data_9CLO
# 
_entry.id   9CLO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9CLO         pdb_00009clo 10.2210/pdb9clo/pdb 
WWPDB D_1000285861 ?            ?                   
EMDB  EMD-45727    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-20 
2 'Structure model' 1 1 2024-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 2 'Structure model' em_admin 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CLO 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                         EMD-45670 'consensus EM volume'  
EMDB 'C-terminal Map'          EMD-45667 'focused EM volume'    
EMDB 'N-Terminal Map'          EMD-45669 'focused EM volume'    
EMDB 'DosP R97A with c-di-GMP' EMD-45727 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              daniel.kober@utsouthwestern.edu 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Kober 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8657-9348 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kumar, P.'   1 0000-0002-7025-5530 
'Kober, D.L.' 2 0000-0001-8657-9348 
# 
_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            15 
_citation.language                  ? 
_citation.page_first                9653 
_citation.page_last                 9653 
_citation.title                     
'Structures of the multi-domain oxygen sensor DosP: remote control of a c-di-GMP phosphodiesterase by a regulatory PAS domain.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-53942-7 
_citation.pdbx_database_id_PubMed   39511182 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, W.'                1 ? 
primary 'Kumar, P.'             2 ? 
primary 'Brautigam, C.A.'       3 ? 
primary 'Tso, S.C.'             4 ? 
primary 'Baniasadi, H.R.'       5 ? 
primary 'Kober, D.L.'           6 ? 
primary 'Gilles-Gonzalez, M.A.' 7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Oxygen sensor protein DosP' 89003.695 2 3.1.4.52 R97A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2 ?        ?    ? ? 
3 non-polymer syn 
;9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)
;
690.411   2 ?        ?    ? ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    4 ?        ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Direct oxygen-sensing phosphodiesterase,Direct oxygen sensor protein,Ec DOS,Heme-regulated cyclic di-GMP phosphodiesterase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSAEL
QLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGY
CISEASGMQPDTLLNTPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEE
RQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPA
GILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGV
DHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPL
TLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGE
LYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVS
DAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEK
RILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSAEL
QLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGY
CISEASGMQPDTLLNTPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEE
RQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPA
GILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGV
DHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPL
TLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGE
LYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVS
DAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEK
RILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 
;9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)
;
C2E 
4 'MAGNESIUM ION' MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ILE n 
1 3   PHE n 
1 4   PHE n 
1 5   PRO n 
1 6   ALA n 
1 7   LEU n 
1 8   GLU n 
1 9   GLN n 
1 10  ASN n 
1 11  MET n 
1 12  MET n 
1 13  GLY n 
1 14  ALA n 
1 15  VAL n 
1 16  LEU n 
1 17  ILE n 
1 18  ASN n 
1 19  GLU n 
1 20  ASN n 
1 21  ASP n 
1 22  GLU n 
1 23  VAL n 
1 24  MET n 
1 25  PHE n 
1 26  PHE n 
1 27  ASN n 
1 28  PRO n 
1 29  ALA n 
1 30  ALA n 
1 31  GLU n 
1 32  LYS n 
1 33  LEU n 
1 34  TRP n 
1 35  GLY n 
1 36  TYR n 
1 37  LYS n 
1 38  ARG n 
1 39  GLU n 
1 40  GLU n 
1 41  VAL n 
1 42  ILE n 
1 43  GLY n 
1 44  ASN n 
1 45  ASN n 
1 46  ILE n 
1 47  ASP n 
1 48  MET n 
1 49  LEU n 
1 50  ILE n 
1 51  PRO n 
1 52  ARG n 
1 53  ASP n 
1 54  LEU n 
1 55  ARG n 
1 56  PRO n 
1 57  ALA n 
1 58  HIS n 
1 59  PRO n 
1 60  GLU n 
1 61  TYR n 
1 62  ILE n 
1 63  ARG n 
1 64  HIS n 
1 65  ASN n 
1 66  ARG n 
1 67  GLU n 
1 68  GLY n 
1 69  GLY n 
1 70  LYS n 
1 71  ALA n 
1 72  ARG n 
1 73  VAL n 
1 74  GLU n 
1 75  GLY n 
1 76  MET n 
1 77  SER n 
1 78  ALA n 
1 79  GLU n 
1 80  LEU n 
1 81  GLN n 
1 82  LEU n 
1 83  GLU n 
1 84  LYS n 
1 85  LYS n 
1 86  ASP n 
1 87  GLY n 
1 88  SER n 
1 89  LYS n 
1 90  ILE n 
1 91  TRP n 
1 92  THR n 
1 93  ARG n 
1 94  PHE n 
1 95  ALA n 
1 96  LEU n 
1 97  SER n 
1 98  LYS n 
1 99  VAL n 
1 100 SER n 
1 101 ALA n 
1 102 GLU n 
1 103 GLY n 
1 104 LYS n 
1 105 VAL n 
1 106 TYR n 
1 107 TYR n 
1 108 LEU n 
1 109 ALA n 
1 110 LEU n 
1 111 VAL n 
1 112 ARG n 
1 113 ASP n 
1 114 ALA n 
1 115 SER n 
1 116 VAL n 
1 117 GLU n 
1 118 MET n 
1 119 ALA n 
1 120 GLN n 
1 121 LYS n 
1 122 GLU n 
1 123 GLN n 
1 124 THR n 
1 125 ARG n 
1 126 GLN n 
1 127 LEU n 
1 128 ILE n 
1 129 ILE n 
1 130 ALA n 
1 131 VAL n 
1 132 ASP n 
1 133 HIS n 
1 134 LEU n 
1 135 ASP n 
1 136 ARG n 
1 137 PRO n 
1 138 VAL n 
1 139 ILE n 
1 140 VAL n 
1 141 LEU n 
1 142 ASP n 
1 143 PRO n 
1 144 GLU n 
1 145 ARG n 
1 146 HIS n 
1 147 ILE n 
1 148 VAL n 
1 149 GLN n 
1 150 CYS n 
1 151 ASN n 
1 152 ARG n 
1 153 ALA n 
1 154 PHE n 
1 155 THR n 
1 156 GLU n 
1 157 MET n 
1 158 PHE n 
1 159 GLY n 
1 160 TYR n 
1 161 CYS n 
1 162 ILE n 
1 163 SER n 
1 164 GLU n 
1 165 ALA n 
1 166 SER n 
1 167 GLY n 
1 168 MET n 
1 169 GLN n 
1 170 PRO n 
1 171 ASP n 
1 172 THR n 
1 173 LEU n 
1 174 LEU n 
1 175 ASN n 
1 176 THR n 
1 177 PRO n 
1 178 GLU n 
1 179 PHE n 
1 180 PRO n 
1 181 ALA n 
1 182 ASP n 
1 183 ASN n 
1 184 ARG n 
1 185 ILE n 
1 186 ARG n 
1 187 LEU n 
1 188 GLN n 
1 189 GLN n 
1 190 LEU n 
1 191 LEU n 
1 192 TRP n 
1 193 LYS n 
1 194 THR n 
1 195 ALA n 
1 196 ARG n 
1 197 ASP n 
1 198 GLN n 
1 199 ASP n 
1 200 GLU n 
1 201 PHE n 
1 202 LEU n 
1 203 LEU n 
1 204 LEU n 
1 205 THR n 
1 206 ARG n 
1 207 THR n 
1 208 GLY n 
1 209 GLU n 
1 210 LYS n 
1 211 ILE n 
1 212 TRP n 
1 213 ILE n 
1 214 LYS n 
1 215 ALA n 
1 216 SER n 
1 217 ILE n 
1 218 SER n 
1 219 PRO n 
1 220 VAL n 
1 221 TYR n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 ALA n 
1 226 HIS n 
1 227 LEU n 
1 228 GLN n 
1 229 ASN n 
1 230 LEU n 
1 231 VAL n 
1 232 MET n 
1 233 THR n 
1 234 PHE n 
1 235 SER n 
1 236 ASP n 
1 237 ILE n 
1 238 THR n 
1 239 GLU n 
1 240 GLU n 
1 241 ARG n 
1 242 GLN n 
1 243 ILE n 
1 244 ARG n 
1 245 GLN n 
1 246 LEU n 
1 247 GLU n 
1 248 GLY n 
1 249 ASN n 
1 250 ILE n 
1 251 LEU n 
1 252 ALA n 
1 253 ALA n 
1 254 MET n 
1 255 CYS n 
1 256 SER n 
1 257 SER n 
1 258 PRO n 
1 259 PRO n 
1 260 PHE n 
1 261 HIS n 
1 262 GLU n 
1 263 MET n 
1 264 GLY n 
1 265 GLU n 
1 266 ILE n 
1 267 ILE n 
1 268 CYS n 
1 269 ARG n 
1 270 ASN n 
1 271 ILE n 
1 272 GLU n 
1 273 SER n 
1 274 VAL n 
1 275 LEU n 
1 276 ASN n 
1 277 GLU n 
1 278 SER n 
1 279 HIS n 
1 280 VAL n 
1 281 SER n 
1 282 LEU n 
1 283 PHE n 
1 284 ALA n 
1 285 LEU n 
1 286 ARG n 
1 287 ASN n 
1 288 GLY n 
1 289 MET n 
1 290 PRO n 
1 291 ILE n 
1 292 HIS n 
1 293 TRP n 
1 294 ALA n 
1 295 SER n 
1 296 SER n 
1 297 SER n 
1 298 HIS n 
1 299 GLY n 
1 300 ALA n 
1 301 GLU n 
1 302 ILE n 
1 303 GLN n 
1 304 ASN n 
1 305 ALA n 
1 306 GLN n 
1 307 SER n 
1 308 TRP n 
1 309 SER n 
1 310 ALA n 
1 311 THR n 
1 312 ILE n 
1 313 ARG n 
1 314 GLN n 
1 315 ARG n 
1 316 ASP n 
1 317 GLY n 
1 318 ALA n 
1 319 PRO n 
1 320 ALA n 
1 321 GLY n 
1 322 ILE n 
1 323 LEU n 
1 324 GLN n 
1 325 ILE n 
1 326 LYS n 
1 327 THR n 
1 328 SER n 
1 329 SER n 
1 330 GLY n 
1 331 ALA n 
1 332 GLU n 
1 333 THR n 
1 334 SER n 
1 335 ALA n 
1 336 PHE n 
1 337 ILE n 
1 338 GLU n 
1 339 ARG n 
1 340 VAL n 
1 341 ALA n 
1 342 ASP n 
1 343 ILE n 
1 344 SER n 
1 345 GLN n 
1 346 HIS n 
1 347 MET n 
1 348 ALA n 
1 349 ALA n 
1 350 LEU n 
1 351 ALA n 
1 352 LEU n 
1 353 GLU n 
1 354 GLN n 
1 355 GLU n 
1 356 LYS n 
1 357 SER n 
1 358 ARG n 
1 359 GLN n 
1 360 HIS n 
1 361 ILE n 
1 362 GLU n 
1 363 GLN n 
1 364 LEU n 
1 365 ILE n 
1 366 GLN n 
1 367 PHE n 
1 368 ASP n 
1 369 PRO n 
1 370 MET n 
1 371 THR n 
1 372 GLY n 
1 373 LEU n 
1 374 PRO n 
1 375 ASN n 
1 376 ARG n 
1 377 ASN n 
1 378 ASN n 
1 379 LEU n 
1 380 HIS n 
1 381 ASN n 
1 382 TYR n 
1 383 LEU n 
1 384 ASP n 
1 385 ASP n 
1 386 LEU n 
1 387 VAL n 
1 388 ASP n 
1 389 LYS n 
1 390 ALA n 
1 391 VAL n 
1 392 SER n 
1 393 PRO n 
1 394 VAL n 
1 395 VAL n 
1 396 TYR n 
1 397 LEU n 
1 398 ILE n 
1 399 GLY n 
1 400 VAL n 
1 401 ASP n 
1 402 HIS n 
1 403 ILE n 
1 404 GLN n 
1 405 ASP n 
1 406 VAL n 
1 407 ILE n 
1 408 ASP n 
1 409 SER n 
1 410 LEU n 
1 411 GLY n 
1 412 TYR n 
1 413 ALA n 
1 414 TRP n 
1 415 ALA n 
1 416 ASP n 
1 417 GLN n 
1 418 ALA n 
1 419 LEU n 
1 420 LEU n 
1 421 GLU n 
1 422 VAL n 
1 423 VAL n 
1 424 ASN n 
1 425 ARG n 
1 426 PHE n 
1 427 ARG n 
1 428 GLU n 
1 429 LYS n 
1 430 LEU n 
1 431 LYS n 
1 432 PRO n 
1 433 ASP n 
1 434 GLN n 
1 435 TYR n 
1 436 LEU n 
1 437 CYS n 
1 438 ARG n 
1 439 ILE n 
1 440 GLU n 
1 441 GLY n 
1 442 THR n 
1 443 GLN n 
1 444 PHE n 
1 445 VAL n 
1 446 LEU n 
1 447 VAL n 
1 448 SER n 
1 449 LEU n 
1 450 GLU n 
1 451 ASN n 
1 452 ASP n 
1 453 VAL n 
1 454 SER n 
1 455 ASN n 
1 456 ILE n 
1 457 THR n 
1 458 GLN n 
1 459 ILE n 
1 460 ALA n 
1 461 ASP n 
1 462 GLU n 
1 463 LEU n 
1 464 ARG n 
1 465 ASN n 
1 466 VAL n 
1 467 VAL n 
1 468 SER n 
1 469 LYS n 
1 470 PRO n 
1 471 ILE n 
1 472 MET n 
1 473 ILE n 
1 474 ASP n 
1 475 ASP n 
1 476 LYS n 
1 477 PRO n 
1 478 PHE n 
1 479 PRO n 
1 480 LEU n 
1 481 THR n 
1 482 LEU n 
1 483 SER n 
1 484 ILE n 
1 485 GLY n 
1 486 ILE n 
1 487 SER n 
1 488 TYR n 
1 489 ASP n 
1 490 LEU n 
1 491 GLY n 
1 492 LYS n 
1 493 ASN n 
1 494 ARG n 
1 495 ASP n 
1 496 TYR n 
1 497 LEU n 
1 498 LEU n 
1 499 SER n 
1 500 THR n 
1 501 ALA n 
1 502 HIS n 
1 503 ASN n 
1 504 ALA n 
1 505 MET n 
1 506 ASP n 
1 507 TYR n 
1 508 ILE n 
1 509 ARG n 
1 510 LYS n 
1 511 ASN n 
1 512 GLY n 
1 513 GLY n 
1 514 ASN n 
1 515 GLY n 
1 516 TRP n 
1 517 GLN n 
1 518 PHE n 
1 519 PHE n 
1 520 SER n 
1 521 PRO n 
1 522 ALA n 
1 523 MET n 
1 524 ASN n 
1 525 GLU n 
1 526 MET n 
1 527 VAL n 
1 528 LYS n 
1 529 GLU n 
1 530 ARG n 
1 531 LEU n 
1 532 VAL n 
1 533 LEU n 
1 534 GLY n 
1 535 ALA n 
1 536 ALA n 
1 537 LEU n 
1 538 LYS n 
1 539 GLU n 
1 540 ALA n 
1 541 ILE n 
1 542 SER n 
1 543 ASN n 
1 544 ASN n 
1 545 GLN n 
1 546 LEU n 
1 547 LYS n 
1 548 LEU n 
1 549 VAL n 
1 550 TYR n 
1 551 GLN n 
1 552 PRO n 
1 553 GLN n 
1 554 ILE n 
1 555 PHE n 
1 556 ALA n 
1 557 GLU n 
1 558 THR n 
1 559 GLY n 
1 560 GLU n 
1 561 LEU n 
1 562 TYR n 
1 563 GLY n 
1 564 ILE n 
1 565 GLU n 
1 566 ALA n 
1 567 LEU n 
1 568 ALA n 
1 569 ARG n 
1 570 TRP n 
1 571 HIS n 
1 572 ASP n 
1 573 PRO n 
1 574 LEU n 
1 575 HIS n 
1 576 GLY n 
1 577 HIS n 
1 578 VAL n 
1 579 PRO n 
1 580 PRO n 
1 581 SER n 
1 582 ARG n 
1 583 PHE n 
1 584 ILE n 
1 585 PRO n 
1 586 LEU n 
1 587 ALA n 
1 588 GLU n 
1 589 GLU n 
1 590 ILE n 
1 591 GLY n 
1 592 GLU n 
1 593 ILE n 
1 594 GLU n 
1 595 ASN n 
1 596 ILE n 
1 597 GLY n 
1 598 ARG n 
1 599 TRP n 
1 600 VAL n 
1 601 ILE n 
1 602 ALA n 
1 603 GLU n 
1 604 ALA n 
1 605 CYS n 
1 606 ARG n 
1 607 GLN n 
1 608 LEU n 
1 609 ALA n 
1 610 GLU n 
1 611 TRP n 
1 612 ARG n 
1 613 SER n 
1 614 GLN n 
1 615 ASN n 
1 616 ILE n 
1 617 HIS n 
1 618 ILE n 
1 619 PRO n 
1 620 ALA n 
1 621 LEU n 
1 622 SER n 
1 623 VAL n 
1 624 ASN n 
1 625 LEU n 
1 626 SER n 
1 627 ALA n 
1 628 LEU n 
1 629 HIS n 
1 630 PHE n 
1 631 ARG n 
1 632 SER n 
1 633 ASN n 
1 634 GLN n 
1 635 LEU n 
1 636 PRO n 
1 637 ASN n 
1 638 GLN n 
1 639 VAL n 
1 640 SER n 
1 641 ASP n 
1 642 ALA n 
1 643 MET n 
1 644 HIS n 
1 645 ALA n 
1 646 TRP n 
1 647 GLY n 
1 648 ILE n 
1 649 ASP n 
1 650 GLY n 
1 651 HIS n 
1 652 GLN n 
1 653 LEU n 
1 654 THR n 
1 655 VAL n 
1 656 GLU n 
1 657 ILE n 
1 658 THR n 
1 659 GLU n 
1 660 SER n 
1 661 MET n 
1 662 MET n 
1 663 MET n 
1 664 GLU n 
1 665 HIS n 
1 666 ASP n 
1 667 THR n 
1 668 GLU n 
1 669 ILE n 
1 670 PHE n 
1 671 LYS n 
1 672 ARG n 
1 673 ILE n 
1 674 GLN n 
1 675 ILE n 
1 676 LEU n 
1 677 ARG n 
1 678 ASP n 
1 679 MET n 
1 680 GLY n 
1 681 VAL n 
1 682 GLY n 
1 683 LEU n 
1 684 SER n 
1 685 VAL n 
1 686 ASP n 
1 687 ASP n 
1 688 PHE n 
1 689 GLY n 
1 690 THR n 
1 691 GLY n 
1 692 PHE n 
1 693 SER n 
1 694 GLY n 
1 695 LEU n 
1 696 SER n 
1 697 ARG n 
1 698 LEU n 
1 699 VAL n 
1 700 SER n 
1 701 LEU n 
1 702 PRO n 
1 703 VAL n 
1 704 THR n 
1 705 GLU n 
1 706 ILE n 
1 707 LYS n 
1 708 ILE n 
1 709 ASP n 
1 710 LYS n 
1 711 SER n 
1 712 PHE n 
1 713 VAL n 
1 714 ASP n 
1 715 ARG n 
1 716 CYS n 
1 717 LEU n 
1 718 THR n 
1 719 GLU n 
1 720 LYS n 
1 721 ARG n 
1 722 ILE n 
1 723 LEU n 
1 724 ALA n 
1 725 LEU n 
1 726 LEU n 
1 727 GLU n 
1 728 ALA n 
1 729 ILE n 
1 730 THR n 
1 731 SER n 
1 732 ILE n 
1 733 GLY n 
1 734 GLN n 
1 735 SER n 
1 736 LEU n 
1 737 ASN n 
1 738 LEU n 
1 739 THR n 
1 740 VAL n 
1 741 VAL n 
1 742 ALA n 
1 743 GLU n 
1 744 GLY n 
1 745 VAL n 
1 746 GLU n 
1 747 THR n 
1 748 LYS n 
1 749 GLU n 
1 750 GLN n 
1 751 PHE n 
1 752 GLU n 
1 753 MET n 
1 754 LEU n 
1 755 ARG n 
1 756 LYS n 
1 757 ILE n 
1 758 HIS n 
1 759 CYS n 
1 760 ARG n 
1 761 VAL n 
1 762 ILE n 
1 763 GLN n 
1 764 GLY n 
1 765 TYR n 
1 766 PHE n 
1 767 PHE n 
1 768 SER n 
1 769 ARG n 
1 770 PRO n 
1 771 LEU n 
1 772 PRO n 
1 773 ALA n 
1 774 GLU n 
1 775 GLU n 
1 776 ILE n 
1 777 PRO n 
1 778 GLY n 
1 779 TRP n 
1 780 MET n 
1 781 SER n 
1 782 SER n 
1 783 VAL n 
1 784 LEU n 
1 785 PRO n 
1 786 LEU n 
1 787 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   787 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'dosP, dos, pdeO, yddU, b1489, JW1484' 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                                            'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE ?                                            'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                                            'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                                            'C4 H7 N O4'         133.103 
C2E non-polymer         . 
;9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)
;
'c-di-GMP; Cyclic diguanosine monophosphate' 'C20 H24 N10 O14 P2' 690.411 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME                                         'C34 H32 Fe N4 O4'   
616.487 
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 
# 
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   GLY 1   20  20  GLY GLY A . n 
A 1 2   ILE 2   21  21  ILE ILE A . n 
A 1 3   PHE 3   22  22  PHE PHE A . n 
A 1 4   PHE 4   23  23  PHE PHE A . n 
A 1 5   PRO 5   24  24  PRO PRO A . n 
A 1 6   ALA 6   25  25  ALA ALA A . n 
A 1 7   LEU 7   26  26  LEU LEU A . n 
A 1 8   GLU 8   27  27  GLU GLU A . n 
A 1 9   GLN 9   28  28  GLN GLN A . n 
A 1 10  ASN 10  29  29  ASN ASN A . n 
A 1 11  MET 11  30  30  MET MET A . n 
A 1 12  MET 12  31  31  MET MET A . n 
A 1 13  GLY 13  32  32  GLY GLY A . n 
A 1 14  ALA 14  33  33  ALA ALA A . n 
A 1 15  VAL 15  34  34  VAL VAL A . n 
A 1 16  LEU 16  35  35  LEU LEU A . n 
A 1 17  ILE 17  36  36  ILE ILE A . n 
A 1 18  ASN 18  37  37  ASN ASN A . n 
A 1 19  GLU 19  38  38  GLU GLU A . n 
A 1 20  ASN 20  39  39  ASN ASN A . n 
A 1 21  ASP 21  40  40  ASP ASP A . n 
A 1 22  GLU 22  41  41  GLU GLU A . n 
A 1 23  VAL 23  42  42  VAL VAL A . n 
A 1 24  MET 24  43  43  MET MET A . n 
A 1 25  PHE 25  44  44  PHE PHE A . n 
A 1 26  PHE 26  45  45  PHE PHE A . n 
A 1 27  ASN 27  46  46  ASN ASN A . n 
A 1 28  PRO 28  47  47  PRO PRO A . n 
A 1 29  ALA 29  48  48  ALA ALA A . n 
A 1 30  ALA 30  49  49  ALA ALA A . n 
A 1 31  GLU 31  50  50  GLU GLU A . n 
A 1 32  LYS 32  51  51  LYS LYS A . n 
A 1 33  LEU 33  52  52  LEU LEU A . n 
A 1 34  TRP 34  53  53  TRP TRP A . n 
A 1 35  GLY 35  54  54  GLY GLY A . n 
A 1 36  TYR 36  55  55  TYR TYR A . n 
A 1 37  LYS 37  56  56  LYS LYS A . n 
A 1 38  ARG 38  57  57  ARG ARG A . n 
A 1 39  GLU 39  58  58  GLU GLU A . n 
A 1 40  GLU 40  59  59  GLU GLU A . n 
A 1 41  VAL 41  60  60  VAL VAL A . n 
A 1 42  ILE 42  61  61  ILE ILE A . n 
A 1 43  GLY 43  62  62  GLY GLY A . n 
A 1 44  ASN 44  63  63  ASN ASN A . n 
A 1 45  ASN 45  64  64  ASN ASN A . n 
A 1 46  ILE 46  65  65  ILE ILE A . n 
A 1 47  ASP 47  66  66  ASP ASP A . n 
A 1 48  MET 48  67  67  MET MET A . n 
A 1 49  LEU 49  68  68  LEU LEU A . n 
A 1 50  ILE 50  69  69  ILE ILE A . n 
A 1 51  PRO 51  70  70  PRO PRO A . n 
A 1 52  ARG 52  71  71  ARG ARG A . n 
A 1 53  ASP 53  72  72  ASP ASP A . n 
A 1 54  LEU 54  73  73  LEU LEU A . n 
A 1 55  ARG 55  74  74  ARG ARG A . n 
A 1 56  PRO 56  75  75  PRO PRO A . n 
A 1 57  ALA 57  76  76  ALA ALA A . n 
A 1 58  HIS 58  77  77  HIS HIS A . n 
A 1 59  PRO 59  78  78  PRO PRO A . n 
A 1 60  GLU 60  79  79  GLU GLU A . n 
A 1 61  TYR 61  80  80  TYR TYR A . n 
A 1 62  ILE 62  81  81  ILE ILE A . n 
A 1 63  ARG 63  82  82  ARG ARG A . n 
A 1 64  HIS 64  83  83  HIS HIS A . n 
A 1 65  ASN 65  84  84  ASN ASN A . n 
A 1 66  ARG 66  85  85  ARG ARG A . n 
A 1 67  GLU 67  86  86  GLU GLU A . n 
A 1 68  GLY 68  87  87  GLY GLY A . n 
A 1 69  GLY 69  88  88  GLY GLY A . n 
A 1 70  LYS 70  89  89  LYS LYS A . n 
A 1 71  ALA 71  90  90  ALA ALA A . n 
A 1 72  ARG 72  91  91  ARG ARG A . n 
A 1 73  VAL 73  92  92  VAL VAL A . n 
A 1 74  GLU 74  93  93  GLU GLU A . n 
A 1 75  GLY 75  94  94  GLY GLY A . n 
A 1 76  MET 76  95  95  MET MET A . n 
A 1 77  SER 77  96  96  SER SER A . n 
A 1 78  ALA 78  97  97  ALA ALA A . n 
A 1 79  GLU 79  98  98  GLU GLU A . n 
A 1 80  LEU 80  99  99  LEU LEU A . n 
A 1 81  GLN 81  100 100 GLN GLN A . n 
A 1 82  LEU 82  101 101 LEU LEU A . n 
A 1 83  GLU 83  102 102 GLU GLU A . n 
A 1 84  LYS 84  103 103 LYS LYS A . n 
A 1 85  LYS 85  104 104 LYS LYS A . n 
A 1 86  ASP 86  105 105 ASP ASP A . n 
A 1 87  GLY 87  106 106 GLY GLY A . n 
A 1 88  SER 88  107 107 SER SER A . n 
A 1 89  LYS 89  108 108 LYS LYS A . n 
A 1 90  ILE 90  109 109 ILE ILE A . n 
A 1 91  TRP 91  110 110 TRP TRP A . n 
A 1 92  THR 92  111 111 THR THR A . n 
A 1 93  ARG 93  112 112 ARG ARG A . n 
A 1 94  PHE 94  113 113 PHE PHE A . n 
A 1 95  ALA 95  114 114 ALA ALA A . n 
A 1 96  LEU 96  115 115 LEU LEU A . n 
A 1 97  SER 97  116 116 SER SER A . n 
A 1 98  LYS 98  117 117 LYS LYS A . n 
A 1 99  VAL 99  118 118 VAL VAL A . n 
A 1 100 SER 100 119 119 SER SER A . n 
A 1 101 ALA 101 120 120 ALA ALA A . n 
A 1 102 GLU 102 121 121 GLU GLU A . n 
A 1 103 GLY 103 122 122 GLY GLY A . n 
A 1 104 LYS 104 123 123 LYS LYS A . n 
A 1 105 VAL 105 124 124 VAL VAL A . n 
A 1 106 TYR 106 125 125 TYR TYR A . n 
A 1 107 TYR 107 126 126 TYR TYR A . n 
A 1 108 LEU 108 127 127 LEU LEU A . n 
A 1 109 ALA 109 128 128 ALA ALA A . n 
A 1 110 LEU 110 129 129 LEU LEU A . n 
A 1 111 VAL 111 130 130 VAL VAL A . n 
A 1 112 ARG 112 131 131 ARG ARG A . n 
A 1 113 ASP 113 132 132 ASP ASP A . n 
A 1 114 ALA 114 133 133 ALA ALA A . n 
A 1 115 SER 115 134 134 SER SER A . n 
A 1 116 VAL 116 135 135 VAL VAL A . n 
A 1 117 GLU 117 136 136 GLU GLU A . n 
A 1 118 MET 118 137 137 MET MET A . n 
A 1 119 ALA 119 138 138 ALA ALA A . n 
A 1 120 GLN 120 139 139 GLN GLN A . n 
A 1 121 LYS 121 140 140 LYS LYS A . n 
A 1 122 GLU 122 141 141 GLU GLU A . n 
A 1 123 GLN 123 142 142 GLN GLN A . n 
A 1 124 THR 124 143 143 THR THR A . n 
A 1 125 ARG 125 144 144 ARG ARG A . n 
A 1 126 GLN 126 145 145 GLN GLN A . n 
A 1 127 LEU 127 146 146 LEU LEU A . n 
A 1 128 ILE 128 147 147 ILE ILE A . n 
A 1 129 ILE 129 148 148 ILE ILE A . n 
A 1 130 ALA 130 149 149 ALA ALA A . n 
A 1 131 VAL 131 150 150 VAL VAL A . n 
A 1 132 ASP 132 151 151 ASP ASP A . n 
A 1 133 HIS 133 152 152 HIS HIS A . n 
A 1 134 LEU 134 153 153 LEU LEU A . n 
A 1 135 ASP 135 154 154 ASP ASP A . n 
A 1 136 ARG 136 155 155 ARG ARG A . n 
A 1 137 PRO 137 156 156 PRO PRO A . n 
A 1 138 VAL 138 157 157 VAL VAL A . n 
A 1 139 ILE 139 158 158 ILE ILE A . n 
A 1 140 VAL 140 159 159 VAL VAL A . n 
A 1 141 LEU 141 160 160 LEU LEU A . n 
A 1 142 ASP 142 161 161 ASP ASP A . n 
A 1 143 PRO 143 162 162 PRO PRO A . n 
A 1 144 GLU 144 163 163 GLU GLU A . n 
A 1 145 ARG 145 164 164 ARG ARG A . n 
A 1 146 HIS 146 165 165 HIS HIS A . n 
A 1 147 ILE 147 166 166 ILE ILE A . n 
A 1 148 VAL 148 167 167 VAL VAL A . n 
A 1 149 GLN 149 168 168 GLN GLN A . n 
A 1 150 CYS 150 169 169 CYS CYS A . n 
A 1 151 ASN 151 170 170 ASN ASN A . n 
A 1 152 ARG 152 171 171 ARG ARG A . n 
A 1 153 ALA 153 172 172 ALA ALA A . n 
A 1 154 PHE 154 173 173 PHE PHE A . n 
A 1 155 THR 155 174 174 THR THR A . n 
A 1 156 GLU 156 175 175 GLU GLU A . n 
A 1 157 MET 157 176 176 MET MET A . n 
A 1 158 PHE 158 177 177 PHE PHE A . n 
A 1 159 GLY 159 178 178 GLY GLY A . n 
A 1 160 TYR 160 179 179 TYR TYR A . n 
A 1 161 CYS 161 180 180 CYS CYS A . n 
A 1 162 ILE 162 181 181 ILE ILE A . n 
A 1 163 SER 163 182 182 SER SER A . n 
A 1 164 GLU 164 183 183 GLU GLU A . n 
A 1 165 ALA 165 184 184 ALA ALA A . n 
A 1 166 SER 166 185 185 SER SER A . n 
A 1 167 GLY 167 186 186 GLY GLY A . n 
A 1 168 MET 168 187 187 MET MET A . n 
A 1 169 GLN 169 188 188 GLN GLN A . n 
A 1 170 PRO 170 189 189 PRO PRO A . n 
A 1 171 ASP 171 190 190 ASP ASP A . n 
A 1 172 THR 172 191 191 THR THR A . n 
A 1 173 LEU 173 192 192 LEU LEU A . n 
A 1 174 LEU 174 193 193 LEU LEU A . n 
A 1 175 ASN 175 194 194 ASN ASN A . n 
A 1 176 THR 176 195 195 THR THR A . n 
A 1 177 PRO 177 196 196 PRO PRO A . n 
A 1 178 GLU 178 197 197 GLU GLU A . n 
A 1 179 PHE 179 198 198 PHE PHE A . n 
A 1 180 PRO 180 199 199 PRO PRO A . n 
A 1 181 ALA 181 200 200 ALA ALA A . n 
A 1 182 ASP 182 201 201 ASP ASP A . n 
A 1 183 ASN 183 202 202 ASN ASN A . n 
A 1 184 ARG 184 203 203 ARG ARG A . n 
A 1 185 ILE 185 204 204 ILE ILE A . n 
A 1 186 ARG 186 205 205 ARG ARG A . n 
A 1 187 LEU 187 206 206 LEU LEU A . n 
A 1 188 GLN 188 207 207 GLN GLN A . n 
A 1 189 GLN 189 208 208 GLN GLN A . n 
A 1 190 LEU 190 209 209 LEU LEU A . n 
A 1 191 LEU 191 210 210 LEU LEU A . n 
A 1 192 TRP 192 211 211 TRP TRP A . n 
A 1 193 LYS 193 212 212 LYS LYS A . n 
A 1 194 THR 194 213 213 THR THR A . n 
A 1 195 ALA 195 214 214 ALA ALA A . n 
A 1 196 ARG 196 215 215 ARG ARG A . n 
A 1 197 ASP 197 216 216 ASP ASP A . n 
A 1 198 GLN 198 217 217 GLN GLN A . n 
A 1 199 ASP 199 218 218 ASP ASP A . n 
A 1 200 GLU 200 219 219 GLU GLU A . n 
A 1 201 PHE 201 220 220 PHE PHE A . n 
A 1 202 LEU 202 221 221 LEU LEU A . n 
A 1 203 LEU 203 222 222 LEU LEU A . n 
A 1 204 LEU 204 223 223 LEU LEU A . n 
A 1 205 THR 205 224 224 THR THR A . n 
A 1 206 ARG 206 225 225 ARG ARG A . n 
A 1 207 THR 207 226 226 THR THR A . n 
A 1 208 GLY 208 227 227 GLY GLY A . n 
A 1 209 GLU 209 228 228 GLU GLU A . n 
A 1 210 LYS 210 229 229 LYS LYS A . n 
A 1 211 ILE 211 230 230 ILE ILE A . n 
A 1 212 TRP 212 231 231 TRP TRP A . n 
A 1 213 ILE 213 232 232 ILE ILE A . n 
A 1 214 LYS 214 233 233 LYS LYS A . n 
A 1 215 ALA 215 234 234 ALA ALA A . n 
A 1 216 SER 216 235 235 SER SER A . n 
A 1 217 ILE 217 236 236 ILE ILE A . n 
A 1 218 SER 218 237 237 SER SER A . n 
A 1 219 PRO 219 238 238 PRO PRO A . n 
A 1 220 VAL 220 239 239 VAL VAL A . n 
A 1 221 TYR 221 240 240 TYR TYR A . n 
A 1 222 ASP 222 241 241 ASP ASP A . n 
A 1 223 VAL 223 242 242 VAL VAL A . n 
A 1 224 LEU 224 243 243 LEU LEU A . n 
A 1 225 ALA 225 244 244 ALA ALA A . n 
A 1 226 HIS 226 245 245 HIS HIS A . n 
A 1 227 LEU 227 246 246 LEU LEU A . n 
A 1 228 GLN 228 247 247 GLN GLN A . n 
A 1 229 ASN 229 248 248 ASN ASN A . n 
A 1 230 LEU 230 249 249 LEU LEU A . n 
A 1 231 VAL 231 250 250 VAL VAL A . n 
A 1 232 MET 232 251 251 MET MET A . n 
A 1 233 THR 233 252 252 THR THR A . n 
A 1 234 PHE 234 253 253 PHE PHE A . n 
A 1 235 SER 235 254 254 SER SER A . n 
A 1 236 ASP 236 255 255 ASP ASP A . n 
A 1 237 ILE 237 256 256 ILE ILE A . n 
A 1 238 THR 238 257 257 THR THR A . n 
A 1 239 GLU 239 258 258 GLU GLU A . n 
A 1 240 GLU 240 259 259 GLU GLU A . n 
A 1 241 ARG 241 260 260 ARG ARG A . n 
A 1 242 GLN 242 261 261 GLN GLN A . n 
A 1 243 ILE 243 262 262 ILE ILE A . n 
A 1 244 ARG 244 263 263 ARG ARG A . n 
A 1 245 GLN 245 264 264 GLN GLN A . n 
A 1 246 LEU 246 265 265 LEU LEU A . n 
A 1 247 GLU 247 266 266 GLU GLU A . n 
A 1 248 GLY 248 267 267 GLY GLY A . n 
A 1 249 ASN 249 268 268 ASN ASN A . n 
A 1 250 ILE 250 269 269 ILE ILE A . n 
A 1 251 LEU 251 270 270 LEU LEU A . n 
A 1 252 ALA 252 271 271 ALA ALA A . n 
A 1 253 ALA 253 272 272 ALA ALA A . n 
A 1 254 MET 254 273 273 MET MET A . n 
A 1 255 CYS 255 274 274 CYS CYS A . n 
A 1 256 SER 256 275 275 SER SER A . n 
A 1 257 SER 257 276 276 SER SER A . n 
A 1 258 PRO 258 277 277 PRO PRO A . n 
A 1 259 PRO 259 278 278 PRO PRO A . n 
A 1 260 PHE 260 279 279 PHE PHE A . n 
A 1 261 HIS 261 280 280 HIS HIS A . n 
A 1 262 GLU 262 281 281 GLU GLU A . n 
A 1 263 MET 263 282 282 MET MET A . n 
A 1 264 GLY 264 283 283 GLY GLY A . n 
A 1 265 GLU 265 284 284 GLU GLU A . n 
A 1 266 ILE 266 285 285 ILE ILE A . n 
A 1 267 ILE 267 286 286 ILE ILE A . n 
A 1 268 CYS 268 287 287 CYS CYS A . n 
A 1 269 ARG 269 288 288 ARG ARG A . n 
A 1 270 ASN 270 289 289 ASN ASN A . n 
A 1 271 ILE 271 290 290 ILE ILE A . n 
A 1 272 GLU 272 291 291 GLU GLU A . n 
A 1 273 SER 273 292 292 SER SER A . n 
A 1 274 VAL 274 293 293 VAL VAL A . n 
A 1 275 LEU 275 294 294 LEU LEU A . n 
A 1 276 ASN 276 295 295 ASN ASN A . n 
A 1 277 GLU 277 296 296 GLU GLU A . n 
A 1 278 SER 278 297 297 SER SER A . n 
A 1 279 HIS 279 298 298 HIS HIS A . n 
A 1 280 VAL 280 299 299 VAL VAL A . n 
A 1 281 SER 281 300 300 SER SER A . n 
A 1 282 LEU 282 301 301 LEU LEU A . n 
A 1 283 PHE 283 302 302 PHE PHE A . n 
A 1 284 ALA 284 303 303 ALA ALA A . n 
A 1 285 LEU 285 304 304 LEU LEU A . n 
A 1 286 ARG 286 305 305 ARG ARG A . n 
A 1 287 ASN 287 306 306 ASN ASN A . n 
A 1 288 GLY 288 307 307 GLY GLY A . n 
A 1 289 MET 289 308 308 MET MET A . n 
A 1 290 PRO 290 309 309 PRO PRO A . n 
A 1 291 ILE 291 310 310 ILE ILE A . n 
A 1 292 HIS 292 311 311 HIS HIS A . n 
A 1 293 TRP 293 312 312 TRP TRP A . n 
A 1 294 ALA 294 313 313 ALA ALA A . n 
A 1 295 SER 295 314 314 SER SER A . n 
A 1 296 SER 296 315 315 SER SER A . n 
A 1 297 SER 297 316 316 SER SER A . n 
A 1 298 HIS 298 317 317 HIS HIS A . n 
A 1 299 GLY 299 318 318 GLY GLY A . n 
A 1 300 ALA 300 319 319 ALA ALA A . n 
A 1 301 GLU 301 320 320 GLU GLU A . n 
A 1 302 ILE 302 321 321 ILE ILE A . n 
A 1 303 GLN 303 322 322 GLN GLN A . n 
A 1 304 ASN 304 323 323 ASN ASN A . n 
A 1 305 ALA 305 324 324 ALA ALA A . n 
A 1 306 GLN 306 325 325 GLN GLN A . n 
A 1 307 SER 307 326 326 SER SER A . n 
A 1 308 TRP 308 327 327 TRP TRP A . n 
A 1 309 SER 309 328 328 SER SER A . n 
A 1 310 ALA 310 329 329 ALA ALA A . n 
A 1 311 THR 311 330 330 THR THR A . n 
A 1 312 ILE 312 331 331 ILE ILE A . n 
A 1 313 ARG 313 332 332 ARG ARG A . n 
A 1 314 GLN 314 333 333 GLN GLN A . n 
A 1 315 ARG 315 334 334 ARG ARG A . n 
A 1 316 ASP 316 335 335 ASP ASP A . n 
A 1 317 GLY 317 336 336 GLY GLY A . n 
A 1 318 ALA 318 337 337 ALA ALA A . n 
A 1 319 PRO 319 338 338 PRO PRO A . n 
A 1 320 ALA 320 339 339 ALA ALA A . n 
A 1 321 GLY 321 340 340 GLY GLY A . n 
A 1 322 ILE 322 341 341 ILE ILE A . n 
A 1 323 LEU 323 342 342 LEU LEU A . n 
A 1 324 GLN 324 343 343 GLN GLN A . n 
A 1 325 ILE 325 344 344 ILE ILE A . n 
A 1 326 LYS 326 345 345 LYS LYS A . n 
A 1 327 THR 327 346 346 THR THR A . n 
A 1 328 SER 328 347 347 SER SER A . n 
A 1 329 SER 329 348 348 SER SER A . n 
A 1 330 GLY 330 349 349 GLY GLY A . n 
A 1 331 ALA 331 350 350 ALA ALA A . n 
A 1 332 GLU 332 351 351 GLU GLU A . n 
A 1 333 THR 333 352 352 THR THR A . n 
A 1 334 SER 334 353 353 SER SER A . n 
A 1 335 ALA 335 354 354 ALA ALA A . n 
A 1 336 PHE 336 355 355 PHE PHE A . n 
A 1 337 ILE 337 356 356 ILE ILE A . n 
A 1 338 GLU 338 357 357 GLU GLU A . n 
A 1 339 ARG 339 358 358 ARG ARG A . n 
A 1 340 VAL 340 359 359 VAL VAL A . n 
A 1 341 ALA 341 360 360 ALA ALA A . n 
A 1 342 ASP 342 361 361 ASP ASP A . n 
A 1 343 ILE 343 362 362 ILE ILE A . n 
A 1 344 SER 344 363 363 SER SER A . n 
A 1 345 GLN 345 364 364 GLN GLN A . n 
A 1 346 HIS 346 365 365 HIS HIS A . n 
A 1 347 MET 347 366 366 MET MET A . n 
A 1 348 ALA 348 367 367 ALA ALA A . n 
A 1 349 ALA 349 368 368 ALA ALA A . n 
A 1 350 LEU 350 369 369 LEU LEU A . n 
A 1 351 ALA 351 370 370 ALA ALA A . n 
A 1 352 LEU 352 371 371 LEU LEU A . n 
A 1 353 GLU 353 372 372 GLU GLU A . n 
A 1 354 GLN 354 373 373 GLN GLN A . n 
A 1 355 GLU 355 374 374 GLU GLU A . n 
A 1 356 LYS 356 375 375 LYS LYS A . n 
A 1 357 SER 357 376 376 SER SER A . n 
A 1 358 ARG 358 377 377 ARG ARG A . n 
A 1 359 GLN 359 378 378 GLN GLN A . n 
A 1 360 HIS 360 379 379 HIS HIS A . n 
A 1 361 ILE 361 380 380 ILE ILE A . n 
A 1 362 GLU 362 381 381 GLU GLU A . n 
A 1 363 GLN 363 382 382 GLN GLN A . n 
A 1 364 LEU 364 383 383 LEU LEU A . n 
A 1 365 ILE 365 384 384 ILE ILE A . n 
A 1 366 GLN 366 385 385 GLN GLN A . n 
A 1 367 PHE 367 386 386 PHE PHE A . n 
A 1 368 ASP 368 387 387 ASP ASP A . n 
A 1 369 PRO 369 388 388 PRO PRO A . n 
A 1 370 MET 370 389 389 MET MET A . n 
A 1 371 THR 371 390 390 THR THR A . n 
A 1 372 GLY 372 391 391 GLY GLY A . n 
A 1 373 LEU 373 392 392 LEU LEU A . n 
A 1 374 PRO 374 393 393 PRO PRO A . n 
A 1 375 ASN 375 394 394 ASN ASN A . n 
A 1 376 ARG 376 395 395 ARG ARG A . n 
A 1 377 ASN 377 396 396 ASN ASN A . n 
A 1 378 ASN 378 397 397 ASN ASN A . n 
A 1 379 LEU 379 398 398 LEU LEU A . n 
A 1 380 HIS 380 399 399 HIS HIS A . n 
A 1 381 ASN 381 400 400 ASN ASN A . n 
A 1 382 TYR 382 401 401 TYR TYR A . n 
A 1 383 LEU 383 402 402 LEU LEU A . n 
A 1 384 ASP 384 403 403 ASP ASP A . n 
A 1 385 ASP 385 404 404 ASP ASP A . n 
A 1 386 LEU 386 405 405 LEU LEU A . n 
A 1 387 VAL 387 406 406 VAL VAL A . n 
A 1 388 ASP 388 407 407 ASP ASP A . n 
A 1 389 LYS 389 408 408 LYS LYS A . n 
A 1 390 ALA 390 409 409 ALA ALA A . n 
A 1 391 VAL 391 410 410 VAL VAL A . n 
A 1 392 SER 392 411 411 SER SER A . n 
A 1 393 PRO 393 412 412 PRO PRO A . n 
A 1 394 VAL 394 413 413 VAL VAL A . n 
A 1 395 VAL 395 414 414 VAL VAL A . n 
A 1 396 TYR 396 415 415 TYR TYR A . n 
A 1 397 LEU 397 416 416 LEU LEU A . n 
A 1 398 ILE 398 417 417 ILE ILE A . n 
A 1 399 GLY 399 418 418 GLY GLY A . n 
A 1 400 VAL 400 419 419 VAL VAL A . n 
A 1 401 ASP 401 420 420 ASP ASP A . n 
A 1 402 HIS 402 421 421 HIS HIS A . n 
A 1 403 ILE 403 422 422 ILE ILE A . n 
A 1 404 GLN 404 423 423 GLN GLN A . n 
A 1 405 ASP 405 424 424 ASP ASP A . n 
A 1 406 VAL 406 425 425 VAL VAL A . n 
A 1 407 ILE 407 426 426 ILE ILE A . n 
A 1 408 ASP 408 427 427 ASP ASP A . n 
A 1 409 SER 409 428 428 SER SER A . n 
A 1 410 LEU 410 429 429 LEU LEU A . n 
A 1 411 GLY 411 430 430 GLY GLY A . n 
A 1 412 TYR 412 431 431 TYR TYR A . n 
A 1 413 ALA 413 432 432 ALA ALA A . n 
A 1 414 TRP 414 433 433 TRP TRP A . n 
A 1 415 ALA 415 434 434 ALA ALA A . n 
A 1 416 ASP 416 435 435 ASP ASP A . n 
A 1 417 GLN 417 436 436 GLN GLN A . n 
A 1 418 ALA 418 437 437 ALA ALA A . n 
A 1 419 LEU 419 438 438 LEU LEU A . n 
A 1 420 LEU 420 439 439 LEU LEU A . n 
A 1 421 GLU 421 440 440 GLU GLU A . n 
A 1 422 VAL 422 441 441 VAL VAL A . n 
A 1 423 VAL 423 442 442 VAL VAL A . n 
A 1 424 ASN 424 443 443 ASN ASN A . n 
A 1 425 ARG 425 444 444 ARG ARG A . n 
A 1 426 PHE 426 445 445 PHE PHE A . n 
A 1 427 ARG 427 446 446 ARG ARG A . n 
A 1 428 GLU 428 447 447 GLU GLU A . n 
A 1 429 LYS 429 448 448 LYS LYS A . n 
A 1 430 LEU 430 449 449 LEU LEU A . n 
A 1 431 LYS 431 450 450 LYS LYS A . n 
A 1 432 PRO 432 451 451 PRO PRO A . n 
A 1 433 ASP 433 452 452 ASP ASP A . n 
A 1 434 GLN 434 453 453 GLN GLN A . n 
A 1 435 TYR 435 454 454 TYR TYR A . n 
A 1 436 LEU 436 455 455 LEU LEU A . n 
A 1 437 CYS 437 456 456 CYS CYS A . n 
A 1 438 ARG 438 457 457 ARG ARG A . n 
A 1 439 ILE 439 458 458 ILE ILE A . n 
A 1 440 GLU 440 459 459 GLU GLU A . n 
A 1 441 GLY 441 460 460 GLY GLY A . n 
A 1 442 THR 442 461 461 THR THR A . n 
A 1 443 GLN 443 462 462 GLN GLN A . n 
A 1 444 PHE 444 463 463 PHE PHE A . n 
A 1 445 VAL 445 464 464 VAL VAL A . n 
A 1 446 LEU 446 465 465 LEU LEU A . n 
A 1 447 VAL 447 466 466 VAL VAL A . n 
A 1 448 SER 448 467 467 SER SER A . n 
A 1 449 LEU 449 468 468 LEU LEU A . n 
A 1 450 GLU 450 469 469 GLU GLU A . n 
A 1 451 ASN 451 470 470 ASN ASN A . n 
A 1 452 ASP 452 471 471 ASP ASP A . n 
A 1 453 VAL 453 472 472 VAL VAL A . n 
A 1 454 SER 454 473 473 SER SER A . n 
A 1 455 ASN 455 474 474 ASN ASN A . n 
A 1 456 ILE 456 475 475 ILE ILE A . n 
A 1 457 THR 457 476 476 THR THR A . n 
A 1 458 GLN 458 477 477 GLN GLN A . n 
A 1 459 ILE 459 478 478 ILE ILE A . n 
A 1 460 ALA 460 479 479 ALA ALA A . n 
A 1 461 ASP 461 480 480 ASP ASP A . n 
A 1 462 GLU 462 481 481 GLU GLU A . n 
A 1 463 LEU 463 482 482 LEU LEU A . n 
A 1 464 ARG 464 483 483 ARG ARG A . n 
A 1 465 ASN 465 484 484 ASN ASN A . n 
A 1 466 VAL 466 485 485 VAL VAL A . n 
A 1 467 VAL 467 486 486 VAL VAL A . n 
A 1 468 SER 468 487 487 SER SER A . n 
A 1 469 LYS 469 488 488 LYS LYS A . n 
A 1 470 PRO 470 489 489 PRO PRO A . n 
A 1 471 ILE 471 490 490 ILE ILE A . n 
A 1 472 MET 472 491 491 MET MET A . n 
A 1 473 ILE 473 492 492 ILE ILE A . n 
A 1 474 ASP 474 493 493 ASP ASP A . n 
A 1 475 ASP 475 494 494 ASP ASP A . n 
A 1 476 LYS 476 495 495 LYS LYS A . n 
A 1 477 PRO 477 496 496 PRO PRO A . n 
A 1 478 PHE 478 497 497 PHE PHE A . n 
A 1 479 PRO 479 498 498 PRO PRO A . n 
A 1 480 LEU 480 499 499 LEU LEU A . n 
A 1 481 THR 481 500 500 THR THR A . n 
A 1 482 LEU 482 501 501 LEU LEU A . n 
A 1 483 SER 483 502 502 SER SER A . n 
A 1 484 ILE 484 503 503 ILE ILE A . n 
A 1 485 GLY 485 504 504 GLY GLY A . n 
A 1 486 ILE 486 505 505 ILE ILE A . n 
A 1 487 SER 487 506 506 SER SER A . n 
A 1 488 TYR 488 507 507 TYR TYR A . n 
A 1 489 ASP 489 508 508 ASP ASP A . n 
A 1 490 LEU 490 509 509 LEU LEU A . n 
A 1 491 GLY 491 510 510 GLY GLY A . n 
A 1 492 LYS 492 511 511 LYS LYS A . n 
A 1 493 ASN 493 512 512 ASN ASN A . n 
A 1 494 ARG 494 513 513 ARG ARG A . n 
A 1 495 ASP 495 514 514 ASP ASP A . n 
A 1 496 TYR 496 515 515 TYR TYR A . n 
A 1 497 LEU 497 516 516 LEU LEU A . n 
A 1 498 LEU 498 517 517 LEU LEU A . n 
A 1 499 SER 499 518 518 SER SER A . n 
A 1 500 THR 500 519 519 THR THR A . n 
A 1 501 ALA 501 520 520 ALA ALA A . n 
A 1 502 HIS 502 521 521 HIS HIS A . n 
A 1 503 ASN 503 522 522 ASN ASN A . n 
A 1 504 ALA 504 523 523 ALA ALA A . n 
A 1 505 MET 505 524 524 MET MET A . n 
A 1 506 ASP 506 525 525 ASP ASP A . n 
A 1 507 TYR 507 526 526 TYR TYR A . n 
A 1 508 ILE 508 527 527 ILE ILE A . n 
A 1 509 ARG 509 528 528 ARG ARG A . n 
A 1 510 LYS 510 529 529 LYS LYS A . n 
A 1 511 ASN 511 530 530 ASN ASN A . n 
A 1 512 GLY 512 531 531 GLY GLY A . n 
A 1 513 GLY 513 532 532 GLY GLY A . n 
A 1 514 ASN 514 533 533 ASN ASN A . n 
A 1 515 GLY 515 534 534 GLY GLY A . n 
A 1 516 TRP 516 535 535 TRP TRP A . n 
A 1 517 GLN 517 536 536 GLN GLN A . n 
A 1 518 PHE 518 537 537 PHE PHE A . n 
A 1 519 PHE 519 538 538 PHE PHE A . n 
A 1 520 SER 520 539 539 SER SER A . n 
A 1 521 PRO 521 540 540 PRO PRO A . n 
A 1 522 ALA 522 541 541 ALA ALA A . n 
A 1 523 MET 523 542 542 MET MET A . n 
A 1 524 ASN 524 543 543 ASN ASN A . n 
A 1 525 GLU 525 544 544 GLU GLU A . n 
A 1 526 MET 526 545 545 MET MET A . n 
A 1 527 VAL 527 546 546 VAL VAL A . n 
A 1 528 LYS 528 547 547 LYS LYS A . n 
A 1 529 GLU 529 548 548 GLU GLU A . n 
A 1 530 ARG 530 549 549 ARG ARG A . n 
A 1 531 LEU 531 550 550 LEU LEU A . n 
A 1 532 VAL 532 551 551 VAL VAL A . n 
A 1 533 LEU 533 552 552 LEU LEU A . n 
A 1 534 GLY 534 553 553 GLY GLY A . n 
A 1 535 ALA 535 554 554 ALA ALA A . n 
A 1 536 ALA 536 555 555 ALA ALA A . n 
A 1 537 LEU 537 556 556 LEU LEU A . n 
A 1 538 LYS 538 557 557 LYS LYS A . n 
A 1 539 GLU 539 558 558 GLU GLU A . n 
A 1 540 ALA 540 559 559 ALA ALA A . n 
A 1 541 ILE 541 560 560 ILE ILE A . n 
A 1 542 SER 542 561 561 SER SER A . n 
A 1 543 ASN 543 562 562 ASN ASN A . n 
A 1 544 ASN 544 563 563 ASN ASN A . n 
A 1 545 GLN 545 564 564 GLN GLN A . n 
A 1 546 LEU 546 565 565 LEU LEU A . n 
A 1 547 LYS 547 566 566 LYS LYS A . n 
A 1 548 LEU 548 567 567 LEU LEU A . n 
A 1 549 VAL 549 568 568 VAL VAL A . n 
A 1 550 TYR 550 569 569 TYR TYR A . n 
A 1 551 GLN 551 570 570 GLN GLN A . n 
A 1 552 PRO 552 571 571 PRO PRO A . n 
A 1 553 GLN 553 572 572 GLN GLN A . n 
A 1 554 ILE 554 573 573 ILE ILE A . n 
A 1 555 PHE 555 574 574 PHE PHE A . n 
A 1 556 ALA 556 575 575 ALA ALA A . n 
A 1 557 GLU 557 576 576 GLU GLU A . n 
A 1 558 THR 558 577 577 THR THR A . n 
A 1 559 GLY 559 578 578 GLY GLY A . n 
A 1 560 GLU 560 579 579 GLU GLU A . n 
A 1 561 LEU 561 580 580 LEU LEU A . n 
A 1 562 TYR 562 581 581 TYR TYR A . n 
A 1 563 GLY 563 582 582 GLY GLY A . n 
A 1 564 ILE 564 583 583 ILE ILE A . n 
A 1 565 GLU 565 584 584 GLU GLU A . n 
A 1 566 ALA 566 585 585 ALA ALA A . n 
A 1 567 LEU 567 586 586 LEU LEU A . n 
A 1 568 ALA 568 587 587 ALA ALA A . n 
A 1 569 ARG 569 588 588 ARG ARG A . n 
A 1 570 TRP 570 589 589 TRP TRP A . n 
A 1 571 HIS 571 590 590 HIS HIS A . n 
A 1 572 ASP 572 591 591 ASP ASP A . n 
A 1 573 PRO 573 592 592 PRO PRO A . n 
A 1 574 LEU 574 593 593 LEU LEU A . n 
A 1 575 HIS 575 594 594 HIS HIS A . n 
A 1 576 GLY 576 595 595 GLY GLY A . n 
A 1 577 HIS 577 596 596 HIS HIS A . n 
A 1 578 VAL 578 597 597 VAL VAL A . n 
A 1 579 PRO 579 598 598 PRO PRO A . n 
A 1 580 PRO 580 599 599 PRO PRO A . n 
A 1 581 SER 581 600 600 SER SER A . n 
A 1 582 ARG 582 601 601 ARG ARG A . n 
A 1 583 PHE 583 602 602 PHE PHE A . n 
A 1 584 ILE 584 603 603 ILE ILE A . n 
A 1 585 PRO 585 604 604 PRO PRO A . n 
A 1 586 LEU 586 605 605 LEU LEU A . n 
A 1 587 ALA 587 606 606 ALA ALA A . n 
A 1 588 GLU 588 607 607 GLU GLU A . n 
A 1 589 GLU 589 608 608 GLU GLU A . n 
A 1 590 ILE 590 609 609 ILE ILE A . n 
A 1 591 GLY 591 610 610 GLY GLY A . n 
A 1 592 GLU 592 611 611 GLU GLU A . n 
A 1 593 ILE 593 612 612 ILE ILE A . n 
A 1 594 GLU 594 613 613 GLU GLU A . n 
A 1 595 ASN 595 614 614 ASN ASN A . n 
A 1 596 ILE 596 615 615 ILE ILE A . n 
A 1 597 GLY 597 616 616 GLY GLY A . n 
A 1 598 ARG 598 617 617 ARG ARG A . n 
A 1 599 TRP 599 618 618 TRP TRP A . n 
A 1 600 VAL 600 619 619 VAL VAL A . n 
A 1 601 ILE 601 620 620 ILE ILE A . n 
A 1 602 ALA 602 621 621 ALA ALA A . n 
A 1 603 GLU 603 622 622 GLU GLU A . n 
A 1 604 ALA 604 623 623 ALA ALA A . n 
A 1 605 CYS 605 624 624 CYS CYS A . n 
A 1 606 ARG 606 625 625 ARG ARG A . n 
A 1 607 GLN 607 626 626 GLN GLN A . n 
A 1 608 LEU 608 627 627 LEU LEU A . n 
A 1 609 ALA 609 628 628 ALA ALA A . n 
A 1 610 GLU 610 629 629 GLU GLU A . n 
A 1 611 TRP 611 630 630 TRP TRP A . n 
A 1 612 ARG 612 631 631 ARG ARG A . n 
A 1 613 SER 613 632 632 SER SER A . n 
A 1 614 GLN 614 633 633 GLN GLN A . n 
A 1 615 ASN 615 634 634 ASN ASN A . n 
A 1 616 ILE 616 635 635 ILE ILE A . n 
A 1 617 HIS 617 636 636 HIS HIS A . n 
A 1 618 ILE 618 637 637 ILE ILE A . n 
A 1 619 PRO 619 638 638 PRO PRO A . n 
A 1 620 ALA 620 639 639 ALA ALA A . n 
A 1 621 LEU 621 640 640 LEU LEU A . n 
A 1 622 SER 622 641 641 SER SER A . n 
A 1 623 VAL 623 642 642 VAL VAL A . n 
A 1 624 ASN 624 643 643 ASN ASN A . n 
A 1 625 LEU 625 644 644 LEU LEU A . n 
A 1 626 SER 626 645 645 SER SER A . n 
A 1 627 ALA 627 646 646 ALA ALA A . n 
A 1 628 LEU 628 647 647 LEU LEU A . n 
A 1 629 HIS 629 648 648 HIS HIS A . n 
A 1 630 PHE 630 649 649 PHE PHE A . n 
A 1 631 ARG 631 650 650 ARG ARG A . n 
A 1 632 SER 632 651 651 SER SER A . n 
A 1 633 ASN 633 652 652 ASN ASN A . n 
A 1 634 GLN 634 653 653 GLN GLN A . n 
A 1 635 LEU 635 654 654 LEU LEU A . n 
A 1 636 PRO 636 655 655 PRO PRO A . n 
A 1 637 ASN 637 656 656 ASN ASN A . n 
A 1 638 GLN 638 657 657 GLN GLN A . n 
A 1 639 VAL 639 658 658 VAL VAL A . n 
A 1 640 SER 640 659 659 SER SER A . n 
A 1 641 ASP 641 660 660 ASP ASP A . n 
A 1 642 ALA 642 661 661 ALA ALA A . n 
A 1 643 MET 643 662 662 MET MET A . n 
A 1 644 HIS 644 663 663 HIS HIS A . n 
A 1 645 ALA 645 664 664 ALA ALA A . n 
A 1 646 TRP 646 665 665 TRP TRP A . n 
A 1 647 GLY 647 666 666 GLY GLY A . n 
A 1 648 ILE 648 667 667 ILE ILE A . n 
A 1 649 ASP 649 668 668 ASP ASP A . n 
A 1 650 GLY 650 669 669 GLY GLY A . n 
A 1 651 HIS 651 670 670 HIS HIS A . n 
A 1 652 GLN 652 671 671 GLN GLN A . n 
A 1 653 LEU 653 672 672 LEU LEU A . n 
A 1 654 THR 654 673 673 THR THR A . n 
A 1 655 VAL 655 674 674 VAL VAL A . n 
A 1 656 GLU 656 675 675 GLU GLU A . n 
A 1 657 ILE 657 676 676 ILE ILE A . n 
A 1 658 THR 658 677 677 THR THR A . n 
A 1 659 GLU 659 678 678 GLU GLU A . n 
A 1 660 SER 660 679 679 SER SER A . n 
A 1 661 MET 661 680 680 MET MET A . n 
A 1 662 MET 662 681 681 MET MET A . n 
A 1 663 MET 663 682 682 MET MET A . n 
A 1 664 GLU 664 683 683 GLU GLU A . n 
A 1 665 HIS 665 684 684 HIS HIS A . n 
A 1 666 ASP 666 685 685 ASP ASP A . n 
A 1 667 THR 667 686 686 THR THR A . n 
A 1 668 GLU 668 687 687 GLU GLU A . n 
A 1 669 ILE 669 688 688 ILE ILE A . n 
A 1 670 PHE 670 689 689 PHE PHE A . n 
A 1 671 LYS 671 690 690 LYS LYS A . n 
A 1 672 ARG 672 691 691 ARG ARG A . n 
A 1 673 ILE 673 692 692 ILE ILE A . n 
A 1 674 GLN 674 693 693 GLN GLN A . n 
A 1 675 ILE 675 694 694 ILE ILE A . n 
A 1 676 LEU 676 695 695 LEU LEU A . n 
A 1 677 ARG 677 696 696 ARG ARG A . n 
A 1 678 ASP 678 697 697 ASP ASP A . n 
A 1 679 MET 679 698 698 MET MET A . n 
A 1 680 GLY 680 699 699 GLY GLY A . n 
A 1 681 VAL 681 700 700 VAL VAL A . n 
A 1 682 GLY 682 701 701 GLY GLY A . n 
A 1 683 LEU 683 702 702 LEU LEU A . n 
A 1 684 SER 684 703 703 SER SER A . n 
A 1 685 VAL 685 704 704 VAL VAL A . n 
A 1 686 ASP 686 705 705 ASP ASP A . n 
A 1 687 ASP 687 706 706 ASP ASP A . n 
A 1 688 PHE 688 707 707 PHE PHE A . n 
A 1 689 GLY 689 708 708 GLY GLY A . n 
A 1 690 THR 690 709 709 THR THR A . n 
A 1 691 GLY 691 710 710 GLY GLY A . n 
A 1 692 PHE 692 711 711 PHE PHE A . n 
A 1 693 SER 693 712 712 SER SER A . n 
A 1 694 GLY 694 713 713 GLY GLY A . n 
A 1 695 LEU 695 714 714 LEU LEU A . n 
A 1 696 SER 696 715 715 SER SER A . n 
A 1 697 ARG 697 716 716 ARG ARG A . n 
A 1 698 LEU 698 717 717 LEU LEU A . n 
A 1 699 VAL 699 718 718 VAL VAL A . n 
A 1 700 SER 700 719 719 SER SER A . n 
A 1 701 LEU 701 720 720 LEU LEU A . n 
A 1 702 PRO 702 721 721 PRO PRO A . n 
A 1 703 VAL 703 722 722 VAL VAL A . n 
A 1 704 THR 704 723 723 THR THR A . n 
A 1 705 GLU 705 724 724 GLU GLU A . n 
A 1 706 ILE 706 725 725 ILE ILE A . n 
A 1 707 LYS 707 726 726 LYS LYS A . n 
A 1 708 ILE 708 727 727 ILE ILE A . n 
A 1 709 ASP 709 728 728 ASP ASP A . n 
A 1 710 LYS 710 729 729 LYS LYS A . n 
A 1 711 SER 711 730 730 SER SER A . n 
A 1 712 PHE 712 731 731 PHE PHE A . n 
A 1 713 VAL 713 732 732 VAL VAL A . n 
A 1 714 ASP 714 733 733 ASP ASP A . n 
A 1 715 ARG 715 734 734 ARG ARG A . n 
A 1 716 CYS 716 735 735 CYS CYS A . n 
A 1 717 LEU 717 736 736 LEU LEU A . n 
A 1 718 THR 718 737 737 THR THR A . n 
A 1 719 GLU 719 738 738 GLU GLU A . n 
A 1 720 LYS 720 739 739 LYS LYS A . n 
A 1 721 ARG 721 740 740 ARG ARG A . n 
A 1 722 ILE 722 741 741 ILE ILE A . n 
A 1 723 LEU 723 742 742 LEU LEU A . n 
A 1 724 ALA 724 743 743 ALA ALA A . n 
A 1 725 LEU 725 744 744 LEU LEU A . n 
A 1 726 LEU 726 745 745 LEU LEU A . n 
A 1 727 GLU 727 746 746 GLU GLU A . n 
A 1 728 ALA 728 747 747 ALA ALA A . n 
A 1 729 ILE 729 748 748 ILE ILE A . n 
A 1 730 THR 730 749 749 THR THR A . n 
A 1 731 SER 731 750 750 SER SER A . n 
A 1 732 ILE 732 751 751 ILE ILE A . n 
A 1 733 GLY 733 752 752 GLY GLY A . n 
A 1 734 GLN 734 753 753 GLN GLN A . n 
A 1 735 SER 735 754 754 SER SER A . n 
A 1 736 LEU 736 755 755 LEU LEU A . n 
A 1 737 ASN 737 756 756 ASN ASN A . n 
A 1 738 LEU 738 757 757 LEU LEU A . n 
A 1 739 THR 739 758 758 THR THR A . n 
A 1 740 VAL 740 759 759 VAL VAL A . n 
A 1 741 VAL 741 760 760 VAL VAL A . n 
A 1 742 ALA 742 761 761 ALA ALA A . n 
A 1 743 GLU 743 762 762 GLU GLU A . n 
A 1 744 GLY 744 763 763 GLY GLY A . n 
A 1 745 VAL 745 764 764 VAL VAL A . n 
A 1 746 GLU 746 765 765 GLU GLU A . n 
A 1 747 THR 747 766 766 THR THR A . n 
A 1 748 LYS 748 767 767 LYS LYS A . n 
A 1 749 GLU 749 768 768 GLU GLU A . n 
A 1 750 GLN 750 769 769 GLN GLN A . n 
A 1 751 PHE 751 770 770 PHE PHE A . n 
A 1 752 GLU 752 771 771 GLU GLU A . n 
A 1 753 MET 753 772 772 MET MET A . n 
A 1 754 LEU 754 773 773 LEU LEU A . n 
A 1 755 ARG 755 774 774 ARG ARG A . n 
A 1 756 LYS 756 775 775 LYS LYS A . n 
A 1 757 ILE 757 776 776 ILE ILE A . n 
A 1 758 HIS 758 777 777 HIS HIS A . n 
A 1 759 CYS 759 778 778 CYS CYS A . n 
A 1 760 ARG 760 779 779 ARG ARG A . n 
A 1 761 VAL 761 780 780 VAL VAL A . n 
A 1 762 ILE 762 781 781 ILE ILE A . n 
A 1 763 GLN 763 782 782 GLN GLN A . n 
A 1 764 GLY 764 783 783 GLY GLY A . n 
A 1 765 TYR 765 784 784 TYR TYR A . n 
A 1 766 PHE 766 785 785 PHE PHE A . n 
A 1 767 PHE 767 786 786 PHE PHE A . n 
A 1 768 SER 768 787 787 SER SER A . n 
A 1 769 ARG 769 788 788 ARG ARG A . n 
A 1 770 PRO 770 789 789 PRO PRO A . n 
A 1 771 LEU 771 790 790 LEU LEU A . n 
A 1 772 PRO 772 791 791 PRO PRO A . n 
A 1 773 ALA 773 792 792 ALA ALA A . n 
A 1 774 GLU 774 793 793 GLU GLU A . n 
A 1 775 GLU 775 794 794 GLU GLU A . n 
A 1 776 ILE 776 795 795 ILE ILE A . n 
A 1 777 PRO 777 796 796 PRO PRO A . n 
A 1 778 GLY 778 797 797 GLY GLY A . n 
A 1 779 TRP 779 798 798 TRP TRP A . n 
A 1 780 MET 780 799 799 MET MET A . n 
A 1 781 SER 781 800 800 SER SER A . n 
A 1 782 SER 782 801 801 SER SER A . n 
A 1 783 VAL 783 802 802 VAL VAL A . n 
A 1 784 LEU 784 803 803 LEU LEU A . n 
A 1 785 PRO 785 804 804 PRO PRO A . n 
A 1 786 LEU 786 805 805 LEU LEU A . n 
A 1 787 LYS 787 806 806 LYS LYS A . n 
B 1 1   GLY 1   20  20  GLY GLY B . n 
B 1 2   ILE 2   21  21  ILE ILE B . n 
B 1 3   PHE 3   22  22  PHE PHE B . n 
B 1 4   PHE 4   23  23  PHE PHE B . n 
B 1 5   PRO 5   24  24  PRO PRO B . n 
B 1 6   ALA 6   25  25  ALA ALA B . n 
B 1 7   LEU 7   26  26  LEU LEU B . n 
B 1 8   GLU 8   27  27  GLU GLU B . n 
B 1 9   GLN 9   28  28  GLN GLN B . n 
B 1 10  ASN 10  29  29  ASN ASN B . n 
B 1 11  MET 11  30  30  MET MET B . n 
B 1 12  MET 12  31  31  MET MET B . n 
B 1 13  GLY 13  32  32  GLY GLY B . n 
B 1 14  ALA 14  33  33  ALA ALA B . n 
B 1 15  VAL 15  34  34  VAL VAL B . n 
B 1 16  LEU 16  35  35  LEU LEU B . n 
B 1 17  ILE 17  36  36  ILE ILE B . n 
B 1 18  ASN 18  37  37  ASN ASN B . n 
B 1 19  GLU 19  38  38  GLU GLU B . n 
B 1 20  ASN 20  39  39  ASN ASN B . n 
B 1 21  ASP 21  40  40  ASP ASP B . n 
B 1 22  GLU 22  41  41  GLU GLU B . n 
B 1 23  VAL 23  42  42  VAL VAL B . n 
B 1 24  MET 24  43  43  MET MET B . n 
B 1 25  PHE 25  44  44  PHE PHE B . n 
B 1 26  PHE 26  45  45  PHE PHE B . n 
B 1 27  ASN 27  46  46  ASN ASN B . n 
B 1 28  PRO 28  47  47  PRO PRO B . n 
B 1 29  ALA 29  48  48  ALA ALA B . n 
B 1 30  ALA 30  49  49  ALA ALA B . n 
B 1 31  GLU 31  50  50  GLU GLU B . n 
B 1 32  LYS 32  51  51  LYS LYS B . n 
B 1 33  LEU 33  52  52  LEU LEU B . n 
B 1 34  TRP 34  53  53  TRP TRP B . n 
B 1 35  GLY 35  54  54  GLY GLY B . n 
B 1 36  TYR 36  55  55  TYR TYR B . n 
B 1 37  LYS 37  56  56  LYS LYS B . n 
B 1 38  ARG 38  57  57  ARG ARG B . n 
B 1 39  GLU 39  58  58  GLU GLU B . n 
B 1 40  GLU 40  59  59  GLU GLU B . n 
B 1 41  VAL 41  60  60  VAL VAL B . n 
B 1 42  ILE 42  61  61  ILE ILE B . n 
B 1 43  GLY 43  62  62  GLY GLY B . n 
B 1 44  ASN 44  63  63  ASN ASN B . n 
B 1 45  ASN 45  64  64  ASN ASN B . n 
B 1 46  ILE 46  65  65  ILE ILE B . n 
B 1 47  ASP 47  66  66  ASP ASP B . n 
B 1 48  MET 48  67  67  MET MET B . n 
B 1 49  LEU 49  68  68  LEU LEU B . n 
B 1 50  ILE 50  69  69  ILE ILE B . n 
B 1 51  PRO 51  70  70  PRO PRO B . n 
B 1 52  ARG 52  71  71  ARG ARG B . n 
B 1 53  ASP 53  72  72  ASP ASP B . n 
B 1 54  LEU 54  73  73  LEU LEU B . n 
B 1 55  ARG 55  74  74  ARG ARG B . n 
B 1 56  PRO 56  75  75  PRO PRO B . n 
B 1 57  ALA 57  76  76  ALA ALA B . n 
B 1 58  HIS 58  77  77  HIS HIS B . n 
B 1 59  PRO 59  78  78  PRO PRO B . n 
B 1 60  GLU 60  79  79  GLU GLU B . n 
B 1 61  TYR 61  80  80  TYR TYR B . n 
B 1 62  ILE 62  81  81  ILE ILE B . n 
B 1 63  ARG 63  82  82  ARG ARG B . n 
B 1 64  HIS 64  83  83  HIS HIS B . n 
B 1 65  ASN 65  84  84  ASN ASN B . n 
B 1 66  ARG 66  85  85  ARG ARG B . n 
B 1 67  GLU 67  86  86  GLU GLU B . n 
B 1 68  GLY 68  87  87  GLY GLY B . n 
B 1 69  GLY 69  88  88  GLY GLY B . n 
B 1 70  LYS 70  89  89  LYS LYS B . n 
B 1 71  ALA 71  90  90  ALA ALA B . n 
B 1 72  ARG 72  91  91  ARG ARG B . n 
B 1 73  VAL 73  92  92  VAL VAL B . n 
B 1 74  GLU 74  93  93  GLU GLU B . n 
B 1 75  GLY 75  94  94  GLY GLY B . n 
B 1 76  MET 76  95  95  MET MET B . n 
B 1 77  SER 77  96  96  SER SER B . n 
B 1 78  ALA 78  97  97  ALA ALA B . n 
B 1 79  GLU 79  98  98  GLU GLU B . n 
B 1 80  LEU 80  99  99  LEU LEU B . n 
B 1 81  GLN 81  100 100 GLN GLN B . n 
B 1 82  LEU 82  101 101 LEU LEU B . n 
B 1 83  GLU 83  102 102 GLU GLU B . n 
B 1 84  LYS 84  103 103 LYS LYS B . n 
B 1 85  LYS 85  104 104 LYS LYS B . n 
B 1 86  ASP 86  105 105 ASP ASP B . n 
B 1 87  GLY 87  106 106 GLY GLY B . n 
B 1 88  SER 88  107 107 SER SER B . n 
B 1 89  LYS 89  108 108 LYS LYS B . n 
B 1 90  ILE 90  109 109 ILE ILE B . n 
B 1 91  TRP 91  110 110 TRP TRP B . n 
B 1 92  THR 92  111 111 THR THR B . n 
B 1 93  ARG 93  112 112 ARG ARG B . n 
B 1 94  PHE 94  113 113 PHE PHE B . n 
B 1 95  ALA 95  114 114 ALA ALA B . n 
B 1 96  LEU 96  115 115 LEU LEU B . n 
B 1 97  SER 97  116 116 SER SER B . n 
B 1 98  LYS 98  117 117 LYS LYS B . n 
B 1 99  VAL 99  118 118 VAL VAL B . n 
B 1 100 SER 100 119 119 SER SER B . n 
B 1 101 ALA 101 120 120 ALA ALA B . n 
B 1 102 GLU 102 121 121 GLU GLU B . n 
B 1 103 GLY 103 122 122 GLY GLY B . n 
B 1 104 LYS 104 123 123 LYS LYS B . n 
B 1 105 VAL 105 124 124 VAL VAL B . n 
B 1 106 TYR 106 125 125 TYR TYR B . n 
B 1 107 TYR 107 126 126 TYR TYR B . n 
B 1 108 LEU 108 127 127 LEU LEU B . n 
B 1 109 ALA 109 128 128 ALA ALA B . n 
B 1 110 LEU 110 129 129 LEU LEU B . n 
B 1 111 VAL 111 130 130 VAL VAL B . n 
B 1 112 ARG 112 131 131 ARG ARG B . n 
B 1 113 ASP 113 132 132 ASP ASP B . n 
B 1 114 ALA 114 133 133 ALA ALA B . n 
B 1 115 SER 115 134 134 SER SER B . n 
B 1 116 VAL 116 135 135 VAL VAL B . n 
B 1 117 GLU 117 136 136 GLU GLU B . n 
B 1 118 MET 118 137 137 MET MET B . n 
B 1 119 ALA 119 138 138 ALA ALA B . n 
B 1 120 GLN 120 139 139 GLN GLN B . n 
B 1 121 LYS 121 140 140 LYS LYS B . n 
B 1 122 GLU 122 141 141 GLU GLU B . n 
B 1 123 GLN 123 142 142 GLN GLN B . n 
B 1 124 THR 124 143 143 THR THR B . n 
B 1 125 ARG 125 144 144 ARG ARG B . n 
B 1 126 GLN 126 145 145 GLN GLN B . n 
B 1 127 LEU 127 146 146 LEU LEU B . n 
B 1 128 ILE 128 147 147 ILE ILE B . n 
B 1 129 ILE 129 148 148 ILE ILE B . n 
B 1 130 ALA 130 149 149 ALA ALA B . n 
B 1 131 VAL 131 150 150 VAL VAL B . n 
B 1 132 ASP 132 151 151 ASP ASP B . n 
B 1 133 HIS 133 152 152 HIS HIS B . n 
B 1 134 LEU 134 153 153 LEU LEU B . n 
B 1 135 ASP 135 154 154 ASP ASP B . n 
B 1 136 ARG 136 155 155 ARG ARG B . n 
B 1 137 PRO 137 156 156 PRO PRO B . n 
B 1 138 VAL 138 157 157 VAL VAL B . n 
B 1 139 ILE 139 158 158 ILE ILE B . n 
B 1 140 VAL 140 159 159 VAL VAL B . n 
B 1 141 LEU 141 160 160 LEU LEU B . n 
B 1 142 ASP 142 161 161 ASP ASP B . n 
B 1 143 PRO 143 162 162 PRO PRO B . n 
B 1 144 GLU 144 163 163 GLU GLU B . n 
B 1 145 ARG 145 164 164 ARG ARG B . n 
B 1 146 HIS 146 165 165 HIS HIS B . n 
B 1 147 ILE 147 166 166 ILE ILE B . n 
B 1 148 VAL 148 167 167 VAL VAL B . n 
B 1 149 GLN 149 168 168 GLN GLN B . n 
B 1 150 CYS 150 169 169 CYS CYS B . n 
B 1 151 ASN 151 170 170 ASN ASN B . n 
B 1 152 ARG 152 171 171 ARG ARG B . n 
B 1 153 ALA 153 172 172 ALA ALA B . n 
B 1 154 PHE 154 173 173 PHE PHE B . n 
B 1 155 THR 155 174 174 THR THR B . n 
B 1 156 GLU 156 175 175 GLU GLU B . n 
B 1 157 MET 157 176 176 MET MET B . n 
B 1 158 PHE 158 177 177 PHE PHE B . n 
B 1 159 GLY 159 178 178 GLY GLY B . n 
B 1 160 TYR 160 179 179 TYR TYR B . n 
B 1 161 CYS 161 180 180 CYS CYS B . n 
B 1 162 ILE 162 181 181 ILE ILE B . n 
B 1 163 SER 163 182 182 SER SER B . n 
B 1 164 GLU 164 183 183 GLU GLU B . n 
B 1 165 ALA 165 184 184 ALA ALA B . n 
B 1 166 SER 166 185 185 SER SER B . n 
B 1 167 GLY 167 186 186 GLY GLY B . n 
B 1 168 MET 168 187 187 MET MET B . n 
B 1 169 GLN 169 188 188 GLN GLN B . n 
B 1 170 PRO 170 189 189 PRO PRO B . n 
B 1 171 ASP 171 190 190 ASP ASP B . n 
B 1 172 THR 172 191 191 THR THR B . n 
B 1 173 LEU 173 192 192 LEU LEU B . n 
B 1 174 LEU 174 193 193 LEU LEU B . n 
B 1 175 ASN 175 194 194 ASN ASN B . n 
B 1 176 THR 176 195 195 THR THR B . n 
B 1 177 PRO 177 196 196 PRO PRO B . n 
B 1 178 GLU 178 197 197 GLU GLU B . n 
B 1 179 PHE 179 198 198 PHE PHE B . n 
B 1 180 PRO 180 199 199 PRO PRO B . n 
B 1 181 ALA 181 200 200 ALA ALA B . n 
B 1 182 ASP 182 201 201 ASP ASP B . n 
B 1 183 ASN 183 202 202 ASN ASN B . n 
B 1 184 ARG 184 203 203 ARG ARG B . n 
B 1 185 ILE 185 204 204 ILE ILE B . n 
B 1 186 ARG 186 205 205 ARG ARG B . n 
B 1 187 LEU 187 206 206 LEU LEU B . n 
B 1 188 GLN 188 207 207 GLN GLN B . n 
B 1 189 GLN 189 208 208 GLN GLN B . n 
B 1 190 LEU 190 209 209 LEU LEU B . n 
B 1 191 LEU 191 210 210 LEU LEU B . n 
B 1 192 TRP 192 211 211 TRP TRP B . n 
B 1 193 LYS 193 212 212 LYS LYS B . n 
B 1 194 THR 194 213 213 THR THR B . n 
B 1 195 ALA 195 214 214 ALA ALA B . n 
B 1 196 ARG 196 215 215 ARG ARG B . n 
B 1 197 ASP 197 216 216 ASP ASP B . n 
B 1 198 GLN 198 217 217 GLN GLN B . n 
B 1 199 ASP 199 218 218 ASP ASP B . n 
B 1 200 GLU 200 219 219 GLU GLU B . n 
B 1 201 PHE 201 220 220 PHE PHE B . n 
B 1 202 LEU 202 221 221 LEU LEU B . n 
B 1 203 LEU 203 222 222 LEU LEU B . n 
B 1 204 LEU 204 223 223 LEU LEU B . n 
B 1 205 THR 205 224 224 THR THR B . n 
B 1 206 ARG 206 225 225 ARG ARG B . n 
B 1 207 THR 207 226 226 THR THR B . n 
B 1 208 GLY 208 227 227 GLY GLY B . n 
B 1 209 GLU 209 228 228 GLU GLU B . n 
B 1 210 LYS 210 229 229 LYS LYS B . n 
B 1 211 ILE 211 230 230 ILE ILE B . n 
B 1 212 TRP 212 231 231 TRP TRP B . n 
B 1 213 ILE 213 232 232 ILE ILE B . n 
B 1 214 LYS 214 233 233 LYS LYS B . n 
B 1 215 ALA 215 234 234 ALA ALA B . n 
B 1 216 SER 216 235 235 SER SER B . n 
B 1 217 ILE 217 236 236 ILE ILE B . n 
B 1 218 SER 218 237 237 SER SER B . n 
B 1 219 PRO 219 238 238 PRO PRO B . n 
B 1 220 VAL 220 239 239 VAL VAL B . n 
B 1 221 TYR 221 240 240 TYR TYR B . n 
B 1 222 ASP 222 241 241 ASP ASP B . n 
B 1 223 VAL 223 242 242 VAL VAL B . n 
B 1 224 LEU 224 243 243 LEU LEU B . n 
B 1 225 ALA 225 244 244 ALA ALA B . n 
B 1 226 HIS 226 245 245 HIS HIS B . n 
B 1 227 LEU 227 246 246 LEU LEU B . n 
B 1 228 GLN 228 247 247 GLN GLN B . n 
B 1 229 ASN 229 248 248 ASN ASN B . n 
B 1 230 LEU 230 249 249 LEU LEU B . n 
B 1 231 VAL 231 250 250 VAL VAL B . n 
B 1 232 MET 232 251 251 MET MET B . n 
B 1 233 THR 233 252 252 THR THR B . n 
B 1 234 PHE 234 253 253 PHE PHE B . n 
B 1 235 SER 235 254 254 SER SER B . n 
B 1 236 ASP 236 255 255 ASP ASP B . n 
B 1 237 ILE 237 256 256 ILE ILE B . n 
B 1 238 THR 238 257 257 THR THR B . n 
B 1 239 GLU 239 258 258 GLU GLU B . n 
B 1 240 GLU 240 259 259 GLU GLU B . n 
B 1 241 ARG 241 260 260 ARG ARG B . n 
B 1 242 GLN 242 261 261 GLN GLN B . n 
B 1 243 ILE 243 262 262 ILE ILE B . n 
B 1 244 ARG 244 263 263 ARG ARG B . n 
B 1 245 GLN 245 264 264 GLN GLN B . n 
B 1 246 LEU 246 265 265 LEU LEU B . n 
B 1 247 GLU 247 266 266 GLU GLU B . n 
B 1 248 GLY 248 267 267 GLY GLY B . n 
B 1 249 ASN 249 268 268 ASN ASN B . n 
B 1 250 ILE 250 269 269 ILE ILE B . n 
B 1 251 LEU 251 270 270 LEU LEU B . n 
B 1 252 ALA 252 271 271 ALA ALA B . n 
B 1 253 ALA 253 272 272 ALA ALA B . n 
B 1 254 MET 254 273 273 MET MET B . n 
B 1 255 CYS 255 274 274 CYS CYS B . n 
B 1 256 SER 256 275 275 SER SER B . n 
B 1 257 SER 257 276 276 SER SER B . n 
B 1 258 PRO 258 277 277 PRO PRO B . n 
B 1 259 PRO 259 278 278 PRO PRO B . n 
B 1 260 PHE 260 279 279 PHE PHE B . n 
B 1 261 HIS 261 280 280 HIS HIS B . n 
B 1 262 GLU 262 281 281 GLU GLU B . n 
B 1 263 MET 263 282 282 MET MET B . n 
B 1 264 GLY 264 283 283 GLY GLY B . n 
B 1 265 GLU 265 284 284 GLU GLU B . n 
B 1 266 ILE 266 285 285 ILE ILE B . n 
B 1 267 ILE 267 286 286 ILE ILE B . n 
B 1 268 CYS 268 287 287 CYS CYS B . n 
B 1 269 ARG 269 288 288 ARG ARG B . n 
B 1 270 ASN 270 289 289 ASN ASN B . n 
B 1 271 ILE 271 290 290 ILE ILE B . n 
B 1 272 GLU 272 291 291 GLU GLU B . n 
B 1 273 SER 273 292 292 SER SER B . n 
B 1 274 VAL 274 293 293 VAL VAL B . n 
B 1 275 LEU 275 294 294 LEU LEU B . n 
B 1 276 ASN 276 295 295 ASN ASN B . n 
B 1 277 GLU 277 296 296 GLU GLU B . n 
B 1 278 SER 278 297 297 SER SER B . n 
B 1 279 HIS 279 298 298 HIS HIS B . n 
B 1 280 VAL 280 299 299 VAL VAL B . n 
B 1 281 SER 281 300 300 SER SER B . n 
B 1 282 LEU 282 301 301 LEU LEU B . n 
B 1 283 PHE 283 302 302 PHE PHE B . n 
B 1 284 ALA 284 303 303 ALA ALA B . n 
B 1 285 LEU 285 304 304 LEU LEU B . n 
B 1 286 ARG 286 305 305 ARG ARG B . n 
B 1 287 ASN 287 306 306 ASN ASN B . n 
B 1 288 GLY 288 307 307 GLY GLY B . n 
B 1 289 MET 289 308 308 MET MET B . n 
B 1 290 PRO 290 309 309 PRO PRO B . n 
B 1 291 ILE 291 310 310 ILE ILE B . n 
B 1 292 HIS 292 311 311 HIS HIS B . n 
B 1 293 TRP 293 312 312 TRP TRP B . n 
B 1 294 ALA 294 313 313 ALA ALA B . n 
B 1 295 SER 295 314 314 SER SER B . n 
B 1 296 SER 296 315 315 SER SER B . n 
B 1 297 SER 297 316 316 SER SER B . n 
B 1 298 HIS 298 317 317 HIS HIS B . n 
B 1 299 GLY 299 318 318 GLY GLY B . n 
B 1 300 ALA 300 319 319 ALA ALA B . n 
B 1 301 GLU 301 320 320 GLU GLU B . n 
B 1 302 ILE 302 321 321 ILE ILE B . n 
B 1 303 GLN 303 322 322 GLN GLN B . n 
B 1 304 ASN 304 323 323 ASN ASN B . n 
B 1 305 ALA 305 324 324 ALA ALA B . n 
B 1 306 GLN 306 325 325 GLN GLN B . n 
B 1 307 SER 307 326 326 SER SER B . n 
B 1 308 TRP 308 327 327 TRP TRP B . n 
B 1 309 SER 309 328 328 SER SER B . n 
B 1 310 ALA 310 329 329 ALA ALA B . n 
B 1 311 THR 311 330 330 THR THR B . n 
B 1 312 ILE 312 331 331 ILE ILE B . n 
B 1 313 ARG 313 332 332 ARG ARG B . n 
B 1 314 GLN 314 333 333 GLN GLN B . n 
B 1 315 ARG 315 334 334 ARG ARG B . n 
B 1 316 ASP 316 335 335 ASP ASP B . n 
B 1 317 GLY 317 336 336 GLY GLY B . n 
B 1 318 ALA 318 337 337 ALA ALA B . n 
B 1 319 PRO 319 338 338 PRO PRO B . n 
B 1 320 ALA 320 339 339 ALA ALA B . n 
B 1 321 GLY 321 340 340 GLY GLY B . n 
B 1 322 ILE 322 341 341 ILE ILE B . n 
B 1 323 LEU 323 342 342 LEU LEU B . n 
B 1 324 GLN 324 343 343 GLN GLN B . n 
B 1 325 ILE 325 344 344 ILE ILE B . n 
B 1 326 LYS 326 345 345 LYS LYS B . n 
B 1 327 THR 327 346 346 THR THR B . n 
B 1 328 SER 328 347 347 SER SER B . n 
B 1 329 SER 329 348 348 SER SER B . n 
B 1 330 GLY 330 349 349 GLY GLY B . n 
B 1 331 ALA 331 350 350 ALA ALA B . n 
B 1 332 GLU 332 351 351 GLU GLU B . n 
B 1 333 THR 333 352 352 THR THR B . n 
B 1 334 SER 334 353 353 SER SER B . n 
B 1 335 ALA 335 354 354 ALA ALA B . n 
B 1 336 PHE 336 355 355 PHE PHE B . n 
B 1 337 ILE 337 356 356 ILE ILE B . n 
B 1 338 GLU 338 357 357 GLU GLU B . n 
B 1 339 ARG 339 358 358 ARG ARG B . n 
B 1 340 VAL 340 359 359 VAL VAL B . n 
B 1 341 ALA 341 360 360 ALA ALA B . n 
B 1 342 ASP 342 361 361 ASP ASP B . n 
B 1 343 ILE 343 362 362 ILE ILE B . n 
B 1 344 SER 344 363 363 SER SER B . n 
B 1 345 GLN 345 364 364 GLN GLN B . n 
B 1 346 HIS 346 365 365 HIS HIS B . n 
B 1 347 MET 347 366 366 MET MET B . n 
B 1 348 ALA 348 367 367 ALA ALA B . n 
B 1 349 ALA 349 368 368 ALA ALA B . n 
B 1 350 LEU 350 369 369 LEU LEU B . n 
B 1 351 ALA 351 370 370 ALA ALA B . n 
B 1 352 LEU 352 371 371 LEU LEU B . n 
B 1 353 GLU 353 372 372 GLU GLU B . n 
B 1 354 GLN 354 373 373 GLN GLN B . n 
B 1 355 GLU 355 374 374 GLU GLU B . n 
B 1 356 LYS 356 375 375 LYS LYS B . n 
B 1 357 SER 357 376 376 SER SER B . n 
B 1 358 ARG 358 377 377 ARG ARG B . n 
B 1 359 GLN 359 378 378 GLN GLN B . n 
B 1 360 HIS 360 379 379 HIS HIS B . n 
B 1 361 ILE 361 380 380 ILE ILE B . n 
B 1 362 GLU 362 381 381 GLU GLU B . n 
B 1 363 GLN 363 382 382 GLN GLN B . n 
B 1 364 LEU 364 383 383 LEU LEU B . n 
B 1 365 ILE 365 384 384 ILE ILE B . n 
B 1 366 GLN 366 385 385 GLN GLN B . n 
B 1 367 PHE 367 386 386 PHE PHE B . n 
B 1 368 ASP 368 387 387 ASP ASP B . n 
B 1 369 PRO 369 388 388 PRO PRO B . n 
B 1 370 MET 370 389 389 MET MET B . n 
B 1 371 THR 371 390 390 THR THR B . n 
B 1 372 GLY 372 391 391 GLY GLY B . n 
B 1 373 LEU 373 392 392 LEU LEU B . n 
B 1 374 PRO 374 393 393 PRO PRO B . n 
B 1 375 ASN 375 394 394 ASN ASN B . n 
B 1 376 ARG 376 395 395 ARG ARG B . n 
B 1 377 ASN 377 396 396 ASN ASN B . n 
B 1 378 ASN 378 397 397 ASN ASN B . n 
B 1 379 LEU 379 398 398 LEU LEU B . n 
B 1 380 HIS 380 399 399 HIS HIS B . n 
B 1 381 ASN 381 400 400 ASN ASN B . n 
B 1 382 TYR 382 401 401 TYR TYR B . n 
B 1 383 LEU 383 402 402 LEU LEU B . n 
B 1 384 ASP 384 403 403 ASP ASP B . n 
B 1 385 ASP 385 404 404 ASP ASP B . n 
B 1 386 LEU 386 405 405 LEU LEU B . n 
B 1 387 VAL 387 406 406 VAL VAL B . n 
B 1 388 ASP 388 407 407 ASP ASP B . n 
B 1 389 LYS 389 408 408 LYS LYS B . n 
B 1 390 ALA 390 409 409 ALA ALA B . n 
B 1 391 VAL 391 410 410 VAL VAL B . n 
B 1 392 SER 392 411 411 SER SER B . n 
B 1 393 PRO 393 412 412 PRO PRO B . n 
B 1 394 VAL 394 413 413 VAL VAL B . n 
B 1 395 VAL 395 414 414 VAL VAL B . n 
B 1 396 TYR 396 415 415 TYR TYR B . n 
B 1 397 LEU 397 416 416 LEU LEU B . n 
B 1 398 ILE 398 417 417 ILE ILE B . n 
B 1 399 GLY 399 418 418 GLY GLY B . n 
B 1 400 VAL 400 419 419 VAL VAL B . n 
B 1 401 ASP 401 420 420 ASP ASP B . n 
B 1 402 HIS 402 421 421 HIS HIS B . n 
B 1 403 ILE 403 422 422 ILE ILE B . n 
B 1 404 GLN 404 423 423 GLN GLN B . n 
B 1 405 ASP 405 424 424 ASP ASP B . n 
B 1 406 VAL 406 425 425 VAL VAL B . n 
B 1 407 ILE 407 426 426 ILE ILE B . n 
B 1 408 ASP 408 427 427 ASP ASP B . n 
B 1 409 SER 409 428 428 SER SER B . n 
B 1 410 LEU 410 429 429 LEU LEU B . n 
B 1 411 GLY 411 430 430 GLY GLY B . n 
B 1 412 TYR 412 431 431 TYR TYR B . n 
B 1 413 ALA 413 432 432 ALA ALA B . n 
B 1 414 TRP 414 433 433 TRP TRP B . n 
B 1 415 ALA 415 434 434 ALA ALA B . n 
B 1 416 ASP 416 435 435 ASP ASP B . n 
B 1 417 GLN 417 436 436 GLN GLN B . n 
B 1 418 ALA 418 437 437 ALA ALA B . n 
B 1 419 LEU 419 438 438 LEU LEU B . n 
B 1 420 LEU 420 439 439 LEU LEU B . n 
B 1 421 GLU 421 440 440 GLU GLU B . n 
B 1 422 VAL 422 441 441 VAL VAL B . n 
B 1 423 VAL 423 442 442 VAL VAL B . n 
B 1 424 ASN 424 443 443 ASN ASN B . n 
B 1 425 ARG 425 444 444 ARG ARG B . n 
B 1 426 PHE 426 445 445 PHE PHE B . n 
B 1 427 ARG 427 446 446 ARG ARG B . n 
B 1 428 GLU 428 447 447 GLU GLU B . n 
B 1 429 LYS 429 448 448 LYS LYS B . n 
B 1 430 LEU 430 449 449 LEU LEU B . n 
B 1 431 LYS 431 450 450 LYS LYS B . n 
B 1 432 PRO 432 451 451 PRO PRO B . n 
B 1 433 ASP 433 452 452 ASP ASP B . n 
B 1 434 GLN 434 453 453 GLN GLN B . n 
B 1 435 TYR 435 454 454 TYR TYR B . n 
B 1 436 LEU 436 455 455 LEU LEU B . n 
B 1 437 CYS 437 456 456 CYS CYS B . n 
B 1 438 ARG 438 457 457 ARG ARG B . n 
B 1 439 ILE 439 458 458 ILE ILE B . n 
B 1 440 GLU 440 459 459 GLU GLU B . n 
B 1 441 GLY 441 460 460 GLY GLY B . n 
B 1 442 THR 442 461 461 THR THR B . n 
B 1 443 GLN 443 462 462 GLN GLN B . n 
B 1 444 PHE 444 463 463 PHE PHE B . n 
B 1 445 VAL 445 464 464 VAL VAL B . n 
B 1 446 LEU 446 465 465 LEU LEU B . n 
B 1 447 VAL 447 466 466 VAL VAL B . n 
B 1 448 SER 448 467 467 SER SER B . n 
B 1 449 LEU 449 468 468 LEU LEU B . n 
B 1 450 GLU 450 469 469 GLU GLU B . n 
B 1 451 ASN 451 470 470 ASN ASN B . n 
B 1 452 ASP 452 471 471 ASP ASP B . n 
B 1 453 VAL 453 472 472 VAL VAL B . n 
B 1 454 SER 454 473 473 SER SER B . n 
B 1 455 ASN 455 474 474 ASN ASN B . n 
B 1 456 ILE 456 475 475 ILE ILE B . n 
B 1 457 THR 457 476 476 THR THR B . n 
B 1 458 GLN 458 477 477 GLN GLN B . n 
B 1 459 ILE 459 478 478 ILE ILE B . n 
B 1 460 ALA 460 479 479 ALA ALA B . n 
B 1 461 ASP 461 480 480 ASP ASP B . n 
B 1 462 GLU 462 481 481 GLU GLU B . n 
B 1 463 LEU 463 482 482 LEU LEU B . n 
B 1 464 ARG 464 483 483 ARG ARG B . n 
B 1 465 ASN 465 484 484 ASN ASN B . n 
B 1 466 VAL 466 485 485 VAL VAL B . n 
B 1 467 VAL 467 486 486 VAL VAL B . n 
B 1 468 SER 468 487 487 SER SER B . n 
B 1 469 LYS 469 488 488 LYS LYS B . n 
B 1 470 PRO 470 489 489 PRO PRO B . n 
B 1 471 ILE 471 490 490 ILE ILE B . n 
B 1 472 MET 472 491 491 MET MET B . n 
B 1 473 ILE 473 492 492 ILE ILE B . n 
B 1 474 ASP 474 493 493 ASP ASP B . n 
B 1 475 ASP 475 494 494 ASP ASP B . n 
B 1 476 LYS 476 495 495 LYS LYS B . n 
B 1 477 PRO 477 496 496 PRO PRO B . n 
B 1 478 PHE 478 497 497 PHE PHE B . n 
B 1 479 PRO 479 498 498 PRO PRO B . n 
B 1 480 LEU 480 499 499 LEU LEU B . n 
B 1 481 THR 481 500 500 THR THR B . n 
B 1 482 LEU 482 501 501 LEU LEU B . n 
B 1 483 SER 483 502 502 SER SER B . n 
B 1 484 ILE 484 503 503 ILE ILE B . n 
B 1 485 GLY 485 504 504 GLY GLY B . n 
B 1 486 ILE 486 505 505 ILE ILE B . n 
B 1 487 SER 487 506 506 SER SER B . n 
B 1 488 TYR 488 507 507 TYR TYR B . n 
B 1 489 ASP 489 508 508 ASP ASP B . n 
B 1 490 LEU 490 509 509 LEU LEU B . n 
B 1 491 GLY 491 510 510 GLY GLY B . n 
B 1 492 LYS 492 511 511 LYS LYS B . n 
B 1 493 ASN 493 512 512 ASN ASN B . n 
B 1 494 ARG 494 513 513 ARG ARG B . n 
B 1 495 ASP 495 514 514 ASP ASP B . n 
B 1 496 TYR 496 515 515 TYR TYR B . n 
B 1 497 LEU 497 516 516 LEU LEU B . n 
B 1 498 LEU 498 517 517 LEU LEU B . n 
B 1 499 SER 499 518 518 SER SER B . n 
B 1 500 THR 500 519 519 THR THR B . n 
B 1 501 ALA 501 520 520 ALA ALA B . n 
B 1 502 HIS 502 521 521 HIS HIS B . n 
B 1 503 ASN 503 522 522 ASN ASN B . n 
B 1 504 ALA 504 523 523 ALA ALA B . n 
B 1 505 MET 505 524 524 MET MET B . n 
B 1 506 ASP 506 525 525 ASP ASP B . n 
B 1 507 TYR 507 526 526 TYR TYR B . n 
B 1 508 ILE 508 527 527 ILE ILE B . n 
B 1 509 ARG 509 528 528 ARG ARG B . n 
B 1 510 LYS 510 529 529 LYS LYS B . n 
B 1 511 ASN 511 530 530 ASN ASN B . n 
B 1 512 GLY 512 531 531 GLY GLY B . n 
B 1 513 GLY 513 532 532 GLY GLY B . n 
B 1 514 ASN 514 533 533 ASN ASN B . n 
B 1 515 GLY 515 534 534 GLY GLY B . n 
B 1 516 TRP 516 535 535 TRP TRP B . n 
B 1 517 GLN 517 536 536 GLN GLN B . n 
B 1 518 PHE 518 537 537 PHE PHE B . n 
B 1 519 PHE 519 538 538 PHE PHE B . n 
B 1 520 SER 520 539 539 SER SER B . n 
B 1 521 PRO 521 540 540 PRO PRO B . n 
B 1 522 ALA 522 541 541 ALA ALA B . n 
B 1 523 MET 523 542 542 MET MET B . n 
B 1 524 ASN 524 543 543 ASN ASN B . n 
B 1 525 GLU 525 544 544 GLU GLU B . n 
B 1 526 MET 526 545 545 MET MET B . n 
B 1 527 VAL 527 546 546 VAL VAL B . n 
B 1 528 LYS 528 547 547 LYS LYS B . n 
B 1 529 GLU 529 548 548 GLU GLU B . n 
B 1 530 ARG 530 549 549 ARG ARG B . n 
B 1 531 LEU 531 550 550 LEU LEU B . n 
B 1 532 VAL 532 551 551 VAL VAL B . n 
B 1 533 LEU 533 552 552 LEU LEU B . n 
B 1 534 GLY 534 553 553 GLY GLY B . n 
B 1 535 ALA 535 554 554 ALA ALA B . n 
B 1 536 ALA 536 555 555 ALA ALA B . n 
B 1 537 LEU 537 556 556 LEU LEU B . n 
B 1 538 LYS 538 557 557 LYS LYS B . n 
B 1 539 GLU 539 558 558 GLU GLU B . n 
B 1 540 ALA 540 559 559 ALA ALA B . n 
B 1 541 ILE 541 560 560 ILE ILE B . n 
B 1 542 SER 542 561 561 SER SER B . n 
B 1 543 ASN 543 562 562 ASN ASN B . n 
B 1 544 ASN 544 563 563 ASN ASN B . n 
B 1 545 GLN 545 564 564 GLN GLN B . n 
B 1 546 LEU 546 565 565 LEU LEU B . n 
B 1 547 LYS 547 566 566 LYS LYS B . n 
B 1 548 LEU 548 567 567 LEU LEU B . n 
B 1 549 VAL 549 568 568 VAL VAL B . n 
B 1 550 TYR 550 569 569 TYR TYR B . n 
B 1 551 GLN 551 570 570 GLN GLN B . n 
B 1 552 PRO 552 571 571 PRO PRO B . n 
B 1 553 GLN 553 572 572 GLN GLN B . n 
B 1 554 ILE 554 573 573 ILE ILE B . n 
B 1 555 PHE 555 574 574 PHE PHE B . n 
B 1 556 ALA 556 575 575 ALA ALA B . n 
B 1 557 GLU 557 576 576 GLU GLU B . n 
B 1 558 THR 558 577 577 THR THR B . n 
B 1 559 GLY 559 578 578 GLY GLY B . n 
B 1 560 GLU 560 579 579 GLU GLU B . n 
B 1 561 LEU 561 580 580 LEU LEU B . n 
B 1 562 TYR 562 581 581 TYR TYR B . n 
B 1 563 GLY 563 582 582 GLY GLY B . n 
B 1 564 ILE 564 583 583 ILE ILE B . n 
B 1 565 GLU 565 584 584 GLU GLU B . n 
B 1 566 ALA 566 585 585 ALA ALA B . n 
B 1 567 LEU 567 586 586 LEU LEU B . n 
B 1 568 ALA 568 587 587 ALA ALA B . n 
B 1 569 ARG 569 588 588 ARG ARG B . n 
B 1 570 TRP 570 589 589 TRP TRP B . n 
B 1 571 HIS 571 590 590 HIS HIS B . n 
B 1 572 ASP 572 591 591 ASP ASP B . n 
B 1 573 PRO 573 592 592 PRO PRO B . n 
B 1 574 LEU 574 593 593 LEU LEU B . n 
B 1 575 HIS 575 594 594 HIS HIS B . n 
B 1 576 GLY 576 595 595 GLY GLY B . n 
B 1 577 HIS 577 596 596 HIS HIS B . n 
B 1 578 VAL 578 597 597 VAL VAL B . n 
B 1 579 PRO 579 598 598 PRO PRO B . n 
B 1 580 PRO 580 599 599 PRO PRO B . n 
B 1 581 SER 581 600 600 SER SER B . n 
B 1 582 ARG 582 601 601 ARG ARG B . n 
B 1 583 PHE 583 602 602 PHE PHE B . n 
B 1 584 ILE 584 603 603 ILE ILE B . n 
B 1 585 PRO 585 604 604 PRO PRO B . n 
B 1 586 LEU 586 605 605 LEU LEU B . n 
B 1 587 ALA 587 606 606 ALA ALA B . n 
B 1 588 GLU 588 607 607 GLU GLU B . n 
B 1 589 GLU 589 608 608 GLU GLU B . n 
B 1 590 ILE 590 609 609 ILE ILE B . n 
B 1 591 GLY 591 610 610 GLY GLY B . n 
B 1 592 GLU 592 611 611 GLU GLU B . n 
B 1 593 ILE 593 612 612 ILE ILE B . n 
B 1 594 GLU 594 613 613 GLU GLU B . n 
B 1 595 ASN 595 614 614 ASN ASN B . n 
B 1 596 ILE 596 615 615 ILE ILE B . n 
B 1 597 GLY 597 616 616 GLY GLY B . n 
B 1 598 ARG 598 617 617 ARG ARG B . n 
B 1 599 TRP 599 618 618 TRP TRP B . n 
B 1 600 VAL 600 619 619 VAL VAL B . n 
B 1 601 ILE 601 620 620 ILE ILE B . n 
B 1 602 ALA 602 621 621 ALA ALA B . n 
B 1 603 GLU 603 622 622 GLU GLU B . n 
B 1 604 ALA 604 623 623 ALA ALA B . n 
B 1 605 CYS 605 624 624 CYS CYS B . n 
B 1 606 ARG 606 625 625 ARG ARG B . n 
B 1 607 GLN 607 626 626 GLN GLN B . n 
B 1 608 LEU 608 627 627 LEU LEU B . n 
B 1 609 ALA 609 628 628 ALA ALA B . n 
B 1 610 GLU 610 629 629 GLU GLU B . n 
B 1 611 TRP 611 630 630 TRP TRP B . n 
B 1 612 ARG 612 631 631 ARG ARG B . n 
B 1 613 SER 613 632 632 SER SER B . n 
B 1 614 GLN 614 633 633 GLN GLN B . n 
B 1 615 ASN 615 634 634 ASN ASN B . n 
B 1 616 ILE 616 635 635 ILE ILE B . n 
B 1 617 HIS 617 636 636 HIS HIS B . n 
B 1 618 ILE 618 637 637 ILE ILE B . n 
B 1 619 PRO 619 638 638 PRO PRO B . n 
B 1 620 ALA 620 639 639 ALA ALA B . n 
B 1 621 LEU 621 640 640 LEU LEU B . n 
B 1 622 SER 622 641 641 SER SER B . n 
B 1 623 VAL 623 642 642 VAL VAL B . n 
B 1 624 ASN 624 643 643 ASN ASN B . n 
B 1 625 LEU 625 644 644 LEU LEU B . n 
B 1 626 SER 626 645 645 SER SER B . n 
B 1 627 ALA 627 646 646 ALA ALA B . n 
B 1 628 LEU 628 647 647 LEU LEU B . n 
B 1 629 HIS 629 648 648 HIS HIS B . n 
B 1 630 PHE 630 649 649 PHE PHE B . n 
B 1 631 ARG 631 650 650 ARG ARG B . n 
B 1 632 SER 632 651 651 SER SER B . n 
B 1 633 ASN 633 652 652 ASN ASN B . n 
B 1 634 GLN 634 653 653 GLN GLN B . n 
B 1 635 LEU 635 654 654 LEU LEU B . n 
B 1 636 PRO 636 655 655 PRO PRO B . n 
B 1 637 ASN 637 656 656 ASN ASN B . n 
B 1 638 GLN 638 657 657 GLN GLN B . n 
B 1 639 VAL 639 658 658 VAL VAL B . n 
B 1 640 SER 640 659 659 SER SER B . n 
B 1 641 ASP 641 660 660 ASP ASP B . n 
B 1 642 ALA 642 661 661 ALA ALA B . n 
B 1 643 MET 643 662 662 MET MET B . n 
B 1 644 HIS 644 663 663 HIS HIS B . n 
B 1 645 ALA 645 664 664 ALA ALA B . n 
B 1 646 TRP 646 665 665 TRP TRP B . n 
B 1 647 GLY 647 666 666 GLY GLY B . n 
B 1 648 ILE 648 667 667 ILE ILE B . n 
B 1 649 ASP 649 668 668 ASP ASP B . n 
B 1 650 GLY 650 669 669 GLY GLY B . n 
B 1 651 HIS 651 670 670 HIS HIS B . n 
B 1 652 GLN 652 671 671 GLN GLN B . n 
B 1 653 LEU 653 672 672 LEU LEU B . n 
B 1 654 THR 654 673 673 THR THR B . n 
B 1 655 VAL 655 674 674 VAL VAL B . n 
B 1 656 GLU 656 675 675 GLU GLU B . n 
B 1 657 ILE 657 676 676 ILE ILE B . n 
B 1 658 THR 658 677 677 THR THR B . n 
B 1 659 GLU 659 678 678 GLU GLU B . n 
B 1 660 SER 660 679 679 SER SER B . n 
B 1 661 MET 661 680 680 MET MET B . n 
B 1 662 MET 662 681 681 MET MET B . n 
B 1 663 MET 663 682 682 MET MET B . n 
B 1 664 GLU 664 683 683 GLU GLU B . n 
B 1 665 HIS 665 684 684 HIS HIS B . n 
B 1 666 ASP 666 685 685 ASP ASP B . n 
B 1 667 THR 667 686 686 THR THR B . n 
B 1 668 GLU 668 687 687 GLU GLU B . n 
B 1 669 ILE 669 688 688 ILE ILE B . n 
B 1 670 PHE 670 689 689 PHE PHE B . n 
B 1 671 LYS 671 690 690 LYS LYS B . n 
B 1 672 ARG 672 691 691 ARG ARG B . n 
B 1 673 ILE 673 692 692 ILE ILE B . n 
B 1 674 GLN 674 693 693 GLN GLN B . n 
B 1 675 ILE 675 694 694 ILE ILE B . n 
B 1 676 LEU 676 695 695 LEU LEU B . n 
B 1 677 ARG 677 696 696 ARG ARG B . n 
B 1 678 ASP 678 697 697 ASP ASP B . n 
B 1 679 MET 679 698 698 MET MET B . n 
B 1 680 GLY 680 699 699 GLY GLY B . n 
B 1 681 VAL 681 700 700 VAL VAL B . n 
B 1 682 GLY 682 701 701 GLY GLY B . n 
B 1 683 LEU 683 702 702 LEU LEU B . n 
B 1 684 SER 684 703 703 SER SER B . n 
B 1 685 VAL 685 704 704 VAL VAL B . n 
B 1 686 ASP 686 705 705 ASP ASP B . n 
B 1 687 ASP 687 706 706 ASP ASP B . n 
B 1 688 PHE 688 707 707 PHE PHE B . n 
B 1 689 GLY 689 708 708 GLY GLY B . n 
B 1 690 THR 690 709 709 THR THR B . n 
B 1 691 GLY 691 710 710 GLY GLY B . n 
B 1 692 PHE 692 711 711 PHE PHE B . n 
B 1 693 SER 693 712 712 SER SER B . n 
B 1 694 GLY 694 713 713 GLY GLY B . n 
B 1 695 LEU 695 714 714 LEU LEU B . n 
B 1 696 SER 696 715 715 SER SER B . n 
B 1 697 ARG 697 716 716 ARG ARG B . n 
B 1 698 LEU 698 717 717 LEU LEU B . n 
B 1 699 VAL 699 718 718 VAL VAL B . n 
B 1 700 SER 700 719 719 SER SER B . n 
B 1 701 LEU 701 720 720 LEU LEU B . n 
B 1 702 PRO 702 721 721 PRO PRO B . n 
B 1 703 VAL 703 722 722 VAL VAL B . n 
B 1 704 THR 704 723 723 THR THR B . n 
B 1 705 GLU 705 724 724 GLU GLU B . n 
B 1 706 ILE 706 725 725 ILE ILE B . n 
B 1 707 LYS 707 726 726 LYS LYS B . n 
B 1 708 ILE 708 727 727 ILE ILE B . n 
B 1 709 ASP 709 728 728 ASP ASP B . n 
B 1 710 LYS 710 729 729 LYS LYS B . n 
B 1 711 SER 711 730 730 SER SER B . n 
B 1 712 PHE 712 731 731 PHE PHE B . n 
B 1 713 VAL 713 732 732 VAL VAL B . n 
B 1 714 ASP 714 733 733 ASP ASP B . n 
B 1 715 ARG 715 734 734 ARG ARG B . n 
B 1 716 CYS 716 735 735 CYS CYS B . n 
B 1 717 LEU 717 736 736 LEU LEU B . n 
B 1 718 THR 718 737 737 THR THR B . n 
B 1 719 GLU 719 738 738 GLU GLU B . n 
B 1 720 LYS 720 739 739 LYS LYS B . n 
B 1 721 ARG 721 740 740 ARG ARG B . n 
B 1 722 ILE 722 741 741 ILE ILE B . n 
B 1 723 LEU 723 742 742 LEU LEU B . n 
B 1 724 ALA 724 743 743 ALA ALA B . n 
B 1 725 LEU 725 744 744 LEU LEU B . n 
B 1 726 LEU 726 745 745 LEU LEU B . n 
B 1 727 GLU 727 746 746 GLU GLU B . n 
B 1 728 ALA 728 747 747 ALA ALA B . n 
B 1 729 ILE 729 748 748 ILE ILE B . n 
B 1 730 THR 730 749 749 THR THR B . n 
B 1 731 SER 731 750 750 SER SER B . n 
B 1 732 ILE 732 751 751 ILE ILE B . n 
B 1 733 GLY 733 752 752 GLY GLY B . n 
B 1 734 GLN 734 753 753 GLN GLN B . n 
B 1 735 SER 735 754 754 SER SER B . n 
B 1 736 LEU 736 755 755 LEU LEU B . n 
B 1 737 ASN 737 756 756 ASN ASN B . n 
B 1 738 LEU 738 757 757 LEU LEU B . n 
B 1 739 THR 739 758 758 THR THR B . n 
B 1 740 VAL 740 759 759 VAL VAL B . n 
B 1 741 VAL 741 760 760 VAL VAL B . n 
B 1 742 ALA 742 761 761 ALA ALA B . n 
B 1 743 GLU 743 762 762 GLU GLU B . n 
B 1 744 GLY 744 763 763 GLY GLY B . n 
B 1 745 VAL 745 764 764 VAL VAL B . n 
B 1 746 GLU 746 765 765 GLU GLU B . n 
B 1 747 THR 747 766 766 THR THR B . n 
B 1 748 LYS 748 767 767 LYS LYS B . n 
B 1 749 GLU 749 768 768 GLU GLU B . n 
B 1 750 GLN 750 769 769 GLN GLN B . n 
B 1 751 PHE 751 770 770 PHE PHE B . n 
B 1 752 GLU 752 771 771 GLU GLU B . n 
B 1 753 MET 753 772 772 MET MET B . n 
B 1 754 LEU 754 773 773 LEU LEU B . n 
B 1 755 ARG 755 774 774 ARG ARG B . n 
B 1 756 LYS 756 775 775 LYS LYS B . n 
B 1 757 ILE 757 776 776 ILE ILE B . n 
B 1 758 HIS 758 777 777 HIS HIS B . n 
B 1 759 CYS 759 778 778 CYS CYS B . n 
B 1 760 ARG 760 779 779 ARG ARG B . n 
B 1 761 VAL 761 780 780 VAL VAL B . n 
B 1 762 ILE 762 781 781 ILE ILE B . n 
B 1 763 GLN 763 782 782 GLN GLN B . n 
B 1 764 GLY 764 783 783 GLY GLY B . n 
B 1 765 TYR 765 784 784 TYR TYR B . n 
B 1 766 PHE 766 785 785 PHE PHE B . n 
B 1 767 PHE 767 786 786 PHE PHE B . n 
B 1 768 SER 768 787 787 SER SER B . n 
B 1 769 ARG 769 788 788 ARG ARG B . n 
B 1 770 PRO 770 789 789 PRO PRO B . n 
B 1 771 LEU 771 790 790 LEU LEU B . n 
B 1 772 PRO 772 791 791 PRO PRO B . n 
B 1 773 ALA 773 792 792 ALA ALA B . n 
B 1 774 GLU 774 793 793 GLU GLU B . n 
B 1 775 GLU 775 794 794 GLU GLU B . n 
B 1 776 ILE 776 795 795 ILE ILE B . n 
B 1 777 PRO 777 796 796 PRO PRO B . n 
B 1 778 GLY 778 797 797 GLY GLY B . n 
B 1 779 TRP 779 798 798 TRP TRP B . n 
B 1 780 MET 780 799 799 MET MET B . n 
B 1 781 SER 781 800 800 SER SER B . n 
B 1 782 SER 782 801 801 SER SER B . n 
B 1 783 VAL 783 802 802 VAL VAL B . n 
B 1 784 LEU 784 803 803 LEU LEU B . n 
B 1 785 PRO 785 804 804 PRO PRO B . n 
B 1 786 LEU 786 805 805 LEU LEU B . n 
B 1 787 LYS 787 806 806 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM 1 901 2135 HEM HEM A . 
D 3 C2E 1 902 2136 C2E C2E A . 
E 4 MG  1 903 1    MG  MG  A . 
F 4 MG  1 904 4    MG  MG  A . 
G 3 C2E 1 901 1137 C2E C2E B . 
H 2 HEM 1 902 2135 HEM HEM B . 
I 4 MG  1 903 2    MG  MG  B . 
J 4 MG  1 904 3    MG  MG  B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B GLU 544 ? CG  ? B GLU 525 CG  
2 1 Y 1 B GLU 544 ? CD  ? B GLU 525 CD  
3 1 Y 1 B GLU 544 ? OE1 ? B GLU 525 OE1 
4 1 Y 1 B GLU 544 ? OE2 ? B GLU 525 OE2 
# 
_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                     9CLO 
_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                         9CLO 
_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                   9CLO 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9CLO 
_struct.title                        'DosP R97A with c-di-GMP' 
_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        9CLO 
_struct_keywords.text            'Heme, DosP, Phosphodiesterase, c-di-GMP, OXYGEN BINDING' 
_struct_keywords.pdbx_keywords   'OXYGEN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 3 ? 
H N N 2 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DOSP_ECOLI 
_struct_ref.pdbx_db_accession          P76129 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSREL
QLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGY
CISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEE
RQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPA
GILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGV
DHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPL
TLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGE
LYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVS
DAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEK
RILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLK
;
_struct_ref.pdbx_align_begin           12 
# 
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 9CLO A 1 ? 787 ? P76129 12 ? 798 ? 20 806 
2 1 9CLO B 1 ? 787 ? P76129 12 ? 798 ? 20 806 
# 
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 9CLO ALA A 78  ? UNP P76129 ARG 89  'engineered mutation' 97  1 
1 9CLO THR A 176 ? UNP P76129 ILE 187 conflict              195 2 
2 9CLO ALA B 78  ? UNP P76129 ARG 89  'engineered mutation' 97  3 
2 9CLO THR B 176 ? UNP P76129 ILE 187 conflict              195 4 
# 
_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,H,I,J 
# 
_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 ILE A 2   ? GLN A 9   ? ILE A 21  GLN A 28  1 ? 8  
HELX_P HELX_P2  AA2 ASN A 27  ? GLY A 35  ? ASN A 46  GLY A 54  1 ? 9  
HELX_P HELX_P3  AA3 LYS A 37  ? ILE A 42  ? LYS A 56  ILE A 61  1 ? 6  
HELX_P HELX_P4  AA4 ASN A 45  ? LEU A 49  ? ASN A 64  LEU A 68  5 ? 5  
HELX_P HELX_P5  AA5 PRO A 51  ? ARG A 55  ? PRO A 70  ARG A 74  5 ? 5  
HELX_P HELX_P6  AA6 HIS A 58  ? GLU A 67  ? HIS A 77  GLU A 86  1 ? 10 
HELX_P HELX_P7  AA7 ALA A 114 ? LEU A 134 ? ALA A 133 LEU A 153 1 ? 21 
HELX_P HELX_P8  AA8 ASN A 151 ? GLY A 159 ? ASN A 170 GLY A 178 1 ? 9  
HELX_P HELX_P9  AA9 ASP A 182 ? LEU A 191 ? ASP A 201 LEU A 210 1 ? 10 
HELX_P HELX_P10 AB1 ILE A 237 ? CYS A 255 ? ILE A 256 CYS A 274 1 ? 19 
HELX_P HELX_P11 AB2 PRO A 259 ? LEU A 275 ? PRO A 278 LEU A 294 1 ? 17 
HELX_P HELX_P12 AB3 THR A 333 ? GLN A 363 ? THR A 352 GLN A 382 1 ? 31 
HELX_P HELX_P13 AB4 ASN A 375 ? LYS A 389 ? ASN A 394 LYS A 408 1 ? 15 
HELX_P HELX_P14 AB5 ILE A 403 ? LEU A 410 ? ILE A 422 LEU A 429 1 ? 8  
HELX_P HELX_P15 AB6 GLY A 411 ? LYS A 429 ? GLY A 430 LYS A 448 1 ? 19 
HELX_P HELX_P16 AB7 ASP A 452 ? VAL A 467 ? ASP A 471 VAL A 486 1 ? 16 
HELX_P HELX_P17 AB8 ASN A 493 ? ASN A 511 ? ASN A 512 ASN A 530 1 ? 19 
HELX_P HELX_P18 AB9 SER A 520 ? MET A 523 ? SER A 539 MET A 542 5 ? 4  
HELX_P HELX_P19 AC1 ASN A 524 ? ASN A 544 ? ASN A 543 ASN A 563 1 ? 21 
HELX_P HELX_P20 AC2 PRO A 579 ? GLY A 591 ? PRO A 598 GLY A 610 1 ? 13 
HELX_P HELX_P21 AC3 GLU A 592 ? GLN A 614 ? GLU A 611 GLN A 633 1 ? 23 
HELX_P HELX_P22 AC4 SER A 626 ? SER A 632 ? SER A 645 SER A 651 1 ? 7  
HELX_P HELX_P23 AC5 GLN A 634 ? GLY A 647 ? GLN A 653 GLY A 666 1 ? 14 
HELX_P HELX_P24 AC6 THR A 658 ? GLU A 664 ? THR A 677 GLU A 683 1 ? 7  
HELX_P HELX_P25 AC7 ASP A 666 ? MET A 679 ? ASP A 685 MET A 698 1 ? 14 
HELX_P HELX_P26 AC8 GLY A 691 ? LEU A 701 ? GLY A 710 LEU A 720 1 ? 11 
HELX_P HELX_P27 AC9 ASP A 709 ? CYS A 716 ? ASP A 728 CYS A 735 1 ? 8  
HELX_P HELX_P28 AD1 GLU A 719 ? ARG A 721 ? GLU A 738 ARG A 740 5 ? 3  
HELX_P HELX_P29 AD2 ILE A 722 ? ASN A 737 ? ILE A 741 ASN A 756 1 ? 16 
HELX_P HELX_P30 AD3 THR A 747 ? LYS A 756 ? THR A 766 LYS A 775 1 ? 10 
HELX_P HELX_P31 AD4 GLU A 775 ? VAL A 783 ? GLU A 794 VAL A 802 1 ? 9  
HELX_P HELX_P32 AD5 ASN B 27  ? GLY B 35  ? ASN B 46  GLY B 54  1 ? 9  
HELX_P HELX_P33 AD6 HIS B 58  ? GLY B 69  ? HIS B 77  GLY B 88  1 ? 12 
HELX_P HELX_P34 AD7 ALA B 114 ? HIS B 133 ? ALA B 133 HIS B 152 1 ? 20 
HELX_P HELX_P35 AD8 ASN B 151 ? GLY B 159 ? ASN B 170 GLY B 178 1 ? 9  
HELX_P HELX_P36 AD9 CYS B 161 ? SER B 166 ? CYS B 180 SER B 185 1 ? 6  
HELX_P HELX_P37 AE1 ASN B 183 ? GLN B 189 ? ASN B 202 GLN B 208 1 ? 7  
HELX_P HELX_P38 AE2 GLN B 189 ? THR B 194 ? GLN B 208 THR B 213 1 ? 6  
HELX_P HELX_P39 AE3 ILE B 237 ? CYS B 255 ? ILE B 256 CYS B 274 1 ? 19 
HELX_P HELX_P40 AE4 PRO B 259 ? LEU B 275 ? PRO B 278 LEU B 294 1 ? 17 
HELX_P HELX_P41 AE5 THR B 333 ? ILE B 365 ? THR B 352 ILE B 384 1 ? 33 
HELX_P HELX_P42 AE6 ASN B 375 ? LYS B 389 ? ASN B 394 LYS B 408 1 ? 15 
HELX_P HELX_P43 AE7 ILE B 403 ? GLY B 411 ? ILE B 422 GLY B 430 1 ? 9  
HELX_P HELX_P44 AE8 GLY B 411 ? LEU B 430 ? GLY B 430 LEU B 449 1 ? 20 
HELX_P HELX_P45 AE9 ASP B 452 ? VAL B 466 ? ASP B 471 VAL B 485 1 ? 15 
HELX_P HELX_P46 AF1 ASN B 493 ? GLY B 512 ? ASN B 512 GLY B 531 1 ? 20 
HELX_P HELX_P47 AF2 ALA B 522 ? ASN B 544 ? ALA B 541 ASN B 563 1 ? 23 
HELX_P HELX_P48 AF3 PRO B 579 ? GLY B 591 ? PRO B 598 GLY B 610 1 ? 13 
HELX_P HELX_P49 AF4 GLU B 592 ? GLN B 614 ? GLU B 611 GLN B 633 1 ? 23 
HELX_P HELX_P50 AF5 SER B 626 ? ARG B 631 ? SER B 645 ARG B 650 1 ? 6  
HELX_P HELX_P51 AF6 GLN B 634 ? ALA B 645 ? GLN B 653 ALA B 664 1 ? 12 
HELX_P HELX_P52 AF7 THR B 658 ? GLU B 664 ? THR B 677 GLU B 683 1 ? 7  
HELX_P HELX_P53 AF8 ASP B 666 ? MET B 679 ? ASP B 685 MET B 698 1 ? 14 
HELX_P HELX_P54 AF9 GLY B 691 ? LEU B 701 ? GLY B 710 LEU B 720 1 ? 11 
HELX_P HELX_P55 AG1 ASP B 709 ? GLU B 719 ? ASP B 728 GLU B 738 1 ? 11 
HELX_P HELX_P56 AG2 ILE B 722 ? ASN B 737 ? ILE B 741 ASN B 756 1 ? 16 
HELX_P HELX_P57 AG3 THR B 747 ? LYS B 756 ? THR B 766 LYS B 775 1 ? 10 
HELX_P HELX_P58 AG4 GLU B 775 ? VAL B 783 ? GLU B 794 VAL B 802 1 ? 9  
# 
_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 GLU 565 OE2 ? ? ? 1_555 E MG . MG ? ? A GLU 584 A MG 903 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc2  metalc ? ? A ASP 686 OD2 ? ? ? 1_555 F MG . MG ? ? A ASP 705 A MG 904 1_555 ? ? ? ? ? ? ? 2.635 ? ? 
metalc3  metalc ? ? A GLU 743 OE1 ? ? ? 1_555 F MG . MG ? ? A GLU 762 A MG 904 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc4  metalc ? ? D C2E .   O2P ? ? ? 1_555 E MG . MG ? ? A C2E 902 A MG 903 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc5  metalc ? ? D C2E .   O1P ? ? ? 1_555 F MG . MG ? ? A C2E 902 A MG 904 1_555 ? ? ? ? ? ? ? 2.760 ? ? 
metalc6  metalc ? ? B GLU 565 OE2 ? ? ? 1_555 I MG . MG ? ? B GLU 584 B MG 903 1_555 ? ? ? ? ? ? ? 2.782 ? ? 
metalc7  metalc ? ? B ASN 624 OD1 ? ? ? 1_555 I MG . MG ? ? B ASN 643 B MG 903 1_555 ? ? ? ? ? ? ? 2.305 ? ? 
metalc8  metalc ? ? B ASP 686 OD2 ? ? ? 1_555 J MG . MG ? ? B ASP 705 B MG 904 1_555 ? ? ? ? ? ? ? 2.728 ? ? 
metalc9  metalc ? ? B ASP 709 OD1 ? ? ? 1_555 J MG . MG ? ? B ASP 728 B MG 904 1_555 ? ? ? ? ? ? ? 2.902 ? ? 
metalc10 metalc ? ? G C2E .   O2P ? ? ? 1_555 I MG . MG ? ? B C2E 901 B MG 903 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc11 metalc ? ? G C2E .   O1P ? ? ? 1_555 J MG . MG ? ? B C2E 901 B MG 904 1_555 ? ? ? ? ? ? ? 2.994 ? ? 
# 
_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  OE2 ? A GLU 565 ? A GLU 584 ? 1_555 MG ? E MG . ? A MG 903 ? 1_555 O2P ? D C2E .   ? A C2E 902 ? 1_555 126.0 ? 
2  OD2 ? A ASP 686 ? A ASP 705 ? 1_555 MG ? F MG . ? A MG 904 ? 1_555 OE1 ? A GLU 743 ? A GLU 762 ? 1_555 84.8  ? 
3  OD2 ? A ASP 686 ? A ASP 705 ? 1_555 MG ? F MG . ? A MG 904 ? 1_555 O1P ? D C2E .   ? A C2E 902 ? 1_555 118.2 ? 
4  OE1 ? A GLU 743 ? A GLU 762 ? 1_555 MG ? F MG . ? A MG 904 ? 1_555 O1P ? D C2E .   ? A C2E 902 ? 1_555 95.5  ? 
5  OE2 ? B GLU 565 ? B GLU 584 ? 1_555 MG ? I MG . ? B MG 903 ? 1_555 OD1 ? B ASN 624 ? B ASN 643 ? 1_555 90.4  ? 
6  OE2 ? B GLU 565 ? B GLU 584 ? 1_555 MG ? I MG . ? B MG 903 ? 1_555 O2P ? G C2E .   ? B C2E 901 ? 1_555 95.1  ? 
7  OD1 ? B ASN 624 ? B ASN 643 ? 1_555 MG ? I MG . ? B MG 903 ? 1_555 O2P ? G C2E .   ? B C2E 901 ? 1_555 100.9 ? 
8  OD2 ? B ASP 686 ? B ASP 705 ? 1_555 MG ? J MG . ? B MG 904 ? 1_555 OD1 ? B ASP 709 ? B ASP 728 ? 1_555 107.5 ? 
9  OD2 ? B ASP 686 ? B ASP 705 ? 1_555 MG ? J MG . ? B MG 904 ? 1_555 O1P ? G C2E .   ? B C2E 901 ? 1_555 91.5  ? 
10 OD1 ? B ASP 709 ? B ASP 728 ? 1_555 MG ? J MG . ? B MG 904 ? 1_555 O1P ? G C2E .   ? B C2E 901 ? 1_555 123.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 784 A . ? LEU 803 A PRO 785 A ? PRO 804 A 1 -4.96 
2 LEU 784 B . ? LEU 803 B PRO 785 B ? PRO 804 B 1 -5.81 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 2  ? 
AA3 ? 5  ? 
AA4 ? 4  ? 
AA5 ? 5  ? 
AA6 ? 2  ? 
AA7 ? 10 ? 
AA8 ? 2  ? 
AA9 ? 5  ? 
AB1 ? 5  ? 
AB2 ? 4  ? 
AB3 ? 5  ? 
AB4 ? 4  ? 
AB5 ? 10 ? 
# 
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  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA4 1 2  ? anti-parallel 
AA4 2 3  ? anti-parallel 
AA4 3 4  ? anti-parallel 
AA5 1 2  ? anti-parallel 
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA6 1 2  ? anti-parallel 
AA7 1 2  ? anti-parallel 
AA7 2 3  ? anti-parallel 
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? parallel      
AA7 8 9  ? parallel      
AA7 9 10 ? anti-parallel 
AA8 1 2  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AB1 1 2  ? anti-parallel 
AB1 2 3  ? anti-parallel 
AB1 3 4  ? anti-parallel 
AB1 4 5  ? anti-parallel 
AB2 1 2  ? anti-parallel 
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? parallel      
AB4 1 2  ? anti-parallel 
AB4 2 3  ? anti-parallel 
AB4 3 4  ? anti-parallel 
AB5 1 2  ? anti-parallel 
AB5 2 3  ? parallel      
AB5 3 4  ? parallel      
AB5 4 5  ? parallel      
AB5 5 6  ? parallel      
AB5 6 7  ? parallel      
AB5 7 8  ? parallel      
AB5 8 9  ? anti-parallel 
AB5 9 10 ? 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  GLY A 13  ? ALA A 14  ? GLY A 32  ALA A 33  
AA1 2  LYS A 104 ? VAL A 111 ? LYS A 123 VAL A 130 
AA1 3  LEU A 96  ? ALA A 101 ? LEU A 115 ALA A 120 
AA2 1  LEU A 80  ? GLU A 83  ? LEU A 99  GLU A 102 
AA2 2  LYS A 89  ? THR A 92  ? LYS A 108 THR A 111 
AA3 1  ILE A 147 ? GLN A 149 ? ILE A 166 GLN A 168 
AA3 2  VAL A 138 ? LEU A 141 ? VAL A 157 LEU A 160 
AA3 3  LEU A 227 ? ASP A 236 ? LEU A 246 ASP A 255 
AA3 4  LYS A 210 ? TYR A 221 ? LYS A 229 TYR A 240 
AA3 5  ASP A 197 ? LEU A 204 ? ASP A 216 LEU A 223 
AA4 1  MET A 289 ? SER A 295 ? MET A 308 SER A 314 
AA4 2  HIS A 279 ? ARG A 286 ? HIS A 298 ARG A 305 
AA4 3  PRO A 319 ? SER A 328 ? PRO A 338 SER A 347 
AA4 4  ALA A 305 ? ARG A 313 ? ALA A 324 ARG A 332 
AA5 1  TYR A 435 ? GLU A 440 ? TYR A 454 GLU A 459 
AA5 2  GLN A 443 ? SER A 448 ? GLN A 462 SER A 467 
AA5 3  VAL A 394 ? ASP A 401 ? VAL A 413 ASP A 420 
AA5 4  THR A 481 ? SER A 487 ? THR A 500 SER A 506 
AA5 5  GLY A 515 ? PHE A 518 ? GLY A 534 PHE A 537 
AA6 1  ILE A 471 ? ILE A 473 ? ILE A 490 ILE A 492 
AA6 2  LYS A 476 ? PHE A 478 ? LYS A 495 PHE A 497 
AA7 1  LEU A 771 ? PRO A 772 ? LEU A 790 PRO A 791 
AA7 2  LYS A 547 ? PHE A 555 ? LYS A 566 PHE A 574 
AA7 3  VAL A 761 ? GLY A 764 ? VAL A 780 GLY A 783 
AA7 4  THR A 739 ? VAL A 745 ? THR A 758 VAL A 764 
AA7 5  GLU A 705 ? ILE A 708 ? GLU A 724 ILE A 727 
AA7 6  GLY A 682 ? ASP A 686 ? GLY A 701 ASP A 705 
AA7 7  LEU A 653 ? ILE A 657 ? LEU A 672 ILE A 676 
AA7 8  LEU A 621 ? ASN A 624 ? LEU A 640 ASN A 643 
AA7 9  LEU A 561 ? ARG A 569 ? LEU A 580 ARG A 588 
AA7 10 LYS A 547 ? PHE A 555 ? LYS A 566 PHE A 574 
AA8 1  HIS A 571 ? ASP A 572 ? HIS A 590 ASP A 591 
AA8 2  GLY A 576 ? HIS A 577 ? GLY A 595 HIS A 596 
AA9 1  VAL B 23  ? PHE B 25  ? VAL B 42  PHE B 44  
AA9 2  LEU B 16  ? ILE B 17  ? LEU B 35  ILE B 36  
AA9 3  LYS B 104 ? ARG B 112 ? LYS B 123 ARG B 131 
AA9 4  LYS B 89  ? ALA B 101 ? LYS B 108 ALA B 120 
AA9 5  LEU B 80  ? GLU B 83  ? LEU B 99  GLU B 102 
AB1 1  ILE B 147 ? GLN B 149 ? ILE B 166 GLN B 168 
AB1 2  VAL B 138 ? LEU B 141 ? VAL B 157 LEU B 160 
AB1 3  LEU B 227 ? ASP B 236 ? LEU B 246 ASP B 255 
AB1 4  ILE B 213 ? TYR B 221 ? ILE B 232 TYR B 240 
AB1 5  GLU B 200 ? PHE B 201 ? GLU B 219 PHE B 220 
AB2 1  MET B 289 ? SER B 295 ? MET B 308 SER B 314 
AB2 2  SER B 278 ? ARG B 286 ? SER B 297 ARG B 305 
AB2 3  PRO B 319 ? SER B 328 ? PRO B 338 SER B 347 
AB2 4  ALA B 305 ? ARG B 313 ? ALA B 324 ARG B 332 
AB3 1  TYR B 435 ? GLU B 440 ? TYR B 454 GLU B 459 
AB3 2  GLN B 443 ? SER B 448 ? GLN B 462 SER B 467 
AB3 3  VAL B 394 ? ASP B 401 ? VAL B 413 ASP B 420 
AB3 4  THR B 481 ? SER B 487 ? THR B 500 SER B 506 
AB3 5  GLY B 515 ? PHE B 518 ? GLY B 534 PHE B 537 
AB4 1  GLY B 576 ? HIS B 577 ? GLY B 595 HIS B 596 
AB4 2  LEU B 561 ? ASP B 572 ? LEU B 580 ASP B 591 
AB4 3  LEU B 546 ? PHE B 555 ? LEU B 565 PHE B 574 
AB4 4  LEU B 771 ? PRO B 772 ? LEU B 790 PRO B 791 
AB5 1  GLY B 576 ? HIS B 577 ? GLY B 595 HIS B 596 
AB5 2  LEU B 561 ? ASP B 572 ? LEU B 580 ASP B 591 
AB5 3  LEU B 621 ? ASN B 624 ? LEU B 640 ASN B 643 
AB5 4  LEU B 653 ? ILE B 657 ? LEU B 672 ILE B 676 
AB5 5  GLY B 682 ? ASP B 686 ? GLY B 701 ASP B 705 
AB5 6  GLU B 705 ? ILE B 708 ? GLU B 724 ILE B 727 
AB5 7  THR B 739 ? VAL B 745 ? THR B 758 VAL B 764 
AB5 8  VAL B 761 ? GLY B 764 ? VAL B 780 GLY B 783 
AB5 9  LEU B 546 ? PHE B 555 ? LEU B 565 PHE B 574 
AB5 10 LEU B 771 ? PRO B 772 ? LEU B 790 PRO B 791 
# 
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  N GLY A 13  ? N GLY A 32  O VAL A 111 ? O VAL A 130 
AA1 2 3  O TYR A 106 ? O TYR A 125 N VAL A 99  ? N VAL A 118 
AA2 1 2  N LEU A 80  ? N LEU A 99  O THR A 92  ? O THR A 111 
AA3 1 2  O VAL A 148 ? O VAL A 167 N VAL A 140 ? N VAL A 159 
AA3 2 3  N ILE A 139 ? N ILE A 158 O MET A 232 ? O MET A 251 
AA3 3 4  O ASN A 229 ? O ASN A 248 N VAL A 220 ? N VAL A 239 
AA3 4 5  O ILE A 217 ? O ILE A 236 N ASP A 197 ? N ASP A 216 
AA4 1 2  O ILE A 291 ? O ILE A 310 N ALA A 284 ? N ALA A 303 
AA4 2 3  N HIS A 279 ? N HIS A 298 O LYS A 326 ? O LYS A 345 
AA4 3 4  O ALA A 320 ? O ALA A 339 N ILE A 312 ? N ILE A 331 
AA5 1 2  N TYR A 435 ? N TYR A 454 O VAL A 447 ? O VAL A 466 
AA5 2 3  O SER A 448 ? O SER A 467 N VAL A 394 ? N VAL A 413 
AA5 3 4  N LEU A 397 ? N LEU A 416 O GLY A 485 ? O GLY A 504 
AA5 4 5  N ILE A 484 ? N ILE A 503 O GLY A 515 ? O GLY A 534 
AA6 1 2  N ILE A 471 ? N ILE A 490 O PHE A 478 ? O PHE A 497 
AA7 1 2  O LEU A 771 ? O LEU A 790 N TYR A 550 ? N TYR A 569 
AA7 2 3  N ILE A 554 ? N ILE A 573 O ILE A 762 ? O ILE A 781 
AA7 3 4  O VAL A 761 ? O VAL A 780 N VAL A 740 ? N VAL A 759 
AA7 4 5  O VAL A 741 ? O VAL A 760 N ILE A 706 ? N ILE A 725 
AA7 5 6  O LYS A 707 ? O LYS A 726 N VAL A 685 ? N VAL A 704 
AA7 6 7  O SER A 684 ? O SER A 703 N VAL A 655 ? N VAL A 674 
AA7 7 8  O THR A 654 ? O THR A 673 N VAL A 623 ? N VAL A 642 
AA7 8 9  O SER A 622 ? O SER A 641 N ALA A 566 ? N ALA A 585 
AA7 9 10 O GLY A 563 ? O GLY A 582 N GLN A 553 ? N GLN A 572 
AA8 1 2  N ASP A 572 ? N ASP A 591 O GLY A 576 ? O GLY A 595 
AA9 1 2  O MET B 24  ? O MET B 43  N LEU B 16  ? N LEU B 35  
AA9 2 3  N ILE B 17  ? N ILE B 36  O TYR B 107 ? O TYR B 126 
AA9 3 4  O LEU B 108 ? O LEU B 127 N SER B 97  ? N SER B 116 
AA9 4 5  O THR B 92  ? O THR B 111 N LEU B 80  ? N LEU B 99  
AB1 1 2  O VAL B 148 ? O VAL B 167 N VAL B 140 ? N VAL B 159 
AB1 2 3  N LEU B 141 ? N LEU B 160 O LEU B 230 ? O LEU B 249 
AB1 3 4  O ASN B 229 ? O ASN B 248 N VAL B 220 ? N VAL B 239 
AB1 4 5  O ILE B 213 ? O ILE B 232 N PHE B 201 ? N PHE B 220 
AB2 1 2  O ALA B 294 ? O ALA B 313 N LEU B 282 ? N LEU B 301 
AB2 2 3  N HIS B 279 ? N HIS B 298 O LYS B 326 ? O LYS B 345 
AB2 3 4  O ALA B 320 ? O ALA B 339 N ILE B 312 ? N ILE B 331 
AB3 1 2  N GLU B 440 ? N GLU B 459 O GLN B 443 ? O GLN B 462 
AB3 2 3  O SER B 448 ? O SER B 467 N VAL B 394 ? N VAL B 413 
AB3 3 4  N LEU B 397 ? N LEU B 416 O GLY B 485 ? O GLY B 504 
AB3 4 5  N ILE B 486 ? N ILE B 505 O GLN B 517 ? O GLN B 536 
AB4 1 2  O GLY B 576 ? O GLY B 595 N ASP B 572 ? N ASP B 591 
AB4 2 3  O ARG B 569 ? O ARG B 588 N LYS B 547 ? N LYS B 566 
AB4 3 4  N TYR B 550 ? N TYR B 569 O LEU B 771 ? O LEU B 790 
AB5 1 2  O GLY B 576 ? O GLY B 595 N ASP B 572 ? N ASP B 591 
AB5 2 3  N ALA B 566 ? N ALA B 585 O SER B 622 ? O SER B 641 
AB5 3 4  N LEU B 621 ? N LEU B 640 O THR B 654 ? O THR B 673 
AB5 4 5  N ILE B 657 ? N ILE B 676 O SER B 684 ? O SER B 703 
AB5 5 6  N VAL B 685 ? N VAL B 704 O LYS B 707 ? O LYS B 726 
AB5 6 7  N ILE B 708 ? N ILE B 727 O GLU B 743 ? O GLU B 762 
AB5 7 8  N ALA B 742 ? N ALA B 761 O GLN B 763 ? O GLN B 782 
AB5 8 9  O ILE B 762 ? O ILE B 781 N ILE B 554 ? N ILE B 573 
AB5 9 10 N TYR B 550 ? N TYR B 569 O LEU B 771 ? O LEU B 790 
# 
_pdbx_entry_details.entry_id                   9CLO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 HIS A 77  ? ? -150.52 -38.96  
2  1 PRO A 196 ? ? -66.93  -173.46 
3  1 PHE A 198 ? ? -56.94  107.36  
4  1 SER A 276 ? ? 59.47   72.76   
5  1 PRO A 388 ? ? -68.29  0.84    
6  1 LYS A 511 ? ? -120.50 -62.48  
7  1 ASN A 512 ? ? 178.47  160.77  
8  1 ASN A 530 ? ? -96.85  59.07   
9  1 SER A 539 ? ? 53.96   76.57   
10 1 PRO A 540 ? ? -54.74  -4.24   
11 1 ILE A 637 ? ? 41.71   74.94   
12 1 ASN A 652 ? ? -87.84  49.50   
13 1 ASP A 668 ? ? -38.74  142.44  
14 1 ASP A 706 ? ? 65.55   162.99  
15 1 PRO B 189 ? ? -86.53  44.07   
16 1 GLN B 217 ? ? -170.97 148.98  
17 1 GLU B 296 ? ? 60.27   60.43   
18 1 GLN B 333 ? ? -78.80  -166.77 
19 1 PRO B 388 ? ? -83.27  42.82   
20 1 TYR B 507 ? ? -160.46 119.36  
21 1 SER B 539 ? ? 73.29   147.26  
22 1 ALA B 541 ? ? 73.46   -14.62  
23 1 ILE B 637 ? ? 42.12   75.13   
24 1 ASP B 668 ? ? -39.80  143.58  
25 1 ASP B 706 ? ? 64.43   167.55  
26 1 ASN B 756 ? ? 60.00   64.20   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CLO 
_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                    9CLO 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.1 
_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               186761 
_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            7.5 
# 
_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                 'Dimer of DosP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9CLO 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS 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             800 
_em_imaging.nominal_defocus_max             2000 
_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              9CLO 
_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                9CLO 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
C2E P1     P  N N 74  
C2E O2P    O  N N 75  
C2E O1P    O  N N 76  
C2E "O5'"  O  N N 77  
C2E "C5'"  C  N N 78  
C2E "C4'"  C  N R 79  
C2E "O4'"  O  N N 80  
C2E "C3'"  C  N S 81  
C2E "O3'"  O  N N 82  
C2E "C2'"  C  N R 83  
C2E "O2'"  O  N N 84  
C2E "C1'"  C  N R 85  
C2E N9     N  Y N 86  
C2E C8     C  Y N 87  
C2E N7     N  Y N 88  
C2E C5     C  Y N 89  
C2E C6     C  N N 90  
C2E O6     O  N N 91  
C2E N1     N  N N 92  
C2E C2     C  N N 93  
C2E N2     N  N N 94  
C2E N3     N  N N 95  
C2E C4     C  Y N 96  
C2E P11    P  N N 97  
C2E O21    O  N N 98  
C2E O11    O  N N 99  
C2E O5A    O  N N 100 
C2E C5A    C  N N 101 
C2E C4A    C  N R 102 
C2E O4A    O  N N 103 
C2E C3A    C  N S 104 
C2E O3A    O  N N 105 
C2E C2A    C  N R 106 
C2E O2A    O  N N 107 
C2E C1A    C  N R 108 
C2E N91    N  Y N 109 
C2E C81    C  Y N 110 
C2E N71    N  Y N 111 
C2E C51    C  Y N 112 
C2E C61    C  N N 113 
C2E O61    O  N N 114 
C2E N11    N  N N 115 
C2E C21    C  N N 116 
C2E N21    N  N N 117 
C2E N31    N  N N 118 
C2E C41    C  Y N 119 
C2E HO2P   H  N N 120 
C2E "H5'1" H  N N 121 
C2E "H5'2" H  N N 122 
C2E "H4'"  H  N N 123 
C2E "H3'"  H  N N 124 
C2E "H2'"  H  N N 125 
C2E "HO2'" H  N N 126 
C2E "H1'"  H  N N 127 
C2E H8     H  N N 128 
C2E HN1    H  N N 129 
C2E HN21   H  N N 130 
C2E HN22   H  N N 131 
C2E HO21   H  N N 132 
C2E H511   H  N N 133 
C2E H512   H  N N 134 
C2E H4A    H  N N 135 
C2E H3A    H  N N 136 
C2E H2A    H  N N 137 
C2E HO2A   H  N N 138 
C2E H1A    H  N N 139 
C2E H81    H  N N 140 
C2E HN11   H  N N 141 
C2E HN24   H  N N 142 
C2E HN23   H  N N 143 
CYS N      N  N N 144 
CYS CA     C  N R 145 
CYS C      C  N N 146 
CYS O      O  N N 147 
CYS CB     C  N N 148 
CYS SG     S  N N 149 
CYS OXT    O  N N 150 
CYS H      H  N N 151 
CYS H2     H  N N 152 
CYS HA     H  N N 153 
CYS HB2    H  N N 154 
CYS HB3    H  N N 155 
CYS HG     H  N N 156 
CYS HXT    H  N N 157 
GLN N      N  N N 158 
GLN CA     C  N S 159 
GLN C      C  N N 160 
GLN O      O  N N 161 
GLN CB     C  N N 162 
GLN CG     C  N N 163 
GLN CD     C  N N 164 
GLN OE1    O  N N 165 
GLN NE2    N  N N 166 
GLN OXT    O  N N 167 
GLN H      H  N N 168 
GLN H2     H  N N 169 
GLN HA     H  N N 170 
GLN HB2    H  N N 171 
GLN HB3    H  N N 172 
GLN HG2    H  N N 173 
GLN HG3    H  N N 174 
GLN HE21   H  N N 175 
GLN HE22   H  N N 176 
GLN HXT    H  N N 177 
GLU N      N  N N 178 
GLU CA     C  N S 179 
GLU C      C  N N 180 
GLU O      O  N N 181 
GLU CB     C  N N 182 
GLU CG     C  N N 183 
GLU CD     C  N N 184 
GLU OE1    O  N N 185 
GLU OE2    O  N N 186 
GLU OXT    O  N N 187 
GLU H      H  N N 188 
GLU H2     H  N N 189 
GLU HA     H  N N 190 
GLU HB2    H  N N 191 
GLU HB3    H  N N 192 
GLU HG2    H  N N 193 
GLU HG3    H  N N 194 
GLU HE2    H  N N 195 
GLU HXT    H  N N 196 
GLY N      N  N N 197 
GLY CA     C  N N 198 
GLY C      C  N N 199 
GLY O      O  N N 200 
GLY OXT    O  N N 201 
GLY H      H  N N 202 
GLY H2     H  N N 203 
GLY HA2    H  N N 204 
GLY HA3    H  N N 205 
GLY HXT    H  N N 206 
HEM CHA    C  N N 207 
HEM CHB    C  N N 208 
HEM CHC    C  N N 209 
HEM CHD    C  N N 210 
HEM C1A    C  Y N 211 
HEM C2A    C  Y N 212 
HEM C3A    C  Y N 213 
HEM C4A    C  Y N 214 
HEM CMA    C  N N 215 
HEM CAA    C  N N 216 
HEM CBA    C  N N 217 
HEM CGA    C  N N 218 
HEM O1A    O  N N 219 
HEM O2A    O  N N 220 
HEM C1B    C  N N 221 
HEM C2B    C  N N 222 
HEM C3B    C  N N 223 
HEM C4B    C  N N 224 
HEM CMB    C  N N 225 
HEM CAB    C  N N 226 
HEM CBB    C  N N 227 
HEM C1C    C  Y N 228 
HEM C2C    C  Y N 229 
HEM C3C    C  Y N 230 
HEM C4C    C  Y N 231 
HEM CMC    C  N N 232 
HEM CAC    C  N N 233 
HEM CBC    C  N N 234 
HEM C1D    C  N N 235 
HEM C2D    C  N N 236 
HEM C3D    C  N N 237 
HEM C4D    C  N N 238 
HEM CMD    C  N N 239 
HEM CAD    C  N N 240 
HEM CBD    C  N N 241 
HEM CGD    C  N N 242 
HEM O1D    O  N N 243 
HEM O2D    O  N N 244 
HEM NA     N  Y N 245 
HEM NB     N  N N 246 
HEM NC     N  Y N 247 
HEM ND     N  N N 248 
HEM FE     FE N N 249 
HEM HHB    H  N N 250 
HEM HHC    H  N N 251 
HEM HHD    H  N N 252 
HEM HMA    H  N N 253 
HEM HMAA   H  N N 254 
HEM HMAB   H  N N 255 
HEM HAA    H  N N 256 
HEM HAAA   H  N N 257 
HEM HBA    H  N N 258 
HEM HBAA   H  N N 259 
HEM HMB    H  N N 260 
HEM HMBA   H  N N 261 
HEM HMBB   H  N N 262 
HEM HAB    H  N N 263 
HEM HBB    H  N N 264 
HEM HBBA   H  N N 265 
HEM HMC    H  N N 266 
HEM HMCA   H  N N 267 
HEM HMCB   H  N N 268 
HEM HAC    H  N N 269 
HEM HBC    H  N N 270 
HEM HBCA   H  N N 271 
HEM HMD    H  N N 272 
HEM HMDA   H  N N 273 
HEM HMDB   H  N N 274 
HEM HAD    H  N N 275 
HEM HADA   H  N N 276 
HEM HBD    H  N N 277 
HEM HBDA   H  N N 278 
HEM H2A    H  N N 279 
HEM H2D    H  N N 280 
HEM HHA    H  N N 281 
HIS N      N  N N 282 
HIS CA     C  N S 283 
HIS C      C  N N 284 
HIS O      O  N N 285 
HIS CB     C  N N 286 
HIS CG     C  Y N 287 
HIS ND1    N  Y N 288 
HIS CD2    C  Y N 289 
HIS CE1    C  Y N 290 
HIS NE2    N  Y N 291 
HIS OXT    O  N N 292 
HIS H      H  N N 293 
HIS H2     H  N N 294 
HIS HA     H  N N 295 
HIS HB2    H  N N 296 
HIS HB3    H  N N 297 
HIS HD1    H  N N 298 
HIS HD2    H  N N 299 
HIS HE1    H  N N 300 
HIS HE2    H  N N 301 
HIS HXT    H  N N 302 
ILE N      N  N N 303 
ILE CA     C  N S 304 
ILE C      C  N N 305 
ILE O      O  N N 306 
ILE CB     C  N S 307 
ILE CG1    C  N N 308 
ILE CG2    C  N N 309 
ILE CD1    C  N N 310 
ILE OXT    O  N N 311 
ILE H      H  N N 312 
ILE H2     H  N N 313 
ILE HA     H  N N 314 
ILE HB     H  N N 315 
ILE HG12   H  N N 316 
ILE HG13   H  N N 317 
ILE HG21   H  N N 318 
ILE HG22   H  N N 319 
ILE HG23   H  N N 320 
ILE HD11   H  N N 321 
ILE HD12   H  N N 322 
ILE HD13   H  N N 323 
ILE HXT    H  N N 324 
LEU N      N  N N 325 
LEU CA     C  N S 326 
LEU C      C  N N 327 
LEU O      O  N N 328 
LEU CB     C  N N 329 
LEU CG     C  N N 330 
LEU CD1    C  N N 331 
LEU CD2    C  N N 332 
LEU OXT    O  N N 333 
LEU H      H  N N 334 
LEU H2     H  N N 335 
LEU HA     H  N N 336 
LEU HB2    H  N N 337 
LEU HB3    H  N N 338 
LEU HG     H  N N 339 
LEU HD11   H  N N 340 
LEU HD12   H  N N 341 
LEU HD13   H  N N 342 
LEU HD21   H  N N 343 
LEU HD22   H  N N 344 
LEU HD23   H  N N 345 
LEU HXT    H  N N 346 
LYS N      N  N N 347 
LYS CA     C  N S 348 
LYS C      C  N N 349 
LYS O      O  N N 350 
LYS CB     C  N N 351 
LYS CG     C  N N 352 
LYS CD     C  N N 353 
LYS CE     C  N N 354 
LYS NZ     N  N N 355 
LYS OXT    O  N N 356 
LYS H      H  N N 357 
LYS H2     H  N N 358 
LYS HA     H  N N 359 
LYS HB2    H  N N 360 
LYS HB3    H  N N 361 
LYS HG2    H  N N 362 
LYS HG3    H  N N 363 
LYS HD2    H  N N 364 
LYS HD3    H  N N 365 
LYS HE2    H  N N 366 
LYS HE3    H  N N 367 
LYS HZ1    H  N N 368 
LYS HZ2    H  N N 369 
LYS HZ3    H  N N 370 
LYS HXT    H  N N 371 
MET N      N  N N 372 
MET CA     C  N S 373 
MET C      C  N N 374 
MET O      O  N N 375 
MET CB     C  N N 376 
MET CG     C  N N 377 
MET SD     S  N N 378 
MET CE     C  N N 379 
MET OXT    O  N N 380 
MET H      H  N N 381 
MET H2     H  N N 382 
MET HA     H  N N 383 
MET HB2    H  N N 384 
MET HB3    H  N N 385 
MET HG2    H  N N 386 
MET HG3    H  N N 387 
MET HE1    H  N N 388 
MET HE2    H  N N 389 
MET HE3    H  N N 390 
MET HXT    H  N N 391 
MG  MG     MG N N 392 
PHE N      N  N N 393 
PHE CA     C  N S 394 
PHE C      C  N N 395 
PHE O      O  N N 396 
PHE CB     C  N N 397 
PHE CG     C  Y N 398 
PHE CD1    C  Y N 399 
PHE CD2    C  Y N 400 
PHE CE1    C  Y N 401 
PHE CE2    C  Y N 402 
PHE CZ     C  Y N 403 
PHE OXT    O  N N 404 
PHE H      H  N N 405 
PHE H2     H  N N 406 
PHE HA     H  N N 407 
PHE HB2    H  N N 408 
PHE HB3    H  N N 409 
PHE HD1    H  N N 410 
PHE HD2    H  N N 411 
PHE HE1    H  N N 412 
PHE HE2    H  N N 413 
PHE HZ     H  N N 414 
PHE HXT    H  N N 415 
PRO N      N  N N 416 
PRO CA     C  N S 417 
PRO C      C  N N 418 
PRO O      O  N N 419 
PRO CB     C  N N 420 
PRO CG     C  N N 421 
PRO CD     C  N N 422 
PRO OXT    O  N N 423 
PRO H      H  N N 424 
PRO HA     H  N N 425 
PRO HB2    H  N N 426 
PRO HB3    H  N N 427 
PRO HG2    H  N N 428 
PRO HG3    H  N N 429 
PRO HD2    H  N N 430 
PRO HD3    H  N N 431 
PRO HXT    H  N N 432 
SER N      N  N N 433 
SER CA     C  N S 434 
SER C      C  N N 435 
SER O      O  N N 436 
SER CB     C  N N 437 
SER OG     O  N N 438 
SER OXT    O  N N 439 
SER H      H  N N 440 
SER H2     H  N N 441 
SER HA     H  N N 442 
SER HB2    H  N N 443 
SER HB3    H  N N 444 
SER HG     H  N N 445 
SER HXT    H  N N 446 
THR N      N  N N 447 
THR CA     C  N S 448 
THR C      C  N N 449 
THR O      O  N N 450 
THR CB     C  N R 451 
THR OG1    O  N N 452 
THR CG2    C  N N 453 
THR OXT    O  N N 454 
THR H      H  N N 455 
THR H2     H  N N 456 
THR HA     H  N N 457 
THR HB     H  N N 458 
THR HG1    H  N N 459 
THR HG21   H  N N 460 
THR HG22   H  N N 461 
THR HG23   H  N N 462 
THR HXT    H  N N 463 
TRP N      N  N N 464 
TRP CA     C  N S 465 
TRP C      C  N N 466 
TRP O      O  N N 467 
TRP CB     C  N N 468 
TRP CG     C  Y N 469 
TRP CD1    C  Y N 470 
TRP CD2    C  Y N 471 
TRP NE1    N  Y N 472 
TRP CE2    C  Y N 473 
TRP CE3    C  Y N 474 
TRP CZ2    C  Y N 475 
TRP CZ3    C  Y N 476 
TRP CH2    C  Y N 477 
TRP OXT    O  N N 478 
TRP H      H  N N 479 
TRP H2     H  N N 480 
TRP HA     H  N N 481 
TRP HB2    H  N N 482 
TRP HB3    H  N N 483 
TRP HD1    H  N N 484 
TRP HE1    H  N N 485 
TRP HE3    H  N N 486 
TRP HZ2    H  N N 487 
TRP HZ3    H  N N 488 
TRP HH2    H  N N 489 
TRP HXT    H  N N 490 
TYR N      N  N N 491 
TYR CA     C  N S 492 
TYR C      C  N N 493 
TYR O      O  N N 494 
TYR CB     C  N N 495 
TYR CG     C  Y N 496 
TYR CD1    C  Y N 497 
TYR CD2    C  Y N 498 
TYR CE1    C  Y N 499 
TYR CE2    C  Y N 500 
TYR CZ     C  Y N 501 
TYR OH     O  N N 502 
TYR OXT    O  N N 503 
TYR H      H  N N 504 
TYR H2     H  N N 505 
TYR HA     H  N N 506 
TYR HB2    H  N N 507 
TYR HB3    H  N N 508 
TYR HD1    H  N N 509 
TYR HD2    H  N N 510 
TYR HE1    H  N N 511 
TYR HE2    H  N N 512 
TYR HH     H  N N 513 
TYR HXT    H  N N 514 
VAL N      N  N N 515 
VAL CA     C  N S 516 
VAL C      C  N N 517 
VAL O      O  N N 518 
VAL CB     C  N N 519 
VAL CG1    C  N N 520 
VAL CG2    C  N N 521 
VAL OXT    O  N N 522 
VAL H      H  N N 523 
VAL H2     H  N N 524 
VAL HA     H  N N 525 
VAL HB     H  N N 526 
VAL HG11   H  N N 527 
VAL HG12   H  N N 528 
VAL HG13   H  N N 529 
VAL HG21   H  N N 530 
VAL HG22   H  N N 531 
VAL HG23   H  N N 532 
VAL HXT    H  N N 533 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
C2E P1    O2P    sing N N 70  
C2E O1P   P1     doub N N 71  
C2E "O5'" P1     sing N N 72  
C2E "C5'" "O5'"  sing N N 73  
C2E "C4'" "O4'"  sing N N 74  
C2E "C4'" "C5'"  sing N N 75  
C2E "C3'" "C4'"  sing N N 76  
C2E "O3'" P11    sing N N 77  
C2E "O3'" "C3'"  sing N N 78  
C2E "C2'" "C3'"  sing N N 79  
C2E "C2'" "C1'"  sing N N 80  
C2E "O2'" "C2'"  sing N N 81  
C2E "C1'" "O4'"  sing N N 82  
C2E "C1'" N9     sing N N 83  
C2E N9    C4     sing Y N 84  
C2E N9    C8     sing Y N 85  
C2E C8    N7     doub Y N 86  
C2E C5    N7     sing Y N 87  
C2E C5    C6     sing N N 88  
C2E C6    O6     doub N N 89  
C2E N1    C6     sing N N 90  
C2E C2    N1     sing N N 91  
C2E N2    C2     sing N N 92  
C2E N3    C2     doub N N 93  
C2E N3    C4     sing N N 94  
C2E C4    C5     doub Y N 95  
C2E P11   O21    sing N N 96  
C2E P11   O5A    sing N N 97  
C2E O11   P11    doub N N 98  
C2E C5A   O5A    sing N N 99  
C2E C5A   C4A    sing N N 100 
C2E C4A   O4A    sing N N 101 
C2E C4A   C3A    sing N N 102 
C2E O4A   C1A    sing N N 103 
C2E C3A   C2A    sing N N 104 
C2E O3A   C3A    sing N N 105 
C2E O3A   P1     sing N N 106 
C2E C2A   O2A    sing N N 107 
C2E C1A   C2A    sing N N 108 
C2E C1A   N91    sing N N 109 
C2E N91   C41    sing Y N 110 
C2E C81   N71    doub Y N 111 
C2E C81   N91    sing Y N 112 
C2E N71   C51    sing Y N 113 
C2E C51   C41    doub Y N 114 
C2E C51   C61    sing N N 115 
C2E C61   O61    doub N N 116 
C2E C61   N11    sing N N 117 
C2E C21   N11    sing N N 118 
C2E C21   N21    sing N N 119 
C2E N31   C21    doub N N 120 
C2E C41   N31    sing N N 121 
C2E O2P   HO2P   sing N N 122 
C2E "C5'" "H5'1" sing N N 123 
C2E "C5'" "H5'2" sing N N 124 
C2E "C4'" "H4'"  sing N N 125 
C2E "C3'" "H3'"  sing N N 126 
C2E "C2'" "H2'"  sing N N 127 
C2E "O2'" "HO2'" sing N N 128 
C2E "C1'" "H1'"  sing N N 129 
C2E C8    H8     sing N N 130 
C2E N1    HN1    sing N N 131 
C2E N2    HN21   sing N N 132 
C2E N2    HN22   sing N N 133 
C2E O21   HO21   sing N N 134 
C2E C5A   H511   sing N N 135 
C2E C5A   H512   sing N N 136 
C2E C4A   H4A    sing N N 137 
C2E C3A   H3A    sing N N 138 
C2E C2A   H2A    sing N N 139 
C2E O2A   HO2A   sing N N 140 
C2E C1A   H1A    sing N N 141 
C2E C81   H81    sing N N 142 
C2E N11   HN11   sing N N 143 
C2E N21   HN24   sing N N 144 
C2E N21   HN23   sing N N 145 
CYS N     CA     sing N N 146 
CYS N     H      sing N N 147 
CYS N     H2     sing N N 148 
CYS CA    C      sing N N 149 
CYS CA    CB     sing N N 150 
CYS CA    HA     sing N N 151 
CYS C     O      doub N N 152 
CYS C     OXT    sing N N 153 
CYS CB    SG     sing N N 154 
CYS CB    HB2    sing N N 155 
CYS CB    HB3    sing N N 156 
CYS SG    HG     sing N N 157 
CYS OXT   HXT    sing N N 158 
GLN N     CA     sing N N 159 
GLN N     H      sing N N 160 
GLN N     H2     sing N N 161 
GLN CA    C      sing N N 162 
GLN CA    CB     sing N N 163 
GLN CA    HA     sing N N 164 
GLN C     O      doub N N 165 
GLN C     OXT    sing N N 166 
GLN CB    CG     sing N N 167 
GLN CB    HB2    sing N N 168 
GLN CB    HB3    sing N N 169 
GLN CG    CD     sing N N 170 
GLN CG    HG2    sing N N 171 
GLN CG    HG3    sing N N 172 
GLN CD    OE1    doub N N 173 
GLN CD    NE2    sing N N 174 
GLN NE2   HE21   sing N N 175 
GLN NE2   HE22   sing N N 176 
GLN OXT   HXT    sing N N 177 
GLU N     CA     sing N N 178 
GLU N     H      sing N N 179 
GLU N     H2     sing N N 180 
GLU CA    C      sing N N 181 
GLU CA    CB     sing N N 182 
GLU CA    HA     sing N N 183 
GLU C     O      doub N N 184 
GLU C     OXT    sing N N 185 
GLU CB    CG     sing N N 186 
GLU CB    HB2    sing N N 187 
GLU CB    HB3    sing N N 188 
GLU CG    CD     sing N N 189 
GLU CG    HG2    sing N N 190 
GLU CG    HG3    sing N N 191 
GLU CD    OE1    doub N N 192 
GLU CD    OE2    sing N N 193 
GLU OE2   HE2    sing N N 194 
GLU OXT   HXT    sing N N 195 
GLY N     CA     sing N N 196 
GLY N     H      sing N N 197 
GLY N     H2     sing N N 198 
GLY CA    C      sing N N 199 
GLY CA    HA2    sing N N 200 
GLY CA    HA3    sing N N 201 
GLY C     O      doub N N 202 
GLY C     OXT    sing N N 203 
GLY OXT   HXT    sing N N 204 
HEM CHA   C1A    sing N N 205 
HEM CHA   C4D    doub N N 206 
HEM CHA   HHA    sing N N 207 
HEM CHB   C4A    sing N N 208 
HEM CHB   C1B    doub N N 209 
HEM CHB   HHB    sing N N 210 
HEM CHC   C4B    sing N N 211 
HEM CHC   C1C    doub N N 212 
HEM CHC   HHC    sing N N 213 
HEM CHD   C4C    doub N N 214 
HEM CHD   C1D    sing N N 215 
HEM CHD   HHD    sing N N 216 
HEM C1A   C2A    doub Y N 217 
HEM C1A   NA     sing Y N 218 
HEM C2A   C3A    sing Y N 219 
HEM C2A   CAA    sing N N 220 
HEM C3A   C4A    doub Y N 221 
HEM C3A   CMA    sing N N 222 
HEM C4A   NA     sing Y N 223 
HEM CMA   HMA    sing N N 224 
HEM CMA   HMAA   sing N N 225 
HEM CMA   HMAB   sing N N 226 
HEM CAA   CBA    sing N N 227 
HEM CAA   HAA    sing N N 228 
HEM CAA   HAAA   sing N N 229 
HEM CBA   CGA    sing N N 230 
HEM CBA   HBA    sing N N 231 
HEM CBA   HBAA   sing N N 232 
HEM CGA   O1A    doub N N 233 
HEM CGA   O2A    sing N N 234 
HEM C1B   C2B    sing N N 235 
HEM C1B   NB     sing N N 236 
HEM C2B   C3B    doub N N 237 
HEM C2B   CMB    sing N N 238 
HEM C3B   C4B    sing N N 239 
HEM C3B   CAB    sing N N 240 
HEM C4B   NB     doub N N 241 
HEM CMB   HMB    sing N N 242 
HEM CMB   HMBA   sing N N 243 
HEM CMB   HMBB   sing N N 244 
HEM CAB   CBB    doub N N 245 
HEM CAB   HAB    sing N N 246 
HEM CBB   HBB    sing N N 247 
HEM CBB   HBBA   sing N N 248 
HEM C1C   C2C    sing Y N 249 
HEM C1C   NC     sing Y N 250 
HEM C2C   C3C    doub Y N 251 
HEM C2C   CMC    sing N N 252 
HEM C3C   C4C    sing Y N 253 
HEM C3C   CAC    sing N N 254 
HEM C4C   NC     sing Y N 255 
HEM CMC   HMC    sing N N 256 
HEM CMC   HMCA   sing N N 257 
HEM CMC   HMCB   sing N N 258 
HEM CAC   CBC    doub N N 259 
HEM CAC   HAC    sing N N 260 
HEM CBC   HBC    sing N N 261 
HEM CBC   HBCA   sing N N 262 
HEM C1D   C2D    sing N N 263 
HEM C1D   ND     doub N N 264 
HEM C2D   C3D    doub N N 265 
HEM C2D   CMD    sing N N 266 
HEM C3D   C4D    sing N N 267 
HEM C3D   CAD    sing N N 268 
HEM C4D   ND     sing N N 269 
HEM CMD   HMD    sing N N 270 
HEM CMD   HMDA   sing N N 271 
HEM CMD   HMDB   sing N N 272 
HEM CAD   CBD    sing N N 273 
HEM CAD   HAD    sing N N 274 
HEM CAD   HADA   sing N N 275 
HEM CBD   CGD    sing N N 276 
HEM CBD   HBD    sing N N 277 
HEM CBD   HBDA   sing N N 278 
HEM CGD   O1D    doub N N 279 
HEM CGD   O2D    sing N N 280 
HEM O2A   H2A    sing N N 281 
HEM O2D   H2D    sing N N 282 
HEM FE    NA     sing N N 283 
HEM FE    NB     sing N N 284 
HEM FE    NC     sing N N 285 
HEM FE    ND     sing N N 286 
HIS N     CA     sing N N 287 
HIS N     H      sing N N 288 
HIS N     H2     sing N N 289 
HIS CA    C      sing N N 290 
HIS CA    CB     sing N N 291 
HIS CA    HA     sing N N 292 
HIS C     O      doub N N 293 
HIS C     OXT    sing N N 294 
HIS CB    CG     sing N N 295 
HIS CB    HB2    sing N N 296 
HIS CB    HB3    sing N N 297 
HIS CG    ND1    sing Y N 298 
HIS CG    CD2    doub Y N 299 
HIS ND1   CE1    doub Y N 300 
HIS ND1   HD1    sing N N 301 
HIS CD2   NE2    sing Y N 302 
HIS CD2   HD2    sing N N 303 
HIS CE1   NE2    sing Y N 304 
HIS CE1   HE1    sing N N 305 
HIS NE2   HE2    sing N N 306 
HIS OXT   HXT    sing N N 307 
ILE N     CA     sing N N 308 
ILE N     H      sing N N 309 
ILE N     H2     sing N N 310 
ILE CA    C      sing N N 311 
ILE CA    CB     sing N N 312 
ILE CA    HA     sing N N 313 
ILE C     O      doub N N 314 
ILE C     OXT    sing N N 315 
ILE CB    CG1    sing N N 316 
ILE CB    CG2    sing N N 317 
ILE CB    HB     sing N N 318 
ILE CG1   CD1    sing N N 319 
ILE CG1   HG12   sing N N 320 
ILE CG1   HG13   sing N N 321 
ILE CG2   HG21   sing N N 322 
ILE CG2   HG22   sing N N 323 
ILE CG2   HG23   sing N N 324 
ILE CD1   HD11   sing N N 325 
ILE CD1   HD12   sing N N 326 
ILE CD1   HD13   sing N N 327 
ILE OXT   HXT    sing N N 328 
LEU N     CA     sing N N 329 
LEU N     H      sing N N 330 
LEU N     H2     sing N N 331 
LEU CA    C      sing N N 332 
LEU CA    CB     sing N N 333 
LEU CA    HA     sing N N 334 
LEU C     O      doub N N 335 
LEU C     OXT    sing N N 336 
LEU CB    CG     sing N N 337 
LEU CB    HB2    sing N N 338 
LEU CB    HB3    sing N N 339 
LEU CG    CD1    sing N N 340 
LEU CG    CD2    sing N N 341 
LEU CG    HG     sing N N 342 
LEU CD1   HD11   sing N N 343 
LEU CD1   HD12   sing N N 344 
LEU CD1   HD13   sing N N 345 
LEU CD2   HD21   sing N N 346 
LEU CD2   HD22   sing N N 347 
LEU CD2   HD23   sing N N 348 
LEU OXT   HXT    sing N N 349 
LYS N     CA     sing N N 350 
LYS N     H      sing N N 351 
LYS N     H2     sing N N 352 
LYS CA    C      sing N N 353 
LYS CA    CB     sing N N 354 
LYS CA    HA     sing N N 355 
LYS C     O      doub N N 356 
LYS C     OXT    sing N N 357 
LYS CB    CG     sing N N 358 
LYS CB    HB2    sing N N 359 
LYS CB    HB3    sing N N 360 
LYS CG    CD     sing N N 361 
LYS CG    HG2    sing N N 362 
LYS CG    HG3    sing N N 363 
LYS CD    CE     sing N N 364 
LYS CD    HD2    sing N N 365 
LYS CD    HD3    sing N N 366 
LYS CE    NZ     sing N N 367 
LYS CE    HE2    sing N N 368 
LYS CE    HE3    sing N N 369 
LYS NZ    HZ1    sing N N 370 
LYS NZ    HZ2    sing N N 371 
LYS NZ    HZ3    sing N N 372 
LYS OXT   HXT    sing N N 373 
MET N     CA     sing N N 374 
MET N     H      sing N N 375 
MET N     H2     sing N N 376 
MET CA    C      sing N N 377 
MET CA    CB     sing N N 378 
MET CA    HA     sing N N 379 
MET C     O      doub N N 380 
MET C     OXT    sing N N 381 
MET CB    CG     sing N N 382 
MET CB    HB2    sing N N 383 
MET CB    HB3    sing N N 384 
MET CG    SD     sing N N 385 
MET CG    HG2    sing N N 386 
MET CG    HG3    sing N N 387 
MET SD    CE     sing N N 388 
MET CE    HE1    sing N N 389 
MET CE    HE2    sing N N 390 
MET CE    HE3    sing N N 391 
MET OXT   HXT    sing N N 392 
PHE N     CA     sing N N 393 
PHE N     H      sing N N 394 
PHE N     H2     sing N N 395 
PHE CA    C      sing N N 396 
PHE CA    CB     sing N N 397 
PHE CA    HA     sing N N 398 
PHE C     O      doub N N 399 
PHE C     OXT    sing N N 400 
PHE CB    CG     sing N N 401 
PHE CB    HB2    sing N N 402 
PHE CB    HB3    sing N N 403 
PHE CG    CD1    doub Y N 404 
PHE CG    CD2    sing Y N 405 
PHE CD1   CE1    sing Y N 406 
PHE CD1   HD1    sing N N 407 
PHE CD2   CE2    doub Y N 408 
PHE CD2   HD2    sing N N 409 
PHE CE1   CZ     doub Y N 410 
PHE CE1   HE1    sing N N 411 
PHE CE2   CZ     sing Y N 412 
PHE CE2   HE2    sing N N 413 
PHE CZ    HZ     sing N N 414 
PHE OXT   HXT    sing N N 415 
PRO N     CA     sing N N 416 
PRO N     CD     sing N N 417 
PRO N     H      sing N N 418 
PRO CA    C      sing N N 419 
PRO CA    CB     sing N N 420 
PRO CA    HA     sing N N 421 
PRO C     O      doub N N 422 
PRO C     OXT    sing N N 423 
PRO CB    CG     sing N N 424 
PRO CB    HB2    sing N N 425 
PRO CB    HB3    sing N N 426 
PRO CG    CD     sing N N 427 
PRO CG    HG2    sing N N 428 
PRO CG    HG3    sing N N 429 
PRO CD    HD2    sing N N 430 
PRO CD    HD3    sing N N 431 
PRO OXT   HXT    sing N N 432 
SER N     CA     sing N N 433 
SER N     H      sing N N 434 
SER N     H2     sing N N 435 
SER CA    C      sing N N 436 
SER CA    CB     sing N N 437 
SER CA    HA     sing N N 438 
SER C     O      doub N N 439 
SER C     OXT    sing N N 440 
SER CB    OG     sing N N 441 
SER CB    HB2    sing N N 442 
SER CB    HB3    sing N N 443 
SER OG    HG     sing N N 444 
SER OXT   HXT    sing N N 445 
THR N     CA     sing N N 446 
THR N     H      sing N N 447 
THR N     H2     sing N N 448 
THR CA    C      sing N N 449 
THR CA    CB     sing N N 450 
THR CA    HA     sing N N 451 
THR C     O      doub N N 452 
THR C     OXT    sing N N 453 
THR CB    OG1    sing N N 454 
THR CB    CG2    sing N N 455 
THR CB    HB     sing N N 456 
THR OG1   HG1    sing N N 457 
THR CG2   HG21   sing N N 458 
THR CG2   HG22   sing N N 459 
THR CG2   HG23   sing N N 460 
THR OXT   HXT    sing N N 461 
TRP N     CA     sing N N 462 
TRP N     H      sing N N 463 
TRP N     H2     sing N N 464 
TRP CA    C      sing N N 465 
TRP CA    CB     sing N N 466 
TRP CA    HA     sing N N 467 
TRP C     O      doub N N 468 
TRP C     OXT    sing N N 469 
TRP CB    CG     sing N N 470 
TRP CB    HB2    sing N N 471 
TRP CB    HB3    sing N N 472 
TRP CG    CD1    doub Y N 473 
TRP CG    CD2    sing Y N 474 
TRP CD1   NE1    sing Y N 475 
TRP CD1   HD1    sing N N 476 
TRP CD2   CE2    doub Y N 477 
TRP CD2   CE3    sing Y N 478 
TRP NE1   CE2    sing Y N 479 
TRP NE1   HE1    sing N N 480 
TRP CE2   CZ2    sing Y N 481 
TRP CE3   CZ3    doub Y N 482 
TRP CE3   HE3    sing N N 483 
TRP CZ2   CH2    doub Y N 484 
TRP CZ2   HZ2    sing N N 485 
TRP CZ3   CH2    sing Y N 486 
TRP CZ3   HZ3    sing N N 487 
TRP CH2   HH2    sing N N 488 
TRP OXT   HXT    sing N N 489 
TYR N     CA     sing N N 490 
TYR N     H      sing N N 491 
TYR N     H2     sing N N 492 
TYR CA    C      sing N N 493 
TYR CA    CB     sing N N 494 
TYR CA    HA     sing N N 495 
TYR C     O      doub N N 496 
TYR C     OXT    sing N N 497 
TYR CB    CG     sing N N 498 
TYR CB    HB2    sing N N 499 
TYR CB    HB3    sing N N 500 
TYR CG    CD1    doub Y N 501 
TYR CG    CD2    sing Y N 502 
TYR CD1   CE1    sing Y N 503 
TYR CD1   HD1    sing N N 504 
TYR CD2   CE2    doub Y N 505 
TYR CD2   HD2    sing N N 506 
TYR CE1   CZ     doub Y N 507 
TYR CE1   HE1    sing N N 508 
TYR CE2   CZ     sing Y N 509 
TYR CE2   HE2    sing N N 510 
TYR CZ    OH     sing N N 511 
TYR OH    HH     sing N N 512 
TYR OXT   HXT    sing N N 513 
VAL N     CA     sing N N 514 
VAL N     H      sing N N 515 
VAL N     H2     sing N N 516 
VAL CA    C      sing N N 517 
VAL CA    CB     sing N N 518 
VAL CA    HA     sing N N 519 
VAL C     O      doub N N 520 
VAL C     OXT    sing N N 521 
VAL CB    CG1    sing N N 522 
VAL CB    CG2    sing N N 523 
VAL CB    HB     sing N N 524 
VAL CG1   HG11   sing N N 525 
VAL CG1   HG12   sing N N 526 
VAL CG1   HG13   sing N N 527 
VAL CG2   HG21   sing N N 528 
VAL CG2   HG22   sing N N 529 
VAL CG2   HG23   sing N N 530 
VAL OXT   HXT    sing N N 531 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-11 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CLO 
_em_admin.last_update        2024-11-27 
_em_admin.map_release_date   2024-11-20 
_em_admin.title              'DosP R97A with c-di-GMP' 
# 
_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_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.2 
# 
_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          562 
_em_entity_assembly_naturalsource.organism             'Escherichia coli' 
_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          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_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         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ?         ?   
