.459 135.556 123.138 1.00 34.91  ? 133 VAL B N     1 
ATOM   5226 C  CA    . VAL B 2 133 ? 114.074 136.595 122.312 1.00 32.35  ? 133 VAL B CA    1 
ATOM   5227 C  C     . VAL B 2 133 ? 115.304 136.051 121.592 1.00 33.46  ? 133 VAL B C     1 
ATOM   5228 O  O     . VAL B 2 133 ? 115.537 136.347 120.410 1.00 37.73  ? 133 VAL B O     1 
ATOM   5229 C  CB    . VAL B 2 133 ? 114.411 137.833 123.164 1.00 31.97  ? 133 VAL B CB    1 
ATOM   5230 C  CG1   . VAL B 2 133 ? 115.037 138.908 122.303 1.00 32.62  ? 133 VAL B CG1   1 
ATOM   5231 C  CG2   . VAL B 2 133 ? 113.160 138.365 123.834 1.00 33.02  ? 133 VAL B CG2   1 
ATOM   5232 N  N     . GLN B 2 134 ? 116.111 135.246 122.290 1.00 33.11  ? 134 GLN B N     1 
ATOM   5233 C  CA    . GLN B 2 134 ? 117.290 134.659 121.661 1.00 34.51  ? 134 GLN B CA    1 
ATOM   5234 C  C     . GLN B 2 134 ? 116.907 133.739 120.508 1.00 33.69  ? 134 GLN B C     1 
ATOM   5235 O  O     . GLN B 2 134 ? 117.570 133.734 119.464 1.00 34.62  ? 134 GLN B O     1 
ATOM   5236 C  CB    . GLN B 2 134 ? 118.115 133.900 122.698 1.00 39.56  ? 134 GLN B CB    1 
ATOM   5237 C  CG    . GLN B 2 134 ? 119.515 133.555 122.231 1.00 43.37  ? 134 GLN B CG    1 
ATOM   5238 C  CD    . GLN B 2 134 ? 119.890 132.115 122.512 1.00 53.00  ? 134 GLN B CD    1 
ATOM   5239 O  OE1   . GLN B 2 134 ? 119.039 131.294 122.854 1.00 51.44  ? 134 GLN B OE1   1 
ATOM   5240 N  NE2   . GLN B 2 134 ? 121.171 131.800 122.370 1.00 54.96  ? 134 GLN B NE2   1 
ATOM   5241 N  N     . ALA B 2 135 ? 115.845 132.948 120.678 1.00 33.36  ? 135 ALA B N     1 
ATOM   5242 C  CA    . ALA B 2 135 ? 115.393 132.072 119.601 1.00 31.49  ? 135 ALA B CA    1 
ATOM   5243 C  C     . ALA B 2 135 ? 114.930 132.871 118.390 1.00 33.72  ? 135 ALA B C     1 
ATOM   5244 O  O     . ALA B 2 135 ? 115.203 132.493 117.243 1.00 37.60  ? 135 ALA B O     1 
ATOM   5245 C  CB    . ALA B 2 135 ? 114.274 131.161 120.102 1.00 26.93  ? 135 ALA B CB    1 
ATOM   5246 N  N     . ARG B 2 136 ? 114.219 133.977 118.621 1.00 31.99  ? 136 ARG B N     1 
ATOM   5247 C  CA    . ARG B 2 136 ? 113.789 134.811 117.500 1.00 29.15  ? 136 ARG B CA    1 
ATOM   5248 C  C     . ARG B 2 136 ? 114.981 135.402 116.752 1.00 35.11  ? 136 ARG B C     1 
ATOM   5249 O  O     . ARG B 2 136 ? 115.015 135.405 115.510 1.00 39.97  ? 136 ARG B O     1 
ATOM   5250 C  CB    . ARG B 2 136 ? 112.862 135.913 118.001 1.00 26.69  ? 136 ARG B CB    1 
ATOM   5251 C  CG    . ARG B 2 136 ? 111.485 135.410 118.363 1.00 29.59  ? 136 ARG B CG    1 
ATOM   5252 C  CD    . ARG B 2 136 ? 110.503 136.547 118.510 1.00 34.46  ? 136 ARG B CD    1 
ATOM   5253 N  NE    . ARG B 2 136 ? 110.276 137.239 117.249 1.00 33.73  ? 136 ARG B NE    1 
ATOM   5254 C  CZ    . ARG B 2 136 ? 109.080 137.463 116.725 1.00 36.20  ? 136 ARG B CZ    1 
ATOM   5255 N  NH1   . ARG B 2 136 ? 107.978 137.032 117.312 1.00 35.43  ? 136 ARG B NH1   1 
ATOM   5256 N  NH2   . ARG B 2 136 ? 108.988 138.138 115.584 1.00 41.38  ? 136 ARG B NH2   1 
ATOM   5257 N  N     . LEU B 2 137 ? 115.975 135.902 117.491 1.00 33.20  ? 137 LEU B N     1 
ATOM   5258 C  CA    . LEU B 2 137 ? 117.164 136.446 116.842 1.00 32.67  ? 137 LEU B CA    1 
ATOM   5259 C  C     . LEU B 2 137 ? 117.912 135.367 116.065 1.00 35.60  ? 137 LEU B C     1 
ATOM   5260 O  O     . LEU B 2 137 ? 118.435 135.623 114.971 1.00 40.33  ? 137 LEU B O     1 
ATOM   5261 C  CB    . LEU B 2 137 ? 118.078 137.093 117.879 1.00 34.84  ? 137 LEU B CB    1 
ATOM   5262 C  CG    . LEU B 2 137 ? 117.541 138.322 118.608 1.00 38.74  ? 137 LEU B CG    1 
ATOM   5263 C  CD1   . LEU B 2 137 ? 118.677 139.050 119.297 1.00 38.79  ? 137 LEU B CD1   1 
ATOM   5264 C  CD2   . LEU B 2 137 ? 116.810 139.244 117.650 1.00 37.31  ? 137 LEU B CD2   1 
ATOM   5265 N  N     . LEU B 2 138 ? 117.978 134.156 116.620 1.00 30.12  ? 138 LEU B N     1 
ATOM   5266 C  CA    . LEU B 2 138 ? 118.622 133.054 115.917 1.00 30.54  ? 138 LEU B CA    1 
ATOM   5267 C  C     . LEU B 2 138 ? 117.904 132.739 114.616 1.00 34.34  ? 138 LEU B C     1 
ATOM   5268 O  O     . LEU B 2 138 ? 118.547 132.479 113.594 1.00 44.03  ? 138 LEU B O     1 
ATOM   5269 C  CB    . LEU B 2 138 ? 118.670 131.814 116.806 1.00 32.35  ? 138 LEU B CB    1 
ATOM   5270 C  CG    . LEU B 2 138 ? 119.990 131.525 117.515 1.00 37.17  ? 138 LEU B CG    1 
ATOM   5271 C  CD1   . LEU B 2 138 ? 119.817 130.365 118.472 1.00 44.87  ? 138 LEU B CD1   1 
ATOM   5272 C  CD2   . LEU B 2 138 ? 121.088 131.240 116.509 1.00 35.00  ? 138 LEU B CD2   1 
ATOM   5273 N  N     . ASN B 2 139 ? 116.572 132.737 114.637 1.00 32.80  ? 139 ASN B N     1 
ATOM   5274 C  CA    . ASN B 2 139 ? 115.817 132.483 113.413 1.00 32.11  ? 139 ASN B CA    1 
ATOM   5275 C  C     . ASN B 2 139 ? 116.130 133.536 112.358 1.00 32.84  ? 139 ASN B C     1 
ATOM   5276 O  O     . ASN B 2 139 ? 116.357 133.213 111.182 1.00 37.05  ? 139 ASN B O     1 
ATOM   5277 C  CB    . ASN B 2 139 ? 114.322 132.453 113.724 1.00 38.03  ? 139 ASN B CB    1 
ATOM   5278 C  CG    . ASN B 2 139 ? 113.467 132.405 112.477 1.00 47.44  ? 139 ASN B CG    1 
ATOM   5279 O  OD1   . ASN B 2 139 ? 112.536 133.195 112.321 1.00 43.19  ? 139 ASN B OD1   1 
ATOM   5280 N  ND2   . ASN B 2 139 ? 113.767 131.467 111.589 1.00 48.54  ? 139 ASN B ND2   1 
ATOM   5281 N  N     . VAL B 2 140 ? 116.167 134.805 112.771 1.00 33.77  ? 140 VAL B N     1 
ATOM   5282 C  CA    . VAL B 2 140 ? 116.469 135.883 111.829 1.00 33.66  ? 140 VAL B CA    1 
ATOM   5283 C  C     . VAL B 2 140 ? 117.845 135.678 111.199 1.00 36.74  ? 140 VAL B C     1 
ATOM   5284 O  O     . VAL B 2 140 ? 118.005 135.746 109.971 1.00 37.47  ? 140 VAL B O     1 
ATOM   5285 C  CB    . VAL B 2 140 ? 116.368 137.249 112.529 1.00 31.39  ? 140 VAL B CB    1 
ATOM   5286 C  CG1   . VAL B 2 140 ? 117.014 138.327 111.680 1.00 35.45  ? 140 VAL B CG1   1 
ATOM   5287 C  CG2   . VAL B 2 140 ? 114.919 137.592 112.807 1.00 29.75  ? 140 VAL B CG2   1 
ATOM   5288 N  N     . THR B 2 141 ? 118.858 135.409 112.027 1.00 35.95  ? 141 THR B N     1 
ATOM   5289 C  CA    . THR B 2 141 ? 120.212 135.294 111.488 1.00 33.31  ? 141 THR B CA    1 
ATOM   5290 C  C     . THR B 2 141 ? 120.368 134.045 110.620 1.00 36.08  ? 141 THR B C     1 
ATOM   5291 O  O     . THR B 2 141 ? 121.073 134.075 109.602 1.00 41.32  ? 141 THR B O     1 
ATOM   5292 C  CB    . THR B 2 141 ? 121.246 135.331 112.622 1.00 34.89  ? 141 THR B CB    1 
ATOM   5293 O  OG1   . THR B 2 141 ? 122.530 135.674 112.090 1.00 39.46  ? 141 THR B OG1   1 
ATOM   5294 C  CG2   . THR B 2 141 ? 121.348 134.001 113.352 1.00 34.30  ? 141 THR B CG2   1 
ATOM   5295 N  N     . VAL B 2 142 ? 119.694 132.949 110.981 1.00 30.90  ? 142 VAL B N     1 
ATOM   5296 C  CA    . VAL B 2 142 ? 119.764 131.735 110.173 1.00 30.79  ? 142 VAL B CA    1 
ATOM   5297 C  C     . VAL B 2 142 ? 119.171 131.983 108.795 1.00 36.49  ? 142 VAL B C     1 
ATOM   5298 O  O     . VAL B 2 142 ? 119.747 131.586 107.773 1.00 43.89  ? 142 VAL B O     1 
ATOM   5299 C  CB    . VAL B 2 142 ? 119.056 130.572 110.893 1.00 30.25  ? 142 VAL B CB    1 
ATOM   5300 C  CG1   . VAL B 2 142 ? 118.707 129.468 109.912 1.00 30.82  ? 142 VAL B CG1   1 
ATOM   5301 C  CG2   . VAL B 2 142 ? 119.929 130.032 112.008 1.00 31.86  ? 142 VAL B CG2   1 
ATOM   5302 N  N     . GLN B 2 143 ? 118.016 132.649 108.741 1.00 32.66  ? 143 GLN B N     1 
ATOM   5303 C  CA    . GLN B 2 143 ? 117.426 132.944 107.442 1.00 28.78  ? 143 GLN B CA    1 
ATOM   5304 C  C     . GLN B 2 143 ? 118.293 133.899 106.635 1.00 33.80  ? 143 GLN B C     1 
ATOM   5305 O  O     . GLN B 2 143 ? 118.358 133.780 105.405 1.00 37.79  ? 143 GLN B O     1 
ATOM   5306 C  CB    . GLN B 2 143 ? 116.016 133.498 107.615 1.00 31.87  ? 143 GLN B CB    1 
ATOM   5307 C  CG    . GLN B 2 143 ? 115.033 132.473 108.151 1.00 37.99  ? 143 GLN B CG    1 
ATOM   5308 C  CD    . GLN B 2 143 ? 115.079 131.161 107.389 1.00 42.80  ? 143 GLN B CD    1 
ATOM   5309 O  OE1   . GLN B 2 143 ? 115.193 131.143 106.165 1.00 44.26  ? 143 GLN B OE1   1 
ATOM   5310 N  NE2   . GLN B 2 143 ? 114.990 130.055 108.114 1.00 40.73  ? 143 GLN B NE2   1 
ATOM   5311 N  N     . ARG B 2 144 ? 118.972 134.839 107.298 1.00 35.33  ? 144 ARG B N     1 
ATOM   5312 C  CA    . ARG B 2 144 ? 119.888 135.721 106.579 1.00 32.58  ? 144 ARG B CA    1 
ATOM   5313 C  C     . ARG B 2 144 ? 120.999 134.928 105.898 1.00 32.06  ? 144 ARG B C     1 
ATOM   5314 O  O     . ARG B 2 144 ? 121.275 135.114 104.703 1.00 35.73  ? 144 ARG B O     1 
ATOM   5315 C  CB    . ARG B 2 144 ? 120.479 136.756 107.534 1.00 35.57  ? 144 ARG B CB    1 
ATOM   5316 C  CG    . ARG B 2 144 ? 119.580 137.945 107.801 1.00 40.32  ? 144 ARG B CG    1 
ATOM   5317 C  CD    . ARG B 2 144 ? 120.267 138.952 108.705 1.00 47.31  ? 144 ARG B CD    1 
ATOM   5318 N  NE    . ARG B 2 144 ? 119.402 140.082 109.018 1.00 56.49  ? 144 ARG B NE    1 
ATOM   5319 C  CZ    . ARG B 2 144 ? 119.785 141.153 109.699 1.00 56.17  ? 144 ARG B CZ    1 
ATOM   5320 N  NH1   . ARG B 2 144 ? 121.022 141.279 110.149 1.00 53.39  ? 144 ARG B NH1   1 
ATOM   5321 N  NH2   . ARG B 2 144 ? 118.905 142.122 109.933 1.00 51.37  ? 144 ARG B NH2   1 
ATOM   5322 N  N     . THR B 2 145 ? 121.647 134.030 106.645 1.00 32.85  ? 145 THR B N     1 
ATOM   5323 C  CA    . THR B 2 145 ? 122.716 133.238 106.039 1.00 34.36  ? 145 THR B CA    1 
ATOM   5324 C  C     . THR B 2 145 ? 122.192 132.318 104.945 1.00 33.78  ? 145 THR B C     1 
ATOM   5325 O  O     . THR B 2 145 ? 122.889 132.081 103.955 1.00 38.98  ? 145 THR B O     1 
ATOM   5326 C  CB    . THR B 2 145 ? 123.471 132.421 107.089 1.00 39.37  ? 145 THR B CB    1 
ATOM   5327 O  OG1   . THR B 2 145 ? 122.779 131.192 107.341 1.00 39.17  ? 145 THR B OG1   1 
ATOM   5328 C  CG2   . THR B 2 145 ? 123.643 133.203 108.370 1.00 45.84  ? 145 THR B CG2   1 
ATOM   5329 N  N     . MET B 2 146 ? 120.976 131.791 105.095 1.00 32.20  ? 146 MET B N     1 
ATOM   5330 C  CA    . MET B 2 146 ? 120.430 130.919 104.057 1.00 32.72  ? 146 MET B CA    1 
ATOM   5331 C  C     . MET B 2 146 ? 120.137 131.686 102.770 1.00 32.38  ? 146 MET B C     1 
ATOM   5332 O  O     . MET B 2 146 ? 120.390 131.183 101.666 1.00 36.52  ? 146 MET B O     1 
ATOM   5333 C  CB    . MET B 2 146 ? 119.179 130.222 104.577 1.00 29.42  ? 146 MET B CB    1 
ATOM   5334 C  CG    . MET B 2 146 ? 119.492 129.008 105.418 1.00 35.24  ? 146 MET B CG    1 
ATOM   5335 S  SD    . MET B 2 146 ? 120.933 128.102 104.830 1.00 59.76  ? 146 MET B SD    1 
ATOM   5336 C  CE    . MET B 2 146 ? 121.973 128.125 106.286 1.00 47.07  ? 146 MET B CE    1 
ATOM   5337 N  N     . VAL B 2 147 ? 119.601 132.903 102.889 1.00 31.95  ? 147 VAL B N     1 
ATOM   5338 C  CA    . VAL B 2 147 ? 119.395 133.738 101.708 1.00 32.32  ? 147 VAL B CA    1 
ATOM   5339 C  C     . VAL B 2 147 ? 120.725 134.031 101.031 1.00 34.45  ? 147 VAL B C     1 
ATOM   5340 O  O     . VAL B 2 147 ? 120.848 133.949 99.799  1.00 32.41  ? 147 VAL B O     1 
ATOM   5341 C  CB    . VAL B 2 147 ? 118.665 135.037 102.093 1.00 28.75  ? 147 VAL B CB    1 
ATOM   5342 C  CG1   . VAL B 2 147 ? 118.682 136.020 100.938 1.00 32.67  ? 147 VAL B CG1   1 
ATOM   5343 C  CG2   . VAL B 2 147 ? 117.259 134.733 102.493 1.00 28.80  ? 147 VAL B CG2   1 
ATOM   5344 N  N     . ALA B 2 148 ? 121.742 134.380 101.825 1.00 35.45  ? 148 ALA B N     1 
ATOM   5345 C  CA    . ALA B 2 148 ? 123.056 134.646 101.254 1.00 28.37  ? 148 ALA B CA    1 
ATOM   5346 C  C     . ALA B 2 148 ? 123.603 133.418 100.540 1.00 32.02  ? 148 ALA B C     1 
ATOM   5347 O  O     . ALA B 2 148 ? 124.192 133.530 99.458  1.00 41.85  ? 148 ALA B O     1 
ATOM   5348 C  CB    . ALA B 2 148 ? 124.019 135.107 102.345 1.00 34.47  ? 148 ALA B CB    1 
ATOM   5349 N  N     . LEU B 2 149 ? 123.413 132.236 101.127 1.00 30.87  ? 149 LEU B N     1 
ATOM   5350 C  CA    . LEU B 2 149 ? 123.933 131.010 100.532 1.00 29.75  ? 149 LEU B CA    1 
ATOM   5351 C  C     . LEU B 2 149 ? 123.263 130.719 99.197  1.00 29.69  ? 149 LEU B C     1 
ATOM   5352 O  O     . LEU B 2 149 ? 123.932 130.368 98.217  1.00 33.60  ? 149 LEU B O     1 
ATOM   5353 C  CB    . LEU B 2 149 ? 123.736 129.842 101.498 1.00 31.15  ? 149 LEU B CB    1 
ATOM   5354 C  CG    . LEU B 2 149 ? 124.497 128.557 101.174 1.00 37.82  ? 149 LEU B CG    1 
ATOM   5355 C  CD1   . LEU B 2 149 ? 125.985 128.750 101.406 1.00 34.61  ? 149 LEU B CD1   1 
ATOM   5356 C  CD2   . LEU B 2 149 ? 123.965 127.398 101.995 1.00 37.57  ? 149 LEU B CD2   1 
ATOM   5357 N  N     . ARG B 2 150 ? 121.938 130.855 99.138  1.00 32.06  ? 150 ARG B N     1 
ATOM   5358 C  CA    . ARG B 2 150 ? 121.238 130.601 97.881  1.00 28.56  ? 150 ARG B CA    1 
ATOM   5359 C  C     . ARG B 2 150 ? 121.643 131.606 96.808  1.00 27.39  ? 150 ARG B C     1 
ATOM   5360 O  O     . ARG B 2 150 ? 121.831 131.239 95.639  1.00 30.24  ? 150 ARG B O     1 
ATOM   5361 C  CB    . ARG B 2 150 ? 119.728 130.621 98.105  1.00 32.40  ? 150 ARG B CB    1 
ATOM   5362 C  CG    . ARG B 2 150 ? 119.186 129.349 98.733  1.00 33.81  ? 150 ARG B CG    1 
ATOM   5363 C  CD    . ARG B 2 150 ? 117.668 129.363 98.813  1.00 40.49  ? 150 ARG B CD    1 
ATOM   5364 N  NE    . ARG B 2 150 ? 117.152 128.351 99.727  1.00 45.05  ? 150 ARG B NE    1 
ATOM   5365 C  CZ    . ARG B 2 150 ? 116.963 127.078 99.408  1.00 50.50  ? 150 ARG B CZ    1 
ATOM   5366 N  NH1   . ARG B 2 150 ? 117.242 126.618 98.200  1.00 45.53  ? 150 ARG B NH1   1 
ATOM   5367 N  NH2   . ARG B 2 150 ? 116.480 126.244 100.325 1.00 45.81  ? 150 ARG B NH2   1 
ATOM   5368 N  N     . ALA B 2 151 ? 121.795 132.880 97.184  1.00 29.31  ? 151 ALA B N     1 
ATOM   5369 C  CA    . ALA B 2 151 ? 122.230 133.881 96.214  1.00 30.97  ? 151 ALA B CA    1 
ATOM   5370 C  C     . ALA B 2 151 ? 123.633 133.581 95.694  1.00 34.12  ? 151 ALA B C     1 
ATOM   5371 O  O     . ALA B 2 151 ? 123.904 133.721 94.493  1.00 35.82  ? 151 ALA B O     1 
ATOM   5372 C  CB    . ALA B 2 151 ? 122.171 135.273 96.839  1.00 29.78  ? 151 ALA B CB    1 
ATOM   5373 N  N     . GLU B 2 152 ? 124.538 133.166 96.583  1.00 34.02  ? 152 GLU B N     1 
ATOM   5374 C  CA    . GLU B 2 152 ? 125.891 132.823 96.158  1.00 33.99  ? 152 GLU B CA    1 
ATOM   5375 C  C     . GLU B 2 152 ? 125.891 131.615 95.230  1.00 34.84  ? 152 GLU B C     1 
ATOM   5376 O  O     . GLU B 2 152 ? 126.652 131.571 94.256  1.00 39.19  ? 152 GLU B O     1 
ATOM   5377 C  CB    . GLU B 2 152 ? 126.773 132.564 97.377  1.00 32.90  ? 152 GLU B CB    1 
ATOM   5378 C  CG    . GLU B 2 152 ? 128.173 133.128 97.251  1.00 44.59  ? 152 GLU B CG    1 
ATOM   5379 C  CD    . GLU B 2 152 ? 129.133 132.535 98.257  1.00 55.97  ? 152 GLU B CD    1 
ATOM   5380 O  OE1   . GLU B 2 152 ? 128.711 132.288 99.404  1.00 59.21  ? 152 GLU B OE1   1 
ATOM   5381 O  OE2   . GLU B 2 152 ? 130.310 132.316 97.903  1.00 60.36  ? 152 GLU B OE2   1 
ATOM   5382 N  N     . VAL B 2 153 ? 125.046 130.623 95.516  1.00 33.27  ? 153 VAL B N     1 
ATOM   5383 C  CA    . VAL B 2 153 ? 124.951 129.457 94.641  1.00 32.60  ? 153 VAL B CA    1 
ATOM   5384 C  C     . VAL B 2 153 ? 124.465 129.865 93.256  1.00 32.90  ? 153 VAL B C     1 
ATOM   5385 O  O     . VAL B 2 153 ? 124.985 129.397 92.235  1.00 37.20  ? 153 VAL B O     1 
ATOM   5386 C  CB    . VAL B 2 153 ? 124.038 128.388 95.271  1.00 29.62  ? 153 VAL B CB    1 
ATOM   5387 C  CG1   . VAL B 2 153 ? 123.651 127.346 94.241  1.00 30.01  ? 153 VAL B CG1   1 
ATOM   5388 C  CG2   . VAL B 2 153 ? 124.730 127.736 96.450  1.00 31.23  ? 153 VAL B CG2   1 
ATOM   5389 N  N     . GLN B 2 154 ? 123.458 130.741 93.197  1.00 33.01  ? 154 GLN B N     1 
ATOM   5390 C  CA    . GLN B 2 154 ? 122.950 131.183 91.900  1.00 33.30  ? 154 GLN B CA    1 
ATOM   5391 C  C     . GLN B 2 154 ? 124.012 131.948 91.115  1.00 35.36  ? 154 GLN B C     1 
ATOM   5392 O  O     . GLN B 2 154 ? 124.180 131.739 89.903  1.00 39.88  ? 154 GLN B O     1 
ATOM   5393 C  CB    . GLN B 2 154 ? 121.702 132.040 92.095  1.00 37.90  ? 154 GLN B CB    1 
ATOM   5394 C  CG    . GLN B 2 154 ? 120.663 131.853 91.010  1.00 39.48  ? 154 GLN B CG    1 
ATOM   5395 C  CD    . GLN B 2 154 ? 120.539 133.062 90.117  1.00 48.61  ? 154 GLN B CD    1 
ATOM   5396 O  OE1   . GLN B 2 154 ? 121.101 134.116 90.402  1.00 52.77  ? 154 GLN B OE1   1 
ATOM   5397 N  NE2   . GLN B 2 154 ? 119.808 132.913 89.023  1.00 51.48  ? 154 GLN B NE2   1 
ATOM   5398 N  N     . GLU B 2 155 ? 124.747 132.834 91.790  1.00 35.96  ? 155 GLU B N     1 
ATOM   5399 C  CA    . GLU B 2 155 ? 125.811 133.565 91.110  1.00 34.55  ? 155 GLU B CA    1 
ATOM   5400 C  C     . GLU B 2 155 ? 126.892 132.619 90.604  1.00 36.51  ? 155 GLU B C     1 
ATOM   5401 O  O     . GLU B 2 155 ? 127.400 132.787 89.488  1.00 40.50  ? 155 GLU B O     1 
ATOM   5402 C  CB    . GLU B 2 155 ? 126.409 134.616 92.042  1.00 37.85  ? 155 GLU B CB    1 
ATOM   5403 C  CG    . GLU B 2 155 ? 125.423 135.679 92.492  1.00 46.99  ? 155 GLU B CG    1 
ATOM   5404 C  CD    . GLU B 2 155 ? 124.797 136.432 91.337  1.00 56.40  ? 155 GLU B CD    1 
ATOM   5405 O  OE1   . GLU B 2 155 ? 125.485 136.649 90.318  1.00 64.16  ? 155 GLU B OE1   1 
ATOM   5406 O  OE2   . GLU B 2 155 ? 123.611 136.805 91.448  1.00 51.78  ? 155 GLU B OE2   1 
ATOM   5407 N  N     . LYS B 2 156 ? 127.252 131.615 91.407  1.00 38.73  ? 156 LYS B N     1 
ATOM   5408 C  CA    . LYS B 2 156 ? 128.244 130.638 90.971  1.00 37.41  ? 156 LYS B CA    1 
ATOM   5409 C  C     . LYS B 2 156 ? 127.764 129.879 89.742  1.00 37.47  ? 156 LYS B C     1 
ATOM   5410 O  O     . LYS B 2 156 ? 128.543 129.630 88.815  1.00 37.64  ? 156 LYS B O     1 
ATOM   5411 C  CB    . LYS B 2 156 ? 128.560 129.671 92.109  1.00 37.22  ? 156 LYS B CB    1 
ATOM   5412 C  CG    . LYS B 2 156 ? 129.792 128.826 91.870  1.00 38.46  ? 156 LYS B CG    1 
ATOM   5413 C  CD    . LYS B 2 156 ? 131.049 129.662 91.934  1.00 36.70  ? 156 LYS B CD    1 
ATOM   5414 C  CE    . LYS B 2 156 ? 132.251 128.849 91.521  1.00 38.79  ? 156 LYS B CE    1 
ATOM   5415 N  NZ    . LYS B 2 156 ? 133.524 129.518 91.884  1.00 41.25  ? 156 LYS B NZ    1 
ATOM   5416 N  N     . ILE B 2 157 ? 126.484 129.505 89.717  1.00 39.14  ? 157 ILE B N     1 
ATOM   5417 C  CA    . ILE B 2 157 ? 125.925 128.851 88.536  1.00 33.99  ? 157 ILE B CA    1 
ATOM   5418 C  C     . ILE B 2 157 ? 126.087 129.740 87.313  1.00 35.90  ? 157 ILE B C     1 
ATOM   5419 O  O     . ILE B 2 157 ? 126.465 129.275 86.232  1.00 36.51  ? 157 ILE B O     1 
ATOM   5420 C  CB    . ILE B 2 157 ? 124.448 128.488 88.769  1.00 38.74  ? 157 ILE B CB    1 
ATOM   5421 C  CG1   . ILE B 2 157 ? 124.326 127.270 89.676  1.00 40.75  ? 157 ILE B CG1   1 
ATOM   5422 C  CG2   . ILE B 2 157 ? 123.743 128.231 87.449  1.00 40.31  ? 157 ILE B CG2   1 
ATOM   5423 C  CD1   . ILE B 2 157 ? 122.916 127.023 90.124  1.00 43.53  ? 157 ILE B CD1   1 
ATOM   5424 N  N     . HIS B 2 158 ? 125.804 131.033 87.461  1.00 44.30  ? 158 HIS B N     1 
ATOM   5425 C  CA    . HIS B 2 158 ? 125.943 131.930 86.318  1.00 44.70  ? 158 HIS B CA    1 
ATOM   5426 C  C     . HIS B 2 158 ? 127.391 132.274 85.986  1.00 44.33  ? 158 HIS B C     1 
ATOM   5427 O  O     . HIS B 2 158 ? 127.638 132.873 84.935  1.00 39.31  ? 158 HIS B O     1 
ATOM   5428 C  CB    . HIS B 2 158 ? 125.152 133.215 86.552  1.00 43.03  ? 158 HIS B CB    1 
ATOM   5429 C  CG    . HIS B 2 158 ? 123.676 133.040 86.399  1.00 50.40  ? 158 HIS B CG    1 
ATOM   5430 N  ND1   . HIS B 2 158 ? 123.118 132.345 85.348  1.00 51.41  ? 158 HIS B ND1   1 
ATOM   5431 C  CD2   . HIS B 2 158 ? 122.641 133.470 87.158  1.00 56.35  ? 158 HIS B CD2   1 
ATOM   5432 C  CE1   . HIS B 2 158 ? 121.803 132.350 85.469  1.00 58.01  ? 158 HIS B CE1   1 
ATOM   5433 N  NE2   . HIS B 2 158 ? 121.488 133.027 86.558  1.00 59.96  ? 158 HIS B NE2   1 
ATOM   5434 N  N     . ARG B 2 159 ? 128.349 131.918 86.841  1.00 46.57  ? 159 ARG B N     1 
ATOM   5435 C  CA    . ARG B 2 159 ? 129.750 132.235 86.586  1.00 39.03  ? 159 ARG B CA    1 
ATOM   5436 C  C     . ARG B 2 159 ? 130.584 131.041 86.136  1.00 41.94  ? 159 ARG B C     1 
ATOM   5437 O  O     . ARG B 2 159 ? 131.720 131.239 85.696  1.00 47.55  ? 159 ARG B O     1 
ATOM   5438 C  CB    . ARG B 2 159 ? 130.387 132.841 87.840  1.00 46.97  ? 159 ARG B CB    1 
ATOM   5439 C  CG    . ARG B 2 159 ? 130.145 134.329 88.010  1.00 49.60  ? 159 ARG B CG    1 
ATOM   5440 C  CD    . ARG B 2 159 ? 131.008 135.135 87.059  1.00 56.30  ? 159 ARG B CD    1 
ATOM   5441 N  NE    . ARG B 2 159 ? 132.429 134.889 87.279  1.00 63.32  ? 159 ARG B NE    1 
ATOM   5442 C  CZ    . ARG B 2 159 ? 133.348 134.899 86.323  1.00 63.53  ? 159 ARG B CZ    1 
ATOM   5443 N  NH1   . ARG B 2 159 ? 133.031 135.134 85.061  1.00 61.29  ? 159 ARG B NH1   1 
ATOM   5444 N  NH2   . ARG B 2 159 ? 134.618 134.668 86.643  1.00 62.29  ? 159 ARG B NH2   1 
ATOM   5445 N  N     . LEU B 2 160 ? 130.064 129.818 86.233  1.00 40.36  ? 160 LEU B N     1 
ATOM   5446 C  CA    . LEU B 2 160 ? 130.864 128.638 85.937  1.00 34.20  ? 160 LEU B CA    1 
ATOM   5447 C  C     . LEU B 2 160 ? 131.101 128.483 84.435  1.00 38.86  ? 160 LEU B C     1 
ATOM   5448 O  O     . LEU B 2 160 ? 130.309 128.961 83.621  1.00 41.76  ? 160 LEU B O     1 
ATOM   5449 C  CB    . LEU B 2 160 ? 130.184 127.384 86.476  1.00 30.85  ? 160 LEU B CB    1 
ATOM   5450 C  CG    . LEU B 2 160 ? 130.385 127.094 87.963  1.00 34.06  ? 160 LEU B CG    1 
ATOM   5451 C  CD1   . LEU B 2 160 ? 129.423 126.019 88.433  1.00 32.20  ? 160 LEU B CD1   1 
ATOM   5452 C  CD2   . LEU B 2 160 ? 131.820 126.697 88.245  1.00 32.20  ? 160 LEU B CD2   1 
ATOM   5453 N  N     . PRO B 2 161 ? 132.193 127.828 84.046  1.00 42.87  ? 161 PRO B N     1 
ATOM   5454 C  CA    . PRO B 2 161 ? 132.400 127.502 82.633  1.00 42.56  ? 161 PRO B CA    1 
ATOM   5455 C  C     . PRO B 2 161 ? 131.512 126.350 82.180  1.00 39.53  ? 161 PRO B C     1 
ATOM   5456 O  O     . PRO B 2 161 ? 130.995 125.568 82.978  1.00 38.34  ? 161 PRO B O     1 
ATOM   5457 C  CB    . PRO B 2 161 ? 133.881 127.114 82.574  1.00 35.87  ? 161 PRO B CB    1 
ATOM   5458 C  CG    . PRO B 2 161 ? 134.191 126.633 83.934  1.00 34.06  ? 161 PRO B CG    1 
ATOM   5459 C  CD    . PRO B 2 161 ? 133.352 127.449 84.872  1.00 39.50  ? 161 PRO B CD    1 
ATOM   5460 N  N     . LEU B 2 162 ? 131.344 126.262 80.859  1.00 37.02  ? 162 LEU B N     1 
ATOM   5461 C  CA    . LEU B 2 162 ? 130.485 125.229 80.289  1.00 38.16  ? 162 LEU B CA    1 
ATOM   5462 C  C     . LEU B 2 162 ? 131.063 123.834 80.490  1.00 41.75  ? 162 LEU B C     1 
ATOM   5463 O  O     . LEU B 2 162 ? 130.306 122.861 80.600  1.00 43.02  ? 162 LEU B O     1 
ATOM   5464 C  CB    . LEU B 2 162 ? 130.257 125.498 78.803  1.00 40.15  ? 162 LEU B CB    1 
ATOM   5465 C  CG    . LEU B 2 162 ? 129.331 126.661 78.451  1.00 41.01  ? 162 LEU B CG    1 
ATOM   5466 C  CD1   . LEU B 2 162 ? 129.252 126.837 76.948  1.00 40.79  ? 162 LEU B CD1   1 
ATOM   5467 C  CD2   . LEU B 2 162 ? 127.947 126.455 79.040  1.00 36.71  ? 162 LEU B CD2   1 
ATOM   5468 N  N     . SER B 2 163 ? 132.391 123.714 80.534  1.00 42.84  ? 163 SER B N     1 
ATOM   5469 C  CA    . SER B 2 163 ? 133.015 122.413 80.738  1.00 39.38  ? 163 SER B CA    1 
ATOM   5470 C  C     . SER B 2 163 ? 132.686 121.825 82.101  1.00 38.03  ? 163 SER B C     1 
ATOM   5471 O  O     . SER B 2 163 ? 132.783 120.606 82.276  1.00 45.00  ? 163 SER B O     1 
ATOM   5472 C  CB    . SER B 2 163 ? 134.530 122.522 80.570  1.00 34.80  ? 163 SER B CB    1 
ATOM   5473 O  OG    . SER B 2 163 ? 135.095 123.348 81.570  1.00 39.27  ? 163 SER B OG    1 
ATOM   5474 N  N     . TYR B 2 164 ? 132.312 122.658 83.074  1.00 32.97  ? 164 TYR B N     1 
ATOM   5475 C  CA    . TYR B 2 164 ? 131.885 122.134 84.366  1.00 31.67  ? 164 TYR B CA    1 
ATOM   5476 C  C     . TYR B 2 164 ? 130.595 121.339 84.226  1.00 34.34  ? 164 TYR B C     1 
ATOM   5477 O  O     . TYR B 2 164 ? 130.473 120.229 84.754  1.00 40.19  ? 164 TYR B O     1 
ATOM   5478 C  CB    . TYR B 2 164 ? 131.709 123.277 85.366  1.00 30.82  ? 164 TYR B CB    1 
ATOM   5479 C  CG    . TYR B 2 164 ? 131.284 122.814 86.740  1.00 31.87  ? 164 TYR B CG    1 
ATOM   5480 C  CD1   . TYR B 2 164 ? 132.224 122.429 87.683  1.00 31.55  ? 164 TYR B CD1   1 
ATOM   5481 C  CD2   . TYR B 2 164 ? 129.943 122.750 87.090  1.00 33.53  ? 164 TYR B CD2   1 
ATOM   5482 C  CE1   . TYR B 2 164 ? 131.842 122.001 88.935  1.00 33.03  ? 164 TYR B CE1   1 
ATOM   5483 C  CE2   . TYR B 2 164 ? 129.553 122.320 88.338  1.00 35.83  ? 164 TYR B CE2   1 
ATOM   5484 C  CZ    . TYR B 2 164 ? 130.506 121.947 89.257  1.00 38.54  ? 164 TYR B CZ    1 
ATOM   5485 O  OH    . TYR B 2 164 ? 130.119 121.519 90.505  1.00 42.18  ? 164 TYR B OH    1 
ATOM   5486 N  N     . PHE B 2 165 ? 129.614 121.900 83.516  1.00 37.00  ? 165 PHE B N     1 
ATOM   5487 C  CA    . PHE B 2 165 ? 128.358 121.194 83.299  1.00 36.84  ? 165 PHE B CA    1 
ATOM   5488 C  C     . PHE B 2 165 ? 128.529 120.030 82.336  1.00 40.14  ? 165 PHE B C     1 
ATOM   5489 O  O     . PHE B 2 165 ? 127.846 119.010 82.474  1.00 39.34  ? 165 PHE B O     1 
ATOM   5490 C  CB    . PHE B 2 165 ? 127.297 122.164 82.781  1.00 30.72  ? 165 PHE B CB    1 
ATOM   5491 C  CG    . PHE B 2 165 ? 127.144 123.394 83.622  1.00 30.91  ? 165 PHE B CG    1 
ATOM   5492 C  CD1   . PHE B 2 165 ? 126.479 123.340 84.833  1.00 30.76  ? 165 PHE B CD1   1 
ATOM   5493 C  CD2   . PHE B 2 165 ? 127.670 124.602 83.206  1.00 33.43  ? 165 PHE B CD2   1 
ATOM   5494 C  CE1   . PHE B 2 165 ? 126.339 124.467 85.612  1.00 29.78  ? 165 PHE B CE1   1 
ATOM   5495 C  CE2   . PHE B 2 165 ? 127.532 125.733 83.983  1.00 35.27  ? 165 PHE B CE2   1 
ATOM   5496 C  CZ    . PHE B 2 165 ? 126.865 125.664 85.187  1.00 34.63  ? 165 PHE B CZ    1 
ATOM   5497 N  N     . ASP B 2 166 ? 129.426 120.164 81.357  1.00 38.29  ? 166 ASP B N     1 
ATOM   5498 C  CA    . ASP B 2 166 ? 129.640 119.083 80.402  1.00 39.78  ? 166 ASP B CA    1 
ATOM   5499 C  C     . ASP B 2 166 ? 130.259 117.857 81.060  1.00 46.12  ? 166 ASP B C     1 
ATOM   5500 O  O     . ASP B 2 166 ? 129.943 116.725 80.678  1.00 52.10  ? 166 ASP B O     1 
ATOM   5501 C  CB    . ASP B 2 166 ? 130.522 119.565 79.252  1.00 43.03  ? 166 ASP B CB    1 
ATOM   5502 C  CG    . ASP B 2 166 ? 129.847 120.623 78.405  1.00 50.65  ? 166 ASP B CG    1 
ATOM   5503 O  OD1   . ASP B 2 166 ? 128.667 120.931 78.669  1.00 46.32  ? 166 ASP B OD1   1 
ATOM   5504 O  OD2   . ASP B 2 166 ? 130.493 121.144 77.472  1.00 54.21  ? 166 ASP B OD2   1 
ATOM   5505 N  N     . SER B 2 167 ? 131.127 118.056 82.049  1.00 43.74  ? 167 SER B N     1 
ATOM   5506 C  CA    . SER B 2 167 ? 131.863 116.964 82.673  1.00 42.29  ? 167 SER B CA    1 
ATOM   5507 C  C     . SER B 2 167 ? 131.085 116.265 83.779  1.00 45.00  ? 167 SER B C     1 
ATOM   5508 O  O     . SER B 2 167 ? 131.619 115.336 84.394  1.00 48.33  ? 167 SER B O     1 
ATOM   5509 C  CB    . SER B 2 167 ? 133.188 117.483 83.234  1.00 43.58  ? 167 SER B CB    1 
ATOM   5510 O  OG    . SER B 2 167 ? 134.032 116.416 83.625  1.00 54.71  ? 167 SER B OG    1 
ATOM   5511 N  N     . ARG B 2 168 ? 129.851 116.679 84.051  1.00 44.66  ? 168 ARG B N     1 
ATOM   5512 C  CA    . ARG B 2 168 ? 129.064 116.118 85.136  1.00 41.20  ? 168 ARG B CA    1 
ATOM   5513 C  C     . ARG B 2 168 ? 127.654 115.841 84.642  1.00 44.84  ? 168 ARG B C     1 
ATOM   5514 O  O     . ARG B 2 168 ? 127.237 116.317 83.583  1.00 50.09  ? 168 ARG B O     1 
ATOM   5515 C  CB    . ARG B 2 168 ? 129.034 117.058 86.346  1.00 39.71  ? 168 ARG B CB    1 
ATOM   5516 C  CG    . ARG B 2 168 ? 130.348 117.134 87.091  1.00 43.76  ? 168 ARG B CG    1 
ATOM   5517 C  CD    . ARG B 2 168 ? 130.448 118.400 87.913  1.00 42.14  ? 168 ARG B CD    1 
ATOM   5518 N  NE    . ARG B 2 168 ? 131.730 118.499 88.600  1.00 44.09  ? 168 ARG B NE    1 
ATOM   5519 C  CZ    . ARG B 2 168 ? 132.882 118.782 88.007  1.00 43.78  ? 168 ARG B CZ    1 
ATOM   5520 N  NH1   . ARG B 2 168 ? 132.955 119.007 86.706  1.00 38.67  ? 168 ARG B NH1   1 
ATOM   5521 N  NH2   . ARG B 2 168 ? 133.990 118.843 88.740  1.00 45.11  ? 168 ARG B NH2   1 
ATOM   5522 N  N     . GLN B 2 169 ? 126.919 115.054 85.420  1.00 43.64  ? 169 GLN B N     1 
ATOM   5523 C  CA    . GLN B 2 169 ? 125.519 114.795 85.123  1.00 44.68  ? 169 GLN B CA    1 
ATOM   5524 C  C     . GLN B 2 169 ? 124.655 115.942 85.627  1.00 44.16  ? 169 GLN B C     1 
ATOM   5525 O  O     . GLN B 2 169 ? 124.961 116.570 86.643  1.00 46.46  ? 169 GLN B O     1 
ATOM   5526 C  CB    . GLN B 2 169 ? 125.074 113.477 85.753  1.00 45.77  ? 169 GLN B CB    1 
ATOM   5527 C  CG    . GLN B 2 169 ? 125.736 112.257 85.143  1.00 46.69  ? 169 GLN B CG    1 
ATOM   5528 C  CD    . GLN B 2 169 ? 124.928 110.994 85.341  1.00 52.02  ? 169 GLN B CD    1 
ATOM   5529 O  OE1   . GLN B 2 169 ? 123.920 110.993 86.044  1.00 54.10  ? 169 GLN B OE1   1 
ATOM   5530 N  NE2   . GLN B 2 169 ? 125.367 109.910 84.718  1.00 49.46  ? 169 GLN B NE2   1 
ATOM   5531 N  N     . ARG B 2 170 ? 123.571 116.220 84.900  1.00 44.78  ? 170 ARG B N     1 
ATOM   5532 C  CA    . ARG B 2 170 ? 122.710 117.343 85.257  1.00 46.55  ? 170 ARG B CA    1 
ATOM   5533 C  C     . ARG B 2 170 ? 122.039 117.125 86.606  1.00 45.56  ? 170 ARG B C     1 
ATOM   5534 O  O     . ARG B 2 170 ? 121.882 118.069 87.388  1.00 47.70  ? 170 ARG B O     1 
ATOM   5535 C  CB    . ARG B 2 170 ? 121.667 117.574 84.165  1.00 49.72  ? 170 ARG B CB    1 
ATOM   5536 C  CG    . ARG B 2 170 ? 122.258 118.041 82.848  1.00 61.87  ? 170 ARG B CG    1 
ATOM   5537 C  CD    . ARG B 2 170 ? 121.444 119.170 82.242  1.00 69.22  ? 170 ARG B CD    1 
ATOM   5538 N  NE    . ARG B 2 170 ? 120.014 118.889 82.265  1.00 75.00  ? 170 ARG B NE    1 
ATOM   5539 C  CZ    . ARG B 2 170 ? 119.386 118.134 81.375  1.00 77.92  ? 170 ARG B CZ    1 
ATOM   5540 N  NH1   . ARG B 2 170 ? 120.035 117.556 80.378  1.00 77.26  ? 170 ARG B NH1   1 
ATOM   5541 N  NH2   . ARG B 2 170 ? 118.073 117.956 81.486  1.00 75.28  ? 170 ARG B NH2   1 
ATOM   5542 N  N     . GLY B 2 171 ? 121.629 115.889 86.892  1.00 43.35  ? 171 GLY B N     1 
ATOM   5543 C  CA    . GLY B 2 171 ? 120.975 115.614 88.160  1.00 38.69  ? 171 GLY B CA    1 
ATOM   5544 C  C     . GLY B 2 171 ? 121.899 115.786 89.349  1.00 41.47  ? 171 GLY B C     1 
ATOM   5545 O  O     . GLY B 2 171 ? 121.476 116.241 90.413  1.00 41.72  ? 171 GLY B O     1 
ATOM   5546 N  N     . GLU B 2 172 ? 123.172 115.423 89.189  1.00 41.25  ? 172 GLU B N     1 
ATOM   5547 C  CA    . GLU B 2 172 ? 124.131 115.587 90.276  1.00 42.67  ? 172 GLU B CA    1 
ATOM   5548 C  C     . GLU B 2 172 ? 124.340 117.060 90.607  1.00 42.22  ? 172 GLU B C     1 
ATOM   5549 O  O     . GLU B 2 172 ? 124.339 117.454 91.781  1.00 45.30  ? 172 GLU B O     1 
ATOM   5550 C  CB    . GLU B 2 172 ? 125.455 114.920 89.904  1.00 45.36  ? 172 GLU B CB    1 
ATOM   5551 C  CG    . GLU B 2 172 ? 126.546 115.082 90.942  1.00 52.46  ? 172 GLU B CG    1 
ATOM   5552 C  CD    . GLU B 2 172 ? 127.880 115.440 90.327  1.00 62.07  ? 172 GLU B CD    1 
ATOM   5553 O  OE1   . GLU B 2 172 ? 128.283 114.772 89.353  1.00 60.74  ? 172 GLU B OE1   1 
ATOM   5554 O  OE2   . GLU B 2 172 ? 128.529 116.388 90.817  1.00 65.33  ? 172 GLU B OE2   1 
ATOM   5555 N  N     . VAL B 2 173 ? 124.504 117.893 89.578  1.00 42.61  ? 173 VAL B N     1 
ATOM   5556 C  CA    . VAL B 2 173 ? 124.654 119.329 89.795  1.00 40.41  ? 173 VAL B CA    1 
ATOM   5557 C  C     . VAL B 2 173 ? 123.385 119.909 90.400  1.00 38.40  ? 173 VAL B C     1 
ATOM   5558 O  O     . VAL B 2 173 ? 123.438 120.758 91.297  1.00 37.61  ? 173 VAL B O     1 
ATOM   5559 C  CB    . VAL B 2 173 ? 125.027 120.033 88.477  1.00 36.82  ? 173 VAL B CB    1 
ATOM   5560 C  CG1   . VAL B 2 173 ? 125.256 121.515 88.712  1.00 39.65  ? 173 VAL B CG1   1 
ATOM   5561 C  CG2   . VAL B 2 173 ? 126.260 119.395 87.868  1.00 44.46  ? 173 VAL B CG2   1 
ATOM   5562 N  N     . LEU B 2 174 ? 122.223 119.462 89.919  1.00 37.76  ? 174 LEU B N     1 
ATOM   5563 C  CA    . LEU B 2 174 ? 120.959 119.957 90.451  1.00 35.11  ? 174 LEU B CA    1 
ATOM   5564 C  C     . LEU B 2 174 ? 120.801 119.609 91.926  1.00 36.59  ? 174 LEU B C     1 
ATOM   5565 O  O     . LEU B 2 174 ? 120.353 120.441 92.723  1.00 41.19  ? 174 LEU B O     1 
ATOM   5566 C  CB    . LEU B 2 174 ? 119.800 119.391 89.633  1.00 34.34  ? 174 LEU B CB    1 
ATOM   5567 C  CG    . LEU B 2 174 ? 118.399 119.867 90.001  1.00 33.73  ? 174 LEU B CG    1 
ATOM   5568 C  CD1   . LEU B 2 174 ? 118.296 121.364 89.815  1.00 33.70  ? 174 LEU B CD1   1 
ATOM   5569 C  CD2   . LEU B 2 174 ? 117.361 119.150 89.163  1.00 40.74  ? 174 LEU B CD2   1 
ATOM   5570 N  N     . SER B 2 175 ? 121.156 118.380 92.308  1.00 39.35  ? 175 SER B N     1 
ATOM   5571 C  CA    . SER B 2 175 ? 121.081 117.988 93.711  1.00 40.21  ? 175 SER B CA    1 
ATOM   5572 C  C     . SER B 2 175 ? 122.066 118.779 94.560  1.00 40.76  ? 175 SER B C     1 
ATOM   5573 O  O     . SER B 2 175 ? 121.741 119.183 95.681  1.00 44.31  ? 175 SER B O     1 
ATOM   5574 C  CB    . SER B 2 175 ? 121.340 116.490 93.854  1.00 41.76  ? 175 SER B CB    1 
ATOM   5575 O  OG    . SER B 2 175 ? 122.622 116.152 93.358  1.00 43.63  ? 175 SER B OG    1 
ATOM   5576 N  N     . ARG B 2 176 ? 123.277 119.002 94.048  1.00 39.14  ? 176 ARG B N     1 
ATOM   5577 C  CA    . ARG B 2 176 ? 124.244 119.813 94.779  1.00 38.82  ? 176 ARG B CA    1 
ATOM   5578 C  C     . ARG B 2 176 ? 123.778 121.257 94.916  1.00 44.08  ? 176 ARG B C     1 
ATOM   5579 O  O     . ARG B 2 176 ? 124.164 121.946 95.867  1.00 47.60  ? 176 ARG B O     1 
ATOM   5580 C  CB    . ARG B 2 176 ? 125.601 119.755 94.080  1.00 38.88  ? 176 ARG B CB    1 
ATOM   5581 C  CG    . ARG B 2 176 ? 126.733 120.369 94.866  1.00 44.18  ? 176 ARG B CG    1 
ATOM   5582 C  CD    . ARG B 2 176 ? 128.054 120.142 94.165  1.00 50.20  ? 176 ARG B CD    1 
ATOM   5583 N  NE    . ARG B 2 176 ? 128.425 118.733 94.162  1.00 51.35  ? 176 ARG B NE    1 
ATOM   5584 C  CZ    . ARG B 2 176 ? 129.600 118.270 94.560  1.00 51.83  ? 176 ARG B CZ    1 
ATOM   5585 N  NH1   . ARG B 2 176 ? 130.552 119.081 94.987  1.00 49.53  ? 176 ARG B NH1   1 
ATOM   5586 N  NH2   . ARG B 2 176 ? 129.827 116.961 94.524  1.00 51.43  ? 176 ARG B NH2   1 
ATOM   5587 N  N     . VAL B 2 177 ? 122.951 121.726 93.988  1.00 45.15  ? 177 VAL B N     1 
ATOM   5588 C  CA    . VAL B 2 177 ? 122.511 123.115 93.996  1.00 38.30  ? 177 VAL B CA    1 
ATOM   5589 C  C     . VAL B 2 177 ? 121.207 123.305 94.767  1.00 38.66  ? 177 VAL B C     1 
ATOM   5590 O  O     . VAL B 2 177 ? 121.043 124.311 95.464  1.00 45.45  ? 177 VAL B O     1 
ATOM   5591 C  CB    . VAL B 2 177 ? 122.386 123.614 92.547  1.00 31.80  ? 177 VAL B CB    1 
ATOM   5592 C  CG1   . VAL B 2 177 ? 121.407 124.766 92.450  1.00 31.37  ? 177 VAL B CG1   1 
ATOM   5593 C  CG2   . VAL B 2 177 ? 123.748 124.016 92.015  1.00 34.83  ? 177 VAL B CG2   1 
ATOM   5594 N  N     . THR B 2 178 ? 120.275 122.361 94.668  1.00 36.11  ? 178 THR B N     1 
ATOM   5595 C  CA    . THR B 2 178 ? 118.978 122.471 95.320  1.00 34.36  ? 178 THR B CA    1 
ATOM   5596 C  C     . THR B 2 178 ? 118.875 121.631 96.584  1.00 38.34  ? 178 THR B C     1 
ATOM   5597 O  O     . THR B 2 178 ? 118.527 122.154 97.645  1.00 42.79  ? 178 THR B O     1 
ATOM   5598 C  CB    . THR B 2 178 ? 117.860 122.066 94.348  1.00 38.27  ? 178 THR B CB    1 
ATOM   5599 O  OG1   . THR B 2 178 ? 118.012 120.689 93.988  1.00 42.29  ? 178 THR B OG1   1 
ATOM   5600 C  CG2   . THR B 2 178 ? 117.905 122.917 93.095  1.00 32.79  ? 178 THR B CG2   1 
ATOM   5601 N  N     . ASN B 2 179 ? 119.165 120.333 96.493  1.00 40.62  ? 179 ASN B N     1 
ATOM   5602 C  CA    . ASN B 2 179 ? 118.955 119.438 97.626  1.00 39.74  ? 179 ASN B CA    1 
ATOM   5603 C  C     . ASN B 2 179 ? 119.910 119.743 98.773  1.00 41.44  ? 179 ASN B C     1 
ATOM   5604 O  O     . ASN B 2 179 ? 119.510 119.721 99.942  1.00 46.02  ? 179 ASN B O     1 
ATOM   5605 C  CB    . ASN B 2 179 ? 119.110 117.988 97.173  1.00 43.78  ? 179 ASN B CB    1 
ATOM   5606 C  CG    . ASN B 2 179 ? 117.929 117.506 96.361  1.00 55.82  ? 179 ASN B CG    1 
ATOM   5607 O  OD1   . ASN B 2 179 ? 116.832 118.053 96.454  1.00 55.98  ? 179 ASN B OD1   1 
ATOM   5608 N  ND2   . ASN B 2 179 ? 118.154 116.489 95.540  1.00 56.25  ? 179 ASN B ND2   1 
ATOM   5609 N  N     . ASP B 2 180 ? 121.179 120.017 98.464  1.00 39.13  ? 180 ASP B N     1 
ATOM   5610 C  CA    . ASP B 2 180 ? 122.163 120.237 99.519  1.00 37.65  ? 180 ASP B CA    1 
ATOM   5611 C  C     . ASP B 2 180 ? 121.880 121.517 100.293 1.00 40.53  ? 180 ASP B C     1 
ATOM   5612 O  O     . ASP B 2 180 ? 122.063 121.562 101.514 1.00 42.35  ? 180 ASP B O     1 
ATOM   5613 C  CB    . ASP B 2 180 ? 123.568 120.264 98.927  1.00 38.70  ? 180 ASP B CB    1 
ATOM   5614 C  CG    . ASP B 2 180 ? 124.076 118.884 98.583  1.00 48.08  ? 180 ASP B CG    1 
ATOM   5615 O  OD1   . ASP B 2 180 ? 123.442 117.895 99.001  1.00 47.43  ? 180 ASP B OD1   1 
ATOM   5616 O  OD2   . ASP B 2 180 ? 125.113 118.786 97.898  1.00 54.36  ? 180 ASP B OD2   1 
ATOM   5617 N  N     . VAL B 2 181 ? 121.439 122.570 99.602  1.00 39.85  ? 181 VAL B N     1 
ATOM   5618 C  CA    . VAL B 2 181 ? 121.105 123.817 100.283 1.00 34.62  ? 181 VAL B CA    1 
ATOM   5619 C  C     . VAL B 2 181 ? 119.909 123.620 101.209 1.00 35.08  ? 181 VAL B C     1 
ATOM   5620 O  O     . VAL B 2 181 ? 119.892 124.119 102.341 1.00 38.37  ? 181 VAL B O     1 
ATOM   5621 C  CB    . VAL B 2 181 ? 120.856 124.930 99.252  1.00 34.79  ? 181 VAL B CB    1 
ATOM   5622 C  CG1   . VAL B 2 181 ? 120.514 126.232 99.950  1.00 40.16  ? 181 VAL B CG1   1 
ATOM   5623 C  CG2   . VAL B 2 181 ? 122.081 125.107 98.375  1.00 29.46  ? 181 VAL B CG2   1 
ATOM   5624 N  N     . ASP B 2 182 ? 118.895 122.888 100.747 1.00 35.15  ? 182 ASP B N     1 
ATOM   5625 C  CA    . ASP B 2 182 ? 117.747 122.595 101.598 1.00 36.62  ? 182 ASP B CA    1 
ATOM   5626 C  C     . ASP B 2 182 ? 118.152 121.753 102.800 1.00 38.24  ? 182 ASP B C     1 
ATOM   5627 O  O     . ASP B 2 182 ? 117.639 121.950 103.908 1.00 40.55  ? 182 ASP B O     1 
ATOM   5628 C  CB    . ASP B 2 182 ? 116.663 121.887 100.787 1.00 41.34  ? 182 ASP B CB    1 
ATOM   5629 C  CG    . ASP B 2 182 ? 116.232 122.683 99.572  1.00 55.72  ? 182 ASP B CG    1 
ATOM   5630 O  OD1   . ASP B 2 182 ? 116.404 123.920 99.575  1.00 55.58  ? 182 ASP B OD1   1 
ATOM   5631 O  OD2   . ASP B 2 182 ? 115.725 122.070 98.609  1.00 59.62  ? 182 ASP B OD2   1 
ATOM   5632 N  N     . ASN B 2 183 ? 119.062 120.799 102.596 1.00 39.58  ? 183 ASN B N     1 
ATOM   5633 C  CA    . ASN B 2 183 ? 119.549 119.984 103.704 1.00 36.21  ? 183 ASN B CA    1 
ATOM   5634 C  C     . ASN B 2 183 ? 120.294 120.832 104.725 1.00 35.71  ? 183 ASN B C     1 
ATOM   5635 O  O     . ASN B 2 183 ? 120.141 120.636 105.936 1.00 41.41  ? 183 ASN B O     1 
ATOM   5636 C  CB    . ASN B 2 183 ? 120.440 118.864 103.170 1.00 36.86  ? 183 ASN B CB    1 
ATOM   5637 C  CG    . ASN B 2 183 ? 120.563 117.705 104.133 1.00 42.37  ? 183 ASN B CG    1 
ATOM   5638 O  OD1   . ASN B 2 183 ? 121.546 117.590 104.862 1.00 42.25  ? 183 ASN B OD1   1 
ATOM   5639 N  ND2   . ASN B 2 183 ? 119.561 116.836 104.142 1.00 47.69  ? 183 ASN B ND2   1 
ATOM   5640 N  N     . ILE B 2 184 ? 121.109 121.779 104.256 1.00 33.30  ? 184 ILE B N     1 
ATOM   5641 C  CA    . ILE B 2 184 ? 121.797 122.691 105.168 1.00 33.55  ? 184 ILE B CA    1 
ATOM   5642 C  C     . ILE B 2 184 ? 120.785 123.510 105.958 1.00 41.34  ? 184 ILE B C     1 
ATOM   5643 O  O     . ILE B 2 184 ? 120.912 123.679 107.177 1.00 42.30  ? 184 ILE B O     1 
ATOM   5644 C  CB    . ILE B 2 184 ? 122.769 123.600 104.396 1.00 33.37  ? 184 ILE B CB    1 
ATOM   5645 C  CG1   . ILE B 2 184 ? 123.920 122.787 103.811 1.00 34.17  ? 184 ILE B CG1   1 
ATOM   5646 C  CG2   . ILE B 2 184 ? 123.314 124.683 105.303 1.00 36.00  ? 184 ILE B CG2   1 
ATOM   5647 C  CD1   . ILE B 2 184 ? 124.591 123.457 102.642 1.00 30.28  ? 184 ILE B CD1   1 
ATOM   5648 N  N     . GLN B 2 185 ? 119.766 124.035 105.272 1.00 41.62  ? 185 GLN B N     1 
ATOM   5649 C  CA    . GLN B 2 185 ? 118.720 124.792 105.954 1.00 37.82  ? 185 GLN B CA    1 
ATOM   5650 C  C     . GLN B 2 185 ? 118.062 123.963 107.047 1.00 39.17  ? 185 GLN B C     1 
ATOM   5651 O  O     . GLN B 2 185 ? 117.907 124.422 108.185 1.00 42.84  ? 185 GLN B O     1 
ATOM   5652 C  CB    . GLN B 2 185 ? 117.667 125.263 104.952 1.00 41.09  ? 185 GLN B CB    1 
ATOM   5653 C  CG    . GLN B 2 185 ? 117.091 126.627 105.264 1.00 48.14  ? 185 GLN B CG    1 
ATOM   5654 C  CD    . GLN B 2 185 ? 115.625 126.737 104.922 1.00 59.94  ? 185 GLN B CD    1 
ATOM   5655 O  OE1   . GLN B 2 185 ? 114.798 125.996 105.450 1.00 69.29  ? 185 GLN B OE1   1 
ATOM   5656 N  NE2   . GLN B 2 185 ? 115.290 127.669 104.037 1.00 58.57  ? 185 GLN B NE2   1 
ATOM   5657 N  N     . ASN B 2 186 ? 117.660 122.736 106.715 1.00 38.46  ? 186 ASN B N     1 
ATOM   5658 C  CA    . ASN B 2 186 ? 116.960 121.898 107.681 1.00 39.03  ? 186 ASN B CA    1 
ATOM   5659 C  C     . ASN B 2 186 ? 117.849 121.566 108.872 1.00 44.09  ? 186 ASN B C     1 
ATOM   5660 O  O     . ASN B 2 186 ? 117.427 121.687 110.029 1.00 50.51  ? 186 ASN B O     1 
ATOM   5661 C  CB    . ASN B 2 186 ? 116.467 120.624 107.001 1.00 40.54  ? 186 ASN B CB    1 
ATOM   5662 C  CG    . ASN B 2 186 ? 114.995 120.679 106.670 1.00 55.68  ? 186 ASN B CG    1 
ATOM   5663 O  OD1   . ASN B 2 186 ? 114.178 120.023 107.315 1.00 66.78  ? 186 ASN B OD1   1 
ATOM   5664 N  ND2   . ASN B 2 186 ? 114.643 121.473 105.667 1.00 51.78  ? 186 ASN B ND2   1 
ATOM   5665 N  N     . SER B 2 187 ? 119.092 121.159 108.608 1.00 40.45  ? 187 SER B N     1 
ATOM   5666 C  CA    . SER B 2 187 ? 119.993 120.794 109.694 1.00 34.33  ? 187 SER B CA    1 
ATOM   5667 C  C     . SER B 2 187 ? 120.270 121.981 110.604 1.00 36.99  ? 187 SER B C     1 
ATOM   5668 O  O     . SER B 2 187 ? 120.252 121.847 111.833 1.00 44.01  ? 187 SER B O     1 
ATOM   5669 C  CB    . SER B 2 187 ? 121.296 120.238 109.125 1.00 34.22  ? 187 SER B CB    1 
ATOM   5670 O  OG    . SER B 2 187 ? 121.043 119.138 108.272 1.00 44.27  ? 187 SER B OG    1 
ATOM   5671 N  N     . VAL B 2 188 ? 120.515 123.156 110.022 1.00 38.55  ? 188 VAL B N     1 
ATOM   5672 C  CA    . VAL B 2 188 ? 120.795 124.331 110.838 1.00 36.81  ? 188 VAL B CA    1 
ATOM   5673 C  C     . VAL B 2 188 ? 119.577 124.695 111.675 1.00 38.40  ? 188 VAL B C     1 
ATOM   5674 O  O     . VAL B 2 188 ? 119.671 124.855 112.897 1.00 43.62  ? 188 VAL B O     1 
ATOM   5675 C  CB    . VAL B 2 188 ? 121.249 125.503 109.951 1.00 37.07  ? 188 VAL B CB    1 
ATOM   5676 C  CG1   . VAL B 2 188 ? 121.208 126.797 110.732 1.00 40.91  ? 188 VAL B CG1   1 
ATOM   5677 C  CG2   . VAL B 2 188 ? 122.647 125.244 109.423 1.00 39.68  ? 188 VAL B CG2   1 
ATOM   5678 N  N     . SER B 2 189 ? 118.406 124.788 111.041 1.00 41.77  ? 189 SER B N     1 
ATOM   5679 C  CA    . SER B 2 189 ? 117.204 125.179 111.767 1.00 44.12  ? 189 SER B CA    1 
ATOM   5680 C  C     . SER B 2 189 ? 116.806 124.161 112.826 1.00 44.73  ? 189 SER B C     1 
ATOM   5681 O  O     . SER B 2 189 ? 116.087 124.516 113.766 1.00 50.61  ? 189 SER B O     1 
ATOM   5682 C  CB    . SER B 2 189 ? 116.045 125.392 110.795 1.00 36.62  ? 189 SER B CB    1 
ATOM   5683 O  OG    . SER B 2 189 ? 115.630 124.165 110.225 1.00 37.89  ? 189 SER B OG    1 
ATOM   5684 N  N     . MET B 2 190 ? 117.242 122.909 112.703 1.00 41.14  ? 190 MET B N     1 
ATOM   5685 C  CA    . MET B 2 190 ? 116.925 121.917 113.720 1.00 42.64  ? 190 MET B CA    1 
ATOM   5686 C  C     . MET B 2 190 ? 118.030 121.714 114.750 1.00 47.01  ? 190 MET B C     1 
ATOM   5687 O  O     . MET B 2 190 ? 117.796 121.022 115.745 1.00 48.13  ? 190 MET B O     1 
ATOM   5688 C  CB    . MET B 2 190 ? 116.588 120.571 113.066 1.00 39.91  ? 190 MET B CB    1 
ATOM   5689 C  CG    . MET B 2 190 ? 115.304 120.594 112.254 1.00 55.79  ? 190 MET B CG    1 
ATOM   5690 S  SD    . MET B 2 190 ? 114.829 119.001 111.551 1.00 77.50  ? 190 MET B SD    1 
ATOM   5691 C  CE    . MET B 2 190 ? 116.390 118.133 111.555 1.00 54.30  ? 190 MET B CE    1 
ATOM   5692 N  N     . THR B 2 191 ? 119.222 122.282 114.551 1.00 45.19  ? 191 THR B N     1 
ATOM   5693 C  CA    . THR B 2 191 ? 120.314 122.024 115.484 1.00 42.06  ? 191 THR B CA    1 
ATOM   5694 C  C     . THR B 2 191 ? 120.983 123.249 116.100 1.00 42.46  ? 191 THR B C     1 
ATOM   5695 O  O     . THR B 2 191 ? 121.647 123.085 117.129 1.00 50.61  ? 191 THR B O     1 
ATOM   5696 C  CB    . THR B 2 191 ? 121.409 121.183 114.810 1.00 41.66  ? 191 THR B CB    1 
ATOM   5697 O  OG1   . THR B 2 191 ? 121.915 121.881 113.667 1.00 46.90  ? 191 THR B OG1   1 
ATOM   5698 C  CG2   . THR B 2 191 ? 120.863 119.837 114.376 1.00 41.68  ? 191 THR B CG2   1 
ATOM   5699 N  N     . ILE B 2 192 ? 120.864 124.449 115.524 1.00 43.48  ? 192 ILE B N     1 
ATOM   5700 C  CA    . ILE B 2 192 ? 121.739 125.542 115.954 1.00 46.22  ? 192 ILE B CA    1 
ATOM   5701 C  C     . ILE B 2 192 ? 121.392 126.006 117.370 1.00 47.48  ? 192 ILE B C     1 
ATOM   5702 O  O     . ILE B 2 192 ? 122.286 126.238 118.200 1.00 50.02  ? 192 ILE B O     1 
ATOM   5703 C  CB    . ILE B 2 192 ? 121.705 126.696 114.930 1.00 42.97  ? 192 ILE B CB    1 
ATOM   5704 C  CG1   . ILE B 2 192 ? 122.715 127.785 115.300 1.00 46.09  ? 192 ILE B CG1   1 
ATOM   5705 C  CG2   . ILE B 2 192 ? 120.308 127.280 114.779 1.00 47.07  ? 192 ILE B CG2   1 
ATOM   5706 C  CD1   . ILE B 2 192 ? 124.145 127.298 115.351 1.00 48.87  ? 192 ILE B CD1   1 
ATOM   5707 N  N     . SER B 2 193 ? 120.099 126.149 117.672 1.00 47.39  ? 193 SER B N     1 
ATOM   5708 C  CA    . SER B 2 193 ? 119.691 126.593 119.001 1.00 47.61  ? 193 SER B CA    1 
ATOM   5709 C  C     . SER B 2 193 ? 120.044 125.557 120.057 1.00 49.60  ? 193 SER B C     1 
ATOM   5710 O  O     . SER B 2 193 ? 120.515 125.904 121.147 1.00 50.83  ? 193 SER B O     1 
ATOM   5711 C  CB    . SER B 2 193 ? 118.193 126.889 119.014 1.00 53.86  ? 193 SER B CB    1 
ATOM   5712 O  OG    . SER B 2 193 ? 117.782 127.420 120.261 1.00 57.39  ? 193 SER B OG    1 
ATOM   5713 N  N     . GLN B 2 194 ? 119.826 124.278 119.743 1.00 51.27  ? 194 GLN B N     1 
ATOM   5714 C  CA    . GLN B 2 194 ? 120.231 123.202 120.637 1.00 46.39  ? 194 GLN B CA    1 
ATOM   5715 C  C     . GLN B 2 194 ? 121.727 123.253 120.901 1.00 46.41  ? 194 GLN B C     1 
ATOM   5716 O  O     . GLN B 2 194 ? 122.168 123.095 122.043 1.00 50.34  ? 194 GLN B O     1 
ATOM   5717 C  CB    . GLN B 2 194 ? 119.859 121.852 120.028 1.00 50.93  ? 194 GLN B CB    1 
ATOM   5718 C  CG    . GLN B 2 194 ? 118.377 121.516 120.009 1.00 54.71  ? 194 GLN B CG    1 
ATOM   5719 C  CD    . GLN B 2 194 ? 117.679 121.990 118.745 1.00 64.94  ? 194 GLN B CD    1 
ATOM   5720 O  OE1   . GLN B 2 194 ? 118.026 123.024 118.173 1.00 63.39  ? 194 GLN B OE1   1 
ATOM   5721 N  NE2   . GLN B 2 194 ? 116.723 121.201 118.272 1.00 64.06  ? 194 GLN B NE2   1 
ATOM   5722 N  N     . LEU B 2 195 ? 122.525 123.480 119.856 1.00 46.38  ? 195 LEU B N     1 
ATOM   5723 C  CA    . LEU B 2 195 ? 123.971 123.544 120.026 1.00 43.55  ? 195 LEU B CA    1 
ATOM   5724 C  C     . LEU B 2 195 ? 124.363 124.670 120.971 1.00 47.19  ? 195 LEU B C     1 
ATOM   5725 O  O     . LEU B 2 195 ? 125.128 124.463 121.922 1.00 50.55  ? 195 LEU B O     1 
ATOM   5726 C  CB    . LEU B 2 195 ? 124.656 123.728 118.672 1.00 44.84  ? 195 LEU B CB    1 
ATOM   5727 C  CG    . LEU B 2 195 ? 124.955 122.470 117.858 1.00 48.86  ? 195 LEU B CG    1 
ATOM   5728 C  CD1   . LEU B 2 195 ? 125.238 122.810 116.402 1.00 41.42  ? 195 LEU B CD1   1 
ATOM   5729 C  CD2   . LEU B 2 195 ? 126.098 121.686 118.480 1.00 51.04  ? 195 LEU B CD2   1 
ATOM   5730 N  N     . LEU B 2 196 ? 123.846 125.876 120.721 1.00 47.44  ? 196 LEU B N     1 
ATOM   5731 C  CA    . LEU B 2 196 ? 124.218 127.019 121.551 1.00 48.66  ? 196 LEU B CA    1 
ATOM   5732 C  C     . LEU B 2 196 ? 123.789 126.815 122.999 1.00 50.16  ? 196 LEU B C     1 
ATOM   5733 O  O     . LEU B 2 196 ? 124.582 127.018 123.934 1.00 51.55  ? 196 LEU B O     1 
ATOM   5734 C  CB    . LEU B 2 196 ? 123.610 128.300 120.981 1.00 46.07  ? 196 LEU B CB    1 
ATOM   5735 C  CG    . LEU B 2 196 ? 124.159 128.731 119.623 1.00 54.46  ? 196 LEU B CG    1 
ATOM   5736 C  CD1   . LEU B 2 196 ? 123.410 129.937 119.103 1.00 60.78  ? 196 LEU B CD1   1 
ATOM   5737 C  CD2   . LEU B 2 196 ? 125.641 129.031 119.732 1.00 52.24  ? 196 LEU B CD2   1 
ATOM   5738 N  N     . THR B 2 197 ? 122.536 126.399 123.206 1.00 47.41  ? 197 THR B N     1 
ATOM   5739 C  CA    . THR B 2 197 ? 122.042 126.214 124.563 1.00 47.07  ? 197 THR B CA    1 
ATOM   5740 C  C     . THR B 2 197 ? 122.823 125.129 125.286 1.00 48.27  ? 197 THR B C     1 
ATOM   5741 O  O     . THR B 2 197 ? 123.144 125.279 126.467 1.00 50.66  ? 197 THR B O     1 
ATOM   5742 C  CB    . THR B 2 197 ? 120.549 125.884 124.553 1.00 49.33  ? 197 THR B CB    1 
ATOM   5743 O  OG1   . THR B 2 197 ? 120.303 124.775 123.682 1.00 54.72  ? 197 THR B OG1   1 
ATOM   5744 C  CG2   . THR B 2 197 ? 119.738 127.084 124.086 1.00 46.13  ? 197 THR B CG2   1 
ATOM   5745 N  N     . SER B 2 198 ? 123.147 124.034 124.595 1.00 45.73  ? 198 SER B N     1 
ATOM   5746 C  CA    . SER B 2 198 ? 123.885 122.947 125.226 1.00 45.49  ? 198 SER B CA    1 
ATOM   5747 C  C     . SER B 2 198 ? 125.281 123.391 125.642 1.00 47.44  ? 198 SER B C     1 
ATOM   5748 O  O     . SER B 2 198 ? 125.726 123.108 126.764 1.00 53.30  ? 198 SER B O     1 
ATOM   5749 C  CB    . SER B 2 198 ? 123.956 121.757 124.272 1.00 47.97  ? 198 SER B CB    1 
ATOM   5750 O  OG    . SER B 2 198 ? 122.657 121.262 123.996 1.00 54.14  ? 198 SER B OG    1 
ATOM   5751 N  N     . VAL B 2 199 ? 125.988 124.095 124.754 1.00 50.55  ? 199 VAL B N     1 
ATOM   5752 C  CA    . VAL B 2 199 ? 127.338 124.535 125.091 1.00 53.68  ? 199 VAL B CA    1 
ATOM   5753 C  C     . VAL B 2 199 ? 127.310 125.479 126.284 1.00 54.29  ? 199 VAL B C     1 
ATOM   5754 O  O     . VAL B 2 199 ? 128.128 125.358 127.202 1.00 53.64  ? 199 VAL B O     1 
ATOM   5755 C  CB    . VAL B 2 199 ? 128.027 125.176 123.873 1.00 56.12  ? 199 VAL B CB    1 
ATOM   5756 C  CG1   . VAL B 2 199 ? 129.419 125.651 124.249 1.00 52.57  ? 199 VAL B CG1   1 
ATOM   5757 C  CG2   . VAL B 2 199 ? 128.121 124.176 122.741 1.00 55.61  ? 199 VAL B CG2   1 
ATOM   5758 N  N     . LEU B 2 200 ? 126.370 126.428 126.303 1.00 51.52  ? 200 LEU B N     1 
ATOM   5759 C  CA    . LEU B 2 200 ? 126.311 127.346 127.440 1.00 48.70  ? 200 LEU B CA    1 
ATOM   5760 C  C     . LEU B 2 200 ? 125.915 126.623 128.727 1.00 49.08  ? 200 LEU B C     1 
ATOM   5761 O  O     . LEU B 2 200 ? 126.484 126.883 129.801 1.00 52.60  ? 200 LEU B O     1 
ATOM   5762 C  CB    . LEU B 2 200 ? 125.342 128.484 127.135 1.00 51.39  ? 200 LEU B CB    1 
ATOM   5763 C  CG    . LEU B 2 200 ? 125.725 129.309 125.907 1.00 50.69  ? 200 LEU B CG    1 
ATOM   5764 C  CD1   . LEU B 2 200 ? 124.712 130.406 125.654 1.00 49.02  ? 200 LEU B CD1   1 
ATOM   5765 C  CD2   . LEU B 2 200 ? 127.123 129.883 126.062 1.00 45.49  ? 200 LEU B CD2   1 
ATOM   5766 N  N     . THR B 2 201 ? 124.950 125.705 128.630 1.00 48.34  ? 201 THR B N     1 
ATOM   5767 C  CA    . THR B 2 201 ? 124.428 125.020 129.803 1.00 45.11  ? 201 THR B CA    1 
ATOM   5768 C  C     . THR B 2 201 ? 125.492 124.159 130.460 1.00 44.13  ? 201 THR B C     1 
ATOM   5769 O  O     . THR B 2 201 ? 125.547 124.068 131.690 1.00 48.06  ? 201 THR B O     1 
ATOM   5770 C  CB    . THR B 2 201 ? 123.220 124.168 129.413 1.00 45.49  ? 201 THR B CB    1 
ATOM   5771 O  OG1   . THR B 2 201 ? 122.236 124.994 128.782 1.00 48.65  ? 201 THR B OG1   1 
ATOM   5772 C  CG2   . THR B 2 201 ? 122.605 123.508 130.636 1.00 45.01  ? 201 THR B CG2   1 
ATOM   5773 N  N     . VAL B 2 202 ? 126.341 123.511 129.660 1.00 44.62  ? 202 VAL B N     1 
ATOM   5774 C  CA    . VAL B 2 202 ? 127.362 122.643 130.240 1.00 46.22  ? 202 VAL B CA    1 
ATOM   5775 C  C     . VAL B 2 202 ? 128.243 123.428 131.206 1.00 45.45  ? 202 VAL B C     1 
ATOM   5776 O  O     . VAL B 2 202 ? 128.431 123.032 132.362 1.00 45.87  ? 202 VAL B O     1 
ATOM   5777 C  CB    . VAL B 2 202 ? 128.188 121.966 129.132 1.00 49.13  ? 202 VAL B CB    1 
ATOM   5778 C  CG1   . VAL B 2 202 ? 129.535 121.523 129.666 1.00 45.51  ? 202 VAL B CG1   1 
ATOM   5779 C  CG2   . VAL B 2 202 ? 127.428 120.773 128.571 1.00 44.52  ? 202 VAL B CG2   1 
ATOM   5780 N  N     . PHE B 2 203 ? 128.754 124.580 130.766 1.00 49.24  ? 203 PHE B N     1 
ATOM   5781 C  CA    . PHE B 2 203 ? 129.645 125.357 131.623 1.00 52.77  ? 203 PHE B CA    1 
ATOM   5782 C  C     . PHE B 2 203 ? 128.901 126.006 132.787 1.00 48.62  ? 203 PHE B C     1 
ATOM   5783 O  O     . PHE B 2 203 ? 129.431 126.062 133.903 1.00 47.48  ? 203 PHE B O     1 
ATOM   5784 C  CB    . PHE B 2 203 ? 130.397 126.408 130.806 1.00 59.85  ? 203 PHE B CB    1 
ATOM   5785 C  CG    . PHE B 2 203 ? 131.262 125.827 129.726 1.00 68.19  ? 203 PHE B CG    1 
ATOM   5786 C  CD1   . PHE B 2 203 ? 130.766 125.620 128.454 1.00 68.48  ? 203 PHE B CD1   1 
ATOM   5787 C  CD2   . PHE B 2 203 ? 132.575 125.476 129.991 1.00 70.15  ? 203 PHE B CD2   1 
ATOM   5788 C  CE1   . PHE B 2 203 ? 131.560 125.080 127.462 1.00 73.41  ? 203 PHE B CE1   1 
ATOM   5789 C  CE2   . PHE B 2 203 ? 133.374 124.936 129.004 1.00 76.10  ? 203 PHE B CE2   1 
ATOM   5790 C  CZ    . PHE B 2 203 ? 132.866 124.738 127.737 1.00 78.67  ? 203 PHE B CZ    1 
ATOM   5791 N  N     . ALA B 2 204 ? 127.680 126.504 132.561 1.00 44.57  ? 204 ALA B N     1 
ATOM   5792 C  CA    . ALA B 2 204 ? 126.943 127.111 133.670 1.00 41.78  ? 204 ALA B CA    1 
ATOM   5793 C  C     . ALA B 2 204 ? 126.658 126.087 134.768 1.00 43.23  ? 204 ALA B C     1 
ATOM   5794 O  O     . ALA B 2 204 ? 126.855 126.355 135.965 1.00 47.53  ? 204 ALA B O     1 
ATOM   5795 C  CB    . ALA B 2 204 ? 125.645 127.733 133.159 1.00 40.12  ? 204 ALA B CB    1 
ATOM   5796 N  N     . VAL B 2 205 ? 126.214 124.893 134.372 1.00 43.97  ? 205 VAL B N     1 
ATOM   5797 C  CA    . VAL B 2 205 ? 125.929 123.842 135.337 1.00 39.02  ? 205 VAL B CA    1 
ATOM   5798 C  C     . VAL B 2 205 ? 127.207 123.377 136.018 1.00 41.76  ? 205 VAL B C     1 
ATOM   5799 O  O     . VAL B 2 205 ? 127.209 123.087 137.217 1.00 47.39  ? 205 VAL B O     1 
ATOM   5800 C  CB    . VAL B 2 205 ? 125.197 122.679 134.647 1.00 35.01  ? 205 VAL B CB    1 
ATOM   5801 C  CG1   . VAL B 2 205 ? 125.133 121.491 135.567 1.00 36.39  ? 205 VAL B CG1   1 
ATOM   5802 C  CG2   . VAL B 2 205 ? 123.806 123.108 134.238 1.00 36.88  ? 205 VAL B CG2   1 
ATOM   5803 N  N     . LEU B 2 206 ? 128.312 123.294 135.272 1.00 43.41  ? 206 LEU B N     1 
ATOM   5804 C  CA    . LEU B 2 206 ? 129.579 122.921 135.888 1.00 41.64  ? 206 LEU B CA    1 
ATOM   5805 C  C     . LEU B 2 206 ? 129.983 123.931 136.951 1.00 42.73  ? 206 LEU B C     1 
ATOM   5806 O  O     . LEU B 2 206 ? 130.481 123.556 138.018 1.00 46.02  ? 206 LEU B O     1 
ATOM   5807 C  CB    . LEU B 2 206 ? 130.665 122.798 134.822 1.00 45.05  ? 206 LEU B CB    1 
ATOM   5808 C  CG    . LEU B 2 206 ? 131.999 122.214 135.283 1.00 47.73  ? 206 LEU B CG    1 
ATOM   5809 C  CD1   . LEU B 2 206 ? 131.838 120.745 135.620 1.00 52.75  ? 206 LEU B CD1   1 
ATOM   5810 C  CD2   . LEU B 2 206 ? 133.066 122.408 134.221 1.00 45.32  ? 206 LEU B CD2   1 
ATOM   5811 N  N     . VAL B 2 207 ? 129.768 125.220 136.680 1.00 43.68  ? 207 VAL B N     1 
ATOM   5812 C  CA    . VAL B 2 207 ? 130.087 126.253 137.662 1.00 41.88  ? 207 VAL B CA    1 
ATOM   5813 C  C     . VAL B 2 207 ? 129.248 126.070 138.921 1.00 43.52  ? 207 VAL B C     1 
ATOM   5814 O  O     . VAL B 2 207 ? 129.760 126.130 140.047 1.00 48.11  ? 207 VAL B O     1 
ATOM   5815 C  CB    . VAL B 2 207 ? 129.887 127.651 137.049 1.00 41.22  ? 207 VAL B CB    1 
ATOM   5816 C  CG1   . VAL B 2 207 ? 129.853 128.710 138.136 1.00 40.16  ? 207 VAL B CG1   1 
ATOM   5817 C  CG2   . VAL B 2 207 ? 130.985 127.949 136.046 1.00 41.46  ? 207 VAL B CG2   1 
ATOM   5818 N  N     . MET B 2 208 ? 127.946 125.833 138.753 1.00 42.72  ? 208 MET B N     1 
ATOM   5819 C  CA    . MET B 2 208 ? 127.095 125.707 139.935 1.00 39.33  ? 208 MET B CA    1 
ATOM   5820 C  C     . MET B 2 208 ? 127.405 124.436 140.725 1.00 43.77  ? 208 MET B C     1 
ATOM   5821 O  O     . MET B 2 208 ? 127.348 124.436 141.962 1.00 45.41  ? 208 MET B O     1 
ATOM   5822 C  CB    . MET B 2 208 ? 125.623 125.762 139.540 1.00 37.58  ? 208 MET B CB    1 
ATOM   5823 C  CG    . MET B 2 208 ? 125.224 127.089 138.933 1.00 42.94  ? 208 MET B CG    1 
ATOM   5824 S  SD    . MET B 2 208 ? 124.828 128.357 140.151 1.00 67.53  ? 208 MET B SD    1 
ATOM   5825 C  CE    . MET B 2 208 ? 124.033 127.387 141.423 1.00 45.20  ? 208 MET B CE    1 
ATOM   5826 N  N     . MET B 2 209 ? 127.737 123.344 140.033 1.00 44.98  ? 209 MET B N     1 
ATOM   5827 C  CA    . MET B 2 209 ? 128.142 122.123 140.725 1.00 40.37  ? 209 MET B CA    1 
ATOM   5828 C  C     . MET B 2 209 ? 129.470 122.304 141.449 1.00 40.19  ? 209 MET B C     1 
ATOM   5829 O  O     . MET B 2 209 ? 129.676 121.731 142.523 1.00 39.21  ? 209 MET B O     1 
ATOM   5830 C  CB    . MET B 2 209 ? 128.210 120.956 139.741 1.00 37.97  ? 209 MET B CB    1 
ATOM   5831 C  CG    . MET B 2 209 ? 126.898 120.667 139.037 1.00 39.22  ? 209 MET B CG    1 
ATOM   5832 S  SD    . MET B 2 209 ? 126.896 119.130 138.103 1.00 51.61  ? 209 MET B SD    1 
ATOM   5833 C  CE    . MET B 2 209 ? 128.621 119.008 137.657 1.00 39.17  ? 209 MET B CE    1 
ATOM   5834 N  N     . LEU B 2 210 ? 130.387 123.086 140.876 1.00 43.73  ? 210 LEU B N     1 
ATOM   5835 C  CA    . LEU B 2 210 ? 131.597 123.448 141.607 1.00 43.92  ? 210 LEU B CA    1 
ATOM   5836 C  C     . LEU B 2 210 ? 131.248 124.230 142.864 1.00 45.08  ? 210 LEU B C     1 
ATOM   5837 O  O     . LEU B 2 210 ? 131.878 124.055 143.914 1.00 44.87  ? 210 LEU B O     1 
ATOM   5838 C  CB    . LEU B 2 210 ? 132.532 124.273 140.724 1.00 39.90  ? 210 LEU B CB    1 
ATOM   5839 C  CG    . LEU B 2 210 ? 133.764 123.583 140.141 1.00 40.29  ? 210 LEU B CG    1 
ATOM   5840 C  CD1   . LEU B 2 210 ? 134.639 123.018 141.249 1.00 38.58  ? 210 LEU B CD1   1 
ATOM   5841 C  CD2   . LEU B 2 210 ? 133.380 122.519 139.132 1.00 46.00  ? 210 LEU B CD2   1 
ATOM   5842 N  N     . THR B 2 211 ? 130.251 125.110 142.765 1.00 43.95  ? 211 THR B N     1 
ATOM   5843 C  CA    . THR B 2 211 ? 129.804 125.867 143.929 1.00 43.84  ? 211 THR B CA    1 
ATOM   5844 C  C     . THR B 2 211 ? 129.274 124.944 145.022 1.00 46.94  ? 211 THR B C     1 
ATOM   5845 O  O     . THR B 2 211 ? 129.579 125.134 146.205 1.00 50.31  ? 211 THR B O     1 
ATOM   5846 C  CB    . THR B 2 211 ? 128.737 126.881 143.513 1.00 48.14  ? 211 THR B CB    1 
ATOM   5847 O  OG1   . THR B 2 211 ? 129.368 128.039 142.956 1.00 52.38  ? 211 THR B OG1   1 
ATOM   5848 C  CG2   . THR B 2 211 ? 127.892 127.300 144.702 1.00 44.91  ? 211 THR B CG2   1 
ATOM   5849 N  N     . ILE B 2 212 ? 128.491 123.929 144.649 1.00 48.42  ? 212 ILE B N     1 
ATOM   5850 C  CA    . ILE B 2 212 ? 127.863 123.075 145.659 1.00 44.48  ? 212 ILE B CA    1 
ATOM   5851 C  C     . ILE B 2 212 ? 128.897 122.174 146.329 1.00 43.15  ? 212 ILE B C     1 
ATOM   5852 O  O     . ILE B 2 212 ? 129.094 122.231 147.547 1.00 43.16  ? 212 ILE B O     1 
ATOM   5853 C  CB    . ILE B 2 212 ? 126.718 122.251 145.046 1.00 41.64  ? 212 ILE B CB    1 
ATOM   5854 C  CG1   . ILE B 2 212 ? 125.555 123.161 144.660 1.00 41.13  ? 212 ILE B CG1   1 
ATOM   5855 C  CG2   . ILE B 2 212 ? 126.241 121.203 146.032 1.00 33.17  ? 212 ILE B CG2   1 
ATOM   5856 C  CD1   . ILE B 2 212 ? 124.536 122.497 143.772 1.00 38.56  ? 212 ILE B CD1   1 
ATOM   5857 N  N     . SER B 2 213 ? 129.564 121.318 145.550 1.00 45.11  ? 213 SER B N     1 
ATOM   5858 C  CA    . SER B 2 213 ? 130.507 120.369 146.137 1.00 42.69  ? 213 SER B CA    1 
ATOM   5859 C  C     . SER B 2 213 ? 131.553 119.909 145.127 1.00 44.37  ? 213 SER B C     1 
ATOM   5860 O  O     . SER B 2 213 ? 131.203 119.371 144.070 1.00 47.31  ? 213 SER B O     1 
ATOM   5861 C  CB    . SER B 2 213 ? 129.761 119.160 146.698 1.00 43.32  ? 213 SER B CB    1 
ATOM   5862 O  OG    . SER B 2 213 ? 129.689 118.125 145.737 1.00 47.25  ? 213 SER B OG    1 
ATOM   5863 N  N     . PRO B 2 214 ? 132.841 120.103 145.418 1.00 45.60  ? 214 PRO B N     1 
ATOM   5864 C  CA    . PRO B 2 214 ? 133.884 119.710 144.455 1.00 43.44  ? 214 PRO B CA    1 
ATOM   5865 C  C     . PRO B 2 214 ? 133.950 118.218 144.169 1.00 48.18  ? 214 PRO B C     1 
ATOM   5866 O  O     . PRO B 2 214 ? 134.270 117.830 143.039 1.00 52.65  ? 214 PRO B O     1 
ATOM   5867 C  CB    . PRO B 2 214 ? 135.173 120.211 145.120 1.00 47.75  ? 214 PRO B CB    1 
ATOM   5868 C  CG    . PRO B 2 214 ? 134.727 121.266 146.075 1.00 50.21  ? 214 PRO B CG    1 
ATOM   5869 C  CD    . PRO B 2 214 ? 133.405 120.799 146.584 1.00 47.08  ? 214 PRO B CD    1 
ATOM   5870 N  N     . LEU B 2 215 ? 133.674 117.363 145.153 1.00 47.10  ? 215 LEU B N     1 
ATOM   5871 C  CA    . LEU B 2 215 ? 133.829 115.926 144.938 1.00 43.96  ? 215 LEU B CA    1 
ATOM   5872 C  C     . LEU B 2 215 ? 132.791 115.401 143.952 1.00 46.61  ? 215 LEU B C     1 
ATOM   5873 O  O     . LEU B 2 215 ? 133.123 114.684 142.997 1.00 49.22  ? 215 LEU B O     1 
ATOM   5874 C  CB    . LEU B 2 215 ? 133.731 115.191 146.274 1.00 44.56  ? 215 LEU B CB    1 
ATOM   5875 C  CG    . LEU B 2 215 ? 134.117 113.714 146.266 1.00 49.87  ? 215 LEU B CG    1 
ATOM   5876 C  CD1   . LEU B 2 215 ? 135.593 113.557 145.949 1.00 45.20  ? 215 LEU B CD1   1 
ATOM   5877 C  CD2   . LEU B 2 215 ? 133.781 113.071 147.598 1.00 46.04  ? 215 LEU B CD2   1 
ATOM   5878 N  N     . LEU B 2 216 ? 131.527 115.758 144.161 1.00 44.07  ? 216 LEU B N     1 
ATOM   5879 C  CA    . LEU B 2 216 ? 130.478 115.291 143.267 1.00 40.53  ? 216 LEU B CA    1 
ATOM   5880 C  C     . LEU B 2 216 ? 130.591 115.926 141.888 1.00 43.03  ? 216 LEU B C     1 
ATOM   5881 O  O     . LEU B 2 216 ? 130.263 115.283 140.886 1.00 44.96  ? 216 LEU B O     1 
ATOM   5882 C  CB    . LEU B 2 216 ? 129.110 115.565 143.889 1.00 39.64  ? 216 LEU B CB    1 
ATOM   5883 C  CG    . LEU B 2 216 ? 128.892 114.966 145.276 1.00 38.45  ? 216 LEU B CG    1 
ATOM   5884 C  CD1   . LEU B 2 216 ? 127.568 115.423 145.850 1.00 38.12  ? 216 LEU B CD1   1 
ATOM   5885 C  CD2   . LEU B 2 216 ? 128.958 113.454 145.208 1.00 39.52  ? 216 LEU B CD2   1 
ATOM   5886 N  N     . THR B 2 217 ? 131.062 117.173 141.803 1.00 42.30  ? 217 THR B N     1 
ATOM   5887 C  CA    . THR B 2 217 ? 131.279 117.758 140.485 1.00 44.42  ? 217 THR B CA    1 
ATOM   5888 C  C     . THR B 2 217 ? 132.451 117.097 139.769 1.00 47.38  ? 217 THR B C     1 
ATOM   5889 O  O     . THR B 2 217 ? 132.438 116.998 138.539 1.00 52.03  ? 217 THR B O     1 
ATOM   5890 C  CB    . THR B 2 217 ? 131.477 119.274 140.580 1.00 41.82  ? 217 THR B CB    1 
ATOM   5891 O  OG1   . THR B 2 217 ? 131.273 119.861 139.290 1.00 42.63  ? 217 THR B OG1   1 
ATOM   5892 C  CG2   . THR B 2 217 ? 132.860 119.621 141.045 1.00 42.67  ? 217 THR B CG2   1 
ATOM   5893 N  N     . LEU B 2 218 ? 133.453 116.616 140.509 1.00 47.19  ? 218 LEU B N     1 
ATOM   5894 C  CA    . LEU B 2 218 ? 134.496 115.802 139.891 1.00 49.29  ? 218 LEU B CA    1 
ATOM   5895 C  C     . LEU B 2 218 ? 133.916 114.505 139.343 1.00 52.70  ? 218 LEU B C     1 
ATOM   5896 O  O     . LEU B 2 218 ? 134.212 114.101 138.209 1.00 58.40  ? 218 LEU B O     1 
ATOM   5897 C  CB    . LEU B 2 218 ? 135.601 115.511 140.906 1.00 50.68  ? 218 LEU B CB    1 
ATOM   5898 C  CG    . LEU B 2 218 ? 136.572 114.381 140.559 1.00 53.27  ? 218 LEU B CG    1 
ATOM   5899 C  CD1   . LEU B 2 218 ? 137.399 114.735 139.336 1.00 53.50  ? 218 LEU B CD1   1 
ATOM   5900 C  CD2   . LEU B 2 218 ? 137.466 114.069 141.743 1.00 51.32  ? 218 LEU B CD2   1 
ATOM   5901 N  N     . PHE B 2 219 ? 133.073 113.842 140.139 1.00 50.58  ? 219 PHE B N     1 
ATOM   5902 C  CA    . PHE B 2 219 ? 132.431 112.614 139.676 1.00 46.06  ? 219 PHE B CA    1 
ATOM   5903 C  C     . PHE B 2 219 ? 131.601 112.866 138.424 1.00 48.27  ? 219 PHE B C     1 
ATOM   5904 O  O     . PHE B 2 219 ? 131.562 112.029 137.515 1.00 48.78  ? 219 PHE B O     1 
ATOM   5905 C  CB    . PHE B 2 219 ? 131.554 112.022 140.778 1.00 43.62  ? 219 PHE B CB    1 
ATOM   5906 C  CG    . PHE B 2 219 ? 132.326 111.361 141.879 1.00 48.33  ? 219 PHE B CG    1 
ATOM   5907 C  CD1   . PHE B 2 219 ? 133.672 111.083 141.729 1.00 55.41  ? 219 PHE B CD1   1 
ATOM   5908 C  CD2   . PHE B 2 219 ? 131.704 111.013 143.063 1.00 46.66  ? 219 PHE B CD2   1 
ATOM   5909 C  CE1   . PHE B 2 219 ? 134.383 110.474 142.742 1.00 55.19  ? 219 PHE B CE1   1 
ATOM   5910 C  CE2   . PHE B 2 219 ? 132.410 110.404 144.078 1.00 50.66  ? 219 PHE B CE2   1 
ATOM   5911 C  CZ    . PHE B 2 219 ? 133.751 110.134 143.917 1.00 54.56  ? 219 PHE B CZ    1 
ATOM   5912 N  N     . THR B 2 220 ? 130.919 114.009 138.366 1.00 46.13  ? 220 THR B N     1 
ATOM   5913 C  CA    . THR B 2 220 ? 130.086 114.318 137.209 1.00 47.08  ? 220 THR B CA    1 
ATOM   5914 C  C     . THR B 2 220 ? 130.927 114.654 135.983 1.00 49.74  ? 220 THR B C     1 
ATOM   5915 O  O     . THR B 2 220 ? 130.614 114.215 134.871 1.00 55.23  ? 220 THR B O     1 
ATOM   5916 C  CB    . THR B 2 220 ? 129.142 115.469 137.538 1.00 47.04  ? 220 THR B CB    1 
ATOM   5917 O  OG1   . THR B 2 220 ? 128.761 115.392 138.916 1.00 46.41  ? 220 THR B OG1   1 
ATOM   5918 C  CG2   . THR B 2 220 ? 127.898 115.400 136.670 1.00 48.61  ? 220 THR B CG2   1 
ATOM   5919 N  N     . VAL B 2 221 ? 131.997 115.434 136.162 1.00 50.60  ? 221 VAL B N     1 
ATOM   5920 C  CA    . VAL B 2 221 ? 132.842 115.829 135.037 1.00 50.60  ? 221 VAL B CA    1 
ATOM   5921 C  C     . VAL B 2 221 ? 133.733 114.701 134.548 1.00 54.35  ? 221 VAL B C     1 
ATOM   5922 O  O     . VAL B 2 221 ? 134.334 114.824 133.474 1.00 61.11  ? 221 VAL B O     1 
ATOM   5923 C  CB    . VAL B 2 221 ? 133.699 117.051 135.417 1.00 53.00  ? 221 VAL B CB    1 
ATOM   5924 C  CG1   . VAL B 2 221 ? 134.993 116.616 136.089 1.00 49.72  ? 221 VAL B CG1   1 
ATOM   5925 C  CG2   . VAL B 2 221 ? 133.975 117.908 134.194 1.00 54.14  ? 221 VAL B CG2   1 
ATOM   5926 N  N     . VAL B 2 222 ? 133.839 113.605 135.304 1.00 55.96  ? 222 VAL B N     1 
ATOM   5927 C  CA    . VAL B 2 222 ? 134.563 112.433 134.812 1.00 55.47  ? 222 VAL B CA    1 
ATOM   5928 C  C     . VAL B 2 222 ? 133.944 111.902 133.519 1.00 57.13  ? 222 VAL B C     1 
ATOM   5929 O  O     . VAL B 2 222 ? 134.633 111.279 132.701 1.00 59.63  ? 222 VAL B O     1 
ATOM   5930 C  CB    . VAL B 2 222 ? 134.619 111.359 135.920 1.00 52.91  ? 222 VAL B CB    1 
ATOM   5931 C  CG1   . VAL B 2 222 ? 134.743 109.958 135.347 1.00 47.52  ? 222 VAL B CG1   1 
ATOM   5932 C  CG2   . VAL B 2 222 ? 135.778 111.641 136.860 1.00 54.48  ? 222 VAL B CG2   1 
ATOM   5933 N  N     . THR B 2 223 ? 132.653 112.165 133.294 1.00 54.22  ? 223 THR B N     1 
ATOM   5934 C  CA    . THR B 2 223 ? 131.989 111.657 132.095 1.00 54.69  ? 223 THR B CA    1 
ATOM   5935 C  C     . THR B 2 223 ? 132.619 112.201 130.821 1.00 55.16  ? 223 THR B C     1 
ATOM   5936 O  O     . THR B 2 223 ? 132.790 111.463 129.845 1.00 56.86  ? 223 THR B O     1 
ATOM   5937 C  CB    . THR B 2 223 ? 130.502 112.006 132.115 1.00 55.83  ? 223 THR B CB    1 
ATOM   5938 O  OG1   . THR B 2 223 ? 130.338 113.413 132.326 1.00 62.07  ? 223 THR B OG1   1 
ATOM   5939 C  CG2   . THR B 2 223 ? 129.805 111.258 133.207 1.00 50.72  ? 223 THR B CG2   1 
ATOM   5940 N  N     . VAL B 2 224 ? 132.959 113.493 130.805 1.00 58.25  ? 224 VAL B N     1 
ATOM   5941 C  CA    . VAL B 2 224 ? 133.400 114.130 129.562 1.00 58.70  ? 224 VAL B CA    1 
ATOM   5942 C  C     . VAL B 2 224 ? 134.594 113.414 128.938 1.00 56.16  ? 224 VAL B C     1 
ATOM   5943 O  O     . VAL B 2 224 ? 134.564 113.159 127.723 1.00 53.85  ? 224 VAL B O     1 
ATOM   5944 C  CB    . VAL B 2 224 ? 133.651 115.630 129.796 1.00 58.97  ? 224 VAL B CB    1 
ATOM   5945 C  CG1   . VAL B 2 224 ? 134.606 116.184 128.754 1.00 59.59  ? 224 VAL B CG1   1 
ATOM   5946 C  CG2   . VAL B 2 224 ? 132.337 116.392 129.773 1.00 52.43  ? 224 VAL B CG2   1 
ATOM   5947 N  N     . PRO B 2 225 ? 135.650 113.053 129.678 1.00 53.25  ? 225 PRO B N     1 
ATOM   5948 C  CA    . PRO B 2 225 ? 136.701 112.226 129.055 1.00 53.81  ? 225 PRO B CA    1 
ATOM   5949 C  C     . PRO B 2 225 ? 136.190 110.902 128.511 1.00 56.12  ? 225 PRO B C     1 
ATOM   5950 O  O     . PRO B 2 225 ? 136.466 110.564 127.353 1.00 62.35  ? 225 PRO B O     1 
ATOM   5951 C  CB    . PRO B 2 225 ? 137.706 112.032 130.198 1.00 53.40  ? 225 PRO B CB    1 
ATOM   5952 C  CG    . PRO B 2 225 ? 137.525 113.220 131.047 1.00 55.68  ? 225 PRO B CG    1 
ATOM   5953 C  CD    . PRO B 2 225 ? 136.059 113.517 131.016 1.00 52.79  ? 225 PRO B CD    1 
ATOM   5954 N  N     . ALA B 2 226 ? 135.451 110.137 129.319 1.00 56.56  ? 226 ALA B N     1 
ATOM   5955 C  CA    . ALA B 2 226 ? 134.957 108.839 128.868 1.00 49.22  ? 226 ALA B CA    1 
ATOM   5956 C  C     . ALA B 2 226 ? 133.966 108.986 127.722 1.00 50.02  ? 226 ALA B C     1 
ATOM   5957 O  O     . ALA B 2 226 ? 134.015 108.224 126.748 1.00 57.09  ? 226 ALA B O     1 
ATOM   5958 C  CB    . ALA B 2 226 ? 134.319 108.086 130.033 1.00 44.33  ? 226 ALA B CB    1 
ATOM   5959 N  N     . SER B 2 227 ? 133.053 109.954 127.823 1.00 48.05  ? 227 SER B N     1 
ATOM   5960 C  CA    . SER B 2 227 ? 132.085 110.166 126.753 1.00 47.95  ? 227 SER B CA    1 
ATOM   5961 C  C     . SER B 2 227 ? 132.778 110.558 125.458 1.00 49.45  ? 227 SER B C     1 
ATOM   5962 O  O     . SER B 2 227 ? 132.422 110.064 124.385 1.00 50.12  ? 227 SER B O     1 
ATOM   5963 C  CB    . SER B 2 227 ? 131.067 111.231 127.160 1.00 51.21  ? 227 SER B CB    1 
ATOM   5964 O  OG    . SER B 2 227 ? 130.329 110.826 128.298 1.00 54.41  ? 227 SER B OG    1 
ATOM   5965 N  N     . LEU B 2 228 ? 133.777 111.439 125.538 1.00 52.63  ? 228 LEU B N     1 
ATOM   5966 C  CA    . LEU B 2 228 ? 134.502 111.846 124.340 1.00 49.22  ? 228 LEU B CA    1 
ATOM   5967 C  C     . LEU B 2 228 ? 135.293 110.686 123.750 1.00 50.03  ? 228 LEU B C     1 
ATOM   5968 O  O     . LEU B 2 228 ? 135.385 110.555 122.527 1.00 56.60  ? 228 LEU B O     1 
ATOM   5969 C  CB    . LEU B 2 228 ? 135.424 113.021 124.657 1.00 48.24  ? 228 LEU B CB    1 
ATOM   5970 C  CG    . LEU B 2 228 ? 134.740 114.385 124.747 1.00 46.40  ? 228 LEU B CG    1 
ATOM   5971 C  CD1   . LEU B 2 228 ? 135.714 115.443 125.239 1.00 47.63  ? 228 LEU B CD1   1 
ATOM   5972 C  CD2   . LEU B 2 228 ? 134.146 114.779 123.407 1.00 40.49  ? 228 LEU B CD2   1 
ATOM   5973 N  N     . TRP B 2 229 ? 135.868 109.830 124.597 1.00 46.37  ? 229 TRP B N     1 
ATOM   5974 C  CA    . TRP B 2 229 ? 136.605 108.679 124.085 1.00 51.65  ? 229 TRP B CA    1 
ATOM   5975 C  C     . TRP B 2 229 ? 135.680 107.706 123.358 1.00 53.96  ? 229 TRP B C     1 
ATOM   5976 O  O     . TRP B 2 229 ? 135.994 107.234 122.256 1.00 59.24  ? 229 TRP B O     1 
ATOM   5977 C  CB    . TRP B 2 229 ? 137.335 107.977 125.229 1.00 53.36  ? 229 TRP B CB    1 
ATOM   5978 C  CG    . TRP B 2 229 ? 138.327 106.969 124.762 1.00 63.18  ? 229 TRP B CG    1 
ATOM   5979 C  CD1   . TRP B 2 229 ? 139.655 107.171 124.539 1.00 66.61  ? 229 TRP B CD1   1 
ATOM   5980 C  CD2   . TRP B 2 229 ? 138.072 105.595 124.451 1.00 66.90  ? 229 TRP B CD2   1 
ATOM   5981 N  NE1   . TRP B 2 229 ? 140.246 106.007 124.111 1.00 70.26  ? 229 TRP B NE1   1 
ATOM   5982 C  CE2   . TRP B 2 229 ? 139.294 105.025 124.048 1.00 69.03  ? 229 TRP B CE2   1 
ATOM   5983 C  CE3   . TRP B 2 229 ? 136.928 104.791 124.474 1.00 64.48  ? 229 TRP B CE3   1 
ATOM   5984 C  CZ2   . TRP B 2 229 ? 139.406 103.690 123.673 1.00 70.60  ? 229 TRP B CZ2   1 
ATOM   5985 C  CZ3   . TRP B 2 229 ? 137.042 103.466 124.102 1.00 68.67  ? 229 TRP B CZ3   1 
ATOM   5986 C  CH2   . TRP B 2 229 ? 138.270 102.929 123.706 1.00 70.67  ? 229 TRP B CH2   1 
ATOM   5987 N  N     . VAL B 2 230 ? 134.529 107.396 123.960 1.00 52.78  ? 230 VAL B N     1 
ATOM   5988 C  CA    . VAL B 2 230 ? 133.588 106.485 123.316 1.00 47.86  ? 230 VAL B CA    1 
ATOM   5989 C  C     . VAL B 2 230 ? 133.027 107.110 122.045 1.00 48.31  ? 230 VAL B C     1 
ATOM   5990 O  O     . VAL B 2 230 ? 132.822 106.422 121.037 1.00 52.86  ? 230 VAL B O     1 
ATOM   5991 C  CB    . VAL B 2 230 ? 132.476 106.081 124.298 1.00 46.61  ? 230 VAL B CB    1 
ATOM   5992 C  CG1   . VAL B 2 230 ? 131.477 105.161 123.623 1.00 45.70  ? 230 VAL B CG1   1 
ATOM   5993 C  CG2   . VAL B 2 230 ? 133.075 105.399 125.512 1.00 52.14  ? 230 VAL B CG2   1 
ATOM   5994 N  N     . THR B 2 231 ? 132.775 108.420 122.066 1.00 48.79  ? 231 THR B N     1 
ATOM   5995 C  CA    . THR B 2 231 ? 132.314 109.111 120.869 1.00 45.25  ? 231 THR B CA    1 
ATOM   5996 C  C     . THR B 2 231 ? 133.356 109.044 119.764 1.00 50.12  ? 231 THR B C     1 
ATOM   5997 O  O     . THR B 2 231 ? 133.017 108.845 118.595 1.00 54.79  ? 231 THR B O     1 
ATOM   5998 C  CB    . THR B 2 231 ? 131.979 110.564 121.203 1.00 44.37  ? 231 THR B CB    1 
ATOM   5999 O  OG1   . THR B 2 231 ? 130.986 110.602 122.233 1.00 48.79  ? 231 THR B OG1   1 
ATOM   6000 C  CG2   . THR B 2 231 ? 131.456 111.291 119.977 1.00 39.23  ? 231 THR B CG2   1 
ATOM   6001 N  N     . ARG B 2 232 ? 134.631 109.211 120.116 1.00 49.98  ? 232 ARG B N     1 
ATOM   6002 C  CA    . ARG B 2 232 ? 135.698 109.109 119.129 1.00 47.24  ? 232 ARG B CA    1 
ATOM   6003 C  C     . ARG B 2 232 ? 135.746 107.716 118.523 1.00 48.50  ? 232 ARG B C     1 
ATOM   6004 O  O     . ARG B 2 232 ? 135.881 107.563 117.306 1.00 55.78  ? 232 ARG B O     1 
ATOM   6005 C  CB    . ARG B 2 232 ? 137.038 109.463 119.773 1.00 54.16  ? 232 ARG B CB    1 
ATOM   6006 C  CG    . ARG B 2 232 ? 138.246 109.091 118.935 1.00 60.15  ? 232 ARG B CG    1 
ATOM   6007 C  CD    . ARG B 2 232 ? 139.314 108.421 119.780 1.00 67.99  ? 232 ARG B CD    1 
ATOM   6008 N  NE    . ARG B 2 232 ? 140.181 109.392 120.436 1.00 82.15  ? 232 ARG B NE    1 
ATOM   6009 C  CZ    . ARG B 2 232 ? 141.384 109.116 120.917 1.00 84.51  ? 232 ARG B CZ    1 
ATOM   6010 N  NH1   . ARG B 2 232 ? 141.899 107.900 120.835 1.00 80.10  ? 232 ARG B NH1   1 
ATOM   6011 N  NH2   . ARG B 2 232 ? 142.089 110.082 121.498 1.00 84.13  ? 232 ARG B NH2   1 
ATOM   6012 N  N     . TRP B 2 233 ? 135.631 106.685 119.360 1.00 47.31  ? 233 TRP B N     1 
ATOM   6013 C  CA    . TRP B 2 233 ? 135.648 105.315 118.851 1.00 49.13  ? 233 TRP B CA    1 
ATOM   6014 C  C     . TRP B 2 233 ? 134.482 105.066 117.898 1.00 50.42  ? 233 TRP B C     1 
ATOM   6015 O  O     . TRP B 2 233 ? 134.660 104.529 116.795 1.00 53.95  ? 233 TRP B O     1 
ATOM   6016 C  CB    . TRP B 2 233 ? 135.611 104.332 120.020 1.00 49.98  ? 233 TRP B CB    1 
ATOM   6017 C  CG    . TRP B 2 233 ? 135.734 102.901 119.617 1.00 61.87  ? 233 TRP B CG    1 
ATOM   6018 C  CD1   . TRP B 2 233 ? 136.884 102.180 119.496 1.00 65.92  ? 233 TRP B CD1   1 
ATOM   6019 C  CD2   . TRP B 2 233 ? 134.663 102.006 119.293 1.00 64.12  ? 233 TRP B CD2   1 
ATOM   6020 N  NE1   . TRP B 2 233 ? 136.598 100.894 119.111 1.00 67.09  ? 233 TRP B NE1   1 
ATOM   6021 C  CE2   . TRP B 2 233 ? 135.241 100.761 118.980 1.00 65.73  ? 233 TRP B CE2   1 
ATOM   6022 C  CE3   . TRP B 2 233 ? 133.273 102.138 119.234 1.00 58.27  ? 233 TRP B CE3   1 
ATOM   6023 C  CZ2   . TRP B 2 233 ? 134.479 99.656  118.614 1.00 64.05  ? 233 TRP B CZ2   1 
ATOM   6024 C  CZ3   . TRP B 2 233 ? 132.518 101.039 118.870 1.00 59.78  ? 233 TRP B CZ3   1 
ATOM   6025 C  CH2   . TRP B 2 233 ? 133.122 99.815  118.565 1.00 62.36  ? 233 TRP B CH2   1 
ATOM   6026 N  N     . ILE B 2 234 ? 133.280 105.479 118.300 1.00 51.93  ? 234 ILE B N     1 
ATOM   6027 C  CA    . ILE B 2 234 ? 132.096 105.252 117.479 1.00 49.42  ? 234 ILE B CA    1 
ATOM   6028 C  C     . ILE B 2 234 ? 132.182 106.036 116.174 1.00 48.99  ? 234 ILE B C     1 
ATOM   6029 O  O     . ILE B 2 234 ? 131.813 105.533 115.108 1.00 46.20  ? 234 ILE B O     1 
ATOM   6030 C  CB    . ILE B 2 234 ? 130.828 105.607 118.274 1.00 44.17  ? 234 ILE B CB    1 
ATOM   6031 C  CG1   . ILE B 2 234 ? 130.666 104.663 119.464 1.00 41.44  ? 234 ILE B CG1   1 
ATOM   6032 C  CG2   . ILE B 2 234 ? 129.614 105.526 117.390 1.00 39.95  ? 234 ILE B CG2   1 
ATOM   6033 C  CD1   . ILE B 2 234 ? 129.614 105.108 120.449 1.00 36.37  ? 234 ILE B CD1   1 
ATOM   6034 N  N     . THR B 2 235 ? 132.665 107.279 116.232 1.00 45.30  ? 235 THR B N     1 
ATOM   6035 C  CA    . THR B 2 235 ? 132.772 108.090 115.025 1.00 42.87  ? 235 THR B CA    1 
ATOM   6036 C  C     . THR B 2 235 ? 133.847 107.552 114.089 1.00 50.84  ? 235 THR B C     1 
ATOM   6037 O  O     . THR B 2 235 ? 133.694 107.610 112.865 1.00 58.67  ? 235 THR B O     1 
ATOM   6038 C  CB    . THR B 2 235 ? 133.055 109.541 115.397 1.00 44.96  ? 235 THR B CB    1 
ATOM   6039 O  OG1   . THR B 2 235 ? 132.095 109.975 116.367 1.00 45.30  ? 235 THR B OG1   1 
ATOM   6040 C  CG2   . THR B 2 235 ? 132.956 110.431 114.172 1.00 50.47  ? 235 THR B CG2   1 
ATOM   6041 N  N     . ARG B 2 236 ? 134.941 107.023 114.641 1.00 48.34  ? 236 ARG B N     1 
ATOM   6042 C  CA    . ARG B 2 236 ? 135.933 106.361 113.806 1.00 48.94  ? 236 ARG B CA    1 
ATOM   6043 C  C     . ARG B 2 236 ? 135.346 105.139 113.120 1.00 50.31  ? 236 ARG B C     1 
ATOM   6044 O  O     . ARG B 2 236 ? 135.680 104.855 111.964 1.00 54.06  ? 236 ARG B O     1 
ATOM   6045 C  CB    . ARG B 2 236 ? 137.151 105.967 114.642 1.00 54.15  ? 236 ARG B CB    1 
ATOM   6046 C  CG    . ARG B 2 236 ? 138.114 107.111 114.908 1.00 59.53  ? 236 ARG B CG    1 
ATOM   6047 C  CD    . ARG B 2 236 ? 139.191 106.710 115.900 1.00 64.47  ? 236 ARG B CD    1 
ATOM   6048 N  NE    . ARG B 2 236 ? 139.301 105.262 116.032 1.00 70.67  ? 236 ARG B NE    1 
ATOM   6049 C  CZ    . ARG B 2 236 ? 139.590 104.633 117.163 1.00 73.23  ? 236 ARG B CZ    1 
ATOM   6050 N  NH1   . ARG B 2 236 ? 139.811 105.296 118.286 1.00 69.50  ? 236 ARG B NH1   1 
ATOM   6051 N  NH2   . ARG B 2 236 ? 139.659 103.305 117.167 1.00 77.82  ? 236 ARG B NH2   1 
ATOM   6052 N  N     . ARG B 2 237 ? 134.481 104.400 113.812 1.00 51.45  ? 237 ARG B N     1 
ATOM   6053 C  CA    . ARG B 2 237 ? 133.844 103.250 113.183 1.00 52.35  ? 237 ARG B CA    1 
ATOM   6054 C  C     . ARG B 2 237 ? 132.728 103.634 112.216 1.00 49.11  ? 237 ARG B C     1 
ATOM   6055 O  O     . ARG B 2 237 ? 132.379 102.825 111.351 1.00 54.83  ? 237 ARG B O     1 
ATOM   6056 C  CB    . ARG B 2 237 ? 133.294 102.304 114.250 1.00 54.83  ? 237 ARG B CB    1 
ATOM   6057 C  CG    . ARG B 2 237 ? 134.370 101.566 115.030 1.00 61.56  ? 237 ARG B CG    1 
ATOM   6058 C  CD    . ARG B 2 237 ? 134.150 100.066 114.997 1.00 71.37  ? 237 ARG B CD    1 
ATOM   6059 N  NE    . ARG B 2 237 ? 135.408 99.331  114.951 1.00 80.11  ? 237 ARG B NE    1 
ATOM   6060 C  CZ    . ARG B 2 237 ? 135.501 98.010  114.886 1.00 85.28  ? 237 ARG B CZ    1 
ATOM   6061 N  NH1   . ARG B 2 237 ? 134.423 97.242  114.867 1.00 84.45  ? 237 ARG B NH1   1 
ATOM   6062 N  NH2   . ARG B 2 237 ? 136.704 97.445  114.840 1.00 85.28  ? 237 ARG B NH2   1 
ATOM   6063 N  N     . SER B 2 238 ? 132.157 104.833 112.339 1.00 47.36  ? 238 SER B N     1 
ATOM   6064 C  CA    . SER B 2 238 ? 130.995 105.202 111.536 1.00 48.31  ? 238 SER B CA    1 
ATOM   6065 C  C     . SER B 2 238 ? 131.306 106.122 110.363 1.00 50.90  ? 238 SER B C     1 
ATOM   6066 O  O     . SER B 2 238 ? 130.505 106.189 109.426 1.00 50.67  ? 238 SER B O     1 
ATOM   6067 C  CB    . SER B 2 238 ? 129.931 105.875 112.409 1.00 44.41  ? 238 SER B CB    1 
ATOM   6068 O  OG    . SER B 2 238 ? 130.433 107.038 113.034 1.00 51.68  ? 238 SER B OG    1 
ATOM   6069 N  N     . GLN B 2 239 ? 132.421 106.849 110.390 1.00 51.72  ? 239 GLN B N     1 
ATOM   6070 C  CA    . GLN B 2 239 ? 132.744 107.729 109.269 1.00 50.87  ? 239 GLN B CA    1 
ATOM   6071 C  C     . GLN B 2 239 ? 132.944 106.982 107.953 1.00 50.46  ? 239 GLN B C     1 
ATOM   6072 O  O     . GLN B 2 239 ? 132.397 107.437 106.931 1.00 51.75  ? 239 GLN B O     1 
ATOM   6073 C  CB    . GLN B 2 239 ? 133.973 108.579 109.615 1.00 51.02  ? 239 GLN B CB    1 
ATOM   6074 C  CG    . GLN B 2 239 ? 133.995 109.943 108.943 1.00 55.78  ? 239 GLN B CG    1 
ATOM   6075 C  CD    . GLN B 2 239 ? 132.703 110.716 109.132 1.00 60.74  ? 239 GLN B CD    1 
ATOM   6076 O  OE1   . GLN B 2 239 ? 132.228 111.394 108.219 1.00 58.87  ? 239 GLN B OE1   1 
ATOM   6077 N  NE2   . GLN B 2 239 ? 132.129 110.620 110.324 1.00 58.36  ? 239 GLN B NE2   1 
ATOM   6078 N  N     . PRO B 2 240 ? 133.695 105.872 107.887 1.00 51.18  ? 240 PRO B N     1 
ATOM   6079 C  CA    . PRO B 2 240 ? 133.737 105.116 106.625 1.00 50.70  ? 240 PRO B CA    1 
ATOM   6080 C  C     . PRO B 2 240 ? 132.367 104.654 106.169 1.00 50.38  ? 240 PRO B C     1 
ATOM   6081 O  O     . PRO B 2 240 ? 132.098 104.616 104.963 1.00 53.33  ? 240 PRO B O     1 
ATOM   6082 C  CB    . PRO B 2 240 ? 134.655 103.933 106.959 1.00 49.56  ? 240 PRO B CB    1 
ATOM   6083 C  CG    . PRO B 2 240 ? 135.494 104.413 108.073 1.00 48.28  ? 240 PRO B CG    1 
ATOM   6084 C  CD    . PRO B 2 240 ? 134.606 105.291 108.890 1.00 47.09  ? 240 PRO B CD    1 
ATOM   6085 N  N     . LEU B 2 241 ? 131.488 104.305 107.109 1.00 43.54  ? 241 LEU B N     1 
ATOM   6086 C  CA    . LEU B 2 241 ? 130.137 103.894 106.747 1.00 41.20  ? 241 LEU B CA    1 
ATOM   6087 C  C     . LEU B 2 241 ? 129.355 105.043 106.124 1.00 44.61  ? 241 LEU B C     1 
ATOM   6088 O  O     . LEU B 2 241 ? 128.612 104.840 105.161 1.00 45.86  ? 241 LEU B O     1 
ATOM   6089 C  CB    . LEU B 2 241 ? 129.412 103.346 107.972 1.00 37.54  ? 241 LEU B CB    1 
ATOM   6090 C  CG    . LEU B 2 241 ? 129.785 101.908 108.331 1.00 36.73  ? 241 LEU B CG    1 
ATOM   6091 C  CD1   . LEU B 2 241 ? 129.768 101.712 109.829 1.00 37.95  ? 241 LEU B CD1   1 
ATOM   6092 C  CD2   . LEU B 2 241 ? 128.846 100.931 107.648 1.00 38.14  ? 241 LEU B CD2   1 
ATOM   6093 N  N     . PHE B 2 242 ? 129.508 106.256 106.658 1.00 43.74  ? 242 PHE B N     1 
ATOM   6094 C  CA    . PHE B 2 242 ? 128.848 107.414 106.063 1.00 38.41  ? 242 PHE B CA    1 
ATOM   6095 C  C     . PHE B 2 242 ? 129.394 107.708 104.672 1.00 43.04  ? 242 PHE B C     1 
ATOM   6096 O  O     . PHE B 2 242 ? 128.633 108.043 103.753 1.00 49.72  ? 242 PHE B O     1 
ATOM   6097 C  CB    . PHE B 2 242 ? 129.013 108.632 106.966 1.00 41.40  ? 242 PHE B CB    1 
ATOM   6098 C  CG    . PHE B 2 242 ? 127.951 108.757 108.013 1.00 45.03  ? 242 PHE B CG    1 
ATOM   6099 C  CD1   . PHE B 2 242 ? 126.618 108.846 107.658 1.00 47.18  ? 242 PHE B CD1   1 
ATOM   6100 C  CD2   . PHE B 2 242 ? 128.286 108.791 109.354 1.00 45.72  ? 242 PHE B CD2   1 
ATOM   6101 C  CE1   . PHE B 2 242 ? 125.639 108.961 108.622 1.00 45.05  ? 242 PHE B CE1   1 
ATOM   6102 C  CE2   . PHE B 2 242 ? 127.312 108.908 110.320 1.00 43.89  ? 242 PHE B CE2   1 
ATOM   6103 C  CZ    . PHE B 2 242 ? 125.988 108.993 109.954 1.00 44.01  ? 242 PHE B CZ    1 
ATOM   6104 N  N     . VAL B 2 243 ? 130.713 107.597 104.501 1.00 41.61  ? 243 VAL B N     1 
ATOM   6105 C  CA    . VAL B 2 243 ? 131.311 107.810 103.186 1.00 45.10  ? 243 VAL B CA    1 
ATOM   6106 C  C     . VAL B 2 243 ? 130.770 106.796 102.188 1.00 48.10  ? 243 VAL B C     1 
ATOM   6107 O  O     . VAL B 2 243 ? 130.414 107.144 101.053 1.00 51.10  ? 243 VAL B O     1 
ATOM   6108 C  CB    . VAL B 2 243 ? 132.846 107.749 103.286 1.00 44.81  ? 243 VAL B CB    1 
ATOM   6109 C  CG1   . VAL B 2 243 ? 133.471 107.647 101.907 1.00 44.70  ? 243 VAL B CG1   1 
ATOM   6110 C  CG2   . VAL B 2 243 ? 133.373 108.965 104.024 1.00 53.18  ? 243 VAL B CG2   1 
ATOM   6111 N  N     . ALA B 2 244 ? 130.692 105.528 102.597 1.00 43.50  ? 244 ALA B N     1 
ATOM   6112 C  CA    . ALA B 2 244 ? 130.142 104.495 101.729 1.00 37.48  ? 244 ALA B CA    1 
ATOM   6113 C  C     . ALA B 2 244 ? 128.677 104.758 101.417 1.00 36.30  ? 244 ALA B C     1 
ATOM   6114 O  O     . ALA B 2 244 ? 128.225 104.527 100.291 1.00 42.27  ? 244 ALA B O     1 
ATOM   6115 C  CB    . ALA B 2 244 ? 130.316 103.122 102.374 1.00 33.80  ? 244 ALA B CB    1 
ATOM   6116 N  N     . GLN B 2 245 ? 127.916 105.232 102.405 1.00 35.18  ? 245 GLN B N     1 
ATOM   6117 C  CA    . GLN B 2 245 ? 126.507 105.525 102.175 1.00 36.83  ? 245 GLN B CA    1 
ATOM   6118 C  C     . GLN B 2 245 ? 126.336 106.610 101.125 1.00 41.60  ? 245 GLN B C     1 
ATOM   6119 O  O     . GLN B 2 245 ? 125.514 106.476 100.211 1.00 41.81  ? 245 GLN B O     1 
ATOM   6120 C  CB    . GLN B 2 245 ? 125.834 105.939 103.482 1.00 35.42  ? 245 GLN B CB    1 
ATOM   6121 C  CG    . GLN B 2 245 ? 124.351 106.223 103.341 1.00 39.71  ? 245 GLN B CG    1 
ATOM   6122 C  CD    . GLN B 2 245 ? 123.815 107.088 104.458 1.00 45.94  ? 245 GLN B CD    1 
ATOM   6123 O  OE1   . GLN B 2 245 ? 124.543 107.886 105.041 1.00 54.51  ? 245 GLN B OE1   1 
ATOM   6124 N  NE2   . GLN B 2 245 ? 122.536 106.931 104.764 1.00 43.86  ? 245 GLN B NE2   1 
ATOM   6125 N  N     . TRP B 2 246 ? 127.115 107.688 101.225 1.00 42.39  ? 246 TRP B N     1 
ATOM   6126 C  CA    . TRP B 2 246 ? 127.013 108.743 100.222 1.00 39.13  ? 246 TRP B CA    1 
ATOM   6127 C  C     . TRP B 2 246 ? 127.502 108.288 98.852  1.00 39.55  ? 246 TRP B C     1 
ATOM   6128 O  O     . TRP B 2 246 ? 126.909 108.664 97.836  1.00 40.71  ? 246 TRP B O     1 
ATOM   6129 C  CB    . TRP B 2 246 ? 127.777 109.989 100.664 1.00 41.86  ? 246 TRP B CB    1 
ATOM   6130 C  CG    . TRP B 2 246 ? 127.459 110.436 102.053 1.00 49.95  ? 246 TRP B CG    1 
ATOM   6131 C  CD1   . TRP B 2 246 ? 126.228 110.494 102.634 1.00 51.02  ? 246 TRP B CD1   1 
ATOM   6132 C  CD2   . TRP B 2 246 ? 128.385 110.928 103.027 1.00 56.24  ? 246 TRP B CD2   1 
ATOM   6133 N  NE1   . TRP B 2 246 ? 126.332 110.971 103.918 1.00 56.09  ? 246 TRP B NE1   1 
ATOM   6134 C  CE2   . TRP B 2 246 ? 127.648 111.246 104.181 1.00 54.90  ? 246 TRP B CE2   1 
ATOM   6135 C  CE3   . TRP B 2 246 ? 129.768 111.117 103.039 1.00 56.05  ? 246 TRP B CE3   1 
ATOM   6136 C  CZ2   . TRP B 2 246 ? 128.249 111.744 105.330 1.00 51.31  ? 246 TRP B CZ2   1 
ATOM   6137 C  CZ3   . TRP B 2 246 ? 130.361 111.611 104.178 1.00 54.74  ? 246 TRP B CZ3   1 
ATOM   6138 C  CH2   . TRP B 2 246 ? 129.605 111.920 105.306 1.00 52.17  ? 246 TRP B CH2   1 
ATOM   6139 N  N     . ARG B 2 247 ? 128.566 107.485 98.797  1.00 37.78  ? 247 ARG B N     1 
ATOM   6140 C  CA    . ARG B 2 247 ? 129.033 106.973 97.512  1.00 35.42  ? 247 ARG B CA    1 
ATOM   6141 C  C     . ARG B 2 247 ? 127.976 106.099 96.846  1.00 36.91  ? 247 ARG B C     1 
ATOM   6142 O  O     . ARG B 2 247 ? 127.713 106.229 95.643  1.00 40.18  ? 247 ARG B O     1 
ATOM   6143 C  CB    . ARG B 2 247 ? 130.334 106.196 97.708  1.00 35.74  ? 247 ARG B CB    1 
ATOM   6144 C  CG    . ARG B 2 247 ? 130.961 105.691 96.427  1.00 42.32  ? 247 ARG B CG    1 
ATOM   6145 C  CD    . ARG B 2 247 ? 131.754 104.421 96.670  1.00 40.95  ? 247 ARG B CD    1 
ATOM   6146 N  NE    . ARG B 2 247 ? 132.564 104.508 97.880  1.00 56.82  ? 247 ARG B NE    1 
ATOM   6147 C  CZ    . ARG B 2 247 ? 132.469 103.676 98.908  1.00 59.88  ? 247 ARG B CZ    1 
ATOM   6148 N  NH1   . ARG B 2 247 ? 131.608 102.672 98.908  1.00 58.94  ? 247 ARG B NH1   1 
ATOM   6149 N  NH2   . ARG B 2 247 ? 133.260 103.854 99.961  1.00 54.79  ? 247 ARG B NH2   1 
ATOM   6150 N  N     . ASN B 2 248 ? 127.352 105.208 97.617  1.00 35.09  ? 248 ASN B N     1 
ATOM   6151 C  CA    . ASN B 2 248 ? 126.330 104.331 97.065  1.00 32.06  ? 248 ASN B CA    1 
ATOM   6152 C  C     . ASN B 2 248 ? 125.088 105.113 96.659  1.00 31.66  ? 248 ASN B C     1 
ATOM   6153 O  O     . ASN B 2 248 ? 124.452 104.796 95.648  1.00 35.79  ? 248 ASN B O     1 
ATOM   6154 C  CB    . ASN B 2 248 ? 125.987 103.243 98.078  1.00 34.29  ? 248 ASN B CB    1 
ATOM   6155 C  CG    . ASN B 2 248 ? 127.162 102.336 98.370  1.00 36.70  ? 248 ASN B CG    1 
ATOM   6156 O  OD1   . ASN B 2 248 ? 127.227 101.703 99.420  1.00 37.52  ? 248 ASN B OD1   1 
ATOM   6157 N  ND2   . ASN B 2 248 ? 128.098 102.265 97.434  1.00 39.60  ? 248 ASN B ND2   1 
ATOM   6158 N  N     . THR B 2 249 ? 124.728 106.138 97.434  1.00 32.13  ? 249 THR B N     1 
ATOM   6159 C  CA    . THR B 2 249 ? 123.610 106.994 97.055  1.00 33.12  ? 249 THR B CA    1 
ATOM   6160 C  C     . THR B 2 249 ? 123.896 107.723 95.750  1.00 32.67  ? 249 THR B C     1 
ATOM   6161 O  O     . THR B 2 249 ? 123.017 107.839 94.889  1.00 33.75  ? 249 THR B O     1 
ATOM   6162 C  CB    . THR B 2 249 ? 123.313 107.992 98.174  1.00 31.87  ? 249 THR B CB    1 
ATOM   6163 O  OG1   . THR B 2 249 ? 122.977 107.281 99.370  1.00 39.75  ? 249 THR B OG1   1 
ATOM   6164 C  CG2   . THR B 2 249 ? 122.160 108.901 97.794  1.00 31.44  ? 249 THR B CG2   1 
ATOM   6165 N  N     . GLY B 2 250 ? 125.124 108.218 95.584  1.00 32.07  ? 250 GLY B N     1 
ATOM   6166 C  CA    . GLY B 2 250 ? 125.485 108.868 94.336  1.00 29.48  ? 250 GLY B CA    1 
ATOM   6167 C  C     . GLY B 2 250 ? 125.438 107.923 93.153  1.00 28.93  ? 250 GLY B C     1 
ATOM   6168 O  O     . GLY B 2 250 ? 124.967 108.289 92.074  1.00 31.79  ? 250 GLY B O     1 
ATOM   6169 N  N     . ARG B 2 251 ? 125.921 106.692 93.338  1.00 31.67  ? 251 ARG B N     1 
ATOM   6170 C  CA    . ARG B 2 251 ? 125.848 105.701 92.267  1.00 31.16  ? 251 ARG B CA    1 
ATOM   6171 C  C     . ARG B 2 251 ? 124.403 105.376 91.901  1.00 30.17  ? 251 ARG B C     1 
ATOM   6172 O  O     . ARG B 2 251 ? 124.058 105.277 90.715  1.00 35.55  ? 251 ARG B O     1 
ATOM   6173 C  CB    . ARG B 2 251 ? 126.593 104.432 92.676  1.00 29.06  ? 251 ARG B CB    1 
ATOM   6174 C  CG    . ARG B 2 251 ? 128.087 104.490 92.439  1.00 32.18  ? 251 ARG B CG    1 
ATOM   6175 C  CD    . ARG B 2 251 ? 128.848 103.896 93.603  1.00 36.55  ? 251 ARG B CD    1 
ATOM   6176 N  NE    . ARG B 2 251 ? 128.414 102.538 93.905  1.00 42.83  ? 251 ARG B NE    1 
ATOM   6177 C  CZ    . ARG B 2 251 ? 128.716 101.472 93.176  1.00 47.84  ? 251 ARG B CZ    1 
ATOM   6178 N  NH1   . ARG B 2 251 ? 129.463 101.567 92.089  1.00 44.64  ? 251 ARG B NH1   1 
ATOM   6179 N  NH2   . ARG B 2 251 ? 128.259 100.280 93.550  1.00 42.91  ? 251 ARG B NH2   1 
ATOM   6180 N  N     . LEU B 2 252 ? 123.543 105.207 92.907  1.00 26.52  ? 252 LEU B N     1 
ATOM   6181 C  CA    . LEU B 2 252 ? 122.138 104.922 92.641  1.00 27.99  ? 252 LEU B CA    1 
ATOM   6182 C  C     . LEU B 2 252 ? 121.466 106.079 91.912  1.00 29.39  ? 252 LEU B C     1 
ATOM   6183 O  O     . LEU B 2 252 ? 120.696 105.865 90.967  1.00 32.69  ? 252 LEU B O     1 
ATOM   6184 C  CB    . LEU B 2 252 ? 121.413 104.619 93.951  1.00 29.39  ? 252 LEU B CB    1 
ATOM   6185 C  CG    . LEU B 2 252 ? 119.940 104.235 93.837  1.00 25.58  ? 252 LEU B CG    1 
ATOM   6186 C  CD1   . LEU B 2 252 ? 119.808 102.957 93.048  1.00 30.24  ? 252 LEU B CD1   1 
ATOM   6187 C  CD2   . LEU B 2 252 ? 119.325 104.082 95.210  1.00 25.41  ? 252 LEU B CD2   1 
ATOM   6188 N  N     . ALA B 2 253 ? 121.744 107.314 92.336  1.00 26.69  ? 253 ALA B N     1 
ATOM   6189 C  CA    . ALA B 2 253 ? 121.162 108.475 91.675  1.00 24.43  ? 253 ALA B CA    1 
ATOM   6190 C  C     . ALA B 2 253 ? 121.658 108.606 90.242  1.00 27.46  ? 253 ALA B C     1 
ATOM   6191 O  O     . ALA B 2 253 ? 120.891 108.972 89.347  1.00 34.77  ? 253 ALA B O     1 
ATOM   6192 C  CB    . ALA B 2 253 ? 121.472 109.741 92.469  1.00 27.79  ? 253 ALA B CB    1 
ATOM   6193 N  N     . ALA B 2 254 ? 122.940 108.318 90.005  1.00 27.20  ? 254 ALA B N     1 
ATOM   6194 C  CA    . ALA B 2 254 ? 123.471 108.368 88.648  1.00 27.43  ? 254 ALA B CA    1 
ATOM   6195 C  C     . ALA B 2 254 ? 122.794 107.340 87.753  1.00 33.35  ? 254 ALA B C     1 
ATOM   6196 O  O     . ALA B 2 254 ? 122.413 107.648 86.615  1.00 39.75  ? 254 ALA B O     1 
ATOM   6197 C  CB    . ALA B 2 254 ? 124.982 108.148 88.670  1.00 27.60  ? 254 ALA B CB    1 
ATOM   6198 N  N     . HIS B 2 255 ? 122.632 106.112 88.251  1.00 32.08  ? 255 HIS B N     1 
ATOM   6199 C  CA    . HIS B 2 255 ? 121.955 105.087 87.465  1.00 25.75  ? 255 HIS B CA    1 
ATOM   6200 C  C     . HIS B 2 255 ? 120.511 105.475 87.182  1.00 27.77  ? 255 HIS B C     1 
ATOM   6201 O  O     . HIS B 2 255 ? 120.021 105.294 86.061  1.00 30.44  ? 255 HIS B O     1 
ATOM   6202 C  CB    . HIS B 2 255 ? 122.009 103.744 88.187  1.00 28.43  ? 255 HIS B CB    1 
ATOM   6203 C  CG    . HIS B 2 255 ? 121.122 102.702 87.583  1.00 29.53  ? 255 HIS B CG    1 