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?         ?   
MASKING                         ? 3  ? ? ? ?         ?   
'CTF CORRECTION'                ? 4  1 ? ? ?         ?   
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ?   
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ?   
'MODEL FITTING'                 ? 7  ? ? ? ?         ?   
'MODEL REFINEMENT'              ? 8  ? ? ? ?         ?   
OTHER                           ? 9  ? ? ? ?         ?   
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? cryoSPARC 4.2 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 4.2 
CLASSIFICATION                  ? 12 1 ? ? ?         ?   
RECONSTRUCTION                  ? 13 1 ? ? ?         ?   
'VOLUME SELECTION'              ? 14 1 1 1 ?         ?   
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ?   
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ?   
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ?   
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ?   
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 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 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'R00 GM141261' 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'U24 GM129547' 2 
# 
_atom_sites.entry_id                    9CLO 
_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  
FE 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . GLY A 1 1   ? 166.284 188.312 85.740  1.00 106.98 ?  20  GLY A N     1 
ATOM   2     C  CA    . GLY A 1 1   ? 166.310 188.128 87.179  1.00 105.31 ?  20  GLY A CA    1 
ATOM   3     C  C     . GLY A 1 1   ? 166.796 189.351 87.929  1.00 107.10 ?  20  GLY A C     1 
ATOM   4     O  O     . GLY A 1 1   ? 167.779 189.983 87.539  1.00 107.85 ?  20  GLY A O     1 
ATOM   5     N  N     . ILE A 1 2   ? 166.101 189.686 89.020  1.00 103.65 ?  21  ILE A N     1 
ATOM   6     C  CA    . ILE A 1 2   ? 166.451 190.869 89.803  1.00 103.27 ?  21  ILE A CA    1 
ATOM   7     C  C     . ILE A 1 2   ? 167.474 190.584 90.888  1.00 104.21 ?  21  ILE A C     1 
ATOM   8     O  O     . ILE A 1 2   ? 167.844 191.502 91.631  1.00 105.74 ?  21  ILE A O     1 
ATOM   9     C  CB    . ILE A 1 2   ? 165.195 191.488 90.443  1.00 102.76 ?  21  ILE A CB    1 
ATOM   10    C  CG1   . ILE A 1 2   ? 164.426 190.432 91.238  1.00 103.21 ?  21  ILE A CG1   1 
ATOM   11    C  CG2   . ILE A 1 2   ? 164.302 192.103 89.376  1.00 104.02 ?  21  ILE A CG2   1 
ATOM   12    C  CD1   . ILE A 1 2   ? 163.268 190.997 92.027  1.00 104.23 ?  21  ILE A CD1   1 
ATOM   13    N  N     . PHE A 1 3   ? 167.941 189.340 91.010  1.00 102.71 ?  22  PHE A N     1 
ATOM   14    C  CA    . PHE A 1 3   ? 168.947 189.031 92.019  1.00 102.43 ?  22  PHE A CA    1 
ATOM   15    C  C     . PHE A 1 3   ? 170.320 189.562 91.625  1.00 100.76 ?  22  PHE A C     1 
ATOM   16    O  O     . PHE A 1 3   ? 171.132 189.883 92.500  1.00 98.70  ?  22  PHE A O     1 
ATOM   17    C  CB    . PHE A 1 3   ? 169.003 187.522 92.265  1.00 102.30 ?  22  PHE A CB    1 
ATOM   18    C  CG    . PHE A 1 3   ? 167.832 186.991 93.047  1.00 102.10 ?  22  PHE A CG    1 
ATOM   19    C  CD1   . PHE A 1 3   ? 166.594 186.825 92.446  1.00 102.08 ?  22  PHE A CD1   1 
ATOM   20    C  CD2   . PHE A 1 3   ? 167.970 186.661 94.385  1.00 102.25 ?  22  PHE A CD2   1 
ATOM   21    C  CE1   . PHE A 1 3   ? 165.518 186.337 93.165  1.00 102.29 ?  22  PHE A CE1   1 
ATOM   22    C  CE2   . PHE A 1 3   ? 166.897 186.174 95.109  1.00 103.28 ?  22  PHE A CE2   1 
ATOM   23    C  CZ    . PHE A 1 3   ? 165.670 186.012 94.498  1.00 101.94 ?  22  PHE A CZ    1 
ATOM   24    N  N     . PHE A 1 4   ? 170.600 189.651 90.321  1.00 95.69  ?  23  PHE A N     1 
ATOM   25    C  CA    . PHE A 1 4   ? 171.874 190.209 89.867  1.00 94.32  ?  23  PHE A CA    1 
ATOM   26    C  C     . PHE A 1 4   ? 172.063 191.653 90.323  1.00 96.37  ?  23  PHE A C     1 
ATOM   27    O  O     . PHE A 1 4   ? 173.101 191.958 90.936  1.00 97.12  ?  23  PHE A O     1 
ATOM   28    C  CB    . PHE A 1 4   ? 171.977 190.034 88.346  1.00 93.83  ?  23  PHE A CB    1 
ATOM   29    C  CG    . PHE A 1 4   ? 173.107 190.797 87.707  1.00 97.44  ?  23  PHE A CG    1 
ATOM   30    C  CD1   . PHE A 1 4   ? 174.329 190.185 87.486  1.00 98.48  ?  23  PHE A CD1   1 
ATOM   31    C  CD2   . PHE A 1 4   ? 172.936 192.108 87.287  1.00 97.16  ?  23  PHE A CD2   1 
ATOM   32    C  CE1   . PHE A 1 4   ? 175.369 190.873 86.887  1.00 97.61  ?  23  PHE A CE1   1 
ATOM   33    C  CE2   . PHE A 1 4   ? 173.973 192.801 86.689  1.00 96.56  ?  23  PHE A CE2   1 
ATOM   34    C  CZ    . PHE A 1 4   ? 175.190 192.182 86.489  1.00 96.88  ?  23  PHE A CZ    1 
ATOM   35    N  N     . PRO A 1 5   ? 171.122 192.580 90.088  1.00 99.10  ?  24  PRO A N     1 
ATOM   36    C  CA    . PRO A 1 5   ? 171.285 193.917 90.682  1.00 100.91 ?  24  PRO A CA    1 
ATOM   37    C  C     . PRO A 1 5   ? 171.151 193.909 92.193  1.00 97.18  ?  24  PRO A C     1 
ATOM   38    O  O     . PRO A 1 5   ? 171.746 194.765 92.862  1.00 97.17  ?  24  PRO A O     1 
ATOM   39    C  CB    . PRO A 1 5   ? 170.175 194.742 90.017  1.00 100.40 ?  24  PRO A CB    1 
ATOM   40    C  CG    . PRO A 1 5   ? 169.148 193.749 89.639  1.00 100.24 ?  24  PRO A CG    1 
ATOM   41    C  CD    . PRO A 1 5   ? 169.893 192.499 89.274  1.00 98.23  ?  24  PRO A CD    1 
ATOM   42    N  N     . ALA A 1 6   ? 170.387 192.968 92.752  1.00 96.70  ?  25  ALA A N     1 
ATOM   43    C  CA    . ALA A 1 6   ? 170.300 192.849 94.203  1.00 99.18  ?  25  ALA A CA    1 
ATOM   44    C  C     . ALA A 1 6   ? 171.662 192.525 94.802  1.00 97.69  ?  25  ALA A C     1 
ATOM   45    O  O     . ALA A 1 6   ? 172.067 193.114 95.809  1.00 98.38  ?  25  ALA A O     1 
ATOM   46    C  CB    . ALA A 1 6   ? 169.273 191.782 94.582  1.00 98.25  ?  25  ALA A CB    1 
ATOM   47    N  N     . LEU A 1 7   ? 172.393 191.596 94.184  1.00 91.95  ?  26  LEU A N     1 
ATOM   48    C  CA    . LEU A 1 7   ? 173.744 191.303 94.646  1.00 93.83  ?  26  LEU A CA    1 
ATOM   49    C  C     . LEU A 1 7   ? 174.705 192.440 94.319  1.00 93.86  ?  26  LEU A C     1 
ATOM   50    O  O     . LEU A 1 7   ? 175.685 192.648 95.043  1.00 93.75  ?  26  LEU A O     1 
ATOM   51    C  CB    . LEU A 1 7   ? 174.237 189.990 94.039  1.00 96.14  ?  26  LEU A CB    1 
ATOM   52    C  CG    . LEU A 1 7   ? 173.503 188.731 94.505  1.00 94.56  ?  26  LEU A CG    1 
ATOM   53    C  CD1   . LEU A 1 7   ? 173.755 187.573 93.550  1.00 92.85  ?  26  LEU A CD1   1 
ATOM   54    C  CD2   . LEU A 1 7   ? 173.903 188.360 95.926  1.00 93.13  ?  26  LEU A CD2   1 
ATOM   55    N  N     . GLU A 1 8   ? 174.448 193.174 93.233  1.00 92.34  ?  27  GLU A N     1 
ATOM   56    C  CA    . GLU A 1 8   ? 175.281 194.329 92.907  1.00 94.22  ?  27  GLU A CA    1 
ATOM   57    C  C     . GLU A 1 8   ? 175.188 195.403 93.986  1.00 96.41  ?  27  GLU A C     1 
ATOM   58    O  O     . GLU A 1 8   ? 176.202 195.992 94.378  1.00 97.95  ?  27  GLU A O     1 
ATOM   59    C  CB    . GLU A 1 8   ? 174.875 194.891 91.544  1.00 96.81  ?  27  GLU A CB    1 
ATOM   60    C  CG    . GLU A 1 8   ? 175.905 195.804 90.900  1.00 98.81  ?  27  GLU A CG    1 
ATOM   61    C  CD    . GLU A 1 8   ? 175.790 197.239 91.375  1.00 97.98  ?  27  GLU A CD    1 
ATOM   62    O  OE1   . GLU A 1 8   ? 174.652 197.697 91.613  1.00 95.40  ?  27  GLU A OE1   1 
ATOM   63    O  OE2   . GLU A 1 8   ? 176.834 197.910 91.507  1.00 97.40  -1 27  GLU A OE2   1 
ATOM   64    N  N     . GLN A 1 9   ? 173.981 195.672 94.475  1.00 96.36  ?  28  GLN A N     1 
ATOM   65    C  CA    . GLN A 1 9   ? 173.766 196.667 95.518  1.00 95.21  ?  28  GLN A CA    1 
ATOM   66    C  C     . GLN A 1 9   ? 173.791 196.076 96.922  1.00 94.17  ?  28  GLN A C     1 
ATOM   67    O  O     . GLN A 1 9   ? 173.560 196.806 97.890  1.00 92.45  ?  28  GLN A O     1 
ATOM   68    C  CB    . GLN A 1 9   ? 172.439 197.399 95.288  1.00 95.87  ?  28  GLN A CB    1 
ATOM   69    C  CG    . GLN A 1 9   ? 172.361 198.140 93.962  1.00 95.00  ?  28  GLN A CG    1 
ATOM   70    C  CD    . GLN A 1 9   ? 170.992 198.738 93.706  1.00 95.17  ?  28  GLN A CD    1 
ATOM   71    O  OE1   . GLN A 1 9   ? 170.393 198.520 92.652  1.00 97.22  ?  28  GLN A OE1   1 
ATOM   72    N  NE2   . GLN A 1 9   ? 170.486 199.494 94.673  1.00 93.29  ?  28  GLN A NE2   1 
ATOM   73    N  N     . ASN A 1 10  ? 174.059 194.781 97.054  1.00 87.62  ?  29  ASN A N     1 
ATOM   74    C  CA    . ASN A 1 10  ? 174.068 194.121 98.348  1.00 84.19  ?  29  ASN A CA    1 
ATOM   75    C  C     . ASN A 1 10  ? 175.342 194.444 99.125  1.00 80.73  ?  29  ASN A C     1 
ATOM   76    O  O     . ASN A 1 10  ? 176.319 194.972 98.587  1.00 82.21  ?  29  ASN A O     1 
ATOM   77    C  CB    . ASN A 1 10  ? 173.939 192.608 98.172  1.00 82.79  ?  29  ASN A CB    1 
ATOM   78    C  CG    . ASN A 1 10  ? 173.441 191.916 99.422  1.00 82.91  ?  29  ASN A CG    1 
ATOM   79    O  OD1   . ASN A 1 10  ? 172.812 192.534 100.280 1.00 82.35  ?  29  ASN A OD1   1 
ATOM   80    N  ND2   . ASN A 1 10  ? 173.736 190.629 99.539  1.00 84.06  ?  29  ASN A ND2   1 
ATOM   81    N  N     . MET A 1 11  ? 175.315 194.113 100.418 1.00 71.88  ?  30  MET A N     1 
ATOM   82    C  CA    . MET A 1 11  ? 176.493 194.265 101.264 1.00 71.78  ?  30  MET A CA    1 
ATOM   83    C  C     . MET A 1 11  ? 177.402 193.045 101.194 1.00 77.37  ?  30  MET A C     1 
ATOM   84    O  O     . MET A 1 11  ? 178.621 193.175 101.353 1.00 76.72  ?  30  MET A O     1 
ATOM   85    C  CB    . MET A 1 11  ? 176.068 194.518 102.711 1.00 72.58  ?  30  MET A CB    1 
ATOM   86    C  CG    . MET A 1 11  ? 177.187 194.989 103.621 1.00 75.42  ?  30  MET A CG    1 
ATOM   87    S  SD    . MET A 1 11  ? 177.070 194.274 105.272 1.00 75.20  ?  30  MET A SD    1 
ATOM   88    C  CE    . MET A 1 11  ? 178.037 192.781 105.063 1.00 74.06  ?  30  MET A CE    1 
ATOM   89    N  N     . MET A 1 12  ? 176.834 191.866 100.957 1.00 80.49  ?  31  MET A N     1 
ATOM   90    C  CA    . MET A 1 12  ? 177.614 190.647 100.835 1.00 75.94  ?  31  MET A CA    1 
ATOM   91    C  C     . MET A 1 12  ? 178.302 190.596 99.473  1.00 77.97  ?  31  MET A C     1 
ATOM   92    O  O     . MET A 1 12  ? 177.995 191.368 98.561  1.00 80.50  ?  31  MET A O     1 
ATOM   93    C  CB    . MET A 1 12  ? 176.721 189.422 101.022 1.00 74.76  ?  31  MET A CB    1 
ATOM   94    C  CG    . MET A 1 12  ? 175.831 189.481 102.252 1.00 77.35  ?  31  MET A CG    1 
ATOM   95    S  SD    . MET A 1 12  ? 176.726 189.177 103.783 1.00 83.21  ?  31  MET A SD    1 
ATOM   96    C  CE    . MET A 1 12  ? 176.017 187.611 104.285 1.00 74.80  ?  31  MET A CE    1 
ATOM   97    N  N     . GLY A 1 13  ? 179.245 189.668 99.335  1.00 65.56  ?  32  GLY A N     1 
ATOM   98    C  CA    . GLY A 1 13  ? 179.932 189.450 98.079  1.00 64.33  ?  32  GLY A CA    1 
ATOM   99    C  C     . GLY A 1 13  ? 179.503 188.144 97.439  1.00 61.24  ?  32  GLY A C     1 
ATOM   100   O  O     . GLY A 1 13  ? 179.521 187.093 98.070  1.00 61.28  ?  32  GLY A O     1 
ATOM   101   N  N     . ALA A 1 14  ? 179.107 188.219 96.172  1.00 66.90  ?  33  ALA A N     1 
ATOM   102   C  CA    . ALA A 1 14  ? 178.664 187.038 95.438  1.00 67.33  ?  33  ALA A CA    1 
ATOM   103   C  C     . ALA A 1 14  ? 179.702 186.721 94.372  1.00 69.52  ?  33  ALA A C     1 
ATOM   104   O  O     . ALA A 1 14  ? 179.972 187.550 93.498  1.00 73.72  ?  33  ALA A O     1 
ATOM   105   C  CB    . ALA A 1 14  ? 177.284 187.253 94.817  1.00 67.58  ?  33  ALA A CB    1 
ATOM   106   N  N     . VAL A 1 15  ? 180.282 185.530 94.448  1.00 62.70  ?  34  VAL A N     1 
ATOM   107   C  CA    . VAL A 1 15  ? 181.267 185.059 93.476  1.00 60.42  ?  34  VAL A CA    1 
ATOM   108   C  C     . VAL A 1 15  ? 180.743 183.730 92.945  1.00 58.81  ?  34  VAL A C     1 
ATOM   109   O  O     . VAL A 1 15  ? 180.961 182.670 93.539  1.00 65.01  ?  34  VAL A O     1 
ATOM   110   C  CB    . VAL A 1 15  ? 182.667 184.913 94.079  1.00 63.97  ?  34  VAL A CB    1 
ATOM   111   C  CG1   . VAL A 1 15  ? 183.680 184.590 92.992  1.00 65.05  ?  34  VAL A CG1   1 
ATOM   112   C  CG2   . VAL A 1 15  ? 183.065 186.179 94.822  1.00 62.75  ?  34  VAL A CG2   1 
ATOM   113   N  N     . LEU A 1 16  ? 180.042 183.778 91.816  1.00 66.78  ?  35  LEU A N     1 
ATOM   114   C  CA    . LEU A 1 16  ? 179.463 182.585 91.215  1.00 71.78  ?  35  LEU A CA    1 
ATOM   115   C  C     . LEU A 1 16  ? 180.410 182.033 90.157  1.00 80.03  ?  35  LEU A C     1 
ATOM   116   O  O     . LEU A 1 16  ? 180.864 182.768 89.274  1.00 87.87  ?  35  LEU A O     1 
ATOM   117   C  CB    . LEU A 1 16  ? 178.099 182.899 90.600  1.00 74.00  ?  35  LEU A CB    1 
ATOM   118   C  CG    . LEU A 1 16  ? 177.403 181.766 89.843  1.00 77.15  ?  35  LEU A CG    1 
ATOM   119   C  CD1   . LEU A 1 16  ? 176.650 180.861 90.805  1.00 78.47  ?  35  LEU A CD1   1 
ATOM   120   C  CD2   . LEU A 1 16  ? 176.462 182.328 88.788  1.00 77.01  ?  35  LEU A CD2   1 
ATOM   121   N  N     . ILE A 1 17  ? 180.702 180.738 90.252  1.00 84.93  ?  36  ILE A N     1 
ATOM   122   C  CA    . ILE A 1 17  ? 181.628 180.063 89.351  1.00 82.96  ?  36  ILE A CA    1 
ATOM   123   C  C     . ILE A 1 17  ? 180.868 179.007 88.558  1.00 83.93  ?  36  ILE A C     1 
ATOM   124   O  O     . ILE A 1 17  ? 179.953 178.352 89.077  1.00 87.72  ?  36  ILE A O     1 
ATOM   125   C  CB    . ILE A 1 17  ? 182.822 179.445 90.107  1.00 88.08  ?  36  ILE A CB    1 
ATOM   126   C  CG1   . ILE A 1 17  ? 182.406 178.188 90.873  1.00 89.35  ?  36  ILE A CG1   1 
ATOM   127   C  CG2   . ILE A 1 17  ? 183.436 180.466 91.054  1.00 88.70  ?  36  ILE A CG2   1 
ATOM   128   C  CD1   . ILE A 1 17  ? 183.563 177.276 91.221  1.00 87.85  ?  36  ILE A CD1   1 
ATOM   129   N  N     . ASN A 1 18  ? 181.238 178.873 87.286  1.00 98.39  ?  37  ASN A N     1 
ATOM   130   C  CA    . ASN A 1 18  ? 180.616 177.958 86.340  1.00 101.29 ?  37  ASN A CA    1 
ATOM   131   C  C     . ASN A 1 18  ? 181.377 176.629 86.332  1.00 100.82 ?  37  ASN A C     1 
ATOM   132   O  O     . ASN A 1 18  ? 182.164 176.343 87.238  1.00 101.53 ?  37  ASN A O     1 
ATOM   133   C  CB    . ASN A 1 18  ? 180.549 178.613 84.956  1.00 101.56 ?  37  ASN A CB    1 
ATOM   134   C  CG    . ASN A 1 18  ? 181.902 179.110 84.476  1.00 101.96 ?  37  ASN A CG    1 
ATOM   135   O  OD1   . ASN A 1 18  ? 182.939 178.786 85.053  1.00 100.03 ?  37  ASN A OD1   1 
ATOM   136   N  ND2   . ASN A 1 18  ? 181.893 179.903 83.411  1.00 101.94 ?  37  ASN A ND2   1 
ATOM   137   N  N     . GLU A 1 19  ? 181.135 175.802 85.311  1.00 100.40 ?  38  GLU A N     1 
ATOM   138   C  CA    . GLU A 1 19  ? 181.773 174.490 85.230  1.00 102.30 ?  38  GLU A CA    1 
ATOM   139   C  C     . GLU A 1 19  ? 183.292 174.603 85.180  1.00 103.03 ?  38  GLU A C     1 
ATOM   140   O  O     . GLU A 1 19  ? 184.000 173.840 85.848  1.00 101.66 ?  38  GLU A O     1 
ATOM   141   C  CB    . GLU A 1 19  ? 181.258 173.738 84.003  1.00 102.35 ?  38  GLU A CB    1 
ATOM   142   C  CG    . GLU A 1 19  ? 179.849 173.193 84.143  1.00 101.57 ?  38  GLU A CG    1 
ATOM   143   C  CD    . GLU A 1 19  ? 179.792 171.943 84.997  1.00 105.89 ?  38  GLU A CD    1 
ATOM   144   O  OE1   . GLU A 1 19  ? 180.730 171.123 84.915  1.00 104.90 ?  38  GLU A OE1   1 
ATOM   145   O  OE2   . GLU A 1 19  ? 178.810 171.778 85.751  1.00 108.29 -1 38  GLU A OE2   1 
ATOM   146   N  N     . ASN A 1 20  ? 183.813 175.546 84.396  1.00 107.81 ?  39  ASN A N     1 
ATOM   147   C  CA    . ASN A 1 20  ? 185.247 175.675 84.176  1.00 110.34 ?  39  ASN A CA    1 
ATOM   148   C  C     . ASN A 1 20  ? 185.936 176.535 85.230  1.00 109.05 ?  39  ASN A C     1 
ATOM   149   O  O     . ASN A 1 20  ? 187.020 177.069 84.965  1.00 110.16 ?  39  ASN A O     1 
ATOM   150   C  CB    . ASN A 1 20  ? 185.515 176.244 82.780  1.00 110.21 ?  39  ASN A CB    1 
ATOM   151   C  CG    . ASN A 1 20  ? 184.966 175.362 81.677  1.00 109.42 ?  39  ASN A CG    1 
ATOM   152   O  OD1   . ASN A 1 20  ? 184.177 175.808 80.844  1.00 109.57 ?  39  ASN A OD1   1 
ATOM   153   N  ND2   . ASN A 1 20  ? 185.382 174.101 81.665  1.00 109.60 ?  39  ASN A ND2   1 
ATOM   154   N  N     . ASP A 1 21  ? 185.334 176.679 86.413  1.00 108.72 ?  40  ASP A N     1 
ATOM   155   C  CA    . ASP A 1 21  ? 185.902 177.466 87.509  1.00 109.18 ?  40  ASP A CA    1 
ATOM   156   C  C     . ASP A 1 21  ? 186.177 178.908 87.092  1.00 110.39 ?  40  ASP A C     1 
ATOM   157   O  O     . ASP A 1 21  ? 187.156 179.517 87.530  1.00 111.53 ?  40  ASP A O     1 
ATOM   158   C  CB    . ASP A 1 21  ? 187.175 176.818 88.062  1.00 107.95 ?  40  ASP A CB    1 
ATOM   159   C  CG    . ASP A 1 21  ? 186.955 175.387 88.509  1.00 109.83 ?  40  ASP A CG    1 
ATOM   160   O  OD1   . ASP A 1 21  ? 185.876 175.097 89.069  1.00 111.57 ?  40  ASP A OD1   1 
ATOM   161   O  OD2   . ASP A 1 21  ? 187.859 174.551 88.301  1.00 109.72 -1 40  ASP A OD2   1 
ATOM   162   N  N     . GLU A 1 22  ? 185.317 179.463 86.244  1.00 109.25 ?  41  GLU A N     1 
ATOM   163   C  CA    . GLU A 1 22  ? 185.431 180.844 85.801  1.00 109.29 ?  41  GLU A CA    1 
ATOM   164   C  C     . GLU A 1 22  ? 184.415 181.706 86.537  1.00 108.19 ?  41  GLU A C     1 
ATOM   165   O  O     . GLU A 1 22  ? 183.249 181.326 86.681  1.00 108.79 ?  41  GLU A O     1 
ATOM   166   C  CB    . GLU A 1 22  ? 185.220 180.956 84.290  1.00 106.80 ?  41  GLU A CB    1 
ATOM   167   C  CG    . GLU A 1 22  ? 186.385 180.441 83.461  1.00 107.17 ?  41  GLU A CG    1 
ATOM   168   C  CD    . GLU A 1 22  ? 185.961 179.984 82.079  1.00 110.21 ?  41  GLU A CD    1 
ATOM   169   O  OE1   . GLU A 1 22  ? 184.882 180.408 81.616  1.00 110.13 ?  41  GLU A OE1   1 
ATOM   170   O  OE2   . GLU A 1 22  ? 186.709 179.202 81.455  1.00 110.13 -1 41  GLU A OE2   1 
ATOM   171   N  N     . VAL A 1 23  ? 184.866 182.864 87.007  1.00 98.25  ?  42  VAL A N     1 
ATOM   172   C  CA    . VAL A 1 23  ? 184.015 183.768 87.773  1.00 98.76  ?  42  VAL A CA    1 
ATOM   173   C  C     . VAL A 1 23  ? 183.059 184.469 86.816  1.00 97.04  ?  42  VAL A C     1 
ATOM   174   O  O     . VAL A 1 23  ? 183.488 185.208 85.923  1.00 100.17 ?  42  VAL A O     1 
ATOM   175   C  CB    . VAL A 1 23  ? 184.857 184.781 88.560  1.00 99.84  ?  42  VAL A CB    1 
ATOM   176   C  CG1   . VAL A 1 23  ? 183.966 185.657 89.420  1.00 100.98 ?  42  VAL A CG1   1 
ATOM   177   C  CG2   . VAL A 1 23  ? 185.889 184.059 89.415  1.00 98.84  ?  42  VAL A CG2   1 
ATOM   178   N  N     . MET A 1 24  ? 181.759 184.239 87.001  1.00 91.25  ?  43  MET A N     1 
ATOM   179   C  CA    . MET A 1 24  ? 180.736 184.802 86.132  1.00 90.44  ?  43  MET A CA    1 
ATOM   180   C  C     . MET A 1 24  ? 179.981 185.964 86.763  1.00 92.99  ?  43  MET A C     1 
ATOM   181   O  O     . MET A 1 24  ? 179.102 186.539 86.111  1.00 97.92  ?  43  MET A O     1 
ATOM   182   C  CB    . MET A 1 24  ? 179.745 183.712 85.710  1.00 94.16  ?  43  MET A CB    1 
ATOM   183   C  CG    . MET A 1 24  ? 180.401 182.391 85.344  1.00 96.59  ?  43  MET A CG    1 
ATOM   184   S  SD    . MET A 1 24  ? 181.720 182.587 84.130  1.00 104.81 ?  43  MET A SD    1 
ATOM   185   C  CE    . MET A 1 24  ? 180.794 183.161 82.710  1.00 98.05  ?  43  MET A CE    1 
ATOM   186   N  N     . PHE A 1 25  ? 180.292 186.325 88.005  1.00 82.49  ?  44  PHE A N     1 
ATOM   187   C  CA    . PHE A 1 25  ? 179.691 187.494 88.630  1.00 83.87  ?  44  PHE A CA    1 
ATOM   188   C  C     . PHE A 1 25  ? 180.675 188.073 89.634  1.00 82.57  ?  44  PHE A C     1 
ATOM   189   O  O     . PHE A 1 25  ? 181.420 187.340 90.288  1.00 85.13  ?  44  PHE A O     1 
ATOM   190   C  CB    . PHE A 1 25  ? 178.360 187.162 89.314  1.00 85.49  ?  44  PHE A CB    1 
ATOM   191   C  CG    . PHE A 1 25  ? 177.759 188.320 90.058  1.00 86.85  ?  44  PHE A CG    1 
ATOM   192   C  CD1   . PHE A 1 25  ? 177.175 189.370 89.371  1.00 85.90  ?  44  PHE A CD1   1 
ATOM   193   C  CD2   . PHE A 1 25  ? 177.779 188.362 91.440  1.00 87.21  ?  44  PHE A CD2   1 
ATOM   194   C  CE1   . PHE A 1 25  ? 176.625 190.440 90.048  1.00 86.64  ?  44  PHE A CE1   1 
ATOM   195   C  CE2   . PHE A 1 25  ? 177.228 189.431 92.122  1.00 84.52  ?  44  PHE A CE2   1 
ATOM   196   C  CZ    . PHE A 1 25  ? 176.650 190.470 91.425  1.00 86.70  ?  44  PHE A CZ    1 
ATOM   197   N  N     . PHE A 1 26  ? 180.659 189.400 89.761  1.00 90.85  ?  45  PHE A N     1 
ATOM   198   C  CA    . PHE A 1 26  ? 181.608 190.097 90.628  1.00 94.81  ?  45  PHE A CA    1 
ATOM   199   C  C     . PHE A 1 26  ? 180.923 191.363 91.136  1.00 98.67  ?  45  PHE A C     1 
ATOM   200   O  O     . PHE A 1 26  ? 180.838 192.359 90.412  1.00 100.62 ?  45  PHE A O     1 
ATOM   201   C  CB    . PHE A 1 26  ? 182.894 190.418 89.878  1.00 99.14  ?  45  PHE A CB    1 
ATOM   202   C  CG    . PHE A 1 26  ? 184.116 190.439 90.749  1.00 98.74  ?  45  PHE A CG    1 
ATOM   203   C  CD1   . PHE A 1 26  ? 184.524 189.300 91.422  1.00 95.15  ?  45  PHE A CD1   1 
ATOM   204   C  CD2   . PHE A 1 26  ? 184.862 191.598 90.889  1.00 99.79  ?  45  PHE A CD2   1 
ATOM   205   C  CE1   . PHE A 1 26  ? 185.651 189.316 92.222  1.00 97.66  ?  45  PHE A CE1   1 
ATOM   206   C  CE2   . PHE A 1 26  ? 185.990 191.621 91.688  1.00 100.51 ?  45  PHE A CE2   1 
ATOM   207   C  CZ    . PHE A 1 26  ? 186.384 190.478 92.355  1.00 100.23 ?  45  PHE A CZ    1 
ATOM   208   N  N     . ASN A 1 27  ? 180.439 191.313 92.373  1.00 95.59  ?  46  ASN A N     1 
ATOM   209   C  CA    . ASN A 1 27  ? 179.765 192.451 92.973  1.00 95.76  ?  46  ASN A CA    1 
ATOM   210   C  C     . ASN A 1 27  ? 180.780 193.475 93.475  1.00 94.99  ?  46  ASN A C     1 
ATOM   211   O  O     . ASN A 1 27  ? 181.950 193.150 93.689  1.00 98.38  ?  46  ASN A O     1 
ATOM   212   C  CB    . ASN A 1 27  ? 178.858 191.984 94.110  1.00 96.28  ?  46  ASN A CB    1 
ATOM   213   C  CG    . ASN A 1 27  ? 179.609 191.758 95.405  1.00 94.93  ?  46  ASN A CG    1 
ATOM   214   O  OD1   . ASN A 1 27  ? 180.711 191.210 95.415  1.00 92.09  ?  46  ASN A OD1   1 
ATOM   215   N  ND2   . ASN A 1 27  ? 179.012 192.185 96.511  1.00 94.99  ?  46  ASN A ND2   1 
ATOM   216   N  N     . PRO A 1 28  ? 180.358 194.731 93.654  1.00 97.14  ?  47  PRO A N     1 
ATOM   217   C  CA    . PRO A 1 28  ? 181.305 195.765 94.108  1.00 97.68  ?  47  PRO A CA    1 
ATOM   218   C  C     . PRO A 1 28  ? 181.979 195.456 95.435  1.00 96.85  ?  47  PRO A C     1 
ATOM   219   O  O     . PRO A 1 28  ? 183.140 195.839 95.624  1.00 97.06  ?  47  PRO A O     1 
ATOM   220   C  CB    . PRO A 1 28  ? 180.426 197.019 94.202  1.00 96.99  ?  47  PRO A CB    1 
ATOM   221   C  CG    . PRO A 1 28  ? 179.357 196.788 93.198  1.00 97.15  ?  47  PRO A CG    1 
ATOM   222   C  CD    . PRO A 1 28  ? 179.072 195.314 93.230  1.00 98.47  ?  47  PRO A CD    1 
ATOM   223   N  N     . ALA A 1 29  ? 181.296 194.782 96.364  1.00 98.07  ?  48  ALA A N     1 
ATOM   224   C  CA    . ALA A 1 29  ? 181.928 194.437 97.633  1.00 97.74  ?  48  ALA A CA    1 
ATOM   225   C  C     . ALA A 1 29  ? 183.079 193.455 97.456  1.00 100.07 ?  48  ALA A C     1 
ATOM   226   O  O     . ALA A 1 29  ? 183.963 193.390 98.318  1.00 101.91 ?  48  ALA A O     1 
ATOM   227   C  CB    . ALA A 1 29  ? 180.896 193.863 98.603  1.00 96.46  ?  48  ALA A CB    1 
ATOM   228   N  N     . ALA A 1 30  ? 183.091 192.694 96.359  1.00 105.10 ?  49  ALA A N     1 
ATOM   229   C  CA    . ALA A 1 30  ? 184.226 191.822 96.083  1.00 105.64 ?  49  ALA A CA    1 
ATOM   230   C  C     . ALA A 1 30  ? 185.494 192.625 95.833  1.00 103.46 ?  49  ALA A C     1 
ATOM   231   O  O     . ALA A 1 30  ? 186.596 192.149 96.124  1.00 103.31 ?  49  ALA A O     1 
ATOM   232   C  CB    . ALA A 1 30  ? 183.921 190.918 94.889  1.00 103.20 ?  49  ALA A CB    1 
ATOM   233   N  N     . GLU A 1 31  ? 185.362 193.839 95.291  1.00 104.20 ?  50  GLU A N     1 
ATOM   234   C  CA    . GLU A 1 31  ? 186.526 194.705 95.128  1.00 104.57 ?  50  GLU A CA    1 
ATOM   235   C  C     . GLU A 1 31  ? 187.125 195.080 96.478  1.00 104.70 ?  50  GLU A C     1 
ATOM   236   O  O     . GLU A 1 31  ? 188.350 195.104 96.637  1.00 107.98 ?  50  GLU A O     1 
ATOM   237   C  CB    . GLU A 1 31  ? 186.145 195.960 94.343  1.00 105.25 ?  50  GLU A CB    1 
ATOM   238   C  CG    . GLU A 1 31  ? 185.422 195.686 93.035  1.00 107.65 ?  50  GLU A CG    1 
ATOM   239   C  CD    . GLU A 1 31  ? 184.539 196.842 92.606  1.00 108.09 ?  50  GLU A CD    1 
ATOM   240   O  OE1   . GLU A 1 31  ? 184.772 197.976 93.076  1.00 107.25 ?  50  GLU A OE1   1 
ATOM   241   O  OE2   . GLU A 1 31  ? 183.616 196.619 91.795  1.00 108.60 -1 50  GLU A OE2   1 
ATOM   242   N  N     . LYS A 1 32  ? 186.275 195.383 97.462  1.00 101.61 ?  51  LYS A N     1 
ATOM   243   C  CA    . LYS A 1 32  ? 186.775 195.687 98.798  1.00 103.06 ?  51  LYS A CA    1 
ATOM   244   C  C     . LYS A 1 32  ? 187.338 194.446 99.478  1.00 102.69 ?  51  LYS A C     1 
ATOM   245   O  O     . LYS A 1 32  ? 188.313 194.540 100.232 1.00 103.72 ?  51  LYS A O     1 
ATOM   246   C  CB    . LYS A 1 32  ? 185.663 196.298 99.650  1.00 103.41 ?  51  LYS A CB    1 
ATOM   247   C  CG    . LYS A 1 32  ? 185.216 197.678 99.199  1.00 104.00 ?  51  LYS A CG    1 
ATOM   248   C  CD    . LYS A 1 32  ? 183.945 197.596 98.370  1.00 104.83 ?  51  LYS A CD    1 
ATOM   249   C  CE    . LYS A 1 32  ? 183.234 198.938 98.309  1.00 103.50 ?  51  LYS A CE    1 
ATOM   250   N  NZ    . LYS A 1 32  ? 182.111 198.927 97.332  1.00 102.28 1  51  LYS A NZ    1 
ATOM   251   N  N     . LEU A 1 33  ? 186.739 193.282 99.226  1.00 99.22  ?  52  LEU A N     1 
ATOM   252   C  CA    . LEU A 1 33  ? 187.190 192.046 99.854  1.00 100.77 ?  52  LEU A CA    1 
ATOM   253   C  C     . LEU A 1 33  ? 188.485 191.507 99.258  1.00 102.09 ?  52  LEU A C     1 
ATOM   254   O  O     . LEU A 1 33  ? 189.228 190.811 99.957  1.00 100.81 ?  52  LEU A O     1 
ATOM   255   C  CB    . LEU A 1 33  ? 186.098 190.978 99.748  1.00 100.58 ?  52  LEU A CB    1 
ATOM   256   C  CG    . LEU A 1 33  ? 184.929 191.107 100.727 1.00 100.43 ?  52  LEU A CG    1 
ATOM   257   C  CD1   . LEU A 1 33  ? 183.793 190.177 100.332 1.00 99.77  ?  52  LEU A CD1   1 
ATOM   258   C  CD2   . LEU A 1 33  ? 185.386 190.825 102.150 1.00 98.16  ?  52  LEU A CD2   1 
ATOM   259   N  N     . TRP A 1 34  ? 188.768 191.802 97.989  1.00 105.69 ?  53  TRP A N     1 
ATOM   260   C  CA    . TRP A 1 34  ? 189.922 191.237 97.298  1.00 104.17 ?  53  TRP A CA    1 
ATOM   261   C  C     . TRP A 1 34  ? 190.875 192.261 96.700  1.00 101.30 ?  53  TRP A C     1 
ATOM   262   O  O     . TRP A 1 34  ? 192.018 191.898 96.400  1.00 101.80 ?  53  TRP A O     1 
ATOM   263   C  CB    . TRP A 1 34  ? 189.465 190.297 96.171  1.00 103.88 ?  53  TRP A CB    1 
ATOM   264   C  CG    . TRP A 1 34  ? 189.042 188.939 96.635  1.00 103.15 ?  53  TRP A CG    1 
ATOM   265   C  CD1   . TRP A 1 34  ? 189.859 187.896 96.954  1.00 102.90 ?  53  TRP A CD1   1 
ATOM   266   C  CD2   . TRP A 1 34  ? 187.700 188.470 96.825  1.00 102.37 ?  53  TRP A CD2   1 
ATOM   267   N  NE1   . TRP A 1 34  ? 189.113 186.807 97.328  1.00 105.09 ?  53  TRP A NE1   1 
ATOM   268   C  CE2   . TRP A 1 34  ? 187.784 187.134 97.262  1.00 105.17 ?  53  TRP A CE2   1 
ATOM   269   C  CE3   . TRP A 1 34  ? 186.438 189.050 96.671  1.00 100.87 ?  53  TRP A CE3   1 
ATOM   270   C  CZ2   . TRP A 1 34  ? 186.656 186.367 97.546  1.00 104.65 ?  53  TRP A CZ2   1 
ATOM   271   C  CZ3   . TRP A 1 34  ? 185.317 188.287 96.954  1.00 102.25 ?  53  TRP A CZ3   1 
ATOM   272   C  CH2   . TRP A 1 34  ? 185.435 186.961 97.387  1.00 104.06 ?  53  TRP A CH2   1 
ATOM   273   N  N     . GLY A 1 35  ? 190.462 193.509 96.517  1.00 99.78  ?  54  GLY A N     1 
ATOM   274   C  CA    . GLY A 1 35  ? 191.280 194.447 95.768  1.00 98.14  ?  54  GLY A CA    1 
ATOM   275   C  C     . GLY A 1 35  ? 191.376 194.097 94.299  1.00 95.00  ?  54  GLY A C     1 
ATOM   276   O  O     . GLY A 1 35  ? 192.447 194.248 93.696  1.00 97.63  ?  54  GLY A O     1 
ATOM   277   N  N     . TYR A 1 36  ? 190.281 193.635 93.708  1.00 95.25  ?  55  TYR A N     1 
ATOM   278   C  CA    . TYR A 1 36  ? 190.217 193.240 92.308  1.00 99.39  ?  55  TYR A CA    1 
ATOM   279   C  C     . TYR A 1 36  ? 189.209 194.129 91.579  1.00 100.60 ?  55  TYR A C     1 
ATOM   280   O  O     . TYR A 1 36  ? 188.673 195.090 92.138  1.00 100.30 ?  55  TYR A O     1 
ATOM   281   C  CB    . TYR A 1 36  ? 189.845 191.760 92.182  1.00 101.32 ?  55  TYR A CB    1 
ATOM   282   C  CG    . TYR A 1 36  ? 190.977 190.798 92.466  1.00 101.15 ?  55  TYR A CG    1 
ATOM   283   C  CD1   . TYR A 1 36  ? 192.296 191.228 92.489  1.00 99.99  ?  55  TYR A CD1   1 
ATOM   284   C  CD2   . TYR A 1 36  ? 190.723 189.454 92.707  1.00 102.36 ?  55  TYR A CD2   1 
ATOM   285   C  CE1   . TYR A 1 36  ? 193.330 190.346 92.747  1.00 98.87  ?  55  TYR A CE1   1 
ATOM   286   C  CE2   . TYR A 1 36  ? 191.749 188.566 92.966  1.00 101.10 ?  55  TYR A CE2   1 
ATOM   287   C  CZ    . TYR A 1 36  ? 193.051 189.017 92.985  1.00 100.35 ?  55  TYR A CZ    1 
ATOM   288   O  OH    . TYR A 1 36  ? 194.075 188.134 93.243  1.00 101.14 ?  55  TYR A OH    1 
ATOM   289   N  N     . LYS A 1 37  ? 188.953 193.796 90.316  1.00 109.54 ?  56  LYS A N     1 
ATOM   290   C  CA    . LYS A 1 37  ? 187.981 194.514 89.506  1.00 108.69 ?  56  LYS A CA    1 
ATOM   291   C  C     . LYS A 1 37  ? 187.184 193.518 88.676  1.00 108.89 ?  56  LYS A C     1 
ATOM   292   O  O     . LYS A 1 37  ? 187.671 192.435 88.339  1.00 108.23 ?  56  LYS A O     1 
ATOM   293   C  CB    . LYS A 1 37  ? 188.654 195.545 88.590  1.00 109.38 ?  56  LYS A CB    1 
ATOM   294   C  CG    . LYS A 1 37  ? 189.165 196.777 89.318  1.00 108.75 ?  56  LYS A CG    1 
ATOM   295   C  CD    . LYS A 1 37  ? 188.022 197.711 89.681  1.00 107.48 ?  56  LYS A CD    1 
ATOM   296   C  CE    . LYS A 1 37  ? 188.454 198.747 90.705  1.00 108.66 ?  56  LYS A CE    1 
ATOM   297   N  NZ    . LYS A 1 37  ? 187.340 199.671 91.057  1.00 107.72 1  56  LYS A NZ    1 
ATOM   298   N  N     . ARG A 1 38  ? 185.945 193.899 88.354  1.00 111.35 ?  57  ARG A N     1 
ATOM   299   C  CA    . ARG A 1 38  ? 185.089 193.022 87.564  1.00 111.31 ?  57  ARG A CA    1 
ATOM   300   C  C     . ARG A 1 38  ? 185.667 192.793 86.172  1.00 112.49 ?  57  ARG A C     1 
ATOM   301   O  O     . ARG A 1 38  ? 185.585 191.683 85.636  1.00 110.81 ?  57  ARG A O     1 
ATOM   302   C  CB    . ARG A 1 38  ? 183.671 193.596 87.490  1.00 109.67 ?  57  ARG A CB    1 
ATOM   303   C  CG    . ARG A 1 38  ? 183.547 194.916 86.748  1.00 111.22 ?  57  ARG A CG    1 
ATOM   304   C  CD    . ARG A 1 38  ? 182.222 195.592 87.055  1.00 110.47 ?  57  ARG A CD    1 
ATOM   305   N  NE    . ARG A 1 38  ? 182.220 196.206 88.377  1.00 112.53 ?  57  ARG A NE    1 
ATOM   306   C  CZ    . ARG A 1 38  ? 181.128 196.596 89.021  1.00 112.44 ?  57  ARG A CZ    1 
ATOM   307   N  NH1   . ARG A 1 38  ? 179.925 196.451 88.491  1.00 111.63 1  57  ARG A NH1   1 
ATOM   308   N  NH2   . ARG A 1 38  ? 181.247 197.144 90.227  1.00 111.59 ?  57  ARG A NH2   1 
ATOM   309   N  N     . GLU A 1 39  ? 186.270 193.824 85.577  1.00 121.39 ?  58  GLU A N     1 
ATOM   310   C  CA    . GLU A 1 39  ? 186.935 193.640 84.291  1.00 120.75 ?  58  GLU A CA    1 
ATOM   311   C  C     . GLU A 1 39  ? 188.117 192.688 84.419  1.00 120.17 ?  58  GLU A C     1 
ATOM   312   O  O     . GLU A 1 39  ? 188.388 191.893 83.511  1.00 121.32 ?  58  GLU A O     1 
ATOM   313   C  CB    . GLU A 1 39  ? 187.387 194.990 83.734  1.00 119.88 ?  58  GLU A CB    1 
ATOM   314   C  CG    . GLU A 1 39  ? 186.270 195.802 83.099  1.00 120.03 ?  58  GLU A CG    1 
ATOM   315   C  CD    . GLU A 1 39  ? 185.531 196.663 84.103  1.00 120.21 ?  58  GLU A CD    1 
ATOM   316   O  OE1   . GLU A 1 39  ? 186.197 197.308 84.940  1.00 119.43 ?  58  GLU A OE1   1 
ATOM   317   O  OE2   . GLU A 1 39  ? 184.283 196.693 84.056  1.00 119.72 -1 58  GLU A OE2   1 
ATOM   318   N  N     . GLU A 1 40  ? 188.834 192.756 85.541  1.00 116.03 ?  59  GLU A N     1 
ATOM   319   C  CA    . GLU A 1 40  ? 189.995 191.904 85.764  1.00 116.64 ?  59  GLU A CA    1 
ATOM   320   C  C     . GLU A 1 40  ? 189.629 190.453 86.053  1.00 119.03 ?  59  GLU A C     1 
ATOM   321   O  O     . GLU A 1 40  ? 190.421 189.558 85.740  1.00 118.67 ?  59  GLU A O     1 
ATOM   322   C  CB    . GLU A 1 40  ? 190.828 192.452 86.925  1.00 114.86 ?  59  GLU A CB    1 
ATOM   323   C  CG    . GLU A 1 40  ? 191.417 193.831 86.679  1.00 116.47 ?  59  GLU A CG    1 
ATOM   324   C  CD    . GLU A 1 40  ? 192.334 194.279 87.801  1.00 117.63 ?  59  GLU A CD    1 
ATOM   325   O  OE1   . GLU A 1 40  ? 193.377 193.627 88.015  1.00 117.07 ?  59  GLU A OE1   1 
ATOM   326   O  OE2   . GLU A 1 40  ? 192.010 195.283 88.470  1.00 117.57 -1 59  GLU A OE2   1 
ATOM   327   N  N     . VAL A 1 41  ? 188.460 190.196 86.636  1.00 115.17 ?  60  VAL A N     1 
ATOM   328   C  CA    . VAL A 1 41  ? 188.120 188.878 87.154  1.00 112.83 ?  60  VAL A CA    1 
ATOM   329   C  C     . VAL A 1 41  ? 187.125 188.147 86.258  1.00 110.19 ?  60  VAL A C     1 
ATOM   330   O  O     . VAL A 1 41  ? 187.254 186.938 86.050  1.00 108.62 ?  60  VAL A O     1 
ATOM   331   C  CB    . VAL A 1 41  ? 187.588 188.981 88.601  1.00 110.95 ?  60  VAL A CB    1 
ATOM   332   C  CG1   . VAL A 1 41  ? 187.219 187.607 89.135  1.00 110.83 ?  60  VAL A CG1   1 
ATOM   333   C  CG2   . VAL A 1 41  ? 188.626 189.630 89.498  1.00 108.64 ?  60  VAL A CG2   1 
ATOM   334   N  N     . ILE A 1 42  ? 186.127 188.855 85.719  1.00 111.09 ?  61  ILE A N     1 
ATOM   335   C  CA    . ILE A 1 42  ? 185.040 188.197 85.001  1.00 111.26 ?  61  ILE A CA    1 
ATOM   336   C  C     . ILE A 1 42  ? 185.588 187.453 83.792  1.00 110.70 ?  61  ILE A C     1 
ATOM   337   O  O     . ILE A 1 42  ? 186.334 188.012 82.978  1.00 110.99 ?  61  ILE A O     1 
ATOM   338   C  CB    . ILE A 1 42  ? 183.974 189.223 84.590  1.00 110.35 ?  61  ILE A CB    1 
ATOM   339   C  CG1   . ILE A 1 42  ? 183.166 189.667 85.810  1.00 110.00 ?  61  ILE A CG1   1 
ATOM   340   C  CG2   . ILE A 1 42  ? 183.051 188.643 83.528  1.00 108.53 ?  61  ILE A CG2   1 
ATOM   341   C  CD1   . ILE A 1 42  ? 182.259 188.597 86.358  1.00 110.60 ?  61  ILE A CD1   1 
ATOM   342   N  N     . GLY A 1 43  ? 185.218 186.177 83.673  1.00 107.52 ?  62  GLY A N     1 
ATOM   343   C  CA    . GLY A 1 43  ? 185.670 185.333 82.594  1.00 105.61 ?  62  GLY A CA    1 
ATOM   344   C  C     . GLY A 1 43  ? 186.969 184.602 82.858  1.00 106.40 ?  62  GLY A C     1 
ATOM   345   O  O     . GLY A 1 43  ? 187.293 183.659 82.129  1.00 103.86 ?  62  GLY A O     1 
ATOM   346   N  N     . ASN A 1 44  ? 187.720 185.008 83.878  1.00 113.21 ?  63  ASN A N     1 
ATOM   347   C  CA    . ASN A 1 44  ? 189.000 184.391 84.181  1.00 113.78 ?  63  ASN A CA    1 
ATOM   348   C  C     . ASN A 1 44  ? 188.834 183.294 85.232  1.00 114.94 ?  63  ASN A C     1 
ATOM   349   O  O     . ASN A 1 44  ? 187.774 183.125 85.839  1.00 116.25 ?  63  ASN A O     1 
ATOM   350   C  CB    . ASN A 1 44  ? 189.998 185.443 84.657  1.00 113.49 ?  63  ASN A CB    1 
ATOM   351   C  CG    . ASN A 1 44  ? 190.282 186.494 83.602  1.00 114.07 ?  63  ASN A CG    1 
ATOM   352   O  OD1   . ASN A 1 44  ? 190.712 186.178 82.492  1.00 114.69 ?  63  ASN A OD1   1 
ATOM   353   N  ND2   . ASN A 1 44  ? 190.041 187.755 83.943  1.00 113.45 ?  63  ASN A ND2   1 
ATOM   354   N  N     . ASN A 1 45  ? 189.913 182.544 85.444  1.00 111.93 ?  64  ASN A N     1 
ATOM   355   C  CA    . ASN A 1 45  ? 189.898 181.444 86.394  1.00 111.82 ?  64  ASN A CA    1 
ATOM   356   C  C     . ASN A 1 45  ? 189.847 181.970 87.828  1.00 109.62 ?  64  ASN A C     1 
ATOM   357   O  O     . ASN A 1 45  ? 190.212 183.113 88.117  1.00 108.03 ?  64  ASN A O     1 
ATOM   358   C  CB    . ASN A 1 45  ? 191.128 180.556 86.201  1.00 114.03 ?  64  ASN A CB    1 
ATOM   359   C  CG    . ASN A 1 45  ? 190.990 179.205 86.878  1.00 113.97 ?  64  ASN A CG    1 
ATOM   360   O  OD1   . ASN A 1 45  ? 190.087 178.989 87.688  1.00 112.03 ?  64  ASN A OD1   1 
ATOM   361   N  ND2   . ASN A 1 45  ? 191.890 178.286 86.550  1.00 112.43 ?  64  ASN A ND2   1 
ATOM   362   N  N     . ILE A 1 46  ? 189.382 181.105 88.736  1.00 106.94 ?  65  ILE A N     1 
ATOM   363   C  CA    . ILE A 1 46  ? 189.264 181.455 90.151  1.00 109.96 ?  65  ILE A CA    1 
ATOM   364   C  C     . ILE A 1 46  ? 190.596 181.407 90.883  1.00 109.13 ?  65  ILE A C     1 
ATOM   365   O  O     . ILE A 1 46  ? 190.635 181.646 92.097  1.00 111.41 ?  65  ILE A O     1 
ATOM   366   C  CB    . ILE A 1 46  ? 188.244 180.523 90.840  1.00 107.23 ?  65  ILE A CB    1 
ATOM   367   C  CG1   . ILE A 1 46  ? 187.631 181.195 92.073  1.00 103.45 ?  65  ILE A CG1   1 
ATOM   368   C  CG2   . ILE A 1 46  ? 188.882 179.185 91.198  1.00 106.29 ?  65  ILE A CG2   1 
ATOM   369   C  CD1   . ILE A 1 46  ? 186.626 180.332 92.801  1.00 104.54 ?  65  ILE A CD1   1 
ATOM   370   N  N     . ASP A 1 47  ? 191.697 181.127 90.179  1.00 103.20 ?  66  ASP A N     1 
ATOM   371   C  CA    . ASP A 1 47  ? 192.989 180.965 90.838  1.00 104.27 ?  66  ASP A CA    1 
ATOM   372   C  C     . ASP A 1 47  ? 193.467 182.237 91.528  1.00 105.61 ?  66  ASP A C     1 
ATOM   373   O  O     . ASP A 1 47  ? 194.343 182.163 92.396  1.00 108.25 ?  66  ASP A O     1 
ATOM   374   C  CB    . ASP A 1 47  ? 194.035 180.499 89.825  1.00 106.33 ?  66  ASP A CB    1 
ATOM   375   C  CG    . ASP A 1 47  ? 193.611 179.246 89.085  1.00 108.46 ?  66  ASP A CG    1 
ATOM   376   O  OD1   . ASP A 1 47  ? 192.725 178.526 89.592  1.00 108.13 ?  66  ASP A OD1   1 
ATOM   377   O  OD2   . ASP A 1 47  ? 194.163 178.981 87.996  1.00 109.41 -1 66  ASP A OD2   1 
ATOM   378   N  N     . MET A 1 48  ? 192.918 183.399 91.168  1.00 106.66 ?  67  MET A N     1 
ATOM   379   C  CA    . MET A 1 48  ? 193.330 184.641 91.811  1.00 108.15 ?  67  MET A CA    1 
ATOM   380   C  C     . MET A 1 48  ? 192.762 184.776 93.219  1.00 109.03 ?  67  MET A C     1 
ATOM   381   O  O     . MET A 1 48  ? 193.354 185.465 94.057  1.00 108.63 ?  67  MET A O     1 
ATOM   382   C  CB    . MET A 1 48  ? 192.902 185.841 90.965  1.00 105.81 ?  67  MET A CB    1 
ATOM   383   C  CG    . MET A 1 48  ? 193.782 186.099 89.755  1.00 109.87 ?  67  MET A CG    1 
ATOM   384   S  SD    . MET A 1 48  ? 193.295 185.108 88.331  1.00 117.42 ?  67  MET A SD    1 
ATOM   385   C  CE    . MET A 1 48  ? 192.159 186.228 87.517  1.00 108.71 ?  67  MET A CE    1 
ATOM   386   N  N     . LEU A 1 49  ? 191.630 184.134 93.494  1.00 104.66 ?  68  LEU A N     1 
ATOM   387   C  CA    . LEU A 1 49  ? 190.908 184.316 94.746  1.00 104.29 ?  68  LEU A CA    1 
ATOM   388   C  C     . LEU A 1 49  ? 191.323 183.331 95.833  1.00 101.75 ?  68  LEU A C     1 
ATOM   389   O  O     . LEU A 1 49  ? 190.825 183.434 96.959  1.00 103.74 ?  68  LEU A O     1 
ATOM   390   C  CB    . LEU A 1 49  ? 189.401 184.194 94.497  1.00 104.52 ?  68  LEU A CB    1 
ATOM   391   C  CG    . LEU A 1 49  ? 188.803 185.169 93.480  1.00 103.43 ?  68  LEU A CG    1 
ATOM   392   C  CD1   . LEU A 1 49  ? 187.380 184.770 93.120  1.00 101.63 ?  68  LEU A CD1   1 
ATOM   393   C  CD2   . LEU A 1 49  ? 188.849 186.598 93.987  1.00 100.40 ?  68  LEU A CD2   1 
ATOM   394   N  N     . ILE A 1 50  ? 192.210 182.387 95.534  1.00 95.28  ?  69  ILE A N     1 
ATOM   395   C  CA    . ILE A 1 50  ? 192.576 181.346 96.492  1.00 95.63  ?  69  ILE A CA    1 
ATOM   396   C  C     . ILE A 1 50  ? 193.825 181.770 97.258  1.00 97.60  ?  69  ILE A C     1 
ATOM   397   O  O     . ILE A 1 50  ? 194.754 182.334 96.661  1.00 98.36  ?  69  ILE A O     1 
ATOM   398   C  CB    . ILE A 1 50  ? 192.787 179.997 95.785  1.00 94.99  ?  69  ILE A CB    1 
ATOM   399   C  CG1   . ILE A 1 50  ? 191.537 179.613 94.995  1.00 95.05  ?  69  ILE A CG1   1 
ATOM   400   C  CG2   . ILE A 1 50  ? 193.123 178.902 96.787  1.00 96.02  ?  69  ILE A CG2   1 
ATOM   401   C  CD1   . ILE A 1 50  ? 191.836 178.997 93.650  1.00 98.98  ?  69  ILE A CD1   1 
ATOM   402   N  N     . PRO A 1 51  ? 193.885 181.536 98.571  1.00 101.64 ?  70  PRO A N     1 
ATOM   403   C  CA    . PRO A 1 51  ? 195.116 181.826 99.316  1.00 103.86 ?  70  PRO A CA    1 
ATOM   404   C  C     . PRO A 1 51  ? 196.292 181.017 98.790  1.00 106.28 ?  70  PRO A C     1 
ATOM   405   O  O     . PRO A 1 51  ? 196.148 179.864 98.376  1.00 107.39 ?  70  PRO A O     1 
ATOM   406   C  CB    . PRO A 1 51  ? 194.763 181.427 100.754 1.00 101.75 ?  70  PRO A CB    1 
ATOM   407   C  CG    . PRO A 1 51  ? 193.282 181.553 100.823 1.00 103.03 ?  70  PRO A CG    1 
ATOM   408   C  CD    . PRO A 1 51  ? 192.771 181.173 99.462  1.00 101.52 ?  70  PRO A CD    1 
ATOM   409   N  N     . ARG A 1 52  ? 197.474 181.638 98.829  1.00 106.85 ?  71  ARG A N     1 
ATOM   410   C  CA    . ARG A 1 52  ? 198.663 181.051 98.219  1.00 103.43 ?  71  ARG A CA    1 
ATOM   411   C  C     . ARG A 1 52  ? 199.092 179.751 98.885  1.00 104.12 ?  71  ARG A C     1 
ATOM   412   O  O     . ARG A 1 52  ? 199.906 179.018 98.313  1.00 104.02 ?  71  ARG A O     1 
ATOM   413   C  CB    . ARG A 1 52  ? 199.818 182.053 98.255  1.00 101.37 ?  71  ARG A CB    1 
ATOM   414   C  CG    . ARG A 1 52  ? 199.723 183.147 97.205  1.00 103.39 ?  71  ARG A CG    1 
ATOM   415   C  CD    . ARG A 1 52  ? 201.099 183.653 96.807  1.00 104.59 ?  71  ARG A CD    1 
ATOM   416   N  NE    . ARG A 1 52  ? 202.001 182.559 96.465  1.00 105.45 ?  71  ARG A NE    1 
ATOM   417   C  CZ    . ARG A 1 52  ? 202.046 181.969 95.278  1.00 104.92 ?  71  ARG A CZ    1 
ATOM   418   N  NH1   . ARG A 1 52  ? 201.249 182.342 94.290  1.00 103.36 1  71  ARG A NH1   1 
ATOM   419   N  NH2   . ARG A 1 52  ? 202.912 180.980 95.078  1.00 106.23 ?  71  ARG A NH2   1 
ATOM   420   N  N     . ASP A 1 53  ? 198.576 179.451 100.079 1.00 107.00 ?  72  ASP A N     1 
ATOM   421   C  CA    . ASP A 1 53  ? 198.973 178.227 100.768 1.00 105.51 ?  72  ASP A CA    1 
ATOM   422   C  C     . ASP A 1 53  ? 198.569 176.986 99.981  1.00 106.08 ?  72  ASP A C     1 
ATOM   423   O  O     . ASP A 1 53  ? 199.344 176.027 99.880  1.00 106.74 ?  72  ASP A O     1 
ATOM   424   C  CB    . ASP A 1 53  ? 198.365 178.193 102.169 1.00 105.97 ?  72  ASP A CB    1 
ATOM   425   C  CG    . ASP A 1 53  ? 198.644 176.890 102.894 1.00 108.03 ?  72  ASP A CG    1 
ATOM   426   O  OD1   . ASP A 1 53  ? 199.802 176.425 102.859 1.00 108.13 ?  72  ASP A OD1   1 
ATOM   427   O  OD2   . ASP A 1 53  ? 197.704 176.331 103.499 1.00 108.25 -1 72  ASP A OD2   1 
ATOM   428   N  N     . LEU A 1 54  ? 197.364 176.983 99.415  1.00 101.14 ?  73  LEU A N     1 
ATOM   429   C  CA    . LEU A 1 54  ? 196.836 175.800 98.742  1.00 99.27  ?  73  LEU A CA    1 
ATOM   430   C  C     . LEU A 1 54  ? 196.134 176.191 97.445  1.00 100.40 ?  73  LEU A C     1 
ATOM   431   O  O     . LEU A 1 54  ? 195.019 175.743 97.161  1.00 99.94  ?  73  LEU A O     1 
ATOM   432   C  CB    . LEU A 1 54  ? 195.896 175.025 99.667  1.00 100.40 ?  73  LEU A CB    1 
ATOM   433   C  CG    . LEU A 1 54  ? 195.610 173.562 99.326  1.00 102.35 ?  73  LEU A CG    1 
ATOM   434   C  CD1   . LEU A 1 54  ? 196.876 172.737 99.483  1.00 101.68 ?  73  LEU A CD1   1 
ATOM   435   C  CD2   . LEU A 1 54  ? 194.494 173.012 100.203 1.00 99.86  ?  73  LEU A CD2   1 
ATOM   436   N  N     . ARG A 1 55  ? 196.773 177.053 96.651  1.00 95.71  ?  74  ARG A N     1 
ATOM   437   C  CA    . ARG A 1 55  ? 196.178 177.481 95.385  1.00 94.64  ?  74  ARG A CA    1 
ATOM   438   C  C     . ARG A 1 55  ? 195.933 176.335 94.406  1.00 97.32  ?  74  ARG A C     1 
ATOM   439   O  O     . ARG A 1 55  ? 194.812 176.241 93.876  1.00 96.47  ?  74  ARG A O     1 
ATOM   440   C  CB    . ARG A 1 55  ? 197.046 178.577 94.754  1.00 91.84  ?  74  ARG A CB    1 
ATOM   441   C  CG    . ARG A 1 55  ? 196.789 179.963 95.323  1.00 94.08  ?  74  ARG A CG    1 
ATOM   442   C  CD    . ARG A 1 55  ? 197.545 181.053 94.576  1.00 95.18  ?  74  ARG A CD    1 
ATOM   443   N  NE    . ARG A 1 55  ? 196.989 181.325 93.256  1.00 96.88  ?  74  ARG A NE    1 
ATOM   444   C  CZ    . ARG A 1 55  ? 197.616 181.076 92.115  1.00 96.84  ?  74  ARG A CZ    1 
ATOM   445   N  NH1   . ARG A 1 55  ? 198.826 180.541 92.094  1.00 96.88  1  74  ARG A NH1   1 
ATOM   446   N  NH2   . ARG A 1 55  ? 197.016 181.376 90.966  1.00 95.60  ?  74  ARG A NH2   1 
ATOM   447   N  N     . PRO A 1 56  ? 196.893 175.444 94.116  1.00 98.27  ?  75  PRO A N     1 
ATOM   448   C  CA    . PRO A 1 56  ? 196.624 174.403 93.109  1.00 95.94  ?  75  PRO A CA    1 
ATOM   449   C  C     . PRO A 1 56  ? 195.722 173.281 93.593  1.00 92.47  ?  75  PRO A C     1 
ATOM   450   O  O     . PRO A 1 56  ? 195.037 172.668 92.764  1.00 94.60  ?  75  PRO A O     1 
ATOM   451   C  CB    . PRO A 1 56  ? 198.022 173.873 92.768  1.00 96.14  ?  75  PRO A CB    1 
ATOM   452   C  CG    . PRO A 1 56  ? 198.811 174.096 93.995  1.00 95.90  ?  75  PRO A CG    1 
ATOM   453   C  CD    . PRO A 1 56  ? 198.264 175.334 94.653  1.00 98.10  ?  75  PRO A CD    1 
ATOM   454   N  N     . ALA A 1 57  ? 195.700 172.986 94.891  1.00 88.18  ?  76  ALA A N     1 
ATOM   455   C  CA    . ALA A 1 57  ? 194.877 171.901 95.425  1.00 90.30  ?  76  ALA A CA    1 
ATOM   456   C  C     . ALA A 1 57  ? 193.562 172.463 95.966  1.00 89.71  ?  76  ALA A C     1 
ATOM   457   O  O     . ALA A 1 57  ? 193.339 172.586 97.170  1.00 91.28  ?  76  ALA A O     1 
ATOM   458   C  CB    . ALA A 1 57  ? 195.646 171.128 96.492  1.00 90.21  ?  76  ALA A CB    1 
ATOM   459   N  N     . HIS A 1 58  ? 192.683 172.807 95.029  1.00 84.57  ?  77  HIS A N     1 
ATOM   460   C  CA    . HIS A 1 58  ? 191.355 173.337 95.324  1.00 87.22  ?  77  HIS A CA    1 
ATOM   461   C  C     . HIS A 1 58  ? 190.384 172.955 94.207  1.00 84.03  ?  77  HIS A C     1 
ATOM   462   O  O     . HIS A 1 58  ? 189.217 172.634 94.488  1.00 86.79  ?  77  HIS A O     1 
ATOM   463   C  CB    . HIS A 1 58  ? 191.410 174.855 95.521  1.00 89.65  ?  77  HIS A CB    1 
ATOM   464   C  CG    . HIS A 1 58  ? 190.067 175.519 95.527  1.00 88.21  ?  77  HIS A CG    1 
ATOM   465   N  ND1   . HIS A 1 58  ? 189.826 176.714 94.885  1.00 87.67  ?  77  HIS A ND1   1 
ATOM   466   C  CD2   . HIS A 1 58  ? 188.900 175.167 96.117  1.00 85.84  ?  77  HIS A CD2   1 
ATOM   467   C  CE1   . HIS A 1 58  ? 188.565 177.063 95.066  1.00 88.41  ?  77  HIS A CE1   1 
ATOM   468   N  NE2   . HIS A 1 58  ? 187.981 176.141 95.810  1.00 88.12  ?  77  HIS A NE2   1 
ATOM   469   N  N     . PRO A 1 59  ? 190.803 172.977 92.934  1.00 81.39  ?  78  PRO A N     1 
ATOM   470   C  CA    . PRO A 1 59  ? 189.972 172.334 91.907  1.00 80.06  ?  78  PRO A CA    1 
ATOM   471   C  C     . PRO A 1 59  ? 189.733 170.862 92.177  1.00 78.93  ?  78  PRO A C     1 
ATOM   472   O  O     . PRO A 1 59  ? 188.704 170.331 91.751  1.00 84.33  ?  78  PRO A O     1 
ATOM   473   C  CB    . PRO A 1 59  ? 190.769 172.555 90.610  1.00 81.74  ?  78  PRO A CB    1 
ATOM   474   C  CG    . PRO A 1 59  ? 192.133 172.992 91.047  1.00 85.57  ?  78  PRO A CG    1 
ATOM   475   C  CD    . PRO A 1 59  ? 191.897 173.743 92.310  1.00 86.13  ?  78  PRO A CD    1 
ATOM   476   N  N     . GLU A 1 60  ? 190.644 170.184 92.881  1.00 82.16  ?  79  GLU A N     1 
ATOM   477   C  CA    . GLU A 1 60  ? 190.384 168.804 93.281  1.00 87.20  ?  79  GLU A CA    1 
ATOM   478   C  C     . GLU A 1 60  ? 189.191 168.718 94.226  1.00 88.21  ?  79  GLU A C     1 
ATOM   479   O  O     . GLU A 1 60  ? 188.318 167.858 94.057  1.00 89.29  ?  79  GLU A O     1 
ATOM   480   C  CB    . GLU A 1 60  ? 191.627 168.198 93.932  1.00 87.90  ?  79  GLU A CB    1 
ATOM   481   C  CG    . GLU A 1 60  ? 191.574 166.684 94.081  1.00 89.30  ?  79  GLU A CG    1 
ATOM   482   C  CD    . GLU A 1 60  ? 191.063 165.988 92.835  1.00 88.97  ?  79  GLU A CD    1 
ATOM   483   O  OE1   . GLU A 1 60  ? 190.024 165.300 92.921  1.00 86.73  ?  79  GLU A OE1   1 
ATOM   484   O  OE2   . GLU A 1 60  ? 191.701 166.127 91.771  1.00 88.02  -1 79  GLU A OE2   1 
ATOM   485   N  N     . TYR A 1 61  ? 189.133 169.604 95.225  1.00 84.80  ?  80  TYR A N     1 
ATOM   486   C  CA    . TYR A 1 61  ? 187.979 169.643 96.119  1.00 84.32  ?  80  TYR A CA    1 
ATOM   487   C  C     . TYR A 1 61  ? 186.705 169.967 95.349  1.00 82.43  ?  80  TYR A C     1 
ATOM   488   O  O     . TYR A 1 61  ? 185.655 169.347 95.570  1.00 82.57  ?  80  TYR A O     1 
ATOM   489   C  CB    . TYR A 1 61  ? 188.202 170.680 97.221  1.00 81.29  ?  80  TYR A CB    1 
ATOM   490   C  CG    . TYR A 1 61  ? 189.000 170.185 98.404  1.00 82.21  ?  80  TYR A CG    1 
ATOM   491   C  CD1   . TYR A 1 61  ? 188.822 168.902 98.902  1.00 83.74  ?  80  TYR A CD1   1 
ATOM   492   C  CD2   . TYR A 1 61  ? 189.927 171.008 99.030  1.00 79.20  ?  80  TYR A CD2   1 
ATOM   493   C  CE1   . TYR A 1 61  ? 189.551 168.450 99.986  1.00 82.20  ?  80  TYR A CE1   1 
ATOM   494   C  CE2   . TYR A 1 61  ? 190.660 170.566 100.114 1.00 79.34  ?  80  TYR A CE2   1 
ATOM   495   C  CZ    . TYR A 1 61  ? 190.468 169.287 100.588 1.00 79.82  ?  80  TYR A CZ    1 
ATOM   496   O  OH    . TYR A 1 61  ? 191.197 168.844 101.668 1.00 82.09  ?  80  TYR A OH    1 
ATOM   497   N  N     . ILE A 1 62  ? 186.784 170.942 94.440  1.00 80.67  ?  81  ILE A N     1 
ATOM   498   C  CA    . ILE A 1 62  ? 185.611 171.329 93.661  1.00 80.98  ?  81  ILE A CA    1 
ATOM   499   C  C     . ILE A 1 62  ? 185.111 170.151 92.834  1.00 84.95  ?  81  ILE A C     1 
ATOM   500   O  O     . ILE A 1 62  ? 183.915 169.841 92.824  1.00 86.64  ?  81  ILE A O     1 
ATOM   501   C  CB    . ILE A 1 62  ? 185.932 172.547 92.776  1.00 81.04  ?  81  ILE A CB    1 
ATOM   502   C  CG1   . ILE A 1 62  ? 186.143 173.791 93.640  1.00 80.64  ?  81  ILE A CG1   1 
ATOM   503   C  CG2   . ILE A 1 62  ? 184.819 172.785 91.767  1.00 82.93  ?  81  ILE A CG2   1 
ATOM   504   C  CD1   . ILE A 1 62  ? 186.738 174.959 92.887  1.00 81.83  ?  81  ILE A CD1   1 
ATOM   505   N  N     . ARG A 1 63  ? 186.026 169.462 92.147  1.00 84.98  ?  82  ARG A N     1 
ATOM   506   C  CA    . ARG A 1 63  ? 185.655 168.313 91.327  1.00 82.54  ?  82  ARG A CA    1 
ATOM   507   C  C     . ARG A 1 63  ? 185.081 167.185 92.173  1.00 82.41  ?  82  ARG A C     1 
ATOM   508   O  O     . ARG A 1 63  ? 184.132 166.511 91.756  1.00 85.40  ?  82  ARG A O     1 
ATOM   509   C  CB    . ARG A 1 63  ? 186.870 167.830 90.534  1.00 83.65  ?  82  ARG A CB    1 
ATOM   510   C  CG    . ARG A 1 63  ? 186.541 166.879 89.398  1.00 85.38  ?  82  ARG A CG    1 
ATOM   511   C  CD    . ARG A 1 63  ? 187.637 165.837 89.233  1.00 85.71  ?  82  ARG A CD    1 
ATOM   512   N  NE    . ARG A 1 63  ? 187.756 164.969 90.399  1.00 86.81  ?  82  ARG A NE    1 
ATOM   513   C  CZ    . ARG A 1 63  ? 186.933 163.968 90.680  1.00 87.02  ?  82  ARG A CZ    1 
ATOM   514   N  NH1   . ARG A 1 63  ? 185.914 163.667 89.892  1.00 87.01  1  82  ARG A NH1   1 
ATOM   515   N  NH2   . ARG A 1 63  ? 187.140 163.247 91.779  1.00 85.23  ?  82  ARG A NH2   1 
ATOM   516   N  N     . HIS A 1 64  ? 185.649 166.955 93.359  1.00 85.25  ?  83  HIS A N     1 
ATOM   517   C  CA    . HIS A 1 64  ? 185.104 165.934 94.246  1.00 89.74  ?  83  HIS A CA    1 
ATOM   518   C  C     . HIS A 1 64  ? 183.676 166.270 94.653  1.00 89.53  ?  83  HIS A C     1 
ATOM   519   O  O     . HIS A 1 64  ? 182.822 165.381 94.749  1.00 84.89  ?  83  HIS A O     1 
ATOM   520   C  CB    . HIS A 1 64  ? 185.994 165.778 95.479  1.00 87.95  ?  83  HIS A CB    1 
ATOM   521   C  CG    . HIS A 1 64  ? 185.295 165.174 96.657  1.00 90.12  ?  83  HIS A CG    1 
ATOM   522   N  ND1   . HIS A 1 64  ? 184.657 165.931 97.615  1.00 92.37  ?  83  HIS A ND1   1 
ATOM   523   C  CD2   . HIS A 1 64  ? 185.130 163.882 97.027  1.00 89.15  ?  83  HIS A CD2   1 
ATOM   524   C  CE1   . HIS A 1 64  ? 184.132 165.132 98.527  1.00 90.23  ?  83  HIS A CE1   1 
ATOM   525   N  NE2   . HIS A 1 64  ? 184.405 163.883 98.194  1.00 89.11  ?  83  HIS A NE2   1 
ATOM   526   N  N     . ASN A 1 65  ? 183.398 167.553 94.901  1.00 89.11  ?  84  ASN A N     1 
ATOM   527   C  CA    . ASN A 1 65  ? 182.028 167.957 95.205  1.00 86.30  ?  84  ASN A CA    1 
ATOM   528   C  C     . ASN A 1 65  ? 181.117 167.806 93.989  1.00 87.09  ?  84  ASN A C     1 
ATOM   529   O  O     . ASN A 1 65  ? 179.940 167.457 94.136  1.00 89.56  ?  84  ASN A O     1 
ATOM   530   C  CB    . ASN A 1 65  ? 182.009 169.403 95.708  1.00 86.20  ?  84  ASN A CB    1 
ATOM   531   C  CG    . ASN A 1 65  ? 180.648 169.828 96.248  1.00 88.65  ?  84  ASN A CG    1 
ATOM   532   O  OD1   . ASN A 1 65  ? 180.465 170.952 96.713  1.00 90.90  ?  84  ASN A OD1   1 
ATOM   533   N  ND2   . ASN A 1 65  ? 179.686 168.914 96.196  1.00 89.00  ?  84  ASN A ND2   1 
ATOM   534   N  N     . ARG A 1 66  ? 181.648 168.050 92.787  1.00 89.25  ?  85  ARG A N     1 
ATOM   535   C  CA    . ARG A 1 66  ? 180.806 168.133 91.594  1.00 91.80  ?  85  ARG A CA    1 
ATOM   536   C  C     . ARG A 1 66  ? 180.068 166.826 91.326  1.00 92.31  ?  85  ARG A C     1 
ATOM   537   O  O     . ARG A 1 66  ? 178.877 166.836 90.993  1.00 91.69  ?  85  ARG A O     1 
ATOM   538   C  CB    . ARG A 1 66  ? 181.654 168.520 90.381  1.00 91.56  ?  85  ARG A CB    1 
ATOM   539   C  CG    . ARG A 1 66  ? 182.141 169.959 90.399  1.00 92.07  ?  85  ARG A CG    1 
ATOM   540   C  CD    . ARG A 1 66  ? 182.706 170.403 89.061  1.00 90.98  ?  85  ARG A CD    1 
ATOM   541   N  NE    . ARG A 1 66  ? 182.753 171.857 88.966  1.00 87.99  ?  85  ARG A NE    1 
ATOM   542   C  CZ    . ARG A 1 66  ? 181.784 172.610 88.468  1.00 89.36  ?  85  ARG A CZ    1 
ATOM   543   N  NH1   . ARG A 1 66  ? 180.670 172.078 87.993  1.00 93.02  1  85  ARG A NH1   1 
ATOM   544   N  NH2   . ARG A 1 66  ? 181.933 173.932 88.452  1.00 90.90  ?  85  ARG A NH2   1 
ATOM   545   N  N     . GLU A 1 67  ? 180.754 165.692 91.464  1.00 91.74  ?  86  GLU A N     1 
ATOM   546   C  CA    . GLU A 1 67  ? 180.158 164.405 91.126  1.00 90.51  ?  86  GLU A CA    1 
ATOM   547   C  C     . GLU A 1 67  ? 179.211 163.880 92.197  1.00 91.84  ?  86  GLU A C     1 
ATOM   548   O  O     . GLU A 1 67  ? 178.470 162.928 91.927  1.00 89.59  ?  86  GLU A O     1 
ATOM   549   C  CB    . GLU A 1 67  ? 181.255 163.368 90.872  1.00 90.64  ?  86  GLU A CB    1 
ATOM   550   C  CG    . GLU A 1 67  ? 182.273 163.254 91.993  1.00 92.24  ?  86  GLU A CG    1 
ATOM   551   C  CD    . GLU A 1 67  ? 181.920 162.165 92.988  1.00 95.28  ?  86  GLU A CD    1 
ATOM   552   O  OE1   . GLU A 1 67  ? 181.122 161.271 92.635  1.00 94.90  ?  86  GLU A OE1   1 
ATOM   553   O  OE2   . GLU A 1 67  ? 182.438 162.203 94.124  1.00 93.59  -1 86  GLU A OE2   1 
ATOM   554   N  N     . GLY A 1 68  ? 179.218 164.466 93.396  1.00 96.17  ?  87  GLY A N     1 
ATOM   555   C  CA    . GLY A 1 68  ? 178.385 163.943 94.467  1.00 95.51  ?  87  GLY A CA    1 
ATOM   556   C  C     . GLY A 1 68  ? 176.900 164.087 94.193  1.00 95.72  ?  87  GLY A C     1 
ATOM   557   O  O     . GLY A 1 68  ? 176.124 163.155 94.427  1.00 96.43  ?  87  GLY A O     1 
ATOM   558   N  N     . GLY A 1 69  ? 176.482 165.249 93.698  1.00 95.86  ?  88  GLY A N     1 
ATOM   559   C  CA    . GLY A 1 69  ? 175.079 165.509 93.459  1.00 95.47  ?  88  GLY A CA    1 
ATOM   560   C  C     . GLY A 1 69  ? 174.281 165.893 94.684  1.00 95.63  ?  88  GLY A C     1 
ATOM   561   O  O     . GLY A 1 69  ? 173.052 166.008 94.590  1.00 95.02  ?  88  GLY A O     1 
ATOM   562   N  N     . LYS A 1 70  ? 174.932 166.089 95.828  1.00 90.21  ?  89  LYS A N     1 
ATOM   563   C  CA    . LYS A 1 70  ? 174.229 166.472 97.043  1.00 89.30  ?  89  LYS A CA    1 
ATOM   564   C  C     . LYS A 1 70  ? 173.638 167.871 96.901  1.00 89.53  ?  89  LYS A C     1 
ATOM   565   O  O     . LYS A 1 70  ? 174.199 168.743 96.233  1.00 91.59  ?  89  LYS A O     1 
ATOM   566   C  CB    . LYS A 1 70  ? 175.175 166.422 98.243  1.00 89.50  ?  89  LYS A CB    1 
ATOM   567   C  CG    . LYS A 1 70  ? 174.484 166.498 99.596  1.00 89.16  ?  89  LYS A CG    1 
ATOM   568   C  CD    . LYS A 1 70  ? 173.743 165.208 99.911  1.00 90.13  ?  89  LYS A CD    1 
ATOM   569   C  CE    . LYS A 1 70  ? 174.710 164.045 100.066 1.00 89.34  ?  89  LYS A CE    1 
ATOM   570   N  NZ    . LYS A 1 70  ? 174.006 162.773 100.391 1.00 87.19  1  89  LYS A NZ    1 
ATOM   571   N  N     . ALA A 1 71  ? 172.485 168.078 97.540  1.00 81.18  ?  90  ALA A N     1 
ATOM   572   C  CA    . ALA A 1 71  ? 171.812 169.370 97.455  1.00 82.09  ?  90  ALA A CA    1 
ATOM   573   C  C     . ALA A 1 71  ? 172.572 170.438 98.233  1.00 82.07  ?  90  ALA A C     1 
ATOM   574   O  O     . ALA A 1 71  ? 173.047 171.424 97.659  1.00 81.88  ?  90  ALA A O     1 
ATOM   575   C  CB    . ALA A 1 71  ? 170.375 169.245 97.964  1.00 81.39  ?  90  ALA A CB    1 
ATOM   576   N  N     . ARG A 1 72  ? 172.701 170.256 99.544  1.00 76.73  ?  91  ARG A N     1 
ATOM   577   C  CA    . ARG A 1 72  ? 173.410 171.217 100.376 1.00 75.75  ?  91  ARG A CA    1 
ATOM   578   C  C     . ARG A 1 72  ? 174.916 171.020 100.267 1.00 77.24  ?  91  ARG A C     1 
ATOM   579   O  O     . ARG A 1 72  ? 175.405 169.893 100.151 1.00 78.08  ?  91  ARG A O     1 
ATOM   580   C  CB    . ARG A 1 72  ? 172.977 171.091 101.837 1.00 75.77  ?  91  ARG A CB    1 
ATOM   581   C  CG    . ARG A 1 72  ? 171.514 171.410 102.089 1.00 76.35  ?  91  ARG A CG    1 
ATOM   582   C  CD    . ARG A 1 72  ? 171.178 171.271 103.565 1.00 77.63  ?  91  ARG A CD    1 
ATOM   583   N  NE    . ARG A 1 72  ? 169.755 171.457 103.823 1.00 81.08  ?  91  ARG A NE    1 
ATOM   584   C  CZ    . ARG A 1 72  ? 169.186 172.631 104.058 1.00 83.52  ?  91  ARG A CZ    1 
ATOM   585   N  NH1   . ARG A 1 72  ? 169.891 173.751 104.071 1.00 79.77  1  91  ARG A NH1   1 
ATOM   586   N  NH2   . ARG A 1 72  ? 167.877 172.684 104.285 1.00 84.16  ?  91  ARG A NH2   1 
ATOM   587   N  N     . VAL A 1 73  ? 175.649 172.128 100.309 1.00 74.43  ?  92  VAL A N     1 
ATOM   588   C  CA    . VAL A 1 73  ? 177.110 172.106 100.291 1.00 72.81  ?  92  VAL A CA    1 
ATOM   589   C  C     . VAL A 1 73  ? 177.553 172.293 101.738 1.00 68.80  ?  92  VAL A C     1 
ATOM   590   O  O     . VAL A 1 73  ? 177.722 173.413 102.223 1.00 69.34  ?  92  VAL A O     1 
ATOM   591   C  CB    . VAL A 1 73  ? 177.687 173.173 99.364  1.00 75.48  ?  92  VAL A CB    1 
ATOM   592   C  CG1   . VAL A 1 73  ? 179.176 172.945 99.159  1.00 75.84  ?  92  VAL A CG1   1 
ATOM   593   C  CG2   . VAL A 1 73  ? 176.951 173.175 98.032  1.00 77.22  ?  92  VAL A CG2   1 
ATOM   594   N  N     . GLU A 1 74  ? 177.741 171.174 102.441 1.00 68.66  ?  93  GLU A N     1 
ATOM   595   C  CA    . GLU A 1 74  ? 178.117 171.228 103.850 1.00 74.38  ?  93  GLU A CA    1 
ATOM   596   C  C     . GLU A 1 74  ? 179.538 171.734 104.059 1.00 74.07  ?  93  GLU A C     1 
ATOM   597   O  O     . GLU A 1 74  ? 179.865 172.187 105.161 1.00 74.36  ?  93  GLU A O     1 
ATOM   598   C  CB    . GLU A 1 74  ? 177.955 169.847 104.485 1.00 75.28  ?  93  GLU A CB    1 
ATOM   599   C  CG    . GLU A 1 74  ? 176.576 169.241 104.284 1.00 75.56  ?  93  GLU A CG    1 
ATOM   600   C  CD    . GLU A 1 74  ? 176.513 167.783 104.691 1.00 76.25  ?  93  GLU A CD    1 
ATOM   601   O  OE1   . GLU A 1 74  ? 176.190 167.507 105.866 1.00 76.89  ?  93  GLU A OE1   1 
ATOM   602   O  OE2   . GLU A 1 74  ? 176.788 166.913 103.838 1.00 73.48  -1 93  GLU A OE2   1 
ATOM   603   N  N     . GLY A 1 75  ? 180.385 171.671 103.037 1.00 69.88  ?  94  GLY A N     1 
ATOM   604   C  CA    . GLY A 1 75  ? 181.741 172.158 103.166 1.00 72.38  ?  94  GLY A CA    1 
ATOM   605   C  C     . GLY A 1 75  ? 181.809 173.672 103.142 1.00 69.11  ?  94  GLY A C     1 
ATOM   606   O  O     . GLY A 1 75  ? 180.824 174.372 102.904 1.00 69.75  ?  94  GLY A O     1 
ATOM   607   N  N     . MET A 1 76  ? 183.016 174.180 103.401 1.00 65.55  ?  95  MET A N     1 
ATOM   608   C  CA    . MET A 1 76  ? 183.293 175.616 103.414 1.00 63.91  ?  95  MET A CA    1 
ATOM   609   C  C     . MET A 1 76  ? 182.388 176.325 104.427 1.00 63.09  ?  95  MET A C     1 
ATOM   610   O  O     . MET A 1 76  ? 181.717 177.315 104.129 1.00 66.74  ?  95  MET A O     1 
ATOM   611   C  CB    . MET A 1 76  ? 183.133 176.205 102.007 1.00 65.25  ?  95  MET A CB    1 
ATOM   612   C  CG    . MET A 1 76  ? 183.820 177.536 101.772 1.00 66.14  ?  95  MET A CG    1 
ATOM   613   S  SD    . MET A 1 76  ? 185.599 177.440 102.020 1.00 75.64  ?  95  MET A SD    1 
ATOM   614   C  CE    . MET A 1 76  ? 186.006 179.175 102.169 1.00 68.94  ?  95  MET A CE    1 
ATOM   615   N  N     . SER A 1 77  ? 182.382 175.786 105.649 1.00 48.71  ?  96  SER A N     1 
ATOM   616   C  CA    . SER A 1 77  ? 181.445 176.210 106.679 1.00 51.21  ?  96  SER A CA    1 
ATOM   617   C  C     . SER A 1 77  ? 182.077 176.995 107.819 1.00 55.84  ?  96  SER A C     1 
ATOM   618   O  O     . SER A 1 77  ? 181.342 177.594 108.610 1.00 61.20  ?  96  SER A O     1 
ATOM   619   C  CB    . SER A 1 77  ? 180.718 174.991 107.263 1.00 51.88  ?  96  SER A CB    1 
ATOM   620   O  OG    . SER A 1 77  ? 181.577 174.245 108.108 1.00 54.44  ?  96  SER A OG    1 
ATOM   621   N  N     . ALA A 1 78  ? 183.399 177.010 107.929 1.00 54.19  ?  97  ALA A N     1 
ATOM   622   C  CA    . ALA A 1 78  ? 184.077 177.692 109.020 1.00 53.06  ?  97  ALA A CA    1 
ATOM   623   C  C     . ALA A 1 78  ? 184.719 178.984 108.531 1.00 54.44  ?  97  ALA A C     1 
ATOM   624   O  O     . ALA A 1 78  ? 184.974 179.169 107.338 1.00 56.92  ?  97  ALA A O     1 
ATOM   625   C  CB    . ALA A 1 78  ? 185.137 176.783 109.649 1.00 56.10  ?  97  ALA A CB    1 
ATOM   626   N  N     . GLU A 1 79  ? 184.969 179.889 109.476 1.00 59.26  ?  98  GLU A N     1 
ATOM   627   C  CA    . GLU A 1 79  ? 185.665 181.131 109.167 1.00 59.79  ?  98  GLU A CA    1 
ATOM   628   C  C     . GLU A 1 79  ? 187.056 180.813 108.642 1.00 58.68  ?  98  GLU A C     1 
ATOM   629   O  O     . GLU A 1 79  ? 187.821 180.092 109.292 1.00 66.14  ?  98  GLU A O     1 
ATOM   630   C  CB    . GLU A 1 79  ? 185.758 182.011 110.413 1.00 61.02  ?  98  GLU A CB    1 
ATOM   631   C  CG    . GLU A 1 79  ? 184.446 182.205 111.152 1.00 65.83  ?  98  GLU A CG    1 
ATOM   632   C  CD    . GLU A 1 79  ? 184.250 181.189 112.262 1.00 64.59  ?  98  GLU A CD    1 
ATOM   633   O  OE1   . GLU A 1 79  ? 183.247 181.297 112.999 1.00 61.36  ?  98  GLU A OE1   1 
ATOM   634   O  OE2   . GLU A 1 79  ? 185.099 180.284 112.397 1.00 62.85  -1 98  GLU A OE2   1 
ATOM   635   N  N     . LEU A 1 80  ? 187.394 181.345 107.471 1.00 57.61  ?  99  LEU A N     1 
ATOM   636   C  CA    . LEU A 1 80  ? 188.648 180.983 106.830 1.00 59.69  ?  99  LEU A CA    1 
ATOM   637   C  C     . LEU A 1 80  ? 189.420 182.225 106.412 1.00 70.16  ?  99  LEU A C     1 
ATOM   638   O  O     . LEU A 1 80  ? 188.853 183.291 106.158 1.00 72.52  ?  99  LEU A O     1 
ATOM   639   C  CB    . LEU A 1 80  ? 188.421 180.060 105.624 1.00 61.53  ?  99  LEU A CB    1 
ATOM   640   C  CG    . LEU A 1 80  ? 188.083 178.622 106.029 1.00 70.56  ?  99  LEU A CG    1 
ATOM   641   C  CD1   . LEU A 1 80  ? 187.867 177.727 104.822 1.00 69.86  ?  99  LEU A CD1   1 
ATOM   642   C  CD2   . LEU A 1 80  ? 189.169 178.053 106.931 1.00 71.86  ?  99  LEU A CD2   1 
ATOM   643   N  N     . GLN A 1 81  ? 190.739 182.063 106.356 1.00 79.51  ?  100 GLN A N     1 
ATOM   644   C  CA    . GLN A 1 81  ? 191.655 183.149 106.039 1.00 73.42  ?  100 GLN A CA    1 
ATOM   645   C  C     . GLN A 1 81  ? 191.726 183.324 104.528 1.00 75.72  ?  100 GLN A C     1 
ATOM   646   O  O     . GLN A 1 81  ? 192.027 182.372 103.799 1.00 77.87  ?  100 GLN A O     1 
ATOM   647   C  CB    . GLN A 1 81  ? 193.040 182.863 106.617 1.00 71.95  ?  100 GLN A CB    1 
ATOM   648   C  CG    . GLN A 1 81  ? 193.848 184.102 106.949 1.00 75.86  ?  100 GLN A CG    1 
ATOM   649   C  CD    . GLN A 1 81  ? 195.002 183.805 107.886 1.00 79.69  ?  100 GLN A CD    1 
ATOM   650   O  OE1   . GLN A 1 81  ? 195.863 182.977 107.587 1.00 81.25  ?  100 GLN A OE1   1 
ATOM   651   N  NE2   . GLN A 1 81  ? 195.025 184.481 109.028 1.00 77.57  ?  100 GLN A NE2   1 
ATOM   652   N  N     . LEU A 1 82  ? 191.451 184.538 104.064 1.00 82.64  ?  101 LEU A N     1 
ATOM   653   C  CA    . LEU A 1 82  ? 191.494 184.886 102.652 1.00 84.71  ?  101 LEU A CA    1 
ATOM   654   C  C     . LEU A 1 82  ? 192.578 185.932 102.431 1.00 84.70  ?  101 LEU A C     1 
ATOM   655   O  O     . LEU A 1 82  ? 192.614 186.951 103.130 1.00 84.47  ?  101 LEU A O     1 
ATOM   656   C  CB    . LEU A 1 82  ? 190.139 185.415 102.180 1.00 84.03  ?  101 LEU A CB    1 
ATOM   657   C  CG    . LEU A 1 82  ? 190.149 186.159 100.848 1.00 87.16  ?  101 LEU A CG    1 
ATOM   658   C  CD1   . LEU A 1 82  ? 190.509 185.204 99.722  1.00 86.75  ?  101 LEU A CD1   1 
ATOM   659   C  CD2   . LEU A 1 82  ? 188.803 186.819 100.598 1.00 83.53  ?  101 LEU A CD2   1 
ATOM   660   N  N     . GLU A 1 83  ? 193.457 185.678 101.467 1.00 91.94  ?  102 GLU A N     1 
ATOM   661   C  CA    . GLU A 1 83  ? 194.554 186.586 101.165 1.00 91.64  ?  102 GLU A CA    1 
ATOM   662   C  C     . GLU A 1 83  ? 194.165 187.504 100.013 1.00 91.31  ?  102 GLU A C     1 
ATOM   663   O  O     . GLU A 1 83  ? 193.702 187.038 98.968  1.00 92.75  ?  102 GLU A O     1 
ATOM   664   C  CB    . GLU A 1 83  ? 195.823 185.806 100.819 1.00 93.46  ?  102 GLU A CB    1 
ATOM   665   C  CG    . GLU A 1 83  ? 197.007 186.685 100.454 1.00 96.24  ?  102 GLU A CG    1 
ATOM   666   C  CD    . GLU A 1 83  ? 198.266 185.886 100.191 1.00 95.17  ?  102 GLU A CD    1 
ATOM   667   O  OE1   . GLU A 1 83  ? 198.220 184.644 100.311 1.00 94.50  ?  102 GLU A OE1   1 
ATOM   668   O  OE2   . GLU A 1 83  ? 199.304 186.502 99.867  1.00 94.14  -1 102 GLU A OE2   1 
ATOM   669   N  N     . LYS A 1 84  ? 194.359 188.805 100.209 1.00 93.36  ?  103 LYS A N     1 
ATOM   670   C  CA    . LYS A 1 84  ? 194.015 189.793 99.200  1.00 96.80  ?  103 LYS A CA    1 
ATOM   671   C  C     . LYS A 1 84  ? 195.105 189.860 98.132  1.00 101.11 ?  103 LYS A C     1 
ATOM   672   O  O     . LYS A 1 84  ? 196.075 189.097 98.141  1.00 103.17 ?  103 LYS A O     1 
ATOM   673   C  CB    . LYS A 1 84  ? 193.799 191.159 99.847  1.00 97.83  ?  103 LYS A CB    1 
ATOM   674   C  CG    . LYS A 1 84  ? 192.509 191.285 100.639 1.00 99.49  ?  103 LYS A CG    1 
ATOM   675   C  CD    . LYS A 1 84  ? 192.193 192.743 100.933 1.00 99.56  ?  103 LYS A CD    1 
ATOM   676   C  CE    . LYS A 1 84  ? 190.948 192.880 101.793 1.00 99.14  ?  103 LYS A CE    1 
ATOM   677   N  NZ    . LYS A 1 84  ? 190.509 194.298 101.911 1.00 98.91  1  103 LYS A NZ    1 
ATOM   678   N  N     . LYS A 1 85  ? 194.934 190.787 97.186  1.00 99.13  ?  104 LYS A N     1 
ATOM   679   C  CA    . LYS A 1 85  ? 195.931 190.967 96.135  1.00 94.43  ?  104 LYS A CA    1 
ATOM   680   C  C     . LYS A 1 85  ? 197.261 191.439 96.709  1.00 97.25  ?  104 LYS A C     1 
ATOM   681   O  O     . LYS A 1 85  ? 198.327 190.973 96.290  1.00 99.38  ?  104 LYS A O     1 
ATOM   682   C  CB    . LYS A 1 85  ? 195.418 191.955 95.088  1.00 95.09  ?  104 LYS A CB    1 
ATOM   683   C  CG    . LYS A 1 85  ? 196.349 192.140 93.901  1.00 97.30  ?  104 LYS A CG    1 
ATOM   684   C  CD    . LYS A 1 85  ? 195.700 192.990 92.819  1.00 97.80  ?  104 LYS A CD    1 
ATOM   685   C  CE    . LYS A 1 85  ? 196.537 193.007 91.551  1.00 98.25  ?  104 LYS A CE    1 
ATOM   686   N  NZ    . LYS A 1 85  ? 195.856 193.744 90.450  1.00 96.77  1  104 LYS A NZ    1 
ATOM   687   N  N     . ASP A 1 86  ? 197.219 192.364 97.670  1.00 100.57 ?  105 ASP A N     1 
ATOM   688   C  CA    . ASP A 1 86  ? 198.439 192.885 98.276  1.00 102.02 ?  105 ASP A CA    1 
ATOM   689   C  C     . ASP A 1 86  ? 199.097 191.899 99.231  1.00 99.86  ?  105 ASP A C     1 
ATOM   690   O  O     . ASP A 1 86  ? 200.222 192.153 99.675  1.00 100.93 ?  105 ASP A O     1 
ATOM   691   C  CB    . ASP A 1 86  ? 198.144 194.196 99.009  1.00 101.01 ?  105 ASP A CB    1 
ATOM   692   C  CG    . ASP A 1 86  ? 197.066 194.047 100.067 1.00 99.70  ?  105 ASP A CG    1 
ATOM   693   O  OD1   . ASP A 1 86  ? 196.475 192.952 100.174 1.00 99.52  ?  105 ASP A OD1   1 
ATOM   694   O  OD2   . ASP A 1 86  ? 196.811 195.028 100.796 1.00 97.12  -1 105 ASP A OD2   1 
ATOM   695   N  N     . GLY A 1 87  ? 198.435 190.791 99.557  1.00 93.46  ?  106 GLY A N     1 
ATOM   696   C  CA    . GLY A 1 87  ? 198.969 189.808 100.473 1.00 93.86  ?  106 GLY A CA    1 
ATOM   697   C  C     . GLY A 1 87  ? 198.372 189.836 101.864 1.00 98.14  ?  106 GLY A C     1 
ATOM   698   O  O     . GLY A 1 87  ? 198.666 188.938 102.662 1.00 98.14  ?  106 GLY A O     1 
ATOM   699   N  N     . SER A 1 88  ? 197.552 190.835 102.181 1.00 98.83  ?  107 SER A N     1 
ATOM   700   C  CA    . SER A 1 88  ? 196.892 190.875 103.478 1.00 97.38  ?  107 SER A CA    1 
ATOM   701   C  C     . SER A 1 88  ? 195.874 189.747 103.586 1.00 96.55  ?  107 SER A C     1 
ATOM   702   O  O     . SER A 1 88  ? 195.143 189.455 102.635 1.00 94.73  ?  107 SER A O     1 
ATOM   703   C  CB    . SER A 1 88  ? 196.209 192.225 103.691 1.00 97.09  ?  107 SER A CB    1 
ATOM   704   O  OG    . SER A 1 88  ? 195.217 192.457 102.706 1.00 98.19  ?  107 SER A OG    1 
ATOM   705   N  N     . LYS A 1 89  ? 195.826 189.113 104.754 1.00 92.00  ?  108 LYS A N     1 
ATOM   706   C  CA    . LYS A 1 89  ? 194.980 187.945 104.989 1.00 92.41  ?  108 LYS A CA    1 
ATOM   707   C  C     . LYS A 1 89  ? 193.888 188.317 105.987 1.00 89.82  ?  108 LYS A C     1 
ATOM   708   O  O     . LYS A 1 89  ? 194.103 188.280 107.202 1.00 88.76  ?  108 LYS A O     1 
ATOM   709   C  CB    . LYS A 1 89  ? 195.813 186.767 105.485 1.00 90.35  ?  108 LYS A CB    1 
ATOM   710   C  CG    . LYS A 1 89  ? 196.761 186.201 104.441 1.00 89.46  ?  108 LYS A CG    1 
ATOM   711   C  CD    . LYS A 1 89  ? 197.319 184.855 104.870 1.00 90.01  ?  108 LYS A CD    1 
ATOM   712   C  CE    . LYS A 1 89  ? 198.183 184.245 103.778 1.00 90.49  ?  108 LYS A CE    1 
ATOM   713   N  NZ    . LYS A 1 89  ? 198.700 182.903 104.164 1.00 89.72  1  108 LYS A NZ    1 
ATOM   714   N  N     . ILE A 1 90  ? 192.717 188.677 105.464 1.00 79.68  ?  109 ILE A N     1 
ATOM   715   C  CA    . ILE A 1 90  ? 191.538 188.941 106.281 1.00 78.49  ?  109 ILE A CA    1 
ATOM   716   C  C     . ILE A 1 90  ? 190.862 187.618 106.613 1.00 82.26  ?  109 ILE A C     1 
ATOM   717   O  O     . ILE A 1 90  ? 191.236 186.569 106.079 1.00 85.41  ?  109 ILE A O     1 
ATOM   718   C  CB    . ILE A 1 90  ? 190.565 189.898 105.569 1.00 76.14  ?  109 ILE A CB    1 
ATOM   719   C  CG1   . ILE A 1 90  ? 189.906 189.200 104.378 1.00 76.56  ?  109 ILE A CG1   1 
ATOM   720   C  CG2   . ILE A 1 90  ? 191.291 191.157 105.123 1.00 76.61  ?  109 ILE A CG2   1 
ATOM   721   C  CD1   . ILE A 1 90  ? 188.995 190.099 103.571 1.00 79.97  ?  109 ILE A CD1   1 
ATOM   722   N  N     . TRP A 1 91  ? 189.891 187.649 107.520 1.00 70.39  ?  110 TRP A N     1 
ATOM   723   C  CA    . TRP A 1 91  ? 189.077 186.485 107.846 1.00 65.88  ?  110 TRP A CA    1 
ATOM   724   C  C     . TRP A 1 91  ? 187.687 186.670 107.254 1.00 65.09  ?  110 TRP A C     1 
ATOM   725   O  O     . TRP A 1 91  ? 187.056 187.712 107.461 1.00 69.17  ?  110 TRP A O     1 
ATOM   726   C  CB    . TRP A 1 91  ? 188.989 186.281 109.360 1.00 61.29  ?  110 TRP A CB    1 
ATOM   727   C  CG    . TRP A 1 91  ? 190.249 185.761 109.980 1.00 61.12  ?  110 TRP A CG    1 
ATOM   728   C  CD1   . TRP A 1 91  ? 191.180 186.480 110.671 1.00 66.38  ?  110 TRP A CD1   1 
ATOM   729   C  CD2   . TRP A 1 91  ? 190.712 184.405 109.975 1.00 64.85  ?  110 TRP A CD2   1 
ATOM   730   N  NE1   . TRP A 1 91  ? 192.196 185.657 111.093 1.00 72.68  ?  110 TRP A NE1   1 
ATOM   731   C  CE2   . TRP A 1 91  ? 191.931 184.378 110.680 1.00 70.31  ?  110 TRP A CE2   1 
ATOM   732   C  CE3   . TRP A 1 91  ? 190.214 183.212 109.445 1.00 66.99  ?  110 TRP A CE3   1 
ATOM   733   C  CZ2   . TRP A 1 91  ? 192.661 183.205 110.866 1.00 67.19  ?  110 TRP A CZ2   1 
ATOM   734   C  CZ3   . TRP A 1 91  ? 190.938 182.049 109.630 1.00 68.95  ?  110 TRP A CZ3   1 
ATOM   735   C  CH2   . TRP A 1 91  ? 192.148 182.054 110.334 1.00 66.72  ?  110 TRP A CH2   1 
ATOM   736   N  N     . THR A 1 92  ? 187.212 185.665 106.519 1.00 51.15  ?  111 THR A N     1 
ATOM   737   C  CA    . THR A 1 92  ? 185.932 185.743 105.831 1.00 46.49  ?  111 THR A CA    1 
ATOM   738   C  C     . THR A 1 92  ? 185.062 184.554 106.210 1.00 56.16  ?  111 THR A C     1 
ATOM   739   O  O     . THR A 1 92  ? 185.563 183.472 106.543 1.00 66.33  ?  111 THR A O     1 
ATOM   740   C  CB    . THR A 1 92  ? 186.106 185.777 104.306 1.00 54.64  ?  111 THR A CB    1 
ATOM   741   O  OG1   . THR A 1 92  ? 186.684 184.544 103.861 1.00 61.98  ?  111 THR A OG1   1 
ATOM   742   C  CG2   . THR A 1 92  ? 187.008 186.931 103.895 1.00 64.28  ?  111 THR A CG2   1 
ATOM   743   N  N     . ARG A 1 93  ? 183.747 184.764 106.150 1.00 61.17  ?  112 ARG A N     1 
ATOM   744   C  CA    . ARG A 1 93  ? 182.773 183.709 106.388 1.00 51.06  ?  112 ARG A CA    1 
ATOM   745   C  C     . ARG A 1 93  ? 182.040 183.414 105.089 1.00 52.82  ?  112 ARG A C     1 
ATOM   746   O  O     . ARG A 1 93  ? 181.472 184.320 104.469 1.00 66.91  ?  112 ARG A O     1 
ATOM   747   C  CB    . ARG A 1 93  ? 181.785 184.099 107.486 1.00 50.93  ?  112 ARG A CB    1 
ATOM   748   C  CG    . ARG A 1 93  ? 180.912 182.952 107.964 1.00 58.46  ?  112 ARG A CG    1 
ATOM   749   C  CD    . ARG A 1 93  ? 181.701 181.999 108.842 1.00 59.81  ?  112 ARG A CD    1 
ATOM   750   N  NE    . ARG A 1 93  ? 180.834 181.110 109.604 1.00 59.43  ?  112 ARG A NE    1 
ATOM   751   C  CZ    . ARG A 1 93  ? 180.579 181.242 110.899 1.00 60.65  ?  112 ARG A CZ    1 
ATOM   752   N  NH1   . ARG A 1 93  ? 181.111 182.222 111.611 1.00 58.75  1  112 ARG A NH1   1 
ATOM   753   N  NH2   . ARG A 1 93  ? 179.767 180.372 111.492 1.00 63.72  ?  112 ARG A NH2   1 
ATOM   754   N  N     . PHE A 1 94  ? 182.049 182.149 104.686 1.00 30.31  ?  113 PHE A N     1 
ATOM   755   C  CA    . PHE A 1 94  ? 181.509 181.719 103.408 1.00 39.87  ?  113 PHE A CA    1 
ATOM   756   C  C     . PHE A 1 94  ? 180.151 181.055 103.590 1.00 43.66  ?  113 PHE A C     1 
ATOM   757   O  O     . PHE A 1 94  ? 179.799 180.584 104.675 1.00 49.51  ?  113 PHE A O     1 
ATOM   758   C  CB    . PHE A 1 94  ? 182.468 180.746 102.715 1.00 49.36  ?  113 PHE A CB    1 
ATOM   759   C  CG    . PHE A 1 94  ? 183.440 181.405 101.776 1.00 49.48  ?  113 PHE A CG    1 
ATOM   760   C  CD1   . PHE A 1 94  ? 184.413 182.270 102.251 1.00 49.10  ?  113 PHE A CD1   1 
ATOM   761   C  CD2   . PHE A 1 94  ? 183.402 181.132 100.417 1.00 48.27  ?  113 PHE A CD2   1 
ATOM   762   C  CE1   . PHE A 1 94  ? 185.316 182.865 101.387 1.00 49.59  ?  113 PHE A CE1   1 
ATOM   763   C  CE2   . PHE A 1 94  ? 184.302 181.722 99.549  1.00 53.32  ?  113 PHE A CE2   1 
ATOM   764   C  CZ    . PHE A 1 94  ? 185.261 182.589 100.034 1.00 53.08  ?  113 PHE A CZ    1 
ATOM   765   N  N     . ALA A 1 95  ? 179.388 181.032 102.501 1.00 50.26  ?  114 ALA A N     1 
ATOM   766   C  CA    . ALA A 1 95  ? 178.118 180.314 102.453 1.00 51.03  ?  114 ALA A CA    1 
ATOM   767   C  C     . ALA A 1 95  ? 177.933 179.834 101.022 1.00 52.78  ?  114 ALA A C     1 
ATOM   768   O  O     . ALA A 1 95  ? 177.664 180.645 100.132 1.00 63.62  ?  114 ALA A O     1 
ATOM   769   C  CB    . ALA A 1 95  ? 176.959 181.204 102.894 1.00 56.69  ?  114 ALA A CB    1 
ATOM   770   N  N     . LEU A 1 96  ? 178.088 178.533 100.801 1.00 47.21  ?  115 LEU A N     1 
ATOM   771   C  CA    . LEU A 1 96  ? 178.061 177.987 99.453  1.00 50.67  ?  115 LEU A CA    1 
ATOM   772   C  C     . LEU A 1 96  ? 176.658 177.543 99.054  1.00 51.59  ?  115 LEU A C     1 
ATOM   773   O  O     . LEU A 1 96  ? 175.785 177.302 99.891  1.00 58.85  ?  115 LEU A O     1 
ATOM   774   C  CB    . LEU A 1 96  ? 179.028 176.810 99.320  1.00 56.63  ?  115 LEU A CB    1 
ATOM   775   C  CG    . LEU A 1 96  ? 180.524 177.119 99.391  1.00 58.42  ?  115 LEU A CG    1 
ATOM   776   C  CD1   . LEU A 1 96  ? 181.331 175.900 98.974  1.00 60.76  ?  115 LEU A CD1   1 
ATOM   777   C  CD2   . LEU A 1 96  ? 180.871 178.316 98.524  1.00 58.08  ?  115 LEU A CD2   1 
ATOM   778   N  N     . SER A 1 97  ? 176.461 177.432 97.743  1.00 62.02  ?  116 SER A N     1 
ATOM   779   C  CA    . SER A 1 97  ? 175.189 176.986 97.181  1.00 64.40  ?  116 SER A CA    1 
ATOM   780   C  C     . SER A 1 97  ? 175.464 176.330 95.839  1.00 63.72  ?  116 SER A C     1 
ATOM   781   O  O     . SER A 1 97  ? 176.057 176.958 94.954  1.00 70.27  ?  116 SER A O     1 
ATOM   782   C  CB    . SER A 1 97  ? 174.218 178.155 97.023  1.00 68.04  ?  116 SER A CB    1 
ATOM   783   O  OG    . SER A 1 97  ? 173.727 178.582 98.280  1.00 68.11  ?  116 SER A OG    1 
ATOM   784   N  N     . LYS A 1 98  ? 175.047 175.076 95.691  1.00 75.90  ?  117 LYS A N     1 
ATOM   785   C  CA    . LYS A 1 98  ? 175.210 174.341 94.444  1.00 80.00  ?  117 LYS A CA    1 
ATOM   786   C  C     . LYS A 1 98  ? 173.985 174.573 93.569  1.00 76.48  ?  117 LYS A C     1 
ATOM   787   O  O     . LYS A 1 98  ? 172.854 174.313 93.995  1.00 77.66  ?  117 LYS A O     1 
ATOM   788   C  CB    . LYS A 1 98  ? 175.405 172.850 94.717  1.00 83.48  ?  117 LYS A CB    1 
ATOM   789   C  CG    . LYS A 1 98  ? 175.567 172.006 93.465  1.00 83.45  ?  117 LYS A CG    1 
ATOM   790   C  CD    . LYS A 1 98  ? 175.713 170.532 93.806  1.00 82.31  ?  117 LYS A CD    1 
ATOM   791   C  CE    . LYS A 1 98  ? 177.152 170.183 94.150  1.00 80.84  ?  117 LYS A CE    1 
ATOM   792   N  NZ    . LYS A 1 98  ? 177.386 168.712 94.128  1.00 83.72  1  117 LYS A NZ    1 
ATOM   793   N  N     . VAL A 1 99  ? 174.208 175.063 92.354  1.00 83.66  ?  118 VAL A N     1 
ATOM   794   C  CA    . VAL A 1 99  ? 173.134 175.383 91.420  1.00 87.08  ?  118 VAL A CA    1 
ATOM   795   C  C     . VAL A 1 99  ? 173.331 174.502 90.193  1.00 90.78  ?  118 VAL A C     1 
ATOM   796   O  O     . VAL A 1 99  ? 174.226 174.750 89.375  1.00 97.08  ?  118 VAL A O     1 
ATOM   797   C  CB    . VAL A 1 99  ? 173.115 176.867 91.042  1.00 90.38  ?  118 VAL A CB    1 
ATOM   798   C  CG1   . VAL A 1 99  ? 172.042 177.137 89.997  1.00 91.76  ?  118 VAL A CG1   1 
ATOM   799   C  CG2   . VAL A 1 99  ? 172.896 177.724 92.278  1.00 89.73  ?  118 VAL A CG2   1 
ATOM   800   N  N     . SER A 1 100 ? 172.498 173.470 90.059  1.00 97.89  ?  119 SER A N     1 
ATOM   801   C  CA    . SER A 1 100 ? 172.526 172.596 88.887  1.00 102.01 ?  119 SER A CA    1 
ATOM   802   C  C     . SER A 1 100 ? 171.563 173.163 87.848  1.00 103.75 ?  119 SER A C     1 
ATOM   803   O  O     . SER A 1 100 ? 170.444 172.683 87.652  1.00 102.11 ?  119 SER A O     1 
ATOM   804   C  CB    . SER A 1 100 ? 172.171 171.166 89.273  1.00 102.85 ?  119 SER A CB    1 
ATOM   805   O  OG    . SER A 1 100 ? 172.119 170.327 88.132  1.00 102.74 ?  119 SER A OG    1 
ATOM   806   N  N     . ALA A 1 101 ? 172.018 174.211 87.168  1.00 106.96 ?  120 ALA A N     1 
ATOM   807   C  CA    . ALA A 1 101 ? 171.214 174.918 86.181  1.00 104.75 ?  120 ALA A CA    1 
ATOM   808   C  C     . ALA A 1 101 ? 171.606 174.470 84.780  1.00 104.87 ?  120 ALA A C     1 
ATOM   809   O  O     . ALA A 1 101 ? 172.792 174.475 84.431  1.00 104.02 ?  120 ALA A O     1 
ATOM   810   C  CB    . ALA A 1 101 ? 171.386 176.432 86.319  1.00 101.05 ?  120 ALA A CB    1 
ATOM   811   N  N     . GLU A 1 102 ? 170.605 174.082 83.986  1.00 102.15 ?  121 GLU A N     1 
ATOM   812   C  CA    . GLU A 1 102 ? 170.805 173.639 82.606  1.00 101.60 ?  121 GLU A CA    1 
ATOM   813   C  C     . GLU A 1 102 ? 171.776 172.464 82.523  1.00 103.00 ?  121 GLU A C     1 
ATOM   814   O  O     . GLU A 1 102 ? 172.534 172.338 81.558  1.00 102.79 ?  121 GLU A O     1 
ATOM   815   C  CB    . GLU A 1 102 ? 171.280 174.792 81.716  1.00 100.51 ?  121 GLU A CB    1 
ATOM   816   C  CG    . GLU A 1 102 ? 170.735 174.754 80.296  1.00 100.29 ?  121 GLU A CG    1 
ATOM   817   C  CD    . GLU A 1 102 ? 171.330 175.835 79.415  1.00 100.87 ?  121 GLU A CD    1 
ATOM   818   O  OE1   . GLU A 1 102 ? 172.176 176.608 79.911  1.00 100.49 ?  121 GLU A OE1   1 
ATOM   819   O  OE2   . GLU A 1 102 ? 170.953 175.912 78.226  1.00 98.86  -1 121 GLU A OE2   1 
ATOM   820   N  N     . GLY A 1 103 ? 171.763 171.599 83.534  1.00 101.84 ?  122 GLY A N     1 
ATOM   821   C  CA    . GLY A 1 103 ? 172.652 170.457 83.563  1.00 100.39 ?  122 GLY A CA    1 
ATOM   822   C  C     . GLY A 1 103 ? 174.086 170.771 83.914  1.00 102.63 ?  122 GLY A C     1 
ATOM   823   O  O     . GLY A 1 103 ? 174.936 169.876 83.839  1.00 103.79 ?  122 GLY A O     1 
ATOM   824   N  N     . LYS A 1 104 ? 174.386 172.009 84.296  1.00 97.76  ?  123 LYS A N     1 
ATOM   825   C  CA    . LYS A 1 104 ? 175.731 172.421 84.667  1.00 96.23  ?  123 LYS A CA    1 
ATOM   826   C  C     . LYS A 1 104 ? 175.753 172.813 86.136  1.00 92.54  ?  123 LYS A C     1 
ATOM   827   O  O     . LYS A 1 104 ? 174.901 173.578 86.598  1.00 93.40  ?  123 LYS A O     1 
ATOM   828   C  CB    . LYS A 1 104 ? 176.211 173.590 83.801  1.00 97.15  ?  123 LYS A CB    1 
ATOM   829   C  CG    . LYS A 1 104 ? 176.590 173.193 82.383  1.00 98.38  ?  123 LYS A CG    1 
ATOM   830   C  CD    . LYS A 1 104 ? 176.929 174.409 81.536  1.00 97.61  ?  123 LYS A CD    1 
ATOM   831   C  CE    . LYS A 1 104 ? 175.849 175.474 81.638  1.00 97.05  ?  123 LYS A CE    1 
ATOM   832   N  NZ    . LYS A 1 104 ? 176.144 176.649 80.773  1.00 97.39  1  123 LYS A NZ    1 
ATOM   833   N  N     . VAL A 1 105 ? 176.729 172.284 86.865  1.00 88.86  ?  124 VAL A N     1 
ATOM   834   C  CA    . VAL A 1 105 ? 176.846 172.524 88.298  1.00 91.36  ?  124 VAL A CA    1 
ATOM   835   C  C     . VAL A 1 105 ? 177.570 173.846 88.515  1.00 90.77  ?  124 VAL A C     1 
ATOM   836   O  O     . VAL A 1 105 ? 178.777 173.953 88.270  1.00 94.62  ?  124 VAL A O     1 
ATOM   837   C  CB    . VAL A 1 105 ? 177.581 171.371 88.996  1.00 95.44  ?  124 VAL A CB    1 
ATOM   838   C  CG1   . VAL A 1 105 ? 177.666 171.625 90.492  1.00 93.26  ?  124 VAL A CG1   1 
ATOM   839   C  CG2   . VAL A 1 105 ? 176.885 170.049 88.712  1.00 94.42  ?  124 VAL A CG2   1 
ATOM   840   N  N     . TYR A 1 106 ? 176.833 174.852 88.972  1.00 84.80  ?  125 TYR A N     1 
ATOM   841   C  CA    . TYR A 1 106 ? 177.399 176.136 89.353  1.00 84.59  ?  125 TYR A CA    1 
ATOM   842   C  C     . TYR A 1 106 ? 177.689 176.143 90.849  1.00 81.56  ?  125 TYR A C     1 
ATOM   843   O  O     . TYR A 1 106 ? 177.302 175.234 91.586  1.00 85.33  ?  125 TYR A O     1 
ATOM   844   C  CB    . TYR A 1 106 ? 176.443 177.276 88.988  1.00 84.64  ?  125 TYR A CB    1 
ATOM   845   C  CG    . TYR A 1 106 ? 176.624 177.818 87.589  1.00 85.69  ?  125 TYR A CG    1 
ATOM   846   C  CD1   . TYR A 1 106 ? 176.288 177.054 86.479  1.00 86.58  ?  125 TYR A CD1   1 
ATOM   847   C  CD2   . TYR A 1 106 ? 177.120 179.096 87.377  1.00 85.20  ?  125 TYR A CD2   1 
ATOM   848   C  CE1   . TYR A 1 106 ? 176.448 177.547 85.196  1.00 86.64  ?  125 TYR A CE1   1 
ATOM   849   C  CE2   . TYR A 1 106 ? 177.283 179.598 86.100  1.00 86.91  ?  125 TYR A CE2   1 
ATOM   850   C  CZ    . TYR A 1 106 ? 176.946 178.819 85.013  1.00 87.55  ?  125 TYR A CZ    1 
ATOM   851   O  OH    . TYR A 1 106 ? 177.106 179.315 83.740  1.00 87.87  ?  125 TYR A OH    1 
ATOM   852   N  N     . TYR A 1 107 ? 178.381 177.188 91.298  1.00 70.44  ?  126 TYR A N     1 
ATOM   853   C  CA    . TYR A 1 107 ? 178.651 177.353 92.723  1.00 70.95  ?  126 TYR A CA    1 
ATOM   854   C  C     . TYR A 1 107 ? 178.591 178.827 93.084  1.00 75.07  ?  126 TYR A C     1 
ATOM   855   O  O     . TYR A 1 107 ? 179.341 179.633 92.530  1.00 84.01  ?  126 TYR A O     1 
ATOM   856   C  CB    . TYR A 1 107 ? 180.009 176.760 93.109  1.00 76.62  ?  126 TYR A CB    1 
ATOM   857   C  CG    . TYR A 1 107 ? 180.059 175.252 93.023  1.00 79.95  ?  126 TYR A CG    1 
ATOM   858   C  CD1   . TYR A 1 107 ? 180.634 174.615 91.932  1.00 80.86  ?  126 TYR A CD1   1 
ATOM   859   C  CD2   . TYR A 1 107 ? 179.519 174.466 94.031  1.00 78.66  ?  126 TYR A CD2   1 
ATOM   860   C  CE1   . TYR A 1 107 ? 180.677 173.235 91.852  1.00 81.67  ?  126 TYR A CE1   1 
ATOM   861   C  CE2   . TYR A 1 107 ? 179.557 173.087 93.961  1.00 79.80  ?  126 TYR A CE2   1 
ATOM   862   C  CZ    . TYR A 1 107 ? 180.137 172.477 92.870  1.00 82.79  ?  126 TYR A CZ    1 
ATOM   863   O  OH    . TYR A 1 107 ? 180.174 171.104 92.798  1.00 81.73  ?  126 TYR A OH    1 
ATOM   864   N  N     . LEU A 1 108 ? 177.712 179.170 94.021  1.00 60.22  ?  127 LEU A N     1 
ATOM   865   C  CA    . LEU A 1 108 ? 177.562 180.533 94.508  1.00 59.02  ?  127 LEU A CA    1 
ATOM   866   C  C     . LEU A 1 108 ? 178.105 180.621 95.926  1.00 50.28  ?  127 LEU A C     1 
ATOM   867   O  O     . LEU A 1 108 ? 177.937 179.692 96.722  1.00 55.37  ?  127 LEU A O     1 
ATOM   868   C  CB    . LEU A 1 108 ? 176.094 180.970 94.471  1.00 59.87  ?  127 LEU A CB    1 
ATOM   869   C  CG    . LEU A 1 108 ? 175.758 182.362 95.008  1.00 59.49  ?  127 LEU A CG    1 
ATOM   870   C  CD1   . LEU A 1 108 ? 176.373 183.434 94.126  1.00 62.80  ?  127 LEU A CD1   1 
ATOM   871   C  CD2   . LEU A 1 108 ? 174.250 182.546 95.106  1.00 58.52  ?  127 LEU A CD2   1 
ATOM   872   N  N     . ALA A 1 109 ? 178.763 181.736 96.238  1.00 41.97  ?  128 ALA A N     1 
ATOM   873   C  CA    . ALA A 1 109 ? 179.410 181.922 97.534  1.00 41.62  ?  128 ALA A CA    1 
ATOM   874   C  C     . ALA A 1 109 ? 179.029 183.291 98.078  1.00 47.34  ?  128 ALA A C     1 
ATOM   875   O  O     . ALA A 1 109 ? 179.502 184.314 97.575  1.00 58.90  ?  128 ALA A O     1 
ATOM   876   C  CB    . ALA A 1 109 ? 180.928 181.787 97.418  1.00 53.12  ?  128 ALA A CB    1 
ATOM   877   N  N     . LEU A 1 110 ? 178.176 183.310 99.103  1.00 46.57  ?  129 LEU A N     1 
ATOM   878   C  CA    . LEU A 1 110 ? 177.800 184.551 99.781  1.00 50.17  ?  129 LEU A CA    1 
ATOM   879   C  C     . LEU A 1 110 ? 178.860 184.868 100.832 1.00 49.42  ?  129 LEU A C     1 
ATOM   880   O  O     . LEU A 1 110 ? 178.700 184.623 102.031 1.00 52.82  ?  129 LEU A O     1 
ATOM   881   C  CB    . LEU A 1 110 ? 176.411 184.439 100.396 1.00 54.83  ?  129 LEU A CB    1 
ATOM   882   C  CG    . LEU A 1 110 ? 175.265 185.001 99.552  1.00 54.34  ?  129 LEU A CG    1 
ATOM   883   C  CD1   . LEU A 1 110 ? 175.064 184.179 98.291  1.00 55.76  ?  129 LEU A CD1   1 
ATOM   884   C  CD2   . LEU A 1 110 ? 173.982 185.082 100.360 1.00 53.75  ?  129 LEU A CD2   1 
ATOM   885   N  N     . VAL A 1 111 ? 179.974 185.425 100.357 1.00 54.87  ?  130 VAL A N     1 
ATOM   886   C  CA    . VAL A 1 111 ? 181.070 185.801 101.237 1.00 52.08  ?  130 VAL A CA    1 
ATOM   887   C  C     . VAL A 1 111 ? 180.663 187.008 102.070 1.00 53.21  ?  130 VAL A C     1 
ATOM   888   O  O     . VAL A 1 111 ? 180.050 187.960 101.565 1.00 66.49  ?  130 VAL A O     1 
ATOM   889   C  CB    . VAL A 1 111 ? 182.332 186.102 100.410 1.00 64.48  ?  130 VAL A CB    1 
ATOM   890   C  CG1   . VAL A 1 111 ? 183.468 186.577 101.309 1.00 65.81  ?  130 VAL A CG1   1 
ATOM   891   C  CG2   . VAL A 1 111 ? 182.736 184.891 99.592  1.00 64.58  ?  130 VAL A CG2   1 
ATOM   892   N  N     . ARG A 1 112 ? 180.998 186.975 103.356 1.00 41.08  ?  131 ARG A N     1 
ATOM   893   C  CA    . ARG A 1 112 ? 180.819 188.127 104.222 1.00 45.97  ?  131 ARG A CA    1 
ATOM   894   C  C     . ARG A 1 112 ? 182.112 188.389 104.974 1.00 46.34  ?  131 ARG A C     1 
ATOM   895   O  O     . ARG A 1 112 ? 182.842 187.455 105.328 1.00 57.00  ?  131 ARG A O     1 
ATOM   896   C  CB    . ARG A 1 112 ? 179.655 187.931 105.204 1.00 54.37  ?  131 ARG A CB    1 
ATOM   897   C  CG    . ARG A 1 112 ? 179.786 186.743 106.135 1.00 55.53  ?  131 ARG A CG    1 
ATOM   898   C  CD    . ARG A 1 112 ? 178.732 186.805 107.232 1.00 50.34  ?  131 ARG A CD    1 
ATOM   899   N  NE    . ARG A 1 112 ? 178.901 185.753 108.227 1.00 49.96  ?  131 ARG A NE    1 
ATOM   900   C  CZ    . ARG A 1 112 ? 179.171 185.969 109.507 1.00 51.99  ?  131 ARG A CZ    1 
ATOM   901   N  NH1   . ARG A 1 112 ? 179.314 187.194 109.986 1.00 48.86  1  131 ARG A NH1   1 
ATOM   902   N  NH2   . ARG A 1 112 ? 179.301 184.930 110.327 1.00 54.13  ?  131 ARG A NH2   1 
ATOM   903   N  N     . ASP A 1 113 ? 182.394 189.671 105.202 1.00 58.77  ?  132 ASP A N     1 
ATOM   904   C  CA    . ASP A 1 113 ? 183.611 190.063 105.896 1.00 62.44  ?  132 ASP A CA    1 
ATOM   905   C  C     . ASP A 1 113 ? 183.507 189.709 107.372 1.00 56.69  ?  132 ASP A C     1 
ATOM   906   O  O     . ASP A 1 113 ? 182.975 190.479 108.178 1.00 62.56  ?  132 ASP A O     1 
ATOM   907   C  CB    . ASP A 1 113 ? 183.894 191.558 105.695 1.00 64.87  ?  132 ASP A CB    1 
ATOM   908   C  CG    . ASP A 1 113 ? 182.693 192.437 106.008 1.00 68.05  ?  132 ASP A CG    1 
ATOM   909   O  OD1   . ASP A 1 113 ? 181.602 191.896 106.285 1.00 70.58  ?  132 ASP A OD1   1 
ATOM   910   O  OD2   . ASP A 1 113 ? 182.847 193.677 105.980 1.00 65.39  -1 132 ASP A OD2   1 
ATOM   911   N  N     . ALA A 1 114 ? 184.024 188.539 107.733 1.00 50.93  ?  133 ALA A N     1 
ATOM   912   C  CA    . ALA A 1 114 ? 184.013 188.070 109.108 1.00 50.95  ?  133 ALA A CA    1 
ATOM   913   C  C     . ALA A 1 114 ? 185.105 188.708 109.945 1.00 51.93  ?  133 ALA A C     1 
ATOM   914   O  O     . ALA A 1 114 ? 185.453 188.167 110.998 1.00 56.72  ?  133 ALA A O     1 
ATOM   915   C  CB    . ALA A 1 114 ? 184.146 186.546 109.148 1.00 58.44  ?  133 ALA A CB    1 
ATOM   916   N  N     . SER A 1 115 ? 185.665 189.831 109.489 1.00 55.05  ?  134 SER A N     1 
ATOM   917   C  CA    . SER A 1 115 ? 186.717 190.498 110.245 1.00 58.72  ?  134 SER A CA    1 
ATOM   918   C  C     . SER A 1 115 ? 186.224 190.910 111.625 1.00 59.88  ?  134 SER A C     1 
ATOM   919   O  O     . SER A 1 115 ? 186.888 190.650 112.632 1.00 62.62  ?  134 SER A O     1 
ATOM   920   C  CB    . SER A 1 115 ? 187.230 191.713 109.470 1.00 60.25  ?  134 SER A CB    1 
ATOM   921   O  OG    . SER A 1 115 ? 186.188 192.643 109.231 1.00 60.52  ?  134 SER A OG    1 
ATOM   922   N  N     . VAL A 1 116 ? 185.042 191.526 111.696 1.00 57.39  ?  135 VAL A N     1 
ATOM   923   C  CA    . VAL A 1 116 ? 184.532 191.998 112.981 1.00 54.32  ?  135 VAL A CA    1 
ATOM   924   C  C     . VAL A 1 116 ? 184.143 190.826 113.879 1.00 58.78  ?  135 VAL A C     1 
ATOM   925   O  O     . VAL A 1 116 ? 184.441 190.823 115.080 1.00 58.36  ?  135 VAL A O     1 
ATOM   926   C  CB    . VAL A 1 116 ? 183.360 192.976 112.765 1.00 57.27  ?  135 VAL A CB    1 
ATOM   927   C  CG1   . VAL A 1 116 ? 182.273 192.350 111.900 1.00 57.22  ?  135 VAL A CG1   1 
ATOM   928   C  CG2   . VAL A 1 116 ? 182.789 193.427 114.102 1.00 58.86  ?  135 VAL A CG2   1 
ATOM   929   N  N     . GLU A 1 117 ? 183.484 189.810 113.315 1.00 60.04  ?  136 GLU A N     1 
ATOM   930   C  CA    . GLU A 1 117 ? 183.067 188.665 114.119 1.00 55.17  ?  136 GLU A CA    1 
ATOM   931   C  C     . GLU A 1 117 ? 184.269 187.897 114.654 1.00 55.79  ?  136 GLU A C     1 
ATOM   932   O  O     . GLU A 1 117 ? 184.294 187.503 115.826 1.00 60.15  ?  136 GLU A O     1 
ATOM   933   C  CB    . GLU A 1 117 ? 182.162 187.748 113.297 1.00 57.12  ?  136 GLU A CB    1 
ATOM   934   C  CG    . GLU A 1 117 ? 181.656 186.533 114.056 1.00 60.90  ?  136 GLU A CG    1 
ATOM   935   C  CD    . GLU A 1 117 ? 181.128 185.452 113.135 1.00 62.52  ?  136 GLU A CD    1 
ATOM   936   O  OE1   . GLU A 1 117 ? 181.133 185.664 111.904 1.00 60.92  ?  136 GLU A OE1   1 
ATOM   937   O  OE2   . GLU A 1 117 ? 180.709 184.389 113.640 1.00 62.71  -1 136 GLU A OE2   1 
ATOM   938   N  N     . MET A 1 118 ? 185.286 187.685 113.822 1.00 56.11  ?  137 MET A N     1 
ATOM   939   C  CA    . MET A 1 118 ? 186.467 186.979 114.291 1.00 54.47  ?  137 MET A CA    1 
ATOM   940   C  C     . MET A 1 118 ? 187.366 187.853 115.154 1.00 55.39  ?  137 MET A C     1 
ATOM   941   O  O     . MET A 1 118 ? 188.131 187.316 115.955 1.00 58.49  ?  137 MET A O     1 
ATOM   942   C  CB    . MET A 1 118 ? 187.251 186.408 113.112 1.00 53.80  ?  137 MET A CB    1 
ATOM   943   C  CG    . MET A 1 118 ? 188.084 185.197 113.495 1.00 59.93  ?  137 MET A CG    1 
ATOM   944   S  SD    . MET A 1 118 ? 188.237 183.986 112.173 1.00 79.97  ?  137 MET A SD    1 
ATOM   945   C  CE    . MET A 1 118 ? 189.383 182.827 112.916 1.00 62.64  ?  137 MET A CE    1 
ATOM   946   N  N     . ALA A 1 119 ? 187.271 189.180 115.045 1.00 46.10  ?  138 ALA A N     1 
ATOM   947   C  CA    . ALA A 1 119 ? 187.920 190.035 116.031 1.00 46.87  ?  138 ALA A CA    1 
ATOM   948   C  C     . ALA A 1 119 ? 187.233 189.911 117.383 1.00 52.01  ?  138 ALA A C     1 
ATOM   949   O  O     . ALA A 1 119 ? 187.895 189.899 118.425 1.00 54.96  ?  138 ALA A O     1 
ATOM   950   C  CB    . ALA A 1 119 ? 187.920 191.487 115.554 1.00 48.39  ?  138 ALA A CB    1 
ATOM   951   N  N     . GLN A 1 120 ? 185.903 189.802 117.380 1.00 53.60  ?  139 GLN A N     1 
ATOM   952   C  CA    . GLN A 1 120 ? 185.180 189.512 118.614 1.00 52.39  ?  139 GLN A CA    1 
ATOM   953   C  C     . GLN A 1 120 ? 185.593 188.158 119.179 1.00 55.46  ?  139 GLN A C     1 
ATOM   954   O  O     . GLN A 1 120 ? 185.748 188.004 120.395 1.00 52.03  ?  139 GLN A O     1 
ATOM   955   C  CB    . GLN A 1 120 ? 183.673 189.551 118.360 1.00 50.12  ?  139 GLN A CB    1 
ATOM   956   C  CG    . GLN A 1 120 ? 183.067 190.947 118.390 1.00 54.31  ?  139 GLN A CG    1 
ATOM   957   C  CD    . GLN A 1 120 ? 183.061 191.552 119.779 1.00 55.93  ?  139 GLN A CD    1 
ATOM   958   O  OE1   . GLN A 1 120 ? 182.938 190.843 120.777 1.00 52.62  ?  139 GLN A OE1   1 
ATOM   959   N  NE2   . GLN A 1 120 ? 183.194 192.872 119.850 1.00 53.52  ?  139 GLN A NE2   1 
ATOM   960   N  N     . LYS A 1 121 ? 185.772 187.164 118.307 1.00 50.57  ?  140 LYS A N     1 
ATOM   961   C  CA    . LYS A 1 121 ? 186.188 185.840 118.765 1.00 35.86  ?  140 LYS A CA    1 
ATOM   962   C  C     . LYS A 1 121 ? 187.616 185.855 119.307 1.00 42.00  ?  140 LYS A C     1 
ATOM   963   O  O     . LYS A 1 121 ? 187.916 185.181 120.296 1.00 49.26  ?  140 LYS A O     1 
ATOM   964   C  CB    . LYS A 1 121 ? 186.051 184.822 117.633 1.00 43.54  ?  140 LYS A CB    1 
ATOM   965   C  CG    . LYS A 1 121 ? 185.801 183.400 118.116 1.00 46.43  ?  140 LYS A CG    1 
ATOM   966   C  CD    . LYS A 1 121 ? 185.947 182.388 116.990 1.00 46.65  ?  140 LYS A CD    1 
ATOM   967   C  CE    . LYS A 1 121 ? 185.008 182.696 115.836 1.00 45.04  ?  140 LYS A CE    1 
ATOM   968   N  NZ    . LYS A 1 121 ? 183.629 183.022 116.298 1.00 43.25  1  140 LYS A NZ    1 
ATOM   969   N  N     . GLU A 1 122 ? 188.513 186.610 118.673 1.00 44.81  ?  141 GLU A N     1 
ATOM   970   C  CA    . GLU A 1 122 ? 189.865 186.759 119.203 1.00 43.65  ?  141 GLU A CA    1 
ATOM   971   C  C     . GLU A 1 122 ? 189.847 187.468 120.551 1.00 40.31  ?  141 GLU A C     1 
ATOM   972   O  O     . GLU A 1 122 ? 190.579 187.087 121.475 1.00 43.63  ?  141 GLU A O     1 
ATOM   973   C  CB    . GLU A 1 122 ? 190.733 187.522 118.202 1.00 45.18  ?  141 GLU A CB    1 
ATOM   974   C  CG    . GLU A 1 122 ? 192.210 187.565 118.549 1.00 44.57  ?  141 GLU A CG    1 
ATOM   975   C  CD    . GLU A 1 122 ? 192.721 186.249 119.095 1.00 41.23  ?  141 GLU A CD    1 
ATOM   976   O  OE1   . GLU A 1 122 ? 192.637 185.230 118.378 1.00 45.75  ?  141 GLU A OE1   1 
ATOM   977   O  OE2   . GLU A 1 122 ? 193.211 186.235 120.244 1.00 35.63  -1 141 GLU A OE2   1 
ATOM   978   N  N     . GLN A 1 123 ? 189.006 188.496 120.682 1.00 41.72  ?  142 GLN A N     1 
ATOM   979   C  CA    . GLN A 1 123 ? 188.867 189.190 121.955 1.00 41.46  ?  142 GLN A CA    1 
ATOM   980   C  C     . GLN A 1 123 ? 188.349 188.256 123.038 1.00 52.29  ?  142 GLN A C     1 
ATOM   981   O  O     . GLN A 1 123 ? 188.838 188.283 124.171 1.00 61.72  ?  142 GLN A O     1 
ATOM   982   C  CB    . GLN A 1 123 ? 187.939 190.395 121.800 1.00 39.33  ?  142 GLN A CB    1 
ATOM   983   C  CG    . GLN A 1 123 ? 188.629 191.652 121.304 1.00 45.35  ?  142 GLN A CG    1 
ATOM   984   C  CD    . GLN A 1 123 ? 187.728 192.869 121.364 1.00 52.94  ?  142 GLN A CD    1 
ATOM   985   O  OE1   . GLN A 1 123 ? 186.569 192.778 121.770 1.00 55.66  ?  142 GLN A OE1   1 
ATOM   986   N  NE2   . GLN A 1 123 ? 188.257 194.017 120.961 1.00 51.61  ?  142 GLN A NE2   1 
ATOM   987   N  N     . THR A 1 124 ? 187.361 187.419 122.711 1.00 48.49  ?  143 THR A N     1 
ATOM   988   C  CA    . THR A 1 124 ? 186.826 186.513 123.722 1.00 41.90  ?  143 THR A CA    1 
ATOM   989   C  C     . THR A 1 124 ? 187.803 185.386 124.034 1.00 43.85  ?  143 THR A C     1 
ATOM   990   O  O     . THR A 1 124 ? 187.825 184.893 125.163 1.00 49.04  ?  143 THR A O     1 
ATOM   991   C  CB    . THR A 1 124 ? 185.463 185.955 123.295 1.00 46.39  ?  143 THR A CB    1 
ATOM   992   O  OG1   . THR A 1 124 ? 184.801 185.392 124.434 1.00 50.36  ?  143 THR A OG1   1 
ATOM   993   C  CG2   . THR A 1 124 ? 185.605 184.873 122.243 1.00 47.40  ?  143 THR A CG2   1 
ATOM   994   N  N     . ARG A 1 125 ? 188.644 184.992 123.074 1.00 37.52  ?  144 ARG A N     1 
ATOM   995   C  CA    . ARG A 1 125 ? 189.706 184.037 123.372 1.00 31.83  ?  144 ARG A CA    1 
ATOM   996   C  C     . ARG A 1 125 ? 190.708 184.634 124.353 1.00 38.74  ?  144 ARG A C     1 
ATOM   997   O  O     . ARG A 1 125 ? 191.101 183.987 125.334 1.00 48.18  ?  144 ARG A O     1 
ATOM   998   C  CB    . ARG A 1 125 ? 190.407 183.608 122.082 1.00 34.71  ?  144 ARG A CB    1 
ATOM   999   C  CG    . ARG A 1 125 ? 191.219 182.328 122.208 1.00 44.30  ?  144 ARG A CG    1 
ATOM   1000  C  CD    . ARG A 1 125 ? 191.934 181.978 120.906 1.00 43.42  ?  144 ARG A CD    1 
ATOM   1001  N  NE    . ARG A 1 125 ? 192.838 183.031 120.454 1.00 42.52  ?  144 ARG A NE    1 
ATOM   1002  C  CZ    . ARG A 1 125 ? 194.003 183.318 121.020 1.00 44.11  ?  144 ARG A CZ    1 
ATOM   1003  N  NH1   . ARG A 1 125 ? 194.450 182.642 122.065 1.00 44.97  1  144 ARG A NH1   1 
ATOM   1004  N  NH2   . ARG A 1 125 ? 194.741 184.305 120.520 1.00 45.08  ?  144 ARG A NH2   1 
ATOM   1005  N  N     . GLN A 1 126 ? 191.114 185.883 124.114 1.00 37.26  ?  145 GLN A N     1 
ATOM   1006  C  CA    . GLN A 1 126 ? 192.044 186.544 125.025 1.00 32.94  ?  145 GLN A CA    1 
ATOM   1007  C  C     . GLN A 1 126 ? 191.418 186.755 126.399 1.00 41.93  ?  145 GLN A C     1 
ATOM   1008  O  O     . GLN A 1 126 ? 192.090 186.601 127.425 1.00 52.15  ?  145 GLN A O     1 
ATOM   1009  C  CB    . GLN A 1 126 ? 192.508 187.871 124.427 1.00 28.80  ?  145 GLN A CB    1 
ATOM   1010  C  CG    . GLN A 1 126 ? 193.395 187.710 123.204 1.00 40.61  ?  145 GLN A CG    1 
ATOM   1011  C  CD    . GLN A 1 126 ? 193.223 188.833 122.203 1.00 45.06  ?  145 GLN A CD    1 
ATOM   1012  O  OE1   . GLN A 1 126 ? 192.386 189.718 122.383 1.00 46.83  ?  145 GLN A OE1   1 
ATOM   1013  N  NE2   . GLN A 1 126 ? 194.010 188.799 121.136 1.00 42.25  ?  145 GLN A NE2   1 
ATOM   1014  N  N     . LEU A 1 127 ? 190.127 187.094 126.440 1.00 37.87  ?  146 LEU A N     1 
ATOM   1015  C  CA    . LEU A 1 127 ? 189.449 187.285 127.719 1.00 35.40  ?  146 LEU A CA    1 
ATOM   1016  C  C     . LEU A 1 127 ? 189.286 185.966 128.463 1.00 44.64  ?  146 LEU A C     1 
ATOM   1017  O  O     . LEU A 1 127 ? 189.395 185.927 129.692 1.00 45.84  ?  146 LEU A O     1 
ATOM   1018  C  CB    . LEU A 1 127 ? 188.090 187.953 127.502 1.00 33.15  ?  146 LEU A CB    1 
ATOM   1019  C  CG    . LEU A 1 127 ? 188.127 189.416 127.057 1.00 39.21  ?  146 LEU A CG    1 
ATOM   1020  C  CD1   . LEU A 1 127 ? 186.850 189.788 126.324 1.00 39.14  ?  146 LEU A CD1   1 
ATOM   1021  C  CD2   . LEU A 1 127 ? 188.355 190.335 128.244 1.00 42.26  ?  146 LEU A CD2   1 
ATOM   1022  N  N     . ILE A 1 128 ? 189.027 184.875 127.738 1.00 47.36  ?  147 ILE A N     1 
ATOM   1023  C  CA    . ILE A 1 128 ? 188.970 183.557 128.361 1.00 36.36  ?  147 ILE A CA    1 
ATOM   1024  C  C     . ILE A 1 128 ? 190.324 183.200 128.953 1.00 33.10  ?  147 ILE A C     1 
ATOM   1025  O  O     . ILE A 1 128 ? 190.414 182.683 130.075 1.00 45.73  ?  147 ILE A O     1 
ATOM   1026  C  CB    . ILE A 1 128 ? 188.500 182.505 127.339 1.00 32.51  ?  147 ILE A CB    1 
ATOM   1027  C  CG1   . ILE A 1 128 ? 186.976 182.513 127.218 1.00 29.96  ?  147 ILE A CG1   1 
ATOM   1028  C  CG2   . ILE A 1 128 ? 188.991 181.118 127.725 1.00 31.78  ?  147 ILE A CG2   1 
ATOM   1029  C  CD1   . ILE A 1 128 ? 186.439 181.494 126.240 1.00 31.48  ?  147 ILE A CD1   1 
ATOM   1030  N  N     . ILE A 1 129 ? 191.400 183.481 128.216 1.00 33.59  ?  148 ILE A N     1 
ATOM   1031  C  CA    . ILE A 1 129 ? 192.741 183.227 128.736 1.00 38.15  ?  148 ILE A CA    1 
ATOM   1032  C  C     . ILE A 1 129 ? 192.981 184.042 130.002 1.00 41.86  ?  148 ILE A C     1 
ATOM   1033  O  O     . ILE A 1 129 ? 193.465 183.522 131.014 1.00 44.85  ?  148 ILE A O     1 
ATOM   1034  C  CB    . ILE A 1 129 ? 193.802 183.526 127.662 1.00 34.07  ?  148 ILE A CB    1 
ATOM   1035  C  CG1   . ILE A 1 129 ? 193.709 182.511 126.521 1.00 41.15  ?  148 ILE A CG1   1 
ATOM   1036  C  CG2   . ILE A 1 129 ? 195.187 183.502 128.268 1.00 35.94  ?  148 ILE A CG2   1 
ATOM   1037  C  CD1   . ILE A 1 129 ? 194.780 182.680 125.466 1.00 42.25  ?  148 ILE A CD1   1 
ATOM   1038  N  N     . ALA A 1 130 ? 192.621 185.327 129.972 1.00 36.03  ?  149 ALA A N     1 
ATOM   1039  C  CA    . ALA A 1 130 ? 192.869 186.203 131.111 1.00 34.11  ?  149 ALA A CA    1 
ATOM   1040  C  C     . ALA A 1 130 ? 191.990 185.875 132.312 1.00 38.38  ?  149 ALA A C     1 
ATOM   1041  O  O     . ALA A 1 130 ? 192.379 186.176 133.446 1.00 43.54  ?  149 ALA A O     1 
ATOM   1042  C  CB    . ALA A 1 130 ? 192.665 187.663 130.706 1.00 35.71  ?  149 ALA A CB    1 
ATOM   1043  N  N     . VAL A 1 131 ? 190.820 185.272 132.096 1.00 34.48  ?  150 VAL A N     1 
ATOM   1044  C  CA    . VAL A 1 131 ? 189.941 184.934 133.210 1.00 33.26  ?  150 VAL A CA    1 
ATOM   1045  C  C     . VAL A 1 131 ? 190.225 183.542 133.764 1.00 42.23  ?  150 VAL A C     1 
ATOM   1046  O  O     . VAL A 1 131 ? 189.935 183.283 134.941 1.00 48.37  ?  150 VAL A O     1 
ATOM   1047  C  CB    . VAL A 1 131 ? 188.461 185.056 132.797 1.00 29.09  ?  150 VAL A CB    1 
ATOM   1048  C  CG1   . VAL A 1 131 ? 188.048 183.898 131.901 1.00 33.78  ?  150 VAL A CG1   1 
ATOM   1049  C  CG2   . VAL A 1 131 ? 187.561 185.143 134.023 1.00 36.68  ?  150 VAL A CG2   1 
ATOM   1050  N  N     . ASP A 1 132 ? 190.789 182.643 132.958 1.00 40.40  ?  151 ASP A N     1 
ATOM   1051  C  CA    . ASP A 1 132 ? 191.208 181.337 133.444 1.00 36.75  ?  151 ASP A CA    1 
ATOM   1052  C  C     . ASP A 1 132 ? 192.641 181.334 133.959 1.00 42.22  ?  151 ASP A C     1 
ATOM   1053  O  O     . ASP A 1 132 ? 193.044 180.367 134.614 1.00 49.04  ?  151 ASP A O     1 
ATOM   1054  C  CB    . ASP A 1 132 ? 191.061 180.291 132.334 1.00 36.69  ?  151 ASP A CB    1 
ATOM   1055  C  CG    . ASP A 1 132 ? 189.617 180.069 131.931 1.00 43.44  ?  151 ASP A CG    1 
ATOM   1056  O  OD1   . ASP A 1 132 ? 188.720 180.301 132.768 1.00 43.73  ?  151 ASP A OD1   1 
ATOM   1057  O  OD2   . ASP A 1 132 ? 189.377 179.667 130.774 1.00 48.50  -1 151 ASP A OD2   1 
ATOM   1058  N  N     . HIS A 1 133 ? 193.413 182.386 133.680 1.00 39.83  ?  152 HIS A N     1 
ATOM   1059  C  CA    . HIS A 1 133 ? 194.796 182.445 134.136 1.00 44.75  ?  152 HIS A CA    1 
ATOM   1060  C  C     . HIS A 1 133 ? 194.903 182.789 135.617 1.00 42.10  ?  152 HIS A C     1 
ATOM   1061  O  O     . HIS A 1 133 ? 195.785 182.274 136.313 1.00 51.02  ?  152 HIS A O     1 
ATOM   1062  C  CB    . HIS A 1 133 ? 195.567 183.466 133.298 1.00 43.10  ?  152 HIS A CB    1 
ATOM   1063  C  CG    . HIS A 1 133 ? 197.047 183.422 133.503 1.00 42.85  ?  152 HIS A CG    1 
ATOM   1064  N  ND1   . HIS A 1 133 ? 197.695 184.225 134.417 1.00 36.75  ?  152 HIS A ND1   1 
ATOM   1065  C  CD2   . HIS A 1 133 ? 198.007 182.672 132.913 1.00 47.20  ?  152 HIS A CD2   1 
ATOM   1066  C  CE1   . HIS A 1 133 ? 198.991 183.971 134.381 1.00 45.88  ?  152 HIS A CE1   1 
ATOM   1067  N  NE2   . HIS A 1 133 ? 199.206 183.032 133.477 1.00 49.47  ?  152 HIS A NE2   1 
ATOM   1068  N  N     . LEU A 1 134 ? 194.017 183.650 136.120 1.00 27.51  ?  153 LEU A N     1 
ATOM   1069  C  CA    . LEU A 1 134 ? 194.180 184.206 137.457 1.00 35.53  ?  153 LEU A CA    1 
ATOM   1070  C  C     . LEU A 1 134 ? 193.756 183.257 138.569 1.00 47.54  ?  153 LEU A C     1 
ATOM   1071  O  O     . LEU A 1 134 ? 194.028 183.552 139.739 1.00 54.86  ?  153 LEU A O     1 
ATOM   1072  C  CB    . LEU A 1 134 ? 193.396 185.514 137.584 1.00 44.87  ?  153 LEU A CB    1 
ATOM   1073  C  CG    . LEU A 1 134 ? 194.210 186.788 137.360 1.00 48.88  ?  153 LEU A CG    1 
ATOM   1074  C  CD1   . LEU A 1 134 ? 193.365 188.027 137.612 1.00 49.98  ?  153 LEU A CD1   1 
ATOM   1075  C  CD2   . LEU A 1 134 ? 195.447 186.785 138.236 1.00 44.05  ?  153 LEU A CD2   1 
ATOM   1076  N  N     . ASP A 1 135 ? 193.107 182.138 138.242 1.00 45.39  ?  154 ASP A N     1 
ATOM   1077  C  CA    . ASP A 1 135 ? 192.629 181.180 139.241 1.00 44.84  ?  154 ASP A CA    1 
ATOM   1078  C  C     . ASP A 1 135 ? 191.738 181.870 140.275 1.00 43.04  ?  154 ASP A C     1 
ATOM   1079  O  O     . ASP A 1 135 ? 191.854 181.652 141.483 1.00 40.01  ?  154 ASP A O     1 
ATOM   1080  C  CB    . ASP A 1 135 ? 193.801 180.452 139.908 1.00 40.06  ?  154 ASP A CB    1 
ATOM   1081  C  CG    . ASP A 1 135 ? 193.360 179.247 140.718 1.00 48.57  ?  154 ASP A CG    1 
ATOM   1082  O  OD1   . ASP A 1 135 ? 192.316 178.652 140.382 1.00 49.73  ?  154 ASP A OD1   1 
ATOM   1083  O  OD2   . ASP A 1 135 ? 194.060 178.896 141.692 1.00 52.28  -1 154 ASP A OD2   1 
ATOM   1084  N  N     . ARG A 1 136 ? 190.846 182.724 139.786 1.00 44.34  ?  155 ARG A N     1 
ATOM   1085  C  CA    . ARG A 1 136 ? 189.906 183.458 140.633 1.00 38.38  ?  155 ARG A CA    1 
ATOM   1086  C  C     . ARG A 1 136 ? 188.487 183.153 140.177 1.00 39.75  ?  155 ARG A C     1 
ATOM   1087  O  O     . ARG A 1 136 ? 188.092 183.576 139.070 1.00 50.96  ?  155 ARG A O     1 
ATOM   1088  C  CB    . ARG A 1 136 ? 190.183 184.958 140.589 1.00 40.52  ?  155 ARG A CB    1 
ATOM   1089  C  CG    . ARG A 1 136 ? 189.317 185.773 141.537 1.00 47.45  ?  155 ARG A CG    1 
ATOM   1090  C  CD    . ARG A 1 136 ? 189.933 185.849 142.927 1.00 47.30  ?  155 ARG A CD    1 
ATOM   1091  N  NE    . ARG A 1 136 ? 191.383 185.998 142.878 1.00 50.23  ?  155 ARG A NE    1 
ATOM   1092  C  CZ    . ARG A 1 136 ? 192.166 186.060 143.946 1.00 50.37  ?  155 ARG A CZ    1 
ATOM   1093  N  NH1   . ARG A 1 136 ? 191.673 185.988 145.172 1.00 45.80  1  155 ARG A NH1   1 
ATOM   1094  N  NH2   . ARG A 1 136 ? 193.479 186.198 143.780 1.00 43.94  ?  155 ARG A NH2   1 
ATOM   1095  N  N     . PRO A 1 137 ? 187.697 182.432 140.974 1.00 18.94  ?  156 PRO A N     1 
ATOM   1096  C  CA    . PRO A 1 137 ? 186.333 182.063 140.558 1.00 15.10  ?  156 PRO A CA    1 
ATOM   1097  C  C     . PRO A 1 137 ? 185.448 183.292 140.398 1.00 25.76  ?  156 PRO A C     1 
ATOM   1098  O  O     . PRO A 1 137 ? 185.252 184.059 141.343 1.00 43.46  ?  156 PRO A O     1 
ATOM   1099  C  CB    . PRO A 1 137 ? 185.845 181.160 141.698 1.00 20.30  ?  156 PRO A CB    1 
ATOM   1100  C  CG    . PRO A 1 137 ? 187.087 180.705 142.396 1.00 25.23  ?  156 PRO A CG    1 
ATOM   1101  C  CD    . PRO A 1 137 ? 188.077 181.813 142.254 1.00 28.66  ?  156 PRO A CD    1 
ATOM   1102  N  N     . VAL A 1 138 ? 184.909 183.472 139.194 1.00 18.23  ?  157 VAL A N     1 
ATOM   1103  C  CA    . VAL A 1 138 ? 184.047 184.603 138.871 1.00 9.77   ?  157 VAL A CA    1 
ATOM   1104  C  C     . VAL A 1 138 ? 182.867 184.100 138.051 1.00 23.55  ?  157 VAL A C     1 
ATOM   1105  O  O     . VAL A 1 138 ? 183.056 183.368 137.074 1.00 34.12  ?  157 VAL A O     1 
ATOM   1106  C  CB    . VAL A 1 138 ? 184.811 185.701 138.104 1.00 7.82   ?  157 VAL A CB    1 
ATOM   1107  C  CG1   . VAL A 1 138 ? 183.843 186.617 137.378 1.00 16.25  ?  157 VAL A CG1   1 
ATOM   1108  C  CG2   . VAL A 1 138 ? 185.684 186.498 139.053 1.00 25.15  ?  157 VAL A CG2   1 
ATOM   1109  N  N     . ILE A 1 139 ? 181.653 184.485 138.449 1.00 30.36  ?  158 ILE A N     1 
ATOM   1110  C  CA    . ILE A 1 139 ? 180.449 184.182 137.690 1.00 19.51  ?  158 ILE A CA    1 
ATOM   1111  C  C     . ILE A 1 139 ? 179.680 185.477 137.446 1.00 17.62  ?  158 ILE A C     1 
ATOM   1112  O  O     . ILE A 1 139 ? 179.858 186.481 138.141 1.00 37.17  ?  158 ILE A O     1 
ATOM   1113  C  CB    . ILE A 1 139 ? 179.555 183.137 138.390 1.00 27.37  ?  158 ILE A CB    1 
ATOM   1114  C  CG1   . ILE A 1 139 ? 178.963 183.705 139.678 1.00 36.40  ?  158 ILE A CG1   1 
ATOM   1115  C  CG2   . ILE A 1 139 ? 180.334 181.857 138.673 1.00 29.81  ?  158 ILE A CG2   1 
ATOM   1116  C  CD1   . ILE A 1 139 ? 177.795 182.907 140.213 1.00 37.78  ?  158 ILE A CD1   1 
ATOM   1117  N  N     . VAL A 1 140 ? 178.817 185.443 136.434 1.00 9.39   ?  159 VAL A N     1 
ATOM   1118  C  CA    . VAL A 1 140 ? 178.031 186.598 136.014 1.00 20.31  ?  159 VAL A CA    1 
ATOM   1119  C  C     . VAL A 1 140 ? 176.562 186.199 136.025 1.00 31.25  ?  159 VAL A C     1 
ATOM   1120  O  O     . VAL A 1 140 ? 176.216 185.072 135.655 1.00 43.41  ?  159 VAL A O     1 
ATOM   1121  C  CB    . VAL A 1 140 ? 178.464 187.102 134.619 1.00 18.59  ?  159 VAL A CB    1 
ATOM   1122  C  CG1   . VAL A 1 140 ? 177.563 188.228 134.141 1.00 21.89  ?  159 VAL A CG1   1 
ATOM   1123  C  CG2   . VAL A 1 140 ? 179.914 187.553 134.645 1.00 17.48  ?  159 VAL A CG2   1 
ATOM   1124  N  N     . LEU A 1 141 ? 175.697 187.116 136.461 1.00 19.91  ?  160 LEU A N     1 
ATOM   1125  C  CA    . LEU A 1 141 ? 174.287 186.833 136.663 1.00 8.32   ?  160 LEU A CA    1 
ATOM   1126  C  C     . LEU A 1 141 ? 173.429 187.898 135.998 1.00 23.04  ?  160 LEU A C     1 
ATOM   1127  O  O     . LEU A 1 141 ? 173.790 189.079 135.952 1.00 39.24  ?  160 LEU A O     1 
ATOM   1128  C  CB    . LEU A 1 141 ? 173.942 186.780 138.153 1.00 16.92  ?  160 LEU A CB    1 
ATOM   1129  C  CG    . LEU A 1 141 ? 174.902 186.032 139.072 1.00 23.81  ?  160 LEU A CG    1 
ATOM   1130  C  CD1   . LEU A 1 141 ? 174.379 186.082 140.476 1.00 30.74  ?  160 LEU A CD1   1 
ATOM   1131  C  CD2   . LEU A 1 141 ? 175.026 184.594 138.626 1.00 27.24  ?  160 LEU A CD2   1 
ATOM   1132  N  N     . ASP A 1 142 ? 172.276 187.462 135.514 1.00 34.24  ?  161 ASP A N     1 
ATOM   1133  C  CA    . ASP A 1 142 ? 171.261 188.329 134.938 1.00 37.87  ?  161 ASP A CA    1 
ATOM   1134  C  C     . ASP A 1 142 ? 170.428 188.953 136.048 1.00 38.46  ?  161 ASP A C     1 
ATOM   1135  O  O     . ASP A 1 142 ? 170.591 188.624 137.226 1.00 40.25  ?  161 ASP A O     1 
ATOM   1136  C  CB    . ASP A 1 142 ? 170.392 187.519 133.976 1.00 40.52  ?  161 ASP A CB    1 
ATOM   1137  C  CG    . ASP A 1 142 ? 169.944 186.195 134.567 1.00 45.51  ?  161 ASP A CG    1 
ATOM   1138  O  OD1   . ASP A 1 142 ? 170.200 185.956 135.765 1.00 50.25  ?  161 ASP A OD1   1 
ATOM   1139  O  OD2   . ASP A 1 142 ? 169.328 185.394 133.833 1.00 45.59  -1 161 ASP A OD2   1 
ATOM   1140  N  N     . PRO A 1 143 ? 169.529 189.886 135.716 1.00 37.63  ?  162 PRO A N     1 
ATOM   1141  C  CA    . PRO A 1 143 ? 168.620 190.413 136.749 1.00 38.63  ?  162 PRO A CA    1 
ATOM   1142  C  C     . PRO A 1 143 ? 167.767 189.346 137.414 1.00 44.82  ?  162 PRO A C     1 
ATOM   1143  O  O     . PRO A 1 143 ? 167.333 189.547 138.555 1.00 49.11  ?  162 PRO A O     1 
ATOM   1144  C  CB    . PRO A 1 143 ? 167.762 191.423 135.977 1.00 39.65  ?  162 PRO A CB    1 
ATOM   1145  C  CG    . PRO A 1 143 ? 168.648 191.880 134.877 1.00 42.91  ?  162 PRO A CG    1 
ATOM   1146  C  CD    . PRO A 1 143 ? 169.453 190.678 134.474 1.00 36.83  ?  162 PRO A CD    1 
ATOM   1147  N  N     . GLU A 1 144 ? 167.517 188.220 136.748 1.00 42.58  ?  163 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 144 ? 166.836 187.092 137.371 1.00 37.92  ?  163 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 144 ? 167.752 186.273 138.272 1.00 37.29  ?  163 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 144 ? 167.304 185.263 138.825 1.00 40.73  ?  163 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 144 ? 166.217 186.189 136.302 1.00 46.33  ?  163 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 144 ? 164.855 186.657 135.817 1.00 49.38  ?  163 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 144 ? 164.946 187.555 134.602 1.00 51.48  ?  163 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 144 ? 166.068 187.756 134.092 1.00 49.79  ?  163 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 144 ? 163.894 188.060 134.155 1.00 46.97  -1 163 GLU A OE2   1 
ATOM   1156  N  N     . ARG A 1 145 ? 169.018 186.673 138.407 1.00 37.95  ?  164 ARG A N     1 
ATOM   1157  C  CA    . ARG A 1 145 ? 169.975 186.074 139.337 1.00 35.38  ?  164 ARG A CA    1 
ATOM   1158  C  C     . ARG A 1 145 ? 170.317 184.632 138.972 1.00 37.28  ?  164 ARG A C     1 
ATOM   1159  O  O     . ARG A 1 145 ? 170.501 183.789 139.853 1.00 39.58  ?  164 ARG A O     1 
ATOM   1160  C  CB    . ARG A 1 145 ? 169.475 186.150 140.786 1.00 33.85  ?  164 ARG A CB    1 
ATOM   1161  C  CG    . ARG A 1 145 ? 168.969 187.523 141.215 1.00 38.90  ?  164 ARG A CG    1 
ATOM   1162  C  CD    . ARG A 1 145 ? 169.958 188.626 140.871 1.00 39.02  ?  164 ARG A CD    1 
ATOM   1163  N  NE    . ARG A 1 145 ? 169.317 189.935 140.829 1.00 45.14  ?  164 ARG A NE    1 
ATOM   1164  C  CZ    . ARG A 1 145 ? 169.434 190.859 141.773 1.00 42.69  ?  164 ARG A CZ    1 
ATOM   1165  N  NH1   . ARG A 1 145 ? 170.165 190.653 142.855 1.00 41.31  1  164 ARG A NH1   1 
ATOM   1166  N  NH2   . ARG A 1 145 ? 168.801 192.020 141.626 1.00 41.61  ?  164 ARG A NH2   1 
ATOM   1167  N  N     . HIS A 1 146 ? 170.419 184.337 137.679 1.00 40.07  ?  165 HIS A N     1 
ATOM   1168  C  CA    . HIS A 1 146 ? 170.850 183.032 137.202 1.00 34.68  ?  165 HIS A CA    1 
ATOM   1169  C  C     . HIS A 1 146 ? 172.228 183.143 136.561 1.00 39.63  ?  165 HIS A C     1 
ATOM   1170  O  O     . HIS A 1 146 ? 172.594 184.185 136.010 1.00 47.53  ?  165 HIS A O     1 
ATOM   1171  C  CB    . HIS A 1 146 ? 169.854 182.447 136.196 1.00 36.39  ?  165 HIS A CB    1 
ATOM   1172  C  CG    . HIS A 1 146 ? 168.446 182.391 136.699 1.00 43.30  ?  165 HIS A CG    1 
ATOM   1173  N  ND1   . HIS A 1 146 ? 168.136 182.139 138.019 1.00 47.02  ?  165 HIS A ND1   1 
ATOM   1174  C  CD2   . HIS A 1 146 ? 167.263 182.542 136.058 1.00 45.35  ?  165 HIS A CD2   1 
ATOM   1175  C  CE1   . HIS A 1 146 ? 166.824 182.144 138.169 1.00 45.47  ?  165 HIS A CE1   1 
ATOM   1176  N  NE2   . HIS A 1 146 ? 166.270 182.386 136.995 1.00 48.42  ?  165 HIS A NE2   1 
ATOM   1177  N  N     . ILE A 1 147 ? 172.989 182.056 136.637 1.00 33.30  ?  166 ILE A N     1 
ATOM   1178  C  CA    . ILE A 1 147 ? 174.365 182.046 136.151 1.00 26.08  ?  166 ILE A CA    1 
ATOM   1179  C  C     . ILE A 1 147 ? 174.364 182.017 134.630 1.00 29.73  ?  166 ILE A C     1 
ATOM   1180  O  O     . ILE A 1 147 ? 173.679 181.194 134.012 1.00 45.32  ?  166 ILE A O     1 
ATOM   1181  C  CB    . ILE A 1 147 ? 175.137 180.851 136.731 1.00 29.18  ?  166 ILE A CB    1 
ATOM   1182  C  CG1   . ILE A 1 147 ? 175.156 180.923 138.257 1.00 35.56  ?  166 ILE A CG1   1 
ATOM   1183  C  CG2   . ILE A 1 147 ? 176.558 180.820 136.190 1.00 34.37  ?  166 ILE A CG2   1 
ATOM   1184  C  CD1   . ILE A 1 147 ? 175.968 179.829 138.910 1.00 41.99  ?  166 ILE A CD1   1 
ATOM   1185  N  N     . VAL A 1 148 ? 175.130 182.922 134.022 1.00 15.50  ?  167 VAL A N     1 
ATOM   1186  C  CA    . VAL A 1 148 ? 175.272 182.960 132.577 1.00 23.52  ?  167 VAL A CA    1 
ATOM   1187  C  C     . VAL A 1 148 ? 176.704 182.690 132.124 1.00 30.54  ?  167 VAL A C     1 
ATOM   1188  O  O     . VAL A 1 148 ? 176.904 182.233 130.992 1.00 43.11  ?  167 VAL A O     1 
ATOM   1189  C  CB    . VAL A 1 148 ? 174.765 184.302 132.006 1.00 29.40  ?  167 VAL A CB    1 
ATOM   1190  C  CG1   . VAL A 1 148 ? 173.278 184.465 132.274 1.00 34.74  ?  167 VAL A CG1   1 
ATOM   1191  C  CG2   . VAL A 1 148 ? 175.546 185.465 132.591 1.00 36.73  ?  167 VAL A CG2   1 
ATOM   1192  N  N     . GLN A 1 149 ? 177.702 182.959 132.964 1.00 27.19  ?  168 GLN A N     1 
ATOM   1193  C  CA    . GLN A 1 149 ? 179.096 182.718 132.623 1.00 30.45  ?  168 GLN A CA    1 
ATOM   1194  C  C     . GLN A 1 149 ? 179.859 182.319 133.877 1.00 28.96  ?  168 GLN A C     1 
ATOM   1195  O  O     . GLN A 1 149 ? 179.678 182.921 134.937 1.00 40.66  ?  168 GLN A O     1 
ATOM   1196  C  CB    . GLN A 1 149 ? 179.736 183.959 131.988 1.00 16.91  ?  168 GLN A CB    1 
ATOM   1197  C  CG    . GLN A 1 149 ? 181.062 183.692 131.303 1.00 26.70  ?  168 GLN A CG    1 
ATOM   1198  C  CD    . GLN A 1 149 ? 182.246 184.033 132.180 1.00 43.92  ?  168 GLN A CD    1 
ATOM   1199  O  OE1   . GLN A 1 149 ? 182.176 184.937 133.013 1.00 46.85  ?  168 GLN A OE1   1 
ATOM   1200  N  NE2   . GLN A 1 149 ? 183.341 183.304 132.005 1.00 42.42  ?  168 GLN A NE2   1 
ATOM   1201  N  N     . CYS A 1 150 ? 180.703 181.298 133.753 1.00 22.72  ?  169 CYS A N     1 
ATOM   1202  C  CA    . CYS A 1 150 ? 181.560 180.840 134.837 1.00 22.42  ?  169 CYS A CA    1 
ATOM   1203  C  C     . CYS A 1 150 ? 182.994 180.756 134.332 1.00 30.72  ?  169 CYS A C     1 
ATOM   1204  O  O     . CYS A 1 150 ? 183.282 181.059 133.171 1.00 36.24  ?  169 CYS A O     1 
ATOM   1205  C  CB    . CYS A 1 150 ? 181.096 179.484 135.389 1.00 30.03  ?  169 CYS A CB    1 
ATOM   1206  S  SG    . CYS A 1 150 ? 181.138 178.129 134.197 1.00 58.89  ?  169 CYS A SG    1 
ATOM   1207  N  N     . ASN A 1 151 ? 183.906 180.344 135.211 1.00 24.78  ?  170 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 151 ? 185.317 180.274 134.859 1.00 23.14  ?  170 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 151 ? 185.959 179.017 135.445 1.00 29.18  ?  170 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 151 ? 185.346 178.260 136.212 1.00 44.70  ?  170 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 151 ? 186.065 181.538 135.306 1.00 28.89  ?  170 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 151 ? 186.151 181.668 136.808 1.00 33.63  ?  170 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 151 ? 185.300 181.165 137.535 1.00 37.07  ?  170 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 151 ? 187.187 182.348 137.283 1.00 35.54  ?  170 ASN A ND2   1 
ATOM   1215  N  N     . ARG A 1 152 ? 187.222 178.812 135.059 1.00 30.50  ?  171 ARG A N     1 
ATOM   1216  C  CA    . ARG A 1 152 ? 187.920 177.565 135.354 1.00 30.75  ?  171 ARG A CA    1 
ATOM   1217  C  C     . ARG A 1 152 ? 188.150 177.391 136.850 1.00 32.06  ?  171 ARG A C     1 
ATOM   1218  O  O     . ARG A 1 152 ? 188.080 176.270 137.362 1.00 39.26  ?  171 ARG A O     1 
ATOM   1219  C  CB    . ARG A 1 152 ? 189.240 177.524 134.575 1.00 32.25  ?  171 ARG A CB    1 
ATOM   1220  C  CG    . ARG A 1 152 ? 189.996 176.196 134.609 1.00 34.57  ?  171 ARG A CG    1 
ATOM   1221  C  CD    . ARG A 1 152 ? 190.932 176.085 135.803 1.00 35.87  ?  171 ARG A CD    1 
ATOM   1222  N  NE    . ARG A 1 152 ? 191.887 177.185 135.857 1.00 35.84  ?  171 ARG A NE    1 
ATOM   1223  C  CZ    . ARG A 1 152 ? 193.016 177.229 135.163 1.00 38.65  ?  171 ARG A CZ    1 
ATOM   1224  N  NH1   . ARG A 1 152 ? 193.365 176.247 134.349 1.00 36.91  1  171 ARG A NH1   1 
ATOM   1225  N  NH2   . ARG A 1 152 ? 193.815 178.284 135.292 1.00 37.79  ?  171 ARG A NH2   1 
ATOM   1226  N  N     . ALA A 1 153 ? 188.444 178.477 137.568 1.00 24.62  ?  172 ALA A N     1 
ATOM   1227  C  CA    . ALA A 1 153 ? 188.627 178.373 139.013 1.00 31.76  ?  172 ALA A CA    1 
ATOM   1228  C  C     . ALA A 1 153 ? 187.328 177.984 139.711 1.00 35.97  ?  172 ALA A C     1 
ATOM   1229  O  O     . ALA A 1 153 ? 187.335 177.176 140.650 1.00 43.27  ?  172 ALA A O     1 
ATOM   1230  C  CB    . ALA A 1 153 ? 189.164 179.689 139.569 1.00 30.45  ?  172 ALA A CB    1 
ATOM   1231  N  N     . PHE A 1 154 ? 186.207 178.559 139.271 1.00 35.87  ?  173 PHE A N     1 
ATOM   1232  C  CA    . PHE A 1 154 ? 184.904 178.178 139.806 1.00 34.52  ?  173 PHE A CA    1 
ATOM   1233  C  C     . PHE A 1 154 ? 184.631 176.702 139.554 1.00 30.50  ?  173 PHE A C     1 
ATOM   1234  O  O     . PHE A 1 154 ? 184.160 175.982 140.444 1.00 43.63  ?  173 PHE A O     1 
ATOM   1235  C  CB    . PHE A 1 154 ? 183.817 179.048 139.170 1.00 36.14  ?  173 PHE A CB    1 
ATOM   1236  C  CG    . PHE A 1 154 ? 182.419 178.703 139.596 1.00 30.56  ?  173 PHE A CG    1 
ATOM   1237  C  CD1   . PHE A 1 154 ? 181.914 179.156 140.803 1.00 40.17  ?  173 PHE A CD1   1 
ATOM   1238  C  CD2   . PHE A 1 154 ? 181.605 177.934 138.781 1.00 28.94  ?  173 PHE A CD2   1 
ATOM   1239  C  CE1   . PHE A 1 154 ? 180.622 178.845 141.188 1.00 36.35  ?  173 PHE A CE1   1 
ATOM   1240  C  CE2   . PHE A 1 154 ? 180.316 177.615 139.164 1.00 34.53  ?  173 PHE A CE2   1 
ATOM   1241  C  CZ    . PHE A 1 154 ? 179.824 178.071 140.369 1.00 35.20  ?  173 PHE A CZ    1 
ATOM   1242  N  N     . THR A 1 155 ? 184.941 176.233 138.342 1.00 26.59  ?  174 THR A N     1 
ATOM   1243  C  CA    . THR A 1 155 ? 184.770 174.818 138.029 1.00 29.80  ?  174 THR A CA    1 
ATOM   1244  C  C     . THR A 1 155 ? 185.659 173.944 138.908 1.00 28.59  ?  174 THR A C     1 
ATOM   1245  O  O     . THR A 1 155 ? 185.230 172.887 139.384 1.00 38.40  ?  174 THR A O     1 
ATOM   1246  C  CB    . THR A 1 155 ? 185.069 174.568 136.549 1.00 38.05  ?  174 THR A CB    1 
ATOM   1247  O  OG1   . THR A 1 155 ? 184.130 175.287 135.740 1.00 39.30  ?  174 THR A OG1   1 
ATOM   1248  C  CG2   . THR A 1 155 ? 184.978 173.082 136.220 1.00 39.85  ?  174 THR A CG2   1 
ATOM   1249  N  N     . GLU A 1 156 ? 186.903 174.370 139.132 1.00 32.98  ?  175 GLU A N     1 
ATOM   1250  C  CA    . GLU A 1 156 ? 187.827 173.581 139.940 1.00 38.58  ?  175 GLU A CA    1 
ATOM   1251  C  C     . GLU A 1 156 ? 187.359 173.479 141.384 1.00 43.93  ?  175 GLU A C     1 
ATOM   1252  O  O     . GLU A 1 156 ? 187.425 172.404 141.991 1.00 49.12  ?  175 GLU A O     1 
ATOM   1253  C  CB    . GLU A 1 156 ? 189.228 174.190 139.883 1.00 39.67  ?  175 GLU A CB    1 
ATOM   1254  C  CG    . GLU A 1 156 ? 190.086 173.689 138.737 1.00 42.98  ?  175 GLU A CG    1 
ATOM   1255  C  CD    . GLU A 1 156 ? 191.436 174.376 138.683 1.00 46.47  ?  175 GLU A CD    1 
ATOM   1256  O  OE1   . GLU A 1 156 ? 191.548 175.512 139.190 1.00 44.91  ?  175 GLU A OE1   1 
ATOM   1257  O  OE2   . GLU A 1 156 ? 192.384 173.782 138.128 1.00 42.51  -1 175 GLU A OE2   1 
ATOM   1258  N  N     . MET A 1 157 ? 186.881 174.585 141.953 1.00 46.16  ?  176 MET A N     1 
ATOM   1259  C  CA    . MET A 1 157 ? 186.554 174.590 143.372 1.00 44.55  ?  176 MET A CA    1 
ATOM   1260  C  C     . MET A 1 157 ? 185.154 174.074 143.675 1.00 41.63  ?  176 MET A C     1 
ATOM   1261  O  O     . MET A 1 157 ? 184.918 173.603 144.794 1.00 44.87  ?  176 MET A O     1 
ATOM   1262  C  CB    . MET A 1 157 ? 186.718 175.998 143.955 1.00 43.89  ?  176 MET A CB    1 
ATOM   1263  C  CG    . MET A 1 157 ? 185.498 176.887 143.825 1.00 48.20  ?  176 MET A CG    1 
ATOM   1264  S  SD    . MET A 1 157 ? 185.723 178.461 144.669 1.00 66.46  ?  176 MET A SD    1 
ATOM   1265  C  CE    . MET A 1 157 ? 185.897 177.915 146.365 1.00 51.15  ?  176 MET A CE    1 
ATOM   1266  N  N     . PHE A 1 158 ? 184.221 174.137 142.722 1.00 39.44  ?  177 PHE A N     1 
ATOM   1267  C  CA    . PHE A 1 158 ? 182.865 173.665 142.967 1.00 33.38  ?  177 PHE A CA    1 
ATOM   1268  C  C     . PHE A 1 158 ? 182.456 172.484 142.099 1.00 37.56  ?  177 PHE A C     1 
ATOM   1269  O  O     . PHE A 1 158 ? 181.374 171.928 142.315 1.00 46.89  ?  177 PHE A O     1 
ATOM   1270  C  CB    . PHE A 1 158 ? 181.856 174.807 142.774 1.00 42.70  ?  177 PHE A CB    1 
ATOM   1271  C  CG    . PHE A 1 158 ? 181.820 175.787 143.916 1.00 50.07  ?  177 PHE A CG    1 
ATOM   1272  C  CD1   . PHE A 1 158 ? 182.539 175.556 145.077 1.00 49.55  ?  177 PHE A CD1   1 
ATOM   1273  C  CD2   . PHE A 1 158 ? 181.056 176.937 143.829 1.00 51.66  ?  177 PHE A CD2   1 
ATOM   1274  C  CE1   . PHE A 1 158 ? 182.504 176.459 146.123 1.00 46.85  ?  177 PHE A CE1   1 
ATOM   1275  C  CE2   . PHE A 1 158 ? 181.016 177.842 144.871 1.00 48.05  ?  177 PHE A CE2   1 
ATOM   1276  C  CZ    . PHE A 1 158 ? 181.740 177.602 146.020 1.00 43.03  ?  177 PHE A CZ    1 
ATOM   1277  N  N     . GLY A 1 159 ? 183.276 172.087 141.129 1.00 47.79  ?  178 GLY A N     1 
ATOM   1278  C  CA    . GLY A 1 159 ? 182.993 170.900 140.349 1.00 55.22  ?  178 GLY A CA    1 
ATOM   1279  C  C     . GLY A 1 159 ? 181.840 171.012 139.380 1.00 56.49  ?  178 GLY A C     1 
ATOM   1280  O  O     . GLY A 1 159 ? 181.242 169.986 139.037 1.00 57.75  ?  178 GLY A O     1 
ATOM   1281  N  N     . TYR A 1 160 ? 181.502 172.217 138.929 1.00 48.04  ?  179 TYR A N     1 
ATOM   1282  C  CA    . TYR A 1 160 ? 180.423 172.420 137.975 1.00 49.54  ?  179 TYR A CA    1 
ATOM   1283  C  C     . TYR A 1 160 ? 180.946 173.180 136.766 1.00 50.79  ?  179 TYR A C     1 
ATOM   1284  O  O     . TYR A 1 160 ? 181.840 174.023 136.890 1.00 55.77  ?  179 TYR A O     1 
ATOM   1285  C  CB    . TYR A 1 160 ? 179.253 173.179 138.612 1.00 52.84  ?  179 TYR A CB    1 
ATOM   1286  C  CG    . TYR A 1 160 ? 178.441 172.340 139.571 1.00 52.47  ?  179 TYR A CG    1 
ATOM   1287  C  CD1   . TYR A 1 160 ? 177.897 171.128 139.172 1.00 52.72  ?  179 TYR A CD1   1 
ATOM   1288  C  CD2   . TYR A 1 160 ? 178.215 172.761 140.874 1.00 53.88  ?  179 TYR A CD2   1 
ATOM   1289  C  CE1   . TYR A 1 160 ? 177.153 170.356 140.044 1.00 54.96  ?  179 TYR A CE1   1 
ATOM   1290  C  CE2   . TYR A 1 160 ? 177.471 171.997 141.753 1.00 54.49  ?  179 TYR A CE2   1 
ATOM   1291  C  CZ    . TYR A 1 160 ? 176.943 170.796 141.333 1.00 57.75  ?  179 TYR A CZ    1 
ATOM   1292  O  OH    . TYR A 1 160 ? 176.203 170.033 142.205 1.00 62.54  ?  179 TYR A OH    1 
ATOM   1293  N  N     . CYS A 1 161 ? 180.383 172.882 135.602 1.00 56.70  ?  180 CYS A N     1 
ATOM   1294  C  CA    . CYS A 1 161 ? 180.807 173.468 134.341 1.00 59.09  ?  180 CYS A CA    1 
ATOM   1295  C  C     . CYS A 1 161 ? 179.743 174.436 133.836 1.00 49.78  ?  180 CYS A C     1 
ATOM   1296  O  O     . CYS A 1 161 ? 178.705 174.646 134.470 1.00 49.92  ?  180 CYS A O     1 
ATOM   1297  C  CB    . CYS A 1 161 ? 181.094 172.371 133.313 1.00 61.69  ?  180 CYS A CB    1 
ATOM   1298  S  SG    . CYS A 1 161 ? 181.855 172.958 131.784 1.00 72.06  ?  180 CYS A SG    1 
ATOM   1299  N  N     . ILE A 1 162 ? 180.016 175.035 132.675 1.00 55.59  ?  181 ILE A N     1 
ATOM   1300  C  CA    . ILE A 1 162 ? 179.090 176.011 132.107 1.00 64.99  ?  181 ILE A CA    1 
ATOM   1301  C  C     . ILE A 1 162 ? 177.775 175.343 131.724 1.00 66.35  ?  181 ILE A C     1 
ATOM   1302  O  O     . ILE A 1 162 ? 176.698 175.934 131.867 1.00 66.98  ?  181 ILE A O     1 
ATOM   1303  C  CB    . ILE A 1 162 ? 179.740 176.731 130.910 1.00 66.84  ?  181 ILE A CB    1 
ATOM   1304  C  CG1   . ILE A 1 162 ? 178.731 177.646 130.212 1.00 63.78  ?  181 ILE A CG1   1 
ATOM   1305  C  CG2   . ILE A 1 162 ? 180.333 175.728 129.928 1.00 62.13  ?  181 ILE A CG2   1 
ATOM   1306  C  CD1   . ILE A 1 162 ? 178.227 178.780 131.083 1.00 58.73  ?  181 ILE A CD1   1 
ATOM   1307  N  N     . SER A 1 163 ? 177.836 174.099 131.244 1.00 65.23  ?  182 SER A N     1 
ATOM   1308  C  CA    . SER A 1 163 ? 176.620 173.403 130.836 1.00 64.64  ?  182 SER A CA    1 
ATOM   1309  C  C     . SER A 1 163 ? 175.714 173.127 132.030 1.00 62.48  ?  182 SER A C     1 
ATOM   1310  O  O     . SER A 1 163 ? 174.512 173.414 131.992 1.00 64.62  ?  182 SER A O     1 
ATOM   1311  C  CB    . SER A 1 163 ? 176.980 172.101 130.119 1.00 64.57  ?  182 SER A CB    1 
ATOM   1312  O  OG    . SER A 1 163 ? 177.821 171.291 130.922 1.00 63.88  ?  182 SER A OG    1 
ATOM   1313  N  N     . GLU A 1 164 ? 176.275 172.567 133.104 1.00 55.13  ?  183 GLU A N     1 
ATOM   1314  C  CA    . GLU A 1 164 ? 175.458 172.198 134.256 1.00 58.06  ?  183 GLU A CA    1 
ATOM   1315  C  C     . GLU A 1 164 ? 175.017 173.428 135.042 1.00 62.94  ?  183 GLU A C     1 
ATOM   1316  O  O     . GLU A 1 164 ? 173.849 173.540 135.432 1.00 60.17  ?  183 GLU A O     1 
ATOM   1317  C  CB    . GLU A 1 164 ? 176.228 171.227 135.154 1.00 62.17  ?  183 GLU A CB    1 
ATOM   1318  C  CG    . GLU A 1 164 ? 175.347 170.311 135.998 1.00 64.58  ?  183 GLU A CG    1 
ATOM   1319  C  CD    . GLU A 1 164 ? 174.744 171.008 137.203 1.00 66.19  ?  183 GLU A CD    1 
ATOM   1320  O  OE1   . GLU A 1 164 ? 175.327 172.009 137.668 1.00 66.72  ?  183 GLU A OE1   1 
ATOM   1321  O  OE2   . GLU A 1 164 ? 173.685 170.554 137.686 1.00 64.04  -1 183 GLU A OE2   1 
ATOM   1322  N  N     . ALA A 1 165 ? 175.937 174.361 135.290 1.00 62.74  ?  184 ALA A N     1 
ATOM   1323  C  CA    . ALA A 1 165 ? 175.653 175.525 136.131 1.00 56.86  ?  184 ALA A CA    1 
ATOM   1324  C  C     . ALA A 1 165 ? 175.307 176.732 135.256 1.00 57.88  ?  184 ALA A C     1 
ATOM   1325  O  O     . ALA A 1 165 ? 176.065 177.695 135.126 1.00 55.26  ?  184 ALA A O     1 
ATOM   1326  C  CB    . ALA A 1 165 ? 176.832 175.815 137.050 1.00 55.32  ?  184 ALA A CB    1 
ATOM   1327  N  N     . SER A 1 166 ? 174.126 176.660 134.645 1.00 55.48  ?  185 SER A N     1 
ATOM   1328  C  CA    . SER A 1 166 ? 173.610 177.753 133.827 1.00 50.70  ?  185 SER A CA    1 
ATOM   1329  C  C     . SER A 1 166 ? 172.093 177.760 133.908 1.00 47.60  ?  185 SER A C     1 
ATOM   1330  O  O     . SER A 1 166 ? 171.452 176.737 133.650 1.00 51.06  ?  185 SER A O     1 
ATOM   1331  C  CB    . SER A 1 166 ? 174.068 177.622 132.372 1.00 52.49  ?  185 SER A CB    1 
ATOM   1332  O  OG    . SER A 1 166 ? 173.371 178.531 131.538 1.00 50.62  ?  185 SER A OG    1 
ATOM   1333  N  N     . GLY A 1 167 ? 171.522 178.910 134.262 1.00 40.17  ?  186 GLY A N     1 
ATOM   1334  C  CA    . GLY A 1 167 ? 170.091 179.091 134.314 1.00 46.01  ?  186 GLY A CA    1 
ATOM   1335  C  C     . GLY A 1 167 ? 169.474 178.923 135.687 1.00 52.03  ?  186 GLY A C     1 
ATOM   1336  O  O     . GLY A 1 167 ? 168.314 179.306 135.877 1.00 55.53  ?  186 GLY A O     1 
ATOM   1337  N  N     . MET A 1 168 ? 170.209 178.366 136.644 1.00 52.77  ?  187 MET A N     1 
ATOM   1338  C  CA    . MET A 1 168 ? 169.705 178.155 137.992 1.00 59.69  ?  187 MET A CA    1 
ATOM   1339  C  C     . MET A 1 168 ? 170.384 179.104 138.971 1.00 61.77  ?  187 MET A C     1 
ATOM   1340  O  O     . MET A 1 168 ? 171.498 179.584 138.740 1.00 57.96  ?  187 MET A O     1 
ATOM   1341  C  CB    . MET A 1 168 ? 169.912 176.704 138.442 1.00 59.30  ?  187 MET A CB    1 
ATOM   1342  C  CG    . MET A 1 168 ? 171.361 176.256 138.466 1.00 58.95  ?  187 MET A CG    1 
ATOM   1343  S  SD    . MET A 1 168 ? 172.022 175.998 136.813 1.00 77.97  ?  187 MET A SD    1 
ATOM   1344  C  CE    . MET A 1 168 ? 170.896 174.747 136.202 1.00 60.33  ?  187 MET A CE    1 
ATOM   1345  N  N     . GLN A 1 169 ? 169.686 179.374 140.071 1.00 59.44  ?  188 GLN A N     1 
ATOM   1346  C  CA    . GLN A 1 169 ? 170.229 180.227 141.114 1.00 48.07  ?  188 GLN A CA    1 
ATOM   1347  C  C     . GLN A 1 169 ? 171.482 179.586 141.708 1.00 42.08  ?  188 GLN A C     1 
ATOM   1348  O  O     . GLN A 1 169 ? 171.580 178.358 141.791 1.00 59.95  ?  188 GLN A O     1 
ATOM   1349  C  CB    . GLN A 1 169 ? 169.194 180.453 142.212 1.00 53.68  ?  188 GLN A CB    1 
ATOM   1350  C  CG    . GLN A 1 169 ? 167.929 181.162 141.764 1.00 54.83  ?  188 GLN A CG    1 
ATOM   1351  C  CD    . GLN A 1 169 ? 168.073 182.668 141.767 1.00 61.62  ?  188 GLN A CD    1 
ATOM   1352  O  OE1   . GLN A 1 169 ? 167.891 183.320 140.741 1.00 62.90  ?  188 GLN A OE1   1 
ATOM   1353  N  NE2   . GLN A 1 169 ? 168.401 183.230 142.924 1.00 58.88  ?  188 GLN A NE2   1 
ATOM   1354  N  N     . PRO A 1 170 ? 172.455 180.392 142.131 1.00 27.39  ?  189 PRO A N     1 
ATOM   1355  C  CA    . PRO A 1 170 ? 173.691 179.824 142.690 1.00 53.38  ?  189 PRO A CA    1 
ATOM   1356  C  C     . PRO A 1 170 ? 173.503 179.177 144.055 1.00 64.08  ?  189 PRO A C     1 
ATOM   1357  O  O     . PRO A 1 170 ? 174.487 178.811 144.704 1.00 68.72  ?  189 PRO A O     1 
ATOM   1358  C  CB    . PRO A 1 170 ? 174.633 181.036 142.781 1.00 57.98  ?  189 PRO A CB    1 
ATOM   1359  C  CG    . PRO A 1 170 ? 173.760 182.226 142.642 1.00 53.06  ?  189 PRO A CG    1 
ATOM   1360  C  CD    . PRO A 1 170 ? 172.605 181.817 141.801 1.00 42.34  ?  189 PRO A CD    1 
ATOM   1361  N  N     . ASP A 1 171 ? 172.259 179.048 144.515 1.00 68.86  ?  190 ASP A N     1 
ATOM   1362  C  CA    . ASP A 1 171 ? 171.966 178.324 145.745 1.00 62.62  ?  190 ASP A CA    1 
ATOM   1363  C  C     . ASP A 1 171 ? 171.233 177.011 145.516 1.00 61.18  ?  190 ASP A C     1 
ATOM   1364  O  O     . ASP A 1 171 ? 171.388 176.087 146.317 1.00 63.50  ?  190 ASP A O     1 
ATOM   1365  C  CB    . ASP A 1 171 ? 171.150 179.203 146.706 1.00 56.67  ?  190 ASP A CB    1 
ATOM   1366  C  CG    . ASP A 1 171 ? 169.780 179.569 146.161 1.00 59.56  ?  190 ASP A CG    1 
ATOM   1367  O  OD1   . ASP A 1 171 ? 169.457 179.192 145.018 1.00 63.22  ?  190 ASP A OD1   1 
ATOM   1368  O  OD2   . ASP A 1 171 ? 169.021 180.249 146.884 1.00 59.49  -1 190 ASP A OD2   1 
ATOM   1369  N  N     . THR A 1 172 ? 170.458 176.906 144.433 1.00 58.46  ?  191 THR A N     1 
ATOM   1370  C  CA    . THR A 1 172 ? 169.730 175.674 144.146 1.00 59.39  ?  191 THR A CA    1 
ATOM   1371  C  C     . THR A 1 172 ? 170.682 174.495 143.972 1.00 61.86  ?  191 THR A C     1 
ATOM   1372  O  O     . THR A 1 172 ? 170.451 173.411 144.520 1.00 57.05  ?  191 THR A O     1 
ATOM   1373  C  CB    . THR A 1 172 ? 168.866 175.857 142.897 1.00 55.71  ?  191 THR A CB    1 
ATOM   1374  O  OG1   . THR A 1 172 ? 169.711 176.055 141.756 1.00 54.17  ?  191 THR A OG1   1 
ATOM   1375  C  CG2   . THR A 1 172 ? 167.949 177.060 143.055 1.00 55.16  ?  191 THR A CG2   1 
ATOM   1376  N  N     . LEU A 1 173 ? 171.759 174.685 143.211 1.00 69.60  ?  192 LEU A N     1 
ATOM   1377  C  CA    . LEU A 1 173 ? 172.764 173.644 143.044 1.00 72.80  ?  192 LEU A CA    1 
ATOM   1378  C  C     . LEU A 1 173 ? 173.883 173.725 144.075 1.00 72.02  ?  192 LEU A C     1 
ATOM   1379  O  O     . LEU A 1 173 ? 174.708 172.808 144.143 1.00 69.41  ?  192 LEU A O     1 
ATOM   1380  C  CB    . LEU A 1 173 ? 173.373 173.699 141.636 1.00 67.57  ?  192 LEU A CB    1 
ATOM   1381  C  CG    . LEU A 1 173 ? 174.421 174.772 141.326 1.00 62.88  ?  192 LEU A CG    1 
ATOM   1382  C  CD1   . LEU A 1 173 ? 175.173 174.416 140.056 1.00 64.58  ?  192 LEU A CD1   1 
ATOM   1383  C  CD2   . LEU A 1 173 ? 173.798 176.150 141.198 1.00 60.79  ?  192 LEU A CD2   1 
ATOM   1384  N  N     . LEU A 1 174 ? 173.930 174.790 144.875 1.00 60.69  ?  193 LEU A N     1 
ATOM   1385  C  CA    . LEU A 1 174 ? 174.966 174.946 145.888 1.00 56.18  ?  193 LEU A CA    1 
ATOM   1386  C  C     . LEU A 1 174 ? 174.340 175.129 147.265 1.00 66.03  ?  193 LEU A C     1 
ATOM   1387  O  O     . LEU A 1 174 ? 174.757 176.002 148.032 1.00 67.03  ?  193 LEU A O     1 
ATOM   1388  C  CB    . LEU A 1 174 ? 175.874 176.129 145.546 1.00 57.00  ?  193 LEU A CB    1 
ATOM   1389  C  CG    . LEU A 1 174 ? 176.483 176.119 144.141 1.00 63.78  ?  193 LEU A CG    1 
ATOM   1390  C  CD1   . LEU A 1 174 ? 177.353 177.343 143.903 1.00 65.47  ?  193 LEU A CD1   1 
ATOM   1391  C  CD2   . LEU A 1 174 ? 177.285 174.849 143.920 1.00 64.98  ?  193 LEU A CD2   1 
ATOM   1392  N  N     . ASN A 1 175 ? 173.328 174.321 147.571 1.00 76.31  ?  194 ASN A N     1 
ATOM   1393  C  CA    . ASN A 1 175 ? 172.652 174.403 148.858 1.00 74.82  ?  194 ASN A CA    1 
ATOM   1394  C  C     . ASN A 1 175 ? 173.624 174.175 150.011 1.00 66.04  ?  194 ASN A C     1 
ATOM   1395  O  O     . ASN A 1 175 ? 174.567 173.384 149.919 1.00 59.54  ?  194 ASN A O     1 
ATOM   1396  C  CB    . ASN A 1 175 ? 171.513 173.383 148.924 1.00 76.28  ?  194 ASN A CB    1 
ATOM   1397  C  CG    . ASN A 1 175 ? 171.945 171.995 148.488 1.00 75.77  ?  194 ASN A CG    1 
ATOM   1398  O  OD1   . ASN A 1 175 ? 173.086 171.786 148.077 1.00 74.16  ?  194 ASN A OD1   1 
ATOM   1399  N  ND2   . ASN A 1 175 ? 171.029 171.036 148.578 1.00 73.29  ?  194 ASN A ND2   1 
ATOM   1400  N  N     . THR A 1 176 ? 173.380 174.889 151.102 1.00 70.11  ?  195 THR A N     1 
ATOM   1401  C  CA    . THR A 1 176 ? 174.220 174.842 152.288 1.00 75.52  ?  195 THR A CA    1 
ATOM   1402  C  C     . THR A 1 176 ? 173.981 173.546 153.055 1.00 77.64  ?  195 THR A C     1 
ATOM   1403  O  O     . THR A 1 176 ? 172.996 172.842 152.824 1.00 75.26  ?  195 THR A O     1 
ATOM   1404  C  CB    . THR A 1 176 ? 173.931 176.060 153.165 1.00 79.17  ?  195 THR A CB    1 
ATOM   1405  O  OG1   . THR A 1 176 ? 172.690 175.871 153.856 1.00 79.81  ?  195 THR A OG1   1 
ATOM   1406  C  CG2   . THR A 1 176 ? 173.843 177.319 152.315 1.00 75.17  ?  195 THR A CG2   1 
ATOM   1407  N  N     . PRO A 1 177 ? 174.884 173.194 153.989 1.00 86.53  ?  196 PRO A N     1 
ATOM   1408  C  CA    . PRO A 1 177 ? 174.691 171.965 154.776 1.00 84.90  ?  196 PRO A CA    1 
ATOM   1409  C  C     . PRO A 1 177 ? 173.493 172.026 155.714 1.00 83.77  ?  196 PRO A C     1 
ATOM   1410  O  O     . PRO A 1 177 ? 172.709 172.980 155.679 1.00 83.94  ?  196 PRO A O     1 
ATOM   1411  C  CB    . PRO A 1 177 ? 176.005 171.836 155.560 1.00 83.76  ?  196 PRO A CB    1 
ATOM   1412  C  CG    . PRO A 1 177 ? 176.616 173.196 155.527 1.00 82.14  ?  196 PRO A CG    1 
ATOM   1413  C  CD    . PRO A 1 177 ? 176.224 173.767 154.206 1.00 82.38  ?  196 PRO A CD    1 
ATOM   1414  N  N     . GLU A 1 178 ? 173.353 170.990 156.549 1.00 89.23  ?  197 GLU A N     1 
ATOM   1415  C  CA    . GLU A 1 178 ? 172.134 170.786 157.331 1.00 90.50  ?  197 GLU A CA    1 
ATOM   1416  C  C     . GLU A 1 178 ? 171.748 172.016 158.145 1.00 86.89  ?  197 GLU A C     1 
ATOM   1417  O  O     . GLU A 1 178 ? 170.559 172.320 158.287 1.00 86.79  ?  197 GLU A O     1 
ATOM   1418  C  CB    . GLU A 1 178 ? 172.310 169.576 158.252 1.00 92.47  ?  197 GLU A CB    1 
ATOM   1419  C  CG    . GLU A 1 178 ? 171.137 169.320 159.185 1.00 90.59  ?  197 GLU A CG    1 
ATOM   1420  C  CD    . GLU A 1 178 ? 169.904 168.825 158.455 1.00 88.92  ?  197 GLU A CD    1 
ATOM   1421  O  OE1   . GLU A 1 178 ? 170.057 168.176 157.400 1.00 89.15  ?  197 GLU A OE1   1 
ATOM   1422  O  OE2   . GLU A 1 178 ? 168.782 169.086 158.937 1.00 88.16  -1 197 GLU A OE2   1 
ATOM   1423  N  N     . PHE A 1 179 ? 172.736 172.732 158.690 1.00 78.97  ?  198 PHE A N     1 
ATOM   1424  C  CA    . PHE A 1 179 ? 172.515 173.934 159.490 1.00 78.30  ?  198 PHE A CA    1 
ATOM   1425  C  C     . PHE A 1 179 ? 171.725 174.961 158.685 1.00 85.26  ?  198 PHE A C     1 
ATOM   1426  O  O     . PHE A 1 179 ? 172.262 175.554 157.743 1.00 84.10  ?  198 PHE A O     1 
ATOM   1427  C  CB    . PHE A 1 179 ? 173.859 174.504 159.951 1.00 80.01  ?  198 PHE A CB    1 
ATOM   1428  C  CG    . PHE A 1 179 ? 173.813 175.955 160.336 1.00 81.94  ?  198 PHE A CG    1 
ATOM   1429  C  CD1   . PHE A 1 179 ? 173.152 176.364 161.480 1.00 81.61  ?  198 PHE A CD1   1 
ATOM   1430  C  CD2   . PHE A 1 179 ? 174.449 176.909 159.558 1.00 85.39  ?  198 PHE A CD2   1 
ATOM   1431  C  CE1   . PHE A 1 179 ? 173.118 177.698 161.836 1.00 82.86  ?  198 PHE A CE1   1 
ATOM   1432  C  CE2   . PHE A 1 179 ? 174.416 178.243 159.907 1.00 85.30  ?  198 PHE A CE2   1 
ATOM   1433  C  CZ    . PHE A 1 179 ? 173.749 178.639 161.047 1.00 83.70  ?  198 PHE A CZ    1 
ATOM   1434  N  N     . PRO A 1 180 ? 170.440 175.181 159.006 1.00 96.13  ?  199 PRO A N     1 
ATOM   1435  C  CA    . PRO A 1 180 ? 169.596 176.018 158.145 1.00 93.93  ?  199 PRO A CA    1 
ATOM   1436  C  C     . PRO A 1 180 ? 169.414 177.454 158.619 1.00 91.89  ?  199 PRO A C     1 
ATOM   1437  O  O     . PRO A 1 180 ? 168.839 178.272 157.894 1.00 90.68  ?  199 PRO A O     1 
ATOM   1438  C  CB    . PRO A 1 180 ? 168.259 175.267 158.163 1.00 91.33  ?  199 PRO A CB    1 
ATOM   1439  C  CG    . PRO A 1 180 ? 168.258 174.512 159.507 1.00 90.00  ?  199 PRO A CG    1 
ATOM   1440  C  CD    . PRO A 1 180 ? 169.655 174.587 160.100 1.00 93.04  ?  199 PRO A CD    1 
ATOM   1441  N  N     . ALA A 1 181 ? 169.888 177.772 159.826 1.00 91.68  ?  200 ALA A N     1 
ATOM   1442  C  CA    . ALA A 1 181 ? 169.445 178.994 160.494 1.00 91.64  ?  200 ALA A CA    1 
ATOM   1443  C  C     . ALA A 1 181 ? 169.910 180.252 159.767 1.00 92.30  ?  200 ALA A C     1 
ATOM   1444  O  O     . ALA A 1 181 ? 169.125 181.190 159.584 1.00 90.26  ?  200 ALA A O     1 
ATOM   1445  C  CB    . ALA A 1 181 ? 169.929 179.007 161.943 1.00 89.91  ?  200 ALA A CB    1 
ATOM   1446  N  N     . ASP A 1 182 ? 171.170 180.299 159.347 1.00 87.17  ?  201 ASP A N     1 
ATOM   1447  C  CA    . ASP A 1 182 ? 171.731 181.541 158.826 1.00 83.92  ?  201 ASP A CA    1 
ATOM   1448  C  C     . ASP A 1 182 ? 172.300 181.430 157.422 1.00 81.23  ?  201 ASP A C     1 
ATOM   1449  O  O     . ASP A 1 182 ? 172.154 182.368 156.637 1.00 80.63  ?  201 ASP A O     1 
ATOM   1450  C  CB    . ASP A 1 182 ? 172.829 182.060 159.768 1.00 80.68  ?  201 ASP A CB    1 
ATOM   1451  C  CG    . ASP A 1 182 ? 172.270 182.661 161.043 1.00 82.32  ?  201 ASP A CG    1 
ATOM   1452  O  OD1   . ASP A 1 182 ? 171.031 182.767 161.161 1.00 79.82  ?  201 ASP A OD1   1 
ATOM   1453  O  OD2   . ASP A 1 182 ? 173.071 183.032 161.926 1.00 84.82  -1 201 ASP A OD2   1 
ATOM   1454  N  N     . ASN A 1 183 ? 172.960 180.319 157.088 1.00 70.71  ?  202 ASN A N     1 
ATOM   1455  C  CA    . ASN A 1 183 ? 173.692 180.242 155.826 1.00 70.07  ?  202 ASN A CA    1 
ATOM   1456  C  C     . ASN A 1 183 ? 172.752 180.320 154.629 1.00 74.75  ?  202 ASN A C     1 
ATOM   1457  O  O     . ASN A 1 183 ? 173.002 181.070 153.679 1.00 78.34  ?  202 ASN A O     1 
ATOM   1458  C  CB    . ASN A 1 183 ? 174.516 178.956 155.782 1.00 73.21  ?  202 ASN A CB    1 
ATOM   1459  C  CG    . ASN A 1 183 ? 173.719 177.749 156.209 1.00 79.78  ?  202 ASN A CG    1 
ATOM   1460  O  OD1   . ASN A 1 183 ? 172.503 177.832 156.387 1.00 76.70  ?  202 ASN A OD1   1 
ATOM   1461  N  ND2   . ASN A 1 183 ? 174.394 176.617 156.380 1.00 81.11  ?  202 ASN A ND2   1 
ATOM   1462  N  N     . ARG A 1 184 ? 171.663 179.547 154.656 1.00 68.53  ?  203 ARG A N     1 
ATOM   1463  C  CA    . ARG A 1 184 ? 170.729 179.538 153.532 1.00 66.02  ?  203 ARG A CA    1 
ATOM   1464  C  C     . ARG A 1 184 ? 170.093 180.907 153.337 1.00 66.54  ?  203 ARG A C     1 
ATOM   1465  O  O     . ARG A 1 184 ? 170.008 181.414 152.210 1.00 68.80  ?  203 ARG A O     1 
ATOM   1466  C  CB    . ARG A 1 184 ? 169.653 178.474 153.756 1.00 67.51  ?  203 ARG A CB    1 
ATOM   1467  C  CG    . ARG A 1 184 ? 169.922 177.150 153.063 1.00 67.98  ?  203 ARG A CG    1 
ATOM   1468  C  CD    . ARG A 1 184 ? 168.835 176.135 153.382 1.00 69.73  ?  203 ARG A CD    1 
ATOM   1469  N  NE    . ARG A 1 184 ? 169.214 174.780 152.999 1.00 70.30  ?  203 ARG A NE    1 
ATOM   1470  C  CZ    . ARG A 1 184 ? 169.252 173.750 153.833 1.00 70.71  ?  203 ARG A CZ    1 
ATOM   1471  N  NH1   . ARG A 1 184 ? 168.937 173.883 155.111 1.00 69.09  1  203 ARG A NH1   1 
ATOM   1472  N  NH2   . ARG A 1 184 ? 169.615 172.556 153.373 1.00 69.80  ?  203 ARG A NH2   1 
ATOM   1473  N  N     . ILE A 1 185 ? 169.647 181.527 154.431 1.00 61.24  ?  204 ILE A N     1 
ATOM   1474  C  CA    . ILE A 1 185 ? 168.982 182.822 154.332 1.00 63.40  ?  204 ILE A CA    1 
ATOM   1475  C  C     . ILE A 1 185 ? 169.957 183.893 153.861 1.00 66.84  ?  204 ILE A C     1 
ATOM   1476  O  O     . ILE A 1 185 ? 169.610 184.741 153.032 1.00 66.15  ?  204 ILE A O     1 
ATOM   1477  C  CB    . ILE A 1 185 ? 168.333 183.191 155.678 1.00 63.40  ?  204 ILE A CB    1 
ATOM   1478  C  CG1   . ILE A 1 185 ? 167.295 182.139 156.071 1.00 64.59  ?  204 ILE A CG1   1 
ATOM   1479  C  CG2   . ILE A 1 185 ? 167.692 184.570 155.605 1.00 59.64  ?  204 ILE A CG2   1 
ATOM   1480  C  CD1   . ILE A 1 185 ? 166.136 182.036 155.105 1.00 63.87  ?  204 ILE A CD1   1 
ATOM   1481  N  N     . ARG A 1 186 ? 171.195 183.865 154.361 1.00 66.53  ?  205 ARG A N     1 
ATOM   1482  C  CA    . ARG A 1 186 ? 172.181 184.857 153.948 1.00 60.86  ?  205 ARG A CA    1 
ATOM   1483  C  C     . ARG A 1 186 ? 172.565 184.678 152.485 1.00 54.72  ?  205 ARG A C     1 
ATOM   1484  O  O     . ARG A 1 186 ? 172.741 185.664 151.758 1.00 56.38  ?  205 ARG A O     1 
ATOM   1485  C  CB    . ARG A 1 186 ? 173.409 184.768 154.855 1.00 55.09  ?  205 ARG A CB    1 
ATOM   1486  C  CG    . ARG A 1 186 ? 174.375 185.934 154.738 1.00 57.21  ?  205 ARG A CG    1 
ATOM   1487  C  CD    . ARG A 1 186 ? 175.453 185.851 155.810 1.00 58.43  ?  205 ARG A CD    1 
ATOM   1488  N  NE    . ARG A 1 186 ? 176.267 184.648 155.683 1.00 59.71  ?  205 ARG A NE    1 
ATOM   1489  C  CZ    . ARG A 1 186 ? 176.276 183.653 156.560 1.00 61.65  ?  205 ARG A CZ    1 
ATOM   1490  N  NH1   . ARG A 1 186 ? 175.529 183.686 157.650 1.00 63.95  1  205 ARG A NH1   1 
ATOM   1491  N  NH2   . ARG A 1 186 ? 177.055 182.598 156.336 1.00 61.48  ?  205 ARG A NH2   1 
ATOM   1492  N  N     . LEU A 1 187 ? 172.693 183.428 152.032 1.00 47.53  ?  206 LEU A N     1 
ATOM   1493  C  CA    . LEU A 1 187 ? 173.010 183.177 150.630 1.00 47.09  ?  206 LEU A CA    1 
ATOM   1494  C  C     . LEU A 1 187 ? 171.866 183.614 149.725 1.00 48.64  ?  206 LEU A C     1 
ATOM   1495  O  O     . LEU A 1 187 ? 172.099 184.147 148.635 1.00 53.49  ?  206 LEU A O     1 
ATOM   1496  C  CB    . LEU A 1 187 ? 173.338 181.695 150.432 1.00 56.40  ?  206 LEU A CB    1 
ATOM   1497  C  CG    . LEU A 1 187 ? 173.355 181.083 149.028 1.00 57.45  ?  206 LEU A CG    1 
ATOM   1498  C  CD1   . LEU A 1 187 ? 174.257 181.865 148.084 1.00 50.52  ?  206 LEU A CD1   1 
ATOM   1499  C  CD2   . LEU A 1 187 ? 173.795 179.630 149.103 1.00 55.80  ?  206 LEU A CD2   1 
ATOM   1500  N  N     . GLN A 1 188 ? 170.621 183.411 150.162 1.00 50.70  ?  207 GLN A N     1 
ATOM   1501  C  CA    . GLN A 1 188 ? 169.490 183.856 149.357 1.00 50.71  ?  207 GLN A CA    1 
ATOM   1502  C  C     . GLN A 1 188 ? 169.350 185.374 149.374 1.00 52.21  ?  207 GLN A C     1 
ATOM   1503  O  O     . GLN A 1 188 ? 168.874 185.961 148.396 1.00 53.87  ?  207 GLN A O     1 
ATOM   1504  C  CB    . GLN A 1 188 ? 168.205 183.191 149.850 1.00 48.92  ?  207 GLN A CB    1 
ATOM   1505  C  CG    . GLN A 1 188 ? 167.057 183.237 148.857 1.00 49.01  ?  207 GLN A CG    1 
ATOM   1506  C  CD    . GLN A 1 188 ? 166.038 184.305 149.198 1.00 56.01  ?  207 GLN A CD    1 
ATOM   1507  O  OE1   . GLN A 1 188 ? 165.924 184.725 150.349 1.00 58.87  ?  207 GLN A OE1   1 
ATOM   1508  N  NE2   . GLN A 1 188 ? 165.290 184.752 148.196 1.00 53.35  ?  207 GLN A NE2   1 
ATOM   1509  N  N     . GLN A 1 189 ? 169.764 186.024 150.463 1.00 44.55  ?  208 GLN A N     1 
ATOM   1510  C  CA    . GLN A 1 189 ? 169.641 187.473 150.565 1.00 44.18  ?  208 GLN A CA    1 
ATOM   1511  C  C     . GLN A 1 189 ? 170.746 188.200 149.811 1.00 50.58  ?  208 GLN A C     1 
ATOM   1512  O  O     . GLN A 1 189 ? 170.512 189.297 149.291 1.00 52.22  ?  208 GLN A O     1 
ATOM   1513  C  CB    . GLN A 1 189 ? 169.647 187.897 152.034 1.00 47.22  ?  208 GLN A CB    1 
ATOM   1514  C  CG    . GLN A 1 189 ? 168.309 187.723 152.733 1.00 52.04  ?  208 GLN A CG    1 
ATOM   1515  C  CD    . GLN A 1 189 ? 167.449 188.969 152.667 1.00 56.69  ?  208 GLN A CD    1 
ATOM   1516  O  OE1   . GLN A 1 189 ? 167.376 189.633 151.633 1.00 54.97  ?  208 GLN A OE1   1 
ATOM   1517  N  NE2   . GLN A 1 189 ? 166.794 189.294 153.775 1.00 53.75  ?  208 GLN A NE2   1 
ATOM   1518  N  N     . LEU A 1 190 ? 171.947 187.620 149.751 1.00 42.66  ?  209 LEU A N     1 
ATOM   1519  C  CA    . LEU A 1 190 ? 173.039 188.260 149.023 1.00 24.93  ?  209 LEU A CA    1 
ATOM   1520  C  C     . LEU A 1 190 ? 172.718 188.362 147.537 1.00 28.11  ?  209 LEU A C     1 
ATOM   1521  O  O     . LEU A 1 190 ? 173.045 189.362 146.887 1.00 36.94  ?  209 LEU A O     1 
ATOM   1522  C  CB    . LEU A 1 190 ? 174.342 187.490 149.245 1.00 24.01  ?  209 LEU A CB    1 
ATOM   1523  C  CG    . LEU A 1 190 ? 175.573 188.031 148.519 1.00 28.01  ?  209 LEU A CG    1 
ATOM   1524  C  CD1   . LEU A 1 190 ? 176.204 189.153 149.325 1.00 35.63  ?  209 LEU A CD1   1 
ATOM   1525  C  CD2   . LEU A 1 190 ? 176.581 186.928 148.257 1.00 32.67  ?  209 LEU A CD2   1 
ATOM   1526  N  N     . LEU A 1 191 ? 172.081 187.329 146.982 1.00 39.72  ?  210 LEU A N     1 
ATOM   1527  C  CA    . LEU A 1 191 ? 171.682 187.346 145.580 1.00 41.95  ?  210 LEU A CA    1 
ATOM   1528  C  C     . LEU A 1 191 ? 170.647 188.417 145.269 1.00 49.93  ?  210 LEU A C     1 
ATOM   1529  O  O     . LEU A 1 191 ? 170.472 188.767 144.097 1.00 46.12  ?  210 LEU A O     1 
ATOM   1530  C  CB    . LEU A 1 191 ? 171.141 185.976 145.166 1.00 31.24  ?  210 LEU A CB    1 
ATOM   1531  C  CG    . LEU A 1 191 ? 172.171 184.935 144.731 1.00 42.00  ?  210 LEU A CG    1 
ATOM   1532  C  CD1   . LEU A 1 191 ? 172.826 185.467 143.489 1.00 45.74  ?  210 LEU A CD1   1 
ATOM   1533  C  CD2   . LEU A 1 191 ? 173.215 184.627 145.786 1.00 43.58  ?  210 LEU A CD2   1 
ATOM   1534  N  N     . TRP A 1 192 ? 169.954 188.942 146.276 1.00 47.78  ?  211 TRP A N     1 
ATOM   1535  C  CA    . TRP A 1 192 ? 168.920 189.934 146.013 1.00 39.48  ?  211 TRP A CA    1 
ATOM   1536  C  C     . TRP A 1 192 ? 169.249 191.254 146.698 1.00 35.03  ?  211 TRP A C     1 
ATOM   1537  O  O     . TRP A 1 192 ? 168.380 191.877 147.316 1.00 41.61  ?  211 TRP A O     1 
ATOM   1538  C  CB    . TRP A 1 192 ? 167.554 189.409 146.456 1.00 30.70  ?  211 TRP A CB    1 
ATOM   1539  C  CG    . TRP A 1 192 ? 167.088 188.249 145.632 1.00 26.66  ?  211 TRP A CG    1 
ATOM   1540  C  CD1   . TRP A 1 192 ? 167.163 186.928 145.963 1.00 31.02  ?  211 TRP A CD1   1 
ATOM   1541  C  CD2   . TRP A 1 192 ? 166.502 188.303 144.327 1.00 36.84  ?  211 TRP A CD2   1 
ATOM   1542  N  NE1   . TRP A 1 192 ? 166.647 186.156 144.951 1.00 35.11  ?  211 TRP A NE1   1 
ATOM   1543  C  CE2   . TRP A 1 192 ? 166.236 186.976 143.934 1.00 41.00  ?  211 TRP A CE2   1 
ATOM   1544  C  CE3   . TRP A 1 192 ? 166.172 189.344 143.454 1.00 40.11  ?  211 TRP A CE3   1 
ATOM   1545  C  CZ2   . TRP A 1 192 ? 165.654 186.664 142.708 1.00 43.58  ?  211 TRP A CZ2   1 
ATOM   1546  C  CZ3   . TRP A 1 192 ? 165.595 189.031 142.238 1.00 41.12  ?  211 TRP A CZ3   1 
ATOM   1547  C  CH2   . TRP A 1 192 ? 165.342 187.703 141.875 1.00 43.81  ?  211 TRP A CH2   1 
ATOM   1548  N  N     . LYS A 1 193 ? 170.503 191.682 146.592 1.00 25.39  ?  212 LYS A N     1 
ATOM   1549  C  CA    . LYS A 1 193 ? 170.942 192.985 147.067 1.00 28.83  ?  212 LYS A CA    1 
ATOM   1550  C  C     . LYS A 1 193 ? 171.200 193.876 145.860 1.00 36.05  ?  212 LYS A C     1 
ATOM   1551  O  O     . LYS A 1 193 ? 171.930 193.486 144.942 1.00 38.93  ?  212 LYS A O     1 
ATOM   1552  C  CB    . LYS A 1 193 ? 172.204 192.865 147.925 1.00 24.81  ?  212 LYS A CB    1 
ATOM   1553  C  CG    . LYS A 1 193 ? 172.572 194.135 148.673 1.00 24.68  ?  212 LYS A CG    1 
ATOM   1554  C  CD    . LYS A 1 193 ? 171.540 194.463 149.740 1.00 37.30  ?  212 LYS A CD    1 
ATOM   1555  C  CE    . LYS A 1 193 ? 171.444 193.352 150.775 1.00 37.35  ?  212 LYS A CE    1 
ATOM   1556  N  NZ    . LYS A 1 193 ? 172.709 193.196 151.544 1.00 36.69  1  212 LYS A NZ    1 
ATOM   1557  N  N     . THR A 1 194 ? 170.604 195.066 145.864 1.00 35.07  ?  213 THR A N     1 
ATOM   1558  C  CA    . THR A 1 194 ? 170.674 195.961 144.716 1.00 30.25  ?  213 THR A CA    1 
ATOM   1559  C  C     . THR A 1 194 ? 171.943 196.803 144.688 1.00 28.92  ?  213 THR A C     1 
ATOM   1560  O  O     . THR A 1 194 ? 172.130 197.579 143.745 1.00 25.23  ?  213 THR A O     1 
ATOM   1561  C  CB    . THR A 1 194 ? 169.451 196.883 144.691 1.00 35.97  ?  213 THR A CB    1 
ATOM   1562  O  OG1   . THR A 1 194 ? 169.385 197.559 143.429 1.00 40.16  ?  213 THR A OG1   1 
ATOM   1563  C  CG2   . THR A 1 194 ? 169.536 197.909 145.811 1.00 33.98  ?  213 THR A CG2   1 
ATOM   1564  N  N     . ALA A 1 195 ? 172.809 196.675 145.688 1.00 30.03  ?  214 ALA A N     1 
ATOM   1565  C  CA    . ALA A 1 195 ? 174.054 197.424 145.753 1.00 22.67  ?  214 ALA A CA    1 
ATOM   1566  C  C     . ALA A 1 195 ? 175.209 196.456 145.971 1.00 26.55  ?  214 ALA A C     1 
ATOM   1567  O  O     . ALA A 1 195 ? 175.012 195.258 146.198 1.00 34.30  ?  214 ALA A O     1 
ATOM   1568  C  CB    . ALA A 1 195 ? 174.007 198.484 146.861 1.00 24.23  ?  214 ALA A CB    1 
ATOM   1569  N  N     . ARG A 1 196 ? 176.426 196.988 145.888 1.00 29.16  ?  215 ARG A N     1 
ATOM   1570  C  CA    . ARG A 1 196 ? 177.618 196.195 146.155 1.00 25.88  ?  215 ARG A CA    1 
ATOM   1571  C  C     . ARG A 1 196 ? 177.568 195.625 147.567 1.00 32.50  ?  215 ARG A C     1 
ATOM   1572  O  O     . ARG A 1 196 ? 177.301 196.348 148.532 1.00 49.01  ?  215 ARG A O     1 
ATOM   1573  C  CB    . ARG A 1 196 ? 178.866 197.059 145.971 1.00 25.87  ?  215 ARG A CB    1 
ATOM   1574  C  CG    . ARG A 1 196 ? 180.119 196.514 146.630 1.00 26.38  ?  215 ARG A CG    1 
ATOM   1575  C  CD    . ARG A 1 196 ? 180.868 195.580 145.700 1.00 33.26  ?  215 ARG A CD    1 
ATOM   1576  N  NE    . ARG A 1 196 ? 182.106 195.095 146.297 1.00 44.18  ?  215 ARG A NE    1 
ATOM   1577  C  CZ    . ARG A 1 196 ? 182.225 193.944 146.942 1.00 45.09  ?  215 ARG A CZ    1 
ATOM   1578  N  NH1   . ARG A 1 196 ? 181.194 193.129 147.097 1.00 41.02  1  215 ARG A NH1   1 
ATOM   1579  N  NH2   . ARG A 1 196 ? 183.407 193.602 147.448 1.00 40.03  ?  215 ARG A NH2   1 
ATOM   1580  N  N     . ASP A 1 197 ? 177.823 194.325 147.688 1.00 17.92  ?  216 ASP A N     1 
ATOM   1581  C  CA    . ASP A 1 197 ? 177.768 193.661 148.983 1.00 21.50  ?  216 ASP A CA    1 
ATOM   1582  C  C     . ASP A 1 197 ? 178.607 192.395 148.913 1.00 25.32  ?  216 ASP A C     1 
ATOM   1583  O  O     . ASP A 1 197 ? 179.081 191.997 147.847 1.00 36.23  ?  216 ASP A O     1 
ATOM   1584  C  CB    . ASP A 1 197 ? 176.322 193.351 149.388 1.00 29.68  ?  216 ASP A CB    1 
ATOM   1585  C  CG    . ASP A 1 197 ? 176.142 193.256 150.891 1.00 43.18  ?  216 ASP A CG    1 
ATOM   1586  O  OD1   . ASP A 1 197 ? 177.082 192.803 151.578 1.00 45.81  ?  216 ASP A OD1   1 
ATOM   1587  O  OD2   . ASP A 1 197 ? 175.061 193.638 151.385 1.00 44.97  -1 216 ASP A OD2   1 
ATOM   1588  N  N     . GLN A 1 198 ? 178.787 191.763 150.069 1.00 27.09  ?  217 GLN A N     1 
ATOM   1589  C  CA    . GLN A 1 198 ? 179.567 190.537 150.140 1.00 21.90  ?  217 GLN A CA    1 
ATOM   1590  C  C     . GLN A 1 198 ? 179.219 189.802 151.425 1.00 27.82  ?  217 GLN A C     1 
ATOM   1591  O  O     . GLN A 1 198 ? 178.725 190.393 152.388 1.00 42.41  ?  217 GLN A O     1 
ATOM   1592  C  CB    . GLN A 1 198 ? 181.070 190.826 150.063 1.00 26.06  ?  217 GLN A CB    1 
ATOM   1593  C  CG    . GLN A 1 198 ? 181.605 191.662 151.211 1.00 35.78  ?  217 GLN A CG    1 
ATOM   1594  C  CD    . GLN A 1 198 ? 183.059 192.037 151.018 1.00 39.36  ?  217 GLN A CD    1 
ATOM   1595  O  OE1   . GLN A 1 198 ? 183.689 191.641 150.036 1.00 37.53  ?  217 GLN A OE1   1 
ATOM   1596  N  NE2   . GLN A 1 198 ? 183.602 192.804 151.956 1.00 37.45  ?  217 GLN A NE2   1 
ATOM   1597  N  N     . ASP A 1 199 ? 179.491 188.499 151.422 1.00 27.14  ?  218 ASP A N     1 
ATOM   1598  C  CA    . ASP A 1 199 ? 179.180 187.631 152.548 1.00 30.11  ?  218 ASP A CA    1 
ATOM   1599  C  C     . ASP A 1 199 ? 180.106 186.421 152.503 1.00 36.66  ?  218 ASP A C     1 
ATOM   1600  O  O     . ASP A 1 199 ? 180.918 186.269 151.586 1.00 51.89  ?  218 ASP A O     1 
ATOM   1601  C  CB    . ASP A 1 199 ? 177.710 187.202 152.522 1.00 34.79  ?  218 ASP A CB    1 
ATOM   1602  C  CG    . ASP A 1 199 ? 176.794 188.207 153.190 1.00 47.37  ?  218 ASP A CG    1 
ATOM   1603  O  OD1   . ASP A 1 199 ? 177.206 188.813 154.199 1.00 49.32  ?  218 ASP A OD1   1 
ATOM   1604  O  OD2   . ASP A 1 199 ? 175.661 188.395 152.699 1.00 49.70  -1 218 ASP A OD2   1 
ATOM   1605  N  N     . GLU A 1 200 ? 179.980 185.558 153.509 1.00 32.05  ?  219 GLU A N     1 
ATOM   1606  C  CA    . GLU A 1 200 ? 180.754 184.328 153.599 1.00 33.81  ?  219 GLU A CA    1 
ATOM   1607  C  C     . GLU A 1 200 ? 179.810 183.158 153.838 1.00 38.26  ?  219 GLU A C     1 
ATOM   1608  O  O     . GLU A 1 200 ? 178.889 183.252 154.655 1.00 45.12  ?  219 GLU A O     1 
ATOM   1609  C  CB    . GLU A 1 200 ? 181.797 184.414 154.719 1.00 37.27  ?  219 GLU A CB    1 
ATOM   1610  C  CG    . GLU A 1 200 ? 182.710 185.626 154.610 1.00 42.79  ?  219 GLU A CG    1 
ATOM   1611  C  CD    . GLU A 1 200 ? 183.755 185.671 155.705 1.00 46.88  ?  219 GLU A CD    1 
ATOM   1612  O  OE1   . GLU A 1 200 ? 183.581 184.971 156.724 1.00 49.00  ?  219 GLU A OE1   1 
ATOM   1613  O  OE2   . GLU A 1 200 ? 184.753 186.405 155.545 1.00 43.00  -1 219 GLU A OE2   1 
ATOM   1614  N  N     . PHE A 1 201 ? 180.050 182.052 153.135 1.00 35.21  ?  220 PHE A N     1 
ATOM   1615  C  CA    . PHE A 1 201 ? 179.106 180.944 153.104 1.00 33.91  ?  220 PHE A CA    1 
ATOM   1616  C  C     . PHE A 1 201 ? 179.825 179.608 153.219 1.00 49.17  ?  220 PHE A C     1 
ATOM   1617  O  O     . PHE A 1 201 ? 181.021 179.488 152.944 1.00 53.70  ?  220 PHE A O     1 
ATOM   1618  C  CB    . PHE A 1 201 ? 178.280 180.929 151.811 1.00 37.78  ?  220 PHE A CB    1 
ATOM   1619  C  CG    . PHE A 1 201 ? 177.552 182.205 151.535 1.00 35.24  ?  220 PHE A CG    1 
ATOM   1620  C  CD1   . PHE A 1 201 ? 176.722 182.770 152.486 1.00 42.41  ?  220 PHE A CD1   1 
ATOM   1621  C  CD2   . PHE A 1 201 ? 177.686 182.832 150.310 1.00 36.26  ?  220 PHE A CD2   1 
ATOM   1622  C  CE1   . PHE A 1 201 ? 176.050 183.945 152.223 1.00 47.78  ?  220 PHE A CE1   1 
ATOM   1623  C  CE2   . PHE A 1 201 ? 177.017 184.001 150.040 1.00 38.86  ?  220 PHE A CE2   1 
ATOM   1624  C  CZ    . PHE A 1 201 ? 176.196 184.560 150.996 1.00 45.16  ?  220 PHE A CZ    1 
ATOM   1625  N  N     . LEU A 1 202 ? 179.060 178.601 153.639 1.00 57.98  ?  221 LEU A N     1 
ATOM   1626  C  CA    . LEU A 1 202 ? 179.403 177.198 153.449 1.00 45.69  ?  221 LEU A CA    1 
ATOM   1627  C  C     . LEU A 1 202 ? 178.640 176.682 152.238 1.00 49.87  ?  221 LEU A C     1 
ATOM   1628  O  O     . LEU A 1 202 ? 177.405 176.670 152.240 1.00 59.03  ?  221 LEU A O     1 
ATOM   1629  C  CB    . LEU A 1 202 ? 179.053 176.364 154.681 1.00 44.95  ?  221 LEU A CB    1 
ATOM   1630  C  CG    . LEU A 1 202 ? 180.028 176.335 155.852 1.00 45.97  ?  221 LEU A CG    1 
ATOM   1631  C  CD1   . LEU A 1 202 ? 179.381 175.667 157.053 1.00 54.31  ?  221 LEU A CD1   1 
ATOM   1632  C  CD2   . LEU A 1 202 ? 181.288 175.592 155.444 1.00 51.12  ?  221 LEU A CD2   1 
ATOM   1633  N  N     . LEU A 1 203 ? 179.370 176.251 151.216 1.00 48.78  ?  222 LEU A N     1 
ATOM   1634  C  CA    . LEU A 1 203 ? 178.771 175.671 150.026 1.00 56.82  ?  222 LEU A CA    1 
ATOM   1635  C  C     . LEU A 1 203 ? 179.249 174.235 149.864 1.00 59.13  ?  222 LEU A C     1 
ATOM   1636  O  O     . LEU A 1 203 ? 180.317 173.853 150.350 1.00 56.67  ?  222 LEU A O     1 
ATOM   1637  C  CB    . LEU A 1 203 ? 179.104 176.491 148.771 1.00 57.07  ?  222 LEU A CB    1 
ATOM   1638  C  CG    . LEU A 1 203 ? 178.449 177.873 148.680 1.00 57.28  ?  222 LEU A CG    1 
ATOM   1639  C  CD1   . LEU A 1 203 ? 178.371 178.334 147.236 1.00 53.02  ?  222 LEU A CD1   1 
ATOM   1640  C  CD2   . LEU A 1 203 ? 177.067 177.880 149.317 1.00 59.25  ?  222 LEU A CD2   1 
ATOM   1641  N  N     . LEU A 1 204 ? 178.440 173.439 149.174 1.00 70.74  ?  223 LEU A N     1 
ATOM   1642  C  CA    . LEU A 1 204 ? 178.695 172.016 149.005 1.00 71.43  ?  223 LEU A CA    1 
ATOM   1643  C  C     . LEU A 1 204 ? 179.229 171.759 147.604 1.00 71.93  ?  223 LEU A C     1 
ATOM   1644  O  O     . LEU A 1 204 ? 178.647 172.220 146.617 1.00 72.93  ?  223 LEU A O     1 
ATOM   1645  C  CB    . LEU A 1 204 ? 177.422 171.200 149.243 1.00 70.47  ?  223 LEU A CB    1 
ATOM   1646  C  CG    . LEU A 1 204 ? 176.879 171.151 150.672 1.00 72.23  ?  223 LEU A CG    1 
ATOM   1647  C  CD1   . LEU A 1 204 ? 175.865 170.025 150.817 1.00 72.24  ?  223 LEU A CD1   1 
ATOM   1648  C  CD2   . LEU A 1 204 ? 178.005 170.998 151.685 1.00 68.84  ?  223 LEU A CD2   1 
ATOM   1649  N  N     . THR A 1 205 ? 180.337 171.026 147.523 1.00 64.41  ?  224 THR A N     1 
ATOM   1650  C  CA    . THR A 1 205 ? 180.888 170.643 146.237 1.00 60.14  ?  224 THR A CA    1 
ATOM   1651  C  C     . THR A 1 205 ? 180.056 169.520 145.623 1.00 64.25  ?  224 THR A C     1 
ATOM   1652  O  O     . THR A 1 205 ? 179.170 168.942 146.261 1.00 66.41  ?  224 THR A O     1 
ATOM   1653  C  CB    . THR A 1 205 ? 182.344 170.201 146.382 1.00 65.05  ?  224 THR A CB    1 
ATOM   1654  O  OG1   . THR A 1 205 ? 182.401 168.976 147.123 1.00 69.82  ?  224 THR A OG1   1 
ATOM   1655  C  CG2   . THR A 1 205 ? 183.153 171.263 147.110 1.00 64.83  ?  224 THR A CG2   1 
ATOM   1656  N  N     . ARG A 1 206 ? 180.345 169.218 144.356 1.00 65.97  ?  225 ARG A N     1 
ATOM   1657  C  CA    . ARG A 1 206 ? 179.656 168.118 143.690 1.00 64.98  ?  225 ARG A CA    1 
ATOM   1658  C  C     . ARG A 1 206 ? 179.936 166.794 144.390 1.00 67.62  ?  225 ARG A C     1 
ATOM   1659  O  O     . ARG A 1 206 ? 179.040 165.952 144.523 1.00 70.75  ?  225 ARG A O     1 
ATOM   1660  C  CB    . ARG A 1 206 ? 180.066 168.055 142.220 1.00 63.47  ?  225 ARG A CB    1 
ATOM   1661  C  CG    . ARG A 1 206 ? 179.098 167.279 141.342 1.00 65.23  ?  225 ARG A CG    1 
ATOM   1662  C  CD    . ARG A 1 206 ? 179.579 167.233 139.903 1.00 67.56  ?  225 ARG A CD    1 
ATOM   1663  N  NE    . ARG A 1 206 ? 180.855 166.540 139.772 1.00 69.14  ?  225 ARG A NE    1 
ATOM   1664  C  CZ    . ARG A 1 206 ? 181.476 166.329 138.620 1.00 70.47  ?  225 ARG A CZ    1 
ATOM   1665  N  NH1   . ARG A 1 206 ? 180.968 166.749 137.473 1.00 71.56  1  225 ARG A NH1   1 
ATOM   1666  N  NH2   . ARG A 1 206 ? 182.639 165.683 138.618 1.00 67.79  ?  225 ARG A NH2   1 
ATOM   1667  N  N     . THR A 1 207 ? 181.174 166.593 144.846 1.00 66.38  ?  226 THR A N     1 
ATOM   1668  C  CA    . THR A 1 207 ? 181.488 165.393 145.614 1.00 68.07  ?  226 THR A CA    1 
ATOM   1669  C  C     . THR A 1 207 ? 180.923 165.476 147.029 1.00 69.94  ?  226 THR A C     1 
ATOM   1670  O  O     . THR A 1 207 ? 180.400 164.485 147.551 1.00 70.58  ?  226 THR A O     1 
ATOM   1671  C  CB    . THR A 1 207 ? 182.999 165.168 145.648 1.00 69.53  ?  226 THR A CB    1 
ATOM   1672  O  OG1   . THR A 1 207 ? 183.635 166.286 146.277 1.00 71.67  ?  226 THR A OG1   1 
ATOM   1673  C  CG2   . THR A 1 207 ? 183.544 165.011 144.236 1.00 68.23  ?  226 THR A CG2   1 
ATOM   1674  N  N     . GLY A 1 208 ? 181.018 166.644 147.665 1.00 71.97  ?  227 GLY A N     1 
ATOM   1675  C  CA    . GLY A 1 208 ? 180.382 166.834 148.955 1.00 68.37  ?  227 GLY A CA    1 
ATOM   1676  C  C     . GLY A 1 208 ? 181.240 167.422 150.059 1.00 68.81  ?  227 GLY A C     1 
ATOM   1677  O  O     . GLY A 1 208 ? 180.846 167.385 151.228 1.00 70.03  ?  227 GLY A O     1 
ATOM   1678  N  N     . GLU A 1 209 ? 182.407 167.964 149.719 1.00 73.03  ?  228 GLU A N     1 
ATOM   1679  C  CA    . GLU A 1 209 ? 183.256 168.569 150.736 1.00 75.03  ?  228 GLU A CA    1 
ATOM   1680  C  C     . GLU A 1 209 ? 182.664 169.888 151.228 1.00 74.42  ?  228 GLU A C     1 
ATOM   1681  O  O     . GLU A 1 209 ? 181.861 170.537 150.552 1.00 73.96  ?  228 GLU A O     1 
ATOM   1682  C  CB    . GLU A 1 209 ? 184.670 168.804 150.205 1.00 74.71  ?  228 GLU A CB    1 
ATOM   1683  C  CG    . GLU A 1 209 ? 185.453 167.536 149.911 1.00 73.12  ?  228 GLU A CG    1 
ATOM   1684  C  CD    . GLU A 1 209 ? 186.817 167.816 149.321 1.00 75.61  ?  228 GLU A CD    1 
ATOM   1685  O  OE1   . GLU A 1 209 ? 187.078 168.983 148.965 1.00 76.78  ?  228 GLU A OE1   1 
ATOM   1686  O  OE2   . GLU A 1 209 ? 187.626 166.871 149.214 1.00 74.46  -1 228 GLU A OE2   1 
ATOM   1687  N  N     . LYS A 1 210 ? 183.079 170.282 152.432 1.00 65.13  ?  229 LYS A N     1 
ATOM   1688  C  CA    . LYS A 1 210 ? 182.641 171.525 153.058 1.00 67.72  ?  229 LYS A CA    1 
ATOM   1689  C  C     . LYS A 1 210 ? 183.720 172.579 152.841 1.00 68.44  ?  229 LYS A C     1 
ATOM   1690  O  O     . LYS A 1 210 ? 184.814 172.480 153.406 1.00 67.83  ?  229 LYS A O     1 
ATOM   1691  C  CB    . LYS A 1 210 ? 182.377 171.318 154.547 1.00 68.68  ?  229 LYS A CB    1 
ATOM   1692  C  CG    . LYS A 1 210 ? 181.102 170.560 154.864 1.00 68.97  ?  229 LYS A CG    1 
ATOM   1693  C  CD    . LYS A 1 210 ? 180.989 170.292 156.356 1.00 67.97  ?  229 LYS A CD    1 
ATOM   1694  C  CE    . LYS A 1 210 ? 179.766 169.452 156.681 1.00 67.97  ?  229 LYS A CE    1 
ATOM   1695  N  NZ    . LYS A 1 210 ? 179.714 169.102 158.127 1.00 67.78  1  229 LYS A NZ    1 
ATOM   1696  N  N     . ILE A 1 211 ? 183.414 173.587 152.028 1.00 56.48  ?  230 ILE A N     1 
ATOM   1697  C  CA    . ILE A 1 211 ? 184.350 174.660 151.715 1.00 53.33  ?  230 ILE A CA    1 
ATOM   1698  C  C     . ILE A 1 211 ? 183.724 175.989 152.111 1.00 49.60  ?  230 ILE A C     1 
ATOM   1699  O  O     . ILE A 1 211 ? 182.615 176.315 151.672 1.00 56.70  ?  230 ILE A O     1 
ATOM   1700  C  CB    . ILE A 1 211 ? 184.738 174.664 150.226 1.00 54.01  ?  230 ILE A CB    1 
ATOM   1701  C  CG1   . ILE A 1 211 ? 185.548 173.413 149.881 1.00 57.38  ?  230 ILE A CG1   1 
ATOM   1702  C  CG2   . ILE A 1 211 ? 185.524 175.918 149.887 1.00 53.63  ?  230 ILE A CG2   1 
ATOM   1703  C  CD1   . ILE A 1 211 ? 185.911 173.310 148.418 1.00 56.68  ?  230 ILE A CD1   1 
ATOM   1704  N  N     . TRP A 1 212 ? 184.438 176.754 152.935 1.00 32.84  ?  231 TRP A N     1 
ATOM   1705  C  CA    . TRP A 1 212 ? 184.060 178.123 153.256 1.00 36.37  ?  231 TRP A CA    1 
ATOM   1706  C  C     . TRP A 1 212 ? 184.515 179.046 152.134 1.00 43.26  ?  231 TRP A C     1 
ATOM   1707  O  O     . TRP A 1 212 ? 185.687 179.028 151.745 1.00 51.77  ?  231 TRP A O     1 
ATOM   1708  C  CB    . TRP A 1 212 ? 184.684 178.562 154.581 1.00 42.33  ?  231 TRP A CB    1 
ATOM   1709  C  CG    . TRP A 1 212 ? 183.936 178.135 155.808 1.00 48.85  ?  231 TRP A CG    1 
ATOM   1710  C  CD1   . TRP A 1 212 ? 184.231 177.084 156.625 1.00 46.69  ?  231 TRP A CD1   1 
ATOM   1711  C  CD2   . TRP A 1 212 ? 182.794 178.781 156.384 1.00 47.72  ?  231 TRP A CD2   1 
ATOM   1712  N  NE1   . TRP A 1 212 ? 183.331 177.021 157.661 1.00 48.25  ?  231 TRP A NE1   1 
ATOM   1713  C  CE2   . TRP A 1 212 ? 182.440 178.054 157.538 1.00 49.32  ?  231 TRP A CE2   1 
ATOM   1714  C  CE3   . TRP A 1 212 ? 182.031 179.899 156.031 1.00 41.34  ?  231 TRP A CE3   1 
ATOM   1715  C  CZ2   . TRP A 1 212 ? 181.356 178.407 158.340 1.00 50.38  ?  231 TRP A CZ2   1 
ATOM   1716  C  CZ3   . TRP A 1 212 ? 180.955 180.247 156.828 1.00 42.49  ?  231 TRP A CZ3   1 
ATOM   1717  C  CH2   . TRP A 1 212 ? 180.627 179.503 157.968 1.00 48.66  ?  231 TRP A CH2   1 
ATOM   1718  N  N     . ILE A 1 213 ? 183.587 179.846 151.611 1.00 20.91  ?  232 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 183.876 180.753 150.510 1.00 9.03   ?  232 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 183.431 182.158 150.888 1.00 28.97  ?  232 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 182.585 182.357 151.762 1.00 44.29  ?  232 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 183.195 180.320 149.194 1.00 15.20  ?  232 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 181.698 180.618 149.245 1.00 33.89  ?  232 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 183.437 178.842 148.924 1.00 34.16  ?  232 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 181.044 180.640 147.888 1.00 43.92  ?  232 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 184.027 183.140 150.214 1.00 38.27  ?  233 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 183.653 184.544 150.345 1.00 26.11  ?  233 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 183.079 184.996 149.010 1.00 23.09  ?  233 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 183.800 185.051 148.009 1.00 39.39  ?  233 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 184.853 185.400 150.742 1.00 21.97  ?  233 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 184.631 186.896 150.610 1.00 30.18  ?  233 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 185.937 187.654 150.784 1.00 37.33  ?  233 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 185.713 189.154 150.708 1.00 37.00  ?  233 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 184.883 189.632 151.845 1.00 33.96  1  233 LYS A NZ    1 
ATOM   1735  N  N     . ALA A 1 215 ? 181.789 185.308 148.994 1.00 17.35  ?  234 ALA A N     1 
ATOM   1736  C  CA    . ALA A 1 215 ? 181.104 185.715 147.778 1.00 15.15  ?  234 ALA A CA    1 
ATOM   1737  C  C     . ALA A 1 215 ? 180.854 187.215 147.794 1.00 18.75  ?  234 ALA A C     1 
ATOM   1738  O  O     . ALA A 1 215 ? 180.279 187.750 148.745 1.00 38.99  ?  234 ALA A O     1 
ATOM   1739  C  CB    . ALA A 1 215 ? 179.779 184.969 147.623 1.00 27.32  ?  234 ALA A CB    1 
ATOM   1740  N  N     . SER A 1 216 ? 181.268 187.886 146.723 1.00 13.53  ?  235 SER A N     1 
ATOM   1741  C  CA    . SER A 1 216 ? 181.106 189.329 146.597 1.00 28.70  ?  235 SER A CA    1 
ATOM   1742  C  C     . SER A 1 216 ? 180.270 189.614 145.362 1.00 16.24  ?  235 SER A C     1 
ATOM   1743  O  O     . SER A 1 216 ? 180.682 189.287 144.245 1.00 21.80  ?  235 SER A O     1 
ATOM   1744  C  CB    . SER A 1 216 ? 182.462 190.035 146.502 1.00 38.98  ?  235 SER A CB    1 
ATOM   1745  O  OG    . SER A 1 216 ? 182.989 189.956 145.189 1.00 41.14  ?  235 SER A OG    1 
ATOM   1746  N  N     . ILE A 1 217 ? 179.103 190.219 145.563 1.00 12.30  ?  236 ILE A N     1 
ATOM   1747  C  CA    . ILE A 1 217 ? 178.195 190.576 144.481 1.00 12.92  ?  236 ILE A CA    1 
ATOM   1748  C  C     . ILE A 1 217 ? 178.300 192.076 144.243 1.00 16.06  ?  236 ILE A C     1 
ATOM   1749  O  O     . ILE A 1 217 ? 178.327 192.868 145.195 1.00 38.95  ?  236 ILE A O     1 
ATOM   1750  C  CB    . ILE A 1 217 ? 176.746 190.150 144.783 1.00 23.75  ?  236 ILE A CB    1 
ATOM   1751  C  CG1   . ILE A 1 217 ? 175.857 190.371 143.559 1.00 24.72  ?  236 ILE A CG1   1 
ATOM   1752  C  CG2   . ILE A 1 217 ? 176.189 190.873 146.006 1.00 26.99  ?  236 ILE A CG2   1 
ATOM   1753  C  CD1   . ILE A 1 217 ? 174.535 189.647 143.629 1.00 27.58  ?  236 ILE A CD1   1 
ATOM   1754  N  N     . SER A 1 218 ? 178.407 192.463 142.972 1.00 20.75  ?  237 SER A N     1 
ATOM   1755  C  CA    . SER A 1 218 ? 178.439 193.873 142.621 1.00 26.82  ?  237 SER A CA    1 
ATOM   1756  C  C     . SER A 1 218 ? 177.631 194.074 141.344 1.00 25.65  ?  237 SER A C     1 
ATOM   1757  O  O     . SER A 1 218 ? 177.795 193.303 140.377 1.00 38.95  ?  237 SER A O     1 
ATOM   1758  C  CB    . SER A 1 218 ? 179.867 194.395 142.442 1.00 28.19  ?  237 SER A CB    1 
ATOM   1759  O  OG    . SER A 1 218 ? 180.486 193.843 141.298 1.00 30.20  ?  237 SER A OG    1 
ATOM   1760  N  N     . PRO A 1 219 ? 176.747 195.067 141.312 1.00 17.13  ?  238 PRO A N     1 
ATOM   1761  C  CA    . PRO A 1 219 ? 175.943 195.307 140.113 1.00 22.98  ?  238 PRO A CA    1 
ATOM   1762  C  C     . PRO A 1 219 ? 176.683 196.145 139.085 1.00 21.81  ?  238 PRO A C     1 
ATOM   1763  O  O     . PRO A 1 219 ? 177.505 197.005 139.411 1.00 27.17  ?  238 PRO A O     1 
ATOM   1764  C  CB    . PRO A 1 219 ? 174.724 196.061 140.656 1.00 24.46  ?  238 PRO A CB    1 
ATOM   1765  C  CG    . PRO A 1 219 ? 175.250 196.791 141.837 1.00 26.55  ?  238 PRO A CG    1 
ATOM   1766  C  CD    . PRO A 1 219 ? 176.333 195.927 142.435 1.00 28.37  ?  238 PRO A CD    1 
ATOM   1767  N  N     . VAL A 1 220 ? 176.372 195.877 137.821 1.00 28.82  ?  239 VAL A N     1 
ATOM   1768  C  CA    . VAL A 1 220 ? 176.854 196.657 136.691 1.00 30.47  ?  239 VAL A CA    1 
ATOM   1769  C  C     . VAL A 1 220 ? 175.632 197.219 135.983 1.00 38.52  ?  239 VAL A C     1 
ATOM   1770  O  O     . VAL A 1 220 ? 174.748 196.459 135.562 1.00 40.48  ?  239 VAL A O     1 
ATOM   1771  C  CB    . VAL A 1 220 ? 177.711 195.816 135.735 1.00 32.57  ?  239 VAL A CB    1 
ATOM   1772  C  CG1   . VAL A 1 220 ? 178.032 196.607 134.475 1.00 35.54  ?  239 VAL A CG1   1 
ATOM   1773  C  CG2   . VAL A 1 220 ? 178.983 195.375 136.432 1.00 36.45  ?  239 VAL A CG2   1 
ATOM   1774  N  N     . TYR A 1 221 ? 175.589 198.543 135.851 1.00 42.40  ?  240 TYR A N     1 
ATOM   1775  C  CA    . TYR A 1 221 ? 174.417 199.265 135.381 1.00 39.18  ?  240 TYR A CA    1 
ATOM   1776  C  C     . TYR A 1 221 ? 174.596 199.691 133.931 1.00 42.31  ?  240 TYR A C     1 
ATOM   1777  O  O     . TYR A 1 221 ? 175.713 199.965 133.484 1.00 42.03  ?  240 TYR A O     1 
ATOM   1778  C  CB    . TYR A 1 221 ? 174.158 200.498 136.248 1.00 38.40  ?  240 TYR A CB    1 
ATOM   1779  C  CG    . TYR A 1 221 ? 173.666 200.183 137.642 1.00 40.22  ?  240 TYR A CG    1 
ATOM   1780  C  CD1   . TYR A 1 221 ? 172.315 200.004 137.902 1.00 42.10  ?  240 TYR A CD1   1 
ATOM   1781  C  CD2   . TYR A 1 221 ? 174.557 200.071 138.700 1.00 38.81  ?  240 TYR A CD2   1 
ATOM   1782  C  CE1   . TYR A 1 221 ? 171.866 199.718 139.176 1.00 43.92  ?  240 TYR A CE1   1 
ATOM   1783  C  CE2   . TYR A 1 221 ? 174.117 199.785 139.976 1.00 40.10  ?  240 TYR A CE2   1 
ATOM   1784  C  CZ    . TYR A 1 221 ? 172.772 199.610 140.209 1.00 42.91  ?  240 TYR A CZ    1 
ATOM   1785  O  OH    . TYR A 1 221 ? 172.331 199.325 141.480 1.00 42.58  ?  240 TYR A OH    1 
ATOM   1786  N  N     . ASP A 1 222 ? 173.486 199.747 133.201 1.00 59.75  ?  241 ASP A N     1 
ATOM   1787  C  CA    . ASP A 1 222 ? 173.515 200.156 131.807 1.00 66.16  ?  241 ASP A CA    1 
ATOM   1788  C  C     . ASP A 1 222 ? 173.658 201.675 131.705 1.00 65.02  ?  241 ASP A C     1 
ATOM   1789  O  O     . ASP A 1 222 ? 173.833 202.385 132.700 1.00 64.43  ?  241 ASP A O     1 
ATOM   1790  C  CB    . ASP A 1 222 ? 172.258 199.671 131.088 1.00 62.48  ?  241 ASP A CB    1 
ATOM   1791  C  CG    . ASP A 1 222 ? 172.498 199.394 129.618 1.00 64.09  ?  241 ASP A CG    1 
ATOM   1792  O  OD1   . ASP A 1 222 ? 173.676 199.369 129.202 1.00 61.80  ?  241 ASP A OD1   1 
ATOM   1793  O  OD2   . ASP A 1 222 ? 171.511 199.201 128.877 1.00 65.28  -1 241 ASP A OD2   1 
ATOM   1794  N  N     . VAL A 1 223 ? 173.588 202.177 130.469 1.00 72.81  ?  242 VAL A N     1 
ATOM   1795  C  CA    . VAL A 1 223 ? 173.675 203.616 130.238 1.00 72.15  ?  242 VAL A CA    1 
ATOM   1796  C  C     . VAL A 1 223 ? 172.481 204.334 130.853 1.00 72.85  ?  242 VAL A C     1 
ATOM   1797  O  O     . VAL A 1 223 ? 172.614 205.449 131.373 1.00 76.56  ?  242 VAL A O     1 
ATOM   1798  C  CB    . VAL A 1 223 ? 173.795 203.902 128.728 1.00 74.13  ?  242 VAL A CB    1 
ATOM   1799  C  CG1   . VAL A 1 223 ? 173.843 205.399 128.465 1.00 74.23  ?  242 VAL A CG1   1 
ATOM   1800  C  CG2   . VAL A 1 223 ? 175.025 203.214 128.154 1.00 73.24  ?  242 VAL A CG2   1 
ATOM   1801  N  N     . LEU A 1 224 ? 171.305 203.709 130.820 1.00 73.88  ?  243 LEU A N     1 
ATOM   1802  C  CA    . LEU A 1 224 ? 170.086 204.281 131.377 1.00 75.93  ?  243 LEU A CA    1 
ATOM   1803  C  C     . LEU A 1 224 ? 170.004 204.146 132.896 1.00 76.75  ?  243 LEU A C     1 
ATOM   1804  O  O     . LEU A 1 224 ? 168.909 204.293 133.454 1.00 77.86  ?  243 LEU A O     1 
ATOM   1805  C  CB    . LEU A 1 224 ? 168.855 203.636 130.732 1.00 76.75  ?  243 LEU A CB    1 
ATOM   1806  C  CG    . LEU A 1 224 ? 168.357 204.170 129.383 1.00 77.89  ?  243 LEU A CG    1 
ATOM   1807  C  CD1   . LEU A 1 224 ? 167.895 205.617 129.512 1.00 76.87  ?  243 LEU A CD1   1 
ATOM   1808  C  CD2   . LEU A 1 224 ? 169.399 204.027 128.278 1.00 76.59  ?  243 LEU A CD2   1 
ATOM   1809  N  N     . ALA A 1 225 ? 171.128 203.867 133.562 1.00 68.54  ?  244 ALA A N     1 
ATOM   1810  C  CA    . ALA A 1 225 ? 171.173 203.684 135.014 1.00 66.40  ?  244 ALA A CA    1 
ATOM   1811  C  C     . ALA A 1 225 ? 170.214 202.585 135.465 1.00 70.01  ?  244 ALA A C     1 
ATOM   1812  O  O     . ALA A 1 225 ? 169.502 202.724 136.462 1.00 70.76  ?  244 ALA A O     1 
ATOM   1813  C  CB    . ALA A 1 225 ? 170.888 204.996 135.750 1.00 66.21  ?  244 ALA A CB    1 
ATOM   1814  N  N     . HIS A 1 226 ? 170.198 201.482 134.724 1.00 60.59  ?  245 HIS A N     1 
ATOM   1815  C  CA    . HIS A 1 226 ? 169.374 200.327 135.040 1.00 59.42  ?  245 HIS A CA    1 
ATOM   1816  C  C     . HIS A 1 226 ? 170.261 199.106 135.238 1.00 60.18  ?  245 HIS A C     1 
ATOM   1817  O  O     . HIS A 1 226 ? 171.307 198.970 134.596 1.00 59.37  ?  245 HIS A O     1 
ATOM   1818  C  CB    . HIS A 1 226 ? 168.345 200.052 133.937 1.00 58.90  ?  245 HIS A CB    1 
ATOM   1819  C  CG    . HIS A 1 226 ? 167.077 200.832 134.089 1.00 59.44  ?  245 HIS A CG    1 
ATOM   1820  N  ND1   . HIS A 1 226 ? 166.319 200.802 135.240 1.00 61.09  ?  245 HIS A ND1   1 
ATOM   1821  C  CD2   . HIS A 1 226 ? 166.433 201.663 133.236 1.00 59.82  ?  245 HIS A CD2   1 
ATOM   1822  C  CE1   . HIS A 1 226 ? 165.263 201.581 135.090 1.00 61.72  ?  245 HIS A CE1   1 
ATOM   1823  N  NE2   . HIS A 1 226 ? 165.308 202.115 133.882 1.00 63.19  ?  245 HIS A NE2   1 
ATOM   1824  N  N     . LEU A 1 227 ? 169.836 198.222 136.141 1.00 45.58  ?  246 LEU A N     1 
ATOM   1825  C  CA    . LEU A 1 227 ? 170.587 197.009 136.441 1.00 39.30  ?  246 LEU A CA    1 
ATOM   1826  C  C     . LEU A 1 227 ? 170.773 196.158 135.192 1.00 45.64  ?  246 LEU A C     1 
ATOM   1827  O  O     . LEU A 1 227 ? 169.807 195.595 134.667 1.00 42.56  ?  246 LEU A O     1 
ATOM   1828  C  CB    . LEU A 1 227 ? 169.878 196.201 137.530 1.00 39.39  ?  246 LEU A CB    1 
ATOM   1829  C  CG    . LEU A 1 227 ? 170.540 194.885 137.942 1.00 43.92  ?  246 LEU A CG    1 
ATOM   1830  C  CD1   . LEU A 1 227 ? 171.841 195.146 138.680 1.00 37.48  ?  246 LEU A CD1   1 
ATOM   1831  C  CD2   . LEU A 1 227 ? 169.597 194.043 138.787 1.00 44.40  ?  246 LEU A CD2   1 
ATOM   1832  N  N     . GLN A 1 228 ? 172.011 196.058 134.711 1.00 43.49  ?  247 GLN A N     1 
ATOM   1833  C  CA    . GLN A 1 228 ? 172.333 195.239 133.549 1.00 37.75  ?  247 GLN A CA    1 
ATOM   1834  C  C     . GLN A 1 228 ? 172.811 193.847 133.939 1.00 45.10  ?  247 GLN A C     1 
ATOM   1835  O  O     . GLN A 1 228 ? 172.321 192.850 133.402 1.00 49.56  ?  247 GLN A O     1 
ATOM   1836  C  CB    . GLN A 1 228 ? 173.399 195.928 132.688 1.00 35.02  ?  247 GLN A CB    1 
ATOM   1837  C  CG    . GLN A 1 228 ? 173.355 195.535 131.221 1.00 44.36  ?  247 GLN A CG    1 
ATOM   1838  C  CD    . GLN A 1 228 ? 174.157 196.474 130.343 1.00 46.30  ?  247 GLN A CD    1 
ATOM   1839  O  OE1   . GLN A 1 228 ? 174.930 197.295 130.836 1.00 45.96  ?  247 GLN A OE1   1 
ATOM   1840  N  NE2   . GLN A 1 228 ? 173.972 196.360 129.033 1.00 42.44  ?  247 GLN A NE2   1 
ATOM   1841  N  N     . ASN A 1 229 ? 173.762 193.759 134.866 1.00 37.45  ?  248 ASN A N     1 
ATOM   1842  C  CA    . ASN A 1 229 ? 174.273 192.465 135.297 1.00 26.14  ?  248 ASN A CA    1 
ATOM   1843  C  C     . ASN A 1 229 ? 174.658 192.541 136.766 1.00 24.57  ?  248 ASN A C     1 
ATOM   1844  O  O     . ASN A 1 229 ? 174.679 193.614 137.371 1.00 34.82  ?  248 ASN A O     1 
ATOM   1845  C  CB    . ASN A 1 229 ? 175.470 192.025 134.447 1.00 30.67  ?  248 ASN A CB    1 
ATOM   1846  C  CG    . ASN A 1 229 ? 175.070 191.606 133.046 1.00 34.92  ?  248 ASN A CG    1 
ATOM   1847  O  OD1   . ASN A 1 229 ? 175.393 192.280 132.068 1.00 44.16  ?  248 ASN A OD1   1 
ATOM   1848  N  ND2   . ASN A 1 229 ? 174.364 190.487 132.940 1.00 32.38  ?  248 ASN A ND2   1 
ATOM   1849  N  N     . LEU A 1 230 ? 174.966 191.380 137.339 1.00 17.41  ?  249 LEU A N     1 
ATOM   1850  C  CA    . LEU A 1 230 ? 175.504 191.302 138.694 1.00 10.97  ?  249 LEU A CA    1 
ATOM   1851  C  C     . LEU A 1 230 ? 176.623 190.276 138.700 1.00 21.98  ?  249 LEU A C     1 
ATOM   1852  O  O     . LEU A 1 230 ? 176.384 189.098 138.422 1.00 43.19  ?  249 LEU A O     1 
ATOM   1853  C  CB    . LEU A 1 230 ? 174.425 190.926 139.715 1.00 20.41  ?  249 LEU A CB    1 
ATOM   1854  C  CG    . LEU A 1 230 ? 173.163 191.788 139.753 1.00 33.70  ?  249 LEU A CG    1 
ATOM   1855  C  CD1   . LEU A 1 230 ? 172.017 191.106 139.023 1.00 35.25  ?  249 LEU A CD1   1 
ATOM   1856  C  CD2   . LEU A 1 230 ? 172.782 192.103 141.189 1.00 29.78  ?  249 LEU A CD2   1 
ATOM   1857  N  N     . VAL A 1 231 ? 177.836 190.711 139.002 1.00 4.45   ?  250 VAL A N     1 
ATOM   1858  C  CA    . VAL A 1 231 ? 178.987 189.815 138.993 1.00 2.81   ?  250 VAL A CA    1 
ATOM   1859  C  C     . VAL A 1 231 ? 179.274 189.353 140.413 1.00 17.57  ?  250 VAL A C     1 
ATOM   1860  O  O     . VAL A 1 231 ? 179.261 190.150 141.364 1.00 42.54  ?  250 VAL A O     1 
ATOM   1861  C  CB    . VAL A 1 231 ? 180.219 190.478 138.346 1.00 15.04  ?  250 VAL A CB    1 
ATOM   1862  C  CG1   . VAL A 1 231 ? 179.925 190.811 136.902 1.00 26.21  ?  250 VAL A CG1   1 
ATOM   1863  C  CG2   . VAL A 1 231 ? 180.611 191.730 139.085 1.00 28.27  ?  250 VAL A CG2   1 
ATOM   1864  N  N     . MET A 1 232 ? 179.502 188.050 140.557 1.00 15.54  ?  251 MET A N     1 
ATOM   1865  C  CA    . MET A 1 232 ? 179.835 187.424 141.827 1.00 19.49  ?  251 MET A CA    1 
ATOM   1866  C  C     . MET A 1 232 ? 181.251 186.875 141.750 1.00 16.15  ?  251 MET A C     1 
ATOM   1867  O  O     . MET A 1 232 ? 181.568 186.077 140.862 1.00 32.61  ?  251 MET A O     1 
ATOM   1868  C  CB    . MET A 1 232 ? 178.854 186.299 142.156 1.00 21.40  ?  251 MET A CB    1 
ATOM   1869  C  CG    . MET A 1 232 ? 177.415 186.748 142.315 1.00 23.92  ?  251 MET A CG    1 
ATOM   1870  S  SD    . MET A 1 232 ? 176.491 185.669 143.423 1.00 49.86  ?  251 MET A SD    1 
ATOM   1871  C  CE    . MET A 1 232 ? 177.481 185.786 144.906 1.00 35.31  ?  251 MET A CE    1 
ATOM   1872  N  N     . THR A 1 233 ? 182.093 187.296 142.683 1.00 21.67  ?  252 THR A N     1 
ATOM   1873  C  CA    . THR A 1 233 ? 183.465 186.810 142.784 1.00 16.83  ?  252 THR A CA    1 
ATOM   1874  C  C     . THR A 1 233 ? 183.542 185.943 144.035 1.00 27.19  ?  252 THR A C     1 
ATOM   1875  O  O     . THR A 1 233 ? 183.206 186.397 145.133 1.00 44.76  ?  252 THR A O     1 
ATOM   1876  C  CB    . THR A 1 233 ? 184.461 187.964 142.839 1.00 34.60  ?  252 THR A CB    1 
ATOM   1877  O  OG1   . THR A 1 233 ? 184.452 188.542 144.151 1.00 43.73  ?  252 THR A OG1   1 
ATOM   1878  C  CG2   . THR A 1 233 ? 184.086 189.031 141.821 1.00 33.69  ?  252 THR A CG2   1 
ATOM   1879  N  N     . PHE A 1 234 ? 183.965 184.694 143.864 1.00 28.26  ?  253 PHE A N     1 
ATOM   1880  C  CA    . PHE A 1 234 ? 184.138 183.796 144.993 1.00 24.44  ?  253 PHE A CA    1 
ATOM   1881  C  C     . PHE A 1 234 ? 185.616 183.617 145.296 1.00 25.37  ?  253 PHE A C     1 
ATOM   1882  O  O     . PHE A 1 234 ? 186.418 183.315 144.409 1.00 39.98  ?  253 PHE A O     1 
ATOM   1883  C  CB    . PHE A 1 234 ? 183.503 182.434 144.715 1.00 29.41  ?  253 PHE A CB    1 
ATOM   1884  C  CG    . PHE A 1 234 ? 182.082 182.509 144.248 1.00 21.88  ?  253 PHE A CG    1 
ATOM   1885  C  CD1   . PHE A 1 234 ? 181.071 182.867 145.123 1.00 26.93  ?  253 PHE A CD1   1 
ATOM   1886  C  CD2   . PHE A 1 234 ? 181.752 182.202 142.941 1.00 27.98  ?  253 PHE A CD2   1 
ATOM   1887  C  CE1   . PHE A 1 234 ? 179.758 182.928 144.700 1.00 34.97  ?  253 PHE A CE1   1 
ATOM   1888  C  CE2   . PHE A 1 234 ? 180.443 182.261 142.513 1.00 30.61  ?  253 PHE A CE2   1 
ATOM   1889  C  CZ    . PHE A 1 234 ? 179.444 182.625 143.394 1.00 38.00  ?  253 PHE A CZ    1 
ATOM   1890  N  N     . SER A 1 235 ? 185.973 183.817 146.558 1.00 21.97  ?  254 SER A N     1 
ATOM   1891  C  CA    . SER A 1 235 ? 187.329 183.602 147.033 1.00 20.51  ?  254 SER A CA    1 
ATOM   1892  C  C     . SER A 1 235 ? 187.321 182.403 147.966 1.00 32.44  ?  254 SER A C     1 
ATOM   1893  O  O     . SER A 1 235 ? 186.519 182.352 148.906 1.00 44.11  ?  254 SER A O     1 
ATOM   1894  C  CB    . SER A 1 235 ? 187.871 184.843 147.751 1.00 30.64  ?  254 SER A CB    1 
ATOM   1895  O  OG    . SER A 1 235 ? 189.098 184.564 148.402 1.00 40.09  ?  254 SER A OG    1 
ATOM   1896  N  N     . ASP A 1 236 ? 188.185 181.431 147.688 1.00 41.12  ?  255 ASP A N     1 
ATOM   1897  C  CA    . ASP A 1 236 ? 188.353 180.292 148.584 1.00 41.21  ?  255 ASP A CA    1 
ATOM   1898  C  C     . ASP A 1 236 ? 189.043 180.775 149.850 1.00 33.16  ?  255 ASP A C     1 
ATOM   1899  O  O     . ASP A 1 236 ? 190.241 181.077 149.839 1.00 36.29  ?  255 ASP A O     1 
ATOM   1900  C  CB    . ASP A 1 236 ? 189.153 179.186 147.904 1.00 44.02  ?  255 ASP A CB    1 
ATOM   1901  C  CG    . ASP A 1 236 ? 188.967 177.835 148.573 1.00 52.47  ?  255 ASP A CG    1 
ATOM   1902  O  OD1   . ASP A 1 236 ? 188.505 177.800 149.733 1.00 52.37  ?  255 ASP A OD1   1 
ATOM   1903  O  OD2   . ASP A 1 236 ? 189.279 176.805 147.939 1.00 50.92  -1 255 ASP A OD2   1 
ATOM   1904  N  N     . ILE A 1 237 ? 188.293 180.842 150.945 1.00 23.33  ?  256 ILE A N     1 
ATOM   1905  C  CA    . ILE A 1 237 ? 188.774 181.494 152.155 1.00 29.51  ?  256 ILE A CA    1 
ATOM   1906  C  C     . ILE A 1 237 ? 188.894 180.494 153.295 1.00 42.68  ?  256 ILE A C     1 
ATOM   1907  O  O     . ILE A 1 237 ? 188.689 180.844 154.460 1.00 47.07  ?  256 ILE A O     1 
ATOM   1908  C  CB    . ILE A 1 237 ? 187.864 182.675 152.546 1.00 29.17  ?  256 ILE A CB    1 
ATOM   1909  C  CG1   . ILE A 1 237 ? 186.441 182.192 152.843 1.00 30.84  ?  256 ILE A CG1   1 
ATOM   1910  C  CG2   . ILE A 1 237 ? 187.879 183.739 151.462 1.00 35.57  ?  256 ILE A CG2   1 
ATOM   1911  C  CD1   . ILE A 1 237 ? 185.588 183.218 153.548 1.00 34.77  ?  256 ILE A CD1   1 
ATOM   1912  N  N     . THR A 1 238 ? 189.226 179.244 152.975 1.00 44.83  ?  257 THR A N     1 
ATOM   1913  C  CA    . THR A 1 238 ? 189.577 178.299 154.030 1.00 38.10  ?  257 THR A CA    1 
ATOM   1914  C  C     . THR A 1 238 ? 190.817 178.770 154.781 1.00 40.41  ?  257 THR A C     1 
ATOM   1915  O  O     . THR A 1 238 ? 190.803 178.903 156.011 1.00 47.66  ?  257 THR A O     1 
ATOM   1916  C  CB    . THR A 1 238 ? 189.800 176.907 153.438 1.00 42.71  ?  257 THR A CB    1 
ATOM   1917  O  OG1   . THR A 1 238 ? 188.543 176.353 153.026 1.00 42.61  ?  257 THR A OG1   1 
ATOM   1918  C  CG2   . THR A 1 238 ? 190.444 175.987 154.467 1.00 44.72  ?  257 THR A CG2   1 
ATOM   1919  N  N     . GLU A 1 239 ? 191.893 179.067 154.048 1.00 39.02  ?  258 GLU A N     1 
ATOM   1920  C  CA    . GLU A 1 239 ? 193.104 179.580 154.679 1.00 39.56  ?  258 GLU A CA    1 
ATOM   1921  C  C     . GLU A 1 239 ? 192.890 180.975 155.250 1.00 45.07  ?  258 GLU A C     1 
ATOM   1922  O  O     . GLU A 1 239 ? 193.466 181.314 156.292 1.00 49.28  ?  258 GLU A O     1 
ATOM   1923  C  CB    . GLU A 1 239 ? 194.254 179.587 153.673 1.00 46.10  ?  258 GLU A CB    1 
ATOM   1924  C  CG    . GLU A 1 239 ? 194.274 178.381 152.748 1.00 47.44  ?  258 GLU A CG    1 
ATOM   1925  C  CD    . GLU A 1 239 ? 194.715 177.113 153.450 1.00 53.27  ?  258 GLU A CD    1 
ATOM   1926  O  OE1   . GLU A 1 239 ? 195.371 177.214 154.508 1.00 53.38  ?  258 GLU A OE1   1 
ATOM   1927  O  OE2   . GLU A 1 239 ? 194.407 176.014 152.943 1.00 55.64  -1 258 GLU A OE2   1 
ATOM   1928  N  N     . GLU A 1 240 ? 192.078 181.796 154.581 1.00 41.05  ?  259 GLU A N     1 
ATOM   1929  C  CA    . GLU A 1 240 ? 191.767 183.121 155.107 1.00 35.92  ?  259 GLU A CA    1 
ATOM   1930  C  C     . GLU A 1 240 ? 191.062 183.020 156.453 1.00 36.42  ?  259 GLU A C     1 
ATOM   1931  O  O     . GLU A 1 240 ? 191.388 183.749 157.392 1.00 46.47  ?  259 GLU A O     1 
ATOM   1932  C  CB    . GLU A 1 240 ? 190.916 183.901 154.105 1.00 32.78  ?  259 GLU A CB    1 
ATOM   1933  C  CG    . GLU A 1 240 ? 191.721 184.709 153.096 1.00 46.63  ?  259 GLU A CG    1 
ATOM   1934  C  CD    . GLU A 1 240 ? 192.167 183.887 151.901 1.00 49.71  ?  259 GLU A CD    1 
ATOM   1935  O  OE1   . GLU A 1 240 ? 191.911 182.665 151.883 1.00 49.37  ?  259 GLU A OE1   1 
ATOM   1936  O  OE2   . GLU A 1 240 ? 192.774 184.468 150.977 1.00 45.17  -1 259 GLU A OE2   1 
ATOM   1937  N  N     . ARG A 1 241 ? 190.100 182.105 156.576 1.00 40.62  ?  260 ARG A N     1 
ATOM   1938  C  CA    . ARG A 1 241 ? 189.420 181.935 157.853 1.00 34.00  ?  260 ARG A CA    1 
ATOM   1939  C  C     . ARG A 1 241 ? 190.319 181.279 158.890 1.00 36.62  ?  260 ARG A C     1 
ATOM   1940  O  O     . ARG A 1 241 ? 190.164 181.539 160.085 1.00 47.30  ?  260 ARG A O     1 
ATOM   1941  C  CB    . ARG A 1 241 ? 188.136 181.125 157.684 1.00 37.61  ?  260 ARG A CB    1 
ATOM   1942  C  CG    . ARG A 1 241 ? 186.973 181.918 157.119 1.00 45.73  ?  260 ARG A CG    1 
ATOM   1943  C  CD    . ARG A 1 241 ? 185.795 181.009 156.851 1.00 45.11  ?  260 ARG A CD    1 
ATOM   1944  N  NE    . ARG A 1 241 ? 185.835 179.838 157.718 1.00 41.29  ?  260 ARG A NE    1 
ATOM   1945  C  CZ    . ARG A 1 241 ? 185.027 179.642 158.750 1.00 39.38  ?  260 ARG A CZ    1 
ATOM   1946  N  NH1   . ARG A 1 241 ? 184.095 180.524 159.075 1.00 35.24  1  260 ARG A NH1   1 
ATOM   1947  N  NH2   . ARG A 1 241 ? 185.161 178.538 159.479 1.00 40.64  ?  260 ARG A NH2   1 
ATOM   1948  N  N     . GLN A 1 242 ? 191.260 180.433 158.465 1.00 45.13  ?  261 GLN A N     1 
ATOM   1949  C  CA    . GLN A 1 242 ? 192.241 179.912 159.413 1.00 51.31  ?  261 GLN A CA    1 
ATOM   1950  C  C     . GLN A 1 242 ? 193.077 181.042 160.005 1.00 49.56  ?  261 GLN A C     1 
ATOM   1951  O  O     . GLN A 1 242 ? 193.262 181.124 161.226 1.00 44.64  ?  261 GLN A O     1 
ATOM   1952  C  CB    . GLN A 1 242 ? 193.138 178.874 158.734 1.00 46.77  ?  261 GLN A CB    1 
ATOM   1953  C  CG    . GLN A 1 242 ? 192.428 177.584 158.352 1.00 43.26  ?  261 GLN A CG    1 
ATOM   1954  C  CD    . GLN A 1 242 ? 192.645 176.478 159.363 1.00 51.92  ?  261 GLN A CD    1 
ATOM   1955  O  OE1   . GLN A 1 242 ? 193.661 176.446 160.057 1.00 58.86  ?  261 GLN A OE1   1 
ATOM   1956  N  NE2   . GLN A 1 242 ? 191.690 175.558 159.449 1.00 51.28  ?  261 GLN A NE2   1 
ATOM   1957  N  N     . ILE A 1 243 ? 193.574 181.941 159.150 1.00 45.92  ?  262 ILE A N     1 
ATOM   1958  C  CA    . ILE A 1 243 ? 194.365 183.061 159.654 1.00 35.15  ?  262 ILE A CA    1 
ATOM   1959  C  C     . ILE A 1 243 ? 193.491 184.032 160.442 1.00 32.32  ?  262 ILE A C     1 
ATOM   1960  O  O     . ILE A 1 243 ? 193.970 184.690 161.370 1.00 40.70  ?  262 ILE A O     1 
ATOM   1961  C  CB    . ILE A 1 243 ? 195.123 183.765 158.511 1.00 36.70  ?  262 ILE A CB    1 
ATOM   1962  C  CG1   . ILE A 1 243 ? 196.388 184.432 159.055 1.00 40.45  ?  262 ILE A CG1   1 
ATOM   1963  C  CG2   . ILE A 1 243 ? 194.262 184.808 157.826 1.00 38.16  ?  262 ILE A CG2   1 
ATOM   1964  C  CD1   . ILE A 1 243 ? 197.346 183.473 159.715 1.00 43.98  ?  262 ILE A CD1   1 
ATOM   1965  N  N     . ARG A 1 244 ? 192.200 184.122 160.117 1.00 41.73  ?  263 ARG A N     1 
ATOM   1966  C  CA    . ARG A 1 244 ? 191.308 184.992 160.877 1.00 33.55  ?  263 ARG A CA    1 
ATOM   1967  C  C     . ARG A 1 244 ? 191.026 184.419 162.260 1.00 39.92  ?  263 ARG A C     1 
ATOM   1968  O  O     . ARG A 1 244 ? 190.938 185.166 163.240 1.00 47.05  ?  263 ARG A O     1 
ATOM   1969  C  CB    . ARG A 1 244 ? 190.011 185.210 160.101 1.00 32.69  ?  263 ARG A CB    1 
ATOM   1970  C  CG    . ARG A 1 244 ? 190.172 186.146 158.918 1.00 34.79  ?  263 ARG A CG    1 
ATOM   1971  C  CD    . ARG A 1 244 ? 188.841 186.642 158.394 1.00 40.81  ?  263 ARG A CD    1 
ATOM   1972  N  NE    . ARG A 1 244 ? 188.933 186.968 156.977 1.00 43.28  ?  263 ARG A NE    1 
ATOM   1973  C  CZ    . ARG A 1 244 ? 188.058 186.580 156.059 1.00 46.93  ?  263 ARG A CZ    1 
ATOM   1974  N  NH1   . ARG A 1 244 ? 187.002 185.849 156.376 1.00 40.88  1  263 ARG A NH1   1 
ATOM   1975  N  NH2   . ARG A 1 244 ? 188.247 186.936 154.792 1.00 46.85  ?  263 ARG A NH2   1 
ATOM   1976  N  N     . GLN A 1 245 ? 190.890 183.096 162.362 1.00 38.19  ?  264 GLN A N     1 
ATOM   1977  C  CA    . GLN A 1 245 ? 190.770 182.460 163.670 1.00 41.67  ?  264 GLN A CA    1 
ATOM   1978  C  C     . GLN A 1 245 ? 192.054 182.622 164.472 1.00 45.95  ?  264 GLN A C     1 
ATOM   1979  O  O     . GLN A 1 245 ? 192.013 182.818 165.692 1.00 47.77  ?  264 GLN A O     1 
ATOM   1980  C  CB    . GLN A 1 245 ? 190.418 180.983 163.507 1.00 42.33  ?  264 GLN A CB    1 
ATOM   1981  C  CG    . GLN A 1 245 ? 189.835 180.347 164.756 1.00 38.17  ?  264 GLN A CG    1 
ATOM   1982  C  CD    . GLN A 1 245 ? 189.901 178.835 164.724 1.00 45.87  ?  264 GLN A CD    1 
ATOM   1983  O  OE1   . GLN A 1 245 ? 190.391 178.243 163.762 1.00 52.24  ?  264 GLN A OE1   1 
ATOM   1984  N  NE2   . GLN A 1 245 ? 189.399 178.199 165.775 1.00 45.91  ?  264 GLN A NE2   1 
ATOM   1985  N  N     . LEU A 1 246 ? 193.205 182.534 163.799 1.00 43.21  ?  265 LEU A N     1 
ATOM   1986  C  CA    . LEU A 1 246 ? 194.477 182.825 164.454 1.00 40.32  ?  265 LEU A CA    1 
ATOM   1987  C  C     . LEU A 1 246 ? 194.494 184.247 165.004 1.00 39.03  ?  265 LEU A C     1 
ATOM   1988  O  O     . LEU A 1 246 ? 194.887 184.479 166.154 1.00 44.14  ?  265 LEU A O     1 
ATOM   1989  C  CB    . LEU A 1 246 ? 195.624 182.604 163.465 1.00 43.03  ?  265 LEU A CB    1 
ATOM   1990  C  CG    . LEU A 1 246 ? 197.053 182.976 163.865 1.00 41.81  ?  265 LEU A CG    1 
ATOM   1991  C  CD1   . LEU A 1 246 ? 198.033 181.926 163.372 1.00 41.51  ?  265 LEU A CD1   1 
ATOM   1992  C  CD2   . LEU A 1 246 ? 197.420 184.340 163.300 1.00 46.15  ?  265 LEU A CD2   1 
ATOM   1993  N  N     . GLU A 1 247 ? 194.059 185.211 164.189 1.00 33.61  ?  266 GLU A N     1 
ATOM   1994  C  CA    . GLU A 1 247 ? 193.992 186.601 164.627 1.00 30.77  ?  266 GLU A CA    1 
ATOM   1995  C  C     . GLU A 1 247 ? 193.075 186.746 165.831 1.00 34.82  ?  266 GLU A C     1 
ATOM   1996  O  O     . GLU A 1 247 ? 193.416 187.419 166.808 1.00 43.82  ?  266 GLU A O     1 
ATOM   1997  C  CB    . GLU A 1 247 ? 193.505 187.487 163.480 1.00 33.36  ?  266 GLU A CB    1 
ATOM   1998  C  CG    . GLU A 1 247 ? 194.534 187.760 162.397 1.00 40.27  ?  266 GLU A CG    1 
ATOM   1999  C  CD    . GLU A 1 247 ? 193.974 188.615 161.275 1.00 46.94  ?  266 GLU A CD    1 
ATOM   2000  O  OE1   . GLU A 1 247 ? 192.795 188.421 160.908 1.00 47.14  ?  266 GLU A OE1   1 
ATOM   2001  O  OE2   . GLU A 1 247 ? 194.710 189.481 160.760 1.00 47.89  -1 266 GLU A OE2   1 
ATOM   2002  N  N     . GLY A 1 248 ? 191.905 186.109 165.779 1.00 30.13  ?  267 GLY A N     1 
ATOM   2003  C  CA    . GLY A 1 248 ? 190.966 186.209 166.883 1.00 30.92  ?  267 GLY A CA    1 
ATOM   2004  C  C     . GLY A 1 248 ? 191.507 185.622 168.170 1.00 36.05  ?  267 GLY A C     1 
ATOM   2005  O  O     . GLY A 1 248 ? 191.354 186.209 169.243 1.00 40.42  ?  267 GLY A O     1 
ATOM   2006  N  N     . ASN A 1 249 ? 192.157 184.459 168.083 1.00 34.12  ?  268 ASN A N     1 
ATOM   2007  C  CA    . ASN A 1 249 ? 192.683 183.823 169.286 1.00 29.30  ?  268 ASN A CA    1 
ATOM   2008  C  C     . ASN A 1 249 ? 193.839 184.624 169.874 1.00 35.38  ?  268 ASN A C     1 
ATOM   2009  O  O     . ASN A 1 249 ? 193.901 184.835 171.094 1.00 41.88  ?  268 ASN A O     1 
ATOM   2010  C  CB    . ASN A 1 249 ? 193.115 182.391 168.973 1.00 26.94  ?  268 ASN A CB    1 
ATOM   2011  C  CG    . ASN A 1 249 ? 191.944 181.426 168.921 1.00 29.44  ?  268 ASN A CG    1 
ATOM   2012  O  OD1   . ASN A 1 249 ? 190.820 181.774 169.283 1.00 25.28  ?  268 ASN A OD1   1 
ATOM   2013  N  ND2   . ASN A 1 249 ? 192.204 180.207 168.467 1.00 38.43  ?  268 ASN A ND2   1 
ATOM   2014  N  N     . ILE A 1 250 ? 194.754 185.099 169.024 1.00 30.21  ?  269 ILE A N     1 
ATOM   2015  C  CA    . ILE A 1 250 ? 195.866 185.907 169.516 1.00 23.30  ?  269 ILE A CA    1 
ATOM   2016  C  C     . ILE A 1 250 ? 195.361 187.224 170.094 1.00 32.81  ?  269 ILE A C     1 
ATOM   2017  O  O     . ILE A 1 250 ? 195.914 187.736 171.073 1.00 37.31  ?  269 ILE A O     1 
ATOM   2018  C  CB    . ILE A 1 250 ? 196.905 186.127 168.401 1.00 32.01  ?  269 ILE A CB    1 
ATOM   2019  C  CG1   . ILE A 1 250 ? 197.436 184.785 167.896 1.00 31.64  ?  269 ILE A CG1   1 
ATOM   2020  C  CG2   . ILE A 1 250 ? 198.048 186.989 168.890 1.00 31.00  ?  269 ILE A CG2   1 
ATOM   2021  C  CD1   . ILE A 1 250 ? 198.354 184.909 166.706 1.00 27.94  ?  269 ILE A CD1   1 
ATOM   2022  N  N     . LEU A 1 251 ? 194.310 187.796 169.503 1.00 34.03  ?  270 LEU A N     1 
ATOM   2023  C  CA    . LEU A 1 251 ? 193.726 189.015 170.049 1.00 33.45  ?  270 LEU A CA    1 
ATOM   2024  C  C     . LEU A 1 251 ? 193.098 188.758 171.413 1.00 37.35  ?  270 LEU A C     1 
ATOM   2025  O  O     . LEU A 1 251 ? 193.315 189.519 172.363 1.00 50.58  ?  270 LEU A O     1 
ATOM   2026  C  CB    . LEU A 1 251 ? 192.694 189.576 169.071 1.00 25.57  ?  270 LEU A CB    1 
ATOM   2027  C  CG    . LEU A 1 251 ? 193.189 190.664 168.117 1.00 27.30  ?  270 LEU A CG    1 
ATOM   2028  C  CD1   . LEU A 1 251 ? 192.059 191.155 167.228 1.00 30.85  ?  270 LEU A CD1   1 
ATOM   2029  C  CD2   . LEU A 1 251 ? 193.797 191.814 168.899 1.00 32.50  ?  270 LEU A CD2   1 
ATOM   2030  N  N     . ALA A 1 252 ? 192.310 187.684 171.527 1.00 21.36  ?  271 ALA A N     1 
ATOM   2031  C  CA    . ALA A 1 252 ? 191.682 187.356 172.802 1.00 29.32  ?  271 ALA A CA    1 
ATOM   2032  C  C     . ALA A 1 252 ? 192.721 187.052 173.871 1.00 36.92  ?  271 ALA A C     1 
ATOM   2033  O  O     . ALA A 1 252 ? 192.461 187.247 175.064 1.00 46.68  ?  271 ALA A O     1 
ATOM   2034  C  CB    . ALA A 1 252 ? 190.730 186.171 172.634 1.00 29.82  ?  271 ALA A CB    1 
ATOM   2035  N  N     . ALA A 1 253 ? 193.898 186.575 173.468 1.00 20.46  ?  272 ALA A N     1 
ATOM   2036  C  CA    . ALA A 1 253 ? 194.975 186.367 174.430 1.00 25.51  ?  272 ALA A CA    1 
ATOM   2037  C  C     . ALA A 1 253 ? 195.626 187.689 174.828 1.00 27.65  ?  272 ALA A C     1 
ATOM   2038  O  O     . ALA A 1 253 ? 195.662 188.047 176.010 1.00 27.71  ?  272 ALA A O     1 
ATOM   2039  C  CB    . ALA A 1 253 ? 196.015 185.403 173.852 1.00 35.36  ?  272 ALA A CB    1 
ATOM   2040  N  N     . MET A 1 254 ? 196.129 188.438 173.843 1.00 35.21  ?  273 MET A N     1 
ATOM   2041  C  CA    . MET A 1 254 ? 196.907 189.641 174.126 1.00 30.61  ?  273 MET A CA    1 
ATOM   2042  C  C     . MET A 1 254 ? 196.076 190.697 174.842 1.00 34.01  ?  273 MET A C     1 
ATOM   2043  O  O     . MET A 1 254 ? 196.558 191.339 175.782 1.00 41.79  ?  273 MET A O     1 
ATOM   2044  C  CB    . MET A 1 254 ? 197.490 190.198 172.828 1.00 27.75  ?  273 MET A CB    1 
ATOM   2045  C  CG    . MET A 1 254 ? 198.517 189.280 172.190 1.00 32.08  ?  273 MET A CG    1 
ATOM   2046  S  SD    . MET A 1 254 ? 199.197 189.887 170.636 1.00 43.89  ?  273 MET A SD    1 
ATOM   2047  C  CE    . MET A 1 254 ? 200.334 191.131 171.229 1.00 41.72  ?  273 MET A CE    1 
ATOM   2048  N  N     . CYS A 1 255 ? 194.828 190.905 174.410 1.00 20.37  ?  274 CYS A N     1 
ATOM   2049  C  CA    . CYS A 1 255 ? 193.959 191.847 175.102 1.00 28.20  ?  274 CYS A CA    1 
ATOM   2050  C  C     . CYS A 1 255 ? 193.660 191.405 176.527 1.00 40.68  ?  274 CYS A C     1 
ATOM   2051  O  O     . CYS A 1 255 ? 193.338 192.247 177.373 1.00 47.13  ?  274 CYS A O     1 
ATOM   2052  C  CB    . CYS A 1 255 ? 192.656 192.027 174.323 1.00 28.40  ?  274 CYS A CB    1 
ATOM   2053  S  SG    . CYS A 1 255 ? 192.847 192.898 172.751 1.00 52.39  ?  274 CYS A SG    1 
ATOM   2054  N  N     . SER A 1 256 ? 193.763 190.109 176.812 1.00 24.87  ?  275 SER A N     1 
ATOM   2055  C  CA    . SER A 1 256 ? 193.620 189.597 178.167 1.00 17.71  ?  275 SER A CA    1 
ATOM   2056  C  C     . SER A 1 256 ? 194.944 189.547 178.917 1.00 21.87  ?  275 SER A C     1 
ATOM   2057  O  O     . SER A 1 256 ? 194.955 189.192 180.100 1.00 25.54  ?  275 SER A O     1 
ATOM   2058  C  CB    . SER A 1 256 ? 192.990 188.202 178.140 1.00 27.30  ?  275 SER A CB    1 
ATOM   2059  O  OG    . SER A 1 256 ? 193.764 187.308 177.360 1.00 39.57  ?  275 SER A OG    1 
ATOM   2060  N  N     . SER A 1 257 ? 196.052 189.884 178.253 1.00 33.55  ?  276 SER A N     1 
ATOM   2061  C  CA    . SER A 1 257 ? 197.361 190.029 178.884 1.00 30.79  ?  276 SER A CA    1 
ATOM   2062  C  C     . SER A 1 257 ? 197.817 188.738 179.556 1.00 28.16  ?  276 SER A C     1 
ATOM   2063  O  O     . SER A 1 257 ? 197.817 188.645 180.790 1.00 28.11  ?  276 SER A O     1 
ATOM   2064  C  CB    . SER A 1 257 ? 197.338 191.173 179.900 1.00 31.02  ?  276 SER A CB    1 
ATOM   2065  O  OG    . SER A 1 257 ? 196.737 192.333 179.352 1.00 32.45  ?  276 SER A OG    1 
ATOM   2066  N  N     . PRO A 1 258 ? 198.206 187.727 178.786 1.00 35.95  ?  277 PRO A N     1 
ATOM   2067  C  CA    . PRO A 1 258 ? 198.601 186.451 179.374 1.00 30.68  ?  277 PRO A CA    1 
ATOM   2068  C  C     . PRO A 1 258 ? 200.081 186.448 179.711 1.00 28.88  ?  277 PRO A C     1 
ATOM   2069  O  O     . PRO A 1 258 ? 200.802 187.401 179.378 1.00 36.69  ?  277 PRO A O     1 
ATOM   2070  C  CB    . PRO A 1 258 ? 198.279 185.447 178.258 1.00 32.46  ?  277 PRO A CB    1 
ATOM   2071  C  CG    . PRO A 1 258 ? 198.423 186.245 176.986 1.00 32.62  ?  277 PRO A CG    1 
ATOM   2072  C  CD    . PRO A 1 258 ? 198.377 187.721 177.325 1.00 37.31  ?  277 PRO A CD    1 
ATOM   2073  N  N     . PRO A 1 259 ? 200.574 185.408 180.386 1.00 44.41  ?  278 PRO A N     1 
ATOM   2074  C  CA    . PRO A 1 259 ? 202.019 185.308 180.621 1.00 45.35  ?  278 PRO A CA    1 
ATOM   2075  C  C     . PRO A 1 259 ? 202.791 185.166 179.316 1.00 44.41  ?  278 PRO A C     1 
ATOM   2076  O  O     . PRO A 1 259 ? 202.249 184.794 178.274 1.00 46.66  ?  278 PRO A O     1 
ATOM   2077  C  CB    . PRO A 1 259 ? 202.160 184.054 181.497 1.00 52.17  ?  278 PRO A CB    1 
ATOM   2078  C  CG    . PRO A 1 259 ? 200.852 183.340 181.391 1.00 52.73  ?  278 PRO A CG    1 
ATOM   2079  C  CD    . PRO A 1 259 ? 199.825 184.392 181.144 1.00 52.28  ?  278 PRO A CD    1 
ATOM   2080  N  N     . PHE A 1 260 ? 204.085 185.488 179.392 1.00 48.43  ?  279 PHE A N     1 
ATOM   2081  C  CA    . PHE A 1 260 ? 204.924 185.562 178.198 1.00 48.38  ?  279 PHE A CA    1 
ATOM   2082  C  C     . PHE A 1 260 ? 205.031 184.203 177.509 1.00 48.37  ?  279 PHE A C     1 
ATOM   2083  O  O     . PHE A 1 260 ? 204.766 184.074 176.304 1.00 55.07  ?  279 PHE A O     1 
ATOM   2084  C  CB    . PHE A 1 260 ? 206.306 186.081 178.600 1.00 49.67  ?  279 PHE A CB    1 
ATOM   2085  C  CG    . PHE A 1 260 ? 207.237 186.333 177.448 1.00 48.69  ?  279 PHE A CG    1 
ATOM   2086  C  CD1   . PHE A 1 260 ? 206.778 186.909 176.277 1.00 49.72  ?  279 PHE A CD1   1 
ATOM   2087  C  CD2   . PHE A 1 260 ? 208.581 186.010 177.548 1.00 50.85  ?  279 PHE A CD2   1 
ATOM   2088  C  CE1   . PHE A 1 260 ? 207.642 187.158 175.227 1.00 50.87  ?  279 PHE A CE1   1 
ATOM   2089  C  CE2   . PHE A 1 260 ? 209.446 186.248 176.498 1.00 51.87  ?  279 PHE A CE2   1 
ATOM   2090  C  CZ    . PHE A 1 260 ? 208.976 186.821 175.335 1.00 52.63  ?  279 PHE A CZ    1 
ATOM   2091  N  N     . HIS A 1 261 ? 205.404 183.168 178.267 1.00 41.56  ?  280 HIS A N     1 
ATOM   2092  C  CA    . HIS A 1 261 ? 205.619 181.853 177.671 1.00 44.74  ?  280 HIS A CA    1 
ATOM   2093  C  C     . HIS A 1 261 ? 204.306 181.215 177.234 1.00 48.84  ?  280 HIS A C     1 
ATOM   2094  O  O     . HIS A 1 261 ? 204.260 180.522 176.214 1.00 45.25  ?  280 HIS A O     1 
ATOM   2095  C  CB    . HIS A 1 261 ? 206.362 180.946 178.650 1.00 46.73  ?  280 HIS A CB    1 
ATOM   2096  C  CG    . HIS A 1 261 ? 207.698 181.478 179.065 1.00 50.38  ?  280 HIS A CG    1 
ATOM   2097  N  ND1   . HIS A 1 261 ? 207.840 182.496 179.983 1.00 51.98  ?  280 HIS A ND1   1 
ATOM   2098  C  CD2   . HIS A 1 261 ? 208.951 181.145 178.676 1.00 51.59  ?  280 HIS A CD2   1 
ATOM   2099  C  CE1   . HIS A 1 261 ? 209.123 182.762 180.148 1.00 50.42  ?  280 HIS A CE1   1 
ATOM   2100  N  NE2   . HIS A 1 261 ? 209.819 181.956 179.366 1.00 53.70  ?  280 HIS A NE2   1 
ATOM   2101  N  N     . GLU A 1 262 ? 203.227 181.434 177.988 1.00 51.85  ?  281 GLU A N     1 
ATOM   2102  C  CA    . GLU A 1 262 ? 201.930 180.925 177.554 1.00 48.85  ?  281 GLU A CA    1 
ATOM   2103  C  C     . GLU A 1 262 ? 201.455 181.624 176.287 1.00 41.45  ?  281 GLU A C     1 
ATOM   2104  O  O     . GLU A 1 262 ? 200.815 180.996 175.436 1.00 47.28  ?  281 GLU A O     1 
ATOM   2105  C  CB    . GLU A 1 262 ? 200.895 181.080 178.668 1.00 51.12  ?  281 GLU A CB    1 
ATOM   2106  C  CG    . GLU A 1 262 ? 199.594 180.337 178.406 1.00 54.07  ?  281 GLU A CG    1 
ATOM   2107  C  CD    . GLU A 1 262 ? 198.822 180.048 179.678 1.00 57.47  ?  281 GLU A CD    1 
ATOM   2108  O  OE1   . GLU A 1 262 ? 199.252 180.512 180.754 1.00 56.58  ?  281 GLU A OE1   1 
ATOM   2109  O  OE2   . GLU A 1 262 ? 197.786 179.354 179.600 1.00 56.92  -1 281 GLU A OE2   1 
ATOM   2110  N  N     . MET A 1 263 ? 201.751 182.918 176.147 1.00 45.92  ?  282 MET A N     1 
ATOM   2111  C  CA    . MET A 1 263 ? 201.446 183.617 174.904 1.00 48.65  ?  282 MET A CA    1 
ATOM   2112  C  C     . MET A 1 263 ? 202.230 183.021 173.742 1.00 46.09  ?  282 MET A C     1 
ATOM   2113  O  O     . MET A 1 263 ? 201.684 182.810 172.651 1.00 49.94  ?  282 MET A O     1 
ATOM   2114  C  CB    . MET A 1 263 ? 201.756 185.107 175.047 1.00 44.70  ?  282 MET A CB    1 
ATOM   2115  C  CG    . MET A 1 263 ? 201.350 185.919 173.840 1.00 41.57  ?  282 MET A CG    1 
ATOM   2116  S  SD    . MET A 1 263 ? 199.558 185.970 173.714 1.00 45.65  ?  282 MET A SD    1 
ATOM   2117  C  CE    . MET A 1 263 ? 199.328 185.816 171.951 1.00 44.02  ?  282 MET A CE    1 
ATOM   2118  N  N     . GLY A 1 264 ? 203.516 182.743 173.959 1.00 46.56  ?  283 GLY A N     1 
ATOM   2119  C  CA    . GLY A 1 264 ? 204.285 182.054 172.935 1.00 49.68  ?  283 GLY A CA    1 
ATOM   2120  C  C     . GLY A 1 264 ? 203.684 180.708 172.574 1.00 56.97  ?  283 GLY A C     1 
ATOM   2121  O  O     . GLY A 1 264 ? 203.607 180.344 171.397 1.00 60.36  ?  283 GLY A O     1 
ATOM   2122  N  N     . GLU A 1 265 ? 203.236 179.959 173.584 1.00 57.33  ?  284 GLU A N     1 
ATOM   2123  C  CA    . GLU A 1 265 ? 202.653 178.644 173.344 1.00 54.98  ?  284 GLU A CA    1 
ATOM   2124  C  C     . GLU A 1 265 ? 201.365 178.735 172.537 1.00 49.47  ?  284 GLU A C     1 
ATOM   2125  O  O     . GLU A 1 265 ? 201.139 177.925 171.635 1.00 46.37  ?  284 GLU A O     1 
ATOM   2126  C  CB    . GLU A 1 265 ? 202.399 177.927 174.670 1.00 56.45  ?  284 GLU A CB    1 
ATOM   2127  C  CG    . GLU A 1 265 ? 203.663 177.504 175.392 1.00 55.01  ?  284 GLU A CG    1 
ATOM   2128  C  CD    . GLU A 1 265 ? 204.307 176.288 174.759 1.00 59.26  ?  284 GLU A CD    1 
ATOM   2129  O  OE1   . GLU A 1 265 ? 203.586 175.506 174.104 1.00 62.35  ?  284 GLU A OE1   1 
ATOM   2130  O  OE2   . GLU A 1 265 ? 205.533 176.112 174.916 1.00 58.13  -1 284 GLU A OE2   1 
ATOM   2131  N  N     . ILE A 1 266 ? 200.496 179.699 172.853 1.00 49.66  ?  285 ILE A N     1 
ATOM   2132  C  CA    . ILE A 1 266 ? 199.240 179.804 172.114 1.00 47.69  ?  285 ILE A CA    1 
ATOM   2133  C  C     . ILE A 1 266 ? 199.499 180.274 170.686 1.00 48.73  ?  285 ILE A C     1 
ATOM   2134  O  O     . ILE A 1 266 ? 198.841 179.816 169.741 1.00 51.85  ?  285 ILE A O     1 
ATOM   2135  C  CB    . ILE A 1 266 ? 198.229 180.707 172.851 1.00 43.94  ?  285 ILE A CB    1 
ATOM   2136  C  CG1   . ILE A 1 266 ? 196.959 180.885 172.018 1.00 45.86  ?  285 ILE A CG1   1 
ATOM   2137  C  CG2   . ILE A 1 266 ? 198.801 182.063 173.141 1.00 44.10  ?  285 ILE A CG2   1 
ATOM   2138  C  CD1   . ILE A 1 266 ? 195.882 181.690 172.706 1.00 45.36  ?  285 ILE A CD1   1 
ATOM   2139  N  N     . ILE A 1 267 ? 200.467 181.178 170.496 1.00 46.92  ?  286 ILE A N     1 
ATOM   2140  C  CA    . ILE A 1 267 ? 200.850 181.571 169.139 1.00 37.63  ?  286 ILE A CA    1 
ATOM   2141  C  C     . ILE A 1 267 ? 201.326 180.357 168.352 1.00 45.26  ?  286 ILE A C     1 
ATOM   2142  O  O     . ILE A 1 267 ? 200.908 180.128 167.208 1.00 47.76  ?  286 ILE A O     1 
ATOM   2143  C  CB    . ILE A 1 267 ? 201.928 182.670 169.179 1.00 39.98  ?  286 ILE A CB    1 
ATOM   2144  C  CG1   . ILE A 1 267 ? 201.354 183.966 169.744 1.00 45.92  ?  286 ILE A CG1   1 
ATOM   2145  C  CG2   . ILE A 1 267 ? 202.494 182.914 167.789 1.00 46.76  ?  286 ILE A CG2   1 
ATOM   2146  C  CD1   . ILE A 1 267 ? 202.392 185.041 169.976 1.00 42.73  ?  286 ILE A CD1   1 
ATOM   2147  N  N     . CYS A 1 268 ? 202.202 179.553 168.961 1.00 55.84  ?  287 CYS A N     1 
ATOM   2148  C  CA    . CYS A 1 268 ? 202.715 178.366 168.286 1.00 55.70  ?  287 CYS A CA    1 
ATOM   2149  C  C     . CYS A 1 268 ? 201.599 177.370 167.995 1.00 53.80  ?  287 CYS A C     1 
ATOM   2150  O  O     . CYS A 1 268 ? 201.583 176.738 166.934 1.00 59.23  ?  287 CYS A O     1 
ATOM   2151  C  CB    . CYS A 1 268 ? 203.812 177.719 169.131 1.00 56.41  ?  287 CYS A CB    1 
ATOM   2152  S  SG    . CYS A 1 268 ? 205.322 178.707 169.287 1.00 55.16  ?  287 CYS A SG    1 
ATOM   2153  N  N     . ARG A 1 269 ? 200.658 177.217 168.929 1.00 45.73  ?  288 ARG A N     1 
ATOM   2154  C  CA    . ARG A 1 269 ? 199.554 176.283 168.737 1.00 43.25  ?  288 ARG A CA    1 
ATOM   2155  C  C     . ARG A 1 269 ? 198.652 176.716 167.590 1.00 45.16  ?  288 ARG A C     1 
ATOM   2156  O  O     . ARG A 1 269 ? 198.216 175.883 166.791 1.00 48.25  ?  288 ARG A O     1 
ATOM   2157  C  CB    . ARG A 1 269 ? 198.757 176.146 170.033 1.00 45.95  ?  288 ARG A CB    1 
ATOM   2158  C  CG    . ARG A 1 269 ? 197.698 175.058 170.004 1.00 51.29  ?  288 ARG A CG    1 
ATOM   2159  C  CD    . ARG A 1 269 ? 197.056 174.884 171.371 1.00 57.40  ?  288 ARG A CD    1 
ATOM   2160  N  NE    . ARG A 1 269 ? 196.302 176.063 171.780 1.00 58.48  ?  288 ARG A NE    1 
ATOM   2161  C  CZ    . ARG A 1 269 ? 196.645 176.855 172.786 1.00 54.55  ?  288 ARG A CZ    1 
ATOM   2162  N  NH1   . ARG A 1 269 ? 197.731 176.627 173.506 1.00 53.16  1  288 ARG A NH1   1 
ATOM   2163  N  NH2   . ARG A 1 269 ? 195.879 177.903 173.077 1.00 51.18  ?  288 ARG A NH2   1 
ATOM   2164  N  N     . ASN A 1 270 ? 198.356 178.014 167.491 1.00 47.93  ?  289 ASN A N     1 
ATOM   2165  C  CA    . ASN A 1 270 ? 197.574 178.494 166.355 1.00 40.10  ?  289 ASN A CA    1 
ATOM   2166  C  C     . ASN A 1 270 ? 198.326 178.296 165.046 1.00 45.29  ?  289 ASN A C     1 
ATOM   2167  O  O     . ASN A 1 270 ? 197.736 177.885 164.038 1.00 57.87  ?  289 ASN A O     1 
ATOM   2168  C  CB    . ASN A 1 270 ? 197.200 179.966 166.537 1.00 51.59  ?  289 ASN A CB    1 
ATOM   2169  C  CG    . ASN A 1 270 ? 196.284 180.193 167.718 1.00 52.19  ?  289 ASN A CG    1 
ATOM   2170  O  OD1   . ASN A 1 270 ? 195.069 180.028 167.618 1.00 53.04  ?  289 ASN A OD1   1 
ATOM   2171  N  ND2   . ASN A 1 270 ? 196.861 180.588 168.843 1.00 44.29  ?  289 ASN A ND2   1 
ATOM   2172  N  N     . ILE A 1 271 ? 199.633 178.574 165.040 1.00 51.00  ?  290 ILE A N     1 
ATOM   2173  C  CA    . ILE A 1 271 ? 200.406 178.389 163.814 1.00 55.99  ?  290 ILE A CA    1 
ATOM   2174  C  C     . ILE A 1 271 ? 200.389 176.926 163.390 1.00 57.50  ?  290 ILE A C     1 
ATOM   2175  O  O     . ILE A 1 271 ? 200.249 176.614 162.203 1.00 55.55  ?  290 ILE A O     1 
ATOM   2176  C  CB    . ILE A 1 271 ? 201.842 178.918 163.987 1.00 58.88  ?  290 ILE A CB    1 
ATOM   2177  C  CG1   . ILE A 1 271 ? 201.831 180.432 164.192 1.00 52.97  ?  290 ILE A CG1   1 
ATOM   2178  C  CG2   . ILE A 1 271 ? 202.681 178.571 162.770 1.00 62.77  ?  290 ILE A CG2   1 
ATOM   2179  C  CD1   . ILE A 1 271 ? 203.119 180.975 164.758 1.00 51.04  ?  290 ILE A CD1   1 
ATOM   2180  N  N     . GLU A 1 272 ? 200.525 176.006 164.347 1.00 64.09  ?  291 GLU A N     1 
ATOM   2181  C  CA    . GLU A 1 272 ? 200.472 174.584 164.015 1.00 61.06  ?  291 GLU A CA    1 
ATOM   2182  C  C     . GLU A 1 272 ? 199.078 174.164 163.557 1.00 65.58  ?  291 GLU A C     1 
ATOM   2183  O  O     . GLU A 1 272 ? 198.943 173.342 162.644 1.00 70.57  ?  291 GLU A O     1 
ATOM   2184  C  CB    . GLU A 1 272 ? 200.926 173.743 165.209 1.00 65.05  ?  291 GLU A CB    1 
ATOM   2185  C  CG    . GLU A 1 272 ? 202.351 174.029 165.649 1.00 70.80  ?  291 GLU A CG    1 
ATOM   2186  C  CD    . GLU A 1 272 ? 203.376 173.241 164.858 1.00 75.63  ?  291 GLU A CD    1 
ATOM   2187  O  OE1   . GLU A 1 272 ? 202.993 172.586 163.865 1.00 77.47  ?  291 GLU A OE1   1 
ATOM   2188  O  OE2   . GLU A 1 272 ? 204.570 173.286 165.222 1.00 74.75  -1 291 GLU A OE2   1 
ATOM   2189  N  N     . SER A 1 273 ? 198.030 174.705 164.184 1.00 65.97  ?  292 SER A N     1 
ATOM   2190  C  CA    . SER A 1 273 ? 196.671 174.376 163.766 1.00 61.14  ?  292 SER A CA    1 
ATOM   2191  C  C     . SER A 1 273 ? 196.393 174.856 162.349 1.00 57.28  ?  292 SER A C     1 
ATOM   2192  O  O     . SER A 1 273 ? 195.584 174.253 161.636 1.00 59.49  ?  292 SER A O     1 
ATOM   2193  C  CB    . SER A 1 273 ? 195.657 174.980 164.740 1.00 62.67  ?  292 SER A CB    1 
ATOM   2194  O  OG    . SER A 1 273 ? 194.355 174.473 164.501 1.00 67.52  ?  292 SER A OG    1 
ATOM   2195  N  N     . VAL A 1 274 ? 197.050 175.932 161.924 1.00 60.63  ?  293 VAL A N     1 
ATOM   2196  C  CA    . VAL A 1 274 ? 196.907 176.378 160.542 1.00 63.08  ?  293 VAL A CA    1 
ATOM   2197  C  C     . VAL A 1 274 ? 197.850 175.625 159.599 1.00 69.58  ?  293 VAL A C     1 
ATOM   2198  O  O     . VAL A 1 274 ? 197.525 175.435 158.423 1.00 69.37  ?  293 VAL A O     1 
ATOM   2199  C  CB    . VAL A 1 274 ? 197.123 177.899 160.446 1.00 66.91  ?  293 VAL A CB    1 
ATOM   2200  C  CG1   . VAL A 1 274 ? 196.823 178.394 159.046 1.00 64.80  ?  293 VAL A CG1   1 
ATOM   2201  C  CG2   . VAL A 1 274 ? 196.233 178.620 161.442 1.00 66.01  ?  293 VAL A CG2   1 
ATOM   2202  N  N     . LEU A 1 275 ? 198.999 175.169 160.094 1.00 81.06  ?  294 LEU A N     1 
ATOM   2203  C  CA    . LEU A 1 275 ? 200.020 174.505 159.285 1.00 80.48  ?  294 LEU A CA    1 
ATOM   2204  C  C     . LEU A 1 275 ? 200.288 173.133 159.896 1.00 84.82  ?  294 LEU A C     1 
ATOM   2205  O  O     . LEU A 1 275 ? 201.047 173.015 160.864 1.00 86.27  ?  294 LEU A O     1 
ATOM   2206  C  CB    . LEU A 1 275 ? 201.293 175.344 159.231 1.00 76.00  ?  294 LEU A CB    1 
ATOM   2207  C  CG    . LEU A 1 275 ? 201.136 176.784 158.740 1.00 80.29  ?  294 LEU A CG    1 
ATOM   2208  C  CD1   . LEU A 1 275 ? 202.463 177.523 158.818 1.00 80.71  ?  294 LEU A CD1   1 
ATOM   2209  C  CD2   . LEU A 1 275 ? 200.578 176.812 157.327 1.00 80.23  ?  294 LEU A CD2   1 
ATOM   2210  N  N     . ASN A 1 276 ? 199.672 172.099 159.331 1.00 95.32  ?  295 ASN A N     1 
ATOM   2211  C  CA    . ASN A 1 276 ? 199.771 170.759 159.892 1.00 92.80  ?  295 ASN A CA    1 
ATOM   2212  C  C     . ASN A 1 276 ? 201.194 170.216 159.792 1.00 94.85  ?  295 ASN A C     1 
ATOM   2213  O  O     . ASN A 1 276 ? 201.944 170.541 158.866 1.00 94.66  ?  295 ASN A O     1 
ATOM   2214  C  CB    . ASN A 1 276 ? 198.803 169.814 159.181 1.00 93.73  ?  295 ASN A CB    1 
ATOM   2215  C  CG    . ASN A 1 276 ? 197.353 170.153 159.457 1.00 95.38  ?  295 ASN A CG    1 
ATOM   2216  O  OD1   . ASN A 1 276 ? 196.783 169.725 160.460 1.00 96.16  ?  295 ASN A OD1   1 
ATOM   2217  N  ND2   . ASN A 1 276 ? 196.747 170.931 158.567 1.00 95.94  ?  295 ASN A ND2   1 
ATOM   2218  N  N     . GLU A 1 277 ? 201.549 169.377 160.765 1.00 101.87 ?  296 GLU A N     1 
ATOM   2219  C  CA    . GLU A 1 277 ? 202.842 168.689 160.865 1.00 101.43 ?  296 GLU A CA    1 
ATOM   2220  C  C     . GLU A 1 277 ? 204.012 169.604 160.494 1.00 99.23  ?  296 GLU A C     1 
ATOM   2221  O  O     . GLU A 1 277 ? 204.768 169.363 159.552 1.00 102.04 ?  296 GLU A O     1 
ATOM   2222  C  CB    . GLU A 1 277 ? 202.853 167.392 160.043 1.00 102.15 ?  296 GLU A CB    1 
ATOM   2223  C  CG    . GLU A 1 277 ? 202.556 167.513 158.551 1.00 103.20 ?  296 GLU A CG    1 
ATOM   2224  C  CD    . GLU A 1 277 ? 201.135 167.112 158.208 1.00 104.66 ?  296 GLU A CD    1 
ATOM   2225  O  OE1   . GLU A 1 277 ? 200.334 166.897 159.142 1.00 105.26 ?  296 GLU A OE1   1 
ATOM   2226  O  OE2   . GLU A 1 277 ? 200.819 167.010 157.004 1.00 103.46 -1 296 GLU A OE2   1 
ATOM   2227  N  N     . SER A 1 278 ? 204.152 170.671 161.274 1.00 82.91  ?  297 SER A N     1 
ATOM   2228  C  CA    . SER A 1 278 ? 205.243 171.622 161.135 1.00 87.00  ?  297 SER A CA    1 
ATOM   2229  C  C     . SER A 1 278 ? 205.952 171.789 162.474 1.00 86.27  ?  297 SER A C     1 
ATOM   2230  O  O     . SER A 1 278 ? 205.521 171.265 163.504 1.00 86.99  ?  297 SER A O     1 
ATOM   2231  C  CB    . SER A 1 278 ? 204.732 172.977 160.627 1.00 88.38  ?  297 SER A CB    1 
ATOM   2232  O  OG    . SER A 1 278 ? 203.824 173.555 161.548 1.00 89.85  ?  297 SER A OG    1 
ATOM   2233  N  N     . HIS A 1 279 ? 207.064 172.521 162.448 1.00 69.70  ?  298 HIS A N     1 
ATOM   2234  C  CA    . HIS A 1 279 ? 207.812 172.869 163.647 1.00 69.61  ?  298 HIS A CA    1 
ATOM   2235  C  C     . HIS A 1 279 ? 207.929 174.383 163.718 1.00 75.99  ?  298 HIS A C     1 
ATOM   2236  O  O     . HIS A 1 279 ? 208.186 175.036 162.702 1.00 80.23  ?  298 HIS A O     1 
ATOM   2237  C  CB    . HIS A 1 279 ? 209.201 172.224 163.644 1.00 77.39  ?  298 HIS A CB    1 
ATOM   2238  C  CG    . HIS A 1 279 ? 210.106 172.733 164.723 1.00 80.43  ?  298 HIS A CG    1 
ATOM   2239  N  ND1   . HIS A 1 279 ? 209.668 172.984 166.006 1.00 80.03  ?  298 HIS A ND1   1 
ATOM   2240  C  CD2   . HIS A 1 279 ? 211.426 173.039 164.710 1.00 76.72  ?  298 HIS A CD2   1 
ATOM   2241  C  CE1   . HIS A 1 279 ? 210.678 173.422 166.736 1.00 76.21  ?  298 HIS A CE1   1 
ATOM   2242  N  NE2   . HIS A 1 279 ? 211.756 173.464 165.974 1.00 75.67  ?  298 HIS A NE2   1 
ATOM   2243  N  N     . VAL A 1 280 ? 207.725 174.940 164.907 1.00 66.21  ?  299 VAL A N     1 
ATOM   2244  C  CA    . VAL A 1 280 ? 207.745 176.383 165.106 1.00 62.85  ?  299 VAL A CA    1 
ATOM   2245  C  C     . VAL A 1 280 ? 208.671 176.700 166.271 1.00 57.97  ?  299 VAL A C     1 
ATOM   2246  O  O     . VAL A 1 280 ? 208.617 176.037 167.313 1.00 63.34  ?  299 VAL A O     1 
ATOM   2247  C  CB    . VAL A 1 280 ? 206.329 176.942 165.352 1.00 64.54  ?  299 VAL A CB    1 
ATOM   2248  C  CG1   . VAL A 1 280 ? 205.484 176.794 164.102 1.00 62.82  ?  299 VAL A CG1   1 
ATOM   2249  C  CG2   . VAL A 1 280 ? 205.659 176.224 166.504 1.00 64.78  ?  299 VAL A CG2   1 
ATOM   2250  N  N     . SER A 1 281 ? 209.535 177.696 166.087 1.00 50.10  ?  300 SER A N     1 
ATOM   2251  C  CA    . SER A 1 281 ? 210.436 178.153 167.132 1.00 56.59  ?  300 SER A CA    1 
ATOM   2252  C  C     . SER A 1 281 ? 210.411 179.673 167.187 1.00 56.09  ?  300 SER A C     1 
ATOM   2253  O  O     . SER A 1 281 ? 210.240 180.348 166.166 1.00 63.52  ?  300 SER A O     1 
ATOM   2254  C  CB    . SER A 1 281 ? 211.869 177.651 166.903 1.00 64.14  ?  300 SER A CB    1 
ATOM   2255  O  OG    . SER A 1 281 ? 212.433 178.218 165.735 1.00 67.46  ?  300 SER A OG    1 
ATOM   2256  N  N     . LEU A 1 282 ? 210.591 180.206 168.393 1.00 45.49  ?  301 LEU A N     1 
ATOM   2257  C  CA    . LEU A 1 282 ? 210.441 181.632 168.634 1.00 47.66  ?  301 LEU A CA    1 
ATOM   2258  C  C     . LEU A 1 282 ? 211.481 182.077 169.651 1.00 48.05  ?  301 LEU A C     1 
ATOM   2259  O  O     . LEU A 1 282 ? 211.572 181.505 170.742 1.00 59.12  ?  301 LEU A O     1 
ATOM   2260  C  CB    . LEU A 1 282 ? 209.021 181.944 169.123 1.00 54.48  ?  301 LEU A CB    1 
ATOM   2261  C  CG    . LEU A 1 282 ? 208.574 183.399 169.213 1.00 55.75  ?  301 LEU A CG    1 
ATOM   2262  C  CD1   . LEU A 1 282 ? 209.082 184.181 168.018 1.00 62.44  ?  301 LEU A CD1   1 
ATOM   2263  C  CD2   . LEU A 1 282 ? 207.058 183.456 169.273 1.00 52.90  ?  301 LEU A CD2   1 
ATOM   2264  N  N     . PHE A 1 283 ? 212.267 183.090 169.291 1.00 39.47  ?  302 PHE A N     1 
ATOM   2265  C  CA    . PHE A 1 283 ? 213.357 183.556 170.134 1.00 42.45  ?  302 PHE A CA    1 
ATOM   2266  C  C     . PHE A 1 283 ? 213.283 185.068 170.274 1.00 50.47  ?  302 PHE A C     1 
ATOM   2267  O  O     . PHE A 1 283 ? 213.005 185.775 169.303 1.00 57.04  ?  302 PHE A O     1 
ATOM   2268  C  CB    . PHE A 1 283 ? 214.730 183.157 169.560 1.00 49.36  ?  302 PHE A CB    1 
ATOM   2269  C  CG    . PHE A 1 283 ? 214.825 181.712 169.145 1.00 49.24  ?  302 PHE A CG    1 
ATOM   2270  C  CD1   . PHE A 1 283 ? 214.366 181.300 167.904 1.00 52.15  ?  302 PHE A CD1   1 
ATOM   2271  C  CD2   . PHE A 1 283 ? 215.368 180.767 169.999 1.00 52.07  ?  302 PHE A CD2   1 
ATOM   2272  C  CE1   . PHE A 1 283 ? 214.452 179.975 167.522 1.00 49.03  ?  302 PHE A CE1   1 
ATOM   2273  C  CE2   . PHE A 1 283 ? 215.455 179.439 169.622 1.00 53.74  ?  302 PHE A CE2   1 
ATOM   2274  C  CZ    . PHE A 1 283 ? 214.996 179.043 168.382 1.00 47.41  ?  302 PHE A CZ    1 
ATOM   2275  N  N     . ALA A 1 284 ? 213.525 185.554 171.485 1.00 66.00  ?  303 ALA A N     1 
ATOM   2276  C  CA    . ALA A 1 284 ? 213.667 186.977 171.748 1.00 65.77  ?  303 ALA A CA    1 
ATOM   2277  C  C     . ALA A 1 284 ? 215.143 187.356 171.744 1.00 67.04  ?  303 ALA A C     1 
ATOM   2278  O  O     . ALA A 1 284 ? 216.023 186.506 171.887 1.00 71.75  ?  303 ALA A O     1 
ATOM   2279  C  CB    . ALA A 1 284 ? 213.028 187.353 173.088 1.00 66.40  ?  303 ALA A CB    1 
ATOM   2280  N  N     . LEU A 1 285 ? 215.409 188.648 171.579 1.00 73.77  ?  304 LEU A N     1 
ATOM   2281  C  CA    . LEU A 1 285 ? 216.773 189.168 171.528 1.00 78.18  ?  304 LEU A CA    1 
ATOM   2282  C  C     . LEU A 1 285 ? 217.053 189.910 172.830 1.00 79.86  ?  304 LEU A C     1 
ATOM   2283  O  O     . LEU A 1 285 ? 216.656 191.066 172.996 1.00 80.66  ?  304 LEU A O     1 
ATOM   2284  C  CB    . LEU A 1 285 ? 216.963 190.074 170.314 1.00 80.03  ?  304 LEU A CB    1 
ATOM   2285  C  CG    . LEU A 1 285 ? 216.925 189.394 168.944 1.00 80.69  ?  304 LEU A CG    1 
ATOM   2286  C  CD1   . LEU A 1 285 ? 217.205 190.399 167.838 1.00 75.39  ?  304 LEU A CD1   1 
ATOM   2287  C  CD2   . LEU A 1 285 ? 217.918 188.242 168.887 1.00 81.30  ?  304 LEU A CD2   1 
ATOM   2288  N  N     . ARG A 1 286 ? 217.740 189.240 173.749 1.00 93.71  ?  305 ARG A N     1 
ATOM   2289  C  CA    . ARG A 1 286 ? 218.137 189.826 175.023 1.00 94.79  ?  305 ARG A CA    1 
ATOM   2290  C  C     . ARG A 1 286 ? 219.648 190.006 175.018 1.00 95.83  ?  305 ARG A C     1 
ATOM   2291  O  O     . ARG A 1 286 ? 220.391 189.026 174.896 1.00 94.25  ?  305 ARG A O     1 
ATOM   2292  C  CB    . ARG A 1 286 ? 217.695 188.946 176.192 1.00 92.57  ?  305 ARG A CB    1 
ATOM   2293  C  CG    . ARG A 1 286 ? 216.271 188.431 176.067 1.00 90.86  ?  305 ARG A CG    1 
ATOM   2294  C  CD    . ARG A 1 286 ? 215.299 189.272 176.875 1.00 89.92  ?  305 ARG A CD    1 
ATOM   2295  N  NE    . ARG A 1 286 ? 213.956 188.704 176.871 1.00 93.66  ?  305 ARG A NE    1 
ATOM   2296  C  CZ    . ARG A 1 286 ? 213.440 187.996 177.866 1.00 95.41  ?  305 ARG A CZ    1 
ATOM   2297  N  NH1   . ARG A 1 286 ? 214.130 187.742 178.965 1.00 95.00  1  305 ARG A NH1   1 
ATOM   2298  N  NH2   . ARG A 1 286 ? 212.200 187.528 177.753 1.00 92.07  ?  305 ARG A NH2   1 
ATOM   2299  N  N     . ASN A 1 287 ? 220.093 191.258 175.146 1.00 105.26 ?  306 ASN A N     1 
ATOM   2300  C  CA    . ASN A 1 287 ? 221.510 191.616 175.053 1.00 104.39 ?  306 ASN A CA    1 
ATOM   2301  C  C     . ASN A 1 287 ? 222.115 191.167 173.725 1.00 103.40 ?  306 ASN A C     1 
ATOM   2302  O  O     . ASN A 1 287 ? 223.302 190.842 173.649 1.00 103.89 ?  306 ASN A O     1 
ATOM   2303  C  CB    . ASN A 1 287 ? 222.311 191.044 176.227 1.00 103.43 ?  306 ASN A CB    1 
ATOM   2304  C  CG    . ASN A 1 287 ? 221.621 191.254 177.560 1.00 103.77 ?  306 ASN A CG    1 
ATOM   2305  O  OD1   . ASN A 1 287 ? 220.857 192.203 177.735 1.00 103.72 ?  306 ASN A OD1   1 
ATOM   2306  N  ND2   . ASN A 1 287 ? 221.885 190.364 178.509 1.00 102.00 ?  306 ASN A ND2   1 
ATOM   2307  N  N     . GLY A 1 288 ? 221.302 191.146 172.671 1.00 101.88 ?  307 GLY A N     1 
ATOM   2308  C  CA    . GLY A 1 288 ? 221.750 190.677 171.377 1.00 102.86 ?  307 GLY A CA    1 
ATOM   2309  C  C     . GLY A 1 288 ? 221.841 189.175 171.239 1.00 101.11 ?  307 GLY A C     1 
ATOM   2310  O  O     . GLY A 1 288 ? 222.309 188.692 170.202 1.00 100.25 ?  307 GLY A O     1 
ATOM   2311  N  N     . MET A 1 289 ? 221.401 188.420 172.247 1.00 89.09  ?  308 MET A N     1 
ATOM   2312  C  CA    . MET A 1 289 ? 221.478 186.970 172.244 1.00 91.20  ?  308 MET A CA    1 
ATOM   2313  C  C     . MET A 1 289 ? 220.086 186.355 172.131 1.00 90.31  ?  308 MET A C     1 
ATOM   2314  O  O     . MET A 1 289 ? 219.102 186.936 172.602 1.00 88.45  ?  308 MET A O     1 
ATOM   2315  C  CB    . MET A 1 289 ? 222.157 186.450 173.517 1.00 90.63  ?  308 MET A CB    1 
ATOM   2316  C  CG    . MET A 1 289 ? 223.675 186.542 173.498 1.00 89.17  ?  308 MET A CG    1 
ATOM   2317  S  SD    . MET A 1 289 ? 224.417 185.678 172.100 1.00 89.20  ?  308 MET A SD    1 
ATOM   2318  C  CE    . MET A 1 289 ? 224.994 187.057 171.113 1.00 86.80  ?  308 MET A CE    1 
ATOM   2319  N  N     . PRO A 1 290 ? 219.969 185.179 171.508 1.00 80.73  ?  309 PRO A N     1 
ATOM   2320  C  CA    . PRO A 1 290 ? 218.657 184.529 171.369 1.00 77.65  ?  309 PRO A CA    1 
ATOM   2321  C  C     . PRO A 1 290 ? 218.257 183.821 172.656 1.00 75.20  ?  309 PRO A C     1 
ATOM   2322  O  O     . PRO A 1 290 ? 219.013 183.012 173.198 1.00 74.94  ?  309 PRO A O     1 
ATOM   2323  C  CB    . PRO A 1 290 ? 218.877 183.534 170.222 1.00 76.74  ?  309 PRO A CB    1 
ATOM   2324  C  CG    . PRO A 1 290 ? 220.332 183.218 170.278 1.00 76.62  ?  309 PRO A CG    1 
ATOM   2325  C  CD    . PRO A 1 290 ? 221.031 184.452 170.788 1.00 77.67  ?  309 PRO A CD    1 
ATOM   2326  N  N     . ILE A 1 291 ? 217.061 184.134 173.146 1.00 65.08  ?  310 ILE A N     1 