ATOM   6204 N  ND1   . HIS B 2 255 ? 121.273 102.257 86.288  1.00 27.43  ? 255 HIS B ND1   1 
ATOM   6205 C  CD2   . HIS B 2 255 ? 120.063 102.029 88.090  1.00 29.60  ? 255 HIS B CD2   1 
ATOM   6206 C  CE1   . HIS B 2 255 ? 120.353 101.347 86.027  1.00 26.28  ? 255 HIS B CE1   1 
ATOM   6207 N  NE2   . HIS B 2 255 ? 119.604 101.191 87.103  1.00 27.88  ? 255 HIS B NE2   1 
ATOM   6208 N  N     . LEU B 2 256 ? 119.813 106.008 88.187  1.00 31.38  ? 256 LEU B N     1 
ATOM   6209 C  CA    . LEU B 2 256 ? 118.425 106.413 87.990  1.00 27.20  ? 256 LEU B CA    1 
ATOM   6210 C  C     . LEU B 2 256 ? 118.316 107.531 86.966  1.00 30.33  ? 256 LEU B C     1 
ATOM   6211 O  O     . LEU B 2 256 ? 117.412 107.525 86.125  1.00 35.26  ? 256 LEU B O     1 
ATOM   6212 C  CB    . LEU B 2 256 ? 117.810 106.849 89.318  1.00 28.21  ? 256 LEU B CB    1 
ATOM   6213 C  CG    . LEU B 2 256 ? 117.426 105.724 90.272  1.00 29.67  ? 256 LEU B CG    1 
ATOM   6214 C  CD1   . LEU B 2 256 ? 116.969 106.285 91.599  1.00 32.79  ? 256 LEU B CD1   1 
ATOM   6215 C  CD2   . LEU B 2 256 ? 116.346 104.890 89.650  1.00 28.78  ? 256 LEU B CD2   1 
ATOM   6216 N  N     . GLU B 2 257 ? 119.223 108.507 87.028  1.00 32.44  ? 257 GLU B N     1 
ATOM   6217 C  CA    . GLU B 2 257 ? 119.197 109.599 86.064  1.00 35.82  ? 257 GLU B CA    1 
ATOM   6218 C  C     . GLU B 2 257 ? 119.459 109.097 84.651  1.00 39.30  ? 257 GLU B C     1 
ATOM   6219 O  O     . GLU B 2 257 ? 118.788 109.518 83.702  1.00 40.73  ? 257 GLU B O     1 
ATOM   6220 C  CB    . GLU B 2 257 ? 120.221 110.661 86.450  1.00 38.56  ? 257 GLU B CB    1 
ATOM   6221 C  CG    . GLU B 2 257 ? 120.251 111.839 85.507  1.00 44.31  ? 257 GLU B CG    1 
ATOM   6222 C  CD    . GLU B 2 257 ? 121.184 112.924 85.975  1.00 50.61  ? 257 GLU B CD    1 
ATOM   6223 O  OE1   . GLU B 2 257 ? 121.823 112.738 87.030  1.00 57.41  ? 257 GLU B OE1   1 
ATOM   6224 O  OE2   . GLU B 2 257 ? 121.275 113.963 85.292  1.00 48.66  ? 257 GLU B OE2   1 
ATOM   6225 N  N     . GLU B 2 258 ? 120.431 108.198 84.489  1.00 37.50  ? 258 GLU B N     1 
ATOM   6226 C  CA    . GLU B 2 258 ? 120.714 107.668 83.159  1.00 37.17  ? 258 GLU B CA    1 
ATOM   6227 C  C     . GLU B 2 258 ? 119.545 106.850 82.626  1.00 35.90  ? 258 GLU B C     1 
ATOM   6228 O  O     . GLU B 2 258 ? 119.244 106.895 81.429  1.00 35.86  ? 258 GLU B O     1 
ATOM   6229 C  CB    . GLU B 2 258 ? 121.991 106.833 83.184  1.00 38.99  ? 258 GLU B CB    1 
ATOM   6230 C  CG    . GLU B 2 258 ? 123.268 107.655 83.247  1.00 47.77  ? 258 GLU B CG    1 
ATOM   6231 C  CD    . GLU B 2 258 ? 123.432 108.590 82.062  1.00 49.83  ? 258 GLU B CD    1 
ATOM   6232 O  OE1   . GLU B 2 258 ? 122.912 109.724 82.112  1.00 47.43  ? 258 GLU B OE1   1 
ATOM   6233 O  OE2   . GLU B 2 258 ? 124.085 108.191 81.078  1.00 46.73  ? 258 GLU B OE2   1 
ATOM   6234 N  N     . THR B 2 259 ? 118.876 106.092 83.498  1.00 35.08  ? 259 THR B N     1 
ATOM   6235 C  CA    . THR B 2 259 ? 117.742 105.288 83.055  1.00 31.80  ? 259 THR B CA    1 
ATOM   6236 C  C     . THR B 2 259 ? 116.543 106.159 82.698  1.00 35.92  ? 259 THR B C     1 
ATOM   6237 O  O     . THR B 2 259 ? 115.851 105.892 81.710  1.00 38.00  ? 259 THR B O     1 
ATOM   6238 C  CB    . THR B 2 259 ? 117.367 104.274 84.134  1.00 29.75  ? 259 THR B CB    1 
ATOM   6239 O  OG1   . THR B 2 259 ? 118.509 103.468 84.442  1.00 33.66  ? 259 THR B OG1   1 
ATOM   6240 C  CG2   . THR B 2 259 ? 116.241 103.373 83.660  1.00 29.87  ? 259 THR B CG2   1 
ATOM   6241 N  N     . TYR B 2 260 ? 116.279 107.203 83.487  1.00 34.37  ? 260 TYR B N     1 
ATOM   6242 C  CA    . TYR B 2 260 ? 115.107 108.037 83.237  1.00 34.01  ? 260 TYR B CA    1 
ATOM   6243 C  C     . TYR B 2 260 ? 115.312 108.947 82.032  1.00 38.20  ? 260 TYR B C     1 
ATOM   6244 O  O     . TYR B 2 260 ? 114.401 109.110 81.213  1.00 41.95  ? 260 TYR B O     1 
ATOM   6245 C  CB    . TYR B 2 260 ? 114.775 108.865 84.477  1.00 31.70  ? 260 TYR B CB    1 
ATOM   6246 C  CG    . TYR B 2 260 ? 114.249 108.061 85.643  1.00 27.62  ? 260 TYR B CG    1 
ATOM   6247 C  CD1   . TYR B 2 260 ? 113.780 106.769 85.467  1.00 26.11  ? 260 TYR B CD1   1 
ATOM   6248 C  CD2   . TYR B 2 260 ? 114.218 108.598 86.919  1.00 29.61  ? 260 TYR B CD2   1 
ATOM   6249 C  CE1   . TYR B 2 260 ? 113.301 106.035 86.529  1.00 23.69  ? 260 TYR B CE1   1 
ATOM   6250 C  CE2   . TYR B 2 260 ? 113.740 107.872 87.986  1.00 26.22  ? 260 TYR B CE2   1 
ATOM   6251 C  CZ    . TYR B 2 260 ? 113.281 106.593 87.786  1.00 25.52  ? 260 TYR B CZ    1 
ATOM   6252 O  OH    . TYR B 2 260 ? 112.803 105.869 88.850  1.00 30.20  ? 260 TYR B OH    1 
ATOM   6253 N  N     . SER B 2 261 ? 116.495 109.555 81.910  1.00 35.18  ? 261 SER B N     1 
ATOM   6254 C  CA    . SER B 2 261 ? 116.736 110.497 80.822  1.00 37.41  ? 261 SER B CA    1 
ATOM   6255 C  C     . SER B 2 261 ? 116.682 109.808 79.465  1.00 38.98  ? 261 SER B C     1 
ATOM   6256 O  O     . SER B 2 261 ? 116.109 110.344 78.510  1.00 40.25  ? 261 SER B O     1 
ATOM   6257 C  CB    . SER B 2 261 ? 118.083 111.187 81.019  1.00 43.25  ? 261 SER B CB    1 
ATOM   6258 O  OG    . SER B 2 261 ? 118.188 111.726 82.323  1.00 52.61  ? 261 SER B OG    1 
ATOM   6259 N  N     . GLY B 2 262 ? 117.275 108.626 79.358  1.00 34.76  ? 262 GLY B N     1 
ATOM   6260 C  CA    . GLY B 2 262 ? 117.250 107.884 78.116  1.00 37.36  ? 262 GLY B CA    1 
ATOM   6261 C  C     . GLY B 2 262 ? 116.293 106.716 78.164  1.00 42.81  ? 262 GLY B C     1 
ATOM   6262 O  O     . GLY B 2 262 ? 116.607 105.629 77.674  1.00 45.08  ? 262 GLY B O     1 
ATOM   6263 N  N     . PHE B 2 263 ? 115.116 106.934 78.756  1.00 40.33  ? 263 PHE B N     1 
ATOM   6264 C  CA    . PHE B 2 263 ? 114.180 105.837 78.970  1.00 37.88  ? 263 PHE B CA    1 
ATOM   6265 C  C     . PHE B 2 263 ? 113.679 105.248 77.661  1.00 38.47  ? 263 PHE B C     1 
ATOM   6266 O  O     . PHE B 2 263 ? 113.390 104.052 77.599  1.00 44.62  ? 263 PHE B O     1 
ATOM   6267 C  CB    . PHE B 2 263 ? 113.003 106.299 79.826  1.00 40.89  ? 263 PHE B CB    1 
ATOM   6268 C  CG    . PHE B 2 263 ? 112.104 105.181 80.262  1.00 45.05  ? 263 PHE B CG    1 
ATOM   6269 C  CD1   . PHE B 2 263 ? 112.635 103.975 80.685  1.00 48.73  ? 263 PHE B CD1   1 
ATOM   6270 C  CD2   . PHE B 2 263 ? 110.728 105.330 80.239  1.00 46.85  ? 263 PHE B CD2   1 
ATOM   6271 C  CE1   . PHE B 2 263 ? 111.813 102.939 81.080  1.00 49.82  ? 263 PHE B CE1   1 
ATOM   6272 C  CE2   . PHE B 2 263 ? 109.900 104.297 80.635  1.00 51.11  ? 263 PHE B CE2   1 
ATOM   6273 C  CZ    . PHE B 2 263 ? 110.443 103.101 81.055  1.00 51.19  ? 263 PHE B CZ    1 
ATOM   6274 N  N     . THR B 2 264 ? 113.553 106.060 76.612  1.00 37.90  ? 264 THR B N     1 
ATOM   6275 C  CA    . THR B 2 264 ? 113.152 105.514 75.319  1.00 37.67  ? 264 THR B CA    1 
ATOM   6276 C  C     . THR B 2 264 ? 114.210 104.564 74.771  1.00 40.44  ? 264 THR B C     1 
ATOM   6277 O  O     . THR B 2 264 ? 113.884 103.486 74.262  1.00 40.12  ? 264 THR B O     1 
ATOM   6278 C  CB    . THR B 2 264 ? 112.879 106.646 74.331  1.00 43.72  ? 264 THR B CB    1 
ATOM   6279 O  OG1   . THR B 2 264 ? 111.791 107.446 74.810  1.00 47.80  ? 264 THR B OG1   1 
ATOM   6280 C  CG2   . THR B 2 264 ? 112.515 106.087 72.966  1.00 41.27  ? 264 THR B CG2   1 
ATOM   6281 N  N     . ILE B 2 265 ? 115.486 104.941 74.877  1.00 45.75  ? 265 ILE B N     1 
ATOM   6282 C  CA    . ILE B 2 265 ? 116.560 104.084 74.385  1.00 43.91  ? 265 ILE B CA    1 
ATOM   6283 C  C     . ILE B 2 265 ? 116.712 102.850 75.265  1.00 42.43  ? 265 ILE B C     1 
ATOM   6284 O  O     . ILE B 2 265 ? 116.906 101.737 74.764  1.00 44.76  ? 265 ILE B O     1 
ATOM   6285 C  CB    . ILE B 2 265 ? 117.875 104.878 74.287  1.00 43.43  ? 265 ILE B CB    1 
ATOM   6286 C  CG1   . ILE B 2 265 ? 117.696 106.098 73.385  1.00 41.46  ? 265 ILE B CG1   1 
ATOM   6287 C  CG2   . ILE B 2 265 ? 118.991 103.996 73.758  1.00 36.54  ? 265 ILE B CG2   1 
ATOM   6288 C  CD1   . ILE B 2 265 ? 117.265 105.758 71.983  1.00 38.45  ? 265 ILE B CD1   1 
ATOM   6289 N  N     . VAL B 2 266 ? 116.638 103.025 76.587  1.00 41.61  ? 266 VAL B N     1 
ATOM   6290 C  CA    . VAL B 2 266 ? 116.732 101.887 77.500  1.00 42.11  ? 266 VAL B CA    1 
ATOM   6291 C  C     . VAL B 2 266 ? 115.600 100.905 77.235  1.00 43.70  ? 266 VAL B C     1 
ATOM   6292 O  O     . VAL B 2 266 ? 115.806 99.689  77.156  1.00 50.12  ? 266 VAL B O     1 
ATOM   6293 C  CB    . VAL B 2 266 ? 116.716 102.371 78.962  1.00 39.45  ? 266 VAL B CB    1 
ATOM   6294 C  CG1   . VAL B 2 266 ? 116.567 101.196 79.911  1.00 40.66  ? 266 VAL B CG1   1 
ATOM   6295 C  CG2   . VAL B 2 266 ? 117.968 103.153 79.282  1.00 39.13  ? 266 VAL B CG2   1 
ATOM   6296 N  N     . LYS B 2 267 ? 114.387 101.429 77.082  1.00 41.31  ? 267 LYS B N     1 
ATOM   6297 C  CA    . LYS B 2 267 ? 113.204 100.599 76.911  1.00 44.92  ? 267 LYS B CA    1 
ATOM   6298 C  C     . LYS B 2 267 ? 113.209 99.888  75.563  1.00 44.44  ? 267 LYS B C     1 
ATOM   6299 O  O     . LYS B 2 267 ? 113.025 98.668  75.495  1.00 54.10  ? 267 LYS B O     1 
ATOM   6300 C  CB    . LYS B 2 267 ? 111.968 101.482 77.066  1.00 46.71  ? 267 LYS B CB    1 
ATOM   6301 C  CG    . LYS B 2 267 ? 110.645 100.808 76.858  1.00 51.43  ? 267 LYS B CG    1 
ATOM   6302 C  CD    . LYS B 2 267 ? 109.612 101.818 76.388  1.00 56.51  ? 267 LYS B CD    1 
ATOM   6303 C  CE    . LYS B 2 267 ? 109.648 103.081 77.231  1.00 53.54  ? 267 LYS B CE    1 
ATOM   6304 N  NZ    . LYS B 2 267 ? 108.882 104.186 76.600  1.00 59.33  ? 267 LYS B NZ    1 
ATOM   6305 N  N     . THR B 2 268 ? 113.443 100.630 74.481  1.00 43.08  ? 268 THR B N     1 
ATOM   6306 C  CA    . THR B 2 268 ? 113.372 100.084 73.131  1.00 42.81  ? 268 THR B CA    1 
ATOM   6307 C  C     . THR B 2 268 ? 114.513 99.128  72.806  1.00 42.47  ? 268 THR B C     1 
ATOM   6308 O  O     . THR B 2 268 ? 114.287 98.133  72.111  1.00 47.87  ? 268 THR B O     1 
ATOM   6309 C  CB    . THR B 2 268 ? 113.337 101.235 72.116  1.00 44.96  ? 268 THR B CB    1 
ATOM   6310 O  OG1   . THR B 2 268 ? 112.007 101.760 72.038  1.00 49.81  ? 268 THR B OG1   1 
ATOM   6311 C  CG2   . THR B 2 268 ? 113.769 100.774 70.737  1.00 47.80  ? 268 THR B CG2   1 
ATOM   6312 N  N     . PHE B 2 269 ? 115.719 99.375  73.307  1.00 46.66  ? 269 PHE B N     1 
ATOM   6313 C  CA    . PHE B 2 269 ? 116.859 98.523  73.005  1.00 44.13  ? 269 PHE B CA    1 
ATOM   6314 C  C     . PHE B 2 269 ? 116.929 97.298  73.907  1.00 44.65  ? 269 PHE B C     1 
ATOM   6315 O  O     . PHE B 2 269 ? 117.952 96.608  73.919  1.00 50.67  ? 269 PHE B O     1 
ATOM   6316 C  CB    . PHE B 2 269 ? 118.157 99.325  73.092  1.00 44.87  ? 269 PHE B CB    1 
ATOM   6317 C  CG    . PHE B 2 269 ? 118.512 100.035 71.818  1.00 44.76  ? 269 PHE B CG    1 
ATOM   6318 C  CD1   . PHE B 2 269 ? 119.266 99.405  70.845  1.00 44.69  ? 269 PHE B CD1   1 
ATOM   6319 C  CD2   . PHE B 2 269 ? 118.083 101.329 71.589  1.00 39.64  ? 269 PHE B CD2   1 
ATOM   6320 C  CE1   . PHE B 2 269 ? 119.587 100.055 69.670  1.00 40.55  ? 269 PHE B CE1   1 
ATOM   6321 C  CE2   . PHE B 2 269 ? 118.401 101.982 70.419  1.00 39.37  ? 269 PHE B CE2   1 
ATOM   6322 C  CZ    . PHE B 2 269 ? 119.155 101.345 69.458  1.00 37.34  ? 269 PHE B CZ    1 
ATOM   6323 N  N     . GLY B 2 270 ? 115.866 97.012  74.656  1.00 47.80  ? 270 GLY B N     1 
ATOM   6324 C  CA    . GLY B 2 270 ? 115.811 95.797  75.441  1.00 49.05  ? 270 GLY B CA    1 
ATOM   6325 C  C     . GLY B 2 270 ? 116.715 95.773  76.648  1.00 48.46  ? 270 GLY B C     1 
ATOM   6326 O  O     . GLY B 2 270 ? 117.087 94.693  77.109  1.00 48.76  ? 270 GLY B O     1 
ATOM   6327 N  N     . HIS B 2 271 ? 117.088 96.938  77.173  1.00 45.67  ? 271 HIS B N     1 
ATOM   6328 C  CA    . HIS B 2 271 ? 117.965 97.028  78.329  1.00 44.63  ? 271 HIS B CA    1 
ATOM   6329 C  C     . HIS B 2 271 ? 117.212 97.386  79.602  1.00 42.73  ? 271 HIS B C     1 
ATOM   6330 O  O     . HIS B 2 271 ? 117.820 97.868  80.562  1.00 47.37  ? 271 HIS B O     1 
ATOM   6331 C  CB    . HIS B 2 271 ? 119.081 98.036  78.061  1.00 45.51  ? 271 HIS B CB    1 
ATOM   6332 C  CG    . HIS B 2 271 ? 120.283 97.434  77.406  1.00 48.57  ? 271 HIS B CG    1 
ATOM   6333 N  ND1   . HIS B 2 271 ? 121.362 96.963  78.121  1.00 49.06  ? 271 HIS B ND1   1 
ATOM   6334 C  CD2   . HIS B 2 271 ? 120.566 97.205  76.103  1.00 46.08  ? 271 HIS B CD2   1 
ATOM   6335 C  CE1   . HIS B 2 271 ? 122.263 96.479  77.286  1.00 53.92  ? 271 HIS B CE1   1 
ATOM   6336 N  NE2   . HIS B 2 271 ? 121.804 96.613  76.055  1.00 51.93  ? 271 HIS B NE2   1 
ATOM   6337 N  N     . ARG B 2 272 ? 115.897 97.172  79.622  1.00 40.63  ? 272 ARG B N     1 
ATOM   6338 C  CA    . ARG B 2 272 ? 115.116 97.476  80.816  1.00 45.46  ? 272 ARG B CA    1 
ATOM   6339 C  C     . ARG B 2 272 ? 115.449 96.521  81.955  1.00 44.94  ? 272 ARG B C     1 
ATOM   6340 O  O     . ARG B 2 272 ? 115.551 96.940  83.114  1.00 43.83  ? 272 ARG B O     1 
ATOM   6341 C  CB    . ARG B 2 272 ? 113.627 97.432  80.483  1.00 49.46  ? 272 ARG B CB    1 
ATOM   6342 C  CG    . ARG B 2 272 ? 112.733 98.033  81.546  1.00 55.38  ? 272 ARG B CG    1 
ATOM   6343 C  CD    . ARG B 2 272 ? 111.445 98.545  80.934  1.00 57.04  ? 272 ARG B CD    1 
ATOM   6344 N  NE    . ARG B 2 272 ? 110.836 97.565  80.045  1.00 60.96  ? 272 ARG B NE    1 
ATOM   6345 C  CZ    . ARG B 2 272 ? 109.674 97.733  79.431  1.00 60.32  ? 272 ARG B CZ    1 
ATOM   6346 N  NH1   . ARG B 2 272 ? 108.971 98.844  79.573  1.00 55.50  ? 272 ARG B NH1   1 
ATOM   6347 N  NH2   . ARG B 2 272 ? 109.204 96.761  78.654  1.00 62.93  ? 272 ARG B NH2   1 
ATOM   6348 N  N     . GLU B 2 273 ? 115.626 95.234  81.647  1.00 44.41  ? 273 GLU B N     1 
ATOM   6349 C  CA    . GLU B 2 273 ? 115.941 94.257  82.684  1.00 39.94  ? 273 GLU B CA    1 
ATOM   6350 C  C     . GLU B 2 273 ? 117.333 94.485  83.259  1.00 39.41  ? 273 GLU B C     1 
ATOM   6351 O  O     . GLU B 2 273 ? 117.547 94.320  84.466  1.00 45.38  ? 273 GLU B O     1 
ATOM   6352 C  CB    . GLU B 2 273 ? 115.817 92.842  82.125  1.00 45.13  ? 273 GLU B CB    1 
ATOM   6353 C  CG    . GLU B 2 273 ? 114.469 92.543  81.491  1.00 57.92  ? 273 GLU B CG    1 
ATOM   6354 C  CD    . GLU B 2 273 ? 113.328 92.593  82.486  1.00 68.74  ? 273 GLU B CD    1 
ATOM   6355 O  OE1   . GLU B 2 273 ? 113.559 92.294  83.676  1.00 69.15  ? 273 GLU B OE1   1 
ATOM   6356 O  OE2   . GLU B 2 273 ? 112.197 92.929  82.078  1.00 72.36  ? 273 GLU B OE2   1 
ATOM   6357 N  N     . ALA B 2 274 ? 118.297 94.849  82.411  1.00 35.04  ? 274 ALA B N     1 
ATOM   6358 C  CA    . ALA B 2 274 ? 119.635 95.158  82.905  1.00 32.98  ? 274 ALA B CA    1 
ATOM   6359 C  C     . ALA B 2 274 ? 119.612 96.365  83.835  1.00 33.32  ? 274 ALA B C     1 
ATOM   6360 O  O     . ALA B 2 274 ? 120.262 96.362  84.887  1.00 35.52  ? 274 ALA B O     1 
ATOM   6361 C  CB    . ALA B 2 274 ? 120.583 95.398  81.732  1.00 33.43  ? 274 ALA B CB    1 
ATOM   6362 N  N     . ALA B 2 275 ? 118.864 97.404  83.462  1.00 31.71  ? 275 ALA B N     1 
ATOM   6363 C  CA    . ALA B 2 275 ? 118.732 98.571  84.326  1.00 32.93  ? 275 ALA B CA    1 
ATOM   6364 C  C     . ALA B 2 275 ? 118.044 98.212  85.636  1.00 33.48  ? 275 ALA B C     1 
ATOM   6365 O  O     . ALA B 2 275 ? 118.421 98.715  86.699  1.00 32.94  ? 275 ALA B O     1 
ATOM   6366 C  CB    . ALA B 2 275 ? 117.966 99.676  83.600  1.00 33.47  ? 275 ALA B CB    1 
ATOM   6367 N  N     . ALA B 2 276 ? 117.032 97.344  85.580  1.00 35.23  ? 276 ALA B N     1 
ATOM   6368 C  CA    . ALA B 2 276 ? 116.354 96.917  86.800  1.00 33.70  ? 276 ALA B CA    1 
ATOM   6369 C  C     . ALA B 2 276 ? 117.294 96.152  87.725  1.00 32.82  ? 276 ALA B C     1 
ATOM   6370 O  O     . ALA B 2 276 ? 117.298 96.377  88.940  1.00 34.14  ? 276 ALA B O     1 
ATOM   6371 C  CB    . ALA B 2 276 ? 115.134 96.067  86.451  1.00 32.17  ? 276 ALA B CB    1 
ATOM   6372 N  N     . GLY B 2 277 ? 118.099 95.244  87.171  1.00 30.07  ? 277 GLY B N     1 
ATOM   6373 C  CA    . GLY B 2 277 ? 119.047 94.509  87.995  1.00 28.47  ? 277 GLY B CA    1 
ATOM   6374 C  C     . GLY B 2 277 ? 120.124 95.397  88.587  1.00 33.66  ? 277 GLY B C     1 
ATOM   6375 O  O     . GLY B 2 277 ? 120.505 95.240  89.755  1.00 40.46  ? 277 GLY B O     1 
ATOM   6376 N  N     . LYS B 2 278 ? 120.634 96.341  87.793  1.00 30.38  ? 278 LYS B N     1 
ATOM   6377 C  CA    . LYS B 2 278 ? 121.614 97.286  88.312  1.00 26.62  ? 278 LYS B CA    1 
ATOM   6378 C  C     . LYS B 2 278 ? 121.015 98.134  89.424  1.00 31.17  ? 278 LYS B C     1 
ATOM   6379 O  O     . LYS B 2 278 ? 121.669 98.389  90.443  1.00 35.94  ? 278 LYS B O     1 
ATOM   6380 C  CB    . LYS B 2 278 ? 122.143 98.168  87.184  1.00 24.51  ? 278 LYS B CB    1 
ATOM   6381 C  CG    . LYS B 2 278 ? 123.481 98.810  87.486  1.00 38.71  ? 278 LYS B CG    1 
ATOM   6382 C  CD    . LYS B 2 278 ? 123.715 100.039 86.629  1.00 44.62  ? 278 LYS B CD    1 
ATOM   6383 C  CE    . LYS B 2 278 ? 125.033 100.710 86.973  1.00 42.85  ? 278 LYS B CE    1 
ATOM   6384 N  NZ    . LYS B 2 278 ? 125.662 100.119 88.186  1.00 47.30  ? 278 LYS B NZ    1 
ATOM   6385 N  N     . PHE B 2 279 ? 119.765 98.571  89.252  1.00 32.34  ? 279 PHE B N     1 
ATOM   6386 C  CA    . PHE B 2 279 ? 119.102 99.326  90.305  1.00 28.45  ? 279 PHE B CA    1 
ATOM   6387 C  C     . PHE B 2 279 ? 118.931 98.483  91.556  1.00 28.53  ? 279 PHE B C     1 
ATOM   6388 O  O     . PHE B 2 279 ? 119.068 98.990  92.668  1.00 30.82  ? 279 PHE B O     1 
ATOM   6389 C  CB    . PHE B 2 279 ? 117.743 99.840  89.834  1.00 24.68  ? 279 PHE B CB    1 
ATOM   6390 C  CG    . PHE B 2 279 ? 116.919 100.445 90.935  1.00 26.77  ? 279 PHE B CG    1 
ATOM   6391 C  CD1   . PHE B 2 279 ? 117.103 101.763 91.303  1.00 25.56  ? 279 PHE B CD1   1 
ATOM   6392 C  CD2   . PHE B 2 279 ? 115.975 99.694  91.613  1.00 24.00  ? 279 PHE B CD2   1 
ATOM   6393 C  CE1   . PHE B 2 279 ? 116.360 102.321 92.319  1.00 21.39  ? 279 PHE B CE1   1 
ATOM   6394 C  CE2   . PHE B 2 279 ? 115.233 100.250 92.626  1.00 22.14  ? 279 PHE B CE2   1 
ATOM   6395 C  CZ    . PHE B 2 279 ? 115.427 101.564 92.979  1.00 20.20  ? 279 PHE B CZ    1 
ATOM   6396 N  N     . ALA B 2 280 ? 118.594 97.204  91.397  1.00 29.60  ? 280 ALA B N     1 
ATOM   6397 C  CA    . ALA B 2 280 ? 118.422 96.342  92.560  1.00 28.45  ? 280 ALA B CA    1 
ATOM   6398 C  C     . ALA B 2 280 ? 119.725 96.212  93.338  1.00 31.82  ? 280 ALA B C     1 
ATOM   6399 O  O     . ALA B 2 280 ? 119.742 96.327  94.570  1.00 36.60  ? 280 ALA B O     1 
ATOM   6400 C  CB    . ALA B 2 280 ? 117.910 94.969  92.128  1.00 28.36  ? 280 ALA B CB    1 
ATOM   6401 N  N     . GLU B 2 281 ? 120.835 95.994  92.631  1.00 32.99  ? 281 GLU B N     1 
ATOM   6402 C  CA    . GLU B 2 281 ? 122.116 95.860  93.322  1.00 36.54  ? 281 GLU B CA    1 
ATOM   6403 C  C     . GLU B 2 281 ? 122.532 97.173  93.987  1.00 37.78  ? 281 GLU B C     1 
ATOM   6404 O  O     . GLU B 2 281 ? 123.010 97.173  95.131  1.00 39.66  ? 281 GLU B O     1 
ATOM   6405 C  CB    . GLU B 2 281 ? 123.185 95.343  92.353  1.00 33.43  ? 281 GLU B CB    1 
ATOM   6406 C  CG    . GLU B 2 281 ? 124.106 96.386  91.747  1.00 39.89  ? 281 GLU B CG    1 
ATOM   6407 C  CD    . GLU B 2 281 ? 124.815 95.885  90.507  1.00 54.28  ? 281 GLU B CD    1 
ATOM   6408 O  OE1   . GLU B 2 281 ? 124.591 94.717  90.124  1.00 54.27  ? 281 GLU B OE1   1 
ATOM   6409 O  OE2   . GLU B 2 281 ? 125.594 96.659  89.911  1.00 56.09  ? 281 GLU B OE2   1 
ATOM   6410 N  N     . LEU B 2 282 ? 122.323 98.307  93.311  1.00 34.39  ? 282 LEU B N     1 
ATOM   6411 C  CA    . LEU B 2 282 ? 122.704 99.588  93.899  1.00 29.93  ? 282 LEU B CA    1 
ATOM   6412 C  C     . LEU B 2 282 ? 121.799 99.951  95.069  1.00 32.02  ? 282 LEU B C     1 
ATOM   6413 O  O     . LEU B 2 282 ? 122.255 100.545 96.050  1.00 36.92  ? 282 LEU B O     1 
ATOM   6414 C  CB    . LEU B 2 282 ? 122.676 100.683 92.837  1.00 31.19  ? 282 LEU B CB    1 
ATOM   6415 C  CG    . LEU B 2 282 ? 123.750 100.600 91.755  1.00 33.85  ? 282 LEU B CG    1 
ATOM   6416 C  CD1   . LEU B 2 282 ? 123.521 101.664 90.707  1.00 32.20  ? 282 LEU B CD1   1 
ATOM   6417 C  CD2   . LEU B 2 282 ? 125.128 100.733 92.361  1.00 38.74  ? 282 LEU B CD2   1 
ATOM   6418 N  N     . ASN B 2 283 ? 120.515 99.603  94.981  1.00 29.62  ? 283 ASN B N     1 
ATOM   6419 C  CA    . ASN B 2 283 ? 119.586 99.836  96.078  1.00 29.03  ? 283 ASN B CA    1 
ATOM   6420 C  C     . ASN B 2 283 ? 119.957 99.002  97.294  1.00 31.19  ? 283 ASN B C     1 
ATOM   6421 O  O     . ASN B 2 283 ? 119.902 99.491  98.426  1.00 30.32  ? 283 ASN B O     1 
ATOM   6422 C  CB    . ASN B 2 283 ? 118.161 99.521  95.620  1.00 23.44  ? 283 ASN B CB    1 
ATOM   6423 C  CG    . ASN B 2 283 ? 117.114 100.327 96.359  1.00 24.12  ? 283 ASN B CG    1 
ATOM   6424 O  OD1   . ASN B 2 283 ? 117.370 101.445 96.799  1.00 27.82  ? 283 ASN B OD1   1 
ATOM   6425 N  ND2   . ASN B 2 283 ? 115.923 99.764  96.494  1.00 18.84  ? 283 ASN B ND2   1 
ATOM   6426 N  N     . SER B 2 284 ? 120.335 97.739  97.081  1.00 30.75  ? 284 SER B N     1 
ATOM   6427 C  CA    . SER B 2 284 ? 120.765 96.906  98.199  1.00 28.25  ? 284 SER B CA    1 
ATOM   6428 C  C     . SER B 2 284 ? 122.032 97.456  98.840  1.00 30.58  ? 284 SER B C     1 
ATOM   6429 O  O     . SER B 2 284 ? 122.152 97.482  100.071 1.00 37.00  ? 284 SER B O     1 
ATOM   6430 C  CB    . SER B 2 284 ? 120.976 95.468  97.732  1.00 33.12  ? 284 SER B CB    1 
ATOM   6431 O  OG    . SER B 2 284 ? 122.319 95.249  97.344  1.00 42.96  ? 284 SER B OG    1 
ATOM   6432 N  N     . GLU B 2 285 ? 122.991 97.900  98.022  1.00 32.84  ? 285 GLU B N     1 
ATOM   6433 C  CA    . GLU B 2 285 ? 124.209 98.488  98.574  1.00 34.42  ? 285 GLU B CA    1 
ATOM   6434 C  C     . GLU B 2 285 ? 123.904 99.750  99.374  1.00 31.76  ? 285 GLU B C     1 
ATOM   6435 O  O     . GLU B 2 285 ? 124.438 99.944  100.474 1.00 35.81  ? 285 GLU B O     1 
ATOM   6436 C  CB    . GLU B 2 285 ? 125.198 98.794  97.452  1.00 33.65  ? 285 GLU B CB    1 
ATOM   6437 C  CG    . GLU B 2 285 ? 126.300 97.766  97.305  1.00 38.81  ? 285 GLU B CG    1 
ATOM   6438 C  CD    . GLU B 2 285 ? 126.964 97.820  95.946  1.00 54.37  ? 285 GLU B CD    1 
ATOM   6439 O  OE1   . GLU B 2 285 ? 127.084 98.929  95.384  1.00 55.51  ? 285 GLU B OE1   1 
ATOM   6440 O  OE2   . GLU B 2 285 ? 127.364 96.752  95.437  1.00 56.67  ? 285 GLU B OE2   1 
ATOM   6441 N  N     . THR B 2 286 ? 123.043 100.616 98.835  1.00 30.10  ? 286 THR B N     1 
ATOM   6442 C  CA    . THR B 2 286 ? 122.664 101.833 99.543  1.00 30.57  ? 286 THR B CA    1 
ATOM   6443 C  C     . THR B 2 286 ? 121.961 101.510 100.854 1.00 32.62  ? 286 THR B C     1 
ATOM   6444 O  O     . THR B 2 286 ? 122.213 102.157 101.873 1.00 36.46  ? 286 THR B O     1 
ATOM   6445 C  CB    . THR B 2 286 ? 121.768 102.697 98.657  1.00 32.12  ? 286 THR B CB    1 
ATOM   6446 O  OG1   . THR B 2 286 ? 122.419 102.930 97.404  1.00 38.59  ? 286 THR B OG1   1 
ATOM   6447 C  CG2   . THR B 2 286 ? 121.481 104.029 99.323  1.00 30.00  ? 286 THR B CG2   1 
ATOM   6448 N  N     . GLN B 2 287 ? 121.077 100.510 100.849 1.00 31.64  ? 287 GLN B N     1 
ATOM   6449 C  CA    . GLN B 2 287 ? 120.388 100.126 102.075 1.00 27.70  ? 287 GLN B CA    1 
ATOM   6450 C  C     . GLN B 2 287 ? 121.362 99.606  103.123 1.00 30.49  ? 287 GLN B C     1 
ATOM   6451 O  O     . GLN B 2 287 ? 121.265 99.968  104.300 1.00 36.09  ? 287 GLN B O     1 
ATOM   6452 C  CB    . GLN B 2 287 ? 119.325 99.073  101.774 1.00 26.62  ? 287 GLN B CB    1 
ATOM   6453 C  CG    . GLN B 2 287 ? 118.589 98.579  103.000 1.00 29.64  ? 287 GLN B CG    1 
ATOM   6454 C  CD    . GLN B 2 287 ? 118.009 97.198  102.805 1.00 39.15  ? 287 GLN B CD    1 
ATOM   6455 O  OE1   . GLN B 2 287 ? 118.568 96.375  102.082 1.00 41.56  ? 287 GLN B OE1   1 
ATOM   6456 N  NE2   . GLN B 2 287 ? 116.875 96.937  103.442 1.00 36.51  ? 287 GLN B NE2   1 
ATOM   6457 N  N     . GLN B 2 288 ? 122.303 98.749  102.720 1.00 29.92  ? 288 GLN B N     1 
ATOM   6458 C  CA    . GLN B 2 288 ? 123.259 98.204  103.679 1.00 26.00  ? 288 GLN B CA    1 
ATOM   6459 C  C     . GLN B 2 288 ? 124.127 99.306  104.273 1.00 31.71  ? 288 GLN B C     1 
ATOM   6460 O  O     . GLN B 2 288 ? 124.327 99.372  105.495 1.00 36.05  ? 288 GLN B O     1 
ATOM   6461 C  CB    . GLN B 2 288 ? 124.123 97.137  103.008 1.00 27.07  ? 288 GLN B CB    1 
ATOM   6462 C  CG    . GLN B 2 288 ? 123.380 95.847  102.704 1.00 43.17  ? 288 GLN B CG    1 
ATOM   6463 C  CD    . GLN B 2 288 ? 123.972 95.088  101.532 1.00 56.43  ? 288 GLN B CD    1 
ATOM   6464 O  OE1   . GLN B 2 288 ? 124.994 95.484  100.973 1.00 57.64  ? 288 GLN B OE1   1 
ATOM   6465 N  NE2   . GLN B 2 288 ? 123.329 93.990  101.153 1.00 50.12  ? 288 GLN B NE2   1 
ATOM   6466 N  N     . SER B 2 289 ? 124.643 100.194 103.418 1.00 31.46  ? 289 SER B N     1 
ATOM   6467 C  CA    . SER B 2 289 ? 125.476 101.286 103.907 1.00 26.34  ? 289 SER B CA    1 
ATOM   6468 C  C     . SER B 2 289 ? 124.684 102.226 104.805 1.00 28.36  ? 289 SER B C     1 
ATOM   6469 O  O     . SER B 2 289 ? 125.186 102.676 105.842 1.00 37.85  ? 289 SER B O     1 
ATOM   6470 C  CB    . SER B 2 289 ? 126.080 102.047 102.731 1.00 25.85  ? 289 SER B CB    1 
ATOM   6471 O  OG    . SER B 2 289 ? 126.875 101.195 101.930 1.00 30.73  ? 289 SER B OG    1 
ATOM   6472 N  N     . SER B 2 290 ? 123.440 102.530 104.425 1.00 29.92  ? 290 SER B N     1 
ATOM   6473 C  CA    . SER B 2 290 ? 122.609 103.417 105.226 1.00 28.48  ? 290 SER B CA    1 
ATOM   6474 C  C     . SER B 2 290 ? 122.305 102.806 106.582 1.00 27.58  ? 290 SER B C     1 
ATOM   6475 O  O     . SER B 2 290 ? 122.324 103.504 107.598 1.00 31.62  ? 290 SER B O     1 
ATOM   6476 C  CB    . SER B 2 290 ? 121.312 103.735 104.483 1.00 27.16  ? 290 SER B CB    1 
ATOM   6477 O  OG    . SER B 2 290 ? 121.569 104.434 103.280 1.00 36.56  ? 290 SER B OG    1 
ATOM   6478 N  N     . PHE B 2 291 ? 122.013 101.505 106.621 1.00 28.77  ? 291 PHE B N     1 
ATOM   6479 C  CA    . PHE B 2 291 ? 121.742 100.857 107.898 1.00 27.03  ? 291 PHE B CA    1 
ATOM   6480 C  C     . PHE B 2 291 ? 122.969 100.886 108.794 1.00 30.32  ? 291 PHE B C     1 
ATOM   6481 O  O     . PHE B 2 291 ? 122.869 101.192 109.986 1.00 34.27  ? 291 PHE B O     1 
ATOM   6482 C  CB    . PHE B 2 291 ? 121.287 99.417  107.690 1.00 28.14  ? 291 PHE B CB    1 
ATOM   6483 C  CG    . PHE B 2 291 ? 121.461 98.566  108.907 1.00 34.20  ? 291 PHE B CG    1 
ATOM   6484 C  CD1   . PHE B 2 291 ? 120.718 98.813  110.047 1.00 35.09  ? 291 PHE B CD1   1 
ATOM   6485 C  CD2   . PHE B 2 291 ? 122.396 97.551  108.932 1.00 36.88  ? 291 PHE B CD2   1 
ATOM   6486 C  CE1   . PHE B 2 291 ? 120.884 98.047  111.175 1.00 30.50  ? 291 PHE B CE1   1 
ATOM   6487 C  CE2   . PHE B 2 291 ? 122.567 96.784  110.061 1.00 34.34  ? 291 PHE B CE2   1 
ATOM   6488 C  CZ    . PHE B 2 291 ? 121.809 97.033  111.180 1.00 31.68  ? 291 PHE B CZ    1 
ATOM   6489 N  N     . GLY B 2 292 ? 124.138 100.559 108.241 1.00 31.09  ? 292 GLY B N     1 
ATOM   6490 C  CA    . GLY B 2 292 ? 125.344 100.590 109.055 1.00 28.27  ? 292 GLY B CA    1 
ATOM   6491 C  C     . GLY B 2 292 ? 125.633 101.974 109.602 1.00 30.97  ? 292 GLY B C     1 
ATOM   6492 O  O     . GLY B 2 292 ? 125.898 102.148 110.799 1.00 36.22  ? 292 GLY B O     1 
ATOM   6493 N  N     . ALA B 2 293 ? 125.564 102.985 108.731 1.00 28.43  ? 293 ALA B N     1 
ATOM   6494 C  CA    . ALA B 2 293 ? 125.820 104.353 109.161 1.00 28.08  ? 293 ALA B CA    1 
ATOM   6495 C  C     . ALA B 2 293 ? 124.808 104.803 110.201 1.00 32.40  ? 293 ALA B C     1 
ATOM   6496 O  O     . ALA B 2 293 ? 125.177 105.423 111.202 1.00 38.28  ? 293 ALA B O     1 
ATOM   6497 C  CB    . ALA B 2 293 ? 125.803 105.292 107.957 1.00 32.04  ? 293 ALA B CB    1 
ATOM   6498 N  N     . GLN B 2 294 ? 123.527 104.495 109.988 1.00 32.32  ? 294 GLN B N     1 
ATOM   6499 C  CA    . GLN B 2 294 ? 122.489 104.918 110.918 1.00 28.58  ? 294 GLN B CA    1 
ATOM   6500 C  C     . GLN B 2 294 ? 122.656 104.250 112.272 1.00 28.99  ? 294 GLN B C     1 
ATOM   6501 O  O     . GLN B 2 294 ? 122.536 104.907 113.310 1.00 30.09  ? 294 GLN B O     1 
ATOM   6502 C  CB    . GLN B 2 294 ? 121.114 104.609 110.331 1.00 29.83  ? 294 GLN B CB    1 
ATOM   6503 C  CG    . GLN B 2 294 ? 119.971 105.352 110.989 1.00 42.94  ? 294 GLN B CG    1 
ATOM   6504 C  CD    . GLN B 2 294 ? 119.913 106.808 110.577 1.00 51.41  ? 294 GLN B CD    1 
ATOM   6505 O  OE1   . GLN B 2 294 ? 119.903 107.128 109.390 1.00 57.22  ? 294 GLN B OE1   1 
ATOM   6506 N  NE2   . GLN B 2 294 ? 119.868 107.700 111.559 1.00 48.23  ? 294 GLN B NE2   1 
ATOM   6507 N  N     . PHE B 2 295 ? 122.949 102.948 112.283 1.00 27.78  ? 295 PHE B N     1 
ATOM   6508 C  CA    . PHE B 2 295 ? 123.134 102.237 113.541 1.00 25.45  ? 295 PHE B CA    1 
ATOM   6509 C  C     . PHE B 2 295 ? 124.313 102.801 114.319 1.00 28.45  ? 295 PHE B C     1 
ATOM   6510 O  O     . PHE B 2 295 ? 124.201 103.093 115.516 1.00 32.86  ? 295 PHE B O     1 
ATOM   6511 C  CB    . PHE B 2 295 ? 123.328 100.746 113.266 1.00 29.18  ? 295 PHE B CB    1 
ATOM   6512 C  CG    . PHE B 2 295 ? 123.847 99.971  114.442 1.00 31.43  ? 295 PHE B CG    1 
ATOM   6513 C  CD1   . PHE B 2 295 ? 123.104 99.866  115.604 1.00 31.19  ? 295 PHE B CD1   1 
ATOM   6514 C  CD2   . PHE B 2 295 ? 125.077 99.343  114.384 1.00 33.19  ? 295 PHE B CD2   1 
ATOM   6515 C  CE1   . PHE B 2 295 ? 123.581 99.154  116.682 1.00 28.84  ? 295 PHE B CE1   1 
ATOM   6516 C  CE2   . PHE B 2 295 ? 125.558 98.631  115.460 1.00 28.82  ? 295 PHE B CE2   1 
ATOM   6517 C  CZ    . PHE B 2 295 ? 124.809 98.536  116.609 1.00 26.09  ? 295 PHE B CZ    1 
ATOM   6518 N  N     . PHE B 2 296 ? 125.452 102.991 113.651 1.00 33.61  ? 296 PHE B N     1 
ATOM   6519 C  CA    . PHE B 2 296 ? 126.626 103.462 114.378 1.00 33.11  ? 296 PHE B CA    1 
ATOM   6520 C  C     . PHE B 2 296 ? 126.481 104.921 114.798 1.00 33.81  ? 296 PHE B C     1 
ATOM   6521 O  O     . PHE B 2 296 ? 126.943 105.306 115.876 1.00 36.50  ? 296 PHE B O     1 
ATOM   6522 C  CB    . PHE B 2 296 ? 127.883 103.247 113.545 1.00 36.97  ? 296 PHE B CB    1 
ATOM   6523 C  CG    . PHE B 2 296 ? 128.586 101.964 113.854 1.00 39.87  ? 296 PHE B CG    1 
ATOM   6524 C  CD1   . PHE B 2 296 ? 129.378 101.851 114.980 1.00 40.85  ? 296 PHE B CD1   1 
ATOM   6525 C  CD2   . PHE B 2 296 ? 128.439 100.863 113.033 1.00 40.68  ? 296 PHE B CD2   1 
ATOM   6526 C  CE1   . PHE B 2 296 ? 130.020 100.671 115.274 1.00 43.27  ? 296 PHE B CE1   1 
ATOM   6527 C  CE2   . PHE B 2 296 ? 129.078 99.680  113.321 1.00 46.88  ? 296 PHE B CE2   1 
ATOM   6528 C  CZ    . PHE B 2 296 ? 129.870 99.583  114.443 1.00 48.95  ? 296 PHE B CZ    1 
ATOM   6529 N  N     . SER B 2 297 ? 125.838 105.748 113.973 1.00 31.91  ? 297 SER B N     1 
ATOM   6530 C  CA    . SER B 2 297 ? 125.595 107.132 114.357 1.00 28.34  ? 297 SER B CA    1 
ATOM   6531 C  C     . SER B 2 297 ? 124.630 107.220 115.531 1.00 32.10  ? 297 SER B C     1 
ATOM   6532 O  O     . SER B 2 297 ? 124.800 108.062 116.419 1.00 40.55  ? 297 SER B O     1 
ATOM   6533 C  CB    . SER B 2 297 ? 125.059 107.915 113.161 1.00 33.40  ? 297 SER B CB    1 
ATOM   6534 O  OG    . SER B 2 297 ? 124.929 109.289 113.467 1.00 45.06  ? 297 SER B OG    1 
ATOM   6535 N  N     . GLY B 2 298 ? 123.606 106.368 115.553 1.00 29.99  ? 298 GLY B N     1 
ATOM   6536 C  CA    . GLY B 2 298 ? 122.669 106.359 116.653 1.00 25.55  ? 298 GLY B CA    1 
ATOM   6537 C  C     . GLY B 2 298 ? 123.172 105.697 117.909 1.00 31.03  ? 298 GLY B C     1 
ATOM   6538 O  O     . GLY B 2 298 ? 122.556 105.862 118.962 1.00 34.41  ? 298 GLY B O     1 
ATOM   6539 N  N     . LEU B 2 299 ? 124.264 104.936 117.820 1.00 30.92  ? 299 LEU B N     1 
ATOM   6540 C  CA    . LEU B 2 299 ? 124.875 104.388 119.025 1.00 28.29  ? 299 LEU B CA    1 
ATOM   6541 C  C     . LEU B 2 299 ? 125.449 105.463 119.939 1.00 30.66  ? 299 LEU B C     1 
ATOM   6542 O  O     . LEU B 2 299 ? 125.722 105.177 121.108 1.00 36.24  ? 299 LEU B O     1 
ATOM   6543 C  CB    . LEU B 2 299 ? 125.983 103.402 118.662 1.00 25.45  ? 299 LEU B CB    1 
ATOM   6544 C  CG    . LEU B 2 299 ? 125.574 101.959 118.376 1.00 31.84  ? 299 LEU B CG    1 
ATOM   6545 C  CD1   . LEU B 2 299 ? 126.808 101.089 118.242 1.00 33.98  ? 299 LEU B CD1   1 
ATOM   6546 C  CD2   . LEU B 2 299 ? 124.655 101.435 119.461 1.00 27.10  ? 299 LEU B CD2   1 
ATOM   6547 N  N     . VAL B 2 300 ? 125.646 106.682 119.436 1.00 30.45  ? 300 VAL B N     1 
ATOM   6548 C  CA    . VAL B 2 300 ? 126.329 107.711 120.215 1.00 27.83  ? 300 VAL B CA    1 
ATOM   6549 C  C     . VAL B 2 300 ? 125.486 108.136 121.411 1.00 29.70  ? 300 VAL B C     1 
ATOM   6550 O  O     . VAL B 2 300 ? 125.995 108.270 122.530 1.00 33.88  ? 300 VAL B O     1 
ATOM   6551 C  CB    . VAL B 2 300 ? 126.685 108.910 119.318 1.00 31.54  ? 300 VAL B CB    1 
ATOM   6552 C  CG1   . VAL B 2 300 ? 127.460 109.947 120.104 1.00 33.21  ? 300 VAL B CG1   1 
ATOM   6553 C  CG2   . VAL B 2 300 ? 127.499 108.451 118.128 1.00 29.86  ? 300 VAL B CG2   1 
ATOM   6554 N  N     . SER B 2 301 ? 124.188 108.365 121.194 1.00 34.46  ? 301 SER B N     1 
ATOM   6555 C  CA    . SER B 2 301 ? 123.341 108.862 122.279 1.00 33.05  ? 301 SER B CA    1 
ATOM   6556 C  C     . SER B 2 301 ? 123.195 107.864 123.424 1.00 34.21  ? 301 SER B C     1 
ATOM   6557 O  O     . SER B 2 301 ? 123.339 108.274 124.590 1.00 35.47  ? 301 SER B O     1 
ATOM   6558 C  CB    . SER B 2 301 ? 121.984 109.295 121.716 1.00 31.81  ? 301 SER B CB    1 
ATOM   6559 O  OG    . SER B 2 301 ? 121.119 109.734 122.746 1.00 50.20  ? 301 SER B OG    1 
ATOM   6560 N  N     . PRO B 2 302 ? 122.898 106.577 123.192 1.00 30.98  ? 302 PRO B N     1 
ATOM   6561 C  CA    . PRO B 2 302 ? 122.840 105.639 124.326 1.00 29.30  ? 302 PRO B CA    1 
ATOM   6562 C  C     . PRO B 2 302 ? 124.134 105.524 125.114 1.00 29.66  ? 302 PRO B C     1 
ATOM   6563 O  O     . PRO B 2 302 ? 124.078 105.363 126.335 1.00 35.61  ? 302 PRO B O     1 
ATOM   6564 C  CB    . PRO B 2 302 ? 122.466 104.312 123.654 1.00 29.02  ? 302 PRO B CB    1 
ATOM   6565 C  CG    . PRO B 2 302 ? 121.705 104.714 122.468 1.00 30.81  ? 302 PRO B CG    1 
ATOM   6566 C  CD    . PRO B 2 302 ? 122.374 105.951 121.966 1.00 31.39  ? 302 PRO B CD    1 
ATOM   6567 N  N     . ALA B 2 303 ? 125.297 105.592 124.465 1.00 27.24  ? 303 ALA B N     1 
ATOM   6568 C  CA    . ALA B 2 303 ? 126.553 105.493 125.206 1.00 28.10  ? 303 ALA B CA    1 
ATOM   6569 C  C     . ALA B 2 303 ? 126.767 106.705 126.106 1.00 32.14  ? 303 ALA B C     1 
ATOM   6570 O  O     . ALA B 2 303 ? 127.190 106.568 127.264 1.00 34.36  ? 303 ALA B O     1 
ATOM   6571 C  CB    . ALA B 2 303 ? 127.721 105.331 124.236 1.00 29.97  ? 303 ALA B CB    1 
ATOM   6572 N  N     . THR B 2 304 ? 126.485 107.901 125.585 1.00 31.19  ? 304 THR B N     1 
ATOM   6573 C  CA    . THR B 2 304 ? 126.567 109.106 126.400 1.00 30.98  ? 304 THR B CA    1 
ATOM   6574 C  C     . THR B 2 304 ? 125.593 109.039 127.566 1.00 35.15  ? 304 THR B C     1 
ATOM   6575 O  O     . THR B 2 304 ? 125.944 109.387 128.700 1.00 39.65  ? 304 THR B O     1 
ATOM   6576 C  CB    . THR B 2 304 ? 126.292 110.336 125.534 1.00 31.71  ? 304 THR B CB    1 
ATOM   6577 O  OG1   . THR B 2 304 ? 127.336 110.480 124.566 1.00 37.11  ? 304 THR B OG1   1 
ATOM   6578 C  CG2   . THR B 2 304 ? 126.222 111.591 126.382 1.00 37.21  ? 304 THR B CG2   1 
ATOM   6579 N  N     . MET B 2 305 ? 124.368 108.577 127.308 1.00 32.68  ? 305 MET B N     1 
ATOM   6580 C  CA    . MET B 2 305 ? 123.392 108.428 128.380 1.00 28.99  ? 305 MET B CA    1 
ATOM   6581 C  C     . MET B 2 305 ? 123.865 107.421 129.419 1.00 31.52  ? 305 MET B C     1 
ATOM   6582 O  O     . MET B 2 305 ? 123.663 107.620 130.618 1.00 39.76  ? 305 MET B O     1 
ATOM   6583 C  CB    . MET B 2 305 ? 122.041 108.010 127.802 1.00 31.17  ? 305 MET B CB    1 
ATOM   6584 C  CG    . MET B 2 305 ? 120.891 108.087 128.788 1.00 37.03  ? 305 MET B CG    1 
ATOM   6585 S  SD    . MET B 2 305 ? 119.468 108.971 128.128 1.00 64.79  ? 305 MET B SD    1 
ATOM   6586 C  CE    . MET B 2 305 ? 119.493 108.420 126.424 1.00 50.70  ? 305 MET B CE    1 
ATOM   6587 N  N     . PHE B 2 306 ? 124.497 106.334 128.978 1.00 28.67  ? 306 PHE B N     1 
ATOM   6588 C  CA    . PHE B 2 306 ? 124.973 105.314 129.905 1.00 25.34  ? 306 PHE B CA    1 
ATOM   6589 C  C     . PHE B 2 306 ? 126.062 105.858 130.816 1.00 29.66  ? 306 PHE B C     1 
ATOM   6590 O  O     . PHE B 2 306 ? 126.044 105.623 132.030 1.00 34.98  ? 306 PHE B O     1 
ATOM   6591 C  CB    . PHE B 2 306 ? 125.486 104.109 129.122 1.00 29.55  ? 306 PHE B CB    1 
ATOM   6592 C  CG    . PHE B 2 306 ? 126.135 103.059 129.973 1.00 32.30  ? 306 PHE B CG    1 
ATOM   6593 C  CD1   . PHE B 2 306 ? 125.410 102.385 130.938 1.00 34.65  ? 306 PHE B CD1   1 
ATOM   6594 C  CD2   . PHE B 2 306 ? 127.467 102.738 129.800 1.00 29.88  ? 306 PHE B CD2   1 
ATOM   6595 C  CE1   . PHE B 2 306 ? 126.002 101.417 131.716 1.00 31.19  ? 306 PHE B CE1   1 
ATOM   6596 C  CE2   . PHE B 2 306 ? 128.063 101.772 130.577 1.00 32.15  ? 306 PHE B CE2   1 
ATOM   6597 C  CZ    . PHE B 2 306 ? 127.330 101.111 131.535 1.00 31.57  ? 306 PHE B CZ    1 
ATOM   6598 N  N     . ILE B 2 307 ? 127.026 106.582 130.248 1.00 34.08  ? 307 ILE B N     1 
ATOM   6599 C  CA    . ILE B 2 307 ? 128.092 107.150 131.069 1.00 35.72  ? 307 ILE B CA    1 
ATOM   6600 C  C     . ILE B 2 307 ? 127.534 108.206 132.019 1.00 36.84  ? 307 ILE B C     1 
ATOM   6601 O  O     . ILE B 2 307 ? 127.917 108.274 133.198 1.00 34.56  ? 307 ILE B O     1 
ATOM   6602 C  CB    . ILE B 2 307 ? 129.210 107.707 130.172 1.00 35.97  ? 307 ILE B CB    1 
ATOM   6603 C  CG1   . ILE B 2 307 ? 129.794 106.586 129.314 1.00 36.62  ? 307 ILE B CG1   1 
ATOM   6604 C  CG2   . ILE B 2 307 ? 130.304 108.330 131.009 1.00 40.49  ? 307 ILE B CG2   1 
ATOM   6605 C  CD1   . ILE B 2 307 ? 130.584 107.071 128.128 1.00 45.53  ? 307 ILE B CD1   1 
ATOM   6606 N  N     . GLY B 2 308 ? 126.612 109.039 131.528 1.00 36.51  ? 308 GLY B N     1 
ATOM   6607 C  CA    . GLY B 2 308 ? 125.974 110.012 132.395 1.00 32.16  ? 308 GLY B CA    1 
ATOM   6608 C  C     . GLY B 2 308 ? 125.195 109.368 133.525 1.00 34.26  ? 308 GLY B C     1 
ATOM   6609 O  O     . GLY B 2 308 ? 125.176 109.877 134.644 1.00 39.35  ? 308 GLY B O     1 
ATOM   6610 N  N     . ASN B 2 309 ? 124.548 108.234 133.251 1.00 32.01  ? 309 ASN B N     1 
ATOM   6611 C  CA    . ASN B 2 309 ? 123.811 107.532 134.295 1.00 29.32  ? 309 ASN B CA    1 
ATOM   6612 C  C     . ASN B 2 309 ? 124.743 106.869 135.298 1.00 31.32  ? 309 ASN B C     1 
ATOM   6613 O  O     . ASN B 2 309 ? 124.414 106.793 136.485 1.00 39.95  ? 309 ASN B O     1 
ATOM   6614 C  CB    . ASN B 2 309 ? 122.877 106.496 133.676 1.00 27.73  ? 309 ASN B CB    1 
ATOM   6615 C  CG    . ASN B 2 309 ? 121.640 107.116 133.074 1.00 33.35  ? 309 ASN B CG    1 
ATOM   6616 O  OD1   . ASN B 2 309 ? 121.323 108.273 133.337 1.00 36.50  ? 309 ASN B OD1   1 
ATOM   6617 N  ND2   . ASN B 2 309 ? 120.928 106.347 132.265 1.00 34.58  ? 309 ASN B ND2   1 
ATOM   6618 N  N     . LEU B 2 310 ? 125.899 106.378 134.851 1.00 30.19  ? 310 LEU B N     1 
ATOM   6619 C  CA    . LEU B 2 310 ? 126.889 105.872 135.796 1.00 28.58  ? 310 LEU B CA    1 
ATOM   6620 C  C     . LEU B 2 310 ? 127.342 106.977 136.741 1.00 35.03  ? 310 LEU B C     1 
ATOM   6621 O  O     . LEU B 2 310 ? 127.418 106.782 137.964 1.00 37.89  ? 310 LEU B O     1 
ATOM   6622 C  CB    . LEU B 2 310 ? 128.086 105.288 135.048 1.00 31.45  ? 310 LEU B CB    1 
ATOM   6623 C  CG    . LEU B 2 310 ? 127.875 104.000 134.256 1.00 32.88  ? 310 LEU B CG    1 
ATOM   6624 C  CD1   . LEU B 2 310 ? 129.160 103.606 133.557 1.00 30.18  ? 310 LEU B CD1   1 
ATOM   6625 C  CD2   . LEU B 2 310 ? 127.391 102.885 135.162 1.00 33.72  ? 310 LEU B CD2   1 
ATOM   6626 N  N     . SER B 2 311 ? 127.635 108.157 136.188 1.00 36.13  ? 311 SER B N     1 
ATOM   6627 C  CA    . SER B 2 311 ? 128.010 109.278 137.044 1.00 32.39  ? 311 SER B CA    1 
ATOM   6628 C  C     . SER B 2 311 ? 126.861 109.699 137.944 1.00 35.44  ? 311 SER B C     1 
ATOM   6629 O  O     . SER B 2 311 ? 127.089 110.104 139.086 1.00 44.44  ? 311 SER B O     1 
ATOM   6630 C  CB    . SER B 2 311 ? 128.472 110.465 136.211 1.00 39.16  ? 311 SER B CB    1 
ATOM   6631 O  OG    . SER B 2 311 ? 127.368 111.200 135.718 1.00 51.66  ? 311 SER B OG    1 
ATOM   6632 N  N     . TYR B 2 312 ? 125.626 109.628 137.446 1.00 35.15  ? 312 TYR B N     1 
ATOM   6633 C  CA    . TYR B 2 312 ? 124.467 109.955 138.267 1.00 33.63  ? 312 TYR B CA    1 
ATOM   6634 C  C     . TYR B 2 312 ? 124.341 109.003 139.446 1.00 33.75  ? 312 TYR B C     1 
ATOM   6635 O  O     . TYR B 2 312 ? 124.044 109.429 140.564 1.00 37.55  ? 312 TYR B O     1 
ATOM   6636 C  CB    . TYR B 2 312 ? 123.200 109.924 137.413 1.00 36.13  ? 312 TYR B CB    1 
ATOM   6637 C  CG    . TYR B 2 312 ? 121.928 110.175 138.187 1.00 40.49  ? 312 TYR B CG    1 
ATOM   6638 C  CD1   . TYR B 2 312 ? 121.865 111.167 139.154 1.00 43.34  ? 312 TYR B CD1   1 
ATOM   6639 C  CD2   . TYR B 2 312 ? 120.791 109.417 137.955 1.00 39.76  ? 312 TYR B CD2   1 
ATOM   6640 C  CE1   . TYR B 2 312 ? 120.708 111.395 139.865 1.00 44.19  ? 312 TYR B CE1   1 
ATOM   6641 C  CE2   . TYR B 2 312 ? 119.630 109.641 138.662 1.00 36.19  ? 312 TYR B CE2   1 
ATOM   6642 C  CZ    . TYR B 2 312 ? 119.595 110.630 139.615 1.00 38.21  ? 312 TYR B CZ    1 
ATOM   6643 O  OH    . TYR B 2 312 ? 118.440 110.858 140.322 1.00 43.87  ? 312 TYR B OH    1 
ATOM   6644 N  N     . VAL B 2 313 ? 124.558 107.709 139.215 1.00 31.29  ? 313 VAL B N     1 
ATOM   6645 C  CA    . VAL B 2 313 ? 124.498 106.736 140.303 1.00 32.34  ? 313 VAL B CA    1 
ATOM   6646 C  C     . VAL B 2 313 ? 125.587 107.020 141.328 1.00 35.35  ? 313 VAL B C     1 
ATOM   6647 O  O     . VAL B 2 313 ? 125.343 107.010 142.541 1.00 41.59  ? 313 VAL B O     1 
ATOM   6648 C  CB    . VAL B 2 313 ? 124.605 105.304 139.753 1.00 35.31  ? 313 VAL B CB    1 
ATOM   6649 C  CG1   . VAL B 2 313 ? 124.746 104.313 140.892 1.00 32.71  ? 313 VAL B CG1   1 
ATOM   6650 C  CG2   . VAL B 2 313 ? 123.392 104.971 138.905 1.00 39.15  ? 313 VAL B CG2   1 
ATOM   6651 N  N     . ALA B 2 314 ? 126.809 107.277 140.855 1.00 36.57  ? 314 ALA B N     1 
ATOM   6652 C  CA    . ALA B 2 314 ? 127.902 107.568 141.780 1.00 36.15  ? 314 ALA B CA    1 
ATOM   6653 C  C     . ALA B 2 314 ? 127.610 108.822 142.597 1.00 36.12  ? 314 ALA B C     1 
ATOM   6654 O  O     . ALA B 2 314 ? 127.806 108.845 143.820 1.00 37.07  ? 314 ALA B O     1 
ATOM   6655 C  CB    . ALA B 2 314 ? 129.214 107.714 141.012 1.00 31.32  ? 314 ALA B CB    1 
ATOM   6656 N  N     . VAL B 2 315 ? 127.125 109.873 141.934 1.00 35.92  ? 315 VAL B N     1 
ATOM   6657 C  CA    . VAL B 2 315 ? 126.809 111.123 142.615 1.00 35.83  ? 315 VAL B CA    1 
ATOM   6658 C  C     . VAL B 2 315 ? 125.696 110.913 143.629 1.00 38.91  ? 315 VAL B C     1 
ATOM   6659 O  O     . VAL B 2 315 ? 125.772 111.407 144.755 1.00 44.64  ? 315 VAL B O     1 
ATOM   6660 C  CB    . VAL B 2 315 ? 126.443 112.211 141.589 1.00 32.37  ? 315 VAL B CB    1 
ATOM   6661 C  CG1   . VAL B 2 315 ? 125.677 113.340 142.257 1.00 28.49  ? 315 VAL B CG1   1 
ATOM   6662 C  CG2   . VAL B 2 315 ? 127.691 112.740 140.913 1.00 36.94  ? 315 VAL B CG2   1 
ATOM   6663 N  N     . ALA B 2 316 ? 124.650 110.175 143.252 1.00 35.98  ? 316 ALA B N     1 
ATOM   6664 C  CA    . ALA B 2 316 ? 123.540 109.942 144.168 1.00 30.94  ? 316 ALA B CA    1 
ATOM   6665 C  C     . ALA B 2 316 ? 123.992 109.173 145.399 1.00 37.43  ? 316 ALA B C     1 
ATOM   6666 O  O     . ALA B 2 316 ? 123.639 109.534 146.526 1.00 43.52  ? 316 ALA B O     1 
ATOM   6667 C  CB    . ALA B 2 316 ? 122.416 109.196 143.452 1.00 29.30  ? 316 ALA B CB    1 
ATOM   6668 N  N     . VAL B 2 317 ? 124.797 108.125 145.209 1.00 37.90  ? 317 VAL B N     1 
ATOM   6669 C  CA    . VAL B 2 317 ? 125.239 107.319 146.345 1.00 35.14  ? 317 VAL B CA    1 
ATOM   6670 C  C     . VAL B 2 317 ? 126.132 108.137 147.268 1.00 41.11  ? 317 VAL B C     1 
ATOM   6671 O  O     . VAL B 2 317 ? 125.931 108.165 148.489 1.00 46.03  ? 317 VAL B O     1 
ATOM   6672 C  CB    . VAL B 2 317 ? 125.951 106.046 145.858 1.00 37.77  ? 317 VAL B CB    1 
ATOM   6673 C  CG1   . VAL B 2 317 ? 126.597 105.323 147.027 1.00 36.73  ? 317 VAL B CG1   1 
ATOM   6674 C  CG2   . VAL B 2 317 ? 124.971 105.139 145.159 1.00 41.52  ? 317 VAL B CG2   1 
ATOM   6675 N  N     . VAL B 2 318 ? 127.129 108.820 146.701 1.00 43.52  ? 318 VAL B N     1 
ATOM   6676 C  CA    . VAL B 2 318 ? 128.064 109.567 147.536 1.00 42.59  ? 318 VAL B CA    1 
ATOM   6677 C  C     . VAL B 2 318 ? 127.364 110.744 148.207 1.00 46.81  ? 318 VAL B C     1 
ATOM   6678 O  O     . VAL B 2 318 ? 127.638 111.062 149.369 1.00 54.89  ? 318 VAL B O     1 
ATOM   6679 C  CB    . VAL B 2 318 ? 129.282 110.012 146.708 1.00 45.91  ? 318 VAL B CB    1 
ATOM   6680 C  CG1   . VAL B 2 318 ? 130.226 110.842 147.552 1.00 43.49  ? 318 VAL B CG1   1 
ATOM   6681 C  CG2   . VAL B 2 318 ? 130.006 108.797 146.163 1.00 43.70  ? 318 VAL B CG2   1 
ATOM   6682 N  N     . GLY B 2 319 ? 126.435 111.393 147.503 1.00 43.40  ? 319 GLY B N     1 
ATOM   6683 C  CA    . GLY B 2 319 ? 125.688 112.479 148.105 1.00 44.44  ? 319 GLY B CA    1 
ATOM   6684 C  C     . GLY B 2 319 ? 124.780 112.018 149.226 1.00 46.16  ? 319 GLY B C     1 
ATOM   6685 O  O     . GLY B 2 319 ? 124.665 112.690 150.250 1.00 54.12  ? 319 GLY B O     1 
ATOM   6686 N  N     . GLY B 2 320 ? 124.115 110.876 149.049 1.00 40.25  ? 320 GLY B N     1 
ATOM   6687 C  CA    . GLY B 2 320 ? 123.321 110.330 150.136 1.00 40.38  ? 320 GLY B CA    1 
ATOM   6688 C  C     . GLY B 2 320 ? 124.168 109.974 151.341 1.00 47.23  ? 320 GLY B C     1 
ATOM   6689 O  O     . GLY B 2 320 ? 123.784 110.241 152.483 1.00 57.24  ? 320 GLY B O     1 
ATOM   6690 N  N     . LEU B 2 321 ? 125.341 109.383 151.103 1.00 46.52  ? 321 LEU B N     1 
ATOM   6691 C  CA    . LEU B 2 321 ? 126.243 109.066 152.205 1.00 46.42  ? 321 LEU B CA    1 
ATOM   6692 C  C     . LEU B 2 321 ? 126.697 110.329 152.924 1.00 52.43  ? 321 LEU B C     1 