ATOM   2327  C  CA    . ILE A 1 291 ? 216.473 183.480 174.309 1.00 61.01  ?  310 ILE A CA    1 
ATOM   2328  C  C     . ILE A 1 291 ? 215.199 182.782 173.858 1.00 59.34  ?  310 ILE A C     1 
ATOM   2329  O  O     . ILE A 1 291 ? 214.318 183.411 173.262 1.00 67.40  ?  310 ILE A O     1 
ATOM   2330  C  CB    . ILE A 1 291 ? 216.183 184.482 175.442 1.00 66.55  ?  310 ILE A CB    1 
ATOM   2331  C  CG1   . ILE A 1 291 ? 217.492 185.058 175.985 1.00 69.84  ?  310 ILE A CG1   1 
ATOM   2332  C  CG2   . ILE A 1 291 ? 215.387 183.817 176.553 1.00 65.33  ?  310 ILE A CG2   1 
ATOM   2333  C  CD1   . ILE A 1 291 ? 218.435 184.013 176.538 1.00 68.14  ?  310 ILE A CD1   1 
ATOM   2334  N  N     . HIS A 1 292 ? 215.105 181.487 174.146 1.00 54.94  ?  311 HIS A N     1 
ATOM   2335  C  CA    . HIS A 1 292 ? 214.023 180.649 173.635 1.00 52.96  ?  311 HIS A CA    1 
ATOM   2336  C  C     . HIS A 1 292 ? 212.719 180.994 174.342 1.00 52.08  ?  311 HIS A C     1 
ATOM   2337  O  O     . HIS A 1 292 ? 212.515 180.618 175.501 1.00 54.76  ?  311 HIS A O     1 
ATOM   2338  C  CB    . HIS A 1 292 ? 214.377 179.179 173.833 1.00 48.67  ?  311 HIS A CB    1 
ATOM   2339  C  CG    . HIS A 1 292 ? 213.391 178.230 173.230 1.00 47.59  ?  311 HIS A CG    1 
ATOM   2340  N  ND1   . HIS A 1 292 ? 212.225 177.864 173.867 1.00 57.98  ?  311 HIS A ND1   1 
ATOM   2341  C  CD2   . HIS A 1 292 ? 213.403 177.562 172.053 1.00 49.92  ?  311 HIS A CD2   1 
ATOM   2342  C  CE1   . HIS A 1 292 ? 211.558 177.016 173.105 1.00 58.69  ?  311 HIS A CE1   1 
ATOM   2343  N  NE2   . HIS A 1 292 ? 212.252 176.815 171.999 1.00 57.98  ?  311 HIS A NE2   1 
ATOM   2344  N  N     . TRP A 1 293 ? 211.828 181.710 173.650 1.00 50.02  ?  312 TRP A N     1 
ATOM   2345  C  CA    . TRP A 1 293 ? 210.545 182.063 174.244 1.00 46.54  ?  312 TRP A CA    1 
ATOM   2346  C  C     . TRP A 1 293 ? 209.593 180.870 174.240 1.00 49.27  ?  312 TRP A C     1 
ATOM   2347  O  O     . TRP A 1 293 ? 209.065 180.488 175.291 1.00 55.28  ?  312 TRP A O     1 
ATOM   2348  C  CB    . TRP A 1 293 ? 209.949 183.265 173.499 1.00 54.69  ?  312 TRP A CB    1 
ATOM   2349  C  CG    . TRP A 1 293 ? 208.519 183.627 173.835 1.00 55.29  ?  312 TRP A CG    1 
ATOM   2350  C  CD1   . TRP A 1 293 ? 207.761 183.155 174.871 1.00 56.49  ?  312 TRP A CD1   1 
ATOM   2351  C  CD2   . TRP A 1 293 ? 207.689 184.558 173.129 1.00 49.56  ?  312 TRP A CD2   1 
ATOM   2352  N  NE1   . TRP A 1 293 ? 206.512 183.721 174.841 1.00 61.29  ?  312 TRP A NE1   1 
ATOM   2353  C  CE2   . TRP A 1 293 ? 206.442 184.587 173.782 1.00 55.56  ?  312 TRP A CE2   1 
ATOM   2354  C  CE3   . TRP A 1 293 ? 207.880 185.369 172.008 1.00 43.73  ?  312 TRP A CE3   1 
ATOM   2355  C  CZ2   . TRP A 1 293 ? 205.391 185.396 173.353 1.00 59.15  ?  312 TRP A CZ2   1 
ATOM   2356  C  CZ3   . TRP A 1 293 ? 206.835 186.167 171.578 1.00 50.66  ?  312 TRP A CZ3   1 
ATOM   2357  C  CH2   . TRP A 1 293 ? 205.607 186.176 172.250 1.00 59.55  ?  312 TRP A CH2   1 
ATOM   2358  N  N     . ALA A 1 294 ? 209.367 180.263 173.077 1.00 43.93  ?  313 ALA A N     1 
ATOM   2359  C  CA    . ALA A 1 294 ? 208.453 179.132 172.999 1.00 48.79  ?  313 ALA A CA    1 
ATOM   2360  C  C     . ALA A 1 294 ? 208.739 178.328 171.740 1.00 49.66  ?  313 ALA A C     1 
ATOM   2361  O  O     . ALA A 1 294 ? 209.395 178.804 170.809 1.00 56.35  ?  313 ALA A O     1 
ATOM   2362  C  CB    . ALA A 1 294 ? 206.991 179.590 173.017 1.00 57.12  ?  313 ALA A CB    1 
ATOM   2363  N  N     . SER A 1 295 ? 208.227 177.099 171.728 1.00 55.62  ?  314 SER A N     1 
ATOM   2364  C  CA    . SER A 1 295 ? 208.324 176.199 170.587 1.00 56.98  ?  314 SER A CA    1 
ATOM   2365  C  C     . SER A 1 295 ? 207.327 175.067 170.778 1.00 53.61  ?  314 SER A C     1 
ATOM   2366  O  O     . SER A 1 295 ? 206.979 174.717 171.909 1.00 58.16  ?  314 SER A O     1 
ATOM   2367  C  CB    . SER A 1 295 ? 209.741 175.633 170.426 1.00 59.85  ?  314 SER A CB    1 
ATOM   2368  O  OG    . SER A 1 295 ? 210.035 174.695 171.447 1.00 60.95  ?  314 SER A OG    1 
ATOM   2369  N  N     . SER A 1 296 ? 206.875 174.501 169.663 1.00 74.21  ?  315 SER A N     1 
ATOM   2370  C  CA    . SER A 1 296 ? 205.939 173.388 169.720 1.00 79.66  ?  315 SER A CA    1 
ATOM   2371  C  C     . SER A 1 296 ? 206.636 172.129 170.220 1.00 82.24  ?  315 SER A C     1 
ATOM   2372  O  O     . SER A 1 296 ? 207.790 171.858 169.876 1.00 82.35  ?  315 SER A O     1 
ATOM   2373  C  CB    . SER A 1 296 ? 205.327 173.132 168.344 1.00 80.91  ?  315 SER A CB    1 
ATOM   2374  O  OG    . SER A 1 296 ? 206.321 173.126 167.335 1.00 81.43  ?  315 SER A OG    1 
ATOM   2375  N  N     . SER A 1 297 ? 205.923 171.354 171.038 1.00 99.52  ?  316 SER A N     1 
ATOM   2376  C  CA    . SER A 1 297 ? 206.459 170.098 171.547 1.00 101.75 ?  316 SER A CA    1 
ATOM   2377  C  C     . SER A 1 297 ? 206.509 169.006 170.488 1.00 101.92 ?  316 SER A C     1 
ATOM   2378  O  O     . SER A 1 297 ? 207.171 167.985 170.708 1.00 101.19 ?  316 SER A O     1 
ATOM   2379  C  CB    . SER A 1 297 ? 205.629 169.620 172.740 1.00 100.58 ?  316 SER A CB    1 
ATOM   2380  O  OG    . SER A 1 297 ? 204.307 169.298 172.343 1.00 98.63  ?  316 SER A OG    1 
ATOM   2381  N  N     . HIS A 1 298 ? 205.833 169.191 169.353 1.00 109.38 ?  317 HIS A N     1 
ATOM   2382  C  CA    . HIS A 1 298 ? 205.821 168.199 168.278 1.00 109.04 ?  317 HIS A CA    1 
ATOM   2383  C  C     . HIS A 1 298 ? 207.063 168.403 167.414 1.00 111.08 ?  317 HIS A C     1 
ATOM   2384  O  O     . HIS A 1 298 ? 207.039 169.047 166.362 1.00 110.83 ?  317 HIS A O     1 
ATOM   2385  C  CB    . HIS A 1 298 ? 204.540 168.308 167.460 1.00 109.32 ?  317 HIS A CB    1 
ATOM   2386  C  CG    . HIS A 1 298 ? 204.272 167.116 166.595 1.00 110.47 ?  317 HIS A CG    1 
ATOM   2387  N  ND1   . HIS A 1 298 ? 203.196 167.046 165.737 1.00 111.17 ?  317 HIS A ND1   1 
ATOM   2388  C  CD2   . HIS A 1 298 ? 204.940 165.946 166.458 1.00 109.71 ?  317 HIS A CD2   1 
ATOM   2389  C  CE1   . HIS A 1 298 ? 203.212 165.885 165.107 1.00 110.88 ?  317 HIS A CE1   1 
ATOM   2390  N  NE2   . HIS A 1 298 ? 204.260 165.199 165.526 1.00 109.66 ?  317 HIS A NE2   1 
ATOM   2391  N  N     . GLY A 1 299 ? 208.174 167.836 167.878 1.00 121.94 ?  318 GLY A N     1 
ATOM   2392  C  CA    . GLY A 1 299 ? 209.432 167.944 167.166 1.00 122.62 ?  318 GLY A CA    1 
ATOM   2393  C  C     . GLY A 1 299 ? 209.669 166.809 166.191 1.00 123.08 ?  318 GLY A C     1 
ATOM   2394  O  O     . GLY A 1 299 ? 210.750 166.214 166.173 1.00 120.31 ?  318 GLY A O     1 
ATOM   2395  N  N     . ALA A 1 300 ? 208.662 166.497 165.378 1.00 127.16 ?  319 ALA A N     1 
ATOM   2396  C  CA    . ALA A 1 300 ? 208.792 165.424 164.403 1.00 124.93 ?  319 ALA A CA    1 
ATOM   2397  C  C     . ALA A 1 300 ? 209.774 165.812 163.304 1.00 125.64 ?  319 ALA A C     1 
ATOM   2398  O  O     . ALA A 1 300 ? 209.817 166.964 162.863 1.00 126.35 ?  319 ALA A O     1 
ATOM   2399  C  CB    . ALA A 1 300 ? 207.430 165.088 163.798 1.00 123.51 ?  319 ALA A CB    1 
ATOM   2400  N  N     . GLU A 1 301 ? 210.565 164.838 162.862 1.00 124.49 ?  320 GLU A N     1 
ATOM   2401  C  CA    . GLU A 1 301 ? 211.542 165.072 161.809 1.00 124.80 ?  320 GLU A CA    1 
ATOM   2402  C  C     . GLU A 1 301 ? 210.859 165.124 160.449 1.00 123.86 ?  320 GLU A C     1 
ATOM   2403  O  O     . GLU A 1 301 ? 209.994 164.300 160.138 1.00 121.96 ?  320 GLU A O     1 
ATOM   2404  C  CB    . GLU A 1 301 ? 212.609 163.977 161.816 1.00 125.12 ?  320 GLU A CB    1 
ATOM   2405  C  CG    . GLU A 1 301 ? 213.398 163.886 163.111 1.00 124.95 ?  320 GLU A CG    1 
ATOM   2406  C  CD    . GLU A 1 301 ? 214.431 162.776 163.087 1.00 124.49 ?  320 GLU A CD    1 
ATOM   2407  O  OE1   . GLU A 1 301 ? 214.743 162.277 161.985 1.00 123.84 ?  320 GLU A OE1   1 
ATOM   2408  O  OE2   . GLU A 1 301 ? 214.930 162.403 164.169 1.00 123.76 -1 320 GLU A OE2   1 
ATOM   2409  N  N     . ILE A 1 302 ? 211.254 166.102 159.637 1.00 119.55 ?  321 ILE A N     1 
ATOM   2410  C  CA    . ILE A 1 302 ? 210.707 166.297 158.300 1.00 118.24 ?  321 ILE A CA    1 
ATOM   2411  C  C     . ILE A 1 302 ? 211.861 166.298 157.307 1.00 118.20 ?  321 ILE A C     1 
ATOM   2412  O  O     . ILE A 1 302 ? 212.861 166.994 157.513 1.00 118.55 ?  321 ILE A O     1 
ATOM   2413  C  CB    . ILE A 1 302 ? 209.900 167.604 158.199 1.00 118.99 ?  321 ILE A CB    1 
ATOM   2414  C  CG1   . ILE A 1 302 ? 208.817 167.648 159.279 1.00 118.89 ?  321 ILE A CG1   1 
ATOM   2415  C  CG2   . ILE A 1 302 ? 209.274 167.732 156.821 1.00 119.13 ?  321 ILE A CG2   1 
ATOM   2416  C  CD1   . ILE A 1 302 ? 208.035 168.943 159.305 1.00 117.16 ?  321 ILE A CD1   1 
ATOM   2417  N  N     . GLN A 1 303 ? 211.720 165.521 156.237 1.00 118.29 ?  322 GLN A N     1 
ATOM   2418  C  CA    . GLN A 1 303 ? 212.753 165.414 155.217 1.00 119.39 ?  322 GLN A CA    1 
ATOM   2419  C  C     . GLN A 1 303 ? 212.534 166.454 154.127 1.00 119.46 ?  322 GLN A C     1 
ATOM   2420  O  O     . GLN A 1 303 ? 211.401 166.691 153.696 1.00 119.24 ?  322 GLN A O     1 
ATOM   2421  C  CB    . GLN A 1 303 ? 212.763 164.012 154.607 1.00 118.26 ?  322 GLN A CB    1 
ATOM   2422  C  CG    . GLN A 1 303 ? 212.841 162.891 155.631 1.00 118.64 ?  322 GLN A CG    1 
ATOM   2423  C  CD    . GLN A 1 303 ? 212.824 161.516 154.993 1.00 118.94 ?  322 GLN A CD    1 
ATOM   2424  O  OE1   . GLN A 1 303 ? 212.830 161.386 153.769 1.00 119.32 ?  322 GLN A OE1   1 
ATOM   2425  N  NE2   . GLN A 1 303 ? 212.803 160.480 155.823 1.00 117.53 ?  322 GLN A NE2   1 
ATOM   2426  N  N     . ASN A 1 304 ? 213.633 167.071 153.684 1.00 122.25 ?  323 ASN A N     1 
ATOM   2427  C  CA    . ASN A 1 304 ? 213.606 168.095 152.636 1.00 121.93 ?  323 ASN A CA    1 
ATOM   2428  C  C     . ASN A 1 304 ? 212.657 169.236 152.997 1.00 121.78 ?  323 ASN A C     1 
ATOM   2429  O  O     . ASN A 1 304 ? 211.936 169.762 152.147 1.00 122.66 ?  323 ASN A O     1 
ATOM   2430  C  CB    . ASN A 1 304 ? 213.237 167.489 151.279 1.00 121.60 ?  323 ASN A CB    1 
ATOM   2431  C  CG    . ASN A 1 304 ? 214.239 166.451 150.813 1.00 120.60 ?  323 ASN A CG    1 
ATOM   2432  O  OD1   . ASN A 1 304 ? 215.449 166.666 150.879 1.00 120.13 ?  323 ASN A OD1   1 
ATOM   2433  N  ND2   . ASN A 1 304 ? 213.738 165.317 150.336 1.00 120.39 ?  323 ASN A ND2   1 
ATOM   2434  N  N     . ALA A 1 305 ? 212.659 169.621 154.269 1.00 114.42 ?  324 ALA A N     1 
ATOM   2435  C  CA    . ALA A 1 305 ? 211.777 170.675 154.743 1.00 113.08 ?  324 ALA A CA    1 
ATOM   2436  C  C     . ALA A 1 305 ? 212.373 172.050 154.470 1.00 112.17 ?  324 ALA A C     1 
ATOM   2437  O  O     . ALA A 1 305 ? 213.593 172.219 154.388 1.00 113.45 ?  324 ALA A O     1 
ATOM   2438  C  CB    . ALA A 1 305 ? 211.508 170.516 156.239 1.00 112.43 ?  324 ALA A CB    1 
ATOM   2439  N  N     . GLN A 1 306 ? 211.494 173.037 154.331 1.00 97.19  ?  325 GLN A N     1 
ATOM   2440  C  CA    . GLN A 1 306 ? 211.890 174.425 154.154 1.00 97.84  ?  325 GLN A CA    1 
ATOM   2441  C  C     . GLN A 1 306 ? 211.643 175.193 155.445 1.00 100.13 ?  325 GLN A C     1 
ATOM   2442  O  O     . GLN A 1 306 ? 210.589 175.051 156.074 1.00 99.08  ?  325 GLN A O     1 
ATOM   2443  C  CB    . GLN A 1 306 ? 211.123 175.075 153.001 1.00 97.23  ?  325 GLN A CB    1 
ATOM   2444  C  CG    . GLN A 1 306 ? 211.504 176.524 152.741 1.00 97.56  ?  325 GLN A CG    1 
ATOM   2445  C  CD    . GLN A 1 306 ? 212.685 176.659 151.801 1.00 99.83  ?  325 GLN A CD    1 
ATOM   2446  O  OE1   . GLN A 1 306 ? 212.793 175.934 150.812 1.00 100.71 ?  325 GLN A OE1   1 
ATOM   2447  N  NE2   . GLN A 1 306 ? 213.580 177.592 152.106 1.00 99.04  ?  325 GLN A NE2   1 
ATOM   2448  N  N     . SER A 1 307 ? 212.626 175.998 155.839 1.00 92.96  ?  326 SER A N     1 
ATOM   2449  C  CA    . SER A 1 307 ? 212.564 176.790 157.060 1.00 90.90  ?  326 SER A CA    1 
ATOM   2450  C  C     . SER A 1 307 ? 212.550 178.268 156.693 1.00 88.33  ?  326 SER A C     1 
ATOM   2451  O  O     . SER A 1 307 ? 213.538 178.789 156.164 1.00 88.99  ?  326 SER A O     1 
ATOM   2452  C  CB    . SER A 1 307 ? 213.745 176.474 157.977 1.00 87.68  ?  326 SER A CB    1 
ATOM   2453  O  OG    . SER A 1 307 ? 213.815 175.087 158.259 1.00 87.89  ?  326 SER A OG    1 
ATOM   2454  N  N     . TRP A 1 308 ? 211.435 178.934 156.973 1.00 69.47  ?  327 TRP A N     1 
ATOM   2455  C  CA    . TRP A 1 308 ? 211.295 180.367 156.753 1.00 66.65  ?  327 TRP A CA    1 
ATOM   2456  C  C     . TRP A 1 308 ? 211.500 181.085 158.081 1.00 66.41  ?  327 TRP A C     1 
ATOM   2457  O  O     . TRP A 1 308 ? 210.829 180.773 159.071 1.00 71.84  ?  327 TRP A O     1 
ATOM   2458  C  CB    . TRP A 1 308 ? 209.924 180.704 156.164 1.00 64.54  ?  327 TRP A CB    1 
ATOM   2459  C  CG    . TRP A 1 308 ? 209.809 182.113 155.649 1.00 66.46  ?  327 TRP A CG    1 
ATOM   2460  C  CD1   . TRP A 1 308 ? 208.822 183.009 155.939 1.00 68.37  ?  327 TRP A CD1   1 
ATOM   2461  C  CD2   . TRP A 1 308 ? 210.699 182.778 154.740 1.00 71.82  ?  327 TRP A CD2   1 
ATOM   2462  N  NE1   . TRP A 1 308 ? 209.047 184.193 155.280 1.00 70.53  ?  327 TRP A NE1   1 
ATOM   2463  C  CE2   . TRP A 1 308 ? 210.193 184.077 154.537 1.00 70.89  ?  327 TRP A CE2   1 
ATOM   2464  C  CE3   . TRP A 1 308 ? 211.876 182.404 154.083 1.00 71.66  ?  327 TRP A CE3   1 
ATOM   2465  C  CZ2   . TRP A 1 308 ? 210.821 185.002 153.705 1.00 70.28  ?  327 TRP A CZ2   1 
ATOM   2466  C  CZ3   . TRP A 1 308 ? 212.498 183.324 153.259 1.00 70.00  ?  327 TRP A CZ3   1 
ATOM   2467  C  CH2   . TRP A 1 308 ? 211.969 184.607 153.077 1.00 70.24  ?  327 TRP A CH2   1 
ATOM   2468  N  N     . SER A 1 309 ? 212.427 182.038 158.100 1.00 59.25  ?  328 SER A N     1 
ATOM   2469  C  CA    . SER A 1 309 ? 212.750 182.799 159.298 1.00 60.62  ?  328 SER A CA    1 
ATOM   2470  C  C     . SER A 1 309 ? 212.397 184.261 159.072 1.00 61.94  ?  328 SER A C     1 
ATOM   2471  O  O     . SER A 1 309 ? 212.746 184.835 158.035 1.00 62.87  ?  328 SER A O     1 
ATOM   2472  C  CB    . SER A 1 309 ? 214.230 182.659 159.661 1.00 63.82  ?  328 SER A CB    1 
ATOM   2473  O  OG    . SER A 1 309 ? 215.058 183.209 158.651 1.00 66.50  ?  328 SER A OG    1 
ATOM   2474  N  N     . ALA A 1 310 ? 211.708 184.855 160.041 1.00 62.03  ?  329 ALA A N     1 
ATOM   2475  C  CA    . ALA A 1 310 ? 211.306 186.252 159.988 1.00 58.06  ?  329 ALA A CA    1 
ATOM   2476  C  C     . ALA A 1 310 ? 211.931 186.991 161.161 1.00 57.88  ?  329 ALA A C     1 
ATOM   2477  O  O     . ALA A 1 310 ? 211.898 186.505 162.299 1.00 59.14  ?  329 ALA A O     1 
ATOM   2478  C  CB    . ALA A 1 310 ? 209.782 186.391 160.020 1.00 52.88  ?  329 ALA A CB    1 
ATOM   2479  N  N     . THR A 1 311 ? 212.508 188.156 160.880 1.00 62.36  ?  330 THR A N     1 
ATOM   2480  C  CA    . THR A 1 311 ? 213.124 188.988 161.907 1.00 61.59  ?  330 THR A CA    1 
ATOM   2481  C  C     . THR A 1 311 ? 212.047 189.876 162.519 1.00 63.25  ?  330 THR A C     1 
ATOM   2482  O  O     . THR A 1 311 ? 211.664 190.896 161.936 1.00 67.36  ?  330 THR A O     1 
ATOM   2483  C  CB    . THR A 1 311 ? 214.260 189.824 161.322 1.00 62.46  ?  330 THR A CB    1 
ATOM   2484  O  OG1   . THR A 1 311 ? 213.714 190.916 160.570 1.00 66.14  ?  330 THR A OG1   1 
ATOM   2485  C  CG2   . THR A 1 311 ? 215.135 188.972 160.412 1.00 61.04  ?  330 THR A CG2   1 
ATOM   2486  N  N     . ILE A 1 312 ? 211.554 189.480 163.690 1.00 62.00  ?  331 ILE A N     1 
ATOM   2487  C  CA    . ILE A 1 312 ? 210.582 190.275 164.431 1.00 65.01  ?  331 ILE A CA    1 
ATOM   2488  C  C     . ILE A 1 312 ? 211.266 191.571 164.853 1.00 64.67  ?  331 ILE A C     1 
ATOM   2489  O  O     . ILE A 1 312 ? 212.213 191.551 165.645 1.00 62.29  ?  331 ILE A O     1 
ATOM   2490  C  CB    . ILE A 1 312 ? 210.041 189.511 165.644 1.00 72.10  ?  331 ILE A CB    1 
ATOM   2491  C  CG1   . ILE A 1 312 ? 209.079 188.408 165.198 1.00 71.33  ?  331 ILE A CG1   1 
ATOM   2492  C  CG2   . ILE A 1 312 ? 209.364 190.459 166.613 1.00 68.02  ?  331 ILE A CG2   1 
ATOM   2493  C  CD1   . ILE A 1 312 ? 208.865 187.333 166.233 1.00 67.03  ?  331 ILE A CD1   1 
ATOM   2494  N  N     . ARG A 1 313 ? 210.791 192.692 164.323 1.00 83.98  ?  332 ARG A N     1 
ATOM   2495  C  CA    . ARG A 1 313 ? 211.377 194.002 164.562 1.00 86.35  ?  332 ARG A CA    1 
ATOM   2496  C  C     . ARG A 1 313 ? 210.526 194.801 165.542 1.00 85.69  ?  332 ARG A C     1 
ATOM   2497  O  O     . ARG A 1 313 ? 209.386 194.445 165.849 1.00 86.59  ?  332 ARG A O     1 
ATOM   2498  C  CB    . ARG A 1 313 ? 211.520 194.772 163.247 1.00 84.62  ?  332 ARG A CB    1 
ATOM   2499  C  CG    . ARG A 1 313 ? 212.678 194.311 162.382 1.00 83.61  ?  332 ARG A CG    1 
ATOM   2500  C  CD    . ARG A 1 313 ? 213.005 195.340 161.314 1.00 80.63  ?  332 ARG A CD    1 
ATOM   2501  N  NE    . ARG A 1 313 ? 214.149 194.942 160.504 1.00 85.12  ?  332 ARG A NE    1 
ATOM   2502  C  CZ    . ARG A 1 313 ? 215.414 195.106 160.865 1.00 87.10  ?  332 ARG A CZ    1 
ATOM   2503  N  NH1   . ARG A 1 313 ? 215.737 195.655 162.024 1.00 87.45  1  332 ARG A NH1   1 
ATOM   2504  N  NH2   . ARG A 1 313 ? 216.380 194.709 160.041 1.00 85.36  ?  332 ARG A NH2   1 
ATOM   2505  N  N     . GLN A 1 314 ? 211.101 195.896 166.032 1.00 94.56  ?  333 GLN A N     1 
ATOM   2506  C  CA    . GLN A 1 314 ? 210.396 196.789 166.935 1.00 94.64  ?  333 GLN A CA    1 
ATOM   2507  C  C     . GLN A 1 314 ? 209.633 197.847 166.140 1.00 92.54  ?  333 GLN A C     1 
ATOM   2508  O  O     . GLN A 1 314 ? 209.610 197.842 164.907 1.00 94.49  ?  333 GLN A O     1 
ATOM   2509  C  CB    . GLN A 1 314 ? 211.369 197.432 167.922 1.00 96.76  ?  333 GLN A CB    1 
ATOM   2510  C  CG    . GLN A 1 314 ? 211.805 196.512 169.051 1.00 97.55  ?  333 GLN A CG    1 
ATOM   2511  C  CD    . GLN A 1 314 ? 212.715 197.202 170.048 1.00 97.05  ?  333 GLN A CD    1 
ATOM   2512  O  OE1   . GLN A 1 314 ? 213.738 197.777 169.678 1.00 96.30  ?  333 GLN A OE1   1 
ATOM   2513  N  NE2   . GLN A 1 314 ? 212.345 197.150 171.322 1.00 95.78  ?  333 GLN A NE2   1 
ATOM   2514  N  N     . ARG A 1 315 ? 208.988 198.766 166.863 1.00 99.56  ?  334 ARG A N     1 
ATOM   2515  C  CA    . ARG A 1 315 ? 208.236 199.831 166.205 1.00 103.06 ?  334 ARG A CA    1 
ATOM   2516  C  C     . ARG A 1 315 ? 209.158 200.752 165.416 1.00 104.49 ?  334 ARG A C     1 
ATOM   2517  O  O     . ARG A 1 315 ? 208.826 201.169 164.300 1.00 102.39 ?  334 ARG A O     1 
ATOM   2518  C  CB    . ARG A 1 315 ? 207.439 200.626 167.240 1.00 104.23 ?  334 ARG A CB    1 
ATOM   2519  C  CG    . ARG A 1 315 ? 206.671 201.805 166.663 1.00 103.95 ?  334 ARG A CG    1 
ATOM   2520  C  CD    . ARG A 1 315 ? 205.552 201.336 165.746 1.00 103.89 ?  334 ARG A CD    1 
ATOM   2521  N  NE    . ARG A 1 315 ? 205.898 201.483 164.338 1.00 103.35 ?  334 ARG A NE    1 
ATOM   2522  C  CZ    . ARG A 1 315 ? 205.048 201.310 163.335 1.00 102.29 ?  334 ARG A CZ    1 
ATOM   2523  N  NH1   . ARG A 1 315 ? 203.784 200.983 163.550 1.00 102.20 1  334 ARG A NH1   1 
ATOM   2524  N  NH2   . ARG A 1 315 ? 205.476 201.468 162.086 1.00 101.45 ?  334 ARG A NH2   1 
ATOM   2525  N  N     . ASP A 1 316 ? 210.322 201.078 165.977 1.00 112.49 ?  335 ASP A N     1 
ATOM   2526  C  CA    . ASP A 1 316 ? 211.276 201.955 165.311 1.00 111.14 ?  335 ASP A CA    1 
ATOM   2527  C  C     . ASP A 1 316 ? 212.121 201.236 164.268 1.00 112.04 ?  335 ASP A C     1 
ATOM   2528  O  O     . ASP A 1 316 ? 212.868 201.899 163.540 1.00 111.46 ?  335 ASP A O     1 
ATOM   2529  C  CB    . ASP A 1 316 ? 212.191 202.618 166.345 1.00 110.84 ?  335 ASP A CB    1 
ATOM   2530  C  CG    . ASP A 1 316 ? 212.846 201.614 167.274 1.00 112.37 ?  335 ASP A CG    1 
ATOM   2531  O  OD1   . ASP A 1 316 ? 212.530 200.410 167.172 1.00 112.52 ?  335 ASP A OD1   1 
ATOM   2532  O  OD2   . ASP A 1 316 ? 213.680 202.029 168.107 1.00 112.32 -1 335 ASP A OD2   1 
ATOM   2533  N  N     . GLY A 1 317 ? 212.025 199.912 164.177 1.00 106.49 ?  336 GLY A N     1 
ATOM   2534  C  CA    . GLY A 1 317 ? 212.791 199.137 163.221 1.00 104.22 ?  336 GLY A CA    1 
ATOM   2535  C  C     . GLY A 1 317 ? 213.935 198.348 163.816 1.00 105.92 ?  336 GLY A C     1 
ATOM   2536  O  O     . GLY A 1 317 ? 214.544 197.541 163.101 1.00 107.79 ?  336 GLY A O     1 
ATOM   2537  N  N     . ALA A 1 318 ? 214.257 198.555 165.089 1.00 100.68 ?  337 ALA A N     1 
ATOM   2538  C  CA    . ALA A 1 318 ? 215.318 197.783 165.716 1.00 101.29 ?  337 ALA A CA    1 
ATOM   2539  C  C     . ALA A 1 318 ? 214.889 196.323 165.861 1.00 100.78 ?  337 ALA A C     1 
ATOM   2540  O  O     . ALA A 1 318 ? 213.726 196.045 166.167 1.00 101.41 ?  337 ALA A O     1 
ATOM   2541  C  CB    . ALA A 1 318 ? 215.671 198.364 167.084 1.00 100.97 ?  337 ALA A CB    1 
ATOM   2542  N  N     . PRO A 1 319 ? 215.797 195.373 165.635 1.00 89.07  ?  338 PRO A N     1 
ATOM   2543  C  CA    . PRO A 1 319 ? 215.428 193.958 165.760 1.00 89.94  ?  338 PRO A CA    1 
ATOM   2544  C  C     . PRO A 1 319 ? 215.043 193.600 167.187 1.00 92.19  ?  338 PRO A C     1 
ATOM   2545  O  O     . PRO A 1 319 ? 215.569 194.152 168.156 1.00 92.49  ?  338 PRO A O     1 
ATOM   2546  C  CB    . PRO A 1 319 ? 216.698 193.217 165.321 1.00 91.46  ?  338 PRO A CB    1 
ATOM   2547  C  CG    . PRO A 1 319 ? 217.495 194.228 164.552 1.00 90.90  ?  338 PRO A CG    1 
ATOM   2548  C  CD    . PRO A 1 319 ? 217.188 195.546 165.189 1.00 90.57  ?  338 PRO A CD    1 
ATOM   2549  N  N     . ALA A 1 320 ? 214.109 192.656 167.307 1.00 84.87  ?  339 ALA A N     1 
ATOM   2550  C  CA    . ALA A 1 320 ? 213.633 192.198 168.607 1.00 83.90  ?  339 ALA A CA    1 
ATOM   2551  C  C     . ALA A 1 320 ? 213.593 190.685 168.761 1.00 81.32  ?  339 ALA A C     1 
ATOM   2552  O  O     . ALA A 1 320 ? 213.643 190.204 169.899 1.00 77.18  ?  339 ALA A O     1 
ATOM   2553  C  CB    . ALA A 1 320 ? 212.231 192.756 168.894 1.00 80.49  ?  339 ALA A CB    1 
ATOM   2554  N  N     . GLY A 1 321 ? 213.518 189.922 167.678 1.00 68.59  ?  340 GLY A N     1 
ATOM   2555  C  CA    . GLY A 1 321 ? 213.469 188.479 167.824 1.00 66.49  ?  340 GLY A CA    1 
ATOM   2556  C  C     . GLY A 1 321 ? 213.510 187.782 166.483 1.00 62.79  ?  340 GLY A C     1 
ATOM   2557  O  O     . GLY A 1 321 ? 213.561 188.414 165.427 1.00 64.89  ?  340 GLY A O     1 
ATOM   2558  N  N     . ILE A 1 322 ? 213.475 186.454 166.546 1.00 54.53  ?  341 ILE A N     1 
ATOM   2559  C  CA    . ILE A 1 322 ? 213.497 185.599 165.366 1.00 57.30  ?  341 ILE A CA    1 
ATOM   2560  C  C     . ILE A 1 322 ? 212.351 184.601 165.468 1.00 58.21  ?  341 ILE A C     1 
ATOM   2561  O  O     . ILE A 1 322 ? 212.188 183.937 166.499 1.00 62.45  ?  341 ILE A O     1 
ATOM   2562  C  CB    . ILE A 1 322 ? 214.847 184.869 165.219 1.00 60.36  ?  341 ILE A CB    1 
ATOM   2563  C  CG1   . ILE A 1 322 ? 215.950 185.864 164.850 1.00 58.86  ?  341 ILE A CG1   1 
ATOM   2564  C  CG2   . ILE A 1 322 ? 214.752 183.765 164.176 1.00 60.25  ?  341 ILE A CG2   1 
ATOM   2565  C  CD1   . ILE A 1 322 ? 215.672 186.642 163.579 1.00 59.37  ?  341 ILE A CD1   1 
ATOM   2566  N  N     . LEU A 1 323 ? 211.563 184.492 164.399 1.00 53.30  ?  342 LEU A N     1 
ATOM   2567  C  CA    . LEU A 1 323 ? 210.438 183.564 164.329 1.00 52.96  ?  342 LEU A CA    1 
ATOM   2568  C  C     . LEU A 1 323 ? 210.696 182.600 163.178 1.00 54.42  ?  342 LEU A C     1 
ATOM   2569  O  O     . LEU A 1 323 ? 210.693 183.009 162.012 1.00 62.43  ?  342 LEU A O     1 
ATOM   2570  C  CB    . LEU A 1 323 ? 209.125 184.326 164.144 1.00 53.04  ?  342 LEU A CB    1 
ATOM   2571  C  CG    . LEU A 1 323 ? 207.794 183.579 164.228 1.00 56.25  ?  342 LEU A CG    1 
ATOM   2572  C  CD1   . LEU A 1 323 ? 206.742 184.460 164.874 1.00 53.80  ?  342 LEU A CD1   1 
ATOM   2573  C  CD2   . LEU A 1 323 ? 207.341 183.170 162.842 1.00 59.29  ?  342 LEU A CD2   1 
ATOM   2574  N  N     . GLN A 1 324 ? 210.921 181.326 163.497 1.00 49.34  ?  343 GLN A N     1 
ATOM   2575  C  CA    . GLN A 1 324 ? 211.335 180.333 162.516 1.00 53.21  ?  343 GLN A CA    1 
ATOM   2576  C  C     . GLN A 1 324 ? 210.257 179.267 162.383 1.00 58.24  ?  343 GLN A C     1 
ATOM   2577  O  O     . GLN A 1 324 ? 209.814 178.698 163.386 1.00 65.20  ?  343 GLN A O     1 
ATOM   2578  C  CB    . GLN A 1 324 ? 212.671 179.703 162.921 1.00 62.44  ?  343 GLN A CB    1 
ATOM   2579  C  CG    . GLN A 1 324 ? 213.301 178.807 161.872 1.00 68.99  ?  343 GLN A CG    1 
ATOM   2580  C  CD    . GLN A 1 324 ? 214.765 178.530 162.158 1.00 69.82  ?  343 GLN A CD    1 
ATOM   2581  O  OE1   . GLN A 1 324 ? 215.337 179.068 163.107 1.00 69.45  ?  343 GLN A OE1   1 
ATOM   2582  N  NE2   . GLN A 1 324 ? 215.381 177.690 161.335 1.00 66.03  ?  343 GLN A NE2   1 
ATOM   2583  N  N     . ILE A 1 325 ? 209.832 179.002 161.150 1.00 71.41  ?  344 ILE A N     1 
ATOM   2584  C  CA    . ILE A 1 325 ? 208.819 177.993 160.861 1.00 74.44  ?  344 ILE A CA    1 
ATOM   2585  C  C     . ILE A 1 325 ? 209.409 177.016 159.856 1.00 77.94  ?  344 ILE A C     1 
ATOM   2586  O  O     . ILE A 1 325 ? 209.739 177.404 158.729 1.00 80.62  ?  344 ILE A O     1 
ATOM   2587  C  CB    . ILE A 1 325 ? 207.524 178.616 160.312 1.00 72.53  ?  344 ILE A CB    1 
ATOM   2588  C  CG1   . ILE A 1 325 ? 207.166 179.894 161.074 1.00 72.65  ?  344 ILE A CG1   1 
ATOM   2589  C  CG2   . ILE A 1 325 ? 206.380 177.616 160.386 1.00 72.34  ?  344 ILE A CG2   1 
ATOM   2590  C  CD1   . ILE A 1 325 ? 206.802 179.664 162.519 1.00 75.54  ?  344 ILE A CD1   1 
ATOM   2591  N  N     . LYS A 1 326 ? 209.545 175.755 160.258 1.00 84.67  ?  345 LYS A N     1 
ATOM   2592  C  CA    . LYS A 1 326 ? 210.016 174.695 159.379 1.00 78.90  ?  345 LYS A CA    1 
ATOM   2593  C  C     . LYS A 1 326 ? 208.835 173.815 159.000 1.00 85.11  ?  345 LYS A C     1 
ATOM   2594  O  O     . LYS A 1 326 ? 208.078 173.373 159.872 1.00 82.16  ?  345 LYS A O     1 
ATOM   2595  C  CB    . LYS A 1 326 ? 211.113 173.866 160.052 1.00 82.64  ?  345 LYS A CB    1 
ATOM   2596  C  CG    . LYS A 1 326 ? 211.580 172.670 159.235 1.00 88.08  ?  345 LYS A CG    1 
ATOM   2597  C  CD    . LYS A 1 326 ? 212.389 171.698 160.081 1.00 86.91  ?  345 LYS A CD    1 
ATOM   2598  C  CE    . LYS A 1 326 ? 211.520 171.015 161.121 1.00 86.67  ?  345 LYS A CE    1 
ATOM   2599  N  NZ    . LYS A 1 326 ? 211.926 169.601 161.342 1.00 85.59  1  345 LYS A NZ    1 
ATOM   2600  N  N     . THR A 1 327 ? 208.671 173.566 157.703 1.00 107.16 ?  346 THR A N     1 
ATOM   2601  C  CA    . THR A 1 327 ? 207.517 172.811 157.240 1.00 108.03 ?  346 THR A CA    1 
ATOM   2602  C  C     . THR A 1 327 ? 207.864 172.074 155.955 1.00 107.83 ?  346 THR A C     1 
ATOM   2603  O  O     . THR A 1 327 ? 208.824 172.410 155.258 1.00 105.50 ?  346 THR A O     1 
ATOM   2604  C  CB    . THR A 1 327 ? 206.300 173.719 157.018 1.00 106.60 ?  346 THR A CB    1 
ATOM   2605  O  OG1   . THR A 1 327 ? 205.178 172.925 156.611 1.00 105.85 ?  346 THR A OG1   1 
ATOM   2606  C  CG2   . THR A 1 327 ? 206.595 174.756 155.945 1.00 103.92 ?  346 THR A CG2   1 
ATOM   2607  N  N     . SER A 1 328 ? 207.059 171.057 155.654 1.00 111.28 ?  347 SER A N     1 
ATOM   2608  C  CA    . SER A 1 328 ? 207.252 170.274 154.441 1.00 110.80 ?  347 SER A CA    1 
ATOM   2609  C  C     . SER A 1 328 ? 207.106 171.159 153.210 1.00 111.12 ?  347 SER A C     1 
ATOM   2610  O  O     . SER A 1 328 ? 206.166 171.952 153.107 1.00 111.86 ?  347 SER A O     1 
ATOM   2611  C  CB    . SER A 1 328 ? 206.243 169.127 154.388 1.00 109.61 ?  347 SER A CB    1 
ATOM   2612  O  OG    . SER A 1 328 ? 206.403 168.249 155.487 1.00 109.10 ?  347 SER A OG    1 
ATOM   2613  N  N     . SER A 1 329 ? 208.041 171.020 152.275 1.00 112.89 ?  348 SER A N     1 
ATOM   2614  C  CA    . SER A 1 329 ? 207.992 171.787 151.038 1.00 112.09 ?  348 SER A CA    1 
ATOM   2615  C  C     . SER A 1 329 ? 206.939 171.197 150.109 1.00 113.88 ?  348 SER A C     1 
ATOM   2616  O  O     . SER A 1 329 ? 206.989 170.010 149.772 1.00 114.24 ?  348 SER A O     1 
ATOM   2617  C  CB    . SER A 1 329 ? 209.361 171.795 150.360 1.00 112.53 ?  348 SER A CB    1 
ATOM   2618  O  OG    . SER A 1 329 ? 209.861 170.478 150.206 1.00 114.51 ?  348 SER A OG    1 
ATOM   2619  N  N     . GLY A 1 330 ? 205.987 172.031 149.696 1.00 115.08 ?  349 GLY A N     1 
ATOM   2620  C  CA    . GLY A 1 330 ? 204.892 171.615 148.852 1.00 114.68 ?  349 GLY A CA    1 
ATOM   2621  C  C     . GLY A 1 330 ? 203.622 171.259 149.597 1.00 115.86 ?  349 GLY A C     1 
ATOM   2622  O  O     . GLY A 1 330 ? 202.549 171.231 148.984 1.00 115.19 ?  349 GLY A O     1 
ATOM   2623  N  N     . ALA A 1 331 ? 203.714 170.984 150.901 1.00 111.74 ?  350 ALA A N     1 
ATOM   2624  C  CA    . ALA A 1 331 ? 202.513 170.699 151.679 1.00 110.17 ?  350 ALA A CA    1 
ATOM   2625  C  C     . ALA A 1 331 ? 201.690 171.962 151.903 1.00 109.59 ?  350 ALA A C     1 
ATOM   2626  O  O     . ALA A 1 331 ? 200.459 171.937 151.787 1.00 109.59 ?  350 ALA A O     1 
ATOM   2627  C  CB    . ALA A 1 331 ? 202.890 170.057 153.014 1.00 108.29 ?  350 ALA A CB    1 
ATOM   2628  N  N     . GLU A 1 332 ? 202.351 173.071 152.224 1.00 93.23  ?  351 GLU A N     1 
ATOM   2629  C  CA    . GLU A 1 332 ? 201.697 174.359 152.401 1.00 91.38  ?  351 GLU A CA    1 
ATOM   2630  C  C     . GLU A 1 332 ? 202.388 175.387 151.519 1.00 90.73  ?  351 GLU A C     1 
ATOM   2631  O  O     . GLU A 1 332 ? 203.618 175.395 151.410 1.00 90.91  ?  351 GLU A O     1 
ATOM   2632  C  CB    . GLU A 1 332 ? 201.728 174.807 153.868 1.00 93.69  ?  351 GLU A CB    1 
ATOM   2633  C  CG    . GLU A 1 332 ? 200.986 173.874 154.813 1.00 95.37  ?  351 GLU A CG    1 
ATOM   2634  C  CD    . GLU A 1 332 ? 199.497 173.811 154.528 1.00 95.71  ?  351 GLU A CD    1 
ATOM   2635  O  OE1   . GLU A 1 332 ? 198.927 174.836 154.097 1.00 95.48  ?  351 GLU A OE1   1 
ATOM   2636  O  OE2   . GLU A 1 332 ? 198.897 172.735 154.731 1.00 95.96  -1 351 GLU A OE2   1 
ATOM   2637  N  N     . THR A 1 333 ? 201.593 176.249 150.889 1.00 83.75  ?  352 THR A N     1 
ATOM   2638  C  CA    . THR A 1 333 ? 202.131 177.173 149.900 1.00 85.15  ?  352 THR A CA    1 
ATOM   2639  C  C     . THR A 1 333 ? 203.025 178.224 150.552 1.00 83.76  ?  352 THR A C     1 
ATOM   2640  O  O     . THR A 1 333 ? 202.765 178.702 151.662 1.00 84.58  ?  352 THR A O     1 
ATOM   2641  C  CB    . THR A 1 333 ? 200.999 177.851 149.126 1.00 86.15  ?  352 THR A CB    1 
ATOM   2642  O  OG1   . THR A 1 333 ? 200.181 178.603 150.028 1.00 83.89  ?  352 THR A OG1   1 
ATOM   2643  C  CG2   . THR A 1 333 ? 200.142 176.811 148.419 1.00 84.44  ?  352 THR A CG2   1 
ATOM   2644  N  N     . SER A 1 334 ? 204.087 178.589 149.828 1.00 79.48  ?  353 SER A N     1 
ATOM   2645  C  CA    . SER A 1 334 ? 205.088 179.506 150.363 1.00 78.77  ?  353 SER A CA    1 
ATOM   2646  C  C     . SER A 1 334 ? 204.495 180.878 150.654 1.00 79.96  ?  353 SER A C     1 
ATOM   2647  O  O     . SER A 1 334 ? 204.843 181.504 151.659 1.00 82.13  ?  353 SER A O     1 
ATOM   2648  C  CB    . SER A 1 334 ? 206.263 179.624 149.392 1.00 78.89  ?  353 SER A CB    1 
ATOM   2649  O  OG    . SER A 1 334 ? 207.248 180.512 149.891 1.00 77.94  ?  353 SER A OG    1 
ATOM   2650  N  N     . ALA A 1 335 ? 203.613 181.373 149.781 1.00 79.11  ?  354 ALA A N     1 
ATOM   2651  C  CA    . ALA A 1 335 ? 202.995 182.676 150.016 1.00 78.44  ?  354 ALA A CA    1 
ATOM   2652  C  C     . ALA A 1 335 ? 202.132 182.660 151.272 1.00 78.07  ?  354 ALA A C     1 
ATOM   2653  O  O     . ALA A 1 335 ? 202.108 183.636 152.035 1.00 74.37  ?  354 ALA A O     1 
ATOM   2654  C  CB    . ALA A 1 335 ? 202.167 183.091 148.800 1.00 75.83  ?  354 ALA A CB    1 
ATOM   2655  N  N     . PHE A 1 336 ? 201.405 181.564 151.497 1.00 72.77  ?  355 PHE A N     1 
ATOM   2656  C  CA    . PHE A 1 336 ? 200.637 181.435 152.729 1.00 69.40  ?  355 PHE A CA    1 
ATOM   2657  C  C     . PHE A 1 336 ? 201.557 181.406 153.941 1.00 71.25  ?  355 PHE A C     1 
ATOM   2658  O  O     . PHE A 1 336 ? 201.245 182.000 154.981 1.00 76.41  ?  355 PHE A O     1 
ATOM   2659  C  CB    . PHE A 1 336 ? 199.768 180.180 152.682 1.00 66.44  ?  355 PHE A CB    1 
ATOM   2660  C  CG    . PHE A 1 336 ? 198.804 180.073 153.824 1.00 68.03  ?  355 PHE A CG    1 
ATOM   2661  C  CD1   . PHE A 1 336 ? 197.974 181.134 154.144 1.00 70.09  ?  355 PHE A CD1   1 
ATOM   2662  C  CD2   . PHE A 1 336 ? 198.726 178.915 154.577 1.00 68.04  ?  355 PHE A CD2   1 
ATOM   2663  C  CE1   . PHE A 1 336 ? 197.084 181.044 155.194 1.00 70.78  ?  355 PHE A CE1   1 
ATOM   2664  C  CE2   . PHE A 1 336 ? 197.837 178.818 155.629 1.00 68.03  ?  355 PHE A CE2   1 
ATOM   2665  C  CZ    . PHE A 1 336 ? 197.014 179.884 155.936 1.00 70.06  ?  355 PHE A CZ    1 
ATOM   2666  N  N     . ILE A 1 337 ? 202.695 180.713 153.828 1.00 71.12  ?  356 ILE A N     1 
ATOM   2667  C  CA    . ILE A 1 337 ? 203.682 180.741 154.905 1.00 68.65  ?  356 ILE A CA    1 
ATOM   2668  C  C     . ILE A 1 337 ? 204.137 182.171 155.165 1.00 65.56  ?  356 ILE A C     1 
ATOM   2669  O  O     . ILE A 1 337 ? 204.271 182.594 156.318 1.00 64.33  ?  356 ILE A O     1 
ATOM   2670  C  CB    . ILE A 1 337 ? 204.874 179.821 154.576 1.00 75.03  ?  356 ILE A CB    1 
ATOM   2671  C  CG1   . ILE A 1 337 ? 204.398 178.397 154.281 1.00 72.29  ?  356 ILE A CG1   1 
ATOM   2672  C  CG2   . ILE A 1 337 ? 205.878 179.816 155.720 1.00 74.41  ?  356 ILE A CG2   1 
ATOM   2673  C  CD1   . ILE A 1 337 ? 203.491 177.822 155.339 1.00 70.36  ?  356 ILE A CD1   1 
ATOM   2674  N  N     . GLU A 1 338 ? 204.372 182.938 154.096 1.00 68.92  ?  357 GLU A N     1 
ATOM   2675  C  CA    . GLU A 1 338 ? 204.797 184.328 154.243 1.00 71.21  ?  357 GLU A CA    1 
ATOM   2676  C  C     . GLU A 1 338 ? 203.757 185.144 155.000 1.00 74.32  ?  357 GLU A C     1 
ATOM   2677  O  O     . GLU A 1 338 ? 204.090 185.887 155.930 1.00 75.21  ?  357 GLU A O     1 
ATOM   2678  C  CB    . GLU A 1 338 ? 205.053 184.959 152.872 1.00 70.93  ?  357 GLU A CB    1 
ATOM   2679  C  CG    . GLU A 1 338 ? 206.085 184.259 152.009 1.00 71.69  ?  357 GLU A CG    1 
ATOM   2680  C  CD    . GLU A 1 338 ? 207.502 184.473 152.491 1.00 74.73  ?  357 GLU A CD    1 
ATOM   2681  O  OE1   . GLU A 1 338 ? 207.769 185.520 153.117 1.00 74.12  ?  357 GLU A OE1   1 
ATOM   2682  O  OE2   . GLU A 1 338 ? 208.351 183.594 152.233 1.00 74.09  -1 357 GLU A OE2   1 
ATOM   2683  N  N     . ARG A 1 339 ? 202.488 185.025 154.605 1.00 66.57  ?  358 ARG A N     1 
ATOM   2684  C  CA    . ARG A 1 339 ? 201.444 185.828 155.239 1.00 61.35  ?  358 ARG A CA    1 
ATOM   2685  C  C     . ARG A 1 339 ? 201.251 185.438 156.702 1.00 58.12  ?  358 ARG A C     1 
ATOM   2686  O  O     . ARG A 1 339 ? 201.123 186.311 157.575 1.00 62.79  ?  358 ARG A O     1 
ATOM   2687  C  CB    . ARG A 1 339 ? 200.130 185.692 154.471 1.00 61.68  ?  358 ARG A CB    1 
ATOM   2688  C  CG    . ARG A 1 339 ? 199.137 186.804 154.769 1.00 60.18  ?  358 ARG A CG    1 
ATOM   2689  C  CD    . ARG A 1 339 ? 197.759 186.505 154.205 1.00 59.17  ?  358 ARG A CD    1 
ATOM   2690  N  NE    . ARG A 1 339 ? 196.713 187.166 154.977 1.00 56.82  ?  358 ARG A NE    1 
ATOM   2691  C  CZ    . ARG A 1 339 ? 195.416 186.929 154.843 1.00 62.79  ?  358 ARG A CZ    1 
ATOM   2692  N  NH1   . ARG A 1 339 ? 194.962 186.041 153.974 1.00 62.25  1  358 ARG A NH1   1 
ATOM   2693  N  NH2   . ARG A 1 339 ? 194.553 187.600 155.600 1.00 62.64  ?  358 ARG A NH2   1 
ATOM   2694  N  N     . VAL A 1 340 ? 201.230 184.133 156.988 1.00 47.81  ?  359 VAL A N     1 
ATOM   2695  C  CA    . VAL A 1 340 ? 201.081 183.673 158.366 1.00 50.08  ?  359 VAL A CA    1 
ATOM   2696  C  C     . VAL A 1 340 ? 202.252 184.157 159.209 1.00 55.50  ?  359 VAL A C     1 
ATOM   2697  O  O     . VAL A 1 340 ? 202.075 184.644 160.334 1.00 63.11  ?  359 VAL A O     1 
ATOM   2698  C  CB    . VAL A 1 340 ? 200.949 182.139 158.410 1.00 50.37  ?  359 VAL A CB    1 
ATOM   2699  C  CG1   . VAL A 1 340 ? 200.960 181.642 159.845 1.00 47.72  ?  359 VAL A CG1   1 
ATOM   2700  C  CG2   . VAL A 1 340 ? 199.683 181.689 157.700 1.00 55.70  ?  359 VAL A CG2   1 
ATOM   2701  N  N     . ALA A 1 341 ? 203.470 184.039 158.672 1.00 57.53  ?  360 ALA A N     1 
ATOM   2702  C  CA    . ALA A 1 341 ? 204.655 184.462 159.406 1.00 53.69  ?  360 ALA A CA    1 
ATOM   2703  C  C     . ALA A 1 341 ? 204.652 185.965 159.642 1.00 53.10  ?  360 ALA A C     1 
ATOM   2704  O  O     . ALA A 1 341 ? 205.081 186.426 160.699 1.00 59.51  ?  360 ALA A O     1 
ATOM   2705  C  CB    . ALA A 1 341 ? 205.918 184.037 158.658 1.00 57.33  ?  360 ALA A CB    1 
ATOM   2706  N  N     . ASP A 1 342 ? 204.155 186.746 158.681 1.00 54.17  ?  361 ASP A N     1 
ATOM   2707  C  CA    . ASP A 1 342 ? 204.116 188.196 158.854 1.00 58.66  ?  361 ASP A CA    1 
ATOM   2708  C  C     . ASP A 1 342 ? 203.110 188.601 159.927 1.00 63.41  ?  361 ASP A C     1 
ATOM   2709  O  O     . ASP A 1 342 ? 203.403 189.450 160.783 1.00 58.88  ?  361 ASP A O     1 
ATOM   2710  C  CB    . ASP A 1 342 ? 203.785 188.873 157.523 1.00 58.79  ?  361 ASP A CB    1 
ATOM   2711  C  CG    . ASP A 1 342 ? 203.891 190.384 157.596 1.00 64.04  ?  361 ASP A CG    1 
ATOM   2712  O  OD1   . ASP A 1 342 ? 204.682 190.886 158.421 1.00 63.45  ?  361 ASP A OD1   1 
ATOM   2713  O  OD2   . ASP A 1 342 ? 203.182 191.069 156.829 1.00 63.80  -1 361 ASP A OD2   1 
ATOM   2714  N  N     . ILE A 1 343 ? 201.910 188.014 159.894 1.00 59.97  ?  362 ILE A N     1 
ATOM   2715  C  CA    . ILE A 1 343 ? 200.904 188.347 160.902 1.00 48.76  ?  362 ILE A CA    1 
ATOM   2716  C  C     . ILE A 1 343 ? 201.386 187.930 162.289 1.00 45.89  ?  362 ILE A C     1 
ATOM   2717  O  O     . ILE A 1 343 ? 201.289 188.694 163.262 1.00 53.91  ?  362 ILE A O     1 
ATOM   2718  C  CB    . ILE A 1 343 ? 199.553 187.698 160.550 1.00 43.99  ?  362 ILE A CB    1 
ATOM   2719  C  CG1   . ILE A 1 343 ? 198.993 188.303 159.262 1.00 49.26  ?  362 ILE A CG1   1 
ATOM   2720  C  CG2   . ILE A 1 343 ? 198.566 187.870 161.694 1.00 48.45  ?  362 ILE A CG2   1 
ATOM   2721  C  CD1   . ILE A 1 343 ? 198.904 189.813 159.281 1.00 50.93  ?  362 ILE A CD1   1 
ATOM   2722  N  N     . SER A 1 344 ? 201.924 186.711 162.398 1.00 41.44  ?  363 SER A N     1 
ATOM   2723  C  CA    . SER A 1 344 ? 202.473 186.262 163.671 1.00 45.69  ?  363 SER A CA    1 
ATOM   2724  C  C     . SER A 1 344 ? 203.667 187.108 164.088 1.00 56.79  ?  363 SER A C     1 
ATOM   2725  O  O     . SER A 1 344 ? 203.906 187.293 165.284 1.00 58.87  ?  363 SER A O     1 
ATOM   2726  C  CB    . SER A 1 344 ? 202.862 184.787 163.581 1.00 52.43  ?  363 SER A CB    1 
ATOM   2727  O  OG    . SER A 1 344 ? 201.822 184.026 162.991 1.00 57.09  ?  363 SER A OG    1 
ATOM   2728  N  N     . GLN A 1 345 ? 204.422 187.635 163.120 1.00 62.14  ?  364 GLN A N     1 
ATOM   2729  C  CA    . GLN A 1 345 ? 205.534 188.521 163.432 1.00 54.70  ?  364 GLN A CA    1 
ATOM   2730  C  C     . GLN A 1 345 ? 205.042 189.805 164.074 1.00 52.63  ?  364 GLN A C     1 
ATOM   2731  O  O     . GLN A 1 345 ? 205.620 190.270 165.057 1.00 54.81  ?  364 GLN A O     1 
ATOM   2732  C  CB    . GLN A 1 345 ? 206.330 188.827 162.161 1.00 55.36  ?  364 GLN A CB    1 
ATOM   2733  C  CG    . GLN A 1 345 ? 207.463 189.826 162.354 1.00 60.79  ?  364 GLN A CG    1 
ATOM   2734  C  CD    . GLN A 1 345 ? 207.091 191.230 161.918 1.00 65.50  ?  364 GLN A CD    1 
ATOM   2735  O  OE1   . GLN A 1 345 ? 206.650 191.447 160.789 1.00 66.50  ?  364 GLN A OE1   1 
ATOM   2736  N  NE2   . GLN A 1 345 ? 207.267 192.194 162.815 1.00 61.17  ?  364 GLN A NE2   1 
ATOM   2737  N  N     . HIS A 1 346 ? 203.969 190.387 163.538 1.00 49.24  ?  365 HIS A N     1 
ATOM   2738  C  CA    . HIS A 1 346 ? 203.399 191.582 164.160 1.00 50.61  ?  365 HIS A CA    1 
ATOM   2739  C  C     . HIS A 1 346 ? 202.884 191.277 165.565 1.00 49.22  ?  365 HIS A C     1 
ATOM   2740  O  O     . HIS A 1 346 ? 203.125 192.041 166.516 1.00 49.50  ?  365 HIS A O     1 
ATOM   2741  C  CB    . HIS A 1 346 ? 202.281 192.150 163.286 1.00 46.80  ?  365 HIS A CB    1 
ATOM   2742  C  CG    . HIS A 1 346 ? 202.727 193.260 162.386 1.00 46.98  ?  365 HIS A CG    1 
ATOM   2743  N  ND1   . HIS A 1 346 ? 203.047 194.514 162.859 1.00 51.50  ?  365 HIS A ND1   1 
ATOM   2744  C  CD2   . HIS A 1 346 ? 202.908 193.306 161.045 1.00 46.38  ?  365 HIS A CD2   1 
ATOM   2745  C  CE1   . HIS A 1 346 ? 203.405 195.285 161.848 1.00 52.95  ?  365 HIS A CE1   1 
ATOM   2746  N  NE2   . HIS A 1 346 ? 203.329 194.576 160.736 1.00 46.77  ?  365 HIS A NE2   1 
ATOM   2747  N  N     . MET A 1 347 ? 202.172 190.155 165.715 1.00 52.59  ?  366 MET A N     1 
ATOM   2748  C  CA    . MET A 1 347 ? 201.634 189.788 167.023 1.00 44.55  ?  366 MET A CA    1 
ATOM   2749  C  C     . MET A 1 347 ? 202.752 189.613 168.045 1.00 43.80  ?  366 MET A C     1 
ATOM   2750  O  O     . MET A 1 347 ? 202.737 190.225 169.123 1.00 50.13  ?  366 MET A O     1 
ATOM   2751  C  CB    . MET A 1 347 ? 200.823 188.498 166.909 1.00 53.01  ?  366 MET A CB    1 
ATOM   2752  C  CG    . MET A 1 347 ? 199.584 188.607 166.053 1.00 48.94  ?  366 MET A CG    1 
ATOM   2753  S  SD    . MET A 1 347 ? 198.371 189.751 166.722 1.00 61.81  ?  366 MET A SD    1 
ATOM   2754  C  CE    . MET A 1 347 ? 197.175 189.726 165.397 1.00 50.30  ?  366 MET A CE    1 
ATOM   2755  N  N     . ALA A 1 348 ? 203.743 188.785 167.709 1.00 46.24  ?  367 ALA A N     1 
ATOM   2756  C  CA    . ALA A 1 348 ? 204.853 188.534 168.613 1.00 54.80  ?  367 ALA A CA    1 
ATOM   2757  C  C     . ALA A 1 348 ? 205.708 189.776 168.803 1.00 57.87  ?  367 ALA A C     1 
ATOM   2758  O  O     . ALA A 1 348 ? 206.339 189.927 169.847 1.00 57.77  ?  367 ALA A O     1 
ATOM   2759  C  CB    . ALA A 1 348 ? 205.701 187.374 168.095 1.00 56.43  ?  367 ALA A CB    1 
ATOM   2760  N  N     . ALA A 1 349 ? 205.725 190.684 167.825 1.00 58.44  ?  368 ALA A N     1 
ATOM   2761  C  CA    . ALA A 1 349 ? 206.445 191.938 167.994 1.00 56.44  ?  368 ALA A CA    1 
ATOM   2762  C  C     . ALA A 1 349 ? 205.821 192.775 169.095 1.00 49.34  ?  368 ALA A C     1 
ATOM   2763  O  O     . ALA A 1 349 ? 206.524 193.269 169.985 1.00 51.08  ?  368 ALA A O     1 
ATOM   2764  C  CB    . ALA A 1 349 ? 206.470 192.710 166.674 1.00 55.74  ?  368 ALA A CB    1 
ATOM   2765  N  N     . LEU A 1 350 ? 204.496 192.943 169.055 1.00 49.06  ?  369 LEU A N     1 
ATOM   2766  C  CA    . LEU A 1 350 ? 203.851 193.699 170.125 1.00 48.49  ?  369 LEU A CA    1 
ATOM   2767  C  C     . LEU A 1 350 ? 204.008 192.988 171.464 1.00 49.15  ?  369 LEU A C     1 
ATOM   2768  O  O     . LEU A 1 350 ? 204.250 193.634 172.494 1.00 56.70  ?  369 LEU A O     1 
ATOM   2769  C  CB    . LEU A 1 350 ? 202.377 193.951 169.809 1.00 53.19  ?  369 LEU A CB    1 
ATOM   2770  C  CG    . LEU A 1 350 ? 201.787 195.067 170.680 1.00 56.50  ?  369 LEU A CG    1 
ATOM   2771  C  CD1   . LEU A 1 350 ? 200.786 195.859 169.889 1.00 52.64  ?  369 LEU A CD1   1 
ATOM   2772  C  CD2   . LEU A 1 350 ? 201.133 194.536 171.955 1.00 52.48  ?  369 LEU A CD2   1 
ATOM   2773  N  N     . ALA A 1 351 ? 203.881 191.658 171.466 1.00 50.74  ?  370 ALA A N     1 
ATOM   2774  C  CA    . ALA A 1 351 ? 204.114 190.902 172.693 1.00 50.07  ?  370 ALA A CA    1 
ATOM   2775  C  C     . ALA A 1 351 ? 205.525 191.139 173.220 1.00 60.16  ?  370 ALA A C     1 
ATOM   2776  O  O     . ALA A 1 351 ? 205.735 191.242 174.434 1.00 62.89  ?  370 ALA A O     1 
ATOM   2777  C  CB    . ALA A 1 351 ? 203.871 189.412 172.449 1.00 49.66  ?  370 ALA A CB    1 
ATOM   2778  N  N     . LEU A 1 352 ? 206.501 191.256 172.317 1.00 63.69  ?  371 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 352 ? 207.886 191.434 172.730 1.00 57.26  ?  371 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 352 ? 208.141 192.839 173.258 1.00 57.57  ?  371 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 352 ? 208.914 193.007 174.204 1.00 58.85  ?  371 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 352 ? 208.832 191.110 171.574 1.00 59.85  ?  371 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 352 ? 209.071 189.614 171.351 1.00 62.93  ?  371 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 352 ? 209.875 189.374 170.086 1.00 62.28  ?  371 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 352 ? 209.758 188.998 172.556 1.00 62.00  ?  371 LEU A CD2   1 
ATOM   2786  N  N     . GLU A 1 353 ? 207.521 193.866 172.665 1.00 64.09  ?  372 GLU A N     1 
ATOM   2787  C  CA    . GLU A 1 353 ? 207.669 195.190 173.270 1.00 62.70  ?  372 GLU A CA    1 
ATOM   2788  C  C     . GLU A 1 353 ? 207.012 195.239 174.643 1.00 59.38  ?  372 GLU A C     1 
ATOM   2789  O  O     . GLU A 1 353 ? 207.548 195.861 175.570 1.00 63.39  ?  372 GLU A O     1 
ATOM   2790  C  CB    . GLU A 1 353 ? 207.121 196.323 172.394 1.00 66.22  ?  372 GLU A CB    1 
ATOM   2791  C  CG    . GLU A 1 353 ? 207.930 196.647 171.144 1.00 69.21  ?  372 GLU A CG    1 
ATOM   2792  C  CD    . GLU A 1 353 ? 207.301 196.131 169.877 1.00 70.51  ?  372 GLU A CD    1 
ATOM   2793  O  OE1   . GLU A 1 353 ? 206.103 195.796 169.913 1.00 70.04  ?  372 GLU A OE1   1 
ATOM   2794  O  OE2   . GLU A 1 353 ? 207.997 196.062 168.845 1.00 71.94  -1 372 GLU A OE2   1 
ATOM   2795  N  N     . GLN A 1 354 ? 205.855 194.587 174.800 1.00 61.59  ?  373 GLN A N     1 
ATOM   2796  C  CA    . GLN A 1 354 ? 205.232 194.528 176.119 1.00 64.06  ?  373 GLN A CA    1 
ATOM   2797  C  C     . GLN A 1 354 ? 206.137 193.823 177.123 1.00 62.61  ?  373 GLN A C     1 
ATOM   2798  O  O     . GLN A 1 354 ? 206.316 194.295 178.254 1.00 68.14  ?  373 GLN A O     1 
ATOM   2799  C  CB    . GLN A 1 354 ? 203.879 193.825 176.030 1.00 61.10  ?  373 GLN A CB    1 
ATOM   2800  C  CG    . GLN A 1 354 ? 202.835 194.382 176.983 1.00 58.60  ?  373 GLN A CG    1 
ATOM   2801  C  CD    . GLN A 1 354 ? 201.422 194.009 176.585 1.00 62.81  ?  373 GLN A CD    1 
ATOM   2802  O  OE1   . GLN A 1 354 ? 201.177 193.559 175.465 1.00 66.55  ?  373 GLN A OE1   1 
ATOM   2803  N  NE2   . GLN A 1 354 ? 200.482 194.195 177.504 1.00 63.96  ?  373 GLN A NE2   1 
ATOM   2804  N  N     . GLU A 1 355 ? 206.735 192.701 176.720 1.00 60.26  ?  374 GLU A N     1 
ATOM   2805  C  CA    . GLU A 1 355 ? 207.632 191.976 177.612 1.00 65.69  ?  374 GLU A CA    1 
ATOM   2806  C  C     . GLU A 1 355 ? 208.882 192.786 177.929 1.00 70.12  ?  374 GLU A C     1 
ATOM   2807  O  O     . GLU A 1 355 ? 209.375 192.748 179.058 1.00 73.55  ?  374 GLU A O     1 
ATOM   2808  C  CB    . GLU A 1 355 ? 208.004 190.624 177.001 1.00 69.55  ?  374 GLU A CB    1 
ATOM   2809  C  CG    . GLU A 1 355 ? 208.588 189.641 178.001 1.00 69.02  ?  374 GLU A CG    1 
ATOM   2810  C  CD    . GLU A 1 355 ? 207.582 189.190 179.043 1.00 71.90  ?  374 GLU A CD    1 
ATOM   2811  O  OE1   . GLU A 1 355 ? 208.011 188.686 180.103 1.00 72.21  ?  374 GLU A OE1   1 
ATOM   2812  O  OE2   . GLU A 1 355 ? 206.364 189.330 178.804 1.00 72.58  -1 374 GLU A OE2   1 
ATOM   2813  N  N     . LYS A 1 356 ? 209.418 193.512 176.946 1.00 67.34  ?  375 LYS A N     1 
ATOM   2814  C  CA    . LYS A 1 356 ? 210.593 194.342 177.190 1.00 65.90  ?  375 LYS A CA    1 
ATOM   2815  C  C     . LYS A 1 356 ? 210.276 195.468 178.164 1.00 63.34  ?  375 LYS A C     1 
ATOM   2816  O  O     . LYS A 1 356 ? 211.092 195.794 179.033 1.00 70.18  ?  375 LYS A O     1 
ATOM   2817  C  CB    . LYS A 1 356 ? 211.121 194.904 175.870 1.00 71.86  ?  375 LYS A CB    1 
ATOM   2818  C  CG    . LYS A 1 356 ? 212.468 195.607 175.973 1.00 72.88  ?  375 LYS A CG    1 
ATOM   2819  C  CD    . LYS A 1 356 ? 213.426 194.843 176.873 1.00 71.73  ?  375 LYS A CD    1 
ATOM   2820  C  CE    . LYS A 1 356 ? 214.633 195.687 177.243 1.00 70.35  ?  375 LYS A CE    1 
ATOM   2821  N  NZ    . LYS A 1 356 ? 214.247 196.904 178.006 1.00 70.88  1  375 LYS A NZ    1 
ATOM   2822  N  N     . SER A 1 357 ? 209.096 196.078 178.029 1.00 59.53  ?  376 SER A N     1 
ATOM   2823  C  CA    . SER A 1 357 ? 208.672 197.083 178.996 1.00 65.02  ?  376 SER A CA    1 
ATOM   2824  C  C     . SER A 1 357 ? 208.536 196.476 180.386 1.00 64.22  ?  376 SER A C     1 
ATOM   2825  O  O     . SER A 1 357 ? 208.908 197.102 181.386 1.00 65.88  ?  376 SER A O     1 
ATOM   2826  C  CB    . SER A 1 357 ? 207.354 197.718 178.552 1.00 66.56  ?  376 SER A CB    1 
ATOM   2827  O  OG    . SER A 1 357 ? 206.702 198.356 179.635 1.00 68.42  ?  376 SER A OG    1 
ATOM   2828  N  N     . ARG A 1 358 ? 208.001 195.256 180.468 1.00 59.92  ?  377 ARG A N     1 
ATOM   2829  C  CA    . ARG A 1 358 ? 207.826 194.612 181.766 1.00 59.42  ?  377 ARG A CA    1 
ATOM   2830  C  C     . ARG A 1 358 ? 209.156 194.163 182.367 1.00 58.38  ?  377 ARG A C     1 
ATOM   2831  O  O     . ARG A 1 358 ? 209.267 194.038 183.591 1.00 59.62  ?  377 ARG A O     1 
ATOM   2832  C  CB    . ARG A 1 358 ? 206.866 193.425 181.627 1.00 64.33  ?  377 ARG A CB    1 
ATOM   2833  C  CG    . ARG A 1 358 ? 206.203 192.970 182.924 1.00 65.35  ?  377 ARG A CG    1 
ATOM   2834  C  CD    . ARG A 1 358 ? 207.013 191.903 183.651 1.00 64.29  ?  377 ARG A CD    1 
ATOM   2835  N  NE    . ARG A 1 358 ? 207.204 190.703 182.845 1.00 65.26  ?  377 ARG A NE    1 
ATOM   2836  C  CZ    . ARG A 1 358 ? 206.364 189.678 182.822 1.00 67.43  ?  377 ARG A CZ    1 
ATOM   2837  N  NH1   . ARG A 1 358 ? 205.260 189.673 183.550 1.00 66.11  1  377 ARG A NH1   1 
ATOM   2838  N  NH2   . ARG A 1 358 ? 206.641 188.629 182.052 1.00 65.47  ?  377 ARG A NH2   1 
ATOM   2839  N  N     . GLN A 1 359 ? 210.168 193.909 181.533 1.00 61.04  ?  378 GLN A N     1 
ATOM   2840  C  CA    . GLN A 1 359 ? 211.402 193.301 182.026 1.00 68.64  ?  378 GLN A CA    1 
ATOM   2841  C  C     . GLN A 1 359 ? 212.154 194.219 182.983 1.00 70.94  ?  378 GLN A C     1 
ATOM   2842  O  O     . GLN A 1 359 ? 212.632 193.768 184.030 1.00 69.23  ?  378 GLN A O     1 
ATOM   2843  C  CB    . GLN A 1 359 ? 212.301 192.905 180.855 1.00 67.18  ?  378 GLN A CB    1 
ATOM   2844  C  CG    . GLN A 1 359 ? 211.993 191.534 180.276 1.00 70.32  ?  378 GLN A CG    1 
ATOM   2845  C  CD    . GLN A 1 359 ? 212.689 190.417 181.029 1.00 71.67  ?  378 GLN A CD    1 
ATOM   2846  O  OE1   . GLN A 1 359 ? 213.620 190.658 181.798 1.00 73.01  ?  378 GLN A OE1   1 
ATOM   2847  N  NE2   . GLN A 1 359 ? 212.237 189.187 180.814 1.00 67.46  ?  378 GLN A NE2   1 
ATOM   2848  N  N     . HIS A 1 360 ? 212.278 195.500 182.649 1.00 62.19  ?  379 HIS A N     1 
ATOM   2849  C  CA    . HIS A 1 360 ? 213.037 196.419 183.486 1.00 60.84  ?  379 HIS A CA    1 
ATOM   2850  C  C     . HIS A 1 360 ? 212.189 197.064 184.573 1.00 63.13  ?  379 HIS A C     1 
ATOM   2851  O  O     . HIS A 1 360 ? 212.690 197.929 185.299 1.00 64.82  ?  379 HIS A O     1 
ATOM   2852  C  CB    . HIS A 1 360 ? 213.698 197.507 182.631 1.00 59.28  ?  379 HIS A CB    1 
ATOM   2853  C  CG    . HIS A 1 360 ? 212.738 198.289 181.791 1.00 63.24  ?  379 HIS A CG    1 
ATOM   2854  N  ND1   . HIS A 1 360 ? 212.313 197.861 180.552 1.00 62.35  ?  379 HIS A ND1   1 
ATOM   2855  C  CD2   . HIS A 1 360 ? 212.131 199.479 182.007 1.00 67.58  ?  379 HIS A CD2   1 
ATOM   2856  C  CE1   . HIS A 1 360 ? 211.480 198.752 180.044 1.00 65.33  ?  379 HIS A CE1   1 
ATOM   2857  N  NE2   . HIS A 1 360 ? 211.352 199.743 180.907 1.00 65.72  ?  379 HIS A NE2   1 
ATOM   2858  N  N     . ILE A 1 361 ? 210.924 196.671 184.700 1.00 56.31  ?  380 ILE A N     1 
ATOM   2859  C  CA    . ILE A 1 361 ? 210.051 197.197 185.743 1.00 52.36  ?  380 ILE A CA    1 
ATOM   2860  C  C     . ILE A 1 361 ? 209.520 196.116 186.673 1.00 55.43  ?  380 ILE A C     1 
ATOM   2861  O  O     . ILE A 1 361 ? 208.966 196.451 187.731 1.00 58.91  ?  380 ILE A O     1 
ATOM   2862  C  CB    . ILE A 1 361 ? 208.878 198.000 185.140 1.00 55.63  ?  380 ILE A CB    1 
ATOM   2863  C  CG1   . ILE A 1 361 ? 208.416 199.088 186.109 1.00 54.39  ?  380 ILE A CG1   1 
ATOM   2864  C  CG2   . ILE A 1 361 ? 207.725 197.077 184.769 1.00 54.97  ?  380 ILE A CG2   1 
ATOM   2865  C  CD1   . ILE A 1 361 ? 207.359 200.002 185.537 1.00 55.88  ?  380 ILE A CD1   1 
ATOM   2866  N  N     . GLU A 1 362 ? 209.668 194.834 186.326 1.00 46.23  ?  381 GLU A N     1 
ATOM   2867  C  CA    . GLU A 1 362 ? 209.179 193.774 187.201 1.00 49.19  ?  381 GLU A CA    1 
ATOM   2868  C  C     . GLU A 1 362 ? 209.984 193.703 188.493 1.00 49.11  ?  381 GLU A C     1 
ATOM   2869  O  O     . GLU A 1 362 ? 209.419 193.471 189.567 1.00 53.27  ?  381 GLU A O     1 
ATOM   2870  C  CB    . GLU A 1 362 ? 209.200 192.432 186.467 1.00 55.96  ?  381 GLU A CB    1 
ATOM   2871  C  CG    . GLU A 1 362 ? 210.540 192.045 185.860 1.00 55.91  ?  381 GLU A CG    1 
ATOM   2872  C  CD    . GLU A 1 362 ? 211.359 191.148 186.767 1.00 56.93  ?  381 GLU A CD    1 
ATOM   2873  O  OE1   . GLU A 1 362 ? 210.786 190.577 187.720 1.00 57.48  ?  381 GLU A OE1   1 
ATOM   2874  O  OE2   . GLU A 1 362 ? 212.575 191.006 186.521 1.00 52.27  -1 381 GLU A OE2   1 
ATOM   2875  N  N     . GLN A 1 363 ? 211.300 193.902 188.414 1.00 38.02  ?  382 GLN A N     1 
ATOM   2876  C  CA    . GLN A 1 363 ? 212.122 193.909 189.617 1.00 42.21  ?  382 GLN A CA    1 
ATOM   2877  C  C     . GLN A 1 363 ? 211.860 195.121 190.500 1.00 45.19  ?  382 GLN A C     1 
ATOM   2878  O  O     . GLN A 1 363 ? 212.327 195.144 191.643 1.00 50.07  ?  382 GLN A O     1 
ATOM   2879  C  CB    . GLN A 1 363 ? 213.605 193.855 189.245 1.00 49.74  ?  382 GLN A CB    1 
ATOM   2880  C  CG    . GLN A 1 363 ? 214.123 192.457 188.958 1.00 51.71  ?  382 GLN A CG    1 
ATOM   2881  C  CD    . GLN A 1 363 ? 214.258 191.616 190.213 1.00 53.53  ?  382 GLN A CD    1 
ATOM   2882  O  OE1   . GLN A 1 363 ? 214.445 192.143 191.309 1.00 52.90  ?  382 GLN A OE1   1 
ATOM   2883  N  NE2   . GLN A 1 363 ? 214.166 190.301 190.057 1.00 50.78  ?  382 GLN A NE2   1 
ATOM   2884  N  N     . LEU A 1 364 ? 211.133 196.120 190.002 1.00 39.72  ?  383 LEU A N     1 
ATOM   2885  C  CA    . LEU A 1 364 ? 210.848 197.331 190.757 1.00 37.77  ?  383 LEU A CA    1 
ATOM   2886  C  C     . LEU A 1 364 ? 209.414 197.423 191.254 1.00 40.42  ?  383 LEU A C     1 
ATOM   2887  O  O     . LEU A 1 364 ? 209.170 198.085 192.264 1.00 50.32  ?  383 LEU A O     1 
ATOM   2888  C  CB    . LEU A 1 364 ? 211.158 198.572 189.909 1.00 44.15  ?  383 LEU A CB    1 
ATOM   2889  C  CG    . LEU A 1 364 ? 212.538 199.217 190.061 1.00 44.11  ?  383 LEU A CG    1 
ATOM   2890  C  CD1   . LEU A 1 364 ? 212.668 199.896 191.416 1.00 41.60  ?  383 LEU A CD1   1 
ATOM   2891  C  CD2   . LEU A 1 364 ? 213.652 198.205 189.855 1.00 42.49  ?  383 LEU A CD2   1 
ATOM   2892  N  N     . ILE A 1 365 ? 208.461 196.783 190.572 1.00 29.32  ?  384 ILE A N     1 
ATOM   2893  C  CA    . ILE A 1 365 ? 207.074 196.830 191.018 1.00 31.05  ?  384 ILE A CA    1 
ATOM   2894  C  C     . ILE A 1 365 ? 206.904 195.981 192.273 1.00 34.15  ?  384 ILE A C     1 
ATOM   2895  O  O     . ILE A 1 365 ? 207.624 194.998 192.495 1.00 41.43  ?  384 ILE A O     1 
ATOM   2896  C  CB    . ILE A 1 365 ? 206.118 196.367 189.903 1.00 29.35  ?  384 ILE A CB    1 
ATOM   2897  C  CG1   . ILE A 1 365 ? 206.532 194.991 189.380 1.00 37.08  ?  384 ILE A CG1   1 
ATOM   2898  C  CG2   . ILE A 1 365 ? 206.065 197.388 188.778 1.00 33.55  ?  384 ILE A CG2   1 
ATOM   2899  C  CD1   . ILE A 1 365 ? 205.619 194.444 188.303 1.00 38.33  ?  384 ILE A CD1   1 
ATOM   2900  N  N     . GLN A 1 366 ? 205.938 196.366 193.106 1.00 26.24  ?  385 GLN A N     1 
ATOM   2901  C  CA    . GLN A 1 366 ? 205.681 195.686 194.364 1.00 23.38  ?  385 GLN A CA    1 
ATOM   2902  C  C     . GLN A 1 366 ? 204.292 195.069 194.448 1.00 35.16  ?  385 GLN A C     1 
ATOM   2903  O  O     . GLN A 1 366 ? 203.979 194.427 195.458 1.00 43.02  ?  385 GLN A O     1 
ATOM   2904  C  CB    . GLN A 1 366 ? 205.879 196.654 195.539 1.00 31.37  ?  385 GLN A CB    1 
ATOM   2905  C  CG    . GLN A 1 366 ? 207.325 197.053 195.782 1.00 35.16  ?  385 GLN A CG    1 
ATOM   2906  C  CD    . GLN A 1 366 ? 208.187 195.887 196.217 1.00 41.22  ?  385 GLN A CD    1 
ATOM   2907  O  OE1   . GLN A 1 366 ? 208.223 195.533 197.395 1.00 46.19  ?  385 GLN A OE1   1 
ATOM   2908  N  NE2   . GLN A 1 366 ? 208.898 195.291 195.269 1.00 42.91  ?  385 GLN A NE2   1 
ATOM   2909  N  N     . PHE A 1 367 ? 203.451 195.238 193.429 1.00 27.68  ?  386 PHE A N     1 
ATOM   2910  C  CA    . PHE A 1 367 ? 202.096 194.711 193.456 1.00 15.49  ?  386 PHE A CA    1 
ATOM   2911  C  C     . PHE A 1 367 ? 201.755 194.085 192.114 1.00 20.93  ?  386 PHE A C     1 
ATOM   2912  O  O     . PHE A 1 367 ? 202.299 194.468 191.074 1.00 31.07  ?  386 PHE A O     1 
ATOM   2913  C  CB    . PHE A 1 367 ? 201.072 195.802 193.789 1.00 18.65  ?  386 PHE A CB    1 
ATOM   2914  C  CG    . PHE A 1 367 ? 201.004 196.138 195.245 1.00 16.41  ?  386 PHE A CG    1 
ATOM   2915  C  CD1   . PHE A 1 367 ? 200.180 195.424 196.097 1.00 21.97  ?  386 PHE A CD1   1 
ATOM   2916  C  CD2   . PHE A 1 367 ? 201.769 197.166 195.766 1.00 22.38  ?  386 PHE A CD2   1 
ATOM   2917  C  CE1   . PHE A 1 367 ? 200.116 195.731 197.438 1.00 25.05  ?  386 PHE A CE1   1 
ATOM   2918  C  CE2   . PHE A 1 367 ? 201.709 197.475 197.106 1.00 26.37  ?  386 PHE A CE2   1 
ATOM   2919  C  CZ    . PHE A 1 367 ? 200.882 196.758 197.942 1.00 31.06  ?  386 PHE A CZ    1 
ATOM   2920  N  N     . ASP A 1 368 ? 200.846 193.121 192.149 1.00 20.37  ?  387 ASP A N     1 
ATOM   2921  C  CA    . ASP A 1 368 ? 200.359 192.504 190.925 1.00 16.61  ?  387 ASP A CA    1 
ATOM   2922  C  C     . ASP A 1 368 ? 199.273 193.382 190.317 1.00 24.03  ?  387 ASP A C     1 
ATOM   2923  O  O     . ASP A 1 368 ? 198.244 193.610 190.962 1.00 31.03  ?  387 ASP A O     1 
ATOM   2924  C  CB    . ASP A 1 368 ? 199.812 191.113 191.209 1.00 26.36  ?  387 ASP A CB    1 
ATOM   2925  C  CG    . ASP A 1 368 ? 199.730 190.256 189.963 1.00 37.64  ?  387 ASP A CG    1 
ATOM   2926  O  OD1   . ASP A 1 368 ? 200.737 190.181 189.228 1.00 31.60  ?  387 ASP A OD1   1 
ATOM   2927  O  OD2   . ASP A 1 368 ? 198.662 189.659 189.719 1.00 46.42  -1 387 ASP A OD2   1 
ATOM   2928  N  N     . PRO A 1 369 ? 199.453 193.887 189.093 1.00 31.39  ?  388 PRO A N     1 
ATOM   2929  C  CA    . PRO A 1 369 ? 198.445 194.789 188.512 1.00 28.18  ?  388 PRO A CA    1 
ATOM   2930  C  C     . PRO A 1 369 ? 197.124 194.114 188.185 1.00 27.60  ?  388 PRO A C     1 
ATOM   2931  O  O     . PRO A 1 369 ? 196.221 194.789 187.674 1.00 33.60  ?  388 PRO A O     1 
ATOM   2932  C  CB    . PRO A 1 369 ? 199.130 195.305 187.241 1.00 23.17  ?  388 PRO A CB    1 
ATOM   2933  C  CG    . PRO A 1 369 ? 200.104 194.233 186.884 1.00 37.09  ?  388 PRO A CG    1 
ATOM   2934  C  CD    . PRO A 1 369 ? 200.594 193.670 188.187 1.00 33.65  ?  388 PRO A CD    1 
ATOM   2935  N  N     . MET A 1 370 ? 196.977 192.817 188.453 1.00 24.34  ?  389 MET A N     1 
ATOM   2936  C  CA    . MET A 1 370 ? 195.747 192.096 188.144 1.00 32.03  ?  389 MET A CA    1 
ATOM   2937  C  C     . MET A 1 370 ? 194.857 191.911 189.370 1.00 38.20  ?  389 MET A C     1 
ATOM   2938  O  O     . MET A 1 370 ? 193.705 192.355 189.377 1.00 38.54  ?  389 MET A O     1 
ATOM   2939  C  CB    . MET A 1 370 ? 196.087 190.737 187.519 1.00 28.03  ?  389 MET A CB    1 
ATOM   2940  C  CG    . MET A 1 370 ? 194.877 189.859 187.272 1.00 28.91  ?  389 MET A CG    1 
ATOM   2941  S  SD    . MET A 1 370 ? 193.526 190.773 186.509 1.00 42.02  ?  389 MET A SD    1 
ATOM   2942  C  CE    . MET A 1 370 ? 192.122 189.994 187.296 1.00 34.01  ?  389 MET A CE    1 
ATOM   2943  N  N     . THR A 1 371 ? 195.373 191.266 190.414 1.00 26.07  ?  390 THR A N     1 
ATOM   2944  C  CA    . THR A 1 371 ? 194.581 190.939 191.591 1.00 20.63  ?  390 THR A CA    1 
ATOM   2945  C  C     . THR A 1 371 ? 194.837 191.872 192.767 1.00 22.03  ?  390 THR A C     1 
ATOM   2946  O  O     . THR A 1 371 ? 194.223 191.695 193.823 1.00 27.39  ?  390 THR A O     1 
ATOM   2947  C  CB    . THR A 1 371 ? 194.847 189.492 192.021 1.00 29.19  ?  390 THR A CB    1 
ATOM   2948  O  OG1   . THR A 1 371 ? 196.071 189.429 192.763 1.00 31.78  ?  390 THR A OG1   1 
ATOM   2949  C  CG2   . THR A 1 371 ? 194.952 188.586 190.804 1.00 29.96  ?  390 THR A CG2   1 
ATOM   2950  N  N     . GLY A 1 372 ? 195.722 192.854 192.616 1.00 26.55  ?  391 GLY A N     1 
ATOM   2951  C  CA    . GLY A 1 372 ? 196.030 193.757 193.706 1.00 27.95  ?  391 GLY A CA    1 
ATOM   2952  C  C     . GLY A 1 372 ? 196.821 193.153 194.842 1.00 30.88  ?  391 GLY A C     1 
ATOM   2953  O  O     . GLY A 1 372 ? 197.029 193.824 195.858 1.00 35.54  ?  391 GLY A O     1 
ATOM   2954  N  N     . LEU A 1 373 ? 197.267 191.908 194.709 1.00 27.11  ?  392 LEU A N     1 
ATOM   2955  C  CA    . LEU A 1 373 ? 198.042 191.238 195.738 1.00 16.24  ?  392 LEU A CA    1 
ATOM   2956  C  C     . LEU A 1 373 ? 199.523 191.541 195.577 1.00 13.87  ?  392 LEU A C     1 
ATOM   2957  O  O     . LEU A 1 373 ? 199.991 191.852 194.477 1.00 33.29  ?  392 LEU A O     1 
ATOM   2958  C  CB    . LEU A 1 373 ? 197.806 189.730 195.673 1.00 27.42  ?  392 LEU A CB    1 
ATOM   2959  C  CG    . LEU A 1 373 ? 196.550 189.210 196.374 1.00 25.93  ?  392 LEU A CG    1 
ATOM   2960  C  CD1   . LEU A 1 373 ? 196.125 187.863 195.811 1.00 20.72  ?  392 LEU A CD1   1 
ATOM   2961  C  CD2   . LEU A 1 373 ? 196.773 189.124 197.873 1.00 24.18  ?  392 LEU A CD2   1 
ATOM   2962  N  N     . PRO A 1 374 ? 200.289 191.468 196.665 1.00 9.98   ?  393 PRO A N     1 
ATOM   2963  C  CA    . PRO A 1 374 ? 201.741 191.643 196.554 1.00 23.52  ?  393 PRO A CA    1 
ATOM   2964  C  C     . PRO A 1 374 ? 202.353 190.591 195.643 1.00 28.64  ?  393 PRO A C     1 
ATOM   2965  O  O     . PRO A 1 374 ? 201.868 189.462 195.544 1.00 41.74  ?  393 PRO A O     1 
ATOM   2966  C  CB    . PRO A 1 374 ? 202.228 191.488 197.998 1.00 28.75  ?  393 PRO A CB    1 
ATOM   2967  C  CG    . PRO A 1 374 ? 201.052 191.863 198.831 1.00 26.41  ?  393 PRO A CG    1 
ATOM   2968  C  CD    . PRO A 1 374 ? 199.843 191.413 198.068 1.00 22.50  ?  393 PRO A CD    1 
ATOM   2969  N  N     . ASN A 1 375 ? 203.422 190.979 194.959 1.00 23.21  ?  394 ASN A N     1 
ATOM   2970  C  CA    . ASN A 1 375 ? 204.042 190.141 193.949 1.00 20.98  ?  394 ASN A CA    1 
ATOM   2971  C  C     . ASN A 1 375 ? 205.225 189.368 194.533 1.00 33.37  ?  394 ASN A C     1 
ATOM   2972  O  O     . ASN A 1 375 ? 205.452 189.339 195.750 1.00 40.96  ?  394 ASN A O     1 
ATOM   2973  C  CB    . ASN A 1 375 ? 204.453 190.993 192.746 1.00 25.27  ?  394 ASN A CB    1 
ATOM   2974  C  CG    . ASN A 1 375 ? 205.574 191.959 193.068 1.00 36.64  ?  394 ASN A CG    1 
ATOM   2975  O  OD1   . ASN A 1 375 ? 205.777 192.333 194.223 1.00 42.03  ?  394 ASN A OD1   1 
ATOM   2976  N  ND2   . ASN A 1 375 ? 206.311 192.371 192.042 1.00 38.81  ?  394 ASN A ND2   1 
ATOM   2977  N  N     . ARG A 1 376 ? 205.986 188.721 193.645 1.00 39.72  ?  395 ARG A N     1 
ATOM   2978  C  CA    . ARG A 1 376 ? 207.105 187.888 194.073 1.00 29.70  ?  395 ARG A CA    1 
ATOM   2979  C  C     . ARG A 1 376 ? 208.176 188.710 194.779 1.00 38.60  ?  395 ARG A C     1 
ATOM   2980  O  O     . ARG A 1 376 ? 208.785 188.243 195.747 1.00 40.90  ?  395 ARG A O     1 
ATOM   2981  C  CB    . ARG A 1 376 ? 207.700 187.153 192.871 1.00 28.23  ?  395 ARG A CB    1 
ATOM   2982  C  CG    . ARG A 1 376 ? 208.594 185.978 193.239 1.00 35.42  ?  395 ARG A CG    1 
ATOM   2983  C  CD    . ARG A 1 376 ? 209.268 185.388 192.010 1.00 34.99  ?  395 ARG A CD    1 
ATOM   2984  N  NE    . ARG A 1 376 ? 208.533 184.252 191.469 1.00 40.75  ?  395 ARG A NE    1 
ATOM   2985  C  CZ    . ARG A 1 376 ? 208.635 183.010 191.921 1.00 43.92  ?  395 ARG A CZ    1 
ATOM   2986  N  NH1   . ARG A 1 376 ? 209.437 182.704 192.927 1.00 43.88  1  395 ARG A NH1   1 
ATOM   2987  N  NH2   . ARG A 1 376 ? 207.915 182.049 191.348 1.00 34.98  ?  395 ARG A NH2   1 
ATOM   2988  N  N     . ASN A 1 377 ? 208.435 189.929 194.299 1.00 40.15  ?  396 ASN A N     1 
ATOM   2989  C  CA    . ASN A 1 377 ? 209.432 190.778 194.945 1.00 32.44  ?  396 ASN A CA    1 
ATOM   2990  C  C     . ASN A 1 377 ? 209.008 191.153 196.359 1.00 30.59  ?  396 ASN A C     1 
ATOM   2991  O  O     . ASN A 1 377 ? 209.826 191.138 197.288 1.00 38.03  ?  396 ASN A O     1 
ATOM   2992  C  CB    . ASN A 1 377 ? 209.670 192.033 194.106 1.00 30.28  ?  396 ASN A CB    1 
ATOM   2993  C  CG    . ASN A 1 377 ? 209.954 191.715 192.654 1.00 43.08  ?  396 ASN A CG    1 
ATOM   2994  O  OD1   . ASN A 1 377 ? 209.091 191.878 191.793 1.00 40.96  ?  396 ASN A OD1   1 
ATOM   2995  N  ND2   . ASN A 1 377 ? 211.168 191.255 192.374 1.00 46.70  ?  396 ASN A ND2   1 
ATOM   2996  N  N     . ASN A 1 378 ? 207.732 191.500 196.540 1.00 31.54  ?  397 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 378 ? 207.229 191.809 197.875 1.00 32.23  ?  397 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 378 ? 207.312 190.591 198.784 1.00 36.99  ?  397 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 378 ? 207.664 190.710 199.964 1.00 40.97  ?  397 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 378 ? 205.791 192.322 197.787 1.00 29.14  ?  397 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 378 ? 205.380 193.124 199.008 1.00 36.68  ?  397 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 378 ? 205.955 192.976 200.087 1.00 44.02  ?  397 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 378 ? 204.375 193.975 198.845 1.00 34.40  ?  397 ASN A ND2   1 
ATOM   3004  N  N     . LEU A 1 379 ? 206.988 189.408 198.254 1.00 45.34  ?  398 LEU A N     1 
ATOM   3005  C  CA    . LEU A 1 379 ? 207.116 188.188 199.046 1.00 41.80  ?  398 LEU A CA    1 
ATOM   3006  C  C     . LEU A 1 379 ? 208.564 187.945 199.452 1.00 38.49  ?  398 LEU A C     1 
ATOM   3007  O  O     . LEU A 1 379 ? 208.842 187.565 200.596 1.00 43.44  ?  398 LEU A O     1 
ATOM   3008  C  CB    . LEU A 1 379 ? 206.577 186.993 198.261 1.00 43.98  ?  398 LEU A CB    1 
ATOM   3009  C  CG    . LEU A 1 379 ? 207.079 185.618 198.709 1.00 42.68  ?  398 LEU A CG    1 
ATOM   3010  C  CD1   . LEU A 1 379 ? 206.489 185.234 200.057 1.00 37.59  ?  398 LEU A CD1   1 
ATOM   3011  C  CD2   . LEU A 1 379 ? 206.769 184.561 197.664 1.00 41.72  ?  398 LEU A CD2   1 
ATOM   3012  N  N     . HIS A 1 380 ? 209.500 188.154 198.523 1.00 39.33  ?  399 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 380 ? 210.914 187.975 198.835 1.00 40.20  ?  399 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 380 ? 211.362 188.943 199.920 1.00 45.09  ?  399 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 380 ? 212.085 188.557 200.844 1.00 51.11  ?  399 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 380 ? 211.760 188.160 197.576 1.00 38.09  ?  399 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 380 ? 211.591 187.069 196.565 1.00 37.65  ?  399 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 380 ? 211.156 185.805 196.899 1.00 45.07  ?  399 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 380 ? 211.813 187.050 195.230 1.00 38.46  ?  399 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 380 ? 211.108 185.057 195.812 1.00 48.86  ?  399 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 380 ? 211.504 185.788 194.785 1.00 42.90  ?  399 HIS A NE2   1 
ATOM   3022  N  N     . ASN A 1 381 ? 210.939 190.206 199.826 1.00 46.24  ?  400 ASN A N     1 
ATOM   3023  C  CA    . ASN A 1 381 ? 211.304 191.186 200.845 1.00 43.12  ?  400 ASN A CA    1 
ATOM   3024  C  C     . ASN A 1 381 ? 210.721 190.816 202.203 1.00 45.93  ?  400 ASN A C     1 
ATOM   3025  O  O     . ASN A 1 381 ? 211.404 190.918 203.230 1.00 48.60  ?  400 ASN A O     1 
ATOM   3026  C  CB    . ASN A 1 381 ? 210.838 192.579 200.422 1.00 43.18  ?  400 ASN A CB    1 
ATOM   3027  C  CG    . ASN A 1 381 ? 211.745 193.204 199.382 1.00 46.91  ?  400 ASN A CG    1 
ATOM   3028  O  OD1   . ASN A 1 381 ? 212.899 192.804 199.228 1.00 46.51  ?  400 ASN A OD1   1 
ATOM   3029  N  ND2   . ASN A 1 381 ? 211.228 194.192 198.662 1.00 48.10  ?  400 ASN A ND2   1 
ATOM   3030  N  N     . TYR A 1 382 ? 209.459 190.380 202.228 1.00 46.31  ?  401 TYR A N     1 
ATOM   3031  C  CA    . TYR A 1 382 ? 208.823 189.997 203.485 1.00 41.54  ?  401 TYR A CA    1 
ATOM   3032  C  C     . TYR A 1 382 ? 209.527 188.801 204.117 1.00 42.94  ?  401 TYR A C     1 
ATOM   3033  O  O     . TYR A 1 382 ? 209.791 188.788 205.327 1.00 46.41  ?  401 TYR A O     1 
ATOM   3034  C  CB    . TYR A 1 382 ? 207.344 189.696 203.233 1.00 40.77  ?  401 TYR A CB    1 
ATOM   3035  C  CG    . TYR A 1 382 ? 206.500 189.539 204.476 1.00 44.14  ?  401 TYR A CG    1 
ATOM   3036  C  CD1   . TYR A 1 382 ? 206.315 188.296 205.064 1.00 47.75  ?  401 TYR A CD1   1 
ATOM   3037  C  CD2   . TYR A 1 382 ? 205.877 190.636 205.055 1.00 43.33  ?  401 TYR A CD2   1 
ATOM   3038  C  CE1   . TYR A 1 382 ? 205.536 188.152 206.197 1.00 46.27  ?  401 TYR A CE1   1 
ATOM   3039  C  CE2   . TYR A 1 382 ? 205.099 190.501 206.188 1.00 44.95  ?  401 TYR A CE2   1 
ATOM   3040  C  CZ    . TYR A 1 382 ? 204.933 189.257 206.755 1.00 49.17  ?  401 TYR A CZ    1 
ATOM   3041  O  OH    . TYR A 1 382 ? 204.159 189.117 207.884 1.00 50.65  ?  401 TYR A OH    1 
ATOM   3042  N  N     . LEU A 1 383 ? 209.858 187.792 203.307 1.00 47.04  ?  402 LEU A N     1 
ATOM   3043  C  CA    . LEU A 1 383 ? 210.542 186.614 203.830 1.00 49.00  ?  402 LEU A CA    1 
ATOM   3044  C  C     . LEU A 1 383 ? 211.953 186.952 204.296 1.00 53.94  ?  402 LEU A C     1 
ATOM   3045  O  O     . LEU A 1 383 ? 212.425 186.411 205.303 1.00 62.94  ?  402 LEU A O     1 
ATOM   3046  C  CB    . LEU A 1 383 ? 210.569 185.513 202.770 1.00 49.57  ?  402 LEU A CB    1 
ATOM   3047  C  CG    . LEU A 1 383 ? 209.294 184.678 202.643 1.00 51.67  ?  402 LEU A CG    1 
ATOM   3048  C  CD1   . LEU A 1 383 ? 209.477 183.557 201.633 1.00 46.05  ?  402 LEU A CD1   1 
ATOM   3049  C  CD2   . LEU A 1 383 ? 208.878 184.122 203.996 1.00 54.19  ?  402 LEU A CD2   1 
ATOM   3050  N  N     . ASP A 1 384 ? 212.647 187.836 203.571 1.00 53.34  ?  403 ASP A N     1 
ATOM   3051  C  CA    . ASP A 1 384 ? 213.972 188.268 204.002 1.00 50.19  ?  403 ASP A CA    1 
ATOM   3052  C  C     . ASP A 1 384 ? 213.900 189.008 205.329 1.00 51.04  ?  403 ASP A C     1 
ATOM   3053  O  O     . ASP A 1 384 ? 214.746 188.807 206.207 1.00 55.87  ?  403 ASP A O     1 
ATOM   3054  C  CB    . ASP A 1 384 ? 214.617 189.147 202.930 1.00 52.63  ?  403 ASP A CB    1 
ATOM   3055  C  CG    . ASP A 1 384 ? 215.066 188.353 201.719 1.00 55.63  ?  403 ASP A CG    1 
ATOM   3056  O  OD1   . ASP A 1 384 ? 214.541 187.240 201.507 1.00 52.45  ?  403 ASP A OD1   1 
ATOM   3057  O  OD2   . ASP A 1 384 ? 215.945 188.842 200.979 1.00 58.63  -1 403 ASP A OD2   1 
ATOM   3058  N  N     . ASP A 1 385 ? 212.892 189.867 205.497 1.00 56.91  ?  404 ASP A N     1 
ATOM   3059  C  CA    . ASP A 1 385 ? 212.710 190.546 206.775 1.00 58.43  ?  404 ASP A CA    1 
ATOM   3060  C  C     . ASP A 1 385 ? 212.448 189.545 207.893 1.00 58.88  ?  404 ASP A C     1 
ATOM   3061  O  O     . ASP A 1 385 ? 213.000 189.671 208.992 1.00 59.31  ?  404 ASP A O     1 
ATOM   3062  C  CB    . ASP A 1 385 ? 211.567 191.556 206.678 1.00 60.08  ?  404 ASP A CB    1 
ATOM   3063  C  CG    . ASP A 1 385 ? 211.971 192.825 205.956 1.00 63.09  ?  404 ASP A CG    1 
ATOM   3064  O  OD1   . ASP A 1 385 ? 213.187 193.040 205.762 1.00 62.26  ?  404 ASP A OD1   1 
ATOM   3065  O  OD2   . ASP A 1 385 ? 211.074 193.610 205.582 1.00 62.79  -1 404 ASP A OD2   1 
ATOM   3066  N  N     . LEU A 1 386 ? 211.613 188.536 207.626 1.00 62.12  ?  405 LEU A N     1 
ATOM   3067  C  CA    . LEU A 1 386 ? 211.332 187.520 208.638 1.00 59.73  ?  405 LEU A CA    1 
ATOM   3068  C  C     . LEU A 1 386 ? 212.599 186.771 209.042 1.00 60.98  ?  405 LEU A C     1 
ATOM   3069  O  O     . LEU A 1 386 ? 212.900 186.629 210.234 1.00 65.21  ?  405 LEU A O     1 
ATOM   3070  C  CB    . LEU A 1 386 ? 210.276 186.543 208.121 1.00 61.86  ?  405 LEU A CB    1 
ATOM   3071  C  CG    . LEU A 1 386 ? 208.811 186.958 208.255 1.00 64.10  ?  405 LEU A CG    1 
ATOM   3072  C  CD1   . LEU A 1 386 ? 207.923 185.988 207.495 1.00 63.19  ?  405 LEU A CD1   1 
ATOM   3073  C  CD2   . LEU A 1 386 ? 208.401 187.032 209.717 1.00 62.56  ?  405 LEU A CD2   1 
ATOM   3074  N  N     . VAL A 1 387 ? 213.361 186.286 208.057 1.00 61.02  ?  406 VAL A N     1 
ATOM   3075  C  CA    . VAL A 1 387 ? 214.550 185.501 208.379 1.00 62.84  ?  406 VAL A CA    1 
ATOM   3076  C  C     . VAL A 1 387 ? 215.615 186.367 209.045 1.00 63.44  ?  406 VAL A C     1 
ATOM   3077  O  O     . VAL A 1 387 ? 216.367 185.884 209.900 1.00 68.34  ?  406 VAL A O     1 
ATOM   3078  C  CB    . VAL A 1 387 ? 215.092 184.778 207.129 1.00 63.26  ?  406 VAL A CB    1 
ATOM   3079  C  CG1   . VAL A 1 387 ? 214.022 183.870 206.535 1.00 61.87  ?  406 VAL A CG1   1 
ATOM   3080  C  CG2   . VAL A 1 387 ? 215.593 185.766 206.092 1.00 61.55  ?  406 VAL A CG2   1 
ATOM   3081  N  N     . ASP A 1 388 ? 215.709 187.649 208.673 1.00 66.36  ?  407 ASP A N     1 
ATOM   3082  C  CA    . ASP A 1 388 ? 216.637 188.546 209.353 1.00 69.56  ?  407 ASP A CA    1 
ATOM   3083  C  C     . ASP A 1 388 ? 216.212 188.804 210.792 1.00 69.38  ?  407 ASP A C     1 
ATOM   3084  O  O     . ASP A 1 388 ? 217.067 188.913 211.679 1.00 70.55  ?  407 ASP A O     1 
ATOM   3085  C  CB    . ASP A 1 388 ? 216.756 189.861 208.585 1.00 70.40  ?  407 ASP A CB    1 
ATOM   3086  C  CG    . ASP A 1 388 ? 217.558 189.718 207.307 1.00 71.97  ?  407 ASP A CG    1 
ATOM   3087  O  OD1   . ASP A 1 388 ? 218.211 188.668 207.129 1.00 72.14  ?  407 ASP A OD1   1 
ATOM   3088  O  OD2   . ASP A 1 388 ? 217.538 190.655 206.482 1.00 69.91  -1 407 ASP A OD2   1 
ATOM   3089  N  N     . LYS A 1 389 ? 214.908 188.908 211.045 1.00 70.31  ?  408 LYS A N     1 
ATOM   3090  C  CA    . LYS A 1 389 ? 214.397 189.008 212.406 1.00 69.34  ?  408 LYS A CA    1 
ATOM   3091  C  C     . LYS A 1 389 ? 214.378 187.664 213.121 1.00 69.78  ?  408 LYS A C     1 
ATOM   3092  O  O     . LYS A 1 389 ? 213.941 187.601 214.275 1.00 69.86  ?  408 LYS A O     1 
ATOM   3093  C  CB    . LYS A 1 389 ? 212.991 189.612 212.400 1.00 68.57  ?  408 LYS A CB    1 
ATOM   3094  C  CG    . LYS A 1 389 ? 212.714 190.550 213.563 1.00 68.56  ?  408 LYS A CG    1 
ATOM   3095  C  CD    . LYS A 1 389 ? 211.563 191.491 213.253 1.00 69.71  ?  408 LYS A CD    1 
ATOM   3096  C  CE    . LYS A 1 389 ? 210.293 190.724 212.926 1.00 70.92  ?  408 LYS A CE    1 
ATOM   3097  N  NZ    . LYS A 1 389 ? 209.191 191.633 212.507 1.00 67.35  1  408 LYS A NZ    1 
ATOM   3098  N  N     . ALA A 1 390 ? 214.820 186.596 212.449 1.00 73.26  ?  409 ALA A N     1 
ATOM   3099  C  CA    . ALA A 1 390 ? 214.943 185.261 213.040 1.00 74.85  ?  409 ALA A CA    1 
ATOM   3100  C  C     . ALA A 1 390 ? 213.572 184.704 213.420 1.00 77.93  ?  409 ALA A C     1 
ATOM   3101  O  O     . ALA A 1 390 ? 213.355 184.229 214.536 1.00 78.51  ?  409 ALA A O     1 
ATOM   3102  C  CB    . ALA A 1 390 ? 215.895 185.262 214.240 1.00 73.37  ?  409 ALA A CB    1 
ATOM   3103  N  N     . VAL A 1 391 ? 212.644 184.770 212.471 1.00 73.89  ?  410 VAL A N     1 
ATOM   3104  C  CA    . VAL A 1 391 ? 211.324 184.170 212.596 1.00 71.16  ?  410 VAL A CA    1 
ATOM   3105  C  C     . VAL A 1 391 ? 211.221 183.061 211.562 1.00 69.58  ?  410 VAL A C     1 
ATOM   3106  O  O     . VAL A 1 391 ? 211.665 183.225 210.420 1.00 68.44  ?  410 VAL A O     1 
ATOM   3107  C  CB    . VAL A 1 391 ? 210.198 185.207 212.401 1.00 70.94  ?  410 VAL A CB    1 
ATOM   3108  C  CG1   . VAL A 1 391 ? 208.854 184.621 212.811 1.00 68.49  ?  410 VAL A CG1   1 
ATOM   3109  C  CG2   . VAL A 1 391 ? 210.498 186.473 213.188 1.00 69.57  ?  410 VAL A CG2   1 
ATOM   3110  N  N     . SER A 1 392 ? 210.650 181.932 211.963 1.00 70.29  ?  411 SER A N     1 
ATOM   3111  C  CA    . SER A 1 392 ? 210.530 180.808 211.048 1.00 69.01  ?  411 SER A CA    1 
ATOM   3112  C  C     . SER A 1 392 ? 209.121 180.773 210.471 1.00 67.31  ?  411 SER A C     1 
ATOM   3113  O  O     . SER A 1 392 ? 208.169 180.411 211.173 1.00 68.11  ?  411 SER A O     1 
ATOM   3114  C  CB    . SER A 1 392 ? 210.856 179.494 211.758 1.00 69.60  ?  411 SER A CB    1 
ATOM   3115  O  OG    . SER A 1 392 ? 210.965 178.430 210.830 1.00 71.79  ?  411 SER A OG    1 
ATOM   3116  N  N     . PRO A 1 393 ? 208.947 181.139 209.206 1.00 53.51  ?  412 PRO A N     1 
ATOM   3117  C  CA    . PRO A 1 393 ? 207.611 181.157 208.613 1.00 52.06  ?  412 PRO A CA    1 
ATOM   3118  C  C     . PRO A 1 393 ? 207.269 179.815 207.979 1.00 56.27  ?  412 PRO A C     1 
ATOM   3119  O  O     . PRO A 1 393 ? 208.133 178.980 207.707 1.00 62.84  ?  412 PRO A O     1 
ATOM   3120  C  CB    . PRO A 1 393 ? 207.724 182.257 207.555 1.00 55.20  ?  412 PRO A CB    1 
ATOM   3121  C  CG    . PRO A 1 393 ? 209.157 182.171 207.105 1.00 56.48  ?  412 PRO A CG    1 
ATOM   3122  C  CD    . PRO A 1 393 ? 209.972 181.616 208.261 1.00 56.17  ?  412 PRO A CD    1 
ATOM   3123  N  N     . VAL A 1 394 ? 205.975 179.625 207.738 1.00 46.66  ?  413 VAL A N     1 
ATOM   3124  C  CA    . VAL A 1 394 ? 205.462 178.439 207.068 1.00 40.50  ?  413 VAL A CA    1 
ATOM   3125  C  C     . VAL A 1 394 ? 204.855 178.904 205.756 1.00 37.49  ?  413 VAL A C     1 
ATOM   3126  O  O     . VAL A 1 394 ? 203.958 179.757 205.756 1.00 49.70  ?  413 VAL A O     1 
ATOM   3127  C  CB    . VAL A 1 394 ? 204.412 177.702 207.914 1.00 44.51  ?  413 VAL A CB    1 
ATOM   3128  C  CG1   . VAL A 1 394 ? 204.148 176.318 207.344 1.00 46.39  ?  413 VAL A CG1   1 
ATOM   3129  C  CG2   . VAL A 1 394 ? 204.838 177.636 209.368 1.00 49.94  ?  413 VAL A CG2   1 
ATOM   3130  N  N     . VAL A 1 395 ? 205.338 178.361 204.642 1.00 29.25  ?  414 VAL A N     1 
ATOM   3131  C  CA    . VAL A 1 395 ? 204.896 178.801 203.326 1.00 25.85  ?  414 VAL A CA    1 
ATOM   3132  C  C     . VAL A 1 395 ? 203.995 177.731 202.721 1.00 27.31  ?  414 VAL A C     1 
ATOM   3133  O  O     . VAL A 1 395 ? 204.359 176.549 202.660 1.00 44.66  ?  414 VAL A O     1 
ATOM   3134  C  CB    . VAL A 1 395 ? 206.085 179.139 202.410 1.00 29.30  ?  414 VAL A CB    1 
ATOM   3135  C  CG1   . VAL A 1 395 ? 206.875 180.298 202.989 1.00 38.96  ?  414 VAL A CG1   1 
ATOM   3136  C  CG2   . VAL A 1 395 ? 206.999 177.950 202.229 1.00 34.21  ?  414 VAL A CG2   1 
ATOM   3137  N  N     . TYR A 1 396 ? 202.798 178.148 202.311 1.00 20.56  ?  415 TYR A N     1 
ATOM   3138  C  CA    . TYR A 1 396 ? 201.850 177.300 201.598 1.00 18.79  ?  415 TYR A CA    1 
ATOM   3139  C  C     . TYR A 1 396 ? 201.816 177.795 200.158 1.00 21.72  ?  415 TYR A C     1 
ATOM   3140  O  O     . TYR A 1 396 ? 201.296 178.880 199.883 1.00 41.17  ?  415 TYR A O     1 
ATOM   3141  C  CB    . TYR A 1 396 ? 200.457 177.374 202.213 1.00 26.85  ?  415 TYR A CB    1 
ATOM   3142  C  CG    . TYR A 1 396 ? 200.379 177.127 203.700 1.00 31.74  ?  415 TYR A CG    1 
ATOM   3143  C  CD1   . TYR A 1 396 ? 201.253 176.260 204.333 1.00 41.23  ?  415 TYR A CD1   1 
ATOM   3144  C  CD2   . TYR A 1 396 ? 199.417 177.764 204.470 1.00 28.76  ?  415 TYR A CD2   1 
ATOM   3145  C  CE1   . TYR A 1 396 ? 201.170 176.036 205.692 1.00 41.08  ?  415 TYR A CE1   1 
ATOM   3146  C  CE2   . TYR A 1 396 ? 199.329 177.549 205.827 1.00 27.42  ?  415 TYR A CE2   1 
ATOM   3147  C  CZ    . TYR A 1 396 ? 200.208 176.686 206.435 1.00 31.16  ?  415 TYR A CZ    1 
ATOM   3148  O  OH    . TYR A 1 396 ? 200.119 176.472 207.790 1.00 36.67  ?  415 TYR A OH    1 
ATOM   3149  N  N     . LEU A 1 397 ? 202.385 177.019 199.240 1.00 14.96  ?  416 LEU A N     1 
ATOM   3150  C  CA    . LEU A 1 397 ? 202.162 177.270 197.822 1.00 21.38  ?  416 LEU A CA    1 
ATOM   3151  C  C     . LEU A 1 397 ? 200.829 176.657 197.426 1.00 23.33  ?  416 LEU A C     1 
ATOM   3152  O  O     . LEU A 1 397 ? 200.652 175.434 197.479 1.00 31.98  ?  416 LEU A O     1 
ATOM   3153  C  CB    . LEU A 1 397 ? 203.299 176.730 196.959 1.00 25.09  ?  416 LEU A CB    1 
ATOM   3154  C  CG    . LEU A 1 397 ? 204.593 177.532 197.063 1.00 31.98  ?  416 LEU A CG    1 
ATOM   3155  C  CD1   . LEU A 1 397 ? 205.681 176.914 196.229 1.00 37.44  ?  416 LEU A CD1   1 
ATOM   3156  C  CD2   . LEU A 1 397 ? 204.337 178.934 196.593 1.00 28.22  ?  416 LEU A CD2   1 
ATOM   3157  N  N     . ILE A 1 398 ? 199.894 177.515 197.043 1.00 21.37  ?  417 ILE A N     1 
ATOM   3158  C  CA    . ILE A 1 398 ? 198.574 177.105 196.597 1.00 9.16   ?  417 ILE A CA    1 
ATOM   3159  C  C     . ILE A 1 398 ? 198.557 177.144 195.078 1.00 13.23  ?  417 ILE A C     1 
ATOM   3160  O  O     . ILE A 1 398 ? 198.766 178.202 194.473 1.00 34.18  ?  417 ILE A O     1 
ATOM   3161  C  CB    . ILE A 1 398 ? 197.487 178.025 197.177 1.00 22.72  ?  417 ILE A CB    1 
ATOM   3162  C  CG1   . ILE A 1 398 ? 197.702 178.242 198.676 1.00 21.30  ?  417 ILE A CG1   1 
ATOM   3163  C  CG2   . ILE A 1 398 ? 196.108 177.451 196.905 1.00 31.90  ?  417 ILE A CG2   1 
ATOM   3164  C  CD1   . ILE A 1 398 ? 197.646 176.981 199.494 1.00 33.24  ?  417 ILE A CD1   1 
ATOM   3165  N  N     . GLY A 1 399 ? 198.311 175.996 194.461 1.00 14.71  ?  418 GLY A N     1 
ATOM   3166  C  CA    . GLY A 1 399 ? 198.141 175.936 193.029 1.00 25.91  ?  418 GLY A CA    1 
ATOM   3167  C  C     . GLY A 1 399 ? 196.689 175.675 192.708 1.00 22.41  ?  418 GLY A C     1 
ATOM   3168  O  O     . GLY A 1 399 ? 196.166 174.591 192.988 1.00 27.14  ?  418 GLY A O     1 
ATOM   3169  N  N     . VAL A 1 400 ? 196.021 176.683 192.152 1.00 17.02  ?  419 VAL A N     1 
ATOM   3170  C  CA    . VAL A 1 400 ? 194.610 176.576 191.795 1.00 23.98  ?  419 VAL A CA    1 
ATOM   3171  C  C     . VAL A 1 400 ? 194.556 175.839 190.461 1.00 28.15  ?  419 VAL A C     1 
ATOM   3172  O  O     . VAL A 1 400 ? 194.734 176.444 189.404 1.00 29.21  ?  419 VAL A O     1 
ATOM   3173  C  CB    . VAL A 1 400 ? 193.936 177.948 191.714 1.00 28.79  ?  419 VAL A CB    1 
ATOM   3174  C  CG1   . VAL A 1 400 ? 192.463 177.797 191.365 1.00 34.70  ?  419 VAL A CG1   1 
ATOM   3175  C  CG2   . VAL A 1 400 ? 194.117 178.712 193.014 1.00 26.35  ?  419 VAL A CG2   1 
ATOM   3176  N  N     . ASP A 1 401 ? 194.328 174.530 190.500 1.00 29.06  ?  420 ASP A N     1 
ATOM   3177  C  CA    . ASP A 1 401 ? 194.347 173.745 189.277 1.00 32.14  ?  420 ASP A CA    1 
ATOM   3178  C  C     . ASP A 1 401 ? 192.942 173.685 188.684 1.00 32.22  ?  420 ASP A C     1 
ATOM   3179  O  O     . ASP A 1 401 ? 191.992 174.273 189.208 1.00 34.36  ?  420 ASP A O     1 
ATOM   3180  C  CB    . ASP A 1 401 ? 194.933 172.351 189.533 1.00 39.83  ?  420 ASP A CB    1 
ATOM   3181  C  CG    . ASP A 1 401 ? 194.215 171.595 190.635 1.00 42.59  ?  420 ASP A CG    1 
ATOM   3182  O  OD1   . ASP A 1 401 ? 193.012 171.835 190.848 1.00 42.29  ?  420 ASP A OD1   1 
ATOM   3183  O  OD2   . ASP A 1 401 ? 194.861 170.755 191.293 1.00 41.36  -1 420 ASP A OD2   1 
ATOM   3184  N  N     . HIS A 1 402 ? 192.819 172.968 187.566 1.00 37.82  ?  421 HIS A N     1 
ATOM   3185  C  CA    . HIS A 1 402 ? 191.569 172.887 186.811 1.00 34.44  ?  421 HIS A CA    1 
ATOM   3186  C  C     . HIS A 1 402 ? 191.091 174.274 186.391 1.00 45.49  ?  421 HIS A C     1 
ATOM   3187  O  O     . HIS A 1 402 ? 189.897 174.575 186.421 1.00 53.69  ?  421 HIS A O     1 
ATOM   3188  C  CB    . HIS A 1 402 ? 190.485 172.150 187.600 1.00 37.03  ?  421 HIS A CB    1 
ATOM   3189  C  CG    . HIS A 1 402 ? 190.743 170.685 187.761 1.00 44.62  ?  421 HIS A CG    1 
ATOM   3190  N  ND1   . HIS A 1 402 ? 191.850 170.193 188.418 1.00 46.27  ?  421 HIS A ND1   1 
ATOM   3191  C  CD2   . HIS A 1 402 ? 190.039 169.605 187.348 1.00 44.29  ?  421 HIS A CD2   1 
ATOM   3192  C  CE1   . HIS A 1 402 ? 191.815 168.873 188.405 1.00 43.06  ?  421 HIS A CE1   1 
ATOM   3193  N  NE2   . HIS A 1 402 ? 190.727 168.491 187.762 1.00 43.22  ?  421 HIS A NE2   1 
ATOM   3194  N  N     . ILE A 1 403 ? 192.039 175.135 186.020 1.00 45.43  ?  422 ILE A N     1 
ATOM   3195  C  CA    . ILE A 1 403 ? 191.705 176.436 185.451 1.00 45.18  ?  422 ILE A CA    1 
ATOM   3196  C  C     . ILE A 1 403 ? 191.576 176.360 183.932 1.00 41.96  ?  422 ILE A C     1 
ATOM   3197  O  O     . ILE A 1 403 ? 190.862 177.180 183.334 1.00 50.31  ?  422 ILE A O     1 
ATOM   3198  C  CB    . ILE A 1 403 ? 192.756 177.479 185.882 1.00 41.75  ?  422 ILE A CB    1 
ATOM   3199  C  CG1   . ILE A 1 403 ? 192.667 177.726 187.389 1.00 40.89  ?  422 ILE A CG1   1 
ATOM   3200  C  CG2   . ILE A 1 403 ? 192.582 178.798 185.144 1.00 43.87  ?  422 ILE A CG2   1 
ATOM   3201  C  CD1   . ILE A 1 403 ? 191.540 178.645 187.803 1.00 36.93  ?  422 ILE A CD1   1 
ATOM   3202  N  N     . GLN A 1 404 ? 192.213 175.373 183.297 1.00 45.09  ?  423 GLN A N     1 
ATOM   3203  C  CA    . GLN A 1 404 ? 192.117 175.224 181.848 1.00 50.13  ?  423 GLN A CA    1 
ATOM   3204  C  C     . GLN A 1 404 ? 190.676 175.038 181.391 1.00 55.52  ?  423 GLN A C     1 
ATOM   3205  O  O     . GLN A 1 404 ? 190.333 175.408 180.262 1.00 58.28  ?  423 GLN A O     1 
ATOM   3206  C  CB    . GLN A 1 404 ? 192.978 174.044 181.393 1.00 54.04  ?  423 GLN A CB    1 
ATOM   3207  C  CG    . GLN A 1 404 ? 193.180 173.944 179.890 1.00 57.57  ?  423 GLN A CG    1 
ATOM   3208  C  CD    . GLN A 1 404 ? 193.735 175.216 179.283 1.00 57.60  ?  423 GLN A CD    1 
ATOM   3209  O  OE1   . GLN A 1 404 ? 193.069 175.881 178.492 1.00 56.66  ?  423 GLN A OE1   1 
ATOM   3210  N  NE2   . GLN A 1 404 ? 194.963 175.561 179.652 1.00 54.07  ?  423 GLN A NE2   1 
ATOM   3211  N  N     . ASP A 1 405 ? 189.816 174.483 182.250 1.00 55.57  ?  424 ASP A N     1 
ATOM   3212  C  CA    . ASP A 1 405 ? 188.420 174.283 181.870 1.00 56.07  ?  424 ASP A CA    1 
ATOM   3213  C  C     . ASP A 1 405 ? 187.718 175.615 181.624 1.00 59.92  ?  424 ASP A C     1 
ATOM   3214  O  O     . ASP A 1 405 ? 187.070 175.805 180.590 1.00 64.68  ?  424 ASP A O     1 
ATOM   3215  C  CB    . ASP A 1 405 ? 187.690 173.461 182.938 1.00 58.08  ?  424 ASP A CB    1 
ATOM   3216  C  CG    . ASP A 1 405 ? 187.709 174.116 184.311 1.00 63.39  ?  424 ASP A CG    1 
ATOM   3217  O  OD1   . ASP A 1 405 ? 188.203 175.256 184.435 1.00 61.22  ?  424 ASP A OD1   1 
ATOM   3218  O  OD2   . ASP A 1 405 ? 187.225 173.484 185.273 1.00 65.23  -1 424 ASP A OD2   1 
ATOM   3219  N  N     . VAL A 1 406 ? 187.845 176.560 182.558 1.00 54.36  ?  425 VAL A N     1 
ATOM   3220  C  CA    . VAL A 1 406 ? 187.266 177.876 182.324 1.00 52.72  ?  425 VAL A CA    1 
ATOM   3221  C  C     . VAL A 1 406 ? 188.042 178.631 181.251 1.00 49.37  ?  425 VAL A C     1 
ATOM   3222  O  O     . VAL A 1 406 ? 187.445 179.417 180.504 1.00 58.96  ?  425 VAL A O     1 
ATOM   3223  C  CB    . VAL A 1 406 ? 187.162 178.673 183.643 1.00 52.64  ?  425 VAL A CB    1 
ATOM   3224  C  CG1   . VAL A 1 406 ? 188.526 178.923 184.246 1.00 51.85  ?  425 VAL A CG1   1 
ATOM   3225  C  CG2   . VAL A 1 406 ? 186.415 179.985 183.423 1.00 51.75  ?  425 VAL A CG2   1 
ATOM   3226  N  N     . ILE A 1 407 ? 189.352 178.378 181.124 1.00 45.26  ?  426 ILE A N     1 
ATOM   3227  C  CA    . ILE A 1 407 ? 190.136 179.001 180.057 1.00 51.48  ?  426 ILE A CA    1 
ATOM   3228  C  C     . ILE A 1 407 ? 189.536 178.679 178.694 1.00 55.56  ?  426 ILE A C     1 
ATOM   3229  O  O     . ILE A 1 407 ? 189.291 179.574 177.876 1.00 61.39  ?  426 ILE A O     1 
ATOM   3230  C  CB    . ILE A 1 407 ? 191.608 178.551 180.130 1.00 57.06  ?  426 ILE A CB    1 
ATOM   3231  C  CG1   . ILE A 1 407 ? 192.321 179.127 181.354 1.00 55.34  ?  426 ILE A CG1   1 
ATOM   3232  C  CG2   . ILE A 1 407 ? 192.347 178.958 178.864 1.00 59.03  ?  426 ILE A CG2   1 
ATOM   3233  C  CD1   . ILE A 1 407 ? 192.656 180.595 181.226 1.00 53.57  ?  426 ILE A CD1   1 
ATOM   3234  N  N     . ASP A 1 408 ? 189.281 177.397 178.431 1.00 56.80  ?  427 ASP A N     1 
ATOM   3235  C  CA    . ASP A 1 408 ? 188.804 176.979 177.119 1.00 61.56  ?  427 ASP A CA    1 
ATOM   3236  C  C     . ASP A 1 408 ? 187.285 176.892 177.018 1.00 61.36  ?  427 ASP A C     1 
ATOM   3237  O  O     . ASP A 1 408 ? 186.774 176.564 175.942 1.00 60.87  ?  427 ASP A O     1 
ATOM   3238  C  CB    . ASP A 1 408 ? 189.435 175.633 176.718 1.00 63.14  ?  427 ASP A CB    1 
ATOM   3239  C  CG    . ASP A 1 408 ? 188.843 174.447 177.461 1.00 66.20  ?  427 ASP A CG    1 
ATOM   3240  O  OD1   . ASP A 1 408 ? 188.269 174.632 178.551 1.00 66.44  ?  427 ASP A OD1   1 
ATOM   3241  O  OD2   . ASP A 1 408 ? 188.955 173.315 176.945 1.00 65.16  -1 427 ASP A OD2   1 
ATOM   3242  N  N     . SER A 1 409 ? 186.553 177.172 178.098 1.00 58.73  ?  428 SER A N     1 
ATOM   3243  C  CA    . SER A 1 409 ? 185.099 177.226 178.011 1.00 58.07  ?  428 SER A CA    1 
ATOM   3244  C  C     . SER A 1 409 ? 184.569 178.654 177.939 1.00 61.73  ?  428 SER A C     1 
ATOM   3245  O  O     . SER A 1 409 ? 183.631 178.923 177.183 1.00 63.68  ?  428 SER A O     1 
ATOM   3246  C  CB    . SER A 1 409 ? 184.473 176.501 179.206 1.00 63.30  ?  428 SER A CB    1 
ATOM   3247  O  OG    . SER A 1 409 ? 183.058 176.510 179.128 1.00 66.40  ?  428 SER A OG    1 
ATOM   3248  N  N     . LEU A 1 410 ? 185.147 179.578 178.708 1.00 64.97  ?  429 LEU A N     1 
ATOM   3249  C  CA    . LEU A 1 410 ? 184.680 180.959 178.744 1.00 60.10  ?  429 LEU A CA    1 
ATOM   3250  C  C     . LEU A 1 410 ? 185.702 181.925 178.158 1.00 55.91  ?  429 LEU A C     1 
ATOM   3251  O  O     . LEU A 1 410 ? 185.381 182.686 177.241 1.00 57.20  ?  429 LEU A O     1 
ATOM   3252  C  CB    . LEU A 1 410 ? 184.332 181.361 180.184 1.00 59.39  ?  429 LEU A CB    1 
ATOM   3253  C  CG    . LEU A 1 410 ? 182.914 181.100 180.701 1.00 61.75  ?  429 LEU A CG    1 
ATOM   3254  C  CD1   . LEU A 1 410 ? 181.900 181.911 179.906 1.00 58.48  ?  429 LEU A CD1   1 
ATOM   3255  C  CD2   . LEU A 1 410 ? 182.563 179.621 180.679 1.00 62.71  ?  429 LEU A CD2   1 
ATOM   3256  N  N     . GLY A 1 411 ? 186.923 181.913 178.660 1.00 51.96  ?  430 GLY A N     1 
ATOM   3257  C  CA    . GLY A 1 411 ? 187.953 182.806 178.167 1.00 53.89  ?  430 GLY A CA    1 
ATOM   3258  C  C     . GLY A 1 411 ? 188.907 183.194 179.275 1.00 59.19  ?  430 GLY A C     1 
ATOM   3259  O  O     . GLY A 1 411 ? 188.685 182.918 180.454 1.00 63.62  ?  430 GLY A O     1 
ATOM   3260  N  N     . TYR A 1 412 ? 189.994 183.854 178.868 1.00 49.55  ?  431 TYR A N     1 
ATOM   3261  C  CA    . TYR A 1 412 ? 190.997 184.286 179.835 1.00 44.88  ?  431 TYR A CA    1 
ATOM   3262  C  C     . TYR A 1 412 ? 190.427 185.310 180.806 1.00 43.91  ?  431 TYR A C     1 
ATOM   3263  O  O     . TYR A 1 412 ? 190.785 185.315 181.987 1.00 44.16  ?  431 TYR A O     1 
ATOM   3264  C  CB    . TYR A 1 412 ? 192.218 184.852 179.115 1.00 42.86  ?  431 TYR A CB    1 
ATOM   3265  C  CG    . TYR A 1 412 ? 192.914 183.862 178.212 1.00 42.48  ?  431 TYR A CG    1 
ATOM   3266  C  CD1   . TYR A 1 412 ? 192.614 183.794 176.858 1.00 41.87  ?  431 TYR A CD1   1 
ATOM   3267  C  CD2   . TYR A 1 412 ? 193.872 182.994 178.715 1.00 46.24  ?  431 TYR A CD2   1 
ATOM   3268  C  CE1   . TYR A 1 412 ? 193.250 182.889 176.031 1.00 47.93  ?  431 TYR A CE1   1 
ATOM   3269  C  CE2   . TYR A 1 412 ? 194.513 182.087 177.898 1.00 47.23  ?  431 TYR A CE2   1 
ATOM   3270  C  CZ    . TYR A 1 412 ? 194.199 182.038 176.557 1.00 50.21  ?  431 TYR A CZ    1 
ATOM   3271  O  OH    . TYR A 1 412 ? 194.837 181.133 175.742 1.00 52.44  ?  431 TYR A OH    1 
ATOM   3272  N  N     . ALA A 1 413 ? 189.532 186.179 180.331 1.00 43.50  ?  432 ALA A N     1 
ATOM   3273  C  CA    . ALA A 1 413 ? 188.923 187.171 181.211 1.00 45.07  ?  432 ALA A CA    1 
ATOM   3274  C  C     . ALA A 1 413 ? 188.105 186.503 182.310 1.00 49.71  ?  432 ALA A C     1 
ATOM   3275  O  O     . ALA A 1 413 ? 188.278 186.798 183.499 1.00 56.19  ?  432 ALA A O     1 
ATOM   3276  C  CB    . ALA A 1 413 ? 188.053 188.128 180.397 1.00 44.27  ?  432 ALA A CB    1 
ATOM   3277  N  N     . TRP A 1 414 ? 187.211 185.586 181.929 1.00 41.83  ?  433 TRP A N     1 
ATOM   3278  C  CA    . TRP A 1 414 ? 186.397 184.893 182.922 1.00 40.94  ?  433 TRP A CA    1 
ATOM   3279  C  C     . TRP A 1 414 ? 187.244 184.011 183.828 1.00 43.39  ?  433 TRP A C     1 
ATOM   3280  O  O     . TRP A 1 414 ? 186.920 183.847 185.008 1.00 49.08  ?  433 TRP A O     1 
ATOM   3281  C  CB    . TRP A 1 414 ? 185.321 184.057 182.233 1.00 45.44  ?  433 TRP A CB    1 
ATOM   3282  C  CG    . TRP A 1 414 ? 184.054 184.797 181.932 1.00 42.50  ?  433 TRP A CG    1 
ATOM   3283  C  CD1   . TRP A 1 414 ? 183.570 185.127 180.701 1.00 49.35  ?  433 TRP A CD1   1 
ATOM   3284  C  CD2   . TRP A 1 414 ? 183.097 185.282 182.882 1.00 41.68  ?  433 TRP A CD2   1 
ATOM   3285  N  NE1   . TRP A 1 414 ? 182.375 185.794 180.824 1.00 51.52  ?  433 TRP A NE1   1 
ATOM   3286  C  CE2   . TRP A 1 414 ? 182.064 185.902 182.154 1.00 44.79  ?  433 TRP A CE2   1 
ATOM   3287  C  CE3   . TRP A 1 414 ? 183.020 185.260 184.277 1.00 47.91  ?  433 TRP A CE3   1 
ATOM   3288  C  CZ2   . TRP A 1 414 ? 180.962 186.488 182.774 1.00 48.59  ?  433 TRP A CZ2   1 
ATOM   3289  C  CZ3   . TRP A 1 414 ? 181.926 185.839 184.891 1.00 53.43  ?  433 TRP A CZ3   1 
ATOM   3290  C  CH2   . TRP A 1 414 ? 180.913 186.447 184.140 1.00 52.21  ?  433 TRP A CH2   1 
ATOM   3291  N  N     . ALA A 1 415 ? 188.327 183.435 183.305 1.00 39.13  ?  434 ALA A N     1 
ATOM   3292  C  CA    . ALA A 1 415 ? 189.210 182.642 184.154 1.00 43.27  ?  434 ALA A CA    1 
ATOM   3293  C  C     . ALA A 1 415 ? 189.923 183.516 185.177 1.00 41.83  ?  434 ALA A C     1 
ATOM   3294  O  O     . ALA A 1 415 ? 190.084 183.125 186.340 1.00 50.88  ?  434 ALA A O     1 
ATOM   3295  C  CB    . ALA A 1 415 ? 190.223 181.893 183.297 1.00 46.15  ?  434 ALA A CB    1 
ATOM   3296  N  N     . ASP A 1 416 ? 190.361 184.703 184.759 1.00 38.01  ?  435 ASP A N     1 
ATOM   3297  C  CA    . ASP A 1 416 ? 190.965 185.640 185.694 1.00 36.25  ?  435 ASP A CA    1 
ATOM   3298  C  C     . ASP A 1 416 ? 189.949 186.100 186.730 1.00 34.52  ?  435 ASP A C     1 
ATOM   3299  O  O     . ASP A 1 416 ? 190.306 186.344 187.888 1.00 41.44  ?  435 ASP A O     1 
ATOM   3300  C  CB    . ASP A 1 416 ? 191.544 186.827 184.924 1.00 40.45  ?  435 ASP A CB    1 
ATOM   3301  C  CG    . ASP A 1 416 ? 192.860 187.306 185.497 1.00 46.39  ?  435 ASP A CG    1 
ATOM   3302  O  OD1   . ASP A 1 416 ? 193.234 186.853 186.599 1.00 43.31  ?  435 ASP A OD1   1 
ATOM   3303  O  OD2   . ASP A 1 416 ? 193.526 188.129 184.835 1.00 46.97  -1 435 ASP A OD2   1 
ATOM   3304  N  N     . GLN A 1 417 ? 188.678 186.205 186.340 1.00 33.90  ?  436 GLN A N     1 
ATOM   3305  C  CA    . GLN A 1 417 ? 187.638 186.523 187.314 1.00 33.10  ?  436 GLN A CA    1 
ATOM   3306  C  C     . GLN A 1 417 ? 187.391 185.363 188.273 1.00 34.50  ?  436 GLN A C     1 
ATOM   3307  O  O     . GLN A 1 417 ? 187.061 185.587 189.440 1.00 40.61  ?  436 GLN A O     1 
ATOM   3308  C  CB    . GLN A 1 417 ? 186.346 186.912 186.599 1.00 33.24  ?  436 GLN A CB    1 
ATOM   3309  C  CG    . GLN A 1 417 ? 186.511 188.084 185.646 1.00 34.88  ?  436 GLN A CG    1 
ATOM   3310  C  CD    . GLN A 1 417 ? 187.219 189.267 186.279 1.00 44.20  ?  436 GLN A CD    1 
ATOM   3311  O  OE1   . GLN A 1 417 ? 186.989 189.598 187.442 1.00 48.76  ?  436 GLN A OE1   1 
ATOM   3312  N  NE2   . GLN A 1 417 ? 188.092 189.910 185.513 1.00 41.06  ?  436 GLN A NE2   1 
ATOM   3313  N  N     . ALA A 1 418 ? 187.531 184.124 187.798 1.00 36.60  ?  437 ALA A N     1 
ATOM   3314  C  CA    . ALA A 1 418 ? 187.504 182.978 188.702 1.00 38.52  ?  437 ALA A CA    1 
ATOM   3315  C  C     . ALA A 1 418 ? 188.643 183.060 189.706 1.00 35.77  ?  437 ALA A C     1 
ATOM   3316  O  O     . ALA A 1 418 ? 188.462 182.775 190.896 1.00 46.51  ?  437 ALA A O     1 
ATOM   3317  C  CB    . ALA A 1 418 ? 187.595 181.675 187.910 1.00 39.52  ?  437 ALA A CB    1 
ATOM   3318  N  N     . LEU A 1 419 ? 189.829 183.441 189.231 1.00 23.91  ?  438 LEU A N     1 
ATOM   3319  C  CA    . LEU A 1 419 ? 190.957 183.663 190.128 1.00 15.53  ?  438 LEU A CA    1 
ATOM   3320  C  C     . LEU A 1 419 ? 190.633 184.741 191.155 1.00 28.08  ?  438 LEU A C     1 
ATOM   3321  O  O     . LEU A 1 419 ? 190.958 184.600 192.340 1.00 36.71  ?  438 LEU A O     1 
ATOM   3322  C  CB    . LEU A 1 419 ? 192.199 184.046 189.321 1.00 27.96  ?  438 LEU A CB    1 
ATOM   3323  C  CG    . LEU A 1 419 ? 193.170 182.917 188.971 1.00 38.84  ?  438 LEU A CG    1 
ATOM   3324  C  CD1   . LEU A 1 419 ? 194.377 183.461 188.223 1.00 33.92  ?  438 LEU A CD1   1 
ATOM   3325  C  CD2   . LEU A 1 419 ? 193.605 182.186 190.229 1.00 33.75  ?  438 LEU A CD2   1 
ATOM   3326  N  N     . LEU A 1 420 ? 189.993 185.828 190.716 1.00 31.89  ?  439 LEU A N     1 
ATOM   3327  C  CA    . LEU A 1 420 ? 189.605 186.888 191.644 1.00 21.92  ?  439 LEU A CA    1 
ATOM   3328  C  C     . LEU A 1 420 ? 188.600 186.390 192.676 1.00 30.61  ?  439 LEU A C     1 
ATOM   3329  O  O     . LEU A 1 420 ? 188.686 186.748 193.853 1.00 38.02  ?  439 LEU A O     1 
ATOM   3330  C  CB    . LEU A 1 420 ? 189.034 188.086 190.887 1.00 20.09  ?  439 LEU A CB    1 
ATOM   3331  C  CG    . LEU A 1 420 ? 190.020 188.922 190.073 1.00 16.76  ?  439 LEU A CG    1 
ATOM   3332  C  CD1   . LEU A 1 420 ? 189.314 190.118 189.473 1.00 18.66  ?  439 LEU A CD1   1 
ATOM   3333  C  CD2   . LEU A 1 420 ? 191.184 189.366 190.939 1.00 25.46  ?  439 LEU A CD2   1 
ATOM   3334  N  N     . GLU A 1 421 ? 187.629 185.578 192.256 1.00 36.42  ?  440 GLU A N     1 
ATOM   3335  C  CA    . GLU A 1 421 ? 186.668 185.032 193.212 1.00 32.22  ?  440 GLU A CA    1 
ATOM   3336  C  C     . GLU A 1 421 ? 187.355 184.125 194.227 1.00 34.26  ?  440 GLU A C     1 
ATOM   3337  O  O     . GLU A 1 421 ? 187.040 184.164 195.424 1.00 45.84  ?  440 GLU A O     1 
ATOM   3338  C  CB    . GLU A 1 421 ? 185.558 184.277 192.480 1.00 37.26  ?  440 GLU A CB    1 
ATOM   3339  C  CG    . GLU A 1 421 ? 184.678 185.155 191.604 1.00 44.18  ?  440 GLU A CG    1 
ATOM   3340  C  CD    . GLU A 1 421 ? 183.480 184.409 191.050 1.00 51.80  ?  440 GLU A CD    1 
ATOM   3341  O  OE1   . GLU A 1 421 ? 183.340 183.204 191.347 1.00 53.65  ?  440 GLU A OE1   1 
ATOM   3342  O  OE2   . GLU A 1 421 ? 182.679 185.026 190.316 1.00 50.07  -1 440 GLU A OE2   1 
ATOM   3343  N  N     . VAL A 1 422 ? 188.302 183.304 193.767 1.00 24.37  ?  441 VAL A N     1 
ATOM   3344  C  CA    . VAL A 1 422 ? 189.039 182.432 194.678 1.00 23.53  ?  441 VAL A CA    1 
ATOM   3345  C  C     . VAL A 1 422 ? 189.846 183.255 195.677 1.00 29.26  ?  441 VAL A C     1 
ATOM   3346  O  O     . VAL A 1 422 ? 189.844 182.971 196.883 1.00 40.32  ?  441 VAL A O     1 
ATOM   3347  C  CB    . VAL A 1 422 ? 189.934 181.462 193.881 1.00 29.87  ?  441 VAL A CB    1 
ATOM   3348  C  CG1   . VAL A 1 422 ? 190.829 180.679 194.815 1.00 31.90  ?  441 VAL A CG1   1 
ATOM   3349  C  CG2   . VAL A 1 422 ? 189.084 180.509 193.053 1.00 31.31  ?  441 VAL A CG2   1 
ATOM   3350  N  N     . VAL A 1 423 ? 190.539 184.293 195.201 1.00 34.50  ?  442 VAL A N     1 
ATOM   3351  C  CA    . VAL A 1 423 ? 191.342 185.095 196.120 1.00 28.94  ?  442 VAL A CA    1 
ATOM   3352  C  C     . VAL A 1 423 ? 190.455 185.924 197.039 1.00 31.10  ?  442 VAL A C     1 
ATOM   3353  O  O     . VAL A 1 423 ? 190.853 186.245 198.161 1.00 36.19  ?  442 VAL A O     1 
ATOM   3354  C  CB    . VAL A 1 423 ? 192.358 185.975 195.365 1.00 25.56  ?  442 VAL A CB    1 
ATOM   3355  C  CG1   . VAL A 1 423 ? 193.196 185.131 194.423 1.00 33.06  ?  442 VAL A CG1   1 
ATOM   3356  C  CG2   . VAL A 1 423 ? 191.668 187.100 194.620 1.00 28.85  ?  442 VAL A CG2   1 
ATOM   3357  N  N     . ASN A 1 424 ? 189.239 186.267 196.608 1.00 30.71  ?  443 ASN A N     1 
ATOM   3358  C  CA    . ASN A 1 424 ? 188.326 186.974 197.501 1.00 28.57  ?  443 ASN A CA    1 
ATOM   3359  C  C     . ASN A 1 424 ? 187.786 186.047 198.583 1.00 35.80  ?  443 ASN A C     1 
ATOM   3360  O  O     . ASN A 1 424 ? 187.579 186.472 199.725 1.00 45.84  ?  443 ASN A O     1 
ATOM   3361  C  CB    . ASN A 1 424 ? 187.187 187.607 196.704 1.00 30.12  ?  443 ASN A CB    1 
ATOM   3362  C  CG    . ASN A 1 424 ? 187.556 188.968 196.147 1.00 42.32  ?  443 ASN A CG    1 
ATOM   3363  O  OD1   . ASN A 1 424 ? 187.838 189.111 194.958 1.00 48.34  ?  443 ASN A OD1   1 
ATOM   3364  N  ND2   . ASN A 1 424 ? 187.563 189.976 197.011 1.00 39.13  ?  443 ASN A ND2   1 
ATOM   3365  N  N     . ARG A 1 425 ? 187.555 184.777 198.245 1.00 39.92  ?  444 ARG A N     1 
ATOM   3366  C  CA    . ARG A 1 425 ? 187.246 183.795 199.280 1.00 31.37  ?  444 ARG A CA    1 
ATOM   3367  C  C     . ARG A 1 425 ? 188.411 183.650 200.254 1.00 29.19  ?  444 ARG A C     1 
ATOM   3368  O  O     . ARG A 1 425 ? 188.212 183.557 201.474 1.00 36.91  ?  444 ARG A O     1 
ATOM   3369  C  CB    . ARG A 1 425 ? 186.907 182.449 198.644 1.00 32.00  ?  444 ARG A CB    1 
ATOM   3370  C  CG    . ARG A 1 425 ? 185.608 182.430 197.857 1.00 35.60  ?  444 ARG A CG    1 
ATOM   3371  C  CD    . ARG A 1 425 ? 184.979 181.046 197.901 1.00 29.44  ?  444 ARG A CD    1 
ATOM   3372  N  NE    . ARG A 1 425 ? 184.034 180.823 196.815 1.00 32.06  ?  444 ARG A NE    1 
ATOM   3373  C  CZ    . ARG A 1 425 ? 183.796 179.641 196.263 1.00 35.39  ?  444 ARG A CZ    1 
ATOM   3374  N  NH1   . ARG A 1 425 ? 184.423 178.550 196.671 1.00 41.19  1  444 ARG A NH1   1 
ATOM   3375  N  NH2   . ARG A 1 425 ? 182.904 179.551 195.281 1.00 37.52  ?  444 ARG A NH2   1 
ATOM   3376  N  N     . PHE A 1 426 ? 189.638 183.637 199.727 1.00 34.88  ?  445 PHE A N     1 
ATOM   3377  C  CA    . PHE A 1 426 ? 190.819 183.603 200.585 1.00 38.84  ?  445 PHE A CA    1 
ATOM   3378  C  C     . PHE A 1 426 ? 190.861 184.814 201.509 1.00 39.94  ?  445 PHE A C     1 
ATOM   3379  O  O     . PHE A 1 426 ? 191.193 184.691 202.691 1.00 45.21  ?  445 PHE A O     1 
ATOM   3380  C  CB    . PHE A 1 426 ? 192.089 183.546 199.736 1.00 42.15  ?  445 PHE A CB    1 
ATOM   3381  C  CG    . PHE A 1 426 ? 192.396 182.184 199.192 1.00 39.97  ?  445 PHE A CG    1 
ATOM   3382  C  CD1   . PHE A 1 426 ? 192.250 181.056 199.982 1.00 39.09  ?  445 PHE A CD1   1 
ATOM   3383  C  CD2   . PHE A 1 426 ? 192.847 182.031 197.892 1.00 37.36  ?  445 PHE A CD2   1 
ATOM   3384  C  CE1   . PHE A 1 426 ? 192.536 179.802 199.480 1.00 44.62  ?  445 PHE A CE1   1 
ATOM   3385  C  CE2   . PHE A 1 426 ? 193.139 180.780 197.387 1.00 35.49  ?  445 PHE A CE2   1 
ATOM   3386  C  CZ    . PHE A 1 426 ? 192.981 179.664 198.183 1.00 40.60  ?  445 PHE A CZ    1 
ATOM   3387  N  N     . ARG A 1 427 ? 190.543 185.995 200.979 1.00 37.50  ?  446 ARG A N     1 
ATOM   3388  C  CA    . ARG A 1 427 ? 190.510 187.207 201.790 1.00 38.73  ?  446 ARG A CA    1 
ATOM   3389  C  C     . ARG A 1 427 ? 189.444 187.132 202.873 1.00 37.10  ?  446 ARG A C     1 
ATOM   3390  O  O     . ARG A 1 427 ? 189.695 187.528 204.017 1.00 36.49  ?  446 ARG A O     1 
ATOM   3391  C  CB    . ARG A 1 427 ? 190.253 188.424 200.902 1.00 33.58  ?  446 ARG A CB    1 
ATOM   3392  C  CG    . ARG A 1 427 ? 191.366 188.748 199.927 1.00 30.77  ?  446 ARG A CG    1 
ATOM   3393  C  CD    . ARG A 1 427 ? 191.009 189.977 199.110 1.00 36.28  ?  446 ARG A CD    1 
ATOM   3394  N  NE    . ARG A 1 427 ? 191.954 190.213 198.026 1.00 37.03  ?  446 ARG A NE    1 
ATOM   3395  C  CZ    . ARG A 1 427 ? 193.074 190.910 198.148 1.00 34.81  ?  446 ARG A CZ    1 
ATOM   3396  N  NH1   . ARG A 1 427 ? 193.431 191.448 199.303 1.00 35.56  1  446 ARG A NH1   1 
ATOM   3397  N  NH2   . ARG A 1 427 ? 193.856 191.071 197.085 1.00 34.57  ?  446 ARG A NH2   1 
ATOM   3398  N  N     . GLU A 1 428 ? 188.251 186.639 202.533 1.00 36.44  ?  447 GLU A N     1 
ATOM   3399  C  CA    . GLU A 1 428 ? 187.173 186.572 203.511 1.00 35.41  ?  447 GLU A CA    1 
ATOM   3400  C  C     . GLU A 1 428 ? 187.431 185.521 204.582 1.00 34.83  ?  447 GLU A C     1 
ATOM   3401  O  O     . GLU A 1 428 ? 186.888 185.637 205.686 1.00 41.82  ?  447 GLU A O     1 
ATOM   3402  C  CB    . GLU A 1 428 ? 185.835 186.307 202.816 1.00 35.28  ?  447 GLU A CB    1 
ATOM   3403  C  CG    . GLU A 1 428 ? 185.508 184.841 202.588 1.00 38.71  ?  447 GLU A CG    1 
ATOM   3404  C  CD    . GLU A 1 428 ? 184.302 184.649 201.690 1.00 46.12  ?  447 GLU A CD    1 
ATOM   3405  O  OE1   . GLU A 1 428 ? 183.776 185.658 201.175 1.00 44.90  ?  447 GLU A OE1   1 
ATOM   3406  O  OE2   . GLU A 1 428 ? 183.879 183.490 201.502 1.00 47.22  -1 447 GLU A OE2   1 
ATOM   3407  N  N     . LYS A 1 429 ? 188.238 184.500 204.291 1.00 33.04  ?  448 LYS A N     1 
ATOM   3408  C  CA    . LYS A 1 429 ? 188.658 183.552 205.316 1.00 35.71  ?  448 LYS A CA    1 
ATOM   3409  C  C     . LYS A 1 429 ? 190.075 183.810 205.819 1.00 43.90  ?  448 LYS A C     1 
ATOM   3410  O  O     . LYS A 1 429 ? 190.640 182.959 206.513 1.00 47.78  ?  448 LYS A O     1 
ATOM   3411  C  CB    . LYS A 1 429 ? 188.537 182.115 204.809 1.00 37.58  ?  448 LYS A CB    1 
ATOM   3412  C  CG    . LYS A 1 429 ? 187.103 181.631 204.689 1.00 41.87  ?  448 LYS A CG    1 
ATOM   3413  C  CD    . LYS A 1 429 ? 187.041 180.231 204.112 1.00 47.61  ?  448 LYS A CD    1 
ATOM   3414  C  CE    . LYS A 1 429 ? 187.566 179.205 205.103 1.00 48.29  ?  448 LYS A CE    1 
ATOM   3415  N  NZ    . LYS A 1 429 ? 187.409 177.813 204.600 1.00 44.11  1  448 LYS A NZ    1 
ATOM   3416  N  N     . LEU A 1 430 ? 190.657 184.958 205.488 1.00 46.85  ?  449 LEU A N     1 
ATOM   3417  C  CA    . LEU A 1 430 ? 192.014 185.273 205.900 1.00 42.75  ?  449 LEU A CA    1 
ATOM   3418  C  C     . LEU A 1 430 ? 192.052 185.687 207.369 1.00 37.94  ?  449 LEU A C     1 
ATOM   3419  O  O     . LEU A 1 430 ? 191.023 185.929 208.005 1.00 42.25  ?  449 LEU A O     1 
ATOM   3420  C  CB    . LEU A 1 430 ? 192.598 186.381 205.021 1.00 42.11  ?  449 LEU A CB    1 
ATOM   3421  C  CG    . LEU A 1 430 ? 194.110 186.348 204.785 1.00 43.17  ?  449 LEU A CG    1 
ATOM   3422  C  CD1   . LEU A 1 430 ? 194.485 185.210 203.849 1.00 37.59  ?  449 LEU A CD1   1 
ATOM   3423  C  CD2   . LEU A 1 430 ? 194.597 187.680 204.237 1.00 40.43  ?  449 LEU A CD2   1 
ATOM   3424  N  N     . LYS A 1 431 ? 193.264 185.763 207.902 1.00 37.92  ?  450 LYS A N     1 
ATOM   3425  C  CA    . LYS A 1 431 ? 193.529 186.096 209.290 1.00 42.64  ?  450 LYS A CA    1 
ATOM   3426  C  C     . LYS A 1 431 ? 194.530 187.244 209.368 1.00 47.23  ?  450 LYS A C     1 
ATOM   3427  O  O     . LYS A 1 431 ? 195.306 187.466 208.431 1.00 49.58  ?  450 LYS A O     1 
ATOM   3428  C  CB    . LYS A 1 431 ? 194.068 184.872 210.045 1.00 44.09  ?  450 LYS A CB    1 
ATOM   3429  C  CG    . LYS A 1 431 ? 192.977 183.961 210.588 1.00 44.37  ?  450 LYS A CG    1 
ATOM   3430  C  CD    . LYS A 1 431 ? 193.441 182.516 210.655 1.00 45.37  ?  450 LYS A CD    1 
ATOM   3431  C  CE    . LYS A 1 431 ? 192.264 181.566 210.797 1.00 45.05  ?  450 LYS A CE    1 
ATOM   3432  N  NZ    . LYS A 1 431 ? 191.639 181.660 212.144 1.00 45.52  1  450 LYS A NZ    1 
ATOM   3433  N  N     . PRO A 1 432 ? 194.528 188.004 210.468 1.00 45.17  ?  451 PRO A N     1 
ATOM   3434  C  CA    . PRO A 1 432 ? 195.407 189.185 210.546 1.00 45.47  ?  451 PRO A CA    1 
ATOM   3435  C  C     . PRO A 1 432 ? 196.888 188.874 210.399 1.00 39.25  ?  451 PRO A C     1 
ATOM   3436  O  O     . PRO A 1 432 ? 197.633 189.712 209.875 1.00 35.28  ?  451 PRO A O     1 
ATOM   3437  C  CB    . PRO A 1 432 ? 195.091 189.760 211.934 1.00 44.46  ?  451 PRO A CB    1 
ATOM   3438  C  CG    . PRO A 1 432 ? 193.709 189.294 212.224 1.00 42.20  ?  451 PRO A CG    1 
ATOM   3439  C  CD    . PRO A 1 432 ? 193.608 187.927 211.617 1.00 40.56  ?  451 PRO A CD    1 
ATOM   3440  N  N     . ASP A 1 433 ? 197.344 187.703 210.846 1.00 42.47  ?  452 ASP A N     1 
ATOM   3441  C  CA    . ASP A 1 433 ? 198.759 187.353 210.812 1.00 45.41  ?  452 ASP A CA    1 
ATOM   3442  C  C     . ASP A 1 433 ? 199.099 186.427 209.647 1.00 46.24  ?  452 ASP A C     1 
ATOM   3443  O  O     . ASP A 1 433 ? 199.944 185.536 209.783 1.00 50.46  ?  452 ASP A O     1 
ATOM   3444  C  CB    . ASP A 1 433 ? 199.175 186.723 212.143 1.00 50.17  ?  452 ASP A CB    1 
ATOM   3445  C  CG    . ASP A 1 433 ? 200.678 186.759 212.362 1.00 50.86  ?  452 ASP A CG    1 
ATOM   3446  O  OD1   . ASP A 1 433 ? 201.214 187.855 212.628 1.00 44.56  ?  452 ASP A OD1   1 
ATOM   3447  O  OD2   . ASP A 1 433 ? 201.322 185.692 212.276 1.00 53.66  -1 452 ASP A OD2   1 
ATOM   3448  N  N     . GLN A 1 434 ? 198.450 186.616 208.500 1.00 39.02  ?  453 GLN A N     1 
ATOM   3449  C  CA    . GLN A 1 434 ? 198.696 185.813 207.312 1.00 38.09  ?  453 GLN A CA    1 
ATOM   3450  C  C     . GLN A 1 434 ? 199.028 186.725 206.142 1.00 40.55  ?  453 GLN A C     1 
ATOM   3451  O  O     . GLN A 1 434 ? 198.393 187.768 205.958 1.00 47.87  ?  453 GLN A O     1 
ATOM   3452  C  CB    . GLN A 1 434 ? 197.484 184.940 206.969 1.00 40.53  ?  453 GLN A CB    1 
ATOM   3453  C  CG    . GLN A 1 434 ? 197.062 184.002 208.087 1.00 43.41  ?  453 GLN A CG    1 
ATOM   3454  C  CD    . GLN A 1 434 ? 196.179 182.872 207.598 1.00 48.98  ?  453 GLN A CD    1 
ATOM   3455  O  OE1   . GLN A 1 434 ? 195.422 183.030 206.640 1.00 52.53  ?  453 GLN A OE1   1 
ATOM   3456  N  NE2   . GLN A 1 434 ? 196.267 181.724 208.258 1.00 46.75  ?  453 GLN A NE2   1 
ATOM   3457  N  N     . TYR A 1 435 ? 200.021 186.328 205.352 1.00 31.47  ?  454 TYR A N     1 
ATOM   3458  C  CA    . TYR A 1 435 ? 200.484 187.103 204.207 1.00 30.68  ?  454 TYR A CA    1 
ATOM   3459  C  C     . TYR A 1 435 ? 200.120 186.365 202.926 1.00 29.53  ?  454 TYR A C     1 
ATOM   3460  O  O     . TYR A 1 435 ? 200.569 185.237 202.711 1.00 44.82  ?  454 TYR A O     1 
ATOM   3461  C  CB    . TYR A 1 435 ? 201.993 187.331 204.302 1.00 39.78  ?  454 TYR A CB    1 
ATOM   3462  C  CG    . TYR A 1 435 ? 202.598 188.093 203.148 1.00 41.17  ?  454 TYR A CG    1 
ATOM   3463  C  CD1   . TYR A 1 435 ? 202.194 189.387 202.850 1.00 35.30  ?  454 TYR A CD1   1 
ATOM   3464  C  CD2   . TYR A 1 435 ? 203.593 187.523 202.367 1.00 44.22  ?  454 TYR A CD2   1 
ATOM   3465  C  CE1   . TYR A 1 435 ? 202.755 190.085 201.796 1.00 33.20  ?  454 TYR A CE1   1 
ATOM   3466  C  CE2   . TYR A 1 435 ? 204.160 188.211 201.316 1.00 40.87  ?  454 TYR A CE2   1 
ATOM   3467  C  CZ    . TYR A 1 435 ? 203.739 189.490 201.033 1.00 37.70  ?  454 TYR A CZ    1 
ATOM   3468  O  OH    . TYR A 1 435 ? 204.308 190.173 199.984 1.00 43.16  ?  454 TYR A OH    1 
ATOM   3469  N  N     . LEU A 1 436 ? 199.318 186.997 202.076 1.00 17.38  ?  455 LEU A N     1 
ATOM   3470  C  CA    . LEU A 1 436 ? 198.859 186.388 200.835 1.00 20.59  ?  455 LEU A CA    1 
ATOM   3471  C  C     . LEU A 1 436 ? 199.488 187.109 199.653 1.00 29.37  ?  455 LEU A C     1 
ATOM   3472  O  O     . LEU A 1 436 ? 199.458 188.343 199.586 1.00 41.69  ?  455 LEU A O     1 
ATOM   3473  C  CB    . LEU A 1 436 ? 197.333 186.432 200.731 1.00 27.60  ?  455 LEU A CB    1 
ATOM   3474  C  CG    . LEU A 1 436 ? 196.718 185.651 199.567 1.00 25.57  ?  455 LEU A CG    1 
ATOM   3475  C  CD1   . LEU A 1 436 ? 196.938 184.157 199.746 1.00 28.09  ?  455 LEU A CD1   1 
ATOM   3476  C  CD2   . LEU A 1 436 ? 195.238 185.967 199.434 1.00 28.70  ?  455 LEU A CD2   1 
ATOM   3477  N  N     . CYS A 1 437 ? 200.066 186.343 198.730 1.00 20.69  ?  456 CYS A N     1 
ATOM   3478  C  CA    . CYS A 1 437 ? 200.661 186.947 197.546 1.00 14.03  ?  456 CYS A CA    1 
ATOM   3479  C  C     . CYS A 1 437 ? 200.520 185.998 196.364 1.00 14.09  ?  456 CYS A C     1 
ATOM   3480  O  O     . CYS A 1 437 ? 200.225 184.814 196.525 1.00 36.04  ?  456 CYS A O     1 
ATOM   3481  C  CB    . CYS A 1 437 ? 202.132 187.313 197.775 1.00 17.83  ?  456 CYS A CB    1 
ATOM   3482  S  SG    . CYS A 1 437 ? 203.242 185.915 197.869 1.00 40.25  ?  456 CYS A SG    1 
ATOM   3483  N  N     . ARG A 1 438 ? 200.721 186.542 195.169 1.00 6.80   ?  457 ARG A N     1 
ATOM   3484  C  CA    . ARG A 1 438 ? 200.661 185.794 193.920 1.00 21.46  ?  457 ARG A CA    1 
ATOM   3485  C  C     . ARG A 1 438 ? 202.037 185.800 193.272 1.00 36.11  ?  457 ARG A C     1 
ATOM   3486  O  O     . ARG A 1 438 ? 202.634 186.868 193.101 1.00 36.50  ?  457 ARG A O     1 
ATOM   3487  C  CB    . ARG A 1 438 ? 199.631 186.416 192.978 1.00 17.73  ?  457 ARG A CB    1 
ATOM   3488  C  CG    . ARG A 1 438 ? 199.690 185.924 191.547 1.00 18.10  ?  457 ARG A CG    1 
ATOM   3489  C  CD    . ARG A 1 438 ? 198.441 186.356 190.808 1.00 18.85  ?  457 ARG A CD    1 
ATOM   3490  N  NE    . ARG A 1 438 ? 198.225 185.608 189.577 1.00 25.81  ?  457 ARG A NE    1 
ATOM   3491  C  CZ    . ARG A 1 438 ? 197.739 186.139 188.465 1.00 27.43  ?  457 ARG A CZ    1 
ATOM   3492  N  NH1   . ARG A 1 438 ? 197.404 187.417 188.399 1.00 26.60  1  457 ARG A NH1   1 
ATOM   3493  N  NH2   . ARG A 1 438 ? 197.584 185.369 187.392 1.00 27.75  ?  457 ARG A NH2   1 
ATOM   3494  N  N     . ILE A 1 439 ? 202.546 184.626 192.913 1.00 25.81  ?  458 ILE A N     1 
ATOM   3495  C  CA    . ILE A 1 439 ? 203.897 184.524 192.363 1.00 18.80  ?  458 ILE A CA    1 
ATOM   3496  C  C     . ILE A 1 439 ? 203.885 184.336 190.851 1.00 26.85  ?  458 ILE A C     1 
ATOM   3497  O  O     . ILE A 1 439 ? 204.561 185.066 190.127 1.00 46.18  ?  458 ILE A O     1 
ATOM   3498  C  CB    . ILE A 1 439 ? 204.699 183.408 193.070 1.00 13.94  ?  458 ILE A CB    1 
ATOM   3499  C  CG1   . ILE A 1 439 ? 203.902 182.105 193.151 1.00 31.74  ?  458 ILE A CG1   1 
ATOM   3500  C  CG2   . ILE A 1 439 ? 205.136 183.873 194.444 1.00 19.07  ?  458 ILE A CG2   1 
ATOM   3501  C  CD1   . ILE A 1 439 ? 204.767 180.879 193.344 1.00 38.24  ?  458 ILE A CD1   1 
ATOM   3502  N  N     . GLU A 1 440 ? 203.116 183.373 190.349 1.00 16.63  ?  459 GLU A N     1 
ATOM   3503  C  CA    . GLU A 1 440 ? 203.058 183.151 188.906 1.00 30.25  ?  459 GLU A CA    1 
ATOM   3504  C  C     . GLU A 1 440 ? 201.737 182.477 188.558 1.00 28.32  ?  459 GLU A C     1 
ATOM   3505  O  O     . GLU A 1 440 ? 201.532 181.305 188.888 1.00 36.44  ?  459 GLU A O     1 
ATOM   3506  C  CB    . GLU A 1 440 ? 204.250 182.323 188.434 1.00 35.48  ?  459 GLU A CB    1 
ATOM   3507  C  CG    . GLU A 1 440 ? 204.629 181.159 189.336 1.00 33.23  ?  459 GLU A CG    1 
ATOM   3508  C  CD    . GLU A 1 440 ? 205.827 180.393 188.809 1.00 41.09  ?  459 GLU A CD    1 
ATOM   3509  O  OE1   . GLU A 1 440 ? 206.358 180.780 187.748 1.00 44.43  ?  459 GLU A OE1   1 
ATOM   3510  O  OE2   . GLU A 1 440 ? 206.241 179.408 189.456 1.00 41.33  -1 459 GLU A OE2   1 
ATOM   3511  N  N     . GLY A 1 441 ? 200.854 183.219 187.894 1.00 18.53  ?  460 GLY A N     1 
ATOM   3512  C  CA    . GLY A 1 441 ? 199.598 182.675 187.419 1.00 22.08  ?  460 GLY A CA    1 
ATOM   3513  C  C     . GLY A 1 441 ? 198.711 182.130 188.516 1.00 29.59  ?  460 GLY A C     1 
ATOM   3514  O  O     . GLY A 1 441 ? 198.269 182.870 189.400 1.00 32.01  ?  460 GLY A O     1 
ATOM   3515  N  N     . THR A 1 442 ? 198.446 180.828 188.464 1.00 29.96  ?  461 THR A N     1 
ATOM   3516  C  CA    . THR A 1 442 ? 197.588 180.152 189.426 1.00 25.29  ?  461 THR A CA    1 
ATOM   3517  C  C     . THR A 1 442 ? 198.328 179.739 190.691 1.00 22.80  ?  461 THR A C     1 
ATOM   3518  O  O     . THR A 1 442 ? 197.848 178.850 191.411 1.00 36.58  ?  461 THR A O     1 
ATOM   3519  C  CB    . THR A 1 442 ? 196.943 178.926 188.776 1.00 32.65  ?  461 THR A CB    1 
ATOM   3520  O  OG1   . THR A 1 442 ? 197.967 178.059 188.273 1.00 37.74  ?  461 THR A OG1   1 
ATOM   3521  C  CG2   . THR A 1 442 ? 196.045 179.353 187.624 1.00 29.59  ?  461 THR A CG2   1 
ATOM   3522  N  N     . GLN A 1 443 ? 199.477 180.348 190.972 1.00 17.46  ?  462 GLN A N     1 
ATOM   3523  C  CA    . GLN A 1 443 ? 200.298 179.998 192.123 1.00 14.45  ?  462 GLN A CA    1 
ATOM   3524  C  C     . GLN A 1 443 ? 200.316 181.156 193.113 1.00 26.31  ?  462 GLN A C     1 
ATOM   3525  O  O     . GLN A 1 443 ? 200.739 182.271 192.775 1.00 43.88  ?  462 GLN A O     1 
ATOM   3526  C  CB    . GLN A 1 443 ? 201.719 179.635 191.695 1.00 23.26  ?  462 GLN A CB    1 
ATOM   3527  C  CG    . GLN A 1 443 ? 201.878 178.184 191.285 1.00 32.21  ?  462 GLN A CG    1 
ATOM   3528  C  CD    . GLN A 1 443 ? 203.214 177.911 190.633 1.00 36.57  ?  462 GLN A CD    1 
ATOM   3529  O  OE1   . GLN A 1 443 ? 204.254 178.368 191.108 1.00 34.85  ?  462 GLN A OE1   1 
ATOM   3530  N  NE2   . GLN A 1 443 ? 203.195 177.169 189.534 1.00 35.27  ?  462 GLN A NE2   1 
ATOM   3531  N  N     . PHE A 1 444 ? 199.875 180.878 194.334 1.00 17.41  ?  463 PHE A N     1 
ATOM   3532  C  CA    . PHE A 1 444 ? 199.853 181.846 195.415 1.00 14.46  ?  463 PHE A CA    1 
ATOM   3533  C  C     . PHE A 1 444 ? 200.698 181.337 196.572 1.00 10.23  ?  463 PHE A C     1 
ATOM   3534  O  O     . PHE A 1 444 ? 200.991 180.146 196.679 1.00 19.90  ?  463 PHE A O     1 
ATOM   3535  C  CB    . PHE A 1 444 ? 198.421 182.119 195.891 1.00 10.28  ?  463 PHE A CB    1 
ATOM   3536  C  CG    . PHE A 1 444 ? 197.504 182.589 194.803 1.00 12.87  ?  463 PHE A CG    1 
ATOM   3537  C  CD1   . PHE A 1 444 ? 196.802 181.680 194.029 1.00 17.73  ?  463 PHE A CD1   1 
ATOM   3538  C  CD2   . PHE A 1 444 ? 197.357 183.940 194.542 1.00 17.22  ?  463 PHE A CD2   1 
ATOM   3539  C  CE1   . PHE A 1 444 ? 195.964 182.111 193.021 1.00 22.78  ?  463 PHE A CE1   1 
ATOM   3540  C  CE2   . PHE A 1 444 ? 196.521 184.377 193.535 1.00 18.54  ?  463 PHE A CE2   1 
ATOM   3541  C  CZ    . PHE A 1 444 ? 195.823 183.462 192.773 1.00 17.01  ?  463 PHE A CZ    1 
ATOM   3542  N  N     . VAL A 1 445 ? 201.088 182.263 197.438 1.00 13.53  ?  464 VAL A N     1 
ATOM   3543  C  CA    . VAL A 1 445 ? 201.835 181.954 198.647 1.00 8.92   ?  464 VAL A CA    1 
ATOM   3544  C  C     . VAL A 1 445 ? 201.045 182.482 199.830 1.00 21.85  ?  464 VAL A C     1 
ATOM   3545  O  O     . VAL A 1 445 ? 200.650 183.656 199.846 1.00 37.98  ?  464 VAL A O     1 
ATOM   3546  C  CB    . VAL A 1 445 ? 203.245 182.569 198.630 1.00 15.14  ?  464 VAL A CB    1 
ATOM   3547  C  CG1   . VAL A 1 445 ? 204.048 182.093 199.830 1.00 24.18  ?  464 VAL A CG1   1 
ATOM   3548  C  CG2   . VAL A 1 445 ? 203.950 182.262 197.339 1.00 24.73  ?  464 VAL A CG2   1 
ATOM   3549  N  N     . LEU A 1 446 ? 200.806 181.611 200.804 1.00 29.76  ?  465 LEU A N     1 
ATOM   3550  C  CA    . LEU A 1 446 ? 200.296 182.000 202.112 1.00 22.19  ?  465 LEU A CA    1 
ATOM   3551  C  C     . LEU A 1 446 ? 201.442 181.816 203.100 1.00 31.42  ?  465 LEU A C     1 
ATOM   3552  O  O     . LEU A 1 446 ? 201.886 180.689 203.342 1.00 51.19  ?  465 LEU A O     1 
ATOM   3553  C  CB    . LEU A 1 446 ? 199.071 181.174 202.502 1.00 25.95  ?  465 LEU A CB    1 
ATOM   3554  C  CG    . LEU A 1 446 ? 198.114 181.744 203.558 1.00 35.66  ?  465 LEU A CG    1 
ATOM   3555  C  CD1   . LEU A 1 446 ? 196.779 181.018 203.519 1.00 37.13  ?  465 LEU A CD1   1 
ATOM   3556  C  CD2   . LEU A 1 446 ? 198.702 181.670 204.960 1.00 39.73  ?  465 LEU A CD2   1 
ATOM   3557  N  N     . VAL A 1 447 ? 201.930 182.922 203.646 1.00 28.93  ?  466 VAL A N     1 
ATOM   3558  C  CA    . VAL A 1 447 ? 202.983 182.919 204.651 1.00 29.42  ?  466 VAL A CA    1 
ATOM   3559  C  C     . VAL A 1 447 ? 202.313 183.052 206.009 1.00 37.47  ?  466 VAL A C     1 
ATOM   3560  O  O     . VAL A 1 447 ? 201.638 184.054 206.282 1.00 50.95  ?  466 VAL A O     1 
ATOM   3561  C  CB    . VAL A 1 447 ? 203.992 184.054 204.415 1.00 30.97  ?  466 VAL A CB    1 
ATOM   3562  C  CG1   . VAL A 1 447 ? 205.079 184.032 205.477 1.00 36.18  ?  466 VAL A CG1   1 
ATOM   3563  C  CG2   . VAL A 1 447 ? 204.597 183.948 203.027 1.00 36.91  ?  466 VAL A CG2   1 
ATOM   3564  N  N     . SER A 1 448 ? 202.476 182.035 206.848 1.00 45.95  ?  467 SER A N     1 
ATOM   3565  C  CA    . SER A 1 448 ? 201.881 182.005 208.172 1.00 46.64  ?  467 SER A CA    1 
ATOM   3566  C  C     . SER A 1 448 ? 202.969 181.823 209.221 1.00 51.79  ?  467 SER A C     1 
ATOM   3567  O  O     . SER A 1 448 ? 204.127 181.532 208.910 1.00 59.18  ?  467 SER A O     1 
ATOM   3568  C  CB    . SER A 1 448 ? 200.838 180.885 208.282 1.00 55.16  ?  467 SER A CB    1 
ATOM   3569  O  OG    . SER A 1 448 ? 200.611 180.530 209.634 1.00 57.75  ?  467 SER A OG    1 
ATOM   3570  N  N     . LEU A 1 449 ? 202.576 181.988 210.480 1.00 60.92  ?  468 LEU A N     1 
ATOM   3571  C  CA    . LEU A 1 449 ? 203.476 181.854 211.618 1.00 66.01  ?  468 LEU A CA    1 
ATOM   3572  C  C     . LEU A 1 449 ? 202.914 180.865 212.628 1.00 71.01  ?  468 LEU A C     1 
ATOM   3573  O  O     . LEU A 1 449 ? 202.942 181.100 213.840 1.00 71.53  ?  468 LEU A O     1 
ATOM   3574  C  CB    . LEU A 1 449 ? 203.735 183.210 212.269 1.00 64.34  ?  468 LEU A CB    1 
ATOM   3575  C  CG    . LEU A 1 449 ? 204.486 184.226 211.406 1.00 64.97  ?  468 LEU A CG    1 
ATOM   3576  C  CD1   . LEU A 1 449 ? 204.740 185.512 212.179 1.00 67.82  ?  468 LEU A CD1   1 
ATOM   3577  C  CD2   . LEU A 1 449 ? 205.791 183.633 210.898 1.00 63.70  ?  468 LEU A CD2   1 
ATOM   3578  N  N     . GLU A 1 450 ? 202.401 179.739 212.142 1.00 78.57  ?  469 GLU A N     1 
ATOM   3579  C  CA    . GLU A 1 450 ? 201.831 178.699 212.987 1.00 76.47  ?  469 GLU A CA    1 
ATOM   3580  C  C     . GLU A 1 450 ? 202.747 177.483 212.974 1.00 75.81  ?  469 GLU A C     1 
ATOM   3581  O  O     . GLU A 1 450 ? 203.053 176.942 211.906 1.00 73.36  ?  469 GLU A O     1 
ATOM   3582  C  CB    . GLU A 1 450 ? 200.428 178.314 212.512 1.00 74.53  ?  469 GLU A CB    1 
ATOM   3583  C  CG    . GLU A 1 450 ? 199.436 179.469 212.505 1.00 75.09  ?  469 GLU A CG    1 
ATOM   3584  C  CD    . GLU A 1 450 ? 199.540 180.337 213.745 1.00 78.88  ?  469 GLU A CD    1 
ATOM   3585  O  OE1   . GLU A 1 450 ? 199.276 179.828 214.854 1.00 79.33  ?  469 GLU A OE1   1 
ATOM   3586  O  OE2   . GLU A 1 450 ? 199.886 181.530 213.611 1.00 80.12  -1 469 GLU A OE2   1 
ATOM   3587  N  N     . ASN A 1 451 ? 203.172 177.053 214.160 1.00 89.77  ?  470 ASN A N     1 
ATOM   3588  C  CA    . ASN A 1 451 ? 204.128 175.961 214.295 1.00 89.89  ?  470 ASN A CA    1 
ATOM   3589  C  C     . ASN A 1 451 ? 203.472 174.595 214.430 1.00 91.69  ?  470 ASN A C     1 
ATOM   3590  O  O     . ASN A 1 451 ? 204.058 173.596 213.999 1.00 91.39  ?  470 ASN A O     1 
ATOM   3591  C  CB    . ASN A 1 451 ? 205.031 176.197 215.511 1.00 90.48  ?  470 ASN A CB    1 
ATOM   3592  C  CG    . ASN A 1 451 ? 206.169 177.155 215.216 1.00 92.65  ?  470 ASN A CG    1 
ATOM   3593  O  OD1   . ASN A 1 451 ? 207.041 176.868 214.398 1.00 92.22  ?  470 ASN A OD1   1 
ATOM   3594  N  ND2   . ASN A 1 451 ? 206.165 178.301 215.886 1.00 91.81  ?  470 ASN A ND2   1 
ATOM   3595  N  N     . ASP A 1 452 ? 202.280 174.525 215.015 1.00 88.88  ?  471 ASP A N     1 
ATOM   3596  C  CA    . ASP A 1 452 ? 201.659 173.245 215.322 1.00 88.04  ?  471 ASP A CA    1 
ATOM   3597  C  C     . ASP A 1 452 ? 201.149 172.557 214.062 1.00 87.51  ?  471 ASP A C     1 
ATOM   3598  O  O     . ASP A 1 452 ? 200.539 173.184 213.188 1.00 89.69  ?  471 ASP A O     1 
ATOM   3599  C  CB    . ASP A 1 452 ? 200.513 173.431 216.315 1.00 90.33  ?  471 ASP A CB    1 
ATOM   3600  C  CG    . ASP A 1 452 ? 200.239 172.182 217.129 1.00 92.28  ?  471 ASP A CG    1 
ATOM   3601  O  OD1   . ASP A 1 452 ? 199.581 171.260 216.605 1.00 92.20  ?  471 ASP A OD1   1 
ATOM   3602  O  OD2   . ASP A 1 452 ? 200.686 172.122 218.294 1.00 92.93  -1 471 ASP A OD2   1 
ATOM   3603  N  N     . VAL A 1 453 ? 201.394 171.246 213.986 1.00 77.77  ?  472 VAL A N     1 
ATOM   3604  C  CA    . VAL A 1 453 ? 200.944 170.461 212.843 1.00 79.08  ?  472 VAL A CA    1 
ATOM   3605  C  C     . VAL A 1 453 ? 199.425 170.430 212.774 1.00 77.65  ?  472 VAL A C     1 
ATOM   3606  O  O     . VAL A 1 453 ? 198.848 170.427 211.682 1.00 82.87  ?  472 VAL A O     1 
ATOM   3607  C  CB    . VAL A 1 453 ? 201.535 169.039 212.903 1.00 80.05  ?  472 VAL A CB    1 
ATOM   3608  C  CG1   . VAL A 1 453 ? 201.294 168.308 211.592 1.00 76.53  ?  472 VAL A CG1   1 
ATOM   3609  C  CG2   . VAL A 1 453 ? 203.021 169.095 213.223 1.00 80.36  ?  472 VAL A CG2   1 
ATOM   3610  N  N     . SER A 1 454 ? 198.752 170.401 213.927 1.00 77.56  ?  473 SER A N     1 
ATOM   3611  C  CA    . SER A 1 454 ? 197.291 170.418 213.930 1.00 80.78  ?  473 SER A CA    1 
ATOM   3612  C  C     . SER A 1 454 ? 196.757 171.719 213.342 1.00 81.71  ?  473 SER A C     1 
ATOM   3613  O  O     . SER A 1 454 ? 195.811 171.713 212.544 1.00 81.80  ?  473 SER A O     1 
ATOM   3614  C  CB    . SER A 1 454 ? 196.767 170.213 215.351 1.00 82.50  ?  473 SER A CB    1 
ATOM   3615  O  OG    . SER A 1 454 ? 197.191 171.260 216.207 1.00 84.16  ?  473 SER A OG    1 
ATOM   3616  N  N     . ASN A 1 455 ? 197.353 172.850 213.728 1.00 78.76  ?  474 ASN A N     1 
ATOM   3617  C  CA    . ASN A 1 455 ? 196.939 174.131 213.163 1.00 74.14  ?  474 ASN A CA    1 
ATOM   3618  C  C     . ASN A 1 455 ? 197.219 174.191 211.667 1.00 72.55  ?  474 ASN A C     1 
ATOM   3619  O  O     . ASN A 1 455 ? 196.394 174.696 210.894 1.00 72.16  ?  474 ASN A O     1 
ATOM   3620  C  CB    . ASN A 1 455 ? 197.638 175.282 213.887 1.00 76.54  ?  474 ASN A CB    1 
ATOM   3621  C  CG    . ASN A 1 455 ? 197.220 175.398 215.340 1.00 79.08  ?  474 ASN A CG    1 
ATOM   3622  O  OD1   . ASN A 1 455 ? 198.060 175.445 216.238 1.00 80.68  ?  474 ASN A OD1   1 
ATOM   3623  N  ND2   . ASN A 1 455 ? 195.914 175.440 215.578 1.00 76.61  ?  474 ASN A ND2   1 
ATOM   3624  N  N     . ILE A 1 456 ? 198.379 173.685 211.239 1.00 62.99  ?  475 ILE A N     1 
ATOM   3625  C  CA    . ILE A 1 456 ? 198.692 173.681 209.812 1.00 59.81  ?  475 ILE A CA    1 
ATOM   3626  C  C     . ILE A 1 456 ? 197.686 172.827 209.050 1.00 59.26  ?  475 ILE A C     1 
ATOM   3627  O  O     . ILE A 1 456 ? 197.229 173.201 207.962 1.00 63.39  ?  475 ILE A O     1 
ATOM   3628  C  CB    . ILE A 1 456 ? 200.137 173.203 209.577 1.00 55.73  ?  475 ILE A CB    1 
ATOM   3629  C  CG1   . ILE A 1 456 ? 201.131 174.224 210.126 1.00 58.90  ?  475 ILE A CG1   1 
ATOM   3630  C  CG2   . ILE A 1 456 ? 200.388 172.996 208.094 1.00 58.10  ?  475 ILE A CG2   1 
ATOM   3631  C  CD1   . ILE A 1 456 ? 202.456 173.623 210.537 1.00 62.09  ?  475 ILE A CD1   1 
ATOM   3632  N  N     . THR A 1 457 ? 197.320 171.672 209.610 1.00 60.09  ?  476 THR A N     1 
ATOM   3633  C  CA    . THR A 1 457 ? 196.338 170.801 208.971 1.00 61.77  ?  476 THR A CA    1 
ATOM   3634  C  C     . THR A 1 457 ? 194.971 171.470 208.890 1.00 64.98  ?  476 THR A C     1 
ATOM   3635  O  O     . THR A 1 457 ? 194.282 171.361 207.871 1.00 65.79  ?  476 THR A O     1 
ATOM   3636  C  CB    . THR A 1 457 ? 196.244 169.476 209.729 1.00 62.28  ?  476 THR A CB    1 
ATOM   3637  O  OG1   . THR A 1 457 ? 197.516 168.817 209.705 1.00 67.85  ?  476 THR A OG1   1 
ATOM   3638  C  CG2   . THR A 1 457 ? 195.193 168.568 209.104 1.00 58.55  ?  476 THR A CG2   1 
ATOM   3639  N  N     . GLN A 1 458 ? 194.559 172.161 209.956 1.00 68.84  ?  477 GLN A N     1 
ATOM   3640  C  CA    . GLN A 1 458 ? 193.281 172.867 209.930 1.00 63.59  ?  477 GLN A CA    1 
ATOM   3641  C  C     . GLN A 1 458 ? 193.277 173.966 208.875 1.00 63.80  ?  477 GLN A C     1 
ATOM   3642  O  O     . GLN A 1 458 ? 192.292 174.136 208.144 1.00 63.32  ?  477 GLN A O     1 
ATOM   3643  C  CB    . GLN A 1 458 ? 192.976 173.445 211.313 1.00 66.98  ?  477 GLN A CB    1 
ATOM   3644  C  CG    . GLN A 1 458 ? 191.548 173.940 211.482 1.00 70.42  ?  477 GLN A CG    1 
ATOM   3645  C  CD    . GLN A 1 458 ? 191.414 175.431 211.239 1.00 71.12  ?  477 GLN A CD    1 
ATOM   3646  O  OE1   . GLN A 1 458 ? 192.405 176.159 211.209 1.00 70.07  ?  477 GLN A OE1   1 
ATOM   3647  N  NE2   . GLN A 1 458 ? 190.180 175.893 211.067 1.00 68.15  ?  477 GLN A NE2   1 
ATOM   3648  N  N     . ILE A 1 459 ? 194.372 174.725 208.781 1.00 60.92  ?  478 ILE A N     1 
ATOM   3649  C  CA    . ILE A 1 459 ? 194.465 175.771 207.765 1.00 57.10  ?  478 ILE A CA    1 
ATOM   3650  C  C     . ILE A 1 459 ? 194.424 175.162 206.369 1.00 54.86  ?  478 ILE A C     1 
ATOM   3651  O  O     . ILE A 1 459 ? 193.756 175.684 205.468 1.00 57.67  ?  478 ILE A O     1 
ATOM   3652  C  CB    . ILE A 1 459 ? 195.731 176.621 207.978 1.00 52.34  ?  478 ILE A CB    1 
ATOM   3653  C  CG1   . ILE A 1 459 ? 195.672 177.339 209.326 1.00 54.78  ?  478 ILE A CG1   1 
ATOM   3654  C  CG2   . ILE A 1 459 ? 195.884 177.635 206.860 1.00 53.22  ?  478 ILE A CG2   1 
ATOM   3655  C  CD1   . ILE A 1 459 ? 196.913 178.144 209.642 1.00 56.13  ?  478 ILE A CD1   1 
ATOM   3656  N  N     . ALA A 1 460 ? 195.137 174.053 206.166 1.00 49.53  ?  479 ALA A N     1 
ATOM   3657  C  CA    . ALA A 1 460 ? 195.128 173.395 204.864 1.00 52.00  ?  479 ALA A CA    1 
ATOM   3658  C  C     . ALA A 1 460 ? 193.733 172.898 204.507 1.00 55.62  ?  479 ALA A C     1 
ATOM   3659  O  O     . ALA A 1 460 ? 193.302 173.012 203.355 1.00 53.46  ?  479 ALA A O     1 
ATOM   3660  C  CB    . ALA A 1 460 ? 196.131 172.242 204.850 1.00 55.29  ?  479 ALA A CB    1 
ATOM   3661  N  N     . ASP A 1 461 ? 193.013 172.341 205.484 1.00 63.19  ?  480 ASP A N     1 
ATOM   3662  C  CA    . ASP A 1 461 ? 191.658 171.863 205.228 1.00 60.00  ?  480 ASP A CA    1 
ATOM   3663  C  C     . ASP A 1 461 ? 190.718 173.012 204.886 1.00 57.04  ?  480 ASP A C     1 
ATOM   3664  O  O     . ASP A 1 461 ? 189.882 172.888 203.982 1.00 57.99  ?  480 ASP A O     1 
ATOM   3665  C  CB    . ASP A 1 461 ? 191.138 171.084 206.435 1.00 56.91  ?  480 ASP A CB    1 
ATOM   3666  C  CG    . ASP A 1 461 ? 191.780 169.717 206.566 1.00 62.57  ?  480 ASP A CG    1 
ATOM   3667  O  OD1   . ASP A 1 461 ? 191.888 169.009 205.542 1.00 62.98  ?  480 ASP A OD1   1 
ATOM   3668  O  OD2   . ASP A 1 461 ? 192.174 169.349 207.692 1.00 66.19  -1 480 ASP A OD2   1 
ATOM   3669  N  N     . GLU A 1 462 ? 190.830 174.138 205.596 1.00 51.62  ?  481 GLU A N     1 
ATOM   3670  C  CA    . GLU A 1 462 ? 189.974 175.276 205.272 1.00 47.51  ?  481 GLU A CA    1 
ATOM   3671  C  C     . GLU A 1 462 ? 190.311 175.839 203.893 1.00 50.85  ?  481 GLU A C     1 
ATOM   3672  O  O     . GLU A 1 462 ? 189.411 176.219 203.134 1.00 55.65  ?  481 GLU A O     1 
ATOM   3673  C  CB    . GLU A 1 462 ? 190.072 176.347 206.364 1.00 45.64  ?  481 GLU A CB    1 
ATOM   3674  C  CG    . GLU A 1 462 ? 191.212 177.341 206.228 1.00 53.39  ?  481 GLU A CG    1 
ATOM   3675  C  CD    . GLU A 1 462 ? 191.086 178.506 207.189 1.00 60.95  ?  481 GLU A CD    1 
ATOM   3676  O  OE1   . GLU A 1 462 ? 190.076 178.566 207.921 1.00 57.20  ?  481 GLU A OE1   1 
ATOM   3677  O  OE2   . GLU A 1 462 ? 191.996 179.362 207.211 1.00 60.68  -1 481 GLU A OE2   1 
ATOM   3678  N  N     . LEU A 1 463 ? 191.598 175.865 203.535 1.00 48.90  ?  482 LEU A N     1 
ATOM   3679  C  CA    . LEU A 1 463 ? 191.981 176.324 202.204 1.00 47.43  ?  482 LEU A CA    1 
ATOM   3680  C  C     . LEU A 1 463 ? 191.462 175.380 201.126 1.00 49.51  ?  482 LEU A C     1 
ATOM   3681  O  O     . LEU A 1 463 ? 191.036 175.825 200.055 1.00 51.42  ?  482 LEU A O     1 
ATOM   3682  C  CB    . LEU A 1 463 ? 193.501 176.462 202.112 1.00 48.18  ?  482 LEU A CB    1 
ATOM   3683  C  CG    . LEU A 1 463 ? 194.139 177.570 202.952 1.00 47.07  ?  482 LEU A CG    1 
ATOM   3684  C  CD1   . LEU A 1 463 ? 195.631 177.661 202.674 1.00 48.83  ?  482 LEU A CD1   1 
ATOM   3685  C  CD2   . LEU A 1 463 ? 193.455 178.907 202.712 1.00 47.60  ?  482 LEU A CD2   1 
ATOM   3686  N  N     . ARG A 1 464 ? 191.489 174.073 201.387 1.00 47.11  ?  483 ARG A N     1 
ATOM   3687  C  CA    . ARG A 1 464 ? 191.044 173.119 200.380 1.00 50.00  ?  483 ARG A CA    1 
ATOM   3688  C  C     . ARG A 1 464 ? 189.525 173.075 200.255 1.00 51.67  ?  483 ARG A C     1 
ATOM   3689  O  O     . ARG A 1 464 ? 189.012 172.760 199.176 1.00 51.34  ?  483 ARG A O     1 
ATOM   3690  C  CB    . ARG A 1 464 ? 191.600 171.724 200.688 1.00 54.27  ?  483 ARG A CB    1 
ATOM   3691  C  CG    . ARG A 1 464 ? 190.804 170.923 201.704 1.00 53.32  ?  483 ARG A CG    1 
ATOM   3692  C  CD    . ARG A 1 464 ? 191.422 169.556 201.948 1.00 49.99  ?  483 ARG A CD    1 
ATOM   3693  N  NE    . ARG A 1 464 ? 191.396 168.715 200.757 1.00 50.41  ?  483 ARG A NE    1 
ATOM   3694  C  CZ    . ARG A 1 464 ? 191.965 167.521 200.673 1.00 53.49  ?  483 ARG A CZ    1 
ATOM   3695  N  NH1   . ARG A 1 464 ? 192.615 166.992 201.697 1.00 53.85  1  483 ARG A NH1   1 
ATOM   3696  N  NH2   . ARG A 1 464 ? 191.881 166.840 199.533 1.00 51.88  ?  483 ARG A NH2   1 
ATOM   3697  N  N     . ASN A 1 465 ? 188.788 173.381 201.326 1.00 47.70  ?  484 ASN A N     1 
ATOM   3698  C  CA    . ASN A 1 465 ? 187.334 173.325 201.238 1.00 47.12  ?  484 ASN A CA    1 
ATOM   3699  C  C     . ASN A 1 465 ? 186.687 174.679 200.963 1.00 46.74  ?  484 ASN A C     1 
ATOM   3700  O  O     . ASN A 1 465 ? 185.475 174.723 200.723 1.00 47.81  ?  484 ASN A O     1 
ATOM   3701  C  CB    . ASN A 1 465 ? 186.736 172.687 202.508 1.00 45.81  ?  484 ASN A CB    1 
ATOM   3702  C  CG    . ASN A 1 465 ? 186.753 173.609 203.719 1.00 48.87  ?  484 ASN A CG    1 
ATOM   3703  O  OD1   . ASN A 1 465 ? 187.300 174.706 203.687 1.00 53.37  ?  484 ASN A OD1   1 
ATOM   3704  N  ND2   . ASN A 1 465 ? 186.141 173.150 204.805 1.00 47.21  ?  484 ASN A ND2   1 
ATOM   3705  N  N     . VAL A 1 466 ? 187.447 175.779 200.987 1.00 50.35  ?  485 VAL A N     1 
ATOM   3706  C  CA    . VAL A 1 466 ? 186.876 177.045 200.539 1.00 48.54  ?  485 VAL A CA    1 
ATOM   3707  C  C     . VAL A 1 466 ? 186.558 177.007 199.049 1.00 45.33  ?  485 VAL A C     1 
ATOM   3708  O  O     . VAL A 1 466 ? 185.650 177.711 198.592 1.00 51.93  ?  485 VAL A O     1 
ATOM   3709  C  CB    . VAL A 1 466 ? 187.810 178.226 200.870 1.00 44.68  ?  485 VAL A CB    1 
ATOM   3710  C  CG1   . VAL A 1 466 ? 189.066 178.183 200.023 1.00 43.77  ?  485 VAL A CG1   1 
ATOM   3711  C  CG2   . VAL A 1 466 ? 187.083 179.545 200.675 1.00 50.99  ?  485 VAL A CG2   1 
ATOM   3712  N  N     . VAL A 1 467 ? 187.274 176.187 198.276 1.00 44.23  ?  486 VAL A N     1 
ATOM   3713  C  CA    . VAL A 1 467 ? 187.017 176.038 196.849 1.00 48.66  ?  486 VAL A CA    1 
ATOM   3714  C  C     . VAL A 1 467 ? 186.096 174.859 196.559 1.00 52.26  ?  486 VAL A C     1 
ATOM   3715  O  O     . VAL A 1 467 ? 185.750 174.615 195.395 1.00 53.28  ?  486 VAL A O     1 
ATOM   3716  C  CB    . VAL A 1 467 ? 188.349 175.901 196.078 1.00 49.27  ?  486 VAL A CB    1 
ATOM   3717  C  CG1   . VAL A 1 467 ? 189.005 174.555 196.367 1.00 48.89  ?  486 VAL A CG1   1 
ATOM   3718  C  CG2   . VAL A 1 467 ? 188.173 176.155 194.580 1.00 47.46  ?  486 VAL A CG2   1 
ATOM   3719  N  N     . SER A 1 468 ? 185.670 174.130 197.596 1.00 56.56  ?  487 SER A N     1 
ATOM   3720  C  CA    . SER A 1 468 ? 184.781 172.990 197.394 1.00 56.81  ?  487 SER A CA    1 
ATOM   3721  C  C     . SER A 1 468 ? 183.451 173.426 196.792 1.00 54.07  ?  487 SER A C     1 
ATOM   3722  O  O     . SER A 1 468 ? 182.910 172.751 195.909 1.00 52.71  ?  487 SER A O     1 
ATOM   3723  C  CB    . SER A 1 468 ? 184.557 172.260 198.718 1.00 51.51  ?  487 SER A CB    1 
ATOM   3724  O  OG    . SER A 1 468 ? 184.107 173.154 199.722 1.00 52.21  ?  487 SER A OG    1 
ATOM   3725  N  N     . LYS A 1 469 ? 182.905 174.542 197.263 1.00 47.63  ?  488 LYS A N     1 
ATOM   3726  C  CA    . LYS A 1 469 ? 181.696 175.082 196.662 1.00 47.29  ?  488 LYS A CA    1 
ATOM   3727  C  C     . LYS A 1 469 ? 181.996 175.523 195.232 1.00 51.31  ?  488 LYS A C     1 
ATOM   3728  O  O     . LYS A 1 469 ? 183.003 176.207 194.998 1.00 53.49  ?  488 LYS A O     1 
ATOM   3729  C  CB    . LYS A 1 469 ? 181.164 176.254 197.486 1.00 45.53  ?  488 LYS A CB    1 
ATOM   3730  C  CG    . LYS A 1 469 ? 180.103 177.084 196.781 1.00 48.11  ?  488 LYS A CG    1 
ATOM   3731  C  CD    . LYS A 1 469 ? 179.316 177.929 197.771 1.00 51.85  ?  488 LYS A CD    1 
ATOM   3732  C  CE    . LYS A 1 469 ? 180.193 178.975 198.437 1.00 52.20  ?  488 LYS A CE    1 
ATOM   3733  N  NZ    . LYS A 1 469 ? 180.818 179.891 197.446 1.00 54.73  1  488 LYS A NZ    1 
ATOM   3734  N  N     . PRO A 1 470 ? 181.171 175.146 194.255 1.00 58.11  ?  489 PRO A N     1 
ATOM   3735  C  CA    . PRO A 1 470 ? 181.494 175.447 192.854 1.00 56.72  ?  489 PRO A CA    1 
ATOM   3736  C  C     . PRO A 1 470 ? 181.588 176.943 192.595 1.00 58.46  ?  489 PRO A C     1 
ATOM   3737  O  O     . PRO A 1 470 ? 180.851 177.745 193.173 1.00 58.95  ?  489 PRO A O     1 
ATOM   3738  C  CB    . PRO A 1 470 ? 180.331 174.816 192.079 1.00 59.31  ?  489 PRO A CB    1 
ATOM   3739  C  CG    . PRO A 1 470 ? 179.767 173.785 193.002 1.00 58.54  ?  489 PRO A CG    1 
ATOM   3740  C  CD    . PRO A 1 470 ? 179.946 174.338 194.382 1.00 60.49  ?  489 PRO A CD    1 
ATOM   3741  N  N     . ILE A 1 471 ? 182.511 177.311 191.711 1.00 57.71  ?  490 ILE A N     1 
ATOM   3742  C  CA    . ILE A 1 471 ? 182.681 178.702 191.303 1.00 56.76  ?  490 ILE A CA    1 
ATOM   3743  C  C     . ILE A 1 471 ? 181.593 179.043 190.294 1.00 57.81  ?  490 ILE A C     1 
ATOM   3744  O  O     . ILE A 1 471 ? 181.463 178.382 189.259 1.00 58.36  ?  490 ILE A O     1 
ATOM   3745  C  CB    . ILE A 1 471 ? 184.078 178.938 190.711 1.00 58.27  ?  490 ILE A CB    1 
ATOM   3746  C  CG1   . ILE A 1 471 ? 185.156 178.761 191.783 1.00 56.54  ?  490 ILE A CG1   1 
ATOM   3747  C  CG2   . ILE A 1 471 ? 184.164 180.320 190.084 1.00 58.61  ?  490 ILE A CG2   1 
ATOM   3748  C  CD1   . ILE A 1 471 ? 185.109 179.805 192.872 1.00 54.88  ?  490 ILE A CD1   1 
ATOM   3749  N  N     . MET A 1 472 ? 180.812 180.079 190.591 1.00 65.57  ?  491 MET A N     1 
ATOM   3750  C  CA    . MET A 1 472 ? 179.721 180.497 189.720 1.00 65.22  ?  491 MET A CA    1 
ATOM   3751  C  C     . MET A 1 472 ? 180.243 181.513 188.713 1.00 65.38  ?  491 MET A C     1 
ATOM   3752  O  O     . MET A 1 472 ? 180.658 182.615 189.090 1.00 69.62  ?  491 MET A O     1 
ATOM   3753  C  CB    . MET A 1 472 ? 178.568 181.083 190.534 1.00 69.68  ?  491 MET A CB    1 
ATOM   3754  C  CG    . MET A 1 472 ? 177.675 180.034 191.174 1.00 69.62  ?  491 MET A CG    1 
ATOM   3755  S  SD    . MET A 1 472 ? 176.797 179.038 189.954 1.00 78.76  ?  491 MET A SD    1 
ATOM   3756  C  CE    . MET A 1 472 ? 175.119 179.614 190.189 1.00 69.44  ?  491 MET A CE    1 
ATOM   3757  N  N     . ILE A 1 473 ? 180.215 181.141 187.435 1.00 59.27  ?  492 ILE A N     1 
ATOM   3758  C  CA    . ILE A 1 473 ? 180.725 181.969 186.347 1.00 61.27  ?  492 ILE A CA    1 
ATOM   3759  C  C     . ILE A 1 473 ? 179.686 181.939 185.236 1.00 67.21  ?  492 ILE A C     1 
ATOM   3760  O  O     . ILE A 1 473 ? 179.450 180.884 184.637 1.00 71.63  ?  492 ILE A O     1 
ATOM   3761  C  CB    . ILE A 1 473 ? 182.083 181.478 185.826 1.00 64.36  ?  492 ILE A CB    1 
ATOM   3762  C  CG1   . ILE A 1 473 ? 183.210 181.939 186.745 1.00 62.08  ?  492 ILE A CG1   1 
ATOM   3763  C  CG2   . ILE A 1 473 ? 182.332 181.950 184.400 1.00 63.54  ?  492 ILE A CG2   1 
ATOM   3764  C  CD1   . ILE A 1 473 ? 184.513 181.278 186.428 1.00 62.15  ?  492 ILE A CD1   1 
ATOM   3765  N  N     . ASP A 1 474 ? 179.062 183.086 184.966 1.00 67.63  ?  493 ASP A N     1 
ATOM   3766  C  CA    . ASP A 1 474 ? 178.044 183.194 183.921 1.00 71.03  ?  493 ASP A CA    1 
ATOM   3767  C  C     . ASP A 1 474 ? 176.966 182.128 184.104 1.00 70.88  ?  493 ASP A C     1 
ATOM   3768  O  O     . ASP A 1 474 ? 176.496 181.515 183.143 1.00 71.44  ?  493 ASP A O     1 
ATOM   3769  C  CB    . ASP A 1 474 ? 178.677 183.104 182.531 1.00 72.86  ?  493 ASP A CB    1 
ATOM   3770  C  CG    . ASP A 1 474 ? 177.921 183.906 181.491 1.00 74.55  ?  493 ASP A CG    1 
ATOM   3771  O  OD1   . ASP A 1 474 ? 176.673 183.876 181.504 1.00 72.49  ?  493 ASP A OD1   1 
ATOM   3772  O  OD2   . ASP A 1 474 ? 178.578 184.568 180.660 1.00 74.31  -1 493 ASP A OD2   1 
ATOM   3773  N  N     . ASP A 1 475 ? 176.580 181.905 185.363 1.00 71.89  ?  494 ASP A N     1 
ATOM   3774  C  CA    . ASP A 1 475 ? 175.636 180.850 185.734 1.00 73.42  ?  494 ASP A CA    1 
ATOM   3775  C  C     . ASP A 1 475 ? 176.114 179.480 185.253 1.00 75.02  ?  494 ASP A C     1 
ATOM   3776  O  O     . ASP A 1 475 ? 175.338 178.679 184.730 1.00 73.66  ?  494 ASP A O     1 
ATOM   3777  C  CB    . ASP A 1 475 ? 174.232 181.155 185.207 1.00 75.97  ?  494 ASP A CB    1 
ATOM   3778  C  CG    . ASP A 1 475 ? 173.604 182.354 185.890 1.00 74.89  ?  494 ASP A CG    1 
ATOM   3779  O  OD1   . ASP A 1 475 ? 173.949 182.622 187.059 1.00 75.56  ?  494 ASP A OD1   1 
ATOM   3780  O  OD2   . ASP A 1 475 ? 172.768 183.031 185.255 1.00 74.91  -1 494 ASP A OD2   1 
ATOM   3781  N  N     . LYS A 1 476 ? 177.407 179.209 185.431 1.00 74.01  ?  495 LYS A N     1 
ATOM   3782  C  CA    . LYS A 1 476 ? 177.998 177.919 185.082 1.00 69.57  ?  495 LYS A CA    1 
ATOM   3783  C  C     . LYS A 1 476 ? 178.944 177.516 186.204 1.00 70.44  ?  495 LYS A C     1 
ATOM   3784  O  O     . LYS A 1 476 ? 179.953 178.213 186.441 1.00 73.77  ?  495 LYS A O     1 
ATOM   3785  C  CB    . LYS A 1 476 ? 178.738 177.982 183.743 1.00 66.94  ?  495 LYS A CB    1 
ATOM   3786  C  CG    . LYS A 1 476 ? 177.832 178.002 182.524 1.00 72.27  ?  495 LYS A CG    1 
ATOM   3787  C  CD    . LYS A 1 476 ? 178.623 178.295 181.258 1.00 73.84  ?  495 LYS A CD    1 
ATOM   3788  C  CE    . LYS A 1 476 ? 178.765 179.791 181.024 1.00 70.65  ?  495 LYS A CE    1 
ATOM   3789  N  NZ    . LYS A 1 476 ? 177.467 180.430 180.668 1.00 70.81  1  495 LYS A NZ    1 
ATOM   3790  N  N     . PRO A 1 477 ? 178.672 176.429 186.921 1.00 66.92  ?  496 PRO A N     1 
ATOM   3791  C  CA    . PRO A 1 477 ? 179.570 176.018 188.005 1.00 66.90  ?  496 PRO A CA    1 
ATOM   3792  C  C     . PRO A 1 477 ? 180.894 175.479 187.483 1.00 69.61  ?  496 PRO A C     1 
ATOM   3793  O  O     . PRO A 1 477 ? 180.986 174.950 186.372 1.00 70.05  ?  496 PRO A O     1 
ATOM   3794  C  CB    . PRO A 1 477 ? 178.773 174.928 188.729 1.00 63.22  ?  496 PRO A CB    1 
ATOM   3795  C  CG    . PRO A 1 477 ? 177.877 174.366 187.676 1.00 62.78  ?  496 PRO A CG    1 
ATOM   3796  C  CD    . PRO A 1 477 ? 177.525 175.516 186.771 1.00 66.01  ?  496 PRO A CD    1 
ATOM   3797  N  N     . PHE A 1 478 ? 181.930 175.623 188.310 1.00 64.00  ?  497 PHE A N     1 
ATOM   3798  C  CA    . PHE A 1 478 ? 183.251 175.084 188.014 1.00 56.65  ?  497 PHE A CA    1 
ATOM   3799  C  C     . PHE A 1 478 ? 183.890 174.534 189.283 1.00 56.42  ?  497 PHE A C     1 
ATOM   3800  O  O     . PHE A 1 478 ? 184.272 175.305 190.174 1.00 56.82  ?  497 PHE A O     1 
ATOM   3801  C  CB    . PHE A 1 478 ? 184.153 176.150 187.389 1.00 54.22  ?  497 PHE A CB    1 
ATOM   3802  C  CG    . PHE A 1 478 ? 183.784 176.506 185.977 1.00 52.84  ?  497 PHE A CG    1 
ATOM   3803  C  CD1   . PHE A 1 478 ? 182.914 177.550 185.714 1.00 56.67  ?  497 PHE A CD1   1 
ATOM   3804  C  CD2   . PHE A 1 478 ? 184.306 175.791 184.913 1.00 54.69  ?  497 PHE A CD2   1 
ATOM   3805  C  CE1   . PHE A 1 478 ? 182.574 177.877 184.413 1.00 59.92  ?  497 PHE A CE1   1 
ATOM   3806  C  CE2   . PHE A 1 478 ? 183.970 176.112 183.612 1.00 55.10  ?  497 PHE A CE2   1 
ATOM   3807  C  CZ    . PHE A 1 478 ? 183.103 177.156 183.362 1.00 59.07  ?  497 PHE A CZ    1 
ATOM   3808  N  N     . PRO A 1 479 ? 184.026 173.212 189.405 1.00 48.64  ?  498 PRO A N     1 
ATOM   3809  C  CA    . PRO A 1 479 ? 184.646 172.615 190.609 1.00 53.31  ?  498 PRO A CA    1 
ATOM   3810  C  C     . PRO A 1 479 ? 186.171 172.690 190.590 1.00 53.42  ?  498 PRO A C     1 
ATOM   3811  O  O     . PRO A 1 479 ? 186.888 171.734 190.295 1.00 56.07  ?  498 PRO A O     1 
ATOM   3812  C  CB    . PRO A 1 479 ? 184.144 171.170 190.561 1.00 52.39  ?  498 PRO A CB    1 
ATOM   3813  C  CG    . PRO A 1 479 ? 183.941 170.897 189.111 1.00 50.12  ?  498 PRO A CG    1 
ATOM   3814  C  CD    . PRO A 1 479 ? 183.494 172.191 188.488 1.00 48.02  ?  498 PRO A CD    1 
ATOM   3815  N  N     . LEU A 1 480 ? 186.688 173.870 190.920 1.00 42.82  ?  499 LEU A N     1 
ATOM   3816  C  CA    . LEU A 1 480 ? 188.128 174.066 190.987 1.00 37.35  ?  499 LEU A CA    1 
ATOM   3817  C  C     . LEU A 1 480 ? 188.700 173.373 192.221 1.00 38.55  ?  499 LEU A C     1 
ATOM   3818  O  O     . LEU A 1 480 ? 188.004 173.125 193.210 1.00 44.15  ?  499 LEU A O     1 
ATOM   3819  C  CB    . LEU A 1 480 ? 188.469 175.557 191.009 1.00 43.42  ?  499 LEU A CB    1 
ATOM   3820  C  CG    . LEU A 1 480 ? 187.759 176.462 190.000 1.00 44.85  ?  499 LEU A CG    1 
ATOM   3821  C  CD1   . LEU A 1 480 ? 188.339 177.866 190.044 1.00 44.03  ?  499 LEU A CD1   1 
ATOM   3822  C  CD2   . LEU A 1 480 ? 187.848 175.890 188.594 1.00 43.57  ?  499 LEU A CD2   1 
ATOM   3823  N  N     . THR A 1 481 ? 189.992 173.058 192.154 1.00 39.90  ?  500 THR A N     1 
ATOM   3824  C  CA    . THR A 1 481 ? 190.659 172.329 193.222 1.00 40.43  ?  500 THR A CA    1 
ATOM   3825  C  C     . THR A 1 481 ? 192.023 172.949 193.496 1.00 39.60  ?  500 THR A C     1 
ATOM   3826  O  O     . THR A 1 481 ? 192.544 173.741 192.704 1.00 45.79  ?  500 THR A O     1 
ATOM   3827  C  CB    . THR A 1 481 ? 190.804 170.839 192.883 1.00 41.83  ?  500 THR A CB    1 
ATOM   3828  O  OG1   . THR A 1 481 ? 191.258 170.693 191.532 1.00 41.92  ?  500 THR A OG1   1 
ATOM   3829  C  CG2   . THR A 1 481 ? 189.472 170.121 193.048 1.00 40.35  ?  500 THR A CG2   1 
ATOM   3830  N  N     . LEU A 1 482 ? 192.598 172.574 194.639 1.00 27.10  ?  501 LEU A N     1 
ATOM   3831  C  CA    . LEU A 1 482 ? 193.820 173.188 195.140 1.00 30.00  ?  501 LEU A CA    1 
ATOM   3832  C  C     . LEU A 1 482 ? 194.879 172.127 195.402 1.00 30.21  ?  501 LEU A C     1 
ATOM   3833  O  O     . LEU A 1 482 ? 194.599 171.098 196.030 1.00 37.00  ?  501 LEU A O     1 
ATOM   3834  C  CB    . LEU A 1 482 ? 193.546 173.979 196.426 1.00 29.07  ?  501 LEU A CB    1 
ATOM   3835  C  CG    . LEU A 1 482 ? 192.643 175.208 196.312 1.00 32.04  ?  501 LEU A CG    1 
ATOM   3836  C  CD1   . LEU A 1 482 ? 192.827 176.120 197.508 1.00 32.12  ?  501 LEU A CD1   1 
ATOM   3837  C  CD2   . LEU A 1 482 ? 192.912 175.963 195.027 1.00 27.96  ?  501 LEU A CD2   1 
ATOM   3838  N  N     . SER A 1 483 ? 196.095 172.387 194.922 1.00 26.96  ?  502 SER A N     1 
ATOM   3839  C  CA    . SER A 1 483 ? 197.275 171.594 195.251 1.00 18.70  ?  502 SER A CA    1 
ATOM   3840  C  C     . SER A 1 483 ? 198.144 172.434 196.180 1.00 26.66  ?  502 SER A C     1 
ATOM   3841  O  O     . SER A 1 483 ? 198.685 173.464 195.768 1.00 46.36  ?  502 SER A O     1 
ATOM   3842  C  CB    . SER A 1 483 ? 198.037 171.192 193.990 1.00 33.19  ?  502 SER A CB    1 
ATOM   3843  O  OG    . SER A 1 483 ? 199.376 170.837 194.293 1.00 43.09  ?  502 SER A OG    1 
ATOM   3844  N  N     . ILE A 1 484 ? 198.272 172.002 197.430 1.00 12.92  ?  503 ILE A N     1 
ATOM   3845  C  CA    . ILE A 1 484 ? 198.944 172.775 198.468 1.00 13.55  ?  503 ILE A CA    1 
ATOM   3846  C  C     . ILE A 1 484 ? 200.271 172.106 198.794 1.00 16.25  ?  503 ILE A C     1 
ATOM   3847  O  O     . ILE A 1 484 ? 200.315 170.908 199.102 1.00 30.32  ?  503 ILE A O     1 
ATOM   3848  C  CB    . ILE A 1 484 ? 198.074 172.907 199.730 1.00 19.56  ?  503 ILE A CB    1 
ATOM   3849  C  CG1   . ILE A 1 484 ? 196.710 173.516 199.392 1.00 23.71  ?  503 ILE A CG1   1 
ATOM   3850  C  CG2   . ILE A 1 484 ? 198.783 173.750 200.779 1.00 24.30  ?  503 ILE A CG2   1 
ATOM   3851  C  CD1   . ILE A 1 484 ? 195.609 172.492 199.177 1.00 31.99  ?  503 ILE A CD1   1 
ATOM   3852  N  N     . GLY A 1 485 ? 201.349 172.882 198.727 1.00 21.32  ?  504 GLY A N     1 
ATOM   3853  C  CA    . GLY A 1 485 ? 202.666 172.434 199.147 1.00 22.00  ?  504 GLY A CA    1 
ATOM   3854  C  C     . GLY A 1 485 ? 203.127 173.239 200.351 1.00 20.44  ?  504 GLY A C     1 
ATOM   3855  O  O     . GLY A 1 485 ? 203.221 174.466 200.287 1.00 41.43  ?  504 GLY A O     1 
ATOM   3856  N  N     . ILE A 1 486 ? 203.417 172.535 201.440 1.00 9.86   ?  505 ILE A N     1 
ATOM   3857  C  CA    . ILE A 1 486 ? 203.727 173.165 202.717 1.00 18.08  ?  505 ILE A CA    1 
ATOM   3858  C  C     . ILE A 1 486 ? 205.215 172.993 202.986 1.00 28.80  ?  505 ILE A C     1 
ATOM   3859  O  O     . ILE A 1 486 ? 205.715 171.862 203.062 1.00 42.16  ?  505 ILE A O     1 
ATOM   3860  C  CB    . ILE A 1 486 ? 202.892 172.569 203.859 1.00 26.88  ?  505 ILE A CB    1 
ATOM   3861  C  CG1   . ILE A 1 486 ? 201.402 172.808 203.611 1.00 30.81  ?  505 ILE A CG1   1 
ATOM   3862  C  CG2   . ILE A 1 486 ? 203.303 173.182 205.184 1.00 29.78  ?  505 ILE A CG2   1 
ATOM   3863  C  CD1   . ILE A 1 486 ? 200.663 171.585 203.106 1.00 39.40  ?  505 ILE A CD1   1 
ATOM   3864  N  N     . SER A 1 487 ? 205.918 174.110 203.155 1.00 30.73  ?  506 SER A N     1 
ATOM   3865  C  CA    . SER A 1 487 ? 207.333 174.088 203.496 1.00 29.15  ?  506 SER A CA    1 
ATOM   3866  C  C     . SER A 1 487 ? 207.553 174.851 204.793 1.00 33.05  ?  506 SER A C     1 
ATOM   3867  O  O     . SER A 1 487 ? 206.987 175.935 204.992 1.00 42.93  ?  506 SER A O     1 
ATOM   3868  C  CB    . SER A 1 487 ? 208.187 174.678 202.373 1.00 35.23  ?  506 SER A CB    1 
ATOM   3869  O  OG    . SER A 1 487 ? 209.544 174.778 202.766 1.00 44.50  ?  506 SER A OG    1 
ATOM   3870  N  N     . TYR A 1 488 ? 208.374 174.276 205.670 1.00 53.87  ?  507 TYR A N     1 
ATOM   3871  C  CA    . TYR A 1 488 ? 208.693 174.874 206.962 1.00 57.93  ?  507 TYR A CA    1 
ATOM   3872  C  C     . TYR A 1 488 ? 209.967 174.245 207.501 1.00 64.35  ?  507 TYR A C     1 
ATOM   3873  O  O     . TYR A 1 488 ? 210.055 173.019 207.622 1.00 62.57  ?  507 TYR A O     1 
ATOM   3874  C  CB    . TYR A 1 488 ? 207.549 174.692 207.959 1.00 54.48  ?  507 TYR A CB    1 
ATOM   3875  C  CG    . TYR A 1 488 ? 207.907 175.137 209.358 1.00 58.40  ?  507 TYR A CG    1 
ATOM   3876  C  CD1   . TYR A 1 488 ? 207.992 176.482 209.679 1.00 59.34  ?  507 TYR A CD1   1 
ATOM   3877  C  CD2   . TYR A 1 488 ? 208.159 174.208 210.360 1.00 60.06  ?  507 TYR A CD2   1 
ATOM   3878  C  CE1   . TYR A 1 488 ? 208.316 176.894 210.955 1.00 61.56  ?  507 TYR A CE1   1 
ATOM   3879  C  CE2   . TYR A 1 488 ? 208.486 174.610 211.639 1.00 64.33  ?  507 TYR A CE2   1 
ATOM   3880  C  CZ    . TYR A 1 488 ? 208.564 175.955 211.931 1.00 65.64  ?  507 TYR A CZ    1 
ATOM   3881  O  OH    . TYR A 1 488 ? 208.889 176.364 213.203 1.00 65.06  ?  507 TYR A OH    1 
ATOM   3882  N  N     . ASP A 1 489 ? 210.944 175.086 207.824 1.00 71.36  ?  508 ASP A N     1 
ATOM   3883  C  CA    . ASP A 1 489 ? 212.173 174.670 208.480 1.00 69.62  ?  508 ASP A CA    1 
ATOM   3884  C  C     . ASP A 1 489 ? 212.430 175.605 209.651 1.00 72.52  ?  508 ASP A C     1 
ATOM   3885  O  O     . ASP A 1 489 ? 211.796 176.655 209.776 1.00 75.64  ?  508 ASP A O     1 
ATOM   3886  C  CB    . ASP A 1 489 ? 213.367 174.685 207.514 1.00 68.98  ?  508 ASP A CB    1 
ATOM   3887  C  CG    . ASP A 1 489 ? 213.252 173.635 206.428 1.00 73.17  ?  508 ASP A CG    1 
ATOM   3888  O  OD1   . ASP A 1 489 ? 212.741 172.531 206.715 1.00 71.87  ?  508 ASP A OD1   1 
ATOM   3889  O  OD2   . ASP A 1 489 ? 213.671 173.913 205.285 1.00 73.19  -1 508 ASP A OD2   1 
ATOM   3890  N  N     . LEU A 1 490 ? 213.357 175.209 210.527 1.00 82.87  ?  509 LEU A N     1 
ATOM   3891  C  CA    . LEU A 1 490 ? 213.745 176.096 211.619 1.00 82.70  ?  509 LEU A CA    1 
ATOM   3892  C  C     . LEU A 1 490 ? 214.283 177.413 211.070 1.00 81.60  ?  509 LEU A C     1 
ATOM   3893  O  O     . LEU A 1 490 ? 213.856 178.496 211.488 1.00 83.07  ?  509 LEU A O     1 
ATOM   3894  C  CB    . LEU A 1 490 ? 214.756 175.394 212.535 1.00 84.70  ?  509 LEU A CB    1 
ATOM   3895  C  CG    . LEU A 1 490 ? 216.125 174.901 212.048 1.00 86.17  ?  509 LEU A CG    1 
ATOM   3896  C  CD1   . LEU A 1 490 ? 217.210 175.965 212.193 1.00 83.05  ?  509 LEU A CD1   1 
ATOM   3897  C  CD2   . LEU A 1 490 ? 216.520 173.622 212.777 1.00 82.10  ?  509 LEU A CD2   1 
ATOM   3898  N  N     . GLY A 1 491 ? 215.229 177.340 210.139 1.00 80.90  ?  510 GLY A N     1 
ATOM   3899  C  CA    . GLY A 1 491 ? 215.463 178.410 209.192 1.00 81.62  ?  510 GLY A CA    1 
ATOM   3900  C  C     . GLY A 1 491 ? 216.503 178.007 208.169 1.00 83.09  ?  510 GLY A C     1 
ATOM   3901  O  O     . GLY A 1 491 ? 217.610 177.611 208.545 1.00 82.79  ?  510 GLY A O     1 
ATOM   3902  N  N     . LYS A 1 492 ? 216.180 178.098 206.879 1.00 73.18  ?  511 LYS A N     1 
ATOM   3903  C  CA    . LYS A 1 492 ? 217.186 177.884 205.845 1.00 74.06  ?  511 LYS A CA    1 
ATOM   3904  C  C     . LYS A 1 492 ? 217.358 179.103 204.949 1.00 74.83  ?  511 LYS A C     1 
ATOM   3905  O  O     . LYS A 1 492 ? 218.439 179.701 204.934 1.00 75.33  ?  511 LYS A O     1 
ATOM   3906  C  CB    . LYS A 1 492 ? 216.815 176.650 205.013 1.00 71.34  ?  511 LYS A CB    1 
ATOM   3907  C  CG    . LYS A 1 492 ? 217.464 175.366 205.497 1.00 73.74  ?  511 LYS A CG    1 
ATOM   3908  C  CD    . LYS A 1 492 ? 218.976 175.430 205.382 1.00 78.19  ?  511 LYS A CD    1 
ATOM   3909  C  CE    . LYS A 1 492 ? 219.606 174.085 205.703 1.00 79.08  ?  511 LYS A CE    1 
ATOM   3910  N  NZ    . LYS A 1 492 ? 219.039 172.987 204.873 1.00 74.30  1  511 LYS A NZ    1 
ATOM   3911  N  N     . ASN A 1 493 ? 216.312 179.500 204.226 1.00 63.86  ?  512 ASN A N     1 
ATOM   3912  C  CA    . ASN A 1 493 ? 216.289 180.663 203.347 1.00 61.62  ?  512 ASN A CA    1 
ATOM   3913  C  C     . ASN A 1 493 ? 214.918 180.728 202.689 1.00 57.95  ?  512 ASN A C     1 
ATOM   3914  O  O     . ASN A 1 493 ? 214.196 179.727 202.617 1.00 63.82  ?  512 ASN A O     1 
ATOM   3915  C  CB    . ASN A 1 493 ? 217.382 180.612 202.272 1.00 63.73  ?  512 ASN A CB    1 
ATOM   3916  C  CG    . ASN A 1 493 ? 217.956 181.982 201.960 1.00 66.79  ?  512 ASN A CG    1 
ATOM   3917  O  OD1   . ASN A 1 493 ? 217.434 183.003 202.407 1.00 68.16  ?  512 ASN A OD1   1 
ATOM   3918  N  ND2   . ASN A 1 493 ? 219.038 182.009 201.190 1.00 62.16  ?  512 ASN A ND2   1 
ATOM   3919  N  N     . ARG A 1 494 ? 214.582 181.915 202.179 1.00 44.35  ?  513 ARG A N     1 
ATOM   3920  C  CA    . ARG A 1 494 ? 213.358 182.059 201.399 1.00 48.34  ?  513 ARG A CA    1 
ATOM   3921  C  C     . ARG A 1 494 ? 213.420 181.226 200.124 1.00 53.84  ?  513 ARG A C     1 
ATOM   3922  O  O     . ARG A 1 494 ? 212.423 180.611 199.726 1.00 61.29  ?  513 ARG A O     1 
ATOM   3923  C  CB    . ARG A 1 494 ? 213.105 183.535 201.081 1.00 50.73  ?  513 ARG A CB    1 
ATOM   3924  C  CG    . ARG A 1 494 ? 214.163 184.206 200.212 1.00 51.69  ?  513 ARG A CG    1 
ATOM   3925  C  CD    . ARG A 1 494 ? 213.531 185.130 199.182 1.00 53.07  ?  513 ARG A CD    1 
ATOM   3926  N  NE    . ARG A 1 494 ? 214.517 185.981 198.527 1.00 54.06  ?  513 ARG A NE    1 
ATOM   3927  C  CZ    . ARG A 1 494 ? 214.958 185.807 197.288 1.00 52.70  ?  513 ARG A CZ    1 
ATOM   3928  N  NH1   . ARG A 1 494 ? 214.513 184.819 196.529 1.00 49.23  1  513 ARG A NH1   1 
ATOM   3929  N  NH2   . ARG A 1 494 ? 215.864 186.648 196.797 1.00 53.44  ?  513 ARG A NH2   1 
ATOM   3930  N  N     . ASP A 1 495 ? 214.588 181.185 199.476 1.00 53.14  ?  514 ASP A N     1 
ATOM   3931  C  CA    . ASP A 1 495 ? 214.744 180.374 198.273 1.00 53.11  ?  514 ASP A CA    1 
ATOM   3932  C  C     . ASP A 1 495 ? 214.548 178.895 198.578 1.00 54.15  ?  514 ASP A C     1 
ATOM   3933  O  O     . ASP A 1 495 ? 213.879 178.181 197.823 1.00 60.38  ?  514 ASP A O     1 
ATOM   3934  C  CB    . ASP A 1 495 ? 216.121 180.615 197.654 1.00 58.05  ?  514 ASP A CB    1 
ATOM   3935  C  CG    . ASP A 1 495 ? 216.250 181.993 197.034 1.00 62.94  ?  514 ASP A CG    1 
ATOM   3936  O  OD1   . ASP A 1 495 ? 215.227 182.534 196.565 1.00 62.42  ?  514 ASP A OD1   1 
ATOM   3937  O  OD2   . ASP A 1 495 ? 217.375 182.535 197.017 1.00 57.37  -1 514 ASP A OD2   1 
ATOM   3938  N  N     . TYR A 1 496 ? 215.124 178.420 199.686 1.00 44.91  ?  515 TYR A N     1 
ATOM   3939  C  CA    . TYR A 1 496 ? 214.956 177.024 200.079 1.00 45.78  ?  515 TYR A CA    1 
ATOM   3940  C  C     . TYR A 1 496 ? 213.496 176.707 200.373 1.00 48.36  ?  515 TYR A C     1 
ATOM   3941  O  O     . TYR A 1 496 ? 212.970 175.675 199.932 1.00 49.99  ?  515 TYR A O     1 
ATOM   3942  C  CB    . TYR A 1 496 ? 215.830 176.719 201.296 1.00 49.40  ?  515 TYR A CB    1 
ATOM   3943  C  CG    . TYR A 1 496 ? 216.038 175.245 201.556 1.00 53.12  ?  515 TYR A CG    1 
ATOM   3944  C  CD1   . TYR A 1 496 ? 215.170 174.538 202.377 1.00 50.46  ?  515 TYR A CD1   1 
ATOM   3945  C  CD2   . TYR A 1 496 ? 217.101 174.560 200.984 1.00 54.71  ?  515 TYR A CD2   1 
ATOM   3946  C  CE1   . TYR A 1 496 ? 215.353 173.191 202.621 1.00 51.80  ?  515 TYR A CE1   1 
ATOM   3947  C  CE2   . TYR A 1 496 ? 217.293 173.211 201.222 1.00 54.72  ?  515 TYR A CE2   1 
ATOM   3948  C  CZ    . TYR A 1 496 ? 216.416 172.533 202.041 1.00 53.65  ?  515 TYR A CZ    1 
ATOM   3949  O  OH    . TYR A 1 496 ? 216.601 171.191 202.282 1.00 51.36  ?  515 TYR A OH    1 
ATOM   3950  N  N     . LEU A 1 497 ? 212.823 177.586 201.121 1.00 41.80  ?  516 LEU A N     1 
ATOM   3951  C  CA    . LEU A 1 497 ? 211.417 177.357 201.437 1.00 34.82  ?  516 LEU A CA    1 
ATOM   3952  C  C     . LEU A 1 497 ? 210.576 177.295 200.168 1.00 32.93  ?  516 LEU A C     1 
ATOM   3953  O  O     . LEU A 1 497 ? 209.748 176.390 199.998 1.00 46.76  ?  516 LEU A O     1 
ATOM   3954  C  CB    . LEU A 1 497 ? 210.902 178.454 202.371 1.00 31.79  ?  516 LEU A CB    1 
ATOM   3955  C  CG    . LEU A 1 497 ? 211.442 178.475 203.803 1.00 39.79  ?  516 LEU A CG    1 
ATOM   3956  C  CD1   . LEU A 1 497 ? 210.540 179.310 204.698 1.00 40.72  ?  516 LEU A CD1   1 
ATOM   3957  C  CD2   . LEU A 1 497 ? 211.588 177.063 204.350 1.00 43.18  ?  516 LEU A CD2   1 
ATOM   3958  N  N     . LEU A 1 498 ? 210.796 178.242 199.251 1.00 26.74  ?  517 LEU A N     1 
ATOM   3959  C  CA    . LEU A 1 498 ? 210.021 178.272 198.016 1.00 33.20  ?  517 LEU A CA    1 
ATOM   3960  C  C     . LEU A 1 498 ? 210.291 177.040 197.162 1.00 42.42  ?  517 LEU A C     1 
ATOM   3961  O  O     . LEU A 1 498 ? 209.360 176.457 196.598 1.00 48.29  ?  517 LEU A O     1 
ATOM   3962  C  CB    . LEU A 1 498 ? 210.329 179.548 197.232 1.00 36.78  ?  517 LEU A CB    1 
ATOM   3963  C  CG    . LEU A 1 498 ? 209.303 180.679 197.335 1.00 41.06  ?  517 LEU A CG    1 
ATOM   3964  C  CD1   . LEU A 1 498 ? 209.084 181.090 198.782 1.00 41.90  ?  517 LEU A CD1   1 
ATOM   3965  C  CD2   . LEU A 1 498 ? 209.740 181.868 196.496 1.00 37.04  ?  517 LEU A CD2   1 
ATOM   3966  N  N     . SER A 1 499 ? 211.556 176.623 197.059 1.00 35.89  ?  518 SER A N     1 
ATOM   3967  C  CA    . SER A 1 499 ? 211.885 175.457 196.246 1.00 31.39  ?  518 SER A CA    1 
ATOM   3968  C  C     . SER A 1 499 ? 211.262 174.187 196.814 1.00 37.76  ?  518 SER A C     1 
ATOM   3969  O  O     . SER A 1 499 ? 210.704 173.374 196.067 1.00 47.08  ?  518 SER A O     1 
ATOM   3970  C  CB    . SER A 1 499 ? 213.402 175.309 196.132 1.00 32.12  ?  518 SER A CB    1 
ATOM   3971  O  OG    . SER A 1 499 ? 214.000 175.189 197.411 1.00 36.37  ?  518 SER A OG    1 
ATOM   3972  N  N     . THR A 1 500 ? 211.346 173.997 198.134 1.00 29.13  ?  519 THR A N     1 
ATOM   3973  C  CA    . THR A 1 500 ? 210.763 172.803 198.740 1.00 24.13  ?  519 THR A CA    1 
ATOM   3974  C  C     . THR A 1 500 ? 209.244 172.795 198.596 1.00 28.13  ?  519 THR A C     1 
ATOM   3975  O  O     . THR A 1 500 ? 208.642 171.758 198.268 1.00 39.72  ?  519 THR A O     1 
ATOM   3976  C  CB    . THR A 1 500 ? 211.164 172.717 200.212 1.00 33.83  ?  519 THR A CB    1 
ATOM   3977  O  OG1   . THR A 1 500 ? 210.973 173.993 200.834 1.00 38.45  ?  519 THR A OG1   1 
ATOM   3978  C  CG2   . THR A 1 500 ? 212.629 172.328 200.334 1.00 36.81  ?  519 THR A CG2   1 
ATOM   3979  N  N     . ALA A 1 501 ? 208.605 173.945 198.828 1.00 23.15  ?  520 ALA A N     1 
ATOM   3980  C  CA    . ALA A 1 501 ? 207.156 174.015 198.686 1.00 23.23  ?  520 ALA A CA    1 
ATOM   3981  C  C     . ALA A 1 501 ? 206.736 173.790 197.239 1.00 24.25  ?  520 ALA A C     1 
ATOM   3982  O  O     . ALA A 1 501 ? 205.698 173.173 196.978 1.00 35.24  ?  520 ALA A O     1 
ATOM   3983  C  CB    . ALA A 1 501 ? 206.642 175.357 199.204 1.00 23.21  ?  520 ALA A CB    1 
ATOM   3984  N  N     . HIS A 1 502 ? 207.538 174.266 196.284 1.00 22.98  ?  521 HIS A N     1 
ATOM   3985  C  CA    . HIS A 1 502 ? 207.229 174.036 194.878 1.00 27.55  ?  521 HIS A CA    1 
ATOM   3986  C  C     . HIS A 1 502 ? 207.389 172.569 194.515 1.00 36.10  ?  521 HIS A C     1 
ATOM   3987  O  O     . HIS A 1 502 ? 206.604 172.035 193.726 1.00 36.70  ?  521 HIS A O     1 
ATOM   3988  C  CB    . HIS A 1 502 ? 208.115 174.907 193.988 1.00 30.49  ?  521 HIS A CB    1 
ATOM   3989  C  CG    . HIS A 1 502 ? 207.616 175.029 192.582 1.00 38.69  ?  521 HIS A CG    1 
ATOM   3990  N  ND1   . HIS A 1 502 ? 208.061 174.217 191.561 1.00 40.83  ?  521 HIS A ND1   1 
ATOM   3991  C  CD2   . HIS A 1 502 ? 206.699 175.858 192.031 1.00 32.67  ?  521 HIS A CD2   1 
ATOM   3992  C  CE1   . HIS A 1 502 ? 207.445 174.546 190.441 1.00 37.60  ?  521 HIS A CE1   1 
ATOM   3993  N  NE2   . HIS A 1 502 ? 206.613 175.539 190.699 1.00 34.14  ?  521 HIS A NE2   1 
ATOM   3994  N  N     . ASN A 1 503 ? 208.404 171.906 195.071 1.00 41.75  ?  522 ASN A N     1 
ATOM   3995  C  CA    . ASN A 1 503 ? 208.550 170.469 194.864 1.00 32.45  ?  522 ASN A CA    1 
ATOM   3996  C  C     . ASN A 1 503 ? 207.313 169.725 195.353 1.00 29.94  ?  522 ASN A C     1 
ATOM   3997  O  O     . ASN A 1 503 ? 206.745 168.893 194.632 1.00 36.90  ?  522 ASN A O     1 
ATOM   3998  C  CB    . ASN A 1 503 ? 209.807 169.963 195.573 1.00 31.31  ?  522 ASN A CB    1 
ATOM   3999  C  CG    . ASN A 1 503 ? 210.233 168.588 195.096 1.00 39.82  ?  522 ASN A CG    1 
ATOM   4000  O  OD1   . ASN A 1 503 ? 209.597 167.995 194.225 1.00 45.36  ?  522 ASN A OD1   1 
ATOM   4001  N  ND2   . ASN A 1 503 ? 211.316 168.073 195.667 1.00 39.45  ?  522 ASN A ND2   1 
ATOM   4002  N  N     . ALA A 1 504 ? 206.865 170.038 196.572 1.00 26.13  ?  523 ALA A N     1 
ATOM   4003  C  CA    . ALA A 1 504 ? 205.670 169.387 197.106 1.00 29.08  ?  523 ALA A CA    1 
ATOM   4004  C  C     . ALA A 1 504 ? 204.442 169.680 196.247 1.00 25.16  ?  523 ALA A C     1 
ATOM   4005  O  O     . ALA A 1 504 ? 203.653 168.774 195.939 1.00 35.43  ?  523 ALA A O     1 
ATOM   4006  C  CB    . ALA A 1 504 ? 205.434 169.829 198.550 1.00 24.31  ?  523 ALA A CB    1 
ATOM   4007  N  N     . MET A 1 505 ? 204.266 170.942 195.847 1.00 23.58  ?  524 MET A N     1 
ATOM   4008  C  CA    . MET A 1 505 ? 203.090 171.324 195.074 1.00 20.96  ?  524 MET A CA    1 
ATOM   4009  C  C     . MET A 1 505 ? 203.076 170.652 193.708 1.00 35.20  ?  524 MET A C     1 
ATOM   4010  O  O     . MET A 1 505 ? 202.025 170.184 193.257 1.00 42.00  ?  524 MET A O     1 
ATOM   4011  C  CB    . MET A 1 505 ? 203.033 172.844 194.925 1.00 26.50  ?  524 MET A CB    1 
ATOM   4012  C  CG    . MET A 1 505 ? 201.717 173.361 194.374 1.00 21.79  ?  524 MET A CG    1 
ATOM   4013  S  SD    . MET A 1 505 ? 201.833 173.849 192.644 1.00 40.40  ?  524 MET A SD    1 
ATOM   4014  C  CE    . MET A 1 505 ? 203.181 175.028 192.718 1.00 36.50  ?  524 MET A CE    1 
ATOM   4015  N  N     . ASP A 1 506 ? 204.226 170.592 193.027 1.00 41.68  ?  525 ASP A N     1 
ATOM   4016  C  CA    . ASP A 1 506 ? 204.250 169.941 191.724 1.00 37.06  ?  525 ASP A CA    1 
ATOM   4017  C  C     . ASP A 1 506 ? 204.059 168.438 191.855 1.00 33.93  ?  525 ASP A C     1 
ATOM   4018  O  O     . ASP A 1 506 ? 203.430 167.823 190.989 1.00 31.22  ?  525 ASP A O     1 
ATOM   4019  C  CB    . ASP A 1 506 ? 205.542 170.272 190.962 1.00 35.10  ?  525 ASP A CB    1 
ATOM   4020  C  CG    . ASP A 1 506 ? 206.796 169.696 191.609 1.00 40.80  ?  525 ASP A CG    1 
ATOM   4021  O  OD1   . ASP A 1 506 ? 206.857 168.477 191.879 1.00 42.17  ?  525 ASP A OD1   1 
ATOM   4022  O  OD2   . ASP A 1 506 ? 207.752 170.471 191.812 1.00 38.65  -1 525 ASP A OD2   1 
ATOM   4023  N  N     . TYR A 1 507 ? 204.578 167.830 192.928 1.00 37.02  ?  526 TYR A N     1 
ATOM   4024  C  CA    . TYR A 1 507 ? 204.302 166.418 193.171 1.00 35.34  ?  526 TYR A CA    1 
ATOM   4025  C  C     . TYR A 1 507 ? 202.805 166.175 193.301 1.00 33.24  ?  526 TYR A C     1 
ATOM   4026  O  O     . TYR A 1 507 ? 202.253 165.267 192.665 1.00 33.85  ?  526 TYR A O     1 
ATOM   4027  C  CB    . TYR A 1 507 ? 205.040 165.946 194.426 1.00 38.51  ?  526 TYR A CB    1 
ATOM   4028  C  CG    . TYR A 1 507 ? 205.056 164.442 194.609 1.00 40.96  ?  526 TYR A CG    1 
ATOM   4029  C  CD1   . TYR A 1 507 ? 203.962 163.774 195.145 1.00 35.67  ?  526 TYR A CD1   1 
ATOM   4030  C  CD2   . TYR A 1 507 ? 206.165 163.690 194.242 1.00 38.72  ?  526 TYR A CD2   1 
ATOM   4031  C  CE1   . TYR A 1 507 ? 203.971 162.403 195.313 1.00 34.94  ?  526 TYR A CE1   1 
ATOM   4032  C  CE2   . TYR A 1 507 ? 206.183 162.316 194.407 1.00 40.18  ?  526 TYR A CE2   1 
ATOM   4033  C  CZ    . TYR A 1 507 ? 205.084 161.678 194.943 1.00 43.42  ?  526 TYR A CZ    1 
ATOM   4034  O  OH    . TYR A 1 507 ? 205.096 160.312 195.109 1.00 43.77  ?  526 TYR A OH    1 
ATOM   4035  N  N     . ILE A 1 508 ? 202.127 166.989 194.116 1.00 36.74  ?  527 ILE A N     1 
ATOM   4036  C  CA    . ILE A 1 508 ? 200.687 166.820 194.300 1.00 31.34  ?  527 ILE A CA    1 
ATOM   4037  C  C     . ILE A 1 508 ? 199.946 167.052 192.989 1.00 38.28  ?  527 ILE A C     1 
ATOM   4038  O  O     . ILE A 1 508 ? 199.019 166.309 192.643 1.00 43.87  ?  527 ILE A O     1 
ATOM   4039  C  CB    . ILE A 1 508 ? 200.174 167.750 195.416 1.00 30.27  ?  527 ILE A CB    1 
ATOM   4040  C  CG1   . ILE A 1 508 ? 200.675 167.264 196.772 1.00 33.90  ?  527 ILE A CG1   1 
ATOM   4041  C  CG2   . ILE A 1 508 ? 198.654 167.821 195.408 1.00 29.80  ?  527 ILE A CG2   1 
ATOM   4042  C  CD1   . ILE A 1 508 ? 200.027 165.973 197.221 1.00 34.04  ?  527 ILE A CD1   1 
ATOM   4043  N  N     . ARG A 1 509 ? 200.343 168.080 192.238 1.00 34.90  ?  528 ARG A N     1 
ATOM   4044  C  CA    . ARG A 1 509 ? 199.658 168.400 190.991 1.00 36.87  ?  528 ARG A CA    1 
ATOM   4045  C  C     . ARG A 1 509 ? 199.816 167.287 189.962 1.00 44.25  ?  528 ARG A C     1 
ATOM   4046  O  O     . ARG A 1 509 ? 198.854 166.935 189.271 1.00 48.85  ?  528 ARG A O     1 
ATOM   4047  C  CB    . ARG A 1 509 ? 200.179 169.724 190.435 1.00 35.50  ?  528 ARG A CB    1 
ATOM   4048  C  CG    . ARG A 1 509 ? 199.137 170.539 189.687 1.00 42.15  ?  528 ARG A CG    1 
ATOM   4049  C  CD    . ARG A 1 509 ? 199.746 171.802 189.098 1.00 44.12  ?  528 ARG A CD    1 
ATOM   4050  N  NE    . ARG A 1 509 ? 198.727 172.717 188.597 1.00 46.83  ?  528 ARG A NE    1 
ATOM   4051  C  CZ    . ARG A 1 509 ? 198.578 173.047 187.322 1.00 47.01  ?  528 ARG A CZ    1 
ATOM   4052  N  NH1   . ARG A 1 509 ? 199.368 172.553 186.383 1.00 43.65  1  528 ARG A NH1   1 
ATOM   4053  N  NH2   . ARG A 1 509 ? 197.611 173.894 186.979 1.00 43.40  ?  528 ARG A NH2   1 
ATOM   4054  N  N     . LYS A 1 510 ? 201.019 166.720 189.843 1.00 42.00  ?  529 LYS A N     1 
ATOM   4055  C  CA    . LYS A 1 510 ? 201.249 165.699 188.827 1.00 43.09  ?  529 LYS A CA    1 
ATOM   4056  C  C     . LYS A 1 510 ? 200.663 164.351 189.229 1.00 40.58  ?  529 LYS A C     1 
ATOM   4057  O  O     . LYS A 1 510 ? 200.165 163.614 188.371 1.00 41.18  ?  529 LYS A O     1 
ATOM   4058  C  CB    . LYS A 1 510 ? 202.746 165.570 188.526 1.00 43.16  ?  529 LYS A CB    1 
ATOM   4059  C  CG    . LYS A 1 510 ? 203.597 164.994 189.650 1.00 44.20  ?  529 LYS A CG    1 
ATOM   4060  C  CD    . LYS A 1 510 ? 205.059 164.907 189.233 1.00 45.74  ?  529 LYS A CD    1 
ATOM   4061  C  CE    . LYS A 1 510 ? 205.954 164.507 190.396 1.00 48.15  ?  529 LYS A CE    1 
ATOM   4062  N  NZ    . LYS A 1 510 ? 206.693 165.672 190.959 1.00 41.64  1  529 LYS A NZ    1 
ATOM   4063  N  N     . ASN A 1 511 ? 200.704 164.003 190.516 1.00 38.13  ?  530 ASN A N     1 
ATOM   4064  C  CA    . ASN A 1 511 ? 200.211 162.700 190.962 1.00 38.20  ?  530 ASN A CA    1 
ATOM   4065  C  C     . ASN A 1 511 ? 198.776 162.808 191.480 1.00 36.63  ?  530 ASN A C     1 
ATOM   4066  O  O     . ASN A 1 511 ? 198.466 162.490 192.628 1.00 47.59  ?  530 ASN A O     1 
ATOM   4067  C  CB    . ASN A 1 511 ? 201.144 162.118 192.017 1.00 42.73  ?  530 ASN A CB    1 
ATOM   4068  C  CG    . ASN A 1 511 ? 202.419 161.559 191.419 1.00 49.02  ?  530 ASN A CG    1 
ATOM   4069  O  OD1   . ASN A 1 511 ? 202.430 161.083 190.284 1.00 53.04  ?  530 ASN A OD1   1 
ATOM   4070  N  ND2   . ASN A 1 511 ? 203.504 161.615 192.181 1.00 44.51  ?  530 ASN A ND2   1 
ATOM   4071  N  N     . GLY A 1 512 ? 197.888 163.266 190.596 1.00 33.19  ?  531 GLY A N     1 
ATOM   4072  C  CA    . GLY A 1 512 ? 196.467 163.318 190.876 1.00 39.89  ?  531 GLY A CA    1 
ATOM   4073  C  C     . GLY A 1 512 ? 195.931 164.739 190.789 1.00 40.56  ?  531 GLY A C     1 
ATOM   4074  O  O     . GLY A 1 512 ? 196.252 165.484 189.855 1.00 37.16  ?  531 GLY A O     1 
ATOM   4075  N  N     . GLY A 1 513 ? 195.116 165.107 191.773 1.00 40.84  ?  532 GLY A N     1 
ATOM   4076  C  CA    . GLY A 1 513 ? 194.431 166.384 191.770 1.00 42.59  ?  532 GLY A CA    1 
ATOM   4077  C  C     . GLY A 1 513 ? 194.531 167.130 193.083 1.00 44.17  ?  532 GLY A C     1 
ATOM   4078  O  O     . GLY A 1 513 ? 195.632 167.431 193.556 1.00 44.06  ?  532 GLY A O     1 
ATOM   4079  N  N     . ASN A 1 514 ? 193.378 167.442 193.672 1.00 42.37  ?  533 ASN A N     1 
ATOM   4080  C  CA    . ASN A 1 514 ? 193.340 168.214 194.908 1.00 36.38  ?  533 ASN A CA    1 
ATOM   4081  C  C     . ASN A 1 514 ? 194.070 167.500 196.039 1.00 27.97  ?  533 ASN A C     1 
ATOM   4082  O  O     . ASN A 1 514 ? 194.133 166.268 196.087 1.00 35.90  ?  533 ASN A O     1 
ATOM   4083  C  CB    . ASN A 1 514 ? 191.889 168.503 195.307 1.00 40.19  ?  533 ASN A CB    1 
ATOM   4084  C  CG    . ASN A 1 514 ? 191.060 167.242 195.516 1.00 41.23  ?  533 ASN A CG    1 
ATOM   4085  O  OD1   . ASN A 1 514 ? 191.567 166.122 195.467 1.00 38.28  ?  533 ASN A OD1   1 
ATOM   4086  N  ND2   . ASN A 1 514 ? 189.767 167.427 195.754 1.00 42.53  ?  533 ASN A ND2   1 
ATOM   4087  N  N     . GLY A 1 515 ? 194.648 168.284 196.934 1.00 29.14  ?  534 GLY A N     1 
ATOM   4088  C  CA    . GLY A 1 515 ? 195.304 167.724 198.098 1.00 28.60  ?  534 GLY A CA    1 
ATOM   4089  C  C     . GLY A 1 515 ? 196.411 168.627 198.580 1.00 34.62  ?  534 GLY A C     1 
ATOM   4090  O  O     . GLY A 1 515 ? 196.775 169.607 197.935 1.00 47.08  ?  534 GLY A O     1 
ATOM   4091  N  N     . TRP A 1 516 ? 196.949 168.276 199.746 1.00 30.52  ?  535 TRP A N     1 
ATOM   4092  C  CA    . TRP A 1 516 ? 198.037 169.031 200.348 1.00 33.16  ?  535 TRP A CA    1 
ATOM   4093  C  C     . TRP A 1 516 ? 199.116 168.068 200.820 1.00 33.98  ?  535 TRP A C     1 
ATOM   4094  O  O     . TRP A 1 516 ? 198.833 166.927 201.193 1.00 41.92  ?  535 TRP A O     1 
ATOM   4095  C  CB    . TRP A 1 516 ? 197.557 169.902 201.519 1.00 38.12  ?  535 TRP A CB    1 
ATOM   4096  C  CG    . TRP A 1 516 ? 196.850 169.155 202.601 1.00 37.69  ?  535 TRP A CG    1 
ATOM   4097  C  CD1   . TRP A 1 516 ? 195.605 168.603 202.538 1.00 41.77  ?  535 TRP A CD1   1 
ATOM   4098  C  CD2   . TRP A 1 516 ? 197.344 168.880 203.918 1.00 30.94  ?  535 TRP A CD2   1 
ATOM   4099  N  NE1   . TRP A 1 516 ? 195.294 167.999 203.731 1.00 41.25  ?  535 TRP A NE1   1 
ATOM   4100  C  CE2   . TRP A 1 516 ? 196.345 168.156 204.595 1.00 38.70  ?  535 TRP A CE2   1 
ATOM   4101  C  CE3   . TRP A 1 516 ? 198.535 169.175 204.588 1.00 32.31  ?  535 TRP A CE3   1 
ATOM   4102  C  CZ2   . TRP A 1 516 ? 196.500 167.721 205.909 1.00 43.81  ?  535 TRP A CZ2   1 
ATOM   4103  C  CZ3   . TRP A 1 516 ? 198.686 168.743 205.893 1.00 35.86  ?  535 TRP A CZ3   1 
ATOM   4104  C  CH2   . TRP A 1 516 ? 197.675 168.024 206.539 1.00 42.33  ?  535 TRP A CH2   1 
ATOM   4105  N  N     . GLN A 1 517 ? 200.359 168.541 200.795 1.00 31.55  ?  536 GLN A N     1 
ATOM   4106  C  CA    . GLN A 1 517 ? 201.488 167.711 201.188 1.00 23.81  ?  536 GLN A CA    1 
ATOM   4107  C  C     . GLN A 1 517 ? 202.591 168.573 201.783 1.00 29.91  ?  536 GLN A C     1 
ATOM   4108  O  O     . GLN A 1 517 ? 202.862 169.676 201.299 1.00 46.85  ?  536 GLN A O     1 
ATOM   4109  C  CB    . GLN A 1 517 ? 202.031 166.912 199.998 1.00 30.35  ?  536 GLN A CB    1 
ATOM   4110  C  CG    . GLN A 1 517 ? 203.243 166.053 200.310 1.00 35.32  ?  536 GLN A CG    1 
ATOM   4111  C  CD    . GLN A 1 517 ? 203.836 165.415 199.069 1.00 42.63  ?  536 GLN A CD    1 
ATOM   4112  O  OE1   . GLN A 1 517 ? 203.110 164.943 198.193 1.00 48.22  ?  536 GLN A OE1   1 
ATOM   4113  N  NE2   . GLN A 1 517 ? 205.160 165.405 198.982 1.00 37.03  ?  536 GLN A NE2   1 
ATOM   4114  N  N     . PHE A 1 518 ? 203.211 168.058 202.841 1.00 32.10  ?  537 PHE A N     1 
ATOM   4115  C  CA    . PHE A 1 518 ? 204.411 168.635 203.419 1.00 36.20  ?  537 PHE A CA    1 
ATOM   4116  C  C     . PHE A 1 518 ? 205.642 168.254 202.605 1.00 42.12  ?  537 PHE A C     1 
ATOM   4117  O  O     . PHE A 1 518 ? 205.686 167.216 201.941 1.00 48.63  ?  537 PHE A O     1 
ATOM   4118  C  CB    . PHE A 1 518 ? 204.617 168.145 204.853 1.00 36.05  ?  537 PHE A CB    1 
ATOM   4119  C  CG    . PHE A 1 518 ? 203.812 168.880 205.881 1.00 34.86  ?  537 PHE A CG    1 
ATOM   4120  C  CD1   . PHE A 1 518 ? 202.519 168.489 206.180 1.00 35.28  ?  537 PHE A CD1   1 
ATOM   4121  C  CD2   . PHE A 1 518 ? 204.365 169.940 206.579 1.00 34.11  ?  537 PHE A CD2   1 
ATOM   4122  C  CE1   . PHE A 1 518 ? 201.787 169.158 207.140 1.00 39.10  ?  537 PHE A CE1   1 
ATOM   4123  C  CE2   . PHE A 1 518 ? 203.638 170.610 207.538 1.00 42.90  ?  537 PHE A CE2   1 
ATOM   4124  C  CZ    . PHE A 1 518 ? 202.349 170.217 207.819 1.00 45.93  ?  537 PHE A CZ    1 
ATOM   4125  N  N     . PHE A 1 519 ? 206.653 169.113 202.665 1.00 37.49  ?  538 PHE A N     1 
ATOM   4126  C  CA    . PHE A 1 519 ? 207.993 168.629 202.383 1.00 36.37  ?  538 PHE A CA    1 
ATOM   4127  C  C     . PHE A 1 519 ? 208.532 167.915 203.621 1.00 42.15  ?  538 PHE A C     1 
ATOM   4128  O  O     . PHE A 1 519 ? 207.919 167.939 204.693 1.00 49.87  ?  538 PHE A O     1 
ATOM   4129  C  CB    . PHE A 1 519 ? 208.913 169.775 201.964 1.00 41.10  ?  538 PHE A CB    1 
ATOM   4130  C  CG    . PHE A 1 519 ? 210.053 169.343 201.083 1.00 42.54  ?  538 PHE A CG    1 
ATOM   4131  C  CD1   . PHE A 1 519 ? 209.833 169.013 199.755 1.00 43.59  ?  538 PHE A CD1   1 
ATOM   4132  C  CD2   . PHE A 1 519 ? 211.340 169.257 201.585 1.00 36.18  ?  538 PHE A CD2   1 
ATOM   4133  C  CE1   . PHE A 1 519 ? 210.878 168.612 198.943 1.00 41.01  ?  538 PHE A CE1   1 
ATOM   4134  C  CE2   . PHE A 1 519 ? 212.389 168.855 200.778 1.00 38.57  ?  538 PHE A CE2   1 
ATOM   4135  C  CZ    . PHE A 1 519 ? 212.158 168.533 199.456 1.00 41.53  ?  538 PHE A CZ    1 
ATOM   4136  N  N     . SER A 1 520 ? 209.702 167.284 203.473 1.00 41.46  ?  539 SER A N     1 
ATOM   4137  C  CA    . SER A 1 520 ? 210.310 166.530 204.567 1.00 50.18  ?  539 SER A CA    1 
ATOM   4138  C  C     . SER A 1 520 ? 209.326 165.502 205.117 1.00 51.72  ?  539 SER A C     1 
ATOM   4139  O  O     . SER A 1 520 ? 208.733 165.720 206.182 1.00 54.59  ?  539 SER A O     1 
ATOM   4140  C  CB    . SER A 1 520 ? 210.788 167.469 205.677 1.00 50.86  ?  539 SER A CB    1 
ATOM   4141  O  OG    . SER A 1 520 ? 211.266 166.736 206.791 1.00 54.25  ?  539 SER A OG    1 
ATOM   4142  N  N     . PRO A 1 521 ? 209.118 164.381 204.414 1.00 49.50  ?  540 PRO A N     1 
ATOM   4143  C  CA    . PRO A 1 521 ? 208.017 163.462 204.767 1.00 53.81  ?  540 PRO A CA    1 
ATOM   4144  C  C     . PRO A 1 521 ? 208.015 162.978 206.213 1.00 53.02  ?  540 PRO A C     1 
ATOM   4145  O  O     . PRO A 1 521 ? 207.089 162.248 206.597 1.00 52.20  ?  540 PRO A O     1 
ATOM   4146  C  CB    . PRO A 1 521 ? 208.215 162.291 203.794 1.00 49.92  ?  540 PRO A CB    1 
ATOM   4147  C  CG    . PRO A 1 521 ? 209.661 162.350 203.422 1.00 47.38  ?  540 PRO A CG    1 
ATOM   4148  C  CD    . PRO A 1 521 ? 210.006 163.810 203.389 1.00 46.92  ?  540 PRO A CD    1 
ATOM   4149  N  N     . ALA A 1 522 ? 209.021 163.332 207.015 1.00 49.92  ?  541 ALA A N     1 
ATOM   4150  C  CA    . ALA A 1 522 ? 208.935 163.097 208.450 1.00 46.05  ?  541 ALA A CA    1 
ATOM   4151  C  C     . ALA A 1 522 ? 207.775 163.858 209.079 1.00 51.23  ?  541 ALA A C     1 
ATOM   4152  O  O     . ALA A 1 522 ? 207.288 163.458 210.142 1.00 56.15  ?  541 ALA A O     1 
ATOM   4153  C  CB    . ALA A 1 522 ? 210.250 163.484 209.128 1.00 48.78  ?  541 ALA A CB    1 
ATOM   4154  N  N     . MET A 1 523 ? 207.327 164.945 208.451 1.00 55.15  ?  542 MET A N     1 
ATOM   4155  C  CA    . MET A 1 523 ? 206.169 165.698 208.911 1.00 54.14  ?  542 MET A CA    1 
ATOM   4156  C  C     . MET A 1 523 ? 204.876 165.268 208.227 1.00 51.38  ?  542 MET A C     1 
ATOM   4157  O  O     . MET A 1 523 ? 203.807 165.781 208.572 1.00 58.01  ?  542 MET A O     1 
ATOM   4158  C  CB    . MET A 1 523 ? 206.402 167.198 208.698 1.00 57.50  ?  542 MET A CB    1 
ATOM   4159  C  CG    . MET A 1 523 ? 205.779 168.084 209.767 1.00 59.37  ?  542 MET A CG    1 
ATOM   4160  S  SD    . MET A 1 523 ? 206.296 169.807 209.639 1.00 74.89  ?  542 MET A SD    1 
ATOM   4161  C  CE    . MET A 1 523 ? 208.033 169.674 210.056 1.00 56.81  ?  542 MET A CE    1 
ATOM   4162  N  N     . ASN A 1 524 ? 204.948 164.339 207.274 1.00 36.89  ?  543 ASN A N     1 
ATOM   4163  C  CA    . ASN A 1 524 ? 203.767 163.755 206.646 1.00 42.67  ?  543 ASN A CA    1 
ATOM   4164  C  C     . ASN A 1 524 ? 203.420 162.385 207.208 1.00 54.50  ?  543 ASN A C     1 
ATOM   4165  O  O     . ASN A 1 524 ? 202.239 162.013 207.240 1.00 57.04  ?  543 ASN A O     1 
ATOM   4166  C  CB    . ASN A 1 524 ? 203.974 163.637 205.132 1.00 43.64  ?  543 ASN A CB    1 
ATOM   4167  C  CG    . ASN A 1 524 ? 202.723 163.974 204.345 1.00 51.22  ?  543 ASN A CG    1 
ATOM   4168  O  OD1   . ASN A 1 524 ? 201.645 164.147 204.913 1.00 58.62  ?  543 ASN A OD1   1 
ATOM   4169  N  ND2   . ASN A 1 524 ? 202.860 164.063 203.027 1.00 50.62  ?  543 ASN A ND2   1 
ATOM   4170  N  N     . GLU A 1 525 ? 204.427 161.628 207.647 1.00 61.74  ?  544 GLU A N     1 
ATOM   4171  C  CA    . GLU A 1 525 ? 204.149 160.387 208.361 1.00 58.44  ?  544 GLU A CA    1 
ATOM   4172  C  C     . GLU A 1 525 ? 203.386 160.657 209.651 1.00 56.28  ?  544 GLU A C     1 
ATOM   4173  O  O     . GLU A 1 525 ? 202.576 159.827 210.079 1.00 59.02  ?  544 GLU A O     1 
ATOM   4174  C  CB    . GLU A 1 525 ? 205.451 159.632 208.641 1.00 59.79  ?  544 GLU A CB    1 
ATOM   4175  C  CG    . GLU A 1 525 ? 206.460 160.389 209.488 1.00 62.24  ?  544 GLU A CG    1 
ATOM   4176  C  CD    . GLU A 1 525 ? 206.347 160.067 210.965 1.00 64.90  ?  544 GLU A CD    1 
ATOM   4177  O  OE1   . GLU A 1 525 ? 205.758 159.018 211.304 1.00 64.94  ?  544 GLU A OE1   1 
ATOM   4178  O  OE2   . GLU A 1 525 ? 206.848 160.862 211.787 1.00 63.23  -1 544 GLU A OE2   1 
ATOM   4179  N  N     . MET A 1 526 ? 203.614 161.818 210.273 1.00 53.74  ?  545 MET A N     1 
ATOM   4180  C  CA    . MET A 1 526 ? 202.826 162.203 211.440 1.00 55.03  ?  545 MET A CA    1 
ATOM   4181  C  C     . MET A 1 526 ? 201.357 162.382 211.078 1.00 58.08  ?  545 MET A C     1 
ATOM   4182  O  O     . MET A 1 526 ? 200.467 161.943 211.819 1.00 65.69  ?  545 MET A O     1 
ATOM   4183  C  CB    . MET A 1 526 ? 203.389 163.489 212.046 1.00 53.68  ?  545 MET A CB    1 
ATOM   4184  C  CG    . MET A 1 526 ? 204.755 163.327 212.689 1.00 57.94  ?  545 MET A CG    1 
ATOM   4185  S  SD    . MET A 1 526 ? 205.247 164.777 213.641 1.00 71.28  ?  545 MET A SD    1 
ATOM   4186  C  CE    . MET A 1 526 ? 204.241 164.575 215.109 1.00 59.05  ?  545 MET A CE    1 
ATOM   4187  N  N     . VAL A 1 527 ? 201.083 163.030 209.943 1.00 49.41  ?  546 VAL A N     1 
ATOM   4188  C  CA    . VAL A 1 527 ? 199.705 163.199 209.488 1.00 52.14  ?  546 VAL A CA    1 
ATOM   4189  C  C     . VAL A 1 527 ? 199.073 161.844 209.199 1.00 57.39  ?  546 VAL A C     1 
ATOM   4190  O  O     . VAL A 1 527 ? 197.910 161.598 209.543 1.00 62.64  ?  546 VAL A O     1 
ATOM   4191  C  CB    . VAL A 1 527 ? 199.658 164.123 208.256 1.00 51.34  ?  546 VAL A CB    1 
ATOM   4192  C  CG1   . VAL A 1 527 ? 198.290 164.065 207.595 1.00 52.81  ?  546 VAL A CG1   1 
ATOM   4193  C  CG2   . VAL A 1 527 ? 199.996 165.550 208.651 1.00 57.43  ?  546 VAL A CG2   1 
ATOM   4194  N  N     . LYS A 1 528 ? 199.825 160.948 208.555 1.00 52.46  ?  547 LYS A N     1 
ATOM   4195  C  CA    . LYS A 1 528 ? 199.304 159.610 208.279 1.00 51.08  ?  547 LYS A CA    1 
ATOM   4196  C  C     . LYS A 1 528 ? 198.981 158.864 209.570 1.00 55.59  ?  547 LYS A C     1 
ATOM   4197  O  O     . LYS A 1 528 ? 197.937 158.204 209.674 1.00 62.44  ?  547 LYS A O     1 
ATOM   4198  C  CB    . LYS A 1 528 ? 200.306 158.818 207.439 1.00 57.00  ?  547 LYS A CB    1 
ATOM   4199  C  CG    . LYS A 1 528 ? 199.688 157.696 206.612 1.00 59.02  ?  547 LYS A CG    1 
ATOM   4200  C  CD    . LYS A 1 528 ? 198.375 158.122 205.972 1.00 60.99  ?  547 LYS A CD    1 
ATOM   4201  C  CE    . LYS A 1 528 ? 197.807 157.017 205.094 1.00 60.30  ?  547 LYS A CE    1 
ATOM   4202  N  NZ    . LYS A 1 528 ? 196.498 157.395 204.494 1.00 60.65  1  547 LYS A NZ    1 
ATOM   4203  N  N     . GLU A 1 529 ? 199.866 158.957 210.566 1.00 52.07  ?  548 GLU A N     1 
ATOM   4204  C  CA    . GLU A 1 529 ? 199.625 158.297 211.845 1.00 51.03  ?  548 GLU A CA    1 
ATOM   4205  C  C     . GLU A 1 529 ? 198.395 158.868 212.538 1.00 51.68  ?  548 GLU A C     1 
ATOM   4206  O  O     . GLU A 1 529 ? 197.582 158.120 213.093 1.00 59.13  ?  548 GLU A O     1 
ATOM   4207  C  CB    . GLU A 1 529 ? 200.856 158.430 212.741 1.00 53.32  ?  548 GLU A CB    1 
ATOM   4208  C  CG    . GLU A 1 529 ? 202.010 157.520 212.353 1.00 60.46  ?  548 GLU A CG    1 
ATOM   4209  C  CD    . GLU A 1 529 ? 202.967 157.275 213.502 1.00 62.30  ?  548 GLU A CD    1 
ATOM   4210  O  OE1   . GLU A 1 529 ? 203.412 158.262 214.125 1.00 58.06  ?  548 GLU A OE1   1 
ATOM   4211  O  OE2   . GLU A 1 529 ? 203.274 156.097 213.781 1.00 60.85  -1 548 GLU A OE2   1 
ATOM   4212  N  N     . ARG A 1 530 ? 198.241 160.193 212.520 1.00 44.53  ?  549 ARG A N     1 
ATOM   4213  C  CA    . ARG A 1 530 ? 197.069 160.796 213.145 1.00 45.80  ?  549 ARG A CA    1 
ATOM   4214  C  C     . ARG A 1 530 ? 195.790 160.390 212.422 1.00 50.44  ?  549 ARG A C     1 
ATOM   4215  O  O     . ARG A 1 530 ? 194.760 160.142 213.060 1.00 59.18  ?  549 ARG A O     1 
ATOM   4216  C  CB    . ARG A 1 530 ? 197.210 162.316 213.185 1.00 50.91  ?  549 ARG A CB    1 
ATOM   4217  C  CG    . ARG A 1 530 ? 196.277 162.974 214.183 1.00 52.72  ?  549 ARG A CG    1 
ATOM   4218  C  CD    . ARG A 1 530 ? 196.603 164.442 214.385 1.00 56.47  ?  549 ARG A CD    1 
ATOM   4219  N  NE    . ARG A 1 530 ? 195.695 165.064 215.340 1.00 53.39  ?  549 ARG A NE    1 
ATOM   4220  C  CZ    . ARG A 1 530 ? 195.840 165.006 216.657 1.00 55.99  ?  549 ARG A CZ    1 
ATOM   4221  N  NH1   . ARG A 1 530 ? 196.849 164.355 217.213 1.00 57.01  1  549 ARG A NH1   1 
ATOM   4222  N  NH2   . ARG A 1 530 ? 194.950 165.613 217.436 1.00 54.98  ?  549 ARG A NH2   1 
ATOM   4223  N  N     . LEU A 1 531 ? 195.836 160.309 211.090 1.00 46.25  ?  550 LEU A N     1 
ATOM   4224  C  CA    . LEU A 1 531 ? 194.659 159.894 210.333 1.00 50.20  ?  550 LEU A CA    1 
ATOM   4225  C  C     . LEU A 1 531 ? 194.278 158.450 210.639 1.00 50.06  ?  550 LEU A C     1 
ATOM   4226  O  O     . LEU A 1 531 ? 193.092 158.135 210.801 1.00 47.94  ?  550 LEU A O     1 
ATOM   4227  C  CB    . LEU A 1 531 ? 194.907 160.079 208.835 1.00 49.27  ?  550 LEU A CB    1 
ATOM   4228  C  CG    . LEU A 1 531 ? 193.664 160.130 207.944 1.00 48.28  ?  550 LEU A CG    1 
ATOM   4229  C  CD1   . LEU A 1 531 ? 192.727 161.245 208.385 1.00 46.61  ?  550 LEU A CD1   1 
ATOM   4230  C  CD2   . LEU A 1 531 ? 194.057 160.302 206.484 1.00 49.12  ?  550 LEU A CD2   1 
ATOM   4231  N  N     . VAL A 1 532 ? 195.266 157.554 210.719 1.00 47.31  ?  551 VAL A N     1 
ATOM   4232  C  CA    . VAL A 1 532 ? 194.947 156.160 211.018 1.00 47.03  ?  551 VAL A CA    1 
ATOM   4233  C  C     . VAL A 1 532 ? 194.440 156.023 212.451 1.00 48.95  ?  551 VAL A C     1 
ATOM   4234  O  O     . VAL A 1 532 ? 193.542 155.218 212.730 1.00 48.58  ?  551 VAL A O     1 
ATOM   4235  C  CB    . VAL A 1 532 ? 196.152 155.242 210.727 1.00 47.49  ?  551 VAL A CB    1 
ATOM   4236  C  CG1   . VAL A 1 532 ? 197.226 155.355 211.796 1.00 43.12  ?  551 VAL A CG1   1 
ATOM   4237  C  CG2   . VAL A 1 532 ? 195.693 153.796 210.584 1.00 45.35  ?  551 VAL A CG2   1 
ATOM   4238  N  N     . LEU A 1 533 ? 194.983 156.821 213.378 1.00 48.79  ?  552 LEU A N     1 
ATOM   4239  C  CA    . LEU A 1 533 ? 194.465 156.822 214.743 1.00 41.33  ?  552 LEU A CA    1 
ATOM   4240  C  C     . LEU A 1 533 ? 193.023 157.311 214.782 1.00 41.09  ?  552 LEU A C     1 
ATOM   4241  O  O     . LEU A 1 533 ? 192.193 156.769 215.521 1.00 45.94  ?  552 LEU A O     1 
ATOM   4242  C  CB    . LEU A 1 533 ? 195.350 157.687 215.640 1.00 37.68  ?  552 LEU A CB    1 
ATOM   4243  C  CG    . LEU A 1 533 ? 194.771 158.070 217.004 1.00 40.23  ?  552 LEU A CG    1 
ATOM   4244  C  CD1   . LEU A 1 533 ? 194.561 156.839 217.874 1.00 48.29  ?  552 LEU A CD1   1 
ATOM   4245  C  CD2   . LEU A 1 533 ? 195.661 159.081 217.707 1.00 42.53  ?  552 LEU A CD2   1 
ATOM   4246  N  N     . GLY A 1 534 ? 192.706 158.342 213.998 1.00 47.35  ?  553 GLY A N     1 
ATOM   4247  C  CA    . GLY A 1 534 ? 191.334 158.817 213.935 1.00 49.80  ?  553 GLY A CA    1 
ATOM   4248  C  C     . GLY A 1 534 ? 190.384 157.786 213.356 1.00 51.34  ?  553 GLY A C     1 
ATOM   4249  O  O     . GLY A 1 534 ? 189.254 157.634 213.827 1.00 55.56  ?  553 GLY A O     1 
ATOM   4250  N  N     . ALA A 1 535 ? 190.825 157.073 212.318 1.00 49.17  ?  554 ALA A N     1 
ATOM   4251  C  CA    . ALA A 1 535 ? 190.007 155.998 211.766 1.00 47.81  ?  554 ALA A CA    1 
ATOM   4252  C  C     . ALA A 1 535 ? 189.779 154.899 212.797 1.00 43.56  ?  554 ALA A C     1 
ATOM   4253  O  O     . ALA A 1 535 ? 188.671 154.357 212.909 1.00 39.89  ?  554 ALA A O     1 
ATOM   4254  C  CB    . ALA A 1 535 ? 190.662 155.430 210.507 1.00 47.99  ?  554 ALA A CB    1 
ATOM   4255  N  N     . ALA A 1 536 ? 190.821 154.557 213.561 1.00 47.93  ?  555 ALA A N     1 
ATOM   4256  C  CA    . ALA A 1 536 ? 190.668 153.574 214.629 1.00 45.11  ?  555 ALA A CA    1 
ATOM   4257  C  C     . ALA A 1 536 ? 189.677 154.054 215.682 1.00 48.18  ?  555 ALA A C     1 
ATOM   4258  O  O     . ALA A 1 536 ? 188.859 153.272 216.178 1.00 52.87  ?  555 ALA A O     1 
ATOM   4259  C  CB    . ALA A 1 536 ? 192.025 153.272 215.264 1.00 46.54  ?  555 ALA A CB    1 
ATOM   4260  N  N     . LEU A 1 537 ? 189.735 155.339 216.036 1.00 47.57  ?  556 LEU A N     1 
ATOM   4261  C  CA    . LEU A 1 537 ? 188.783 155.887 216.998 1.00 42.72  ?  556 LEU A CA    1 
ATOM   4262  C  C     . LEU A 1 537 ? 187.356 155.807 216.470 1.00 45.88  ?  556 LEU A C     1 
ATOM   4263  O  O     . LEU A 1 537 ? 186.433 155.433 217.205 1.00 48.14  ?  556 LEU A O     1 
ATOM   4264  C  CB    . LEU A 1 537 ? 189.146 157.333 217.333 1.00 41.72  ?  556 LEU A CB    1 
ATOM   4265  C  CG    . LEU A 1 537 ? 188.270 158.023 218.381 1.00 48.66  ?  556 LEU A CG    1 
ATOM   4266  C  CD1   . LEU A 1 537 ? 188.199 157.199 219.656 1.00 48.01  ?  556 LEU A CD1   1 
ATOM   4267  C  CD2   . LEU A 1 537 ? 188.778 159.427 218.670 1.00 55.10  ?  556 LEU A CD2   1 
ATOM   4268  N  N     . LYS A 1 538 ? 187.157 156.153 215.196 1.00 50.13  ?  557 LYS A N     1 
ATOM   4269  C  CA    . LYS A 1 538 ? 185.817 156.103 214.619 1.00 51.57  ?  557 LYS A CA    1 
ATOM   4270  C  C     . LYS A 1 538 ? 185.277 154.678 214.600 1.00 50.59  ?  557 LYS A C     1 
ATOM   4271  O  O     . LYS A 1 538 ? 184.115 154.442 214.956 1.00 47.07  ?  557 LYS A O     1 
ATOM   4272  C  CB    . LYS A 1 538 ? 185.825 156.694 213.209 1.00 50.67  ?  557 LYS A CB    1 
ATOM   4273  C  CG    . LYS A 1 538 ? 184.534 156.462 212.439 1.00 50.07  ?  557 LYS A CG    1 
ATOM   4274  C  CD    . LYS A 1 538 ? 184.729 156.668 210.947 1.00 52.22  ?  557 LYS A CD    1 
ATOM   4275  C  CE    . LYS A 1 538 ? 185.049 158.118 210.631 1.00 53.89  ?  557 LYS A CE    1 
ATOM   4276  N  NZ    . LYS A 1 538 ? 183.822 158.961 210.612 1.00 51.79  1  557 LYS A NZ    1 
ATOM   4277  N  N     . GLU A 1 539 ? 186.108 153.710 214.204 1.00 50.97  ?  558 GLU A N     1 
ATOM   4278  C  CA    . GLU A 1 539 ? 185.628 152.331 214.165 1.00 48.50  ?  558 GLU A CA    1 
ATOM   4279  C  C     . GLU A 1 539 ? 185.391 151.783 215.568 1.00 45.29  ?  558 GLU A C     1 
ATOM   4280  O  O     . GLU A 1 539 ? 184.462 150.995 215.769 1.00 50.60  ?  558 GLU A O     1 
ATOM   4281  C  CB    . GLU A 1 539 ? 186.596 151.437 213.381 1.00 51.69  ?  558 GLU A CB    1 
ATOM   4282  C  CG    . GLU A 1 539 ? 187.998 151.314 213.951 1.00 54.08  ?  558 GLU A CG    1 
ATOM   4283  C  CD    . GLU A 1 539 ? 188.116 150.219 214.994 1.00 54.33  ?  558 GLU A CD    1 
ATOM   4284  O  OE1   . GLU A 1 539 ? 187.248 149.321 215.014 1.00 50.13  ?  558 GLU A OE1   1 
ATOM   4285  O  OE2   . GLU A 1 539 ? 189.072 150.259 215.797 1.00 53.38  -1 558 GLU A OE2   1 
ATOM   4286  N  N     . ALA A 1 540 ? 186.201 152.192 216.549 1.00 43.98  ?  559 ALA A N     1 
ATOM   4287  C  CA    . ALA A 1 540 ? 185.956 151.778 217.926 1.00 48.47  ?  559 ALA A CA    1 
ATOM   4288  C  C     . ALA A 1 540 ? 184.639 152.341 218.445 1.00 46.84  ?  559 ALA A C     1 
ATOM   4289  O  O     . ALA A 1 540 ? 183.880 151.638 219.123 1.00 47.02  ?  559 ALA A O     1 
ATOM   4290  C  CB    . ALA A 1 540 ? 187.117 152.213 218.820 1.00 48.49  ?  559 ALA A CB    1 
ATOM   4291  N  N     . ILE A 1 541 ? 184.350 153.607 218.131 1.00 50.38  ?  560 ILE A N     1 
ATOM   4292  C  CA    . ILE A 1 541 ? 183.070 154.194 218.521 1.00 52.08  ?  560 ILE A CA    1 
ATOM   4293  C  C     . ILE A 1 541 ? 181.922 153.442 217.863 1.00 49.79  ?  560 ILE A C     1 
ATOM   4294  O  O     . ILE A 1 541 ? 180.900 153.156 218.499 1.00 48.34  ?  560 ILE A O     1 
ATOM   4295  C  CB    . ILE A 1 541 ? 183.039 155.694 218.171 1.00 53.46  ?  560 ILE A CB    1 
ATOM   4296  C  CG1   . ILE A 1 541 ? 184.026 156.469 219.045 1.00 55.36  ?  560 ILE A CG1   1 
ATOM   4297  C  CG2   . ILE A 1 541 ? 181.633 156.256 218.331 1.00 48.03  ?  560 ILE A CG2   1 
ATOM   4298  C  CD1   . ILE A 1 541 ? 184.252 157.893 218.589 1.00 54.23  ?  560 ILE A CD1   1 
ATOM   4299  N  N     . SER A 1 542 ? 182.073 153.107 216.580 1.00 55.18  ?  561 SER A N     1 
ATOM   4300  C  CA    . SER A 1 542 ? 181.023 152.376 215.876 1.00 51.66  ?  561 SER A CA    1 
ATOM   4301  C  C     . SER A 1 542 ? 180.798 150.995 216.483 1.00 52.19  ?  561 SER A C     1 
ATOM   4302  O  O     . SER A 1 542 ? 179.651 150.558 216.641 1.00 55.21  ?  561 SER A O     1 
ATOM   4303  C  CB    . SER A 1 542 ? 181.371 152.259 214.392 1.00 53.06  ?  561 SER A CB    1 
ATOM   4304  O  OG    . SER A 1 542 ? 180.523 151.329 213.740 1.00 53.93  ?  561 SER A OG    1 
ATOM   4305  N  N     . ASN A 1 543 ? 181.875 150.294 216.833 1.00 54.09  ?  562 ASN A N     1 
ATOM   4306  C  CA    . ASN A 1 543 ? 181.791 148.921 217.314 1.00 53.50  ?  562 ASN A CA    1 
ATOM   4307  C  C     . ASN A 1 543 ? 181.660 148.818 218.830 1.00 53.85  ?  562 ASN A C     1 
ATOM   4308  O  O     . ASN A 1 543 ? 181.690 147.703 219.361 1.00 57.81  ?  562 ASN A O     1 
ATOM   4309  C  CB    . ASN A 1 543 ? 183.011 148.123 216.848 1.00 53.24  ?  562 ASN A CB    1 
ATOM   4310  C  CG    . ASN A 1 543 ? 183.244 148.234 215.354 1.00 59.08  ?  562 ASN A CG    1 
ATOM   4311  O  OD1   . ASN A 1 543 ? 182.300 148.365 214.575 1.00 60.94  ?  562 ASN A OD1   1 
ATOM   4312  N  ND2   . ASN A 1 543 ? 184.507 148.179 214.947 1.00 55.03  ?  562 ASN A ND2   1 
ATOM   4313  N  N     . ASN A 1 544 ? 181.538 149.946 219.534 1.00 49.72  ?  563 ASN A N     1 
ATOM   4314  C  CA    . ASN A 1 544 ? 181.228 149.949 220.967 1.00 52.75  ?  563 ASN A CA    1 
ATOM   4315  C  C     . ASN A 1 544 ? 182.357 149.328 221.789 1.00 55.88  ?  563 ASN A C     1 
ATOM   4316  O  O     . ASN A 1 544 ? 182.123 148.527 222.696 1.00 55.13  ?  563 ASN A O     1 
ATOM   4317  C  CB    . ASN A 1 544 ? 179.895 149.242 221.240 1.00 52.45  ?  563 ASN A CB    1 
ATOM   4318  C  CG    . ASN A 1 544 ? 179.329 149.560 222.610 1.00 54.55  ?  563 ASN A CG    1 
ATOM   4319  O  OD1   . ASN A 1 544 ? 179.920 150.316 223.378 1.00 54.86  ?  563 ASN A OD1   1 
ATOM   4320  N  ND2   . ASN A 1 544 ? 178.176 148.980 222.923 1.00 53.75  ?  563 ASN A ND2   1 
ATOM   4321  N  N     . GLN A 1 545 ? 183.597 149.693 221.466 1.00 55.13  ?  564 GLN A N     1 
ATOM   4322  C  CA    . GLN A 1 545 ? 184.755 149.245 222.229 1.00 51.94  ?  564 GLN A CA    1 
ATOM   4323  C  C     . GLN A 1 545 ? 185.210 150.249 223.280 1.00 50.28  ?  564 GLN A C     1 
ATOM   4324  O  O     . GLN A 1 545 ? 186.147 149.953 224.029 1.00 53.42  ?  564 GLN A O     1 
ATOM   4325  C  CB    . GLN A 1 545 ? 185.925 148.930 221.290 1.00 53.28  ?  564 GLN A CB    1 
ATOM   4326  C  CG    . GLN A 1 545 ? 185.647 147.801 220.315 1.00 53.65  ?  564 GLN A CG    1 
ATOM   4327  C  CD    . GLN A 1 545 ? 186.890 146.994 219.998 1.00 56.30  ?  564 GLN A CD    1 
ATOM   4328  O  OE1   . GLN A 1 545 ? 187.966 147.254 220.536 1.00 56.02  ?  564 GLN A OE1   1 
ATOM   4329  N  NE2   . GLN A 1 545 ? 186.747 146.008 219.121 1.00 54.94  ?  564 GLN A NE2   1 
ATOM   4330  N  N     . LEU A 1 546 ? 184.582 151.419 223.347 1.00 39.67  ?  565 LEU A N     1 
ATOM   4331  C  CA    . LEU A 1 546 ? 184.939 152.408 224.351 1.00 32.35  ?  565 LEU A CA    1 
ATOM   4332  C  C     . LEU A 1 546 ? 184.481 151.954 225.735 1.00 32.60  ?  565 LEU A C     1 
ATOM   4333  O  O     . LEU A 1 546 ? 183.611 151.092 225.882 1.00 45.28  ?  565 LEU A O     1 
ATOM   4334  C  CB    . LEU A 1 546 ? 184.323 153.768 224.012 1.00 31.81  ?  565 LEU A CB    1 
ATOM   4335  C  CG    . LEU A 1 546 ? 185.049 154.698 223.031 1.00 31.81  ?  565 LEU A CG    1 
ATOM   4336  C  CD1   . LEU A 1 546 ? 185.439 154.000 221.738 1.00 40.93  ?  565 LEU A CD1   1 
ATOM   4337  C  CD2   . LEU A 1 546 ? 184.195 155.919 222.732 1.00 32.92  ?  565 LEU A CD2   1 
ATOM   4338  N  N     . LYS A 1 547 ? 185.094 152.540 226.760 1.00 19.91  ?  566 LYS A N     1 
ATOM   4339  C  CA    . LYS A 1 547 ? 184.762 152.229 228.142 1.00 25.66  ?  566 LYS A CA    1 
ATOM   4340  C  C     . LYS A 1 547 ? 184.723 153.512 228.958 1.00 31.91  ?  566 LYS A C     1 
ATOM   4341  O  O     . LYS A 1 547 ? 185.376 154.502 228.618 1.00 45.46  ?  566 LYS A O     1 
ATOM   4342  C  CB    . LYS A 1 547 ? 185.767 151.249 228.759 1.00 33.08  ?  566 LYS A CB    1 
ATOM   4343  C  CG    . LYS A 1 547 ? 185.560 149.809 228.332 1.00 42.69  ?  566 LYS A CG    1 
ATOM   4344  C  CD    . LYS A 1 547 ? 186.739 148.942 228.733 1.00 45.43  ?  566 LYS A CD    1 
ATOM   4345  C  CE    . LYS A 1 547 ? 186.525 147.503 228.302 1.00 41.98  ?  566 LYS A CE    1 
ATOM   4346  N  NZ    . LYS A 1 547 ? 185.093 147.104 228.397 1.00 41.48  1  566 LYS A NZ    1 
ATOM   4347  N  N     . LEU A 1 548 ? 183.949 153.482 230.040 1.00 27.36  ?  567 LEU A N     1 
ATOM   4348  C  CA    . LEU A 1 548 ? 183.847 154.600 230.964 1.00 33.67  ?  567 LEU A CA    1 
ATOM   4349  C  C     . LEU A 1 548 ? 184.381 154.194 232.330 1.00 33.92  ?  567 LEU A C     1 
ATOM   4350  O  O     . LEU A 1 548 ? 184.227 153.047 232.761 1.00 44.50  ?  567 LEU A O     1 
ATOM   4351  C  CB    . LEU A 1 548 ? 182.398 155.086 231.106 1.00 38.00  ?  567 LEU A CB    1 
ATOM   4352  C  CG    . LEU A 1 548 ? 181.698 155.619 229.856 1.00 31.52  ?  567 LEU A CG    1 
ATOM   4353  C  CD1   . LEU A 1 548 ? 180.410 156.334 230.237 1.00 38.09  ?  567 LEU A CD1   1 
ATOM   4354  C  CD2   . LEU A 1 548 ? 182.612 156.536 229.063 1.00 36.05  ?  567 LEU A CD2   1 
ATOM   4355  N  N     . VAL A 1 549 ? 185.011 155.149 233.009 1.00 17.00  ?  568 VAL A N     1 
ATOM   4356  C  CA    . VAL A 1 549 ? 185.562 154.946 234.342 1.00 23.28  ?  568 VAL A CA    1 
ATOM   4357  C  C     . VAL A 1 549 ? 185.078 156.083 235.231 1.00 26.88  ?  568 VAL A C     1 
ATOM   4358  O  O     . VAL A 1 549 ? 185.007 157.236 234.794 1.00 31.96  ?  568 VAL A O     1 
ATOM   4359  C  CB    . VAL A 1 549 ? 187.104 154.866 234.318 1.00 38.04  ?  568 VAL A CB    1 
ATOM   4360  C  CG1   . VAL A 1 549 ? 187.636 154.526 235.685 1.00 43.18  ?  568 VAL A CG1   1 
ATOM   4361  C  CG2   . VAL A 1 549 ? 187.562 153.812 233.330 1.00 41.77  ?  568 VAL A CG2   1 
ATOM   4362  N  N     . TYR A 1 550 ? 184.746 155.755 236.478 1.00 38.71  ?  569 TYR A N     1 
ATOM   4363  C  CA    . TYR A 1 550 ? 183.988 156.635 237.356 1.00 33.27  ?  569 TYR A CA    1 
ATOM   4364  C  C     . TYR A 1 550 ? 184.835 157.078 238.541 1.00 36.45  ?  569 TYR A C     1 
ATOM   4365  O  O     . TYR A 1 550 ? 185.542 156.269 239.149 1.00 48.91  ?  569 TYR A O     1 
ATOM   4366  C  CB    . TYR A 1 550 ? 182.725 155.926 237.848 1.00 29.51  ?  569 TYR A CB    1 
ATOM   4367  C  CG    . TYR A 1 550 ? 181.804 155.531 236.721 1.00 33.22  ?  569 TYR A CG    1 
ATOM   4368  C  CD1   . TYR A 1 550 ? 180.932 156.450 236.157 1.00 37.42  ?  569 TYR A CD1   1 
ATOM   4369  C  CD2   . TYR A 1 550 ? 181.835 154.250 236.193 1.00 34.33  ?  569 TYR A CD2   1 
ATOM   4370  C  CE1   . TYR A 1 550 ? 180.096 156.095 235.118 1.00 37.84  ?  569 TYR A CE1   1 
ATOM   4371  C  CE2   . TYR A 1 550 ? 181.009 153.889 235.150 1.00 35.56  ?  569 TYR A CE2   1 
ATOM   4372  C  CZ    . TYR A 1 550 ? 180.138 154.814 234.618 1.00 37.78  ?  569 TYR A CZ    1 
ATOM   4373  O  OH    . TYR A 1 550 ? 179.311 154.454 233.579 1.00 42.74  ?  569 TYR A OH    1 
ATOM   4374  N  N     . GLN A 1 551 ? 184.753 158.364 238.863 1.00 29.91  ?  570 GLN A N     1 
ATOM   4375  C  CA    . GLN A 1 551 ? 185.499 158.947 239.978 1.00 21.69  ?  570 GLN A CA    1 
ATOM   4376  C  C     . GLN A 1 551 ? 184.538 159.532 241.002 1.00 26.23  ?  570 GLN A C     1 
ATOM   4377  O  O     . GLN A 1 551 ? 183.874 160.547 240.716 1.00 43.24  ?  570 GLN A O     1 
ATOM   4378  C  CB    . GLN A 1 551 ? 186.463 160.024 239.485 1.00 28.74  ?  570 GLN A CB    1 
ATOM   4379  C  CG    . GLN A 1 551 ? 187.239 160.696 240.601 1.00 35.00  ?  570 GLN A CG    1 
ATOM   4380  C  CD    . GLN A 1 551 ? 188.384 161.536 240.086 1.00 40.44  ?  570 GLN A CD    1 
ATOM   4381  O  OE1   . GLN A 1 551 ? 188.215 162.344 239.173 1.00 42.64  ?  570 GLN A OE1   1 
ATOM   4382  N  NE2   . GLN A 1 551 ? 189.562 161.350 240.669 1.00 41.87  ?  570 GLN A NE2   1 
ATOM   4383  N  N     . PRO A 1 552 ? 184.419 158.936 242.187 1.00 35.46  ?  571 PRO A N     1 
ATOM   4384  C  CA    . PRO A 1 552 ? 183.503 159.473 243.199 1.00 43.71  ?  571 PRO A CA    1 
ATOM   4385  C  C     . PRO A 1 552 ? 183.864 160.887 243.630 1.00 53.71  ?  571 PRO A C     1 
ATOM   4386  O  O     . PRO A 1 552 ? 185.036 161.258 243.723 1.00 58.11  ?  571 PRO A O     1 
ATOM   4387  C  CB    . PRO A 1 552 ? 183.648 158.486 244.362 1.00 47.05  ?  571 PRO A CB    1 
ATOM   4388  C  CG    . PRO A 1 552 ? 184.095 157.216 243.719 1.00 48.43  ?  571 PRO A CG    1 
ATOM   4389  C  CD    . PRO A 1 552 ? 184.984 157.636 242.586 1.00 47.24  ?  571 PRO A CD    1 
ATOM   4390  N  N     . GLN A 1 553 ? 182.825 161.676 243.890 1.00 49.49  ?  572 GLN A N     1 
ATOM   4391  C  CA    . GLN A 1 553 ? 182.940 162.984 244.517 1.00 45.77  ?  572 GLN A CA    1 
ATOM   4392  C  C     . GLN A 1 553 ? 182.403 162.888 245.939 1.00 45.36  ?  572 GLN A C     1 
ATOM   4393  O  O     . GLN A 1 553 ? 181.427 162.177 246.192 1.00 49.05  ?  572 GLN A O     1 
ATOM   4394  C  CB    . GLN A 1 553 ? 182.164 164.044 243.732 1.00 47.38  ?  572 GLN A CB    1 
ATOM   4395  C  CG    . GLN A 1 553 ? 182.149 163.818 242.233 1.00 41.47  ?  572 GLN A CG    1 
ATOM   4396  C  CD    . GLN A 1 553 ? 181.578 164.996 241.476 1.00 46.15  ?  572 GLN A CD    1 
ATOM   4397  O  OE1   . GLN A 1 553 ? 180.589 165.597 241.897 1.00 54.67  ?  572 GLN A OE1   1 
ATOM   4398  N  NE2   . GLN A 1 553 ? 182.193 165.332 240.350 1.00 49.17  ?  572 GLN A NE2   1 
ATOM   4399  N  N     . ILE A 1 554 ? 183.034 163.604 246.864 1.00 60.04  ?  573 ILE A N     1 
ATOM   4400  C  CA    . ILE A 1 554 ? 182.735 163.436 248.281 1.00 64.98  ?  573 ILE A CA    1 
ATOM   4401  C  C     . ILE A 1 554 ? 182.253 164.755 248.869 1.00 68.19  ?  573 ILE A C     1 
ATOM   4402  O  O     . ILE A 1 554 ? 182.623 165.840 248.411 1.00 69.88  ?  573 ILE A O     1 
ATOM   4403  C  CB    . ILE A 1 554 ? 183.961 162.900 249.056 1.00 63.88  ?  573 ILE A CB    1 
ATOM   4404  C  CG1   . ILE A 1 554 ? 183.509 162.087 250.269 1.00 65.23  ?  573 ILE A CG1   1 
ATOM   4405  C  CG2   . ILE A 1 554 ? 184.881 164.032 249.479 1.00 61.46  ?  573 ILE A CG2   1 
ATOM   4406  C  CD1   . ILE A 1 554 ? 182.746 160.839 249.903 1.00 66.24  ?  573 ILE A CD1   1 
ATOM   4407  N  N     . PHE A 1 555 ? 181.395 164.650 249.882 1.00 72.52  ?  574 PHE A N     1 
ATOM   4408  C  CA    . PHE A 1 555 ? 180.981 165.816 250.648 1.00 65.30  ?  574 PHE A CA    1 
ATOM   4409  C  C     . PHE A 1 555 ? 182.094 166.244 251.596 1.00 66.69  ?  574 PHE A C     1 
ATOM   4410  O  O     . PHE A 1 555 ? 182.911 165.430 252.037 1.00 72.84  ?  574 PHE A O     1 
ATOM   4411  C  CB    . PHE A 1 555 ? 179.708 165.515 251.441 1.00 65.76  ?  574 PHE A CB    1 
ATOM   4412  C  CG    . PHE A 1 555 ? 178.438 165.736 250.668 1.00 68.82  ?  574 PHE A CG    1 
ATOM   4413  C  CD1   . PHE A 1 555 ? 178.254 166.892 249.929 1.00 69.80  ?  574 PHE A CD1   1 
ATOM   4414  C  CD2   . PHE A 1 555 ? 177.426 164.792 250.687 1.00 71.22  ?  574 PHE A CD2   1 
ATOM   4415  C  CE1   . PHE A 1 555 ? 177.086 167.101 249.220 1.00 70.74  ?  574 PHE A CE1   1 
ATOM   4416  C  CE2   . PHE A 1 555 ? 176.255 164.995 249.980 1.00 70.86  ?  574 PHE A CE2   1 
ATOM   4417  C  CZ    . PHE A 1 555 ? 176.085 166.151 249.246 1.00 69.75  ?  574 PHE A CZ    1 
ATOM   4418  N  N     . ALA A 1 556 ? 182.131 167.543 251.904 1.00 80.31  ?  575 ALA A N     1 
ATOM   4419  C  CA    . ALA A 1 556 ? 183.177 168.051 252.787 1.00 80.69  ?  575 ALA A CA    1 
ATOM   4420  C  C     . ALA A 1 556 ? 183.069 167.470 254.192 1.00 86.71  ?  575 ALA A C     1 
ATOM   4421  O  O     . ALA A 1 556 ? 184.072 167.035 254.769 1.00 89.08  ?  575 ALA A O     1 
ATOM   4422  C  CB    . ALA A 1 556 ? 183.123 169.575 252.845 1.00 82.85  ?  575 ALA A CB    1 
ATOM   4423  N  N     . GLU A 1 557 ? 181.863 167.449 254.760 1.00 95.54  ?  576 GLU A N     1 
ATOM   4424  C  CA    . GLU A 1 557 ? 181.681 167.119 256.169 1.00 92.19  ?  576 GLU A CA    1 
ATOM   4425  C  C     . GLU A 1 557 ? 181.147 165.710 256.395 1.00 89.29  ?  576 GLU A C     1 
ATOM   4426  O  O     . GLU A 1 557 ? 181.690 164.968 257.219 1.00 89.05  ?  576 GLU A O     1 
ATOM   4427  C  CB    . GLU A 1 557 ? 180.742 168.138 256.826 1.00 90.74  ?  576 GLU A CB    1 
ATOM   4428  C  CG    . GLU A 1 557 ? 180.998 169.577 256.413 1.00 93.26  ?  576 GLU A CG    1 
ATOM   4429  C  CD    . GLU A 1 557 ? 182.319 170.105 256.933 1.00 94.32  ?  576 GLU A CD    1 
ATOM   4430  O  OE1   . GLU A 1 557 ? 182.735 169.687 258.034 1.00 96.01  ?  576 GLU A OE1   1 
ATOM   4431  O  OE2   . GLU A 1 557 ? 182.939 170.944 256.245 1.00 91.93  -1 576 GLU A OE2   1 
ATOM   4432  N  N     . THR A 1 558 ? 180.090 165.323 255.683 1.00 85.96  ?  577 THR A N     1 
ATOM   4433  C  CA    . THR A 1 558 ? 179.469 164.028 255.924 1.00 88.13  ?  577 THR A CA    1 
ATOM   4434  C  C     . THR A 1 558 ? 180.258 162.873 255.324 1.00 85.18  ?  577 THR A C     1 
ATOM   4435  O  O     . THR A 1 558 ? 180.013 161.718 255.692 1.00 85.10  ?  577 THR A O     1 
ATOM   4436  C  CB    . THR A 1 558 ? 178.044 164.011 255.368 1.00 87.38  ?  577 THR A CB    1 
ATOM   4437  O  OG1   . THR A 1 558 ? 178.082 164.148 253.942 1.00 84.89  ?  577 THR A OG1   1 
ATOM   4438  C  CG2   . THR A 1 558 ? 177.229 165.150 255.960 1.00 84.44  ?  577 THR A CG2   1 
ATOM   4439  N  N     . GLY A 1 559 ? 181.196 163.151 254.425 1.00 79.92  ?  578 GLY A N     1 
ATOM   4440  C  CA    . GLY A 1 559 ? 181.915 162.080 253.754 1.00 80.96  ?  578 GLY A CA    1 
ATOM   4441  C  C     . GLY A 1 559 ? 181.011 161.196 252.925 1.00 81.86  ?  578 GLY A C     1 
ATOM   4442  O  O     . GLY A 1 559 ? 181.170 159.968 252.927 1.00 83.22  ?  578 GLY A O     1 
ATOM   4443  N  N     . GLU A 1 560 ? 180.064 161.795 252.209 1.00 72.92  ?  579 GLU A N     1 
ATOM   4444  C  CA    . GLU A 1 560 ? 179.073 161.067 251.435 1.00 69.91  ?  579 GLU A CA    1 
ATOM   4445  C  C     . GLU A 1 560 ? 179.254 161.378 249.956 1.00 66.55  ?  579 GLU A C     1 
ATOM   4446  O  O     . GLU A 1 560 ? 179.678 162.476 249.582 1.00 70.09  ?  579 GLU A O     1 
ATOM   4447  C  CB    . GLU A 1 560 ? 177.647 161.429 251.889 1.00 69.29  ?  579 GLU A CB    1 
ATOM   4448  C  CG    . GLU A 1 560 ? 176.531 160.716 251.138 1.00 71.07  ?  579 GLU A CG    1 
ATOM   4449  C  CD    . GLU A 1 560 ? 176.602 159.208 251.277 1.00 73.98  ?  579 GLU A CD    1 
ATOM   4450  O  OE1   . GLU A 1 560 ? 176.319 158.506 250.284 1.00 73.67  ?  579 GLU A OE1   1 
ATOM   4451  O  OE2   . GLU A 1 560 ? 176.939 158.725 252.378 1.00 74.37  -1 579 GLU A OE2   1 
ATOM   4452  N  N     . LEU A 1 561 ? 178.933 160.397 249.117 1.00 54.16  ?  580 LEU A N     1 
ATOM   4453  C  CA    . LEU A 1 561 ? 179.123 160.527 247.678 1.00 50.67  ?  580 LEU A CA    1 
ATOM   4454  C  C     . LEU A 1 561 ? 178.046 161.432 247.092 1.00 49.31  ?  580 LEU A C     1 
ATOM   4455  O  O     . LEU A 1 561 ? 176.877 161.044 247.000 1.00 45.29  ?  580 LEU A O     1 
ATOM   4456  C  CB    . LEU A 1 561 ? 179.107 159.149 247.023 1.00 48.21  ?  580 LEU A CB    1 
ATOM   4457  C  CG    . LEU A 1 561 ? 179.494 159.061 245.547 1.00 54.42  ?  580 LEU A CG    1 
ATOM   4458  C  CD1   . LEU A 1 561 ? 180.233 157.773 245.287 1.00 55.44  ?  580 LEU A CD1   1 
ATOM   4459  C  CD2   . LEU A 1 561 ? 178.254 159.116 244.673 1.00 53.84  ?  580 LEU A CD2   1 
ATOM   4460  N  N     . TYR A 1 562 ? 178.441 162.644 246.699 1.00 58.62  ?  581 TYR A N     1 
ATOM   4461  C  CA    . TYR A 1 562 ? 177.526 163.532 245.992 1.00 60.19  ?  581 TYR A CA    1 
ATOM   4462  C  C     . TYR A 1 562 ? 177.230 163.008 244.593 1.00 60.12  ?  581 TYR A C     1 
ATOM   4463  O  O     . TYR A 1 562 ? 176.085 163.056 244.129 1.00 63.01  ?  581 TYR A O     1 
ATOM   4464  C  CB    . TYR A 1 562 ? 178.113 164.941 245.927 1.00 57.84  ?  581 TYR A CB    1 
ATOM   4465  C  CG    . TYR A 1 562 ? 177.334 165.901 245.056 1.00 61.07  ?  581 TYR A CG    1 
ATOM   4466  C  CD1   . TYR A 1 562 ? 176.041 166.281 245.389 1.00 63.03  ?  581 TYR A CD1   1 
ATOM   4467  C  CD2   . TYR A 1 562 ? 177.896 166.431 243.902 1.00 58.65  ?  581 TYR A CD2   1 
ATOM   4468  C  CE1   . TYR A 1 562 ? 175.329 167.159 244.595 1.00 61.54  ?  581 TYR A CE1   1 
ATOM   4469  C  CE2   . TYR A 1 562 ? 177.191 167.310 243.103 1.00 58.72  ?  581 TYR A CE2   1 
ATOM   4470  C  CZ    . TYR A 1 562 ? 175.909 167.671 243.453 1.00 62.12  ?  581 TYR A CZ    1 
ATOM   4471  O  OH    . TYR A 1 562 ? 175.204 168.546 242.659 1.00 63.32  ?  581 TYR A OH    1 
ATOM   4472  N  N     . GLY A 1 563 ? 178.248 162.499 243.910 1.00 47.44  ?  582 GLY A N     1 
ATOM   4473  C  CA    . GLY A 1 563 ? 178.060 161.971 242.573 1.00 49.74  ?  582 GLY A CA    1 
ATOM   4474  C  C     . GLY A 1 563 ? 179.324 161.300 242.087 1.00 53.09  ?  582 GLY A C     1 
ATOM   4475  O  O     . GLY A 1 563 ? 180.347 161.271 242.776 1.00 51.85  ?  582 GLY A O     1 
ATOM   4476  N  N     . ILE A 1 564 ? 179.230 160.742 240.884 1.00 46.76  ?  583 ILE A N     1 
ATOM   4477  C  CA    . ILE A 1 564 ? 180.366 160.140 240.196 1.00 32.44  ?  583 ILE A CA    1 
ATOM   4478  C  C     . ILE A 1 564 ? 180.400 160.678 238.773 1.00 38.11  ?  583 ILE A C     1 
ATOM   4479  O  O     . ILE A 1 564 ? 179.356 160.815 238.128 1.00 46.32  ?  583 ILE A O     1 
ATOM   4480  C  CB    . ILE A 1 564 ? 180.300 158.598 240.195 1.00 28.10  ?  583 ILE A CB    1 
ATOM   4481  C  CG1   . ILE A 1 564 ? 178.900 158.111 239.845 1.00 32.69  ?  583 ILE A CG1   1 
ATOM   4482  C  CG2   . ILE A 1 564 ? 180.703 158.037 241.545 1.00 41.08  ?  583 ILE A CG2   1 
ATOM   4483  C  CD1   . ILE A 1 564 ? 178.826 156.617 239.657 1.00 40.71  ?  583 ILE A CD1   1 
ATOM   4484  N  N     . GLU A 1 565 ? 181.596 161.003 238.291 1.00 39.67  ?  584 GLU A N     1 
ATOM   4485  C  CA    . GLU A 1 565 ? 181.775 161.555 236.956 1.00 32.68  ?  584 GLU A CA    1 
ATOM   4486  C  C     . GLU A 1 565 ? 182.214 160.458 235.997 1.00 33.46  ?  584 GLU A C     1 
ATOM   4487  O  O     . GLU A 1 565 ? 183.145 159.702 236.294 1.00 41.86  ?  584 GLU A O     1 
ATOM   4488  C  CB    . GLU A 1 565 ? 182.799 162.690 236.960 1.00 38.20  ?  584 GLU A CB    1 
ATOM   4489  C  CG    . GLU A 1 565 ? 182.902 163.421 235.629 1.00 50.46  ?  584 GLU A CG    1 
ATOM   4490  C  CD    . GLU A 1 565 ? 183.390 164.848 235.776 1.00 55.28  ?  584 GLU A CD    1 
ATOM   4491  O  OE1   . GLU A 1 565 ? 183.079 165.476 236.809 1.00 54.18  ?  584 GLU A OE1   1 
ATOM   4492  O  OE2   . GLU A 1 565 ? 184.078 165.342 234.858 1.00 49.23  -1 584 GLU A OE2   1 
ATOM   4493  N  N     . ALA A 1 566 ? 181.546 160.378 234.849 1.00 29.29  ?  585 ALA A N     1 
ATOM   4494  C  CA    . ALA A 1 566 ? 181.853 159.379 233.832 1.00 30.87  ?  585 ALA A CA    1 
ATOM   4495  C  C     . ALA A 1 566 ? 182.908 159.943 232.887 1.00 43.71  ?  585 ALA A C     1 
ATOM   4496  O  O     . ALA A 1 566 ? 182.610 160.801 232.050 1.00 41.89  ?  585 ALA A O     1 
ATOM   4497  C  CB    . ALA A 1 566 ? 180.592 158.977 233.072 1.00 37.38  ?  585 ALA A CB    1 
ATOM   4498  N  N     . LEU A 1 567 ? 184.140 159.458 233.021 1.00 45.56  ?  586 LEU A N     1 
ATOM   4499  C  CA    . LEU A 1 567 ? 185.249 159.865 232.168 1.00 29.35  ?  586 LEU A CA    1 
ATOM   4500  C  C     . LEU A 1 567 ? 185.523 158.769 231.147 1.00 25.16  ?  586 LEU A C     1 
ATOM   4501  O  O     . LEU A 1 567 ? 185.632 157.592 231.506 1.00 39.83  ?  586 LEU A O     1 
ATOM   4502  C  CB    . LEU A 1 567 ? 186.502 160.146 233.000 1.00 23.66  ?  586 LEU A CB    1 
ATOM   4503  C  CG    . LEU A 1 567 ? 186.329 161.087 234.194 1.00 22.61  ?  586 LEU A CG    1 
ATOM   4504  C  CD1   . LEU A 1 567 ? 187.600 161.147 235.026 1.00 31.18  ?  586 LEU A CD1   1 
ATOM   4505  C  CD2   . LEU A 1 567 ? 185.933 162.478 233.724 1.00 39.78  ?  586 LEU A CD2   1 
ATOM   4506  N  N     . ALA A 1 568 ? 185.633 159.159 229.881 1.00 23.90  ?  587 ALA A N     1 
ATOM   4507  C  CA    . ALA A 1 568 ? 185.811 158.188 228.812 1.00 27.80  ?  587 ALA A CA    1 
ATOM   4508  C  C     . ALA A 1 568 ? 187.203 157.568 228.857 1.00 44.76  ?  587 ALA A C     1 
ATOM   4509  O  O     . ALA A 1 568 ? 188.161 158.166 229.352 1.00 48.04  ?  587 ALA A O     1 
ATOM   4510  C  CB    . ALA A 1 568 ? 185.573 158.843 227.452 1.00 30.28  ?  587 ALA A CB    1 
ATOM   4511  N  N     . ARG A 1 569 ? 187.302 156.347 228.333 1.00 41.67  ?  588 ARG A N     1 
ATOM   4512  C  CA    . ARG A 1 569 ? 188.573 155.652 228.188 1.00 24.00  ?  588 ARG A CA    1 
ATOM   4513  C  C     . ARG A 1 569 ? 188.541 154.830 226.908 1.00 28.42  ?  588 ARG A C     1 
ATOM   4514  O  O     . ARG A 1 569 ? 187.475 154.491 226.388 1.00 41.53  ?  588 ARG A O     1 
ATOM   4515  C  CB    . ARG A 1 569 ? 188.879 154.745 229.386 1.00 16.52  ?  588 ARG A CB    1 
ATOM   4516  C  CG    . ARG A 1 569 ? 189.212 155.461 230.683 1.00 22.88  ?  588 ARG A CG    1 
ATOM   4517  C  CD    . ARG A 1 569 ? 190.506 156.248 230.580 1.00 24.35  ?  588 ARG A CD    1 
ATOM   4518  N  NE    . ARG A 1 569 ? 190.920 156.788 231.870 1.00 28.00  ?  588 ARG A NE    1 
ATOM   4519  C  CZ    . ARG A 1 569 ? 190.541 157.963 232.354 1.00 29.04  ?  588 ARG A CZ    1 
ATOM   4520  N  NH1   . ARG A 1 569 ? 189.724 158.756 231.681 1.00 28.54  1  588 ARG A NH1   1 
ATOM   4521  N  NH2   . ARG A 1 569 ? 190.998 158.355 233.539 1.00 34.83  ?  588 ARG A NH2   1 
ATOM   4522  N  N     . TRP A 1 570 ? 189.731 154.505 226.410 1.00 33.79  ?  589 TRP A N     1 
ATOM   4523  C  CA    . TRP A 1 570 ? 189.873 153.715 225.196 1.00 31.77  ?  589 TRP A CA    1 
ATOM   4524  C  C     . TRP A 1 570 ? 191.094 152.819 225.335 1.00 38.12  ?  589 TRP A C     1 
ATOM   4525  O  O     . TRP A 1 570 ? 192.084 153.201 225.964 1.00 38.30  ?  589 TRP A O     1 
ATOM   4526  C  CB    . TRP A 1 570 ? 190.013 154.609 223.960 1.00 24.35  ?  589 TRP A CB    1 
ATOM   4527  C  CG    . TRP A 1 570 ? 189.975 153.864 222.663 1.00 25.02  ?  589 TRP A CG    1 
ATOM   4528  C  CD1   . TRP A 1 570 ? 189.394 152.653 222.427 1.00 33.03  ?  589 TRP A CD1   1 
ATOM   4529  C  CD2   . TRP A 1 570 ? 190.560 154.276 221.424 1.00 27.57  ?  589 TRP A CD2   1 
ATOM   4530  N  NE1   . TRP A 1 570 ? 189.575 152.289 221.115 1.00 31.85  ?  589 TRP A NE1   1 
ATOM   4531  C  CE2   . TRP A 1 570 ? 190.288 153.269 220.478 1.00 30.19  ?  589 TRP A CE2   1 
ATOM   4532  C  CE3   . TRP A 1 570 ? 191.284 155.401 221.021 1.00 37.32  ?  589 TRP A CE3   1 
ATOM   4533  C  CZ2   . TRP A 1 570 ? 190.715 153.354 219.155 1.00 40.95  ?  589 TRP A CZ2   1 
ATOM   4534  C  CZ3   . TRP A 1 570 ? 191.708 155.483 219.709 1.00 35.59  ?  589 TRP A CZ3   1 
ATOM   4535  C  CH2   . TRP A 1 570 ? 191.423 154.465 218.791 1.00 37.22  ?  589 TRP A CH2   1 
ATOM   4536  N  N     . HIS A 1 571 ? 191.016 151.629 224.743 1.00 39.38  ?  590 HIS A N     1 
ATOM   4537  C  CA    . HIS A 1 571 ? 192.125 150.675 224.761 1.00 37.16  ?  590 HIS A CA    1 
ATOM   4538  C  C     . HIS A 1 571 ? 192.109 149.915 223.439 1.00 37.44  ?  590 HIS A C     1 
ATOM   4539  O  O     . HIS A 1 571 ? 191.307 148.995 223.253 1.00 41.92  ?  590 HIS A O     1 
ATOM   4540  C  CB    . HIS A 1 571 ? 192.022 149.724 225.946 1.00 38.71  ?  590 HIS A CB    1 
ATOM   4541  C  CG    . HIS A 1 571 ? 192.974 148.572 225.877 1.00 40.41  ?  590 HIS A CG    1 
ATOM   4542  N  ND1   . HIS A 1 571 ? 194.271 148.653 226.334 1.00 38.45  ?  590 HIS A ND1   1 
ATOM   4543  C  CD2   . HIS A 1 571 ? 192.820 147.314 225.401 1.00 41.00  ?  590 HIS A CD2   1 
ATOM   4544  C  CE1   . HIS A 1 571 ? 194.875 147.493 226.145 1.00 40.91  ?  590 HIS A CE1   1 
ATOM   4545  N  NE2   . HIS A 1 571 ? 194.017 146.664 225.580 1.00 41.61  ?  590 HIS A NE2   1 
ATOM   4546  N  N     . ASP A 1 572 ? 192.993 150.306 222.525 1.00 38.91  ?  591 ASP A N     1 
ATOM   4547  C  CA    . ASP A 1 572 ? 193.139 149.656 221.232 1.00 39.77  ?  591 ASP A CA    1 
ATOM   4548  C  C     . ASP A 1 572 ? 194.298 148.667 221.261 1.00 42.80  ?  591 ASP A C     1 
ATOM   4549  O  O     . ASP A 1 572 ? 195.332 148.940 221.882 1.00 47.86  ?  591 ASP A O     1 
ATOM   4550  C  CB    . ASP A 1 572 ? 193.381 150.691 220.133 1.00 40.05  ?  591 ASP A CB    1 
ATOM   4551  C  CG    . ASP A 1 572 ? 193.072 150.156 218.749 1.00 47.05  ?  591 ASP A CG    1 
ATOM   4552  O  OD1   . ASP A 1 572 ? 191.889 150.185 218.350 1.00 48.37  ?  591 ASP A OD1   1 
ATOM   4553  O  OD2   . ASP A 1 572 ? 194.012 149.707 218.061 1.00 50.21  -1 591 ASP A OD2   1 
ATOM   4554  N  N     . PRO A 1 573 ? 194.143 147.509 220.611 1.00 42.17  ?  592 PRO A N     1 
ATOM   4555  C  CA    . PRO A 1 573 ? 195.248 146.535 220.589 1.00 41.35  ?  592 PRO A CA    1 
ATOM   4556  C  C     . PRO A 1 573 ? 196.524 147.079 219.970 1.00 42.17  ?  592 PRO A C     1 
ATOM   4557  O  O     . PRO A 1 573 ? 197.624 146.714 220.405 1.00 49.74  ?  592 PRO A O     1 
ATOM   4558  C  CB    . PRO A 1 573 ? 194.668 145.375 219.768 1.00 46.35  ?  592 PRO A CB    1 
ATOM   4559  C  CG    . PRO A 1 573 ? 193.189 145.496 219.945 1.00 47.82  ?  592 PRO A CG    1 
ATOM   4560  C  CD    . PRO A 1 573 ? 192.915 146.969 220.004 1.00 45.60  ?  592 PRO A CD    1 
ATOM   4561  N  N     . LEU A 1 574 ? 196.410 147.943 218.960 1.00 41.24  ?  593 LEU A N     1 
ATOM   4562  C  CA    . LEU A 1 574 ? 197.596 148.473 218.296 1.00 42.47  ?  593 LEU A CA    1 
ATOM   4563  C  C     . LEU A 1 574 ? 198.159 149.682 219.035 1.00 40.62  ?  593 LEU A C     1 
ATOM   4564  O  O     . LEU A 1 574 ? 199.360 149.739 219.322 1.00 38.17  ?  593 LEU A O     1 
ATOM   4565  C  CB    . LEU A 1 574 ? 197.272 148.840 216.845 1.00 45.14  ?  593 LEU A CB    1 
ATOM   4566  C  CG    . LEU A 1 574 ? 197.168 147.706 215.820 1.00 47.38  ?  593 LEU A CG    1 
ATOM   4567  C  CD1   . LEU A 1 574 ? 195.848 146.957 215.942 1.00 44.70  ?  593 LEU A CD1   1 
ATOM   4568  C  CD2   . LEU A 1 574 ? 197.354 148.245 214.409 1.00 43.40  ?  593 LEU A CD2   1 
ATOM   4569  N  N     . HIS A 1 575 ? 197.307 150.653 219.354 1.00 46.36  ?  594 HIS A N     1 
ATOM   4570  C  CA    . HIS A 1 575 ? 197.741 151.917 219.935 1.00 46.22  ?  594 HIS A CA    1 
ATOM   4571  C  C     . HIS A 1 575 ? 197.839 151.883 221.454 1.00 44.84  ?  594 HIS A C     1 
ATOM   4572  O  O     . HIS A 1 575 ? 198.210 152.895 222.057 1.00 43.99  ?  594 HIS A O     1 
ATOM   4573  C  CB    . HIS A 1 575 ? 196.790 153.040 219.510 1.00 40.64  ?  594 HIS A CB    1 
ATOM   4574  C  CG    . HIS A 1 575 ? 196.615 153.156 218.028 1.00 41.19  ?  594 HIS A CG    1 
ATOM   4575  N  ND1   . HIS A 1 575 ? 195.794 152.313 217.310 1.00 43.36  ?  594 HIS A ND1   1 
ATOM   4576  C  CD2   . HIS A 1 575 ? 197.151 154.015 217.130 1.00 43.57  ?  594 HIS A CD2   1 
ATOM   4577  C  CE1   . HIS A 1 575 ? 195.834 152.646 216.032 1.00 45.09  ?  594 HIS A CE1   1 
ATOM   4578  N  NE2   . HIS A 1 575 ? 196.650 153.676 215.896 1.00 45.85  ?  594 HIS A NE2   1 
ATOM   4579  N  N     . GLY A 1 576 ? 197.523 150.755 222.087 1.00 44.48  ?  595 GLY A N     1 
ATOM   4580  C  CA    . GLY A 1 576 ? 197.571 150.703 223.540 1.00 41.45  ?  595 GLY A CA    1 
ATOM   4581  C  C     . GLY A 1 576 ? 196.439 151.501 224.159 1.00 38.35  ?  595 GLY A C     1 
ATOM   4582  O  O     . GLY A 1 576 ? 195.282 151.422 223.732 1.00 42.57  ?  595 GLY A O     1 
ATOM   4583  N  N     . HIS A 1 577 ? 196.772 152.281 225.184 1.00 31.46  ?  596 HIS A N     1 
ATOM   4584  C  CA    . HIS A 1 577 ? 195.806 153.122 225.879 1.00 30.04  ?  596 HIS A CA    1 
ATOM   4585  C  C     . HIS A 1 577 ? 195.936 154.549 225.366 1.00 36.30  ?  596 HIS A C     1 
ATOM   4586  O  O     . HIS A 1 577 ? 196.992 155.173 225.519 1.00 42.21  ?  596 HIS A O     1 
ATOM   4587  C  CB    . HIS A 1 577 ? 196.025 153.073 227.390 1.00 30.70  ?  596 HIS A CB    1 
ATOM   4588  C  CG    . HIS A 1 577 ? 195.841 151.712 227.985 1.00 34.95  ?  596 HIS A CG    1 
ATOM   4589  N  ND1   . HIS A 1 577 ? 196.826 150.749 227.955 1.00 38.61  ?  596 HIS A ND1   1 
ATOM   4590  C  CD2   . HIS A 1 577 ? 194.788 151.153 228.627 1.00 38.56  ?  596 HIS A CD2   1 
ATOM   4591  C  CE1   . HIS A 1 577 ? 196.388 149.655 228.551 1.00 39.08  ?  596 HIS A CE1   1 
ATOM   4592  N  NE2   . HIS A 1 577 ? 195.154 149.874 228.969 1.00 41.60  ?  596 HIS A NE2   1 
ATOM   4593  N  N     . VAL A 1 578 ? 194.870 155.060 224.763 1.00 31.63  ?  597 VAL A N     1 
ATOM   4594  C  CA    . VAL A 1 578 ? 194.843 156.410 224.208 1.00 23.38  ?  597 VAL A CA    1 
ATOM   4595  C  C     . VAL A 1 578 ? 194.148 157.319 225.216 1.00 30.82  ?  597 VAL A C     1 
ATOM   4596  O  O     . VAL A 1 578 ? 192.953 157.121 225.487 1.00 38.98  ?  597 VAL A O     1 
ATOM   4597  C  CB    . VAL A 1 578 ? 194.132 156.449 222.848 1.00 18.52  ?  597 VAL A CB    1 
ATOM   4598  C  CG1   . VAL A 1 578 ? 194.025 157.879 222.352 1.00 30.95  ?  597 VAL A CG1   1 
ATOM   4599  C  CG2   . VAL A 1 578 ? 194.866 155.581 221.839 1.00 21.99  ?  597 VAL A CG2   1 
ATOM   4600  N  N     . PRO A 1 579 ? 194.840 158.305 225.789 1.00 28.99  ?  598 PRO A N     1 
ATOM   4601  C  CA    . PRO A 1 579 ? 194.227 159.111 226.842 1.00 31.69  ?  598 PRO A CA    1 
ATOM   4602  C  C     . PRO A 1 579 ? 193.084 159.949 226.303 1.00 37.89  ?  598 PRO A C     1 
ATOM   4603  O  O     . PRO A 1 579 ? 193.072 160.325 225.116 1.00 47.19  ?  598 PRO A O     1 
ATOM   4604  C  CB    . PRO A 1 579 ? 195.388 159.998 227.329 1.00 37.54  ?  598 PRO A CB    1 
ATOM   4605  C  CG    . PRO A 1 579 ? 196.617 159.259 226.936 1.00 35.99  ?  598 PRO A CG    1 
ATOM   4606  C  CD    . PRO A 1 579 ? 196.276 158.591 225.639 1.00 34.64  ?  598 PRO A CD    1 
ATOM   4607  N  N     . PRO A 1 580 ? 192.089 160.264 227.139 1.00 25.31  ?  599 PRO A N     1 
ATOM   4608  C  CA    . PRO A 1 580 ? 191.058 161.222 226.711 1.00 25.35  ?  599 PRO A CA    1 
ATOM   4609  C  C     . PRO A 1 580 ? 191.636 162.569 226.334 1.00 41.84  ?  599 PRO A C     1 
ATOM   4610  O  O     . PRO A 1 580 ? 191.210 163.163 225.338 1.00 47.39  ?  599 PRO A O     1 
ATOM   4611  C  CB    . PRO A 1 580 ? 190.133 161.319 227.934 1.00 33.60  ?  599 PRO A CB    1 
ATOM   4612  C  CG    . PRO A 1 580 ? 190.472 160.144 228.786 1.00 43.86  ?  599 PRO A CG    1 
ATOM   4613  C  CD    . PRO A 1 580 ? 191.904 159.829 228.532 1.00 38.61  ?  599 PRO A CD    1 
ATOM   4614  N  N     . SER A 1 581 ? 192.644 163.040 227.069 1.00 44.79  ?  600 SER A N     1 
ATOM   4615  C  CA    . SER A 1 581 ? 193.302 164.300 226.747 1.00 38.08  ?  600 SER A CA    1 
ATOM   4616  C  C     . SER A 1 581 ? 194.035 164.255 225.417 1.00 36.09  ?  600 SER A C     1 
ATOM   4617  O  O     . SER A 1 581 ? 194.628 165.265 225.018 1.00 46.98  ?  600 SER A O     1 
ATOM   4618  C  CB    . SER A 1 581 ? 194.277 164.681 227.863 1.00 42.81  ?  600 SER A CB    1 
ATOM   4619  O  OG    . SER A 1 581 ? 194.875 165.940 227.611 1.00 48.84  ?  600 SER A OG    1 
ATOM   4620  N  N     . ARG A 1 582 ? 194.010 163.120 224.728 1.00 32.98  ?  601 ARG A N     1 
ATOM   4621  C  CA    . ARG A 1 582 ? 194.599 162.978 223.406 1.00 38.34  ?  601 ARG A CA    1 
ATOM   4622  C  C     . ARG A 1 582 ? 193.573 162.659 222.332 1.00 40.90  ?  601 ARG A C     1 
ATOM   4623  O  O     . ARG A 1 582 ? 193.704 163.144 221.205 1.00 47.25  ?  601 ARG A O     1 
ATOM   4624  C  CB    . ARG A 1 582 ? 195.682 161.887 223.426 1.00 39.96  ?  601 ARG A CB    1 
ATOM   4625  C  CG    . ARG A 1 582 ? 196.361 161.646 222.085 1.00 42.12  ?  601 ARG A CG    1 
ATOM   4626  C  CD    . ARG A 1 582 ? 197.506 160.653 222.223 1.00 45.52  ?  601 ARG A CD    1 
ATOM   4627  N  NE    . ARG A 1 582 ? 197.762 159.930 220.984 1.00 44.44  ?  601 ARG A NE    1 
ATOM   4628  C  CZ    . ARG A 1 582 ? 198.521 160.383 219.995 1.00 48.22  ?  601 ARG A CZ    1 
ATOM   4629  N  NH1   . ARG A 1 582 ? 199.117 161.562 220.065 1.00 45.17  1  601 ARG A NH1   1 
ATOM   4630  N  NH2   . ARG A 1 582 ? 198.689 159.633 218.910 1.00 47.61  ?  601 ARG A NH2   1 
ATOM   4631  N  N     . PHE A 1 583 ? 192.540 161.871 222.643 1.00 42.29  ?  602 PHE A N     1 
ATOM   4632  C  CA    . PHE A 1 583 ? 191.557 161.510 221.626 1.00 48.36  ?  602 PHE A CA    1 
ATOM   4633  C  C     . PHE A 1 583 ? 190.268 162.324 221.696 1.00 50.08  ?  602 PHE A C     1 
ATOM   4634  O  O     . PHE A 1 583 ? 189.405 162.153 220.830 1.00 46.91  ?  602 PHE A O     1 
ATOM   4635  C  CB    . PHE A 1 583 ? 191.253 159.999 221.677 1.00 42.07  ?  602 PHE A CB    1 
ATOM   4636  C  CG    . PHE A 1 583 ? 190.178 159.595 222.658 1.00 36.33  ?  602 PHE A CG    1 
ATOM   4637  C  CD1   . PHE A 1 583 ? 188.839 159.589 222.291 1.00 38.82  ?  602 PHE A CD1   1 
ATOM   4638  C  CD2   . PHE A 1 583 ? 190.514 159.163 223.927 1.00 43.37  ?  602 PHE A CD2   1 
ATOM   4639  C  CE1   . PHE A 1 583 ? 187.861 159.203 223.186 1.00 44.72  ?  602 PHE A CE1   1 
ATOM   4640  C  CE2   . PHE A 1 583 ? 189.539 158.771 224.823 1.00 44.09  ?  602 PHE A CE2   1 
ATOM   4641  C  CZ    . PHE A 1 583 ? 188.213 158.792 224.452 1.00 42.35  ?  602 PHE A CZ    1 
ATOM   4642  N  N     . ILE A 1 584 ? 190.119 163.222 222.667 1.00 52.97  ?  603 ILE A N     1 
ATOM   4643  C  CA    . ILE A 1 584 ? 188.961 164.114 222.693 1.00 46.72  ?  603 ILE A CA    1 
ATOM   4644  C  C     . ILE A 1 584 ? 189.189 165.280 221.733 1.00 53.01  ?  603 ILE A C     1 
ATOM   4645  O  O     . ILE A 1 584 ? 188.275 165.614 220.967 1.00 51.63  ?  603 ILE A O     1 
ATOM   4646  C  CB    . ILE A 1 584 ? 188.651 164.593 224.122 1.00 50.13  ?  603 ILE A CB    1 
ATOM   4647  C  CG1   . ILE A 1 584 ? 188.072 163.448 224.958 1.00 50.64  ?  603 ILE A CG1   1 
ATOM   4648  C  CG2   . ILE A 1 584 ? 187.688 165.769 224.098 1.00 55.29  ?  603 ILE A CG2   1 
ATOM   4649  C  CD1   . ILE A 1 584 ? 186.886 162.764 224.326 1.00 48.12  ?  603 ILE A CD1   1 
ATOM   4650  N  N     . PRO A 1 585 ? 190.357 165.943 221.731 1.00 55.93  ?  604 PRO A N     1 
ATOM   4651  C  CA    . PRO A 1 585 ? 190.616 166.907 220.646 1.00 55.65  ?  604 PRO A CA    1 
ATOM   4652  C  C     . PRO A 1 585 ? 190.600 166.266 219.269 1.00 55.83  ?  604 PRO A C     1 
ATOM   4653  O  O     . PRO A 1 585 ? 190.159 166.892 218.296 1.00 61.24  ?  604 PRO A O     1 
ATOM   4654  C  CB    . PRO A 1 585 ? 191.999 167.467 221.002 1.00 54.66  ?  604 PRO A CB    1 
ATOM   4655  C  CG    . PRO A 1 585 ? 192.093 167.302 222.468 1.00 49.11  ?  604 PRO A CG    1 
ATOM   4656  C  CD    . PRO A 1 585 ? 191.425 165.992 222.746 1.00 51.62  ?  604 PRO A CD    1 
ATOM   4657  N  N     . LEU A 1 586 ? 191.070 165.021 219.163 1.00 52.14  ?  605 LEU A N     1 
ATOM   4658  C  CA    . LEU A 1 586 ? 190.994 164.304 217.896 1.00 54.92  ?  605 LEU A CA    1 
ATOM   4659  C  C     . LEU A 1 586 ? 189.546 164.085 217.478 1.00 57.10  ?  605 LEU A C     1 
ATOM   4660  O  O     . LEU A 1 586 ? 189.197 164.243 216.302 1.00 62.54  ?  605 LEU A O     1 
ATOM   4661  C  CB    . LEU A 1 586 ? 191.732 162.970 218.010 1.00 51.59  ?  605 LEU A CB    1 
ATOM   4662  C  CG    . LEU A 1 586 ? 191.909 162.159 216.728 1.00 54.01  ?  605 LEU A CG    1 
ATOM   4663  C  CD1   . LEU A 1 586 ? 193.140 162.622 215.971 1.00 55.12  ?  605 LEU A CD1   1 
ATOM   4664  C  CD2   . LEU A 1 586 ? 192.002 160.676 217.047 1.00 54.84  ?  605 LEU A CD2   1 
ATOM   4665  N  N     . ALA A 1 587 ? 188.687 163.722 218.433 1.00 58.58  ?  606 ALA A N     1 
ATOM   4666  C  CA    . ALA A 1 587 ? 187.269 163.565 218.132 1.00 62.78  ?  606 ALA A CA    1 