ATOM   6693 O  O     . LEU B 2 321 ? 126.803 110.348 154.156 1.00 59.21  ? 321 LEU B O     1 
ATOM   6694 C  CB    . LEU B 2 321 ? 127.449 108.282 151.692 1.00 45.15  ? 321 LEU B CB    1 
ATOM   6695 C  CG    . LEU B 2 321 ? 127.198 106.871 151.165 1.00 52.62  ? 321 LEU B CG    1 
ATOM   6696 C  CD1   . LEU B 2 321 ? 128.473 106.295 150.576 1.00 49.25  ? 321 LEU B CD1   1 
ATOM   6697 C  CD2   . LEU B 2 321 ? 126.662 105.974 152.262 1.00 53.64  ? 321 LEU B CD2   1 
ATOM   6698 N  N     . GLN B 2 322 ? 126.982 111.392 152.170 1.00 51.37  ? 322 GLN B N     1 
ATOM   6699 C  CA    . GLN B 2 322 ? 127.456 112.628 152.782 1.00 51.15  ? 322 GLN B CA    1 
ATOM   6700 C  C     . GLN B 2 322 ? 126.346 113.337 153.548 1.00 53.81  ? 322 GLN B C     1 
ATOM   6701 O  O     . GLN B 2 322 ? 126.587 113.888 154.627 1.00 59.74  ? 322 GLN B O     1 
ATOM   6702 C  CB    . GLN B 2 322 ? 128.048 113.543 151.714 1.00 49.61  ? 322 GLN B CB    1 
ATOM   6703 C  CG    . GLN B 2 322 ? 129.392 113.069 151.193 1.00 50.58  ? 322 GLN B CG    1 
ATOM   6704 C  CD    . GLN B 2 322 ? 130.127 114.137 150.419 1.00 58.33  ? 322 GLN B CD    1 
ATOM   6705 O  OE1   . GLN B 2 322 ? 129.760 114.466 149.293 1.00 61.76  ? 322 GLN B OE1   1 
ATOM   6706 N  NE2   . GLN B 2 322 ? 131.174 114.686 151.020 1.00 61.06  ? 322 GLN B NE2   1 
ATOM   6707 N  N     . VAL B 2 323 ? 125.128 113.344 153.004 1.00 51.71  ? 323 VAL B N     1 
ATOM   6708 C  CA    . VAL B 2 323 ? 124.010 113.974 153.699 1.00 49.91  ? 323 VAL B CA    1 
ATOM   6709 C  C     . VAL B 2 323 ? 123.679 113.212 154.974 1.00 54.27  ? 323 VAL B C     1 
ATOM   6710 O  O     . VAL B 2 323 ? 123.415 113.815 156.021 1.00 58.76  ? 323 VAL B O     1 
ATOM   6711 C  CB    . VAL B 2 323 ? 122.788 114.084 152.769 1.00 50.40  ? 323 VAL B CB    1 
ATOM   6712 C  CG1   . VAL B 2 323 ? 121.603 114.646 153.524 1.00 52.86  ? 323 VAL B CG1   1 
ATOM   6713 C  CG2   . VAL B 2 323 ? 123.103 114.968 151.580 1.00 48.89  ? 323 VAL B CG2   1 
ATOM   6714 N  N     . ALA B 2 324 ? 123.692 111.877 154.913 1.00 55.05  ? 324 ALA B N     1 
ATOM   6715 C  CA    . ALA B 2 324 ? 123.476 111.087 156.119 1.00 55.73  ? 324 ALA B CA    1 
ATOM   6716 C  C     . ALA B 2 324 ? 124.552 111.359 157.163 1.00 60.93  ? 324 ALA B C     1 
ATOM   6717 O  O     . ALA B 2 324 ? 124.282 111.284 158.367 1.00 68.33  ? 324 ALA B O     1 
ATOM   6718 C  CB    . ALA B 2 324 ? 123.431 109.600 155.773 1.00 50.99  ? 324 ALA B CB    1 
ATOM   6719 N  N     . THR B 2 325 ? 125.770 111.672 156.725 1.00 58.83  ? 325 THR B N     1 
ATOM   6720 C  CA    . THR B 2 325 ? 126.845 112.052 157.630 1.00 61.81  ? 325 THR B CA    1 
ATOM   6721 C  C     . THR B 2 325 ? 126.758 113.509 158.067 1.00 66.32  ? 325 THR B C     1 
ATOM   6722 O  O     . THR B 2 325 ? 127.284 113.858 159.131 1.00 75.10  ? 325 THR B O     1 
ATOM   6723 C  CB    . THR B 2 325 ? 128.201 111.790 156.963 1.00 63.79  ? 325 THR B CB    1 
ATOM   6724 O  OG1   . THR B 2 325 ? 128.209 110.469 156.409 1.00 62.44  ? 325 THR B OG1   1 
ATOM   6725 C  CG2   . THR B 2 325 ? 129.334 111.900 157.970 1.00 68.24  ? 325 THR B CG2   1 
ATOM   6726 N  N     . GLY B 2 326 ? 126.092 114.359 157.288 1.00 61.53  ? 326 GLY B N     1 
ATOM   6727 C  CA    . GLY B 2 326 ? 125.922 115.753 157.634 1.00 57.57  ? 326 GLY B CA    1 
ATOM   6728 C  C     . GLY B 2 326 ? 126.825 116.722 156.904 1.00 59.14  ? 326 GLY B C     1 
ATOM   6729 O  O     . GLY B 2 326 ? 126.787 117.921 157.204 1.00 63.95  ? 326 GLY B O     1 
ATOM   6730 N  N     . GLN B 2 327 ? 127.637 116.249 155.957 1.00 61.70  ? 327 GLN B N     1 
ATOM   6731 C  CA    . GLN B 2 327 ? 128.541 117.142 155.241 1.00 61.52  ? 327 GLN B CA    1 
ATOM   6732 C  C     . GLN B 2 327 ? 127.815 117.995 154.209 1.00 61.60  ? 327 GLN B C     1 
ATOM   6733 O  O     . GLN B 2 327 ? 128.253 119.113 153.919 1.00 69.38  ? 327 GLN B O     1 
ATOM   6734 C  CB    . GLN B 2 327 ? 129.649 116.335 154.566 1.00 55.61  ? 327 GLN B CB    1 
ATOM   6735 C  CG    . GLN B 2 327 ? 130.672 115.767 155.533 1.00 59.97  ? 327 GLN B CG    1 
ATOM   6736 C  CD    . GLN B 2 327 ? 131.294 114.481 155.034 1.00 76.63  ? 327 GLN B CD    1 
ATOM   6737 O  OE1   . GLN B 2 327 ? 130.593 113.564 154.608 1.00 74.98  ? 327 GLN B OE1   1 
ATOM   6738 N  NE2   . GLN B 2 327 ? 132.618 114.406 155.084 1.00 86.71  ? 327 GLN B NE2   1 
ATOM   6739 N  N     . ILE B 2 328 ? 126.720 117.494 153.645 1.00 55.54  ? 328 ILE B N     1 
ATOM   6740 C  CA    . ILE B 2 328 ? 125.942 118.214 152.646 1.00 53.71  ? 328 ILE B CA    1 
ATOM   6741 C  C     . ILE B 2 328 ? 124.487 118.216 153.090 1.00 53.75  ? 328 ILE B C     1 
ATOM   6742 O  O     . ILE B 2 328 ? 124.005 117.233 153.662 1.00 55.35  ? 328 ILE B O     1 
ATOM   6743 C  CB    . ILE B 2 328 ? 126.089 117.581 151.244 1.00 54.64  ? 328 ILE B CB    1 
ATOM   6744 C  CG1   . ILE B 2 328 ? 127.563 117.316 150.931 1.00 59.48  ? 328 ILE B CG1   1 
ATOM   6745 C  CG2   . ILE B 2 328 ? 125.483 118.483 150.182 1.00 50.66  ? 328 ILE B CG2   1 
ATOM   6746 C  CD1   . ILE B 2 328 ? 127.882 117.234 149.457 1.00 60.24  ? 328 ILE B CD1   1 
ATOM   6747 N  N     . THR B 2 329 ? 123.794 119.325 152.852 1.00 50.78  ? 329 THR B N     1 
ATOM   6748 C  CA    . THR B 2 329 ? 122.384 119.392 153.200 1.00 53.80  ? 329 THR B CA    1 
ATOM   6749 C  C     . THR B 2 329 ? 121.534 118.713 152.128 1.00 50.64  ? 329 THR B C     1 
ATOM   6750 O  O     . THR B 2 329 ? 121.968 118.499 150.995 1.00 48.93  ? 329 THR B O     1 
ATOM   6751 C  CB    . THR B 2 329 ? 121.933 120.841 153.392 1.00 50.13  ? 329 THR B CB    1 
ATOM   6752 O  OG1   . THR B 2 329 ? 121.837 121.490 152.120 1.00 50.09  ? 329 THR B OG1   1 
ATOM   6753 C  CG2   . THR B 2 329 ? 122.919 121.591 154.264 1.00 52.95  ? 329 THR B CG2   1 
ATOM   6754 N  N     . LEU B 2 330 ? 120.305 118.364 152.511 1.00 46.22  ? 330 LEU B N     1 
ATOM   6755 C  CA    . LEU B 2 330 ? 119.410 117.669 151.592 1.00 48.11  ? 330 LEU B CA    1 
ATOM   6756 C  C     . LEU B 2 330 ? 118.999 118.560 150.425 1.00 49.06  ? 330 LEU B C     1 
ATOM   6757 O  O     . LEU B 2 330 ? 118.888 118.089 149.287 1.00 50.81  ? 330 LEU B O     1 
ATOM   6758 C  CB    . LEU B 2 330 ? 118.181 117.164 152.345 1.00 46.45  ? 330 LEU B CB    1 
ATOM   6759 C  CG    . LEU B 2 330 ? 117.127 116.454 151.502 1.00 47.47  ? 330 LEU B CG    1 
ATOM   6760 C  CD1   . LEU B 2 330 ? 117.759 115.318 150.727 1.00 49.92  ? 330 LEU B CD1   1 
ATOM   6761 C  CD2   . LEU B 2 330 ? 116.021 115.938 152.388 1.00 50.57  ? 330 LEU B CD2   1 
ATOM   6762 N  N     . GLY B 2 331 ? 118.755 119.844 150.685 1.00 40.90  ? 331 GLY B N     1 
ATOM   6763 C  CA    . GLY B 2 331 ? 118.428 120.751 149.598 1.00 39.58  ? 331 GLY B CA    1 
ATOM   6764 C  C     . GLY B 2 331 ? 119.577 120.928 148.626 1.00 47.83  ? 331 GLY B C     1 
ATOM   6765 O  O     . GLY B 2 331 ? 119.371 121.034 147.413 1.00 46.78  ? 331 GLY B O     1 
ATOM   6766 N  N     . SER B 2 332 ? 120.806 120.962 149.145 1.00 46.66  ? 332 SER B N     1 
ATOM   6767 C  CA    . SER B 2 332 ? 121.973 121.031 148.274 1.00 40.04  ? 332 SER B CA    1 
ATOM   6768 C  C     . SER B 2 332 ? 122.076 119.791 147.402 1.00 39.15  ? 332 SER B C     1 
ATOM   6769 O  O     . SER B 2 332 ? 122.417 119.883 146.219 1.00 41.10  ? 332 SER B O     1 
ATOM   6770 C  CB    . SER B 2 332 ? 123.241 121.213 149.104 1.00 39.85  ? 332 SER B CB    1 
ATOM   6771 O  OG    . SER B 2 332 ? 123.191 122.414 149.850 1.00 48.28  ? 332 SER B OG    1 
ATOM   6772 N  N     . ILE B 2 333 ? 121.784 118.617 147.965 1.00 36.60  ? 333 ILE B N     1 
ATOM   6773 C  CA    . ILE B 2 333 ? 121.837 117.399 147.167 1.00 34.83  ? 333 ILE B CA    1 
ATOM   6774 C  C     . ILE B 2 333 ? 120.721 117.387 146.130 1.00 36.52  ? 333 ILE B C     1 
ATOM   6775 O  O     . ILE B 2 333 ? 120.914 116.889 145.017 1.00 41.47  ? 333 ILE B O     1 
ATOM   6776 C  CB    . ILE B 2 333 ? 121.818 116.154 148.077 1.00 37.81  ? 333 ILE B CB    1 
ATOM   6777 C  CG1   . ILE B 2 333 ? 122.853 115.140 147.593 1.00 41.36  ? 333 ILE B CG1   1 
ATOM   6778 C  CG2   . ILE B 2 333 ? 120.452 115.498 148.114 1.00 40.20  ? 333 ILE B CG2   1 
ATOM   6779 C  CD1   . ILE B 2 333 ? 124.242 115.712 147.463 1.00 41.65  ? 333 ILE B CD1   1 
ATOM   6780 N  N     . GLN B 2 334 ? 119.552 117.944 146.455 1.00 33.28  ? 334 GLN B N     1 
ATOM   6781 C  CA    . GLN B 2 334 ? 118.484 118.049 145.466 1.00 35.17  ? 334 GLN B CA    1 
ATOM   6782 C  C     . GLN B 2 334 ? 118.902 118.946 144.308 1.00 34.61  ? 334 GLN B C     1 
ATOM   6783 O  O     . GLN B 2 334 ? 118.715 118.603 143.131 1.00 36.62  ? 334 GLN B O     1 
ATOM   6784 C  CB    . GLN B 2 334 ? 117.212 118.579 146.128 1.00 36.47  ? 334 GLN B CB    1 
ATOM   6785 C  CG    . GLN B 2 334 ? 116.093 118.896 145.153 1.00 39.99  ? 334 GLN B CG    1 
ATOM   6786 C  CD    . GLN B 2 334 ? 114.953 119.652 145.795 1.00 40.19  ? 334 GLN B CD    1 
ATOM   6787 O  OE1   . GLN B 2 334 ? 114.109 119.067 146.468 1.00 43.49  ? 334 GLN B OE1   1 
ATOM   6788 N  NE2   . GLN B 2 334 ? 114.918 120.959 145.585 1.00 38.14  ? 334 GLN B NE2   1 
ATOM   6789 N  N     . ALA B 2 335 ? 119.489 120.099 144.630 1.00 35.66  ? 335 ALA B N     1 
ATOM   6790 C  CA    . ALA B 2 335 ? 119.983 120.996 143.593 1.00 30.33  ? 335 ALA B CA    1 
ATOM   6791 C  C     . ALA B 2 335 ? 121.065 120.327 142.758 1.00 31.91  ? 335 ALA B C     1 
ATOM   6792 O  O     . ALA B 2 335 ? 121.108 120.496 141.535 1.00 34.94  ? 335 ALA B O     1 
ATOM   6793 C  CB    . ALA B 2 335 ? 120.510 122.284 144.223 1.00 33.95  ? 335 ALA B CB    1 
ATOM   6794 N  N     . PHE B 2 336 ? 121.946 119.556 143.398 1.00 35.23  ? 336 PHE B N     1 
ATOM   6795 C  CA    . PHE B 2 336 ? 123.015 118.895 142.660 1.00 33.41  ? 336 PHE B CA    1 
ATOM   6796 C  C     . PHE B 2 336 ? 122.479 117.799 141.748 1.00 31.87  ? 336 PHE B C     1 
ATOM   6797 O  O     . PHE B 2 336 ? 123.006 117.594 140.653 1.00 37.91  ? 336 PHE B O     1 
ATOM   6798 C  CB    . PHE B 2 336 ? 124.059 118.324 143.616 1.00 30.15  ? 336 PHE B CB    1 
ATOM   6799 C  CG    . PHE B 2 336 ? 125.409 118.168 142.989 1.00 34.25  ? 336 PHE B CG    1 
ATOM   6800 C  CD1   . PHE B 2 336 ? 125.676 117.099 142.154 1.00 34.13  ? 336 PHE B CD1   1 
ATOM   6801 C  CD2   . PHE B 2 336 ? 126.397 119.106 143.201 1.00 40.90  ? 336 PHE B CD2   1 
ATOM   6802 C  CE1   . PHE B 2 336 ? 126.903 116.964 141.561 1.00 34.77  ? 336 PHE B CE1   1 
ATOM   6803 C  CE2   . PHE B 2 336 ? 127.628 118.972 142.613 1.00 41.29  ? 336 PHE B CE2   1 
ATOM   6804 C  CZ    . PHE B 2 336 ? 127.881 117.902 141.788 1.00 38.72  ? 336 PHE B CZ    1 
ATOM   6805 N  N     . ILE B 2 337 ? 121.456 117.066 142.184 1.00 28.18  ? 337 ILE B N     1 
ATOM   6806 C  CA    . ILE B 2 337 ? 120.848 116.063 141.313 1.00 28.00  ? 337 ILE B CA    1 
ATOM   6807 C  C     . ILE B 2 337 ? 120.199 116.736 140.109 1.00 30.80  ? 337 ILE B C     1 
ATOM   6808 O  O     . ILE B 2 337 ? 120.330 116.271 138.964 1.00 33.11  ? 337 ILE B O     1 
ATOM   6809 C  CB    . ILE B 2 337 ? 119.844 115.208 142.107 1.00 32.50  ? 337 ILE B CB    1 
ATOM   6810 C  CG1   . ILE B 2 337 ? 120.588 114.279 143.066 1.00 32.73  ? 337 ILE B CG1   1 
ATOM   6811 C  CG2   . ILE B 2 337 ? 118.971 114.398 141.173 1.00 36.08  ? 337 ILE B CG2   1 
ATOM   6812 C  CD1   . ILE B 2 337 ? 119.832 113.984 144.340 1.00 35.74  ? 337 ILE B CD1   1 
ATOM   6813 N  N     . GLN B 2 338 ? 119.506 117.855 140.345 1.00 31.83  ? 338 GLN B N     1 
ATOM   6814 C  CA    . GLN B 2 338 ? 118.953 118.625 139.235 1.00 30.37  ? 338 GLN B CA    1 
ATOM   6815 C  C     . GLN B 2 338 ? 120.048 119.068 138.274 1.00 31.38  ? 338 GLN B C     1 
ATOM   6816 O  O     . GLN B 2 338 ? 119.880 118.996 137.051 1.00 35.80  ? 338 GLN B O     1 
ATOM   6817 C  CB    . GLN B 2 338 ? 118.193 119.839 139.762 1.00 28.97  ? 338 GLN B CB    1 
ATOM   6818 C  CG    . GLN B 2 338 ? 116.826 119.532 140.328 1.00 34.14  ? 338 GLN B CG    1 
ATOM   6819 C  CD    . GLN B 2 338 ? 115.931 120.752 140.356 1.00 42.99  ? 338 GLN B CD    1 
ATOM   6820 O  OE1   . GLN B 2 338 ? 115.737 121.368 141.403 1.00 50.08  ? 338 GLN B OE1   1 
ATOM   6821 N  NE2   . GLN B 2 338 ? 115.379 121.108 139.204 1.00 32.80  ? 338 GLN B NE2   1 
ATOM   6822 N  N     . TYR B 2 339 ? 121.178 119.528 138.811 1.00 29.36  ? 339 TYR B N     1 
ATOM   6823 C  CA    . TYR B 2 339 ? 122.273 119.986 137.964 1.00 30.12  ? 339 TYR B CA    1 
ATOM   6824 C  C     . TYR B 2 339 ? 122.930 118.838 137.212 1.00 31.71  ? 339 TYR B C     1 
ATOM   6825 O  O     . TYR B 2 339 ? 123.364 119.021 136.076 1.00 38.18  ? 339 TYR B O     1 
ATOM   6826 C  CB    . TYR B 2 339 ? 123.304 120.740 138.800 1.00 30.35  ? 339 TYR B CB    1 
ATOM   6827 C  CG    . TYR B 2 339 ? 122.825 122.104 139.226 1.00 31.30  ? 339 TYR B CG    1 
ATOM   6828 C  CD1   . TYR B 2 339 ? 122.051 122.875 138.376 1.00 33.59  ? 339 TYR B CD1   1 
ATOM   6829 C  CD2   . TYR B 2 339 ? 123.135 122.616 140.475 1.00 27.51  ? 339 TYR B CD2   1 
ATOM   6830 C  CE1   . TYR B 2 339 ? 121.602 124.113 138.755 1.00 36.86  ? 339 TYR B CE1   1 
ATOM   6831 C  CE2   . TYR B 2 339 ? 122.688 123.859 140.863 1.00 28.72  ? 339 TYR B CE2   1 
ATOM   6832 C  CZ    . TYR B 2 339 ? 121.923 124.602 139.998 1.00 35.68  ? 339 TYR B CZ    1 
ATOM   6833 O  OH    . TYR B 2 339 ? 121.473 125.842 140.371 1.00 42.95  ? 339 TYR B OH    1 
ATOM   6834 N  N     . VAL B 2 340 ? 123.015 117.656 137.816 1.00 29.64  ? 340 VAL B N     1 
ATOM   6835 C  CA    . VAL B 2 340 ? 123.546 116.499 137.102 1.00 27.75  ? 340 VAL B CA    1 
ATOM   6836 C  C     . VAL B 2 340 ? 122.653 116.157 135.918 1.00 31.56  ? 340 VAL B C     1 
ATOM   6837 O  O     . VAL B 2 340 ? 123.137 115.869 134.815 1.00 32.99  ? 340 VAL B O     1 
ATOM   6838 C  CB    . VAL B 2 340 ? 123.708 115.306 138.062 1.00 29.12  ? 340 VAL B CB    1 
ATOM   6839 C  CG1   . VAL B 2 340 ? 123.869 114.012 137.288 1.00 35.97  ? 340 VAL B CG1   1 
ATOM   6840 C  CG2   . VAL B 2 340 ? 124.894 115.524 138.974 1.00 26.26  ? 340 VAL B CG2   1 
ATOM   6841 N  N     . ARG B 2 341 ? 121.333 116.191 136.122 1.00 30.91  ? 341 ARG B N     1 
ATOM   6842 C  CA    . ARG B 2 341 ? 120.421 115.949 135.006 1.00 26.03  ? 341 ARG B CA    1 
ATOM   6843 C  C     . ARG B 2 341 ? 120.565 117.019 133.926 1.00 31.88  ? 341 ARG B C     1 
ATOM   6844 O  O     . ARG B 2 341 ? 120.610 116.704 132.730 1.00 40.08  ? 341 ARG B O     1 
ATOM   6845 C  CB    . ARG B 2 341 ? 118.980 115.879 135.507 1.00 32.43  ? 341 ARG B CB    1 
ATOM   6846 C  CG    . ARG B 2 341 ? 117.957 115.648 134.405 1.00 41.28  ? 341 ARG B CG    1 
ATOM   6847 C  CD    . ARG B 2 341 ? 116.657 115.065 134.942 1.00 37.70  ? 341 ARG B CD    1 
ATOM   6848 N  NE    . ARG B 2 341 ? 116.601 113.616 134.806 1.00 32.37  ? 341 ARG B NE    1 
ATOM   6849 C  CZ    . ARG B 2 341 ? 116.831 112.760 135.792 1.00 34.59  ? 341 ARG B CZ    1 
ATOM   6850 N  NH1   . ARG B 2 341 ? 117.132 113.174 137.011 1.00 33.55  ? 341 ARG B NH1   1 
ATOM   6851 N  NH2   . ARG B 2 341 ? 116.755 111.456 135.549 1.00 36.56  ? 341 ARG B NH2   1 
ATOM   6852 N  N     . GLN B 2 342 ? 120.646 118.291 134.328 1.00 33.81  ? 342 GLN B N     1 
ATOM   6853 C  CA    . GLN B 2 342 ? 120.778 119.394 133.379 1.00 32.77  ? 342 GLN B CA    1 
ATOM   6854 C  C     . GLN B 2 342 ? 122.158 119.473 132.741 1.00 36.04  ? 342 GLN B C     1 
ATOM   6855 O  O     . GLN B 2 342 ? 122.335 120.234 131.786 1.00 42.07  ? 342 GLN B O     1 
ATOM   6856 C  CB    . GLN B 2 342 ? 120.467 120.722 134.067 1.00 32.20  ? 342 GLN B CB    1 
ATOM   6857 C  CG    . GLN B 2 342 ? 119.020 120.885 134.474 1.00 41.23  ? 342 GLN B CG    1 
ATOM   6858 C  CD    . GLN B 2 342 ? 118.771 122.178 135.218 1.00 45.37  ? 342 GLN B CD    1 
ATOM   6859 O  OE1   . GLN B 2 342 ? 119.630 123.057 135.261 1.00 46.84  ? 342 GLN B OE1   1 
ATOM   6860 N  NE2   . GLN B 2 342 ? 117.590 122.301 135.809 1.00 42.10  ? 342 GLN B NE2   1 
ATOM   6861 N  N     . PHE B 2 343 ? 123.139 118.751 133.270 1.00 35.73  ? 343 PHE B N     1 
ATOM   6862 C  CA    . PHE B 2 343 ? 124.456 118.623 132.664 1.00 34.32  ? 343 PHE B CA    1 
ATOM   6863 C  C     . PHE B 2 343 ? 124.502 117.466 131.681 1.00 36.53  ? 343 PHE B C     1 
ATOM   6864 O  O     . PHE B 2 343 ? 125.150 117.564 130.634 1.00 38.79  ? 343 PHE B O     1 
ATOM   6865 C  CB    . PHE B 2 343 ? 125.511 118.423 133.755 1.00 34.50  ? 343 PHE B CB    1 
ATOM   6866 C  CG    . PHE B 2 343 ? 126.921 118.357 133.244 1.00 34.74  ? 343 PHE B CG    1 
ATOM   6867 C  CD1   . PHE B 2 343 ? 127.680 119.505 133.124 1.00 41.27  ? 343 PHE B CD1   1 
ATOM   6868 C  CD2   . PHE B 2 343 ? 127.495 117.146 132.908 1.00 37.57  ? 343 PHE B CD2   1 
ATOM   6869 C  CE1   . PHE B 2 343 ? 128.977 119.446 132.664 1.00 44.58  ? 343 PHE B CE1   1 
ATOM   6870 C  CE2   . PHE B 2 343 ? 128.790 117.082 132.445 1.00 39.91  ? 343 PHE B CE2   1 
ATOM   6871 C  CZ    . PHE B 2 343 ? 129.532 118.233 132.324 1.00 47.05  ? 343 PHE B CZ    1 
ATOM   6872 N  N     . ASN B 2 344 ? 123.821 116.368 132.006 1.00 35.55  ? 344 ASN B N     1 
ATOM   6873 C  CA    . ASN B 2 344 ? 123.794 115.220 131.112 1.00 34.25  ? 344 ASN B CA    1 
ATOM   6874 C  C     . ASN B 2 344 ? 122.880 115.444 129.917 1.00 38.86  ? 344 ASN B C     1 
ATOM   6875 O  O     . ASN B 2 344 ? 123.142 114.898 128.841 1.00 48.38  ? 344 ASN B O     1 
ATOM   6876 C  CB    . ASN B 2 344 ? 123.364 113.970 131.878 1.00 35.64  ? 344 ASN B CB    1 
ATOM   6877 C  CG    . ASN B 2 344 ? 124.459 113.435 132.778 1.00 45.17  ? 344 ASN B CG    1 
ATOM   6878 O  OD1   . ASN B 2 344 ? 125.615 113.839 132.674 1.00 41.57  ? 344 ASN B OD1   1 
ATOM   6879 N  ND2   . ASN B 2 344 ? 124.097 112.522 133.671 1.00 45.29  ? 344 ASN B ND2   1 
ATOM   6880 N  N     . GLN B 2 345 ? 121.810 116.225 130.078 1.00 36.50  ? 345 GLN B N     1 
ATOM   6881 C  CA    . GLN B 2 345 ? 120.872 116.425 128.972 1.00 41.90  ? 345 GLN B CA    1 
ATOM   6882 C  C     . GLN B 2 345 ? 121.504 117.069 127.743 1.00 41.96  ? 345 GLN B C     1 
ATOM   6883 O  O     . GLN B 2 345 ? 121.236 116.595 126.625 1.00 47.43  ? 345 GLN B O     1 
ATOM   6884 C  CB    . GLN B 2 345 ? 119.663 117.229 129.460 1.00 43.08  ? 345 GLN B CB    1 
ATOM   6885 C  CG    . GLN B 2 345 ? 118.593 116.387 130.125 1.00 51.68  ? 345 GLN B CG    1 
ATOM   6886 C  CD    . GLN B 2 345 ? 117.389 117.202 130.546 1.00 63.91  ? 345 GLN B CD    1 
ATOM   6887 O  OE1   . GLN B 2 345 ? 117.419 118.432 130.523 1.00 58.95  ? 345 GLN B OE1   1 
ATOM   6888 N  NE2   . GLN B 2 345 ? 116.319 116.519 130.936 1.00 60.63  ? 345 GLN B NE2   1 
ATOM   6889 N  N     . PRO B 2 346 ? 122.297 118.145 127.850 1.00 43.19  ? 346 PRO B N     1 
ATOM   6890 C  CA    . PRO B 2 346 ? 122.899 118.719 126.634 1.00 43.75  ? 346 PRO B CA    1 
ATOM   6891 C  C     . PRO B 2 346 ? 123.768 117.749 125.854 1.00 41.95  ? 346 PRO B C     1 
ATOM   6892 O  O     . PRO B 2 346 ? 123.720 117.734 124.616 1.00 48.18  ? 346 PRO B O     1 
ATOM   6893 C  CB    . PRO B 2 346 ? 123.720 119.891 127.187 1.00 43.34  ? 346 PRO B CB    1 
ATOM   6894 C  CG    . PRO B 2 346 ? 123.028 120.269 128.426 1.00 40.67  ? 346 PRO B CG    1 
ATOM   6895 C  CD    . PRO B 2 346 ? 122.588 118.979 129.027 1.00 43.00  ? 346 PRO B CD    1 
ATOM   6896 N  N     . LEU B 2 347 ? 124.562 116.932 126.547 1.00 37.32  ? 347 LEU B N     1 
ATOM   6897 C  CA    . LEU B 2 347 ? 125.404 115.961 125.858 1.00 38.65  ? 347 LEU B CA    1 
ATOM   6898 C  C     . LEU B 2 347 ? 124.561 114.942 125.103 1.00 40.26  ? 347 LEU B C     1 
ATOM   6899 O  O     . LEU B 2 347 ? 124.865 114.601 123.955 1.00 45.17  ? 347 LEU B O     1 
ATOM   6900 C  CB    . LEU B 2 347 ? 126.323 115.266 126.860 1.00 39.32  ? 347 LEU B CB    1 
ATOM   6901 C  CG    . LEU B 2 347 ? 127.146 116.181 127.768 1.00 39.69  ? 347 LEU B CG    1 
ATOM   6902 C  CD1   . LEU B 2 347 ? 127.898 115.365 128.800 1.00 36.09  ? 347 LEU B CD1   1 
ATOM   6903 C  CD2   . LEU B 2 347 ? 128.106 117.022 126.949 1.00 38.02  ? 347 LEU B CD2   1 
ATOM   6904 N  N     . THR B 2 348 ? 123.492 114.453 125.732 1.00 39.61  ? 348 THR B N     1 
ATOM   6905 C  CA    . THR B 2 348 ? 122.621 113.485 125.076 1.00 40.36  ? 348 THR B CA    1 
ATOM   6906 C  C     . THR B 2 348 ? 121.901 114.104 123.884 1.00 43.65  ? 348 THR B C     1 
ATOM   6907 O  O     . THR B 2 348 ? 121.717 113.445 122.856 1.00 46.46  ? 348 THR B O     1 
ATOM   6908 C  CB    . THR B 2 348 ? 121.620 112.915 126.080 1.00 40.68  ? 348 THR B CB    1 
ATOM   6909 O  OG1   . THR B 2 348 ? 122.315 112.503 127.262 1.00 37.50  ? 348 THR B OG1   1 
ATOM   6910 C  CG2   . THR B 2 348 ? 120.905 111.715 125.493 1.00 43.33  ? 348 THR B CG2   1 
ATOM   6911 N  N     . GLN B 2 349 ? 121.487 115.368 124.000 1.00 42.06  ? 349 GLN B N     1 
ATOM   6912 C  CA    . GLN B 2 349 ? 120.841 116.042 122.877 1.00 41.79  ? 349 GLN B CA    1 
ATOM   6913 C  C     . GLN B 2 349 ? 121.799 116.192 121.700 1.00 45.10  ? 349 GLN B C     1 
ATOM   6914 O  O     . GLN B 2 349 ? 121.437 115.924 120.546 1.00 49.55  ? 349 GLN B O     1 
ATOM   6915 C  CB    . GLN B 2 349 ? 120.322 117.409 123.319 1.00 43.67  ? 349 GLN B CB    1 
ATOM   6916 C  CG    . GLN B 2 349 ? 118.909 117.392 123.861 1.00 54.30  ? 349 GLN B CG    1 
ATOM   6917 C  CD    . GLN B 2 349 ? 118.296 118.775 123.909 1.00 69.23  ? 349 GLN B CD    1 
ATOM   6918 O  OE1   . GLN B 2 349 ? 118.683 119.665 123.152 1.00 68.56  ? 349 GLN B OE1   1 
ATOM   6919 N  NE2   . GLN B 2 349 ? 117.335 118.966 124.804 1.00 70.17  ? 349 GLN B NE2   1 
ATOM   6920 N  N     . VAL B 2 350 ? 123.034 116.616 121.979 1.00 40.73  ? 350 VAL B N     1 
ATOM   6921 C  CA    . VAL B 2 350 ? 124.029 116.760 120.921 1.00 40.76  ? 350 VAL B CA    1 
ATOM   6922 C  C     . VAL B 2 350 ? 124.317 115.412 120.275 1.00 45.92  ? 350 VAL B C     1 
ATOM   6923 O  O     . VAL B 2 350 ? 124.422 115.304 119.047 1.00 52.23  ? 350 VAL B O     1 
ATOM   6924 C  CB    . VAL B 2 350 ? 125.308 117.411 121.477 1.00 41.75  ? 350 VAL B CB    1 
ATOM   6925 C  CG1   . VAL B 2 350 ? 126.438 117.321 120.467 1.00 44.14  ? 350 VAL B CG1   1 
ATOM   6926 C  CG2   . VAL B 2 350 ? 125.043 118.859 121.845 1.00 40.34  ? 350 VAL B CG2   1 
ATOM   6927 N  N     . ALA B 2 351 ? 124.441 114.362 121.087 1.00 42.55  ? 351 ALA B N     1 
ATOM   6928 C  CA    . ALA B 2 351 ? 124.686 113.033 120.541 1.00 39.82  ? 351 ALA B CA    1 
ATOM   6929 C  C     . ALA B 2 351 ? 123.524 112.564 119.673 1.00 43.90  ? 351 ALA B C     1 
ATOM   6930 O  O     . ALA B 2 351 ? 123.734 111.946 118.624 1.00 50.37  ? 351 ALA B O     1 
ATOM   6931 C  CB    . ALA B 2 351 ? 124.944 112.048 121.678 1.00 39.43  ? 351 ALA B CB    1 
ATOM   6932 N  N     . GLY B 2 352 ? 122.290 112.842 120.097 1.00 44.48  ? 352 GLY B N     1 
ATOM   6933 C  CA    . GLY B 2 352 ? 121.138 112.430 119.313 1.00 49.32  ? 352 GLY B CA    1 
ATOM   6934 C  C     . GLY B 2 352 ? 121.032 113.160 117.989 1.00 53.35  ? 352 GLY B C     1 
ATOM   6935 O  O     . GLY B 2 352 ? 120.617 112.581 116.982 1.00 58.57  ? 352 GLY B O     1 
ATOM   6936 N  N     . MET B 2 353 ? 121.395 114.438 117.970 1.00 50.00  ? 353 MET B N     1 
ATOM   6937 C  CA    . MET B 2 353 ? 121.349 115.234 116.749 1.00 52.34  ? 353 MET B CA    1 
ATOM   6938 C  C     . MET B 2 353 ? 122.659 115.199 115.961 1.00 47.78  ? 353 MET B C     1 
ATOM   6939 O  O     . MET B 2 353 ? 122.789 115.910 114.955 1.00 49.86  ? 353 MET B O     1 
ATOM   6940 C  CB    . MET B 2 353 ? 120.929 116.665 117.100 1.00 51.05  ? 353 MET B CB    1 
ATOM   6941 C  CG    . MET B 2 353 ? 122.047 117.643 117.362 1.00 53.15  ? 353 MET B CG    1 
ATOM   6942 S  SD    . MET B 2 353 ? 121.383 119.072 118.232 1.00 53.47  ? 353 MET B SD    1 
ATOM   6943 C  CE    . MET B 2 353 ? 122.884 119.803 118.858 1.00 49.76  ? 353 MET B CE    1 
ATOM   6944 N  N     . TYR B 2 354 ? 123.622 114.385 116.403 1.00 45.72  ? 354 TYR B N     1 
ATOM   6945 C  CA    . TYR B 2 354 ? 124.855 114.171 115.648 1.00 46.69  ? 354 TYR B CA    1 
ATOM   6946 C  C     . TYR B 2 354 ? 124.598 113.725 114.212 1.00 47.95  ? 354 TYR B C     1 
ATOM   6947 O  O     . TYR B 2 354 ? 125.319 114.134 113.300 1.00 48.89  ? 354 TYR B O     1 
ATOM   6948 C  CB    . TYR B 2 354 ? 125.727 113.144 116.374 1.00 45.41  ? 354 TYR B CB    1 
ATOM   6949 C  CG    . TYR B 2 354 ? 126.761 112.458 115.506 1.00 48.66  ? 354 TYR B CG    1 
ATOM   6950 C  CD1   . TYR B 2 354 ? 127.791 113.172 114.908 1.00 47.88  ? 354 TYR B CD1   1 
ATOM   6951 C  CD2   . TYR B 2 354 ? 126.707 111.089 115.291 1.00 47.04  ? 354 TYR B CD2   1 
ATOM   6952 C  CE1   . TYR B 2 354 ? 128.732 112.538 114.116 1.00 51.52  ? 354 TYR B CE1   1 
ATOM   6953 C  CE2   . TYR B 2 354 ? 127.641 110.451 114.504 1.00 43.80  ? 354 TYR B CE2   1 
ATOM   6954 C  CZ    . TYR B 2 354 ? 128.650 111.177 113.920 1.00 48.75  ? 354 TYR B CZ    1 
ATOM   6955 O  OH    . TYR B 2 354 ? 129.578 110.534 113.137 1.00 56.43  ? 354 TYR B OH    1 
ATOM   6956 N  N     . ASN B 2 355 ? 123.600 112.868 113.986 1.00 49.60  ? 355 ASN B N     1 
ATOM   6957 C  CA    . ASN B 2 355 ? 123.342 112.393 112.626 1.00 45.66  ? 355 ASN B CA    1 
ATOM   6958 C  C     . ASN B 2 355 ? 122.875 113.531 111.720 1.00 43.77  ? 355 ASN B C     1 
ATOM   6959 O  O     . ASN B 2 355 ? 123.328 113.650 110.573 1.00 45.10  ? 355 ASN B O     1 
ATOM   6960 C  CB    . ASN B 2 355 ? 122.308 111.268 112.655 1.00 52.08  ? 355 ASN B CB    1 
ATOM   6961 C  CG    . ASN B 2 355 ? 122.111 110.607 111.299 1.00 54.90  ? 355 ASN B CG    1 
ATOM   6962 O  OD1   . ASN B 2 355 ? 121.237 109.759 111.140 1.00 56.02  ? 355 ASN B OD1   1 
ATOM   6963 N  ND2   . ASN B 2 355 ? 122.943 110.966 110.329 1.00 54.22  ? 355 ASN B ND2   1 
ATOM   6964 N  N     . THR B 2 356 ? 121.966 114.371 112.218 1.00 44.93  ? 356 THR B N     1 
ATOM   6965 C  CA    . THR B 2 356 ? 121.530 115.530 111.452 1.00 40.86  ? 356 THR B CA    1 
ATOM   6966 C  C     . THR B 2 356 ? 122.690 116.482 111.200 1.00 37.51  ? 356 THR B C     1 
ATOM   6967 O  O     . THR B 2 356 ? 122.841 117.011 110.092 1.00 39.61  ? 356 THR B O     1 
ATOM   6968 C  CB    . THR B 2 356 ? 120.397 116.246 112.189 1.00 43.87  ? 356 THR B CB    1 
ATOM   6969 O  OG1   . THR B 2 356 ? 119.289 115.352 112.351 1.00 45.00  ? 356 THR B OG1   1 
ATOM   6970 C  CG2   . THR B 2 356 ? 119.943 117.472 111.420 1.00 39.32  ? 356 THR B CG2   1 
ATOM   6971 N  N     . LEU B 2 357 ? 123.528 116.702 112.217 1.00 37.90  ? 357 LEU B N     1 
ATOM   6972 C  CA    . LEU B 2 357 ? 124.697 117.559 112.042 1.00 39.31  ? 357 LEU B CA    1 
ATOM   6973 C  C     . LEU B 2 357 ? 125.638 116.999 110.987 1.00 39.94  ? 357 LEU B C     1 
ATOM   6974 O  O     . LEU B 2 357 ? 126.207 117.747 110.188 1.00 40.82  ? 357 LEU B O     1 
ATOM   6975 C  CB    . LEU B 2 357 ? 125.439 117.715 113.366 1.00 38.66  ? 357 LEU B CB    1 
ATOM   6976 C  CG    . LEU B 2 357 ? 124.778 118.539 114.463 1.00 45.38  ? 357 LEU B CG    1 
ATOM   6977 C  CD1   . LEU B 2 357 ? 125.501 118.306 115.776 1.00 46.35  ? 357 LEU B CD1   1 
ATOM   6978 C  CD2   . LEU B 2 357 ? 124.790 120.003 114.086 1.00 44.52  ? 357 LEU B CD2   1 
ATOM   6979 N  N     . GLN B 2 358 ? 125.820 115.682 110.984 1.00 39.64  ? 358 GLN B N     1 
ATOM   6980 C  CA    . GLN B 2 358 ? 126.736 115.037 110.055 1.00 38.57  ? 358 GLN B CA    1 
ATOM   6981 C  C     . GLN B 2 358 ? 126.230 115.154 108.624 1.00 38.03  ? 358 GLN B C     1 
ATOM   6982 O  O     . GLN B 2 358 ? 126.998 115.468 107.704 1.00 39.60  ? 358 GLN B O     1 
ATOM   6983 C  CB    . GLN B 2 358 ? 126.901 113.577 110.483 1.00 43.08  ? 358 GLN B CB    1 
ATOM   6984 C  CG    . GLN B 2 358 ? 127.326 112.605 109.424 1.00 44.01  ? 358 GLN B CG    1 
ATOM   6985 C  CD    . GLN B 2 358 ? 128.818 112.647 109.199 1.00 54.26  ? 358 GLN B CD    1 
ATOM   6986 O  OE1   . GLN B 2 358 ? 129.565 113.149 110.028 1.00 52.40  ? 358 GLN B OE1   1 
ATOM   6987 N  NE2   . GLN B 2 358 ? 129.259 112.106 108.072 1.00 54.02  ? 358 GLN B NE2   1 
ATOM   6988 N  N     . SER B 2 359 ? 124.928 114.935 108.425 1.00 38.26  ? 359 SER B N     1 
ATOM   6989 C  CA    . SER B 2 359 ? 124.337 115.139 107.106 1.00 35.24  ? 359 SER B CA    1 
ATOM   6990 C  C     . SER B 2 359 ? 124.465 116.592 106.654 1.00 36.09  ? 359 SER B C     1 
ATOM   6991 O  O     . SER B 2 359 ? 124.811 116.864 105.496 1.00 43.74  ? 359 SER B O     1 
ATOM   6992 C  CB    . SER B 2 359 ? 122.871 114.715 107.123 1.00 36.36  ? 359 SER B CB    1 
ATOM   6993 O  OG    . SER B 2 359 ? 122.332 114.694 105.815 1.00 38.97  ? 359 SER B OG    1 
ATOM   6994 N  N     . GLY B 2 360 ? 124.193 117.538 107.554 1.00 33.17  ? 360 GLY B N     1 
ATOM   6995 C  CA    . GLY B 2 360 ? 124.308 118.940 107.193 1.00 30.56  ? 360 GLY B CA    1 
ATOM   6996 C  C     . GLY B 2 360 ? 125.728 119.345 106.854 1.00 35.87  ? 360 GLY B C     1 
ATOM   6997 O  O     . GLY B 2 360 ? 125.953 120.152 105.950 1.00 34.43  ? 360 GLY B O     1 
ATOM   6998 N  N     . ILE B 2 361 ? 126.706 118.794 107.573 1.00 39.90  ? 361 ILE B N     1 
ATOM   6999 C  CA    . ILE B 2 361 ? 128.105 119.105 107.300 1.00 34.11  ? 361 ILE B CA    1 
ATOM   7000 C  C     . ILE B 2 361 ? 128.535 118.510 105.965 1.00 36.73  ? 361 ILE B C     1 
ATOM   7001 O  O     . ILE B 2 361 ? 129.301 119.127 105.218 1.00 45.40  ? 361 ILE B O     1 
ATOM   7002 C  CB    . ILE B 2 361 ? 128.993 118.626 108.462 1.00 39.02  ? 361 ILE B CB    1 
ATOM   7003 C  CG1   . ILE B 2 361 ? 128.863 119.581 109.650 1.00 38.59  ? 361 ILE B CG1   1 
ATOM   7004 C  CG2   . ILE B 2 361 ? 130.445 118.533 108.035 1.00 46.05  ? 361 ILE B CG2   1 
ATOM   7005 C  CD1   . ILE B 2 361 ? 129.307 118.985 110.965 1.00 38.55  ? 361 ILE B CD1   1 
ATOM   7006 N  N     . ALA B 2 362 ? 128.050 117.310 105.635 1.00 35.85  ? 362 ALA B N     1 
ATOM   7007 C  CA    . ALA B 2 362 ? 128.333 116.755 104.313 1.00 35.97  ? 362 ALA B CA    1 
ATOM   7008 C  C     . ALA B 2 362 ? 127.744 117.626 103.207 1.00 39.71  ? 362 ALA B C     1 
ATOM   7009 O  O     . ALA B 2 362 ? 128.402 117.893 102.190 1.00 41.93  ? 362 ALA B O     1 
ATOM   7010 C  CB    . ALA B 2 362 ? 127.794 115.329 104.217 1.00 39.02  ? 362 ALA B CB    1 
ATOM   7011 N  N     . SER B 2 363 ? 126.502 118.084 103.392 1.00 38.83  ? 363 SER B N     1 
ATOM   7012 C  CA    . SER B 2 363 ? 125.887 118.963 102.402 1.00 30.81  ? 363 SER B CA    1 
ATOM   7013 C  C     . SER B 2 363 ? 126.654 120.272 102.275 1.00 32.53  ? 363 SER B C     1 
ATOM   7014 O  O     . SER B 2 363 ? 126.824 120.796 101.169 1.00 39.06  ? 363 SER B O     1 
ATOM   7015 C  CB    . SER B 2 363 ? 124.428 119.228 102.765 1.00 32.60  ? 363 SER B CB    1 
ATOM   7016 O  OG    . SER B 2 363 ? 123.674 118.032 102.759 1.00 41.38  ? 363 SER B OG    1 
ATOM   7017 N  N     . ALA B 2 364 ? 127.116 120.820 103.401 1.00 33.96  ? 364 ALA B N     1 
ATOM   7018 C  CA    . ALA B 2 364 ? 127.912 122.042 103.362 1.00 34.06  ? 364 ALA B CA    1 
ATOM   7019 C  C     . ALA B 2 364 ? 129.233 121.814 102.642 1.00 37.18  ? 364 ALA B C     1 
ATOM   7020 O  O     . ALA B 2 364 ? 129.709 122.690 101.914 1.00 40.17  ? 364 ALA B O     1 
ATOM   7021 C  CB    . ALA B 2 364 ? 128.153 122.556 104.780 1.00 34.11  ? 364 ALA B CB    1 
ATOM   7022 N  N     . GLU B 2 365 ? 129.840 120.643 102.836 1.00 42.50  ? 365 GLU B N     1 
ATOM   7023 C  CA    . GLU B 2 365 ? 131.062 120.303 102.116 1.00 43.82  ? 365 GLU B CA    1 
ATOM   7024 C  C     . GLU B 2 365 ? 130.822 120.296 100.614 1.00 42.18  ? 365 GLU B C     1 
ATOM   7025 O  O     . GLU B 2 365 ? 131.609 120.855 99.845  1.00 46.22  ? 365 GLU B O     1 
ATOM   7026 C  CB    . GLU B 2 365 ? 131.579 118.942 102.586 1.00 49.10  ? 365 GLU B CB    1 
ATOM   7027 C  CG    . GLU B 2 365 ? 133.087 118.746 102.490 1.00 60.21  ? 365 GLU B CG    1 
ATOM   7028 C  CD    . GLU B 2 365 ? 133.611 118.819 101.068 1.00 73.68  ? 365 GLU B CD    1 
ATOM   7029 O  OE1   . GLU B 2 365 ? 133.507 117.807 100.342 1.00 80.45  ? 365 GLU B OE1   1 
ATOM   7030 O  OE2   . GLU B 2 365 ? 134.130 119.885 100.677 1.00 70.78  ? 365 GLU B OE2   1 
ATOM   7031 N  N     . ARG B 2 366 ? 129.725 119.675 100.178 1.00 43.90  ? 366 ARG B N     1 
ATOM   7032 C  CA    . ARG B 2 366 ? 129.433 119.637 98.745  1.00 40.02  ? 366 ARG B CA    1 
ATOM   7033 C  C     . ARG B 2 366 ? 129.145 121.031 98.192  1.00 40.01  ? 366 ARG B C     1 
ATOM   7034 O  O     . ARG B 2 366 ? 129.621 121.389 97.105  1.00 46.89  ? 366 ARG B O     1 
ATOM   7035 C  CB    . ARG B 2 366 ? 128.266 118.693 98.473  1.00 36.51  ? 366 ARG B CB    1 
ATOM   7036 C  CG    . ARG B 2 366 ? 128.645 117.230 98.558  1.00 34.52  ? 366 ARG B CG    1 
ATOM   7037 C  CD    . ARG B 2 366 ? 127.507 116.335 98.123  1.00 38.59  ? 366 ARG B CD    1 
ATOM   7038 N  NE    . ARG B 2 366 ? 126.356 116.448 99.008  1.00 47.56  ? 366 ARG B NE    1 
ATOM   7039 C  CZ    . ARG B 2 366 ? 126.141 115.673 100.061 1.00 46.06  ? 366 ARG B CZ    1 
ATOM   7040 N  NH1   . ARG B 2 366 ? 126.993 114.722 100.404 1.00 44.71  ? 366 ARG B NH1   1 
ATOM   7041 N  NH2   . ARG B 2 366 ? 125.044 115.857 100.788 1.00 46.08  ? 366 ARG B NH2   1 
ATOM   7042 N  N     . VAL B 2 367 ? 128.376 121.836 98.927  1.00 39.33  ? 367 VAL B N     1 
ATOM   7043 C  CA    . VAL B 2 367 ? 128.046 123.178 98.456  1.00 36.19  ? 367 VAL B CA    1 
ATOM   7044 C  C     . VAL B 2 367 ? 129.296 124.044 98.375  1.00 38.24  ? 367 VAL B C     1 
ATOM   7045 O  O     . VAL B 2 367 ? 129.482 124.794 97.410  1.00 43.75  ? 367 VAL B O     1 
ATOM   7046 C  CB    . VAL B 2 367 ? 126.969 123.812 99.354  1.00 38.82  ? 367 VAL B CB    1 
ATOM   7047 C  CG1   . VAL B 2 367 ? 126.843 125.299 99.070  1.00 37.77  ? 367 VAL B CG1   1 
ATOM   7048 C  CG2   . VAL B 2 367 ? 125.642 123.126 99.137  1.00 36.84  ? 367 VAL B CG2   1 
ATOM   7049 N  N     . PHE B 2 368 ? 130.172 123.966 99.379  1.00 36.87  ? 368 PHE B N     1 
ATOM   7050 C  CA    . PHE B 2 368 ? 131.399 124.751 99.342  1.00 39.22  ? 368 PHE B CA    1 
ATOM   7051 C  C     . PHE B 2 368 ? 132.355 124.246 98.273  1.00 41.06  ? 368 PHE B C     1 
ATOM   7052 O  O     . PHE B 2 368 ? 133.121 125.035 97.711  1.00 44.63  ? 368 PHE B O     1 
ATOM   7053 C  CB    . PHE B 2 368 ? 132.075 124.746 100.712 1.00 41.19  ? 368 PHE B CB    1 
ATOM   7054 C  CG    . PHE B 2 368 ? 131.304 125.483 101.769 1.00 42.24  ? 368 PHE B CG    1 
ATOM   7055 C  CD1   . PHE B 2 368 ? 130.529 126.579 101.440 1.00 41.79  ? 368 PHE B CD1   1 
ATOM   7056 C  CD2   . PHE B 2 368 ? 131.352 125.078 103.090 1.00 45.47  ? 368 PHE B CD2   1 
ATOM   7057 C  CE1   . PHE B 2 368 ? 129.817 127.255 102.407 1.00 42.26  ? 368 PHE B CE1   1 
ATOM   7058 C  CE2   . PHE B 2 368 ? 130.641 125.750 104.059 1.00 43.19  ? 368 PHE B CE2   1 
ATOM   7059 C  CZ    . PHE B 2 368 ? 129.874 126.839 103.717 1.00 39.79  ? 368 PHE B CZ    1 
ATOM   7060 N  N     . ASP B 2 369 ? 132.332 122.945 97.978  1.00 44.96  ? 369 ASP B N     1 
ATOM   7061 C  CA    . ASP B 2 369 ? 133.103 122.441 96.849  1.00 43.51  ? 369 ASP B CA    1 
ATOM   7062 C  C     . ASP B 2 369 ? 132.615 123.051 95.545  1.00 45.07  ? 369 ASP B C     1 
ATOM   7063 O  O     . ASP B 2 369 ? 133.421 123.447 94.696  1.00 47.12  ? 369 ASP B O     1 
ATOM   7064 C  CB    . ASP B 2 369 ? 133.015 120.917 96.792  1.00 46.62  ? 369 ASP B CB    1 
ATOM   7065 C  CG    . ASP B 2 369 ? 133.729 120.339 95.589  1.00 64.37  ? 369 ASP B CG    1 
ATOM   7066 O  OD1   . ASP B 2 369 ? 134.791 120.876 95.211  1.00 72.39  ? 369 ASP B OD1   1 
ATOM   7067 O  OD2   . ASP B 2 369 ? 133.225 119.350 95.015  1.00 65.62  ? 369 ASP B OD2   1 
ATOM   7068 N  N     . LEU B 2 370 ? 131.294 123.133 95.368  1.00 43.63  ? 370 LEU B N     1 
ATOM   7069 C  CA    . LEU B 2 370 ? 130.755 123.784 94.177  1.00 39.80  ? 370 LEU B CA    1 
ATOM   7070 C  C     . LEU B 2 370 ? 131.124 125.262 94.140  1.00 39.16  ? 370 LEU B C     1 
ATOM   7071 O  O     . LEU B 2 370 ? 131.449 125.802 93.077  1.00 41.49  ? 370 LEU B O     1 
ATOM   7072 C  CB    . LEU B 2 370 ? 129.239 123.606 94.116  1.00 44.77  ? 370 LEU B CB    1 
ATOM   7073 C  CG    . LEU B 2 370 ? 128.528 124.237 92.917  1.00 42.15  ? 370 LEU B CG    1 
ATOM   7074 C  CD1   . LEU B 2 370 ? 127.639 123.222 92.228  1.00 42.39  ? 370 LEU B CD1   1 
ATOM   7075 C  CD2   . LEU B 2 370 ? 127.710 125.441 93.349  1.00 42.67  ? 370 LEU B CD2   1 
ATOM   7076 N  N     . LEU B 2 371 ? 131.077 125.932 95.291  1.00 39.38  ? 371 LEU B N     1 
ATOM   7077 C  CA    . LEU B 2 371 ? 131.373 127.359 95.353  1.00 38.02  ? 371 LEU B CA    1 
ATOM   7078 C  C     . LEU B 2 371 ? 132.856 127.662 95.181  1.00 41.84  ? 371 LEU B C     1 
ATOM   7079 O  O     . LEU B 2 371 ? 133.207 128.798 94.848  1.00 42.58  ? 371 LEU B O     1 
ATOM   7080 C  CB    . LEU B 2 371 ? 130.879 127.940 96.677  1.00 38.87  ? 371 LEU B CB    1 
ATOM   7081 C  CG    . LEU B 2 371 ? 129.363 128.022 96.859  1.00 39.23  ? 371 LEU B CG    1 
ATOM   7082 C  CD1   . LEU B 2 371 ? 129.020 128.602 98.218  1.00 39.15  ? 371 LEU B CD1   1 
ATOM   7083 C  CD2   . LEU B 2 371 ? 128.738 128.846 95.750  1.00 39.84  ? 371 LEU B CD2   1 
ATOM   7084 N  N     . ASP B 2 372 ? 133.731 126.685 95.407  1.00 44.68  ? 372 ASP B N     1 
ATOM   7085 C  CA    . ASP B 2 372 ? 135.167 126.879 95.256  1.00 43.93  ? 372 ASP B CA    1 
ATOM   7086 C  C     . ASP B 2 372 ? 135.682 126.497 93.875  1.00 45.43  ? 372 ASP B C     1 
ATOM   7087 O  O     . ASP B 2 372 ? 136.889 126.588 93.636  1.00 48.33  ? 372 ASP B O     1 
ATOM   7088 C  CB    . ASP B 2 372 ? 135.922 126.078 96.319  1.00 48.91  ? 372 ASP B CB    1 
ATOM   7089 C  CG    . ASP B 2 372 ? 135.710 126.621 97.715  1.00 55.61  ? 372 ASP B CG    1 
ATOM   7090 O  OD1   . ASP B 2 372 ? 135.189 127.749 97.841  1.00 54.19  ? 372 ASP B OD1   1 
ATOM   7091 O  OD2   . ASP B 2 372 ? 136.062 125.919 98.686  1.00 56.08  ? 372 ASP B OD2   1 
ATOM   7092 N  N     . THR B 2 373 ? 134.805 126.067 92.970  1.00 43.37  ? 373 THR B N     1 
ATOM   7093 C  CA    . THR B 2 373 ? 135.228 125.712 91.622  1.00 42.63  ? 373 THR B CA    1 
ATOM   7094 C  C     . THR B 2 373 ? 135.749 126.941 90.886  1.00 48.10  ? 373 THR B C     1 
ATOM   7095 O  O     . THR B 2 373 ? 135.276 128.060 91.097  1.00 50.64  ? 373 THR B O     1 
ATOM   7096 C  CB    . THR B 2 373 ? 134.061 125.089 90.853  1.00 39.94  ? 373 THR B CB    1 
ATOM   7097 O  OG1   . THR B 2 373 ? 133.453 124.068 91.651  1.00 42.76  ? 373 THR B OG1   1 
ATOM   7098 C  CG2   . THR B 2 373 ? 134.539 124.475 89.552  1.00 34.54  ? 373 THR B CG2   1 
ATOM   7099 N  N     . GLU B 2 374 ? 136.748 126.730 90.031  1.00 49.26  ? 374 GLU B N     1 
ATOM   7100 C  CA    . GLU B 2 374 ? 137.271 127.817 89.214  1.00 54.16  ? 374 GLU B CA    1 
ATOM   7101 C  C     . GLU B 2 374 ? 136.214 128.294 88.226  1.00 55.81  ? 374 GLU B C     1 
ATOM   7102 O  O     . GLU B 2 374 ? 135.448 127.498 87.676  1.00 56.36  ? 374 GLU B O     1 
ATOM   7103 C  CB    . GLU B 2 374 ? 138.522 127.361 88.466  1.00 58.43  ? 374 GLU B CB    1 
ATOM   7104 C  CG    . GLU B 2 374 ? 139.776 127.330 89.318  1.00 72.61  ? 374 GLU B CG    1 
ATOM   7105 C  CD    . GLU B 2 374 ? 141.018 127.020 88.509  1.00 85.05  ? 374 GLU B CD    1 
ATOM   7106 O  OE1   . GLU B 2 374 ? 140.876 126.541 87.365  1.00 82.26  ? 374 GLU B OE1   1 
ATOM   7107 O  OE2   . GLU B 2 374 ? 142.134 127.255 89.018  1.00 89.40  ? 374 GLU B OE2   1 
ATOM   7108 N  N     . GLU B 2 375 ? 136.175 129.603 88.001  1.00 50.28  ? 375 GLU B N     1 
ATOM   7109 C  CA    . GLU B 2 375 ? 135.191 130.211 87.124  1.00 48.87  ? 375 GLU B CA    1 
ATOM   7110 C  C     . GLU B 2 375 ? 135.805 130.488 85.754  1.00 52.38  ? 375 GLU B C     1 
ATOM   7111 O  O     . GLU B 2 375 ? 136.967 130.173 85.489  1.00 57.99  ? 375 GLU B O     1 
ATOM   7112 C  CB    . GLU B 2 375 ? 134.635 131.485 87.758  1.00 51.88  ? 375 GLU B CB    1 
ATOM   7113 C  CG    . GLU B 2 375 ? 133.825 131.231 89.012  1.00 49.50  ? 375 GLU B CG    1 
ATOM   7114 C  CD    . GLU B 2 375 ? 133.510 132.501 89.765  1.00 60.36  ? 375 GLU B CD    1 
ATOM   7115 O  OE1   . GLU B 2 375 ? 133.682 133.592 89.184  1.00 62.19  ? 375 GLU B OE1   1 
ATOM   7116 O  OE2   . GLU B 2 375 ? 133.090 132.408 90.937  1.00 64.70  ? 375 GLU B OE2   1 
ATOM   7117 N  N     . GLU B 2 376 ? 135.005 131.087 84.871  1.00 50.85  ? 376 GLU B N     1 
ATOM   7118 C  CA    . GLU B 2 376 ? 135.422 131.327 83.495  1.00 57.08  ? 376 GLU B CA    1 
ATOM   7119 C  C     . GLU B 2 376 ? 136.634 132.244 83.420  1.00 65.79  ? 376 GLU B C     1 
ATOM   7120 O  O     . GLU B 2 376 ? 137.722 131.815 83.026  1.00 69.74  ? 376 GLU B O     1 
ATOM   7121 C  CB    . GLU B 2 376 ? 134.277 131.943 82.691  1.00 58.26  ? 376 GLU B CB    1 
ATOM   7122 C  CG    . GLU B 2 376 ? 133.307 130.951 82.093  1.00 52.04  ? 376 GLU B CG    1 
ATOM   7123 C  CD    . GLU B 2 376 ? 132.234 131.630 81.267  1.00 63.08  ? 376 GLU B CD    1 
ATOM   7124 O  OE1   . GLU B 2 376 ? 131.351 132.285 81.860  1.00 61.19  ? 376 GLU B OE1   1 
ATOM   7125 O  OE2   . GLU B 2 376 ? 132.275 131.512 80.025  1.00 63.37  ? 376 GLU B OE2   1 
ATOM   7126 N  N     . SER B 2 377 ? 136.451 133.502 83.810  1.00 67.54  ? 377 SER B N     1 
ATOM   7127 C  CA    . SER B 2 377 ? 137.485 134.528 83.756  1.00 72.65  ? 377 SER B CA    1 
ATOM   7128 C  C     . SER B 2 377 ? 136.886 135.802 84.336  1.00 79.85  ? 377 SER B C     1 
ATOM   7129 O  O     . SER B 2 377 ? 135.676 135.895 84.563  1.00 77.98  ? 377 SER B O     1 
ATOM   7130 C  CB    . SER B 2 377 ? 137.993 134.782 82.336  1.00 70.39  ? 377 SER B CB    1 
ATOM   7131 O  OG    . SER B 2 377 ? 138.855 133.743 81.908  1.00 69.85  ? 377 SER B OG    1 
ATOM   7132 N  N     . ALA B 2 378 ? 137.749 136.787 84.566  1.00 82.82  ? 378 ALA B N     1 
ATOM   7133 C  CA    . ALA B 2 378 ? 137.299 138.094 85.027  1.00 84.09  ? 378 ALA B CA    1 
ATOM   7134 C  C     . ALA B 2 378 ? 136.566 138.792 83.889  1.00 84.04  ? 378 ALA B C     1 
ATOM   7135 O  O     . ALA B 2 378 ? 137.190 139.244 82.924  1.00 81.03  ? 378 ALA B O     1 
ATOM   7136 C  CB    . ALA B 2 378 ? 138.485 138.923 85.509  1.00 89.44  ? 378 ALA B CB    1 
ATOM   7137 N  N     . ASP B 2 379 ? 135.243 138.873 83.993  1.00 81.41  ? 379 ASP B N     1 
ATOM   7138 C  CA    . ASP B 2 379 ? 134.442 139.470 82.934  1.00 83.43  ? 379 ASP B CA    1 
ATOM   7139 C  C     . ASP B 2 379 ? 134.676 140.974 82.895  1.00 88.32  ? 379 ASP B C     1 
ATOM   7140 O  O     . ASP B 2 379 ? 134.531 141.659 83.912  1.00 92.56  ? 379 ASP B O     1 
ATOM   7141 C  CB    . ASP B 2 379 ? 132.965 139.160 83.154  1.00 83.03  ? 379 ASP B CB    1 
ATOM   7142 C  CG    . ASP B 2 379 ? 132.139 139.348 81.901  1.00 86.00  ? 379 ASP B CG    1 
ATOM   7143 O  OD1   . ASP B 2 379 ? 132.728 139.360 80.801  1.00 86.43  ? 379 ASP B OD1   1 
ATOM   7144 O  OD2   . ASP B 2 379 ? 130.903 139.483 82.015  1.00 84.62  ? 379 ASP B OD2   1 
ATOM   7145 N  N     . SER B 2 380 ? 135.036 141.484 81.721  1.00 85.65  ? 380 SER B N     1 
ATOM   7146 C  CA    . SER B 2 380 ? 135.315 142.901 81.580  1.00 88.22  ? 380 SER B CA    1 
ATOM   7147 C  C     . SER B 2 380 ? 134.038 143.718 81.767  1.00 90.11  ? 380 SER B C     1 
ATOM   7148 O  O     . SER B 2 380 ? 132.945 143.266 81.420  1.00 89.45  ? 380 SER B O     1 
ATOM   7149 C  CB    . SER B 2 380 ? 135.924 143.192 80.212  1.00 84.97  ? 380 SER B CB    1 
ATOM   7150 O  OG    . SER B 2 380 ? 137.259 142.724 80.141  1.00 84.38  ? 380 SER B OG    1 
ATOM   7151 N  N     . PRO B 2 381 ? 134.147 144.924 82.331  1.00 91.55  ? 381 PRO B N     1 
ATOM   7152 C  CA    . PRO B 2 381 ? 132.955 145.762 82.517  1.00 89.98  ? 381 PRO B CA    1 
ATOM   7153 C  C     . PRO B 2 381 ? 132.531 146.525 81.274  1.00 86.96  ? 381 PRO B C     1 
ATOM   7154 O  O     . PRO B 2 381 ? 131.463 147.151 81.293  1.00 81.78  ? 381 PRO B O     1 
ATOM   7155 C  CB    . PRO B 2 381 ? 133.385 146.725 83.629  1.00 89.04  ? 381 PRO B CB    1 
ATOM   7156 C  CG    . PRO B 2 381 ? 134.855 146.862 83.436  1.00 87.77  ? 381 PRO B CG    1 
ATOM   7157 C  CD    . PRO B 2 381 ? 135.347 145.524 82.942  1.00 86.78  ? 381 PRO B CD    1 
ATOM   7158 N  N     . ARG B 2 382 ? 133.323 146.498 80.205  1.00 85.89  ? 382 ARG B N     1 
ATOM   7159 C  CA    . ARG B 2 382 ? 132.997 147.264 79.009  1.00 86.98  ? 382 ARG B CA    1 
ATOM   7160 C  C     . ARG B 2 382 ? 131.739 146.722 78.344  1.00 88.84  ? 382 ARG B C     1 
ATOM   7161 O  O     . ARG B 2 382 ? 131.541 145.509 78.245  1.00 89.39  ? 382 ARG B O     1 
ATOM   7162 C  CB    . ARG B 2 382 ? 134.161 147.230 78.021  1.00 85.96  ? 382 ARG B CB    1 
ATOM   7163 C  CG    . ARG B 2 382 ? 135.399 147.975 78.482  1.00 90.14  ? 382 ARG B CG    1 
ATOM   7164 C  CD    . ARG B 2 382 ? 136.412 148.089 77.357  1.00 92.18  ? 382 ARG B CD    1 
ATOM   7165 N  NE    . ARG B 2 382 ? 137.629 148.770 77.780  1.00 103.97 ? 382 ARG B NE    1 
ATOM   7166 C  CZ    . ARG B 2 382 ? 138.699 148.934 77.015  1.00 101.99 ? 382 ARG B CZ    1 
ATOM   7167 N  NH1   . ARG B 2 382 ? 138.738 148.476 75.774  1.00 98.04  ? 382 ARG B NH1   1 
ATOM   7168 N  NH2   . ARG B 2 382 ? 139.756 149.573 77.506  1.00 95.55  ? 382 ARG B NH2   1 
ATOM   7169 N  N     . ARG B 2 383 ? 130.887 147.633 77.884  1.00 86.95  ? 383 ARG B N     1 
ATOM   7170 C  CA    . ARG B 2 383 ? 129.672 147.249 77.182  1.00 87.80  ? 383 ARG B CA    1 
ATOM   7171 C  C     . ARG B 2 383 ? 129.953 147.072 75.696  1.00 91.97  ? 383 ARG B C     1 
ATOM   7172 O  O     . ARG B 2 383 ? 130.659 147.876 75.081  1.00 96.79  ? 383 ARG B O     1 
ATOM   7173 C  CB    . ARG B 2 383 ? 128.581 148.299 77.388  1.00 86.79  ? 383 ARG B CB    1 
ATOM   7174 C  CG    . ARG B 2 383 ? 127.803 148.147 78.685  1.00 84.96  ? 383 ARG B CG    1 
ATOM   7175 C  CD    . ARG B 2 383 ? 126.879 146.942 78.639  1.00 83.88  ? 383 ARG B CD    1 
ATOM   7176 N  NE    . ARG B 2 383 ? 127.334 145.870 79.515  1.00 86.48  ? 383 ARG B NE    1 
ATOM   7177 C  CZ    . ARG B 2 383 ? 126.564 144.885 79.955  1.00 85.11  ? 383 ARG B CZ    1 
ATOM   7178 N  NH1   . ARG B 2 383 ? 125.285 144.808 79.626  1.00 87.73  ? 383 ARG B NH1   1 
ATOM   7179 N  NH2   . ARG B 2 383 ? 127.090 143.953 80.745  1.00 78.67  ? 383 ARG B NH2   1 
ATOM   7180 N  N     . ALA B 2 384 ? 129.403 146.006 75.121  1.00 88.42  ? 384 ALA B N     1 
ATOM   7181 C  CA    . ALA B 2 384 ? 129.581 145.753 73.700  1.00 88.66  ? 384 ALA B CA    1 