ATOM   4667  C  C     . ALA A 1 587 ? 186.638 164.896 217.744 1.00 65.09  ?  606 ALA A C     1 
ATOM   4668  O  O     . ALA A 1 587 ? 185.758 164.944 216.879 1.00 65.43  ?  606 ALA A O     1 
ATOM   4669  C  CB    . ALA A 1 587 ? 186.545 162.947 219.327 1.00 65.55  ?  606 ALA A CB    1 
ATOM   4670  N  N     . GLU A 1 588 ? 187.067 165.988 218.383 1.00 66.51  ?  607 GLU A N     1 
ATOM   4671  C  CA    . GLU A 1 588 ? 186.583 167.311 217.999 1.00 64.85  ?  607 GLU A CA    1 
ATOM   4672  C  C     . GLU A 1 588 ? 186.963 167.637 216.562 1.00 66.84  ?  607 GLU A C     1 
ATOM   4673  O  O     . GLU A 1 588 ? 186.142 168.151 215.793 1.00 69.83  ?  607 GLU A O     1 
ATOM   4674  C  CB    . GLU A 1 588 ? 187.140 168.372 218.949 1.00 64.17  ?  607 GLU A CB    1 
ATOM   4675  C  CG    . GLU A 1 588 ? 186.517 168.371 220.334 1.00 66.61  ?  607 GLU A CG    1 
ATOM   4676  C  CD    . GLU A 1 588 ? 187.171 169.368 221.269 1.00 68.42  ?  607 GLU A CD    1 
ATOM   4677  O  OE1   . GLU A 1 588 ? 187.681 170.399 220.783 1.00 65.88  ?  607 GLU A OE1   1 
ATOM   4678  O  OE2   . GLU A 1 588 ? 187.175 169.119 222.493 1.00 71.31  -1 607 GLU A OE2   1 
ATOM   4679  N  N     . GLU A 1 589 ? 188.210 167.349 216.185 1.00 65.32  ?  608 GLU A N     1 
ATOM   4680  C  CA    . GLU A 1 589 ? 188.661 167.631 214.827 1.00 65.93  ?  608 GLU A CA    1 
ATOM   4681  C  C     . GLU A 1 589 ? 187.921 166.777 213.803 1.00 71.16  ?  608 GLU A C     1 
ATOM   4682  O  O     . GLU A 1 589 ? 187.513 167.279 212.748 1.00 74.41  ?  608 GLU A O     1 
ATOM   4683  C  CB    . GLU A 1 589 ? 190.170 167.412 214.723 1.00 64.91  ?  608 GLU A CB    1 
ATOM   4684  C  CG    . GLU A 1 589 ? 190.759 167.757 213.366 1.00 68.35  ?  608 GLU A CG    1 
ATOM   4685  C  CD    . GLU A 1 589 ? 192.275 167.733 213.368 1.00 72.48  ?  608 GLU A CD    1 
ATOM   4686  O  OE1   . GLU A 1 589 ? 192.862 167.360 214.406 1.00 70.68  ?  608 GLU A OE1   1 
ATOM   4687  O  OE2   . GLU A 1 589 ? 192.879 168.089 212.335 1.00 74.55  -1 608 GLU A OE2   1 
ATOM   4688  N  N     . ILE A 1 590 ? 187.741 165.486 214.090 1.00 66.67  ?  609 ILE A N     1 
ATOM   4689  C  CA    . ILE A 1 590 ? 187.108 164.592 213.124 1.00 62.67  ?  609 ILE A CA    1 
ATOM   4690  C  C     . ILE A 1 590 ? 185.619 164.893 213.001 1.00 63.54  ?  609 ILE A C     1 
ATOM   4691  O  O     . ILE A 1 590 ? 185.075 164.980 211.894 1.00 64.80  ?  609 ILE A O     1 
ATOM   4692  C  CB    . ILE A 1 590 ? 187.351 163.124 213.513 1.00 63.69  ?  609 ILE A CB    1 
ATOM   4693  C  CG1   . ILE A 1 590 ? 188.846 162.814 213.514 1.00 63.54  ?  609 ILE A CG1   1 
ATOM   4694  C  CG2   . ILE A 1 590 ? 186.620 162.191 212.560 1.00 63.55  ?  609 ILE A CG2   1 
ATOM   4695  C  CD1   . ILE A 1 590 ? 189.194 161.581 214.297 1.00 63.98  ?  609 ILE A CD1   1 
ATOM   4696  N  N     . GLY A 1 591 ? 184.939 165.060 214.132 1.00 69.64  ?  610 GLY A N     1 
ATOM   4697  C  CA    . GLY A 1 591 ? 183.498 165.197 214.146 1.00 70.45  ?  610 GLY A CA    1 
ATOM   4698  C  C     . GLY A 1 591 ? 182.828 164.042 214.863 1.00 69.78  ?  610 GLY A C     1 
ATOM   4699  O  O     . GLY A 1 591 ? 181.689 163.683 214.550 1.00 70.12  ?  610 GLY A O     1 
ATOM   4700  N  N     . GLU A 1 592 ? 183.528 163.454 215.832 1.00 71.31  ?  611 GLU A N     1 
ATOM   4701  C  CA    . GLU A 1 592 ? 183.031 162.306 216.579 1.00 70.49  ?  611 GLU A CA    1 
ATOM   4702  C  C     . GLU A 1 592 ? 182.518 162.680 217.963 1.00 68.61  ?  611 GLU A C     1 
ATOM   4703  O  O     . GLU A 1 592 ? 182.167 161.788 218.744 1.00 72.10  ?  611 GLU A O     1 
ATOM   4704  C  CB    . GLU A 1 592 ? 184.127 161.243 216.702 1.00 72.59  ?  611 GLU A CB    1 
ATOM   4705  C  CG    . GLU A 1 592 ? 184.702 160.787 215.373 1.00 72.69  ?  611 GLU A CG    1 
ATOM   4706  C  CD    . GLU A 1 592 ? 183.628 160.396 214.378 1.00 74.03  ?  611 GLU A CD    1 
ATOM   4707  O  OE1   . GLU A 1 592 ? 182.768 159.562 214.729 1.00 72.95  ?  611 GLU A OE1   1 
ATOM   4708  O  OE2   . GLU A 1 592 ? 183.644 160.922 213.245 1.00 71.70  -1 611 GLU A OE2   1 
ATOM   4709  N  N     . ILE A 1 593 ? 182.467 163.974 218.286 1.00 64.79  ?  612 ILE A N     1 
ATOM   4710  C  CA    . ILE A 1 593 ? 181.972 164.395 219.594 1.00 64.24  ?  612 ILE A CA    1 
ATOM   4711  C  C     . ILE A 1 593 ? 180.502 164.037 219.752 1.00 67.23  ?  612 ILE A C     1 
ATOM   4712  O  O     . ILE A 1 593 ? 180.059 163.642 220.836 1.00 66.90  ?  612 ILE A O     1 
ATOM   4713  C  CB    . ILE A 1 593 ? 182.215 165.900 219.804 1.00 66.98  ?  612 ILE A CB    1 
ATOM   4714  C  CG1   . ILE A 1 593 ? 183.710 166.200 219.772 1.00 67.17  ?  612 ILE A CG1   1 
ATOM   4715  C  CG2   . ILE A 1 593 ? 181.620 166.360 221.123 1.00 68.45  ?  612 ILE A CG2   1 
ATOM   4716  C  CD1   . ILE A 1 593 ? 184.485 165.498 220.864 1.00 64.99  ?  612 ILE A CD1   1 
ATOM   4717  N  N     . GLU A 1 594 ? 179.721 164.169 218.678 1.00 75.10  ?  613 GLU A N     1 
ATOM   4718  C  CA    . GLU A 1 594 ? 178.310 163.800 218.743 1.00 76.20  ?  613 GLU A CA    1 
ATOM   4719  C  C     . GLU A 1 594 ? 178.148 162.326 219.095 1.00 72.79  ?  613 GLU A C     1 
ATOM   4720  O  O     . GLU A 1 594 ? 177.419 161.973 220.031 1.00 72.66  ?  613 GLU A O     1 
ATOM   4721  C  CB    . GLU A 1 594 ? 177.626 164.114 217.413 1.00 74.51  ?  613 GLU A CB    1 
ATOM   4722  C  CG    . GLU A 1 594 ? 177.841 165.537 216.923 1.00 73.64  ?  613 GLU A CG    1 
ATOM   4723  C  CD    . GLU A 1 594 ? 177.284 166.573 217.876 1.00 76.83  ?  613 GLU A CD    1 
ATOM   4724  O  OE1   . GLU A 1 594 ? 176.125 166.418 218.317 1.00 75.31  ?  613 GLU A OE1   1 
ATOM   4725  O  OE2   . GLU A 1 594 ? 178.005 167.543 218.187 1.00 75.99  -1 613 GLU A OE2   1 
ATOM   4726  N  N     . ASN A 1 595 ? 178.840 161.451 218.360 1.00 62.36  ?  614 ASN A N     1 
ATOM   4727  C  CA    . ASN A 1 595 ? 178.741 160.019 218.615 1.00 63.80  ?  614 ASN A CA    1 
ATOM   4728  C  C     . ASN A 1 595 ? 179.238 159.677 220.012 1.00 66.57  ?  614 ASN A C     1 
ATOM   4729  O  O     . ASN A 1 595 ? 178.653 158.829 220.697 1.00 69.82  ?  614 ASN A O     1 
ATOM   4730  C  CB    . ASN A 1 595 ? 179.527 159.242 217.559 1.00 68.82  ?  614 ASN A CB    1 
ATOM   4731  C  CG    . ASN A 1 595 ? 179.022 159.496 216.153 1.00 70.76  ?  614 ASN A CG    1 
ATOM   4732  O  OD1   . ASN A 1 595 ? 179.741 160.034 215.311 1.00 72.32  ?  614 ASN A OD1   1 
ATOM   4733  N  ND2   . ASN A 1 595 ? 177.778 159.112 215.892 1.00 67.77  ?  614 ASN A ND2   1 
ATOM   4734  N  N     . ILE A 1 596 ? 180.314 160.334 220.454 1.00 64.29  ?  615 ILE A N     1 
ATOM   4735  C  CA    . ILE A 1 596 ? 180.817 160.111 221.805 1.00 62.92  ?  615 ILE A CA    1 
ATOM   4736  C  C     . ILE A 1 596 ? 179.762 160.497 222.832 1.00 63.95  ?  615 ILE A C     1 
ATOM   4737  O  O     . ILE A 1 596 ? 179.555 159.789 223.822 1.00 68.47  ?  615 ILE A O     1 
ATOM   4738  C  CB    . ILE A 1 596 ? 182.134 160.881 222.022 1.00 61.65  ?  615 ILE A CB    1 
ATOM   4739  C  CG1   . ILE A 1 596 ? 183.308 160.098 221.433 1.00 64.96  ?  615 ILE A CG1   1 
ATOM   4740  C  CG2   . ILE A 1 596 ? 182.373 161.144 223.502 1.00 63.41  ?  615 ILE A CG2   1 
ATOM   4741  C  CD1   . ILE A 1 596 ? 184.639 160.795 221.576 1.00 65.50  ?  615 ILE A CD1   1 
ATOM   4742  N  N     . GLY A 1 597 ? 179.070 161.615 222.608 1.00 61.45  ?  616 GLY A N     1 
ATOM   4743  C  CA    . GLY A 1 597 ? 178.034 162.029 223.539 1.00 63.27  ?  616 GLY A CA    1 
ATOM   4744  C  C     . GLY A 1 597 ? 176.878 161.049 223.610 1.00 61.70  ?  616 GLY A C     1 
ATOM   4745  O  O     . GLY A 1 597 ? 176.434 160.679 224.702 1.00 59.26  ?  616 GLY A O     1 
ATOM   4746  N  N     . ARG A 1 598 ? 176.378 160.607 222.448 1.00 65.44  ?  617 ARG A N     1 
ATOM   4747  C  CA    . ARG A 1 598 ? 175.302 159.617 222.461 1.00 62.67  ?  617 ARG A CA    1 
ATOM   4748  C  C     . ARG A 1 598 ? 175.746 158.344 223.173 1.00 60.83  ?  617 ARG A C     1 
ATOM   4749  O  O     . ARG A 1 598 ? 175.011 157.794 224.005 1.00 63.57  ?  617 ARG A O     1 
ATOM   4750  C  CB    . ARG A 1 598 ? 174.817 159.273 221.045 1.00 66.36  ?  617 ARG A CB    1 
ATOM   4751  C  CG    . ARG A 1 598 ? 173.889 160.276 220.343 1.00 66.75  ?  617 ARG A CG    1 
ATOM   4752  C  CD    . ARG A 1 598 ? 174.644 161.278 219.497 1.00 63.63  ?  617 ARG A CD    1 
ATOM   4753  N  NE    . ARG A 1 598 ? 173.776 162.072 218.634 1.00 65.42  ?  617 ARG A NE    1 
ATOM   4754  C  CZ    . ARG A 1 598 ? 173.329 163.286 218.923 1.00 69.47  ?  617 ARG A CZ    1 
ATOM   4755  N  NH1   . ARG A 1 598 ? 173.702 163.915 220.024 1.00 72.41  1  617 ARG A NH1   1 
ATOM   4756  N  NH2   . ARG A 1 598 ? 172.504 163.893 218.074 1.00 67.37  ?  617 ARG A NH2   1 
ATOM   4757  N  N     . TRP A 1 599 ? 176.955 157.866 222.863 1.00 50.79  ?  618 TRP A N     1 
ATOM   4758  C  CA    . TRP A 1 599 ? 177.449 156.638 223.478 1.00 49.78  ?  618 TRP A CA    1 
ATOM   4759  C  C     . TRP A 1 599 ? 177.590 156.782 224.985 1.00 52.90  ?  618 TRP A C     1 
ATOM   4760  O  O     . TRP A 1 599 ? 177.211 155.878 225.738 1.00 58.39  ?  618 TRP A O     1 
ATOM   4761  C  CB    . TRP A 1 599 ? 178.787 156.239 222.859 1.00 45.62  ?  618 TRP A CB    1 
ATOM   4762  C  CG    . TRP A 1 599 ? 179.217 154.868 223.257 1.00 48.80  ?  618 TRP A CG    1 
ATOM   4763  C  CD1   . TRP A 1 599 ? 178.987 153.706 222.584 1.00 54.64  ?  618 TRP A CD1   1 
ATOM   4764  C  CD2   . TRP A 1 599 ? 179.949 154.512 224.436 1.00 43.61  ?  618 TRP A CD2   1 
ATOM   4765  N  NE1   . TRP A 1 599 ? 179.532 152.648 223.269 1.00 55.52  ?  618 TRP A NE1   1 
ATOM   4766  C  CE2   . TRP A 1 599 ? 180.129 153.118 224.410 1.00 46.53  ?  618 TRP A CE2   1 
ATOM   4767  C  CE3   . TRP A 1 599 ? 180.471 155.239 225.509 1.00 45.94  ?  618 TRP A CE3   1 
ATOM   4768  C  CZ2   . TRP A 1 599 ? 180.808 152.434 225.415 1.00 49.82  ?  618 TRP A CZ2   1 
ATOM   4769  C  CZ3   . TRP A 1 599 ? 181.144 154.560 226.505 1.00 48.04  ?  618 TRP A CZ3   1 
ATOM   4770  C  CH2   . TRP A 1 599 ? 181.307 153.172 226.452 1.00 50.56  ?  618 TRP A CH2   1 
ATOM   4771  N  N     . VAL A 1 600 ? 178.146 157.905 225.447 1.00 48.07  ?  619 VAL A N     1 
ATOM   4772  C  CA    . VAL A 1 600 ? 178.357 158.081 226.878 1.00 42.88  ?  619 VAL A CA    1 
ATOM   4773  C  C     . VAL A 1 600 ? 177.024 158.180 227.602 1.00 52.78  ?  619 VAL A C     1 
ATOM   4774  O  O     . VAL A 1 600 ? 176.845 157.585 228.668 1.00 56.30  ?  619 VAL A O     1 
ATOM   4775  C  CB    . VAL A 1 600 ? 179.251 159.304 227.155 1.00 41.16  ?  619 VAL A CB    1 
ATOM   4776  C  CG1   . VAL A 1 600 ? 179.338 159.567 228.649 1.00 42.22  ?  619 VAL A CG1   1 
ATOM   4777  C  CG2   . VAL A 1 600 ? 180.644 159.069 226.606 1.00 50.09  ?  619 VAL A CG2   1 
ATOM   4778  N  N     . ILE A 1 601 ? 176.058 158.905 227.030 1.00 60.57  ?  620 ILE A N     1 
ATOM   4779  C  CA    . ILE A 1 601 ? 174.748 159.011 227.671 1.00 53.19  ?  620 ILE A CA    1 
ATOM   4780  C  C     . ILE A 1 601 ? 174.087 157.639 227.762 1.00 47.41  ?  620 ILE A C     1 
ATOM   4781  O  O     . ILE A 1 601 ? 173.562 157.250 228.815 1.00 49.69  ?  620 ILE A O     1 
ATOM   4782  C  CB    . ILE A 1 601 ? 173.859 160.021 226.923 1.00 48.50  ?  620 ILE A CB    1 
ATOM   4783  C  CG1   . ILE A 1 601 ? 174.435 161.433 227.035 1.00 53.80  ?  620 ILE A CG1   1 
ATOM   4784  C  CG2   . ILE A 1 601 ? 172.446 159.997 227.472 1.00 50.82  ?  620 ILE A CG2   1 
ATOM   4785  C  CD1   . ILE A 1 601 ? 173.934 162.380 225.966 1.00 55.97  ?  620 ILE A CD1   1 
ATOM   4786  N  N     . ALA A 1 602 ? 174.120 156.877 226.664 1.00 45.98  ?  621 ALA A N     1 
ATOM   4787  C  CA    . ALA A 1 602 ? 173.467 155.572 226.651 1.00 48.54  ?  621 ALA A CA    1 
ATOM   4788  C  C     . ALA A 1 602 ? 174.127 154.611 227.635 1.00 50.04  ?  621 ALA A C     1 
ATOM   4789  O  O     . ALA A 1 602 ? 173.444 153.940 228.418 1.00 61.55  ?  621 ALA A O     1 
ATOM   4790  C  CB    . ALA A 1 602 ? 173.483 154.995 225.235 1.00 51.94  ?  621 ALA A CB    1 
ATOM   4791  N  N     . GLU A 1 603 ? 175.461 154.535 227.610 1.00 44.73  ?  622 GLU A N     1 
ATOM   4792  C  CA    . GLU A 1 603 ? 176.174 153.646 228.521 1.00 51.46  ?  622 GLU A CA    1 
ATOM   4793  C  C     . GLU A 1 603 ? 175.981 154.068 229.971 1.00 52.73  ?  622 GLU A C     1 
ATOM   4794  O  O     . GLU A 1 603 ? 175.844 153.217 230.857 1.00 59.37  ?  622 GLU A O     1 
ATOM   4795  C  CB    . GLU A 1 603 ? 177.660 153.612 228.160 1.00 56.07  ?  622 GLU A CB    1 
ATOM   4796  C  CG    . GLU A 1 603 ? 178.544 152.944 229.202 1.00 59.62  ?  622 GLU A CG    1 
ATOM   4797  C  CD    . GLU A 1 603 ? 178.490 151.431 229.137 1.00 61.10  ?  622 GLU A CD    1 
ATOM   4798  O  OE1   . GLU A 1 603 ? 177.971 150.893 228.136 1.00 60.47  ?  622 GLU A OE1   1 
ATOM   4799  O  OE2   . GLU A 1 603 ? 178.963 150.780 230.091 1.00 58.04  -1 622 GLU A OE2   1 
ATOM   4800  N  N     . ALA A 1 604 ? 175.965 155.376 230.231 1.00 44.51  ?  623 ALA A N     1 
ATOM   4801  C  CA    . ALA A 1 604 ? 175.752 155.869 231.583 1.00 50.46  ?  623 ALA A CA    1 
ATOM   4802  C  C     . ALA A 1 604 ? 174.381 155.464 232.102 1.00 54.55  ?  623 ALA A C     1 
ATOM   4803  O  O     . ALA A 1 604 ? 174.254 154.968 233.226 1.00 54.98  ?  623 ALA A O     1 
ATOM   4804  C  CB    . ALA A 1 604 ? 175.914 157.388 231.602 1.00 51.85  ?  623 ALA A CB    1 
ATOM   4805  N  N     . CYS A 1 605 ? 173.341 155.656 231.286 1.00 64.34  ?  624 CYS A N     1 
ATOM   4806  C  CA    . CYS A 1 605 ? 171.998 155.276 231.714 1.00 60.98  ?  624 CYS A CA    1 
ATOM   4807  C  C     . CYS A 1 605 ? 171.881 153.768 231.898 1.00 55.31  ?  624 CYS A C     1 
ATOM   4808  O  O     . CYS A 1 605 ? 171.227 153.302 232.838 1.00 62.61  ?  624 CYS A O     1 
ATOM   4809  C  CB    . CYS A 1 605 ? 170.964 155.789 230.716 1.00 58.57  ?  624 CYS A CB    1 
ATOM   4810  S  SG    . CYS A 1 605 ? 170.824 157.587 230.699 1.00 65.26  ?  624 CYS A SG    1 
ATOM   4811  N  N     . ARG A 1 606 ? 172.515 152.987 231.021 1.00 41.72  ?  625 ARG A N     1 
ATOM   4812  C  CA    . ARG A 1 606 ? 172.503 151.537 231.188 1.00 48.36  ?  625 ARG A CA    1 
ATOM   4813  C  C     . ARG A 1 606 ? 173.155 151.131 232.506 1.00 54.97  ?  625 ARG A C     1 
ATOM   4814  O  O     . ARG A 1 606 ? 172.592 150.341 233.275 1.00 60.57  ?  625 ARG A O     1 
ATOM   4815  C  CB    . ARG A 1 606 ? 173.209 150.871 230.006 1.00 49.34  ?  625 ARG A CB    1 
ATOM   4816  C  CG    . ARG A 1 606 ? 173.293 149.357 230.101 1.00 51.71  ?  625 ARG A CG    1 
ATOM   4817  C  CD    . ARG A 1 606 ? 174.177 148.782 229.005 1.00 53.10  ?  625 ARG A CD    1 
ATOM   4818  N  NE    . ARG A 1 606 ? 175.551 148.583 229.451 1.00 55.44  ?  625 ARG A NE    1 
ATOM   4819  C  CZ    . ARG A 1 606 ? 175.950 147.595 230.240 1.00 58.12  ?  625 ARG A CZ    1 
ATOM   4820  N  NH1   . ARG A 1 606 ? 175.104 146.680 230.685 1.00 58.12  1  625 ARG A NH1   1 
ATOM   4821  N  NH2   . ARG A 1 606 ? 177.231 147.520 230.589 1.00 57.28  ?  625 ARG A NH2   1 
ATOM   4822  N  N     . GLN A 1 607 ? 174.339 151.680 232.790 1.00 50.35  ?  626 GLN A N     1 
ATOM   4823  C  CA    . GLN A 1 607 ? 175.042 151.330 234.019 1.00 51.32  ?  626 GLN A CA    1 
ATOM   4824  C  C     . GLN A 1 607 ? 174.250 151.769 235.242 1.00 59.15  ?  626 GLN A C     1 
ATOM   4825  O  O     . GLN A 1 607 ? 174.245 151.078 236.268 1.00 67.19  ?  626 GLN A O     1 
ATOM   4826  C  CB    . GLN A 1 607 ? 176.438 151.952 234.021 1.00 56.45  ?  626 GLN A CB    1 
ATOM   4827  C  CG    . GLN A 1 607 ? 177.437 151.229 233.131 1.00 62.30  ?  626 GLN A CG    1 
ATOM   4828  C  CD    . GLN A 1 607 ? 177.647 149.782 233.535 1.00 60.56  ?  626 GLN A CD    1 
ATOM   4829  O  OE1   . GLN A 1 607 ? 177.811 148.909 232.684 1.00 57.96  ?  626 GLN A OE1   1 
ATOM   4830  N  NE2   . GLN A 1 607 ? 177.650 149.522 234.837 1.00 58.54  ?  626 GLN A NE2   1 
ATOM   4831  N  N     . LEU A 1 608 ? 173.567 152.914 235.148 1.00 58.92  ?  627 LEU A N     1 
ATOM   4832  C  CA    . LEU A 1 608 ? 172.622 153.300 236.190 1.00 57.50  ?  627 LEU A CA    1 
ATOM   4833  C  C     . LEU A 1 608 ? 171.530 152.251 236.348 1.00 55.27  ?  627 LEU A C     1 
ATOM   4834  O  O     . LEU A 1 608 ? 171.090 151.966 237.466 1.00 50.36  ?  627 LEU A O     1 
ATOM   4835  C  CB    . LEU A 1 608 ? 172.007 154.665 235.871 1.00 61.22  ?  627 LEU A CB    1 
ATOM   4836  C  CG    . LEU A 1 608 ? 172.867 155.921 236.029 1.00 59.81  ?  627 LEU A CG    1 
ATOM   4837  C  CD1   . LEU A 1 608 ? 172.542 156.935 234.949 1.00 55.85  ?  627 LEU A CD1   1 
ATOM   4838  C  CD2   . LEU A 1 608 ? 172.644 156.536 237.397 1.00 60.20  ?  627 LEU A CD2   1 
ATOM   4839  N  N     . ALA A 1 609 ? 171.079 151.666 235.236 1.00 59.61  ?  628 ALA A N     1 
ATOM   4840  C  CA    . ALA A 1 609 ? 170.052 150.631 235.309 1.00 55.88  ?  628 ALA A CA    1 
ATOM   4841  C  C     . ALA A 1 609 ? 170.547 149.410 236.081 1.00 59.13  ?  628 ALA A C     1 
ATOM   4842  O  O     . ALA A 1 609 ? 169.833 148.881 236.941 1.00 69.08  ?  628 ALA A O     1 
ATOM   4843  C  CB    . ALA A 1 609 ? 169.595 150.234 233.905 1.00 59.57  ?  628 ALA A CB    1 
ATOM   4844  N  N     . GLU A 1 610 ? 171.770 148.942 235.793 1.00 59.63  ?  629 GLU A N     1 
ATOM   4845  C  CA    . GLU A 1 610 ? 172.256 147.794 236.567 1.00 65.27  ?  629 GLU A CA    1 
ATOM   4846  C  C     . GLU A 1 610 ? 172.516 148.165 238.026 1.00 63.81  ?  629 GLU A C     1 
ATOM   4847  O  O     . GLU A 1 610 ? 172.241 147.364 238.932 1.00 66.86  ?  629 GLU A O     1 
ATOM   4848  C  CB    . GLU A 1 610 ? 173.514 147.122 235.989 1.00 62.71  ?  629 GLU A CB    1 
ATOM   4849  C  CG    . GLU A 1 610 ? 173.357 146.339 234.680 1.00 63.94  ?  629 GLU A CG    1 
ATOM   4850  C  CD    . GLU A 1 610 ? 173.542 147.164 233.441 1.00 69.32  ?  629 GLU A CD    1 
ATOM   4851  O  OE1   . GLU A 1 610 ? 173.914 148.336 233.580 1.00 71.09  ?  629 GLU A OE1   1 
ATOM   4852  O  OE2   . GLU A 1 610 ? 173.317 146.643 232.329 1.00 68.92  -1 629 GLU A OE2   1 
ATOM   4853  N  N     . TRP A 1 611 ? 173.054 149.360 238.282 1.00 50.57  ?  630 TRP A N     1 
ATOM   4854  C  CA    . TRP A 1 611 ? 173.329 149.752 239.658 1.00 47.97  ?  630 TRP A CA    1 
ATOM   4855  C  C     . TRP A 1 611 ? 172.070 150.107 240.434 1.00 59.56  ?  630 TRP A C     1 
ATOM   4856  O  O     . TRP A 1 611 ? 172.148 150.293 241.652 1.00 59.21  ?  630 TRP A O     1 
ATOM   4857  C  CB    . TRP A 1 611 ? 174.311 150.923 239.701 1.00 57.02  ?  630 TRP A CB    1 
ATOM   4858  C  CG    . TRP A 1 611 ? 175.674 150.582 239.189 1.00 60.74  ?  630 TRP A CG    1 
ATOM   4859  C  CD1   . TRP A 1 611 ? 176.368 149.429 239.413 1.00 60.30  ?  630 TRP A CD1   1 
ATOM   4860  C  CD2   . TRP A 1 611 ? 176.527 151.414 238.397 1.00 57.45  ?  630 TRP A CD2   1 
ATOM   4861  N  NE1   . TRP A 1 611 ? 177.591 149.484 238.793 1.00 62.14  ?  630 TRP A NE1   1 
ATOM   4862  C  CE2   . TRP A 1 611 ? 177.714 150.694 238.163 1.00 59.37  ?  630 TRP A CE2   1 
ATOM   4863  C  CE3   . TRP A 1 611 ? 176.398 152.695 237.854 1.00 56.26  ?  630 TRP A CE3   1 
ATOM   4864  C  CZ2   . TRP A 1 611 ? 178.763 151.213 237.414 1.00 59.65  ?  630 TRP A CZ2   1 
ATOM   4865  C  CZ3   . TRP A 1 611 ? 177.441 153.208 237.111 1.00 54.36  ?  630 TRP A CZ3   1 
ATOM   4866  C  CH2   . TRP A 1 611 ? 178.607 152.469 236.896 1.00 56.83  ?  630 TRP A CH2   1 
ATOM   4867  N  N     . ARG A 1 612 ? 170.929 150.239 239.761 1.00 72.52  ?  631 ARG A N     1 
ATOM   4868  C  CA    . ARG A 1 612 ? 169.649 150.294 240.452 1.00 70.33  ?  631 ARG A CA    1 
ATOM   4869  C  C     . ARG A 1 612 ? 169.034 148.912 240.619 1.00 61.80  ?  631 ARG A C     1 
ATOM   4870  O  O     . ARG A 1 612 ? 168.372 148.653 241.631 1.00 62.21  ?  631 ARG A O     1 
ATOM   4871  C  CB    . ARG A 1 612 ? 168.675 151.201 239.698 1.00 67.25  ?  631 ARG A CB    1 
ATOM   4872  C  CG    . ARG A 1 612 ? 167.330 151.364 240.384 1.00 65.08  ?  631 ARG A CG    1 
ATOM   4873  C  CD    . ARG A 1 612 ? 166.347 152.074 239.481 1.00 66.17  ?  631 ARG A CD    1 
ATOM   4874  N  NE    . ARG A 1 612 ? 166.300 151.452 238.164 1.00 65.76  ?  631 ARG A NE    1 
ATOM   4875  C  CZ    . ARG A 1 612 ? 165.706 151.986 237.106 1.00 67.38  ?  631 ARG A CZ    1 
ATOM   4876  N  NH1   . ARG A 1 612 ? 165.091 153.154 237.176 1.00 69.56  1  631 ARG A NH1   1 
ATOM   4877  N  NH2   . ARG A 1 612 ? 165.733 151.332 235.948 1.00 64.45  ?  631 ARG A NH2   1 
ATOM   4878  N  N     . SER A 1 613 ? 169.242 148.020 239.645 1.00 59.95  ?  632 SER A N     1 
ATOM   4879  C  CA    . SER A 1 613 ? 168.794 146.640 239.793 1.00 65.30  ?  632 SER A CA    1 
ATOM   4880  C  C     . SER A 1 613 ? 169.443 145.987 241.005 1.00 63.80  ?  632 SER A C     1 
ATOM   4881  O  O     . SER A 1 613 ? 168.774 145.294 241.780 1.00 71.27  ?  632 SER A O     1 
ATOM   4882  C  CB    . SER A 1 613 ? 169.103 145.846 238.523 1.00 66.11  ?  632 SER A CB    1 
ATOM   4883  O  OG    . SER A 1 613 ? 168.219 146.198 237.473 1.00 67.51  ?  632 SER A OG    1 
ATOM   4884  N  N     . GLN A 1 614 ? 170.744 146.191 241.181 1.00 58.60  ?  633 GLN A N     1 
ATOM   4885  C  CA    . GLN A 1 614 ? 171.387 145.813 242.430 1.00 62.49  ?  633 GLN A CA    1 
ATOM   4886  C  C     . GLN A 1 614 ? 171.378 146.998 243.394 1.00 66.08  ?  633 GLN A C     1 
ATOM   4887  O  O     . GLN A 1 614 ? 171.199 148.151 242.998 1.00 69.11  ?  633 GLN A O     1 
ATOM   4888  C  CB    . GLN A 1 614 ? 172.809 145.296 242.189 1.00 67.85  ?  633 GLN A CB    1 
ATOM   4889  C  CG    . GLN A 1 614 ? 173.754 146.243 241.475 1.00 70.92  ?  633 GLN A CG    1 
ATOM   4890  C  CD    . GLN A 1 614 ? 174.559 147.096 242.430 1.00 71.39  ?  633 GLN A CD    1 
ATOM   4891  O  OE1   . GLN A 1 614 ? 174.767 146.728 243.586 1.00 70.26  ?  633 GLN A OE1   1 
ATOM   4892  N  NE2   . GLN A 1 614 ? 175.041 148.230 241.942 1.00 68.11  ?  633 GLN A NE2   1 
ATOM   4893  N  N     . ASN A 1 615 ? 171.567 146.697 244.679 1.00 67.74  ?  634 ASN A N     1 
ATOM   4894  C  CA    . ASN A 1 615 ? 171.280 147.651 245.754 1.00 67.60  ?  634 ASN A CA    1 
ATOM   4895  C  C     . ASN A 1 615 ? 172.404 148.679 245.864 1.00 66.58  ?  634 ASN A C     1 
ATOM   4896  O  O     . ASN A 1 615 ? 173.304 148.586 246.703 1.00 67.74  ?  634 ASN A O     1 
ATOM   4897  C  CB    . ASN A 1 615 ? 171.068 146.915 247.071 1.00 71.12  ?  634 ASN A CB    1 
ATOM   4898  C  CG    . ASN A 1 615 ? 169.826 146.046 247.058 1.00 70.29  ?  634 ASN A CG    1 
ATOM   4899  O  OD1   . ASN A 1 615 ? 169.127 145.958 246.048 1.00 67.35  ?  634 ASN A OD1   1 
ATOM   4900  N  ND2   . ASN A 1 615 ? 169.546 145.397 248.182 1.00 70.79  ?  634 ASN A ND2   1 
ATOM   4901  N  N     . ILE A 1 616 ? 172.335 149.690 245.000 1.00 64.92  ?  635 ILE A N     1 
ATOM   4902  C  CA    . ILE A 1 616 ? 173.213 150.855 245.064 1.00 68.73  ?  635 ILE A CA    1 
ATOM   4903  C  C     . ILE A 1 616 ? 172.386 152.094 244.744 1.00 68.36  ?  635 ILE A C     1 
ATOM   4904  O  O     . ILE A 1 616 ? 171.561 152.083 243.825 1.00 64.65  ?  635 ILE A O     1 
ATOM   4905  C  CB    . ILE A 1 616 ? 174.421 150.720 244.110 1.00 71.47  ?  635 ILE A CB    1 
ATOM   4906  C  CG1   . ILE A 1 616 ? 175.453 149.754 244.694 1.00 71.82  ?  635 ILE A CG1   1 
ATOM   4907  C  CG2   . ILE A 1 616 ? 175.063 152.073 243.837 1.00 67.29  ?  635 ILE A CG2   1 
ATOM   4908  C  CD1   . ILE A 1 616 ? 176.069 150.232 245.990 1.00 70.19  ?  635 ILE A CD1   1 
ATOM   4909  N  N     . HIS A 1 617 ? 172.609 153.166 245.509 1.00 70.86  ?  636 HIS A N     1 
ATOM   4910  C  CA    . HIS A 1 617 ? 171.783 154.362 245.380 1.00 68.64  ?  636 HIS A CA    1 
ATOM   4911  C  C     . HIS A 1 617 ? 172.247 155.268 244.243 1.00 68.37  ?  636 HIS A C     1 
ATOM   4912  O  O     . HIS A 1 617 ? 171.412 155.862 243.552 1.00 68.69  ?  636 HIS A O     1 
ATOM   4913  C  CB    . HIS A 1 617 ? 171.766 155.128 246.704 1.00 70.04  ?  636 HIS A CB    1 
ATOM   4914  C  CG    . HIS A 1 617 ? 173.098 155.193 247.386 1.00 73.61  ?  636 HIS A CG    1 
ATOM   4915  N  ND1   . HIS A 1 617 ? 173.629 154.130 248.083 1.00 70.40  ?  636 HIS A ND1   1 
ATOM   4916  C  CD2   . HIS A 1 617 ? 173.998 156.199 247.491 1.00 71.83  ?  636 HIS A CD2   1 
ATOM   4917  C  CE1   . HIS A 1 617 ? 174.804 154.474 248.580 1.00 67.92  ?  636 HIS A CE1   1 
ATOM   4918  N  NE2   . HIS A 1 617 ? 175.051 155.724 248.235 1.00 70.98  ?  636 HIS A NE2   1 
ATOM   4919  N  N     . ILE A 1 618 ? 173.562 155.388 244.047 1.00 61.85  ?  637 ILE A N     1 
ATOM   4920  C  CA    . ILE A 1 618 ? 174.213 156.210 243.017 1.00 60.77  ?  637 ILE A CA    1 
ATOM   4921  C  C     . ILE A 1 618 ? 173.511 157.563 242.896 1.00 58.75  ?  637 ILE A C     1 
ATOM   4922  O  O     . ILE A 1 618 ? 172.742 157.795 241.951 1.00 61.36  ?  637 ILE A O     1 
ATOM   4923  C  CB    . ILE A 1 618 ? 174.340 155.464 241.668 1.00 62.89  ?  637 ILE A CB    1 
ATOM   4924  C  CG1   . ILE A 1 618 ? 175.073 156.335 240.643 1.00 58.57  ?  637 ILE A CG1   1 
ATOM   4925  C  CG2   . ILE A 1 618 ? 173.001 154.944 241.111 1.00 64.23  ?  637 ILE A CG2   1 
ATOM   4926  C  CD1   . ILE A 1 618 ? 175.429 155.611 239.375 1.00 60.37  ?  637 ILE A CD1   1 
ATOM   4927  N  N     . PRO A 1 619 ? 173.725 158.470 243.854 1.00 53.98  ?  638 PRO A N     1 
ATOM   4928  C  CA    . PRO A 1 619 ? 172.919 159.704 243.898 1.00 49.34  ?  638 PRO A CA    1 
ATOM   4929  C  C     . PRO A 1 619 ? 172.980 160.549 242.636 1.00 47.76  ?  638 PRO A C     1 
ATOM   4930  O  O     . PRO A 1 619 ? 171.957 161.124 242.243 1.00 48.26  ?  638 PRO A O     1 
ATOM   4931  C  CB    . PRO A 1 619 ? 173.506 160.455 245.102 1.00 50.99  ?  638 PRO A CB    1 
ATOM   4932  C  CG    . PRO A 1 619 ? 174.133 159.401 245.944 1.00 55.76  ?  638 PRO A CG    1 
ATOM   4933  C  CD    . PRO A 1 619 ? 174.655 158.371 244.991 1.00 55.66  ?  638 PRO A CD    1 
ATOM   4934  N  N     . ALA A 1 620 ? 174.138 160.652 241.987 1.00 48.52  ?  639 ALA A N     1 
ATOM   4935  C  CA    . ALA A 1 620 ? 174.261 161.545 240.843 1.00 49.84  ?  639 ALA A CA    1 
ATOM   4936  C  C     . ALA A 1 620 ? 175.369 161.070 239.916 1.00 49.61  ?  639 ALA A C     1 
ATOM   4937  O  O     . ALA A 1 620 ? 176.377 160.511 240.357 1.00 56.09  ?  639 ALA A O     1 
ATOM   4938  C  CB    . ALA A 1 620 ? 174.535 162.987 241.287 1.00 47.42  ?  639 ALA A CB    1 
ATOM   4939  N  N     . LEU A 1 621 ? 175.180 161.327 238.623 1.00 34.61  ?  640 LEU A N     1 
ATOM   4940  C  CA    . LEU A 1 621 ? 176.149 160.968 237.595 1.00 31.69  ?  640 LEU A CA    1 
ATOM   4941  C  C     . LEU A 1 621 ? 176.401 162.179 236.712 1.00 33.33  ?  640 LEU A C     1 
ATOM   4942  O  O     . LEU A 1 621 ? 175.459 162.757 236.160 1.00 42.65  ?  640 LEU A O     1 
ATOM   4943  C  CB    . LEU A 1 621 ? 175.656 159.779 236.766 1.00 37.07  ?  640 LEU A CB    1 
ATOM   4944  C  CG    . LEU A 1 621 ? 176.646 159.143 235.791 1.00 42.08  ?  640 LEU A CG    1 
ATOM   4945  C  CD1   . LEU A 1 621 ? 177.817 158.531 236.520 1.00 41.39  ?  640 LEU A CD1   1 
ATOM   4946  C  CD2   . LEU A 1 621 ? 175.934 158.081 235.000 1.00 41.41  ?  640 LEU A CD2   1 
ATOM   4947  N  N     . SER A 1 622 ? 177.669 162.557 236.582 1.00 35.13  ?  641 SER A N     1 
ATOM   4948  C  CA    . SER A 1 622 ? 178.081 163.726 235.815 1.00 36.11  ?  641 SER A CA    1 
ATOM   4949  C  C     . SER A 1 622 ? 178.659 163.273 234.479 1.00 32.76  ?  641 SER A C     1 
ATOM   4950  O  O     . SER A 1 622 ? 179.658 162.546 234.443 1.00 46.54  ?  641 SER A O     1 
ATOM   4951  C  CB    . SER A 1 622 ? 179.106 164.550 236.594 1.00 42.56  ?  641 SER A CB    1 
ATOM   4952  O  OG    . SER A 1 622 ? 178.674 164.777 237.925 1.00 53.23  ?  641 SER A OG    1 
ATOM   4953  N  N     . VAL A 1 623 ? 178.047 163.723 233.388 1.00 24.97  ?  642 VAL A N     1 
ATOM   4954  C  CA    . VAL A 1 623 ? 178.430 163.326 232.040 1.00 23.42  ?  642 VAL A CA    1 
ATOM   4955  C  C     . VAL A 1 623 ? 178.967 164.550 231.313 1.00 31.68  ?  642 VAL A C     1 
ATOM   4956  O  O     . VAL A 1 623 ? 178.326 165.607 231.310 1.00 45.31  ?  642 VAL A O     1 
ATOM   4957  C  CB    . VAL A 1 623 ? 177.243 162.708 231.276 1.00 32.20  ?  642 VAL A CB    1 
ATOM   4958  C  CG1   . VAL A 1 623 ? 177.595 162.507 229.815 1.00 39.12  ?  642 VAL A CG1   1 
ATOM   4959  C  CG2   . VAL A 1 623 ? 176.832 161.392 231.916 1.00 40.73  ?  642 VAL A CG2   1 
ATOM   4960  N  N     . ASN A 1 624 ? 180.140 164.407 230.704 1.00 38.03  ?  643 ASN A N     1 
ATOM   4961  C  CA    . ASN A 1 624 ? 180.783 165.519 230.018 1.00 38.07  ?  643 ASN A CA    1 
ATOM   4962  C  C     . ASN A 1 624 ? 180.178 165.713 228.634 1.00 38.20  ?  643 ASN A C     1 
ATOM   4963  O  O     . ASN A 1 624 ? 180.036 164.755 227.868 1.00 51.49  ?  643 ASN A O     1 
ATOM   4964  C  CB    . ASN A 1 624 ? 182.287 165.276 229.905 1.00 41.72  ?  643 ASN A CB    1 
ATOM   4965  C  CG    . ASN A 1 624 ? 183.014 165.511 231.213 1.00 41.78  ?  643 ASN A CG    1 
ATOM   4966  O  OD1   . ASN A 1 624 ? 183.574 166.583 231.442 1.00 38.29  ?  643 ASN A OD1   1 
ATOM   4967  N  ND2   . ASN A 1 624 ? 183.012 164.505 232.078 1.00 44.47  ?  643 ASN A ND2   1 
ATOM   4968  N  N     . LEU A 1 625 ? 179.821 166.954 228.318 1.00 42.03  ?  644 LEU A N     1 
ATOM   4969  C  CA    . LEU A 1 625 ? 179.312 167.340 227.010 1.00 48.51  ?  644 LEU A CA    1 
ATOM   4970  C  C     . LEU A 1 625 ? 180.130 168.509 226.476 1.00 51.60  ?  644 LEU A C     1 
ATOM   4971  O  O     . LEU A 1 625 ? 180.759 169.255 227.231 1.00 59.61  ?  644 LEU A O     1 
ATOM   4972  C  CB    . LEU A 1 625 ? 177.825 167.718 227.071 1.00 56.33  ?  644 LEU A CB    1 
ATOM   4973  C  CG    . LEU A 1 625 ? 176.762 166.613 227.036 1.00 60.58  ?  644 LEU A CG    1 
ATOM   4974  C  CD1   . LEU A 1 625 ? 176.846 165.824 225.734 1.00 60.04  ?  644 LEU A CD1   1 
ATOM   4975  C  CD2   . LEU A 1 625 ? 176.826 165.690 228.244 1.00 54.41  ?  644 LEU A CD2   1 
ATOM   4976  N  N     . SER A 1 626 ? 180.121 168.666 225.157 1.00 66.84  ?  645 SER A N     1 
ATOM   4977  C  CA    . SER A 1 626 ? 180.915 169.689 224.488 1.00 72.41  ?  645 SER A CA    1 
ATOM   4978  C  C     . SER A 1 626 ? 179.997 170.713 223.818 1.00 73.67  ?  645 SER A C     1 
ATOM   4979  O  O     . SER A 1 626 ? 178.769 170.652 223.931 1.00 75.34  ?  645 SER A O     1 
ATOM   4980  C  CB    . SER A 1 626 ? 181.875 169.050 223.483 1.00 73.82  ?  645 SER A CB    1 
ATOM   4981  O  OG    . SER A 1 626 ? 182.582 170.041 222.758 1.00 75.02  ?  645 SER A OG    1 
ATOM   4982  N  N     . ALA A 1 627 ? 180.613 171.663 223.109 1.00 84.95  ?  646 ALA A N     1 
ATOM   4983  C  CA    . ALA A 1 627 ? 179.878 172.768 222.505 1.00 85.21  ?  646 ALA A CA    1 
ATOM   4984  C  C     . ALA A 1 627 ? 178.999 172.343 221.337 1.00 86.99  ?  646 ALA A C     1 
ATOM   4985  O  O     . ALA A 1 627 ? 177.830 172.741 221.285 1.00 88.31  ?  646 ALA A O     1 
ATOM   4986  C  CB    . ALA A 1 627 ? 180.850 173.855 222.040 1.00 86.46  ?  646 ALA A CB    1 
ATOM   4987  N  N     . LEU A 1 628 ? 179.529 171.559 220.400 1.00 87.14  ?  647 LEU A N     1 
ATOM   4988  C  CA    . LEU A 1 628 ? 178.765 171.106 219.243 1.00 87.19  ?  647 LEU A CA    1 
ATOM   4989  C  C     . LEU A 1 628 ? 177.583 170.228 219.626 1.00 86.44  ?  647 LEU A C     1 
ATOM   4990  O  O     . LEU A 1 628 ? 176.518 170.320 219.004 1.00 86.95  ?  647 LEU A O     1 
ATOM   4991  C  CB    . LEU A 1 628 ? 179.673 170.341 218.273 1.00 88.90  ?  647 LEU A CB    1 
ATOM   4992  C  CG    . LEU A 1 628 ? 180.992 171.010 217.879 1.00 90.75  ?  647 LEU A CG    1 
ATOM   4993  C  CD1   . LEU A 1 628 ? 181.710 170.195 216.814 1.00 87.69  ?  647 LEU A CD1   1 
ATOM   4994  C  CD2   . LEU A 1 628 ? 180.757 172.433 217.397 1.00 86.23  ?  647 LEU A CD2   1 
ATOM   4995  N  N     . HIS A 1 629 ? 177.754 169.378 220.642 1.00 82.17  ?  648 HIS A N     1 
ATOM   4996  C  CA    . HIS A 1 629 ? 176.676 168.499 221.078 1.00 81.57  ?  648 HIS A CA    1 
ATOM   4997  C  C     . HIS A 1 629 ? 175.456 169.291 221.531 1.00 81.65  ?  648 HIS A C     1 
ATOM   4998  O  O     . HIS A 1 629 ? 174.319 168.857 221.316 1.00 84.43  ?  648 HIS A O     1 
ATOM   4999  C  CB    . HIS A 1 629 ? 177.174 167.591 222.202 1.00 79.78  ?  648 HIS A CB    1 
ATOM   5000  C  CG    . HIS A 1 629 ? 176.541 166.235 222.211 1.00 78.70  ?  648 HIS A CG    1 
ATOM   5001  N  ND1   . HIS A 1 629 ? 175.317 165.987 222.793 1.00 78.96  ?  648 HIS A ND1   1 
ATOM   5002  C  CD2   . HIS A 1 629 ? 176.965 165.051 221.709 1.00 80.71  ?  648 HIS A CD2   1 
ATOM   5003  C  CE1   . HIS A 1 629 ? 175.016 164.709 222.653 1.00 82.25  ?  648 HIS A CE1   1 
ATOM   5004  N  NE2   . HIS A 1 629 ? 175.998 164.119 221.995 1.00 82.67  ?  648 HIS A NE2   1 
ATOM   5005  N  N     . PHE A 1 630 ? 175.668 170.450 222.156 1.00 84.36  ?  649 PHE A N     1 
ATOM   5006  C  CA    . PHE A 1 630 ? 174.562 171.302 222.568 1.00 84.99  ?  649 PHE A CA    1 
ATOM   5007  C  C     . PHE A 1 630 ? 174.074 172.224 221.460 1.00 87.55  ?  649 PHE A C     1 
ATOM   5008  O  O     . PHE A 1 630 ? 172.869 172.486 221.382 1.00 89.60  ?  649 PHE A O     1 
ATOM   5009  C  CB    . PHE A 1 630 ? 174.958 172.145 223.782 1.00 85.30  ?  649 PHE A CB    1 
ATOM   5010  C  CG    . PHE A 1 630 ? 174.630 171.501 225.097 1.00 86.49  ?  649 PHE A CG    1 
ATOM   5011  C  CD1   . PHE A 1 630 ? 175.370 170.428 225.564 1.00 85.52  ?  649 PHE A CD1   1 
ATOM   5012  C  CD2   . PHE A 1 630 ? 173.573 171.962 225.864 1.00 87.37  ?  649 PHE A CD2   1 
ATOM   5013  C  CE1   . PHE A 1 630 ? 175.067 169.834 226.773 1.00 87.51  ?  649 PHE A CE1   1 
ATOM   5014  C  CE2   . PHE A 1 630 ? 173.265 171.369 227.074 1.00 88.43  ?  649 PHE A CE2   1 
ATOM   5015  C  CZ    . PHE A 1 630 ? 174.014 170.306 227.529 1.00 89.63  ?  649 PHE A CZ    1 
ATOM   5016  N  N     . ARG A 1 631 ? 174.972 172.725 220.610 1.00 92.77  ?  650 ARG A N     1 
ATOM   5017  C  CA    . ARG A 1 631 ? 174.556 173.548 219.482 1.00 91.70  ?  650 ARG A CA    1 
ATOM   5018  C  C     . ARG A 1 631 ? 173.726 172.773 218.469 1.00 92.32  ?  650 ARG A C     1 
ATOM   5019  O  O     . ARG A 1 631 ? 172.934 173.383 217.741 1.00 92.03  ?  650 ARG A O     1 
ATOM   5020  C  CB    . ARG A 1 631 ? 175.777 174.166 218.788 1.00 91.06  ?  650 ARG A CB    1 
ATOM   5021  C  CG    . ARG A 1 631 ? 176.364 173.330 217.662 1.00 91.38  ?  650 ARG A CG    1 
ATOM   5022  C  CD    . ARG A 1 631 ? 177.475 174.075 216.940 1.00 94.50  ?  650 ARG A CD    1 
ATOM   5023  N  NE    . ARG A 1 631 ? 177.065 175.412 216.528 1.00 95.41  ?  650 ARG A NE    1 
ATOM   5024  C  CZ    . ARG A 1 631 ? 176.349 175.676 215.444 1.00 93.19  ?  650 ARG A CZ    1 
ATOM   5025  N  NH1   . ARG A 1 631 ? 175.942 174.712 214.634 1.00 92.65  1  650 ARG A NH1   1 
ATOM   5026  N  NH2   . ARG A 1 631 ? 176.034 176.937 215.165 1.00 91.44  ?  650 ARG A NH2   1 
ATOM   5027  N  N     . SER A 1 632 ? 173.888 171.453 218.403 1.00 99.55  ?  651 SER A N     1 
ATOM   5028  C  CA    . SER A 1 632 ? 173.001 170.638 217.587 1.00 100.51 ?  651 SER A CA    1 
ATOM   5029  C  C     . SER A 1 632 ? 171.605 170.616 218.198 1.00 100.32 ?  651 SER A C     1 
ATOM   5030  O  O     . SER A 1 632 ? 171.443 170.455 219.411 1.00 99.90  ?  651 SER A O     1 
ATOM   5031  C  CB    . SER A 1 632 ? 173.548 169.216 217.459 1.00 98.62  ?  651 SER A CB    1 
ATOM   5032  O  OG    . SER A 1 632 ? 173.658 168.595 218.727 1.00 99.11  ?  651 SER A OG    1 
ATOM   5033  N  N     . ASN A 1 633 ? 170.593 170.783 217.352 1.00 106.75 ?  652 ASN A N     1 
ATOM   5034  C  CA    . ASN A 1 633 ? 169.205 170.866 217.809 1.00 105.09 ?  652 ASN A CA    1 
ATOM   5035  C  C     . ASN A 1 633 ? 168.557 169.488 217.910 1.00 104.46 ?  652 ASN A C     1 
ATOM   5036  O  O     . ASN A 1 633 ? 167.457 169.257 217.411 1.00 105.82 ?  652 ASN A O     1 
ATOM   5037  C  CB    . ASN A 1 633 ? 168.410 171.775 216.879 1.00 107.18 ?  652 ASN A CB    1 
ATOM   5038  C  CG    . ASN A 1 633 ? 168.623 171.442 215.415 1.00 108.04 ?  652 ASN A CG    1 
ATOM   5039  O  OD1   . ASN A 1 633 ? 169.311 170.477 215.080 1.00 108.10 ?  652 ASN A OD1   1 
ATOM   5040  N  ND2   . ASN A 1 633 ? 168.035 172.242 214.534 1.00 106.64 ?  652 ASN A ND2   1 
ATOM   5041  N  N     . GLN A 1 634 ? 169.245 168.557 218.570 1.00 98.33  ?  653 GLN A N     1 
ATOM   5042  C  CA    . GLN A 1 634 ? 168.734 167.206 218.761 1.00 99.94  ?  653 GLN A CA    1 
ATOM   5043  C  C     . GLN A 1 634 ? 168.893 166.670 220.174 1.00 100.86 ?  653 GLN A C     1 
ATOM   5044  O  O     . GLN A 1 634 ? 168.248 165.666 220.500 1.00 99.02  ?  653 GLN A O     1 
ATOM   5045  C  CB    . GLN A 1 634 ? 169.421 166.230 217.794 1.00 100.31 ?  653 GLN A CB    1 
ATOM   5046  C  CG    . GLN A 1 634 ? 168.716 166.066 216.462 1.00 100.59 ?  653 GLN A CG    1 
ATOM   5047  C  CD    . GLN A 1 634 ? 169.090 164.770 215.775 1.00 101.82 ?  653 GLN A CD    1 
ATOM   5048  O  OE1   . GLN A 1 634 ? 169.887 163.988 216.294 1.00 100.99 ?  653 GLN A OE1   1 
ATOM   5049  N  NE2   . GLN A 1 634 ? 168.515 164.534 214.603 1.00 100.20 ?  653 GLN A NE2   1 
ATOM   5050  N  N     . LEU A 1 635 ? 169.695 167.312 221.025 1.00 101.45 ?  654 LEU A N     1 
ATOM   5051  C  CA    . LEU A 1 635 ? 170.088 166.742 222.314 1.00 103.02 ?  654 LEU A CA    1 
ATOM   5052  C  C     . LEU A 1 635 ? 168.922 166.312 223.200 1.00 102.55 ?  654 LEU A C     1 
ATOM   5053  O  O     . LEU A 1 635 ? 168.908 165.143 223.628 1.00 102.36 ?  654 LEU A O     1 
ATOM   5054  C  CB    . LEU A 1 635 ? 170.977 167.762 223.041 1.00 99.97  ?  654 LEU A CB    1 
ATOM   5055  C  CG    . LEU A 1 635 ? 171.509 167.412 224.431 1.00 101.82 ?  654 LEU A CG    1 
ATOM   5056  C  CD1   . LEU A 1 635 ? 172.459 166.233 224.374 1.00 100.36 ?  654 LEU A CD1   1 
ATOM   5057  C  CD2   . LEU A 1 635 ? 172.182 168.619 225.052 1.00 100.93 ?  654 LEU A CD2   1 
ATOM   5058  N  N     . PRO A 1 636 ? 167.921 167.158 223.487 1.00 102.58 ?  655 PRO A N     1 
ATOM   5059  C  CA    . PRO A 1 636 ? 166.890 166.750 224.454 1.00 104.03 ?  655 PRO A CA    1 
ATOM   5060  C  C     . PRO A 1 636 ? 166.133 165.506 224.039 1.00 102.86 ?  655 PRO A C     1 
ATOM   5061  O  O     . PRO A 1 636 ? 165.683 164.756 224.911 1.00 101.88 ?  655 PRO A O     1 
ATOM   5062  C  CB    . PRO A 1 636 ? 165.967 167.976 224.526 1.00 105.40 ?  655 PRO A CB    1 
ATOM   5063  C  CG    . PRO A 1 636 ? 166.780 169.107 224.000 1.00 103.48 ?  655 PRO A CG    1 
ATOM   5064  C  CD    . PRO A 1 636 ? 167.643 168.501 222.947 1.00 101.84 ?  655 PRO A CD    1 
ATOM   5065  N  N     . ASN A 1 637 ? 165.991 165.254 222.736 1.00 101.04 ?  656 ASN A N     1 
ATOM   5066  C  CA    . ASN A 1 637 ? 165.287 164.056 222.291 1.00 100.40 ?  656 ASN A CA    1 
ATOM   5067  C  C     . ASN A 1 637 ? 165.968 162.793 222.808 1.00 101.42 ?  656 ASN A C     1 
ATOM   5068  O  O     . ASN A 1 637 ? 165.338 161.965 223.478 1.00 99.83  ?  656 ASN A O     1 
ATOM   5069  C  CB    . ASN A 1 637 ? 165.199 164.041 220.764 1.00 102.46 ?  656 ASN A CB    1 
ATOM   5070  C  CG    . ASN A 1 637 ? 164.654 165.339 220.199 1.00 102.22 ?  656 ASN A CG    1 
ATOM   5071  O  OD1   . ASN A 1 637 ? 165.384 166.317 220.041 1.00 102.03 ?  656 ASN A OD1   1 
ATOM   5072  N  ND2   . ASN A 1 637 ? 163.362 165.352 219.890 1.00 100.80 ?  656 ASN A ND2   1 
ATOM   5073  N  N     . GLN A 1 638 ? 167.272 162.649 222.550 1.00 99.82  ?  657 GLN A N     1 
ATOM   5074  C  CA    . GLN A 1 638 ? 167.939 161.435 223.004 1.00 99.38  ?  657 GLN A CA    1 
ATOM   5075  C  C     . GLN A 1 638 ? 168.161 161.442 224.508 1.00 99.65  ?  657 GLN A C     1 
ATOM   5076  O  O     . GLN A 1 638 ? 168.209 160.371 225.118 1.00 98.70  ?  657 GLN A O     1 
ATOM   5077  C  CB    . GLN A 1 638 ? 169.279 161.216 222.291 1.00 97.67  ?  657 GLN A CB    1 
ATOM   5078  C  CG    . GLN A 1 638 ? 170.431 162.063 222.799 1.00 96.60  ?  657 GLN A CG    1 
ATOM   5079  C  CD    . GLN A 1 638 ? 170.669 163.289 221.960 1.00 96.96  ?  657 GLN A CD    1 
ATOM   5080  O  OE1   . GLN A 1 638 ? 169.837 163.663 221.139 1.00 95.58  ?  657 GLN A OE1   1 
ATOM   5081  N  NE2   . GLN A 1 638 ? 171.811 163.930 222.165 1.00 97.61  ?  657 GLN A NE2   1 
ATOM   5082  N  N     . VAL A 1 639 ? 168.282 162.616 225.136 1.00 104.76 ?  658 VAL A N     1 
ATOM   5083  C  CA    . VAL A 1 639 ? 168.428 162.621 226.591 1.00 105.45 ?  658 VAL A CA    1 
ATOM   5084  C  C     . VAL A 1 639 ? 167.142 162.133 227.259 1.00 107.42 ?  658 VAL A C     1 
ATOM   5085  O  O     . VAL A 1 639 ? 167.178 161.305 228.181 1.00 106.79 ?  658 VAL A O     1 
ATOM   5086  C  CB    . VAL A 1 639 ? 168.851 164.014 227.090 1.00 105.42 ?  658 VAL A CB    1 
ATOM   5087  C  CG1   . VAL A 1 639 ? 169.140 163.979 228.572 1.00 104.39 ?  658 VAL A CG1   1 
ATOM   5088  C  CG2   . VAL A 1 639 ? 170.093 164.471 226.360 1.00 106.27 ?  658 VAL A CG2   1 
ATOM   5089  N  N     . SER A 1 640 ? 165.987 162.612 226.788 1.00 107.79 ?  659 SER A N     1 
ATOM   5090  C  CA    . SER A 1 640 ? 164.711 162.133 227.308 1.00 105.22 ?  659 SER A CA    1 
ATOM   5091  C  C     . SER A 1 640 ? 164.515 160.654 227.004 1.00 103.94 ?  659 SER A C     1 
ATOM   5092  O  O     . SER A 1 640 ? 163.974 159.910 227.831 1.00 105.57 ?  659 SER A O     1 
ATOM   5093  C  CB    . SER A 1 640 ? 163.563 162.955 226.721 1.00 105.78 ?  659 SER A CB    1 
ATOM   5094  O  OG    . SER A 1 640 ? 163.795 164.343 226.874 1.00 105.55 ?  659 SER A OG    1 
ATOM   5095  N  N     . ASP A 1 641 ? 164.930 160.213 225.812 1.00 101.08 ?  660 ASP A N     1 
ATOM   5096  C  CA    . ASP A 1 641 ? 164.862 158.791 225.497 1.00 104.86 ?  660 ASP A CA    1 
ATOM   5097  C  C     . ASP A 1 641 ? 165.700 157.977 226.472 1.00 102.05 ?  660 ASP A C     1 
ATOM   5098  O  O     . ASP A 1 641 ? 165.262 156.926 226.955 1.00 101.13 ?  660 ASP A O     1 
ATOM   5099  C  CB    . ASP A 1 641 ? 165.319 158.546 224.058 1.00 105.50 ?  660 ASP A CB    1 
ATOM   5100  C  CG    . ASP A 1 641 ? 164.341 159.090 223.035 1.00 103.91 ?  660 ASP A CG    1 
ATOM   5101  O  OD1   . ASP A 1 641 ? 163.134 159.166 223.346 1.00 103.12 ?  660 ASP A OD1   1 
ATOM   5102  O  OD2   . ASP A 1 641 ? 164.780 159.439 221.920 1.00 102.93 -1 660 ASP A OD2   1 
ATOM   5103  N  N     . ALA A 1 642 ? 166.903 158.461 226.788 1.00 98.08  ?  661 ALA A N     1 
ATOM   5104  C  CA    . ALA A 1 642 ? 167.773 157.761 227.722 1.00 99.99  ?  661 ALA A CA    1 
ATOM   5105  C  C     . ALA A 1 642 ? 167.151 157.678 229.109 1.00 102.16 ?  661 ALA A C     1 
ATOM   5106  O  O     . ALA A 1 642 ? 167.228 156.633 229.766 1.00 102.50 ?  661 ALA A O     1 
ATOM   5107  C  CB    . ALA A 1 642 ? 169.135 158.450 227.778 1.00 99.42  ?  661 ALA A CB    1 
ATOM   5108  N  N     . MET A 1 643 ? 166.537 158.768 229.581 1.00 99.42  ?  662 MET A N     1 
ATOM   5109  C  CA    . MET A 1 643 ? 165.883 158.702 230.889 1.00 97.91  ?  662 MET A CA    1 
ATOM   5110  C  C     . MET A 1 643 ? 164.704 157.736 230.883 1.00 100.14 ?  662 MET A C     1 
ATOM   5111  O  O     . MET A 1 643 ? 164.602 156.866 231.757 1.00 98.87  ?  662 MET A O     1 
ATOM   5112  C  CB    . MET A 1 643 ? 165.424 160.079 231.376 1.00 96.26  ?  662 MET A CB    1 
ATOM   5113  C  CG    . MET A 1 643 ? 166.473 160.877 232.141 1.00 97.85  ?  662 MET A CG    1 
ATOM   5114  S  SD    . MET A 1 643 ? 167.638 161.802 231.145 1.00 105.98 ?  662 MET A SD    1 
ATOM   5115  C  CE    . MET A 1 643 ? 166.573 163.176 230.719 1.00 100.68 ?  662 MET A CE    1 
ATOM   5116  N  N     . HIS A 1 644 ? 163.799 157.869 229.916 1.00 104.74 ?  663 HIS A N     1 
ATOM   5117  C  CA    . HIS A 1 644 ? 162.554 157.113 229.979 1.00 104.29 ?  663 HIS A CA    1 
ATOM   5118  C  C     . HIS A 1 644 ? 162.687 155.691 229.446 1.00 102.29 ?  663 HIS A C     1 
ATOM   5119  O  O     . HIS A 1 644 ? 161.721 154.926 229.526 1.00 102.65 ?  663 HIS A O     1 
ATOM   5120  C  CB    . HIS A 1 644 ? 161.432 157.849 229.232 1.00 101.92 ?  663 HIS A CB    1 
ATOM   5121  C  CG    . HIS A 1 644 ? 161.306 157.476 227.788 1.00 102.36 ?  663 HIS A CG    1 
ATOM   5122  N  ND1   . HIS A 1 644 ? 161.976 158.141 226.784 1.00 104.36 ?  663 HIS A ND1   1 
ATOM   5123  C  CD2   . HIS A 1 644 ? 160.569 156.518 227.176 1.00 101.36 ?  663 HIS A CD2   1 
ATOM   5124  C  CE1   . HIS A 1 644 ? 161.666 157.602 225.619 1.00 103.35 ?  663 HIS A CE1   1 
ATOM   5125  N  NE2   . HIS A 1 644 ? 160.815 156.614 225.829 1.00 101.70 ?  663 HIS A NE2   1 
ATOM   5126  N  N     . ALA A 1 645 ? 163.851 155.312 228.910 1.00 91.37  ?  664 ALA A N     1 
ATOM   5127  C  CA    . ALA A 1 645 ? 164.051 153.921 228.521 1.00 92.78  ?  664 ALA A CA    1 
ATOM   5128  C  C     . ALA A 1 645 ? 164.496 153.055 229.691 1.00 91.50  ?  664 ALA A C     1 
ATOM   5129  O  O     . ALA A 1 645 ? 164.277 151.839 229.671 1.00 91.05  ?  664 ALA A O     1 
ATOM   5130  C  CB    . ALA A 1 645 ? 165.072 153.832 227.386 1.00 91.24  ?  664 ALA A CB    1 
ATOM   5131  N  N     . TRP A 1 646 ? 165.118 153.650 230.710 1.00 79.84  ?  665 TRP A N     1 
ATOM   5132  C  CA    . TRP A 1 646 ? 165.626 152.896 231.850 1.00 81.66  ?  665 TRP A CA    1 
ATOM   5133  C  C     . TRP A 1 646 ? 165.149 153.443 233.191 1.00 82.06  ?  665 TRP A C     1 
ATOM   5134  O  O     . TRP A 1 646 ? 165.651 153.009 234.235 1.00 79.05  ?  665 TRP A O     1 
ATOM   5135  C  CB    . TRP A 1 646 ? 167.158 152.856 231.822 1.00 79.40  ?  665 TRP A CB    1 
ATOM   5136  C  CG    . TRP A 1 646 ? 167.717 151.849 230.862 1.00 76.36  ?  665 TRP A CG    1 
ATOM   5137  C  CD1   . TRP A 1 646 ? 167.740 150.494 231.018 1.00 76.34  ?  665 TRP A CD1   1 
ATOM   5138  C  CD2   . TRP A 1 646 ? 168.347 152.118 229.604 1.00 77.60  ?  665 TRP A CD2   1 
ATOM   5139  N  NE1   . TRP A 1 646 ? 168.338 149.902 229.932 1.00 75.23  ?  665 TRP A NE1   1 
ATOM   5140  C  CE2   . TRP A 1 646 ? 168.720 150.878 229.050 1.00 76.82  ?  665 TRP A CE2   1 
ATOM   5141  C  CE3   . TRP A 1 646 ? 168.629 153.287 228.891 1.00 78.32  ?  665 TRP A CE3   1 
ATOM   5142  C  CZ2   . TRP A 1 646 ? 169.360 150.773 227.817 1.00 77.92  ?  665 TRP A CZ2   1 
ATOM   5143  C  CZ3   . TRP A 1 646 ? 169.264 153.181 227.667 1.00 76.22  ?  665 TRP A CZ3   1 
ATOM   5144  C  CH2   . TRP A 1 646 ? 169.623 151.934 227.143 1.00 77.30  ?  665 TRP A CH2   1 
ATOM   5145  N  N     . GLY A 1 647 ? 164.196 154.374 233.197 1.00 84.75  ?  666 GLY A N     1 
ATOM   5146  C  CA    . GLY A 1 647 ? 163.659 154.889 234.443 1.00 81.23  ?  666 GLY A CA    1 
ATOM   5147  C  C     . GLY A 1 647 ? 164.690 155.608 235.289 1.00 80.67  ?  666 GLY A C     1 
ATOM   5148  O  O     . GLY A 1 647 ? 164.785 155.379 236.498 1.00 82.76  ?  666 GLY A O     1 
ATOM   5149  N  N     . ILE A 1 648 ? 165.469 156.482 234.658 1.00 78.55  ?  667 ILE A N     1 
ATOM   5150  C  CA    . ILE A 1 648 ? 166.588 157.156 235.307 1.00 83.49  ?  667 ILE A CA    1 
ATOM   5151  C  C     . ILE A 1 648 ? 166.356 158.666 235.280 1.00 84.14  ?  667 ILE A C     1 
ATOM   5152  O  O     . ILE A 1 648 ? 167.292 159.454 235.095 1.00 83.84  ?  667 ILE A O     1 
ATOM   5153  C  CB    . ILE A 1 648 ? 167.931 156.732 234.673 1.00 83.35  ?  667 ILE A CB    1 
ATOM   5154  C  CG1   . ILE A 1 648 ? 169.096 157.059 235.612 1.00 82.08  ?  667 ILE A CG1   1 
ATOM   5155  C  CG2   . ILE A 1 648 ? 168.110 157.285 233.254 1.00 83.56  ?  667 ILE A CG2   1 
ATOM   5156  C  CD1   . ILE A 1 648 ? 168.994 156.378 236.961 1.00 79.93  ?  667 ILE A CD1   1 
ATOM   5157  N  N     . ASP A 1 649 ? 165.092 159.063 235.471 1.00 81.43  ?  668 ASP A N     1 
ATOM   5158  C  CA    . ASP A 1 649 ? 164.632 160.446 235.339 1.00 81.19  ?  668 ASP A CA    1 
ATOM   5159  C  C     . ASP A 1 649 ? 165.639 161.455 235.881 1.00 78.77  ?  668 ASP A C     1 
ATOM   5160  O  O     . ASP A 1 649 ? 166.286 161.231 236.907 1.00 75.42  ?  668 ASP A O     1 
ATOM   5161  C  CB    . ASP A 1 649 ? 163.294 160.612 236.066 1.00 81.11  ?  668 ASP A CB    1 
ATOM   5162  C  CG    . ASP A 1 649 ? 163.327 160.059 237.479 1.00 81.26  ?  668 ASP A CG    1 
ATOM   5163  O  OD1   . ASP A 1 649 ? 164.343 159.436 237.853 1.00 77.90  ?  668 ASP A OD1   1 
ATOM   5164  O  OD2   . ASP A 1 649 ? 162.339 160.251 238.218 1.00 79.40  -1 668 ASP A OD2   1 
ATOM   5165  N  N     . GLY A 1 650 ? 165.736 162.584 235.182 1.00 70.82  ?  669 GLY A N     1 
ATOM   5166  C  CA    . GLY A 1 650 ? 166.860 163.499 235.253 1.00 70.44  ?  669 GLY A CA    1 
ATOM   5167  C  C     . GLY A 1 650 ? 167.306 164.024 236.603 1.00 67.04  ?  669 GLY A C     1 
ATOM   5168  O  O     . GLY A 1 650 ? 168.323 164.719 236.675 1.00 65.59  ?  669 GLY A O     1 
ATOM   5169  N  N     . HIS A 1 651 ? 166.581 163.719 237.680 1.00 63.73  ?  670 HIS A N     1 
ATOM   5170  C  CA    . HIS A 1 651 ? 167.050 164.172 238.987 1.00 65.51  ?  670 HIS A CA    1 
ATOM   5171  C  C     . HIS A 1 651 ? 168.350 163.496 239.413 1.00 69.36  ?  670 HIS A C     1 
ATOM   5172  O  O     . HIS A 1 651 ? 168.870 163.817 240.488 1.00 66.19  ?  670 HIS A O     1 
ATOM   5173  C  CB    . HIS A 1 651 ? 165.975 163.946 240.054 1.00 67.22  ?  670 HIS A CB    1 
ATOM   5174  C  CG    . HIS A 1 651 ? 165.888 162.533 240.543 1.00 69.97  ?  670 HIS A CG    1 
ATOM   5175  N  ND1   . HIS A 1 651 ? 165.072 161.589 239.959 1.00 72.32  ?  670 HIS A ND1   1 
ATOM   5176  C  CD2   . HIS A 1 651 ? 166.510 161.908 241.571 1.00 69.11  ?  670 HIS A CD2   1 
ATOM   5177  C  CE1   . HIS A 1 651 ? 165.198 160.442 240.602 1.00 72.14  ?  670 HIS A CE1   1 
ATOM   5178  N  NE2   . HIS A 1 651 ? 166.065 160.608 241.584 1.00 72.54  ?  670 HIS A NE2   1 
ATOM   5179  N  N     . GLN A 1 652 ? 168.883 162.581 238.605 1.00 67.14  ?  671 GLN A N     1 
ATOM   5180  C  CA    . GLN A 1 652 ? 170.148 161.909 238.867 1.00 60.05  ?  671 GLN A CA    1 
ATOM   5181  C  C     . GLN A 1 652 ? 171.231 162.293 237.870 1.00 57.79  ?  671 GLN A C     1 
ATOM   5182  O  O     . GLN A 1 652 ? 172.367 162.573 238.266 1.00 61.31  ?  671 GLN A O     1 
ATOM   5183  C  CB    . GLN A 1 652 ? 169.943 160.388 238.852 1.00 55.18  ?  671 GLN A CB    1 
ATOM   5184  C  CG    . GLN A 1 652 ? 169.859 159.761 240.232 1.00 59.00  ?  671 GLN A CG    1 
ATOM   5185  C  CD    . GLN A 1 652 ? 169.635 158.265 240.180 1.00 61.22  ?  671 GLN A CD    1 
ATOM   5186  O  OE1   . GLN A 1 652 ? 168.545 157.801 239.847 1.00 60.63  ?  671 GLN A OE1   1 
ATOM   5187  N  NE2   . GLN A 1 652 ? 170.669 157.499 240.509 1.00 64.24  ?  671 GLN A NE2   1 
ATOM   5188  N  N     . LEU A 1 653 ? 170.905 162.307 236.581 1.00 42.88  ?  672 LEU A N     1 
ATOM   5189  C  CA    . LEU A 1 653 ? 171.879 162.653 235.556 1.00 37.21  ?  672 LEU A CA    1 
ATOM   5190  C  C     . LEU A 1 653 ? 172.293 164.117 235.679 1.00 43.09  ?  672 LEU A C     1 
ATOM   5191  O  O     . LEU A 1 653 ? 171.527 164.968 236.140 1.00 55.28  ?  672 LEU A O     1 
ATOM   5192  C  CB    . LEU A 1 653 ? 171.303 162.378 234.166 1.00 42.66  ?  672 LEU A CB    1 
ATOM   5193  C  CG    . LEU A 1 653 ? 172.276 162.400 232.986 1.00 47.82  ?  672 LEU A CG    1 
ATOM   5194  C  CD1   . LEU A 1 653 ? 173.293 161.283 233.116 1.00 46.23  ?  672 LEU A CD1   1 
ATOM   5195  C  CD2   . LEU A 1 653 ? 171.522 162.284 231.670 1.00 50.58  ?  672 LEU A CD2   1 
ATOM   5196  N  N     . THR A 1 654 ? 173.527 164.401 235.269 1.00 43.94  ?  673 THR A N     1 
ATOM   5197  C  CA    . THR A 1 654 ? 174.073 165.747 235.336 1.00 44.15  ?  673 THR A CA    1 
ATOM   5198  C  C     . THR A 1 654 ? 174.967 165.968 234.123 1.00 36.52  ?  673 THR A C     1 
ATOM   5199  O  O     . THR A 1 654 ? 175.611 165.037 233.632 1.00 52.14  ?  673 THR A O     1 
ATOM   5200  C  CB    . THR A 1 654 ? 174.858 165.966 236.639 1.00 44.54  ?  673 THR A CB    1 
ATOM   5201  O  OG1   . THR A 1 654 ? 174.036 165.610 237.758 1.00 47.41  ?  673 THR A OG1   1 
ATOM   5202  C  CG2   . THR A 1 654 ? 175.280 167.421 236.783 1.00 44.12  ?  673 THR A CG2   1 
ATOM   5203  N  N     . VAL A 1 655 ? 174.997 167.208 233.642 1.00 22.78  ?  674 VAL A N     1 
ATOM   5204  C  CA    . VAL A 1 655 ? 175.771 167.584 232.467 1.00 32.53  ?  674 VAL A CA    1 
ATOM   5205  C  C     . VAL A 1 655 ? 176.711 168.721 232.844 1.00 37.84  ?  674 VAL A C     1 
ATOM   5206  O  O     . VAL A 1 655 ? 176.300 169.689 233.493 1.00 52.88  ?  674 VAL A O     1 
ATOM   5207  C  CB    . VAL A 1 655 ? 174.856 167.999 231.295 1.00 41.27  ?  674 VAL A CB    1 
ATOM   5208  C  CG1   . VAL A 1 655 ? 175.664 168.661 230.192 1.00 43.41  ?  674 VAL A CG1   1 
ATOM   5209  C  CG2   . VAL A 1 655 ? 174.098 166.794 230.760 1.00 45.63  ?  674 VAL A CG2   1 
ATOM   5210  N  N     . GLU A 1 656 ? 177.976 168.597 232.447 1.00 38.86  ?  675 GLU A N     1 
ATOM   5211  C  CA    . GLU A 1 656 ? 178.977 169.645 232.637 1.00 42.54  ?  675 GLU A CA    1 
ATOM   5212  C  C     . GLU A 1 656 ? 179.394 170.142 231.256 1.00 44.50  ?  675 GLU A C     1 
ATOM   5213  O  O     . GLU A 1 656 ? 179.925 169.380 230.444 1.00 57.94  ?  675 GLU A O     1 
ATOM   5214  C  CB    . GLU A 1 656 ? 180.169 169.136 233.447 1.00 47.30  ?  675 GLU A CB    1 
ATOM   5215  C  CG    . GLU A 1 656 ? 180.732 167.805 232.981 1.00 54.66  ?  675 GLU A CG    1 
ATOM   5216  C  CD    . GLU A 1 656 ? 180.147 166.634 233.741 1.00 58.16  ?  675 GLU A CD    1 
ATOM   5217  O  OE1   . GLU A 1 656 ? 179.104 166.818 234.402 1.00 59.93  ?  675 GLU A OE1   1 
ATOM   5218  O  OE2   . GLU A 1 656 ? 180.731 165.532 233.679 1.00 54.49  -1 675 GLU A OE2   1 
ATOM   5219  N  N     . ILE A 1 657 ? 179.139 171.415 230.986 1.00 58.41  ?  676 ILE A N     1 
ATOM   5220  C  CA    . ILE A 1 657 ? 179.415 171.986 229.678 1.00 63.15  ?  676 ILE A CA    1 
ATOM   5221  C  C     . ILE A 1 657 ? 180.712 172.784 229.731 1.00 70.78  ?  676 ILE A C     1 
ATOM   5222  O  O     . ILE A 1 657 ? 181.166 173.220 230.792 1.00 75.52  ?  676 ILE A O     1 
ATOM   5223  C  CB    . ILE A 1 657 ? 178.244 172.859 229.189 1.00 69.62  ?  676 ILE A CB    1 
ATOM   5224  C  CG1   . ILE A 1 657 ? 177.859 173.883 230.258 1.00 72.09  ?  676 ILE A CG1   1 
ATOM   5225  C  CG2   . ILE A 1 657 ? 177.053 171.989 228.825 1.00 70.16  ?  676 ILE A CG2   1 
ATOM   5226  C  CD1   . ILE A 1 657 ? 176.749 174.818 229.836 1.00 69.90  ?  676 ILE A CD1   1 
ATOM   5227  N  N     . THR A 1 658 ? 181.314 172.975 228.561 1.00 91.30  ?  677 THR A N     1 
ATOM   5228  C  CA    . THR A 1 658 ? 182.561 173.718 228.459 1.00 93.41  ?  677 THR A CA    1 
ATOM   5229  C  C     . THR A 1 658 ? 182.329 175.204 228.714 1.00 96.40  ?  677 THR A C     1 
ATOM   5230  O  O     . THR A 1 658 ? 181.279 175.760 228.380 1.00 97.05  ?  677 THR A O     1 
ATOM   5231  C  CB    . THR A 1 658 ? 183.186 173.515 227.077 1.00 93.07  ?  677 THR A CB    1 
ATOM   5232  O  OG1   . THR A 1 658 ? 183.114 172.130 226.717 1.00 93.50  ?  677 THR A OG1   1 
ATOM   5233  C  CG2   . THR A 1 658 ? 184.645 173.954 227.072 1.00 94.86  ?  677 THR A CG2   1 
ATOM   5234  N  N     . GLU A 1 659 ? 183.328 175.847 229.325 1.00 113.57 ?  678 GLU A N     1 
ATOM   5235  C  CA    . GLU A 1 659 ? 183.273 177.288 229.548 1.00 113.73 ?  678 GLU A CA    1 
ATOM   5236  C  C     . GLU A 1 659 ? 183.216 178.065 228.237 1.00 115.16 ?  678 GLU A C     1 
ATOM   5237  O  O     . GLU A 1 659 ? 182.754 179.212 228.224 1.00 113.73 ?  678 GLU A O     1 
ATOM   5238  C  CB    . GLU A 1 659 ? 184.478 177.722 230.390 1.00 114.21 ?  678 GLU A CB    1 
ATOM   5239  C  CG    . GLU A 1 659 ? 184.565 179.214 230.685 1.00 115.80 ?  678 GLU A CG    1 
ATOM   5240  C  CD    . GLU A 1 659 ? 185.461 179.949 229.709 1.00 117.27 ?  678 GLU A CD    1 
ATOM   5241  O  OE1   . GLU A 1 659 ? 186.319 179.294 229.081 1.00 116.51 ?  678 GLU A OE1   1 
ATOM   5242  O  OE2   . GLU A 1 659 ? 185.307 181.180 229.566 1.00 115.35 -1 678 GLU A OE2   1 
ATOM   5243  N  N     . SER A 1 660 ? 183.669 177.462 227.134 1.00 121.34 ?  679 SER A N     1 
ATOM   5244  C  CA    . SER A 1 660 ? 183.545 178.109 225.832 1.00 120.77 ?  679 SER A CA    1 
ATOM   5245  C  C     . SER A 1 660 ? 182.082 178.317 225.460 1.00 120.14 ?  679 SER A C     1 
ATOM   5246  O  O     . SER A 1 660 ? 181.730 179.320 224.829 1.00 119.34 ?  679 SER A O     1 
ATOM   5247  C  CB    . SER A 1 660 ? 184.260 177.282 224.765 1.00 119.88 ?  679 SER A CB    1 
ATOM   5248  O  OG    . SER A 1 660 ? 185.620 177.076 225.106 1.00 119.76 ?  679 SER A OG    1 
ATOM   5249  N  N     . MET A 1 661 ? 181.212 177.378 225.843 1.00 115.65 ?  680 MET A N     1 
ATOM   5250  C  CA    . MET A 1 661 ? 179.784 177.554 225.598 1.00 114.96 ?  680 MET A CA    1 
ATOM   5251  C  C     . MET A 1 661 ? 179.245 178.773 226.332 1.00 114.67 ?  680 MET A C     1 
ATOM   5252  O  O     . MET A 1 661 ? 178.469 179.555 225.770 1.00 114.67 ?  680 MET A O     1 
ATOM   5253  C  CB    . MET A 1 661 ? 179.017 176.303 226.020 1.00 114.10 ?  680 MET A CB    1 
ATOM   5254  C  CG    . MET A 1 661 ? 179.080 175.165 225.026 1.00 113.73 ?  680 MET A CG    1 
ATOM   5255  S  SD    . MET A 1 661 ? 178.248 173.693 225.646 1.00 114.55 ?  680 MET A SD    1 
ATOM   5256  C  CE    . MET A 1 661 ? 176.642 174.375 226.049 1.00 113.29 ?  680 MET A CE    1 
ATOM   5257  N  N     . MET A 1 662 ? 179.644 178.952 227.593 1.00 119.46 ?  681 MET A N     1 
ATOM   5258  C  CA    . MET A 1 662 ? 179.192 180.114 228.349 1.00 120.09 ?  681 MET A CA    1 
ATOM   5259  C  C     . MET A 1 662 ? 179.777 181.404 227.793 1.00 120.65 ?  681 MET A C     1 
ATOM   5260  O  O     . MET A 1 662 ? 179.114 182.447 227.821 1.00 120.74 ?  681 MET A O     1 
ATOM   5261  C  CB    . MET A 1 662 ? 179.550 179.953 229.825 1.00 118.94 ?  681 MET A CB    1 
ATOM   5262  C  CG    . MET A 1 662 ? 178.623 179.006 230.563 1.00 120.55 ?  681 MET A CG    1 
ATOM   5263  S  SD    . MET A 1 662 ? 176.896 179.493 230.399 1.00 121.51 ?  681 MET A SD    1 
ATOM   5264  C  CE    . MET A 1 662 ? 176.970 181.213 230.899 1.00 118.17 ?  681 MET A CE    1 
ATOM   5265  N  N     . MET A 1 663 ? 181.014 181.355 227.296 1.00 125.67 ?  682 MET A N     1 
ATOM   5266  C  CA    . MET A 1 663 ? 181.583 182.515 226.618 1.00 126.52 ?  682 MET A CA    1 
ATOM   5267  C  C     . MET A 1 663 ? 180.775 182.865 225.374 1.00 126.53 ?  682 MET A C     1 
ATOM   5268  O  O     . MET A 1 663 ? 180.540 184.045 225.085 1.00 124.85 ?  682 MET A O     1 
ATOM   5269  C  CB    . MET A 1 663 ? 183.045 182.250 226.258 1.00 125.37 ?  682 MET A CB    1 
ATOM   5270  C  CG    . MET A 1 663 ? 183.733 183.404 225.545 1.00 125.16 ?  682 MET A CG    1 
ATOM   5271  S  SD    . MET A 1 663 ? 183.815 183.174 223.759 1.00 129.07 ?  682 MET A SD    1 
ATOM   5272  C  CE    . MET A 1 663 ? 185.001 181.837 223.643 1.00 124.85 ?  682 MET A CE    1 
ATOM   5273  N  N     . GLU A 1 664 ? 180.345 181.852 224.626 1.00 127.45 ?  683 GLU A N     1 
ATOM   5274  C  CA    . GLU A 1 664 ? 179.468 182.076 223.485 1.00 127.03 ?  683 GLU A CA    1 
ATOM   5275  C  C     . GLU A 1 664 ? 178.110 182.586 223.953 1.00 127.84 ?  683 GLU A C     1 
ATOM   5276  O  O     . GLU A 1 664 ? 177.613 182.197 225.013 1.00 127.13 ?  683 GLU A O     1 
ATOM   5277  C  CB    . GLU A 1 664 ? 179.298 180.783 222.685 1.00 126.27 ?  683 GLU A CB    1 
ATOM   5278  C  CG    . GLU A 1 664 ? 180.548 180.336 221.944 1.00 126.03 ?  683 GLU A CG    1 
ATOM   5279  C  CD    . GLU A 1 664 ? 180.413 178.941 221.364 1.00 126.28 ?  683 GLU A CD    1 
ATOM   5280  O  OE1   . GLU A 1 664 ? 179.337 178.329 221.530 1.00 125.56 ?  683 GLU A OE1   1 
ATOM   5281  O  OE2   . GLU A 1 664 ? 181.382 178.456 220.744 1.00 126.95 -1 683 GLU A OE2   1 
ATOM   5282  N  N     . HIS A 1 665 ? 177.510 183.465 223.154 1.00 128.61 ?  684 HIS A N     1 
ATOM   5283  C  CA    . HIS A 1 665 ? 176.228 184.093 223.471 1.00 128.29 ?  684 HIS A CA    1 
ATOM   5284  C  C     . HIS A 1 665 ? 175.250 183.773 222.343 1.00 127.30 ?  684 HIS A C     1 
ATOM   5285  O  O     . HIS A 1 665 ? 175.144 184.522 221.369 1.00 126.43 ?  684 HIS A O     1 
ATOM   5286  C  CB    . HIS A 1 665 ? 176.392 185.604 223.661 1.00 128.50 ?  684 HIS A CB    1 
ATOM   5287  C  CG    . HIS A 1 665 ? 177.052 185.987 224.949 1.00 127.70 ?  684 HIS A CG    1 
ATOM   5288  N  ND1   . HIS A 1 665 ? 178.235 185.423 225.376 1.00 126.30 ?  684 HIS A ND1   1 
ATOM   5289  C  CD2   . HIS A 1 665 ? 176.699 186.884 225.900 1.00 127.74 ?  684 HIS A CD2   1 
ATOM   5290  C  CE1   . HIS A 1 665 ? 178.580 185.953 226.536 1.00 126.48 ?  684 HIS A CE1   1 
ATOM   5291  N  NE2   . HIS A 1 665 ? 177.664 186.843 226.876 1.00 127.65 ?  684 HIS A NE2   1 
ATOM   5292  N  N     . ASP A 1 666 ? 174.533 182.658 222.478 1.00 125.93 ?  685 ASP A N     1 
ATOM   5293  C  CA    . ASP A 1 666 ? 173.563 182.222 221.479 1.00 126.11 ?  685 ASP A CA    1 
ATOM   5294  C  C     . ASP A 1 666 ? 172.205 182.056 222.141 1.00 125.80 ?  685 ASP A C     1 
ATOM   5295  O  O     . ASP A 1 666 ? 172.079 181.327 223.131 1.00 125.70 ?  685 ASP A O     1 
ATOM   5296  C  CB    . ASP A 1 666 ? 174.003 180.914 220.815 1.00 126.41 ?  685 ASP A CB    1 
ATOM   5297  C  CG    . ASP A 1 666 ? 175.263 181.076 219.988 1.00 126.68 ?  685 ASP A CG    1 
ATOM   5298  O  OD1   . ASP A 1 666 ? 175.508 182.195 219.492 1.00 125.93 ?  685 ASP A OD1   1 
ATOM   5299  O  OD2   . ASP A 1 666 ? 176.007 180.085 219.832 1.00 127.03 -1 685 ASP A OD2   1 
ATOM   5300  N  N     . THR A 1 667 ? 171.191 182.728 221.589 1.00 125.61 ?  686 THR A N     1 
ATOM   5301  C  CA    . THR A 1 667 ? 169.847 182.643 222.153 1.00 125.26 ?  686 THR A CA    1 
ATOM   5302  C  C     . THR A 1 667 ? 169.292 181.227 222.058 1.00 123.91 ?  686 THR A C     1 
ATOM   5303  O  O     . THR A 1 667 ? 168.654 180.739 222.998 1.00 122.88 ?  686 THR A O     1 
ATOM   5304  C  CB    . THR A 1 667 ? 168.915 183.630 221.449 1.00 126.10 ?  686 THR A CB    1 
ATOM   5305  O  OG1   . THR A 1 667 ? 168.820 183.293 220.059 1.00 127.35 ?  686 THR A OG1   1 
ATOM   5306  C  CG2   . THR A 1 667 ? 169.442 185.051 221.588 1.00 125.18 ?  686 THR A CG2   1 
ATOM   5307  N  N     . GLU A 1 668 ? 169.516 180.554 220.927 1.00 120.28 ?  687 GLU A N     1 
ATOM   5308  C  CA    . GLU A 1 668 ? 169.032 179.185 220.773 1.00 119.56 ?  687 GLU A CA    1 
ATOM   5309  C  C     . GLU A 1 668 ? 169.716 178.242 221.756 1.00 120.11 ?  687 GLU A C     1 
ATOM   5310  O  O     . GLU A 1 668 ? 169.064 177.375 222.353 1.00 119.77 ?  687 GLU A O     1 
ATOM   5311  C  CB    . GLU A 1 668 ? 169.246 178.710 219.335 1.00 118.36 ?  687 GLU A CB    1 
ATOM   5312  C  CG    . GLU A 1 668 ? 168.390 179.432 218.305 1.00 119.65 ?  687 GLU A CG    1 
ATOM   5313  C  CD    . GLU A 1 668 ? 168.991 180.753 217.862 1.00 120.94 ?  687 GLU A CD    1 
ATOM   5314  O  OE1   . GLU A 1 668 ? 170.110 181.080 218.310 1.00 120.42 ?  687 GLU A OE1   1 
ATOM   5315  O  OE2   . GLU A 1 668 ? 168.343 181.464 217.065 1.00 120.48 -1 687 GLU A OE2   1 
ATOM   5316  N  N     . ILE A 1 669 ? 171.029 178.396 221.937 1.00 117.97 ?  688 ILE A N     1 
ATOM   5317  C  CA    . ILE A 1 669 ? 171.750 177.569 222.900 1.00 117.54 ?  688 ILE A CA    1 
ATOM   5318  C  C     . ILE A 1 669 ? 171.236 177.824 224.311 1.00 117.05 ?  688 ILE A C     1 
ATOM   5319  O  O     . ILE A 1 669 ? 171.056 176.889 225.099 1.00 116.66 ?  688 ILE A O     1 
ATOM   5320  C  CB    . ILE A 1 669 ? 173.266 177.819 222.789 1.00 117.03 ?  688 ILE A CB    1 
ATOM   5321  C  CG1   . ILE A 1 669 ? 173.809 177.226 221.487 1.00 115.99 ?  688 ILE A CG1   1 
ATOM   5322  C  CG2   . ILE A 1 669 ? 174.000 177.235 223.989 1.00 115.61 ?  688 ILE A CG2   1 
ATOM   5323  C  CD1   . ILE A 1 669 ? 175.319 177.251 221.385 1.00 116.60 ?  688 ILE A CD1   1 
ATOM   5324  N  N     . PHE A 1 670 ? 170.991 179.092 224.652 1.00 115.82 ?  689 PHE A N     1 
ATOM   5325  C  CA    . PHE A 1 670 ? 170.468 179.419 225.976 1.00 115.09 ?  689 PHE A CA    1 
ATOM   5326  C  C     . PHE A 1 670 ? 169.082 178.819 226.188 1.00 114.01 ?  689 PHE A C     1 
ATOM   5327  O  O     . PHE A 1 670 ? 168.778 178.300 227.270 1.00 113.52 ?  689 PHE A O     1 
ATOM   5328  C  CB    . PHE A 1 670 ? 170.430 180.936 226.158 1.00 115.30 ?  689 PHE A CB    1 
ATOM   5329  C  CG    . PHE A 1 670 ? 171.760 181.541 226.511 1.00 117.14 ?  689 PHE A CG    1 
ATOM   5330  C  CD1   . PHE A 1 670 ? 172.943 180.967 226.070 1.00 116.54 ?  689 PHE A CD1   1 
ATOM   5331  C  CD2   . PHE A 1 670 ? 171.826 182.698 227.266 1.00 115.98 ?  689 PHE A CD2   1 
ATOM   5332  C  CE1   . PHE A 1 670 ? 174.163 181.526 226.389 1.00 116.69 ?  689 PHE A CE1   1 
ATOM   5333  C  CE2   . PHE A 1 670 ? 173.043 183.263 227.584 1.00 116.79 ?  689 PHE A CE2   1 
ATOM   5334  C  CZ    . PHE A 1 670 ? 174.214 182.676 227.147 1.00 117.93 ?  689 PHE A CZ    1 
ATOM   5335  N  N     . LYS A 1 671 ? 168.225 178.888 225.167 1.00 111.46 ?  690 LYS A N     1 
ATOM   5336  C  CA    . LYS A 1 671 ? 166.895 178.299 225.273 1.00 112.04 ?  690 LYS A CA    1 
ATOM   5337  C  C     . LYS A 1 671 ? 166.973 176.787 225.440 1.00 110.30 ?  690 LYS A C     1 
ATOM   5338  O  O     . LYS A 1 671 ? 166.224 176.204 226.231 1.00 108.92 ?  690 LYS A O     1 
ATOM   5339  C  CB    . LYS A 1 671 ? 166.059 178.663 224.045 1.00 113.17 ?  690 LYS A CB    1 
ATOM   5340  C  CG    . LYS A 1 671 ? 165.624 180.119 224.001 1.00 113.55 ?  690 LYS A CG    1 
ATOM   5341  C  CD    . LYS A 1 671 ? 164.921 180.526 225.286 1.00 111.69 ?  690 LYS A CD    1 
ATOM   5342  C  CE    . LYS A 1 671 ? 164.493 181.984 225.245 1.00 111.19 ?  690 LYS A CE    1 
ATOM   5343  N  NZ    . LYS A 1 671 ? 165.637 182.890 224.951 1.00 111.12 1  690 LYS A NZ    1 
ATOM   5344  N  N     . ARG A 1 672 ? 167.874 176.135 224.702 1.00 105.52 ?  691 ARG A N     1 
ATOM   5345  C  CA    . ARG A 1 672 ? 168.049 174.694 224.857 1.00 106.61 ?  691 ARG A CA    1 
ATOM   5346  C  C     . ARG A 1 672 ? 168.560 174.353 226.251 1.00 105.94 ?  691 ARG A C     1 
ATOM   5347  O  O     . ARG A 1 672 ? 168.142 173.353 226.848 1.00 106.33 ?  691 ARG A O     1 
ATOM   5348  C  CB    . ARG A 1 672 ? 169.001 174.164 223.786 1.00 106.11 ?  691 ARG A CB    1 
ATOM   5349  C  CG    . ARG A 1 672 ? 169.023 172.650 223.669 1.00 108.56 ?  691 ARG A CG    1 
ATOM   5350  C  CD    . ARG A 1 672 ? 169.745 172.210 222.407 1.00 108.81 ?  691 ARG A CD    1 
ATOM   5351  N  NE    . ARG A 1 672 ? 169.078 172.696 221.205 1.00 109.21 ?  691 ARG A NE    1 
ATOM   5352  C  CZ    . ARG A 1 672 ? 169.578 173.614 220.389 1.00 107.32 ?  691 ARG A CZ    1 
ATOM   5353  N  NH1   . ARG A 1 672 ? 170.759 174.168 220.611 1.00 106.53 1  691 ARG A NH1   1 
ATOM   5354  N  NH2   . ARG A 1 672 ? 168.875 173.987 219.324 1.00 106.60 ?  691 ARG A NH2   1 
ATOM   5355  N  N     . ILE A 1 673 ? 169.465 175.176 226.785 1.00 96.79  ?  692 ILE A N     1 
ATOM   5356  C  CA    . ILE A 1 673 ? 169.952 174.983 228.148 1.00 95.73  ?  692 ILE A CA    1 
ATOM   5357  C  C     . ILE A 1 673 ? 168.802 175.082 229.141 1.00 98.45  ?  692 ILE A C     1 
ATOM   5358  O  O     . ILE A 1 673 ? 168.687 174.269 230.065 1.00 101.22 ?  692 ILE A O     1 
ATOM   5359  C  CB    . ILE A 1 673 ? 171.060 176.005 228.464 1.00 97.55  ?  692 ILE A CB    1 
ATOM   5360  C  CG1   . ILE A 1 673 ? 172.378 175.603 227.798 1.00 97.24  ?  692 ILE A CG1   1 
ATOM   5361  C  CG2   . ILE A 1 673 ? 171.241 176.152 229.968 1.00 99.00  ?  692 ILE A CG2   1 
ATOM   5362  C  CD1   . ILE A 1 673 ? 173.126 174.513 228.525 1.00 94.80  ?  692 ILE A CD1   1 
ATOM   5363  N  N     . GLN A 1 674 ? 167.937 176.085 228.967 1.00 99.47  ?  693 GLN A N     1 
ATOM   5364  C  CA    . GLN A 1 674 ? 166.800 176.250 229.869 1.00 99.83  ?  693 GLN A CA    1 
ATOM   5365  C  C     . GLN A 1 674 ? 165.839 175.069 229.773 1.00 97.61  ?  693 GLN A C     1 
ATOM   5366  O  O     . GLN A 1 674 ? 165.339 174.580 230.794 1.00 98.02  ?  693 GLN A O     1 
ATOM   5367  C  CB    . GLN A 1 674 ? 166.074 177.560 229.563 1.00 99.54  ?  693 GLN A CB    1 
ATOM   5368  C  CG    . GLN A 1 674 ? 164.802 177.770 230.368 1.00 98.24  ?  693 GLN A CG    1 
ATOM   5369  C  CD    . GLN A 1 674 ? 163.549 177.599 229.533 1.00 99.15  ?  693 GLN A CD    1 
ATOM   5370  O  OE1   . GLN A 1 674 ? 163.548 177.869 228.332 1.00 101.07 ?  693 GLN A OE1   1 
ATOM   5371  N  NE2   . GLN A 1 674 ? 162.471 177.150 230.167 1.00 97.97  ?  693 GLN A NE2   1 
ATOM   5372  N  N     . ILE A 1 675 ? 165.572 174.596 228.553 1.00 92.10  ?  694 ILE A N     1 
ATOM   5373  C  CA    . ILE A 1 675 ? 164.693 173.442 228.378 1.00 91.26  ?  694 ILE A CA    1 
ATOM   5374  C  C     . ILE A 1 675 ? 165.281 172.214 229.059 1.00 93.54  ?  694 ILE A C     1 
ATOM   5375  O  O     . ILE A 1 675 ? 164.572 171.469 229.746 1.00 96.83  ?  694 ILE A O     1 
ATOM   5376  C  CB    . ILE A 1 675 ? 164.421 173.187 226.883 1.00 93.28  ?  694 ILE A CB    1 
ATOM   5377  C  CG1   . ILE A 1 675 ? 163.717 174.389 226.253 1.00 95.18  ?  694 ILE A CG1   1 
ATOM   5378  C  CG2   . ILE A 1 675 ? 163.594 171.924 226.696 1.00 94.64  ?  694 ILE A CG2   1 
ATOM   5379  C  CD1   . ILE A 1 675 ? 162.370 174.699 226.871 1.00 93.80  ?  694 ILE A CD1   1 
ATOM   5380  N  N     . LEU A 1 676 ? 166.585 171.985 228.885 1.00 91.27  ?  695 LEU A N     1 
ATOM   5381  C  CA    . LEU A 1 676 ? 167.226 170.847 229.535 1.00 90.08  ?  695 LEU A CA    1 
ATOM   5382  C  C     . LEU A 1 676 ? 167.157 170.970 231.053 1.00 87.71  ?  695 LEU A C     1 
ATOM   5383  O  O     . LEU A 1 676 ? 166.861 169.993 231.749 1.00 87.31  ?  695 LEU A O     1 
ATOM   5384  C  CB    . LEU A 1 676 ? 168.676 170.727 229.065 1.00 88.82  ?  695 LEU A CB    1 
ATOM   5385  C  CG    . LEU A 1 676 ? 169.298 169.333 229.142 1.00 89.89  ?  695 LEU A CG    1 
ATOM   5386  C  CD1   . LEU A 1 676 ? 168.816 168.471 227.986 1.00 91.03  ?  695 LEU A CD1   1 
ATOM   5387  C  CD2   . LEU A 1 676 ? 170.816 169.423 229.150 1.00 87.21  ?  695 LEU A CD2   1 
ATOM   5388  N  N     . ARG A 1 677 ? 167.411 172.170 231.581 1.00 80.62  ?  696 ARG A N     1 
ATOM   5389  C  CA    . ARG A 1 677 ? 167.348 172.383 233.024 1.00 80.98  ?  696 ARG A CA    1 
ATOM   5390  C  C     . ARG A 1 677 ? 165.941 172.161 233.564 1.00 84.33  ?  696 ARG A C     1 
ATOM   5391  O  O     . ARG A 1 677 ? 165.780 171.710 234.704 1.00 85.68  ?  696 ARG A O     1 
ATOM   5392  C  CB    . ARG A 1 677 ? 167.833 173.795 233.358 1.00 80.61  ?  696 ARG A CB    1 
ATOM   5393  C  CG    . ARG A 1 677 ? 167.882 174.127 234.842 1.00 81.47  ?  696 ARG A CG    1 
ATOM   5394  C  CD    . ARG A 1 677 ? 169.056 173.445 235.527 1.00 79.57  ?  696 ARG A CD    1 
ATOM   5395  N  NE    . ARG A 1 677 ? 168.935 173.464 236.980 1.00 78.76  ?  696 ARG A NE    1 
ATOM   5396  C  CZ    . ARG A 1 677 ? 168.103 172.702 237.678 1.00 83.75  ?  696 ARG A CZ    1 
ATOM   5397  N  NH1   . ARG A 1 677 ? 167.302 171.830 237.087 1.00 83.47  1  696 ARG A NH1   1 
ATOM   5398  N  NH2   . ARG A 1 677 ? 168.075 172.816 239.003 1.00 84.75  ?  696 ARG A NH2   1 
ATOM   5399  N  N     . ASP A 1 678 ? 164.916 172.464 232.762 1.00 94.11  ?  697 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 678 ? 163.542 172.248 233.207 1.00 94.85  ?  697 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 678 ? 163.234 170.769 233.401 1.00 93.32  ?  697 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 678 ? 162.364 170.417 234.206 1.00 95.33  ?  697 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 678 ? 162.562 172.862 232.207 1.00 95.58  ?  697 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 678 ? 162.598 174.377 232.209 1.00 96.52  ?  697 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 678 ? 162.926 174.965 233.260 1.00 96.54  ?  697 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 678 ? 162.298 174.980 231.157 1.00 96.02  -1 697 ASP A OD2   1 
ATOM   5407  N  N     . MET A 1 679 ? 163.931 169.889 232.678 1.00 90.81  ?  698 MET A N     1 
ATOM   5408  C  CA    . MET A 1 679 ? 163.673 168.456 232.767 1.00 92.13  ?  698 MET A CA    1 
ATOM   5409  C  C     . MET A 1 679 ? 164.165 167.839 234.069 1.00 91.16  ?  698 MET A C     1 
ATOM   5410  O  O     . MET A 1 679 ? 163.842 166.678 234.342 1.00 88.70  ?  698 MET A O     1 
ATOM   5411  C  CB    . MET A 1 679 ? 164.316 167.735 231.583 1.00 90.87  ?  698 MET A CB    1 
ATOM   5412  C  CG    . MET A 1 679 ? 164.094 168.424 230.250 1.00 92.30  ?  698 MET A CG    1 
ATOM   5413  S  SD    . MET A 1 679 ? 165.231 167.870 228.968 1.00 99.37  ?  698 MET A SD    1 
ATOM   5414  C  CE    . MET A 1 679 ? 165.136 166.097 229.183 1.00 92.24  ?  698 MET A CE    1 
ATOM   5415  N  N     . GLY A 1 680 ? 164.929 168.574 234.873 1.00 82.49  ?  699 GLY A N     1 
ATOM   5416  C  CA    . GLY A 1 680 ? 165.441 168.080 236.129 1.00 80.09  ?  699 GLY A CA    1 
ATOM   5417  C  C     . GLY A 1 680 ? 166.897 167.665 236.101 1.00 81.62  ?  699 GLY A C     1 
ATOM   5418  O  O     . GLY A 1 680 ? 167.496 167.493 237.170 1.00 83.88  ?  699 GLY A O     1 
ATOM   5419  N  N     . VAL A 1 681 ? 167.483 167.498 234.915 1.00 72.85  ?  700 VAL A N     1 
ATOM   5420  C  CA    . VAL A 1 681 ? 168.900 167.169 234.828 1.00 67.65  ?  700 VAL A CA    1 
ATOM   5421  C  C     . VAL A 1 681 ? 169.723 168.391 235.213 1.00 67.91  ?  700 VAL A C     1 
ATOM   5422  O  O     . VAL A 1 681 ? 169.487 169.504 234.724 1.00 70.90  ?  700 VAL A O     1 
ATOM   5423  C  CB    . VAL A 1 681 ? 169.255 166.651 233.424 1.00 64.22  ?  700 VAL A CB    1 
ATOM   5424  C  CG1   . VAL A 1 681 ? 168.849 167.645 232.355 1.00 66.74  ?  700 VAL A CG1   1 
ATOM   5425  C  CG2   . VAL A 1 681 ? 170.744 166.350 233.328 1.00 63.89  ?  700 VAL A CG2   1 
ATOM   5426  N  N     . GLY A 1 682 ? 170.680 168.193 236.111 1.00 52.59  ?  701 GLY A N     1 
ATOM   5427  C  CA    . GLY A 1 682 ? 171.484 169.286 236.609 1.00 47.21  ?  701 GLY A CA    1 
ATOM   5428  C  C     . GLY A 1 682 ? 172.452 169.809 235.566 1.00 48.95  ?  701 GLY A C     1 
ATOM   5429  O  O     . GLY A 1 682 ? 172.628 169.253 234.481 1.00 57.88  ?  701 GLY A O     1 
ATOM   5430  N  N     . LEU A 1 683 ? 173.103 170.914 235.918 1.00 52.08  ?  702 LEU A N     1 
ATOM   5431  C  CA    . LEU A 1 683 ? 174.057 171.551 235.025 1.00 53.31  ?  702 LEU A CA    1 
ATOM   5432  C  C     . LEU A 1 683 ? 175.235 172.056 235.842 1.00 54.64  ?  702 LEU A C     1 
ATOM   5433  O  O     . LEU A 1 683 ? 175.058 172.606 236.933 1.00 62.09  ?  702 LEU A O     1 
ATOM   5434  C  CB    . LEU A 1 683 ? 173.412 172.698 234.238 1.00 52.42  ?  702 LEU A CB    1 
ATOM   5435  C  CG    . LEU A 1 683 ? 174.140 173.149 232.970 1.00 53.90  ?  702 LEU A CG    1 
ATOM   5436  C  CD1   . LEU A 1 683 ? 174.460 171.959 232.084 1.00 56.30  ?  702 LEU A CD1   1 
ATOM   5437  C  CD2   . LEU A 1 683 ? 173.298 174.155 232.211 1.00 56.31  ?  702 LEU A CD2   1 
ATOM   5438  N  N     . SER A 1 684 ? 176.435 171.853 235.307 1.00 47.70  ?  703 SER A N     1 
ATOM   5439  C  CA    . SER A 1 684 ? 177.666 172.261 235.961 1.00 48.27  ?  703 SER A CA    1 
ATOM   5440  C  C     . SER A 1 684 ? 178.533 173.026 234.974 1.00 46.56  ?  703 SER A C     1 
ATOM   5441  O  O     . SER A 1 684 ? 178.531 172.749 233.772 1.00 51.79  ?  703 SER A O     1 
ATOM   5442  C  CB    . SER A 1 684 ? 178.439 171.054 236.508 1.00 54.58  ?  703 SER A CB    1 
ATOM   5443  O  OG    . SER A 1 684 ? 179.636 171.463 237.146 1.00 53.30  ?  703 SER A OG    1 
ATOM   5444  N  N     . VAL A 1 685 ? 179.275 173.995 235.497 1.00 64.63  ?  704 VAL A N     1 
ATOM   5445  C  CA    . VAL A 1 685 ? 180.185 174.811 234.700 1.00 67.48  ?  704 VAL A CA    1 
ATOM   5446  C  C     . VAL A 1 685 ? 181.569 174.733 235.327 1.00 70.99  ?  704 VAL A C     1 
ATOM   5447  O  O     . VAL A 1 685 ? 181.736 175.027 236.517 1.00 73.60  ?  704 VAL A O     1 
ATOM   5448  C  CB    . VAL A 1 685 ? 179.708 176.267 234.593 1.00 72.02  ?  704 VAL A CB    1 
ATOM   5449  C  CG1   . VAL A 1 685 ? 180.800 177.141 233.997 1.00 71.13  ?  704 VAL A CG1   1 
ATOM   5450  C  CG2   . VAL A 1 685 ? 178.456 176.338 233.738 1.00 71.06  ?  704 VAL A CG2   1 
ATOM   5451  N  N     . ASP A 1 686 ? 182.555 174.333 234.529 1.00 82.36  ?  705 ASP A N     1 
ATOM   5452  C  CA    . ASP A 1 686 ? 183.933 174.208 234.976 1.00 83.77  ?  705 ASP A CA    1 
ATOM   5453  C  C     . ASP A 1 686 ? 184.757 175.392 234.484 1.00 86.79  ?  705 ASP A C     1 
ATOM   5454  O  O     . ASP A 1 686 ? 184.401 176.055 233.506 1.00 87.96  ?  705 ASP A O     1 
ATOM   5455  C  CB    . ASP A 1 686 ? 184.552 172.899 234.478 1.00 81.40  ?  705 ASP A CB    1 
ATOM   5456  C  CG    . ASP A 1 686 ? 185.787 172.500 235.264 1.00 84.68  ?  705 ASP A CG    1 
ATOM   5457  O  OD1   . ASP A 1 686 ? 186.167 173.240 236.196 1.00 88.38  ?  705 ASP A OD1   1 
ATOM   5458  O  OD2   . ASP A 1 686 ? 186.378 171.446 234.949 1.00 83.38  -1 705 ASP A OD2   1 
ATOM   5459  N  N     . ASP A 1 687 ? 185.859 175.655 235.192 1.00 91.19  ?  706 ASP A N     1 
ATOM   5460  C  CA    . ASP A 1 687 ? 186.783 176.747 234.894 1.00 92.71  ?  706 ASP A CA    1 
ATOM   5461  C  C     . ASP A 1 687 ? 186.124 178.108 235.090 1.00 90.59  ?  706 ASP A C     1 
ATOM   5462  O  O     . ASP A 1 687 ? 184.894 178.213 235.155 1.00 86.57  ?  706 ASP A O     1 
ATOM   5463  C  CB    . ASP A 1 687 ? 187.342 176.621 233.473 1.00 92.34  ?  706 ASP A CB    1 
ATOM   5464  C  CG    . ASP A 1 687 ? 188.065 175.309 233.247 1.00 91.19  ?  706 ASP A CG    1 
ATOM   5465  O  OD1   . ASP A 1 687 ? 188.045 174.454 234.157 1.00 88.95  ?  706 ASP A OD1   1 
ATOM   5466  O  OD2   . ASP A 1 687 ? 188.654 175.132 232.160 1.00 90.69  -1 706 ASP A OD2   1 
ATOM   5467  N  N     . PHE A 1 688 ? 186.936 179.159 235.192 1.00 97.40  ?  707 PHE A N     1 
ATOM   5468  C  CA    . PHE A 1 688 ? 186.446 180.503 235.471 1.00 100.11 ?  707 PHE A CA    1 
ATOM   5469  C  C     . PHE A 1 688 ? 186.905 181.499 234.412 1.00 101.50 ?  707 PHE A C     1 
ATOM   5470  O  O     . PHE A 1 688 ? 187.165 182.665 234.716 1.00 100.70 ?  707 PHE A O     1 
ATOM   5471  C  CB    . PHE A 1 688 ? 186.881 180.952 236.865 1.00 99.28  ?  707 PHE A CB    1 
ATOM   5472  C  CG    . PHE A 1 688 ? 186.587 179.945 237.939 1.00 99.17  ?  707 PHE A CG    1 
ATOM   5473  C  CD1   . PHE A 1 688 ? 185.334 179.362 238.033 1.00 98.72  ?  707 PHE A CD1   1 
ATOM   5474  C  CD2   . PHE A 1 688 ? 187.566 179.567 238.840 1.00 97.89  ?  707 PHE A CD2   1 
ATOM   5475  C  CE1   . PHE A 1 688 ? 185.061 178.429 239.011 1.00 98.38  ?  707 PHE A CE1   1 
ATOM   5476  C  CE2   . PHE A 1 688 ? 187.298 178.633 239.822 1.00 96.84  ?  707 PHE A CE2   1 
ATOM   5477  C  CZ    . PHE A 1 688 ? 186.044 178.063 239.905 1.00 98.15  ?  707 PHE A CZ    1 
ATOM   5478  N  N     . GLY A 1 689 ? 187.017 181.046 233.161 1.00 117.81 ?  708 GLY A N     1 
ATOM   5479  C  CA    . GLY A 1 689 ? 187.315 181.965 232.077 1.00 116.99 ?  708 GLY A CA    1 
ATOM   5480  C  C     . GLY A 1 689 ? 186.233 183.008 231.883 1.00 117.77 ?  708 GLY A C     1 
ATOM   5481  O  O     . GLY A 1 689 ? 186.531 184.181 231.645 1.00 116.38 ?  708 GLY A O     1 
ATOM   5482  N  N     . THR A 1 690 ? 184.970 182.599 231.978 1.00 120.00 ?  709 THR A N     1 
ATOM   5483  C  CA    . THR A 1 690 ? 183.862 183.541 231.939 1.00 119.12 ?  709 THR A CA    1 
ATOM   5484  C  C     . THR A 1 690 ? 183.859 184.395 233.199 1.00 117.98 ?  709 THR A C     1 
ATOM   5485  O  O     . THR A 1 690 ? 184.202 183.924 234.288 1.00 117.92 ?  709 THR A O     1 
ATOM   5486  C  CB    . THR A 1 690 ? 182.529 182.804 231.803 1.00 118.72 ?  709 THR A CB    1 
ATOM   5487  O  OG1   . THR A 1 690 ? 182.525 181.657 232.661 1.00 119.95 ?  709 THR A OG1   1 
ATOM   5488  C  CG2   . THR A 1 690 ? 182.311 182.359 230.365 1.00 117.85 ?  709 THR A CG2   1 
ATOM   5489  N  N     . GLY A 1 691 ? 183.467 185.654 233.047 1.00 113.55 ?  710 GLY A N     1 
ATOM   5490  C  CA    . GLY A 1 691 ? 183.502 186.582 234.154 1.00 113.05 ?  710 GLY A CA    1 
ATOM   5491  C  C     . GLY A 1 691 ? 182.348 186.398 235.119 1.00 113.30 ?  710 GLY A C     1 
ATOM   5492  O  O     . GLY A 1 691 ? 181.464 185.561 234.943 1.00 114.09 ?  710 GLY A O     1 
ATOM   5493  N  N     . PHE A 1 692 ? 182.368 187.210 236.180 1.00 103.16 ?  711 PHE A N     1 
ATOM   5494  C  CA    . PHE A 1 692 ? 181.292 187.162 237.161 1.00 103.55 ?  711 PHE A CA    1 
ATOM   5495  C  C     . PHE A 1 692 ? 179.989 187.729 236.612 1.00 102.95 ?  711 PHE A C     1 
ATOM   5496  O  O     . PHE A 1 692 ? 178.913 187.327 237.064 1.00 102.36 ?  711 PHE A O     1 
ATOM   5497  C  CB    . PHE A 1 692 ? 181.697 187.901 238.437 1.00 104.70 ?  711 PHE A CB    1 
ATOM   5498  C  CG    . PHE A 1 692 ? 180.769 187.661 239.592 1.00 106.04 ?  711 PHE A CG    1 
ATOM   5499  C  CD1   . PHE A 1 692 ? 180.133 186.439 239.740 1.00 105.06 ?  711 PHE A CD1   1 
ATOM   5500  C  CD2   . PHE A 1 692 ? 180.538 188.648 240.534 1.00 104.47 ?  711 PHE A CD2   1 
ATOM   5501  C  CE1   . PHE A 1 692 ? 179.276 186.210 240.795 1.00 103.62 ?  711 PHE A CE1   1 
ATOM   5502  C  CE2   . PHE A 1 692 ? 179.684 188.423 241.597 1.00 104.02 ?  711 PHE A CE2   1 
ATOM   5503  C  CZ    . PHE A 1 692 ? 179.052 187.201 241.727 1.00 103.87 ?  711 PHE A CZ    1 
ATOM   5504  N  N     . SER A 1 693 ? 180.056 188.644 235.643 1.00 107.20 ?  712 SER A N     1 
ATOM   5505  C  CA    . SER A 1 693 ? 178.846 189.025 234.923 1.00 108.56 ?  712 SER A CA    1 
ATOM   5506  C  C     . SER A 1 693 ? 178.263 187.826 234.187 1.00 107.55 ?  712 SER A C     1 
ATOM   5507  O  O     . SER A 1 693 ? 177.043 187.615 234.187 1.00 106.40 ?  712 SER A O     1 
ATOM   5508  C  CB    . SER A 1 693 ? 179.149 190.165 233.951 1.00 108.02 ?  712 SER A CB    1 
ATOM   5509  O  OG    . SER A 1 693 ? 177.977 190.588 233.277 1.00 108.45 ?  712 SER A OG    1 
ATOM   5510  N  N     . GLY A 1 694 ? 179.127 187.020 233.567 1.00 114.38 ?  713 GLY A N     1 
ATOM   5511  C  CA    . GLY A 1 694 ? 178.675 185.773 232.977 1.00 113.11 ?  713 GLY A CA    1 
ATOM   5512  C  C     . GLY A 1 694 ? 178.119 184.805 234.001 1.00 113.99 ?  713 GLY A C     1 
ATOM   5513  O  O     . GLY A 1 694 ? 177.161 184.086 233.722 1.00 114.02 ?  713 GLY A O     1 
ATOM   5514  N  N     . LEU A 1 695 ? 178.698 184.782 235.204 1.00 112.96 ?  714 LEU A N     1 
ATOM   5515  C  CA    . LEU A 1 695 ? 178.175 183.913 236.255 1.00 112.59 ?  714 LEU A CA    1 
ATOM   5516  C  C     . LEU A 1 695 ? 176.806 184.374 236.744 1.00 111.96 ?  714 LEU A C     1 
ATOM   5517  O  O     . LEU A 1 695 ? 175.960 183.545 237.083 1.00 109.05 ?  714 LEU A O     1 
ATOM   5518  C  CB    . LEU A 1 695 ? 179.161 183.837 237.420 1.00 110.79 ?  714 LEU A CB    1 
ATOM   5519  C  CG    . LEU A 1 695 ? 180.556 183.309 237.080 1.00 109.38 ?  714 LEU A CG    1 
ATOM   5520  C  CD1   . LEU A 1 695 ? 181.383 183.115 238.341 1.00 109.19 ?  714 LEU A CD1   1 
ATOM   5521  C  CD2   . LEU A 1 695 ? 180.463 182.011 236.290 1.00 108.20 ?  714 LEU A CD2   1 
ATOM   5522  N  N     . SER A 1 696 ? 176.567 185.684 236.789 1.00 112.44 ?  715 SER A N     1 
ATOM   5523  C  CA    . SER A 1 696 ? 175.241 186.175 237.159 1.00 110.54 ?  715 SER A CA    1 
ATOM   5524  C  C     . SER A 1 696 ? 174.225 185.897 236.057 1.00 110.04 ?  715 SER A C     1 
ATOM   5525  O  O     . SER A 1 696 ? 173.072 185.537 236.334 1.00 109.22 ?  715 SER A O     1 
ATOM   5526  C  CB    . SER A 1 696 ? 175.308 187.666 237.474 1.00 110.29 ?  715 SER A CB    1 
ATOM   5527  O  OG    . SER A 1 696 ? 176.179 187.896 238.565 1.00 109.89 ?  715 SER A OG    1 
ATOM   5528  N  N     . ARG A 1 697 ? 174.634 186.057 234.797 1.00 114.66 ?  716 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 697 ? 173.798 185.596 233.694 1.00 115.06 ?  716 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 697 ? 173.533 184.098 233.798 1.00 116.04 ?  716 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 697 ? 172.460 183.624 233.413 1.00 117.27 ?  716 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 697 ? 174.465 185.953 232.364 1.00 116.51 ?  716 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 697 ? 173.713 185.513 231.122 1.00 116.40 ?  716 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 697 ? 174.256 184.194 230.603 1.00 116.67 ?  716 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 697 ? 175.707 184.225 230.464 1.00 116.86 ?  716 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 697 ? 176.349 184.738 229.424 1.00 118.09 ?  716 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 697 ? 177.671 184.734 229.358 1.00 118.31 1  716 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 697 ? 175.649 185.270 228.427 1.00 117.89 ?  716 ARG A NH2   1 
ATOM   5539  N  N     . LEU A 1 698 ? 174.492 183.343 234.335 1.00 110.81 ?  717 LEU A N     1 
ATOM   5540  C  CA    . LEU A 1 698 ? 174.297 181.917 234.566 1.00 111.25 ?  717 LEU A CA    1 
ATOM   5541  C  C     . LEU A 1 698 ? 173.331 181.660 235.715 1.00 110.99 ?  717 LEU A C     1 
ATOM   5542  O  O     . LEU A 1 698 ? 172.637 180.640 235.727 1.00 110.86 ?  717 LEU A O     1 
ATOM   5543  C  CB    . LEU A 1 698 ? 175.644 181.258 234.847 1.00 110.79 ?  717 LEU A CB    1 
ATOM   5544  C  CG    . LEU A 1 698 ? 175.672 179.736 234.828 1.00 109.40 ?  717 LEU A CG    1 
ATOM   5545  C  CD1   . LEU A 1 698 ? 175.291 179.243 233.449 1.00 109.13 ?  717 LEU A CD1   1 
ATOM   5546  C  CD2   . LEU A 1 698 ? 177.045 179.237 235.232 1.00 107.31 ?  717 LEU A CD2   1 
ATOM   5547  N  N     . VAL A 1 699 ? 173.308 182.544 236.709 1.00 111.21 ?  718 VAL A N     1 
ATOM   5548  C  CA    . VAL A 1 699 ? 172.276 182.469 237.739 1.00 112.16 ?  718 VAL A CA    1 
ATOM   5549  C  C     . VAL A 1 699 ? 170.906 182.688 237.115 1.00 112.21 ?  718 VAL A C     1 
ATOM   5550  O  O     . VAL A 1 699 ? 169.927 182.015 237.462 1.00 112.02 ?  718 VAL A O     1 
ATOM   5551  C  CB    . VAL A 1 699 ? 172.555 183.485 238.861 1.00 112.18 ?  718 VAL A CB    1 
ATOM   5552  C  CG1   . VAL A 1 699 ? 171.520 183.351 239.966 1.00 112.22 ?  718 VAL A CG1   1 
ATOM   5553  C  CG2   . VAL A 1 699 ? 173.951 183.286 239.413 1.00 110.63 ?  718 VAL A CG2   1 
ATOM   5554  N  N     . SER A 1 700 ? 170.818 183.641 236.186 1.00 110.30 ?  719 SER A N     1 
ATOM   5555  C  CA    . SER A 1 700 ? 169.569 183.857 235.458 1.00 112.17 ?  719 SER A CA    1 
ATOM   5556  C  C     . SER A 1 700 ? 169.182 182.624 234.646 1.00 113.48 ?  719 SER A C     1 
ATOM   5557  O  O     . SER A 1 700 ? 168.008 182.235 234.612 1.00 111.78 ?  719 SER A O     1 
ATOM   5558  C  CB    . SER A 1 700 ? 169.695 185.080 234.551 1.00 110.48 ?  719 SER A CB    1 
ATOM   5559  O  OG    . SER A 1 700 ? 168.535 185.246 233.754 1.00 110.40 ?  719 SER A OG    1 
ATOM   5560  N  N     . LEU A 1 701 ? 170.155 182.001 233.983 1.00 108.50 ?  720 LEU A N     1 
ATOM   5561  C  CA    . LEU A 1 701 ? 169.954 180.775 233.217 1.00 105.97 ?  720 LEU A CA    1 
ATOM   5562  C  C     . LEU A 1 701 ? 170.380 179.584 234.069 1.00 103.40 ?  720 LEU A C     1 
ATOM   5563  O  O     . LEU A 1 701 ? 171.530 179.136 233.980 1.00 98.77  ?  720 LEU A O     1 
ATOM   5564  C  CB    . LEU A 1 701 ? 170.745 180.835 231.909 1.00 104.16 ?  720 LEU A CB    1 
ATOM   5565  C  CG    . LEU A 1 701 ? 170.589 179.702 230.896 1.00 104.92 ?  720 LEU A CG    1 
ATOM   5566  C  CD1   . LEU A 1 701 ? 169.260 179.818 230.172 1.00 105.67 ?  720 LEU A CD1   1 
ATOM   5567  C  CD2   . LEU A 1 701 ? 171.744 179.734 229.908 1.00 104.99 ?  720 LEU A CD2   1 
ATOM   5568  N  N     . PRO A 1 702 ? 169.456 178.996 234.831 1.00 98.32  ?  721 PRO A N     1 
ATOM   5569  C  CA    . PRO A 1 702 ? 169.838 178.273 236.055 1.00 96.46  ?  721 PRO A CA    1 
ATOM   5570  C  C     . PRO A 1 702 ? 170.789 177.107 235.817 1.00 95.12  ?  721 PRO A C     1 
ATOM   5571  O  O     . PRO A 1 702 ? 170.712 176.406 234.806 1.00 96.88  ?  721 PRO A O     1 
ATOM   5572  C  CB    . PRO A 1 702 ? 168.494 177.783 236.609 1.00 97.78  ?  721 PRO A CB    1 
ATOM   5573  C  CG    . PRO A 1 702 ? 167.557 177.813 235.446 1.00 96.43  ?  721 PRO A CG    1 
ATOM   5574  C  CD    . PRO A 1 702 ? 168.006 178.946 234.583 1.00 97.58  ?  721 PRO A CD    1 
ATOM   5575  N  N     . VAL A 1 703 ? 171.697 176.918 236.775 1.00 78.35  ?  722 VAL A N     1 
ATOM   5576  C  CA    . VAL A 1 703 ? 172.579 175.762 236.863 1.00 73.41  ?  722 VAL A CA    1 
ATOM   5577  C  C     . VAL A 1 703 ? 172.573 175.273 238.307 1.00 73.97  ?  722 VAL A C     1 
ATOM   5578  O  O     . VAL A 1 703 ? 171.869 175.812 239.165 1.00 81.12  ?  722 VAL A O     1 
ATOM   5579  C  CB    . VAL A 1 703 ? 174.018 176.078 236.410 1.00 70.54  ?  722 VAL A CB    1 
ATOM   5580  C  CG1   . VAL A 1 703 ? 174.054 176.347 234.925 1.00 76.30  ?  722 VAL A CG1   1 
ATOM   5581  C  CG2   . VAL A 1 703 ? 174.569 177.258 237.192 1.00 70.40  ?  722 VAL A CG2   1 
ATOM   5582  N  N     . THR A 1 704 ? 173.365 174.238 238.575 1.00 59.89  ?  723 THR A N     1 
ATOM   5583  C  CA    . THR A 1 704 ? 173.458 173.674 239.913 1.00 57.58  ?  723 THR A CA    1 
ATOM   5584  C  C     . THR A 1 704 ? 174.872 173.604 240.466 1.00 58.29  ?  723 THR A C     1 
ATOM   5585  O  O     . THR A 1 704 ? 175.044 173.739 241.679 1.00 61.52  ?  723 THR A O     1 
ATOM   5586  C  CB    . THR A 1 704 ? 172.854 172.260 239.949 1.00 60.22  ?  723 THR A CB    1 
ATOM   5587  O  OG1   . THR A 1 704 ? 173.685 171.363 239.200 1.00 66.21  ?  723 THR A OG1   1 
ATOM   5588  C  CG2   . THR A 1 704 ? 171.445 172.256 239.368 1.00 62.55  ?  723 THR A CG2   1 
ATOM   5589  N  N     . GLU A 1 705 ? 175.888 173.398 239.626 1.00 58.13  ?  724 GLU A N     1 
ATOM   5590  C  CA    . GLU A 1 705 ? 177.236 173.148 240.115 1.00 58.74  ?  724 GLU A CA    1 
ATOM   5591  C  C     . GLU A 1 705 ? 178.256 174.034 239.414 1.00 58.02  ?  724 GLU A C     1 
ATOM   5592  O  O     . GLU A 1 705 ? 178.186 174.251 238.199 1.00 58.97  ?  724 GLU A O     1 
ATOM   5593  C  CB    . GLU A 1 705 ? 177.622 171.675 239.930 1.00 62.31  ?  724 GLU A CB    1 
ATOM   5594  C  CG    . GLU A 1 705 ? 176.660 170.695 240.581 1.00 61.11  ?  724 GLU A CG    1 
ATOM   5595  C  CD    . GLU A 1 705 ? 176.819 169.284 240.053 1.00 65.51  ?  724 GLU A CD    1 
ATOM   5596  O  OE1   . GLU A 1 705 ? 177.813 169.020 239.345 1.00 64.15  ?  724 GLU A OE1   1 
ATOM   5597  O  OE2   . GLU A 1 705 ? 175.947 168.438 240.344 1.00 68.58  -1 724 GLU A OE2   1 
ATOM   5598  N  N     . ILE A 1 706 ? 179.218 174.526 240.191 1.00 62.97  ?  725 ILE A N     1 
ATOM   5599  C  CA    . ILE A 1 706 ? 180.367 175.258 239.672 1.00 62.85  ?  725 ILE A CA    1 
ATOM   5600  C  C     . ILE A 1 706 ? 181.624 174.530 240.125 1.00 61.13  ?  725 ILE A C     1 
ATOM   5601  O  O     . ILE A 1 706 ? 181.769 174.217 241.311 1.00 62.61  ?  725 ILE A O     1 
ATOM   5602  C  CB    . ILE A 1 706 ? 180.380 176.725 240.148 1.00 69.05  ?  725 ILE A CB    1 
ATOM   5603  C  CG1   . ILE A 1 706 ? 179.462 177.578 239.271 1.00 70.92  ?  725 ILE A CG1   1 
ATOM   5604  C  CG2   . ILE A 1 706 ? 181.792 177.288 240.131 1.00 67.47  ?  725 ILE A CG2   1 
ATOM   5605  C  CD1   . ILE A 1 706 ? 179.433 179.039 239.660 1.00 66.19  ?  725 ILE A CD1   1 
ATOM   5606  N  N     . LYS A 1 707 ? 182.525 174.257 239.186 1.00 65.02  ?  726 LYS A N     1 
ATOM   5607  C  CA    . LYS A 1 707 ? 183.715 173.459 239.445 1.00 68.37  ?  726 LYS A CA    1 
ATOM   5608  C  C     . LYS A 1 707 ? 184.947 174.352 239.488 1.00 66.94  ?  726 LYS A C     1 
ATOM   5609  O  O     . LYS A 1 707 ? 185.146 175.189 238.602 1.00 69.33  ?  726 LYS A O     1 
ATOM   5610  C  CB    . LYS A 1 707 ? 183.891 172.376 238.377 1.00 68.00  ?  726 LYS A CB    1 
ATOM   5611  C  CG    . LYS A 1 707 ? 183.022 171.150 238.585 1.00 68.09  ?  726 LYS A CG    1 
ATOM   5612  C  CD    . LYS A 1 707 ? 182.979 170.286 237.338 1.00 70.44  ?  726 LYS A CD    1 
ATOM   5613  C  CE    . LYS A 1 707 ? 182.377 168.924 237.637 1.00 71.50  ?  726 LYS A CE    1 
ATOM   5614  N  NZ    . LYS A 1 707 ? 183.223 167.818 237.114 1.00 70.70  1  726 LYS A NZ    1 
ATOM   5615  N  N     . ILE A 1 708 ? 185.766 174.167 240.517 1.00 65.37  ?  727 ILE A N     1 
ATOM   5616  C  CA    . ILE A 1 708 ? 187.055 174.838 240.627 1.00 64.80  ?  727 ILE A CA    1 
ATOM   5617  C  C     . ILE A 1 708 ? 188.099 173.942 239.976 1.00 64.88  ?  727 ILE A C     1 
ATOM   5618  O  O     . ILE A 1 708 ? 188.276 172.786 240.380 1.00 67.45  ?  727 ILE A O     1 
ATOM   5619  C  CB    . ILE A 1 708 ? 187.414 175.132 242.090 1.00 67.91  ?  727 ILE A CB    1 
ATOM   5620  C  CG1   . ILE A 1 708 ? 186.324 175.975 242.751 1.00 70.75  ?  727 ILE A CG1   1 
ATOM   5621  C  CG2   . ILE A 1 708 ? 188.736 175.873 242.168 1.00 68.70  ?  727 ILE A CG2   1 
ATOM   5622  C  CD1   . ILE A 1 708 ? 186.572 176.239 244.216 1.00 72.21  ?  727 ILE A CD1   1 
ATOM   5623  N  N     . ASP A 1 709 ? 188.788 174.482 238.974 1.00 74.41  ?  728 ASP A N     1 
ATOM   5624  C  CA    . ASP A 1 709 ? 189.664 173.691 238.123 1.00 74.89  ?  728 ASP A CA    1 
ATOM   5625  C  C     . ASP A 1 709 ? 190.951 173.309 238.847 1.00 77.74  ?  728 ASP A C     1 
ATOM   5626  O  O     . ASP A 1 709 ? 191.405 173.994 239.770 1.00 83.76  ?  728 ASP A O     1 
ATOM   5627  C  CB    . ASP A 1 709 ? 189.998 174.465 236.845 1.00 74.79  ?  728 ASP A CB    1 
ATOM   5628  C  CG    . ASP A 1 709 ? 190.620 173.590 235.772 1.00 78.87  ?  728 ASP A CG    1 
ATOM   5629  O  OD1   . ASP A 1 709 ? 190.740 172.366 235.988 1.00 82.07  ?  728 ASP A OD1   1 
ATOM   5630  O  OD2   . ASP A 1 709 ? 190.990 174.128 234.707 1.00 78.73  -1 728 ASP A OD2   1 
ATOM   5631  N  N     . LYS A 1 710 ? 191.545 172.200 238.400 1.00 73.27  ?  729 LYS A N     1 
ATOM   5632  C  CA    . LYS A 1 710 ? 192.810 171.746 238.966 1.00 75.34  ?  729 LYS A CA    1 
ATOM   5633  C  C     . LYS A 1 710 ? 193.920 172.764 238.744 1.00 77.80  ?  729 LYS A C     1 
ATOM   5634  O  O     . LYS A 1 710 ? 194.800 172.916 239.598 1.00 80.57  ?  729 LYS A O     1 
ATOM   5635  C  CB    . LYS A 1 710 ? 193.190 170.392 238.361 1.00 76.64  ?  729 LYS A CB    1 
ATOM   5636  C  CG    . LYS A 1 710 ? 194.618 169.947 238.635 1.00 74.73  ?  729 LYS A CG    1 
ATOM   5637  C  CD    . LYS A 1 710 ? 194.851 168.526 238.152 1.00 76.06  ?  729 LYS A CD    1 
ATOM   5638  C  CE    . LYS A 1 710 ? 196.310 168.124 238.303 1.00 76.14  ?  729 LYS A CE    1 
ATOM   5639  N  NZ    . LYS A 1 710 ? 196.785 168.267 239.706 1.00 78.01  1  729 LYS A NZ    1 
ATOM   5640  N  N     . SER A 1 711 ? 193.891 173.478 237.615 1.00 77.71  ?  730 SER A N     1 
ATOM   5641  C  CA    . SER A 1 711 ? 194.914 174.484 237.348 1.00 77.69  ?  730 SER A CA    1 
ATOM   5642  C  C     . SER A 1 711 ? 194.909 175.584 238.400 1.00 76.84  ?  730 SER A C     1 
ATOM   5643  O  O     . SER A 1 711 ? 195.964 176.149 238.712 1.00 79.77  ?  730 SER A O     1 
ATOM   5644  C  CB    . SER A 1 711 ? 194.714 175.081 235.955 1.00 77.63  ?  730 SER A CB    1 
ATOM   5645  O  OG    . SER A 1 711 ? 194.826 174.085 234.952 1.00 80.86  ?  730 SER A OG    1 
ATOM   5646  N  N     . PHE A 1 712 ? 193.741 175.903 238.957 1.00 80.79  ?  731 PHE A N     1 
ATOM   5647  C  CA    . PHE A 1 712 ? 193.652 176.890 240.025 1.00 81.19  ?  731 PHE A CA    1 
ATOM   5648  C  C     . PHE A 1 712 ? 193.890 176.276 241.399 1.00 81.78  ?  731 PHE A C     1 
ATOM   5649  O  O     . PHE A 1 712 ? 194.507 176.910 242.262 1.00 88.93  ?  731 PHE A O     1 
ATOM   5650  C  CB    . PHE A 1 712 ? 192.287 177.583 239.992 1.00 82.38  ?  731 PHE A CB    1 
ATOM   5651  C  CG    . PHE A 1 712 ? 192.167 178.635 238.925 1.00 86.94  ?  731 PHE A CG    1 
ATOM   5652  C  CD1   . PHE A 1 712 ? 193.255 178.972 238.137 1.00 87.75  ?  731 PHE A CD1   1 
ATOM   5653  C  CD2   . PHE A 1 712 ? 190.966 179.292 238.714 1.00 86.53  ?  731 PHE A CD2   1 
ATOM   5654  C  CE1   . PHE A 1 712 ? 193.148 179.940 237.157 1.00 87.38  ?  731 PHE A CE1   1 
ATOM   5655  C  CE2   . PHE A 1 712 ? 190.852 180.262 237.735 1.00 86.61  ?  731 PHE A CE2   1 
ATOM   5656  C  CZ    . PHE A 1 712 ? 191.945 180.586 236.956 1.00 86.78  ?  731 PHE A CZ    1 
ATOM   5657  N  N     . VAL A 1 713 ? 193.419 175.047 241.620 1.00 76.90  ?  732 VAL A N     1 
ATOM   5658  C  CA    . VAL A 1 713 ? 193.617 174.412 242.919 1.00 80.42  ?  732 VAL A CA    1 
ATOM   5659  C  C     . VAL A 1 713 ? 195.098 174.130 243.160 1.00 81.47  ?  732 VAL A C     1 
ATOM   5660  O  O     . VAL A 1 713 ? 195.561 174.140 244.308 1.00 85.06  ?  732 VAL A O     1 
ATOM   5661  C  CB    . VAL A 1 713 ? 192.758 173.137 243.025 1.00 80.92  ?  732 VAL A CB    1 
ATOM   5662  C  CG1   . VAL A 1 713 ? 192.966 172.451 244.360 1.00 79.62  ?  732 VAL A CG1   1 
ATOM   5663  C  CG2   . VAL A 1 713 ? 191.294 173.475 242.850 1.00 82.41  ?  732 VAL A CG2   1 
ATOM   5664  N  N     . ASP A 1 714 ? 195.869 173.887 242.096 1.00 81.09  ?  733 ASP A N     1 
ATOM   5665  C  CA    . ASP A 1 714 ? 197.304 173.671 242.257 1.00 83.84  ?  733 ASP A CA    1 
ATOM   5666  C  C     . ASP A 1 714 ? 198.009 174.946 242.705 1.00 84.71  ?  733 ASP A C     1 
ATOM   5667  O  O     . ASP A 1 714 ? 198.821 174.920 243.637 1.00 82.20  ?  733 ASP A O     1 
ATOM   5668  C  CB    . ASP A 1 714 ? 197.909 173.157 240.952 1.00 82.29  ?  733 ASP A CB    1 
ATOM   5669  C  CG    . ASP A 1 714 ? 197.458 171.751 240.613 1.00 85.14  ?  733 ASP A CG    1 
ATOM   5670  O  OD1   . ASP A 1 714 ? 197.104 170.998 241.544 1.00 86.46  ?  733 ASP A OD1   1 
ATOM   5671  O  OD2   . ASP A 1 714 ? 197.460 171.399 239.415 1.00 83.10  -1 733 ASP A OD2   1 
ATOM   5672  N  N     . ARG A 1 715 ? 197.711 176.073 242.056 1.00 91.04  ?  734 ARG A N     1 
ATOM   5673  C  CA    . ARG A 1 715 ? 198.303 177.346 242.445 1.00 87.53  ?  734 ARG A CA    1 
ATOM   5674  C  C     . ARG A 1 715 ? 197.712 177.900 243.734 1.00 90.55  ?  734 ARG A C     1 
ATOM   5675  O  O     . ARG A 1 715 ? 198.241 178.881 244.267 1.00 93.74  ?  734 ARG A O     1 
ATOM   5676  C  CB    . ARG A 1 715 ? 198.141 178.374 241.322 1.00 88.23  ?  734 ARG A CB    1 
ATOM   5677  C  CG    . ARG A 1 715 ? 198.681 177.914 239.979 1.00 89.35  ?  734 ARG A CG    1 
ATOM   5678  C  CD    . ARG A 1 715 ? 198.391 178.931 238.887 1.00 91.23  ?  734 ARG A CD    1 
ATOM   5679  N  NE    . ARG A 1 715 ? 197.051 179.494 239.002 1.00 93.04  ?  734 ARG A NE    1 
ATOM   5680  C  CZ    . ARG A 1 715 ? 196.777 180.791 238.953 1.00 91.65  ?  734 ARG A CZ    1 
ATOM   5681  N  NH1   . ARG A 1 715 ? 197.731 181.692 238.789 1.00 91.54  1  734 ARG A NH1   1 
ATOM   5682  N  NH2   . ARG A 1 715 ? 195.515 181.193 239.073 1.00 89.49  ?  734 ARG A NH2   1 
ATOM   5683  N  N     . CYS A 1 716 ? 196.621 177.310 244.228 1.00 96.47  ?  735 CYS A N     1 
ATOM   5684  C  CA    . CYS A 1 716 ? 196.083 177.706 245.526 1.00 94.84  ?  735 CYS A CA    1 
ATOM   5685  C  C     . CYS A 1 716 ? 197.123 177.575 246.633 1.00 96.12  ?  735 CYS A C     1 
ATOM   5686  O  O     . CYS A 1 716 ? 197.085 178.330 247.610 1.00 96.64  ?  735 CYS A O     1 
ATOM   5687  C  CB    . CYS A 1 716 ? 194.849 176.863 245.852 1.00 95.94  ?  735 CYS A CB    1 
ATOM   5688  S  SG    . CYS A 1 716 ? 193.831 177.492 247.202 1.00 99.02  ?  735 CYS A SG    1 
ATOM   5689  N  N     . LEU A 1 717 ? 198.053 176.626 246.500 1.00 101.24 ?  736 LEU A N     1 
ATOM   5690  C  CA    . LEU A 1 717 ? 199.096 176.456 247.508 1.00 102.25 ?  736 LEU A CA    1 
ATOM   5691  C  C     . LEU A 1 717 ? 200.032 177.659 247.550 1.00 100.33 ?  736 LEU A C     1 
ATOM   5692  O  O     . LEU A 1 717 ? 200.292 178.219 248.621 1.00 99.92  ?  736 LEU A O     1 
ATOM   5693  C  CB    . LEU A 1 717 ? 199.888 175.177 247.229 1.00 101.58 ?  736 LEU A CB    1 
ATOM   5694  C  CG    . LEU A 1 717 ? 199.186 173.829 247.392 1.00 100.54 ?  736 LEU A CG    1 
ATOM   5695  C  CD1   . LEU A 1 717 ? 200.074 172.710 246.876 1.00 98.23  ?  736 LEU A CD1   1 
ATOM   5696  C  CD2   . LEU A 1 717 ? 198.835 173.587 248.848 1.00 99.13  ?  736 LEU A CD2   1 
ATOM   5697  N  N     . THR A 1 718 ? 200.546 178.074 246.391 1.00 104.71 ?  737 THR A N     1 
ATOM   5698  C  CA    . THR A 1 718 ? 201.576 179.108 246.360 1.00 105.80 ?  737 THR A CA    1 
ATOM   5699  C  C     . THR A 1 718 ? 200.971 180.507 246.295 1.00 107.14 ?  737 THR A C     1 
ATOM   5700  O  O     . THR A 1 718 ? 201.203 181.337 247.180 1.00 106.48 ?  737 THR A O     1 
ATOM   5701  C  CB    . THR A 1 718 ? 202.516 178.876 245.173 1.00 106.46 ?  737 THR A CB    1 
ATOM   5702  O  OG1   . THR A 1 718 ? 201.807 179.100 243.948 1.00 104.93 ?  737 THR A OG1   1 
ATOM   5703  C  CG2   . THR A 1 718 ? 203.053 177.453 245.189 1.00 106.57 ?  737 THR A CG2   1 
ATOM   5704  N  N     . GLU A 1 719 ? 200.192 180.785 245.253 1.00 106.08 ?  738 GLU A N     1 
ATOM   5705  C  CA    . GLU A 1 719 ? 199.630 182.118 245.044 1.00 105.38 ?  738 GLU A CA    1 
ATOM   5706  C  C     . GLU A 1 719 ? 198.455 182.310 245.993 1.00 104.12 ?  738 GLU A C     1 
ATOM   5707  O  O     . GLU A 1 719 ? 197.343 181.844 245.732 1.00 103.05 ?  738 GLU A O     1 
ATOM   5708  C  CB    . GLU A 1 719 ? 199.209 182.302 243.591 1.00 104.76 ?  738 GLU A CB    1 
ATOM   5709  C  CG    . GLU A 1 719 ? 200.300 181.976 242.584 1.00 106.25 ?  738 GLU A CG    1 
ATOM   5710  C  CD    . GLU A 1 719 ? 199.859 182.203 241.152 1.00 106.45 ?  738 GLU A CD    1 
ATOM   5711  O  OE1   . GLU A 1 719 ? 198.709 182.646 240.947 1.00 106.20 ?  738 GLU A OE1   1 
ATOM   5712  O  OE2   . GLU A 1 719 ? 200.662 181.942 240.232 1.00 104.63 -1 738 GLU A OE2   1 
ATOM   5713  N  N     . LYS A 1 720 ? 198.701 183.004 247.106 1.00 102.53 ?  739 LYS A N     1 
ATOM   5714  C  CA    . LYS A 1 720 ? 197.656 183.267 248.088 1.00 102.27 ?  739 LYS A CA    1 
ATOM   5715  C  C     . LYS A 1 720 ? 196.639 184.295 247.610 1.00 102.09 ?  739 LYS A C     1 
ATOM   5716  O  O     . LYS A 1 720 ? 195.600 184.457 248.258 1.00 103.21 ?  739 LYS A O     1 
ATOM   5717  C  CB    . LYS A 1 720 ? 198.284 183.735 249.403 1.00 103.98 ?  739 LYS A CB    1 
ATOM   5718  C  CG    . LYS A 1 720 ? 199.332 182.785 249.959 1.00 103.99 ?  739 LYS A CG    1 
ATOM   5719  C  CD    . LYS A 1 720 ? 199.972 183.346 251.218 1.00 103.19 ?  739 LYS A CD    1 
ATOM   5720  C  CE    . LYS A 1 720 ? 201.043 182.410 251.755 1.00 102.84 ?  739 LYS A CE    1 
ATOM   5721  N  NZ    . LYS A 1 720 ? 201.691 182.946 252.984 1.00 103.84 1  739 LYS A NZ    1 
ATOM   5722  N  N     . ARG A 1 721 ? 196.910 184.990 246.503 1.00 103.34 ?  740 ARG A N     1 
ATOM   5723  C  CA    . ARG A 1 721 ? 195.965 185.984 246.006 1.00 104.42 ?  740 ARG A CA    1 
ATOM   5724  C  C     . ARG A 1 721 ? 194.751 185.334 245.355 1.00 105.25 ?  740 ARG A C     1 
ATOM   5725  O  O     . ARG A 1 721 ? 193.674 185.940 245.317 1.00 107.33 ?  740 ARG A O     1 
ATOM   5726  C  CB    . ARG A 1 721 ? 196.659 186.923 245.019 1.00 105.73 ?  740 ARG A CB    1 
ATOM   5727  C  CG    . ARG A 1 721 ? 197.391 186.213 243.891 1.00 107.10 ?  740 ARG A CG    1 
ATOM   5728  C  CD    . ARG A 1 721 ? 198.218 187.190 243.069 1.00 106.16 ?  740 ARG A CD    1 
ATOM   5729  N  NE    . ARG A 1 721 ? 199.358 187.709 243.814 1.00 107.27 ?  740 ARG A NE    1 
ATOM   5730  C  CZ    . ARG A 1 721 ? 200.546 187.124 243.870 1.00 107.37 ?  740 ARG A CZ    1 
ATOM   5731  N  NH1   . ARG A 1 721 ? 200.789 185.989 243.235 1.00 106.16 1  740 ARG A NH1   1 
ATOM   5732  N  NH2   . ARG A 1 721 ? 201.516 187.692 244.582 1.00 106.63 ?  740 ARG A NH2   1 
ATOM   5733  N  N     . ILE A 1 722 ? 194.900 184.108 244.841 1.00 99.67  ?  741 ILE A N     1 
ATOM   5734  C  CA    . ILE A 1 722 ? 193.794 183.430 244.167 1.00 96.94  ?  741 ILE A CA    1 
ATOM   5735  C  C     . ILE A 1 722 ? 192.865 182.712 245.130 1.00 98.27  ?  741 ILE A C     1 
ATOM   5736  O  O     . ILE A 1 722 ? 191.881 182.106 244.687 1.00 100.69 ?  741 ILE A O     1 
ATOM   5737  C  CB    . ILE A 1 722 ? 194.327 182.436 243.115 1.00 101.69 ?  741 ILE A CB    1 
ATOM   5738  C  CG1   . ILE A 1 722 ? 194.829 181.158 243.786 1.00 101.60 ?  741 ILE A CG1   1 
ATOM   5739  C  CG2   . ILE A 1 722 ? 195.431 183.078 242.288 1.00 101.90 ?  741 ILE A CG2   1 
ATOM   5740  C  CD1   . ILE A 1 722 ? 195.092 180.035 242.815 1.00 100.24 ?  741 ILE A CD1   1 
ATOM   5741  N  N     . LEU A 1 723 ? 193.145 182.756 246.436 1.00 98.47  ?  742 LEU A N     1 
ATOM   5742  C  CA    . LEU A 1 723 ? 192.191 182.257 247.421 1.00 97.98  ?  742 LEU A CA    1 
ATOM   5743  C  C     . LEU A 1 723 ? 190.884 183.036 247.382 1.00 98.16  ?  742 LEU A C     1 
ATOM   5744  O  O     . LEU A 1 723 ? 189.837 182.501 247.774 1.00 98.13  ?  742 LEU A O     1 
ATOM   5745  C  CB    . LEU A 1 723 ? 192.796 182.332 248.825 1.00 96.89  ?  742 LEU A CB    1 
ATOM   5746  C  CG    . LEU A 1 723 ? 193.520 181.097 249.364 1.00 101.12 ?  742 LEU A CG    1 
ATOM   5747  C  CD1   . LEU A 1 723 ? 192.552 179.935 249.527 1.00 102.03 ?  742 LEU A CD1   1 
ATOM   5748  C  CD2   . LEU A 1 723 ? 194.694 180.714 248.474 1.00 101.65 ?  742 LEU A CD2   1 
ATOM   5749  N  N     . ALA A 1 724 ? 190.931 184.288 246.922 1.00 101.37 ?  743 ALA A N     1 
ATOM   5750  C  CA    . ALA A 1 724 ? 189.724 185.099 246.823 1.00 101.24 ?  743 ALA A CA    1 
ATOM   5751  C  C     . ALA A 1 724 ? 188.739 184.503 245.829 1.00 102.24 ?  743 ALA A C     1 
ATOM   5752  O  O     . ALA A 1 724 ? 187.524 184.562 246.043 1.00 102.77 ?  743 ALA A O     1 
ATOM   5753  C  CB    . ALA A 1 724 ? 190.085 186.526 246.425 1.00 100.44 ?  743 ALA A CB    1 
ATOM   5754  N  N     . LEU A 1 725 ? 189.243 183.941 244.727 1.00 100.45 ?  744 LEU A N     1 
ATOM   5755  C  CA    . LEU A 1 725 ? 188.371 183.260 243.776 1.00 100.07 ?  744 LEU A CA    1 
ATOM   5756  C  C     . LEU A 1 725 ? 187.558 182.174 244.466 1.00 99.07  ?  744 LEU A C     1 
ATOM   5757  O  O     . LEU A 1 725 ? 186.325 182.140 244.365 1.00 96.29  ?  744 LEU A O     1 
ATOM   5758  C  CB    . LEU A 1 725 ? 189.205 182.654 242.646 1.00 99.80  ?  744 LEU A CB    1 
ATOM   5759  C  CG    . LEU A 1 725 ? 189.797 183.580 241.586 1.00 100.11 ?  744 LEU A CG    1 
ATOM   5760  C  CD1   . LEU A 1 725 ? 190.984 182.918 240.905 1.00 98.52  ?  744 LEU A CD1   1 
ATOM   5761  C  CD2   . LEU A 1 725 ? 188.741 183.956 240.563 1.00 100.85 ?  744 LEU A CD2   1 
ATOM   5762  N  N     . LEU A 1 726 ? 188.241 181.287 245.192 1.00 98.75  ?  745 LEU A N     1 
ATOM   5763  C  CA    . LEU A 1 726 ? 187.565 180.179 245.856 1.00 99.92  ?  745 LEU A CA    1 
ATOM   5764  C  C     . LEU A 1 726 ? 186.588 180.687 246.908 1.00 99.92  ?  745 LEU A C     1 
ATOM   5765  O  O     . LEU A 1 726 ? 185.452 180.206 247.001 1.00 100.67 ?  745 LEU A O     1 
ATOM   5766  C  CB    . LEU A 1 726 ? 188.600 179.244 246.482 1.00 98.08  ?  745 LEU A CB    1 
ATOM   5767  C  CG    . LEU A 1 726 ? 189.274 178.244 245.539 1.00 96.54  ?  745 LEU A CG    1 
ATOM   5768  C  CD1   . LEU A 1 726 ? 190.441 178.885 244.801 1.00 95.45  ?  745 LEU A CD1   1 
ATOM   5769  C  CD2   . LEU A 1 726 ? 189.732 177.015 246.301 1.00 98.10  ?  745 LEU A CD2   1 
ATOM   5770  N  N     . GLU A 1 727 ? 187.012 181.674 247.703 1.00 97.15  ?  746 GLU A N     1 
ATOM   5771  C  CA    . GLU A 1 727 ? 186.149 182.200 248.757 1.00 93.10  ?  746 GLU A CA    1 
ATOM   5772  C  C     . GLU A 1 727 ? 184.884 182.820 248.176 1.00 93.35  ?  746 GLU A C     1 
ATOM   5773  O  O     . GLU A 1 727 ? 183.770 182.536 248.633 1.00 98.14  ?  746 GLU A O     1 
ATOM   5774  C  CB    . GLU A 1 727 ? 186.916 183.221 249.598 1.00 94.41  ?  746 GLU A CB    1 
ATOM   5775  C  CG    . GLU A 1 727 ? 186.032 184.095 250.474 1.00 98.89  ?  746 GLU A CG    1 
ATOM   5776  C  CD    . GLU A 1 727 ? 185.556 183.378 251.722 1.00 100.11 ?  746 GLU A CD    1 
ATOM   5777  O  OE1   . GLU A 1 727 ? 186.258 182.453 252.181 1.00 99.78  ?  746 GLU A OE1   1 
ATOM   5778  O  OE2   . GLU A 1 727 ? 184.479 183.738 252.242 1.00 96.37  -1 746 GLU A OE2   1 
ATOM   5779  N  N     . ALA A 1 728 ? 185.035 183.659 247.148 1.00 92.73  ?  747 ALA A N     1 
ATOM   5780  C  CA    . ALA A 1 728 ? 183.882 184.316 246.545 1.00 97.41  ?  747 ALA A CA    1 
ATOM   5781  C  C     . ALA A 1 728 ? 182.954 183.310 245.880 1.00 99.47  ?  747 ALA A C     1 
ATOM   5782  O  O     . ALA A 1 728 ? 181.728 183.424 245.986 1.00 98.89  ?  747 ALA A O     1 
ATOM   5783  C  CB    . ALA A 1 728 ? 184.345 185.367 245.538 1.00 97.83  ?  747 ALA A CB    1 
ATOM   5784  N  N     . ILE A 1 729 ? 183.517 182.318 245.184 1.00 97.93  ?  748 ILE A N     1 
ATOM   5785  C  CA    . ILE A 1 729 ? 182.681 181.334 244.504 1.00 96.82  ?  748 ILE A CA    1 
ATOM   5786  C  C     . ILE A 1 729 ? 181.904 180.500 245.515 1.00 96.28  ?  748 ILE A C     1 
ATOM   5787  O  O     . ILE A 1 729 ? 180.710 180.229 245.329 1.00 97.73  ?  748 ILE A O     1 
ATOM   5788  C  CB    . ILE A 1 729 ? 183.542 180.467 243.569 1.00 98.09  ?  748 ILE A CB    1 
ATOM   5789  C  CG1   . ILE A 1 729 ? 183.910 181.269 242.319 1.00 98.70  ?  748 ILE A CG1   1 
ATOM   5790  C  CG2   . ILE A 1 729 ? 182.810 179.190 243.188 1.00 96.26  ?  748 ILE A CG2   1 
ATOM   5791  C  CD1   . ILE A 1 729 ? 185.205 180.853 241.680 1.00 97.49  ?  748 ILE A CD1   1 
ATOM   5792  N  N     . THR A 1 730 ? 182.552 180.104 246.614 1.00 93.52  ?  749 THR A N     1 
ATOM   5793  C  CA    . THR A 1 730 ? 181.829 179.411 247.676 1.00 94.16  ?  749 THR A CA    1 
ATOM   5794  C  C     . THR A 1 730 ? 180.723 180.287 248.250 1.00 92.52  ?  749 THR A C     1 
ATOM   5795  O  O     . THR A 1 730 ? 179.614 179.803 248.517 1.00 95.16  ?  749 THR A O     1 
ATOM   5796  C  CB    . THR A 1 730 ? 182.792 178.983 248.782 1.00 94.64  ?  749 THR A CB    1 
ATOM   5797  O  OG1   . THR A 1 730 ? 183.595 180.104 249.174 1.00 95.11  ?  749 THR A OG1   1 
ATOM   5798  C  CG2   . THR A 1 730 ? 183.690 177.853 248.302 1.00 93.67  ?  749 THR A CG2   1 
ATOM   5799  N  N     . SER A 1 731 ? 181.013 181.577 248.456 1.00 87.29  ?  750 SER A N     1 
ATOM   5800  C  CA    . SER A 1 731 ? 180.009 182.487 248.995 1.00 87.56  ?  750 SER A CA    1 
ATOM   5801  C  C     . SER A 1 731 ? 178.800 182.579 248.074 1.00 89.46  ?  750 SER A C     1 
ATOM   5802  O  O     . SER A 1 731 ? 177.657 182.556 248.541 1.00 89.06  ?  750 SER A O     1 
ATOM   5803  C  CB    . SER A 1 731 ? 180.618 183.870 249.223 1.00 90.06  ?  750 SER A CB    1 
ATOM   5804  O  OG    . SER A 1 731 ? 180.939 184.500 247.995 1.00 88.70  ?  750 SER A OG    1 
ATOM   5805  N  N     . ILE A 1 732 ? 179.032 182.672 246.762 1.00 91.52  ?  751 ILE A N     1 
ATOM   5806  C  CA    . ILE A 1 732 ? 177.925 182.615 245.807 1.00 88.36  ?  751 ILE A CA    1 
ATOM   5807  C  C     . ILE A 1 732 ? 177.184 181.292 245.946 1.00 88.32  ?  751 ILE A C     1 
ATOM   5808  O  O     . ILE A 1 732 ? 175.951 181.230 245.817 1.00 89.28  ?  751 ILE A O     1 
ATOM   5809  C  CB    . ILE A 1 732 ? 178.432 182.825 244.367 1.00 87.53  ?  751 ILE A CB    1 
ATOM   5810  C  CG1   . ILE A 1 732 ? 179.230 184.122 244.250 1.00 89.80  ?  751 ILE A CG1   1 
ATOM   5811  C  CG2   . ILE A 1 732 ? 177.272 182.825 243.379 1.00 86.07  ?  751 ILE A CG2   1 
ATOM   5812  C  CD1   . ILE A 1 732 ? 180.365 184.039 243.252 1.00 87.00  ?  751 ILE A CD1   1 
ATOM   5813  N  N     . GLY A 1 733 ? 177.926 180.216 246.201 1.00 89.75  ?  752 GLY A N     1 
ATOM   5814  C  CA    . GLY A 1 733 ? 177.344 178.917 246.463 1.00 90.90  ?  752 GLY A CA    1 
ATOM   5815  C  C     . GLY A 1 733 ? 176.287 178.951 247.546 1.00 91.36  ?  752 GLY A C     1 
ATOM   5816  O  O     . GLY A 1 733 ? 175.120 178.644 247.279 1.00 87.98  ?  752 GLY A O     1 
ATOM   5817  N  N     . GLN A 1 734 ? 176.668 179.336 248.767 1.00 92.35  ?  753 GLN A N     1 
ATOM   5818  C  CA    . GLN A 1 734 ? 175.621 179.349 249.791 1.00 91.07  ?  753 GLN A CA    1 
ATOM   5819  C  C     . GLN A 1 734 ? 174.666 180.526 249.642 1.00 91.42  ?  753 GLN A C     1 
ATOM   5820  O  O     . GLN A 1 734 ? 173.612 180.528 250.290 1.00 93.88  ?  753 GLN A O     1 
ATOM   5821  C  CB    . GLN A 1 734 ? 176.131 179.351 251.249 1.00 92.51  ?  753 GLN A CB    1 
ATOM   5822  C  CG    . GLN A 1 734 ? 176.791 180.624 251.771 1.00 94.38  ?  753 GLN A CG    1 
ATOM   5823  C  CD    . GLN A 1 734 ? 178.280 180.664 251.564 1.00 95.35  ?  753 GLN A CD    1 
ATOM   5824  O  OE1   . GLN A 1 734 ? 178.827 179.880 250.809 1.00 95.05  ?  753 GLN A OE1   1 
ATOM   5825  N  NE2   . GLN A 1 734 ? 178.948 181.589 252.244 1.00 94.87  ?  753 GLN A NE2   1 
ATOM   5826  N  N     . SER A 1 735 ? 174.994 181.525 248.818 1.00 88.16  ?  754 SER A N     1 
ATOM   5827  C  CA    . SER A 1 735 ? 174.083 182.646 248.618 1.00 91.70  ?  754 SER A CA    1 
ATOM   5828  C  C     . SER A 1 735 ? 172.901 182.266 247.737 1.00 91.24  ?  754 SER A C     1 
ATOM   5829  O  O     . SER A 1 735 ? 171.763 182.653 248.023 1.00 90.36  ?  754 SER A O     1 
ATOM   5830  C  CB    . SER A 1 735 ? 174.835 183.834 248.015 1.00 89.95  ?  754 SER A CB    1 
ATOM   5831  O  OG    . SER A 1 735 ? 176.027 184.103 248.732 1.00 89.57  ?  754 SER A OG    1 
ATOM   5832  N  N     . LEU A 1 736 ? 173.143 181.511 246.662 1.00 84.90  ?  755 LEU A N     1 
ATOM   5833  C  CA    . LEU A 1 736 ? 172.077 181.228 245.706 1.00 86.06  ?  755 LEU A CA    1 
ATOM   5834  C  C     . LEU A 1 736 ? 171.992 179.746 245.349 1.00 86.81  ?  755 LEU A C     1 
ATOM   5835  O  O     . LEU A 1 736 ? 171.527 179.392 244.263 1.00 87.30  ?  755 LEU A O     1 