ATOM   7182 C  C     . ALA B 2 384 ? 128.812 146.775 72.874  1.00 97.44  ? 384 ALA B C     1 
ATOM   7183 O  O     . ALA B 2 384 ? 127.705 147.185 73.234  1.00 100.30 ? 384 ALA B O     1 
ATOM   7184 C  CB    . ALA B 2 384 ? 129.121 144.340 73.345  1.00 82.09  ? 384 ALA B CB    1 
ATOM   7185 N  N     . ASP B 2 385 ? 129.408 147.188 71.760  1.00 100.89 ? 385 ASP B N     1 
ATOM   7186 C  CA    . ASP B 2 385 ? 128.770 148.138 70.855  1.00 107.93 ? 385 ASP B CA    1 
ATOM   7187 C  C     . ASP B 2 385 ? 129.224 147.815 69.440  1.00 110.59 ? 385 ASP B C     1 
ATOM   7188 O  O     . ASP B 2 385 ? 130.336 148.180 69.049  1.00 115.00 ? 385 ASP B O     1 
ATOM   7189 C  CB    . ASP B 2 385 ? 129.120 149.576 71.229  1.00 113.13 ? 385 ASP B CB    1 
ATOM   7190 C  CG    . ASP B 2 385 ? 128.320 150.594 70.444  1.00 119.83 ? 385 ASP B CG    1 
ATOM   7191 O  OD1   . ASP B 2 385 ? 127.300 150.208 69.835  1.00 117.11 ? 385 ASP B OD1   1 
ATOM   7192 O  OD2   . ASP B 2 385 ? 128.713 151.779 70.432  1.00 122.19 ? 385 ASP B OD2   1 
ATOM   7193 N  N     . VAL B 2 386 ? 128.368 147.138 68.676  1.00 109.60 ? 386 VAL B N     1 
ATOM   7194 C  CA    . VAL B 2 386 ? 128.671 146.811 67.282  1.00 115.39 ? 386 VAL B CA    1 
ATOM   7195 C  C     . VAL B 2 386 ? 128.237 148.016 66.446  1.00 117.74 ? 386 VAL B C     1 
ATOM   7196 O  O     . VAL B 2 386 ? 127.055 148.342 66.319  1.00 116.78 ? 386 VAL B O     1 
ATOM   7197 C  CB    . VAL B 2 386 ? 128.042 145.482 66.848  1.00 109.82 ? 386 VAL B CB    1 
ATOM   7198 C  CG1   . VAL B 2 386 ? 128.286 144.433 67.916  1.00 104.52 ? 386 VAL B CG1   1 
ATOM   7199 C  CG2   . VAL B 2 386 ? 126.543 145.579 66.616  1.00 103.99 ? 386 VAL B CG2   1 
ATOM   7200 N  N     . ARG B 2 387 ? 129.232 148.748 65.943  1.00 116.49 ? 387 ARG B N     1 
ATOM   7201 C  CA    . ARG B 2 387 ? 128.939 149.959 65.184  1.00 121.85 ? 387 ARG B CA    1 
ATOM   7202 C  C     . ARG B 2 387 ? 128.455 149.627 63.778  1.00 121.07 ? 387 ARG B C     1 
ATOM   7203 O  O     . ARG B 2 387 ? 127.503 150.240 63.282  1.00 121.23 ? 387 ARG B O     1 
ATOM   7204 C  CB    . ARG B 2 387 ? 130.173 150.858 65.141  1.00 120.96 ? 387 ARG B CB    1 
ATOM   7205 C  CG    . ARG B 2 387 ? 129.869 152.335 65.330  1.00 124.65 ? 387 ARG B CG    1 
ATOM   7206 C  CD    . ARG B 2 387 ? 129.440 152.627 66.761  1.00 125.59 ? 387 ARG B CD    1 
ATOM   7207 N  NE    . ARG B 2 387 ? 129.202 154.048 66.985  1.00 130.53 ? 387 ARG B NE    1 
ATOM   7208 C  CZ    . ARG B 2 387 ? 129.027 154.601 68.178  1.00 131.13 ? 387 ARG B CZ    1 
ATOM   7209 N  NH1   . ARG B 2 387 ? 129.046 153.876 69.285  1.00 127.73 ? 387 ARG B NH1   1 
ATOM   7210 N  NH2   . ARG B 2 387 ? 128.827 155.913 68.262  1.00 129.65 ? 387 ARG B NH2   1 
ATOM   7211 N  N     . THR B 2 388 ? 129.095 148.661 63.122  1.00 116.81 ? 388 THR B N     1 
ATOM   7212 C  CA    . THR B 2 388 ? 128.744 148.261 61.763  1.00 114.37 ? 388 THR B CA    1 
ATOM   7213 C  C     . THR B 2 388 ? 128.396 146.787 61.642  1.00 109.48 ? 388 THR B C     1 
ATOM   7214 O  O     . THR B 2 388 ? 127.467 146.437 60.910  1.00 104.16 ? 388 THR B O     1 
ATOM   7215 C  CB    . THR B 2 388 ? 129.893 148.586 60.794  1.00 115.60 ? 388 THR B CB    1 
ATOM   7216 O  OG1   . THR B 2 388 ? 130.943 147.624 60.953  1.00 113.85 ? 388 THR B OG1   1 
ATOM   7217 C  CG2   . THR B 2 388 ? 130.447 149.979 61.057  1.00 115.72 ? 388 THR B CG2   1 
ATOM   7218 N  N     . GLY B 2 389 ? 129.115 145.912 62.339  1.00 110.24 ? 389 GLY B N     1 
ATOM   7219 C  CA    . GLY B 2 389 ? 128.872 144.487 62.276  1.00 103.58 ? 389 GLY B CA    1 
ATOM   7220 C  C     . GLY B 2 389 ? 129.971 143.655 61.649  1.00 100.94 ? 389 GLY B C     1 
ATOM   7221 O  O     . GLY B 2 389 ? 129.755 142.462 61.409  1.00 100.18 ? 389 GLY B O     1 
ATOM   7222 N  N     . ARG B 2 390 ? 131.135 144.237 61.371  1.00 101.65 ? 390 ARG B N     1 
ATOM   7223 C  CA    . ARG B 2 390 ? 132.226 143.478 60.773  1.00 97.70  ? 390 ARG B CA    1 
ATOM   7224 C  C     . ARG B 2 390 ? 132.844 142.537 61.799  1.00 90.72  ? 390 ARG B C     1 
ATOM   7225 O  O     . ARG B 2 390 ? 133.157 142.944 62.921  1.00 92.16  ? 390 ARG B O     1 
ATOM   7226 C  CB    . ARG B 2 390 ? 133.288 144.426 60.217  1.00 99.59  ? 390 ARG B CB    1 
ATOM   7227 C  CG    . ARG B 2 390 ? 134.615 143.755 59.903  1.00 99.07  ? 390 ARG B CG    1 
ATOM   7228 C  CD    . ARG B 2 390 ? 135.718 144.781 59.717  1.00 103.03 ? 390 ARG B CD    1 
ATOM   7229 N  NE    . ARG B 2 390 ? 136.944 144.186 59.200  1.00 104.96 ? 390 ARG B NE    1 
ATOM   7230 C  CZ    . ARG B 2 390 ? 137.385 144.342 57.959  1.00 107.25 ? 390 ARG B CZ    1 
ATOM   7231 N  NH1   . ARG B 2 390 ? 136.712 145.054 57.071  1.00 104.63 ? 390 ARG B NH1   1 
ATOM   7232 N  NH2   . ARG B 2 390 ? 138.529 143.767 57.600  1.00 102.80 ? 390 ARG B NH2   1 
ATOM   7233 N  N     . VAL B 2 391 ? 133.029 141.279 61.408  1.00 86.94  ? 391 VAL B N     1 
ATOM   7234 C  CA    . VAL B 2 391 ? 133.592 140.247 62.270  1.00 88.17  ? 391 VAL B CA    1 
ATOM   7235 C  C     . VAL B 2 391 ? 134.848 139.703 61.604  1.00 89.42  ? 391 VAL B C     1 
ATOM   7236 O  O     . VAL B 2 391 ? 134.841 139.412 60.402  1.00 93.28  ? 391 VAL B O     1 
ATOM   7237 C  CB    . VAL B 2 391 ? 132.581 139.117 62.539  1.00 82.62  ? 391 VAL B CB    1 
ATOM   7238 C  CG1   . VAL B 2 391 ? 133.195 138.055 63.435  1.00 78.87  ? 391 VAL B CG1   1 
ATOM   7239 C  CG2   . VAL B 2 391 ? 131.319 139.679 63.167  1.00 83.56  ? 391 VAL B CG2   1 
ATOM   7240 N  N     . GLU B 2 392 ? 135.923 139.575 62.379  1.00 84.14  ? 392 GLU B N     1 
ATOM   7241 C  CA    . GLU B 2 392 ? 137.193 139.097 61.855  1.00 83.13  ? 392 GLU B CA    1 
ATOM   7242 C  C     . GLU B 2 392 ? 137.834 138.128 62.837  1.00 85.50  ? 392 GLU B C     1 
ATOM   7243 O  O     . GLU B 2 392 ? 137.798 138.345 64.051  1.00 84.95  ? 392 GLU B O     1 
ATOM   7244 C  CB    . GLU B 2 392 ? 138.144 140.268 61.570  1.00 86.86  ? 392 GLU B CB    1 
ATOM   7245 C  CG    . GLU B 2 392 ? 139.609 139.881 61.495  1.00 91.33  ? 392 GLU B CG    1 
ATOM   7246 C  CD    . GLU B 2 392 ? 140.370 140.675 60.456  1.00 97.63  ? 392 GLU B CD    1 
ATOM   7247 O  OE1   . GLU B 2 392 ? 140.733 141.837 60.738  1.00 99.27  ? 392 GLU B OE1   1 
ATOM   7248 O  OE2   . GLU B 2 392 ? 140.612 140.135 59.358  1.00 97.92  ? 392 GLU B OE2   1 
ATOM   7249 N  N     . PHE B 2 393 ? 138.413 137.055 62.301  1.00 88.43  ? 393 PHE B N     1 
ATOM   7250 C  CA    . PHE B 2 393 ? 139.218 136.110 63.062  1.00 87.54  ? 393 PHE B CA    1 
ATOM   7251 C  C     . PHE B 2 393 ? 140.679 136.278 62.669  1.00 89.56  ? 393 PHE B C     1 
ATOM   7252 O  O     . PHE B 2 393 ? 140.999 136.410 61.484  1.00 91.84  ? 393 PHE B O     1 
ATOM   7253 C  CB    . PHE B 2 393 ? 138.784 134.664 62.802  1.00 82.44  ? 393 PHE B CB    1 
ATOM   7254 C  CG    . PHE B 2 393 ? 137.544 134.247 63.544  1.00 79.47  ? 393 PHE B CG    1 
ATOM   7255 C  CD1   . PHE B 2 393 ? 136.376 134.982 63.445  1.00 81.55  ? 393 PHE B CD1   1 
ATOM   7256 C  CD2   . PHE B 2 393 ? 137.544 133.104 64.322  1.00 75.06  ? 393 PHE B CD2   1 
ATOM   7257 C  CE1   . PHE B 2 393 ? 135.236 134.590 64.118  1.00 76.19  ? 393 PHE B CE1   1 
ATOM   7258 C  CE2   . PHE B 2 393 ? 136.406 132.708 64.998  1.00 69.35  ? 393 PHE B CE2   1 
ATOM   7259 C  CZ    . PHE B 2 393 ? 135.253 133.453 64.896  1.00 65.26  ? 393 PHE B CZ    1 
ATOM   7260 N  N     . GLU B 2 394 ? 141.566 136.274 63.662  1.00 85.97  ? 394 GLU B N     1 
ATOM   7261 C  CA    . GLU B 2 394 ? 142.999 136.456 63.432  1.00 85.45  ? 394 GLU B CA    1 
ATOM   7262 C  C     . GLU B 2 394 ? 143.759 135.297 64.068  1.00 83.19  ? 394 GLU B C     1 
ATOM   7263 O  O     . GLU B 2 394 ? 144.056 135.329 65.266  1.00 86.19  ? 394 GLU B O     1 
ATOM   7264 C  CB    . GLU B 2 394 ? 143.478 137.795 63.984  1.00 88.42  ? 394 GLU B CB    1 
ATOM   7265 C  CG    . GLU B 2 394 ? 142.888 139.010 63.288  1.00 91.05  ? 394 GLU B CG    1 
ATOM   7266 C  CD    . GLU B 2 394 ? 141.838 139.711 64.124  1.00 95.11  ? 394 GLU B CD    1 
ATOM   7267 O  OE1   . GLU B 2 394 ? 141.304 139.082 65.060  1.00 93.39  ? 394 GLU B OE1   1 
ATOM   7268 O  OE2   . GLU B 2 394 ? 141.550 140.895 63.850  1.00 95.89  ? 394 GLU B OE2   1 
ATOM   7269 N  N     . HIS B 2 395 ? 144.082 134.287 63.258  1.00 82.74  ? 395 HIS B N     1 
ATOM   7270 C  CA    . HIS B 2 395 ? 144.894 133.146 63.688  1.00 82.78  ? 395 HIS B CA    1 
ATOM   7271 C  C     . HIS B 2 395 ? 144.320 132.494 64.942  1.00 79.33  ? 395 HIS B C     1 
ATOM   7272 O  O     . HIS B 2 395 ? 145.045 132.139 65.874  1.00 76.46  ? 395 HIS B O     1 
ATOM   7273 C  CB    . HIS B 2 395 ? 146.349 133.561 63.909  1.00 84.54  ? 395 HIS B CB    1 
ATOM   7274 C  CG    . HIS B 2 395 ? 146.992 134.167 62.701  1.00 91.94  ? 395 HIS B CG    1 
ATOM   7275 N  ND1   . HIS B 2 395 ? 146.477 134.022 61.432  1.00 90.84  ? 395 HIS B ND1   1 
ATOM   7276 C  CD2   . HIS B 2 395 ? 148.108 134.923 62.570  1.00 92.40  ? 395 HIS B CD2   1 
ATOM   7277 C  CE1   . HIS B 2 395 ? 147.248 134.660 60.570  1.00 87.53  ? 395 HIS B CE1   1 
ATOM   7278 N  NE2   . HIS B 2 395 ? 148.244 135.216 61.235  1.00 92.63  ? 395 HIS B NE2   1 
ATOM   7279 N  N     . VAL B 2 396 ? 142.998 132.329 64.961  1.00 77.47  ? 396 VAL B N     1 
ATOM   7280 C  CA    . VAL B 2 396 ? 142.328 131.792 66.138  1.00 67.73  ? 396 VAL B CA    1 
ATOM   7281 C  C     . VAL B 2 396 ? 142.581 130.296 66.231  1.00 67.68  ? 396 VAL B C     1 
ATOM   7282 O  O     . VAL B 2 396 ? 142.316 129.544 65.285  1.00 73.99  ? 396 VAL B O     1 
ATOM   7283 C  CB    . VAL B 2 396 ? 140.825 132.100 66.085  1.00 69.06  ? 396 VAL B CB    1 
ATOM   7284 C  CG1   . VAL B 2 396 ? 140.088 131.336 67.174  1.00 66.02  ? 396 VAL B CG1   1 
ATOM   7285 C  CG2   . VAL B 2 396 ? 140.590 133.590 66.218  1.00 70.01  ? 396 VAL B CG2   1 
ATOM   7286 N  N     . SER B 2 397 ? 143.100 129.859 67.374  1.00 65.73  ? 397 SER B N     1 
ATOM   7287 C  CA    . SER B 2 397 ? 143.305 128.447 67.661  1.00 65.63  ? 397 SER B CA    1 
ATOM   7288 C  C     . SER B 2 397 ? 142.603 128.102 68.964  1.00 64.25  ? 397 SER B C     1 
ATOM   7289 O  O     . SER B 2 397 ? 142.731 128.824 69.956  1.00 68.45  ? 397 SER B O     1 
ATOM   7290 C  CB    . SER B 2 397 ? 144.795 128.100 67.759  1.00 65.79  ? 397 SER B CB    1 
ATOM   7291 O  OG    . SER B 2 397 ? 145.475 128.424 66.560  1.00 71.50  ? 397 SER B OG    1 
ATOM   7292 N  N     . PHE B 2 398 ? 141.857 127.002 68.957  1.00 60.20  ? 398 PHE B N     1 
ATOM   7293 C  CA    . PHE B 2 398 ? 141.131 126.573 70.140  1.00 57.18  ? 398 PHE B CA    1 
ATOM   7294 C  C     . PHE B 2 398 ? 141.137 125.056 70.201  1.00 58.44  ? 398 PHE B C     1 
ATOM   7295 O  O     . PHE B 2 398 ? 141.232 124.381 69.174  1.00 62.18  ? 398 PHE B O     1 
ATOM   7296 C  CB    . PHE B 2 398 ? 139.692 127.099 70.140  1.00 54.55  ? 398 PHE B CB    1 
ATOM   7297 C  CG    . PHE B 2 398 ? 138.831 126.498 71.209  1.00 51.90  ? 398 PHE B CG    1 
ATOM   7298 C  CD1   . PHE B 2 398 ? 138.922 126.938 72.515  1.00 51.91  ? 398 PHE B CD1   1 
ATOM   7299 C  CD2   . PHE B 2 398 ? 137.944 125.481 70.913  1.00 46.95  ? 398 PHE B CD2   1 
ATOM   7300 C  CE1   . PHE B 2 398 ? 138.138 126.382 73.500  1.00 47.12  ? 398 PHE B CE1   1 
ATOM   7301 C  CE2   . PHE B 2 398 ? 137.164 124.925 71.893  1.00 43.31  ? 398 PHE B CE2   1 
ATOM   7302 C  CZ    . PHE B 2 398 ? 137.259 125.375 73.189  1.00 41.68  ? 398 PHE B CZ    1 
ATOM   7303 N  N     . SER B 2 399 ? 141.031 124.526 71.418  1.00 59.21  ? 399 SER B N     1 
ATOM   7304 C  CA    . SER B 2 399 ? 141.004 123.084 71.615  1.00 58.44  ? 399 SER B CA    1 
ATOM   7305 C  C     . SER B 2 399 ? 140.364 122.769 72.956  1.00 57.72  ? 399 SER B C     1 
ATOM   7306 O  O     . SER B 2 399 ? 140.844 123.232 73.994  1.00 61.58  ? 399 SER B O     1 
ATOM   7307 C  CB    . SER B 2 399 ? 142.415 122.497 71.563  1.00 63.05  ? 399 SER B CB    1 
ATOM   7308 O  OG    . SER B 2 399 ? 143.200 122.969 72.641  1.00 66.98  ? 399 SER B OG    1 
ATOM   7309 N  N     . TYR B 2 400 ? 139.289 121.987 72.933  1.00 53.77  ? 400 TYR B N     1 
ATOM   7310 C  CA    . TYR B 2 400 ? 138.811 121.364 74.155  1.00 49.96  ? 400 TYR B CA    1 
ATOM   7311 C  C     . TYR B 2 400 ? 139.816 120.311 74.601  1.00 66.30  ? 400 TYR B C     1 
ATOM   7312 O  O     . TYR B 2 400 ? 140.556 119.757 73.782  1.00 74.42  ? 400 TYR B O     1 
ATOM   7313 C  CB    . TYR B 2 400 ? 137.454 120.699 73.940  1.00 47.60  ? 400 TYR B CB    1 
ATOM   7314 C  CG    . TYR B 2 400 ? 136.457 121.472 73.104  1.00 45.25  ? 400 TYR B CG    1 
ATOM   7315 C  CD1   . TYR B 2 400 ? 136.420 121.326 71.724  1.00 45.25  ? 400 TYR B CD1   1 
ATOM   7316 C  CD2   . TYR B 2 400 ? 135.525 122.311 73.697  1.00 38.06  ? 400 TYR B CD2   1 
ATOM   7317 C  CE1   . TYR B 2 400 ? 135.505 122.014 70.958  1.00 39.16  ? 400 TYR B CE1   1 
ATOM   7318 C  CE2   . TYR B 2 400 ? 134.605 123.001 72.938  1.00 37.39  ? 400 TYR B CE2   1 
ATOM   7319 C  CZ    . TYR B 2 400 ? 134.599 122.848 71.569  1.00 39.68  ? 400 TYR B CZ    1 
ATOM   7320 O  OH    . TYR B 2 400 ? 133.685 123.533 70.805  1.00 42.23  ? 400 TYR B OH    1 
ATOM   7321 N  N     . VAL B 2 401 ? 139.831 120.028 75.903  1.00 66.19  ? 401 VAL B N     1 
ATOM   7322 C  CA    . VAL B 2 401 ? 140.684 118.993 76.497  1.00 69.54  ? 401 VAL B CA    1 
ATOM   7323 C  C     . VAL B 2 401 ? 142.105 119.095 75.937  1.00 73.05  ? 401 VAL B C     1 
ATOM   7324 O  O     . VAL B 2 401 ? 142.507 118.312 75.066  1.00 74.15  ? 401 VAL B O     1 
ATOM   7325 C  CB    . VAL B 2 401 ? 140.020 117.599 76.383  1.00 68.91  ? 401 VAL B CB    1 
ATOM   7326 C  CG1   . VAL B 2 401 ? 138.554 117.717 76.743  1.00 68.11  ? 401 VAL B CG1   1 
ATOM   7327 C  CG2   . VAL B 2 401 ? 140.084 116.977 74.984  1.00 66.77  ? 401 VAL B CG2   1 
ATOM   7328 N  N     . PRO B 2 402 ? 142.890 120.067 76.408  1.00 74.52  ? 402 PRO B N     1 
ATOM   7329 C  CA    . PRO B 2 402 ? 144.126 120.447 75.708  1.00 77.09  ? 402 PRO B CA    1 
ATOM   7330 C  C     . PRO B 2 402 ? 145.016 119.253 75.389  1.00 75.97  ? 402 PRO B C     1 
ATOM   7331 O  O     . PRO B 2 402 ? 145.212 118.356 76.210  1.00 69.88  ? 402 PRO B O     1 
ATOM   7332 C  CB    . PRO B 2 402 ? 144.807 121.408 76.690  1.00 81.12  ? 402 PRO B CB    1 
ATOM   7333 C  CG    . PRO B 2 402 ? 144.150 121.151 78.013  1.00 80.10  ? 402 PRO B CG    1 
ATOM   7334 C  CD    . PRO B 2 402 ? 142.745 120.770 77.691  1.00 72.90  ? 402 PRO B CD    1 
ATOM   7335 N  N     . GLY B 2 403 ? 145.555 119.260 74.173  1.00 76.20  ? 403 GLY B N     1 
ATOM   7336 C  CA    . GLY B 2 403 ? 146.211 118.111 73.583  1.00 73.76  ? 403 GLY B CA    1 
ATOM   7337 C  C     . GLY B 2 403 ? 145.504 117.572 72.361  1.00 79.58  ? 403 GLY B C     1 
ATOM   7338 O  O     . GLY B 2 403 ? 146.093 116.768 71.626  1.00 78.50  ? 403 GLY B O     1 
ATOM   7339 N  N     . THR B 2 404 ? 144.263 117.994 72.116  1.00 80.81  ? 404 THR B N     1 
ATOM   7340 C  CA    . THR B 2 404 ? 143.487 117.591 70.943  1.00 75.80  ? 404 THR B CA    1 
ATOM   7341 C  C     . THR B 2 404 ? 142.965 118.851 70.267  1.00 74.42  ? 404 THR B C     1 
ATOM   7342 O  O     . THR B 2 404 ? 141.839 119.292 70.535  1.00 73.23  ? 404 THR B O     1 
ATOM   7343 C  CB    . THR B 2 404 ? 142.336 116.659 71.326  1.00 72.87  ? 404 THR B CB    1 
ATOM   7344 O  OG1   . THR B 2 404 ? 142.829 115.597 72.151  1.00 76.27  ? 404 THR B OG1   1 
ATOM   7345 C  CG2   . THR B 2 404 ? 141.691 116.071 70.082  1.00 71.10  ? 404 THR B CG2   1 
ATOM   7346 N  N     . PRO B 2 405 ? 143.766 119.472 69.401  1.00 72.85  ? 405 PRO B N     1 
ATOM   7347 C  CA    . PRO B 2 405 ? 143.307 120.684 68.713  1.00 68.02  ? 405 PRO B CA    1 
ATOM   7348 C  C     . PRO B 2 405 ? 142.082 120.411 67.852  1.00 67.94  ? 405 PRO B C     1 
ATOM   7349 O  O     . PRO B 2 405 ? 141.963 119.358 67.224  1.00 69.68  ? 405 PRO B O     1 
ATOM   7350 C  CB    . PRO B 2 405 ? 144.515 121.088 67.860  1.00 68.85  ? 405 PRO B CB    1 
ATOM   7351 C  CG    . PRO B 2 405 ? 145.681 120.409 68.496  1.00 68.42  ? 405 PRO B CG    1 
ATOM   7352 C  CD    . PRO B 2 405 ? 145.152 119.127 69.050  1.00 69.00  ? 405 PRO B CD    1 
ATOM   7353 N  N     . VAL B 2 406 ? 141.164 121.377 67.830  1.00 65.38  ? 406 VAL B N     1 
ATOM   7354 C  CA    . VAL B 2 406 ? 139.961 121.269 67.013  1.00 62.80  ? 406 VAL B CA    1 
ATOM   7355 C  C     . VAL B 2 406 ? 139.935 122.414 66.009  1.00 62.96  ? 406 VAL B C     1 
ATOM   7356 O  O     . VAL B 2 406 ? 139.332 122.299 64.938  1.00 61.98  ? 406 VAL B O     1 
ATOM   7357 C  CB    . VAL B 2 406 ? 138.685 121.248 67.878  1.00 53.28  ? 406 VAL B CB    1 
ATOM   7358 C  CG1   . VAL B 2 406 ? 138.828 120.254 69.013  1.00 54.65  ? 406 VAL B CG1   1 
ATOM   7359 C  CG2   . VAL B 2 406 ? 138.368 122.629 68.421  1.00 53.55  ? 406 VAL B CG2   1 
ATOM   7360 N  N     . ILE B 2 407 ? 140.587 123.523 66.350  1.00 62.45  ? 407 ILE B N     1 
ATOM   7361 C  CA    . ILE B 2 407 ? 140.714 124.677 65.467  1.00 64.70  ? 407 ILE B CA    1 
ATOM   7362 C  C     . ILE B 2 407 ? 142.122 125.231 65.626  1.00 68.11  ? 407 ILE B C     1 
ATOM   7363 O  O     . ILE B 2 407 ? 142.598 125.407 66.752  1.00 66.01  ? 407 ILE B O     1 
ATOM   7364 C  CB    . ILE B 2 407 ? 139.662 125.761 65.776  1.00 61.50  ? 407 ILE B CB    1 
ATOM   7365 C  CG1   . ILE B 2 407 ? 138.284 125.329 65.272  1.00 58.19  ? 407 ILE B CG1   1 
ATOM   7366 C  CG2   . ILE B 2 407 ? 140.056 127.092 65.152  1.00 61.49  ? 407 ILE B CG2   1 
ATOM   7367 C  CD1   . ILE B 2 407 ? 137.222 126.382 65.431  1.00 51.75  ? 407 ILE B CD1   1 
ATOM   7368 N  N     . GLU B 2 408 ? 142.792 125.499 64.506  1.00 74.03  ? 408 GLU B N     1 
ATOM   7369 C  CA    . GLU B 2 408 ? 144.159 126.000 64.555  1.00 78.65  ? 408 GLU B CA    1 
ATOM   7370 C  C     . GLU B 2 408 ? 144.434 126.890 63.352  1.00 78.05  ? 408 GLU B C     1 
ATOM   7371 O  O     . GLU B 2 408 ? 144.096 126.530 62.221  1.00 77.86  ? 408 GLU B O     1 
ATOM   7372 C  CB    . GLU B 2 408 ? 145.164 124.844 64.603  1.00 78.51  ? 408 GLU B CB    1 
ATOM   7373 C  CG    . GLU B 2 408 ? 144.931 123.772 63.557  1.00 83.26  ? 408 GLU B CG    1 
ATOM   7374 C  CD    . GLU B 2 408 ? 144.065 122.635 64.060  1.00 85.03  ? 408 GLU B CD    1 
ATOM   7375 O  OE1   . GLU B 2 408 ? 144.614 121.695 64.671  1.00 86.16  ? 408 GLU B OE1   1 
ATOM   7376 O  OE2   . GLU B 2 408 ? 142.836 122.679 63.841  1.00 80.03  ? 408 GLU B OE2   1 
ATOM   7377 N  N     . ASP B 2 409 ? 145.047 128.047 63.612  1.00 77.78  ? 409 ASP B N     1 
ATOM   7378 C  CA    . ASP B 2 409 ? 145.496 128.976 62.573  1.00 79.98  ? 409 ASP B CA    1 
ATOM   7379 C  C     . ASP B 2 409 ? 144.362 129.343 61.618  1.00 81.81  ? 409 ASP B C     1 
ATOM   7380 O  O     . ASP B 2 409 ? 144.522 129.354 60.395  1.00 82.94  ? 409 ASP B O     1 
ATOM   7381 C  CB    . ASP B 2 409 ? 146.689 128.401 61.809  1.00 80.52  ? 409 ASP B CB    1 
ATOM   7382 C  CG    . ASP B 2 409 ? 147.871 128.108 62.711  1.00 84.07  ? 409 ASP B CG    1 
ATOM   7383 O  OD1   . ASP B 2 409 ? 148.469 127.020 62.575  1.00 85.65  ? 409 ASP B OD1   1 
ATOM   7384 O  OD2   . ASP B 2 409 ? 148.204 128.965 63.555  1.00 85.93  ? 409 ASP B OD2   1 
ATOM   7385 N  N     . LEU B 2 410 ? 143.204 129.654 62.189  1.00 80.84  ? 410 LEU B N     1 
ATOM   7386 C  CA    . LEU B 2 410 ? 142.014 129.970 61.413  1.00 81.44  ? 410 LEU B CA    1 
ATOM   7387 C  C     . LEU B 2 410 ? 141.801 131.478 61.361  1.00 82.25  ? 410 LEU B C     1 
ATOM   7388 O  O     . LEU B 2 410 ? 141.956 132.173 62.369  1.00 83.45  ? 410 LEU B O     1 
ATOM   7389 C  CB    . LEU B 2 410 ? 140.782 129.286 62.008  1.00 74.75  ? 410 LEU B CB    1 
ATOM   7390 C  CG    . LEU B 2 410 ? 139.571 129.153 61.085  1.00 74.47  ? 410 LEU B CG    1 
ATOM   7391 C  CD1   . LEU B 2 410 ? 138.819 127.865 61.359  1.00 69.88  ? 410 LEU B CD1   1 
ATOM   7392 C  CD2   . LEU B 2 410 ? 138.657 130.342 61.253  1.00 75.52  ? 410 LEU B CD2   1 
ATOM   7393 N  N     . SER B 2 411 ? 141.444 131.976 60.178  1.00 83.22  ? 411 SER B N     1 
ATOM   7394 C  CA    . SER B 2 411 ? 141.203 133.396 59.966  1.00 83.95  ? 411 SER B CA    1 
ATOM   7395 C  C     . SER B 2 411 ? 140.086 133.580 58.950  1.00 85.03  ? 411 SER B C     1 
ATOM   7396 O  O     . SER B 2 411 ? 140.001 132.834 57.971  1.00 85.83  ? 411 SER B O     1 
ATOM   7397 C  CB    . SER B 2 411 ? 142.469 134.108 59.473  1.00 84.53  ? 411 SER B CB    1 
ATOM   7398 O  OG    . SER B 2 411 ? 143.552 133.910 60.364  1.00 88.29  ? 411 SER B OG    1 
ATOM   7399 N  N     . LEU B 2 412 ? 139.232 134.575 59.186  1.00 85.60  ? 412 LEU B N     1 
ATOM   7400 C  CA    . LEU B 2 412 ? 138.224 134.965 58.210  1.00 87.35  ? 412 LEU B CA    1 
ATOM   7401 C  C     . LEU B 2 412 ? 137.887 136.435 58.399  1.00 87.02  ? 412 LEU B C     1 
ATOM   7402 O  O     . LEU B 2 412 ? 138.146 137.023 59.451  1.00 86.69  ? 412 LEU B O     1 
ATOM   7403 C  CB    . LEU B 2 412 ? 136.938 134.135 58.315  1.00 85.03  ? 412 LEU B CB    1 
ATOM   7404 C  CG    . LEU B 2 412 ? 136.159 134.202 59.629  1.00 84.57  ? 412 LEU B CG    1 
ATOM   7405 C  CD1   . LEU B 2 412 ? 134.671 134.150 59.360  1.00 81.28  ? 412 LEU B CD1   1 
ATOM   7406 C  CD2   . LEU B 2 412 ? 136.549 133.049 60.515  1.00 81.53  ? 412 LEU B CD2   1 
ATOM   7407 N  N     . VAL B 2 413 ? 137.298 137.020 57.360  1.00 88.68  ? 413 VAL B N     1 
ATOM   7408 C  CA    . VAL B 2 413 ? 136.797 138.387 57.393  1.00 92.37  ? 413 VAL B CA    1 
ATOM   7409 C  C     . VAL B 2 413 ? 135.331 138.358 56.994  1.00 93.93  ? 413 VAL B C     1 
ATOM   7410 O  O     . VAL B 2 413 ? 134.978 137.782 55.959  1.00 94.67  ? 413 VAL B O     1 
ATOM   7411 C  CB    . VAL B 2 413 ? 137.590 139.318 56.455  1.00 94.05  ? 413 VAL B CB    1 
ATOM   7412 C  CG1   . VAL B 2 413 ? 137.108 140.751 56.604  1.00 97.35  ? 413 VAL B CG1   1 
ATOM   7413 C  CG2   . VAL B 2 413 ? 139.080 139.216 56.730  1.00 91.31  ? 413 VAL B CG2   1 
ATOM   7414 N  N     . ALA B 2 414 ? 134.481 138.976 57.809  1.00 93.36  ? 414 ALA B N     1 
ATOM   7415 C  CA    . ALA B 2 414 ? 133.051 139.059 57.541  1.00 90.59  ? 414 ALA B CA    1 
ATOM   7416 C  C     . ALA B 2 414 ? 132.670 140.523 57.389  1.00 94.87  ? 414 ALA B C     1 
ATOM   7417 O  O     . ALA B 2 414 ? 132.877 141.320 58.310  1.00 98.96  ? 414 ALA B O     1 
ATOM   7418 C  CB    . ALA B 2 414 ? 132.239 138.402 58.658  1.00 87.08  ? 414 ALA B CB    1 
ATOM   7419 N  N     . GLU B 2 415 ? 132.119 140.873 56.231  1.00 97.68  ? 415 GLU B N     1 
ATOM   7420 C  CA    . GLU B 2 415 ? 131.693 142.240 55.995  1.00 104.72 ? 415 GLU B CA    1 
ATOM   7421 C  C     . GLU B 2 415 ? 130.451 142.553 56.829  1.00 102.60 ? 415 GLU B C     1 
ATOM   7422 O  O     . GLU B 2 415 ? 129.689 141.649 57.180  1.00 103.12 ? 415 GLU B O     1 
ATOM   7423 C  CB    . GLU B 2 415 ? 131.407 142.457 54.511  1.00 106.02 ? 415 GLU B CB    1 
ATOM   7424 C  CG    . GLU B 2 415 ? 132.642 142.357 53.632  1.00 110.03 ? 415 GLU B CG    1 
ATOM   7425 C  CD    . GLU B 2 415 ? 133.728 143.330 54.043  1.00 119.09 ? 415 GLU B CD    1 
ATOM   7426 O  OE1   . GLU B 2 415 ? 133.396 144.481 54.397  1.00 122.30 ? 415 GLU B OE1   1 
ATOM   7427 O  OE2   . GLU B 2 415 ? 134.915 142.943 54.019  1.00 118.79 ? 415 GLU B OE2   1 
ATOM   7428 N  N     . PRO B 2 416 ? 130.225 143.827 57.161  1.00 102.92 ? 416 PRO B N     1 
ATOM   7429 C  CA    . PRO B 2 416 ? 129.117 144.162 58.072  1.00 107.27 ? 416 PRO B CA    1 
ATOM   7430 C  C     . PRO B 2 416 ? 127.743 143.765 57.559  1.00 106.00 ? 416 PRO B C     1 
ATOM   7431 O  O     . PRO B 2 416 ? 126.824 143.601 58.370  1.00 106.98 ? 416 PRO B O     1 
ATOM   7432 C  CB    . PRO B 2 416 ? 129.236 145.686 58.226  1.00 107.70 ? 416 PRO B CB    1 
ATOM   7433 C  CG    . PRO B 2 416 ? 130.043 146.133 57.052  1.00 108.86 ? 416 PRO B CG    1 
ATOM   7434 C  CD    . PRO B 2 416 ? 131.003 145.019 56.788  1.00 103.71 ? 416 PRO B CD    1 
ATOM   7435 N  N     . GLY B 2 417 ? 127.564 143.611 56.253  1.00 102.47 ? 417 GLY B N     1 
ATOM   7436 C  CA    . GLY B 2 417 ? 126.281 143.182 55.733  1.00 104.40 ? 417 GLY B CA    1 
ATOM   7437 C  C     . GLY B 2 417 ? 126.341 141.824 55.068  1.00 104.94 ? 417 GLY B C     1 
ATOM   7438 O  O     . GLY B 2 417 ? 125.326 141.317 54.581  1.00 102.93 ? 417 GLY B O     1 
ATOM   7439 N  N     . SER B 2 418 ? 127.527 141.225 55.049  1.00 103.84 ? 418 SER B N     1 
ATOM   7440 C  CA    . SER B 2 418 ? 127.729 139.965 54.352  1.00 101.66 ? 418 SER B CA    1 
ATOM   7441 C  C     . SER B 2 418 ? 127.079 138.809 55.102  1.00 96.34  ? 418 SER B C     1 
ATOM   7442 O  O     . SER B 2 418 ? 127.027 138.784 56.334  1.00 91.53  ? 418 SER B O     1 
ATOM   7443 C  CB    . SER B 2 418 ? 129.220 139.684 54.167  1.00 102.31 ? 418 SER B CB    1 
ATOM   7444 O  OG    . SER B 2 418 ? 129.858 139.473 55.413  1.00 101.91 ? 418 SER B OG    1 
ATOM   7445 N  N     . THR B 2 419 ? 126.575 137.848 54.334  1.00 95.92  ? 419 THR B N     1 
ATOM   7446 C  CA    . THR B 2 419 ? 126.052 136.598 54.868  1.00 92.97  ? 419 THR B CA    1 
ATOM   7447 C  C     . THR B 2 419 ? 127.128 135.532 54.696  1.00 90.31  ? 419 THR B C     1 
ATOM   7448 O  O     . THR B 2 419 ? 127.399 135.091 53.574  1.00 90.68  ? 419 THR B O     1 
ATOM   7449 C  CB    . THR B 2 419 ? 124.761 136.200 54.158  1.00 94.20  ? 419 THR B CB    1 
ATOM   7450 O  OG1   . THR B 2 419 ? 123.734 137.152 54.461  1.00 98.45  ? 419 THR B OG1   1 
ATOM   7451 C  CG2   . THR B 2 419 ? 124.313 134.822 54.600  1.00 89.98  ? 419 THR B CG2   1 
ATOM   7452 N  N     . VAL B 2 420 ? 127.740 135.122 55.801  1.00 84.19  ? 420 VAL B N     1 
ATOM   7453 C  CA    . VAL B 2 420 ? 128.836 134.161 55.769  1.00 82.11  ? 420 VAL B CA    1 
ATOM   7454 C  C     . VAL B 2 420 ? 128.252 132.766 55.954  1.00 80.26  ? 420 VAL B C     1 
ATOM   7455 O  O     . VAL B 2 420 ? 127.627 132.472 56.976  1.00 81.71  ? 420 VAL B O     1 
ATOM   7456 C  CB    . VAL B 2 420 ? 129.890 134.469 56.838  1.00 79.47  ? 420 VAL B CB    1 
ATOM   7457 C  CG1   . VAL B 2 420 ? 130.968 133.403 56.836  1.00 75.72  ? 420 VAL B CG1   1 
ATOM   7458 C  CG2   . VAL B 2 420 ? 130.499 135.836 56.595  1.00 85.55  ? 420 VAL B CG2   1 
ATOM   7459 N  N     . ALA B 2 421 ? 128.457 131.906 54.963  1.00 74.39  ? 421 ALA B N     1 
ATOM   7460 C  CA    . ALA B 2 421 ? 128.002 130.527 55.025  1.00 68.00  ? 421 ALA B CA    1 
ATOM   7461 C  C     . ALA B 2 421 ? 129.167 129.628 55.410  1.00 69.19  ? 421 ALA B C     1 
ATOM   7462 O  O     . ALA B 2 421 ? 130.257 129.737 54.841  1.00 73.27  ? 421 ALA B O     1 
ATOM   7463 C  CB    . ALA B 2 421 ? 127.414 130.091 53.685  1.00 70.00  ? 421 ALA B CB    1 
ATOM   7464 N  N     . ILE B 2 422 ? 128.939 128.747 56.377  1.00 67.93  ? 422 ILE B N     1 
ATOM   7465 C  CA    . ILE B 2 422 ? 129.953 127.808 56.838  1.00 66.82  ? 422 ILE B CA    1 
ATOM   7466 C  C     . ILE B 2 422 ? 129.482 126.404 56.492  1.00 65.74  ? 422 ILE B C     1 
ATOM   7467 O  O     . ILE B 2 422 ? 128.454 125.942 57.003  1.00 63.55  ? 422 ILE B O     1 
ATOM   7468 C  CB    . ILE B 2 422 ? 130.224 127.946 58.343  1.00 62.00  ? 422 ILE B CB    1 
ATOM   7469 C  CG1   . ILE B 2 422 ? 130.482 129.408 58.702  1.00 66.99  ? 422 ILE B CG1   1 
ATOM   7470 C  CG2   . ILE B 2 422 ? 131.414 127.102 58.742  1.00 59.50  ? 422 ILE B CG2   1 
ATOM   7471 C  CD1   . ILE B 2 422 ? 130.234 129.733 60.151  1.00 65.91  ? 422 ILE B CD1   1 
ATOM   7472 N  N     . VAL B 2 423 ? 130.234 125.728 55.625  1.00 65.94  ? 423 VAL B N     1 
ATOM   7473 C  CA    . VAL B 2 423 ? 129.927 124.374 55.193  1.00 62.40  ? 423 VAL B CA    1 
ATOM   7474 C  C     . VAL B 2 423 ? 131.174 123.523 55.383  1.00 60.65  ? 423 VAL B C     1 
ATOM   7475 O  O     . VAL B 2 423 ? 132.291 124.031 55.495  1.00 65.89  ? 423 VAL B O     1 
ATOM   7476 C  CB    . VAL B 2 423 ? 129.452 124.316 53.725  1.00 61.54  ? 423 VAL B CB    1 
ATOM   7477 C  CG1   . VAL B 2 423 ? 128.262 125.235 53.512  1.00 62.57  ? 423 VAL B CG1   1 
ATOM   7478 C  CG2   . VAL B 2 423 ? 130.583 124.686 52.786  1.00 63.32  ? 423 VAL B CG2   1 
ATOM   7479 N  N     . GLY B 2 424 ? 130.969 122.213 55.435  1.00 57.10  ? 424 GLY B N     1 
ATOM   7480 C  CA    . GLY B 2 424 ? 132.067 121.292 55.583  1.00 56.32  ? 424 GLY B CA    1 
ATOM   7481 C  C     . GLY B 2 424 ? 131.643 119.963 56.169  1.00 60.25  ? 424 GLY B C     1 
ATOM   7482 O  O     . GLY B 2 424 ? 130.458 119.708 56.401  1.00 62.28  ? 424 GLY B O     1 
ATOM   7483 N  N     . PRO B 2 425 ? 132.618 119.088 56.422  1.00 58.94  ? 425 PRO B N     1 
ATOM   7484 C  CA    . PRO B 2 425 ? 132.305 117.760 56.964  1.00 55.06  ? 425 PRO B CA    1 
ATOM   7485 C  C     . PRO B 2 425 ? 131.631 117.797 58.326  1.00 54.49  ? 425 PRO B C     1 
ATOM   7486 O  O     . PRO B 2 425 ? 131.454 118.859 58.929  1.00 54.93  ? 425 PRO B O     1 
ATOM   7487 C  CB    . PRO B 2 425 ? 133.680 117.089 57.043  1.00 53.52  ? 425 PRO B CB    1 
ATOM   7488 C  CG    . PRO B 2 425 ? 134.466 117.748 55.983  1.00 55.17  ? 425 PRO B CG    1 
ATOM   7489 C  CD    . PRO B 2 425 ? 134.014 119.176 55.967  1.00 56.39  ? 425 PRO B CD    1 
ATOM   7490 N  N     . THR B 2 426 ? 131.263 116.617 58.816  1.00 52.99  ? 426 THR B N     1 
ATOM   7491 C  CA    . THR B 2 426 ? 130.426 116.476 59.997  1.00 49.11  ? 426 THR B CA    1 
ATOM   7492 C  C     . THR B 2 426 ? 131.098 116.938 61.285  1.00 48.76  ? 426 THR B C     1 
ATOM   7493 O  O     . THR B 2 426 ? 130.412 117.469 62.161  1.00 50.97  ? 426 THR B O     1 
ATOM   7494 C  CB    . THR B 2 426 ? 129.987 115.016 60.125  1.00 47.86  ? 426 THR B CB    1 
ATOM   7495 O  OG1   . THR B 2 426 ? 129.276 114.627 58.944  1.00 56.42  ? 426 THR B OG1   1 
ATOM   7496 C  CG2   . THR B 2 426 ? 129.092 114.835 61.304  1.00 42.01  ? 426 THR B CG2   1 
ATOM   7497 N  N     . GLY B 2 427 ? 132.407 116.779 61.427  1.00 45.79  ? 427 GLY B N     1 
ATOM   7498 C  CA    . GLY B 2 427 ? 133.058 117.203 62.651  1.00 42.64  ? 427 GLY B CA    1 
ATOM   7499 C  C     . GLY B 2 427 ? 134.134 118.240 62.412  1.00 49.77  ? 427 GLY B C     1 
ATOM   7500 O  O     . GLY B 2 427 ? 135.149 118.269 63.112  1.00 50.60  ? 427 GLY B O     1 
ATOM   7501 N  N     . ALA B 2 428 ? 133.913 119.101 61.418  1.00 53.82  ? 428 ALA B N     1 
ATOM   7502 C  CA    . ALA B 2 428 ? 134.942 120.048 61.004  1.00 50.97  ? 428 ALA B CA    1 
ATOM   7503 C  C     . ALA B 2 428 ? 135.253 121.064 62.096  1.00 54.46  ? 428 ALA B C     1 
ATOM   7504 O  O     . ALA B 2 428 ? 136.423 121.376 62.342  1.00 63.42  ? 428 ALA B O     1 
ATOM   7505 C  CB    . ALA B 2 428 ? 134.512 120.754 59.722  1.00 51.00  ? 428 ALA B CB    1 
ATOM   7506 N  N     . GLY B 2 429 ? 134.229 121.588 62.761  1.00 49.46  ? 429 GLY B N     1 
ATOM   7507 C  CA    . GLY B 2 429 ? 134.433 122.646 63.731  1.00 43.28  ? 429 GLY B CA    1 
ATOM   7508 C  C     . GLY B 2 429 ? 133.546 123.848 63.488  1.00 45.47  ? 429 GLY B C     1 
ATOM   7509 O  O     . GLY B 2 429 ? 133.819 124.943 63.984  1.00 47.67  ? 429 GLY B O     1 
ATOM   7510 N  N     . LYS B 2 430 ? 132.474 123.648 62.718  1.00 47.62  ? 430 LYS B N     1 
ATOM   7511 C  CA    . LYS B 2 430 ? 131.562 124.740 62.396  1.00 40.66  ? 430 LYS B CA    1 
ATOM   7512 C  C     . LYS B 2 430 ? 130.842 125.269 63.631  1.00 42.08  ? 430 LYS B C     1 
ATOM   7513 O  O     . LYS B 2 430 ? 130.696 126.485 63.787  1.00 47.07  ? 430 LYS B O     1 
ATOM   7514 C  CB    . LYS B 2 430 ? 130.556 124.277 61.346  1.00 46.09  ? 430 LYS B CB    1 
ATOM   7515 C  CG    . LYS B 2 430 ? 131.201 123.702 60.094  1.00 51.87  ? 430 LYS B CG    1 
ATOM   7516 C  CD    . LYS B 2 430 ? 130.162 123.264 59.080  1.00 51.88  ? 430 LYS B CD    1 
ATOM   7517 C  CE    . LYS B 2 430 ? 129.242 122.211 59.662  1.00 48.48  ? 430 LYS B CE    1 
ATOM   7518 N  NZ    . LYS B 2 430 ? 129.948 120.926 59.896  1.00 43.49  ? 430 LYS B NZ    1 
ATOM   7519 N  N     . THR B 2 431 ? 130.374 124.381 64.511  1.00 42.12  ? 431 THR B N     1 
ATOM   7520 C  CA    . THR B 2 431 ? 129.748 124.828 65.751  1.00 39.84  ? 431 THR B CA    1 
ATOM   7521 C  C     . THR B 2 431 ? 130.768 125.455 66.692  1.00 42.75  ? 431 THR B C     1 
ATOM   7522 O  O     . THR B 2 431 ? 130.461 126.431 67.385  1.00 49.49  ? 431 THR B O     1 
ATOM   7523 C  CB    . THR B 2 431 ? 129.039 123.661 66.441  1.00 40.30  ? 431 THR B CB    1 
ATOM   7524 O  OG1   . THR B 2 431 ? 128.153 123.021 65.515  1.00 43.23  ? 431 THR B OG1   1 
ATOM   7525 C  CG2   . THR B 2 431 ? 128.244 124.147 67.636  1.00 36.85  ? 431 THR B CG2   1 
ATOM   7526 N  N     . THR B 2 432 ? 131.981 124.902 66.732  1.00 42.37  ? 432 THR B N     1 
ATOM   7527 C  CA    . THR B 2 432 ? 133.027 125.462 67.580  1.00 39.41  ? 432 THR B CA    1 
ATOM   7528 C  C     . THR B 2 432 ? 133.366 126.891 67.179  1.00 41.92  ? 432 THR B C     1 
ATOM   7529 O  O     . THR B 2 432 ? 133.651 127.723 68.045  1.00 45.39  ? 432 THR B O     1 
ATOM   7530 C  CB    . THR B 2 432 ? 134.273 124.577 67.519  1.00 42.77  ? 432 THR B CB    1 
ATOM   7531 O  OG1   . THR B 2 432 ? 133.952 123.268 68.002  1.00 43.49  ? 432 THR B OG1   1 
ATOM   7532 C  CG2   . THR B 2 432 ? 135.394 125.156 68.365  1.00 45.42  ? 432 THR B CG2   1 
ATOM   7533 N  N     . LEU B 2 433 ? 133.322 127.196 65.882  1.00 41.42  ? 433 LEU B N     1 
ATOM   7534 C  CA    . LEU B 2 433 ? 133.652 128.540 65.419  1.00 40.21  ? 433 LEU B CA    1 
ATOM   7535 C  C     . LEU B 2 433 ? 132.671 129.571 65.965  1.00 43.35  ? 433 LEU B C     1 
ATOM   7536 O  O     . LEU B 2 433 ? 133.074 130.608 66.504  1.00 49.41  ? 433 LEU B O     1 
ATOM   7537 C  CB    . LEU B 2 433 ? 133.672 128.565 63.892  1.00 44.62  ? 433 LEU B CB    1 
ATOM   7538 C  CG    . LEU B 2 433 ? 134.364 129.759 63.244  1.00 54.51  ? 433 LEU B CG    1 
ATOM   7539 C  CD1   . LEU B 2 433 ? 135.857 129.535 63.262  1.00 59.22  ? 433 LEU B CD1   1 
ATOM   7540 C  CD2   . LEU B 2 433 ? 133.869 129.960 61.826  1.00 54.52  ? 433 LEU B CD2   1 
ATOM   7541 N  N     . VAL B 2 434 ? 131.370 129.296 65.847  1.00 45.26  ? 434 VAL B N     1 
ATOM   7542 C  CA    . VAL B 2 434 ? 130.376 130.235 66.348  1.00 44.66  ? 434 VAL B CA    1 
ATOM   7543 C  C     . VAL B 2 434 ? 130.291 130.209 67.867  1.00 44.55  ? 434 VAL B C     1 
ATOM   7544 O  O     . VAL B 2 434 ? 129.829 131.184 68.470  1.00 48.60  ? 434 VAL B O     1 
ATOM   7545 C  CB    . VAL B 2 434 ? 129.000 129.959 65.713  1.00 46.04  ? 434 VAL B CB    1 
ATOM   7546 C  CG1   . VAL B 2 434 ? 129.041 130.258 64.224  1.00 46.36  ? 434 VAL B CG1   1 
ATOM   7547 C  CG2   . VAL B 2 434 ? 128.570 128.528 65.961  1.00 45.30  ? 434 VAL B CG2   1 
ATOM   7548 N  N     . ASN B 2 435 ? 130.717 129.119 68.510  1.00 39.84  ? 435 ASN B N     1 
ATOM   7549 C  CA    . ASN B 2 435 ? 130.824 129.130 69.965  1.00 41.25  ? 435 ASN B CA    1 
ATOM   7550 C  C     . ASN B 2 435 ? 131.980 130.004 70.430  1.00 42.53  ? 435 ASN B C     1 
ATOM   7551 O  O     . ASN B 2 435 ? 131.898 130.624 71.496  1.00 43.78  ? 435 ASN B O     1 
ATOM   7552 C  CB    . ASN B 2 435 ? 130.987 127.708 70.496  1.00 41.45  ? 435 ASN B CB    1 
ATOM   7553 C  CG    . ASN B 2 435 ? 129.706 126.912 70.423  1.00 46.23  ? 435 ASN B CG    1 
ATOM   7554 O  OD1   . ASN B 2 435 ? 128.656 127.440 70.065  1.00 51.54  ? 435 ASN B OD1   1 
ATOM   7555 N  ND2   . ASN B 2 435 ? 129.785 125.633 70.762  1.00 44.51  ? 435 ASN B ND2   1 
ATOM   7556 N  N     . LEU B 2 436 ? 133.069 130.047 69.661  1.00 41.57  ? 436 LEU B N     1 
ATOM   7557 C  CA    . LEU B 2 436 ? 134.148 130.986 69.952  1.00 42.68  ? 436 LEU B CA    1 
ATOM   7558 C  C     . LEU B 2 436 ? 133.715 132.420 69.677  1.00 45.36  ? 436 LEU B C     1 
ATOM   7559 O  O     . LEU B 2 436 ? 134.095 133.340 70.408  1.00 48.31  ? 436 LEU B O     1 
ATOM   7560 C  CB    . LEU B 2 436 ? 135.388 130.639 69.131  1.00 40.79  ? 436 LEU B CB    1 
ATOM   7561 C  CG    . LEU B 2 436 ? 136.109 129.340 69.484  1.00 42.97  ? 436 LEU B CG    1 
ATOM   7562 C  CD1   . LEU B 2 436 ? 137.161 129.029 68.437  1.00 43.57  ? 436 LEU B CD1   1 
ATOM   7563 C  CD2   . LEU B 2 436 ? 136.728 129.429 70.865  1.00 46.54  ? 436 LEU B CD2   1 
ATOM   7564 N  N     . LEU B 2 437 ? 132.926 132.627 68.620  1.00 45.78  ? 437 LEU B N     1 
ATOM   7565 C  CA    . LEU B 2 437 ? 132.412 133.962 68.330  1.00 45.66  ? 437 LEU B CA    1 
ATOM   7566 C  C     . LEU B 2 437 ? 131.515 134.464 69.455  1.00 45.24  ? 437 LEU B C     1 
ATOM   7567 O  O     . LEU B 2 437 ? 131.582 135.638 69.835  1.00 51.80  ? 437 LEU B O     1 
ATOM   7568 C  CB    . LEU B 2 437 ? 131.655 133.953 67.004  1.00 45.41  ? 437 LEU B CB    1 
ATOM   7569 C  CG    . LEU B 2 437 ? 130.947 135.249 66.611  1.00 44.70  ? 437 LEU B CG    1 
ATOM   7570 C  CD1   . LEU B 2 437 ? 131.938 136.394 66.541  1.00 50.25  ? 437 LEU B CD1   1 
ATOM   7571 C  CD2   . LEU B 2 437 ? 130.230 135.074 65.287  1.00 53.37  ? 437 LEU B CD2   1 
ATOM   7572 N  N     . MET B 2 438 ? 130.670 133.592 69.997  1.00 45.88  ? 438 MET B N     1 
ATOM   7573 C  CA    . MET B 2 438 ? 129.830 133.939 71.135  1.00 45.63  ? 438 MET B CA    1 
ATOM   7574 C  C     . MET B 2 438 ? 130.591 133.908 72.451  1.00 45.63  ? 438 MET B C     1 
ATOM   7575 O  O     . MET B 2 438 ? 130.016 134.249 73.489  1.00 47.78  ? 438 MET B O     1 
ATOM   7576 C  CB    . MET B 2 438 ? 128.630 132.992 71.211  1.00 47.62  ? 438 MET B CB    1 
ATOM   7577 C  CG    . MET B 2 438 ? 127.581 133.237 70.142  1.00 55.64  ? 438 MET B CG    1 
ATOM   7578 S  SD    . MET B 2 438 ? 126.477 134.607 70.529  1.00 67.76  ? 438 MET B SD    1 
ATOM   7579 C  CE    . MET B 2 438 ? 125.606 133.952 71.944  1.00 54.61  ? 438 MET B CE    1 
ATOM   7580 N  N     . ARG B 2 439 ? 131.861 133.506 72.423  1.00 48.96  ? 439 ARG B N     1 
ATOM   7581 C  CA    . ARG B 2 439 ? 132.705 133.403 73.612  1.00 45.79  ? 439 ARG B CA    1 
ATOM   7582 C  C     . ARG B 2 439 ? 132.106 132.452 74.643  1.00 44.86  ? 439 ARG B C     1 
ATOM   7583 O  O     . ARG B 2 439 ? 132.197 132.675 75.851  1.00 47.56  ? 439 ARG B O     1 
ATOM   7584 C  CB    . ARG B 2 439 ? 132.978 134.776 74.227  1.00 48.89  ? 439 ARG B CB    1 
ATOM   7585 C  CG    . ARG B 2 439 ? 134.328 134.861 74.911  1.00 59.13  ? 439 ARG B CG    1 
ATOM   7586 C  CD    . ARG B 2 439 ? 134.523 136.189 75.604  1.00 66.93  ? 439 ARG B CD    1 
ATOM   7587 N  NE    . ARG B 2 439 ? 135.733 136.191 76.415  1.00 67.87  ? 439 ARG B NE    1 
ATOM   7588 C  CZ    . ARG B 2 439 ? 135.970 137.046 77.399  1.00 70.48  ? 439 ARG B CZ    1 
ATOM   7589 N  NH1   . ARG B 2 439 ? 135.100 137.989 77.718  1.00 68.90  ? 439 ARG B NH1   1 
ATOM   7590 N  NH2   . ARG B 2 439 ? 137.107 136.951 78.081  1.00 71.11  ? 439 ARG B NH2   1 
ATOM   7591 N  N     . PHE B 2 440 ? 131.484 131.375 74.160  1.00 43.30  ? 440 PHE B N     1 
ATOM   7592 C  CA    . PHE B 2 440 ? 131.104 130.288 75.051  1.00 37.64  ? 440 PHE B CA    1 
ATOM   7593 C  C     . PHE B 2 440 ? 132.334 129.614 75.639  1.00 44.24  ? 440 PHE B C     1 
ATOM   7594 O  O     . PHE B 2 440 ? 132.294 129.126 76.774  1.00 46.19  ? 440 PHE B O     1 
ATOM   7595 C  CB    . PHE B 2 440 ? 130.247 129.270 74.302  1.00 40.09  ? 440 PHE B CB    1 
ATOM   7596 C  CG    . PHE B 2 440 ? 128.820 129.693 74.121  1.00 46.36  ? 440 PHE B CG    1 
ATOM   7597 C  CD1   . PHE B 2 440 ? 128.387 130.929 74.566  1.00 45.95  ? 440 PHE B CD1   1 
ATOM   7598 C  CD2   . PHE B 2 440 ? 127.909 128.855 73.503  1.00 50.60  ? 440 PHE B CD2   1 
ATOM   7599 C  CE1   . PHE B 2 440 ? 127.076 131.321 74.400  1.00 43.66  ? 440 PHE B CE1   1 
ATOM   7600 C  CE2   . PHE B 2 440 ? 126.595 129.242 73.334  1.00 51.03  ? 440 PHE B CE2   1 
ATOM   7601 C  CZ    . PHE B 2 440 ? 126.180 130.476 73.783  1.00 49.27  ? 440 PHE B CZ    1 
ATOM   7602 N  N     . TYR B 2 441 ? 133.426 129.578 74.880  1.00 48.10  ? 441 TYR B N     1 
ATOM   7603 C  CA    . TYR B 2 441 ? 134.712 129.079 75.334  1.00 45.29  ? 441 TYR B CA    1 
ATOM   7604 C  C     . TYR B 2 441 ? 135.774 130.124 75.024  1.00 53.24  ? 441 TYR B C     1 
ATOM   7605 O  O     . TYR B 2 441 ? 135.609 130.960 74.133  1.00 57.21  ? 441 TYR B O     1 
ATOM   7606 C  CB    . TYR B 2 441 ? 135.074 127.747 74.666  1.00 44.11  ? 441 TYR B CB    1 
ATOM   7607 C  CG    . TYR B 2 441 ? 134.025 126.670 74.813  1.00 42.44  ? 441 TYR B CG    1 
ATOM   7608 C  CD1   . TYR B 2 441 ? 133.009 126.533 73.881  1.00 38.96  ? 441 TYR B CD1   1 
ATOM   7609 C  CD2   . TYR B 2 441 ? 134.059 125.784 75.879  1.00 42.87  ? 441 TYR B CD2   1 
ATOM   7610 C  CE1   . TYR B 2 441 ? 132.052 125.552 74.012  1.00 39.82  ? 441 TYR B CE1   1 
ATOM   7611 C  CE2   . TYR B 2 441 ? 133.107 124.800 76.016  1.00 42.58  ? 441 TYR B CE2   1 
ATOM   7612 C  CZ    . TYR B 2 441 ? 132.106 124.689 75.080  1.00 43.13  ? 441 TYR B CZ    1 
ATOM   7613 O  OH    . TYR B 2 441 ? 131.154 123.707 75.214  1.00 48.60  ? 441 TYR B OH    1 
ATOM   7614 N  N     . ASP B 2 442 ? 136.871 130.073 75.773  1.00 54.06  ? 442 ASP B N     1 
ATOM   7615 C  CA    . ASP B 2 442 ? 137.961 131.022 75.598  1.00 56.60  ? 442 ASP B CA    1 
ATOM   7616 C  C     . ASP B 2 442 ? 138.929 130.532 74.530  1.00 58.36  ? 442 ASP B C     1 
ATOM   7617 O  O     . ASP B 2 442 ? 139.272 129.349 74.480  1.00 62.85  ? 442 ASP B O     1 
ATOM   7618 C  CB    . ASP B 2 442 ? 138.703 131.243 76.915  1.00 63.24  ? 442 ASP B CB    1 
ATOM   7619 C  CG    . ASP B 2 442 ? 138.068 132.322 77.766  1.00 71.65  ? 442 ASP B CG    1 
ATOM   7620 O  OD1   . ASP B 2 442 ? 137.090 132.021 78.482  1.00 71.91  ? 442 ASP B OD1   1 
ATOM   7621 O  OD2   . ASP B 2 442 ? 138.546 133.474 77.718  1.00 75.35  ? 442 ASP B OD2   1 
ATOM   7622 N  N     . VAL B 2 443 ? 139.367 131.456 73.676  1.00 58.02  ? 443 VAL B N     1 
ATOM   7623 C  CA    . VAL B 2 443 ? 140.276 131.113 72.590  1.00 60.76  ? 443 VAL B CA    1 
ATOM   7624 C  C     . VAL B 2 443 ? 141.661 130.825 73.152  1.00 63.38  ? 443 VAL B C     1 
ATOM   7625 O  O     . VAL B 2 443 ? 142.197 131.597 73.957  1.00 63.72  ? 443 VAL B O     1 
ATOM   7626 C  CB    . VAL B 2 443 ? 140.319 132.245 71.553  1.00 61.75  ? 443 VAL B CB    1 
ATOM   7627 C  CG1   . VAL B 2 443 ? 141.429 132.010 70.564  1.00 61.88  ? 443 VAL B CG1   1 
ATOM   7628 C  CG2   . VAL B 2 443 ? 138.988 132.355 70.835  1.00 59.59  ? 443 VAL B CG2   1 
ATOM   7629 N  N     . ASP B 2 444 ? 142.249 129.702 72.730  1.00 66.73  ? 444 ASP B N     1 
ATOM   7630 C  CA    . ASP B 2 444 ? 143.580 129.337 73.205  1.00 66.26  ? 444 ASP B CA    1 
ATOM   7631 C  C     . ASP B 2 444 ? 144.648 130.277 72.658  1.00 69.27  ? 444 ASP B C     1 
ATOM   7632 O  O     . ASP B 2 444 ? 145.512 130.744 73.408  1.00 73.38  ? 444 ASP B O     1 
ATOM   7633 C  CB    . ASP B 2 444 ? 143.894 127.892 72.822  1.00 62.31  ? 444 ASP B CB    1 
ATOM   7634 C  CG    . ASP B 2 444 ? 143.224 126.889 73.739  1.00 73.95  ? 444 ASP B CG    1 
ATOM   7635 O  OD1   . ASP B 2 444 ? 142.251 127.268 74.425  1.00 70.62  ? 444 ASP B OD1   1 
ATOM   7636 O  OD2   . ASP B 2 444 ? 143.669 125.723 73.774  1.00 84.57  ? 444 ASP B OD2   1 
ATOM   7637 N  N     . SER B 2 445 ? 144.610 130.563 71.359  1.00 68.98  ? 445 SER B N     1 
ATOM   7638 C  CA    . SER B 2 445 ? 145.594 131.435 70.733  1.00 69.41  ? 445 SER B CA    1 
ATOM   7639 C  C     . SER B 2 445 ? 144.915 132.235 69.634  1.00 71.42  ? 445 SER B C     1 
ATOM   7640 O  O     . SER B 2 445 ? 144.054 131.714 68.922  1.00 74.74  ? 445 SER B O     1 
ATOM   7641 C  CB    . SER B 2 445 ? 146.768 130.635 70.160  1.00 69.95  ? 445 SER B CB    1 
ATOM   7642 O  OG    . SER B 2 445 ? 147.630 130.187 71.191  1.00 76.77  ? 445 SER B OG    1 
ATOM   7643 N  N     . GLY B 2 446 ? 145.323 133.489 69.486  1.00 71.19  ? 446 GLY B N     1 
ATOM   7644 C  CA    . GLY B 2 446 ? 144.666 134.388 68.563  1.00 70.72  ? 446 GLY B CA    1 
ATOM   7645 C  C     . GLY B 2 446 ? 143.594 135.207 69.248  1.00 72.30  ? 446 GLY B C     1 
ATOM   7646 O  O     . GLY B 2 446 ? 143.416 135.169 70.469  1.00 71.95  ? 446 GLY B O     1 
ATOM   7647 N  N     . ARG B 2 447 ? 142.864 135.970 68.439  1.00 72.95  ? 447 ARG B N     1 
ATOM   7648 C  CA    . ARG B 2 447 ? 141.802 136.808 68.973  1.00 73.07  ? 447 ARG B CA    1 
ATOM   7649 C  C     . ARG B 2 447 ? 140.711 136.986 67.928  1.00 79.12  ? 447 ARG B C     1 
ATOM   7650 O  O     . ARG B 2 447 ? 140.941 136.841 66.726  1.00 79.64  ? 447 ARG B O     1 
ATOM   7651 C  CB    . ARG B 2 447 ? 142.339 138.168 69.429  1.00 79.66  ? 447 ARG B CB    1 
ATOM   7652 C  CG    . ARG B 2 447 ? 142.841 139.057 68.309  1.00 86.15  ? 447 ARG B CG    1 
ATOM   7653 C  CD    . ARG B 2 447 ? 142.712 140.523 68.689  1.00 90.51  ? 447 ARG B CD    1 
ATOM   7654 N  NE    . ARG B 2 447 ? 142.874 141.406 67.541  1.00 94.97  ? 447 ARG B NE    1 
ATOM   7655 C  CZ    . ARG B 2 447 ? 144.044 141.772 67.037  1.00 100.05 ? 447 ARG B CZ    1 
ATOM   7656 N  NH1   . ARG B 2 447 ? 145.184 141.355 67.563  1.00 101.60 ? 447 ARG B NH1   1 
ATOM   7657 N  NH2   . ARG B 2 447 ? 144.070 142.579 65.980  1.00 96.58  ? 447 ARG B NH2   1 
ATOM   7658 N  N     . ILE B 2 448 ? 139.512 137.301 68.413  1.00 83.40  ? 448 ILE B N     1 
ATOM   7659 C  CA    . ILE B 2 448 ? 138.342 137.546 67.579  1.00 81.72  ? 448 ILE B CA    1 
ATOM   7660 C  C     . ILE B 2 448 ? 137.882 138.974 67.825  1.00 82.48  ? 448 ILE B C     1 
ATOM   7661 O  O     . ILE B 2 448 ? 137.691 139.378 68.977  1.00 83.30  ? 448 ILE B O     1 
ATOM   7662 C  CB    . ILE B 2 448 ? 137.206 136.551 67.880  1.00 71.07  ? 448 ILE B CB    1 
ATOM   7663 C  CG1   . ILE B 2 448 ? 137.689 135.113 67.710  1.00 65.09  ? 448 ILE B CG1   1 
ATOM   7664 C  CG2   . ILE B 2 448 ? 136.006 136.824 66.990  1.00 68.54  ? 448 ILE B CG2   1 
ATOM   7665 C  CD1   . ILE B 2 448 ? 136.754 134.086 68.297  1.00 59.83  ? 448 ILE B CD1   1 
ATOM   7666 N  N     . THR B 2 449 ? 137.705 139.733 66.749  1.00 81.59  ? 449 THR B N     1 
ATOM   7667 C  CA    . THR B 2 449 ? 137.306 141.128 66.837  1.00 82.38  ? 449 THR B CA    1 
ATOM   7668 C  C     . THR B 2 449 ? 135.993 141.342 66.100  1.00 83.57  ? 449 THR B C     1 
ATOM   7669 O  O     . THR B 2 449 ? 135.779 140.787 65.018  1.00 89.23  ? 449 THR B O     1 
ATOM   7670 C  CB    . THR B 2 449 ? 138.375 142.059 66.252  1.00 86.73  ? 449 THR B CB    1 
ATOM   7671 O  OG1   . THR B 2 449 ? 138.255 142.094 64.825  1.00 85.86  ? 449 THR B OG1   1 
ATOM   7672 C  CG2   . THR B 2 449 ? 139.763 141.579 66.625  1.00 86.80  ? 449 THR B CG2   1 
ATOM   7673 N  N     . ILE B 2 450 ? 135.115 142.143 66.695  1.00 81.01  ? 450 ILE B N     1 
ATOM   7674 C  CA    . ILE B 2 450 ? 133.892 142.600 66.048  1.00 84.44  ? 450 ILE B CA    1 
ATOM   7675 C  C     . ILE B 2 450 ? 133.970 144.114 65.951  1.00 90.75  ? 450 ILE B C     1 
ATOM   7676 O  O     . ILE B 2 450 ? 134.033 144.803 66.976  1.00 92.47  ? 450 ILE B O     1 
ATOM   7677 C  CB    . ILE B 2 450 ? 132.633 142.162 66.809  1.00 83.39  ? 450 ILE B CB    1 
ATOM   7678 C  CG1   . ILE B 2 450 ? 132.615 140.644 66.984  1.00 82.58  ? 450 ILE B CG1   1 
ATOM   7679 C  CG2   . ILE B 2 450 ? 131.388 142.622 66.075  1.00 86.77  ? 450 ILE B CG2   1 
ATOM   7680 C  CD1   . ILE B 2 450 ? 131.409 140.131 67.731  1.00 67.73  ? 450 ILE B CD1   1 
ATOM   7681 N  N     . ASP B 2 451 ? 133.971 144.629 64.720  1.00 96.20  ? 451 ASP B N     1 
ATOM   7682 C  CA    . ASP B 2 451 ? 134.119 146.060 64.453  1.00 97.30  ? 451 ASP B CA    1 
ATOM   7683 C  C     . ASP B 2 451 ? 135.407 146.620 65.049  1.00 94.35  ? 451 ASP B C     1 
ATOM   7684 O  O     . ASP B 2 451 ? 135.447 147.765 65.503  1.00 94.99  ? 451 ASP B O     1 
ATOM   7685 C  CB    . ASP B 2 451 ? 132.908 146.849 64.957  1.00 102.20 ? 451 ASP B CB    1 
ATOM   7686 C  CG    . ASP B 2 451 ? 131.880 147.086 63.875  1.00 109.12 ? 451 ASP B CG    1 
ATOM   7687 O  OD1   . ASP B 2 451 ? 131.590 146.140 63.114  1.00 109.13 ? 451 ASP B OD1   1 
ATOM   7688 O  OD2   . ASP B 2 451 ? 131.365 148.218 63.781  1.00 112.63 ? 451 ASP B OD2   1 
ATOM   7689 N  N     . GLY B 2 452 ? 136.469 145.817 65.055  1.00 89.64  ? 452 GLY B N     1 
ATOM   7690 C  CA    . GLY B 2 452 ? 137.767 146.259 65.509  1.00 89.55  ? 452 GLY B CA    1 
ATOM   7691 C  C     . GLY B 2 452 ? 138.027 146.120 66.993  1.00 93.04  ? 452 GLY B C     1 
ATOM   7692 O  O     . GLY B 2 452 ? 139.157 146.375 67.431  1.00 92.76  ? 452 GLY B O     1 
ATOM   7693 N  N     . VAL B 2 453 ? 137.034 145.722 67.784  1.00 92.31  ? 453 VAL B N     1 
ATOM   7694 C  CA    . VAL B 2 453 ? 137.198 145.565 69.225  1.00 87.94  ? 453 VAL B CA    1 
ATOM   7695 C  C     . VAL B 2 453 ? 137.227 144.080 69.555  1.00 86.71  ? 453 VAL B C     1 
ATOM   7696 O  O     . VAL B 2 453 ? 136.460 143.287 68.993  1.00 88.00  ? 453 VAL B O     1 
ATOM   7697 C  CB    . VAL B 2 453 ? 136.091 146.307 70.005  1.00 86.40  ? 453 VAL B CB    1 
ATOM   7698 C  CG1   . VAL B 2 453 ? 135.844 147.677 69.395  1.00 88.93  ? 453 VAL B CG1   1 
ATOM   7699 C  CG2   . VAL B 2 453 ? 134.797 145.510 70.050  1.00 81.75  ? 453 VAL B CG2   1 
ATOM   7700 N  N     . ASP B 2 454 ? 138.148 143.692 70.433  1.00 84.99  ? 454 ASP B N     1 
ATOM   7701 C  CA    . ASP B 2 454 ? 138.281 142.290 70.803  1.00 83.11  ? 454 ASP B CA    1 
ATOM   7702 C  C     . ASP B 2 454 ? 137.106 141.862 71.670  1.00 84.23  ? 454 ASP B C     1 
ATOM   7703 O  O     . ASP B 2 454 ? 136.698 142.586 72.583  1.00 88.16  ? 454 ASP B O     1 
ATOM   7704 C  CB    . ASP B 2 454 ? 139.596 142.057 71.543  1.00 83.21  ? 454 ASP B CB    1 
ATOM   7705 C  CG    . ASP B 2 454 ? 140.791 142.596 70.787  1.00 93.68  ? 454 ASP B CG    1 
ATOM   7706 O  OD1   . ASP B 2 454 ? 140.633 142.943 69.599  1.00 94.34  ? 454 ASP B OD1   1 
ATOM   7707 O  OD2   . ASP B 2 454 ? 141.888 142.670 71.379  1.00 98.29  ? 454 ASP B OD2   1 
ATOM   7708 N  N     . ILE B 2 455 ? 136.555 140.681 71.380  1.00 79.46  ? 455 ILE B N     1 
ATOM   7709 C  CA    . ILE B 2 455 ? 135.437 140.170 72.161  1.00 75.36  ? 455 ILE B CA    1 
ATOM   7710 C  C     . ILE B 2 455 ? 135.867 139.646 73.520  1.00 74.30  ? 455 ILE B C     1 
ATOM   7711 O  O     . ILE B 2 455 ? 135.014 139.416 74.384  1.00 75.29  ? 455 ILE B O     1 
ATOM   7712 C  CB    . ILE B 2 455 ? 134.687 139.072 71.381  1.00 70.69  ? 455 ILE B CB    1 
ATOM   7713 C  CG1   . ILE B 2 455 ? 135.457 137.754 71.421  1.00 65.56  ? 455 ILE B CG1   1 
ATOM   7714 C  CG2   . ILE B 2 455 ? 134.456 139.506 69.947  1.00 72.19  ? 455 ILE B CG2   1 
ATOM   7715 C  CD1   . ILE B 2 455 ? 134.709 136.602 70.796  1.00 61.03  ? 455 ILE B CD1   1 
ATOM   7716 N  N     . ALA B 2 456 ? 137.167 139.450 73.734  1.00 75.20  ? 456 ALA B N     1 
ATOM   7717 C  CA    . ALA B 2 456 ? 137.667 139.019 75.031  1.00 73.95  ? 456 ALA B CA    1 
ATOM   7718 C  C     . ALA B 2 456 ? 137.856 140.174 76.004  1.00 79.56  ? 456 ALA B C     1 
ATOM   7719 O  O     . ALA B 2 456 ? 138.084 139.929 77.194  1.00 82.49  ? 456 ALA B O     1 
ATOM   7720 C  CB    . ALA B 2 456 ? 138.991 138.270 74.864  1.00 68.95  ? 456 ALA B CB    1 
ATOM   7721 N  N     . SER B 2 457 ? 137.769 141.415 75.534  1.00 80.88  ? 457 SER B N     1 
ATOM   7722 C  CA    . SER B 2 457 ? 137.947 142.600 76.365  1.00 80.79  ? 457 SER B CA    1 
ATOM   7723 C  C     . SER B 2 457 ? 136.628 143.341 76.550  1.00 77.89  ? 457 SER B C     1 
ATOM   7724 O  O     . SER B 2 457 ? 136.600 144.551 76.778  1.00 84.94  ? 457 SER B O     1 
ATOM   7725 C  CB    . SER B 2 457 ? 138.999 143.528 75.766  1.00 83.85  ? 457 SER B CB    1 
ATOM   7726 O  OG    . SER B 2 457 ? 138.534 144.111 74.562  1.00 79.09  ? 457 SER B OG    1 
ATOM   7727 N  N     . VAL B 2 458 ? 135.516 142.614 76.446  1.00 77.56  ? 458 VAL B N     1 
ATOM   7728 C  CA    . VAL B 2 458 ? 134.186 143.190 76.595  1.00 79.67  ? 458 VAL B CA    1 
ATOM   7729 C  C     . VAL B 2 458 ? 133.363 142.249 77.461  1.00 80.10  ? 458 VAL B C     1 
ATOM   7730 O  O     . VAL B 2 458 ? 133.702 141.077 77.635  1.00 82.69  ? 458 VAL B O     1 
ATOM   7731 C  CB    . VAL B 2 458 ? 133.506 143.430 75.226  1.00 76.73  ? 458 VAL B CB    1 
ATOM   7732 C  CG1   . VAL B 2 458 ? 132.749 142.190 74.770  1.00 72.21  ? 458 VAL B CG1   1 
ATOM   7733 C  CG2   . VAL B 2 458 ? 132.597 144.640 75.288  1.00 81.64  ? 458 VAL B CG2   1 
ATOM   7734 N  N     . SER B 2 459 ? 132.278 142.775 78.023  1.00 77.08  ? 459 SER B N     1 
ATOM   7735 C  CA    . SER B 2 459 ? 131.419 141.958 78.868  1.00 74.10  ? 459 SER B CA    1 
ATOM   7736 C  C     . SER B 2 459 ? 130.779 140.844 78.052  1.00 72.72  ? 459 SER B C     1 
ATOM   7737 O  O     . SER B 2 459 ? 130.336 141.054 76.921  1.00 74.03  ? 459 SER B O     1 
ATOM   7738 C  CB    . SER B 2 459 ? 130.339 142.818 79.523  1.00 78.94  ? 459 SER B CB    1 
ATOM   7739 O  OG    . SER B 2 459 ? 129.706 143.651 78.570  1.00 82.27  ? 459 SER B OG    1 
ATOM   7740 N  N     . ARG B 2 460 ? 130.743 139.645 78.634  1.00 68.58  ? 460 ARG B N     1 
ATOM   7741 C  CA    . ARG B 2 460 ? 130.137 138.512 77.947  1.00 59.32  ? 460 ARG B CA    1 
ATOM   7742 C  C     . ARG B 2 460 ? 128.644 138.722 77.750  1.00 61.47  ? 460 ARG B C     1 
ATOM   7743 O  O     . ARG B 2 460 ? 128.090 138.338 76.714  1.00 68.45  ? 460 ARG B O     1 
ATOM   7744 C  CB    . ARG B 2 460 ? 130.402 137.228 78.727  1.00 57.09  ? 460 ARG B CB    1 
ATOM   7745 C  CG    . ARG B 2 460 ? 131.861 136.837 78.767  1.00 60.36  ? 460 ARG B CG    1 
ATOM   7746 C  CD    . ARG B 2 460 ? 132.118 135.760 79.799  1.00 62.94  ? 460 ARG B CD    1 
ATOM   7747 N  NE    . ARG B 2 460 ? 133.531 135.681 80.146  1.00 65.93  ? 460 ARG B NE    1 
ATOM   7748 C  CZ    . ARG B 2 460 ? 134.351 134.731 79.723  1.00 67.97  ? 460 ARG B CZ    1 
ATOM   7749 N  NH1   . ARG B 2 460 ? 133.930 133.754 78.939  1.00 67.13  ? 460 ARG B NH1   1 
ATOM   7750 N  NH2   . ARG B 2 460 ? 135.627 134.764 80.094  1.00 69.94  ? 460 ARG B NH2   1 
ATOM   7751 N  N     . GLU B 2 461 ? 127.976 139.327 78.734  1.00 66.63  ? 461 GLU B N     1 
ATOM   7752 C  CA    . GLU B 2 461 ? 126.533 139.524 78.649  1.00 65.72  ? 461 GLU B CA    1 
ATOM   7753 C  C     . GLU B 2 461 ? 126.164 140.418 77.473  1.00 62.59  ? 461 GLU B C     1 
ATOM   7754 O  O     . GLU B 2 461 ? 125.275 140.088 76.682  1.00 64.83  ? 461 GLU B O     1 
ATOM   7755 C  CB    . GLU B 2 461 ? 126.015 140.119 79.957  1.00 69.55  ? 461 GLU B CB    1 
ATOM   7756 C  CG    . GLU B 2 461 ? 125.301 139.133 80.860  1.00 68.31  ? 461 GLU B CG    1 
ATOM   7757 C  CD    . GLU B 2 461 ? 124.337 139.821 81.804  1.00 74.26  ? 461 GLU B CD    1 
ATOM   7758 O  OE1   . GLU B 2 461 ? 123.533 140.649 81.328  1.00 72.92  ? 461 GLU B OE1   1 
ATOM   7759 O  OE2   . GLU B 2 461 ? 124.388 139.541 83.020  1.00 74.24  ? 461 GLU B OE2   1 
ATOM   7760 N  N     . SER B 2 462 ? 126.838 141.562 77.345  1.00 63.51  ? 462 SER B N     1 
ATOM   7761 C  CA    . SER B 2 462 ? 126.533 142.483 76.256  1.00 68.08  ? 462 SER B CA    1 
ATOM   7762 C  C     . SER B 2 462 ? 126.867 141.874 74.901  1.00 66.85  ? 462 SER B C     1 
ATOM   7763 O  O     . SER B 2 462 ? 126.104 142.028 73.940  1.00 66.85  ? 462 SER B O     1 
ATOM   7764 C  CB    . SER B 2 462 ? 127.288 143.795 76.459  1.00 76.10  ? 462 SER B CB    1 
ATOM   7765 O  OG    . SER B 2 462 ? 128.687 143.578 76.450  1.00 77.75  ? 462 SER B OG    1 
ATOM   7766 N  N     . LEU B 2 463 ? 128.001 141.177 74.807  1.00 68.60  ? 463 LEU B N     1 
ATOM   7767 C  CA    . LEU B 2 463 ? 128.375 140.535 73.552  1.00 64.62  ? 463 LEU B CA    1 
ATOM   7768 C  C     . LEU B 2 463 ? 127.353 139.485 73.141  1.00 61.18  ? 463 LEU B C     1 
ATOM   7769 O  O     . LEU B 2 463 ? 126.975 139.400 71.968  1.00 65.36  ? 463 LEU B O     1 
ATOM   7770 C  CB    . LEU B 2 463 ? 129.762 139.906 73.682  1.00 62.74  ? 463 LEU B CB    1 
ATOM   7771 C  CG    . LEU B 2 463 ? 130.194 138.981 72.546  1.00 61.25  ? 463 LEU B CG    1 
ATOM   7772 C  CD1   . LEU B 2 463 ? 130.446 139.779 71.282  1.00 60.43  ? 463 LEU B CD1   1 
ATOM   7773 C  CD2   . LEU B 2 463 ? 131.426 138.189 72.940  1.00 61.69  ? 463 LEU B CD2   1 
ATOM   7774 N  N     . ARG B 2 464 ? 126.886 138.679 74.095  1.00 57.44  ? 464 ARG B N     1 
ATOM   7775 C  CA    . ARG B 2 464 ? 125.931 137.630 73.764  1.00 54.73  ? 464 ARG B CA    1 
ATOM   7776 C  C     . ARG B 2 464 ? 124.540 138.191 73.501  1.00 62.21  ? 464 ARG B C     1 
ATOM   7777 O  O     . ARG B 2 464 ? 123.760 137.582 72.762  1.00 65.65  ? 464 ARG B O     1 
ATOM   7778 C  CB    . ARG B 2 464 ? 125.894 136.590 74.879  1.00 50.20  ? 464 ARG B CB    1 
ATOM   7779 C  CG    . ARG B 2 464 ? 127.162 135.766 74.973  1.00 49.20  ? 464 ARG B CG    1 
ATOM   7780 C  CD    . ARG B 2 464 ? 127.313 135.130 76.337  1.00 47.31  ? 464 ARG B CD    1 
ATOM   7781 N  NE    . ARG B 2 464 ? 128.581 134.424 76.465  1.00 43.31  ? 464 ARG B NE    1 
ATOM   7782 C  CZ    . ARG B 2 464 ? 129.029 133.896 77.594  1.00 51.23  ? 464 ARG B CZ    1 
ATOM   7783 N  NH1   . ARG B 2 464 ? 128.330 133.962 78.713  1.00 51.79  ? 464 ARG B NH1   1 
ATOM   7784 N  NH2   . ARG B 2 464 ? 130.208 133.282 77.598  1.00 55.73  ? 464 ARG B NH2   1 
ATOM   7785 N  N     . ALA B 2 465 ? 124.205 139.338 74.096  1.00 63.80  ? 465 ALA B N     1 
ATOM   7786 C  CA    . ALA B 2 465 ? 122.940 139.987 73.770  1.00 59.24  ? 465 ALA B CA    1 
ATOM   7787 C  C     . ALA B 2 465 ? 122.996 140.659 72.407  1.00 64.80  ? 465 ALA B C     1 
ATOM   7788 O  O     . ALA B 2 465 ? 121.959 140.830 71.758  1.00 66.81  ? 465 ALA B O     1 
ATOM   7789 C  CB    . ALA B 2 465 ? 122.572 141.006 74.845  1.00 54.65  ? 465 ALA B CB    1 
ATOM   7790 N  N     . SER B 2 466 ? 124.191 141.054 71.964  1.00 64.43  ? 466 SER B N     1 
ATOM   7791 C  CA    . SER B 2 466 ? 124.327 141.664 70.647  1.00 66.55  ? 466 SER B CA    1 
ATOM   7792 C  C     . SER B 2 466 ? 124.089 140.658 69.528  1.00 73.37  ? 466 SER B C     1 
ATOM   7793 O  O     . SER B 2 466 ? 123.589 141.031 68.460  1.00 78.82  ? 466 SER B O     1 
ATOM   7794 C  CB    . SER B 2 466 ? 125.711 142.294 70.506  1.00 67.76  ? 466 SER B CB    1 
ATOM   7795 O  OG    . SER B 2 466 ? 126.139 142.284 69.156  1.00 75.60  ? 466 SER B OG    1 
ATOM   7796 N  N     . ILE B 2 467 ? 124.430 139.391 69.748  1.00 68.88  ? 467 ILE B N     1 
ATOM   7797 C  CA    . ILE B 2 467 ? 124.338 138.350 68.731  1.00 68.21  ? 467 ILE B CA    1 
ATOM   7798 C  C     . ILE B 2 467 ? 123.153 137.454 69.055  1.00 68.60  ? 467 ILE B C     1 
ATOM   7799 O  O     . ILE B 2 467 ? 123.056 136.918 70.165  1.00 67.30  ? 467 ILE B O     1 
ATOM   7800 C  CB    . ILE B 2 467 ? 125.634 137.527 68.646  1.00 68.38  ? 467 ILE B CB    1 
ATOM   7801 C  CG1   . ILE B 2 467 ? 126.849 138.447 68.521  1.00 65.15  ? 467 ILE B CG1   1 
ATOM   7802 C  CG2   . ILE B 2 467 ? 125.573 136.556 67.480  1.00 67.84  ? 467 ILE B CG2   1 
ATOM   7803 C  CD1   . ILE B 2 467 ? 128.128 137.840 69.045  1.00 57.60  ? 467 ILE B CD1   1 
ATOM   7804 N  N     . GLY B 2 468 ? 122.254 137.291 68.086  1.00 70.83  ? 468 GLY B N     1 
ATOM   7805 C  CA    . GLY B 2 468 ? 121.115 136.413 68.227  1.00 69.60  ? 468 GLY B CA    1 
ATOM   7806 C  C     . GLY B 2 468 ? 121.377 135.093 67.535  1.00 65.32  ? 468 GLY B C     1 
ATOM   7807 O  O     . GLY B 2 468 ? 121.605 135.050 66.325  1.00 68.63  ? 468 GLY B O     1 
ATOM   7808 N  N     . MET B 2 469 ? 121.334 134.015 68.309  1.00 59.20  ? 469 MET B N     1 
ATOM   7809 C  CA    . MET B 2 469 ? 121.784 132.707 67.860  1.00 59.67  ? 469 MET B CA    1 
ATOM   7810 C  C     . MET B 2 469 ? 120.640 131.707 67.904  1.00 60.72  ? 469 MET B C     1 
ATOM   7811 O  O     . MET B 2 469 ? 119.912 131.632 68.899  1.00 60.02  ? 469 MET B O     1 
ATOM   7812 C  CB    . MET B 2 469 ? 122.952 132.216 68.721  1.00 56.83  ? 469 MET B CB    1 
ATOM   7813 C  CG    . MET B 2 469 ? 123.738 131.074 68.111  1.00 60.66  ? 469 MET B CG    1 
ATOM   7814 S  SD    . MET B 2 469 ? 124.821 130.268 69.303  1.00 77.69  ? 469 MET B SD    1 
ATOM   7815 C  CE    . MET B 2 469 ? 126.378 130.299 68.425  1.00 65.27  ? 469 MET B CE    1 
ATOM   7816 N  N     . VAL B 2 470 ? 120.485 130.947 66.825  1.00 58.95  ? 470 VAL B N     1 
ATOM   7817 C  CA    . VAL B 2 470 ? 119.638 129.761 66.818  1.00 54.45  ? 470 VAL B CA    1 
ATOM   7818 C  C     . VAL B 2 470 ? 120.543 128.574 67.122  1.00 58.22  ? 470 VAL B C     1 
ATOM   7819 O  O     . VAL B 2 470 ? 121.374 128.188 66.297  1.00 64.75  ? 470 VAL B O     1 
ATOM   7820 C  CB    . VAL B 2 470 ? 118.914 129.582 65.479  1.00 58.78  ? 470 VAL B CB    1 
ATOM   7821 C  CG1   . VAL B 2 470 ? 118.133 128.279 65.473  1.00 59.20  ? 470 VAL B CG1   1 
ATOM   7822 C  CG2   . VAL B 2 470 ? 117.988 130.747 65.217  1.00 57.95  ? 470 VAL B CG2   1 
ATOM   7823 N  N     . LEU B 2 471 ? 120.391 128.005 68.313  1.00 54.30  ? 471 LEU B N     1 
ATOM   7824 C  CA    . LEU B 2 471 ? 121.252 126.913 68.740  1.00 53.13  ? 471 LEU B CA    1 
ATOM   7825 C  C     . LEU B 2 471 ? 121.010 125.672 67.889  1.00 58.49  ? 471 LEU B C     1 
ATOM   7826 O  O     . LEU B 2 471 ? 119.902 125.429 67.405  1.00 62.47  ? 471 LEU B O     1 
ATOM   7827 C  CB    . LEU B 2 471 ? 121.010 126.586 70.214  1.00 57.11  ? 471 LEU B CB    1 
ATOM   7828 C  CG    . LEU B 2 471 ? 121.567 127.524 71.289  1.00 59.67  ? 471 LEU B CG    1 
ATOM   7829 C  CD1   . LEU B 2 471 ? 123.031 127.817 71.036  1.00 56.07  ? 471 LEU B CD1   1 
ATOM   7830 C  CD2   . LEU B 2 471 ? 120.766 128.814 71.392  1.00 56.21  ? 471 LEU B CD2   1 
ATOM   7831 N  N     . GLN B 2 472 ? 122.072 124.888 67.696  1.00 59.21  ? 472 GLN B N     1 
ATOM   7832 C  CA    . GLN B 2 472 ? 121.930 123.629 66.973  1.00 58.56  ? 472 GLN B CA    1 
ATOM   7833 C  C     . GLN B 2 472 ? 121.046 122.654 67.738  1.00 57.33  ? 472 GLN B C     1 
ATOM   7834 O  O     . GLN B 2 472 ? 120.248 121.927 67.136  1.00 58.99  ? 472 GLN B O     1 
ATOM   7835 C  CB    . GLN B 2 472 ? 123.303 123.016 66.702  1.00 53.57  ? 472 GLN B CB    1 
ATOM   7836 C  CG    . GLN B 2 472 ? 123.358 122.197 65.428  1.00 55.21  ? 472 GLN B CG    1 
ATOM   7837 C  CD    . GLN B 2 472 ? 124.356 121.065 65.503  1.00 57.64  ? 472 GLN B CD    1 
ATOM   7838 O  OE1   . GLN B 2 472 ? 125.447 121.221 66.046  1.00 60.04  ? 472 GLN B OE1   1 
ATOM   7839 N  NE2   . GLN B 2 472 ? 123.987 119.914 64.956  1.00 52.16  ? 472 GLN B NE2   1 
ATOM   7840 N  N     . ASP B 2 473 ? 121.176 122.620 69.061  1.00 55.35  ? 473 ASP B N     1 
ATOM   7841 C  CA    . ASP B 2 473 ? 120.325 121.799 69.918  1.00 58.21  ? 473 ASP B CA    1 
ATOM   7842 C  C     . ASP B 2 473 ? 119.179 122.677 70.409  1.00 56.89  ? 473 ASP B C     1 
ATOM   7843 O  O     . ASP B 2 473 ? 119.370 123.538 71.270  1.00 59.74  ? 473 ASP B O     1 
ATOM   7844 C  CB    . ASP B 2 473 ? 121.121 121.212 71.079  1.00 64.00  ? 473 ASP B CB    1 
ATOM   7845 C  CG    . ASP B 2 473 ? 122.388 120.511 70.625  1.00 72.83  ? 473 ASP B CG    1 
ATOM   7846 O  OD1   . ASP B 2 473 ? 123.420 120.640 71.316  1.00 73.91  ? 473 ASP B OD1   1 
ATOM   7847 O  OD2   . ASP B 2 473 ? 122.353 119.828 69.580  1.00 70.43  ? 473 ASP B OD2   1 
ATOM   7848 N  N     . THR B 2 474 ? 117.990 122.460 69.854  1.00 54.40  ? 474 THR B N     1 
ATOM   7849 C  CA    . THR B 2 474 ? 116.828 123.251 70.236  1.00 51.92  ? 474 THR B CA    1 
ATOM   7850 C  C     . THR B 2 474 ? 116.428 122.958 71.676  1.00 49.69  ? 474 THR B C     1 
ATOM   7851 O  O     . THR B 2 474 ? 116.480 121.813 72.132  1.00 49.36  ? 474 THR B O     1 
ATOM   7852 C  CB    . THR B 2 474 ? 115.656 122.966 69.297  1.00 49.66  ? 474 THR B CB    1 
ATOM   7853 O  OG1   . THR B 2 474 ? 115.197 121.625 69.496  1.00 52.05  ? 474 THR B OG1   1 
ATOM   7854 C  CG2   . THR B 2 474 ? 116.079 123.136 67.849  1.00 46.99  ? 474 THR B CG2   1 
ATOM   7855 N  N     . TRP B 2 475 ? 116.028 124.004 72.396  1.00 48.99  ? 475 TRP B N     1 
ATOM   7856 C  CA    . TRP B 2 475 ? 115.647 123.880 73.794  1.00 47.90  ? 475 TRP B CA    1 
ATOM   7857 C  C     . TRP B 2 475 ? 114.482 124.809 74.092  1.00 47.86  ? 475 TRP B C     1 
ATOM   7858 O  O     . TRP B 2 475 ? 114.485 125.971 73.682  1.00 50.41  ? 475 TRP B O     1 
ATOM   7859 C  CB    . TRP B 2 475 ? 116.825 124.203 74.723  1.00 47.62  ? 475 TRP B CB    1 
ATOM   7860 C  CG    . TRP B 2 475 ? 116.457 124.272 76.173  1.00 48.98  ? 475 TRP B CG    1 
ATOM   7861 C  CD1   . TRP B 2 475 ? 116.480 123.249 77.072  1.00 45.11  ? 475 TRP B CD1   1 
ATOM   7862 C  CD2   . TRP B 2 475 ? 116.014 125.428 76.893  1.00 47.35  ? 475 TRP B CD2   1 
ATOM   7863 N  NE1   . TRP B 2 475 ? 116.076 123.693 78.305  1.00 43.35  ? 475 TRP B NE1   1 
ATOM   7864 C  CE2   . TRP B 2 475 ? 115.784 125.028 78.221  1.00 45.49  ? 475 TRP B CE2   1 
ATOM   7865 C  CE3   . TRP B 2 475 ? 115.785 126.760 76.541  1.00 47.49  ? 475 TRP B CE3   1 
ATOM   7866 C  CZ2   . TRP B 2 475 ? 115.342 125.913 79.199  1.00 46.42  ? 475 TRP B CZ2   1 
ATOM   7867 C  CZ3   . TRP B 2 475 ? 115.346 127.635 77.512  1.00 48.36  ? 475 TRP B CZ3   1 
ATOM   7868 C  CH2   . TRP B 2 475 ? 115.132 127.210 78.825  1.00 47.90  ? 475 TRP B CH2   1 
ATOM   7869 N  N     . LEU B 2 476 ? 113.491 124.287 74.813  1.00 48.39  ? 476 LEU B N     1 
ATOM   7870 C  CA    . LEU B 2 476 ? 112.349 125.061 75.273  1.00 45.04  ? 476 LEU B CA    1 
ATOM   7871 C  C     . LEU B 2 476 ? 112.134 124.796 76.755  1.00 51.94  ? 476 LEU B C     1 
ATOM   7872 O  O     . LEU B 2 476 ? 112.337 123.679 77.234  1.00 58.34  ? 476 LEU B O     1 
ATOM   7873 C  CB    . LEU B 2 476 ? 111.074 124.707 74.501  1.00 45.73  ? 476 LEU B CB    1 
ATOM   7874 C  CG    . LEU B 2 476 ? 111.111 124.806 72.979  1.00 44.47  ? 476 LEU B CG    1 
ATOM   7875 C  CD1   . LEU B 2 476 ? 109.773 124.402 72.398  1.00 45.00  ? 476 LEU B CD1   1 
ATOM   7876 C  CD2   . LEU B 2 476 ? 111.488 126.204 72.540  1.00 48.38  ? 476 LEU B CD2   1 
ATOM   7877 N  N     . PHE B 2 477 ? 111.716 125.827 77.479  1.00 50.07  ? 477 PHE B N     1 
ATOM   7878 C  CA    . PHE B 2 477 ? 111.440 125.671 78.897  1.00 51.95  ? 477 PHE B CA    1 
ATOM   7879 C  C     . PHE B 2 477 ? 109.970 125.346 79.120  1.00 60.35  ? 477 PHE B C     1 
ATOM   7880 O  O     . PHE B 2 477 ? 109.120 125.571 78.256  1.00 62.80  ? 477 PHE B O     1 
ATOM   7881 C  CB    . PHE B 2 477 ? 111.825 126.930 79.676  1.00 53.30  ? 477 PHE B CB    1 
ATOM   7882 C  CG    . PHE B 2 477 ? 110.972 128.125 79.369  1.00 61.41  ? 477 PHE B CG    1 
ATOM   7883 C  CD1   . PHE B 2 477 ? 109.865 128.423 80.146  1.00 64.56  ? 477 PHE B CD1   1 
ATOM   7884 C  CD2   . PHE B 2 477 ? 111.284 128.961 78.314  1.00 62.93  ? 477 PHE B CD2   1 
ATOM   7885 C  CE1   . PHE B 2 477 ? 109.082 129.521 79.868  1.00 63.19  ? 477 PHE B CE1   1 
ATOM   7886 C  CE2   . PHE B 2 477 ? 110.504 130.060 78.035  1.00 64.03  ? 477 PHE B CE2   1 
ATOM   7887 C  CZ    . PHE B 2 477 ? 109.402 130.340 78.812  1.00 62.08  ? 477 PHE B CZ    1 
ATOM   7888 N  N     . ALA B 2 478 ? 109.679 124.806 80.302  1.00 63.46  ? 478 ALA B N     1 
ATOM   7889 C  CA    . ALA B 2 478 ? 108.311 124.465 80.668  1.00 62.88  ? 478 ALA B CA    1 
ATOM   7890 C  C     . ALA B 2 478 ? 107.445 125.716 80.712  1.00 63.80  ? 478 ALA B C     1 
ATOM   7891 O  O     . ALA B 2 478 ? 107.626 126.577 81.577  1.00 62.46  ? 478 ALA B O     1 
ATOM   7892 C  CB    . ALA B 2 478 ? 108.280 123.742 82.015  1.00 61.20  ? 478 ALA B CB    1 
ATOM   7893 N  N     . GLY B 2 479 ? 106.509 125.824 79.779  1.00 64.22  ? 479 GLY B N     1 
ATOM   7894 C  CA    . GLY B 2 479 ? 105.670 126.999 79.695  1.00 64.17  ? 479 GLY B CA    1 
ATOM   7895 C  C     . GLY B 2 479 ? 104.898 127.000 78.393  1.00 62.36  ? 479 GLY B C     1 
ATOM   7896 O  O     . GLY B 2 479 ? 104.918 126.026 77.638  1.00 63.13  ? 479 GLY B O     1 
ATOM   7897 N  N     . THR B 2 480 ? 104.219 128.113 78.147  1.00 63.87  ? 480 THR B N     1 
ATOM   7898 C  CA    . THR B 2 480 ? 103.435 128.251 76.932  1.00 65.97  ? 480 THR B CA    1 
ATOM   7899 C  C     . THR B 2 480 ? 104.337 128.555 75.740  1.00 59.52  ? 480 THR B C     1 
ATOM   7900 O  O     . THR B 2 480 ? 105.493 128.959 75.885  1.00 58.47  ? 480 THR B O     1 
ATOM   7901 C  CB    . THR B 2 480 ? 102.385 129.351 77.088  1.00 66.86  ? 480 THR B CB    1 
ATOM   7902 O  OG1   . THR B 2 480 ? 103.035 130.617 77.243  1.00 65.23  ? 480 THR B OG1   1 
ATOM   7903 C  CG2   . THR B 2 480 ? 101.514 129.087 78.302  1.00 62.96  ? 480 THR B CG2   1 
ATOM   7904 N  N     . ILE B 2 481 ? 103.786 128.345 74.543  1.00 54.72  ? 481 ILE B N     1 
ATOM   7905 C  CA    . ILE B 2 481 ? 104.499 128.692 73.317  1.00 51.80  ? 481 ILE B CA    1 
ATOM   7906 C  C     . ILE B 2 481 ? 104.797 130.185 73.286  1.00 60.03  ? 481 ILE B C     1 
ATOM   7907 O  O     . ILE B 2 481 ? 105.881 130.613 72.866  1.00 61.92  ? 481 ILE B O     1 
ATOM   7908 C  CB    . ILE B 2 481 ? 103.681 128.246 72.091  1.00 52.05  ? 481 ILE B CB    1 
ATOM   7909 C  CG1   . ILE B 2 481 ? 103.767 126.730 71.919  1.00 48.86  ? 481 ILE B CG1   1 
ATOM   7910 C  CG2   . ILE B 2 481 ? 104.148 128.959 70.835  1.00 53.18  ? 481 ILE B CG2   1 
ATOM   7911 C  CD1   . ILE B 2 481 ? 103.040 126.210 70.704  1.00 49.93  ? 481 ILE B CD1   1 
ATOM   7912 N  N     . TYR B 2 482 ? 103.841 130.999 73.741  1.00 64.65  ? 482 TYR B N     1 
ATOM   7913 C  CA    . TYR B 2 482 ? 104.042 132.442 73.809  1.00 63.25  ? 482 TYR B CA    1 
ATOM   7914 C  C     . TYR B 2 482 ? 105.232 132.800 74.689  1.00 61.53  ? 482 TYR B C     1 
ATOM   7915 O  O     . TYR B 2 482 ? 106.059 133.640 74.321  1.00 59.21  ? 482 TYR B O     1 
ATOM   7916 C  CB    . TYR B 2 482 ? 102.775 133.113 74.335  1.00 62.94  ? 482 TYR B CB    1 
ATOM   7917 C  CG    . TYR B 2 482 ? 102.707 134.590 74.070  1.00 62.40  ? 482 TYR B CG    1 
ATOM   7918 C  CD1   . TYR B 2 482 ? 103.208 135.494 74.993  1.00 61.32  ? 482 TYR B CD1   1 
ATOM   7919 C  CD2   . TYR B 2 482 ? 102.138 135.084 72.908  1.00 67.43  ? 482 TYR B CD2   1 
ATOM   7920 C  CE1   . TYR B 2 482 ? 103.152 136.846 74.767  1.00 69.98  ? 482 TYR B CE1   1 
ATOM   7921 C  CE2   . TYR B 2 482 ? 102.074 136.439 72.672  1.00 73.22  ? 482 TYR B CE2   1 
ATOM   7922 C  CZ    . TYR B 2 482 ? 102.585 137.315 73.606  1.00 77.07  ? 482 TYR B CZ    1 
ATOM   7923 O  OH    . TYR B 2 482 ? 102.531 138.667 73.387  1.00 79.56  ? 482 TYR B OH    1 
ATOM   7924 N  N     . ASP B 2 483 ? 105.322 132.184 75.868  1.00 60.14  ? 483 ASP B N     1 
ATOM   7925 C  CA    . ASP B 2 483 ? 106.434 132.474 76.766  1.00 58.74  ? 483 ASP B CA    1 
ATOM   7926 C  C     . ASP B 2 483 ? 107.760 132.062 76.144  1.00 60.97  ? 483 ASP B C     1 
ATOM   7927 O  O     . ASP B 2 483 ? 108.760 132.779 76.262  1.00 61.94  ? 483 ASP B O     1 
ATOM   7928 C  CB    . ASP B 2 483 ? 106.223 131.767 78.104  1.00 64.37  ? 483 ASP B CB    1 
ATOM   7929 C  CG    . ASP B 2 483 ? 105.481 132.627 79.104  1.00 69.92  ? 483 ASP B CG    1 
ATOM   7930 O  OD1   . ASP B 2 483 ? 104.767 133.556 78.674  1.00 69.07  ? 483 ASP B OD1   1 
ATOM   7931 O  OD2   . ASP B 2 483 ? 105.614 132.374 80.320  1.00 67.96  ? 483 ASP B OD2   1 
ATOM   7932 N  N     . ASN B 2 484 ? 107.782 130.914 75.465  1.00 61.82  ? 484 ASN B N     1 
ATOM   7933 C  CA    . ASN B 2 484 ? 109.009 130.453 74.830  1.00 55.00  ? 484 ASN B CA    1 
ATOM   7934 C  C     . ASN B 2 484 ? 109.454 131.397 73.721  1.00 51.37  ? 484 ASN B C     1 
ATOM   7935 O  O     . ASN B 2 484 ? 110.649 131.673 73.578  1.00 52.56  ? 484 ASN B O     1 
ATOM   7936 C  CB    . ASN B 2 484 ? 108.818 129.037 74.293  1.00 51.15  ? 484 ASN B CB    1 
ATOM   7937 C  CG    . ASN B 2 484 ? 109.164 127.983 75.317  1.00 54.42  ? 484 ASN B CG    1 
ATOM   7938 O  OD1   . ASN B 2 484 ? 110.336 127.713 75.568  1.00 56.16  ? 484 ASN B OD1   1 
ATOM   7939 N  ND2   . ASN B 2 484 ? 108.148 127.385 75.919  1.00 53.66  ? 484 ASN B ND2   1 
ATOM   7940 N  N     . ILE B 2 485 ? 108.513 131.900 72.921  1.00 51.19  ? 485 ILE B N     1 
ATOM   7941 C  CA    . ILE B 2 485 ? 108.890 132.827 71.856  1.00 47.32  ? 485 ILE B CA    1 
ATOM   7942 C  C     . ILE B 2 485 ? 109.326 134.167 72.437  1.00 55.69  ? 485 ILE B C     1 
ATOM   7943 O  O     . ILE B 2 485 ? 110.307 134.764 71.979  1.00 57.97  ? 485 ILE B O     1 
ATOM   7944 C  CB    . ILE B 2 485 ? 107.740 132.993 70.849  1.00 48.99  ? 485 ILE B CB    1 
ATOM   7945 C  CG1   . ILE B 2 485 ? 107.456 131.669 70.146  1.00 48.72  ? 485 ILE B CG1   1 
ATOM   7946 C  CG2   . ILE B 2 485 ? 108.083 134.058 69.823  1.00 49.16  ? 485 ILE B CG2   1 
ATOM   7947 C  CD1   . ILE B 2 485 ? 106.245 131.714 69.262  1.00 53.09  ? 485 ILE B CD1   1 
ATOM   7948 N  N     . ALA B 2 486 ? 108.612 134.662 73.452  1.00 60.83  ? 486 ALA B N     1 
ATOM   7949 C  CA    . ALA B 2 486 ? 108.956 135.933 74.079  1.00 62.80  ? 486 ALA B CA    1 
ATOM   7950 C  C     . ALA B 2 486 ? 110.206 135.847 74.939  1.00 62.50  ? 486 ALA B C     1 
ATOM   7951 O  O     . ALA B 2 486 ? 110.701 136.885 75.387  1.00 64.76  ? 486 ALA B O     1 
ATOM   7952 C  CB    . ALA B 2 486 ? 107.785 136.438 74.922  1.00 61.00  ? 486 ALA B CB    1 
ATOM   7953 N  N     . TYR B 2 487 ? 110.714 134.639 75.187  1.00 60.71  ? 487 TYR B N     1 
ATOM   7954 C  CA    . TYR B 2 487 ? 111.981 134.480 75.892  1.00 59.88  ? 487 TYR B CA    1 
ATOM   7955 C  C     . TYR B 2 487 ? 113.107 135.251 75.215  1.00 61.87  ? 487 TYR B C     1 
ATOM   7956 O  O     . TYR B 2 487 ? 114.058 135.673 75.883  1.00 61.11  ? 487 TYR B O     1 
ATOM   7957 C  CB    . TYR B 2 487 ? 112.319 132.993 75.974  1.00 56.18  ? 487 TYR B CB    1 
ATOM   7958 C  CG    . TYR B 2 487 ? 113.417 132.628 76.937  1.00 60.45  ? 487 TYR B CG    1 
ATOM   7959 C  CD1   . TYR B 2 487 ? 114.744 132.615 76.535  1.00 62.82  ? 487 TYR B CD1   1 
ATOM   7960 C  CD2   . TYR B 2 487 ? 113.124 132.265 78.243  1.00 60.61  ? 487 TYR B CD2   1 
ATOM   7961 C  CE1   . TYR B 2 487 ? 115.749 132.267 77.410  1.00 62.97  ? 487 TYR B CE1   1 
ATOM   7962 C  CE2   . TYR B 2 487 ? 114.121 131.915 79.124  1.00 62.51  ? 487 TYR B CE2   1 
ATOM   7963 C  CZ    . TYR B 2 487 ? 115.430 131.918 78.703  1.00 65.86  ? 487 TYR B CZ    1 
ATOM   7964 O  OH    . TYR B 2 487 ? 116.426 131.572 79.580  1.00 64.52  ? 487 TYR B OH    1 
ATOM   7965 N  N     . GLY B 2 488 ? 113.025 135.438 73.897  1.00 59.27  ? 488 GLY B N     1 
ATOM   7966 C  CA    . GLY B 2 488 ? 114.040 136.217 73.206  1.00 61.24  ? 488 GLY B CA    1 
ATOM   7967 C  C     . GLY B 2 488 ? 114.057 137.672 73.631  1.00 72.71  ? 488 GLY B C     1 
ATOM   7968 O  O     . GLY B 2 488 ? 115.124 138.277 73.764  1.00 74.32  ? 488 GLY B O     1 
ATOM   7969 N  N     . ARG B 2 489 ? 112.878 138.255 73.847  1.00 76.03  ? 489 ARG B N     1 
ATOM   7970 C  CA    . ARG B 2 489 ? 112.766 139.645 74.288  1.00 76.27  ? 489 ARG B CA    1 
ATOM   7971 C  C     . ARG B 2 489 ? 111.492 139.785 75.104  1.00 76.81  ? 489 ARG B C     1 
ATOM   7972 O  O     . ARG B 2 489 ? 110.420 140.091 74.566  1.00 80.36  ? 489 ARG B O     1 
ATOM   7973 C  CB    . ARG B 2 489 ? 112.765 140.615 73.108  1.00 74.36  ? 489 ARG B CB    1 
ATOM   7974 C  CG    . ARG B 2 489 ? 112.783 142.076 73.511  1.00 77.51  ? 489 ARG B CG    1 
ATOM   7975 C  CD    . ARG B 2 489 ? 113.305 142.947 72.386  1.00 82.16  ? 489 ARG B CD    1 
ATOM   7976 N  NE    . ARG B 2 489 ? 112.667 142.630 71.115  1.00 86.23  ? 489 ARG B NE    1 
ATOM   7977 C  CZ    . ARG B 2 489 ? 111.584 143.235 70.649  1.00 88.22  ? 489 ARG B CZ    1 
ATOM   7978 N  NH1   . ARG B 2 489 ? 110.978 144.191 71.333  1.00 86.14  ? 489 ARG B NH1   1 
ATOM   7979 N  NH2   . ARG B 2 489 ? 111.097 142.873 69.466  1.00 84.02  ? 489 ARG B NH2   1 
ATOM   7980 N  N     . PRO B 2 490 ? 111.570 139.565 76.419  1.00 77.07  ? 490 PRO B N     1 
ATOM   7981 C  CA    . PRO B 2 490 ? 110.343 139.532 77.233  1.00 75.97  ? 490 PRO B CA    1 
ATOM   7982 C  C     . PRO B 2 490 ? 109.595 140.853 77.293  1.00 79.31  ? 490 PRO B C     1 
ATOM   7983 O  O     . PRO B 2 490 ? 108.396 140.850 77.597  1.00 77.87  ? 490 PRO B O     1 
ATOM   7984 C  CB    . PRO B 2 490 ? 110.854 139.113 78.618  1.00 70.93  ? 490 PRO B CB    1 
ATOM   7985 C  CG    . PRO B 2 490 ? 112.288 139.509 78.629  1.00 73.58  ? 490 PRO B CG    1 
ATOM   7986 C  CD    . PRO B 2 490 ? 112.781 139.341 77.225  1.00 73.55  ? 490 PRO B CD    1 
ATOM   7987 N  N     . ASP B 2 491 ? 110.249 141.979 77.014  1.00 81.02  ? 491 ASP B N     1 
ATOM   7988 C  CA    . ASP B 2 491 ? 109.581 143.272 77.087  1.00 85.60  ? 491 ASP B CA    1 
ATOM   7989 C  C     . ASP B 2 491 ? 108.806 143.617 75.822  1.00 86.73  ? 491 ASP B C     1 
ATOM   7990 O  O     . ASP B 2 491 ? 108.154 144.666 75.785  1.00 87.38  ? 491 ASP B O     1 
ATOM   7991 C  CB    . ASP B 2 491 ? 110.597 144.380 77.386  1.00 86.75  ? 491 ASP B CB    1 
ATOM   7992 C  CG    . ASP B 2 491 ? 111.755 144.390 76.411  1.00 88.53  ? 491 ASP B CG    1 
ATOM   7993 O  OD1   . ASP B 2 491 ? 112.774 143.725 76.689  1.00 89.13  ? 491 ASP B OD1   1 
ATOM   7994 O  OD2   . ASP B 2 491 ? 111.647 145.065 75.365  1.00 88.31  ? 491 ASP B OD2   1 
ATOM   7995 N  N     . ALA B 2 492 ? 108.860 142.775 74.795  1.00 83.52  ? 492 ALA B N     1 
ATOM   7996 C  CA    . ALA B 2 492 ? 108.126 143.041 73.567  1.00 85.78  ? 492 ALA B CA    1 
ATOM   7997 C  C     . ALA B 2 492 ? 106.625 142.907 73.795  1.00 88.45  ? 492 ALA B C     1 
ATOM   7998 O  O     . ALA B 2 492 ? 106.166 142.124 74.629  1.00 85.67  ? 492 ALA B O     1 
ATOM   7999 C  CB    . ALA B 2 492 ? 108.573 142.087 72.461  1.00 87.27  ? 492 ALA B CB    1 
ATOM   8000 N  N     . ASP B 2 493 ? 105.857 143.687 73.037  1.00 89.02  ? 493 ASP B N     1 
ATOM   8001 C  CA    . ASP B 2 493 ? 104.409 143.664 73.155  1.00 89.53  ? 493 ASP B CA    1 
ATOM   8002 C  C     . ASP B 2 493 ? 103.829 142.486 72.374  1.00 86.30  ? 493 ASP B C     1 
ATOM   8003 O  O     . ASP B 2 493 ? 104.547 141.705 71.744  1.00 87.37  ? 493 ASP B O     1 
ATOM   8004 C  CB    . ASP B 2 493 ? 103.816 144.991 72.683  1.00 93.57  ? 493 ASP B CB    1 
ATOM   8005 C  CG    . ASP B 2 493 ? 104.232 145.346 71.270  1.00 97.54  ? 493 ASP B CG    1 
ATOM   8006 O  OD1   . ASP B 2 493 ? 105.449 145.354 70.996  1.00 97.79  ? 493 ASP B OD1   1 
ATOM   8007 O  OD2   . ASP B 2 493 ? 103.343 145.617 70.436  1.00 96.16  ? 493 ASP B OD2   1 
ATOM   8008 N  N     . GLU B 2 494 ? 102.501 142.357 72.421  1.00 90.55  ? 494 GLU B N     1 
ATOM   8009 C  CA    . GLU B 2 494 ? 101.837 141.225 71.784  1.00 90.44  ? 494 GLU B CA    1 
ATOM   8010 C  C     . GLU B 2 494 ? 102.021 141.244 70.273  1.00 87.48  ? 494 GLU B C     1 
ATOM   8011 O  O     . GLU B 2 494 ? 102.218 140.193 69.651  1.00 84.44  ? 494 GLU B O     1 
ATOM   8012 C  CB    . GLU B 2 494 ? 100.350 141.223 72.140  1.00 94.15  ? 494 GLU B CB    1 
ATOM   8013 C  CG    . GLU B 2 494 ? 99.748  139.836 72.280  1.00 97.92  ? 494 GLU B CG    1 
ATOM   8014 C  CD    . GLU B 2 494 ? 98.271  139.807 71.943  1.00 108.66 ? 494 GLU B CD    1 
ATOM   8015 O  OE1   . GLU B 2 494 ? 97.446  139.815 72.881  1.00 112.16 ? 494 GLU B OE1   1 
ATOM   8016 O  OE2   . GLU B 2 494 ? 97.934  139.775 70.741  1.00 107.05 ? 494 GLU B OE2   1 
ATOM   8017 N  N     . ASP B 2 495 ? 101.948 142.428 69.663  1.00 89.93  ? 495 ASP B N     1 
ATOM   8018 C  CA    . ASP B 2 495 ? 102.061 142.516 68.212  1.00 89.74  ? 495 ASP B CA    1 
ATOM   8019 C  C     . ASP B 2 495 ? 103.429 142.048 67.733  1.00 86.14  ? 495 ASP B C     1 
ATOM   8020 O  O     . ASP B 2 495 ? 103.530 141.348 66.721  1.00 86.39  ? 495 ASP B O     1 
ATOM   8021 C  CB    . ASP B 2 495 ? 101.785 143.946 67.751  1.00 96.91  ? 495 ASP B CB    1 
ATOM   8022 C  CG    . ASP B 2 495 ? 100.396 144.419 68.127  1.00 103.90 ? 495 ASP B CG    1 
ATOM   8023 O  OD1   . ASP B 2 495 ? 99.840  143.900 69.118  1.00 101.64 ? 495 ASP B OD1   1 
ATOM   8024 O  OD2   . ASP B 2 495 ? 99.858  145.306 67.432  1.00 104.20 ? 495 ASP B OD2   1 
ATOM   8025 N  N     . GLU B 2 496 ? 104.492 142.418 68.449  1.00 86.15  ? 496 GLU B N     1 
ATOM   8026 C  CA    . GLU B 2 496 ? 105.832 141.996 68.051  1.00 87.97  ? 496 GLU B CA    1 
ATOM   8027 C  C     . GLU B 2 496 ? 106.002 140.484 68.166  1.00 84.57  ? 496 GLU B C     1 
ATOM   8028 O  O     . GLU B 2 496 ? 106.584 139.853 67.277  1.00 83.71  ? 496 GLU B O     1 
ATOM   8029 C  CB    . GLU B 2 496 ? 106.883 142.722 68.889  1.00 87.56  ? 496 GLU B CB    1 
ATOM   8030 C  CG    . GLU B 2 496 ? 107.071 144.178 68.501  1.00 89.23  ? 496 GLU B CG    1 
ATOM   8031 C  CD    . GLU B 2 496 ? 108.527 144.591 68.472  1.00 96.85  ? 496 GLU B CD    1 
ATOM   8032 O  OE1   . GLU B 2 496 ? 109.117 144.776 69.558  1.00 95.07  ? 496 GLU B OE1   1 
ATOM   8033 O  OE2   . GLU B 2 496 ? 109.083 144.731 67.362  1.00 100.60 ? 496 GLU B OE2   1 
ATOM   8034 N  N     . VAL B 2 497 ? 105.503 139.886 69.250  1.00 80.02  ? 497 VAL B N     1 
ATOM   8035 C  CA    . VAL B 2 497 ? 105.607 138.438 69.411  1.00 72.23  ? 497 VAL B CA    1 
ATOM   8036 C  C     . VAL B 2 497 ? 104.815 137.723 68.325  1.00 71.11  ? 497 VAL B C     1 
ATOM   8037 O  O     . VAL B 2 497 ? 105.277 136.730 67.749  1.00 72.19  ? 497 VAL B O     1 
ATOM   8038 C  CB    . VAL B 2 497 ? 105.143 138.016 70.817  1.00 73.50  ? 497 VAL B CB    1 
ATOM   8039 C  CG1   . VAL B 2 497 ? 105.201 136.505 70.961  1.00 61.76  ? 497 VAL B CG1   1 
ATOM   8040 C  CG2   . VAL B 2 497 ? 105.996 138.684 71.879  1.00 75.12  ? 497 VAL B CG2   1 
ATOM   8041 N  N     . ILE B 2 498 ? 103.609 138.213 68.030  1.00 74.11  ? 498 ILE B N     1 
ATOM   8042 C  CA    . ILE B 2 498 ? 102.789 137.591 66.995  1.00 75.11  ? 498 ILE B CA    1 
ATOM   8043 C  C     . ILE B 2 498 ? 103.462 137.719 65.634  1.00 76.46  ? 498 ILE B C     1 
ATOM   8044 O  O     . ILE B 2 498 ? 103.445 136.782 64.828  1.00 78.00  ? 498 ILE B O     1 
ATOM   8045 C  CB    . ILE B 2 498 ? 101.371 138.196 66.997  1.00 78.21  ? 498 ILE B CB    1 
ATOM   8046 C  CG1   . ILE B 2 498 ? 100.418 137.330 67.825  1.00 77.43  ? 498 ILE B CG1   1 
ATOM   8047 C  CG2   . ILE B 2 498 ? 100.834 138.351 65.580  1.00 74.52  ? 498 ILE B CG2   1 
ATOM   8048 C  CD1   . ILE B 2 498 ? 100.781 137.232 69.290  1.00 76.43  ? 498 ILE B CD1   1 
ATOM   8049 N  N     . GLU B 2 499 ? 104.068 138.875 65.356  1.00 75.48  ? 499 GLU B N     1 
ATOM   8050 C  CA    . GLU B 2 499 ? 104.758 139.062 64.084  1.00 78.28  ? 499 GLU B CA    1 
ATOM   8051 C  C     . GLU B 2 499 ? 105.973 138.151 63.970  1.00 76.89  ? 499 GLU B C     1 
ATOM   8052 O  O     . GLU B 2 499 ? 106.239 137.596 62.898  1.00 76.17  ? 499 GLU B O     1 
ATOM   8053 C  CB    . GLU B 2 499 ? 105.162 140.526 63.918  1.00 82.86  ? 499 GLU B CB    1 
ATOM   8054 C  CG    . GLU B 2 499 ? 105.188 141.002 62.475  1.00 89.13  ? 499 GLU B CG    1 
ATOM   8055 C  CD    . GLU B 2 499 ? 103.894 140.713 61.736  1.00 94.23  ? 499 GLU B CD    1 
ATOM   8056 O  OE1   . GLU B 2 499 ? 102.811 140.862 62.339  1.00 95.63  ? 499 GLU B OE1   1 
ATOM   8057 O  OE2   . GLU B 2 499 ? 103.962 140.335 60.548  1.00 90.69  ? 499 GLU B OE2   1 
ATOM   8058 N  N     . ALA B 2 500 ? 106.730 137.996 65.058  1.00 77.47  ? 500 ALA B N     1 
ATOM   8059 C  CA    . ALA B 2 500 ? 107.871 137.085 65.041  1.00 71.61  ? 500 ALA B CA    1 
ATOM   8060 C  C     . ALA B 2 500 ? 107.423 135.645 64.827  1.00 67.19  ? 500 ALA B C     1 
ATOM   8061 O  O     . ALA B 2 500 ? 108.068 134.889 64.093  1.00 63.02  ? 500 ALA B O     1 
ATOM   8062 C  CB    . ALA B 2 500 ? 108.667 137.214 66.339  1.00 67.00  ? 500 ALA B CB    1 
ATOM   8063 N  N     . ALA B 2 501 ? 106.323 135.245 65.467  1.00 71.11  ? 501 ALA B N     1 
ATOM   8064 C  CA    . ALA B 2 501 ? 105.799 133.898 65.265  1.00 67.41  ? 501 ALA B CA    1 
ATOM   8065 C  C     . ALA B 2 501 ? 105.325 133.695 63.830  1.00 67.86  ? 501 ALA B C     1 
ATOM   8066 O  O     . ALA B 2 501 ? 105.563 132.638 63.235  1.00 70.43  ? 501 ALA B O     1 
ATOM   8067 C  CB    . ALA B 2 501 ? 104.665 133.624 66.251  1.00 65.03  ? 501 ALA B CB    1 
ATOM   8068 N  N     . THR B 2 502 ? 104.647 134.693 63.262  1.00 72.83  ? 502 THR B N     1 
ATOM   8069 C  CA    . THR B 2 502 ? 104.146 134.577 61.895  1.00 75.10  ? 502 THR B CA    1 
ATOM   8070 C  C     . THR B 2 502 ? 105.286 134.527 60.886  1.00 74.02  ? 502 THR B C     1 
ATOM   8071 O  O     . THR B 2 502 ? 105.233 133.760 59.918  1.00 74.95  ? 502 THR B O     1 
ATOM   8072 C  CB    . THR B 2 502 ? 103.204 135.741 61.584  1.00 77.20  ? 502 THR B CB    1 
ATOM   8073 O  OG1   . THR B 2 502 ? 102.073 135.689 62.462  1.00 80.27  ? 502 THR B OG1   1 
ATOM   8074 C  CG2   . THR B 2 502 ? 102.718 135.675 60.145  1.00 69.42  ? 502 THR B CG2   1 
ATOM   8075 N  N     . ALA B 2 503 ? 106.324 135.339 61.096  1.00 73.52  ? 503 ALA B N     1 
ATOM   8076 C  CA    . ALA B 2 503 ? 107.446 135.370 60.165  1.00 75.25  ? 503 ALA B CA    1 
ATOM   8077 C  C     . ALA B 2 503 ? 108.168 134.030 60.121  1.00 80.54  ? 503 ALA B C     1 
ATOM   8078 O  O     . ALA B 2 503 ? 108.559 133.561 59.046  1.00 79.87  ? 503 ALA B O     1 
ATOM   8079 C  CB    . ALA B 2 503 ? 108.409 136.490 60.550  1.00 76.19  ? 503 ALA B CB    1 
ATOM   8080 N  N     . ALA B 2 504 ? 108.353 133.398 61.277  1.00 78.83  ? 504 ALA B N     1 
ATOM   8081 C  CA    . ALA B 2 504 ? 108.954 132.074 61.356  1.00 67.02  ? 504 ALA B CA    1 
ATOM   8082 C  C     . ALA B 2 504 ? 107.949 130.961 61.114  1.00 65.37  ? 504 ALA B C     1 
ATOM   8083 O  O     . ALA B 2 504 ? 108.297 129.787 61.268  1.00 65.18  ? 504 ALA B O     1 
ATOM   8084 C  CB    . ALA B 2 504 ? 109.624 131.880 62.717  1.00 57.79  ? 504 ALA B CB    1 
ATOM   8085 N  N     . TYR B 2 505 ? 106.713 131.313 60.758  1.00 68.59  ? 505 TYR B N     1 
ATOM   8086 C  CA    . TYR B 2 505 ? 105.646 130.354 60.473  1.00 69.21  ? 505 TYR B CA    1 
ATOM   8087 C  C     . TYR B 2 505 ? 105.314 129.494 61.687  1.00 66.43  ? 505 TYR B C     1 
ATOM   8088 O  O     . TYR B 2 505 ? 104.832 128.367 61.554  1.00 64.91  ? 505 TYR B O     1 
ATOM   8089 C  CB    . TYR B 2 505 ? 105.988 129.491 59.257  1.00 74.77  ? 505 TYR B CB    1 
ATOM   8090 C  CG    . TYR B 2 505 ? 105.663 130.194 57.962  1.00 81.28  ? 505 TYR B CG    1 
ATOM   8091 C  CD1   . TYR B 2 505 ? 106.534 131.130 57.424  1.00 80.92  ? 505 TYR B CD1   1 
ATOM   8092 C  CD2   . TYR B 2 505 ? 104.476 129.941 57.291  1.00 83.85  ? 505 TYR B CD2   1 
ATOM   8093 C  CE1   . TYR B 2 505 ? 106.237 131.788 56.251  1.00 84.61  ? 505 TYR B CE1   1 
ATOM   8094 C  CE2   . TYR B 2 505 ? 104.172 130.592 56.113  1.00 88.07  ? 505 TYR B CE2   1 
ATOM   8095 C  CZ    . TYR B 2 505 ? 105.056 131.513 55.597  1.00 88.54  ? 505 TYR B CZ    1 
ATOM   8096 O  OH    . TYR B 2 505 ? 104.758 132.165 54.422  1.00 88.31  ? 505 TYR B OH    1 
ATOM   8097 N  N     . VAL B 2 506 ? 105.578 130.026 62.881  1.00 65.45  ? 506 VAL B N     1 
ATOM   8098 C  CA    . VAL B 2 506 ? 105.043 129.428 64.097  1.00 63.78  ? 506 VAL B CA    1 
ATOM   8099 C  C     . VAL B 2 506 ? 103.535 129.623 64.156  1.00 67.70  ? 506 VAL B C     1 
ATOM   8100 O  O     . VAL B 2 506 ? 102.794 128.739 64.602  1.00 72.88  ? 506 VAL B O     1 
ATOM   8101 C  CB    . VAL B 2 506 ? 105.742 130.020 65.333  1.00 60.63  ? 506 VAL B CB    1 
ATOM   8102 C  CG1   . VAL B 2 506 ? 105.096 129.515 66.607  1.00 57.12  ? 506 VAL B CG1   1 
ATOM   8103 C  CG2   . VAL B 2 506 ? 107.217 129.681 65.315  1.00 61.41  ? 506 VAL B CG2   1 
ATOM   8104 N  N     . ASP B 2 507 ? 103.057 130.782 63.696  1.00 69.60  ? 507 ASP B N     1 
ATOM   8105 C  CA    . ASP B 2 507 ? 101.632 131.088 63.747  1.00 73.00  ? 507 ASP B CA    1 
ATOM   8106 C  C     . ASP B 2 507 ? 100.811 130.100 62.931  1.00 76.08  ? 507 ASP B C     1 
ATOM   8107 O  O     . ASP B 2 507 ? 99.675  129.783 63.303  1.00 80.70  ? 507 ASP B O     1 
ATOM   8108 C  CB    . ASP B 2 507 ? 101.396 132.514 63.251  1.00 79.33  ? 507 ASP B CB    1 
ATOM   8109 C  CG    . ASP B 2 507 ? 100.000 133.016 63.552  1.00 87.51  ? 507 ASP B CG    1 
ATOM   8110 O  OD1   . ASP B 2 507 ? 99.731  133.350 64.725  1.00 88.14  ? 507 ASP B OD1   1 
ATOM   8111 O  OD2   . ASP B 2 507 ? 99.178  133.085 62.616  1.00 87.00  ? 507 ASP B OD2   1 
ATOM   8112 N  N     . ARG B 2 508 ? 101.373 129.589 61.832  1.00 74.06  ? 508 ARG B N     1 
ATOM   8113 C  CA    . ARG B 2 508 ? 100.618 128.701 60.952  1.00 74.41  ? 508 ARG B CA    1 
ATOM   8114 C  C     . ARG B 2 508 ? 100.204 127.421 61.666  1.00 71.85  ? 508 ARG B C     1 
ATOM   8115 O  O     . ARG B 2 508 ? 99.067  126.961 61.515  1.00 73.97  ? 508 ARG B O     1 
ATOM   8116 C  CB    . ARG B 2 508 ? 101.439 128.383 59.703  1.00 79.14  ? 508 ARG B CB    1 
ATOM   8117 C  CG    . ARG B 2 508 ? 100.669 127.635 58.628  1.00 82.22  ? 508 ARG B CG    1 
ATOM   8118 C  CD    . ARG B 2 508 ? 101.382 126.359 58.225  1.00 89.33  ? 508 ARG B CD    1 
ATOM   8119 N  NE    . ARG B 2 508 ? 102.488 126.629 57.313  1.00 99.34  ? 508 ARG B NE    1 
ATOM   8120 C  CZ    . ARG B 2 508 ? 103.498 125.800 57.092  1.00 97.66  ? 508 ARG B CZ    1 
ATOM   8121 N  NH1   . ARG B 2 508 ? 103.577 124.628 57.700  1.00 92.33  ? 508 ARG B NH1   1 
ATOM   8122 N  NH2   . ARG B 2 508 ? 104.453 126.155 56.238  1.00 96.54  ? 508 ARG B NH2   1 
ATOM   8123 N  N     . PHE B 2 509 ? 101.106 126.826 62.448  1.00 69.69  ? 509 PHE B N     1 
ATOM   8124 C  CA    . PHE B 2 509 ? 100.744 125.641 63.213  1.00 69.28  ? 509 PHE B CA    1 
ATOM   8125 C  C     . PHE B 2 509 ? 100.177 125.970 64.585  1.00 73.94  ? 509 PHE B C     1 
ATOM   8126 O  O     . PHE B 2 509 ? 99.546  125.104 65.200  1.00 78.40  ? 509 PHE B O     1 
ATOM   8127 C  CB    . PHE B 2 509 ? 101.949 124.694 63.346  1.00 67.56  ? 509 PHE B CB    1 
ATOM   8128 C  CG    . PHE B 2 509 ? 102.913 125.052 64.450  1.00 65.82  ? 509 PHE B CG    1 
ATOM   8129 C  CD1   . PHE B 2 509 ? 102.719 124.595 65.744  1.00 63.72  ? 509 PHE B CD1   1 
ATOM   8130 C  CD2   . PHE B 2 509 ? 104.046 125.799 64.178  1.00 62.23  ? 509 PHE B CD2   1 
ATOM   8131 C  CE1   . PHE B 2 509 ? 103.610 124.914 66.748  1.00 60.90  ? 509 PHE B CE1   1 
ATOM   8132 C  CE2   . PHE B 2 509 ? 104.943 126.113 65.179  1.00 54.02  ? 509 PHE B CE2   1 
ATOM   8133 C  CZ    . PHE B 2 509 ? 104.724 125.672 66.463  1.00 55.80  ? 509 PHE B CZ    1 
ATOM   8134 N  N     . VAL B 2 510 ? 100.388 127.190 65.080  1.00 76.42  ? 510 VAL B N     1 
ATOM   8135 C  CA    . VAL B 2 510 ? 99.780  127.589 66.345  1.00 78.30  ? 510 VAL B CA    1 
ATOM   8136 C  C     . VAL B 2 510 ? 98.276  127.775 66.180  1.00 83.61  ? 510 VAL B C     1 
ATOM   8137 O  O     . VAL B 2 510 ? 97.492  127.408 67.063  1.00 85.20  ? 510 VAL B O     1 
ATOM   8138 C  CB    . VAL B 2 510 ? 100.466 128.856 66.886  1.00 77.07  ? 510 VAL B CB    1 
ATOM   8139 C  CG1   . VAL B 2 510 ? 99.544  129.612 67.812  1.00 81.10  ? 510 VAL B CG1   1 
ATOM   8140 C  CG2   . VAL B 2 510 ? 101.741 128.484 67.619  1.00 71.04  ? 510 VAL B CG2   1 
ATOM   8141 N  N     . HIS B 2 511 ? 97.849  128.340 65.046  1.00 84.43  ? 511 HIS B N     1 
ATOM   8142 C  CA    . HIS B 2 511 ? 96.423  128.531 64.800  1.00 89.00  ? 511 HIS B CA    1 
ATOM   8143 C  C     . HIS B 2 511 ? 95.666  127.211 64.792  1.00 92.53  ? 511 HIS B C     1 
ATOM   8144 O  O     . HIS B 2 511 ? 94.487  127.170 65.163  1.00 95.66  ? 511 HIS B O     1 
ATOM   8145 C  CB    . HIS B 2 511 ? 96.210  129.265 63.477  1.00 87.07  ? 511 HIS B CB    1 
ATOM   8146 C  CG    . HIS B 2 511 ? 96.421  130.744 63.567  1.00 95.56  ? 511 HIS B CG    1 
ATOM   8147 N  ND1   . HIS B 2 511 ? 96.653  131.390 64.761  1.00 98.21  ? 511 HIS B ND1   1 
ATOM   8148 C  CD2   . HIS B 2 511 ? 96.430  131.703 62.611  1.00 95.09  ? 511 HIS B CD2   1 
ATOM   8149 C  CE1   . HIS B 2 511 ? 96.797  132.684 64.538  1.00 97.13  ? 511 HIS B CE1   1 
ATOM   8150 N  NE2   . HIS B 2 511 ? 96.668  132.900 63.241  1.00 97.79  ? 511 HIS B NE2   1 
ATOM   8151 N  N     . THR B 2 512 ? 96.317  126.126 64.367  1.00 89.55  ? 512 THR B N     1 
ATOM   8152 C  CA    . THR B 2 512 ? 95.661  124.823 64.358  1.00 87.91  ? 512 THR B CA    1 
ATOM   8153 C  C     . THR B 2 512 ? 95.336  124.355 65.772  1.00 86.78  ? 512 THR B C     1 
ATOM   8154 O  O     . THR B 2 512 ? 94.250  123.818 66.018  1.00 90.24  ? 512 THR B O     1 
ATOM   8155 C  CB    . THR B 2 512 ? 96.545  123.803 63.637  1.00 86.94  ? 512 THR B CB    1 
ATOM   8156 O  OG1   . THR B 2 512 ? 96.370  123.935 62.221  1.00 86.20  ? 512 THR B OG1   1 
ATOM   8157 C  CG2   . THR B 2 512 ? 96.194  122.382 64.055  1.00 87.24  ? 512 THR B CG2   1 
ATOM   8158 N  N     . LEU B 2 513 ? 96.250  124.568 66.713  1.00 84.23  ? 513 LEU B N     1 
ATOM   8159 C  CA    . LEU B 2 513 ? 96.056  124.064 68.064  1.00 87.94  ? 513 LEU B CA    1 