ATOM   5836  C  CB    . LEU A 1 736 ? 172.233 182.099 244.456 1.00 88.32  ?  755 LEU A CB    1 
ATOM   5837  C  CG    . LEU A 1 736 ? 173.473 182.046 243.559 1.00 89.46  ?  755 LEU A CG    1 
ATOM   5838  C  CD1   . LEU A 1 736 ? 173.383 180.976 242.491 1.00 87.80  ?  755 LEU A CD1   1 
ATOM   5839  C  CD2   . LEU A 1 736 ? 173.697 183.396 242.925 1.00 89.49  ?  755 LEU A CD2   1 
ATOM   5840  N  N     . ASN A 1 737 ? 172.402 178.870 246.269 1.00 84.31  ?  756 ASN A N     1 
ATOM   5841  C  CA    . ASN A 1 737 ? 172.172 177.429 246.154 1.00 84.81  ?  756 ASN A CA    1 
ATOM   5842  C  C     . ASN A 1 737 ? 172.912 176.833 244.953 1.00 83.23  ?  756 ASN A C     1 
ATOM   5843  O  O     . ASN A 1 737 ? 172.321 176.231 244.054 1.00 82.66  ?  756 ASN A O     1 
ATOM   5844  C  CB    . ASN A 1 737 ? 170.670 177.124 246.088 1.00 82.13  ?  756 ASN A CB    1 
ATOM   5845  C  CG    . ASN A 1 737 ? 170.351 175.679 246.417 1.00 83.02  ?  756 ASN A CG    1 
ATOM   5846  O  OD1   . ASN A 1 737 ? 171.231 174.907 246.799 1.00 84.78  ?  756 ASN A OD1   1 
ATOM   5847  N  ND2   . ASN A 1 737 ? 169.085 175.306 246.271 1.00 83.15  ?  756 ASN A ND2   1 
ATOM   5848  N  N     . LEU A 1 738 ? 174.230 177.014 244.955 1.00 73.82  ?  757 LEU A N     1 
ATOM   5849  C  CA    . LEU A 1 738 ? 175.123 176.339 244.025 1.00 73.63  ?  757 LEU A CA    1 
ATOM   5850  C  C     . LEU A 1 738 ? 176.057 175.422 244.798 1.00 77.68  ?  757 LEU A C     1 
ATOM   5851  O  O     . LEU A 1 738 ? 176.454 175.733 245.926 1.00 77.32  ?  757 LEU A O     1 
ATOM   5852  C  CB    . LEU A 1 738 ? 175.950 177.330 243.198 1.00 75.65  ?  757 LEU A CB    1 
ATOM   5853  C  CG    . LEU A 1 738 ? 175.249 178.044 242.045 1.00 74.32  ?  757 LEU A CG    1 
ATOM   5854  C  CD1   . LEU A 1 738 ? 176.209 178.988 241.340 1.00 73.61  ?  757 LEU A CD1   1 
ATOM   5855  C  CD2   . LEU A 1 738 ? 174.665 177.042 241.064 1.00 76.61  ?  757 LEU A CD2   1 
ATOM   5856  N  N     . THR A 1 739 ? 176.408 174.294 244.189 1.00 70.16  ?  758 THR A N     1 
ATOM   5857  C  CA    . THR A 1 739 ? 177.350 173.353 244.775 1.00 66.01  ?  758 THR A CA    1 
ATOM   5858  C  C     . THR A 1 739 ? 178.717 173.581 244.142 1.00 63.67  ?  758 THR A C     1 
ATOM   5859  O  O     . THR A 1 739 ? 178.853 173.536 242.914 1.00 65.54  ?  758 THR A O     1 
ATOM   5860  C  CB    . THR A 1 739 ? 176.889 171.910 244.565 1.00 65.03  ?  758 THR A CB    1 
ATOM   5861  O  OG1   . THR A 1 739 ? 175.821 171.612 245.473 1.00 62.36  ?  758 THR A OG1   1 
ATOM   5862  C  CG2   . THR A 1 739 ? 178.036 170.941 244.812 1.00 68.58  ?  758 THR A CG2   1 
ATOM   5863  N  N     . VAL A 1 740 ? 179.720 173.835 244.976 1.00 59.26  ?  759 VAL A N     1 
ATOM   5864  C  CA    . VAL A 1 740 ? 181.075 174.065 244.497 1.00 60.76  ?  759 VAL A CA    1 
ATOM   5865  C  C     . VAL A 1 740 ? 181.857 172.757 244.567 1.00 64.82  ?  759 VAL A C     1 
ATOM   5866  O  O     . VAL A 1 740 ? 181.876 172.075 245.603 1.00 70.04  ?  759 VAL A O     1 
ATOM   5867  C  CB    . VAL A 1 740 ? 181.761 175.196 245.288 1.00 66.85  ?  759 VAL A CB    1 
ATOM   5868  C  CG1   . VAL A 1 740 ? 181.954 174.836 246.748 1.00 67.45  ?  759 VAL A CG1   1 
ATOM   5869  C  CG2   . VAL A 1 740 ? 183.089 175.555 244.646 1.00 67.10  ?  759 VAL A CG2   1 
ATOM   5870  N  N     . VAL A 1 741 ? 182.484 172.404 243.447 1.00 61.40  ?  760 VAL A N     1 
ATOM   5871  C  CA    . VAL A 1 741 ? 183.125 171.109 243.243 1.00 55.55  ?  760 VAL A CA    1 
ATOM   5872  C  C     . VAL A 1 741 ? 184.606 171.378 243.021 1.00 58.45  ?  760 VAL A C     1 
ATOM   5873  O  O     . VAL A 1 741 ? 185.009 171.796 241.931 1.00 68.69  ?  760 VAL A O     1 
ATOM   5874  C  CB    . VAL A 1 741 ? 182.524 170.351 242.052 1.00 63.83  ?  760 VAL A CB    1 
ATOM   5875  C  CG1   . VAL A 1 741 ? 182.981 168.896 242.047 1.00 66.08  ?  760 VAL A CG1   1 
ATOM   5876  C  CG2   . VAL A 1 741 ? 181.002 170.471 242.032 1.00 65.68  ?  760 VAL A CG2   1 
ATOM   5877  N  N     . ALA A 1 742 ? 185.424 171.142 244.039 1.00 57.83  ?  761 ALA A N     1 
ATOM   5878  C  CA    . ALA A 1 742 ? 186.864 171.286 243.880 1.00 61.36  ?  761 ALA A CA    1 
ATOM   5879  C  C     . ALA A 1 742 ? 187.410 170.127 243.057 1.00 63.99  ?  761 ALA A C     1 
ATOM   5880  O  O     . ALA A 1 742 ? 186.986 168.981 243.228 1.00 71.40  ?  761 ALA A O     1 
ATOM   5881  C  CB    . ALA A 1 742 ? 187.554 171.336 245.242 1.00 64.48  ?  761 ALA A CB    1 
ATOM   5882  N  N     . GLU A 1 743 ? 188.348 170.424 242.157 1.00 64.10  ?  762 GLU A N     1 
ATOM   5883  C  CA    . GLU A 1 743 ? 188.968 169.398 241.332 1.00 63.94  ?  762 GLU A CA    1 
ATOM   5884  C  C     . GLU A 1 743 ? 190.473 169.370 241.567 1.00 66.59  ?  762 GLU A C     1 
ATOM   5885  O  O     . GLU A 1 743 ? 191.069 170.323 242.075 1.00 71.57  ?  762 GLU A O     1 
ATOM   5886  C  CB    . GLU A 1 743 ? 188.672 169.631 239.845 1.00 66.21  ?  762 GLU A CB    1 
ATOM   5887  C  CG    . GLU A 1 743 ? 187.236 169.344 239.436 1.00 69.53  ?  762 GLU A CG    1 
ATOM   5888  C  CD    . GLU A 1 743 ? 187.071 169.242 237.931 1.00 71.44  ?  762 GLU A CD    1 
ATOM   5889  O  OE1   . GLU A 1 743 ? 187.988 169.673 237.200 1.00 71.83  ?  762 GLU A OE1   1 
ATOM   5890  O  OE2   . GLU A 1 743 ? 186.024 168.733 237.478 1.00 69.95  -1 762 GLU A OE2   1 
ATOM   5891  N  N     . GLY A 1 744 ? 191.083 168.253 241.183 1.00 60.71  ?  763 GLY A N     1 
ATOM   5892  C  CA    . GLY A 1 744 ? 192.531 168.124 241.238 1.00 60.29  ?  763 GLY A CA    1 
ATOM   5893  C  C     . GLY A 1 744 ? 193.126 168.184 242.628 1.00 66.57  ?  763 GLY A C     1 
ATOM   5894  O  O     . GLY A 1 744 ? 194.132 168.874 242.838 1.00 72.20  ?  763 GLY A O     1 
ATOM   5895  N  N     . VAL A 1 745 ? 192.532 167.477 243.584 1.00 59.88  ?  764 VAL A N     1 
ATOM   5896  C  CA    . VAL A 1 745 ? 193.083 167.385 244.931 1.00 58.27  ?  764 VAL A CA    1 
ATOM   5897  C  C     . VAL A 1 745 ? 193.951 166.135 245.019 1.00 59.40  ?  764 VAL A C     1 
ATOM   5898  O  O     . VAL A 1 745 ? 193.575 165.064 244.528 1.00 62.83  ?  764 VAL A O     1 
ATOM   5899  C  CB    . VAL A 1 745 ? 191.965 167.384 245.992 1.00 57.69  ?  764 VAL A CB    1 
ATOM   5900  C  CG1   . VAL A 1 745 ? 191.002 168.531 245.738 1.00 57.68  ?  764 VAL A CG1   1 
ATOM   5901  C  CG2   . VAL A 1 745 ? 191.212 166.063 246.014 1.00 60.37  ?  764 VAL A CG2   1 
ATOM   5902  N  N     . GLU A 1 746 ? 195.146 166.285 245.590 1.00 70.02  ?  765 GLU A N     1 
ATOM   5903  C  CA    . GLU A 1 746 ? 196.093 165.180 245.687 1.00 66.86  ?  765 GLU A CA    1 
ATOM   5904  C  C     . GLU A 1 746 ? 196.738 165.015 247.054 1.00 71.25  ?  765 GLU A C     1 
ATOM   5905  O  O     . GLU A 1 746 ? 197.214 163.912 247.351 1.00 73.41  ?  765 GLU A O     1 
ATOM   5906  C  CB    . GLU A 1 746 ? 197.208 165.329 244.637 1.00 68.69  ?  765 GLU A CB    1 
ATOM   5907  C  CG    . GLU A 1 746 ? 196.712 165.624 243.226 1.00 67.79  ?  765 GLU A CG    1 
ATOM   5908  C  CD    . GLU A 1 746 ? 197.722 165.252 242.157 1.00 72.39  ?  765 GLU A CD    1 
ATOM   5909  O  OE1   . GLU A 1 746 ? 198.389 164.206 242.303 1.00 73.76  ?  765 GLU A OE1   1 
ATOM   5910  O  OE2   . GLU A 1 746 ? 197.843 166.003 241.166 1.00 69.15  -1 765 GLU A OE2   1 
ATOM   5911  N  N     . THR A 1 747 ? 196.775 166.048 247.895 1.00 85.87  ?  766 THR A N     1 
ATOM   5912  C  CA    . THR A 1 747 ? 197.486 165.980 249.162 1.00 87.39  ?  766 THR A CA    1 
ATOM   5913  C  C     . THR A 1 747 ? 196.592 166.424 250.312 1.00 85.22  ?  766 THR A C     1 
ATOM   5914  O  O     . THR A 1 747 ? 195.635 167.187 250.129 1.00 85.92  ?  766 THR A O     1 
ATOM   5915  C  CB    . THR A 1 747 ? 198.768 166.832 249.142 1.00 86.81  ?  766 THR A CB    1 
ATOM   5916  O  OG1   . THR A 1 747 ? 198.445 168.187 248.812 1.00 86.78  ?  766 THR A OG1   1 
ATOM   5917  C  CG2   . THR A 1 747 ? 199.759 166.287 248.123 1.00 84.59  ?  766 THR A CG2   1 
ATOM   5918  N  N     . LYS A 1 748 ? 196.926 165.929 251.507 1.00 86.70  ?  767 LYS A N     1 
ATOM   5919  C  CA    . LYS A 1 748 ? 196.134 166.225 252.695 1.00 88.78  ?  767 LYS A CA    1 
ATOM   5920  C  C     . LYS A 1 748 ? 196.156 167.712 253.023 1.00 90.30  ?  767 LYS A C     1 
ATOM   5921  O  O     . LYS A 1 748 ? 195.140 168.274 253.441 1.00 93.41  ?  767 LYS A O     1 
ATOM   5922  C  CB    . LYS A 1 748 ? 196.642 165.405 253.881 1.00 92.60  ?  767 LYS A CB    1 
ATOM   5923  C  CG    . LYS A 1 748 ? 195.698 165.386 255.073 1.00 93.56  ?  767 LYS A CG    1 
ATOM   5924  C  CD    . LYS A 1 748 ? 196.160 164.394 256.127 1.00 92.23  ?  767 LYS A CD    1 
ATOM   5925  C  CE    . LYS A 1 748 ? 195.134 164.256 257.240 1.00 91.34  ?  767 LYS A CE    1 
ATOM   5926  N  NZ    . LYS A 1 748 ? 195.113 165.452 258.125 1.00 90.96  1  767 LYS A NZ    1 
ATOM   5927  N  N     . GLU A 1 749 ? 197.310 168.364 252.857 1.00 92.96  ?  768 GLU A N     1 
ATOM   5928  C  CA    . GLU A 1 749 ? 197.374 169.805 253.077 1.00 94.25  ?  768 GLU A CA    1 
ATOM   5929  C  C     . GLU A 1 749 ? 196.509 170.551 252.067 1.00 96.52  ?  768 GLU A C     1 
ATOM   5930  O  O     . GLU A 1 749 ? 195.834 171.528 252.414 1.00 96.28  ?  768 GLU A O     1 
ATOM   5931  C  CB    . GLU A 1 749 ? 198.825 170.285 253.009 1.00 93.87  ?  768 GLU A CB    1 
ATOM   5932  C  CG    . GLU A 1 749 ? 199.580 169.846 251.762 1.00 95.81  ?  768 GLU A CG    1 
ATOM   5933  C  CD    . GLU A 1 749 ? 200.410 168.598 251.989 1.00 97.61  ?  768 GLU A CD    1 
ATOM   5934  O  OE1   . GLU A 1 749 ? 200.033 167.779 252.854 1.00 97.40  ?  768 GLU A OE1   1 
ATOM   5935  O  OE2   . GLU A 1 749 ? 201.441 168.435 251.302 1.00 95.96  -1 768 GLU A OE2   1 
ATOM   5936  N  N     . GLN A 1 750 ? 196.506 170.092 250.814 1.00 89.98  ?  769 GLN A N     1 
ATOM   5937  C  CA    . GLN A 1 750 ? 195.706 170.735 249.779 1.00 86.66  ?  769 GLN A CA    1 
ATOM   5938  C  C     . GLN A 1 750 ? 194.218 170.585 250.065 1.00 84.35  ?  769 GLN A C     1 
ATOM   5939  O  O     . GLN A 1 750 ? 193.423 171.481 249.759 1.00 85.80  ?  769 GLN A O     1 
ATOM   5940  C  CB    . GLN A 1 750 ? 196.065 170.139 248.419 1.00 88.02  ?  769 GLN A CB    1 
ATOM   5941  C  CG    . GLN A 1 750 ? 195.483 170.839 247.210 1.00 89.17  ?  769 GLN A CG    1 
ATOM   5942  C  CD    . GLN A 1 750 ? 196.037 170.267 245.919 1.00 86.43  ?  769 GLN A CD    1 
ATOM   5943  O  OE1   . GLN A 1 750 ? 196.810 169.310 245.937 1.00 86.25  ?  769 GLN A OE1   1 
ATOM   5944  N  NE2   . GLN A 1 750 ? 195.658 170.857 244.795 1.00 85.53  ?  769 GLN A NE2   1 
ATOM   5945  N  N     . PHE A 1 751 ? 193.820 169.451 250.647 1.00 89.09  ?  770 PHE A N     1 
ATOM   5946  C  CA    . PHE A 1 751 ? 192.424 169.275 251.041 1.00 90.17  ?  770 PHE A CA    1 
ATOM   5947  C  C     . PHE A 1 751 ? 192.080 170.117 252.268 1.00 89.46  ?  770 PHE A C     1 
ATOM   5948  O  O     . PHE A 1 751 ? 191.027 170.766 252.311 1.00 90.03  ?  770 PHE A O     1 
ATOM   5949  C  CB    . PHE A 1 751 ? 192.140 167.796 251.301 1.00 92.27  ?  770 PHE A CB    1 
ATOM   5950  C  CG    . PHE A 1 751 ? 191.003 167.552 252.252 1.00 90.25  ?  770 PHE A CG    1 
ATOM   5951  C  CD1   . PHE A 1 751 ? 189.694 167.781 251.861 1.00 87.33  ?  770 PHE A CD1   1 
ATOM   5952  C  CD2   . PHE A 1 751 ? 191.244 167.092 253.536 1.00 90.43  ?  770 PHE A CD2   1 
ATOM   5953  C  CE1   . PHE A 1 751 ? 188.647 167.557 252.735 1.00 86.30  ?  770 PHE A CE1   1 
ATOM   5954  C  CE2   . PHE A 1 751 ? 190.201 166.867 254.414 1.00 91.31  ?  770 PHE A CE2   1 
ATOM   5955  C  CZ    . PHE A 1 751 ? 188.901 167.100 254.012 1.00 90.40  ?  770 PHE A CZ    1 
ATOM   5956  N  N     . GLU A 1 752 ? 192.956 170.122 253.275 1.00 96.12  ?  771 GLU A N     1 
ATOM   5957  C  CA    . GLU A 1 752 ? 192.660 170.828 254.514 1.00 96.00  ?  771 GLU A CA    1 
ATOM   5958  C  C     . GLU A 1 752 ? 192.695 172.341 254.344 1.00 96.70  ?  771 GLU A C     1 
ATOM   5959  O  O     . GLU A 1 752 ? 192.061 173.051 255.132 1.00 99.20  ?  771 GLU A O     1 
ATOM   5960  C  CB    . GLU A 1 752 ? 193.636 170.401 255.614 1.00 95.36  ?  771 GLU A CB    1 
ATOM   5961  C  CG    . GLU A 1 752 ? 195.008 171.048 255.528 1.00 94.79  ?  771 GLU A CG    1 
ATOM   5962  C  CD    . GLU A 1 752 ? 196.016 170.407 256.462 1.00 97.66  ?  771 GLU A CD    1 
ATOM   5963  O  OE1   . GLU A 1 752 ? 195.915 169.186 256.704 1.00 98.24  ?  771 GLU A OE1   1 
ATOM   5964  O  OE2   . GLU A 1 752 ? 196.911 171.126 256.956 1.00 97.26  -1 771 GLU A OE2   1 
ATOM   5965  N  N     . MET A 1 753 ? 193.412 172.854 253.340 1.00 93.68  ?  772 MET A N     1 
ATOM   5966  C  CA    . MET A 1 753 ? 193.385 174.293 253.111 1.00 94.53  ?  772 MET A CA    1 
ATOM   5967  C  C     . MET A 1 753 ? 192.060 174.732 252.503 1.00 93.03  ?  772 MET A C     1 
ATOM   5968  O  O     . MET A 1 753 ? 191.612 175.856 252.751 1.00 95.23  ?  772 MET A O     1 
ATOM   5969  C  CB    . MET A 1 753 ? 194.556 174.723 252.224 1.00 94.34  ?  772 MET A CB    1 
ATOM   5970  C  CG    . MET A 1 753 ? 194.317 174.567 250.734 1.00 94.77  ?  772 MET A CG    1 
ATOM   5971  S  SD    . MET A 1 753 ? 195.761 174.994 249.749 1.00 96.77  ?  772 MET A SD    1 
ATOM   5972  C  CE    . MET A 1 753 ? 196.007 176.699 250.237 1.00 96.43  ?  772 MET A CE    1 
ATOM   5973  N  N     . LEU A 1 754 ? 191.423 173.870 251.707 1.00 91.27  ?  773 LEU A N     1 
ATOM   5974  C  CA    . LEU A 1 754 ? 190.085 174.154 251.203 1.00 93.91  ?  773 LEU A CA    1 
ATOM   5975  C  C     . LEU A 1 754 ? 189.002 173.791 252.208 1.00 94.10  ?  773 LEU A C     1 
ATOM   5976  O  O     . LEU A 1 754 ? 187.856 174.227 252.051 1.00 94.33  ?  773 LEU A O     1 
ATOM   5977  C  CB    . LEU A 1 754 ? 189.840 173.402 249.893 1.00 95.53  ?  773 LEU A CB    1 
ATOM   5978  C  CG    . LEU A 1 754 ? 190.087 174.155 248.583 1.00 94.33  ?  773 LEU A CG    1 
ATOM   5979  C  CD1   . LEU A 1 754 ? 191.485 174.745 248.541 1.00 96.44  ?  773 LEU A CD1   1 
ATOM   5980  C  CD2   . LEU A 1 754 ? 189.859 173.239 247.393 1.00 94.16  ?  773 LEU A CD2   1 
ATOM   5981  N  N     . ARG A 1 755 ? 189.342 172.995 253.224 1.00 94.66  ?  774 ARG A N     1 
ATOM   5982  C  CA    . ARG A 1 755 ? 188.366 172.643 254.250 1.00 96.08  ?  774 ARG A CA    1 
ATOM   5983  C  C     . ARG A 1 755 ? 187.839 173.871 254.988 1.00 97.43  ?  774 ARG A C     1 
ATOM   5984  O  O     . ARG A 1 755 ? 186.675 173.889 255.403 1.00 98.35  ?  774 ARG A O     1 
ATOM   5985  C  CB    . ARG A 1 755 ? 188.986 171.654 255.240 1.00 96.04  ?  774 ARG A CB    1 
ATOM   5986  C  CG    . ARG A 1 755 ? 188.031 171.139 256.307 1.00 95.50  ?  774 ARG A CG    1 
ATOM   5987  C  CD    . ARG A 1 755 ? 186.805 170.482 255.694 1.00 93.56  ?  774 ARG A CD    1 
ATOM   5988  N  NE    . ARG A 1 755 ? 185.956 169.864 256.705 1.00 88.94  ?  774 ARG A NE    1 
ATOM   5989  C  CZ    . ARG A 1 755 ? 186.074 168.610 257.119 1.00 92.84  ?  774 ARG A CZ    1 
ATOM   5990  N  NH1   . ARG A 1 755 ? 187.002 167.805 256.630 1.00 93.87  1  774 ARG A NH1   1 
ATOM   5991  N  NH2   . ARG A 1 755 ? 185.241 168.153 258.050 1.00 94.80  ?  774 ARG A NH2   1 
ATOM   5992  N  N     . LYS A 1 756 ? 188.669 174.905 255.158 1.00 98.88  ?  775 LYS A N     1 
ATOM   5993  C  CA    . LYS A 1 756 ? 188.248 176.057 255.951 1.00 97.94  ?  775 LYS A CA    1 
ATOM   5994  C  C     . LYS A 1 756 ? 187.238 176.928 255.210 1.00 97.76  ?  775 LYS A C     1 
ATOM   5995  O  O     . LYS A 1 756 ? 186.351 177.513 255.841 1.00 98.25  ?  775 LYS A O     1 
ATOM   5996  C  CB    . LYS A 1 756 ? 189.460 176.892 256.369 1.00 96.74  ?  775 LYS A CB    1 
ATOM   5997  C  CG    . LYS A 1 756 ? 190.325 177.385 255.221 1.00 99.83  ?  775 LYS A CG    1 
ATOM   5998  C  CD    . LYS A 1 756 ? 191.630 177.977 255.733 1.00 96.96  ?  775 LYS A CD    1 
ATOM   5999  C  CE    . LYS A 1 756 ? 192.561 178.352 254.591 1.00 95.73  ?  775 LYS A CE    1 
ATOM   6000  N  NZ    . LYS A 1 756 ? 191.963 179.390 253.705 1.00 96.09  1  775 LYS A NZ    1 
ATOM   6001  N  N     . ILE A 1 757 ? 187.352 177.032 253.883 1.00 94.70  ?  776 ILE A N     1 
ATOM   6002  C  CA    . ILE A 1 757 ? 186.391 177.811 253.107 1.00 92.72  ?  776 ILE A CA    1 
ATOM   6003  C  C     . ILE A 1 757 ? 185.043 177.110 253.005 1.00 93.35  ?  776 ILE A C     1 
ATOM   6004  O  O     . ILE A 1 757 ? 184.064 177.717 252.553 1.00 95.14  ?  776 ILE A O     1 
ATOM   6005  C  CB    . ILE A 1 757 ? 186.975 178.121 251.710 1.00 94.16  ?  776 ILE A CB    1 
ATOM   6006  C  CG1   . ILE A 1 757 ? 188.373 178.724 251.838 1.00 97.44  ?  776 ILE A CG1   1 
ATOM   6007  C  CG2   . ILE A 1 757 ? 186.119 179.124 250.955 1.00 95.19  ?  776 ILE A CG2   1 
ATOM   6008  C  CD1   . ILE A 1 757 ? 189.485 177.770 251.499 1.00 98.38  ?  776 ILE A CD1   1 
ATOM   6009  N  N     . HIS A 1 758 ? 184.965 175.850 253.444 1.00 98.18  ?  777 HIS A N     1 
ATOM   6010  C  CA    . HIS A 1 758 ? 183.729 175.063 253.430 1.00 100.83 ?  777 HIS A CA    1 
ATOM   6011  C  C     . HIS A 1 758 ? 183.243 174.825 251.999 1.00 101.30 ?  777 HIS A C     1 
ATOM   6012  O  O     . HIS A 1 758 ? 182.092 175.100 251.658 1.00 101.32 ?  777 HIS A O     1 
ATOM   6013  C  CB    . HIS A 1 758 ? 182.632 175.716 254.280 1.00 100.71 ?  777 HIS A CB    1 
ATOM   6014  C  CG    . HIS A 1 758 ? 182.994 175.873 255.724 1.00 102.90 ?  777 HIS A CG    1 
ATOM   6015  N  ND1   . HIS A 1 758 ? 183.702 176.955 256.200 1.00 100.93 ?  777 HIS A ND1   1 
ATOM   6016  C  CD2   . HIS A 1 758 ? 182.743 175.087 256.797 1.00 101.43 ?  777 HIS A CD2   1 
ATOM   6017  C  CE1   . HIS A 1 758 ? 183.872 176.829 257.504 1.00 99.54  ?  777 HIS A CE1   1 
ATOM   6018  N  NE2   . HIS A 1 758 ? 183.300 175.703 257.891 1.00 101.88 ?  777 HIS A NE2   1 
ATOM   6019  N  N     . CYS A 1 759 ? 184.139 174.312 251.159 1.00 91.87  ?  778 CYS A N     1 
ATOM   6020  C  CA    . CYS A 1 759 ? 183.746 173.870 249.829 1.00 88.98  ?  778 CYS A CA    1 
ATOM   6021  C  C     . CYS A 1 759 ? 182.782 172.696 249.944 1.00 89.21  ?  778 CYS A C     1 
ATOM   6022  O  O     . CYS A 1 759 ? 182.907 171.860 250.840 1.00 89.98  ?  778 CYS A O     1 
ATOM   6023  C  CB    . CYS A 1 759 ? 184.974 173.470 249.013 1.00 89.09  ?  778 CYS A CB    1 
ATOM   6024  S  SG    . CYS A 1 759 ? 185.879 174.858 248.289 1.00 99.12  ?  778 CYS A SG    1 
ATOM   6025  N  N     . ARG A 1 760 ? 181.808 172.639 249.037 1.00 81.59  ?  779 ARG A N     1 
ATOM   6026  C  CA    . ARG A 1 760 ? 180.747 171.643 249.156 1.00 77.26  ?  779 ARG A CA    1 
ATOM   6027  C  C     . ARG A 1 760 ? 181.271 170.236 248.891 1.00 77.55  ?  779 ARG A C     1 
ATOM   6028  O  O     . ARG A 1 760 ? 181.226 169.367 249.773 1.00 80.96  ?  779 ARG A O     1 
ATOM   6029  C  CB    . ARG A 1 760 ? 179.595 171.982 248.208 1.00 74.83  ?  779 ARG A CB    1 
ATOM   6030  C  CG    . ARG A 1 760 ? 178.327 171.188 248.488 1.00 76.67  ?  779 ARG A CG    1 
ATOM   6031  C  CD    . ARG A 1 760 ? 177.435 171.904 249.490 1.00 76.76  ?  779 ARG A CD    1 
ATOM   6032  N  NE    . ARG A 1 760 ? 176.180 171.196 249.715 1.00 78.29  ?  779 ARG A NE    1 
ATOM   6033  C  CZ    . ARG A 1 760 ? 175.119 171.279 248.925 1.00 78.52  ?  779 ARG A CZ    1 
ATOM   6034  N  NH1   . ARG A 1 760 ? 175.119 172.042 247.844 1.00 76.97  1  779 ARG A NH1   1 
ATOM   6035  N  NH2   . ARG A 1 760 ? 174.027 170.582 249.229 1.00 77.46  ?  779 ARG A NH2   1 
ATOM   6036  N  N     . VAL A 1 761 ? 181.769 169.983 247.680 1.00 67.05  ?  780 VAL A N     1 
ATOM   6037  C  CA    . VAL A 1 761 ? 182.193 168.641 247.308 1.00 62.22  ?  780 VAL A CA    1 
ATOM   6038  C  C     . VAL A 1 761 ? 183.588 168.687 246.703 1.00 65.52  ?  780 VAL A C     1 
ATOM   6039  O  O     . VAL A 1 761 ? 184.026 169.704 246.154 1.00 72.31  ?  780 VAL A O     1 
ATOM   6040  C  CB    . VAL A 1 761 ? 181.193 167.969 246.341 1.00 64.42  ?  780 VAL A CB    1 
ATOM   6041  C  CG1   . VAL A 1 761 ? 179.825 167.867 246.985 1.00 66.57  ?  780 VAL A CG1   1 
ATOM   6042  C  CG2   . VAL A 1 761 ? 181.092 168.751 245.067 1.00 64.23  ?  780 VAL A CG2   1 
ATOM   6043  N  N     . ILE A 1 762 ? 184.286 167.562 246.817 1.00 59.87  ?  781 ILE A N     1 
ATOM   6044  C  CA    . ILE A 1 762 ? 185.688 167.435 246.442 1.00 58.88  ?  781 ILE A CA    1 
ATOM   6045  C  C     . ILE A 1 762 ? 185.829 166.233 245.517 1.00 60.23  ?  781 ILE A C     1 
ATOM   6046  O  O     . ILE A 1 762 ? 185.212 165.187 245.748 1.00 62.87  ?  781 ILE A O     1 
ATOM   6047  C  CB    . ILE A 1 762 ? 186.595 167.280 247.684 1.00 55.37  ?  781 ILE A CB    1 
ATOM   6048  C  CG1   . ILE A 1 762 ? 186.539 168.531 248.568 1.00 59.06  ?  781 ILE A CG1   1 
ATOM   6049  C  CG2   . ILE A 1 762 ? 188.025 167.001 247.278 1.00 56.69  ?  781 ILE A CG2   1 
ATOM   6050  C  CD1   . ILE A 1 762 ? 185.458 168.496 249.637 1.00 64.95  ?  781 ILE A CD1   1 
ATOM   6051  N  N     . GLN A 1 763 ? 186.639 166.384 244.469 1.00 55.62  ?  782 GLN A N     1 
ATOM   6052  C  CA    . GLN A 1 763 ? 186.890 165.317 243.508 1.00 51.56  ?  782 GLN A CA    1 
ATOM   6053  C  C     . GLN A 1 763 ? 188.375 165.303 243.186 1.00 58.03  ?  782 GLN A C     1 
ATOM   6054  O  O     . GLN A 1 763 ? 188.937 166.337 242.813 1.00 64.05  ?  782 GLN A O     1 
ATOM   6055  C  CB    . GLN A 1 763 ? 186.064 165.524 242.235 1.00 51.05  ?  782 GLN A CB    1 
ATOM   6056  C  CG    . GLN A 1 763 ? 186.666 164.891 240.994 1.00 56.86  ?  782 GLN A CG    1 
ATOM   6057  C  CD    . GLN A 1 763 ? 185.756 164.998 239.789 1.00 57.29  ?  782 GLN A CD    1 
ATOM   6058  O  OE1   . GLN A 1 763 ? 184.547 165.188 239.922 1.00 60.25  ?  782 GLN A OE1   1 
ATOM   6059  N  NE2   . GLN A 1 763 ? 186.335 164.880 238.601 1.00 57.27  ?  782 GLN A NE2   1 
ATOM   6060  N  N     . GLY A 1 764 ? 189.010 164.147 243.336 1.00 56.31  ?  783 GLY A N     1 
ATOM   6061  C  CA    . GLY A 1 764 ? 190.425 164.044 243.048 1.00 51.85  ?  783 GLY A CA    1 
ATOM   6062  C  C     . GLY A 1 764 ? 190.987 162.725 243.538 1.00 54.25  ?  783 GLY A C     1 
ATOM   6063  O  O     . GLY A 1 764 ? 190.252 161.824 243.947 1.00 57.47  ?  783 GLY A O     1 
ATOM   6064  N  N     . TYR A 1 765 ? 192.319 162.636 243.485 1.00 50.47  ?  784 TYR A N     1 
ATOM   6065  C  CA    . TYR A 1 765 ? 193.014 161.414 243.875 1.00 42.72  ?  784 TYR A CA    1 
ATOM   6066  C  C     . TYR A 1 765 ? 193.076 161.228 245.385 1.00 45.35  ?  784 TYR A C     1 
ATOM   6067  O  O     . TYR A 1 765 ? 193.333 160.110 245.845 1.00 49.70  ?  784 TYR A O     1 
ATOM   6068  C  CB    . TYR A 1 765 ? 194.436 161.403 243.307 1.00 45.61  ?  784 TYR A CB    1 
ATOM   6069  C  CG    . TYR A 1 765 ? 194.527 161.312 241.798 1.00 43.25  ?  784 TYR A CG    1 
ATOM   6070  C  CD1   . TYR A 1 765 ? 193.392 161.158 241.014 1.00 44.02  ?  784 TYR A CD1   1 
ATOM   6071  C  CD2   . TYR A 1 765 ? 195.757 161.379 241.159 1.00 45.70  ?  784 TYR A CD2   1 
ATOM   6072  C  CE1   . TYR A 1 765 ? 193.481 161.076 239.637 1.00 44.51  ?  784 TYR A CE1   1 
ATOM   6073  C  CE2   . TYR A 1 765 ? 195.855 161.298 239.785 1.00 47.32  ?  784 TYR A CE2   1 
ATOM   6074  C  CZ    . TYR A 1 765 ? 194.716 161.146 239.028 1.00 45.71  ?  784 TYR A CZ    1 
ATOM   6075  O  OH    . TYR A 1 765 ? 194.813 161.065 237.658 1.00 46.00  ?  784 TYR A OH    1 
ATOM   6076  N  N     . PHE A 1 766 ? 192.860 162.290 246.166 1.00 67.66  ?  785 PHE A N     1 
ATOM   6077  C  CA    . PHE A 1 766 ? 192.961 162.177 247.617 1.00 68.47  ?  785 PHE A CA    1 
ATOM   6078  C  C     . PHE A 1 766 ? 191.913 161.241 248.205 1.00 66.06  ?  785 PHE A C     1 
ATOM   6079  O  O     . PHE A 1 766 ? 192.110 160.726 249.312 1.00 70.26  ?  785 PHE A O     1 
ATOM   6080  C  CB    . PHE A 1 766 ? 192.847 163.557 248.265 1.00 70.33  ?  785 PHE A CB    1 
ATOM   6081  C  CG    . PHE A 1 766 ? 193.123 163.555 249.741 1.00 69.77  ?  785 PHE A CG    1 
ATOM   6082  C  CD1   . PHE A 1 766 ? 194.388 163.260 250.221 1.00 70.30  ?  785 PHE A CD1   1 
ATOM   6083  C  CD2   . PHE A 1 766 ? 192.118 163.845 250.649 1.00 70.77  ?  785 PHE A CD2   1 
ATOM   6084  C  CE1   . PHE A 1 766 ? 194.645 163.252 251.579 1.00 72.80  ?  785 PHE A CE1   1 
ATOM   6085  C  CE2   . PHE A 1 766 ? 192.369 163.840 252.008 1.00 72.08  ?  785 PHE A CE2   1 
ATOM   6086  C  CZ    . PHE A 1 766 ? 193.634 163.544 252.473 1.00 72.94  ?  785 PHE A CZ    1 
ATOM   6087  N  N     . PHE A 1 767 ? 190.817 161.002 247.497 1.00 60.11  ?  786 PHE A N     1 
ATOM   6088  C  CA    . PHE A 1 767 ? 189.769 160.113 247.979 1.00 63.85  ?  786 PHE A CA    1 
ATOM   6089  C  C     . PHE A 1 767 ? 189.574 158.884 247.108 1.00 67.04  ?  786 PHE A C     1 
ATOM   6090  O  O     . PHE A 1 767 ? 189.407 157.783 247.637 1.00 70.92  ?  786 PHE A O     1 
ATOM   6091  C  CB    . PHE A 1 767 ? 188.443 160.877 248.097 1.00 69.89  ?  786 PHE A CB    1 
ATOM   6092  C  CG    . PHE A 1 767 ? 188.434 161.899 249.197 1.00 70.21  ?  786 PHE A CG    1 
ATOM   6093  C  CD1   . PHE A 1 767 ? 188.551 161.509 250.521 1.00 71.46  ?  786 PHE A CD1   1 
ATOM   6094  C  CD2   . PHE A 1 767 ? 188.327 163.248 248.908 1.00 67.57  ?  786 PHE A CD2   1 
ATOM   6095  C  CE1   . PHE A 1 767 ? 188.547 162.445 251.537 1.00 71.25  ?  786 PHE A CE1   1 
ATOM   6096  C  CE2   . PHE A 1 767 ? 188.327 164.190 249.920 1.00 67.97  ?  786 PHE A CE2   1 
ATOM   6097  C  CZ    . PHE A 1 767 ? 188.435 163.787 251.237 1.00 70.45  ?  786 PHE A CZ    1 
ATOM   6098  N  N     . SER A 1 768 ? 189.596 159.037 245.786 1.00 57.73  ?  787 SER A N     1 
ATOM   6099  C  CA    . SER A 1 768 ? 189.433 157.889 244.898 1.00 55.01  ?  787 SER A CA    1 
ATOM   6100  C  C     . SER A 1 768 ? 189.942 158.248 243.513 1.00 52.08  ?  787 SER A C     1 
ATOM   6101  O  O     . SER A 1 768 ? 189.472 159.220 242.914 1.00 52.22  ?  787 SER A O     1 
ATOM   6102  C  CB    . SER A 1 768 ? 187.970 157.453 244.832 1.00 58.90  ?  787 SER A CB    1 
ATOM   6103  O  OG    . SER A 1 768 ? 187.753 156.595 243.727 1.00 55.80  ?  787 SER A OG    1 
ATOM   6104  N  N     . ARG A 1 769 ? 190.893 157.466 243.009 1.00 51.05  ?  788 ARG A N     1 
ATOM   6105  C  CA    . ARG A 1 769 ? 191.236 157.525 241.600 1.00 43.85  ?  788 ARG A CA    1 
ATOM   6106  C  C     . ARG A 1 769 ? 190.054 156.999 240.785 1.00 42.72  ?  788 ARG A C     1 
ATOM   6107  O  O     . ARG A 1 769 ? 189.215 156.265 241.311 1.00 51.12  ?  788 ARG A O     1 
ATOM   6108  C  CB    . ARG A 1 769 ? 192.488 156.688 241.329 1.00 45.42  ?  788 ARG A CB    1 
ATOM   6109  C  CG    . ARG A 1 769 ? 193.347 157.148 240.160 1.00 45.75  ?  788 ARG A CG    1 
ATOM   6110  C  CD    . ARG A 1 769 ? 194.603 156.303 240.018 1.00 46.93  ?  788 ARG A CD    1 
ATOM   6111  N  NE    . ARG A 1 769 ? 195.538 156.532 241.113 1.00 50.79  ?  788 ARG A NE    1 
ATOM   6112  C  CZ    . ARG A 1 769 ? 196.523 157.420 241.086 1.00 54.78  ?  788 ARG A CZ    1 
ATOM   6113  N  NH1   . ARG A 1 769 ? 196.734 158.187 240.029 1.00 54.49  1  788 ARG A NH1   1 
ATOM   6114  N  NH2   . ARG A 1 769 ? 197.317 157.540 242.146 1.00 54.27  ?  788 ARG A NH2   1 
ATOM   6115  N  N     . PRO A 1 770 ? 189.934 157.400 239.507 1.00 35.36  ?  789 PRO A N     1 
ATOM   6116  C  CA    . PRO A 1 770 ? 188.874 156.833 238.661 1.00 38.33  ?  789 PRO A CA    1 
ATOM   6117  C  C     . PRO A 1 770 ? 188.829 155.312 238.713 1.00 46.32  ?  789 PRO A C     1 
ATOM   6118  O  O     . PRO A 1 770 ? 189.778 154.636 238.305 1.00 52.10  ?  789 PRO A O     1 
ATOM   6119  C  CB    . PRO A 1 770 ? 189.244 157.341 237.264 1.00 39.48  ?  789 PRO A CB    1 
ATOM   6120  C  CG    . PRO A 1 770 ? 189.875 158.667 237.524 1.00 45.58  ?  789 PRO A CG    1 
ATOM   6121  C  CD    . PRO A 1 770 ? 190.542 158.591 238.884 1.00 45.66  ?  789 PRO A CD    1 
ATOM   6122  N  N     . LEU A 1 771 ? 187.711 154.765 239.223 1.00 42.51  ?  790 LEU A N     1 
ATOM   6123  C  CA    . LEU A 1 771 ? 187.568 153.333 239.457 1.00 31.32  ?  790 LEU A CA    1 
ATOM   6124  C  C     . LEU A 1 771 ? 186.682 152.702 238.398 1.00 40.61  ?  790 LEU A C     1 
ATOM   6125  O  O     . LEU A 1 771 ? 185.684 153.311 237.985 1.00 51.07  ?  790 LEU A O     1 
ATOM   6126  C  CB    . LEU A 1 771 ? 186.978 153.071 240.838 1.00 39.49  ?  790 LEU A CB    1 
ATOM   6127  C  CG    . LEU A 1 771 ? 187.836 153.485 242.032 1.00 47.01  ?  790 LEU A CG    1 
ATOM   6128  C  CD1   . LEU A 1 771 ? 187.006 153.476 243.298 1.00 45.62  ?  790 LEU A CD1   1 
ATOM   6129  C  CD2   . LEU A 1 771 ? 189.038 152.567 242.168 1.00 50.15  ?  790 LEU A CD2   1 
ATOM   6130  N  N     . PRO A 1 772 ? 187.019 151.501 237.938 1.00 49.44  ?  791 PRO A N     1 
ATOM   6131  C  CA    . PRO A 1 772 ? 186.174 150.816 236.956 1.00 50.92  ?  791 PRO A CA    1 
ATOM   6132  C  C     . PRO A 1 772 ? 184.814 150.432 237.524 1.00 55.07  ?  791 PRO A C     1 
ATOM   6133  O  O     . PRO A 1 772 ? 184.622 150.262 238.732 1.00 57.40  ?  791 PRO A O     1 
ATOM   6134  C  CB    . PRO A 1 772 ? 186.992 149.573 236.595 1.00 50.65  ?  791 PRO A CB    1 
ATOM   6135  C  CG    . PRO A 1 772 ? 188.403 149.981 236.833 1.00 58.84  ?  791 PRO A CG    1 
ATOM   6136  C  CD    . PRO A 1 772 ? 188.362 150.903 238.022 1.00 55.91  ?  791 PRO A CD    1 
ATOM   6137  N  N     . ALA A 1 773 ? 183.861 150.282 236.601 1.00 51.85  ?  792 ALA A N     1 
ATOM   6138  C  CA    . ALA A 1 773 ? 182.474 150.028 236.974 1.00 50.75  ?  792 ALA A CA    1 
ATOM   6139  C  C     . ALA A 1 773 ? 182.301 148.688 237.678 1.00 51.52  ?  792 ALA A C     1 
ATOM   6140  O  O     . ALA A 1 773 ? 181.429 148.558 238.544 1.00 53.92  ?  792 ALA A O     1 
ATOM   6141  C  CB    . ALA A 1 773 ? 181.583 150.092 235.734 1.00 49.59  ?  792 ALA A CB    1 
ATOM   6142  N  N     . GLU A 1 774 ? 183.107 147.682 237.324 1.00 55.46  ?  793 GLU A N     1 
ATOM   6143  C  CA    . GLU A 1 774 ? 182.904 146.356 237.898 1.00 56.40  ?  793 GLU A CA    1 
ATOM   6144  C  C     . GLU A 1 774 ? 183.259 146.310 239.380 1.00 55.38  ?  793 GLU A C     1 
ATOM   6145  O  O     . GLU A 1 774 ? 182.847 145.378 240.080 1.00 58.31  ?  793 GLU A O     1 
ATOM   6146  C  CB    . GLU A 1 774 ? 183.705 145.307 237.122 1.00 59.18  ?  793 GLU A CB    1 
ATOM   6147  C  CG    . GLU A 1 774 ? 185.212 145.410 237.266 1.00 59.89  ?  793 GLU A CG    1 
ATOM   6148  C  CD    . GLU A 1 774 ? 185.831 146.369 236.270 1.00 61.82  ?  793 GLU A CD    1 
ATOM   6149  O  OE1   . GLU A 1 774 ? 185.087 147.172 235.668 1.00 63.24  ?  793 GLU A OE1   1 
ATOM   6150  O  OE2   . GLU A 1 774 ? 187.065 146.318 236.086 1.00 60.48  -1 793 GLU A OE2   1 
ATOM   6151  N  N     . GLU A 1 775 ? 184.014 147.290 239.881 1.00 55.30  ?  794 GLU A N     1 
ATOM   6152  C  CA    . GLU A 1 775 ? 184.281 147.380 241.313 1.00 55.90  ?  794 GLU A CA    1 
ATOM   6153  C  C     . GLU A 1 775 ? 183.893 148.730 241.907 1.00 55.82  ?  794 GLU A C     1 
ATOM   6154  O  O     . GLU A 1 775 ? 184.290 149.032 243.040 1.00 58.04  ?  794 GLU A O     1 
ATOM   6155  C  CB    . GLU A 1 775 ? 185.751 147.065 241.619 1.00 60.32  ?  794 GLU A CB    1 
ATOM   6156  C  CG    . GLU A 1 775 ? 186.744 148.183 241.349 1.00 61.41  ?  794 GLU A CG    1 
ATOM   6157  C  CD    . GLU A 1 775 ? 187.446 148.028 240.019 1.00 66.20  ?  794 GLU A CD    1 
ATOM   6158  O  OE1   . GLU A 1 775 ? 186.850 147.446 239.091 1.00 64.83  ?  794 GLU A OE1   1 
ATOM   6159  O  OE2   . GLU A 1 775 ? 188.610 148.467 239.912 1.00 68.46  -1 794 GLU A OE2   1 
ATOM   6160  N  N     . ILE A 1 776 ? 183.127 149.550 241.181 1.00 63.76  ?  795 ILE A N     1 
ATOM   6161  C  CA    . ILE A 1 776 ? 182.469 150.696 241.813 1.00 65.09  ?  795 ILE A CA    1 
ATOM   6162  C  C     . ILE A 1 776 ? 181.591 150.268 242.991 1.00 67.92  ?  795 ILE A C     1 
ATOM   6163  O  O     . ILE A 1 776 ? 181.711 150.868 244.069 1.00 70.99  ?  795 ILE A O     1 
ATOM   6164  C  CB    . ILE A 1 776 ? 181.704 151.517 240.765 1.00 57.63  ?  795 ILE A CB    1 
ATOM   6165  C  CG1   . ILE A 1 776 ? 182.663 152.387 239.949 1.00 61.58  ?  795 ILE A CG1   1 
ATOM   6166  C  CG2   . ILE A 1 776 ? 180.638 152.379 241.423 1.00 52.20  ?  795 ILE A CG2   1 
ATOM   6167  C  CD1   . ILE A 1 776 ? 183.416 153.406 240.775 1.00 62.80  ?  795 ILE A CD1   1 
ATOM   6168  N  N     . PRO A 1 777 ? 180.713 149.261 242.868 1.00 62.19  ?  796 PRO A N     1 
ATOM   6169  C  CA    . PRO A 1 777 ? 179.919 148.851 244.040 1.00 59.53  ?  796 PRO A CA    1 
ATOM   6170  C  C     . PRO A 1 777 ? 180.759 148.384 245.214 1.00 56.35  ?  796 PRO A C     1 
ATOM   6171  O  O     . PRO A 1 777 ? 180.356 148.582 246.367 1.00 60.31  ?  796 PRO A O     1 
ATOM   6172  C  CB    . PRO A 1 777 ? 179.048 147.716 243.485 1.00 58.72  ?  796 PRO A CB    1 
ATOM   6173  C  CG    . PRO A 1 777 ? 178.915 148.035 242.047 1.00 59.27  ?  796 PRO A CG    1 
ATOM   6174  C  CD    . PRO A 1 777 ? 180.264 148.554 241.654 1.00 58.49  ?  796 PRO A CD    1 
ATOM   6175  N  N     . GLY A 1 778 ? 181.913 147.764 244.960 1.00 59.76  ?  797 GLY A N     1 
ATOM   6176  C  CA    . GLY A 1 778 ? 182.782 147.375 246.059 1.00 63.73  ?  797 GLY A CA    1 
ATOM   6177  C  C     . GLY A 1 778 ? 183.270 148.570 246.853 1.00 65.03  ?  797 GLY A C     1 
ATOM   6178  O  O     . GLY A 1 778 ? 183.252 148.564 248.086 1.00 67.65  ?  797 GLY A O     1 
ATOM   6179  N  N     . TRP A 1 779 ? 183.702 149.620 246.151 1.00 70.38  ?  798 TRP A N     1 
ATOM   6180  C  CA    . TRP A 1 779 ? 184.094 150.852 246.827 1.00 69.18  ?  798 TRP A CA    1 
ATOM   6181  C  C     . TRP A 1 779 ? 182.914 151.461 247.572 1.00 73.20  ?  798 TRP A C     1 
ATOM   6182  O  O     . TRP A 1 779 ? 183.064 151.929 248.708 1.00 76.99  ?  798 TRP A O     1 
ATOM   6183  C  CB    . TRP A 1 779 ? 184.665 151.846 245.816 1.00 68.81  ?  798 TRP A CB    1 
ATOM   6184  C  CG    . TRP A 1 779 ? 185.592 152.865 246.412 1.00 70.46  ?  798 TRP A CG    1 
ATOM   6185  C  CD1   . TRP A 1 779 ? 186.939 152.740 246.593 1.00 71.33  ?  798 TRP A CD1   1 
ATOM   6186  C  CD2   . TRP A 1 779 ? 185.242 154.169 246.894 1.00 72.58  ?  798 TRP A CD2   1 
ATOM   6187  N  NE1   . TRP A 1 779 ? 187.448 153.883 247.161 1.00 71.06  ?  798 TRP A NE1   1 
ATOM   6188  C  CE2   . TRP A 1 779 ? 186.427 154.775 247.356 1.00 73.74  ?  798 TRP A CE2   1 
ATOM   6189  C  CE3   . TRP A 1 779 ? 184.042 154.881 246.982 1.00 73.97  ?  798 TRP A CE3   1 
ATOM   6190  C  CZ2   . TRP A 1 779 ? 186.447 156.059 247.897 1.00 75.70  ?  798 TRP A CZ2   1 
ATOM   6191  C  CZ3   . TRP A 1 779 ? 184.064 156.155 247.520 1.00 74.55  ?  798 TRP A CZ3   1 
ATOM   6192  C  CH2   . TRP A 1 779 ? 185.258 156.730 247.971 1.00 75.15  ?  798 TRP A CH2   1 
ATOM   6193  N  N     . MET A 1 780 ? 181.728 151.441 246.955 1.00 71.63  ?  799 MET A N     1 
ATOM   6194  C  CA    . MET A 1 780 ? 180.542 151.999 247.598 1.00 69.91  ?  799 MET A CA    1 
ATOM   6195  C  C     . MET A 1 780 ? 180.249 151.294 248.916 1.00 70.61  ?  799 MET A C     1 
ATOM   6196  O  O     . MET A 1 780 ? 179.949 151.939 249.928 1.00 74.29  ?  799 MET A O     1 
ATOM   6197  C  CB    . MET A 1 780 ? 179.333 151.888 246.666 1.00 68.73  ?  799 MET A CB    1 
ATOM   6198  C  CG    . MET A 1 780 ? 179.470 152.617 245.343 1.00 69.12  ?  799 MET A CG    1 
ATOM   6199  S  SD    . MET A 1 780 ? 179.929 154.344 245.529 1.00 80.55  ?  799 MET A SD    1 
ATOM   6200  C  CE    . MET A 1 780 ? 181.465 154.378 244.608 1.00 74.51  ?  799 MET A CE    1 
ATOM   6201  N  N     . SER A 1 781 ? 180.332 149.965 248.923 1.00 71.26  ?  800 SER A N     1 
ATOM   6202  C  CA    . SER A 1 781 ? 179.975 149.178 250.094 1.00 74.64  ?  800 SER A CA    1 
ATOM   6203  C  C     . SER A 1 781 ? 181.119 149.008 251.086 1.00 73.62  ?  800 SER A C     1 
ATOM   6204  O  O     . SER A 1 781 ? 180.881 148.524 252.198 1.00 73.91  ?  800 SER A O     1 
ATOM   6205  C  CB    . SER A 1 781 ? 179.471 147.796 249.665 1.00 76.78  ?  800 SER A CB    1 
ATOM   6206  O  OG    . SER A 1 781 ? 178.330 147.905 248.832 1.00 74.92  ?  800 SER A OG    1 
ATOM   6207  N  N     . SER A 1 782 ? 182.343 149.387 250.726 1.00 78.40  ?  801 SER A N     1 
ATOM   6208  C  CA    . SER A 1 782 ? 183.485 149.190 251.611 1.00 80.30  ?  801 SER A CA    1 
ATOM   6209  C  C     . SER A 1 782 ? 184.063 150.474 252.185 1.00 81.77  ?  801 SER A C     1 
ATOM   6210  O  O     . SER A 1 782 ? 184.472 150.486 253.347 1.00 80.48  ?  801 SER A O     1 
ATOM   6211  C  CB    . SER A 1 782 ? 184.595 148.434 250.871 1.00 79.85  ?  801 SER A CB    1 
ATOM   6212  O  OG    . SER A 1 782 ? 185.773 148.362 251.656 1.00 77.41  ?  801 SER A OG    1 
ATOM   6213  N  N     . VAL A 1 783 ? 184.115 151.558 251.416 1.00 85.37  ?  802 VAL A N     1 
ATOM   6214  C  CA    . VAL A 1 783 ? 184.887 152.727 251.833 1.00 83.93  ?  802 VAL A CA    1 
ATOM   6215  C  C     . VAL A 1 783 ? 184.014 153.762 252.530 1.00 83.98  ?  802 VAL A C     1 
ATOM   6216  O  O     . VAL A 1 783 ? 184.387 154.291 253.580 1.00 83.79  ?  802 VAL A O     1 
ATOM   6217  C  CB    . VAL A 1 783 ? 185.620 153.332 250.619 1.00 82.49  ?  802 VAL A CB    1 
ATOM   6218  C  CG1   . VAL A 1 783 ? 186.495 154.493 251.059 1.00 81.85  ?  802 VAL A CG1   1 
ATOM   6219  C  CG2   . VAL A 1 783 ? 186.453 152.266 249.932 1.00 83.37  ?  802 VAL A CG2   1 
ATOM   6220  N  N     . LEU A 1 784 ? 182.855 154.073 251.962 1.00 85.35  ?  803 LEU A N     1 
ATOM   6221  C  CA    . LEU A 1 784 ? 182.008 155.112 252.528 1.00 88.16  ?  803 LEU A CA    1 
ATOM   6222  C  C     . LEU A 1 784 ? 181.504 154.689 253.907 1.00 87.21  ?  803 LEU A C     1 
ATOM   6223  O  O     . LEU A 1 784 ? 181.158 153.519 254.109 1.00 86.51  ?  803 LEU A O     1 
ATOM   6224  C  CB    . LEU A 1 784 ? 180.824 155.398 251.603 1.00 85.06  ?  803 LEU A CB    1 
ATOM   6225  C  CG    . LEU A 1 784 ? 181.147 155.969 250.221 1.00 85.60  ?  803 LEU A CG    1 
ATOM   6226  C  CD1   . LEU A 1 784 ? 180.025 155.665 249.240 1.00 83.80  ?  803 LEU A CD1   1 
ATOM   6227  C  CD2   . LEU A 1 784 ? 181.398 157.464 250.303 1.00 86.12  ?  803 LEU A CD2   1 
ATOM   6228  N  N     . PRO A 1 785 ? 181.450 155.611 254.883 1.00 86.64  ?  804 PRO A N     1 
ATOM   6229  C  CA    . PRO A 1 785 ? 181.928 156.997 254.797 1.00 87.66  ?  804 PRO A CA    1 
ATOM   6230  C  C     . PRO A 1 785 ? 183.438 157.113 255.003 1.00 85.58  ?  804 PRO A C     1 
ATOM   6231  O  O     . PRO A 1 785 ? 184.053 156.191 255.536 1.00 83.01  ?  804 PRO A O     1 
ATOM   6232  C  CB    . PRO A 1 785 ? 181.176 157.704 255.935 1.00 87.98  ?  804 PRO A CB    1 
ATOM   6233  C  CG    . PRO A 1 785 ? 180.123 156.727 256.397 1.00 86.07  ?  804 PRO A CG    1 
ATOM   6234  C  CD    . PRO A 1 785 ? 180.707 155.382 256.131 1.00 85.05  ?  804 PRO A CD    1 
ATOM   6235  N  N     . LEU A 1 786 ? 184.021 158.239 254.598 1.00 90.29  ?  805 LEU A N     1 
ATOM   6236  C  CA    . LEU A 1 786 ? 185.455 158.471 254.732 1.00 92.02  ?  805 LEU A CA    1 
ATOM   6237  C  C     . LEU A 1 786 ? 185.814 159.443 255.845 1.00 91.38  ?  805 LEU A C     1 
ATOM   6238  O  O     . LEU A 1 786 ? 186.819 159.237 256.530 1.00 89.10  ?  805 LEU A O     1 
ATOM   6239  C  CB    . LEU A 1 786 ? 186.036 158.987 253.410 1.00 93.26  ?  805 LEU A CB    1 
ATOM   6240  C  CG    . LEU A 1 786 ? 186.116 157.985 252.256 1.00 93.53  ?  805 LEU A CG    1 
ATOM   6241  C  CD1   . LEU A 1 786 ? 184.893 158.091 251.360 1.00 90.55  ?  805 LEU A CD1   1 
ATOM   6242  C  CD2   . LEU A 1 786 ? 187.394 158.186 251.455 1.00 91.13  ?  805 LEU A CD2   1 
ATOM   6243  N  N     . LYS A 1 787 ? 185.018 160.493 256.038 1.00 99.52  ?  806 LYS A N     1 
ATOM   6244  C  CA    . LYS A 1 787 ? 185.269 161.506 257.065 1.00 101.49 ?  806 LYS A CA    1 
ATOM   6245  C  C     . LYS A 1 787 ? 186.656 162.130 256.928 1.00 97.15  ?  806 LYS A C     1 
ATOM   6246  O  O     . LYS A 1 787 ? 186.948 163.159 257.537 1.00 90.87  ?  806 LYS A O     1 
ATOM   6247  C  CB    . LYS A 1 787 ? 185.100 160.910 258.467 1.00 101.46 ?  806 LYS A CB    1 
ATOM   6248  C  CG    . LYS A 1 787 ? 183.738 160.285 258.720 1.00 98.91  ?  806 LYS A CG    1 
ATOM   6249  C  CD    . LYS A 1 787 ? 182.639 161.335 258.706 1.00 100.44 ?  806 LYS A CD    1 
ATOM   6250  C  CE    . LYS A 1 787 ? 182.701 162.217 259.944 1.00 98.83  ?  806 LYS A CE    1 
ATOM   6251  N  NZ    . LYS A 1 787 ? 182.411 161.452 261.189 1.00 97.69  1  806 LYS A NZ    1 
ATOM   6252  N  N     . GLY B 1 1   ? 167.177 178.330 86.899  1.00 104.87 ?  20  GLY B N     1 
ATOM   6253  C  CA    . GLY B 1 1   ? 167.835 179.601 86.657  1.00 104.43 ?  20  GLY B CA    1 
ATOM   6254  C  C     . GLY B 1 1   ? 168.945 179.902 87.645  1.00 104.19 ?  20  GLY B C     1 
ATOM   6255  O  O     . GLY B 1 1   ? 169.280 179.073 88.491  1.00 103.76 ?  20  GLY B O     1 
ATOM   6256  N  N     . ILE B 1 2   ? 169.521 181.099 87.535  1.00 100.45 ?  21  ILE B N     1 
ATOM   6257  C  CA    . ILE B 1 2   ? 170.593 181.531 88.423  1.00 101.00 ?  21  ILE B CA    1 
ATOM   6258  C  C     . ILE B 1 2   ? 170.091 182.492 89.495  1.00 99.76  ?  21  ILE B C     1 
ATOM   6259  O  O     . ILE B 1 2   ? 170.897 183.062 90.237  1.00 98.74  ?  21  ILE B O     1 
ATOM   6260  C  CB    . ILE B 1 2   ? 171.749 182.158 87.626  1.00 99.22  ?  21  ILE B CB    1 
ATOM   6261  C  CG1   . ILE B 1 2   ? 171.318 183.496 87.023  1.00 98.13  ?  21  ILE B CG1   1 
ATOM   6262  C  CG2   . ILE B 1 2   ? 172.221 181.210 86.536  1.00 98.52  ?  21  ILE B CG2   1 
ATOM   6263  C  CD1   . ILE B 1 2   ? 172.448 184.489 86.869  1.00 96.97  ?  21  ILE B CD1   1 
ATOM   6264  N  N     . PHE B 1 3   ? 168.778 182.685 89.594  1.00 98.40  ?  22  PHE B N     1 
ATOM   6265  C  CA    . PHE B 1 3   ? 168.186 183.623 90.539  1.00 101.03 ?  22  PHE B CA    1 
ATOM   6266  C  C     . PHE B 1 3   ? 167.358 182.939 91.616  1.00 101.11 ?  22  PHE B C     1 
ATOM   6267  O  O     . PHE B 1 3   ? 167.580 183.172 92.808  1.00 102.03 ?  22  PHE B O     1 
ATOM   6268  C  CB    . PHE B 1 3   ? 167.319 184.643 89.784  1.00 102.00 ?  22  PHE B CB    1 
ATOM   6269  C  CG    . PHE B 1 3   ? 167.985 185.218 88.567  1.00 101.43 ?  22  PHE B CG    1 
ATOM   6270  C  CD1   . PHE B 1 3   ? 168.971 186.183 88.690  1.00 102.96 ?  22  PHE B CD1   1 
ATOM   6271  C  CD2   . PHE B 1 3   ? 167.631 184.788 87.298  1.00 98.77  ?  22  PHE B CD2   1 
ATOM   6272  C  CE1   . PHE B 1 3   ? 169.587 186.713 87.573  1.00 101.71 ?  22  PHE B CE1   1 
ATOM   6273  C  CE2   . PHE B 1 3   ? 168.244 185.313 86.176  1.00 99.07  ?  22  PHE B CE2   1 
ATOM   6274  C  CZ    . PHE B 1 3   ? 169.223 186.278 86.314  1.00 100.80 ?  22  PHE B CZ    1 
ATOM   6275  N  N     . PHE B 1 4   ? 166.396 182.091 91.224  1.00 96.95  ?  23  PHE B N     1 
ATOM   6276  C  CA    . PHE B 1 4   ? 165.553 181.433 92.223  1.00 97.28  ?  23  PHE B CA    1 
ATOM   6277  C  C     . PHE B 1 4   ? 166.288 180.311 92.949  1.00 96.33  ?  23  PHE B C     1 
ATOM   6278  O  O     . PHE B 1 4   ? 166.379 180.357 94.188  1.00 94.99  ?  23  PHE B O     1 
ATOM   6279  C  CB    . PHE B 1 4   ? 164.252 180.952 91.573  1.00 98.38  ?  23  PHE B CB    1 
ATOM   6280  C  CG    . PHE B 1 4   ? 163.445 180.027 92.440  1.00 100.64 ?  23  PHE B CG    1 
ATOM   6281  C  CD1   . PHE B 1 4   ? 162.753 180.512 93.537  1.00 98.30  ?  23  PHE B CD1   1 
ATOM   6282  C  CD2   . PHE B 1 4   ? 163.379 178.673 92.157  1.00 99.51  ?  23  PHE B CD2   1 
ATOM   6283  C  CE1   . PHE B 1 4   ? 162.010 179.664 94.337  1.00 96.39  ?  23  PHE B CE1   1 
ATOM   6284  C  CE2   . PHE B 1 4   ? 162.638 177.819 92.953  1.00 98.08  ?  23  PHE B CE2   1 
ATOM   6285  C  CZ    . PHE B 1 4   ? 161.952 178.316 94.045  1.00 96.85  ?  23  PHE B CZ    1 
ATOM   6286  N  N     . PRO B 1 5   ? 166.830 179.289 92.270  1.00 94.12  ?  24  PRO B N     1 
ATOM   6287  C  CA    . PRO B 1 5   ? 167.432 178.169 93.015  1.00 94.65  ?  24  PRO B CA    1 
ATOM   6288  C  C     . PRO B 1 5   ? 168.736 178.519 93.709  1.00 89.98  ?  24  PRO B C     1 
ATOM   6289  O  O     . PRO B 1 5   ? 169.214 177.718 94.522  1.00 86.47  ?  24  PRO B O     1 
ATOM   6290  C  CB    . PRO B 1 5   ? 167.650 177.095 91.935  1.00 96.35  ?  24  PRO B CB    1 
ATOM   6291  C  CG    . PRO B 1 5   ? 166.950 177.604 90.702  1.00 97.28  ?  24  PRO B CG    1 
ATOM   6292  C  CD    . PRO B 1 5   ? 166.970 179.087 90.818  1.00 94.77  ?  24  PRO B CD    1 
ATOM   6293  N  N     . ALA B 1 6   ? 169.332 179.676 93.410  1.00 88.17  ?  25  ALA B N     1 
ATOM   6294  C  CA    . ALA B 1 6   ? 170.626 180.016 93.994  1.00 88.24  ?  25  ALA B CA    1 
ATOM   6295  C  C     . ALA B 1 6   ? 170.542 180.151 95.510  1.00 87.37  ?  25  ALA B C     1 
ATOM   6296  O  O     . ALA B 1 6   ? 171.417 179.662 96.233  1.00 87.97  ?  25  ALA B O     1 
ATOM   6297  C  CB    . ALA B 1 6   ? 171.159 181.305 93.371  1.00 88.14  ?  25  ALA B CB    1 
ATOM   6298  N  N     . LEU B 1 7   ? 169.496 180.806 96.010  1.00 78.63  ?  26  LEU B N     1 
ATOM   6299  C  CA    . LEU B 1 7   ? 169.348 181.068 97.435  1.00 79.53  ?  26  LEU B CA    1 
ATOM   6300  C  C     . LEU B 1 7   ? 168.347 180.139 98.111  1.00 83.84  ?  26  LEU B C     1 
ATOM   6301  O  O     . LEU B 1 7   ? 168.017 180.349 99.282  1.00 83.92  ?  26  LEU B O     1 
ATOM   6302  C  CB    . LEU B 1 7   ? 168.941 182.525 97.662  1.00 79.72  ?  26  LEU B CB    1 
ATOM   6303  C  CG    . LEU B 1 7   ? 170.060 183.563 97.546  1.00 80.37  ?  26  LEU B CG    1 
ATOM   6304  C  CD1   . LEU B 1 7   ? 169.490 184.937 97.234  1.00 80.60  ?  26  LEU B CD1   1 
ATOM   6305  C  CD2   . LEU B 1 7   ? 170.886 183.602 98.822  1.00 78.45  ?  26  LEU B CD2   1 
ATOM   6306  N  N     . GLU B 1 8   ? 167.855 179.121 97.403  1.00 82.17  ?  27  GLU B N     1 
ATOM   6307  C  CA    . GLU B 1 8   ? 166.870 178.223 97.995  1.00 78.00  ?  27  GLU B CA    1 
ATOM   6308  C  C     . GLU B 1 8   ? 167.498 177.305 99.038  1.00 76.32  ?  27  GLU B C     1 
ATOM   6309  O  O     . GLU B 1 8   ? 166.926 177.104 100.115 1.00 81.62  ?  27  GLU B O     1 
ATOM   6310  C  CB    . GLU B 1 8   ? 166.183 177.405 96.900  1.00 77.07  ?  27  GLU B CB    1 
ATOM   6311  C  CG    . GLU B 1 8   ? 164.858 176.792 97.324  1.00 77.86  ?  27  GLU B CG    1 
ATOM   6312  C  CD    . GLU B 1 8   ? 164.971 175.314 97.629  1.00 80.59  ?  27  GLU B CD    1 
ATOM   6313  O  OE1   . GLU B 1 8   ? 164.118 174.793 98.379  1.00 82.34  ?  27  GLU B OE1   1 
ATOM   6314  O  OE2   . GLU B 1 8   ? 165.907 174.670 97.113  1.00 80.27  -1 27  GLU B OE2   1 
ATOM   6315  N  N     . GLN B 1 9   ? 168.669 176.744 98.741  1.00 70.68  ?  28  GLN B N     1 
ATOM   6316  C  CA    . GLN B 1 9   ? 169.366 175.850 99.655  1.00 71.52  ?  28  GLN B CA    1 
ATOM   6317  C  C     . GLN B 1 9   ? 170.488 176.543 100.418 1.00 71.70  ?  28  GLN B C     1 
ATOM   6318  O  O     . GLN B 1 9   ? 171.276 175.868 101.088 1.00 70.44  ?  28  GLN B O     1 
ATOM   6319  C  CB    . GLN B 1 9   ? 169.925 174.647 98.892  1.00 74.28  ?  28  GLN B CB    1 
ATOM   6320  C  CG    . GLN B 1 9   ? 168.979 174.083 97.847  1.00 75.39  ?  28  GLN B CG    1 
ATOM   6321  C  CD    . GLN B 1 9   ? 169.707 173.365 96.728  1.00 75.43  ?  28  GLN B CD    1 
ATOM   6322  O  OE1   . GLN B 1 9   ? 170.462 172.423 96.968  1.00 77.00  ?  28  GLN B OE1   1 
ATOM   6323  N  NE2   . GLN B 1 9   ? 169.482 173.806 95.496  1.00 73.17  ?  28  GLN B NE2   1 
ATOM   6324  N  N     . ASN B 1 10  ? 170.583 177.866 100.327 1.00 67.23  ?  29  ASN B N     1 
ATOM   6325  C  CA    . ASN B 1 10  ? 171.663 178.585 100.981 1.00 62.59  ?  29  ASN B CA    1 
ATOM   6326  C  C     . ASN B 1 10  ? 171.450 178.638 102.491 1.00 60.78  ?  29  ASN B C     1 
ATOM   6327  O  O     . ASN B 1 10  ? 170.330 178.526 102.998 1.00 62.24  ?  29  ASN B O     1 
ATOM   6328  C  CB    . ASN B 1 10  ? 171.777 180.004 100.426 1.00 66.82  ?  29  ASN B CB    1 
ATOM   6329  C  CG    . ASN B 1 10  ? 173.184 180.554 100.524 1.00 67.61  ?  29  ASN B CG    1 
ATOM   6330  O  OD1   . ASN B 1 10  ? 174.142 179.806 100.716 1.00 68.22  ?  29  ASN B OD1   1 
ATOM   6331  N  ND2   . ASN B 1 10  ? 173.317 181.867 100.394 1.00 68.81  ?  29  ASN B ND2   1 
ATOM   6332  N  N     . MET B 1 11  ? 172.559 178.810 103.213 1.00 58.83  ?  30  MET B N     1 
ATOM   6333  C  CA    . MET B 1 11  ? 172.481 179.028 104.654 1.00 58.78  ?  30  MET B CA    1 
ATOM   6334  C  C     . MET B 1 11  ? 171.840 180.374 104.967 1.00 63.47  ?  30  MET B C     1 
ATOM   6335  O  O     . MET B 1 11  ? 171.110 180.508 105.955 1.00 65.40  ?  30  MET B O     1 
ATOM   6336  C  CB    . MET B 1 11  ? 173.875 178.933 105.272 1.00 61.40  ?  30  MET B CB    1 
ATOM   6337  C  CG    . MET B 1 11  ? 173.912 179.141 106.776 1.00 62.91  ?  30  MET B CG    1 
ATOM   6338  S  SD    . MET B 1 11  ? 175.512 178.722 107.495 1.00 74.40  ?  30  MET B SD    1 
ATOM   6339  C  CE    . MET B 1 11  ? 176.374 180.284 107.341 1.00 62.92  ?  30  MET B CE    1 
ATOM   6340  N  N     . MET B 1 12  ? 172.104 181.379 104.137 1.00 60.87  ?  31  MET B N     1 
ATOM   6341  C  CA    . MET B 1 12  ? 171.489 182.687 104.314 1.00 59.88  ?  31  MET B CA    1 
ATOM   6342  C  C     . MET B 1 12  ? 170.021 182.626 103.915 1.00 59.03  ?  31  MET B C     1 
ATOM   6343  O  O     . MET B 1 12  ? 169.679 182.101 102.851 1.00 64.60  ?  31  MET B O     1 
ATOM   6344  C  CB    . MET B 1 12  ? 172.219 183.729 103.469 1.00 60.10  ?  31  MET B CB    1 
ATOM   6345  C  CG    . MET B 1 12  ? 173.695 183.887 103.794 1.00 61.54  ?  31  MET B CG    1 
ATOM   6346  S  SD    . MET B 1 12  ? 174.004 184.773 105.327 1.00 60.14  ?  31  MET B SD    1 
ATOM   6347  C  CE    . MET B 1 12  ? 175.019 183.584 106.199 1.00 59.92  ?  31  MET B CE    1 
ATOM   6348  N  N     . GLY B 1 13  ? 169.147 183.158 104.767 1.00 49.46  ?  32  GLY B N     1 
ATOM   6349  C  CA    . GLY B 1 13  ? 167.736 183.223 104.423 1.00 50.29  ?  32  GLY B CA    1 
ATOM   6350  C  C     . GLY B 1 13  ? 167.468 184.370 103.463 1.00 47.25  ?  32  GLY B C     1 
ATOM   6351  O  O     . GLY B 1 13  ? 167.976 185.477 103.628 1.00 53.30  ?  32  GLY B O     1 
ATOM   6352  N  N     . ALA B 1 14  ? 166.660 184.093 102.446 1.00 63.49  ?  33  ALA B N     1 
ATOM   6353  C  CA    . ALA B 1 14  ? 166.351 185.069 101.411 1.00 67.26  ?  33  ALA B CA    1 
ATOM   6354  C  C     . ALA B 1 14  ? 164.863 185.381 101.433 1.00 71.94  ?  33  ALA B C     1 
ATOM   6355  O  O     . ALA B 1 14  ? 164.031 184.470 101.352 1.00 79.40  ?  33  ALA B O     1 
ATOM   6356  C  CB    . ALA B 1 14  ? 166.767 184.558 100.029 1.00 67.14  ?  33  ALA B CB    1 
ATOM   6357  N  N     . VAL B 1 15  ? 164.532 186.665 101.552 1.00 66.46  ?  34  VAL B N     1 
ATOM   6358  C  CA    . VAL B 1 15  ? 163.151 187.131 101.492 1.00 64.90  ?  34  VAL B CA    1 
ATOM   6359  C  C     . VAL B 1 15  ? 163.090 188.341 100.571 1.00 64.76  ?  34  VAL B C     1 
ATOM   6360  O  O     . VAL B 1 15  ? 163.946 189.230 100.641 1.00 71.84  ?  34  VAL B O     1 
ATOM   6361  C  CB    . VAL B 1 15  ? 162.586 187.467 102.887 1.00 65.92  ?  34  VAL B CB    1 
ATOM   6362  C  CG1   . VAL B 1 15  ? 162.390 186.196 103.691 1.00 69.23  ?  34  VAL B CG1   1 
ATOM   6363  C  CG2   . VAL B 1 15  ? 163.501 188.423 103.629 1.00 70.27  ?  34  VAL B CG2   1 
ATOM   6364  N  N     . LEU B 1 16  ? 162.091 188.363 99.693  1.00 85.14  ?  35  LEU B N     1 
ATOM   6365  C  CA    . LEU B 1 16  ? 161.931 189.418 98.704  1.00 89.83  ?  35  LEU B CA    1 
ATOM   6366  C  C     . LEU B 1 16  ? 160.499 189.932 98.733  1.00 94.47  ?  35  LEU B C     1 
ATOM   6367  O  O     . LEU B 1 16  ? 159.550 189.145 98.787  1.00 98.09  ?  35  LEU B O     1 
ATOM   6368  C  CB    . LEU B 1 16  ? 162.276 188.912 97.299  1.00 88.77  ?  35  LEU B CB    1 
ATOM   6369  C  CG    . LEU B 1 16  ? 162.196 189.924 96.156  1.00 89.51  ?  35  LEU B CG    1 
ATOM   6370  C  CD1   . LEU B 1 16  ? 163.510 190.674 96.009  1.00 88.25  ?  35  LEU B CD1   1 
ATOM   6371  C  CD2   . LEU B 1 16  ? 161.819 189.224 94.861  1.00 90.81  ?  35  LEU B CD2   1 
ATOM   6372  N  N     . ILE B 1 17  ? 160.350 191.254 98.696  1.00 99.10  ?  36  ILE B N     1 
ATOM   6373  C  CA    . ILE B 1 17  ? 159.044 191.900 98.681  1.00 96.53  ?  36  ILE B CA    1 
ATOM   6374  C  C     . ILE B 1 17  ? 158.921 192.728 97.409  1.00 99.28  ?  36  ILE B C     1 
ATOM   6375  O  O     . ILE B 1 17  ? 159.889 193.356 96.959  1.00 101.54 ?  36  ILE B O     1 
ATOM   6376  C  CB    . ILE B 1 17  ? 158.799 192.759 99.943  1.00 97.80  ?  36  ILE B CB    1 
ATOM   6377  C  CG1   . ILE B 1 17  ? 159.469 194.129 99.833  1.00 99.28  ?  36  ILE B CG1   1 
ATOM   6378  C  CG2   . ILE B 1 17  ? 159.281 192.029 101.189 1.00 97.12  ?  36  ILE B CG2   1 
ATOM   6379  C  CD1   . ILE B 1 17  ? 159.031 195.104 100.900 1.00 100.08 ?  36  ILE B CD1   1 
ATOM   6380  N  N     . ASN B 1 18  ? 157.729 192.688 96.816  1.00 113.04 ?  37  ASN B N     1 
ATOM   6381  C  CA    . ASN B 1 18  ? 157.426 193.299 95.531  1.00 114.93 ?  37  ASN B CA    1 
ATOM   6382  C  C     . ASN B 1 18  ? 156.857 194.705 95.722  1.00 113.52 ?  37  ASN B C     1 
ATOM   6383  O  O     . ASN B 1 18  ? 156.964 195.308 96.794  1.00 114.49 ?  37  ASN B O     1 
ATOM   6384  C  CB    . ASN B 1 18  ? 156.469 192.404 94.744  1.00 114.01 ?  37  ASN B CB    1 
ATOM   6385  C  CG    . ASN B 1 18  ? 155.236 192.018 95.544  1.00 113.72 ?  37  ASN B CG    1 
ATOM   6386  O  OD1   . ASN B 1 18  ? 154.923 192.629 96.566  1.00 112.47 ?  37  ASN B OD1   1 
ATOM   6387  N  ND2   . ASN B 1 18  ? 154.530 190.995 95.079  1.00 113.35 ?  37  ASN B ND2   1 
ATOM   6388  N  N     . GLU B 1 19  ? 156.253 195.244 94.658  1.00 110.60 ?  38  GLU B N     1 
ATOM   6389  C  CA    . GLU B 1 19  ? 155.657 196.576 94.717  1.00 111.50 ?  38  GLU B CA    1 
ATOM   6390  C  C     . GLU B 1 19  ? 154.557 196.653 95.768  1.00 110.52 ?  38  GLU B C     1 
ATOM   6391  O  O     . GLU B 1 19  ? 154.478 197.628 96.524  1.00 110.61 ?  38  GLU B O     1 
ATOM   6392  C  CB    . GLU B 1 19  ? 155.101 196.959 93.345  1.00 113.95 ?  38  GLU B CB    1 
ATOM   6393  C  CG    . GLU B 1 19  ? 156.154 197.323 92.316  1.00 112.31 ?  38  GLU B CG    1 
ATOM   6394  C  CD    . GLU B 1 19  ? 156.994 198.510 92.738  1.00 109.44 ?  38  GLU B CD    1 
ATOM   6395  O  OE1   . GLU B 1 19  ? 156.482 199.378 93.476  1.00 109.81 ?  38  GLU B OE1   1 
ATOM   6396  O  OE2   . GLU B 1 19  ? 158.170 198.578 92.333  1.00 107.94 -1 38  GLU B OE2   1 
ATOM   6397  N  N     . ASN B 1 20  ? 153.698 195.638 95.832  1.00 117.65 ?  39  ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 20  ? 152.577 195.628 96.762  1.00 121.09 ?  39  ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 20  ? 152.982 195.233 98.177  1.00 118.89 ?  39  ASN B C     1 
ATOM   6400  O  O     . ASN B 1 20  ? 152.102 194.923 98.991  1.00 117.93 ?  39  ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 20  ? 151.479 194.690 96.253  1.00 120.95 ?  39  ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 20  ? 151.077 194.986 94.822  1.00 119.24 ?  39  ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 20  ? 151.141 194.114 93.955  1.00 116.70 ?  39  ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 20  ? 150.661 196.220 94.566  1.00 119.13 ?  39  ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 21  ? 154.282 195.237 98.479  1.00 111.72 ?  40  ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 21  ? 154.796 194.865 99.798  1.00 111.84 ?  40  ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 21  ? 154.369 193.449 100.181 1.00 113.88 ?  40  ASP B C     1 
ATOM   6408  O  O     . ASP B 1 21  ? 154.121 193.148 101.350 1.00 114.29 ?  40  ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 21  ? 154.365 195.874 100.866 1.00 111.48 ?  40  ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 21  ? 154.640 197.307 100.457 1.00 113.27 ?  40  ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 21  ? 155.697 197.559 99.841  1.00 113.58 ?  40  ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 21  ? 153.799 198.183 100.752 1.00 113.59 -1 40  ASP B OD2   1 
ATOM   6413  N  N     . GLU B 1 22  ? 154.280 192.574 99.184  1.00 110.58 ?  41  GLU B N     1 
ATOM   6414  C  CA    . GLU B 1 22  ? 153.933 191.175 99.392  1.00 111.43 ?  41  GLU B CA    1 
ATOM   6415  C  C     . GLU B 1 22  ? 155.181 190.318 99.231  1.00 111.74 ?  41  GLU B C     1 
ATOM   6416  O  O     . GLU B 1 22  ? 155.948 190.501 98.279  1.00 110.45 ?  41  GLU B O     1 
ATOM   6417  C  CB    . GLU B 1 22  ? 152.850 190.723 98.411  1.00 109.83 ?  41  GLU B CB    1 
ATOM   6418  C  CG    . GLU B 1 22  ? 151.519 191.435 98.584  1.00 109.17 ?  41  GLU B CG    1 
ATOM   6419  C  CD    . GLU B 1 22  ? 150.731 191.518 97.292  1.00 109.82 ?  41  GLU B CD    1 
ATOM   6420  O  OE1   . GLU B 1 22  ? 151.251 191.076 96.246  1.00 111.03 ?  41  GLU B OE1   1 
ATOM   6421  O  OE2   . GLU B 1 22  ? 149.591 192.027 97.322  1.00 110.15 -1 41  GLU B OE2   1 
ATOM   6422  N  N     . VAL B 1 23  ? 155.385 189.391 100.169 1.00 103.88 ?  42  VAL B N     1 
ATOM   6423  C  CA    . VAL B 1 23  ? 156.562 188.535 100.125 1.00 102.15 ?  42  VAL B CA    1 
ATOM   6424  C  C     . VAL B 1 23  ? 156.494 187.622 98.909  1.00 100.50 ?  42  VAL B C     1 
ATOM   6425  O  O     . VAL B 1 23  ? 155.450 187.030 98.604  1.00 100.44 ?  42  VAL B O     1 
ATOM   6426  C  CB    . VAL B 1 23  ? 156.681 187.726 101.427 1.00 99.26  ?  42  VAL B CB    1 
ATOM   6427  C  CG1   . VAL B 1 23  ? 158.007 186.986 101.477 1.00 100.17 ?  42  VAL B CG1   1 
ATOM   6428  C  CG2   . VAL B 1 23  ? 156.526 188.641 102.627 1.00 99.71  ?  42  VAL B CG2   1 
ATOM   6429  N  N     . MET B 1 24  ? 157.618 187.504 98.206  1.00 96.20  ?  43  MET B N     1 
ATOM   6430  C  CA    . MET B 1 24  ? 157.713 186.684 97.007  1.00 96.52  ?  43  MET B CA    1 
ATOM   6431  C  C     . MET B 1 24  ? 158.688 185.524 97.132  1.00 97.51  ?  43  MET B C     1 
ATOM   6432  O  O     . MET B 1 24  ? 158.486 184.498 96.479  1.00 98.97  ?  43  MET B O     1 
ATOM   6433  C  CB    . MET B 1 24  ? 158.123 187.549 95.803  1.00 97.87  ?  43  MET B CB    1 
ATOM   6434  C  CG    . MET B 1 24  ? 157.904 186.891 94.450  1.00 97.78  ?  43  MET B CG    1 
ATOM   6435  S  SD    . MET B 1 24  ? 156.225 186.274 94.229  1.00 100.80 ?  43  MET B SD    1 
ATOM   6436  C  CE    . MET B 1 24  ? 155.297 187.805 94.239  1.00 96.50  ?  43  MET B CE    1 
ATOM   6437  N  N     . PHE B 1 25  ? 159.728 185.651 97.951  1.00 84.40  ?  44  PHE B N     1 
ATOM   6438  C  CA    . PHE B 1 25  ? 160.717 184.600 98.128  1.00 81.00  ?  44  PHE B CA    1 
ATOM   6439  C  C     . PHE B 1 25  ? 160.697 184.105 99.567  1.00 77.99  ?  44  PHE B C     1 
ATOM   6440  O  O     . PHE B 1 25  ? 160.468 184.875 100.505 1.00 79.55  ?  44  PHE B O     1 
ATOM   6441  C  CB    . PHE B 1 25  ? 162.126 185.091 97.764  1.00 82.04  ?  44  PHE B CB    1 
ATOM   6442  C  CG    . PHE B 1 25  ? 163.092 183.982 97.448  1.00 81.91  ?  44  PHE B CG    1 
ATOM   6443  C  CD1   . PHE B 1 25  ? 163.288 183.568 96.142  1.00 84.27  ?  44  PHE B CD1   1 
ATOM   6444  C  CD2   . PHE B 1 25  ? 163.806 183.357 98.457  1.00 81.04  ?  44  PHE B CD2   1 
ATOM   6445  C  CE1   . PHE B 1 25  ? 164.175 182.550 95.848  1.00 84.04  ?  44  PHE B CE1   1 
ATOM   6446  C  CE2   . PHE B 1 25  ? 164.693 182.337 98.170  1.00 81.27  ?  44  PHE B CE2   1 
ATOM   6447  C  CZ    . PHE B 1 25  ? 164.879 181.934 96.864  1.00 83.87  ?  44  PHE B CZ    1 
ATOM   6448  N  N     . PHE B 1 26  ? 160.943 182.807 99.730  1.00 75.36  ?  45  PHE B N     1 
ATOM   6449  C  CA    . PHE B 1 26  ? 160.975 182.187 101.052 1.00 79.42  ?  45  PHE B CA    1 
ATOM   6450  C  C     . PHE B 1 26  ? 161.715 180.866 100.937 1.00 81.59  ?  45  PHE B C     1 
ATOM   6451  O  O     . PHE B 1 26  ? 161.358 180.029 100.101 1.00 84.39  ?  45  PHE B O     1 
ATOM   6452  C  CB    . PHE B 1 26  ? 159.561 181.980 101.594 1.00 84.41  ?  45  PHE B CB    1 
ATOM   6453  C  CG    . PHE B 1 26  ? 159.512 181.722 103.070 1.00 84.75  ?  45  PHE B CG    1 
ATOM   6454  C  CD1   . PHE B 1 26  ? 160.226 182.518 103.947 1.00 79.43  ?  45  PHE B CD1   1 
ATOM   6455  C  CD2   . PHE B 1 26  ? 158.740 180.694 103.583 1.00 83.70  ?  45  PHE B CD2   1 
ATOM   6456  C  CE1   . PHE B 1 26  ? 160.184 182.286 105.305 1.00 76.22  ?  45  PHE B CE1   1 
ATOM   6457  C  CE2   . PHE B 1 26  ? 158.691 180.461 104.943 1.00 83.22  ?  45  PHE B CE2   1 
ATOM   6458  C  CZ    . PHE B 1 26  ? 159.414 181.257 105.805 1.00 80.45  ?  45  PHE B CZ    1 
ATOM   6459  N  N     . ASN B 1 27  ? 162.731 180.676 101.769 1.00 73.88  ?  46  ASN B N     1 
ATOM   6460  C  CA    . ASN B 1 27  ? 163.620 179.529 101.707 1.00 69.92  ?  46  ASN B CA    1 
ATOM   6461  C  C     . ASN B 1 27  ? 163.686 178.823 103.057 1.00 72.10  ?  46  ASN B C     1 
ATOM   6462  O  O     . ASN B 1 27  ? 163.327 179.403 104.089 1.00 77.43  ?  46  ASN B O     1 
ATOM   6463  C  CB    . ASN B 1 27  ? 165.028 179.963 101.266 1.00 71.88  ?  46  ASN B CB    1 
ATOM   6464  C  CG    . ASN B 1 27  ? 165.759 180.758 102.330 1.00 72.54  ?  46  ASN B CG    1 
ATOM   6465  O  OD1   . ASN B 1 27  ? 165.144 181.447 103.143 1.00 74.92  ?  46  ASN B OD1   1 
ATOM   6466  N  ND2   . ASN B 1 27  ? 167.084 180.672 102.322 1.00 70.07  ?  46  ASN B ND2   1 
ATOM   6467  N  N     . PRO B 1 28  ? 164.116 177.556 103.081 1.00 71.89  ?  47  PRO B N     1 
ATOM   6468  C  CA    . PRO B 1 28  ? 164.184 176.828 104.360 1.00 72.51  ?  47  PRO B CA    1 
ATOM   6469  C  C     . PRO B 1 28  ? 165.048 177.500 105.414 1.00 74.41  ?  47  PRO B C     1 
ATOM   6470  O  O     . PRO B 1 28  ? 164.792 177.321 106.611 1.00 79.47  ?  47  PRO B O     1 
ATOM   6471  C  CB    . PRO B 1 28  ? 164.754 175.466 103.948 1.00 70.83  ?  47  PRO B CB    1 
ATOM   6472  C  CG    . PRO B 1 28  ? 164.275 175.282 102.556 1.00 72.46  ?  47  PRO B CG    1 
ATOM   6473  C  CD    . PRO B 1 28  ? 164.279 176.651 101.928 1.00 73.18  ?  47  PRO B CD    1 
ATOM   6474  N  N     . ALA B 1 29  ? 166.066 178.265 105.014 1.00 69.03  ?  48  ALA B N     1 
ATOM   6475  C  CA    . ALA B 1 29  ? 166.863 178.989 106.000 1.00 69.10  ?  48  ALA B CA    1 
ATOM   6476  C  C     . ALA B 1 29  ? 166.013 180.002 106.757 1.00 68.75  ?  48  ALA B C     1 
ATOM   6477  O  O     . ALA B 1 29  ? 166.136 180.137 107.980 1.00 72.46  ?  48  ALA B O     1 
ATOM   6478  C  CB    . ALA B 1 29  ? 168.046 179.676 105.319 1.00 71.63  ?  48  ALA B CB    1 
ATOM   6479  N  N     . ALA B 1 30  ? 165.140 180.723 106.047 1.00 69.90  ?  49  ALA B N     1 
ATOM   6480  C  CA    . ALA B 1 30  ? 164.225 181.641 106.717 1.00 73.01  ?  49  ALA B CA    1 
ATOM   6481  C  C     . ALA B 1 30  ? 163.086 180.898 107.403 1.00 76.62  ?  49  ALA B C     1 
ATOM   6482  O  O     . ALA B 1 30  ? 162.495 181.416 108.358 1.00 77.93  ?  49  ALA B O     1 
ATOM   6483  C  CB    . ALA B 1 30  ? 163.676 182.661 105.720 1.00 71.88  ?  49  ALA B CB    1 
ATOM   6484  N  N     . GLU B 1 31  ? 162.750 179.698 106.922 1.00 75.05  ?  50  GLU B N     1 
ATOM   6485  C  CA    . GLU B 1 31  ? 161.777 178.868 107.625 1.00 70.55  ?  50  GLU B CA    1 
ATOM   6486  C  C     . GLU B 1 31  ? 162.284 178.505 109.014 1.00 71.55  ?  50  GLU B C     1 
ATOM   6487  O  O     . GLU B 1 31  ? 161.541 178.572 110.000 1.00 78.16  ?  50  GLU B O     1 
ATOM   6488  C  CB    . GLU B 1 31  ? 161.478 177.605 106.818 1.00 72.06  ?  50  GLU B CB    1 
ATOM   6489  C  CG    . GLU B 1 31  ? 160.845 177.860 105.464 1.00 76.44  ?  50  GLU B CG    1 
ATOM   6490  C  CD    . GLU B 1 31  ? 160.674 176.592 104.655 1.00 80.32  ?  50  GLU B CD    1 
ATOM   6491  O  OE1   . GLU B 1 31  ? 161.187 175.539 105.087 1.00 79.63  ?  50  GLU B OE1   1 
ATOM   6492  O  OE2   . GLU B 1 31  ? 160.029 176.649 103.586 1.00 82.09  -1 50  GLU B OE2   1 
ATOM   6493  N  N     . LYS B 1 32  ? 163.560 178.131 109.110 1.00 72.38  ?  51  LYS B N     1 
ATOM   6494  C  CA    . LYS B 1 32  ? 164.164 177.791 110.392 1.00 75.87  ?  51  LYS B CA    1 
ATOM   6495  C  C     . LYS B 1 32  ? 164.254 178.983 111.336 1.00 76.47  ?  51  LYS B C     1 
ATOM   6496  O  O     . LYS B 1 32  ? 164.495 178.785 112.532 1.00 78.50  ?  51  LYS B O     1 
ATOM   6497  C  CB    . LYS B 1 32  ? 165.559 177.200 110.178 1.00 75.18  ?  51  LYS B CB    1 
ATOM   6498  C  CG    . LYS B 1 32  ? 165.575 175.910 109.375 1.00 75.27  ?  51  LYS B CG    1 
ATOM   6499  C  CD    . LYS B 1 32  ? 166.919 175.704 108.695 1.00 78.06  ?  51  LYS B CD    1 
ATOM   6500  C  CE    . LYS B 1 32  ? 166.982 174.360 107.990 1.00 77.75  ?  51  LYS B CE    1 
ATOM   6501  N  NZ    . LYS B 1 32  ? 166.015 174.283 106.861 1.00 77.19  1  51  LYS B NZ    1 
ATOM   6502  N  N     . LEU B 1 33  ? 164.068 180.206 110.835 1.00 71.85  ?  52  LEU B N     1 
ATOM   6503  C  CA    . LEU B 1 33  ? 164.125 181.401 111.663 1.00 72.99  ?  52  LEU B CA    1 
ATOM   6504  C  C     . LEU B 1 33  ? 162.762 182.002 111.970 1.00 76.48  ?  52  LEU B C     1 
ATOM   6505  O  O     . LEU B 1 33  ? 162.639 182.731 112.959 1.00 78.18  ?  52  LEU B O     1 
ATOM   6506  C  CB    . LEU B 1 33  ? 164.998 182.475 110.995 1.00 73.75  ?  52  LEU B CB    1 
ATOM   6507  C  CG    . LEU B 1 33  ? 166.425 182.072 110.619 1.00 72.73  ?  52  LEU B CG    1 
ATOM   6508  C  CD1   . LEU B 1 33  ? 167.212 183.279 110.131 1.00 70.45  ?  52  LEU B CD1   1 
ATOM   6509  C  CD2   . LEU B 1 33  ? 167.128 181.406 111.793 1.00 71.79  ?  52  LEU B CD2   1 
ATOM   6510  N  N     . TRP B 1 34  ? 161.746 181.735 111.149 1.00 84.88  ?  53  TRP B N     1 
ATOM   6511  C  CA    . TRP B 1 34  ? 160.418 182.292 111.376 1.00 86.33  ?  53  TRP B CA    1 
ATOM   6512  C  C     . TRP B 1 34  ? 159.386 181.280 111.849 1.00 84.69  ?  53  TRP B C     1 
ATOM   6513  O  O     . TRP B 1 34  ? 158.396 181.677 112.466 1.00 86.78  ?  53  TRP B O     1 
ATOM   6514  C  CB    . TRP B 1 34  ? 159.895 182.971 110.104 1.00 85.24  ?  53  TRP B CB    1 
ATOM   6515  C  CG    . TRP B 1 34  ? 160.547 184.288 109.838 1.00 84.30  ?  53  TRP B CG    1 
ATOM   6516  C  CD1   . TRP B 1 34  ? 161.288 185.020 110.715 1.00 83.83  ?  53  TRP B CD1   1 
ATOM   6517  C  CD2   . TRP B 1 34  ? 160.496 185.048 108.625 1.00 86.69  ?  53  TRP B CD2   1 
ATOM   6518  N  NE1   . TRP B 1 34  ? 161.718 186.179 110.119 1.00 84.27  ?  53  TRP B NE1   1 
ATOM   6519  C  CE2   . TRP B 1 34  ? 161.243 186.223 108.837 1.00 87.31  ?  53  TRP B CE2   1 
ATOM   6520  C  CE3   . TRP B 1 34  ? 159.897 184.847 107.379 1.00 87.73  ?  53  TRP B CE3   1 
ATOM   6521  C  CZ2   . TRP B 1 34  ? 161.407 187.191 107.852 1.00 86.66  ?  53  TRP B CZ2   1 
ATOM   6522  C  CZ3   . TRP B 1 34  ? 160.064 185.809 106.401 1.00 88.79  ?  53  TRP B CZ3   1 
ATOM   6523  C  CH2   . TRP B 1 34  ? 160.810 186.968 106.644 1.00 86.64  ?  53  TRP B CH2   1 
ATOM   6524  N  N     . GLY B 1 35  ? 159.580 179.990 111.577 1.00 78.68  ?  54  GLY B N     1 
ATOM   6525  C  CA    . GLY B 1 35  ? 158.628 178.973 111.956 1.00 77.18  ?  54  GLY B CA    1 
ATOM   6526  C  C     . GLY B 1 35  ? 157.565 178.679 110.919 1.00 75.58  ?  54  GLY B C     1 
ATOM   6527  O  O     . GLY B 1 35  ? 156.898 177.642 111.011 1.00 80.70  ?  54  GLY B O     1 
ATOM   6528  N  N     . TYR B 1 36  ? 157.385 179.562 109.940 1.00 73.80  ?  55  TYR B N     1 
ATOM   6529  C  CA    . TYR B 1 36  ? 156.403 179.355 108.890 1.00 78.75  ?  55  TYR B CA    1 
ATOM   6530  C  C     . TYR B 1 36  ? 156.937 178.378 107.845 1.00 78.72  ?  55  TYR B C     1 
ATOM   6531  O  O     . TYR B 1 36  ? 158.063 177.881 107.929 1.00 80.84  ?  55  TYR B O     1 
ATOM   6532  C  CB    . TYR B 1 36  ? 156.028 180.687 108.244 1.00 81.97  ?  55  TYR B CB    1 
ATOM   6533  C  CG    . TYR B 1 36  ? 155.022 181.497 109.028 1.00 82.58  ?  55  TYR B CG    1 
ATOM   6534  C  CD1   . TYR B 1 36  ? 153.695 181.099 109.111 1.00 84.52  ?  55  TYR B CD1   1 
ATOM   6535  C  CD2   . TYR B 1 36  ? 155.397 182.664 109.681 1.00 82.66  ?  55  TYR B CD2   1 
ATOM   6536  C  CE1   . TYR B 1 36  ? 152.770 181.837 109.824 1.00 86.18  ?  55  TYR B CE1   1 
ATOM   6537  C  CE2   . TYR B 1 36  ? 154.479 183.409 110.397 1.00 84.15  ?  55  TYR B CE2   1 
ATOM   6538  C  CZ    . TYR B 1 36  ? 153.167 182.991 110.466 1.00 86.34  ?  55  TYR B CZ    1 
ATOM   6539  O  OH    . TYR B 1 36  ? 152.248 183.727 111.178 1.00 84.88  ?  55  TYR B OH    1 
ATOM   6540  N  N     . LYS B 1 37  ? 156.109 178.098 106.846 1.00 83.37  ?  56  LYS B N     1 
ATOM   6541  C  CA    . LYS B 1 37  ? 156.469 177.283 105.695 1.00 83.01  ?  56  LYS B CA    1 
ATOM   6542  C  C     . LYS B 1 37  ? 156.269 178.097 104.420 1.00 85.57  ?  56  LYS B C     1 
ATOM   6543  O  O     . LYS B 1 37  ? 155.912 179.277 104.458 1.00 90.96  ?  56  LYS B O     1 
ATOM   6544  C  CB    . LYS B 1 37  ? 155.645 175.992 105.657 1.00 85.70  ?  56  LYS B CB    1 
ATOM   6545  C  CG    . LYS B 1 37  ? 155.626 175.214 106.963 1.00 88.57  ?  56  LYS B CG    1 
ATOM   6546  C  CD    . LYS B 1 37  ? 157.028 174.799 107.383 1.00 89.07  ?  56  LYS B CD    1 
ATOM   6547  C  CE    . LYS B 1 37  ? 157.185 174.826 108.894 1.00 88.69  ?  56  LYS B CE    1 
ATOM   6548  N  NZ    . LYS B 1 37  ? 158.317 173.972 109.347 1.00 86.22  1  56  LYS B NZ    1 
ATOM   6549  N  N     . ARG B 1 38  ? 156.488 177.448 103.278 1.00 88.63  ?  57  ARG B N     1 
ATOM   6550  C  CA    . ARG B 1 38  ? 156.337 178.096 101.981 1.00 92.11  ?  57  ARG B CA    1 
ATOM   6551  C  C     . ARG B 1 38  ? 154.890 178.135 101.502 1.00 94.85  ?  57  ARG B C     1 
ATOM   6552  O  O     . ARG B 1 38  ? 154.650 178.309 100.301 1.00 95.66  ?  57  ARG B O     1 
ATOM   6553  C  CB    . ARG B 1 38  ? 157.217 177.405 100.936 1.00 89.28  ?  57  ARG B CB    1 
ATOM   6554  C  CG    . ARG B 1 38  ? 156.955 175.917 100.776 1.00 92.00  ?  57  ARG B CG    1 
ATOM   6555  C  CD    . ARG B 1 38  ? 158.013 175.270 99.896  1.00 92.64  ?  57  ARG B CD    1 
ATOM   6556  N  NE    . ARG B 1 38  ? 159.321 175.248 100.539 1.00 93.58  ?  57  ARG B NE    1 
ATOM   6557  C  CZ    . ARG B 1 38  ? 159.820 174.205 101.189 1.00 91.85  ?  57  ARG B CZ    1 
ATOM   6558  N  NH1   . ARG B 1 38  ? 159.147 173.072 101.299 1.00 91.04  1  57  ARG B NH1   1 
ATOM   6559  N  NH2   . ARG B 1 38  ? 161.027 174.302 101.741 1.00 90.83  ?  57  ARG B NH2   1 
ATOM   6560  N  N     . GLU B 1 39  ? 153.925 177.969 102.406 1.00 94.27  ?  58  GLU B N     1 
ATOM   6561  C  CA    . GLU B 1 39  ? 152.513 178.057 102.066 1.00 93.33  ?  58  GLU B CA    1 
ATOM   6562  C  C     . GLU B 1 39  ? 151.783 179.156 102.824 1.00 93.48  ?  58  GLU B C     1 
ATOM   6563  O  O     . GLU B 1 39  ? 150.570 179.311 102.641 1.00 94.58  ?  58  GLU B O     1 
ATOM   6564  C  CB    . GLU B 1 39  ? 151.818 176.712 102.323 1.00 92.34  ?  58  GLU B CB    1 
ATOM   6565  C  CG    . GLU B 1 39  ? 151.935 175.723 101.176 1.00 94.72  ?  58  GLU B CG    1 
ATOM   6566  C  CD    . GLU B 1 39  ? 153.321 175.120 101.064 1.00 97.07  ?  58  GLU B CD    1 
ATOM   6567  O  OE1   . GLU B 1 39  ? 153.875 174.701 102.103 1.00 96.54  ?  58  GLU B OE1   1 
ATOM   6568  O  OE2   . GLU B 1 39  ? 153.858 175.068 99.938  1.00 96.20  -1 58  GLU B OE2   1 
ATOM   6569  N  N     . GLU B 1 40  ? 152.479 179.923 103.666 1.00 93.85  ?  59  GLU B N     1 
ATOM   6570  C  CA    . GLU B 1 40  ? 151.842 180.948 104.478 1.00 95.89  ?  59  GLU B CA    1 
ATOM   6571  C  C     . GLU B 1 40  ? 152.528 182.306 104.402 1.00 97.62  ?  59  GLU B C     1 
ATOM   6572  O  O     . GLU B 1 40  ? 152.032 183.262 105.009 1.00 98.25  ?  59  GLU B O     1 
ATOM   6573  C  CB    . GLU B 1 40  ? 151.778 180.501 105.947 1.00 96.22  ?  59  GLU B CB    1 
ATOM   6574  C  CG    . GLU B 1 40  ? 150.977 179.230 106.176 1.00 97.45  ?  59  GLU B CG    1 
ATOM   6575  C  CD    . GLU B 1 40  ? 150.088 179.314 107.401 1.00 98.68  ?  59  GLU B CD    1 
ATOM   6576  O  OE1   . GLU B 1 40  ? 150.181 180.319 108.136 1.00 98.60  ?  59  GLU B OE1   1 
ATOM   6577  O  OE2   . GLU B 1 40  ? 149.297 178.375 107.629 1.00 97.13  -1 59  GLU B OE2   1 
ATOM   6578  N  N     . VAL B 1 41  ? 153.643 182.423 103.683 1.00 95.70  ?  60  VAL B N     1 
ATOM   6579  C  CA    . VAL B 1 41  ? 154.354 183.685 103.572 1.00 93.87  ?  60  VAL B CA    1 
ATOM   6580  C  C     . VAL B 1 41  ? 154.311 184.253 102.157 1.00 98.06  ?  60  VAL B C     1 
ATOM   6581  O  O     . VAL B 1 41  ? 154.431 185.473 101.988 1.00 101.76 ?  60  VAL B O     1 
ATOM   6582  C  CB    . VAL B 1 41  ? 155.812 183.529 104.055 1.00 93.69  ?  60  VAL B CB    1 
ATOM   6583  C  CG1   . VAL B 1 41  ? 156.489 184.886 104.200 1.00 96.00  ?  60  VAL B CG1   1 
ATOM   6584  C  CG2   . VAL B 1 41  ? 155.855 182.772 105.367 1.00 94.68  ?  60  VAL B CG2   1 
ATOM   6585  N  N     . ILE B 1 42  ? 154.132 183.415 101.138 1.00 94.13  ?  61  ILE B N     1 
ATOM   6586  C  CA    . ILE B 1 42  ? 154.050 183.909 99.770  1.00 92.76  ?  61  ILE B CA    1 
ATOM   6587  C  C     . ILE B 1 42  ? 152.663 184.490 99.528  1.00 92.28  ?  61  ILE B C     1 
ATOM   6588  O  O     . ILE B 1 42  ? 151.645 183.869 99.859  1.00 91.31  ?  61  ILE B O     1 
ATOM   6589  C  CB    . ILE B 1 42  ? 154.374 182.790 98.768  1.00 92.29  ?  61  ILE B CB    1 
ATOM   6590  C  CG1   . ILE B 1 42  ? 155.836 182.347 98.901  1.00 93.12  ?  61  ILE B CG1   1 
ATOM   6591  C  CG2   . ILE B 1 42  ? 154.093 183.248 97.346  1.00 93.47  ?  61  ILE B CG2   1 
ATOM   6592  C  CD1   . ILE B 1 42  ? 156.066 181.216 99.884  1.00 92.24  ?  61  ILE B CD1   1 
ATOM   6593  N  N     . GLY B 1 43  ? 152.618 185.687 98.949  1.00 98.54  ?  62  GLY B N     1 
ATOM   6594  C  CA    . GLY B 1 43  ? 151.356 186.332 98.643  1.00 98.39  ?  62  GLY B CA    1 
ATOM   6595  C  C     . GLY B 1 43  ? 150.870 187.329 99.677  1.00 98.19  ?  62  GLY B C     1 
ATOM   6596  O  O     . GLY B 1 43  ? 150.544 188.467 99.329  1.00 99.59  ?  62  GLY B O     1 
ATOM   6597  N  N     . ASN B 1 44  ? 150.809 186.925 100.944 1.00 96.69  ?  63  ASN B N     1 
ATOM   6598  C  CA    . ASN B 1 44  ? 150.281 187.805 101.976 1.00 99.87  ?  63  ASN B CA    1 
ATOM   6599  C  C     . ASN B 1 44  ? 151.290 188.900 102.324 1.00 102.49 ?  63  ASN B C     1 
ATOM   6600  O  O     . ASN B 1 44  ? 152.457 188.865 101.923 1.00 103.39 ?  63  ASN B O     1 
ATOM   6601  C  CB    . ASN B 1 44  ? 149.891 187.005 103.219 1.00 99.68  ?  63  ASN B CB    1 
ATOM   6602  C  CG    . ASN B 1 44  ? 150.931 185.978 103.603 1.00 99.89  ?  63  ASN B CG    1 
ATOM   6603  O  OD1   . ASN B 1 44  ? 152.105 186.116 103.270 1.00 101.08 ?  63  ASN B OD1   1 
ATOM   6604  N  ND2   . ASN B 1 44  ? 150.504 184.936 104.307 1.00 100.10 ?  63  ASN B ND2   1 
ATOM   6605  N  N     . ASN B 1 45  ? 150.818 189.888 103.082 1.00 105.51 ?  64  ASN B N     1 
ATOM   6606  C  CA    . ASN B 1 45  ? 151.597 191.086 103.362 1.00 104.22 ?  64  ASN B CA    1 
ATOM   6607  C  C     . ASN B 1 45  ? 152.750 190.781 104.321 1.00 103.27 ?  64  ASN B C     1 
ATOM   6608  O  O     . ASN B 1 45  ? 152.845 189.703 104.914 1.00 101.44 ?  64  ASN B O     1 
ATOM   6609  C  CB    . ASN B 1 45  ? 150.699 192.182 103.939 1.00 105.40 ?  64  ASN B CB    1 
ATOM   6610  C  CG    . ASN B 1 45  ? 151.289 193.570 103.767 1.00 106.61 ?  64  ASN B CG    1 
ATOM   6611  O  OD1   . ASN B 1 45  ? 151.837 194.145 104.708 1.00 104.60 ?  64  ASN B OD1   1 
ATOM   6612  N  ND2   . ASN B 1 45  ? 151.182 194.115 102.560 1.00 107.23 ?  64  ASN B ND2   1 
ATOM   6613  N  N     . ILE B 1 46  ? 153.639 191.766 104.461 1.00 98.36  ?  65  ILE B N     1 
ATOM   6614  C  CA    . ILE B 1 46  ? 154.831 191.673 105.299 1.00 100.33 ?  65  ILE B CA    1 
ATOM   6615  C  C     . ILE B 1 46  ? 154.443 191.918 106.754 1.00 99.40  ?  65  ILE B C     1 
ATOM   6616  O  O     . ILE B 1 46  ? 155.291 191.886 107.654 1.00 100.25 ?  65  ILE B O     1 
ATOM   6617  C  CB    . ILE B 1 46  ? 155.904 192.675 104.824 1.00 98.17  ?  65  ILE B CB    1 
ATOM   6618  C  CG1   . ILE B 1 46  ? 157.254 192.429 105.505 1.00 95.33  ?  65  ILE B CG1   1 
ATOM   6619  C  CG2   . ILE B 1 46  ? 155.445 194.105 105.070 1.00 98.78  ?  65  ILE B CG2   1 
ATOM   6620  C  CD1   . ILE B 1 46  ? 158.407 193.161 104.853 1.00 99.39  ?  65  ILE B CD1   1 
ATOM   6621  N  N     . ASP B 1 47  ? 153.150 192.151 106.997 1.00 96.97  ?  66  ASP B N     1 
ATOM   6622  C  CA    . ASP B 1 47  ? 152.697 192.521 108.335 1.00 99.74  ?  66  ASP B CA    1 
ATOM   6623  C  C     . ASP B 1 47  ? 152.985 191.433 109.364 1.00 99.23  ?  66  ASP B C     1 
ATOM   6624  O  O     . ASP B 1 47  ? 153.262 191.741 110.528 1.00 101.47 ?  66  ASP B O     1 
ATOM   6625  C  CB    . ASP B 1 47  ? 151.202 192.840 108.309 1.00 101.67 ?  66  ASP B CB    1 
ATOM   6626  C  CG    . ASP B 1 47  ? 150.912 194.232 107.784 1.00 103.06 ?  66  ASP B CG    1 
ATOM   6627  O  OD1   . ASP B 1 47  ? 151.773 195.122 107.944 1.00 102.76 ?  66  ASP B OD1   1 
ATOM   6628  O  OD2   . ASP B 1 47  ? 149.822 194.436 107.210 1.00 101.89 -1 66  ASP B OD2   1 
ATOM   6629  N  N     . MET B 1 48  ? 152.936 190.162 108.959 1.00 92.53  ?  67  MET B N     1 
ATOM   6630  C  CA    . MET B 1 48  ? 153.119 189.076 109.916 1.00 94.79  ?  67  MET B CA    1 
ATOM   6631  C  C     . MET B 1 48  ? 154.577 188.917 110.333 1.00 93.20  ?  67  MET B C     1 
ATOM   6632  O  O     . MET B 1 48  ? 154.853 188.525 111.473 1.00 94.46  ?  67  MET B O     1 
ATOM   6633  C  CB    . MET B 1 48  ? 152.593 187.767 109.328 1.00 94.92  ?  67  MET B CB    1 
ATOM   6634  C  CG    . MET B 1 48  ? 153.177 187.421 107.970 1.00 93.38  ?  67  MET B CG    1 
ATOM   6635  S  SD    . MET B 1 48  ? 152.220 186.155 107.120 1.00 101.90 ?  67  MET B SD    1 
ATOM   6636  C  CE    . MET B 1 48  ? 150.641 186.987 106.976 1.00 96.07  ?  67  MET B CE    1 
ATOM   6637  N  N     . LEU B 1 49  ? 155.518 189.204 109.431 1.00 94.28  ?  68  LEU B N     1 
ATOM   6638  C  CA    . LEU B 1 49  ? 156.926 188.956 109.722 1.00 96.15  ?  68  LEU B CA    1 
ATOM   6639  C  C     . LEU B 1 49  ? 157.471 189.923 110.766 1.00 96.35  ?  68  LEU B C     1 
ATOM   6640  O  O     . LEU B 1 49  ? 158.361 189.557 111.542 1.00 97.44  ?  68  LEU B O     1 
ATOM   6641  C  CB    . LEU B 1 49  ? 157.743 189.047 108.436 1.00 96.58  ?  68  LEU B CB    1 
ATOM   6642  C  CG    . LEU B 1 49  ? 157.071 188.398 107.225 1.00 97.62  ?  68  LEU B CG    1 
ATOM   6643  C  CD1   . LEU B 1 49  ? 157.833 188.727 105.954 1.00 96.09  ?  68  LEU B CD1   1 
ATOM   6644  C  CD2   . LEU B 1 49  ? 156.920 186.893 107.410 1.00 95.90  ?  68  LEU B CD2   1 
ATOM   6645  N  N     . ILE B 1 50  ? 156.964 191.151 110.792 1.00 88.71  ?  69  ILE B N     1 
ATOM   6646  C  CA    . ILE B 1 50  ? 157.398 192.164 111.749 1.00 85.38  ?  69  ILE B CA    1 
ATOM   6647  C  C     . ILE B 1 50  ? 156.986 191.716 113.147 1.00 87.48  ?  69  ILE B C     1 
ATOM   6648  O  O     . ILE B 1 50  ? 155.917 191.110 113.308 1.00 93.40  ?  69  ILE B O     1 
ATOM   6649  C  CB    . ILE B 1 50  ? 156.806 193.541 111.399 1.00 86.80  ?  69  ILE B CB    1 
ATOM   6650  C  CG1   . ILE B 1 50  ? 157.089 193.886 109.936 1.00 88.62  ?  69  ILE B CG1   1 
ATOM   6651  C  CG2   . ILE B 1 50  ? 157.362 194.628 112.307 1.00 89.57  ?  69  ILE B CG2   1 
ATOM   6652  C  CD1   . ILE B 1 50  ? 158.546 193.764 109.550 1.00 90.65  ?  69  ILE B CD1   1 
ATOM   6653  N  N     . PRO B 1 51  ? 157.802 191.960 114.173 1.00 86.49  ?  70  PRO B N     1 
ATOM   6654  C  CA    . PRO B 1 51  ? 157.355 191.689 115.544 1.00 92.44  ?  70  PRO B CA    1 
ATOM   6655  C  C     . PRO B 1 51  ? 156.129 192.518 115.894 1.00 95.97  ?  70  PRO B C     1 
ATOM   6656  O  O     . PRO B 1 51  ? 155.932 193.624 115.384 1.00 97.68  ?  70  PRO B O     1 
ATOM   6657  C  CB    . PRO B 1 51  ? 158.566 192.082 116.398 1.00 93.45  ?  70  PRO B CB    1 
ATOM   6658  C  CG    . PRO B 1 51  ? 159.731 191.942 115.480 1.00 91.01  ?  70  PRO B CG    1 
ATOM   6659  C  CD    . PRO B 1 51  ? 159.230 192.317 114.117 1.00 88.23  ?  70  PRO B CD    1 
ATOM   6660  N  N     . ARG B 1 52  ? 155.298 191.962 116.780 1.00 91.65  ?  71  ARG B N     1 
ATOM   6661  C  CA    . ARG B 1 52  ? 153.991 192.544 117.072 1.00 88.43  ?  71  ARG B CA    1 
ATOM   6662  C  C     . ARG B 1 52  ? 154.078 193.974 117.595 1.00 88.95  ?  71  ARG B C     1 
ATOM   6663  O  O     . ARG B 1 52  ? 153.104 194.725 117.470 1.00 91.42  ?  71  ARG B O     1 
ATOM   6664  C  CB    . ARG B 1 52  ? 153.244 191.669 118.079 1.00 91.28  ?  71  ARG B CB    1 
ATOM   6665  C  CG    . ARG B 1 52  ? 152.570 190.453 117.462 1.00 92.39  ?  71  ARG B CG    1 
ATOM   6666  C  CD    . ARG B 1 52  ? 151.367 190.011 118.280 1.00 92.82  ?  71  ARG B CD    1 
ATOM   6667  N  NE    . ARG B 1 52  ? 150.601 191.146 118.780 1.00 94.13  ?  71  ARG B NE    1 
ATOM   6668  C  CZ    . ARG B 1 52  ? 149.699 191.812 118.072 1.00 91.45  ?  71  ARG B CZ    1 
ATOM   6669  N  NH1   . ARG B 1 52  ? 149.420 191.481 116.822 1.00 90.57  1  71  ARG B NH1   1 
ATOM   6670  N  NH2   . ARG B 1 52  ? 149.060 192.835 118.632 1.00 89.13  ?  71  ARG B NH2   1 
ATOM   6671  N  N     . ASP B 1 53  ? 155.210 194.369 118.175 1.00 88.99  ?  72  ASP B N     1 
ATOM   6672  C  CA    . ASP B 1 53  ? 155.346 195.712 118.724 1.00 88.72  ?  72  ASP B CA    1 
ATOM   6673  C  C     . ASP B 1 53  ? 155.772 196.748 117.690 1.00 88.02  ?  72  ASP B C     1 
ATOM   6674  O  O     . ASP B 1 53  ? 155.873 197.931 118.033 1.00 88.32  ?  72  ASP B O     1 
ATOM   6675  C  CB    . ASP B 1 53  ? 156.345 195.707 119.886 1.00 89.53  ?  72  ASP B CB    1 
ATOM   6676  C  CG    . ASP B 1 53  ? 157.681 195.099 119.506 1.00 91.06  ?  72  ASP B CG    1 
ATOM   6677  O  OD1   . ASP B 1 53  ? 157.795 194.555 118.388 1.00 91.21  ?  72  ASP B OD1   1 
ATOM   6678  O  OD2   . ASP B 1 53  ? 158.620 195.167 120.327 1.00 91.78  -1 72  ASP B OD2   1 
ATOM   6679  N  N     . LEU B 1 54  ? 156.026 196.343 116.443 1.00 85.88  ?  73  LEU B N     1 
ATOM   6680  C  CA    . LEU B 1 54  ? 156.521 197.261 115.425 1.00 87.53  ?  73  LEU B CA    1 
ATOM   6681  C  C     . LEU B 1 54  ? 155.699 197.208 114.139 1.00 85.95  ?  73  LEU B C     1 
ATOM   6682  O  O     . LEU B 1 54  ? 156.081 197.843 113.145 1.00 87.01  ?  73  LEU B O     1 
ATOM   6683  C  CB    . LEU B 1 54  ? 157.999 196.967 115.129 1.00 90.60  ?  73  LEU B CB    1 
ATOM   6684  C  CG    . LEU B 1 54  ? 158.858 198.046 114.465 1.00 90.76  ?  73  LEU B CG    1 
ATOM   6685  C  CD1   . LEU B 1 54  ? 159.029 199.236 115.394 1.00 88.53  ?  73  LEU B CD1   1 
ATOM   6686  C  CD2   . LEU B 1 54  ? 160.212 197.479 114.063 1.00 90.02  ?  73  LEU B CD2   1 
ATOM   6687  N  N     . ARG B 1 55  ? 154.585 196.473 114.131 1.00 83.31  ?  74  ARG B N     1 
ATOM   6688  C  CA    . ARG B 1 55  ? 153.767 196.368 112.923 1.00 89.30  ?  74  ARG B CA    1 
ATOM   6689  C  C     . ARG B 1 55  ? 153.250 197.712 112.426 1.00 93.34  ?  74  ARG B C     1 
ATOM   6690  O  O     . ARG B 1 55  ? 153.321 197.959 111.210 1.00 92.62  ?  74  ARG B O     1 
ATOM   6691  C  CB    . ARG B 1 55  ? 152.612 195.389 113.158 1.00 87.29  ?  74  ARG B CB    1 
ATOM   6692  C  CG    . ARG B 1 55  ? 152.909 194.303 114.168 1.00 85.88  ?  74  ARG B CG    1 
ATOM   6693  C  CD    . ARG B 1 55  ? 153.410 193.044 113.484 1.00 87.42  ?  74  ARG B CD    1 
ATOM   6694  N  NE    . ARG B 1 55  ? 152.394 192.425 112.641 1.00 87.57  ?  74  ARG B NE    1 
ATOM   6695  C  CZ    . ARG B 1 55  ? 151.417 191.649 113.090 1.00 88.30  ?  74  ARG B CZ    1 
ATOM   6696  N  NH1   . ARG B 1 55  ? 151.290 191.372 114.378 1.00 88.27  1  74  ARG B NH1   1 
ATOM   6697  N  NH2   . ARG B 1 55  ? 150.549 191.133 112.225 1.00 88.12  ?  74  ARG B NH2   1 
ATOM   6698  N  N     . PRO B 1 56  ? 152.710 198.606 113.265 1.00 96.81  ?  75  PRO B N     1 
ATOM   6699  C  CA    . PRO B 1 56  ? 152.262 199.901 112.725 1.00 93.77  ?  75  PRO B CA    1 
ATOM   6700  C  C     . PRO B 1 56  ? 153.406 200.826 112.349 1.00 92.61  ?  75  PRO B C     1 
ATOM   6701  O  O     . PRO B 1 56  ? 153.252 201.636 111.426 1.00 92.88  ?  75  PRO B O     1 
ATOM   6702  C  CB    . PRO B 1 56  ? 151.411 200.489 113.862 1.00 92.31  ?  75  PRO B CB    1 
ATOM   6703  C  CG    . PRO B 1 56  ? 151.144 199.348 114.795 1.00 93.43  ?  75  PRO B CG    1 
ATOM   6704  C  CD    . PRO B 1 56  ? 152.340 198.467 114.684 1.00 94.86  ?  75  PRO B CD    1 
ATOM   6705  N  N     . ALA B 1 57  ? 154.545 200.738 113.037 1.00 92.81  ?  76  ALA B N     1 
ATOM   6706  C  CA    . ALA B 1 57  ? 155.654 201.647 112.769 1.00 97.15  ?  76  ALA B CA    1 
ATOM   6707  C  C     . ALA B 1 57  ? 156.428 201.274 111.510 1.00 95.46  ?  76  ALA B C     1 
ATOM   6708  O  O     . ALA B 1 57  ? 156.947 202.163 110.825 1.00 94.01  ?  76  ALA B O     1 
ATOM   6709  C  CB    . ALA B 1 57  ? 156.601 201.687 113.969 1.00 96.13  ?  76  ALA B CB    1 
ATOM   6710  N  N     . HIS B 1 58  ? 156.523 199.982 111.196 1.00 88.55  ?  77  HIS B N     1 
ATOM   6711  C  CA    . HIS B 1 58  ? 157.384 199.544 110.096 1.00 88.39  ?  77  HIS B CA    1 
ATOM   6712  C  C     . HIS B 1 58  ? 156.987 200.085 108.724 1.00 87.46  ?  77  HIS B C     1 
ATOM   6713  O  O     . HIS B 1 58  ? 157.872 200.593 108.014 1.00 89.63  ?  77  HIS B O     1 
ATOM   6714  C  CB    . HIS B 1 58  ? 157.442 198.013 110.072 1.00 91.45  ?  77  HIS B CB    1 
ATOM   6715  C  CG    . HIS B 1 58  ? 158.284 197.463 108.962 1.00 89.84  ?  77  HIS B CG    1 
ATOM   6716  N  ND1   . HIS B 1 58  ? 157.772 197.152 107.721 1.00 90.58  ?  77  HIS B ND1   1 
ATOM   6717  C  CD2   . HIS B 1 58  ? 159.605 197.171 108.907 1.00 88.37  ?  77  HIS B CD2   1 
ATOM   6718  C  CE1   . HIS B 1 58  ? 158.741 196.693 106.950 1.00 87.73  ?  77  HIS B CE1   1 
ATOM   6719  N  NE2   . HIS B 1 58  ? 159.863 196.694 107.646 1.00 88.70  ?  77  HIS B NE2   1 
ATOM   6720  N  N     . PRO B 1 59  ? 155.723 200.014 108.281 1.00 86.53  ?  78  PRO B N     1 
ATOM   6721  C  CA    . PRO B 1 59  ? 155.445 200.176 106.840 1.00 89.83  ?  78  PRO B CA    1 
ATOM   6722  C  C     . PRO B 1 59  ? 155.819 201.531 106.261 1.00 91.83  ?  78  PRO B C     1 
ATOM   6723  O  O     . PRO B 1 59  ? 155.981 201.633 105.039 1.00 89.81  ?  78  PRO B O     1 
ATOM   6724  C  CB    . PRO B 1 59  ? 153.932 199.939 106.745 1.00 88.63  ?  78  PRO B CB    1 
ATOM   6725  C  CG    . PRO B 1 59  ? 153.419 200.270 108.092 1.00 89.50  ?  78  PRO B CG    1 
ATOM   6726  C  CD    . PRO B 1 59  ? 154.477 199.805 109.039 1.00 85.74  ?  78  PRO B CD    1 
ATOM   6727  N  N     . GLU B 1 60  ? 155.958 202.575 107.082 1.00 99.44  ?  79  GLU B N     1 
ATOM   6728  C  CA    . GLU B 1 60  ? 156.314 203.881 106.536 1.00 98.88  ?  79  GLU B CA    1 
ATOM   6729  C  C     . GLU B 1 60  ? 157.759 203.913 106.053 1.00 101.00 ?  79  GLU B C     1 
ATOM   6730  O  O     . GLU B 1 60  ? 158.094 204.689 105.148 1.00 103.14 ?  79  GLU B O     1 
ATOM   6731  C  CB    . GLU B 1 60  ? 156.074 204.972 107.581 1.00 99.20  ?  79  GLU B CB    1 
ATOM   6732  C  CG    . GLU B 1 60  ? 156.124 206.399 107.038 1.00 101.37 ?  79  GLU B CG    1 
ATOM   6733  C  CD    . GLU B 1 60  ? 155.474 206.543 105.673 1.00 101.78 ?  79  GLU B CD    1 
ATOM   6734  O  OE1   . GLU B 1 60  ? 156.113 207.124 104.770 1.00 100.84 ?  79  GLU B OE1   1 
ATOM   6735  O  OE2   . GLU B 1 60  ? 154.319 206.095 105.506 1.00 100.29 -1 79  GLU B OE2   1 
ATOM   6736  N  N     . TYR B 1 61  ? 158.621 203.077 106.638 1.00 92.58  ?  80  TYR B N     1 
ATOM   6737  C  CA    . TYR B 1 61  ? 160.025 203.050 106.241 1.00 90.20  ?  80  TYR B CA    1 
ATOM   6738  C  C     . TYR B 1 61  ? 160.187 202.581 104.801 1.00 92.45  ?  80  TYR B C     1 
ATOM   6739  O  O     . TYR B 1 61  ? 161.038 203.097 104.068 1.00 94.05  ?  80  TYR B O     1 
ATOM   6740  C  CB    . TYR B 1 61  ? 160.818 202.152 107.189 1.00 90.21  ?  80  TYR B CB    1 
ATOM   6741  C  CG    . TYR B 1 61  ? 160.945 202.710 108.587 1.00 90.73  ?  80  TYR B CG    1 
ATOM   6742  C  CD1   . TYR B 1 61  ? 161.412 203.999 108.801 1.00 92.59  ?  80  TYR B CD1   1 
ATOM   6743  C  CD2   . TYR B 1 61  ? 160.594 201.948 109.693 1.00 93.50  ?  80  TYR B CD2   1 
ATOM   6744  C  CE1   . TYR B 1 61  ? 161.529 204.514 110.078 1.00 95.44  ?  80  TYR B CE1   1 
ATOM   6745  C  CE2   . TYR B 1 61  ? 160.707 202.454 110.974 1.00 94.17  ?  80  TYR B CE2   1 
ATOM   6746  C  CZ    . TYR B 1 61  ? 161.175 203.736 111.161 1.00 94.71  ?  80  TYR B CZ    1 
ATOM   6747  O  OH    . TYR B 1 61  ? 161.288 204.242 112.436 1.00 93.15  ?  80  TYR B OH    1 
ATOM   6748  N  N     . ILE B 1 62  ? 159.389 201.596 104.382 1.00 102.54 ?  81  ILE B N     1 
ATOM   6749  C  CA    . ILE B 1 62  ? 159.467 201.102 103.008 1.00 106.18 ?  81  ILE B CA    1 
ATOM   6750  C  C     . ILE B 1 62  ? 159.120 202.213 102.025 1.00 108.79 ?  81  ILE B C     1 
ATOM   6751  O  O     . ILE B 1 62  ? 159.813 202.421 101.021 1.00 109.20 ?  81  ILE B O     1 
ATOM   6752  C  CB    . ILE B 1 62  ? 158.549 199.880 102.827 1.00 106.15 ?  81  ILE B CB    1 
ATOM   6753  C  CG1   . ILE B 1 62  ? 159.070 198.696 103.644 1.00 105.85 ?  81  ILE B CG1   1 
ATOM   6754  C  CG2   . ILE B 1 62  ? 158.433 199.509 101.354 1.00 104.15 ?  81  ILE B CG2   1 
ATOM   6755  C  CD1   . ILE B 1 62  ? 158.191 197.469 103.563 1.00 104.12 ?  81  ILE B CD1   1 
ATOM   6756  N  N     . ARG B 1 63  ? 158.039 202.947 102.304 1.00 109.49 ?  82  ARG B N     1 
ATOM   6757  C  CA    . ARG B 1 63  ? 157.640 204.044 101.427 1.00 108.34 ?  82  ARG B CA    1 
ATOM   6758  C  C     . ARG B 1 63  ? 158.687 205.151 101.416 1.00 105.36 ?  82  ARG B C     1 
ATOM   6759  O  O     . ARG B 1 63  ? 158.972 205.735 100.363 1.00 101.40 ?  82  ARG B O     1 
ATOM   6760  C  CB    . ARG B 1 63  ? 156.280 204.594 101.859 1.00 107.68 ?  82  ARG B CB    1 
ATOM   6761  C  CG    . ARG B 1 63  ? 155.672 205.592 100.885 1.00 108.34 ?  82  ARG B CG    1 
ATOM   6762  C  CD    . ARG B 1 63  ? 155.595 206.986 101.490 1.00 108.80 ?  82  ARG B CD    1 
ATOM   6763  N  NE    . ARG B 1 63  ? 154.623 207.827 100.801 1.00 108.76 ?  82  ARG B NE    1 
ATOM   6764  C  CZ    . ARG B 1 63  ? 154.298 209.057 101.174 1.00 107.65 ?  82  ARG B CZ    1 
ATOM   6765  N  NH1   . ARG B 1 63  ? 154.852 209.628 102.231 1.00 107.03 1  82  ARG B NH1   1 
ATOM   6766  N  NH2   . ARG B 1 63  ? 153.394 209.731 100.469 1.00 107.08 ?  82  ARG B NH2   1 
ATOM   6767  N  N     . HIS B 1 64  ? 159.264 205.462 102.579 1.00 107.10 ?  83  HIS B N     1 
ATOM   6768  C  CA    . HIS B 1 64  ? 160.297 206.493 102.632 1.00 107.72 ?  83  HIS B CA    1 
ATOM   6769  C  C     . HIS B 1 64  ? 161.525 206.087 101.825 1.00 107.22 ?  83  HIS B C     1 
ATOM   6770  O  O     . HIS B 1 64  ? 162.104 206.909 101.105 1.00 105.48 ?  83  HIS B O     1 
ATOM   6771  C  CB    . HIS B 1 64  ? 160.678 206.783 104.082 1.00 107.48 ?  83  HIS B CB    1 
ATOM   6772  C  CG    . HIS B 1 64  ? 161.901 207.634 104.224 1.00 108.37 ?  83  HIS B CG    1 
ATOM   6773  N  ND1   . HIS B 1 64  ? 162.992 207.253 104.975 1.00 109.41 ?  83  HIS B ND1   1 
ATOM   6774  C  CD2   . HIS B 1 64  ? 162.207 208.847 103.705 1.00 106.54 ?  83  HIS B CD2   1 
ATOM   6775  C  CE1   . HIS B 1 64  ? 163.916 208.195 104.916 1.00 108.40 ?  83  HIS B CE1   1 
ATOM   6776  N  NE2   . HIS B 1 64  ? 163.465 209.173 104.151 1.00 107.54 ?  83  HIS B NE2   1 
ATOM   6777  N  N     . ASN B 1 65  ? 161.938 204.822 101.934 1.00 104.97 ?  84  ASN B N     1 
ATOM   6778  C  CA    . ASN B 1 65  ? 163.075 204.341 101.156 1.00 104.77 ?  84  ASN B CA    1 
ATOM   6779  C  C     . ASN B 1 65  ? 162.764 204.361 99.664  1.00 107.30 ?  84  ASN B C     1 
ATOM   6780  O  O     . ASN B 1 65  ? 163.630 204.701 98.848  1.00 108.88 ?  84  ASN B O     1 
ATOM   6781  C  CB    . ASN B 1 65  ? 163.458 202.932 101.612 1.00 103.89 ?  84  ASN B CB    1 
ATOM   6782  C  CG    . ASN B 1 65  ? 164.801 202.480 101.064 1.00 104.72 ?  84  ASN B CG    1 
ATOM   6783  O  OD1   . ASN B 1 65  ? 165.464 203.206 100.322 1.00 105.94 ?  84  ASN B OD1   1 
ATOM   6784  N  ND2   . ASN B 1 65  ? 165.211 201.272 101.432 1.00 104.61 ?  84  ASN B ND2   1 
ATOM   6785  N  N     . ARG B 1 66  ? 161.535 203.997 99.291  1.00 111.81 ?  85  ARG B N     1 
ATOM   6786  C  CA    . ARG B 1 66  ? 161.137 204.052 97.888  1.00 112.45 ?  85  ARG B CA    1 
ATOM   6787  C  C     . ARG B 1 66  ? 161.190 205.479 97.357  1.00 114.69 ?  85  ARG B C     1 
ATOM   6788  O  O     . ARG B 1 66  ? 161.647 205.716 96.233  1.00 114.06 ?  85  ARG B O     1 
ATOM   6789  C  CB    . ARG B 1 66  ? 159.733 203.471 97.722  1.00 108.79 ?  85  ARG B CB    1 
ATOM   6790  C  CG    . ARG B 1 66  ? 159.698 201.957 97.602  1.00 108.66 ?  85  ARG B CG    1 
ATOM   6791  C  CD    . ARG B 1 66  ? 158.273 201.431 97.673  1.00 109.39 ?  85  ARG B CD    1 
ATOM   6792  N  NE    . ARG B 1 66  ? 158.228 199.976 97.591  1.00 111.92 ?  85  ARG B NE    1 
ATOM   6793  C  CZ    . ARG B 1 66  ? 158.191 199.290 96.457  1.00 111.15 ?  85  ARG B CZ    1 
ATOM   6794  N  NH1   . ARG B 1 66  ? 158.187 199.898 95.283  1.00 111.60 1  85  ARG B NH1   1 
ATOM   6795  N  NH2   . ARG B 1 66  ? 158.158 197.961 96.503  1.00 109.56 ?  85  ARG B NH2   1 
ATOM   6796  N  N     . GLU B 1 67  ? 160.718 206.442 98.152  1.00 117.70 ?  86  GLU B N     1 
ATOM   6797  C  CA    . GLU B 1 67  ? 160.794 207.842 97.748  1.00 115.20 ?  86  GLU B CA    1 
ATOM   6798  C  C     . GLU B 1 67  ? 162.241 208.302 97.621  1.00 113.19 ?  86  GLU B C     1 
ATOM   6799  O  O     . GLU B 1 67  ? 162.591 209.022 96.678  1.00 111.44 ?  86  GLU B O     1 
ATOM   6800  C  CB    . GLU B 1 67  ? 160.038 208.719 98.747  1.00 115.49 ?  86  GLU B CB    1 
ATOM   6801  C  CG    . GLU B 1 67  ? 158.529 208.538 98.716  1.00 115.22 ?  86  GLU B CG    1 
ATOM   6802  C  CD    . GLU B 1 67  ? 157.815 209.427 99.715  1.00 115.84 ?  86  GLU B CD    1 
ATOM   6803  O  OE1   . GLU B 1 67  ? 158.330 209.594 100.840 1.00 116.74 ?  86  GLU B OE1   1 
ATOM   6804  O  OE2   . GLU B 1 67  ? 156.737 209.960 99.375  1.00 115.36 -1 86  GLU B OE2   1 
ATOM   6805  N  N     . GLY B 1 68  ? 163.095 207.901 98.565  1.00 117.13 ?  87  GLY B N     1 
ATOM   6806  C  CA    . GLY B 1 68  ? 164.490 208.313 98.510  1.00 117.99 ?  87  GLY B CA    1 
ATOM   6807  C  C     . GLY B 1 68  ? 165.215 207.761 97.298  1.00 118.47 ?  87  GLY B C     1 
ATOM   6808  O  O     . GLY B 1 68  ? 165.936 208.485 96.606  1.00 117.86 ?  87  GLY B O     1 
ATOM   6809  N  N     . GLY B 1 69  ? 165.033 206.471 97.022  1.00 118.21 ?  88  GLY B N     1 
ATOM   6810  C  CA    . GLY B 1 69  ? 165.655 205.861 95.864  1.00 117.81 ?  88  GLY B CA    1 
ATOM   6811  C  C     . GLY B 1 69  ? 167.143 205.620 95.976  1.00 118.44 ?  88  GLY B C     1 
ATOM   6812  O  O     . GLY B 1 69  ? 167.788 205.358 94.956  1.00 118.33 ?  88  GLY B O     1 
ATOM   6813  N  N     . LYS B 1 70  ? 167.710 205.705 97.176  1.00 113.32 ?  89  LYS B N     1 
ATOM   6814  C  CA    . LYS B 1 70  ? 169.142 205.499 97.345  1.00 112.54 ?  89  LYS B CA    1 
ATOM   6815  C  C     . LYS B 1 70  ? 169.517 204.051 97.050  1.00 113.08 ?  89  LYS B C     1 
ATOM   6816  O  O     . LYS B 1 70  ? 168.774 203.120 97.373  1.00 112.76 ?  89  LYS B O     1 
ATOM   6817  C  CB    . LYS B 1 70  ? 169.569 205.876 98.764  1.00 110.68 ?  89  LYS B CB    1 
ATOM   6818  C  CG    . LYS B 1 70  ? 169.230 207.306 99.151  1.00 111.59 ?  89  LYS B CG    1 
ATOM   6819  C  CD    . LYS B 1 70  ? 169.080 207.454 100.657 1.00 112.45 ?  89  LYS B CD    1 
ATOM   6820  C  CE    . LYS B 1 70  ? 170.391 207.172 101.374 1.00 111.82 ?  89  LYS B CE    1 
ATOM   6821  N  NZ    . LYS B 1 70  ? 170.284 207.417 102.839 1.00 110.65 1  89  LYS B NZ    1 
ATOM   6822  N  N     . ALA B 1 71  ? 170.685 203.866 96.431  1.00 111.29 ?  90  ALA B N     1 
ATOM   6823  C  CA    . ALA B 1 71  ? 171.133 202.525 96.071  1.00 112.82 ?  90  ALA B CA    1 
ATOM   6824  C  C     . ALA B 1 71  ? 171.570 201.743 97.304  1.00 112.21 ?  90  ALA B C     1 
ATOM   6825  O  O     . ALA B 1 71  ? 171.003 200.692 97.623  1.00 111.34 ?  90  ALA B O     1 
ATOM   6826  C  CB    . ALA B 1 71  ? 172.270 202.609 95.050  1.00 110.82 ?  90  ALA B CB    1 
ATOM   6827  N  N     . ARG B 1 72  ? 172.580 202.242 98.011  1.00 96.25  ?  91  ARG B N     1 
ATOM   6828  C  CA    . ARG B 1 72  ? 173.057 201.592 99.225  1.00 93.94  ?  91  ARG B CA    1 
ATOM   6829  C  C     . ARG B 1 72  ? 172.150 201.971 100.388 1.00 95.58  ?  91  ARG B C     1 
ATOM   6830  O  O     . ARG B 1 72  ? 171.998 203.157 100.703 1.00 96.40  ?  91  ARG B O     1 
ATOM   6831  C  CB    . ARG B 1 72  ? 174.502 201.992 99.513  1.00 91.68  ?  91  ARG B CB    1 
ATOM   6832  C  CG    . ARG B 1 72  ? 175.030 201.504 100.853 1.00 92.78  ?  91  ARG B CG    1 
ATOM   6833  C  CD    . ARG B 1 72  ? 175.253 199.999 100.850 1.00 94.72  ?  91  ARG B CD    1 
ATOM   6834  N  NE    . ARG B 1 72  ? 174.136 199.275 101.444 1.00 94.13  ?  91  ARG B NE    1 
ATOM   6835  C  CZ    . ARG B 1 72  ? 173.962 197.963 101.353 1.00 93.15  ?  91  ARG B CZ    1 
ATOM   6836  N  NH1   . ARG B 1 72  ? 174.820 197.196 100.701 1.00 93.30  1  91  ARG B NH1   1 
ATOM   6837  N  NH2   . ARG B 1 72  ? 172.901 197.408 101.931 1.00 93.92  ?  91  ARG B NH2   1 
ATOM   6838  N  N     . VAL B 1 73  ? 171.548 200.969 101.025 1.00 90.09  ?  92  VAL B N     1 
ATOM   6839  C  CA    . VAL B 1 73  ? 170.633 201.191 102.139 1.00 87.70  ?  92  VAL B CA    1 
ATOM   6840  C  C     . VAL B 1 73  ? 171.446 201.078 103.424 1.00 87.05  ?  92  VAL B C     1 
ATOM   6841  O  O     . VAL B 1 73  ? 171.763 199.980 103.882 1.00 88.22  ?  92  VAL B O     1 
ATOM   6842  C  CB    . VAL B 1 73  ? 169.463 200.208 102.120 1.00 87.08  ?  92  VAL B CB    1 
ATOM   6843  C  CG1   . VAL B 1 73  ? 168.450 200.581 103.193 1.00 85.40  ?  92  VAL B CG1   1 
ATOM   6844  C  CG2   . VAL B 1 73  ? 168.811 200.183 100.745 1.00 86.55  ?  92  VAL B CG2   1 
ATOM   6845  N  N     . GLU B 1 74  ? 171.790 202.228 104.007 1.00 87.68  ?  93  GLU B N     1 
ATOM   6846  C  CA    . GLU B 1 74  ? 172.530 202.239 105.262 1.00 89.33  ?  93  GLU B CA    1 
ATOM   6847  C  C     . GLU B 1 74  ? 171.683 201.773 106.438 1.00 87.33  ?  93  GLU B C     1 
ATOM   6848  O  O     . GLU B 1 74  ? 172.236 201.445 107.492 1.00 87.02  ?  93  GLU B O     1 
ATOM   6849  C  CB    . GLU B 1 74  ? 173.078 203.641 105.531 1.00 88.63  ?  93  GLU B CB    1 
ATOM   6850  C  CG    . GLU B 1 74  ? 173.917 204.200 104.394 1.00 87.42  ?  93  GLU B CG    1 
ATOM   6851  C  CD    . GLU B 1 74  ? 174.219 205.676 104.560 1.00 88.21  ?  93  GLU B CD    1 
ATOM   6852  O  OE1   . GLU B 1 74  ? 173.419 206.505 104.076 1.00 88.19  ?  93  GLU B OE1   1 
ATOM   6853  O  OE2   . GLU B 1 74  ? 175.257 206.008 105.169 1.00 87.72  -1 93  GLU B OE2   1 
ATOM   6854  N  N     . GLY B 1 75  ? 170.360 201.736 106.283 1.00 81.23  ?  94  GLY B N     1 
ATOM   6855  C  CA    . GLY B 1 75  ? 169.505 201.299 107.365 1.00 80.35  ?  94  GLY B CA    1 
ATOM   6856  C  C     . GLY B 1 75  ? 169.600 199.808 107.617 1.00 79.48  ?  94  GLY B C     1 
ATOM   6857  O  O     . GLY B 1 75  ? 170.071 199.030 106.786 1.00 82.77  ?  94  GLY B O     1 
ATOM   6858  N  N     . MET B 1 76  ? 169.141 199.412 108.805 1.00 70.42  ?  95  MET B N     1 
ATOM   6859  C  CA    . MET B 1 76  ? 169.156 198.024 109.265 1.00 73.68  ?  95  MET B CA    1 
ATOM   6860  C  C     . MET B 1 76  ? 170.562 197.434 109.290 1.00 71.48  ?  95  MET B C     1 
ATOM   6861  O  O     . MET B 1 76  ? 170.729 196.216 109.170 1.00 72.36  ?  95  MET B O     1 
ATOM   6862  C  CB    . MET B 1 76  ? 168.231 197.141 108.419 1.00 77.42  ?  95  MET B CB    1 
ATOM   6863  C  CG    . MET B 1 76  ? 166.771 197.184 108.836 1.00 77.29  ?  95  MET B CG    1 
ATOM   6864  S  SD    . MET B 1 76  ? 165.821 195.817 108.143 1.00 83.46  ?  95  MET B SD    1 
ATOM   6865  C  CE    . MET B 1 76  ? 166.577 195.667 106.527 1.00 70.39  ?  95  MET B CE    1 
ATOM   6866  N  N     . SER B 1 77  ? 171.583 198.280 109.440 1.00 68.12  ?  96  SER B N     1 
ATOM   6867  C  CA    . SER B 1 77  ? 172.958 197.802 109.497 1.00 72.35  ?  96  SER B CA    1 
ATOM   6868  C  C     . SER B 1 77  ? 173.300 197.142 110.826 1.00 73.02  ?  96  SER B C     1 
ATOM   6869  O  O     . SER B 1 77  ? 174.372 196.538 110.938 1.00 76.24  ?  96  SER B O     1 
ATOM   6870  C  CB    . SER B 1 77  ? 173.927 198.957 109.229 1.00 72.03  ?  96  SER B CB    1 
ATOM   6871  O  OG    . SER B 1 77  ? 174.061 199.787 110.369 1.00 69.11  ?  96  SER B OG    1 
ATOM   6872  N  N     . ALA B 1 78  ? 172.430 197.243 111.824 1.00 58.61  ?  97  ALA B N     1 
ATOM   6873  C  CA    . ALA B 1 78  ? 172.655 196.678 113.145 1.00 59.82  ?  97  ALA B CA    1 
ATOM   6874  C  C     . ALA B 1 78  ? 171.779 195.444 113.340 1.00 57.82  ?  97  ALA B C     1 
ATOM   6875  O  O     . ALA B 1 78  ? 170.927 195.117 112.510 1.00 59.67  ?  97  ALA B O     1 
ATOM   6876  C  CB    . ALA B 1 78  ? 172.387 197.725 114.228 1.00 65.00  ?  97  ALA B CB    1 
ATOM   6877  N  N     . GLU B 1 79  ? 172.000 194.760 114.459 1.00 56.63  ?  98  GLU B N     1 
ATOM   6878  C  CA    . GLU B 1 79  ? 171.232 193.567 114.788 1.00 59.44  ?  98  GLU B CA    1 
ATOM   6879  C  C     . GLU B 1 79  ? 169.773 193.919 115.055 1.00 61.11  ?  98  GLU B C     1 
ATOM   6880  O  O     . GLU B 1 79  ? 169.447 195.025 115.495 1.00 61.59  ?  98  GLU B O     1 
ATOM   6881  C  CB    . GLU B 1 79  ? 171.830 192.872 116.012 1.00 61.17  ?  98  GLU B CB    1 
ATOM   6882  C  CG    . GLU B 1 79  ? 171.945 193.762 117.245 1.00 62.82  ?  98  GLU B CG    1 
ATOM   6883  C  CD    . GLU B 1 79  ? 173.227 194.573 117.279 1.00 65.00  ?  98  GLU B CD    1 
ATOM   6884  O  OE1   . GLU B 1 79  ? 173.917 194.648 116.240 1.00 64.65  ?  98  GLU B OE1   1 
ATOM   6885  O  OE2   . GLU B 1 79  ? 173.544 195.138 118.347 1.00 68.05  -1 98  GLU B OE2   1 
ATOM   6886  N  N     . LEU B 1 80  ? 168.884 192.962 114.785 1.00 60.29  ?  99  LEU B N     1 
ATOM   6887  C  CA    . LEU B 1 80  ? 167.457 193.182 114.973 1.00 57.63  ?  99  LEU B CA    1 
ATOM   6888  C  C     . LEU B 1 80  ? 166.825 191.994 115.681 1.00 64.56  ?  99  LEU B C     1 
ATOM   6889  O  O     . LEU B 1 80  ? 167.148 190.838 115.391 1.00 71.28  ?  99  LEU B O     1 
ATOM   6890  C  CB    . LEU B 1 80  ? 166.748 193.423 113.635 1.00 56.57  ?  99  LEU B CB    1 
ATOM   6891  C  CG    . LEU B 1 80  ? 166.946 194.798 112.998 1.00 60.56  ?  99  LEU B CG    1 
ATOM   6892  C  CD1   . LEU B 1 80  ? 166.292 194.841 111.631 1.00 63.67  ?  99  LEU B CD1   1 
ATOM   6893  C  CD2   . LEU B 1 80  ? 166.384 195.887 113.898 1.00 63.33  ?  99  LEU B CD2   1 
ATOM   6894  N  N     . GLN B 1 81  ? 165.926 192.290 116.617 1.00 68.46  ?  100 GLN B N     1 
ATOM   6895  C  CA    . GLN B 1 81  ? 165.121 191.260 117.253 1.00 66.00  ?  100 GLN B CA    1 
ATOM   6896  C  C     . GLN B 1 81  ? 164.059 190.757 116.285 1.00 65.49  ?  100 GLN B C     1 
ATOM   6897  O  O     . GLN B 1 81  ? 163.581 191.491 115.416 1.00 68.44  ?  100 GLN B O     1 
ATOM   6898  C  CB    . GLN B 1 81  ? 164.462 191.796 118.524 1.00 67.32  ?  100 GLN B CB    1 
ATOM   6899  C  CG    . GLN B 1 81  ? 165.343 191.729 119.760 1.00 67.29  ?  100 GLN B CG    1 
ATOM   6900  C  CD    . GLN B 1 81  ? 165.439 190.329 120.334 1.00 71.03  ?  100 GLN B CD    1 
ATOM   6901  O  OE1   . GLN B 1 81  ? 166.045 189.439 119.736 1.00 72.22  ?  100 GLN B OE1   1 
ATOM   6902  N  NE2   . GLN B 1 81  ? 164.843 190.127 121.503 1.00 70.81  ?  100 GLN B NE2   1 
ATOM   6903  N  N     . LEU B 1 82  ? 163.685 189.491 116.447 1.00 70.75  ?  101 LEU B N     1 
ATOM   6904  C  CA    . LEU B 1 82  ? 162.785 188.819 115.523 1.00 74.23  ?  101 LEU B CA    1 
ATOM   6905  C  C     . LEU B 1 82  ? 161.787 187.976 116.298 1.00 79.76  ?  101 LEU B C     1 
ATOM   6906  O  O     . LEU B 1 82  ? 162.179 187.163 117.141 1.00 82.30  ?  101 LEU B O     1 
ATOM   6907  C  CB    . LEU B 1 82  ? 163.576 187.944 114.549 1.00 71.91  ?  101 LEU B CB    1 
ATOM   6908  C  CG    . LEU B 1 82  ? 162.787 187.080 113.572 1.00 75.24  ?  101 LEU B CG    1 
ATOM   6909  C  CD1   . LEU B 1 82  ? 161.799 187.927 112.792 1.00 75.49  ?  101 LEU B CD1   1 
ATOM   6910  C  CD2   . LEU B 1 82  ? 163.752 186.363 112.644 1.00 76.33  ?  101 LEU B CD2   1 
ATOM   6911  N  N     . GLU B 1 83  ? 160.504 188.165 116.002 1.00 86.28  ?  102 GLU B N     1 
ATOM   6912  C  CA    . GLU B 1 83  ? 159.428 187.399 116.617 1.00 83.73  ?  102 GLU B CA    1 
ATOM   6913  C  C     . GLU B 1 83  ? 159.040 186.257 115.685 1.00 84.83  ?  102 GLU B C     1 
ATOM   6914  O  O     . GLU B 1 83  ? 158.678 186.492 114.527 1.00 83.36  ?  102 GLU B O     1 
ATOM   6915  C  CB    . GLU B 1 83  ? 158.223 188.292 116.908 1.00 85.69  ?  102 GLU B CB    1 
ATOM   6916  C  CG    . GLU B 1 83  ? 157.105 187.604 117.672 1.00 86.11  ?  102 GLU B CG    1 
ATOM   6917  C  CD    . GLU B 1 83  ? 156.059 188.579 118.176 1.00 88.76  ?  102 GLU B CD    1 
ATOM   6918  O  OE1   . GLU B 1 83  ? 156.419 189.738 118.471 1.00 88.01  ?  102 GLU B OE1   1 
ATOM   6919  O  OE2   . GLU B 1 83  ? 154.878 188.186 118.278 1.00 90.12  -1 102 GLU B OE2   1 
ATOM   6920  N  N     . LYS B 1 84  ? 159.115 185.029 116.190 1.00 88.47  ?  103 LYS B N     1 
ATOM   6921  C  CA    . LYS B 1 84  ? 158.798 183.855 115.394 1.00 90.54  ?  103 LYS B CA    1 
ATOM   6922  C  C     . LYS B 1 84  ? 157.285 183.678 115.283 1.00 91.03  ?  103 LYS B C     1 
ATOM   6923  O  O     . LYS B 1 84  ? 156.495 184.500 115.757 1.00 92.28  ?  103 LYS B O     1 
ATOM   6924  C  CB    . LYS B 1 84  ? 159.446 182.612 116.001 1.00 90.18  ?  103 LYS B CB    1 
ATOM   6925  C  CG    . LYS B 1 84  ? 160.903 182.410 115.624 1.00 89.01  ?  103 LYS B CG    1 
ATOM   6926  C  CD    . LYS B 1 84  ? 161.432 181.098 116.181 1.00 88.90  ?  103 LYS B CD    1 
ATOM   6927  C  CE    . LYS B 1 84  ? 162.718 180.675 115.492 1.00 88.81  ?  103 LYS B CE    1 
ATOM   6928  N  NZ    . LYS B 1 84  ? 163.453 179.649 116.282 1.00 90.73  1  103 LYS B NZ    1 
ATOM   6929  N  N     . LYS B 1 85  ? 156.876 182.585 114.634 1.00 85.49  ?  104 LYS B N     1 
ATOM   6930  C  CA    . LYS B 1 85  ? 155.457 182.256 114.558 1.00 83.53  ?  104 LYS B CA    1 
ATOM   6931  C  C     . LYS B 1 85  ? 154.892 181.943 115.938 1.00 83.61  ?  104 LYS B C     1 
ATOM   6932  O  O     . LYS B 1 85  ? 153.782 182.370 116.277 1.00 84.37  ?  104 LYS B O     1 
ATOM   6933  C  CB    . LYS B 1 85  ? 155.243 181.077 113.608 1.00 85.29  ?  104 LYS B CB    1 
ATOM   6934  C  CG    . LYS B 1 85  ? 153.855 180.458 113.677 1.00 85.89  ?  104 LYS B CG    1 
ATOM   6935  C  CD    . LYS B 1 85  ? 153.657 179.422 112.581 1.00 85.24  ?  104 LYS B CD    1 
ATOM   6936  C  CE    . LYS B 1 85  ? 152.186 179.263 112.228 1.00 85.82  ?  104 LYS B CE    1 
ATOM   6937  N  NZ    . LYS B 1 85  ? 151.962 178.162 111.251 1.00 85.93  1  104 LYS B NZ    1 
ATOM   6938  N  N     . ASP B 1 86  ? 155.646 181.203 116.752 1.00 90.95  ?  105 ASP B N     1 
ATOM   6939  C  CA    . ASP B 1 86  ? 155.199 180.824 118.086 1.00 96.73  ?  105 ASP B CA    1 
ATOM   6940  C  C     . ASP B 1 86  ? 155.387 181.928 119.120 1.00 94.78  ?  105 ASP B C     1 
ATOM   6941  O  O     . ASP B 1 86  ? 154.949 181.761 120.263 1.00 95.33  ?  105 ASP B O     1 
ATOM   6942  C  CB    . ASP B 1 86  ? 155.928 179.556 118.543 1.00 95.46  ?  105 ASP B CB    1 
ATOM   6943  C  CG    . ASP B 1 86  ? 157.434 179.736 118.618 1.00 95.76  ?  105 ASP B CG    1 
ATOM   6944  O  OD1   . ASP B 1 86  ? 157.940 180.787 118.173 1.00 96.81  ?  105 ASP B OD1   1 
ATOM   6945  O  OD2   . ASP B 1 86  ? 158.115 178.821 119.127 1.00 95.46  -1 105 ASP B OD2   1 
ATOM   6946  N  N     . GLY B 1 87  ? 156.023 183.041 118.755 1.00 90.93  ?  106 GLY B N     1 
ATOM   6947  C  CA    . GLY B 1 87  ? 156.220 184.154 119.659 1.00 93.78  ?  106 GLY B CA    1 
ATOM   6948  C  C     . GLY B 1 87  ? 157.625 184.302 120.205 1.00 95.42  ?  106 GLY B C     1 
ATOM   6949  O  O     . GLY B 1 87  ? 157.934 185.349 120.786 1.00 96.98  ?  106 GLY B O     1 
ATOM   6950  N  N     . SER B 1 88  ? 158.479 183.296 120.041 1.00 89.69  ?  107 SER B N     1 
ATOM   6951  C  CA    . SER B 1 88  ? 159.857 183.407 120.499 1.00 91.93  ?  107 SER B CA    1 
ATOM   6952  C  C     . SER B 1 88  ? 160.632 184.394 119.631 1.00 93.42  ?  107 SER B C     1 
ATOM   6953  O  O     . SER B 1 88  ? 160.344 184.575 118.445 1.00 91.26  ?  107 SER B O     1 
ATOM   6954  C  CB    . SER B 1 88  ? 160.539 182.039 120.482 1.00 92.53  ?  107 SER B CB    1 
ATOM   6955  O  OG    . SER B 1 88  ? 160.441 181.436 119.204 1.00 92.88  ?  107 SER B OG    1 
ATOM   6956  N  N     . LYS B 1 89  ? 161.625 185.037 120.239 1.00 85.62  ?  108 LYS B N     1 
ATOM   6957  C  CA    . LYS B 1 89  ? 162.405 186.081 119.588 1.00 83.27  ?  108 LYS B CA    1 
ATOM   6958  C  C     . LYS B 1 89  ? 163.875 185.687 119.536 1.00 83.03  ?  108 LYS B C     1 
ATOM   6959  O  O     . LYS B 1 89  ? 164.418 185.143 120.503 1.00 82.14  ?  108 LYS B O     1 
ATOM   6960  C  CB    . LYS B 1 89  ? 162.248 187.421 120.316 1.00 79.34  ?  108 LYS B CB    1 
ATOM   6961  C  CG    . LYS B 1 89  ? 160.962 188.157 119.979 1.00 82.15  ?  108 LYS B CG    1 
ATOM   6962  C  CD    . LYS B 1 89  ? 160.822 189.440 120.780 1.00 83.59  ?  108 LYS B CD    1 
ATOM   6963  C  CE    . LYS B 1 89  ? 159.463 190.081 120.552 1.00 83.47  ?  108 LYS B CE    1 
ATOM   6964  N  NZ    . LYS B 1 89  ? 159.527 191.565 120.654 1.00 82.82  1  108 LYS B NZ    1 
ATOM   6965  N  N     . ILE B 1 90  ? 164.514 185.967 118.398 1.00 75.05  ?  109 ILE B N     1 
ATOM   6966  C  CA    . ILE B 1 90  ? 165.928 185.690 118.193 1.00 72.35  ?  109 ILE B CA    1 
ATOM   6967  C  C     . ILE B 1 90  ? 166.578 186.906 117.547 1.00 73.25  ?  109 ILE B C     1 
ATOM   6968  O  O     . ILE B 1 90  ? 165.913 187.752 116.948 1.00 74.28  ?  109 ILE B O     1 
ATOM   6969  C  CB    . ILE B 1 90  ? 166.163 184.436 117.323 1.00 69.75  ?  109 ILE B CB    1 
ATOM   6970  C  CG1   . ILE B 1 90  ? 165.332 184.512 116.042 1.00 66.57  ?  109 ILE B CG1   1 
ATOM   6971  C  CG2   . ILE B 1 90  ? 165.839 183.171 118.105 1.00 72.07  ?  109 ILE B CG2   1 
ATOM   6972  C  CD1   . ILE B 1 90  ? 165.652 183.421 115.048 1.00 69.99  ?  109 ILE B CD1   1 
ATOM   6973  N  N     . TRP B 1 91  ? 167.899 186.987 117.676 1.00 60.22  ?  110 TRP B N     1 
ATOM   6974  C  CA    . TRP B 1 91  ? 168.659 188.075 117.077 1.00 55.45  ?  110 TRP B CA    1 
ATOM   6975  C  C     . TRP B 1 91  ? 169.083 187.693 115.665 1.00 52.97  ?  110 TRP B C     1 
ATOM   6976  O  O     . TRP B 1 91  ? 169.536 186.571 115.423 1.00 61.37  ?  110 TRP B O     1 
ATOM   6977  C  CB    . TRP B 1 91  ? 169.888 188.405 117.925 1.00 59.19  ?  110 TRP B CB    1 
ATOM   6978  C  CG    . TRP B 1 91  ? 169.588 189.284 119.102 1.00 59.67  ?  110 TRP B CG    1 
ATOM   6979  C  CD1   . TRP B 1 91  ? 169.565 188.912 120.414 1.00 60.03  ?  110 TRP B CD1   1 
ATOM   6980  C  CD2   . TRP B 1 91  ? 169.253 190.678 119.075 1.00 53.33  ?  110 TRP B CD2   1 
ATOM   6981  N  NE1   . TRP B 1 91  ? 169.245 189.987 121.207 1.00 60.79  ?  110 TRP B NE1   1 
ATOM   6982  C  CE2   . TRP B 1 91  ? 169.048 191.083 120.409 1.00 58.62  ?  110 TRP B CE2   1 
ATOM   6983  C  CE3   . TRP B 1 91  ? 169.112 191.622 118.055 1.00 52.05  ?  110 TRP B CE3   1 
ATOM   6984  C  CZ2   . TRP B 1 91  ? 168.708 192.390 120.748 1.00 60.61  ?  110 TRP B CZ2   1 
ATOM   6985  C  CZ3   . TRP B 1 91  ? 168.772 192.919 118.393 1.00 56.29  ?  110 TRP B CZ3   1 
ATOM   6986  C  CH2   . TRP B 1 91  ? 168.575 193.292 119.728 1.00 60.14  ?  110 TRP B CH2   1 
ATOM   6987  N  N     . THR B 1 92  ? 168.935 188.633 114.731 1.00 45.30  ?  111 THR B N     1 
ATOM   6988  C  CA    . THR B 1 92  ? 169.261 188.386 113.335 1.00 49.74  ?  111 THR B CA    1 
ATOM   6989  C  C     . THR B 1 92  ? 170.041 189.564 112.771 1.00 50.50  ?  111 THR B C     1 
ATOM   6990  O  O     . THR B 1 92  ? 169.941 190.691 113.266 1.00 59.24  ?  111 THR B O     1 
ATOM   6991  C  CB    . THR B 1 92  ? 168.005 188.148 112.489 1.00 51.66  ?  111 THR B CB    1 
ATOM   6992  O  OG1   . THR B 1 92  ? 166.993 189.094 112.857 1.00 54.25  ?  111 THR B OG1   1 
ATOM   6993  C  CG2   . THR B 1 92  ? 167.481 186.737 112.699 1.00 58.19  ?  111 THR B CG2   1 
ATOM   6994  N  N     . ARG B 1 93  ? 170.829 189.291 111.731 1.00 42.84  ?  112 ARG B N     1 
ATOM   6995  C  CA    . ARG B 1 93  ? 171.582 190.320 111.029 1.00 38.96  ?  112 ARG B CA    1 
ATOM   6996  C  C     . ARG B 1 93  ? 171.063 190.419 109.602 1.00 41.41  ?  112 ARG B C     1 
ATOM   6997  O  O     . ARG B 1 93  ? 170.933 189.402 108.910 1.00 59.80  ?  112 ARG B O     1 
ATOM   6998  C  CB    . ARG B 1 93  ? 173.084 190.023 111.037 1.00 48.55  ?  112 ARG B CB    1 
ATOM   6999  C  CG    . ARG B 1 93  ? 173.834 190.690 112.180 1.00 54.09  ?  112 ARG B CG    1 
ATOM   7000  C  CD    . ARG B 1 93  ? 174.018 192.183 111.955 1.00 55.49  ?  112 ARG B CD    1 
ATOM   7001  N  NE    . ARG B 1 93  ? 175.151 192.484 111.089 1.00 50.22  ?  112 ARG B NE    1 
ATOM   7002  C  CZ    . ARG B 1 93  ? 175.138 193.400 110.131 1.00 48.83  ?  112 ARG B CZ    1 
ATOM   7003  N  NH1   . ARG B 1 93  ? 174.060 194.125 109.883 1.00 49.38  1  112 ARG B NH1   1 
ATOM   7004  N  NH2   . ARG B 1 93  ? 176.236 193.597 109.407 1.00 52.16  ?  112 ARG B NH2   1 
ATOM   7005  N  N     . PHE B 1 94  ? 170.773 191.641 109.168 1.00 32.32  ?  113 PHE B N     1 