ATOM   8160 C  C     . LEU B 2 513 ? 94.884  124.775 68.737  1.00 91.14  ? 513 LEU B C     1 
ATOM   8161 O  O     . LEU B 2 513 ? 94.653  125.963 68.494  1.00 91.11  ? 513 LEU B O     1 
ATOM   8162 C  CB    . LEU B 2 513 ? 97.326  124.251 68.893  1.00 87.79  ? 513 LEU B CB    1 
ATOM   8163 C  CG    . LEU B 2 513 ? 98.649  123.967 68.179  1.00 87.59  ? 513 LEU B CG    1 
ATOM   8164 C  CD1   . LEU B 2 513 ? 99.779  124.766 68.805  1.00 82.77  ? 513 LEU B CD1   1 
ATOM   8165 C  CD2   . LEU B 2 513 ? 98.966  122.482 68.202  1.00 79.93  ? 513 LEU B CD2   1 
ATOM   8166 N  N     . PRO B 2 514 ? 94.123  124.074 69.585  1.00 94.21  ? 514 PRO B N     1 
ATOM   8167 C  CA    . PRO B 2 514 ? 92.991  124.719 70.270  1.00 93.70  ? 514 PRO B CA    1 
ATOM   8168 C  C     . PRO B 2 514 ? 93.401  125.716 71.343  1.00 94.99  ? 514 PRO B C     1 
ATOM   8169 O  O     . PRO B 2 514 ? 92.530  126.427 71.860  1.00 96.86  ? 514 PRO B O     1 
ATOM   8170 C  CB    . PRO B 2 514 ? 92.230  123.535 70.879  1.00 90.63  ? 514 PRO B CB    1 
ATOM   8171 C  CG    . PRO B 2 514 ? 93.255  122.463 71.025  1.00 85.62  ? 514 PRO B CG    1 
ATOM   8172 C  CD    . PRO B 2 514 ? 94.200  122.632 69.874  1.00 91.32  ? 514 PRO B CD    1 
ATOM   8173 N  N     . ASN B 2 515 ? 94.684  125.795 71.694  1.00 93.45  ? 515 ASN B N     1 
ATOM   8174 C  CA    . ASN B 2 515 ? 95.148  126.744 72.699  1.00 89.56  ? 515 ASN B CA    1 
ATOM   8175 C  C     . ASN B 2 515 ? 96.260  127.615 72.132  1.00 88.96  ? 515 ASN B C     1 
ATOM   8176 O  O     . ASN B 2 515 ? 97.326  127.738 72.742  1.00 85.32  ? 515 ASN B O     1 
ATOM   8177 C  CB    . ASN B 2 515 ? 95.642  126.021 73.954  1.00 88.01  ? 515 ASN B CB    1 
ATOM   8178 C  CG    . ASN B 2 515 ? 94.838  124.780 74.267  1.00 92.63  ? 515 ASN B CG    1 
ATOM   8179 O  OD1   . ASN B 2 515 ? 94.758  123.859 73.455  1.00 89.42  ? 515 ASN B OD1   1 
ATOM   8180 N  ND2   . ASN B 2 515 ? 94.243  124.743 75.453  1.00 89.59  ? 515 ASN B ND2   1 
ATOM   8181 N  N     . GLY B 2 516 ? 96.026  128.196 70.955  1.00 90.20  ? 516 GLY B N     1 
ATOM   8182 C  CA    . GLY B 2 516 ? 97.013  129.001 70.261  1.00 87.47  ? 516 GLY B CA    1 
ATOM   8183 C  C     . GLY B 2 516 ? 97.779  129.977 71.131  1.00 85.30  ? 516 GLY B C     1 
ATOM   8184 O  O     . GLY B 2 516 ? 97.188  130.866 71.752  1.00 85.48  ? 516 GLY B O     1 
ATOM   8185 N  N     . TYR B 2 517 ? 99.099  129.781 71.199  1.00 78.02  ? 517 TYR B N     1 
ATOM   8186 C  CA    . TYR B 2 517 ? 100.039 130.594 71.968  1.00 71.19  ? 517 TYR B CA    1 
ATOM   8187 C  C     . TYR B 2 517 ? 99.887  130.349 73.464  1.00 76.24  ? 517 TYR B C     1 
ATOM   8188 O  O     . TYR B 2 517 ? 100.698 130.828 74.261  1.00 75.60  ? 517 TYR B O     1 
ATOM   8189 C  CB    . TYR B 2 517 ? 99.873  132.085 71.662  1.00 71.16  ? 517 TYR B CB    1 
ATOM   8190 C  CG    . TYR B 2 517 ? 100.266 132.479 70.260  1.00 76.23  ? 517 TYR B CG    1 
ATOM   8191 C  CD1   . TYR B 2 517 ? 99.302  132.791 69.314  1.00 78.47  ? 517 TYR B CD1   1 
ATOM   8192 C  CD2   . TYR B 2 517 ? 101.600 132.537 69.882  1.00 72.29  ? 517 TYR B CD2   1 
ATOM   8193 C  CE1   . TYR B 2 517 ? 99.653  133.153 68.031  1.00 78.69  ? 517 TYR B CE1   1 
ATOM   8194 C  CE2   . TYR B 2 517 ? 101.960 132.897 68.599  1.00 75.45  ? 517 TYR B CE2   1 
ATOM   8195 C  CZ    . TYR B 2 517 ? 100.981 133.203 67.678  1.00 79.35  ? 517 TYR B CZ    1 
ATOM   8196 O  OH    . TYR B 2 517 ? 101.330 133.563 66.399  1.00 80.00  ? 517 TYR B OH    1 
ATOM   8197 N  N     . ASP B 2 518 ? 98.868  129.588 73.857  1.00 79.64  ? 518 ASP B N     1 
ATOM   8198 C  CA    . ASP B 2 518 ? 98.632  129.273 75.256  1.00 78.44  ? 518 ASP B CA    1 
ATOM   8199 C  C     . ASP B 2 518 ? 98.872  127.809 75.585  1.00 78.29  ? 518 ASP B C     1 
ATOM   8200 O  O     . ASP B 2 518 ? 98.902  127.455 76.768  1.00 78.37  ? 518 ASP B O     1 
ATOM   8201 C  CB    . ASP B 2 518 ? 97.199  129.653 75.654  1.00 84.80  ? 518 ASP B CB    1 
ATOM   8202 C  CG    . ASP B 2 518 ? 96.997  131.151 75.740  1.00 87.46  ? 518 ASP B CG    1 
ATOM   8203 O  OD1   . ASP B 2 518 ? 97.998  131.877 75.919  1.00 83.19  ? 518 ASP B OD1   1 
ATOM   8204 O  OD2   . ASP B 2 518 ? 95.839  131.604 75.629  1.00 83.89  ? 518 ASP B OD2   1 
ATOM   8205 N  N     . THR B 2 519 ? 99.033  126.956 74.578  1.00 75.75  ? 519 THR B N     1 
ATOM   8206 C  CA    . THR B 2 519 ? 99.377  125.565 74.822  1.00 72.31  ? 519 THR B CA    1 
ATOM   8207 C  C     . THR B 2 519 ? 100.778 125.465 75.409  1.00 68.88  ? 519 THR B C     1 
ATOM   8208 O  O     . THR B 2 519 ? 101.703 126.154 74.974  1.00 67.37  ? 519 THR B O     1 
ATOM   8209 C  CB    . THR B 2 519 ? 99.287  124.765 73.525  1.00 70.91  ? 519 THR B CB    1 
ATOM   8210 O  OG1   . THR B 2 519 ? 100.035 123.549 73.655  1.00 71.57  ? 519 THR B OG1   1 
ATOM   8211 C  CG2   . THR B 2 519 ? 99.825  125.576 72.366  1.00 68.66  ? 519 THR B CG2   1 
ATOM   8212 N  N     . ARG B 2 520 ? 100.931 124.600 76.407  1.00 67.08  ? 520 ARG B N     1 
ATOM   8213 C  CA    . ARG B 2 520 ? 102.183 124.485 77.138  1.00 65.85  ? 520 ARG B CA    1 
ATOM   8214 C  C     . ARG B 2 520 ? 103.105 123.486 76.454  1.00 68.99  ? 520 ARG B C     1 
ATOM   8215 O  O     . ARG B 2 520 ? 102.686 122.377 76.109  1.00 70.50  ? 520 ARG B O     1 
ATOM   8216 C  CB    . ARG B 2 520 ? 101.926 124.061 78.584  1.00 65.99  ? 520 ARG B CB    1 
ATOM   8217 C  CG    . ARG B 2 520 ? 101.061 125.029 79.360  1.00 66.45  ? 520 ARG B CG    1 
ATOM   8218 C  CD    . ARG B 2 520 ? 101.074 124.707 80.840  1.00 68.78  ? 520 ARG B CD    1 
ATOM   8219 N  NE    . ARG B 2 520 ? 102.336 125.079 81.467  1.00 74.10  ? 520 ARG B NE    1 
ATOM   8220 C  CZ    . ARG B 2 520 ? 102.644 126.308 81.855  1.00 71.52  ? 520 ARG B CZ    1 
ATOM   8221 N  NH1   . ARG B 2 520 ? 101.811 127.319 81.674  1.00 66.09  ? 520 ARG B NH1   1 
ATOM   8222 N  NH2   . ARG B 2 520 ? 103.819 126.529 82.439  1.00 63.58  ? 520 ARG B NH2   1 
ATOM   8223 N  N     . VAL B 2 521 ? 104.362 123.884 76.266  1.00 66.70  ? 521 VAL B N     1 
ATOM   8224 C  CA    . VAL B 2 521 ? 105.373 123.042 75.647  1.00 66.02  ? 521 VAL B CA    1 
ATOM   8225 C  C     . VAL B 2 521 ? 106.532 122.880 76.623  1.00 68.88  ? 521 VAL B C     1 
ATOM   8226 O  O     . VAL B 2 521 ? 106.624 123.569 77.638  1.00 70.93  ? 521 VAL B O     1 
ATOM   8227 C  CB    . VAL B 2 521 ? 105.863 123.605 74.301  1.00 62.33  ? 521 VAL B CB    1 
ATOM   8228 C  CG1   . VAL B 2 521 ? 104.765 123.511 73.259  1.00 61.84  ? 521 VAL B CG1   1 
ATOM   8229 C  CG2   . VAL B 2 521 ? 106.324 125.037 74.463  1.00 59.50  ? 521 VAL B CG2   1 
ATOM   8230 N  N     . ASP B 2 522 ? 107.422 121.946 76.300  1.00 72.70  ? 522 ASP B N     1 
ATOM   8231 C  CA    . ASP B 2 522 ? 108.535 121.609 77.173  1.00 71.59  ? 522 ASP B CA    1 
ATOM   8232 C  C     . ASP B 2 522 ? 109.690 121.102 76.322  1.00 75.23  ? 522 ASP B C     1 
ATOM   8233 O  O     . ASP B 2 522 ? 109.534 120.815 75.133  1.00 71.61  ? 522 ASP B O     1 
ATOM   8234 C  CB    . ASP B 2 522 ? 108.124 120.568 78.220  1.00 73.70  ? 522 ASP B CB    1 
ATOM   8235 C  CG    . ASP B 2 522 ? 108.983 120.624 79.465  1.00 82.17  ? 522 ASP B CG    1 
ATOM   8236 O  OD1   . ASP B 2 522 ? 109.913 121.456 79.508  1.00 78.93  ? 522 ASP B OD1   1 
ATOM   8237 O  OD2   . ASP B 2 522 ? 108.726 119.838 80.401  1.00 85.64  ? 522 ASP B OD2   1 
ATOM   8238 N  N     . ASP B 2 523 ? 110.864 121.005 76.949  1.00 72.53  ? 523 ASP B N     1 
ATOM   8239 C  CA    . ASP B 2 523 ? 112.041 120.521 76.235  1.00 69.20  ? 523 ASP B CA    1 
ATOM   8240 C  C     . ASP B 2 523 ? 111.878 119.068 75.811  1.00 74.18  ? 523 ASP B C     1 
ATOM   8241 O  O     . ASP B 2 523 ? 112.214 118.702 74.679  1.00 75.73  ? 523 ASP B O     1 
ATOM   8242 C  CB    . ASP B 2 523 ? 113.286 120.683 77.104  1.00 62.44  ? 523 ASP B CB    1 
ATOM   8243 C  CG    . ASP B 2 523 ? 114.566 120.560 76.309  1.00 65.62  ? 523 ASP B CG    1 
ATOM   8244 O  OD1   . ASP B 2 523 ? 114.579 120.991 75.138  1.00 59.55  ? 523 ASP B OD1   1 
ATOM   8245 O  OD2   . ASP B 2 523 ? 115.558 120.033 76.853  1.00 75.08  ? 523 ASP B OD2   1 
ATOM   8246 N  N     . ASP B 2 524 ? 111.359 118.226 76.700  1.00 75.46  ? 524 ASP B N     1 
ATOM   8247 C  CA    . ASP B 2 524 ? 111.245 116.798 76.443  1.00 80.05  ? 524 ASP B CA    1 
ATOM   8248 C  C     . ASP B 2 524 ? 109.871 116.386 75.935  1.00 79.44  ? 524 ASP B C     1 
ATOM   8249 O  O     . ASP B 2 524 ? 109.634 115.190 75.742  1.00 78.35  ? 524 ASP B O     1 
ATOM   8250 C  CB    . ASP B 2 524 ? 111.577 116.008 77.712  1.00 82.90  ? 524 ASP B CB    1 
ATOM   8251 C  CG    . ASP B 2 524 ? 110.973 116.624 78.957  1.00 81.40  ? 524 ASP B CG    1 
ATOM   8252 O  OD1   . ASP B 2 524 ? 110.758 117.853 78.968  1.00 79.88  ? 524 ASP B OD1   1 
ATOM   8253 O  OD2   . ASP B 2 524 ? 110.710 115.877 79.922  1.00 77.45  ? 524 ASP B OD2   1 
ATOM   8254 N  N     . GLY B 2 525 ? 108.964 117.333 75.714  1.00 79.38  ? 525 GLY B N     1 
ATOM   8255 C  CA    . GLY B 2 525 ? 107.631 116.980 75.270  1.00 79.04  ? 525 GLY B CA    1 
ATOM   8256 C  C     . GLY B 2 525 ? 106.752 118.156 74.901  1.00 85.42  ? 525 GLY B C     1 
ATOM   8257 O  O     . GLY B 2 525 ? 107.227 119.152 74.348  1.00 85.89  ? 525 GLY B O     1 
ATOM   8258 N  N     . GLY B 2 526 ? 105.468 118.047 75.203  1.00 89.09  ? 526 GLY B N     1 
ATOM   8259 C  CA    . GLY B 2 526 ? 104.487 119.046 74.835  1.00 80.60  ? 526 GLY B CA    1 
ATOM   8260 C  C     . GLY B 2 526 ? 103.713 118.628 73.598  1.00 72.06  ? 526 GLY B C     1 
ATOM   8261 O  O     . GLY B 2 526 ? 103.805 117.497 73.117  1.00 67.83  ? 526 GLY B O     1 
ATOM   8262 N  N     . ALA B 2 527 ? 102.945 119.582 73.071  1.00 68.38  ? 527 ALA B N     1 
ATOM   8263 C  CA    . ALA B 2 527 ? 102.142 119.374 71.873  1.00 67.53  ? 527 ALA B CA    1 
ATOM   8264 C  C     . ALA B 2 527 ? 102.888 119.765 70.609  1.00 66.05  ? 527 ALA B C     1 
ATOM   8265 O  O     . ALA B 2 527 ? 102.277 120.261 69.653  1.00 65.27  ? 527 ALA B O     1 
ATOM   8266 C  CB    . ALA B 2 527 ? 100.826 120.146 71.977  1.00 67.59  ? 527 ALA B CB    1 
ATOM   8267 N  N     . ILE B 2 528 ? 104.200 119.554 70.586  1.00 66.95  ? 528 ILE B N     1 
ATOM   8268 C  CA    . ILE B 2 528 ? 105.079 120.108 69.570  1.00 62.17  ? 528 ILE B CA    1 
ATOM   8269 C  C     . ILE B 2 528 ? 105.842 118.977 68.893  1.00 57.52  ? 528 ILE B C     1 
ATOM   8270 O  O     . ILE B 2 528 ? 105.989 117.878 69.432  1.00 62.83  ? 528 ILE B O     1 
ATOM   8271 C  CB    . ILE B 2 528 ? 106.048 121.137 70.187  1.00 61.29  ? 528 ILE B CB    1 
ATOM   8272 C  CG1   . ILE B 2 528 ? 106.330 122.278 69.220  1.00 57.15  ? 528 ILE B CG1   1 
ATOM   8273 C  CG2   . ILE B 2 528 ? 107.341 120.472 70.640  1.00 58.43  ? 528 ILE B CG2   1 
ATOM   8274 C  CD1   . ILE B 2 528 ? 107.222 123.317 69.814  1.00 50.74  ? 528 ILE B CD1   1 
ATOM   8275 N  N     . SER B 2 529 ? 106.318 119.257 67.685  1.00 51.21  ? 529 SER B N     1 
ATOM   8276 C  CA    . SER B 2 529 ? 107.197 118.359 66.953  1.00 48.71  ? 529 SER B CA    1 
ATOM   8277 C  C     . SER B 2 529 ? 108.591 118.967 66.869  1.00 52.84  ? 529 SER B C     1 
ATOM   8278 O  O     . SER B 2 529 ? 108.815 120.121 67.241  1.00 52.06  ? 529 SER B O     1 
ATOM   8279 C  CB    . SER B 2 529 ? 106.646 118.069 65.553  1.00 46.74  ? 529 SER B CB    1 
ATOM   8280 O  OG    . SER B 2 529 ? 106.660 119.225 64.742  1.00 48.62  ? 529 SER B OG    1 
ATOM   8281 N  N     . ALA B 2 530 ? 109.540 118.163 66.384  1.00 50.46  ? 530 ALA B N     1 
ATOM   8282 C  CA    . ALA B 2 530 ? 110.919 118.629 66.287  1.00 45.00  ? 530 ALA B CA    1 
ATOM   8283 C  C     . ALA B 2 530 ? 111.038 119.810 65.335  1.00 49.55  ? 530 ALA B C     1 
ATOM   8284 O  O     . ALA B 2 530 ? 111.715 120.800 65.640  1.00 55.18  ? 530 ALA B O     1 
ATOM   8285 C  CB    . ALA B 2 530 ? 111.827 117.486 65.843  1.00 44.88  ? 530 ALA B CB    1 
ATOM   8286 N  N     . GLY B 2 531 ? 110.379 119.728 64.178  1.00 44.39  ? 531 GLY B N     1 
ATOM   8287 C  CA    . GLY B 2 531 ? 110.377 120.854 63.261  1.00 43.04  ? 531 GLY B CA    1 
ATOM   8288 C  C     . GLY B 2 531 ? 109.700 122.077 63.846  1.00 49.86  ? 531 GLY B C     1 
ATOM   8289 O  O     . GLY B 2 531 ? 110.179 123.200 63.684  1.00 52.11  ? 531 GLY B O     1 
ATOM   8290 N  N     . GLU B 2 532 ? 108.579 121.877 64.541  1.00 50.90  ? 532 GLU B N     1 
ATOM   8291 C  CA    . GLU B 2 532 ? 107.896 123.000 65.171  1.00 41.95  ? 532 GLU B CA    1 
ATOM   8292 C  C     . GLU B 2 532 ? 108.701 123.567 66.333  1.00 41.71  ? 532 GLU B C     1 
ATOM   8293 O  O     . GLU B 2 532 ? 108.677 124.778 66.566  1.00 49.78  ? 532 GLU B O     1 
ATOM   8294 C  CB    . GLU B 2 532 ? 106.504 122.575 65.635  1.00 45.22  ? 532 GLU B CB    1 
ATOM   8295 C  CG    . GLU B 2 532 ? 105.556 122.253 64.493  1.00 52.34  ? 532 GLU B CG    1 
ATOM   8296 C  CD    . GLU B 2 532 ? 104.334 121.477 64.942  1.00 63.61  ? 532 GLU B CD    1 
ATOM   8297 O  OE1   . GLU B 2 532 ? 104.440 120.705 65.917  1.00 64.11  ? 532 GLU B OE1   1 
ATOM   8298 O  OE2   . GLU B 2 532 ? 103.268 121.629 64.311  1.00 65.66  ? 532 GLU B OE2   1 
ATOM   8299 N  N     . LYS B 2 533 ? 109.423 122.717 67.064  1.00 43.30  ? 533 LYS B N     1 
ATOM   8300 C  CA    . LYS B 2 533 ? 110.330 123.214 68.094  1.00 42.69  ? 533 LYS B CA    1 
ATOM   8301 C  C     . LYS B 2 533 ? 111.430 124.074 67.485  1.00 42.56  ? 533 LYS B C     1 
ATOM   8302 O  O     . LYS B 2 533 ? 111.774 125.137 68.020  1.00 45.96  ? 533 LYS B O     1 
ATOM   8303 C  CB    . LYS B 2 533 ? 110.920 122.039 68.872  1.00 42.15  ? 533 LYS B CB    1 
ATOM   8304 C  CG    . LYS B 2 533 ? 111.749 122.430 70.077  1.00 45.38  ? 533 LYS B CG    1 
ATOM   8305 C  CD    . LYS B 2 533 ? 112.117 121.210 70.900  1.00 50.74  ? 533 LYS B CD    1 
ATOM   8306 C  CE    . LYS B 2 533 ? 112.904 121.595 72.138  1.00 52.93  ? 533 LYS B CE    1 
ATOM   8307 N  NZ    . LYS B 2 533 ? 113.416 120.407 72.868  1.00 51.97  ? 533 LYS B NZ    1 
ATOM   8308 N  N     . GLN B 2 534 ? 111.986 123.636 66.354  1.00 40.09  ? 534 GLN B N     1 
ATOM   8309 C  CA    . GLN B 2 534 ? 112.984 124.444 65.664  1.00 40.00  ? 534 GLN B CA    1 
ATOM   8310 C  C     . GLN B 2 534 ? 112.389 125.758 65.172  1.00 46.80  ? 534 GLN B C     1 
ATOM   8311 O  O     . GLN B 2 534 ? 113.049 126.802 65.217  1.00 53.01  ? 534 GLN B O     1 
ATOM   8312 C  CB    . GLN B 2 534 ? 113.585 123.657 64.503  1.00 49.13  ? 534 GLN B CB    1 
ATOM   8313 C  CG    . GLN B 2 534 ? 114.966 124.125 64.107  1.00 54.95  ? 534 GLN B CG    1 
ATOM   8314 C  CD    . GLN B 2 534 ? 115.720 123.095 63.303  1.00 59.49  ? 534 GLN B CD    1 
ATOM   8315 O  OE1   . GLN B 2 534 ? 115.202 122.553 62.332  1.00 63.08  ? 534 GLN B OE1   1 
ATOM   8316 N  NE2   . GLN B 2 534 ? 116.955 122.824 63.701  1.00 61.52  ? 534 GLN B NE2   1 
ATOM   8317 N  N     . LEU B 2 535 ? 111.145 125.726 64.690  1.00 46.79  ? 535 LEU B N     1 
ATOM   8318 C  CA    . LEU B 2 535 ? 110.480 126.956 64.267  1.00 43.16  ? 535 LEU B CA    1 
ATOM   8319 C  C     . LEU B 2 535 ? 110.287 127.910 65.436  1.00 44.68  ? 535 LEU B C     1 
ATOM   8320 O  O     . LEU B 2 535 ? 110.443 129.127 65.287  1.00 53.18  ? 535 LEU B O     1 
ATOM   8321 C  CB    . LEU B 2 535 ? 109.133 126.637 63.619  1.00 44.68  ? 535 LEU B CB    1 
ATOM   8322 C  CG    . LEU B 2 535 ? 109.183 125.884 62.293  1.00 45.93  ? 535 LEU B CG    1 
ATOM   8323 C  CD1   . LEU B 2 535 ? 107.845 125.935 61.588  1.00 53.19  ? 535 LEU B CD1   1 
ATOM   8324 C  CD2   . LEU B 2 535 ? 110.269 126.464 61.427  1.00 44.66  ? 535 LEU B CD2   1 
ATOM   8325 N  N     . ILE B 2 536 ? 109.926 127.379 66.603  1.00 41.26  ? 536 ILE B N     1 
ATOM   8326 C  CA    . ILE B 2 536 ? 109.760 128.225 67.779  1.00 40.95  ? 536 ILE B CA    1 
ATOM   8327 C  C     . ILE B 2 536 ? 111.090 128.851 68.175  1.00 44.53  ? 536 ILE B C     1 
ATOM   8328 O  O     . ILE B 2 536 ? 111.148 130.028 68.545  1.00 47.08  ? 536 ILE B O     1 
ATOM   8329 C  CB    . ILE B 2 536 ? 109.136 127.425 68.936  1.00 42.11  ? 536 ILE B CB    1 
ATOM   8330 C  CG1   . ILE B 2 536 ? 107.625 127.329 68.747  1.00 43.03  ? 536 ILE B CG1   1 
ATOM   8331 C  CG2   . ILE B 2 536 ? 109.441 128.080 70.269  1.00 37.39  ? 536 ILE B CG2   1 
ATOM   8332 C  CD1   . ILE B 2 536 ? 106.906 126.776 69.938  1.00 50.70  ? 536 ILE B CD1   1 
ATOM   8333 N  N     . THR B 2 537 ? 112.177 128.081 68.104  1.00 46.41  ? 537 THR B N     1 
ATOM   8334 C  CA    . THR B 2 537 ? 113.494 128.651 68.387  1.00 44.06  ? 537 THR B CA    1 
ATOM   8335 C  C     . THR B 2 537 ? 113.865 129.729 67.371  1.00 45.50  ? 537 THR B C     1 
ATOM   8336 O  O     . THR B 2 537 ? 114.474 130.747 67.726  1.00 53.80  ? 537 THR B O     1 
ATOM   8337 C  CB    . THR B 2 537 ? 114.552 127.550 68.413  1.00 47.60  ? 537 THR B CB    1 
ATOM   8338 O  OG1   . THR B 2 537 ? 114.588 126.889 67.143  1.00 51.49  ? 537 THR B OG1   1 
ATOM   8339 C  CG2   . THR B 2 537 ? 114.237 126.540 69.503  1.00 45.49  ? 537 THR B CG2   1 
ATOM   8340 N  N     . ILE B 2 538 ? 113.512 129.521 66.101  1.00 42.55  ? 538 ILE B N     1 
ATOM   8341 C  CA    . ILE B 2 538 ? 113.761 130.534 65.078  1.00 46.36  ? 538 ILE B CA    1 
ATOM   8342 C  C     . ILE B 2 538 ? 112.999 131.813 65.395  1.00 52.44  ? 538 ILE B C     1 
ATOM   8343 O  O     . ILE B 2 538 ? 113.545 132.919 65.308  1.00 57.15  ? 538 ILE B O     1 
ATOM   8344 C  CB    . ILE B 2 538 ? 113.389 129.994 63.685  1.00 48.43  ? 538 ILE B CB    1 
ATOM   8345 C  CG1   . ILE B 2 538 ? 114.393 128.938 63.229  1.00 54.21  ? 538 ILE B CG1   1 
ATOM   8346 C  CG2   . ILE B 2 538 ? 113.315 131.126 62.674  1.00 46.17  ? 538 ILE B CG2   1 
ATOM   8347 C  CD1   . ILE B 2 538 ? 113.915 128.131 62.050  1.00 51.02  ? 538 ILE B CD1   1 
ATOM   8348 N  N     . ALA B 2 539 ? 111.723 131.683 65.762  1.00 52.48  ? 539 ALA B N     1 
ATOM   8349 C  CA    . ALA B 2 539 ? 110.927 132.853 66.118  1.00 48.06  ? 539 ALA B CA    1 
ATOM   8350 C  C     . ALA B 2 539 ? 111.488 133.545 67.353  1.00 49.73  ? 539 ALA B C     1 
ATOM   8351 O  O     . ALA B 2 539 ? 111.488 134.778 67.439  1.00 56.42  ? 539 ALA B O     1 
ATOM   8352 C  CB    . ALA B 2 539 ? 109.472 132.448 66.345  1.00 48.31  ? 539 ALA B CB    1 
ATOM   8353 N  N     . ARG B 2 540 ? 111.963 132.762 68.322  1.00 46.19  ? 540 ARG B N     1 
ATOM   8354 C  CA    . ARG B 2 540 ? 112.560 133.328 69.525  1.00 44.33  ? 540 ARG B CA    1 
ATOM   8355 C  C     . ARG B 2 540 ? 113.802 134.141 69.192  1.00 51.12  ? 540 ARG B C     1 
ATOM   8356 O  O     . ARG B 2 540 ? 114.011 135.225 69.748  1.00 60.34  ? 540 ARG B O     1 
ATOM   8357 C  CB    . ARG B 2 540 ? 112.895 132.208 70.506  1.00 38.68  ? 540 ARG B CB    1 
ATOM   8358 C  CG    . ARG B 2 540 ? 113.404 132.678 71.848  1.00 47.25  ? 540 ARG B CG    1 
ATOM   8359 C  CD    . ARG B 2 540 ? 113.709 131.499 72.749  1.00 49.56  ? 540 ARG B CD    1 
ATOM   8360 N  NE    . ARG B 2 540 ? 114.763 130.656 72.203  1.00 51.15  ? 540 ARG B NE    1 
ATOM   8361 C  CZ    . ARG B 2 540 ? 114.879 129.356 72.434  1.00 49.94  ? 540 ARG B CZ    1 
ATOM   8362 N  NH1   . ARG B 2 540 ? 114.015 128.711 73.199  1.00 44.59  ? 540 ARG B NH1   1 
ATOM   8363 N  NH2   . ARG B 2 540 ? 115.888 128.688 71.886  1.00 52.83  ? 540 ARG B NH2   1 
ATOM   8364 N  N     . ALA B 2 541 ? 114.643 133.632 68.292  1.00 51.23  ? 541 ALA B N     1 
ATOM   8365 C  CA    . ALA B 2 541 ? 115.820 134.390 67.883  1.00 51.63  ? 541 ALA B CA    1 
ATOM   8366 C  C     . ALA B 2 541 ? 115.447 135.610 67.051  1.00 57.96  ? 541 ALA B C     1 
ATOM   8367 O  O     . ALA B 2 541 ? 116.141 136.631 67.105  1.00 64.88  ? 541 ALA B O     1 
ATOM   8368 C  CB    . ALA B 2 541 ? 116.781 133.498 67.103  1.00 56.85  ? 541 ALA B CB    1 
ATOM   8369 N  N     . VAL B 2 542 ? 114.372 135.519 66.267  1.00 58.72  ? 542 VAL B N     1 
ATOM   8370 C  CA    . VAL B 2 542 ? 113.961 136.639 65.427  1.00 60.94  ? 542 VAL B CA    1 
ATOM   8371 C  C     . VAL B 2 542 ? 113.404 137.776 66.276  1.00 66.15  ? 542 VAL B C     1 
ATOM   8372 O  O     . VAL B 2 542 ? 113.671 138.954 66.012  1.00 69.36  ? 542 VAL B O     1 
ATOM   8373 C  CB    . VAL B 2 542 ? 112.948 136.157 64.373  1.00 63.72  ? 542 VAL B CB    1 
ATOM   8374 C  CG1   . VAL B 2 542 ? 112.008 137.280 63.962  1.00 67.16  ? 542 VAL B CG1   1 
ATOM   8375 C  CG2   . VAL B 2 542 ? 113.680 135.595 63.171  1.00 74.94  ? 542 VAL B CG2   1 
ATOM   8376 N  N     . LEU B 2 543 ? 112.628 137.445 67.310  1.00 65.09  ? 543 LEU B N     1 
ATOM   8377 C  CA    . LEU B 2 543 ? 112.048 138.471 68.168  1.00 69.56  ? 543 LEU B CA    1 
ATOM   8378 C  C     . LEU B 2 543 ? 113.106 139.284 68.901  1.00 73.75  ? 543 LEU B C     1 
ATOM   8379 O  O     . LEU B 2 543 ? 112.840 140.429 69.281  1.00 79.88  ? 543 LEU B O     1 
ATOM   8380 C  CB    . LEU B 2 543 ? 111.093 137.831 69.176  1.00 66.81  ? 543 LEU B CB    1 
ATOM   8381 C  CG    . LEU B 2 543 ? 110.297 138.784 70.068  1.00 74.81  ? 543 LEU B CG    1 
ATOM   8382 C  CD1   . LEU B 2 543 ? 109.316 139.595 69.240  1.00 76.10  ? 543 LEU B CD1   1 
ATOM   8383 C  CD2   . LEU B 2 543 ? 109.578 138.016 71.156  1.00 72.13  ? 543 LEU B CD2   1 
ATOM   8384 N  N     . ALA B 2 544 ? 114.304 138.732 69.092  1.00 71.02  ? 544 ALA B N     1 
ATOM   8385 C  CA    . ALA B 2 544 ? 115.357 139.443 69.804  1.00 71.21  ? 544 ALA B CA    1 
ATOM   8386 C  C     . ALA B 2 544 ? 115.949 140.591 68.999  1.00 78.91  ? 544 ALA B C     1 
ATOM   8387 O  O     . ALA B 2 544 ? 116.812 141.301 69.526  1.00 80.93  ? 544 ALA B O     1 
ATOM   8388 C  CB    . ALA B 2 544 ? 116.467 138.473 70.207  1.00 69.00  ? 544 ALA B CB    1 
ATOM   8389 N  N     . ARG B 2 545 ? 115.500 140.788 67.757  1.00 80.24  ? 545 ARG B N     1 
ATOM   8390 C  CA    . ARG B 2 545 ? 116.017 141.776 66.812  1.00 85.93  ? 545 ARG B CA    1 
ATOM   8391 C  C     . ARG B 2 545 ? 117.539 141.949 66.931  1.00 89.15  ? 545 ARG B C     1 
ATOM   8392 O  O     . ARG B 2 545 ? 118.024 143.054 67.184  1.00 87.89  ? 545 ARG B O     1 
ATOM   8393 C  CB    . ARG B 2 545 ? 115.298 143.115 66.957  1.00 84.83  ? 545 ARG B CB    1 
ATOM   8394 C  CG    . ARG B 2 545 ? 115.335 143.768 68.337  1.00 86.27  ? 545 ARG B CG    1 
ATOM   8395 C  CD    . ARG B 2 545 ? 114.207 144.770 68.503  1.00 83.83  ? 545 ARG B CD    1 
ATOM   8396 N  NE    . ARG B 2 545 ? 114.007 145.141 69.898  1.00 87.88  ? 545 ARG B NE    1 
ATOM   8397 C  CZ    . ARG B 2 545 ? 113.299 146.187 70.300  1.00 93.29  ? 545 ARG B CZ    1 
ATOM   8398 N  NH1   . ARG B 2 545 ? 112.704 146.992 69.435  1.00 92.31  ? 545 ARG B NH1   1 
ATOM   8399 N  NH2   . ARG B 2 545 ? 113.187 146.433 71.602  1.00 90.96  ? 545 ARG B NH2   1 
ATOM   8400 N  N     . PRO B 2 546 ? 118.306 140.879 66.737  1.00 91.37  ? 546 PRO B N     1 
ATOM   8401 C  CA    . PRO B 2 546 ? 119.747 140.951 66.989  1.00 88.84  ? 546 PRO B CA    1 
ATOM   8402 C  C     . PRO B 2 546 ? 120.470 141.805 65.961  1.00 89.19  ? 546 PRO B C     1 
ATOM   8403 O  O     . PRO B 2 546 ? 120.046 141.949 64.814  1.00 92.99  ? 546 PRO B O     1 
ATOM   8404 C  CB    . PRO B 2 546 ? 120.187 139.491 66.895  1.00 86.75  ? 546 PRO B CB    1 
ATOM   8405 C  CG    . PRO B 2 546 ? 119.236 138.897 65.920  1.00 87.59  ? 546 PRO B CG    1 
ATOM   8406 C  CD    . PRO B 2 546 ? 117.917 139.584 66.151  1.00 85.10  ? 546 PRO B CD    1 
ATOM   8407 N  N     . LYS B 2 547 ? 121.589 142.378 66.400  1.00 84.72  ? 547 LYS B N     1 
ATOM   8408 C  CA    . LYS B 2 547 ? 122.466 143.089 65.480  1.00 86.56  ? 547 LYS B CA    1 
ATOM   8409 C  C     . LYS B 2 547 ? 123.356 142.131 64.702  1.00 86.56  ? 547 LYS B C     1 
ATOM   8410 O  O     . LYS B 2 547 ? 123.758 142.438 63.575  1.00 83.50  ? 547 LYS B O     1 
ATOM   8411 C  CB    . LYS B 2 547 ? 123.317 144.105 66.242  1.00 88.70  ? 547 LYS B CB    1 
ATOM   8412 C  CG    . LYS B 2 547 ? 122.629 145.442 66.492  1.00 91.45  ? 547 LYS B CG    1 
ATOM   8413 C  CD    . LYS B 2 547 ? 121.647 145.361 67.647  1.00 85.90  ? 547 LYS B CD    1 
ATOM   8414 C  CE    . LYS B 2 547 ? 122.355 145.013 68.946  1.00 83.80  ? 547 LYS B CE    1 
ATOM   8415 N  NZ    . LYS B 2 547 ? 121.409 144.938 70.094  1.00 80.16  ? 547 LYS B NZ    1 
ATOM   8416 N  N     . LEU B 2 548 ? 123.669 140.976 65.283  1.00 91.01  ? 548 LEU B N     1 
ATOM   8417 C  CA    . LEU B 2 548 ? 124.421 139.919 64.621  1.00 83.18  ? 548 LEU B CA    1 
ATOM   8418 C  C     . LEU B 2 548 ? 123.599 138.641 64.678  1.00 78.64  ? 548 LEU B C     1 
ATOM   8419 O  O     . LEU B 2 548 ? 123.074 138.285 65.737  1.00 79.71  ? 548 LEU B O     1 
ATOM   8420 C  CB    . LEU B 2 548 ? 125.783 139.707 65.287  1.00 77.41  ? 548 LEU B CB    1 
ATOM   8421 C  CG    . LEU B 2 548 ? 126.977 139.471 64.363  1.00 82.99  ? 548 LEU B CG    1 
ATOM   8422 C  CD1   . LEU B 2 548 ? 127.401 140.772 63.707  1.00 86.06  ? 548 LEU B CD1   1 
ATOM   8423 C  CD2   . LEU B 2 548 ? 128.134 138.852 65.124  1.00 79.63  ? 548 LEU B CD2   1 
ATOM   8424 N  N     . LEU B 2 549 ? 123.485 137.957 63.545  1.00 75.96  ? 549 LEU B N     1 
ATOM   8425 C  CA    . LEU B 2 549 ? 122.644 136.774 63.422  1.00 73.22  ? 549 LEU B CA    1 
ATOM   8426 C  C     . LEU B 2 549 ? 123.513 135.545 63.205  1.00 73.50  ? 549 LEU B C     1 
ATOM   8427 O  O     . LEU B 2 549 ? 124.390 135.545 62.337  1.00 76.43  ? 549 LEU B O     1 
ATOM   8428 C  CB    . LEU B 2 549 ? 121.655 136.928 62.266  1.00 77.44  ? 549 LEU B CB    1 
ATOM   8429 C  CG    . LEU B 2 549 ? 120.172 136.893 62.633  1.00 81.86  ? 549 LEU B CG    1 
ATOM   8430 C  CD1   . LEU B 2 549 ? 119.313 137.004 61.386  1.00 93.66  ? 549 LEU B CD1   1 
ATOM   8431 C  CD2   . LEU B 2 549 ? 119.842 135.629 63.409  1.00 79.70  ? 549 LEU B CD2   1 
ATOM   8432 N  N     . VAL B 2 550 ? 123.273 134.505 63.999  1.00 68.55  ? 550 VAL B N     1 
ATOM   8433 C  CA    . VAL B 2 550 ? 123.938 133.216 63.843  1.00 66.64  ? 550 VAL B CA    1 
ATOM   8434 C  C     . VAL B 2 550 ? 122.856 132.148 63.805  1.00 66.77  ? 550 VAL B C     1 
ATOM   8435 O  O     . VAL B 2 550 ? 122.162 131.928 64.805  1.00 66.74  ? 550 VAL B O     1 
ATOM   8436 C  CB    . VAL B 2 550 ? 124.943 132.934 64.968  1.00 58.81  ? 550 VAL B CB    1 
ATOM   8437 C  CG1   . VAL B 2 550 ? 125.456 131.512 64.871  1.00 56.42  ? 550 VAL B CG1   1 
ATOM   8438 C  CG2   . VAL B 2 550 ? 126.098 133.915 64.906  1.00 59.90  ? 550 VAL B CG2   1 
ATOM   8439 N  N     . LEU B 2 551 ? 122.707 131.487 62.663  1.00 65.42  ? 551 LEU B N     1 
ATOM   8440 C  CA    . LEU B 2 551 ? 121.770 130.378 62.510  1.00 62.77  ? 551 LEU B CA    1 
ATOM   8441 C  C     . LEU B 2 551 ? 122.598 129.109 62.334  1.00 62.60  ? 551 LEU B C     1 
ATOM   8442 O  O     . LEU B 2 551 ? 123.080 128.808 61.242  1.00 65.27  ? 551 LEU B O     1 
ATOM   8443 C  CB    . LEU B 2 551 ? 120.813 130.602 61.341  1.00 66.07  ? 551 LEU B CB    1 
ATOM   8444 C  CG    . LEU B 2 551 ? 120.233 132.007 61.170  1.00 65.85  ? 551 LEU B CG    1 
ATOM   8445 C  CD1   . LEU B 2 551 ? 119.747 132.217 59.749  1.00 67.06  ? 551 LEU B CD1   1 
ATOM   8446 C  CD2   . LEU B 2 551 ? 119.106 132.246 62.153  1.00 65.33  ? 551 LEU B CD2   1 
ATOM   8447 N  N     . ASP B 2 552 ? 122.765 128.369 63.428  1.00 58.27  ? 552 ASP B N     1 
ATOM   8448 C  CA    . ASP B 2 552 ? 123.572 127.151 63.438  1.00 60.94  ? 552 ASP B CA    1 
ATOM   8449 C  C     . ASP B 2 552 ? 122.653 125.976 63.132  1.00 60.93  ? 552 ASP B C     1 
ATOM   8450 O  O     . ASP B 2 552 ? 122.066 125.368 64.028  1.00 59.72  ? 552 ASP B O     1 
ATOM   8451 C  CB    . ASP B 2 552 ? 124.282 126.995 64.777  1.00 63.61  ? 552 ASP B CB    1 
ATOM   8452 C  CG    . ASP B 2 552 ? 125.226 125.809 64.808  1.00 65.73  ? 552 ASP B CG    1 
ATOM   8453 O  OD1   . ASP B 2 552 ? 125.598 125.307 63.728  1.00 64.85  ? 552 ASP B OD1   1 
ATOM   8454 O  OD2   . ASP B 2 552 ? 125.606 125.385 65.919  1.00 64.94  ? 552 ASP B OD2   1 
ATOM   8455 N  N     . GLU B 2 553 ? 122.527 125.659 61.841  1.00 62.79  ? 553 GLU B N     1 
ATOM   8456 C  CA    . GLU B 2 553 ? 121.663 124.584 61.354  1.00 62.23  ? 553 GLU B CA    1 
ATOM   8457 C  C     . GLU B 2 553 ? 120.220 124.798 61.814  1.00 66.74  ? 553 GLU B C     1 
ATOM   8458 O  O     . GLU B 2 553 ? 119.628 123.976 62.515  1.00 70.55  ? 553 GLU B O     1 
ATOM   8459 C  CB    . GLU B 2 553 ? 122.195 123.216 61.790  1.00 59.95  ? 553 GLU B CB    1 
ATOM   8460 C  CG    . GLU B 2 553 ? 123.144 122.581 60.791  1.00 63.55  ? 553 GLU B CG    1 
ATOM   8461 C  CD    . GLU B 2 553 ? 123.870 121.379 61.360  1.00 65.31  ? 553 GLU B CD    1 
ATOM   8462 O  OE1   . GLU B 2 553 ? 125.060 121.516 61.710  1.00 63.20  ? 553 GLU B OE1   1 
ATOM   8463 O  OE2   . GLU B 2 553 ? 123.252 120.298 61.453  1.00 63.29  ? 553 GLU B OE2   1 
ATOM   8464 N  N     . ALA B 2 554 ? 119.661 125.934 61.398  1.00 63.33  ? 554 ALA B N     1 
ATOM   8465 C  CA    . ALA B 2 554 ? 118.357 126.372 61.876  1.00 59.34  ? 554 ALA B CA    1 
ATOM   8466 C  C     . ALA B 2 554 ? 117.189 125.695 61.173  1.00 68.65  ? 554 ALA B C     1 
ATOM   8467 O  O     . ALA B 2 554 ? 116.062 125.785 61.666  1.00 74.08  ? 554 ALA B O     1 
ATOM   8468 C  CB    . ALA B 2 554 ? 118.229 127.888 61.723  1.00 59.35  ? 554 ALA B CB    1 
ATOM   8469 N  N     . THR B 2 555 ? 117.415 125.025 60.044  1.00 70.29  ? 555 THR B N     1 
ATOM   8470 C  CA    . THR B 2 555 ? 116.340 124.382 59.296  1.00 69.76  ? 555 THR B CA    1 
ATOM   8471 C  C     . THR B 2 555 ? 116.621 122.901 59.070  1.00 64.56  ? 555 THR B C     1 
ATOM   8472 O  O     . THR B 2 555 ? 116.155 122.317 58.091  1.00 68.83  ? 555 THR B O     1 
ATOM   8473 C  CB    . THR B 2 555 ? 116.106 125.090 57.961  1.00 76.92  ? 555 THR B CB    1 
ATOM   8474 O  OG1   . THR B 2 555 ? 117.311 125.069 57.186  1.00 77.89  ? 555 THR B OG1   1 
ATOM   8475 C  CG2   . THR B 2 555 ? 115.675 126.532 58.186  1.00 72.15  ? 555 THR B CG2   1 
ATOM   8476 N  N     . SER B 2 556 ? 117.392 122.285 59.967  1.00 61.15  ? 556 SER B N     1 
ATOM   8477 C  CA    . SER B 2 556 ? 117.715 120.871 59.818  1.00 60.02  ? 556 SER B CA    1 
ATOM   8478 C  C     . SER B 2 556 ? 116.473 119.998 59.953  1.00 61.68  ? 556 SER B C     1 
ATOM   8479 O  O     . SER B 2 556 ? 116.315 119.017 59.218  1.00 65.54  ? 556 SER B O     1 
ATOM   8480 C  CB    . SER B 2 556 ? 118.773 120.467 60.843  1.00 58.02  ? 556 SER B CB    1 
ATOM   8481 O  OG    . SER B 2 556 ? 118.294 120.640 62.163  1.00 61.57  ? 556 SER B OG    1 
ATOM   8482 N  N     . SER B 2 557 ? 115.586 120.334 60.886  1.00 59.77  ? 557 SER B N     1 
ATOM   8483 C  CA    . SER B 2 557 ? 114.372 119.566 61.127  1.00 59.76  ? 557 SER B CA    1 
ATOM   8484 C  C     . SER B 2 557 ? 113.152 120.132 60.412  1.00 59.82  ? 557 SER B C     1 
ATOM   8485 O  O     . SER B 2 557 ? 112.046 119.619 60.607  1.00 62.68  ? 557 SER B O     1 
ATOM   8486 C  CB    . SER B 2 557 ? 114.089 119.489 62.630  1.00 55.31  ? 557 SER B CB    1 
ATOM   8487 O  OG    . SER B 2 557 ? 115.106 118.772 63.306  1.00 56.21  ? 557 SER B OG    1 
ATOM   8488 N  N     . VAL B 2 558 ? 113.322 121.164 59.594  1.00 59.22  ? 558 VAL B N     1 
ATOM   8489 C  CA    . VAL B 2 558 ? 112.216 121.828 58.915  1.00 57.66  ? 558 VAL B CA    1 
ATOM   8490 C  C     . VAL B 2 558 ? 112.255 121.467 57.439  1.00 65.92  ? 558 VAL B C     1 
ATOM   8491 O  O     . VAL B 2 558 ? 113.326 121.438 56.821  1.00 75.75  ? 558 VAL B O     1 
ATOM   8492 C  CB    . VAL B 2 558 ? 112.280 123.354 59.116  1.00 65.31  ? 558 VAL B CB    1 
ATOM   8493 C  CG1   . VAL B 2 558 ? 111.028 124.016 58.567  1.00 67.34  ? 558 VAL B CG1   1 
ATOM   8494 C  CG2   . VAL B 2 558 ? 112.462 123.682 60.588  1.00 61.78  ? 558 VAL B CG2   1 
ATOM   8495 N  N     . ASP B 2 559 ? 111.085 121.184 56.873  1.00 68.48  ? 559 ASP B N     1 
ATOM   8496 C  CA    . ASP B 2 559 ? 110.991 120.786 55.479  1.00 74.10  ? 559 ASP B CA    1 
ATOM   8497 C  C     . ASP B 2 559 ? 111.382 121.938 54.556  1.00 77.13  ? 559 ASP B C     1 
ATOM   8498 O  O     . ASP B 2 559 ? 111.393 123.109 54.944  1.00 77.73  ? 559 ASP B O     1 
ATOM   8499 C  CB    . ASP B 2 559 ? 109.577 120.303 55.156  1.00 79.41  ? 559 ASP B CB    1 
ATOM   8500 C  CG    . ASP B 2 559 ? 108.544 121.404 55.269  1.00 79.67  ? 559 ASP B CG    1 
ATOM   8501 O  OD1   . ASP B 2 559 ? 108.353 122.151 54.288  1.00 84.54  ? 559 ASP B OD1   1 
ATOM   8502 O  OD2   . ASP B 2 559 ? 107.918 121.523 56.342  1.00 75.59  ? 559 ASP B OD2   1 
ATOM   8503 N  N     . THR B 2 560 ? 111.713 121.584 53.313  1.00 80.55  ? 560 THR B N     1 
ATOM   8504 C  CA    . THR B 2 560 ? 112.204 122.577 52.363  1.00 83.98  ? 560 THR B CA    1 
ATOM   8505 C  C     . THR B 2 560 ? 111.106 123.547 51.943  1.00 84.66  ? 560 THR B C     1 
ATOM   8506 O  O     . THR B 2 560 ? 111.373 124.735 51.728  1.00 87.18  ? 560 THR B O     1 
ATOM   8507 C  CB    . THR B 2 560 ? 112.804 121.883 51.142  1.00 89.34  ? 560 THR B CB    1 
ATOM   8508 O  OG1   . THR B 2 560 ? 111.753 121.446 50.273  1.00 94.78  ? 560 THR B OG1   1 
ATOM   8509 C  CG2   . THR B 2 560 ? 113.629 120.684 51.575  1.00 87.91  ? 560 THR B CG2   1 
ATOM   8510 N  N     . ARG B 2 561 ? 109.869 123.062 51.814  1.00 81.79  ? 561 ARG B N     1 
ATOM   8511 C  CA    . ARG B 2 561 ? 108.769 123.947 51.441  1.00 82.30  ? 561 ARG B CA    1 
ATOM   8512 C  C     . ARG B 2 561 ? 108.538 125.016 52.501  1.00 84.18  ? 561 ARG B C     1 
ATOM   8513 O  O     . ARG B 2 561 ? 108.302 126.185 52.173  1.00 90.00  ? 561 ARG B O     1 
ATOM   8514 C  CB    . ARG B 2 561 ? 107.495 123.136 51.209  1.00 87.92  ? 561 ARG B CB    1 
ATOM   8515 C  CG    . ARG B 2 561 ? 107.495 122.350 49.910  1.00 94.82  ? 561 ARG B CG    1 
ATOM   8516 C  CD    . ARG B 2 561 ? 106.446 121.251 49.919  1.00 99.02  ? 561 ARG B CD    1 
ATOM   8517 N  NE    . ARG B 2 561 ? 105.089 121.779 50.005  1.00 101.73 ? 561 ARG B NE    1 
ATOM   8518 C  CZ    . ARG B 2 561 ? 104.236 121.498 50.981  1.00 99.25  ? 561 ARG B CZ    1 
ATOM   8519 N  NH1   . ARG B 2 561 ? 104.570 120.700 51.982  1.00 96.16  ? 561 ARG B NH1   1 
ATOM   8520 N  NH2   . ARG B 2 561 ? 103.018 122.029 50.950  1.00 94.54  ? 561 ARG B NH2   1 
ATOM   8521 N  N     . THR B 2 562 ? 108.599 124.636 53.778  1.00 81.02  ? 562 THR B N     1 
ATOM   8522 C  CA    . THR B 2 562 ? 108.466 125.617 54.849  1.00 80.56  ? 562 THR B CA    1 
ATOM   8523 C  C     . THR B 2 562 ? 109.712 126.487 54.956  1.00 81.30  ? 562 THR B C     1 
ATOM   8524 O  O     . THR B 2 562 ? 109.619 127.687 55.247  1.00 81.35  ? 562 THR B O     1 
ATOM   8525 C  CB    . THR B 2 562 ? 108.189 124.907 56.174  1.00 80.36  ? 562 THR B CB    1 
ATOM   8526 O  OG1   . THR B 2 562 ? 107.091 124.003 56.011  1.00 83.13  ? 562 THR B OG1   1 
ATOM   8527 C  CG2   . THR B 2 562 ? 107.844 125.911 57.260  1.00 79.00  ? 562 THR B CG2   1 
ATOM   8528 N  N     . GLU B 2 563 ? 110.889 125.903 54.719  1.00 81.97  ? 563 GLU B N     1 
ATOM   8529 C  CA    . GLU B 2 563 ? 112.125 126.663 54.853  1.00 80.21  ? 563 GLU B CA    1 
ATOM   8530 C  C     . GLU B 2 563 ? 112.256 127.722 53.766  1.00 84.49  ? 563 GLU B C     1 
ATOM   8531 O  O     . GLU B 2 563 ? 112.885 128.759 53.994  1.00 88.35  ? 563 GLU B O     1 
ATOM   8532 C  CB    . GLU B 2 563 ? 113.331 125.722 54.845  1.00 79.99  ? 563 GLU B CB    1 
ATOM   8533 C  CG    . GLU B 2 563 ? 114.132 125.716 53.555  1.00 86.53  ? 563 GLU B CG    1 
ATOM   8534 C  CD    . GLU B 2 563 ? 115.164 124.607 53.519  1.00 90.85  ? 563 GLU B CD    1 
ATOM   8535 O  OE1   . GLU B 2 563 ? 115.825 124.376 54.553  1.00 88.17  ? 563 GLU B OE1   1 
ATOM   8536 O  OE2   . GLU B 2 563 ? 115.317 123.969 52.456  1.00 86.96  ? 563 GLU B OE2   1 
ATOM   8537 N  N     . LEU B 2 564 ? 111.665 127.494 52.590  1.00 82.68  ? 564 LEU B N     1 
ATOM   8538 C  CA    . LEU B 2 564 ? 111.677 128.525 51.556  1.00 86.91  ? 564 LEU B CA    1 
ATOM   8539 C  C     . LEU B 2 564 ? 110.891 129.754 51.998  1.00 87.77  ? 564 LEU B C     1 
ATOM   8540 O  O     . LEU B 2 564 ? 111.354 130.892 51.845  1.00 89.07  ? 564 LEU B O     1 
ATOM   8541 C  CB    . LEU B 2 564 ? 111.115 127.966 50.249  1.00 88.80  ? 564 LEU B CB    1 
ATOM   8542 C  CG    . LEU B 2 564 ? 112.092 127.183 49.373  1.00 94.51  ? 564 LEU B CG    1 
ATOM   8543 C  CD1   . LEU B 2 564 ? 111.371 126.574 48.185  1.00 91.96  ? 564 LEU B CD1   1 
ATOM   8544 C  CD2   . LEU B 2 564 ? 113.226 128.081 48.910  1.00 87.69  ? 564 LEU B CD2   1 
ATOM   8545 N  N     . LEU B 2 565 ? 109.701 129.540 52.561  1.00 83.53  ? 565 LEU B N     1 
ATOM   8546 C  CA    . LEU B 2 565 ? 108.920 130.656 53.083  1.00 84.61  ? 565 LEU B CA    1 
ATOM   8547 C  C     . LEU B 2 565 ? 109.634 131.323 54.250  1.00 87.70  ? 565 LEU B C     1 
ATOM   8548 O  O     . LEU B 2 565 ? 109.584 132.550 54.401  1.00 91.76  ? 565 LEU B O     1 
ATOM   8549 C  CB    . LEU B 2 565 ? 107.534 130.170 53.503  1.00 84.55  ? 565 LEU B CB    1 
ATOM   8550 C  CG    . LEU B 2 565 ? 106.831 129.215 52.538  1.00 86.13  ? 565 LEU B CG    1 
ATOM   8551 C  CD1   . LEU B 2 565 ? 105.567 128.651 53.164  1.00 86.53  ? 565 LEU B CD1   1 
ATOM   8552 C  CD2   . LEU B 2 565 ? 106.515 129.920 51.229  1.00 83.20  ? 565 LEU B CD2   1 
ATOM   8553 N  N     . ILE B 2 566 ? 110.305 130.530 55.087  1.00 87.64  ? 566 ILE B N     1 
ATOM   8554 C  CA    . ILE B 2 566 ? 111.062 131.094 56.200  1.00 84.74  ? 566 ILE B CA    1 
ATOM   8555 C  C     . ILE B 2 566 ? 112.174 131.997 55.684  1.00 89.69  ? 566 ILE B C     1 
ATOM   8556 O  O     . ILE B 2 566 ? 112.400 133.089 56.214  1.00 93.66  ? 566 ILE B O     1 
ATOM   8557 C  CB    . ILE B 2 566 ? 111.616 129.968 57.090  1.00 83.00  ? 566 ILE B CB    1 
ATOM   8558 C  CG1   . ILE B 2 566 ? 110.536 129.472 58.045  1.00 77.59  ? 566 ILE B CG1   1 
ATOM   8559 C  CG2   . ILE B 2 566 ? 112.828 130.445 57.874  1.00 78.60  ? 566 ILE B CG2   1 
ATOM   8560 C  CD1   . ILE B 2 566 ? 110.642 128.007 58.330  1.00 75.51  ? 566 ILE B CD1   1 
ATOM   8561 N  N     . ALA B 2 567 ? 112.892 131.552 54.651  1.00 90.39  ? 567 ALA B N     1 
ATOM   8562 C  CA    . ALA B 2 567 ? 113.952 132.370 54.072  1.00 90.99  ? 567 ALA B CA    1 
ATOM   8563 C  C     . ALA B 2 567 ? 113.388 133.637 53.442  1.00 94.81  ? 567 ALA B C     1 
ATOM   8564 O  O     . ALA B 2 567 ? 113.986 134.714 53.557  1.00 99.73  ? 567 ALA B O     1 
ATOM   8565 C  CB    . ALA B 2 567 ? 114.739 131.561 53.042  1.00 89.83  ? 567 ALA B CB    1 
ATOM   8566 N  N     . HIS B 2 568 ? 112.236 133.529 52.776  1.00 93.44  ? 568 HIS B N     1 
ATOM   8567 C  CA    . HIS B 2 568 ? 111.604 134.716 52.210  1.00 96.65  ? 568 HIS B CA    1 
ATOM   8568 C  C     . HIS B 2 568 ? 111.250 135.719 53.302  1.00 97.26  ? 568 HIS B C     1 
ATOM   8569 O  O     . HIS B 2 568 ? 111.456 136.927 53.137  1.00 97.73  ? 568 HIS B O     1 
ATOM   8570 C  CB    . HIS B 2 568 ? 110.360 134.321 51.414  1.00 99.09  ? 568 HIS B CB    1 
ATOM   8571 C  CG    . HIS B 2 568 ? 109.788 135.431 50.586  1.00 110.18 ? 568 HIS B CG    1 
ATOM   8572 N  ND1   . HIS B 2 568 ? 109.401 136.640 51.122  1.00 111.28 ? 568 HIS B ND1   1 
ATOM   8573 C  CD2   . HIS B 2 568 ? 109.538 135.512 49.258  1.00 111.28 ? 568 HIS B CD2   1 
ATOM   8574 C  CE1   . HIS B 2 568 ? 108.938 137.419 50.160  1.00 109.29 ? 568 HIS B CE1   1 
ATOM   8575 N  NE2   . HIS B 2 568 ? 109.010 136.757 49.019  1.00 109.84 ? 568 HIS B NE2   1 
ATOM   8576 N  N     . ALA B 2 569 ? 110.716 135.237 54.425  1.00 97.17  ? 569 ALA B N     1 
ATOM   8577 C  CA    . ALA B 2 569 ? 110.348 136.136 55.514  1.00 96.05  ? 569 ALA B CA    1 
ATOM   8578 C  C     . ALA B 2 569 ? 111.571 136.706 56.225  1.00 97.86  ? 569 ALA B C     1 
ATOM   8579 O  O     . ALA B 2 569 ? 111.539 137.853 56.683  1.00 102.69 ? 569 ALA B O     1 
ATOM   8580 C  CB    . ALA B 2 569 ? 109.447 135.411 56.512  1.00 89.45  ? 569 ALA B CB    1 
ATOM   8581 N  N     . MET B 2 570 ? 112.646 135.930 56.330  1.00 96.95  ? 570 MET B N     1 
ATOM   8582 C  CA    . MET B 2 570 ? 113.843 136.342 57.048  1.00 99.80  ? 570 MET B CA    1 
ATOM   8583 C  C     . MET B 2 570 ? 114.841 137.082 56.171  1.00 107.62 ? 570 MET B C     1 
ATOM   8584 O  O     . MET B 2 570 ? 115.899 137.481 56.669  1.00 115.72 ? 570 MET B O     1 
ATOM   8585 C  CB    . MET B 2 570 ? 114.523 135.123 57.678  1.00 97.59  ? 570 MET B CB    1 
ATOM   8586 C  CG    . MET B 2 570 ? 114.010 134.788 59.065  1.00 99.31  ? 570 MET B CG    1 
ATOM   8587 S  SD    . MET B 2 570 ? 112.210 134.784 59.124  1.00 97.32  ? 570 MET B SD    1 
ATOM   8588 C  CE    . MET B 2 570 ? 111.911 136.212 60.157  1.00 91.25  ? 570 MET B CE    1 
ATOM   8589 N  N     . ALA B 2 571 ? 114.547 137.247 54.880  1.00 104.31 ? 571 ALA B N     1 
ATOM   8590 C  CA    . ALA B 2 571 ? 115.386 138.094 54.040  1.00 107.54 ? 571 ALA B CA    1 
ATOM   8591 C  C     . ALA B 2 571 ? 115.480 139.513 54.587  1.00 115.10 ? 571 ALA B C     1 
ATOM   8592 O  O     . ALA B 2 571 ? 116.479 140.202 54.352  1.00 115.36 ? 571 ALA B O     1 
ATOM   8593 C  CB    . ALA B 2 571 ? 114.849 138.111 52.609  1.00 101.91 ? 571 ALA B CB    1 
ATOM   8594 N  N     . GLU B 2 572 ? 114.452 139.970 55.309  1.00 116.47 ? 572 GLU B N     1 
ATOM   8595 C  CA    . GLU B 2 572 ? 114.514 141.288 55.933  1.00 119.52 ? 572 GLU B CA    1 
ATOM   8596 C  C     . GLU B 2 572 ? 115.624 141.356 56.975  1.00 117.91 ? 572 GLU B C     1 
ATOM   8597 O  O     . GLU B 2 572 ? 116.383 142.331 57.022  1.00 119.46 ? 572 GLU B O     1 
ATOM   8598 C  CB    . GLU B 2 572 ? 113.167 141.633 56.567  1.00 119.51 ? 572 GLU B CB    1 
ATOM   8599 C  CG    . GLU B 2 572 ? 112.022 141.765 55.579  1.00 124.67 ? 572 GLU B CG    1 
ATOM   8600 C  CD    . GLU B 2 572 ? 110.840 142.513 56.165  1.00 128.74 ? 572 GLU B CD    1 
ATOM   8601 O  OE1   . GLU B 2 572 ? 110.720 142.558 57.407  1.00 128.01 ? 572 GLU B OE1   1 
ATOM   8602 O  OE2   . GLU B 2 572 ? 110.031 143.059 55.385  1.00 128.56 ? 572 GLU B OE2   1 
ATOM   8603 N  N     . LEU B 2 573 ? 115.734 140.330 57.819  1.00 112.50 ? 573 LEU B N     1 
ATOM   8604 C  CA    . LEU B 2 573 ? 116.766 140.294 58.849  1.00 112.03 ? 573 LEU B CA    1 
ATOM   8605 C  C     . LEU B 2 573 ? 118.141 139.957 58.294  1.00 113.41 ? 573 LEU B C     1 
ATOM   8606 O  O     . LEU B 2 573 ? 119.149 140.445 58.817  1.00 115.36 ? 573 LEU B O     1 
ATOM   8607 C  CB    . LEU B 2 573 ? 116.397 139.277 59.933  1.00 110.97 ? 573 LEU B CB    1 
ATOM   8608 C  CG    . LEU B 2 573 ? 115.504 139.770 61.074  1.00 113.92 ? 573 LEU B CG    1 
ATOM   8609 C  CD1   . LEU B 2 573 ? 114.036 139.709 60.678  1.00 110.34 ? 573 LEU B CD1   1 
ATOM   8610 C  CD2   . LEU B 2 573 ? 115.758 138.964 62.338  1.00 100.77 ? 573 LEU B CD2   1 
ATOM   8611 N  N     . ARG B 2 574 ? 118.205 139.134 57.248  1.00 113.46 ? 574 ARG B N     1 
ATOM   8612 C  CA    . ARG B 2 574 ? 119.488 138.696 56.714  1.00 113.95 ? 574 ARG B CA    1 
ATOM   8613 C  C     . ARG B 2 574 ? 120.218 139.803 55.964  1.00 118.93 ? 574 ARG B C     1 
ATOM   8614 O  O     . ARG B 2 574 ? 121.407 139.651 55.663  1.00 118.39 ? 574 ARG B O     1 
ATOM   8615 C  CB    . ARG B 2 574 ? 119.277 137.491 55.796  1.00 111.68 ? 574 ARG B CB    1 
ATOM   8616 C  CG    . ARG B 2 574 ? 120.482 136.580 55.657  1.00 110.94 ? 574 ARG B CG    1 
ATOM   8617 C  CD    . ARG B 2 574 ? 120.271 135.573 54.540  1.00 108.51 ? 574 ARG B CD    1 
ATOM   8618 N  NE    . ARG B 2 574 ? 120.336 136.205 53.228  1.00 116.87 ? 574 ARG B NE    1 
ATOM   8619 C  CZ    . ARG B 2 574 ? 120.613 135.566 52.100  1.00 118.17 ? 574 ARG B CZ    1 
ATOM   8620 N  NH1   . ARG B 2 574 ? 120.866 134.268 52.085  1.00 113.41 ? 574 ARG B NH1   1 
ATOM   8621 N  NH2   . ARG B 2 574 ? 120.639 136.248 50.958  1.00 116.20 ? 574 ARG B NH2   1 
ATOM   8622 N  N     . ARG B 2 575 ? 119.540 140.913 55.662  1.00 120.23 ? 575 ARG B N     1 
ATOM   8623 C  CA    . ARG B 2 575 ? 120.136 141.934 54.805  1.00 122.85 ? 575 ARG B CA    1 
ATOM   8624 C  C     . ARG B 2 575 ? 121.236 142.712 55.518  1.00 121.19 ? 575 ARG B C     1 
ATOM   8625 O  O     . ARG B 2 575 ? 122.308 142.941 54.946  1.00 115.43 ? 575 ARG B O     1 
ATOM   8626 C  CB    . ARG B 2 575 ? 119.053 142.887 54.302  1.00 124.38 ? 575 ARG B CB    1 
ATOM   8627 C  CG    . ARG B 2 575 ? 118.450 142.500 52.962  1.00 126.30 ? 575 ARG B CG    1 
ATOM   8628 C  CD    . ARG B 2 575 ? 117.069 143.107 52.797  1.00 126.70 ? 575 ARG B CD    1 
ATOM   8629 N  NE    . ARG B 2 575 ? 117.044 144.505 53.212  1.00 129.94 ? 575 ARG B NE    1 
ATOM   8630 C  CZ    . ARG B 2 575 ? 115.959 145.144 53.625  1.00 129.91 ? 575 ARG B CZ    1 
ATOM   8631 N  NH1   . ARG B 2 575 ? 114.782 144.542 53.682  1.00 127.81 ? 575 ARG B NH1   1 
ATOM   8632 N  NH2   . ARG B 2 575 ? 116.057 146.418 53.993  1.00 124.99 ? 575 ARG B NH2   1 
ATOM   8633 N  N     . ASP B 2 576 ? 120.994 143.133 56.763  1.00 116.50 ? 576 ASP B N     1 
ATOM   8634 C  CA    . ASP B 2 576 ? 121.872 144.095 57.422  1.00 114.15 ? 576 ASP B CA    1 
ATOM   8635 C  C     . ASP B 2 576 ? 122.332 143.637 58.802  1.00 109.06 ? 576 ASP B C     1 
ATOM   8636 O  O     . ASP B 2 576 ? 122.619 144.480 59.656  1.00 107.12 ? 576 ASP B O     1 
ATOM   8637 C  CB    . ASP B 2 576 ? 121.179 145.456 57.543  1.00 116.80 ? 576 ASP B CB    1 
ATOM   8638 C  CG    . ASP B 2 576 ? 120.825 146.056 56.197  1.00 123.31 ? 576 ASP B CG    1 
ATOM   8639 O  OD1   . ASP B 2 576 ? 121.448 145.674 55.186  1.00 124.58 ? 576 ASP B OD1   1 
ATOM   8640 O  OD2   . ASP B 2 576 ? 119.915 146.911 56.151  1.00 122.39 ? 576 ASP B OD2   1 
ATOM   8641 N  N     . ARG B 2 577 ? 122.414 142.327 59.050  1.00 105.56 ? 577 ARG B N     1 
ATOM   8642 C  CA    . ARG B 2 577 ? 122.757 141.851 60.386  1.00 101.92 ? 577 ARG B CA    1 
ATOM   8643 C  C     . ARG B 2 577 ? 123.916 140.858 60.390  1.00 98.59  ? 577 ARG B C     1 
ATOM   8644 O  O     . ARG B 2 577 ? 124.121 140.173 61.396  1.00 97.85  ? 577 ARG B O     1 
ATOM   8645 C  CB    . ARG B 2 577 ? 121.533 141.234 61.069  1.00 101.81 ? 577 ARG B CB    1 
ATOM   8646 C  CG    . ARG B 2 577 ? 120.380 142.207 61.248  1.00 104.55 ? 577 ARG B CG    1 
ATOM   8647 C  CD    . ARG B 2 577 ? 119.147 141.524 61.814  1.00 105.12 ? 577 ARG B CD    1 
ATOM   8648 N  NE    . ARG B 2 577 ? 117.980 142.398 61.785  1.00 106.29 ? 577 ARG B NE    1 
ATOM   8649 C  CZ    . ARG B 2 577 ? 117.788 143.423 62.605  1.00 105.33 ? 577 ARG B CZ    1 
ATOM   8650 N  NH1   . ARG B 2 577 ? 118.663 143.728 63.549  1.00 101.02 ? 577 ARG B NH1   1 
ATOM   8651 N  NH2   . ARG B 2 577 ? 116.689 144.160 62.475  1.00 109.40 ? 577 ARG B NH2   1 
ATOM   8652 N  N     . THR B 2 578 ? 124.684 140.777 59.303  1.00 97.64  ? 578 THR B N     1 
ATOM   8653 C  CA    . THR B 2 578 ? 125.888 139.945 59.234  1.00 96.31  ? 578 THR B CA    1 
ATOM   8654 C  C     . THR B 2 578 ? 125.598 138.511 59.682  1.00 90.75  ? 578 THR B C     1 
ATOM   8655 O  O     . THR B 2 578 ? 126.105 138.027 60.695  1.00 87.19  ? 578 THR B O     1 
ATOM   8656 C  CB    . THR B 2 578 ? 127.021 140.555 60.061  1.00 91.38  ? 578 THR B CB    1 
ATOM   8657 O  OG1   . THR B 2 578 ? 127.013 141.978 59.909  1.00 93.99  ? 578 THR B OG1   1 
ATOM   8658 C  CG2   . THR B 2 578 ? 128.364 140.011 59.609  1.00 90.93  ? 578 THR B CG2   1 
ATOM   8659 N  N     . SER B 2 579 ? 124.752 137.840 58.910  1.00 84.67  ? 579 SER B N     1 
ATOM   8660 C  CA    . SER B 2 579 ? 124.292 136.511 59.285  1.00 80.06  ? 579 SER B CA    1 
ATOM   8661 C  C     . SER B 2 579 ? 125.396 135.478 59.101  1.00 79.29  ? 579 SER B C     1 
ATOM   8662 O  O     . SER B 2 579 ? 126.053 135.432 58.057  1.00 79.12  ? 579 SER B O     1 
ATOM   8663 C  CB    . SER B 2 579 ? 123.067 136.131 58.459  1.00 88.38  ? 579 SER B CB    1 
ATOM   8664 O  OG    . SER B 2 579 ? 122.119 137.184 58.444  1.00 95.41  ? 579 SER B OG    1 
ATOM   8665 N  N     . PHE B 2 580 ? 125.602 134.649 60.124  1.00 79.66  ? 580 PHE B N     1 
ATOM   8666 C  CA    . PHE B 2 580 ? 126.476 133.483 60.044  1.00 75.89  ? 580 PHE B CA    1 
ATOM   8667 C  C     . PHE B 2 580 ? 125.591 132.255 59.878  1.00 68.02  ? 580 PHE B C     1 
ATOM   8668 O  O     . PHE B 2 580 ? 124.832 131.904 60.787  1.00 68.13  ? 580 PHE B O     1 
ATOM   8669 C  CB    . PHE B 2 580 ? 127.351 133.357 61.289  1.00 72.02  ? 580 PHE B CB    1 
ATOM   8670 C  CG    . PHE B 2 580 ? 128.641 134.116 61.207  1.00 70.48  ? 580 PHE B CG    1 
ATOM   8671 C  CD1   . PHE B 2 580 ? 128.704 135.444 61.591  1.00 75.53  ? 580 PHE B CD1   1 
ATOM   8672 C  CD2   . PHE B 2 580 ? 129.792 133.501 60.753  1.00 62.97  ? 580 PHE B CD2   1 
ATOM   8673 C  CE1   . PHE B 2 580 ? 129.890 136.143 61.520  1.00 75.16  ? 580 PHE B CE1   1 
ATOM   8674 C  CE2   . PHE B 2 580 ? 130.980 134.194 60.680  1.00 64.94  ? 580 PHE B CE2   1 
ATOM   8675 C  CZ    . PHE B 2 580 ? 131.029 135.518 61.064  1.00 73.16  ? 580 PHE B CZ    1 
ATOM   8676 N  N     . ILE B 2 581 ? 125.691 131.599 58.727  1.00 64.78  ? 581 ILE B N     1 
ATOM   8677 C  CA    . ILE B 2 581 ? 124.833 130.470 58.393  1.00 68.03  ? 581 ILE B CA    1 
ATOM   8678 C  C     . ILE B 2 581 ? 125.680 129.209 58.392  1.00 68.88  ? 581 ILE B C     1 
ATOM   8679 O  O     . ILE B 2 581 ? 126.680 129.122 57.669  1.00 69.47  ? 581 ILE B O     1 
ATOM   8680 C  CB    . ILE B 2 581 ? 124.143 130.659 57.034  1.00 67.49  ? 581 ILE B CB    1 
ATOM   8681 C  CG1   . ILE B 2 581 ? 123.702 132.109 56.851  1.00 71.51  ? 581 ILE B CG1   1 
ATOM   8682 C  CG2   . ILE B 2 581 ? 122.950 129.728 56.918  1.00 61.53  ? 581 ILE B CG2   1 
ATOM   8683 C  CD1   . ILE B 2 581 ? 122.661 132.555 57.829  1.00 72.00  ? 581 ILE B CD1   1 
ATOM   8684 N  N     . ILE B 2 582 ? 125.281 128.234 59.201  1.00 62.88  ? 582 ILE B N     1 
ATOM   8685 C  CA    . ILE B 2 582 ? 125.836 126.889 59.161  1.00 62.57  ? 582 ILE B CA    1 
ATOM   8686 C  C     . ILE B 2 582 ? 124.739 125.972 58.651  1.00 66.87  ? 582 ILE B C     1 
ATOM   8687 O  O     . ILE B 2 582 ? 123.680 125.854 59.278  1.00 69.47  ? 582 ILE B O     1 
ATOM   8688 C  CB    . ILE B 2 582 ? 126.345 126.438 60.538  1.00 55.54  ? 582 ILE B CB    1 
ATOM   8689 C  CG1   . ILE B 2 582 ? 127.534 127.294 60.971  1.00 54.97  ? 582 ILE B CG1   1 
ATOM   8690 C  CG2   . ILE B 2 582 ? 126.718 124.969 60.511  1.00 56.31  ? 582 ILE B CG2   1 
ATOM   8691 C  CD1   . ILE B 2 582 ? 127.768 127.296 62.456  1.00 54.25  ? 582 ILE B CD1   1 
ATOM   8692 N  N     . ALA B 2 583 ? 124.979 125.332 57.512  1.00 62.14  ? 583 ALA B N     1 
ATOM   8693 C  CA    . ALA B 2 583 ? 123.955 124.503 56.900  1.00 65.27  ? 583 ALA B CA    1 
ATOM   8694 C  C     . ALA B 2 583 ? 124.607 123.395 56.094  1.00 63.86  ? 583 ALA B C     1 
ATOM   8695 O  O     . ALA B 2 583 ? 125.602 123.622 55.402  1.00 67.02  ? 583 ALA B O     1 
ATOM   8696 C  CB    . ALA B 2 583 ? 123.033 125.333 56.002  1.00 70.93  ? 583 ALA B CB    1 
ATOM   8697 N  N     . HIS B 2 584 ? 124.042 122.195 56.198  1.00 61.72  ? 584 HIS B N     1 
ATOM   8698 C  CA    . HIS B 2 584 ? 124.427 121.099 55.323  1.00 60.27  ? 584 HIS B CA    1 
ATOM   8699 C  C     . HIS B 2 584 ? 123.599 121.055 54.049  1.00 67.54  ? 584 HIS B C     1 
ATOM   8700 O  O     . HIS B 2 584 ? 123.943 120.304 53.129  1.00 70.99  ? 584 HIS B O     1 
ATOM   8701 C  CB    . HIS B 2 584 ? 124.313 119.765 56.065  1.00 57.38  ? 584 HIS B CB    1 
ATOM   8702 C  CG    . HIS B 2 584 ? 125.256 119.637 57.220  1.00 55.58  ? 584 HIS B CG    1 
ATOM   8703 N  ND1   . HIS B 2 584 ? 126.615 119.485 57.056  1.00 55.52  ? 584 HIS B ND1   1 
ATOM   8704 C  CD2   . HIS B 2 584 ? 125.037 119.643 58.555  1.00 53.54  ? 584 HIS B CD2   1 
ATOM   8705 C  CE1   . HIS B 2 584 ? 127.193 119.399 58.240  1.00 52.22  ? 584 HIS B CE1   1 
ATOM   8706 N  NE2   . HIS B 2 584 ? 126.258 119.492 59.167  1.00 54.73  ? 584 HIS B NE2   1 
ATOM   8707 N  N     . ARG B 2 585 ? 122.526 121.839 53.974  1.00 67.82  ? 585 ARG B N     1 
ATOM   8708 C  CA    . ARG B 2 585 ? 121.759 122.006 52.743  1.00 71.41  ? 585 ARG B CA    1 
ATOM   8709 C  C     . ARG B 2 585 ? 122.371 123.161 51.964  1.00 78.73  ? 585 ARG B C     1 
ATOM   8710 O  O     . ARG B 2 585 ? 122.242 124.324 52.351  1.00 80.17  ? 585 ARG B O     1 
ATOM   8711 C  CB    . ARG B 2 585 ? 120.288 122.268 53.046  1.00 74.05  ? 585 ARG B CB    1 
ATOM   8712 C  CG    . ARG B 2 585 ? 119.570 121.141 53.763  1.00 76.81  ? 585 ARG B CG    1 
ATOM   8713 C  CD    . ARG B 2 585 ? 118.105 121.491 53.968  1.00 84.13  ? 585 ARG B CD    1 
ATOM   8714 N  NE    . ARG B 2 585 ? 117.403 120.517 54.794  1.00 84.11  ? 585 ARG B NE    1 
ATOM   8715 C  CZ    . ARG B 2 585 ? 116.213 120.721 55.340  1.00 78.08  ? 585 ARG B CZ    1 
ATOM   8716 N  NH1   . ARG B 2 585 ? 115.563 121.860 55.174  1.00 79.79  ? 585 ARG B NH1   1 
ATOM   8717 N  NH2   . ARG B 2 585 ? 115.660 119.757 56.070  1.00 69.81  ? 585 ARG B NH2   1 
ATOM   8718 N  N     . LEU B 2 586 ? 123.046 122.843 50.859  1.00 80.60  ? 586 LEU B N     1 
ATOM   8719 C  CA    . LEU B 2 586 ? 123.730 123.872 50.086  1.00 79.36  ? 586 LEU B CA    1 
ATOM   8720 C  C     . LEU B 2 586 ? 122.763 124.821 49.391  1.00 82.74  ? 586 LEU B C     1 
ATOM   8721 O  O     . LEU B 2 586 ? 123.145 125.952 49.071  1.00 86.75  ? 586 LEU B O     1 
ATOM   8722 C  CB    . LEU B 2 586 ? 124.663 123.221 49.067  1.00 80.58  ? 586 LEU B CB    1 
ATOM   8723 C  CG    . LEU B 2 586 ? 125.621 122.188 49.664  1.00 80.27  ? 586 LEU B CG    1 
ATOM   8724 C  CD1   . LEU B 2 586 ? 126.546 121.622 48.601  1.00 79.84  ? 586 LEU B CD1   1 
ATOM   8725 C  CD2   . LEU B 2 586 ? 126.416 122.792 50.812  1.00 70.68  ? 586 LEU B CD2   1 
ATOM   8726 N  N     . SER B 2 587 ? 121.521 124.393 49.157  1.00 83.77  ? 587 SER B N     1 
ATOM   8727 C  CA    . SER B 2 587 ? 120.533 125.289 48.568  1.00 83.66  ? 587 SER B CA    1 
ATOM   8728 C  C     . SER B 2 587 ? 120.220 126.460 49.489  1.00 83.24  ? 587 SER B C     1 
ATOM   8729 O  O     . SER B 2 587 ? 120.019 127.584 49.014  1.00 85.63  ? 587 SER B O     1 
ATOM   8730 C  CB    . SER B 2 587 ? 119.257 124.519 48.236  1.00 86.35  ? 587 SER B CB    1 
ATOM   8731 O  OG    . SER B 2 587 ? 118.737 123.879 49.387  1.00 88.37  ? 587 SER B OG    1 
ATOM   8732 N  N     . THR B 2 588 ? 120.171 126.221 50.801  1.00 81.77  ? 588 THR B N     1 
ATOM   8733 C  CA    . THR B 2 588 ? 119.894 127.294 51.748  1.00 81.39  ? 588 THR B CA    1 
ATOM   8734 C  C     . THR B 2 588 ? 121.021 128.315 51.818  1.00 82.75  ? 588 THR B C     1 
ATOM   8735 O  O     . THR B 2 588 ? 120.755 129.493 52.078  1.00 78.28  ? 588 THR B O     1 
ATOM   8736 C  CB    . THR B 2 588 ? 119.637 126.719 53.141  1.00 79.59  ? 588 THR B CB    1 
ATOM   8737 O  OG1   . THR B 2 588 ? 120.861 126.212 53.682  1.00 80.49  ? 588 THR B OG1   1 
ATOM   8738 C  CG2   . THR B 2 588 ? 118.620 125.594 53.071  1.00 82.39  ? 588 THR B CG2   1 
ATOM   8739 N  N     . ILE B 2 589 ? 122.267 127.899 51.595  1.00 85.15  ? 589 ILE B N     1 
ATOM   8740 C  CA    . ILE B 2 589 ? 123.409 128.804 51.636  1.00 81.57  ? 589 ILE B CA    1 
ATOM   8741 C  C     . ILE B 2 589 ? 123.839 129.257 50.256  1.00 86.92  ? 589 ILE B C     1 
ATOM   8742 O  O     . ILE B 2 589 ? 124.852 129.959 50.136  1.00 90.69  ? 589 ILE B O     1 
ATOM   8743 C  CB    . ILE B 2 589 ? 124.600 128.177 52.385  1.00 81.79  ? 589 ILE B CB    1 
ATOM   8744 C  CG1   . ILE B 2 589 ? 124.931 126.795 51.822  1.00 81.94  ? 589 ILE B CG1   1 
ATOM   8745 C  CG2   . ILE B 2 589 ? 124.306 128.095 53.872  1.00 76.10  ? 589 ILE B CG2   1 
ATOM   8746 C  CD1   . ILE B 2 589 ? 126.061 126.793 50.810  1.00 81.51  ? 589 ILE B CD1   1 
ATOM   8747 N  N     . ARG B 2 590 ? 123.117 128.868 49.208  1.00 91.68  ? 590 ARG B N     1 
ATOM   8748 C  CA    . ARG B 2 590 ? 123.390 129.408 47.885  1.00 93.41  ? 590 ARG B CA    1 
ATOM   8749 C  C     . ARG B 2 590 ? 123.183 130.919 47.888  1.00 97.34  ? 590 ARG B C     1 
ATOM   8750 O  O     . ARG B 2 590 ? 122.472 131.467 48.734  1.00 97.48  ? 590 ARG B O     1 
ATOM   8751 C  CB    . ARG B 2 590 ? 122.488 128.744 46.842  1.00 95.95  ? 590 ARG B CB    1 
ATOM   8752 C  CG    . ARG B 2 590 ? 123.032 128.774 45.421  1.00 96.80  ? 590 ARG B CG    1 
ATOM   8753 C  CD    . ARG B 2 590 ? 122.418 129.907 44.613  1.00 102.62 ? 590 ARG B CD    1 
ATOM   8754 N  NE    . ARG B 2 590 ? 123.223 130.253 43.447  1.00 106.74 ? 590 ARG B NE    1 
ATOM   8755 C  CZ    . ARG B 2 590 ? 123.068 129.719 42.244  1.00 111.14 ? 590 ARG B CZ    1 
ATOM   8756 N  NH1   . ARG B 2 590 ? 122.142 128.804 42.007  1.00 113.31 ? 590 ARG B NH1   1 
ATOM   8757 N  NH2   . ARG B 2 590 ? 123.861 130.113 41.252  1.00 108.06 ? 590 ARG B NH2   1 
ATOM   8758 N  N     . ASP B 2 591 ? 123.851 131.593 46.951  1.00 98.85  ? 591 ASP B N     1 
ATOM   8759 C  CA    . ASP B 2 591 ? 123.865 133.044 46.764  1.00 104.40 ? 591 ASP B CA    1 
ATOM   8760 C  C     . ASP B 2 591 ? 124.314 133.806 48.007  1.00 102.58 ? 591 ASP B C     1 
ATOM   8761 O  O     . ASP B 2 591 ? 124.140 135.030 48.071  1.00 104.43 ? 591 ASP B O     1 
ATOM   8762 C  CB    . ASP B 2 591 ? 122.515 133.577 46.242  1.00 105.39 ? 591 ASP B CB    1 
ATOM   8763 C  CG    . ASP B 2 591 ? 121.403 133.604 47.295  1.00 107.44 ? 591 ASP B CG    1 
ATOM   8764 O  OD1   . ASP B 2 591 ? 121.597 134.122 48.415  1.00 106.59 ? 591 ASP B OD1   1 
ATOM   8765 O  OD2   . ASP B 2 591 ? 120.307 133.089 46.988  1.00 103.18 ? 591 ASP B OD2   1 
ATOM   8766 N  N     . ALA B 2 592 ? 124.901 133.126 48.989  1.00 97.62  ? 592 ALA B N     1 
ATOM   8767 C  CA    . ALA B 2 592 ? 125.503 133.814 50.120  1.00 93.43  ? 592 ALA B CA    1 
ATOM   8768 C  C     . ALA B 2 592 ? 126.732 134.594 49.669  1.00 95.42  ? 592 ALA B C     1 
ATOM   8769 O  O     . ALA B 2 592 ? 127.445 134.195 48.744  1.00 94.83  ? 592 ALA B O     1 
ATOM   8770 C  CB    . ALA B 2 592 ? 125.886 132.820 51.215  1.00 87.19  ? 592 ALA B CB    1 
ATOM   8771 N  N     . ASP B 2 593 ? 126.970 135.726 50.333  1.00 96.10  ? 593 ASP B N     1 
ATOM   8772 C  CA    . ASP B 2 593 ? 128.069 136.600 49.935  1.00 95.53  ? 593 ASP B CA    1 
ATOM   8773 C  C     . ASP B 2 593 ? 129.419 135.914 50.102  1.00 94.11  ? 593 ASP B C     1 
ATOM   8774 O  O     . ASP B 2 593 ? 130.292 136.028 49.234  1.00 93.36  ? 593 ASP B O     1 
ATOM   8775 C  CB    . ASP B 2 593 ? 128.011 137.899 50.737  1.00 94.60  ? 593 ASP B CB    1 
ATOM   8776 C  CG    . ASP B 2 593 ? 126.616 138.488 50.781  1.00 100.96 ? 593 ASP B CG    1 
ATOM   8777 O  OD1   . ASP B 2 593 ? 125.740 137.992 50.041  1.00 103.12 ? 593 ASP B OD1   1 
ATOM   8778 O  OD2   . ASP B 2 593 ? 126.390 139.448 51.545  1.00 101.49 ? 593 ASP B OD2   1 
ATOM   8779 N  N     . LEU B 2 594 ? 129.611 135.198 51.205  1.00 92.50  ? 594 LEU B N     1 
ATOM   8780 C  CA    . LEU B 2 594 ? 130.847 134.470 51.458  1.00 86.17  ? 594 LEU B CA    1 
ATOM   8781 C  C     . LEU B 2 594 ? 130.501 133.076 51.955  1.00 81.06  ? 594 LEU B C     1 
ATOM   8782 O  O     . LEU B 2 594 ? 129.658 132.923 52.844  1.00 84.33  ? 594 LEU B O     1 
ATOM   8783 C  CB    . LEU B 2 594 ? 131.721 135.202 52.483  1.00 86.42  ? 594 LEU B CB    1 
ATOM   8784 C  CG    . LEU B 2 594 ? 133.012 134.519 52.943  1.00 83.40  ? 594 LEU B CG    1 
ATOM   8785 C  CD1   . LEU B 2 594 ? 133.810 133.985 51.763  1.00 83.33  ? 594 LEU B CD1   1 
ATOM   8786 C  CD2   . LEU B 2 594 ? 133.854 135.469 53.774  1.00 85.96  ? 594 LEU B CD2   1 
ATOM   8787 N  N     . ILE B 2 595 ? 131.145 132.065 51.380  1.00 79.18  ? 595 ILE B N     1 
ATOM   8788 C  CA    . ILE B 2 595 ? 130.966 130.678 51.785  1.00 77.30  ? 595 ILE B CA    1 
ATOM   8789 C  C     . ILE B 2 595 ? 132.308 130.145 52.263  1.00 77.52  ? 595 ILE B C     1 
ATOM   8790 O  O     . ILE B 2 595 ? 133.301 130.200 51.529  1.00 77.96  ? 595 ILE B O     1 
ATOM   8791 C  CB    . ILE B 2 595 ? 130.413 129.812 50.638  1.00 78.32  ? 595 ILE B CB    1 
ATOM   8792 C  CG1   . ILE B 2 595 ? 129.154 130.447 50.048  1.00 80.55  ? 595 ILE B CG1   1 
ATOM   8793 C  CG2   . ILE B 2 595 ? 130.120 128.405 51.130  1.00 77.55  ? 595 ILE B CG2   1 
ATOM   8794 C  CD1   . ILE B 2 595 ? 128.595 129.696 48.864  1.00 78.90  ? 595 ILE B CD1   1 
ATOM   8795 N  N     . LEU B 2 596 ? 132.334 129.630 53.486  1.00 74.88  ? 596 LEU B N     1 
ATOM   8796 C  CA    . LEU B 2 596 ? 133.534 129.046 54.068  1.00 72.13  ? 596 LEU B CA    1 
ATOM   8797 C  C     . LEU B 2 596 ? 133.410 127.531 54.063  1.00 70.01  ? 596 LEU B C     1 
ATOM   8798 O  O     . LEU B 2 596 ? 132.404 126.984 54.523  1.00 71.56  ? 596 LEU B O     1 
ATOM   8799 C  CB    . LEU B 2 596 ? 133.752 129.545 55.496  1.00 70.43  ? 596 LEU B CB    1 
ATOM   8800 C  CG    . LEU B 2 596 ? 133.995 131.039 55.694  1.00 77.88  ? 596 LEU B CG    1 
ATOM   8801 C  CD1   . LEU B 2 596 ? 134.073 131.351 57.173  1.00 75.37  ? 596 LEU B CD1   1 
ATOM   8802 C  CD2   . LEU B 2 596 ? 135.268 131.469 54.988  1.00 79.35  ? 596 LEU B CD2   1 
ATOM   8803 N  N     . VAL B 2 597 ? 134.427 126.859 53.538  1.00 69.20  ? 597 VAL B N     1 
ATOM   8804 C  CA    . VAL B 2 597 ? 134.506 125.405 53.555  1.00 70.50  ? 597 VAL B CA    1 
ATOM   8805 C  C     . VAL B 2 597 ? 135.667 125.033 54.463  1.00 70.13  ? 597 VAL B C     1 
ATOM   8806 O  O     . VAL B 2 597 ? 136.829 125.318 54.149  1.00 76.78  ? 597 VAL B O     1 
ATOM   8807 C  CB    . VAL B 2 597 ? 134.686 124.821 52.148  1.00 74.44  ? 597 VAL B CB    1 
ATOM   8808 C  CG1   . VAL B 2 597 ? 134.383 123.333 52.152  1.00 67.20  ? 597 VAL B CG1   1 
ATOM   8809 C  CG2   . VAL B 2 597 ? 133.797 125.549 51.153  1.00 75.01  ? 597 VAL B CG2   1 
ATOM   8810 N  N     . MET B 2 598 ? 135.359 124.406 55.592  1.00 64.62  ? 598 MET B N     1 
ATOM   8811 C  CA    . MET B 2 598 ? 136.365 123.975 56.549  1.00 69.33  ? 598 MET B CA    1 
ATOM   8812 C  C     . MET B 2 598 ? 136.231 122.476 56.766  1.00 69.47  ? 598 MET B C     1 
ATOM   8813 O  O     . MET B 2 598 ? 135.120 121.940 56.766  1.00 71.03  ? 598 MET B O     1 
ATOM   8814 C  CB    . MET B 2 598 ? 136.239 124.748 57.872  1.00 68.56  ? 598 MET B CB    1 
ATOM   8815 C  CG    . MET B 2 598 ? 135.310 124.141 58.904  1.00 63.62  ? 598 MET B CG    1 
ATOM   8816 S  SD    . MET B 2 598 ? 135.609 124.797 60.555  1.00 60.30  ? 598 MET B SD    1 
ATOM   8817 C  CE    . MET B 2 598 ? 134.572 126.252 60.524  1.00 60.02  ? 598 MET B CE    1 
ATOM   8818 N  N     . ASP B 2 599 ? 137.366 121.797 56.925  1.00 68.31  ? 599 ASP B N     1 
ATOM   8819 C  CA    . ASP B 2 599 ? 137.387 120.339 56.950  1.00 70.30  ? 599 ASP B CA    1 
ATOM   8820 C  C     . ASP B 2 599 ? 137.840 119.768 58.284  1.00 72.64  ? 599 ASP B C     1 
ATOM   8821 O  O     . ASP B 2 599 ? 137.151 118.911 58.849  1.00 68.66  ? 599 ASP B O     1 
ATOM   8822 C  CB    . ASP B 2 599 ? 138.285 119.809 55.822  1.00 71.27  ? 599 ASP B CB    1 
ATOM   8823 C  CG    . ASP B 2 599 ? 137.898 118.412 55.381  1.00 79.81  ? 599 ASP B CG    1 
ATOM   8824 O  OD1   . ASP B 2 599 ? 138.190 117.450 56.120  1.00 75.39  ? 599 ASP B OD1   1 
ATOM   8825 O  OD2   . ASP B 2 599 ? 137.294 118.277 54.296  1.00 80.40  ? 599 ASP B OD2   1 
ATOM   8826 N  N     . SER B 2 600 ? 138.986 120.201 58.800  1.00 72.03  ? 600 SER B N     1 
ATOM   8827 C  CA    . SER B 2 600 ? 139.524 119.701 60.062  1.00 71.81  ? 600 SER B CA    1 
ATOM   8828 C  C     . SER B 2 600 ? 139.886 120.860 60.976  1.00 73.48  ? 600 SER B C     1 
ATOM   8829 O  O     . SER B 2 600 ? 140.961 120.906 61.576  1.00 78.80  ? 600 SER B O     1 
ATOM   8830 C  CB    . SER B 2 600 ? 140.735 118.805 59.826  1.00 74.79  ? 600 SER B CB    1 
ATOM   8831 O  OG    . SER B 2 600 ? 140.385 117.659 59.071  1.00 81.63  ? 600 SER B OG    1 
ATOM   8832 N  N     . GLY B 2 601 ? 138.976 121.822 61.094  1.00 69.56  ? 601 GLY B N     1 
ATOM   8833 C  CA    . GLY B 2 601 ? 139.247 123.010 61.869  1.00 66.59  ? 601 GLY B CA    1 
ATOM   8834 C  C     . GLY B 2 601 ? 140.010 124.086 61.137  1.00 70.73  ? 601 GLY B C     1 
ATOM   8835 O  O     . GLY B 2 601 ? 140.373 125.093 61.753  1.00 76.40  ? 601 GLY B O     1 
ATOM   8836 N  N     . ARG B 2 602 ? 140.275 123.903 59.848  1.00 73.09  ? 602 ARG B N     1 
ATOM   8837 C  CA    . ARG B 2 602 ? 140.924 124.906 59.020  1.00 76.15  ? 602 ARG B CA    1 
ATOM   8838 C  C     . ARG B 2 602 ? 140.034 125.210 57.826  1.00 75.53  ? 602 ARG B C     1 
ATOM   8839 O  O     . ARG B 2 602 ? 139.431 124.303 57.247  1.00 77.27  ? 602 ARG B O     1 
ATOM   8840 C  CB    . ARG B 2 602 ? 142.292 124.434 58.520  1.00 77.87  ? 602 ARG B CB    1 
ATOM   8841 C  CG    . ARG B 2 602 ? 142.835 123.197 59.206  1.00 80.21  ? 602 ARG B CG    1 
ATOM   8842 C  CD    . ARG B 2 602 ? 144.152 122.787 58.574  1.00 83.22  ? 602 ARG B CD    1 
ATOM   8843 N  NE    . ARG B 2 602 ? 145.189 123.792 58.774  1.00 90.85  ? 602 ARG B NE    1 
ATOM   8844 C  CZ    . ARG B 2 602 ? 146.024 123.808 59.803  1.00 88.32  ? 602 ARG B CZ    1 
ATOM   8845 N  NH1   . ARG B 2 602 ? 146.003 122.860 60.724  1.00 81.65  ? 602 ARG B NH1   1 
ATOM   8846 N  NH2   . ARG B 2 602 ? 146.911 124.794 59.904  1.00 82.20  ? 602 ARG B NH2   1 
ATOM   8847 N  N     . ILE B 2 603 ? 139.953 126.486 57.457  1.00 75.55  ? 603 ILE B N     1 
ATOM   8848 C  CA    . ILE B 2 603 ? 139.227 126.869 56.253  1.00 75.88  ? 603 ILE B CA    1 
ATOM   8849 C  C     . ILE B 2 603 ? 140.086 126.500 55.053  1.00 74.96  ? 603 ILE B C     1 
ATOM   8850 O  O     . ILE B 2 603 ? 141.032 127.216 54.706  1.00 73.06  ? 603 ILE B O     1 
ATOM   8851 C  CB    . ILE B 2 603 ? 138.872 128.366 56.252  1.00 76.87  ? 603 ILE B CB    1 
ATOM   8852 C  CG1   . ILE B 2 603 ? 137.929 128.690 57.410  1.00 73.76  ? 603 ILE B CG1   1 
ATOM   8853 C  CG2   . ILE B 2 603 ? 138.233 128.762 54.931  1.00 75.03  ? 603 ILE B CG2   1 
ATOM   8854 C  CD1   . ILE B 2 603 ? 137.821 130.165 57.706  1.00 77.21  ? 603 ILE B CD1   1 
ATOM   8855 N  N     . ILE B 2 604 ? 139.771 125.370 54.418  1.00 73.07  ? 604 ILE B N     1 
ATOM   8856 C  CA    . ILE B 2 604 ? 140.591 124.889 53.312  1.00 78.89  ? 604 ILE B CA    1 
ATOM   8857 C  C     . ILE B 2 604 ? 140.308 125.634 52.016  1.00 82.06  ? 604 ILE B C     1 
ATOM   8858 O  O     . ILE B 2 604 ? 141.162 125.648 51.121  1.00 83.34  ? 604 ILE B O     1 
ATOM   8859 C  CB    . ILE B 2 604 ? 140.385 123.380 53.105  1.00 76.71  ? 604 ILE B CB    1 
ATOM   8860 C  CG1   . ILE B 2 604 ? 138.903 123.026 53.206  1.00 72.73  ? 604 ILE B CG1   1 
ATOM   8861 C  CG2   . ILE B 2 604 ? 141.183 122.592 54.130  1.00 77.47  ? 604 ILE B CG2   1 
ATOM   8862 C  CD1   . ILE B 2 604 ? 138.502 121.849 52.354  1.00 75.39  ? 604 ILE B CD1   1 
ATOM   8863 N  N     . GLU B 2 605 ? 139.139 126.260 51.893  1.00 79.74  ? 605 GLU B N     1 
ATOM   8864 C  CA    . GLU B 2 605 ? 138.783 127.000 50.689  1.00 82.89  ? 605 GLU B CA    1 
ATOM   8865 C  C     . GLU B 2 605 ? 137.610 127.930 50.974  1.00 83.64  ? 605 GLU B C     1 
ATOM   8866 O  O     . GLU B 2 605 ? 136.727 127.599 51.771  1.00 82.83  ? 605 GLU B O     1 
ATOM   8867 C  CB    . GLU B 2 605 ? 138.474 126.030 49.543  1.00 84.51  ? 605 GLU B CB    1 
ATOM   8868 C  CG    . GLU B 2 605 ? 137.036 125.561 49.457  1.00 85.59  ? 605 GLU B CG    1 
ATOM   8869 C  CD    . GLU B 2 605 ? 136.748 124.814 48.172  1.00 92.09  ? 605 GLU B CD    1 
ATOM   8870 O  OE1   . GLU B 2 605 ? 137.554 124.923 47.225  1.00 97.26  ? 605 GLU B OE1   1 
ATOM   8871 O  OE2   . GLU B 2 605 ? 135.722 124.107 48.111  1.00 92.94  ? 605 GLU B OE2   1 
ATOM   8872 N  N     . ARG B 2 606 ? 137.604 129.106 50.351  1.00 85.86  ? 606 ARG B N     1 
ATOM   8873 C  CA    . ARG B 2 606 ? 136.596 130.112 50.647  1.00 83.96  ? 606 ARG B CA    1 
ATOM   8874 C  C     . ARG B 2 606 ? 136.329 130.948 49.405  1.00 85.92  ? 606 ARG B C     1 
ATOM   8875 O  O     . ARG B 2 606 ? 137.130 130.983 48.468  1.00 90.35  ? 606 ARG B O     1 
ATOM   8876 C  CB    . ARG B 2 606 ? 137.026 131.006 51.815  1.00 84.14  ? 606 ARG B CB    1 
ATOM   8877 C  CG    . ARG B 2 606 ? 138.096 132.024 51.462  1.00 83.51  ? 606 ARG B CG    1 
ATOM   8878 C  CD    . ARG B 2 606 ? 138.592 132.752 52.698  1.00 82.35  ? 606 ARG B CD    1 
ATOM   8879 N  NE    . ARG B 2 606 ? 139.533 131.947 53.468  1.00 77.87  ? 606 ARG B NE    1 
ATOM   8880 C  CZ    . ARG B 2 606 ? 139.763 132.100 54.765  1.00 79.91  ? 606 ARG B CZ    1 
ATOM   8881 N  NH1   . ARG B 2 606 ? 139.127 133.015 55.477  1.00 79.39  ? 606 ARG B NH1   1 
ATOM   8882 N  NH2   . ARG B 2 606 ? 140.654 131.316 55.363  1.00 79.60  ? 606 ARG B NH2   1 
ATOM   8883 N  N     . GLY B 2 607 ? 135.193 131.621 49.415  1.00 80.99  ? 607 GLY B N     1 
ATOM   8884 C  CA    . GLY B 2 607 ? 134.763 132.420 48.284  1.00 83.17  ? 607 GLY B CA    1 
ATOM   8885 C  C     . GLY B 2 607 ? 133.266 132.290 48.096  1.00 84.88  ? 607 GLY B C     1 
ATOM   8886 O  O     . GLY B 2 607 ? 132.580 131.592 48.836  1.00 85.85  ? 607 GLY B O     1 
ATOM   8887 N  N     . THR B 2 608 ? 132.770 132.989 47.080  1.00 89.65  ? 608 THR B N     1 
ATOM   8888 C  CA    . THR B 2 608 ? 131.353 132.915 46.766  1.00 91.08  ? 608 THR B CA    1 
ATOM   8889 C  C     . THR B 2 608 ? 131.043 131.645 45.980  1.00 90.00  ? 608 THR B C     1 
ATOM   8890 O  O     . THR B 2 608 ? 131.931 130.868 45.623  1.00 87.46  ? 608 THR B O     1 
ATOM   8891 C  CB    . THR B 2 608 ? 130.899 134.144 45.976  1.00 94.51  ? 608 THR B CB    1 
ATOM   8892 O  OG1   . THR B 2 608 ? 131.087 133.914 44.574  1.00 97.46  ? 608 THR B OG1   1 
ATOM   8893 C  CG2   . THR B 2 608 ? 131.679 135.374 46.401  1.00 92.89  ? 608 THR B CG2   1 
ATOM   8894 N  N     . HIS B 2 609 ? 129.751 131.447 45.711  1.00 92.50  ? 609 HIS B N     1 
ATOM   8895 C  CA    . HIS B 2 609 ? 129.302 130.233 45.037  1.00 94.26  ? 609 HIS B CA    1 
ATOM   8896 C  C     . HIS B 2 609 ? 129.929 130.104 43.655  1.00 94.15  ? 609 HIS B C     1 
ATOM   8897 O  O     . HIS B 2 609 ? 130.404 129.028 43.272  1.00 95.20  ? 609 HIS B O     1 
ATOM   8898 C  CB    . HIS B 2 609 ? 127.775 130.237 44.946  1.00 97.11  ? 609 HIS B CB    1 
ATOM   8899 C  CG    . HIS B 2 609 ? 127.199 129.011 44.310  1.00 100.10 ? 609 HIS B CG    1 
ATOM   8900 N  ND1   . HIS B 2 609 ? 127.155 127.791 44.949  1.00 99.28  ? 609 HIS B ND1   1 
ATOM   8901 C  CD2   . HIS B 2 609 ? 126.621 128.823 43.100  1.00 98.55  ? 609 HIS B CD2   1 
ATOM   8902 C  CE1   . HIS B 2 609 ? 126.587 126.901 44.155  1.00 97.29  ? 609 HIS B CE1   1 
ATOM   8903 N  NE2   . HIS B 2 609 ? 126.252 127.502 43.028  1.00 99.07  ? 609 HIS B NE2   1 
ATOM   8904 N  N     . GLU B 2 610 ? 129.954 131.202 42.896  1.00 96.28  ? 610 GLU B N     1 
ATOM   8905 C  CA    . GLU B 2 610 ? 130.483 131.154 41.537  1.00 95.37  ? 610 GLU B CA    1 
ATOM   8906 C  C     . GLU B 2 610 ? 131.979 130.868 41.530  1.00 93.53  ? 610 GLU B C     1 
ATOM   8907 O  O     . GLU B 2 610 ? 132.454 130.038 40.745  1.00 92.46  ? 610 GLU B O     1 
ATOM   8908 C  CB    . GLU B 2 610 ? 130.183 132.466 40.813  1.00 97.85  ? 610 GLU B CB    1 
ATOM   8909 C  CG    . GLU B 2 610 ? 128.704 132.713 40.559  1.00 101.21 ? 610 GLU B CG    1 
ATOM   8910 C  CD    . GLU B 2 610 ? 127.978 133.228 41.786  1.00 103.29 ? 610 GLU B CD    1 
ATOM   8911 O  OE1   . GLU B 2 610 ? 128.629 133.875 42.633  1.00 99.96  ? 610 GLU B OE1   1 
ATOM   8912 O  OE2   . GLU B 2 610 ? 126.759 132.985 41.905  1.00 104.55 ? 610 GLU B OE2   1 
ATOM   8913 N  N     . GLU B 2 611 ? 132.741 131.545 42.392  1.00 94.51  ? 611 GLU B N     1 
ATOM   8914 C  CA    . GLU B 2 611 ? 134.180 131.310 42.438  1.00 95.05  ? 611 GLU B CA    1 
ATOM   8915 C  C     . GLU B 2 611 ? 134.500 129.904 42.928  1.00 91.78  ? 611 GLU B C     1 
ATOM   8916 O  O     . GLU B 2 611 ? 135.411 129.251 42.406  1.00 93.37  ? 611 GLU B O     1 
ATOM   8917 C  CB    . GLU B 2 611 ? 134.865 132.353 43.321  1.00 97.60  ? 611 GLU B CB    1 
ATOM   8918 C  CG    . GLU B 2 611 ? 134.280 133.748 43.218  1.00 100.95 ? 611 GLU B CG    1 
ATOM   8919 C  CD    . GLU B 2 611 ? 135.007 134.742 44.100  1.00 105.21 ? 611 GLU B CD    1 
ATOM   8920 O  OE1   . GLU B 2 611 ? 134.337 135.572 44.746  1.00 101.49 ? 611 GLU B OE1   1 
ATOM   8921 O  OE2   . GLU B 2 611 ? 136.253 134.690 44.151  1.00 108.25 ? 611 GLU B OE2   1 
ATOM   8922 N  N     . LEU B 2 612 ? 133.771 129.423 43.936  1.00 93.60  ? 612 LEU B N     1 
ATOM   8923 C  CA    . LEU B 2 612 ? 134.008 128.072 44.436  1.00 91.38  ? 612 LEU B CA    1 
ATOM   8924 C  C     . LEU B 2 612 ? 133.683 127.026 43.378  1.00 90.89  ? 612 LEU B C     1 
ATOM   8925 O  O     . LEU B 2 612 ? 134.386 126.015 43.265  1.00 92.59  ? 612 LEU B O     1 
ATOM   8926 C  CB    . LEU B 2 612 ? 133.198 127.830 45.708  1.00 91.53  ? 612 LEU B CB    1 
ATOM   8927 C  CG    . LEU B 2 612 ? 133.671 128.566 46.963  1.00 88.31  ? 612 LEU B CG    1 
ATOM   8928 C  CD1   . LEU B 2 612 ? 132.948 128.050 48.193  1.00 86.68  ? 612 LEU B CD1   1 
ATOM   8929 C  CD2   . LEU B 2 612 ? 135.173 128.420 47.129  1.00 85.71  ? 612 LEU B CD2   1 
ATOM   8930 N  N     . LEU B 2 613 ? 132.618 127.241 42.603  1.00 93.41  ? 613 LEU B N     1 
ATOM   8931 C  CA    . LEU B 2 613 ? 132.332 126.339 41.491  1.00 96.95  ? 613 LEU B CA    1 
ATOM   8932 C  C     . LEU B 2 613 ? 133.428 126.401 40.433  1.00 96.85  ? 613 LEU B C     1 
ATOM   8933 O  O     . LEU B 2 613 ? 133.856 125.364 39.913  1.00 94.92  ? 613 LEU B O     1 
ATOM   8934 C  CB    . LEU B 2 613 ? 130.976 126.674 40.874  1.00 93.76  ? 613 LEU B CB    1 
ATOM   8935 C  CG    . LEU B 2 613 ? 129.743 126.250 41.669  1.00 92.96  ? 613 LEU B CG    1 
ATOM   8936 C  CD1   . LEU B 2 613 ? 128.485 126.485 40.854  1.00 91.41  ? 613 LEU B CD1   1 
ATOM   8937 C  CD2   . LEU B 2 613 ? 129.852 124.794 42.088  1.00 93.50  ? 613 LEU B CD2   1 
ATOM   8938 N  N     . ALA B 2 614 ? 133.892 127.608 40.100  1.00 96.35  ? 614 ALA B N     1 
ATOM   8939 C  CA    . ALA B 2 614 ? 134.942 127.755 39.097  1.00 93.09  ? 614 ALA B CA    1 
ATOM   8940 C  C     . ALA B 2 614 ? 136.262 127.160 39.568  1.00 96.19  ? 614 ALA B C     1 
ATOM   8941 O  O     . ALA B 2 614 ? 136.982 126.545 38.774  1.00 94.86  ? 614 ALA B O     1 
ATOM   8942 C  CB    . ALA B 2 614 ? 135.123 129.229 38.740  1.00 92.22  ? 614 ALA B CB    1 
ATOM   8943 N  N     . ARG B 2 615 ? 136.596 127.334 40.845  1.00 96.88  ? 615 ARG B N     1 
ATOM   8944 C  CA    . ARG B 2 615 ? 137.830 126.803 41.407  1.00 95.97  ? 615 ARG B CA    1 
ATOM   8945 C  C     . ARG B 2 615 ? 137.790 125.287 41.578  1.00 96.43  ? 615 ARG B C     1 
ATOM   8946 O  O     . ARG B 2 615 ? 138.847 124.669 41.751  1.00 93.47  ? 615 ARG B O     1 
ATOM   8947 C  CB    . ARG B 2 615 ? 138.110 127.510 42.744  1.00 97.36  ? 615 ARG B CB    1 
ATOM   8948 C  CG    . ARG B 2 615 ? 139.069 126.821 43.704  1.00 98.78  ? 615 ARG B CG    1 
ATOM   8949 C  CD    . ARG B 2 615 ? 140.185 127.766 44.134  1.00 99.42  ? 615 ARG B CD    1 
ATOM   8950 N  NE    . ARG B 2 615 ? 139.688 129.077 44.536  1.00 105.36 ? 615 ARG B NE    1 
ATOM   8951 C  CZ    . ARG B 2 615 ? 138.940 129.309 45.607  1.00 106.02 ? 615 ARG B CZ    1 
ATOM   8952 N  NH1   . ARG B 2 615 ? 138.604 128.338 46.441  1.00 100.74 ? 615 ARG B NH1   1 
ATOM   8953 N  NH2   . ARG B 2 615 ? 138.526 130.549 45.852  1.00 102.46 ? 615 ARG B NH2   1 
ATOM   8954 N  N     . HIS B 2 616 ? 136.606 124.678 41.476  1.00 98.20  ? 616 HIS B N     1 
ATOM   8955 C  CA    . HIS B 2 616 ? 136.388 123.251 41.736  1.00 96.98  ? 616 HIS B CA    1 
ATOM   8956 C  C     . HIS B 2 616 ? 136.671 123.013 43.215  1.00 100.65 ? 616 HIS B C     1 
ATOM   8957 O  O     . HIS B 2 616 ? 136.052 123.689 44.056  1.00 98.11  ? 616 HIS B O     1 
ATOM   8958 C  CB    . HIS B 2 616 ? 137.195 122.404 40.748  1.00 94.92  ? 616 HIS B CB    1 
ATOM   8959 C  CG    . HIS B 2 616 ? 136.524 122.221 39.422  1.00 103.00 ? 616 HIS B CG    1 
ATOM   8960 N  ND1   . HIS B 2 616 ? 136.249 123.272 38.575  1.00 102.74 ? 616 HIS B ND1   1 
ATOM   8961 C  CD2   . HIS B 2 616 ? 136.075 121.107 38.797  1.00 104.02 ? 616 HIS B CD2   1 
ATOM   8962 C  CE1   . HIS B 2 616 ? 135.656 122.815 37.487  1.00 98.33  ? 616 HIS B CE1   1 
ATOM   8963 N  NE2   . HIS B 2 616 ? 135.539 121.504 37.596  1.00 100.98 ? 616 HIS B NE2   1 
ATOM   8964 N  N     . GLY B 2 617 ? 137.555 122.095 43.585  1.00 96.63  ? 617 GLY B N     1 
ATOM   8965 C  CA    . GLY B 2 617 ? 137.837 121.880 44.988  1.00 91.79  ? 617 GLY B CA    1 
ATOM   8966 C  C     . GLY B 2 617 ? 136.720 121.139 45.705  1.00 91.26  ? 617 GLY B C     1 
ATOM   8967 O  O     . GLY B 2 617 ? 135.915 120.417 45.107  1.00 90.28  ? 617 GLY B O     1 
ATOM   8968 N  N     . ARG B 2 618 ? 136.680 121.336 47.025  1.00 91.52  ? 618 ARG B N     1 
ATOM   8969 C  CA    . ARG B 2 618 ? 135.752 120.580 47.861  1.00 88.15  ? 618 ARG B CA    1 
ATOM   8970 C  C     . ARG B 2 618 ? 134.306 121.004 47.633  1.00 85.15  ? 618 ARG B C     1 
ATOM   8971 O  O     . ARG B 2 618 ? 133.415 120.152 47.558  1.00 84.97  ? 618 ARG B O     1 
ATOM   8972 C  CB    . ARG B 2 618 ? 136.130 120.732 49.333  1.00 82.11  ? 618 ARG B CB    1 
ATOM   8973 C  CG    . ARG B 2 618 ? 135.204 119.997 50.283  1.00 80.32  ? 618 ARG B CG    1 
ATOM   8974 C  CD    . ARG B 2 618 ? 135.541 118.519 50.353  1.00 82.08  ? 618 ARG B CD    1 
ATOM   8975 N  NE    . ARG B 2 618 ? 136.488 118.214 51.418  1.00 86.70  ? 618 ARG B NE    1 
ATOM   8976 C  CZ    . ARG B 2 618 ? 137.789 118.037 51.235  1.00 87.39  ? 618 ARG B CZ    1 
ATOM   8977 N  NH1   . ARG B 2 618 ? 138.338 118.135 50.036  1.00 86.52  ? 618 ARG B NH1   1 
ATOM   8978 N  NH2   . ARG B 2 618 ? 138.559 117.752 52.281  1.00 83.13  ? 618 ARG B NH2   1 
ATOM   8979 N  N     . TYR B 2 619 ? 134.052 122.310 47.520  1.00 82.86  ? 619 TYR B N     1 
ATOM   8980 C  CA    . TYR B 2 619 ? 132.679 122.788 47.375  1.00 83.18  ? 619 TYR B CA    1 
ATOM   8981 C  C     . TYR B 2 619 ? 132.038 122.260 46.098  1.00 90.02  ? 619 TYR B C     1 
ATOM   8982 O  O     . TYR B 2 619 ? 130.854 121.897 46.089  1.00 90.01  ? 619 TYR B O     1 
ATOM   8983 C  CB    . TYR B 2 619 ? 132.652 124.315 47.395  1.00 82.48  ? 619 TYR B CB    1 
ATOM   8984 C  CG    . TYR B 2 619 ? 131.266 124.908 47.362  1.00 82.16  ? 619 TYR B CG    1 
ATOM   8985 C  CD1   . TYR B 2 619 ? 130.481 124.952 48.505  1.00 84.94  ? 619 TYR B CD1   1 
ATOM   8986 C  CD2   . TYR B 2 619 ? 130.742 125.427 46.187  1.00 83.87  ? 619 TYR B CD2   1 
ATOM   8987 C  CE1   . TYR B 2 619 ? 129.213 125.495 48.478  1.00 86.05  ? 619 TYR B CE1   1 
ATOM   8988 C  CE2   . TYR B 2 619 ? 129.478 125.972 46.150  1.00 86.96  ? 619 TYR B CE2   1 
ATOM   8989 C  CZ    . TYR B 2 619 ? 128.717 126.004 47.297  1.00 88.37  ? 619 TYR B CZ    1 
ATOM   8990 O  OH    . TYR B 2 619 ? 127.454 126.547 47.264  1.00 85.34  ? 619 TYR B OH    1 
ATOM   8991 N  N     . TRP B 2 620 ? 132.805 122.218 45.007  1.00 91.99  ? 620 TRP B N     1 
ATOM   8992 C  CA    . TRP B 2 620 ? 132.301 121.659 43.758  1.00 88.88  ? 620 TRP B CA    1 
ATOM   8993 C  C     . TRP B 2 620 ? 131.920 120.195 43.931  1.00 88.11  ? 620 TRP B C     1 
ATOM   8994 O  O     . TRP B 2 620 ? 130.877 119.754 43.434  1.00 90.18  ? 620 TRP B O     1 
ATOM   8995 C  CB    . TRP B 2 620 ? 133.359 121.817 42.668  1.00 94.58  ? 620 TRP B CB    1 
ATOM   8996 C  CG    . TRP B 2 620 ? 133.012 121.207 41.351  1.00 98.33  ? 620 TRP B CG    1 
ATOM   8997 C  CD1   . TRP B 2 620 ? 132.113 121.677 40.444  1.00 95.27  ? 620 TRP B CD1   1 
ATOM   8998 C  CD2   . TRP B 2 620 ? 133.567 120.015 40.785  1.00 99.87  ? 620 TRP B CD2   1 
ATOM   8999 N  NE1   . TRP B 2 620 ? 132.066 120.850 39.350  1.00 94.45  ? 620 TRP B NE1   1 
ATOM   9000 C  CE2   . TRP B 2 620 ? 132.952 119.822 39.534  1.00 97.61  ? 620 TRP B CE2   1 
ATOM   9001 C  CE3   . TRP B 2 620 ? 134.523 119.091 41.217  1.00 98.59  ? 620 TRP B CE3   1 
ATOM   9002 C  CZ2   . TRP B 2 620 ? 133.261 118.743 38.709  1.00 99.38  ? 620 TRP B CZ2   1 
ATOM   9003 C  CZ3   . TRP B 2 620 ? 134.828 118.021 40.397  1.00 100.24 ? 620 TRP B CZ3   1 
ATOM   9004 C  CH2   . TRP B 2 620 ? 134.200 117.856 39.158  1.00 100.64 ? 620 TRP B CH2   1 
ATOM   9005 N  N     . GLU B 2 621 ? 132.753 119.429 44.638  1.00 88.07  ? 621 GLU B N     1 
ATOM   9006 C  CA    . GLU B 2 621 ? 132.441 118.027 44.895  1.00 88.77  ? 621 GLU B CA    1 
ATOM   9007 C  C     . GLU B 2 621 ? 131.180 117.886 45.738  1.00 90.78  ? 621 GLU B C     1 
ATOM   9008 O  O     . GLU B 2 621 ? 130.345 117.014 45.474  1.00 92.86  ? 621 GLU B O     1 
ATOM   9009 C  CB    . GLU B 2 621 ? 133.623 117.346 45.583  1.00 90.65  ? 621 GLU B CB    1 
ATOM   9010 C  CG    . GLU B 2 621 ? 134.860 117.223 44.711  1.00 94.18  ? 621 GLU B CG    1 
ATOM   9011 C  CD    . GLU B 2 621 ? 136.066 116.714 45.476  1.00 96.85  ? 621 GLU B CD    1 
ATOM   9012 O  OE1   . GLU B 2 621 ? 135.944 116.478 46.696  1.00 92.68  ? 621 GLU B OE1   1 
ATOM   9013 O  OE2   . GLU B 2 621 ? 137.137 116.548 44.855  1.00 93.48  ? 621 GLU B OE2   1 
ATOM   9014 N  N     . MET B 2 622 ? 131.026 118.732 46.761  1.00 87.09  ? 622 MET B N     1 
ATOM   9015 C  CA    . MET B 2 622 ? 129.829 118.673 47.595  1.00 82.16  ? 622 MET B CA    1 
ATOM   9016 C  C     . MET B 2 622 ? 128.577 118.983 46.788  1.00 87.77  ? 622 MET B C     1 
ATOM   9017 O  O     . MET B 2 622 ? 127.544 118.324 46.953  1.00 90.00  ? 622 MET B O     1 
ATOM   9018 C  CB    . MET B 2 622 ? 129.954 119.635 48.777  1.00 76.41  ? 622 MET B CB    1 
ATOM   9019 C  CG    . MET B 2 622 ? 131.228 119.478 49.579  1.00 76.46  ? 622 MET B CG    1 
ATOM   9020 S  SD    . MET B 2 622 ? 131.467 120.779 50.803  1.00 79.22  ? 622 MET B SD    1 
ATOM   9021 C  CE    . MET B 2 622 ? 129.959 120.634 51.754  1.00 56.76  ? 622 MET B CE    1 
ATOM   9022 N  N     . THR B 2 623 ? 128.645 119.987 45.915  1.00 89.10  ? 623 THR B N     1 
ATOM   9023 C  CA    . THR B 2 623 ? 127.475 120.340 45.118  1.00 89.83  ? 623 THR B CA    1 
ATOM   9024 C  C     . THR B 2 623 ? 127.169 119.263 44.082  1.00 94.38  ? 623 THR B C     1 
ATOM   9025 O  O     . THR B 2 623 ? 126.000 119.000 43.777  1.00 99.13  ? 623 THR B O     1 
ATOM   9026 C  CB    . THR B 2 623 ? 127.688 121.696 44.450  1.00 89.78  ? 623 THR B CB    1 
ATOM   9027 O  OG1   . THR B 2 623 ? 127.971 122.676 45.455  1.00 89.13  ? 623 THR B OG1   1 
ATOM   9028 C  CG2   . THR B 2 623 ? 126.436 122.117 43.709  1.00 93.80  ? 623 THR B CG2   1 
ATOM   9029 N  N     . ARG B 2 624 ? 128.205 118.622 43.540  1.00 94.15  ? 624 ARG B N     1 
ATOM   9030 C  CA    . ARG B 2 624 ? 128.035 117.530 42.587  1.00 97.21  ? 624 ARG B CA    1 
ATOM   9031 C  C     . ARG B 2 624 ? 127.485 116.252 43.209  1.00 102.22 ? 624 ARG B C     1 
ATOM   9032 O  O     . ARG B 2 624 ? 127.137 115.333 42.462  1.00 106.18 ? 624 ARG B O     1 
ATOM   9033 C  CB    . ARG B 2 624 ? 129.367 117.240 41.894  1.00 94.50  ? 624 ARG B CB    1 
ATOM   9034 C  CG    . ARG B 2 624 ? 129.759 118.234 40.807  1.00 96.07  ? 624 ARG B CG    1 
ATOM   9035 C  CD    . ARG B 2 624 ? 128.613 118.419 39.801  1.00 101.07 ? 624 ARG B CD    1 
ATOM   9036 N  NE    . ARG B 2 624 ? 127.649 119.493 40.042  1.00 104.73 ? 624 ARG B NE    1 
ATOM   9037 C  CZ    . ARG B 2 624 ? 127.931 120.742 40.397  1.00 102.30 ? 624 ARG B CZ    1 
ATOM   9038 N  NH1   . ARG B 2 624 ? 129.174 121.165 40.540  1.00 96.34  ? 624 ARG B NH1   1 
ATOM   9039 N  NH2   . ARG B 2 624 ? 126.935 121.601 40.580  1.00 100.66 ? 624 ARG B NH2   1 
ATOM   9040 N  N     . VAL B 2 625 ? 127.404 116.161 44.538  1.00 98.54  ? 625 VAL B N     1 
ATOM   9041 C  CA    . VAL B 2 625 ? 126.809 114.977 45.157  1.00 99.24  ? 625 VAL B CA    1 
ATOM   9042 C  C     . VAL B 2 625 ? 125.335 114.867 44.781  1.00 106.72 ? 625 VAL B C     1 
ATOM   9043 O  O     . VAL B 2 625 ? 124.815 113.766 44.559  1.00 104.38 ? 625 VAL B O     1 
ATOM   9044 C  CB    . VAL B 2 625 ? 127.014 115.005 46.683  1.00 93.87  ? 625 VAL B CB    1 
ATOM   9045 C  CG1   . VAL B 2 625 ? 126.264 113.863 47.352  1.00 91.64  ? 625 VAL B CG1   1 
ATOM   9046 C  CG2   . VAL B 2 625 ? 128.491 114.916 47.014  1.00 84.10  ? 625 VAL B CG2   1 
ATOM   9047 N  N     . HIS B 2 626 ? 124.643 116.006 44.691  1.00 109.86 ? 626 HIS B N     1 
ATOM   9048 C  CA    . HIS B 2 626 ? 123.246 115.992 44.265  1.00 113.01 ? 626 HIS B CA    1 
ATOM   9049 C  C     . HIS B 2 626 ? 123.109 115.468 42.841  1.00 113.31 ? 626 HIS B C     1 
ATOM   9050 O  O     . HIS B 2 626 ? 122.188 114.698 42.539  1.00 112.16 ? 626 HIS B O     1 
ATOM   9051 C  CB    . HIS B 2 626 ? 122.649 117.396 44.375  1.00 111.11 ? 626 HIS B CB    1 
ATOM   9052 C  CG    . HIS B 2 626 ? 122.563 117.909 45.779  1.00 113.61 ? 626 HIS B CG    1 
ATOM   9053 N  ND1   . HIS B 2 626 ? 123.675 118.111 46.567  1.00 107.35 ? 626 HIS B ND1   1 
ATOM   9054 C  CD2   . HIS B 2 626 ? 121.497 118.265 46.534  1.00 113.32 ? 626 HIS B CD2   1 
ATOM   9055 C  CE1   . HIS B 2 626 ? 123.298 118.567 47.748  1.00 108.40 ? 626 HIS B CE1   1 
ATOM   9056 N  NE2   . HIS B 2 626 ? 121.982 118.670 47.754  1.00 112.44 ? 626 HIS B NE2   1 
ATOM   9057 N  N     . LEU B 2 627 ? 124.014 115.873 41.950  1.00 111.38 ? 627 LEU B N     1 
ATOM   9058 C  CA    . LEU B 2 627 ? 123.973 115.434 40.562  1.00 115.59 ? 627 LEU B CA    1 
ATOM   9059 C  C     . LEU B 2 627 ? 124.482 114.012 40.372  1.00 116.29 ? 627 LEU B C     1 
ATOM   9060 O  O     . LEU B 2 627 ? 124.246 113.425 39.310  1.00 113.08 ? 627 LEU B O     1 
ATOM   9061 C  CB    . LEU B 2 627 ? 124.787 116.389 39.683  1.00 117.45 ? 627 LEU B CB    1 
ATOM   9062 C  CG    . LEU B 2 627 ? 124.046 117.584 39.080  1.00 119.21 ? 627 LEU B CG    1 
ATOM   9063 C  CD1   . LEU B 2 627 ? 123.616 118.567 40.159  1.00 116.20 ? 627 LEU B CD1   1 
ATOM   9064 C  CD2   . LEU B 2 627 ? 124.910 118.275 38.035  1.00 116.01 ? 627 LEU B CD2   1 
ATOM   9065 N  N     . GLY B 2 628 ? 125.167 113.448 41.362  1.00 115.40 ? 628 GLY B N     1 
ATOM   9066 C  CA    . GLY B 2 628 ? 125.675 112.099 41.250  1.00 116.26 ? 628 GLY B CA    1 
ATOM   9067 C  C     . GLY B 2 628 ? 126.922 112.014 40.391  1.00 122.59 ? 628 GLY B C     1 
ATOM   9068 O  O     . GLY B 2 628 ? 127.501 113.016 39.958  1.00 120.13 ? 628 GLY B O     1 
ATOM   9069 N  N     . GLY B 2 629 ? 127.337 110.777 40.142  1.00 125.65 ? 629 GLY B N     1 
ATOM   9070 C  CA    . GLY B 2 629 ? 128.513 110.513 39.334  1.00 119.11 ? 629 GLY B CA    1 
ATOM   9071 C  C     . GLY B 2 629 ? 128.980 109.073 39.416  1.00 110.33 ? 629 GLY B C     1 
ATOM   9072 O  O     . GLY B 2 629 ? 128.201 108.175 39.734  1.00 111.23 ? 629 GLY B O     1 
HETATM 9073 P  PG    . ATP C 3 .   ? 108.690 117.186 62.105  1.00 51.54  ? 601 ATP A PG    1 
HETATM 9074 O  O1G   . ATP C 3 .   ? 108.237 118.513 62.597  1.00 57.54  ? 601 ATP A O1G   1 
HETATM 9075 O  O2G   . ATP C 3 .   ? 108.618 117.038 60.593  1.00 52.75  ? 601 ATP A O2G   1 
HETATM 9076 O  O3G   . ATP C 3 .   ? 110.085 116.802 62.577  1.00 54.64  ? 601 ATP A O3G   1 
HETATM 9077 P  PB    . ATP C 3 .   ? 106.488 115.174 62.224  1.00 49.57  ? 601 ATP A PB    1 
HETATM 9078 O  O1B   . ATP C 3 .   ? 105.927 115.645 60.949  1.00 56.11  ? 601 ATP A O1B   1 
HETATM 9079 O  O2B   . ATP C 3 .   ? 106.901 113.709 62.269  1.00 53.93  ? 601 ATP A O2B   1 
HETATM 9080 O  O3B   . ATP C 3 .   ? 107.744 116.033 62.666  1.00 56.04  ? 601 ATP A O3B   1 
HETATM 9081 P  PA    . ATP C 3 .   ? 105.129 114.728 64.810  1.00 51.47  ? 601 ATP A PA    1 
HETATM 9082 O  O1A   . ATP C 3 .   ? 106.221 114.853 65.794  1.00 53.09  ? 601 ATP A O1A   1 
HETATM 9083 O  O2A   . ATP C 3 .   ? 104.703 113.299 64.499  1.00 58.46  ? 601 ATP A O2A   1 
HETATM 9084 O  O3A   . ATP C 3 .   ? 105.480 115.424 63.430  1.00 48.26  ? 601 ATP A O3A   1 
HETATM 9085 O  "O5'" . ATP C 3 .   ? 103.848 115.518 65.279  1.00 63.63  ? 601 ATP A "O5'" 1 
HETATM 9086 C  "C5'" . ATP C 3 .   ? 102.667 115.589 64.454  1.00 61.40  ? 601 ATP A "C5'" 1 
HETATM 9087 C  "C4'" . ATP C 3 .   ? 101.647 116.436 65.169  1.00 62.04  ? 601 ATP A "C4'" 1 
HETATM 9088 O  "O4'" . ATP C 3 .   ? 101.426 115.904 66.487  1.00 57.58  ? 601 ATP A "O4'" 1 
HETATM 9089 C  "C3'" . ATP C 3 .   ? 102.047 117.900 65.365  1.00 65.09  ? 601 ATP A "C3'" 1 
HETATM 9090 O  "O3'" . ATP C 3 .   ? 101.313 118.743 64.484  1.00 69.26  ? 601 ATP A "O3'" 1 
HETATM 9091 C  "C2'" . ATP C 3 .   ? 101.717 118.195 66.839  1.00 66.03  ? 601 ATP A "C2'" 1 
HETATM 9092 O  "O2'" . ATP C 3 .   ? 100.906 119.356 66.968  1.00 71.44  ? 601 ATP A "O2'" 1 
HETATM 9093 C  "C1'" . ATP C 3 .   ? 100.930 116.959 67.270  1.00 63.65  ? 601 ATP A "C1'" 1 
HETATM 9094 N  N9    . ATP C 3 .   ? 101.086 116.604 68.676  1.00 65.72  ? 601 ATP A N9    1 
HETATM 9095 C  C8    . ATP C 3 .   ? 100.170 116.787 69.680  1.00 65.07  ? 601 ATP A C8    1 
HETATM 9096 N  N7    . ATP C 3 .   ? 100.571 116.366 70.854  1.00 61.33  ? 601 ATP A N7    1 
HETATM 9097 C  C5    . ATP C 3 .   ? 101.842 115.870 70.607  1.00 62.00  ? 601 ATP A C5    1 
HETATM 9098 C  C6    . ATP C 3 .   ? 102.808 115.276 71.440  1.00 60.92  ? 601 ATP A C6    1 
HETATM 9099 N  N6    . ATP C 3 .   ? 102.638 115.076 72.750  1.00 58.94  ? 601 ATP A N6    1 
HETATM 9100 N  N1    . ATP C 3 .   ? 103.974 114.893 70.876  1.00 65.72  ? 601 ATP A N1    1 
HETATM 9101 C  C2    . ATP C 3 .   ? 104.151 115.092 69.567  1.00 63.38  ? 601 ATP A C2    1 
HETATM 9102 N  N3    . ATP C 3 .   ? 103.314 115.640 68.684  1.00 53.64  ? 601 ATP A N3    1 
HETATM 9103 C  C4    . ATP C 3 .   ? 102.171 116.009 69.268  1.00 57.71  ? 601 ATP A C4    1 
HETATM 9104 MG MG    . MG  D 4 .   ? 109.472 114.306 63.635  1.00 40.65  ? 602 MG  A MG    1 
HETATM 9105 P  PB    . ADP E 5 .   ? 131.202 120.657 63.604  1.00 42.76  ? 701 ADP B PB    1 
HETATM 9106 O  O1B   . ADP E 5 .   ? 130.315 119.495 63.863  1.00 45.09  ? 701 ADP B O1B   1 
HETATM 9107 O  O2B   . ADP E 5 .   ? 131.841 120.608 62.241  1.00 47.87  ? 701 ADP B O2B   1 
HETATM 9108 O  O3B   . ADP E 5 .   ? 130.515 121.962 63.871  1.00 44.54  ? 701 ADP B O3B   1 
HETATM 9109 P  PA    . ADP E 5 .   ? 132.417 120.958 66.245  1.00 39.14  ? 701 ADP B PA    1 
HETATM 9110 O  O1A   . ADP E 5 .   ? 132.021 122.390 66.329  1.00 42.04  ? 701 ADP B O1A   1 
HETATM 9111 O  O2A   . ADP E 5 .   ? 131.649 119.977 67.065  1.00 38.84  ? 701 ADP B O2A   1 
HETATM 9112 O  O3A   . ADP E 5 .   ? 132.371 120.511 64.706  1.00 46.35  ? 701 ADP B O3A   1 
HETATM 9113 O  "O5'" . ADP E 5 .   ? 133.979 120.831 66.581  1.00 45.27  ? 701 ADP B "O5'" 1 
HETATM 9114 C  "C5'" . ADP E 5 .   ? 134.695 119.650 66.148  1.00 40.00  ? 701 ADP B "C5'" 1 
HETATM 9115 C  "C4'" . ADP E 5 .   ? 134.889 118.716 67.318  1.00 36.85  ? 701 ADP B "C4'" 1 
HETATM 9116 O  "O4'" . ADP E 5 .   ? 134.601 119.418 68.552  1.00 40.17  ? 701 ADP B "O4'" 1 
HETATM 9117 C  "C3'" . ADP E 5 .   ? 133.995 117.466 67.331  1.00 41.93  ? 701 ADP B "C3'" 1 
HETATM 9118 O  "O3'" . ADP E 5 .   ? 134.768 116.294 67.104  1.00 45.05  ? 701 ADP B "O3'" 1 
HETATM 9119 C  "C2'" . ADP E 5 .   ? 133.345 117.452 68.722  1.00 40.19  ? 701 ADP B "C2'" 1 
HETATM 9120 O  "O2'" . ADP E 5 .   ? 133.423 116.187 69.343  1.00 51.77  ? 701 ADP B "O2'" 1 
HETATM 9121 C  "C1'" . ADP E 5 .   ? 134.148 118.487 69.502  1.00 37.43  ? 701 ADP B "C1'" 1 
HETATM 9122 N  N9    . ADP E 5 .   ? 133.363 119.198 70.502  1.00 34.60  ? 701 ADP B N9    1 
HETATM 9123 C  C8    . ADP E 5 .   ? 132.330 120.068 70.265  1.00 37.67  ? 701 ADP B C8    1 
HETATM 9124 N  N7    . ADP E 5 .   ? 131.804 120.560 71.358  1.00 38.57  ? 701 ADP B N7    1 
HETATM 9125 C  C5    . ADP E 5 .   ? 132.534 119.975 72.383  1.00 37.14  ? 701 ADP B C5    1 
HETATM 9126 C  C6    . ADP E 5 .   ? 132.459 120.094 73.784  1.00 38.28  ? 701 ADP B C6    1 
HETATM 9127 N  N6    . ADP E 5 .   ? 131.582 120.868 74.414  1.00 38.26  ? 701 ADP B N6    1 
HETATM 9128 N  N1    . ADP E 5 .   ? 133.339 119.373 74.518  1.00 37.62  ? 701 ADP B N1    1 
HETATM 9129 C  C2    . ADP E 5 .   ? 134.220 118.596 73.876  1.00 39.68  ? 701 ADP B C2    1 
HETATM 9130 N  N3    . ADP E 5 .   ? 134.382 118.407 72.571  1.00 39.05  ? 701 ADP B N3    1 
HETATM 9131 C  C4    . ADP E 5 .   ? 133.498 119.132 71.868  1.00 37.60  ? 701 ADP B C4    1 
HETATM 9132 V  V     . VO4 F 6 .   ? 127.538 118.983 62.692  1.00 47.44  ? 702 VO4 B V     1 
HETATM 9133 O  O1    . VO4 F 6 .   ? 128.585 119.372 61.145  1.00 44.46  ? 702 VO4 B O1    1 
HETATM 9134 O  O2    . VO4 F 6 .   ? 125.702 118.856 62.190  1.00 53.85  ? 702 VO4 B O2    1 
HETATM 9135 O  O3    . VO4 F 6 .   ? 128.081 117.324 63.449  1.00 40.68  ? 702 VO4 B O3    1 
HETATM 9136 O  O4    . VO4 F 6 .   ? 127.752 120.374 63.982  1.00 51.54  ? 702 VO4 B O4    1 
HETATM 9137 MG MG    . MG  G 4 .   ? 127.431 121.239 65.702  1.00 38.52  ? 703 MG  B MG    1 
# 