ATOM   7006  C  CA    . PHE B 1 94  ? 170.130 191.897 107.890 1.00 44.46  ?  113 PHE B CA    1 
ATOM   7007  C  C     . PHE B 1 94  ? 171.109 192.520 106.906 1.00 49.14  ?  113 PHE B C     1 
ATOM   7008  O  O     . PHE B 1 94  ? 171.974 193.318 107.280 1.00 56.30  ?  113 PHE B O     1 
ATOM   7009  C  CB    . PHE B 1 94  ? 168.925 192.829 108.061 1.00 55.65  ?  113 PHE B CB    1 
ATOM   7010  C  CG    . PHE B 1 94  ? 167.696 192.150 108.594 1.00 58.97  ?  113 PHE B CG    1 
ATOM   7011  C  CD1   . PHE B 1 94  ? 167.647 191.703 109.904 1.00 57.78  ?  113 PHE B CD1   1 
ATOM   7012  C  CD2   . PHE B 1 94  ? 166.581 191.978 107.790 1.00 55.89  ?  113 PHE B CD2   1 
ATOM   7013  C  CE1   . PHE B 1 94  ? 166.514 191.084 110.398 1.00 52.63  ?  113 PHE B CE1   1 
ATOM   7014  C  CE2   . PHE B 1 94  ? 165.445 191.363 108.279 1.00 56.76  ?  113 PHE B CE2   1 
ATOM   7015  C  CZ    . PHE B 1 94  ? 165.412 190.913 109.584 1.00 55.35  ?  113 PHE B CZ    1 
ATOM   7016  N  N     . ALA B 1 95  ? 170.963 192.144 105.637 1.00 47.11  ?  114 ALA B N     1 
ATOM   7017  C  CA    . ALA B 1 95  ? 171.635 192.807 104.527 1.00 44.59  ?  114 ALA B CA    1 
ATOM   7018  C  C     . ALA B 1 95  ? 170.561 193.170 103.513 1.00 49.86  ?  114 ALA B C     1 
ATOM   7019  O  O     . ALA B 1 95  ? 169.958 192.282 102.900 1.00 63.20  ?  114 ALA B O     1 
ATOM   7020  C  CB    . ALA B 1 95  ? 172.706 191.912 103.905 1.00 54.34  ?  114 ALA B CB    1 
ATOM   7021  N  N     . LEU B 1 96  ? 170.311 194.463 103.342 1.00 59.91  ?  115 LEU B N     1 
ATOM   7022  C  CA    . LEU B 1 96  ? 169.204 194.936 102.524 1.00 65.76  ?  115 LEU B CA    1 
ATOM   7023  C  C     . LEU B 1 96  ? 169.706 195.403 101.166 1.00 63.10  ?  115 LEU B C     1 
ATOM   7024  O  O     . LEU B 1 96  ? 170.700 196.130 101.073 1.00 65.57  ?  115 LEU B O     1 
ATOM   7025  C  CB    . LEU B 1 96  ? 168.456 196.073 103.220 1.00 73.36  ?  115 LEU B CB    1 
ATOM   7026  C  CG    . LEU B 1 96  ? 167.045 196.346 102.695 1.00 74.15  ?  115 LEU B CG    1 
ATOM   7027  C  CD1   . LEU B 1 96  ? 166.151 195.139 102.911 1.00 69.29  ?  115 LEU B CD1   1 
ATOM   7028  C  CD2   . LEU B 1 96  ? 166.454 197.574 103.362 1.00 72.90  ?  115 LEU B CD2   1 
ATOM   7029  N  N     . SER B 1 97  ? 169.010 194.978 100.114 1.00 74.95  ?  116 SER B N     1 
ATOM   7030  C  CA    . SER B 1 97  ? 169.348 195.347 98.748  1.00 80.30  ?  116 SER B CA    1 
ATOM   7031  C  C     . SER B 1 97  ? 168.091 195.810 98.029  1.00 82.12  ?  116 SER B C     1 
ATOM   7032  O  O     . SER B 1 97  ? 167.013 195.234 98.212  1.00 84.08  ?  116 SER B O     1 
ATOM   7033  C  CB    . SER B 1 97  ? 169.988 194.174 97.998  1.00 79.65  ?  116 SER B CB    1 
ATOM   7034  O  OG    . SER B 1 97  ? 169.029 193.178 97.693  1.00 77.98  ?  116 SER B OG    1 
ATOM   7035  N  N     . LYS B 1 98  ? 168.238 196.851 97.218  1.00 92.56  ?  117 LYS B N     1 
ATOM   7036  C  CA    . LYS B 1 98  ? 167.150 197.396 96.423  1.00 91.83  ?  117 LYS B CA    1 
ATOM   7037  C  C     . LYS B 1 98  ? 167.413 197.140 94.945  1.00 91.10  ?  117 LYS B C     1 
ATOM   7038  O  O     . LYS B 1 98  ? 168.559 197.137 94.491  1.00 96.15  ?  117 LYS B O     1 
ATOM   7039  C  CB    . LYS B 1 98  ? 166.991 198.897 96.675  1.00 97.81  ?  117 LYS B CB    1 
ATOM   7040  C  CG    . LYS B 1 98  ? 165.714 199.497 96.111  1.00 98.01  ?  117 LYS B CG    1 
ATOM   7041  C  CD    . LYS B 1 98  ? 165.783 201.014 96.092  1.00 97.43  ?  117 LYS B CD    1 
ATOM   7042  C  CE    . LYS B 1 98  ? 165.607 201.585 97.488  1.00 96.35  ?  117 LYS B CE    1 
ATOM   7043  N  NZ    . LYS B 1 98  ? 165.152 203.001 97.465  1.00 96.54  1  117 LYS B NZ    1 
ATOM   7044  N  N     . VAL B 1 99  ? 166.337 196.913 94.198  1.00 96.55  ?  118 VAL B N     1 
ATOM   7045  C  CA    . VAL B 1 99  ? 166.410 196.645 92.767  1.00 101.37 ?  118 VAL B CA    1 
ATOM   7046  C  C     . VAL B 1 99  ? 165.566 197.679 92.039  1.00 104.08 ?  118 VAL B C     1 
ATOM   7047  O  O     . VAL B 1 99  ? 164.397 197.886 92.381  1.00 104.33 ?  118 VAL B O     1 
ATOM   7048  C  CB    . VAL B 1 99  ? 165.932 195.221 92.430  1.00 102.33 ?  118 VAL B CB    1 
ATOM   7049  C  CG1   . VAL B 1 99  ? 165.982 194.993 90.930  1.00 103.44 ?  118 VAL B CG1   1 
ATOM   7050  C  CG2   . VAL B 1 99  ? 166.777 194.190 93.161  1.00 102.00 ?  118 VAL B CG2   1 
ATOM   7051  N  N     . SER B 1 100 ? 166.159 198.325 91.038  1.00 114.99 ?  119 SER B N     1 
ATOM   7052  C  CA    . SER B 1 100 ? 165.456 199.260 90.163  1.00 115.32 ?  119 SER B CA    1 
ATOM   7053  C  C     . SER B 1 100 ? 165.507 198.675 88.755  1.00 116.94 ?  119 SER B C     1 
ATOM   7054  O  O     . SER B 1 100 ? 166.389 199.011 87.961  1.00 116.66 ?  119 SER B O     1 
ATOM   7055  C  CB    . SER B 1 100 ? 166.080 200.653 90.223  1.00 113.96 ?  119 SER B CB    1 
ATOM   7056  O  OG    . SER B 1 100 ? 165.435 201.539 89.325  1.00 115.21 ?  119 SER B OG    1 
ATOM   7057  N  N     . ALA B 1 101 ? 164.555 197.796 88.450  1.00 124.33 ?  120 ALA B N     1 
ATOM   7058  C  CA    . ALA B 1 101 ? 164.496 197.133 87.156  1.00 125.56 ?  120 ALA B CA    1 
ATOM   7059  C  C     . ALA B 1 101 ? 163.046 197.029 86.707  1.00 124.95 ?  120 ALA B C     1 
ATOM   7060  O  O     . ALA B 1 101 ? 162.133 196.910 87.529  1.00 123.68 ?  120 ALA B O     1 
ATOM   7061  C  CB    . ALA B 1 101 ? 165.133 195.737 87.205  1.00 121.91 ?  120 ALA B CB    1 
ATOM   7062  N  N     . GLU B 1 102 ? 162.849 197.078 85.387  1.00 129.65 ?  121 GLU B N     1 
ATOM   7063  C  CA    . GLU B 1 102 ? 161.524 196.985 84.772  1.00 129.39 ?  121 GLU B CA    1 
ATOM   7064  C  C     . GLU B 1 102 ? 160.578 198.059 85.299  1.00 129.11 ?  121 GLU B C     1 
ATOM   7065  O  O     . GLU B 1 102 ? 159.363 197.854 85.365  1.00 128.02 ?  121 GLU B O     1 
ATOM   7066  C  CB    . GLU B 1 102 ? 160.913 195.594 84.970  1.00 129.85 ?  121 GLU B CB    1 
ATOM   7067  C  CG    . GLU B 1 102 ? 161.872 194.445 84.706  1.00 130.52 ?  121 GLU B CG    1 
ATOM   7068  C  CD    . GLU B 1 102 ? 161.246 193.090 84.976  1.00 129.58 ?  121 GLU B CD    1 
ATOM   7069  O  OE1   . GLU B 1 102 ? 160.101 193.051 85.472  1.00 128.06 ?  121 GLU B OE1   1 
ATOM   7070  O  OE2   . GLU B 1 102 ? 161.901 192.064 84.696  1.00 129.07 -1 121 GLU B OE2   1 
ATOM   7071  N  N     . GLY B 1 103 ? 161.124 199.214 85.673  1.00 131.45 ?  122 GLY B N     1 
ATOM   7072  C  CA    . GLY B 1 103 ? 160.313 200.262 86.262  1.00 131.59 ?  122 GLY B CA    1 
ATOM   7073  C  C     . GLY B 1 103 ? 159.699 199.898 87.592  1.00 131.13 ?  122 GLY B C     1 
ATOM   7074  O  O     . GLY B 1 103 ? 158.707 200.508 87.998  1.00 129.62 ?  122 GLY B O     1 
ATOM   7075  N  N     . LYS B 1 104 ? 160.264 198.914 88.289  1.00 120.58 ?  123 LYS B N     1 
ATOM   7076  C  CA    . LYS B 1 104 ? 159.727 198.436 89.552  1.00 119.28 ?  123 LYS B CA    1 
ATOM   7077  C  C     . LYS B 1 104 ? 160.825 198.421 90.604  1.00 118.50 ?  123 LYS B C     1 
ATOM   7078  O  O     . LYS B 1 104 ? 162.003 198.223 90.293  1.00 118.15 ?  123 LYS B O     1 
ATOM   7079  C  CB    . LYS B 1 104 ? 159.123 197.031 89.411  1.00 117.28 ?  123 LYS B CB    1 
ATOM   7080  C  CG    . LYS B 1 104 ? 158.053 196.919 88.340  1.00 117.01 ?  123 LYS B CG    1 
ATOM   7081  C  CD    . LYS B 1 104 ? 157.147 195.725 88.588  1.00 117.68 ?  123 LYS B CD    1 
ATOM   7082  C  CE    . LYS B 1 104 ? 156.206 195.499 87.417  1.00 117.63 ?  123 LYS B CE    1 
ATOM   7083  N  NZ    . LYS B 1 104 ? 155.182 194.464 87.721  1.00 115.43 1  123 LYS B NZ    1 
ATOM   7084  N  N     . VAL B 1 105 ? 160.426 198.633 91.854  1.00 105.89 ?  124 VAL B N     1 
ATOM   7085  C  CA    . VAL B 1 105 ? 161.342 198.651 92.988  1.00 105.19 ?  124 VAL B CA    1 
ATOM   7086  C  C     . VAL B 1 105 ? 160.955 197.508 93.916  1.00 107.44 ?  124 VAL B C     1 
ATOM   7087  O  O     . VAL B 1 105 ? 159.872 197.524 94.515  1.00 108.59 ?  124 VAL B O     1 
ATOM   7088  C  CB    . VAL B 1 105 ? 161.317 199.995 93.728  1.00 104.13 ?  124 VAL B CB    1 
ATOM   7089  C  CG1   . VAL B 1 105 ? 162.215 199.942 94.954  1.00 103.79 ?  124 VAL B CG1   1 
ATOM   7090  C  CG2   . VAL B 1 105 ? 161.744 201.120 92.798  1.00 106.05 ?  124 VAL B CG2   1 
ATOM   7091  N  N     . TYR B 1 106 ? 161.835 196.520 94.035  1.00 102.52 ?  125 TYR B N     1 
ATOM   7092  C  CA    . TYR B 1 106 ? 161.679 195.411 94.963  1.00 97.98  ?  125 TYR B CA    1 
ATOM   7093  C  C     . TYR B 1 106 ? 162.594 195.627 96.163  1.00 96.45  ?  125 TYR B C     1 
ATOM   7094  O  O     . TYR B 1 106 ? 163.357 196.595 96.228  1.00 99.69  ?  125 TYR B O     1 
ATOM   7095  C  CB    . TYR B 1 106 ? 161.985 194.077 94.274  1.00 98.12  ?  125 TYR B CB    1 
ATOM   7096  C  CG    . TYR B 1 106 ? 160.889 193.573 93.360  1.00 100.68 ?  125 TYR B CG    1 
ATOM   7097  C  CD1   . TYR B 1 106 ? 160.438 194.335 92.291  1.00 101.78 ?  125 TYR B CD1   1 
ATOM   7098  C  CD2   . TYR B 1 106 ? 160.312 192.327 93.565  1.00 101.93 ?  125 TYR B CD2   1 
ATOM   7099  C  CE1   . TYR B 1 106 ? 159.439 193.874 91.455  1.00 102.54 ?  125 TYR B CE1   1 
ATOM   7100  C  CE2   . TYR B 1 106 ? 159.314 191.856 92.734  1.00 101.78 ?  125 TYR B CE2   1 
ATOM   7101  C  CZ    . TYR B 1 106 ? 158.881 192.634 91.681  1.00 102.92 ?  125 TYR B CZ    1 
ATOM   7102  O  OH    . TYR B 1 106 ? 157.886 192.170 90.851  1.00 101.47 ?  125 TYR B OH    1 
ATOM   7103  N  N     . TYR B 1 107 ? 162.515 194.712 97.125  1.00 89.27  ?  126 TYR B N     1 
ATOM   7104  C  CA    . TYR B 1 107 ? 163.391 194.782 98.292  1.00 90.61  ?  126 TYR B CA    1 
ATOM   7105  C  C     . TYR B 1 107 ? 163.777 193.375 98.712  1.00 92.73  ?  126 TYR B C     1 
ATOM   7106  O  O     . TYR B 1 107 ? 162.901 192.564 99.027  1.00 95.76  ?  126 TYR B O     1 
ATOM   7107  C  CB    . TYR B 1 107 ? 162.715 195.521 99.449  1.00 94.78  ?  126 TYR B CB    1 
ATOM   7108  C  CG    . TYR B 1 107 ? 162.698 197.024 99.295  1.00 95.84  ?  126 TYR B CG    1 
ATOM   7109  C  CD1   . TYR B 1 107 ? 163.836 197.779 99.547  1.00 92.45  ?  126 TYR B CD1   1 
ATOM   7110  C  CD2   . TYR B 1 107 ? 161.545 197.688 98.898  1.00 95.20  ?  126 TYR B CD2   1 
ATOM   7111  C  CE1   . TYR B 1 107 ? 163.826 199.153 99.407  1.00 93.57  ?  126 TYR B CE1   1 
ATOM   7112  C  CE2   . TYR B 1 107 ? 161.526 199.063 98.755  1.00 96.09  ?  126 TYR B CE2   1 
ATOM   7113  C  CZ    . TYR B 1 107 ? 162.669 199.790 99.012  1.00 96.11  ?  126 TYR B CZ    1 
ATOM   7114  O  OH    . TYR B 1 107 ? 162.654 201.159 98.871  1.00 94.95  ?  126 TYR B OH    1 
ATOM   7115  N  N     . LEU B 1 108 ? 165.076 193.086 98.721  1.00 76.42  ?  127 LEU B N     1 
ATOM   7116  C  CA    . LEU B 1 108 ? 165.591 191.809 99.191  1.00 71.07  ?  127 LEU B CA    1 
ATOM   7117  C  C     . LEU B 1 108 ? 166.279 192.011 100.533 1.00 67.24  ?  127 LEU B C     1 
ATOM   7118  O  O     . LEU B 1 108 ? 167.036 192.969 100.713 1.00 67.68  ?  127 LEU B O     1 
ATOM   7119  C  CB    . LEU B 1 108 ? 166.569 191.199 98.182  1.00 71.78  ?  127 LEU B CB    1 
ATOM   7120  C  CG    . LEU B 1 108 ? 167.032 189.765 98.446  1.00 71.61  ?  127 LEU B CG    1 
ATOM   7121  C  CD1   . LEU B 1 108 ? 165.925 188.774 98.128  1.00 72.43  ?  127 LEU B CD1   1 
ATOM   7122  C  CD2   . LEU B 1 108 ? 168.285 189.446 97.644  1.00 72.55  ?  127 LEU B CD2   1 
ATOM   7123  N  N     . ALA B 1 109 ? 166.009 191.114 101.478 1.00 56.99  ?  128 ALA B N     1 
ATOM   7124  C  CA    . ALA B 1 109 ? 166.560 191.215 102.830 1.00 59.14  ?  128 ALA B CA    1 
ATOM   7125  C  C     . ALA B 1 109 ? 167.239 189.895 103.167 1.00 55.50  ?  128 ALA B C     1 
ATOM   7126  O  O     . ALA B 1 109 ? 166.621 189.002 103.752 1.00 61.05  ?  128 ALA B O     1 
ATOM   7127  C  CB    . ALA B 1 109 ? 165.473 191.565 103.842 1.00 61.25  ?  128 ALA B CB    1 
ATOM   7128  N  N     . LEU B 1 110 ? 168.513 189.772 102.804 1.00 46.26  ?  129 LEU B N     1 
ATOM   7129  C  CA    . LEU B 1 110 ? 169.270 188.575 103.150 1.00 47.25  ?  129 LEU B CA    1 
ATOM   7130  C  C     . LEU B 1 110 ? 169.489 188.551 104.656 1.00 45.35  ?  129 LEU B C     1 
ATOM   7131  O  O     . LEU B 1 110 ? 170.237 189.369 105.200 1.00 51.68  ?  129 LEU B O     1 
ATOM   7132  C  CB    . LEU B 1 110 ? 170.597 188.538 102.399 1.00 45.68  ?  129 LEU B CB    1 
ATOM   7133  C  CG    . LEU B 1 110 ? 170.495 188.098 100.937 1.00 47.65  ?  129 LEU B CG    1 
ATOM   7134  C  CD1   . LEU B 1 110 ? 171.855 188.117 100.269 1.00 48.55  ?  129 LEU B CD1   1 
ATOM   7135  C  CD2   . LEU B 1 110 ? 169.861 186.723 100.832 1.00 52.27  ?  129 LEU B CD2   1 
ATOM   7136  N  N     . VAL B 1 111 ? 168.820 187.633 105.328 1.00 46.49  ?  130 VAL B N     1 
ATOM   7137  C  CA    . VAL B 1 111 ? 168.901 187.501 106.774 1.00 41.65  ?  130 VAL B CA    1 
ATOM   7138  C  C     . VAL B 1 111 ? 169.893 186.402 107.110 1.00 37.27  ?  130 VAL B C     1 
ATOM   7139  O  O     . VAL B 1 111 ? 170.049 185.418 106.374 1.00 52.52  ?  130 VAL B O     1 
ATOM   7140  C  CB    . VAL B 1 111 ? 167.516 187.208 107.391 1.00 48.84  ?  130 VAL B CB    1 
ATOM   7141  C  CG1   . VAL B 1 111 ? 166.558 188.342 107.096 1.00 51.21  ?  130 VAL B CG1   1 
ATOM   7142  C  CG2   . VAL B 1 111 ? 166.961 185.894 106.867 1.00 49.45  ?  130 VAL B CG2   1 
ATOM   7143  N  N     . ARG B 1 112 ? 170.587 186.578 108.225 1.00 28.25  ?  131 ARG B N     1 
ATOM   7144  C  CA    . ARG B 1 112 ? 171.422 185.526 108.775 1.00 39.28  ?  131 ARG B CA    1 
ATOM   7145  C  C     . ARG B 1 112 ? 171.170 185.439 110.270 1.00 41.27  ?  131 ARG B C     1 
ATOM   7146  O  O     . ARG B 1 112 ? 170.943 186.457 110.936 1.00 50.75  ?  131 ARG B O     1 
ATOM   7147  C  CB    . ARG B 1 112 ? 172.909 185.764 108.473 1.00 50.48  ?  131 ARG B CB    1 
ATOM   7148  C  CG    . ARG B 1 112 ? 173.521 187.008 109.087 1.00 44.94  ?  131 ARG B CG    1 
ATOM   7149  C  CD    . ARG B 1 112 ? 175.003 187.078 108.741 1.00 39.56  ?  131 ARG B CD    1 
ATOM   7150  N  NE    . ARG B 1 112 ? 175.668 188.243 109.311 1.00 44.42  ?  131 ARG B NE    1 
ATOM   7151  C  CZ    . ARG B 1 112 ? 176.168 188.292 110.537 1.00 47.68  ?  131 ARG B CZ    1 
ATOM   7152  N  NH1   . ARG B 1 112 ? 176.088 187.258 111.356 1.00 48.22  1  131 ARG B NH1   1 
ATOM   7153  N  NH2   . ARG B 1 112 ? 176.768 189.405 110.950 1.00 43.17  ?  131 ARG B NH2   1 
ATOM   7154  N  N     . ASP B 1 113 ? 171.189 184.213 110.786 1.00 41.93  ?  132 ASP B N     1 
ATOM   7155  C  CA    . ASP B 1 113 ? 170.877 183.995 112.189 1.00 41.93  ?  132 ASP B CA    1 
ATOM   7156  C  C     . ASP B 1 113 ? 172.002 184.550 113.043 1.00 41.57  ?  132 ASP B C     1 
ATOM   7157  O  O     . ASP B 1 113 ? 173.001 183.868 113.294 1.00 51.24  ?  132 ASP B O     1 
ATOM   7158  C  CB    . ASP B 1 113 ? 170.661 182.509 112.482 1.00 51.32  ?  132 ASP B CB    1 
ATOM   7159  C  CG    . ASP B 1 113 ? 170.132 182.265 113.882 1.00 55.52  ?  132 ASP B CG    1 
ATOM   7160  O  OD1   . ASP B 1 113 ? 169.233 183.017 114.316 1.00 52.83  ?  132 ASP B OD1   1 
ATOM   7161  O  OD2   . ASP B 1 113 ? 170.614 181.326 114.549 1.00 55.26  -1 132 ASP B OD2   1 
ATOM   7162  N  N     . ALA B 1 114 ? 171.848 185.791 113.490 1.00 37.01  ?  133 ALA B N     1 
ATOM   7163  C  CA    . ALA B 1 114 ? 172.829 186.422 114.354 1.00 37.64  ?  133 ALA B CA    1 
ATOM   7164  C  C     . ALA B 1 114 ? 172.691 185.985 115.795 1.00 37.85  ?  133 ALA B C     1 
ATOM   7165  O  O     . ALA B 1 114 ? 173.211 186.662 116.683 1.00 42.00  ?  133 ALA B O     1 
ATOM   7166  C  CB    . ALA B 1 114 ? 172.724 187.945 114.257 1.00 47.35  ?  133 ALA B CB    1 
ATOM   7167  N  N     . SER B 1 115 ? 171.984 184.882 116.048 1.00 46.96  ?  134 SER B N     1 
ATOM   7168  C  CA    . SER B 1 115 ? 171.894 184.354 117.403 1.00 46.31  ?  134 SER B CA    1 
ATOM   7169  C  C     . SER B 1 115 ? 173.278 184.029 117.949 1.00 46.59  ?  134 SER B C     1 
ATOM   7170  O  O     . SER B 1 115 ? 173.641 184.466 119.045 1.00 48.39  ?  134 SER B O     1 
ATOM   7171  C  CB    . SER B 1 115 ? 170.999 183.115 117.426 1.00 48.26  ?  134 SER B CB    1 
ATOM   7172  O  OG    . SER B 1 115 ? 171.591 182.041 116.716 1.00 50.28  ?  134 SER B OG    1 
ATOM   7173  N  N     . VAL B 1 116 ? 174.079 183.288 117.180 1.00 47.49  ?  135 VAL B N     1 
ATOM   7174  C  CA    . VAL B 1 116 ? 175.406 182.900 117.651 1.00 44.03  ?  135 VAL B CA    1 
ATOM   7175  C  C     . VAL B 1 116 ? 176.339 184.107 117.710 1.00 44.80  ?  135 VAL B C     1 
ATOM   7176  O  O     . VAL B 1 116 ? 177.134 184.242 118.646 1.00 47.91  ?  135 VAL B O     1 
ATOM   7177  C  CB    . VAL B 1 116 ? 175.979 181.768 116.775 1.00 46.40  ?  135 VAL B CB    1 
ATOM   7178  C  CG1   . VAL B 1 116 ? 176.088 182.198 115.320 1.00 41.39  ?  135 VAL B CG1   1 
ATOM   7179  C  CG2   . VAL B 1 116 ? 177.332 181.322 117.305 1.00 46.48  ?  135 VAL B CG2   1 
ATOM   7180  N  N     . GLU B 1 117 ? 176.249 185.012 116.731 1.00 47.83  ?  136 GLU B N     1 
ATOM   7181  C  CA    . GLU B 1 117 ? 177.118 186.187 116.729 1.00 52.13  ?  136 GLU B CA    1 
ATOM   7182  C  C     . GLU B 1 117 ? 176.818 187.098 117.915 1.00 48.55  ?  136 GLU B C     1 
ATOM   7183  O  O     . GLU B 1 117 ? 177.734 187.591 118.584 1.00 46.27  ?  136 GLU B O     1 
ATOM   7184  C  CB    . GLU B 1 117 ? 176.971 186.947 115.411 1.00 50.35  ?  136 GLU B CB    1 
ATOM   7185  C  CG    . GLU B 1 117 ? 177.846 186.410 114.291 1.00 51.95  ?  136 GLU B CG    1 
ATOM   7186  C  CD    . GLU B 1 117 ? 177.184 185.286 113.520 1.00 56.44  ?  136 GLU B CD    1 
ATOM   7187  O  OE1   . GLU B 1 117 ? 177.857 184.676 112.662 1.00 54.36  ?  136 GLU B OE1   1 
ATOM   7188  O  OE2   . GLU B 1 117 ? 175.989 185.020 113.765 1.00 58.58  -1 136 GLU B OE2   1 
ATOM   7189  N  N     . MET B 1 118 ? 175.538 187.327 118.199 1.00 49.13  ?  137 MET B N     1 
ATOM   7190  C  CA    . MET B 1 118 ? 175.162 188.160 119.330 1.00 41.42  ?  137 MET B CA    1 
ATOM   7191  C  C     . MET B 1 118 ? 175.383 187.462 120.662 1.00 41.22  ?  137 MET B C     1 
ATOM   7192  O  O     . MET B 1 118 ? 175.667 188.136 121.655 1.00 52.28  ?  137 MET B O     1 
ATOM   7193  C  CB    . MET B 1 118 ? 173.704 188.603 119.197 1.00 44.32  ?  137 MET B CB    1 
ATOM   7194  C  CG    . MET B 1 118 ? 173.528 189.704 118.172 1.00 49.22  ?  137 MET B CG    1 
ATOM   7195  S  SD    . MET B 1 118 ? 174.572 191.124 118.551 1.00 68.04  ?  137 MET B SD    1 
ATOM   7196  C  CE    . MET B 1 118 ? 175.046 191.640 116.904 1.00 51.42  ?  137 MET B CE    1 
ATOM   7197  N  N     . ALA B 1 119 ? 175.281 186.131 120.707 1.00 36.08  ?  138 ALA B N     1 
ATOM   7198  C  CA    . ALA B 1 119 ? 175.702 185.403 121.896 1.00 38.76  ?  138 ALA B CA    1 
ATOM   7199  C  C     . ALA B 1 119 ? 177.194 185.575 122.131 1.00 46.75  ?  138 ALA B C     1 
ATOM   7200  O  O     . ALA B 1 119 ? 177.636 185.721 123.274 1.00 53.85  ?  138 ALA B O     1 
ATOM   7201  C  CB    . ALA B 1 119 ? 175.342 183.923 121.765 1.00 43.93  ?  138 ALA B CB    1 
ATOM   7202  N  N     . GLN B 1 120 ? 177.985 185.567 121.056 1.00 41.07  ?  139 GLN B N     1 
ATOM   7203  C  CA    . GLN B 1 120 ? 179.414 185.832 121.179 1.00 41.32  ?  139 GLN B CA    1 
ATOM   7204  C  C     . GLN B 1 120 ? 179.671 187.248 121.682 1.00 45.83  ?  139 GLN B C     1 
ATOM   7205  O  O     . GLN B 1 120 ? 180.547 187.465 122.525 1.00 45.66  ?  139 GLN B O     1 
ATOM   7206  C  CB    . GLN B 1 120 ? 180.105 185.609 119.835 1.00 41.79  ?  139 GLN B CB    1 
ATOM   7207  C  CG    . GLN B 1 120 ? 181.621 185.564 119.910 1.00 44.01  ?  139 GLN B CG    1 
ATOM   7208  C  CD    . GLN B 1 120 ? 182.121 184.817 121.129 1.00 41.63  ?  139 GLN B CD    1 
ATOM   7209  O  OE1   . GLN B 1 120 ? 182.465 185.421 122.144 1.00 44.61  ?  139 GLN B OE1   1 
ATOM   7210  N  NE2   . GLN B 1 120 ? 182.169 183.495 121.033 1.00 39.17  ?  139 GLN B NE2   1 
ATOM   7211  N  N     . LYS B 1 121 ? 178.923 188.226 121.169 1.00 46.09  ?  140 LYS B N     1 
ATOM   7212  C  CA    . LYS B 1 121 ? 179.093 189.604 121.628 1.00 39.50  ?  140 LYS B CA    1 
ATOM   7213  C  C     . LYS B 1 121 ? 178.714 189.756 123.098 1.00 38.36  ?  140 LYS B C     1 
ATOM   7214  O  O     . LYS B 1 121 ? 179.416 190.432 123.861 1.00 50.32  ?  140 LYS B O     1 
ATOM   7215  C  CB    . LYS B 1 121 ? 178.268 190.556 120.762 1.00 39.98  ?  140 LYS B CB    1 
ATOM   7216  C  CG    . LYS B 1 121 ? 178.466 192.026 121.107 1.00 40.83  ?  140 LYS B CG    1 
ATOM   7217  C  CD    . LYS B 1 121 ? 177.674 192.930 120.178 1.00 42.75  ?  140 LYS B CD    1 
ATOM   7218  C  CE    . LYS B 1 121 ? 178.107 192.753 118.733 1.00 42.66  ?  140 LYS B CE    1 
ATOM   7219  N  NZ    . LYS B 1 121 ? 179.590 192.727 118.595 1.00 44.49  1  140 LYS B NZ    1 
ATOM   7220  N  N     . GLU B 1 122 ? 177.606 189.139 123.512 1.00 34.91  ?  141 GLU B N     1 
ATOM   7221  C  CA    . GLU B 1 122 ? 177.199 189.190 124.911 1.00 33.32  ?  141 GLU B CA    1 
ATOM   7222  C  C     . GLU B 1 122 ? 178.208 188.477 125.801 1.00 39.35  ?  141 GLU B C     1 
ATOM   7223  O  O     . GLU B 1 122 ? 178.502 188.939 126.909 1.00 49.51  ?  141 GLU B O     1 
ATOM   7224  C  CB    . GLU B 1 122 ? 175.810 188.576 125.073 1.00 37.55  ?  141 GLU B CB    1 
ATOM   7225  C  CG    . GLU B 1 122 ? 174.670 189.562 124.880 1.00 40.98  ?  141 GLU B CG    1 
ATOM   7226  C  CD    . GLU B 1 122 ? 174.636 190.630 125.952 1.00 51.12  ?  141 GLU B CD    1 
ATOM   7227  O  OE1   . GLU B 1 122 ? 174.675 190.274 127.148 1.00 47.96  ?  141 GLU B OE1   1 
ATOM   7228  O  OE2   . GLU B 1 122 ? 174.572 191.826 125.597 1.00 55.19  -1 141 GLU B OE2   1 
ATOM   7229  N  N     . GLN B 1 123 ? 178.747 187.350 125.330 1.00 37.48  ?  142 GLN B N     1 
ATOM   7230  C  CA    . GLN B 1 123 ? 179.788 186.648 126.068 1.00 41.06  ?  142 GLN B CA    1 
ATOM   7231  C  C     . GLN B 1 123 ? 181.031 187.513 126.210 1.00 47.17  ?  142 GLN B C     1 
ATOM   7232  O  O     . GLN B 1 123 ? 181.662 187.534 127.270 1.00 50.90  ?  142 GLN B O     1 
ATOM   7233  C  CB    . GLN B 1 123 ? 180.123 185.332 125.365 1.00 39.34  ?  142 GLN B CB    1 
ATOM   7234  C  CG    . GLN B 1 123 ? 181.443 184.711 125.785 1.00 44.56  ?  142 GLN B CG    1 
ATOM   7235  C  CD    . GLN B 1 123 ? 181.487 183.216 125.538 1.00 47.92  ?  142 GLN B CD    1 
ATOM   7236  O  OE1   . GLN B 1 123 ? 180.850 182.709 124.615 1.00 52.02  ?  142 GLN B OE1   1 
ATOM   7237  N  NE2   . GLN B 1 123 ? 182.239 182.501 126.366 1.00 41.54  ?  142 GLN B NE2   1 
ATOM   7238  N  N     . THR B 1 124 ? 181.397 188.235 125.148 1.00 42.57  ?  143 THR B N     1 
ATOM   7239  C  CA    . THR B 1 124 ? 182.538 189.141 125.221 1.00 40.23  ?  143 THR B CA    1 
ATOM   7240  C  C     . THR B 1 124 ? 182.290 190.262 126.221 1.00 40.59  ?  143 THR B C     1 
ATOM   7241  O  O     . THR B 1 124 ? 183.187 190.627 126.986 1.00 46.40  ?  143 THR B O     1 
ATOM   7242  C  CB    . THR B 1 124 ? 182.842 189.718 123.838 1.00 44.83  ?  143 THR B CB    1 
ATOM   7243  O  OG1   . THR B 1 124 ? 182.958 188.651 122.889 1.00 51.38  ?  143 THR B OG1   1 
ATOM   7244  C  CG2   . THR B 1 124 ? 184.142 190.506 123.864 1.00 45.31  ?  143 THR B CG2   1 
ATOM   7245  N  N     . ARG B 1 125 ? 181.078 190.821 126.232 1.00 36.50  ?  144 ARG B N     1 
ATOM   7246  C  CA    . ARG B 1 125 ? 180.756 191.873 127.194 1.00 27.70  ?  144 ARG B CA    1 
ATOM   7247  C  C     . ARG B 1 125 ? 180.829 191.347 128.624 1.00 24.48  ?  144 ARG B C     1 
ATOM   7248  O  O     . ARG B 1 125 ? 181.417 191.985 129.510 1.00 43.55  ?  144 ARG B O     1 
ATOM   7249  C  CB    . ARG B 1 125 ? 179.370 192.446 126.894 1.00 25.78  ?  144 ARG B CB    1 
ATOM   7250  C  CG    . ARG B 1 125 ? 178.829 193.394 127.956 1.00 34.07  ?  144 ARG B CG    1 
ATOM   7251  C  CD    . ARG B 1 125 ? 177.430 193.887 127.600 1.00 35.55  ?  144 ARG B CD    1 
ATOM   7252  N  NE    . ARG B 1 125 ? 176.400 192.878 127.823 1.00 37.11  ?  144 ARG B NE    1 
ATOM   7253  C  CZ    . ARG B 1 125 ? 175.901 192.566 129.011 1.00 34.61  ?  144 ARG B CZ    1 
ATOM   7254  N  NH1   . ARG B 1 125 ? 176.309 193.172 130.114 1.00 38.89  1  144 ARG B NH1   1 
ATOM   7255  N  NH2   . ARG B 1 125 ? 174.964 191.626 129.094 1.00 28.17  ?  144 ARG B NH2   1 
ATOM   7256  N  N     . GLN B 1 126 ? 180.247 190.169 128.862 1.00 19.59  ?  145 GLN B N     1 
ATOM   7257  C  CA    . GLN B 1 126 ? 180.290 189.564 130.189 1.00 27.98  ?  145 GLN B CA    1 
ATOM   7258  C  C     . GLN B 1 126 ? 181.720 189.254 130.609 1.00 32.61  ?  145 GLN B C     1 
ATOM   7259  O  O     . GLN B 1 126 ? 182.087 189.444 131.773 1.00 37.81  ?  145 GLN B O     1 
ATOM   7260  C  CB    . GLN B 1 126 ? 179.438 188.295 130.211 1.00 28.28  ?  145 GLN B CB    1 
ATOM   7261  C  CG    . GLN B 1 126 ? 177.955 188.539 129.993 1.00 28.88  ?  145 GLN B CG    1 
ATOM   7262  C  CD    . GLN B 1 126 ? 177.205 187.269 129.646 1.00 24.73  ?  145 GLN B CD    1 
ATOM   7263  O  OE1   . GLN B 1 126 ? 177.796 186.292 129.186 1.00 23.19  ?  145 GLN B OE1   1 
ATOM   7264  N  NE2   . GLN B 1 126 ? 175.896 187.281 129.854 1.00 29.90  ?  145 GLN B NE2   1 
ATOM   7265  N  N     . LEU B 1 127 ? 182.546 188.782 129.672 1.00 31.28  ?  146 LEU B N     1 
ATOM   7266  C  CA    . LEU B 1 127 ? 183.939 188.488 129.991 1.00 37.22  ?  146 LEU B CA    1 
ATOM   7267  C  C     . LEU B 1 127 ? 184.723 189.763 130.270 1.00 42.52  ?  146 LEU B C     1 
ATOM   7268  O  O     . LEU B 1 127 ? 185.616 189.769 131.120 1.00 41.73  ?  146 LEU B O     1 
ATOM   7269  C  CB    . LEU B 1 127 ? 184.586 187.695 128.856 1.00 34.56  ?  146 LEU B CB    1 
ATOM   7270  C  CG    . LEU B 1 127 ? 184.437 186.176 128.955 1.00 29.43  ?  146 LEU B CG    1 
ATOM   7271  C  CD1   . LEU B 1 127 ? 184.905 185.502 127.678 1.00 38.24  ?  146 LEU B CD1   1 
ATOM   7272  C  CD2   . LEU B 1 127 ? 185.204 185.650 130.156 1.00 30.81  ?  146 LEU B CD2   1 
ATOM   7273  N  N     . ILE B 1 128 ? 184.411 190.849 129.559 1.00 38.07  ?  147 ILE B N     1 
ATOM   7274  C  CA    . ILE B 1 128 ? 185.047 192.131 129.846 1.00 27.29  ?  147 ILE B CA    1 
ATOM   7275  C  C     . ILE B 1 128 ? 184.701 192.585 131.257 1.00 25.47  ?  147 ILE B C     1 
ATOM   7276  O  O     . ILE B 1 128 ? 185.570 193.039 132.011 1.00 36.29  ?  147 ILE B O     1 
ATOM   7277  C  CB    . ILE B 1 128 ? 184.639 193.181 128.797 1.00 19.77  ?  147 ILE B CB    1 
ATOM   7278  C  CG1   . ILE B 1 128 ? 185.327 192.902 127.461 1.00 27.21  ?  147 ILE B CG1   1 
ATOM   7279  C  CG2   . ILE B 1 128 ? 184.985 194.580 129.278 1.00 26.79  ?  147 ILE B CG2   1 
ATOM   7280  C  CD1   . ILE B 1 128 ? 185.011 193.919 126.390 1.00 34.16  ?  147 ILE B CD1   1 
ATOM   7281  N  N     . ILE B 1 129 ? 183.428 192.458 131.639 1.00 22.08  ?  148 ILE B N     1 
ATOM   7282  C  CA    . ILE B 1 129 ? 183.031 192.814 133.000 1.00 30.43  ?  148 ILE B CA    1 
ATOM   7283  C  C     . ILE B 1 129 ? 183.743 191.926 134.015 1.00 34.06  ?  148 ILE B C     1 
ATOM   7284  O  O     . ILE B 1 129 ? 184.205 192.399 135.061 1.00 46.36  ?  148 ILE B O     1 
ATOM   7285  C  CB    . ILE B 1 129 ? 181.501 192.740 133.156 1.00 33.47  ?  148 ILE B CB    1 
ATOM   7286  C  CG1   . ILE B 1 129 ? 180.807 193.577 132.083 1.00 35.52  ?  148 ILE B CG1   1 
ATOM   7287  C  CG2   . ILE B 1 129 ? 181.092 193.218 134.527 1.00 33.08  ?  148 ILE B CG2   1 
ATOM   7288  C  CD1   . ILE B 1 129 ? 179.361 193.197 131.860 1.00 30.44  ?  148 ILE B CD1   1 
ATOM   7289  N  N     . ALA B 1 130 ? 183.844 190.628 133.724 1.00 24.32  ?  149 ALA B N     1 
ATOM   7290  C  CA    . ALA B 1 130 ? 184.509 189.704 134.638 1.00 24.44  ?  149 ALA B CA    1 
ATOM   7291  C  C     . ALA B 1 130 ? 185.986 190.045 134.805 1.00 38.56  ?  149 ALA B C     1 
ATOM   7292  O  O     . ALA B 1 130 ? 186.522 189.988 135.917 1.00 47.91  ?  149 ALA B O     1 
ATOM   7293  C  CB    . ALA B 1 130 ? 184.345 188.269 134.136 1.00 31.04  ?  149 ALA B CB    1 
ATOM   7294  N  N     . VAL B 1 131 ? 186.662 190.385 133.707 1.00 41.70  ?  150 VAL B N     1 
ATOM   7295  C  CA    . VAL B 1 131 ? 188.075 190.745 133.774 1.00 40.46  ?  150 VAL B CA    1 
ATOM   7296  C  C     . VAL B 1 131 ? 188.257 192.063 134.515 1.00 38.02  ?  150 VAL B C     1 
ATOM   7297  O  O     . VAL B 1 131 ? 189.222 192.238 135.269 1.00 42.81  ?  150 VAL B O     1 
ATOM   7298  C  CB    . VAL B 1 131 ? 188.681 190.788 132.359 1.00 35.96  ?  150 VAL B CB    1 
ATOM   7299  C  CG1   . VAL B 1 131 ? 190.107 191.301 132.400 1.00 37.91  ?  150 VAL B CG1   1 
ATOM   7300  C  CG2   . VAL B 1 131 ? 188.658 189.402 131.744 1.00 35.69  ?  150 VAL B CG2   1 
ATOM   7301  N  N     . ASP B 1 132 ? 187.336 193.011 134.319 1.00 29.58  ?  151 ASP B N     1 
ATOM   7302  C  CA    . ASP B 1 132 ? 187.381 194.239 135.102 1.00 29.07  ?  151 ASP B CA    1 
ATOM   7303  C  C     . ASP B 1 132 ? 187.186 193.952 136.583 1.00 28.24  ?  151 ASP B C     1 
ATOM   7304  O  O     . ASP B 1 132 ? 187.770 194.635 137.432 1.00 42.04  ?  151 ASP B O     1 
ATOM   7305  C  CB    . ASP B 1 132 ? 186.321 195.221 134.604 1.00 35.35  ?  151 ASP B CB    1 
ATOM   7306  C  CG    . ASP B 1 132 ? 186.693 195.859 133.280 1.00 41.97  ?  151 ASP B CG    1 
ATOM   7307  O  OD1   . ASP B 1 132 ? 187.893 195.872 132.936 1.00 36.30  ?  151 ASP B OD1   1 
ATOM   7308  O  OD2   . ASP B 1 132 ? 185.782 196.355 132.584 1.00 46.10  -1 151 ASP B OD2   1 
ATOM   7309  N  N     . HIS B 1 133 ? 186.374 192.954 136.911 1.00 16.08  ?  152 HIS B N     1 
ATOM   7310  C  CA    . HIS B 1 133 ? 186.214 192.498 138.291 1.00 22.23  ?  152 HIS B CA    1 
ATOM   7311  C  C     . HIS B 1 133 ? 187.099 191.280 138.557 1.00 29.56  ?  152 HIS B C     1 
ATOM   7312  O  O     . HIS B 1 133 ? 186.628 190.179 138.844 1.00 40.48  ?  152 HIS B O     1 
ATOM   7313  C  CB    . HIS B 1 133 ? 184.746 192.194 138.581 1.00 30.83  ?  152 HIS B CB    1 
ATOM   7314  C  CG    . HIS B 1 133 ? 183.827 193.353 138.349 1.00 35.02  ?  152 HIS B CG    1 
ATOM   7315  N  ND1   . HIS B 1 133 ? 183.565 193.857 137.093 1.00 38.94  ?  152 HIS B ND1   1 
ATOM   7316  C  CD2   . HIS B 1 133 ? 183.110 194.109 139.214 1.00 30.33  ?  152 HIS B CD2   1 
ATOM   7317  C  CE1   . HIS B 1 133 ? 182.725 194.872 137.194 1.00 26.14  ?  152 HIS B CE1   1 
ATOM   7318  N  NE2   . HIS B 1 133 ? 182.433 195.045 138.470 1.00 26.42  ?  152 HIS B NE2   1 
ATOM   7319  N  N     . LEU B 1 134 ? 188.413 191.495 138.451 1.00 34.48  ?  153 LEU B N     1 
ATOM   7320  C  CA    . LEU B 1 134 ? 189.398 190.458 138.725 1.00 36.71  ?  153 LEU B CA    1 
ATOM   7321  C  C     . LEU B 1 134 ? 190.369 190.823 139.839 1.00 35.59  ?  153 LEU B C     1 
ATOM   7322  O  O     . LEU B 1 134 ? 191.076 189.936 140.330 1.00 42.17  ?  153 LEU B O     1 
ATOM   7323  C  CB    . LEU B 1 134 ? 190.196 190.118 137.455 1.00 31.41  ?  153 LEU B CB    1 
ATOM   7324  C  CG    . LEU B 1 134 ? 189.687 188.933 136.629 1.00 28.23  ?  153 LEU B CG    1 
ATOM   7325  C  CD1   . LEU B 1 134 ? 190.580 188.681 135.423 1.00 33.04  ?  153 LEU B CD1   1 
ATOM   7326  C  CD2   . LEU B 1 134 ? 189.578 187.684 137.488 1.00 32.33  ?  153 LEU B CD2   1 
ATOM   7327  N  N     . ASP B 1 135 ? 190.430 192.094 140.241 1.00 37.13  ?  154 ASP B N     1 
ATOM   7328  C  CA    . ASP B 1 135 ? 191.208 192.560 141.388 1.00 45.45  ?  154 ASP B CA    1 
ATOM   7329  C  C     . ASP B 1 135 ? 192.707 192.343 141.217 1.00 48.27  ?  154 ASP B C     1 
ATOM   7330  O  O     . ASP B 1 135 ? 193.429 192.196 142.210 1.00 53.66  ?  154 ASP B O     1 
ATOM   7331  C  CB    . ASP B 1 135 ? 190.732 191.900 142.687 1.00 49.42  ?  154 ASP B CB    1 
ATOM   7332  C  CG    . ASP B 1 135 ? 189.585 192.646 143.333 1.00 55.62  ?  154 ASP B CG    1 
ATOM   7333  O  OD1   . ASP B 1 135 ? 189.216 193.724 142.821 1.00 57.70  ?  154 ASP B OD1   1 
ATOM   7334  O  OD2   . ASP B 1 135 ? 189.053 192.154 144.350 1.00 48.21  -1 154 ASP B OD2   1 
ATOM   7335  N  N     . ARG B 1 136 ? 193.200 192.329 139.975 1.00 50.82  ?  155 ARG B N     1 
ATOM   7336  C  CA    . ARG B 1 136 ? 194.632 192.218 139.738 1.00 47.85  ?  155 ARG B CA    1 
ATOM   7337  C  C     . ARG B 1 136 ? 194.915 192.633 138.306 1.00 44.46  ?  155 ARG B C     1 
ATOM   7338  O  O     . ARG B 1 136 ? 194.224 192.158 137.394 1.00 55.41  ?  155 ARG B O     1 
ATOM   7339  C  CB    . ARG B 1 136 ? 195.135 190.793 139.997 1.00 40.41  ?  155 ARG B CB    1 
ATOM   7340  C  CG    . ARG B 1 136 ? 196.643 190.636 139.894 1.00 42.70  ?  155 ARG B CG    1 
ATOM   7341  C  CD    . ARG B 1 136 ? 197.077 189.222 140.253 1.00 50.24  ?  155 ARG B CD    1 
ATOM   7342  N  NE    . ARG B 1 136 ? 198.510 189.021 140.071 1.00 55.69  ?  155 ARG B NE    1 
ATOM   7343  C  CZ    . ARG B 1 136 ? 199.423 189.273 140.999 1.00 55.13  ?  155 ARG B CZ    1 
ATOM   7344  N  NH1   . ARG B 1 136 ? 199.088 189.741 142.190 1.00 49.51  1  155 ARG B NH1   1 
ATOM   7345  N  NH2   . ARG B 1 136 ? 200.706 189.055 140.722 1.00 51.70  ?  155 ARG B NH2   1 
ATOM   7346  N  N     . PRO B 1 137 ? 195.892 193.509 138.066 1.00 20.30  ?  156 PRO B N     1 
ATOM   7347  C  CA    . PRO B 1 137 ? 196.168 193.968 136.694 1.00 31.65  ?  156 PRO B CA    1 
ATOM   7348  C  C     . PRO B 1 137 ? 196.700 192.833 135.832 1.00 41.15  ?  156 PRO B C     1 
ATOM   7349  O  O     . PRO B 1 137 ? 197.670 192.163 136.192 1.00 48.54  ?  156 PRO B O     1 
ATOM   7350  C  CB    . PRO B 1 137 ? 197.217 195.071 136.891 1.00 24.37  ?  156 PRO B CB    1 
ATOM   7351  C  CG    . PRO B 1 137 ? 197.133 195.436 138.335 1.00 28.31  ?  156 PRO B CG    1 
ATOM   7352  C  CD    . PRO B 1 137 ? 196.755 194.181 139.048 1.00 28.37  ?  156 PRO B CD    1 
ATOM   7353  N  N     . VAL B 1 138 ? 196.061 192.628 134.683 1.00 33.20  ?  157 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 138 ? 196.409 191.558 133.757 1.00 19.10  ?  157 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 138 ? 196.546 192.154 132.364 1.00 32.87  ?  157 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 138 ? 195.670 192.900 131.914 1.00 46.30  ?  157 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 138 ? 195.353 190.435 133.767 1.00 24.99  ?  157 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 138 ? 195.429 189.608 132.493 1.00 33.01  ?  157 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 138 ? 195.530 189.554 134.992 1.00 36.76  ?  157 VAL B CG2   1 
ATOM   7360  N  N     . ILE B 1 139 ? 197.642 191.825 131.682 1.00 42.38  ?  158 ILE B N     1 
ATOM   7361  C  CA    . ILE B 1 139 ? 197.871 192.247 130.308 1.00 39.90  ?  158 ILE B CA    1 
ATOM   7362  C  C     . ILE B 1 139 ? 198.097 190.998 129.465 1.00 33.63  ?  158 ILE B C     1 
ATOM   7363  O  O     . ILE B 1 139 ? 198.626 189.988 129.943 1.00 44.69  ?  158 ILE B O     1 
ATOM   7364  C  CB    . ILE B 1 139 ? 199.066 193.223 130.196 1.00 41.83  ?  158 ILE B CB    1 
ATOM   7365  C  CG1   . ILE B 1 139 ? 199.002 194.031 128.900 1.00 45.62  ?  158 ILE B CG1   1 
ATOM   7366  C  CG2   . ILE B 1 139 ? 200.386 192.484 130.267 1.00 45.12  ?  158 ILE B CG2   1 
ATOM   7367  C  CD1   . ILE B 1 139 ? 197.950 195.109 128.910 1.00 47.65  ?  158 ILE B CD1   1 
ATOM   7368  N  N     . VAL B 1 140 ? 197.674 191.065 128.206 1.00 26.18  ?  159 VAL B N     1 
ATOM   7369  C  CA    . VAL B 1 140 ? 197.792 189.955 127.269 1.00 36.21  ?  159 VAL B CA    1 
ATOM   7370  C  C     . VAL B 1 140 ? 198.695 190.394 126.125 1.00 52.13  ?  159 VAL B C     1 
ATOM   7371  O  O     . VAL B 1 140 ? 198.472 191.449 125.520 1.00 63.16  ?  159 VAL B O     1 
ATOM   7372  C  CB    . VAL B 1 140 ? 196.418 189.500 126.744 1.00 33.87  ?  159 VAL B CB    1 
ATOM   7373  C  CG1   . VAL B 1 140 ? 196.581 188.425 125.683 1.00 39.63  ?  159 VAL B CG1   1 
ATOM   7374  C  CG2   . VAL B 1 140 ? 195.556 188.993 127.885 1.00 41.16  ?  159 VAL B CG2   1 
ATOM   7375  N  N     . LEU B 1 141 ? 199.712 189.586 125.836 1.00 51.12  ?  160 LEU B N     1 
ATOM   7376  C  CA    . LEU B 1 141 ? 200.729 189.901 124.845 1.00 37.90  ?  160 LEU B CA    1 
ATOM   7377  C  C     . LEU B 1 141 ? 200.664 188.898 123.702 1.00 42.84  ?  160 LEU B C     1 
ATOM   7378  O  O     . LEU B 1 141 ? 200.570 187.685 123.932 1.00 53.75  ?  160 LEU B O     1 
ATOM   7379  C  CB    . LEU B 1 141 ? 202.122 189.896 125.478 1.00 49.34  ?  160 LEU B CB    1 
ATOM   7380  C  CG    . LEU B 1 141 ? 202.349 190.858 126.647 1.00 49.81  ?  160 LEU B CG    1 
ATOM   7381  C  CD1   . LEU B 1 141 ? 203.335 190.269 127.646 1.00 50.51  ?  160 LEU B CD1   1 
ATOM   7382  C  CD2   . LEU B 1 141 ? 202.843 192.203 126.140 1.00 56.95  ?  160 LEU B CD2   1 
ATOM   7383  N  N     . ASP B 1 142 ? 200.717 189.409 122.478 1.00 64.22  ?  161 ASP B N     1 
ATOM   7384  C  CA    . ASP B 1 142 ? 200.683 188.596 121.277 1.00 76.55  ?  161 ASP B CA    1 
ATOM   7385  C  C     . ASP B 1 142 ? 202.070 188.044 120.959 1.00 82.07  ?  161 ASP B C     1 
ATOM   7386  O  O     . ASP B 1 142 ? 203.075 188.519 121.493 1.00 81.41  ?  161 ASP B O     1 
ATOM   7387  C  CB    . ASP B 1 142 ? 200.153 189.424 120.107 1.00 73.48  ?  161 ASP B CB    1 
ATOM   7388  C  CG    . ASP B 1 142 ? 200.828 190.781 119.992 1.00 73.07  ?  161 ASP B CG    1 
ATOM   7389  O  OD1   . ASP B 1 142 ? 201.964 190.935 120.483 1.00 77.43  ?  161 ASP B OD1   1 
ATOM   7390  O  OD2   . ASP B 1 142 ? 200.216 191.699 119.405 1.00 74.39  -1 161 ASP B OD2   1 
ATOM   7391  N  N     . PRO B 1 143 ? 202.152 187.022 120.101 1.00 78.44  ?  162 PRO B N     1 
ATOM   7392  C  CA    . PRO B 1 143 ? 203.474 186.561 119.646 1.00 68.42  ?  162 PRO B CA    1 
ATOM   7393  C  C     . PRO B 1 143 ? 204.277 187.641 118.942 1.00 70.20  ?  162 PRO B C     1 
ATOM   7394  O  O     . PRO B 1 143 ? 205.513 187.581 118.943 1.00 74.12  ?  162 PRO B O     1 
ATOM   7395  C  CB    . PRO B 1 143 ? 203.138 185.398 118.702 1.00 68.59  ?  162 PRO B CB    1 
ATOM   7396  C  CG    . PRO B 1 143 ? 201.794 184.939 119.129 1.00 71.62  ?  162 PRO B CG    1 
ATOM   7397  C  CD    . PRO B 1 143 ? 201.066 186.153 119.612 1.00 73.77  ?  162 PRO B CD    1 
ATOM   7398  N  N     . GLU B 1 144 ? 203.613 188.632 118.341 1.00 76.43  ?  163 GLU B N     1 
ATOM   7399  C  CA    . GLU B 1 144 ? 204.279 189.786 117.733 1.00 78.27  ?  163 GLU B CA    1 
ATOM   7400  C  C     . GLU B 1 144 ? 204.887 190.731 118.764 1.00 79.54  ?  163 GLU B C     1 
ATOM   7401  O  O     . GLU B 1 144 ? 205.374 191.810 118.396 1.00 81.08  ?  163 GLU B O     1 
ATOM   7402  C  CB    . GLU B 1 144 ? 203.296 190.541 116.838 1.00 78.04  ?  163 GLU B CB    1 
ATOM   7403  C  CG    . GLU B 1 144 ? 202.376 189.626 116.051 1.00 78.14  ?  163 GLU B CG    1 
ATOM   7404  C  CD    . GLU B 1 144 ? 203.145 188.636 115.197 1.00 80.47  ?  163 GLU B CD    1 
ATOM   7405  O  OE1   . GLU B 1 144 ? 203.889 189.078 114.297 1.00 78.59  ?  163 GLU B OE1   1 
ATOM   7406  O  OE2   . GLU B 1 144 ? 203.014 187.417 115.435 1.00 81.18  -1 163 GLU B OE2   1 
ATOM   7407  N  N     . ARG B 1 145 ? 204.827 190.317 120.028 1.00 80.76  ?  164 ARG B N     1 
ATOM   7408  C  CA    . ARG B 1 145 ? 205.455 190.912 121.203 1.00 80.15  ?  164 ARG B CA    1 
ATOM   7409  C  C     . ARG B 1 145 ? 204.738 192.150 121.734 1.00 83.27  ?  164 ARG B C     1 
ATOM   7410  O  O     . ARG B 1 145 ? 205.240 192.741 122.686 1.00 83.24  ?  164 ARG B O     1 
ATOM   7411  C  CB    . ARG B 1 145 ? 206.933 191.276 120.978 1.00 84.15  ?  164 ARG B CB    1 
ATOM   7412  C  CG    . ARG B 1 145 ? 207.835 190.089 120.675 1.00 86.35  ?  164 ARG B CG    1 
ATOM   7413  C  CD    . ARG B 1 145 ? 209.293 190.399 120.993 1.00 82.35  ?  164 ARG B CD    1 
ATOM   7414  N  NE    . ARG B 1 145 ? 209.763 191.613 120.336 1.00 85.36  ?  164 ARG B NE    1 
ATOM   7415  C  CZ    . ARG B 1 145 ? 210.045 192.745 120.968 1.00 88.69  ?  164 ARG B CZ    1 
ATOM   7416  N  NH1   . ARG B 1 145 ? 210.471 193.813 120.314 1.00 89.14  1  164 ARG B NH1   1 
ATOM   7417  N  NH2   . ARG B 1 145 ? 209.897 192.805 122.288 1.00 86.97  ?  164 ARG B NH2   1 
ATOM   7418  N  N     . HIS B 1 146 ? 203.591 192.545 121.187 1.00 77.79  ?  165 HIS B N     1 
ATOM   7419  C  CA    . HIS B 1 146 ? 202.934 193.780 121.586 1.00 72.11  ?  165 HIS B CA    1 
ATOM   7420  C  C     . HIS B 1 146 ? 201.779 193.502 122.553 1.00 76.24  ?  165 HIS B C     1 
ATOM   7421  O  O     . HIS B 1 146 ? 201.490 192.354 122.905 1.00 78.81  ?  165 HIS B O     1 
ATOM   7422  C  CB    . HIS B 1 146 ? 202.466 194.539 120.343 1.00 74.42  ?  165 HIS B CB    1 
ATOM   7423  C  CG    . HIS B 1 146 ? 203.565 194.835 119.370 1.00 74.13  ?  165 HIS B CG    1 
ATOM   7424  N  ND1   . HIS B 1 146 ? 204.786 195.342 119.759 1.00 74.01  ?  165 HIS B ND1   1 
ATOM   7425  C  CD2   . HIS B 1 146 ? 203.625 194.700 118.024 1.00 75.52  ?  165 HIS B CD2   1 
ATOM   7426  C  CE1   . HIS B 1 146 ? 205.552 195.505 118.695 1.00 77.82  ?  165 HIS B CE1   1 
ATOM   7427  N  NE2   . HIS B 1 146 ? 204.872 195.123 117.630 1.00 78.39  ?  165 HIS B NE2   1 
ATOM   7428  N  N     . ILE B 1 147 ? 201.107 194.571 122.989 1.00 70.79  ?  166 ILE B N     1 
ATOM   7429  C  CA    . ILE B 1 147 ? 200.002 194.501 123.942 1.00 60.60  ?  166 ILE B CA    1 
ATOM   7430  C  C     . ILE B 1 147 ? 198.685 194.491 123.180 1.00 56.45  ?  166 ILE B C     1 
ATOM   7431  O  O     . ILE B 1 147 ? 198.506 195.246 122.216 1.00 68.20  ?  166 ILE B O     1 
ATOM   7432  C  CB    . ILE B 1 147 ? 200.052 195.677 124.938 1.00 61.49  ?  166 ILE B CB    1 
ATOM   7433  C  CG1   . ILE B 1 147 ? 201.055 195.396 126.058 1.00 63.46  ?  166 ILE B CG1   1 
ATOM   7434  C  CG2   . ILE B 1 147 ? 198.678 195.967 125.517 1.00 62.48  ?  166 ILE B CG2   1 
ATOM   7435  C  CD1   . ILE B 1 147 ? 201.238 196.561 127.010 1.00 67.07  ?  166 ILE B CD1   1 
ATOM   7436  N  N     . VAL B 1 148 ? 197.757 193.636 123.611 1.00 40.75  ?  167 VAL B N     1 
ATOM   7437  C  CA    . VAL B 1 148 ? 196.444 193.509 122.983 1.00 47.99  ?  167 VAL B CA    1 
ATOM   7438  C  C     . VAL B 1 148 ? 195.324 193.928 123.937 1.00 59.57  ?  167 VAL B C     1 
ATOM   7439  O  O     . VAL B 1 148 ? 194.588 194.877 123.662 1.00 66.74  ?  167 VAL B O     1 
ATOM   7440  C  CB    . VAL B 1 148 ? 196.219 192.077 122.450 1.00 52.16  ?  167 VAL B CB    1 
ATOM   7441  C  CG1   . VAL B 1 148 ? 194.855 191.971 121.793 1.00 50.83  ?  167 VAL B CG1   1 
ATOM   7442  C  CG2   . VAL B 1 148 ? 197.317 191.699 121.471 1.00 57.69  ?  167 VAL B CG2   1 
ATOM   7443  N  N     . GLN B 1 149 ? 195.182 193.232 125.063 1.00 50.87  ?  168 GLN B N     1 
ATOM   7444  C  CA    . GLN B 1 149 ? 194.092 193.468 126.001 1.00 44.29  ?  168 GLN B CA    1 
ATOM   7445  C  C     . GLN B 1 149 ? 194.634 193.823 127.377 1.00 40.11  ?  168 GLN B C     1 
ATOM   7446  O  O     . GLN B 1 149 ? 195.590 193.207 127.856 1.00 44.02  ?  168 GLN B O     1 
ATOM   7447  C  CB    . GLN B 1 149 ? 193.175 192.246 126.119 1.00 38.22  ?  168 GLN B CB    1 
ATOM   7448  C  CG    . GLN B 1 149 ? 192.098 192.171 125.056 1.00 41.23  ?  168 GLN B CG    1 
ATOM   7449  C  CD    . GLN B 1 149 ? 191.137 191.027 125.293 1.00 47.27  ?  168 GLN B CD    1 
ATOM   7450  O  OE1   . GLN B 1 149 ? 191.288 190.261 126.246 1.00 52.21  ?  168 GLN B OE1   1 
ATOM   7451  N  NE2   . GLN B 1 149 ? 190.135 190.907 124.431 1.00 50.15  ?  168 GLN B NE2   1 
ATOM   7452  N  N     . CYS B 1 150 ? 194.007 194.809 128.012 1.00 43.65  ?  169 CYS B N     1 
ATOM   7453  C  CA    . CYS B 1 150 ? 194.369 195.258 129.348 1.00 45.59  ?  169 CYS B CA    1 
ATOM   7454  C  C     . CYS B 1 150 ? 193.235 194.961 130.325 1.00 46.99  ?  169 CYS B C     1 
ATOM   7455  O  O     . CYS B 1 150 ? 192.211 194.369 129.974 1.00 51.39  ?  169 CYS B O     1 
ATOM   7456  C  CB    . CYS B 1 150 ? 194.708 196.750 129.343 1.00 40.46  ?  169 CYS B CB    1 
ATOM   7457  S  SG    . CYS B 1 150 ? 193.381 197.814 128.732 1.00 58.73  ?  169 CYS B SG    1 
ATOM   7458  N  N     . ASN B 1 151 ? 193.435 195.385 131.567 1.00 33.28  ?  170 ASN B N     1 
ATOM   7459  C  CA    . ASN B 1 151 ? 192.471 195.242 132.650 1.00 29.68  ?  170 ASN B CA    1 
ATOM   7460  C  C     . ASN B 1 151 ? 192.051 196.626 133.138 1.00 33.48  ?  170 ASN B C     1 
ATOM   7461  O  O     . ASN B 1 151 ? 192.505 197.655 132.629 1.00 44.81  ?  170 ASN B O     1 
ATOM   7462  C  CB    . ASN B 1 151 ? 193.067 194.410 133.792 1.00 30.22  ?  170 ASN B CB    1 
ATOM   7463  C  CG    . ASN B 1 151 ? 192.007 193.788 134.682 1.00 36.93  ?  170 ASN B CG    1 
ATOM   7464  O  OD1   . ASN B 1 151 ? 191.191 194.491 135.277 1.00 45.63  ?  170 ASN B OD1   1 
ATOM   7465  N  ND2   . ASN B 1 151 ? 192.024 192.465 134.789 1.00 36.48  ?  170 ASN B ND2   1 
ATOM   7466  N  N     . ARG B 1 152 ? 191.175 196.645 134.142 1.00 33.63  ?  171 ARG B N     1 
ATOM   7467  C  CA    . ARG B 1 152 ? 190.765 197.896 134.766 1.00 36.66  ?  171 ARG B CA    1 
ATOM   7468  C  C     . ARG B 1 152 ? 191.692 198.289 135.909 1.00 44.58  ?  171 ARG B C     1 
ATOM   7469  O  O     . ARG B 1 152 ? 191.942 199.480 136.122 1.00 55.75  ?  171 ARG B O     1 
ATOM   7470  C  CB    . ARG B 1 152 ? 189.321 197.790 135.267 1.00 36.89  ?  171 ARG B CB    1 
ATOM   7471  C  CG    . ARG B 1 152 ? 188.758 199.095 135.807 1.00 35.25  ?  171 ARG B CG    1 
ATOM   7472  C  CD    . ARG B 1 152 ? 187.341 198.927 136.335 1.00 43.64  ?  171 ARG B CD    1 
ATOM   7473  N  NE    . ARG B 1 152 ? 186.350 198.916 135.265 1.00 48.87  ?  171 ARG B NE    1 
ATOM   7474  C  CZ    . ARG B 1 152 ? 185.049 198.737 135.448 1.00 47.63  ?  171 ARG B CZ    1 
ATOM   7475  N  NH1   . ARG B 1 152 ? 184.539 198.552 136.655 1.00 47.81  1  171 ARG B NH1   1 
ATOM   7476  N  NH2   . ARG B 1 152 ? 184.238 198.746 134.394 1.00 43.43  ?  171 ARG B NH2   1 
ATOM   7477  N  N     . ALA B 1 153 ? 192.220 197.309 136.645 1.00 39.43  ?  172 ALA B N     1 
ATOM   7478  C  CA    . ALA B 1 153 ? 193.216 197.611 137.670 1.00 47.31  ?  172 ALA B CA    1 
ATOM   7479  C  C     . ALA B 1 153 ? 194.492 198.167 137.048 1.00 51.98  ?  172 ALA B C     1 
ATOM   7480  O  O     . ALA B 1 153 ? 195.152 199.035 137.634 1.00 53.93  ?  172 ALA B O     1 
ATOM   7481  C  CB    . ALA B 1 153 ? 193.518 196.362 138.496 1.00 42.19  ?  172 ALA B CB    1 
ATOM   7482  N  N     . PHE B 1 154 ? 194.857 197.673 135.861 1.00 44.17  ?  173 PHE B N     1 
ATOM   7483  C  CA    . PHE B 1 154 ? 196.001 198.224 135.141 1.00 42.85  ?  173 PHE B CA    1 
ATOM   7484  C  C     . PHE B 1 154 ? 195.772 199.692 134.801 1.00 43.57  ?  173 PHE B C     1 
ATOM   7485  O  O     . PHE B 1 154 ? 196.659 200.532 134.987 1.00 52.85  ?  173 PHE B O     1 
ATOM   7486  C  CB    . PHE B 1 154 ? 196.259 197.407 133.873 1.00 51.68  ?  173 PHE B CB    1 
ATOM   7487  C  CG    . PHE B 1 154 ? 197.483 197.834 133.108 1.00 50.62  ?  173 PHE B CG    1 
ATOM   7488  C  CD1   . PHE B 1 154 ? 197.382 198.732 132.056 1.00 43.49  ?  173 PHE B CD1   1 
ATOM   7489  C  CD2   . PHE B 1 154 ? 198.732 197.329 133.430 1.00 45.62  ?  173 PHE B CD2   1 
ATOM   7490  C  CE1   . PHE B 1 154 ? 198.503 199.126 131.349 1.00 41.75  ?  173 PHE B CE1   1 
ATOM   7491  C  CE2   . PHE B 1 154 ? 199.858 197.719 132.726 1.00 37.85  ?  173 PHE B CE2   1 
ATOM   7492  C  CZ    . PHE B 1 154 ? 199.742 198.619 131.683 1.00 42.12  ?  173 PHE B CZ    1 
ATOM   7493  N  N     . THR B 1 155 ? 194.576 200.019 134.305 1.00 40.76  ?  174 THR B N     1 
ATOM   7494  C  CA    . THR B 1 155 ? 194.250 201.408 133.998 1.00 41.11  ?  174 THR B CA    1 
ATOM   7495  C  C     . THR B 1 155 ? 194.207 202.264 135.257 1.00 41.29  ?  174 THR B C     1 
ATOM   7496  O  O     . THR B 1 155 ? 194.559 203.448 135.215 1.00 55.18  ?  174 THR B O     1 
ATOM   7497  C  CB    . THR B 1 155 ? 192.912 201.482 133.259 1.00 39.08  ?  174 THR B CB    1 
ATOM   7498  O  OG1   . THR B 1 155 ? 192.923 200.570 132.153 1.00 39.44  ?  174 THR B OG1   1 
ATOM   7499  C  CG2   . THR B 1 155 ? 192.652 202.893 132.746 1.00 46.14  ?  174 THR B CG2   1 
ATOM   7500  N  N     . GLU B 1 156 ? 193.792 201.686 136.383 1.00 36.07  ?  175 GLU B N     1 
ATOM   7501  C  CA    . GLU B 1 156 ? 193.702 202.458 137.617 1.00 48.19  ?  175 GLU B CA    1 
ATOM   7502  C  C     . GLU B 1 156 ? 195.078 202.757 138.203 1.00 56.00  ?  175 GLU B C     1 
ATOM   7503  O  O     . GLU B 1 156 ? 195.330 203.880 138.652 1.00 56.13  ?  175 GLU B O     1 
ATOM   7504  C  CB    . GLU B 1 156 ? 192.838 201.717 138.637 1.00 51.72  ?  175 GLU B CB    1 
ATOM   7505  C  CG    . GLU B 1 156 ? 191.353 202.018 138.531 1.00 56.23  ?  175 GLU B CG    1 
ATOM   7506  C  CD    . GLU B 1 156 ? 191.039 203.485 138.749 1.00 60.32  ?  175 GLU B CD    1 
ATOM   7507  O  OE1   . GLU B 1 156 ? 191.413 204.024 139.813 1.00 58.74  ?  175 GLU B OE1   1 
ATOM   7508  O  OE2   . GLU B 1 156 ? 190.414 204.100 137.858 1.00 60.00  -1 175 GLU B OE2   1 
ATOM   7509  N  N     . MET B 1 157 ? 195.979 201.774 138.209 1.00 54.42  ?  176 MET B N     1 
ATOM   7510  C  CA    . MET B 1 157 ? 197.290 201.952 138.820 1.00 50.83  ?  176 MET B CA    1 
ATOM   7511  C  C     . MET B 1 157 ? 198.384 202.340 137.832 1.00 46.28  ?  176 MET B C     1 
ATOM   7512  O  O     . MET B 1 157 ? 199.542 202.476 138.243 1.00 48.73  ?  176 MET B O     1 
ATOM   7513  C  CB    . MET B 1 157 ? 197.700 200.682 139.577 1.00 49.40  ?  176 MET B CB    1 
ATOM   7514  C  CG    . MET B 1 157 ? 198.330 199.603 138.723 1.00 55.13  ?  176 MET B CG    1 
ATOM   7515  S  SD    . MET B 1 157 ? 199.159 198.371 139.742 1.00 65.71  ?  176 MET B SD    1 
ATOM   7516  C  CE    . MET B 1 157 ? 197.816 197.882 140.824 1.00 53.55  ?  176 MET B CE    1 
ATOM   7517  N  N     . PHE B 1 158 ? 198.057 202.532 136.553 1.00 51.43  ?  177 PHE B N     1 
ATOM   7518  C  CA    . PHE B 1 158 ? 199.012 203.058 135.589 1.00 54.82  ?  177 PHE B CA    1 
ATOM   7519  C  C     . PHE B 1 158 ? 198.461 204.182 134.723 1.00 50.53  ?  177 PHE B C     1 
ATOM   7520  O  O     . PHE B 1 158 ? 199.251 204.882 134.079 1.00 58.44  ?  177 PHE B O     1 
ATOM   7521  C  CB    . PHE B 1 158 ? 199.538 201.939 134.674 1.00 59.90  ?  177 PHE B CB    1 
ATOM   7522  C  CG    . PHE B 1 158 ? 200.406 200.934 135.379 1.00 59.61  ?  177 PHE B CG    1 
ATOM   7523  C  CD1   . PHE B 1 158 ? 201.674 201.281 135.819 1.00 51.29  ?  177 PHE B CD1   1 
ATOM   7524  C  CD2   . PHE B 1 158 ? 199.959 199.642 135.596 1.00 58.91  ?  177 PHE B CD2   1 
ATOM   7525  C  CE1   . PHE B 1 158 ? 202.477 200.358 136.465 1.00 45.06  ?  177 PHE B CE1   1 
ATOM   7526  C  CE2   . PHE B 1 158 ? 200.757 198.715 136.241 1.00 56.82  ?  177 PHE B CE2   1 
ATOM   7527  C  CZ    . PHE B 1 158 ? 202.018 199.074 136.676 1.00 49.32  ?  177 PHE B CZ    1 
ATOM   7528  N  N     . GLY B 1 159 ? 197.146 204.382 134.687 1.00 54.04  ?  178 GLY B N     1 
ATOM   7529  C  CA    . GLY B 1 159 ? 196.585 205.472 133.915 1.00 60.04  ?  178 GLY B CA    1 
ATOM   7530  C  C     . GLY B 1 159 ? 196.558 205.263 132.419 1.00 62.62  ?  178 GLY B C     1 
ATOM   7531  O  O     . GLY B 1 159 ? 196.307 206.221 131.682 1.00 65.96  ?  178 GLY B O     1 
ATOM   7532  N  N     . TYR B 1 160 ? 196.809 204.047 131.943 1.00 57.74  ?  179 TYR B N     1 
ATOM   7533  C  CA    . TYR B 1 160 ? 196.812 203.750 130.518 1.00 63.57  ?  179 TYR B CA    1 
ATOM   7534  C  C     . TYR B 1 160 ? 195.564 202.953 130.165 1.00 59.55  ?  179 TYR B C     1 
ATOM   7535  O  O     . TYR B 1 160 ? 195.217 201.993 130.861 1.00 68.02  ?  179 TYR B O     1 
ATOM   7536  C  CB    . TYR B 1 160 ? 198.072 202.975 130.125 1.00 66.73  ?  179 TYR B CB    1 
ATOM   7537  C  CG    . TYR B 1 160 ? 199.351 203.744 130.369 1.00 66.86  ?  179 TYR B CG    1 
ATOM   7538  C  CD1   . TYR B 1 160 ? 199.710 204.809 129.555 1.00 61.00  ?  179 TYR B CD1   1 
ATOM   7539  C  CD2   . TYR B 1 160 ? 200.198 203.406 131.415 1.00 64.49  ?  179 TYR B CD2   1 
ATOM   7540  C  CE1   . TYR B 1 160 ? 200.875 205.518 129.776 1.00 59.80  ?  179 TYR B CE1   1 
ATOM   7541  C  CE2   . TYR B 1 160 ? 201.367 204.108 131.644 1.00 65.29  ?  179 TYR B CE2   1 
ATOM   7542  C  CZ    . TYR B 1 160 ? 201.700 205.162 130.821 1.00 64.85  ?  179 TYR B CZ    1 
ATOM   7543  O  OH    . TYR B 1 160 ? 202.862 205.863 131.046 1.00 66.65  ?  179 TYR B OH    1 
ATOM   7544  N  N     . CYS B 1 161 ? 194.896 203.349 129.086 1.00 61.98  ?  180 CYS B N     1 
ATOM   7545  C  CA    . CYS B 1 161 ? 193.629 202.749 128.704 1.00 66.47  ?  180 CYS B CA    1 
ATOM   7546  C  C     . CYS B 1 161 ? 193.828 201.822 127.505 1.00 65.08  ?  180 CYS B C     1 
ATOM   7547  O  O     . CYS B 1 161 ? 194.922 201.712 126.945 1.00 66.86  ?  180 CYS B O     1 
ATOM   7548  C  CB    . CYS B 1 161 ? 192.597 203.837 128.415 1.00 70.93  ?  180 CYS B CB    1 
ATOM   7549  S  SG    . CYS B 1 161 ? 192.796 204.641 126.810 1.00 81.07  ?  180 CYS B SG    1 
ATOM   7550  N  N     . ILE B 1 162 ? 192.754 201.143 127.099 1.00 69.72  ?  181 ILE B N     1 
ATOM   7551  C  CA    . ILE B 1 162 ? 192.839 200.182 126.006 1.00 71.55  ?  181 ILE B CA    1 
ATOM   7552  C  C     . ILE B 1 162 ? 193.097 200.886 124.679 1.00 75.40  ?  181 ILE B C     1 
ATOM   7553  O  O     . ILE B 1 162 ? 193.831 200.373 123.828 1.00 79.18  ?  181 ILE B O     1 
ATOM   7554  C  CB    . ILE B 1 162 ? 191.566 199.314 125.961 1.00 75.37  ?  181 ILE B CB    1 
ATOM   7555  C  CG1   . ILE B 1 162 ? 191.657 198.282 124.834 1.00 76.22  ?  181 ILE B CG1   1 
ATOM   7556  C  CG2   . ILE B 1 162 ? 190.317 200.177 125.820 1.00 74.86  ?  181 ILE B CG2   1 
ATOM   7557  C  CD1   . ILE B 1 162 ? 192.731 197.238 125.051 1.00 71.86  ?  181 ILE B CD1   1 
ATOM   7558  N  N     . SER B 1 163 ? 192.510 202.069 124.479 1.00 77.14  ?  182 SER B N     1 
ATOM   7559  C  CA    . SER B 1 163 ? 192.731 202.800 123.234 1.00 75.33  ?  182 SER B CA    1 
ATOM   7560  C  C     . SER B 1 163 ? 194.196 203.188 123.074 1.00 71.05  ?  182 SER B C     1 
ATOM   7561  O  O     . SER B 1 163 ? 194.762 203.071 121.981 1.00 68.99  ?  182 SER B O     1 
ATOM   7562  C  CB    . SER B 1 163 ? 191.840 204.041 123.188 1.00 76.02  ?  182 SER B CB    1 
ATOM   7563  O  OG    . SER B 1 163 ? 192.144 204.927 124.250 1.00 78.49  ?  182 SER B OG    1 
ATOM   7564  N  N     . GLU B 1 164 ? 194.826 203.651 124.154 1.00 68.96  ?  183 GLU B N     1 
ATOM   7565  C  CA    . GLU B 1 164 ? 196.228 204.045 124.089 1.00 68.17  ?  183 GLU B CA    1 
ATOM   7566  C  C     . GLU B 1 164 ? 197.166 202.845 124.033 1.00 76.28  ?  183 GLU B C     1 
ATOM   7567  O  O     . GLU B 1 164 ? 198.172 202.886 123.316 1.00 80.25  ?  183 GLU B O     1 
ATOM   7568  C  CB    . GLU B 1 164 ? 196.581 204.929 125.288 1.00 70.13  ?  183 GLU B CB    1 
ATOM   7569  C  CG    . GLU B 1 164 ? 197.919 205.642 125.165 1.00 75.93  ?  183 GLU B CG    1 
ATOM   7570  C  CD    . GLU B 1 164 ? 197.830 206.917 124.348 1.00 78.23  ?  183 GLU B CD    1 
ATOM   7571  O  OE1   . GLU B 1 164 ? 196.701 207.349 124.036 1.00 76.34  ?  183 GLU B OE1   1 
ATOM   7572  O  OE2   . GLU B 1 164 ? 198.891 207.488 124.017 1.00 77.94  -1 183 GLU B OE2   1 
ATOM   7573  N  N     . ALA B 1 165 ? 196.864 201.777 124.773 1.00 83.34  ?  184 ALA B N     1 
ATOM   7574  C  CA    . ALA B 1 165 ? 197.768 200.641 124.892 1.00 77.05  ?  184 ALA B CA    1 
ATOM   7575  C  C     . ALA B 1 165 ? 197.546 199.559 123.841 1.00 72.58  ?  184 ALA B C     1 
ATOM   7576  O  O     . ALA B 1 165 ? 198.350 198.625 123.765 1.00 72.04  ?  184 ALA B O     1 
ATOM   7577  C  CB    . ALA B 1 165 ? 197.651 200.017 126.288 1.00 74.75  ?  184 ALA B CB    1 
ATOM   7578  N  N     . SER B 1 166 ? 196.496 199.657 123.033 1.00 75.15  ?  185 SER B N     1 
ATOM   7579  C  CA    . SER B 1 166 ? 196.156 198.605 122.090 1.00 74.37  ?  185 SER B CA    1 
ATOM   7580  C  C     . SER B 1 166 ? 196.869 198.808 120.757 1.00 79.55  ?  185 SER B C     1 
ATOM   7581  O  O     . SER B 1 166 ? 197.336 199.901 120.429 1.00 82.07  ?  185 SER B O     1 
ATOM   7582  C  CB    . SER B 1 166 ? 194.644 198.548 121.871 1.00 76.94  ?  185 SER B CB    1 
ATOM   7583  O  OG    . SER B 1 166 ? 194.301 197.536 120.941 1.00 76.92  ?  185 SER B OG    1 
ATOM   7584  N  N     . GLY B 1 167 ? 196.945 197.725 119.987 1.00 83.33  ?  186 GLY B N     1 
ATOM   7585  C  CA    . GLY B 1 167 ? 197.583 197.756 118.686 1.00 83.42  ?  186 GLY B CA    1 
ATOM   7586  C  C     . GLY B 1 167 ? 199.093 197.752 118.785 1.00 83.26  ?  186 GLY B C     1 
ATOM   7587  O  O     . GLY B 1 167 ? 199.743 196.747 118.479 1.00 85.91  ?  186 GLY B O     1 
ATOM   7588  N  N     . MET B 1 168 ? 199.660 198.872 119.218 1.00 85.69  ?  187 MET B N     1 
ATOM   7589  C  CA    . MET B 1 168 ? 201.084 198.984 119.472 1.00 85.97  ?  187 MET B CA    1 
ATOM   7590  C  C     . MET B 1 168 ? 201.367 198.538 120.904 1.00 84.73  ?  187 MET B C     1 
ATOM   7591  O  O     . MET B 1 168 ? 200.495 198.000 121.595 1.00 82.31  ?  187 MET B O     1 
ATOM   7592  C  CB    . MET B 1 168 ? 201.557 200.413 119.193 1.00 86.99  ?  187 MET B CB    1 
ATOM   7593  C  CG    . MET B 1 168 ? 200.760 201.497 119.904 1.00 88.63  ?  187 MET B CG    1 
ATOM   7594  S  SD    . MET B 1 168 ? 201.413 201.909 121.533 1.00 88.15  ?  187 MET B SD    1 
ATOM   7595  C  CE    . MET B 1 168 ? 202.934 202.741 121.085 1.00 85.15  ?  187 MET B CE    1 
ATOM   7596  N  N     . GLN B 1 169 ? 202.590 198.758 121.367 1.00 88.43  ?  188 GLN B N     1 
ATOM   7597  C  CA    . GLN B 1 169 ? 202.999 198.278 122.686 1.00 85.81  ?  188 GLN B CA    1 
ATOM   7598  C  C     . GLN B 1 169 ? 203.592 199.385 123.539 1.00 88.89  ?  188 GLN B C     1 
ATOM   7599  O  O     . GLN B 1 169 ? 204.731 199.820 123.280 1.00 87.68  ?  188 GLN B O     1 
ATOM   7600  C  CB    . GLN B 1 169 ? 204.014 197.145 122.560 1.00 89.47  ?  188 GLN B CB    1 
ATOM   7601  C  CG    . GLN B 1 169 ? 204.245 196.440 123.876 1.00 88.63  ?  188 GLN B CG    1 
ATOM   7602  C  CD    . GLN B 1 169 ? 205.249 195.321 123.776 1.00 92.83  ?  188 GLN B CD    1 
ATOM   7603  O  OE1   . GLN B 1 169 ? 205.540 194.641 124.760 1.00 94.30  ?  188 GLN B OE1   1 
ATOM   7604  N  NE2   . GLN B 1 169 ? 205.796 195.122 122.583 1.00 91.82  ?  188 GLN B NE2   1 
ATOM   7605  N  N     . PRO B 1 170 ? 202.881 199.877 124.554 1.00 97.76  ?  189 PRO B N     1 
ATOM   7606  C  CA    . PRO B 1 170 ? 203.517 200.635 125.638 1.00 95.00  ?  189 PRO B CA    1 
ATOM   7607  C  C     . PRO B 1 170 ? 204.043 199.725 126.747 1.00 98.48  ?  189 PRO B C     1 
ATOM   7608  O  O     . PRO B 1 170 ? 203.846 199.984 127.939 1.00 96.99  ?  189 PRO B O     1 
ATOM   7609  C  CB    . PRO B 1 170 ? 202.385 201.540 126.135 1.00 90.65  ?  189 PRO B CB    1 
ATOM   7610  C  CG    . PRO B 1 170 ? 201.230 201.339 125.183 1.00 94.52  ?  189 PRO B CG    1 
ATOM   7611  C  CD    . PRO B 1 170 ? 201.417 199.980 124.610 1.00 94.26  ?  189 PRO B CD    1 
ATOM   7612  N  N     . ASP B 1 171 ? 204.698 198.629 126.362 1.00 94.80  ?  190 ASP B N     1 
ATOM   7613  C  CA    . ASP B 1 171 ? 205.359 197.781 127.346 1.00 88.34  ?  190 ASP B CA    1 
ATOM   7614  C  C     . ASP B 1 171 ? 206.863 197.784 127.115 1.00 91.55  ?  190 ASP B C     1 
ATOM   7615  O  O     . ASP B 1 171 ? 207.619 198.181 128.002 1.00 94.67  ?  190 ASP B O     1 
ATOM   7616  C  CB    . ASP B 1 171 ? 204.815 196.353 127.302 1.00 85.87  ?  190 ASP B CB    1 
ATOM   7617  C  CG    . ASP B 1 171 ? 205.175 195.553 128.539 1.00 92.08  ?  190 ASP B CG    1 
ATOM   7618  O  OD1   . ASP B 1 171 ? 205.849 196.106 129.434 1.00 93.44  ?  190 ASP B OD1   1 
ATOM   7619  O  OD2   . ASP B 1 171 ? 204.794 194.366 128.613 1.00 94.40  -1 190 ASP B OD2   1 
ATOM   7620  N  N     . THR B 1 172 ? 207.305 197.394 125.917 1.00 93.76  ?  191 THR B N     1 
ATOM   7621  C  CA    . THR B 1 172 ? 208.737 197.400 125.630 1.00 98.25  ?  191 THR B CA    1 
ATOM   7622  C  C     . THR B 1 172 ? 209.321 198.806 125.703 1.00 99.14  ?  191 THR B C     1 
ATOM   7623  O  O     . THR B 1 172 ? 210.448 198.986 126.176 1.00 96.93  ?  191 THR B O     1 
ATOM   7624  C  CB    . THR B 1 172 ? 209.013 196.782 124.258 1.00 96.26  ?  191 THR B CB    1 
ATOM   7625  O  OG1   . THR B 1 172 ? 208.267 197.480 123.252 1.00 94.43  ?  191 THR B OG1   1 
ATOM   7626  C  CG2   . THR B 1 172 ? 208.647 195.307 124.246 1.00 94.58  ?  191 THR B CG2   1 
ATOM   7627  N  N     . LEU B 1 173 ? 208.576 199.808 125.241 1.00 99.72  ?  192 LEU B N     1 
ATOM   7628  C  CA    . LEU B 1 173 ? 209.049 201.187 125.259 1.00 97.78  ?  192 LEU B CA    1 
ATOM   7629  C  C     . LEU B 1 173 ? 208.699 201.932 126.540 1.00 95.42  ?  192 LEU B C     1 
ATOM   7630  O  O     . LEU B 1 173 ? 209.337 202.946 126.843 1.00 97.39  ?  192 LEU B O     1 
ATOM   7631  C  CB    . LEU B 1 173 ? 208.483 201.960 124.061 1.00 97.59  ?  192 LEU B CB    1 
ATOM   7632  C  CG    . LEU B 1 173 ? 209.312 201.981 122.771 1.00 98.43  ?  192 LEU B CG    1 
ATOM   7633  C  CD1   . LEU B 1 173 ? 210.663 202.647 123.002 1.00 95.88  ?  192 LEU B CD1   1 
ATOM   7634  C  CD2   . LEU B 1 173 ? 209.488 200.581 122.193 1.00 96.69  ?  192 LEU B CD2   1 
ATOM   7635  N  N     . LEU B 1 174 ? 207.708 201.466 127.297 1.00 91.48  ?  193 LEU B N     1 
ATOM   7636  C  CA    . LEU B 1 174 ? 207.280 202.150 128.511 1.00 93.99  ?  193 LEU B CA    1 
ATOM   7637  C  C     . LEU B 1 174 ? 207.685 201.427 129.790 1.00 95.98  ?  193 LEU B C     1 
ATOM   7638  O  O     . LEU B 1 174 ? 207.317 201.880 130.879 1.00 96.26  ?  193 LEU B O     1 
ATOM   7639  C  CB    . LEU B 1 174 ? 205.761 202.350 128.501 1.00 89.88  ?  193 LEU B CB    1 
ATOM   7640  C  CG    . LEU B 1 174 ? 205.213 203.639 127.882 1.00 94.59  ?  193 LEU B CG    1 
ATOM   7641  C  CD1   . LEU B 1 174 ? 205.676 204.851 128.678 1.00 96.69  ?  193 LEU B CD1   1 
ATOM   7642  C  CD2   . LEU B 1 174 ? 205.601 203.771 126.416 1.00 96.01  ?  193 LEU B CD2   1 
ATOM   7643  N  N     . ASN B 1 175 ? 208.426 200.322 129.692 1.00 100.25 ?  194 ASN B N     1 
ATOM   7644  C  CA    . ASN B 1 175 ? 208.902 199.642 130.888 1.00 102.76 ?  194 ASN B CA    1 
ATOM   7645  C  C     . ASN B 1 175 ? 210.135 200.320 131.463 1.00 103.23 ?  194 ASN B C     1 
ATOM   7646  O  O     . ASN B 1 175 ? 210.361 200.266 132.677 1.00 102.49 ?  194 ASN B O     1 
ATOM   7647  C  CB    . ASN B 1 175 ? 209.198 198.175 130.568 1.00 99.03  ?  194 ASN B CB    1 
ATOM   7648  C  CG    . ASN B 1 175 ? 209.841 197.442 131.725 1.00 99.29  ?  194 ASN B CG    1 
ATOM   7649  O  OD1   . ASN B 1 175 ? 209.386 197.540 132.864 1.00 100.81 ?  194 ASN B OD1   1 
ATOM   7650  N  ND2   . ASN B 1 175 ? 210.905 196.700 131.440 1.00 98.29  ?  194 ASN B ND2   1 
ATOM   7651  N  N     . THR B 1 176 ? 210.927 200.969 130.614 1.00 116.01 ?  195 THR B N     1 
ATOM   7652  C  CA    . THR B 1 176 ? 212.119 201.705 131.031 1.00 115.46 ?  195 THR B CA    1 
ATOM   7653  C  C     . THR B 1 176 ? 212.027 203.121 130.477 1.00 115.09 ?  195 THR B C     1 
ATOM   7654  O  O     . THR B 1 176 ? 212.767 203.493 129.558 1.00 115.69 ?  195 THR B O     1 
ATOM   7655  C  CB    . THR B 1 176 ? 213.394 201.014 130.545 1.00 114.29 ?  195 THR B CB    1 
ATOM   7656  O  OG1   . THR B 1 176 ? 213.601 201.312 129.159 1.00 113.34 ?  195 THR B OG1   1 
ATOM   7657  C  CG2   . THR B 1 176 ? 213.283 199.506 130.710 1.00 112.84 ?  195 THR B CG2   1 
ATOM   7658  N  N     . PRO B 1 177 ? 211.116 203.940 131.011 1.00 109.24 ?  196 PRO B N     1 
ATOM   7659  C  CA    . PRO B 1 177 ? 210.982 205.309 130.480 1.00 112.96 ?  196 PRO B CA    1 
ATOM   7660  C  C     . PRO B 1 177 ? 212.201 206.171 130.756 1.00 113.45 ?  196 PRO B C     1 
ATOM   7661  O  O     . PRO B 1 177 ? 212.747 206.789 129.832 1.00 111.48 ?  196 PRO B O     1 
ATOM   7662  C  CB    . PRO B 1 177 ? 209.722 205.834 131.191 1.00 110.79 ?  196 PRO B CB    1 
ATOM   7663  C  CG    . PRO B 1 177 ? 209.039 204.601 131.740 1.00 108.38 ?  196 PRO B CG    1 
ATOM   7664  C  CD    . PRO B 1 177 ? 210.162 203.693 132.102 1.00 103.08 ?  196 PRO B CD    1 
ATOM   7665  N  N     . GLU B 1 178 ? 212.647 206.227 132.009 1.00 115.25 ?  197 GLU B N     1 
ATOM   7666  C  CA    . GLU B 1 178 ? 213.865 206.949 132.354 1.00 114.53 ?  197 GLU B CA    1 
ATOM   7667  C  C     . GLU B 1 178 ? 214.778 206.070 133.199 1.00 114.98 ?  197 GLU B C     1 
ATOM   7668  O  O     . GLU B 1 178 ? 216.000 206.257 133.204 1.00 111.44 ?  197 GLU B O     1 
ATOM   7669  C  CB    . GLU B 1 178 ? 213.534 208.254 133.083 1.00 113.28 ?  197 GLU B CB    1 
ATOM   7670  C  CG    . GLU B 1 178 ? 212.868 208.074 134.439 1.00 113.64 ?  197 GLU B CG    1 
ATOM   7671  C  CD    . GLU B 1 178 ? 212.254 209.361 134.959 1.00 113.48 ?  197 GLU B CD    1 
ATOM   7672  O  OE1   . GLU B 1 178 ? 212.341 210.390 134.256 1.00 114.32 ?  197 GLU B OE1   1 
ATOM   7673  O  OE2   . GLU B 1 178 ? 211.686 209.343 136.071 1.00 112.43 -1 197 GLU B OE2   1 
ATOM   7674  N  N     . PHE B 1 179 ? 214.196 205.107 133.915 1.00 115.12 ?  198 PHE B N     1 
ATOM   7675  C  CA    . PHE B 1 179 ? 214.974 204.169 134.710 1.00 115.43 ?  198 PHE B CA    1 
ATOM   7676  C  C     . PHE B 1 179 ? 215.130 202.871 133.936 1.00 115.11 ?  198 PHE B C     1 
ATOM   7677  O  O     . PHE B 1 179 ? 214.118 202.217 133.638 1.00 116.19 ?  198 PHE B O     1 
ATOM   7678  C  CB    . PHE B 1 179 ? 214.298 203.907 136.050 1.00 113.54 ?  198 PHE B CB    1 
ATOM   7679  C  CG    . PHE B 1 179 ? 215.207 203.290 137.074 1.00 115.49 ?  198 PHE B CG    1 
ATOM   7680  C  CD1   . PHE B 1 179 ? 216.038 204.085 137.846 1.00 113.16 ?  198 PHE B CD1   1 
ATOM   7681  C  CD2   . PHE B 1 179 ? 215.239 201.918 137.259 1.00 115.38 ?  198 PHE B CD2   1 
ATOM   7682  C  CE1   . PHE B 1 179 ? 216.878 203.525 138.789 1.00 112.78 ?  198 PHE B CE1   1 
ATOM   7683  C  CE2   . PHE B 1 179 ? 216.078 201.351 138.200 1.00 114.05 ?  198 PHE B CE2   1 
ATOM   7684  C  CZ    . PHE B 1 179 ? 216.898 202.156 138.966 1.00 113.63 ?  198 PHE B CZ    1 
ATOM   7685  N  N     . PRO B 1 180 ? 216.353 202.462 133.587 1.00 114.37 ?  199 PRO B N     1 
ATOM   7686  C  CA    . PRO B 1 180 ? 216.498 201.259 132.750 1.00 115.08 ?  199 PRO B CA    1 
ATOM   7687  C  C     . PRO B 1 180 ? 216.105 199.975 133.458 1.00 114.37 ?  199 PRO B C     1 
ATOM   7688  O  O     . PRO B 1 180 ? 215.557 199.069 132.819 1.00 111.44 ?  199 PRO B O     1 
ATOM   7689  C  CB    . PRO B 1 180 ? 217.988 201.275 132.380 1.00 113.79 ?  199 PRO B CB    1 
ATOM   7690  C  CG    . PRO B 1 180 ? 218.641 202.010 133.505 1.00 112.26 ?  199 PRO B CG    1 
ATOM   7691  C  CD    . PRO B 1 180 ? 217.653 203.053 133.949 1.00 111.66 ?  199 PRO B CD    1 
ATOM   7692  N  N     . ALA B 1 181 ? 216.409 199.857 134.753 1.00 114.46 ?  200 ALA B N     1 
ATOM   7693  C  CA    . ALA B 1 181 ? 216.099 198.679 135.561 1.00 111.86 ?  200 ALA B CA    1 
ATOM   7694  C  C     . ALA B 1 181 ? 216.815 197.428 135.058 1.00 114.49 ?  200 ALA B C     1 
ATOM   7695  O  O     . ALA B 1 181 ? 216.638 196.342 135.620 1.00 116.29 ?  200 ALA B O     1 
ATOM   7696  C  CB    . ALA B 1 181 ? 214.586 198.439 135.614 1.00 111.08 ?  200 ALA B CB    1 
ATOM   7697  N  N     . ASP B 1 182 ? 217.623 197.574 134.004 1.00 112.15 ?  201 ASP B N     1 
ATOM   7698  C  CA    . ASP B 1 182 ? 218.487 196.507 133.493 1.00 112.12 ?  201 ASP B CA    1 
ATOM   7699  C  C     . ASP B 1 182 ? 217.700 195.243 133.147 1.00 112.04 ?  201 ASP B C     1 
ATOM   7700  O  O     . ASP B 1 182 ? 218.205 194.126 133.271 1.00 111.77 ?  201 ASP B O     1 
ATOM   7701  C  CB    . ASP B 1 182 ? 219.609 196.193 134.484 1.00 112.03 ?  201 ASP B CB    1 
ATOM   7702  C  CG    . ASP B 1 182 ? 220.349 197.437 134.937 1.00 113.16 ?  201 ASP B CG    1 
ATOM   7703  O  OD1   . ASP B 1 182 ? 220.839 198.189 134.068 1.00 113.35 ?  201 ASP B OD1   1 
ATOM   7704  O  OD2   . ASP B 1 182 ? 220.439 197.663 136.162 1.00 112.58 -1 201 ASP B OD2   1 
ATOM   7705  N  N     . ASN B 1 183 ? 216.453 195.416 132.697 1.00 104.34 ?  202 ASN B N     1 
ATOM   7706  C  CA    . ASN B 1 183 ? 215.631 194.272 132.322 1.00 104.58 ?  202 ASN B CA    1 
ATOM   7707  C  C     . ASN B 1 183 ? 214.851 194.490 131.029 1.00 102.64 ?  202 ASN B C     1 
ATOM   7708  O  O     . ASN B 1 183 ? 213.942 193.701 130.734 1.00 93.13  ?  202 ASN B O     1 
ATOM   7709  C  CB    . ASN B 1 183 ? 214.652 193.911 133.449 1.00 101.20 ?  202 ASN B CB    1 
ATOM   7710  C  CG    . ASN B 1 183 ? 215.349 193.621 134.765 1.00 96.32  ?  202 ASN B CG    1 
ATOM   7711  O  OD1   . ASN B 1 183 ? 216.304 192.848 134.818 1.00 94.83  ?  202 ASN B OD1   1 
ATOM   7712  N  ND2   . ASN B 1 183 ? 214.867 194.238 135.837 1.00 95.14  ?  202 ASN B ND2   1 
ATOM   7713  N  N     . ARG B 1 184 ? 215.168 195.527 130.249 1.00 110.88 ?  203 ARG B N     1 
ATOM   7714  C  CA    . ARG B 1 184 ? 214.450 195.744 128.997 1.00 110.62 ?  203 ARG B CA    1 
ATOM   7715  C  C     . ARG B 1 184 ? 214.735 194.629 127.997 1.00 107.41 ?  203 ARG B C     1 
ATOM   7716  O  O     . ARG B 1 184 ? 213.835 194.195 127.271 1.00 100.74 ?  203 ARG B O     1 
ATOM   7717  C  CB    . ARG B 1 184 ? 214.803 197.110 128.407 1.00 108.87 ?  203 ARG B CB    1 
ATOM   7718  C  CG    . ARG B 1 184 ? 216.284 197.351 128.171 1.00 108.53 ?  203 ARG B CG    1 
ATOM   7719  C  CD    . ARG B 1 184 ? 216.510 198.738 127.591 1.00 108.73 ?  203 ARG B CD    1 
ATOM   7720  N  NE    . ARG B 1 184 ? 215.984 198.846 126.236 1.00 108.28 ?  203 ARG B NE    1 
ATOM   7721  C  CZ    . ARG B 1 184 ? 215.814 199.989 125.586 1.00 108.00 ?  203 ARG B CZ    1 
ATOM   7722  N  NH1   . ARG B 1 184 ? 216.120 201.151 126.139 1.00 107.94 1  203 ARG B NH1   1 
ATOM   7723  N  NH2   . ARG B 1 184 ? 215.322 199.966 124.350 1.00 107.91 ?  203 ARG B NH2   1 
ATOM   7724  N  N     . ILE B 1 185 ? 215.979 194.147 127.950 1.00 113.90 ?  204 ILE B N     1 
ATOM   7725  C  CA    . ILE B 1 185 ? 216.304 193.032 127.068 1.00 114.68 ?  204 ILE B CA    1 
ATOM   7726  C  C     . ILE B 1 185 ? 215.578 191.768 127.515 1.00 113.78 ?  204 ILE B C     1 
ATOM   7727  O  O     . ILE B 1 185 ? 215.150 190.956 126.685 1.00 112.96 ?  204 ILE B O     1 
ATOM   7728  C  CB    . ILE B 1 185 ? 217.828 192.827 127.004 1.00 113.59 ?  204 ILE B CB    1 
ATOM   7729  C  CG1   . ILE B 1 185 ? 218.413 192.691 128.412 1.00 112.49 ?  204 ILE B CG1   1 
ATOM   7730  C  CG2   . ILE B 1 185 ? 218.487 193.978 126.258 1.00 111.14 ?  204 ILE B CG2   1 
ATOM   7731  C  CD1   . ILE B 1 185 ? 219.856 192.239 128.433 1.00 111.30 ?  204 ILE B CD1   1 
ATOM   7732  N  N     . ARG B 1 186 ? 215.432 191.579 128.829 1.00 95.18  ?  205 ARG B N     1 
ATOM   7733  C  CA    . ARG B 1 186 ? 214.641 190.461 129.332 1.00 92.01  ?  205 ARG B CA    1 
ATOM   7734  C  C     . ARG B 1 186 ? 213.189 190.574 128.892 1.00 95.02  ?  205 ARG B C     1 
ATOM   7735  O  O     . ARG B 1 186 ? 212.589 189.588 128.451 1.00 95.12  ?  205 ARG B O     1 
ATOM   7736  C  CB    . ARG B 1 186 ? 214.742 190.390 130.857 1.00 91.42  ?  205 ARG B CB    1 
ATOM   7737  C  CG    . ARG B 1 186 ? 213.917 189.280 131.506 1.00 91.24  ?  205 ARG B CG    1 
ATOM   7738  C  CD    . ARG B 1 186 ? 212.590 189.821 132.028 1.00 92.30  ?  205 ARG B CD    1 
ATOM   7739  N  NE    . ARG B 1 186 ? 211.769 188.798 132.665 1.00 89.82  ?  205 ARG B NE    1 
ATOM   7740  C  CZ    . ARG B 1 186 ? 210.514 188.983 133.049 1.00 87.23  ?  205 ARG B CZ    1 
ATOM   7741  N  NH1   . ARG B 1 186 ? 209.897 190.138 132.862 1.00 87.67  1  205 ARG B NH1   1 
ATOM   7742  N  NH2   . ARG B 1 186 ? 209.861 187.984 133.637 1.00 87.64  ?  205 ARG B NH2   1 
ATOM   7743  N  N     . LEU B 1 187 ? 212.606 191.771 129.003 1.00 104.13 ?  206 LEU B N     1 
ATOM   7744  C  CA    . LEU B 1 187 ? 211.220 191.964 128.592 1.00 106.25 ?  206 LEU B CA    1 
ATOM   7745  C  C     . LEU B 1 187 ? 211.049 191.886 127.080 1.00 108.57 ?  206 LEU B C     1 
ATOM   7746  O  O     . LEU B 1 187 ? 209.933 191.650 126.604 1.00 106.73 ?  206 LEU B O     1 
ATOM   7747  C  CB    . LEU B 1 187 ? 210.703 193.309 129.115 1.00 104.03 ?  206 LEU B CB    1 
ATOM   7748  C  CG    . LEU B 1 187 ? 209.199 193.595 129.054 1.00 100.35 ?  206 LEU B CG    1 
ATOM   7749  C  CD1   . LEU B 1 187 ? 208.739 194.322 130.304 1.00 102.55 ?  206 LEU B CD1   1 
ATOM   7750  C  CD2   . LEU B 1 187 ? 208.851 194.413 127.821 1.00 101.76 ?  206 LEU B CD2   1 
ATOM   7751  N  N     . GLN B 1 188 ? 212.124 192.072 126.316 1.00 110.48 ?  207 GLN B N     1 
ATOM   7752  C  CA    . GLN B 1 188 ? 212.033 192.038 124.859 1.00 106.03 ?  207 GLN B CA    1 
ATOM   7753  C  C     . GLN B 1 188 ? 212.229 190.630 124.300 1.00 100.78 ?  207 GLN B C     1 
ATOM   7754  O  O     . GLN B 1 188 ? 211.341 190.093 123.630 1.00 95.22  ?  207 GLN B O     1 
ATOM   7755  C  CB    . GLN B 1 188 ? 213.059 192.999 124.249 1.00 106.50 ?  207 GLN B CB    1 
ATOM   7756  C  CG    . GLN B 1 188 ? 213.259 192.817 122.754 1.00 106.82 ?  207 GLN B CG    1 
ATOM   7757  C  CD    . GLN B 1 188 ? 214.310 193.749 122.191 1.00 105.61 ?  207 GLN B CD    1 
ATOM   7758  O  OE1   . GLN B 1 188 ? 214.886 194.563 122.914 1.00 106.06 ?  207 GLN B OE1   1 
ATOM   7759  N  NE2   . GLN B 1 188 ? 214.571 193.634 120.894 1.00 104.29 ?  207 GLN B NE2   1 
ATOM   7760  N  N     . GLN B 1 189 ? 213.383 190.019 124.569 1.00 110.34 ?  208 GLN B N     1 
ATOM   7761  C  CA    . GLN B 1 189 ? 213.736 188.743 123.954 1.00 114.82 ?  208 GLN B CA    1 
ATOM   7762  C  C     . GLN B 1 189 ? 213.527 187.555 124.884 1.00 112.77 ?  208 GLN B C     1 
ATOM   7763  O  O     . GLN B 1 189 ? 212.838 186.598 124.517 1.00 110.82 ?  208 GLN B O     1 
ATOM   7764  C  CB    . GLN B 1 189 ? 215.193 188.773 123.476 1.00 114.96 ?  208 GLN B CB    1 
ATOM   7765  C  CG    . GLN B 1 189 ? 215.664 187.459 122.870 1.00 114.26 ?  208 GLN B CG    1 
ATOM   7766  C  CD    . GLN B 1 189 ? 217.129 187.485 122.483 1.00 112.39 ?  208 GLN B CD    1 
ATOM   7767  O  OE1   . GLN B 1 189 ? 217.478 187.280 121.320 1.00 111.20 ?  208 GLN B OE1   1 
ATOM   7768  N  NE2   . GLN B 1 189 ? 217.995 187.733 123.458 1.00 112.39 ?  208 GLN B NE2   1 
ATOM   7769  N  N     . LEU B 1 190 ? 214.116 187.589 126.082 1.00 110.29 ?  209 LEU B N     1 
ATOM   7770  C  CA    . LEU B 1 190 ? 213.965 186.471 127.008 1.00 109.53 ?  209 LEU B CA    1 
ATOM   7771  C  C     . LEU B 1 190 ? 212.518 186.295 127.447 1.00 107.33 ?  209 LEU B C     1 
ATOM   7772  O  O     . LEU B 1 190 ? 212.133 185.206 127.888 1.00 104.61 ?  209 LEU B O     1 
ATOM   7773  C  CB    . LEU B 1 190 ? 214.866 186.666 128.227 1.00 111.02 ?  209 LEU B CB    1 
ATOM   7774  C  CG    . LEU B 1 190 ? 216.300 187.131 127.963 1.00 109.60 ?  209 LEU B CG    1 
ATOM   7775  C  CD1   . LEU B 1 190 ? 217.061 187.291 129.270 1.00 108.32 ?  209 LEU B CD1   1 
ATOM   7776  C  CD2   . LEU B 1 190 ? 217.019 186.164 127.034 1.00 109.13 ?  209 LEU B CD2   1 
ATOM   7777  N  N     . LEU B 1 191 ? 211.704 187.347 127.338 1.00 96.66  ?  210 LEU B N     1 
ATOM   7778  C  CA    . LEU B 1 191 ? 210.332 187.270 127.827 1.00 100.16 ?  210 LEU B CA    1 
ATOM   7779  C  C     . LEU B 1 191 ? 209.498 186.325 126.970 1.00 101.28 ?  210 LEU B C     1 
ATOM   7780  O  O     . LEU B 1 191 ? 208.650 185.588 127.488 1.00 104.69 ?  210 LEU B O     1 
ATOM   7781  C  CB    . LEU B 1 191 ? 209.711 188.667 127.863 1.00 94.01  ?  210 LEU B CB    1 
ATOM   7782  C  CG    . LEU B 1 191 ? 208.437 188.811 128.686 1.00 97.61  ?  210 LEU B CG    1 
ATOM   7783  C  CD1   . LEU B 1 191 ? 208.798 188.540 130.116 1.00 94.90  ?  210 LEU B CD1   1 
ATOM   7784  C  CD2   . LEU B 1 191 ? 207.852 190.201 128.569 1.00 98.51  ?  210 LEU B CD2   1 
ATOM   7785  N  N     . TRP B 1 192 ? 209.727 186.328 125.656 1.00 91.01  ?  211 TRP B N     1 
ATOM   7786  C  CA    . TRP B 1 192 ? 209.043 185.417 124.746 1.00 89.69  ?  211 TRP B CA    1 
ATOM   7787  C  C     . TRP B 1 192 ? 209.819 184.133 124.483 1.00 93.78  ?  211 TRP B C     1 
ATOM   7788  O  O     . TRP B 1 192 ? 209.328 183.274 123.743 1.00 93.84  ?  211 TRP B O     1 
ATOM   7789  C  CB    . TRP B 1 192 ? 208.754 186.103 123.406 1.00 85.34  ?  211 TRP B CB    1 
ATOM   7790  C  CG    . TRP B 1 192 ? 207.487 186.892 123.405 1.00 83.87  ?  211 TRP B CG    1 
ATOM   7791  C  CD1   . TRP B 1 192 ? 206.322 186.570 122.773 1.00 87.77  ?  211 TRP B CD1   1 
ATOM   7792  C  CD2   . TRP B 1 192 ? 207.262 188.155 124.040 1.00 86.35  ?  211 TRP B CD2   1 
ATOM   7793  N  NE1   . TRP B 1 192 ? 205.378 187.542 122.996 1.00 92.46  ?  211 TRP B NE1   1 
ATOM   7794  C  CE2   . TRP B 1 192 ? 205.932 188.528 123.768 1.00 89.56  ?  211 TRP B CE2   1 
ATOM   7795  C  CE3   . TRP B 1 192 ? 208.053 189.002 124.816 1.00 86.17  ?  211 TRP B CE3   1 
ATOM   7796  C  CZ2   . TRP B 1 192 ? 205.376 189.708 124.253 1.00 86.71  ?  211 TRP B CZ2   1 
ATOM   7797  C  CZ3   . TRP B 1 192 ? 207.503 190.176 125.284 1.00 85.71  ?  211 TRP B CZ3   1 
ATOM   7798  C  CH2   . TRP B 1 192 ? 206.178 190.519 125.003 1.00 84.73  ?  211 TRP B CH2   1 
ATOM   7799  N  N     . LYS B 1 193 ? 211.014 183.982 125.054 1.00 110.30 ?  212 LYS B N     1 
ATOM   7800  C  CA    . LYS B 1 193 ? 211.816 182.787 124.825 1.00 111.23 ?  212 LYS B CA    1 
ATOM   7801  C  C     . LYS B 1 193 ? 211.617 181.744 125.921 1.00 110.09 ?  212 LYS B C     1 
ATOM   7802  O  O     . LYS B 1 193 ? 211.382 180.568 125.626 1.00 109.03 ?  212 LYS B O     1 
ATOM   7803  C  CB    . LYS B 1 193 ? 213.296 183.164 124.709 1.00 108.85 ?  212 LYS B CB    1 
ATOM   7804  C  CG    . LYS B 1 193 ? 214.188 182.035 124.219 1.00 107.17 ?  212 LYS B CG    1 
ATOM   7805  C  CD    . LYS B 1 193 ? 215.649 182.457 124.183 1.00 107.86 ?  212 LYS B CD    1 
ATOM   7806  C  CE    . LYS B 1 193 ? 216.172 182.781 125.573 1.00 108.12 ?  212 LYS B CE    1 
ATOM   7807  N  NZ    . LYS B 1 193 ? 217.624 183.118 125.553 1.00 107.84 1  212 LYS B NZ    1 
ATOM   7808  N  N     . THR B 1 194 ? 211.712 182.156 127.182 1.00 104.11 ?  213 THR B N     1 
ATOM   7809  C  CA    . THR B 1 194 ? 211.548 181.238 128.298 1.00 103.47 ?  213 THR B CA    1 
ATOM   7810  C  C     . THR B 1 194 ? 210.066 181.051 128.619 1.00 99.90  ?  213 THR B C     1 
ATOM   7811  O  O     . THR B 1 194 ? 209.178 181.535 127.910 1.00 96.48  ?  213 THR B O     1 
ATOM   7812  C  CB    . THR B 1 194 ? 212.321 181.739 129.516 1.00 102.37 ?  213 THR B CB    1 
ATOM   7813  O  OG1   . THR B 1 194 ? 212.395 180.700 130.500 1.00 101.82 ?  213 THR B OG1   1 
ATOM   7814  C  CG2   . THR B 1 194 ? 211.643 182.963 130.123 1.00 97.11  ?  213 THR B CG2   1 
ATOM   7815  N  N     . ALA B 1 195 ? 209.794 180.336 129.709 1.00 76.91  ?  214 ALA B N     1 
ATOM   7816  C  CA    . ALA B 1 195 ? 208.435 180.059 130.148 1.00 73.26  ?  214 ALA B CA    1 
ATOM   7817  C  C     . ALA B 1 195 ? 208.336 180.238 131.655 1.00 71.01  ?  214 ALA B C     1 
ATOM   7818  O  O     . ALA B 1 195 ? 209.249 179.855 132.393 1.00 75.27  ?  214 ALA B O     1 
ATOM   7819  C  CB    . ALA B 1 195 ? 208.004 178.639 129.759 1.00 74.91  ?  214 ALA B CB    1 
ATOM   7820  N  N     . ARG B 1 196 ? 207.222 180.822 132.102 1.00 57.38  ?  215 ARG B N     1 
ATOM   7821  C  CA    . ARG B 1 196 ? 206.931 181.011 133.525 1.00 58.74  ?  215 ARG B CA    1 
ATOM   7822  C  C     . ARG B 1 196 ? 208.031 181.825 134.209 1.00 60.77  ?  215 ARG B C     1 
ATOM   7823  O  O     . ARG B 1 196 ? 208.760 181.335 135.075 1.00 65.83  ?  215 ARG B O     1 
ATOM   7824  C  CB    . ARG B 1 196 ? 206.728 179.663 134.226 1.00 65.26  ?  215 ARG B CB    1 
ATOM   7825  C  CG    . ARG B 1 196 ? 205.366 179.026 133.992 1.00 66.29  ?  215 ARG B CG    1 
ATOM   7826  C  CD    . ARG B 1 196 ? 204.290 179.659 134.862 1.00 68.30  ?  215 ARG B CD    1 
ATOM   7827  N  NE    . ARG B 1 196 ? 203.158 178.765 135.082 1.00 71.21  ?  215 ARG B NE    1 
ATOM   7828  C  CZ    . ARG B 1 196 ? 202.265 178.436 134.158 1.00 69.09  ?  215 ARG B CZ    1 
ATOM   7829  N  NH1   . ARG B 1 196 ? 202.342 178.904 132.923 1.00 66.75  1  215 ARG B NH1   1 
ATOM   7830  N  NH2   . ARG B 1 196 ? 201.267 177.618 134.482 1.00 64.76  ?  215 ARG B NH2   1 
ATOM   7831  N  N     . ASP B 1 197 ? 208.146 183.084 133.802 1.00 53.34  ?  216 ASP B N     1 
ATOM   7832  C  CA    . ASP B 1 197 ? 209.173 183.971 134.330 1.00 52.78  ?  216 ASP B CA    1 
ATOM   7833  C  C     . ASP B 1 197 ? 208.532 185.061 135.182 1.00 53.58  ?  216 ASP B C     1 
ATOM   7834  O  O     . ASP B 1 197 ? 207.309 185.209 135.225 1.00 56.67  ?  216 ASP B O     1 
ATOM   7835  C  CB    . ASP B 1 197 ? 210.003 184.576 133.190 1.00 61.47  ?  216 ASP B CB    1 
ATOM   7836  C  CG    . ASP B 1 197 ? 211.370 185.041 133.647 1.00 66.45  ?  216 ASP B CG    1 
ATOM   7837  O  OD1   . ASP B 1 197 ? 212.254 184.182 133.844 1.00 64.65  ?  216 ASP B OD1   1 
ATOM   7838  O  OD2   . ASP B 1 197 ? 211.564 186.264 133.806 1.00 68.43  -1 216 ASP B OD2   1 
ATOM   7839  N  N     . GLN B 1 198 ? 209.373 185.829 135.872 1.00 55.66  ?  217 GLN B N     1 
ATOM   7840  C  CA    . GLN B 1 198 ? 208.884 186.882 136.755 1.00 53.07  ?  217 GLN B CA    1 
ATOM   7841  C  C     . GLN B 1 198 ? 210.057 187.727 137.227 1.00 57.25  ?  217 GLN B C     1 
ATOM   7842  O  O     . GLN B 1 198 ? 211.176 187.226 137.372 1.00 61.05  ?  217 GLN B O     1 
ATOM   7843  C  CB    . GLN B 1 198 ? 208.140 186.297 137.962 1.00 55.36  ?  217 GLN B CB    1 
ATOM   7844  C  CG    . GLN B 1 198 ? 208.906 185.201 138.683 1.00 53.89  ?  217 GLN B CG    1 
ATOM   7845  C  CD    . GLN B 1 198 ? 208.161 184.663 139.886 1.00 54.87  ?  217 GLN B CD    1 
ATOM   7846  O  OE1   . GLN B 1 198 ? 207.158 185.232 140.317 1.00 56.38  ?  217 GLN B OE1   1 
ATOM   7847  N  NE2   . GLN B 1 198 ? 208.648 183.556 140.434 1.00 55.08  ?  217 GLN B NE2   1 
ATOM   7848  N  N     . ASP B 1 199 ? 209.786 189.008 137.467 1.00 56.39  ?  218 ASP B N     1 
ATOM   7849  C  CA    . ASP B 1 199 ? 210.766 189.911 138.061 1.00 58.26  ?  218 ASP B CA    1 
ATOM   7850  C  C     . ASP B 1 199 ? 210.044 191.168 138.541 1.00 56.87  ?  218 ASP B C     1 
ATOM   7851  O  O     . ASP B 1 199 ? 208.811 191.257 138.500 1.00 62.98  ?  218 ASP B O     1 
ATOM   7852  C  CB    . ASP B 1 199 ? 211.891 190.241 137.075 1.00 62.98  ?  218 ASP B CB    1 
ATOM   7853  C  CG    . ASP B 1 199 ? 211.373 190.730 135.742 1.00 67.92  ?  218 ASP B CG    1 
ATOM   7854  O  OD1   . ASP B 1 199 ? 210.140 190.739 135.545 1.00 62.77  ?  218 ASP B OD1   1 
ATOM   7855  O  OD2   . ASP B 1 199 ? 212.204 191.107 134.891 1.00 72.52  -1 218 ASP B OD2   1 
ATOM   7856  N  N     . GLU B 1 200 ? 210.828 192.144 138.999 1.00 55.87  ?  219 GLU B N     1 
ATOM   7857  C  CA    . GLU B 1 200 ? 210.335 193.388 139.571 1.00 58.01  ?  219 GLU B CA    1 
ATOM   7858  C  C     . GLU B 1 200 ? 210.913 194.567 138.800 1.00 56.79  ?  219 GLU B C     1 
ATOM   7859  O  O     . GLU B 1 200 ? 212.086 194.552 138.413 1.00 56.38  ?  219 GLU B O     1 
ATOM   7860  C  CB    . GLU B 1 200 ? 210.709 193.488 141.053 1.00 53.28  ?  219 GLU B CB    1 
ATOM   7861  C  CG    . GLU B 1 200 ? 210.490 192.196 141.823 1.00 54.58  ?  219 GLU B CG    1 
ATOM   7862  C  CD    . GLU B 1 200 ? 211.107 192.224 143.206 1.00 59.43  ?  219 GLU B CD    1 
ATOM   7863  O  OE1   . GLU B 1 200 ? 212.336 192.426 143.303 1.00 63.90  ?  219 GLU B OE1   1 
ATOM   7864  O  OE2   . GLU B 1 200 ? 210.367 192.043 144.194 1.00 58.34  -1 219 GLU B OE2   1 
ATOM   7865  N  N     . PHE B 1 201 ? 210.088 195.594 138.590 1.00 65.37  ?  220 PHE B N     1 
ATOM   7866  C  CA    . PHE B 1 201 ? 210.442 196.708 137.719 1.00 63.22  ?  220 PHE B CA    1 
ATOM   7867  C  C     . PHE B 1 201 ? 210.289 198.059 138.402 1.00 68.12  ?  220 PHE B C     1 
ATOM   7868  O  O     . PHE B 1 201 ? 210.001 198.138 139.600 1.00 69.91  ?  220 PHE B O     1 
ATOM   7869  C  CB    . PHE B 1 201 ? 209.569 196.694 136.462 1.00 66.83  ?  220 PHE B CB    1 
ATOM   7870  C  CG    . PHE B 1 201 ? 209.896 195.594 135.502 1.00 62.76  ?  220 PHE B CG    1 
ATOM   7871  C  CD1   . PHE B 1 201 ? 211.164 195.050 135.458 1.00 66.00  ?  220 PHE B CD1   1 
ATOM   7872  C  CD2   . PHE B 1 201 ? 208.929 195.097 134.646 1.00 62.10  ?  220 PHE B CD2   1 
ATOM   7873  C  CE1   . PHE B 1 201 ? 211.464 194.039 134.574 1.00 68.31  ?  220 PHE B CE1   1 
ATOM   7874  C  CE2   . PHE B 1 201 ? 209.226 194.084 133.758 1.00 62.40  ?  220 PHE B CE2   1 
ATOM   7875  C  CZ    . PHE B 1 201 ? 210.495 193.553 133.723 1.00 67.54  ?  220 PHE B CZ    1 
ATOM   7876  N  N     . LEU B 1 202 ? 210.480 199.125 137.627 1.00 69.69  ?  221 LEU B N     1 
ATOM   7877  C  CA    . LEU B 1 202 ? 210.160 200.491 138.026 1.00 62.86  ?  221 LEU B CA    1 
ATOM   7878  C  C     . LEU B 1 202 ? 209.377 201.174 136.916 1.00 63.90  ?  221 LEU B C     1 
ATOM   7879  O  O     . LEU B 1 202 ? 209.605 202.345 136.594 1.00 68.52  ?  221 LEU B O     1 
ATOM   7880  C  CB    . LEU B 1 202 ? 211.420 201.285 138.371 1.00 63.85  ?  221 LEU B CB    1 
ATOM   7881  C  CG    . LEU B 1 202 ? 211.961 201.110 139.792 1.00 67.48  ?  221 LEU B CG    1 
ATOM   7882  C  CD1   . LEU B 1 202 ? 213.098 202.083 140.066 1.00 72.43  ?  221 LEU B CD1   1 
ATOM   7883  C  CD2   . LEU B 1 202 ? 210.846 201.287 140.809 1.00 63.79  ?  221 LEU B CD2   1 
ATOM   7884  N  N     . LEU B 1 203 ? 208.453 200.432 136.305 1.00 64.14  ?  222 LEU B N     1 
ATOM   7885  C  CA    . LEU B 1 203 ? 207.655 200.950 135.202 1.00 66.86  ?  222 LEU B CA    1 
ATOM   7886  C  C     . LEU B 1 203 ? 206.848 202.160 135.660 1.00 75.30  ?  222 LEU B C     1 
ATOM   7887  O  O     . LEU B 1 203 ? 206.205 202.132 136.713 1.00 81.83  ?  222 LEU B O     1 
ATOM   7888  C  CB    . LEU B 1 203 ? 206.740 199.843 134.671 1.00 70.04  ?  222 LEU B CB    1 
ATOM   7889  C  CG    . LEU B 1 203 ? 206.093 199.940 133.287 1.00 71.75  ?  222 LEU B CG    1 
ATOM   7890  C  CD1   . LEU B 1 203 ? 205.792 198.545 132.765 1.00 69.63  ?  222 LEU B CD1   1 
ATOM   7891  C  CD2   . LEU B 1 203 ? 204.821 200.758 133.319 1.00 70.38  ?  222 LEU B CD2   1 
ATOM   7892  N  N     . LEU B 1 204 ? 206.886 203.226 134.863 1.00 79.80  ?  223 LEU B N     1 
ATOM   7893  C  CA    . LEU B 1 204 ? 206.310 204.502 135.255 1.00 78.94  ?  223 LEU B CA    1 
ATOM   7894  C  C     . LEU B 1 204 ? 204.848 204.594 134.819 1.00 81.06  ?  223 LEU B C     1 
ATOM   7895  O  O     . LEU B 1 204 ? 204.303 203.700 134.170 1.00 81.77  ?  223 LEU B O     1 
ATOM   7896  C  CB    . LEU B 1 204 ? 207.131 205.653 134.675 1.00 76.19  ?  223 LEU B CB    1 
ATOM   7897  C  CG    . LEU B 1 204 ? 208.572 205.783 135.176 1.00 81.19  ?  223 LEU B CG    1 
ATOM   7898  C  CD1   . LEU B 1 204 ? 209.156 207.131 134.782 1.00 80.94  ?  223 LEU B CD1   1 
ATOM   7899  C  CD2   . LEU B 1 204 ? 208.640 205.585 136.682 1.00 79.46  ?  223 LEU B CD2   1 
ATOM   7900  N  N     . THR B 1 205 ? 204.206 205.697 135.182 1.00 69.89  ?  224 THR B N     1 
ATOM   7901  C  CA    . THR B 1 205 ? 202.795 205.930 134.910 1.00 63.60  ?  224 THR B CA    1 
ATOM   7902  C  C     . THR B 1 205 ? 202.645 207.177 134.038 1.00 68.47  ?  224 THR B C     1 
ATOM   7903  O  O     . THR B 1 205 ? 203.624 207.721 133.520 1.00 75.50  ?  224 THR B O     1 
ATOM   7904  C  CB    . THR B 1 205 ? 202.013 206.065 136.218 1.00 61.25  ?  224 THR B CB    1 
ATOM   7905  O  OG1   . THR B 1 205 ? 202.686 206.987 137.085 1.00 62.01  ?  224 THR B OG1   1 
ATOM   7906  C  CG2   . THR B 1 205 ? 201.915 204.720 136.916 1.00 67.04  ?  224 THR B CG2   1 
ATOM   7907  N  N     . ARG B 1 206 ? 201.396 207.617 133.865 1.00 59.90  ?  225 ARG B N     1 
ATOM   7908  C  CA    . ARG B 1 206 ? 201.144 208.887 133.192 1.00 57.41  ?  225 ARG B CA    1 
ATOM   7909  C  C     . ARG B 1 206 ? 201.829 210.031 133.930 1.00 59.96  ?  225 ARG B C     1 
ATOM   7910  O  O     . ARG B 1 206 ? 202.439 210.911 133.312 1.00 62.19  ?  225 ARG B O     1 
ATOM   7911  C  CB    . ARG B 1 206 ? 199.639 209.137 133.091 1.00 52.14  ?  225 ARG B CB    1 
ATOM   7912  C  CG    . ARG B 1 206 ? 198.920 208.298 132.048 1.00 53.45  ?  225 ARG B CG    1 
ATOM   7913  C  CD    . ARG B 1 206 ? 199.364 208.661 130.642 1.00 60.82  ?  225 ARG B CD    1 
ATOM   7914  N  NE    . ARG B 1 206 ? 198.601 207.947 129.625 1.00 65.37  ?  225 ARG B NE    1 
ATOM   7915  C  CZ    . ARG B 1 206 ? 197.373 208.271 129.240 1.00 62.02  ?  225 ARG B CZ    1 
ATOM   7916  N  NH1   . ARG B 1 206 ? 196.729 209.298 129.770 1.00 59.66  1  225 ARG B NH1   1 
ATOM   7917  N  NH2   . ARG B 1 206 ? 196.778 207.546 128.298 1.00 60.23  ?  225 ARG B NH2   1 
ATOM   7918  N  N     . THR B 1 207 ? 201.731 210.037 135.261 1.00 64.53  ?  226 THR B N     1 
ATOM   7919  C  CA    . THR B 1 207 ? 202.427 211.044 136.053 1.00 64.77  ?  226 THR B CA    1 
ATOM   7920  C  C     . THR B 1 207 ? 203.938 210.856 135.986 1.00 65.67  ?  226 THR B C     1 
ATOM   7921  O  O     . THR B 1 207 ? 204.689 211.836 135.920 1.00 69.52  ?  226 THR B O     1 
ATOM   7922  C  CB    . THR B 1 207 ? 201.945 210.998 137.503 1.00 68.87  ?  226 THR B CB    1 
ATOM   7923  O  OG1   . THR B 1 207 ? 200.517 210.888 137.528 1.00 68.67  ?  226 THR B OG1   1 
ATOM   7924  C  CG2   . THR B 1 207 ? 202.364 212.259 138.244 1.00 66.84  ?  226 THR B CG2   1 
ATOM   7925  N  N     . GLY B 1 208 ? 204.402 209.609 135.999 1.00 70.91  ?  227 GLY B N     1 
ATOM   7926  C  CA    . GLY B 1 208 ? 205.818 209.315 135.954 1.00 75.94  ?  227 GLY B CA    1 
ATOM   7927  C  C     . GLY B 1 208 ? 206.455 208.944 137.275 1.00 80.60  ?  227 GLY B C     1 
ATOM   7928  O  O     . GLY B 1 208 ? 207.684 208.820 137.332 1.00 81.05  ?  227 GLY B O     1 
ATOM   7929  N  N     . GLU B 1 209 ? 205.668 208.767 138.332 1.00 74.86  ?  228 GLU B N     1 
ATOM   7930  C  CA    . GLU B 1 209 ? 206.218 208.412 139.632 1.00 73.20  ?  228 GLU B CA    1 
ATOM   7931  C  C     . GLU B 1 209 ? 206.760 206.985 139.618 1.00 76.58  ?  228 GLU B C     1 
ATOM   7932  O  O     . GLU B 1 209 ? 206.231 206.100 138.940 1.00 73.55  ?  228 GLU B O     1 
ATOM   7933  C  CB    . GLU B 1 209 ? 205.150 208.566 140.715 1.00 68.84  ?  228 GLU B CB    1 
ATOM   7934  C  CG    . GLU B 1 209 ? 205.702 208.879 142.096 1.00 73.96  ?  228 GLU B CG    1 
ATOM   7935  C  CD    . GLU B 1 209 ? 205.902 207.639 142.938 1.00 77.69  ?  228 GLU B CD    1 
ATOM   7936  O  OE1   . GLU B 1 209 ? 206.488 207.750 144.035 1.00 79.68  ?  228 GLU B OE1   1 
ATOM   7937  O  OE2   . GLU B 1 209 ? 205.466 206.553 142.503 1.00 74.79  -1 228 GLU B OE2   1 
ATOM   7938  N  N     . LYS B 1 210 ? 207.830 206.767 140.379 1.00 79.94  ?  229 LYS B N     1 
ATOM   7939  C  CA    . LYS B 1 210 ? 208.520 205.483 140.406 1.00 80.82  ?  229 LYS B CA    1 
ATOM   7940  C  C     . LYS B 1 210 ? 207.793 204.509 141.326 1.00 81.03  ?  229 LYS B C     1 
ATOM   7941  O  O     . LYS B 1 210 ? 207.623 204.781 142.518 1.00 76.92  ?  229 LYS B O     1 
ATOM   7942  C  CB    . LYS B 1 210 ? 209.967 205.665 140.870 1.00 80.60  ?  229 LYS B CB    1 
ATOM   7943  C  CG    . LYS B 1 210 ? 210.724 206.761 140.136 1.00 79.96  ?  229 LYS B CG    1 
ATOM   7944  C  CD    . LYS B 1 210 ? 212.220 206.491 140.127 1.00 81.58  ?  229 LYS B CD    1 
ATOM   7945  C  CE    . LYS B 1 210 ? 212.976 207.611 139.431 1.00 81.16  ?  229 LYS B CE    1 
ATOM   7946  N  NZ    . LYS B 1 210 ? 213.258 208.749 140.350 1.00 78.10  1  229 LYS B NZ    1 
ATOM   7947  N  N     . ILE B 1 211 ? 207.375 203.372 140.771 1.00 72.17  ?  230 ILE B N     1 
ATOM   7948  C  CA    . ILE B 1 211 ? 206.649 202.352 141.519 1.00 66.96  ?  230 ILE B CA    1 
ATOM   7949  C  C     . ILE B 1 211 ? 207.245 200.986 141.209 1.00 60.16  ?  230 ILE B C     1 
ATOM   7950  O  O     . ILE B 1 211 ? 207.588 200.691 140.060 1.00 64.84  ?  230 ILE B O     1 
ATOM   7951  C  CB    . ILE B 1 211 ? 205.140 202.373 141.201 1.00 63.05  ?  230 ILE B CB    1 
ATOM   7952  C  CG1   . ILE B 1 211 ? 204.908 202.492 139.695 1.00 57.05  ?  230 ILE B CG1   1 
ATOM   7953  C  CG2   . ILE B 1 211 ? 204.448 203.504 141.947 1.00 65.44  ?  230 ILE B CG2   1 
ATOM   7954  C  CD1   . ILE B 1 211 ? 203.459 202.348 139.292 1.00 60.26  ?  230 ILE B CD1   1 
ATOM   7955  N  N     . TRP B 1 212 ? 207.365 200.153 142.240 1.00 54.20  ?  231 TRP B N     1 
ATOM   7956  C  CA    . TRP B 1 212 ? 207.889 198.800 142.101 1.00 61.47  ?  231 TRP B CA    1 
ATOM   7957  C  C     . TRP B 1 212 ? 206.740 197.854 141.771 1.00 61.83  ?  231 TRP B C     1 
ATOM   7958  O  O     . TRP B 1 212 ? 205.812 197.694 142.573 1.00 67.13  ?  231 TRP B O     1 
ATOM   7959  C  CB    . TRP B 1 212 ? 208.596 198.369 143.386 1.00 62.97  ?  231 TRP B CB    1 
ATOM   7960  C  CG    . TRP B 1 212 ? 209.790 199.210 143.723 1.00 65.35  ?  231 TRP B CG    1 
ATOM   7961  C  CD1   . TRP B 1 212 ? 211.089 198.969 143.382 1.00 64.37  ?  231 TRP B CD1   1 
ATOM   7962  C  CD2   . TRP B 1 212 ? 209.793 200.435 144.468 1.00 67.37  ?  231 TRP B CD2   1 
ATOM   7963  N  NE1   . TRP B 1 212 ? 211.900 199.966 143.869 1.00 62.66  ?  231 TRP B NE1   1 
ATOM   7964  C  CE2   . TRP B 1 212 ? 211.128 200.879 144.539 1.00 64.51  ?  231 TRP B CE2   1 
ATOM   7965  C  CE3   . TRP B 1 212 ? 208.795 201.200 145.081 1.00 65.93  ?  231 TRP B CE3   1 
ATOM   7966  C  CZ2   . TRP B 1 212 ? 211.492 202.052 145.200 1.00 64.61  ?  231 TRP B CZ2   1 
ATOM   7967  C  CZ3   . TRP B 1 212 ? 209.158 202.364 145.737 1.00 63.43  ?  231 TRP B CZ3   1 
ATOM   7968  C  CH2   . TRP B 1 212 ? 210.495 202.778 145.791 1.00 65.36  ?  231 TRP B CH2   1 
ATOM   7969  N  N     . ILE B 1 213 ? 206.803 197.226 140.598 1.00 33.75  ?  232 ILE B N     1 
ATOM   7970  C  CA    . ILE B 1 213 ? 205.719 196.401 140.074 1.00 26.71  ?  232 ILE B CA    1 
ATOM   7971  C  C     . ILE B 1 213 ? 206.271 195.029 139.710 1.00 42.98  ?  232 ILE B C     1 
ATOM   7972  O  O     . ILE B 1 213 ? 207.324 194.931 139.071 1.00 45.79  ?  232 ILE B O     1 
ATOM   7973  C  CB    . ILE B 1 213 ? 205.055 197.052 138.847 1.00 27.83  ?  232 ILE B CB    1 
ATOM   7974  C  CG1   . ILE B 1 213 ? 204.704 198.514 139.128 1.00 49.34  ?  232 ILE B CG1   1 
ATOM   7975  C  CG2   . ILE B 1 213 ? 203.812 196.280 138.449 1.00 39.43  ?  232 ILE B CG2   1 
ATOM   7976  C  CD1   . ILE B 1 213 ? 203.704 198.700 140.242 1.00 56.30  ?  232 ILE B CD1   1 
ATOM   7977  N  N     . LYS B 1 214 ? 205.559 193.976 140.107 1.00 54.49  ?  233 LYS B N     1 
ATOM   7978  C  CA    . LYS B 1 214 ? 205.871 192.630 139.644 1.00 47.59  ?  233 LYS B CA    1 
ATOM   7979  C  C     . LYS B 1 214 ? 205.394 192.443 138.210 1.00 47.28  ?  233 LYS B C     1 
ATOM   7980  O  O     . LYS B 1 214 ? 204.446 193.091 137.759 1.00 58.69  ?  233 LYS B O     1 
ATOM   7981  C  CB    . LYS B 1 214 ? 205.221 191.579 140.545 1.00 43.79  ?  233 LYS B CB    1 
ATOM   7982  C  CG    . LYS B 1 214 ? 205.834 191.471 141.926 1.00 45.05  ?  233 LYS B CG    1 
ATOM   7983  C  CD    . LYS B 1 214 ? 207.152 190.718 141.880 1.00 51.13  ?  233 LYS B CD    1 
ATOM   7984  C  CE    . LYS B 1 214 ? 206.928 189.228 141.686 1.00 49.55  ?  233 LYS B CE    1 
ATOM   7985  N  NZ    . LYS B 1 214 ? 206.271 188.604 142.867 1.00 49.46  1  233 LYS B NZ    1 
ATOM   7986  N  N     . ALA B 1 215 ? 206.060 191.545 137.491 1.00 30.77  ?  234 ALA B N     1 
ATOM   7987  C  CA    . ALA B 1 215 ? 205.779 191.352 136.070 1.00 36.31  ?  234 ALA B CA    1 
ATOM   7988  C  C     . ALA B 1 215 ? 205.664 189.868 135.735 1.00 43.16  ?  234 ALA B C     1 
ATOM   7989  O  O     . ALA B 1 215 ? 206.302 189.371 134.807 1.00 55.22  ?  234 ALA B O     1 
ATOM   7990  C  CB    . ALA B 1 215 ? 206.849 192.022 135.214 1.00 50.30  ?  234 ALA B CB    1 
ATOM   7991  N  N     . SER B 1 216 ? 204.850 189.135 136.497 1.00 39.65  ?  235 SER B N     1 
ATOM   7992  C  CA    . SER B 1 216 ? 204.772 187.690 136.301 1.00 45.00  ?  235 SER B CA    1 
ATOM   7993  C  C     . SER B 1 216 ? 204.260 187.375 134.902 1.00 32.60  ?  235 SER B C     1 
ATOM   7994  O  O     . SER B 1 216 ? 203.215 187.876 134.488 1.00 41.37  ?  235 SER B O     1 
ATOM   7995  C  CB    . SER B 1 216 ? 203.862 187.059 137.355 1.00 51.69  ?  235 SER B CB    1 
ATOM   7996  O  OG    . SER B 1 216 ? 204.473 187.074 138.632 1.00 51.20  ?  235 SER B OG    1 
ATOM   7997  N  N     . ILE B 1 217 ? 204.996 186.545 134.168 1.00 34.68  ?  236 ILE B N     1 
ATOM   7998  C  CA    . ILE B 1 217 ? 204.713 186.270 132.765 1.00 41.53  ?  236 ILE B CA    1 
ATOM   7999  C  C     . ILE B 1 217 ? 204.601 184.764 132.573 1.00 47.37  ?  236 ILE B C     1 
ATOM   8000  O  O     . ILE B 1 217 ? 205.450 184.001 133.056 1.00 60.99  ?  236 ILE B O     1 
ATOM   8001  C  CB    . ILE B 1 217 ? 205.790 186.870 131.843 1.00 49.08  ?  236 ILE B CB    1 
ATOM   8002  C  CG1   . ILE B 1 217 ? 205.505 186.522 130.381 1.00 47.25  ?  236 ILE B CG1   1 
ATOM   8003  C  CG2   . ILE B 1 217 ? 207.170 186.409 132.263 1.00 55.25  ?  236 ILE B CG2   1 
ATOM   8004  C  CD1   . ILE B 1 217 ? 204.243 187.157 129.845 1.00 54.23  ?  236 ILE B CD1   1 
ATOM   8005  N  N     . SER B 1 218 ? 203.541 184.339 131.879 1.00 40.64  ?  237 SER B N     1 
ATOM   8006  C  CA    . SER B 1 218 ? 203.284 182.934 131.615 1.00 42.79  ?  237 SER B CA    1 
ATOM   8007  C  C     . SER B 1 218 ? 202.840 182.758 130.167 1.00 42.40  ?  237 SER B C     1 
ATOM   8008  O  O     . SER B 1 218 ? 201.987 183.526 129.682 1.00 50.44  ?  237 SER B O     1 
ATOM   8009  C  CB    . SER B 1 218 ? 202.222 182.383 132.569 1.00 47.39  ?  237 SER B CB    1 
ATOM   8010  O  OG    . SER B 1 218 ? 201.944 181.023 132.289 1.00 51.93  ?  237 SER B OG    1 
ATOM   8011  N  N     . PRO B 1 219 ? 203.382 181.770 129.454 1.00 36.60  ?  238 PRO B N     1 
ATOM   8012  C  CA    . PRO B 1 219 ? 202.965 181.531 128.069 1.00 35.99  ?  238 PRO B CA    1 
ATOM   8013  C  C     . PRO B 1 219 ? 201.792 180.569 127.975 1.00 37.76  ?  238 PRO B C     1 
ATOM   8014  O  O     . PRO B 1 219 ? 201.673 179.606 128.735 1.00 46.21  ?  238 PRO B O     1 
ATOM   8015  C  CB    . PRO B 1 219 ? 204.221 180.921 127.431 1.00 37.79  ?  238 PRO B CB    1 
ATOM   8016  C  CG    . PRO B 1 219 ? 205.003 180.331 128.574 1.00 46.26  ?  238 PRO B CG    1 
ATOM   8017  C  CD    . PRO B 1 219 ? 204.459 180.860 129.876 1.00 45.67  ?  238 PRO B CD    1 
ATOM   8018  N  N     . VAL B 1 220 ? 200.913 180.842 127.016 1.00 41.25  ?  239 VAL B N     1 
ATOM   8019  C  CA    . VAL B 1 220 ? 199.750 180.012 126.731 1.00 46.17  ?  239 VAL B CA    1 
ATOM   8020  C  C     . VAL B 1 220 ? 199.960 179.382 125.364 1.00 47.74  ?  239 VAL B C     1 
ATOM   8021  O  O     . VAL B 1 220 ? 200.098 180.093 124.358 1.00 50.03  ?  239 VAL B O     1 
ATOM   8022  C  CB    . VAL B 1 220 ? 198.447 180.824 126.771 1.00 51.91  ?  239 VAL B CB    1 
ATOM   8023  C  CG1   . VAL B 1 220 ? 197.311 180.035 126.135 1.00 50.55  ?  239 VAL B CG1   1 
ATOM   8024  C  CG2   . VAL B 1 220 ? 198.107 181.202 128.202 1.00 51.62  ?  239 VAL B CG2   1 
ATOM   8025  N  N     . TYR B 1 221 ? 199.976 178.052 125.332 1.00 59.50  ?  240 TYR B N     1 
ATOM   8026  C  CA    . TYR B 1 221 ? 200.295 177.280 124.143 1.00 55.17  ?  240 TYR B CA    1 
ATOM   8027  C  C     . TYR B 1 221 ? 199.023 176.790 123.462 1.00 59.16  ?  240 TYR B C     1 
ATOM   8028  O  O     . TYR B 1 221 ? 197.979 176.619 124.097 1.00 63.92  ?  240 TYR B O     1 
ATOM   8029  C  CB    . TYR B 1 221 ? 201.181 176.084 124.497 1.00 53.85  ?  240 TYR B CB    1 
ATOM   8030  C  CG    . TYR B 1 221 ? 202.568 176.459 124.964 1.00 56.12  ?  240 TYR B CG    1 
ATOM   8031  C  CD1   . TYR B 1 221 ? 203.451 177.123 124.124 1.00 58.92  ?  240 TYR B CD1   1 
ATOM   8032  C  CD2   . TYR B 1 221 ? 202.995 176.149 126.247 1.00 58.57  ?  240 TYR B CD2   1 
ATOM   8033  C  CE1   . TYR B 1 221 ? 204.719 177.468 124.549 1.00 59.26  ?  240 TYR B CE1   1 
ATOM   8034  C  CE2   . TYR B 1 221 ? 204.260 176.489 126.681 1.00 60.49  ?  240 TYR B CE2   1 
ATOM   8035  C  CZ    . TYR B 1 221 ? 205.118 177.148 125.828 1.00 61.16  ?  240 TYR B CZ    1 
ATOM   8036  O  OH    . TYR B 1 221 ? 206.379 177.488 126.258 1.00 62.46  ?  240 TYR B OH    1 
ATOM   8037  N  N     . ASP B 1 222 ? 199.125 176.566 122.157 1.00 71.30  ?  241 ASP B N     1 
ATOM   8038  C  CA    . ASP B 1 222 ? 198.027 176.031 121.369 1.00 73.33  ?  241 ASP B CA    1 
ATOM   8039  C  C     . ASP B 1 222 ? 198.130 174.506 121.317 1.00 74.97  ?  241 ASP B C     1 
ATOM   8040  O  O     . ASP B 1 222 ? 198.871 173.883 122.081 1.00 74.16  ?  241 ASP B O     1 
ATOM   8041  C  CB    . ASP B 1 222 ? 198.022 176.656 119.976 1.00 73.91  ?  241 ASP B CB    1 
ATOM   8042  C  CG    . ASP B 1 222 ? 199.388 176.632 119.321 1.00 76.79  ?  241 ASP B CG    1 
ATOM   8043  O  OD1   . ASP B 1 222 ? 200.330 176.073 119.921 1.00 79.80  ?  241 ASP B OD1   1 
ATOM   8044  O  OD2   . ASP B 1 222 ? 199.521 177.176 118.205 1.00 76.54  -1 241 ASP B OD2   1 
ATOM   8045  N  N     . VAL B 1 223 ? 197.362 173.890 120.414 1.00 86.00  ?  242 VAL B N     1 
ATOM   8046  C  CA    . VAL B 1 223 ? 197.408 172.439 120.254 1.00 85.77  ?  242 VAL B CA    1 
ATOM   8047  C  C     . VAL B 1 223 ? 198.796 171.991 119.815 1.00 82.74  ?  242 VAL B C     1 
ATOM   8048  O  O     . VAL B 1 223 ? 199.313 170.969 120.285 1.00 82.66  ?  242 VAL B O     1 
ATOM   8049  C  CB    . VAL B 1 223 ? 196.324 171.977 119.262 1.00 84.95  ?  242 VAL B CB    1 
ATOM   8050  C  CG1   . VAL B 1 223 ? 196.158 170.467 119.321 1.00 83.56  ?  242 VAL B CG1   1 
ATOM   8051  C  CG2   . VAL B 1 223 ? 195.006 172.679 119.555 1.00 83.77  ?  242 VAL B CG2   1 
ATOM   8052  N  N     . LEU B 1 224 ? 199.422 172.744 118.912 1.00 76.75  ?  243 LEU B N     1 
ATOM   8053  C  CA    . LEU B 1 224 ? 200.757 172.429 118.420 1.00 78.13  ?  243 LEU B CA    1 
ATOM   8054  C  C     . LEU B 1 224 ? 201.859 172.773 119.417 1.00 79.69  ?  243 LEU B C     1 
ATOM   8055  O  O     . LEU B 1 224 ? 203.038 172.710 119.051 1.00 78.26  ?  243 LEU B O     1 
ATOM   8056  C  CB    . LEU B 1 224 ? 201.015 173.158 117.099 1.00 79.71  ?  243 LEU B CB    1 
ATOM   8057  C  CG    . LEU B 1 224 ? 200.083 172.830 115.931 1.00 80.01  ?  243 LEU B CG    1 
ATOM   8058  C  CD1   . LEU B 1 224 ? 200.471 173.626 114.694 1.00 77.22  ?  243 LEU B CD1   1 
ATOM   8059  C  CD2   . LEU B 1 224 ? 200.095 171.338 115.639 1.00 79.37  ?  243 LEU B CD2   1 
ATOM   8060  N  N     . ALA B 1 225 ? 201.503 173.131 120.654 1.00 79.07  ?  244 ALA B N     1 
ATOM   8061  C  CA    . ALA B 1 225 ? 202.471 173.498 121.690 1.00 79.04  ?  244 ALA B CA    1 
ATOM   8062  C  C     . ALA B 1 225 ? 203.373 174.641 121.229 1.00 79.18  ?  244 ALA B C     1 
ATOM   8063  O  O     . ALA B 1 225 ? 204.576 174.655 121.497 1.00 81.40  ?  244 ALA B O     1 
ATOM   8064  C  CB    . ALA B 1 225 ? 203.302 172.290 122.129 1.00 79.14  ?  244 ALA B CB    1 
ATOM   8065  N  N     . HIS B 1 226 ? 202.786 175.608 120.533 1.00 73.77  ?  245 HIS B N     1 
ATOM   8066  C  CA    . HIS B 1 226 ? 203.493 176.792 120.067 1.00 70.72  ?  245 HIS B CA    1 
ATOM   8067  C  C     . HIS B 1 226 ? 203.038 178.012 120.857 1.00 72.00  ?  245 HIS B C     1 
ATOM   8068  O  O     . HIS B 1 226 ? 202.003 178.004 121.527 1.00 73.13  ?  245 HIS B O     1 
ATOM   8069  C  CB    . HIS B 1 226 ? 203.272 177.007 118.566 1.00 68.54  ?  245 HIS B CB    1 
ATOM   8070  C  CG    . HIS B 1 226 ? 203.821 175.908 117.711 1.00 73.44  ?  245 HIS B CG    1 
ATOM   8071  N  ND1   . HIS B 1 226 ? 204.745 174.997 118.176 1.00 75.83  ?  245 HIS B ND1   1 
ATOM   8072  C  CD2   . HIS B 1 226 ? 203.583 175.578 116.420 1.00 75.77  ?  245 HIS B CD2   1 
ATOM   8073  C  CE1   . HIS B 1 226 ? 205.050 174.151 117.208 1.00 76.46  ?  245 HIS B CE1   1 
ATOM   8074  N  NE2   . HIS B 1 226 ? 204.358 174.481 116.133 1.00 76.28  ?  245 HIS B NE2   1 
ATOM   8075  N  N     . LEU B 1 227 ? 203.827 179.081 120.752 1.00 63.05  ?  246 LEU B N     1 
ATOM   8076  C  CA    . LEU B 1 227 ? 203.625 180.284 121.557 1.00 59.62  ?  246 LEU B CA    1 
ATOM   8077  C  C     . LEU B 1 227 ? 202.394 181.022 121.039 1.00 61.88  ?  246 LEU B C     1 
ATOM   8078  O  O     . LEU B 1 227 ? 202.474 181.978 120.265 1.00 62.46  ?  246 LEU B O     1 
ATOM   8079  C  CB    . LEU B 1 227 ? 204.866 181.168 121.507 1.00 65.46  ?  246 LEU B CB    1 
ATOM   8080  C  CG    . LEU B 1 227 ? 204.968 182.268 122.561 1.00 66.88  ?  246 LEU B CG    1 
ATOM   8081  C  CD1   . LEU B 1 227 ? 204.850 181.667 123.950 1.00 64.89  ?  246 LEU B CD1   1 
ATOM   8082  C  CD2   . LEU B 1 227 ? 206.270 183.036 122.411 1.00 65.93  ?  246 LEU B CD2   1 
ATOM   8083  N  N     . GLN B 1 228 ? 201.222 180.558 121.479 1.00 66.25  ?  247 GLN B N     1 
ATOM   8084  C  CA    . GLN B 1 228 ? 199.976 181.189 121.058 1.00 64.14  ?  247 GLN B CA    1 
ATOM   8085  C  C     . GLN B 1 228 ? 199.830 182.583 121.658 1.00 59.38  ?  247 GLN B C     1 
ATOM   8086  O  O     . GLN B 1 228 ? 199.564 183.552 120.938 1.00 63.11  ?  247 GLN B O     1 
ATOM   8087  C  CB    . GLN B 1 228 ? 198.783 180.313 121.440 1.00 63.08  ?  247 GLN B CB    1 
ATOM   8088  C  CG    . GLN B 1 228 ? 197.452 180.827 120.916 1.00 59.56  ?  247 GLN B CG    1 
ATOM   8089  C  CD    . GLN B 1 228 ? 197.475 181.095 119.424 1.00 62.51  ?  247 GLN B CD    1 
ATOM   8090  O  OE1   . GLN B 1 228 ? 197.447 180.168 118.614 1.00 62.29  ?  247 GLN B OE1   1 
ATOM   8091  N  NE2   . GLN B 1 228 ? 197.532 182.368 119.052 1.00 61.96  ?  247 GLN B NE2   1 
ATOM   8092  N  N     . ASN B 1 229 ? 200.011 182.708 122.973 1.00 43.38  ?  248 ASN B N     1 
ATOM   8093  C  CA    . ASN B 1 229 ? 199.870 184.002 123.632 1.00 41.86  ?  248 ASN B CA    1 
ATOM   8094  C  C     . ASN B 1 229 ? 200.760 184.045 124.864 1.00 45.56  ?  248 ASN B C     1 
ATOM   8095  O  O     . ASN B 1 229 ? 201.378 183.050 125.246 1.00 54.60  ?  248 ASN B O     1 
ATOM   8096  C  CB    . ASN B 1 229 ? 198.413 184.286 124.025 1.00 49.89  ?  248 ASN B CB    1 
ATOM   8097  C  CG    . ASN B 1 229 ? 197.512 184.504 122.827 1.00 51.62  ?  248 ASN B CG    1 
ATOM   8098  O  OD1   . ASN B 1 229 ? 196.618 183.705 122.553 1.00 57.73  ?  248 ASN B OD1   1 
ATOM   8099  N  ND2   . ASN B 1 229 ? 197.742 185.595 122.106 1.00 44.26  ?  248 ASN B ND2   1 
ATOM   8100  N  N     . LEU B 1 230 ? 200.811 185.216 125.497 1.00 45.08  ?  249 LEU B N     1 
ATOM   8101  C  CA    . LEU B 1 230 ? 201.437 185.368 126.800 1.00 40.13  ?  249 LEU B CA    1 
ATOM   8102  C  C     . LEU B 1 230 ? 200.542 186.224 127.681 1.00 40.27  ?  249 LEU B C     1 
ATOM   8103  O  O     . LEU B 1 230 ? 199.773 187.051 127.191 1.00 51.64  ?  249 LEU B O     1 
ATOM   8104  C  CB    . LEU B 1 230 ? 202.831 186.005 126.703 1.00 42.26  ?  249 LEU B CB    1 
ATOM   8105  C  CG    . LEU B 1 230 ? 203.972 185.141 126.162 1.00 47.74  ?  249 LEU B CG    1 
ATOM   8106  C  CD1   . LEU B 1 230 ? 203.951 185.093 124.649 1.00 52.82  ?  249 LEU B CD1   1 
ATOM   8107  C  CD2   . LEU B 1 230 ? 205.315 185.644 126.668 1.00 49.17  ?  249 LEU B CD2   1 
ATOM   8108  N  N     . VAL B 1 231 ? 200.648 186.020 128.990 1.00 26.05  ?  250 VAL B N     1 
ATOM   8109  C  CA    . VAL B 1 231 ? 199.878 186.782 129.963 1.00 22.54  ?  250 VAL B CA    1 
ATOM   8110  C  C     . VAL B 1 231 ? 200.827 187.277 131.041 1.00 37.77  ?  250 VAL B C     1 
ATOM   8111  O  O     . VAL B 1 231 ? 201.579 186.487 131.623 1.00 52.88  ?  250 VAL B O     1 
ATOM   8112  C  CB    . VAL B 1 231 ? 198.745 185.942 130.581 1.00 38.62  ?  250 VAL B CB    1 
ATOM   8113  C  CG1   . VAL B 1 231 ? 198.218 186.603 131.846 1.00 44.06  ?  250 VAL B CG1   1 
ATOM   8114  C  CG2   . VAL B 1 231 ? 197.628 185.755 129.575 1.00 45.15  ?  250 VAL B CG2   1 
ATOM   8115  N  N     . MET B 1 232 ? 200.793 188.581 131.308 1.00 44.18  ?  251 MET B N     1 
ATOM   8116  C  CA    . MET B 1 232 ? 201.593 189.178 132.369 1.00 45.01  ?  251 MET B CA    1 
ATOM   8117  C  C     . MET B 1 232 ? 200.665 189.782 133.410 1.00 33.93  ?  251 MET B C     1 
ATOM   8118  O  O     . MET B 1 232 ? 199.879 190.685 133.105 1.00 41.54  ?  251 MET B O     1 
ATOM   8119  C  CB    . MET B 1 232 ? 202.556 190.235 131.824 1.00 43.62  ?  251 MET B CB    1 
ATOM   8120  C  CG    . MET B 1 232 ? 203.491 190.809 132.879 1.00 47.40  ?  251 MET B CG    1 
ATOM   8121  S  SD    . MET B 1 232 ? 204.647 192.032 132.233 1.00 58.15  ?  251 MET B SD    1 
ATOM   8122  C  CE    . MET B 1 232 ? 205.753 190.982 131.303 1.00 47.60  ?  251 MET B CE    1 
ATOM   8123  N  N     . THR B 1 233 ? 200.765 189.282 134.632 1.00 28.70  ?  252 THR B N     1 
ATOM   8124  C  CA    . THR B 1 233 ? 200.046 189.821 135.773 1.00 33.79  ?  252 THR B CA    1 
ATOM   8125  C  C     . THR B 1 233 ? 200.981 190.725 136.563 1.00 42.28  ?  252 THR B C     1 
ATOM   8126  O  O     . THR B 1 233 ? 202.161 190.398 136.760 1.00 54.68  ?  252 THR B O     1 
ATOM   8127  C  CB    . THR B 1 233 ? 199.505 188.702 136.665 1.00 46.82  ?  252 THR B CB    1 
ATOM   8128  O  OG1   . THR B 1 233 ? 200.595 188.048 137.328 1.00 51.64  ?  252 THR B OG1   1 
ATOM   8129  C  CG2   . THR B 1 233 ? 198.735 187.686 135.834 1.00 44.78  ?  252 THR B CG2   1 
ATOM   8130  N  N     . PHE B 1 234 ? 200.451 191.860 137.001 1.00 33.39  ?  253 PHE B N     1 
ATOM   8131  C  CA    . PHE B 1 234 ? 201.199 192.847 137.757 1.00 22.23  ?  253 PHE B CA    1 
ATOM   8132  C  C     . PHE B 1 234 ? 200.698 192.885 139.193 1.00 19.24  ?  253 PHE B C     1 
ATOM   8133  O  O     . PHE B 1 234 ? 199.556 192.524 139.491 1.00 32.04  ?  253 PHE B O     1 
ATOM   8134  C  CB    . PHE B 1 234 ? 201.073 194.244 137.132 1.00 32.00  ?  253 PHE B CB    1 
ATOM   8135  C  CG    . PHE B 1 234 ? 201.553 194.329 135.707 1.00 32.64  ?  253 PHE B CG    1 
ATOM   8136  C  CD1   . PHE B 1 234 ? 200.774 193.851 134.666 1.00 43.74  ?  253 PHE B CD1   1 
ATOM   8137  C  CD2   . PHE B 1 234 ? 202.781 194.896 135.409 1.00 30.27  ?  253 PHE B CD2   1 
ATOM   8138  C  CE1   . PHE B 1 234 ? 201.213 193.936 133.358 1.00 43.00  ?  253 PHE B CE1   1 
ATOM   8139  C  CE2   . PHE B 1 234 ? 203.225 194.981 134.103 1.00 34.41  ?  253 PHE B CE2   1 
ATOM   8140  C  CZ    . PHE B 1 234 ? 202.440 194.502 133.077 1.00 37.60  ?  253 PHE B CZ    1 
ATOM   8141  N  N     . SER B 1 235 ? 201.578 193.326 140.084 1.00 29.12  ?  254 SER B N     1 
ATOM   8142  C  CA    . SER B 1 235 ? 201.209 193.567 141.474 1.00 39.99  ?  254 SER B CA    1 
ATOM   8143  C  C     . SER B 1 235 ? 202.149 194.630 142.012 1.00 40.20  ?  254 SER B C     1 
ATOM   8144  O  O     . SER B 1 235 ? 203.370 194.460 141.952 1.00 49.99  ?  254 SER B O     1 
ATOM   8145  C  CB    . SER B 1 235 ? 201.292 192.284 142.302 1.00 44.56  ?  254 SER B CB    1 
ATOM   8146  O  OG    . SER B 1 235 ? 202.628 191.829 142.411 1.00 48.66  ?  254 SER B OG    1 
ATOM   8147  N  N     . ASP B 1 236 ? 201.590 195.734 142.496 1.00 34.24  ?  255 ASP B N     1 
ATOM   8148  C  CA    . ASP B 1 236 ? 202.409 196.802 143.050 1.00 40.43  ?  255 ASP B CA    1 
ATOM   8149  C  C     . ASP B 1 236 ? 203.031 196.336 144.358 1.00 42.81  ?  255 ASP B C     1 
ATOM   8150  O  O     . ASP B 1 236 ? 202.315 196.018 145.312 1.00 48.20  ?  255 ASP B O     1 
ATOM   8151  C  CB    . ASP B 1 236 ? 201.569 198.059 143.265 1.00 47.12  ?  255 ASP B CB    1 
ATOM   8152  C  CG    . ASP B 1 236 ? 202.397 199.245 143.726 1.00 50.26  ?  255 ASP B CG    1 
ATOM   8153  O  OD1   . ASP B 1 236 ? 203.603 199.296 143.407 1.00 50.95  ?  255 ASP B OD1   1 
ATOM   8154  O  OD2   . ASP B 1 236 ? 201.841 200.129 144.411 1.00 51.66  -1 255 ASP B OD2   1 
ATOM   8155  N  N     . ILE B 1 237 ? 204.363 196.270 144.392 1.00 45.29  ?  256 ILE B N     1 
ATOM   8156  C  CA    . ILE B 1 237 ? 205.052 195.902 145.625 1.00 43.51  ?  256 ILE B CA    1 
ATOM   8157  C  C     . ILE B 1 237 ? 204.760 196.925 146.714 1.00 43.94  ?  256 ILE B C     1 
ATOM   8158  O  O     . ILE B 1 237 ? 204.599 196.576 147.890 1.00 50.31  ?  256 ILE B O     1 
ATOM   8159  C  CB    . ILE B 1 237 ? 206.563 195.755 145.371 1.00 43.62  ?  256 ILE B CB    1 
ATOM   8160  C  CG1   . ILE B 1 237 ? 206.823 194.650 144.345 1.00 46.29  ?  256 ILE B CG1   1 
ATOM   8161  C  CG2   . ILE B 1 237 ? 207.301 195.460 146.671 1.00 45.37  ?  256 ILE B CG2   1 
ATOM   8162  C  CD1   . ILE B 1 237 ? 206.790 193.252 144.928 1.00 48.13  ?  256 ILE B CD1   1 
ATOM   8163  N  N     . THR B 1 238 ? 204.683 198.204 146.337 1.00 39.33  ?  257 THR B N     1 
ATOM   8164  C  CA    . THR B 1 238 ? 204.311 199.238 147.296 1.00 43.94  ?  257 THR B CA    1 
ATOM   8165  C  C     . THR B 1 238 ? 202.912 198.997 147.846 1.00 50.33  ?  257 THR B C     1 
ATOM   8166  O  O     . THR B 1 238 ? 202.681 199.130 149.052 1.00 52.59  ?  257 THR B O     1 
ATOM   8167  C  CB    . THR B 1 238 ? 204.402 200.619 146.644 1.00 46.05  ?  257 THR B CB    1 
ATOM   8168  O  OG1   . THR B 1 238 ? 205.684 200.776 146.023 1.00 47.75  ?  257 THR B OG1   1 
ATOM   8169  C  CG2   . THR B 1 238 ? 204.210 201.714 147.683 1.00 46.57  ?  257 THR B CG2   1 
ATOM   8170  N  N     . GLU B 1 239 ? 201.966 198.625 146.981 1.00 42.56  ?  258 GLU B N     1 
ATOM   8171  C  CA    . GLU B 1 239 ? 200.612 198.345 147.449 1.00 37.96  ?  258 GLU B CA    1 
ATOM   8172  C  C     . GLU B 1 239 ? 200.580 197.128 148.365 1.00 39.94  ?  258 GLU B C     1 
ATOM   8173  O  O     . GLU B 1 239 ? 199.873 197.126 149.377 1.00 46.20  ?  258 GLU B O     1 
ATOM   8174  C  CB    . GLU B 1 239 ? 199.676 198.148 146.259 1.00 40.46  ?  258 GLU B CB    1 
ATOM   8175  C  CG    . GLU B 1 239 ? 198.945 199.411 145.839 1.00 49.05  ?  258 GLU B CG    1 
ATOM   8176  C  CD    . GLU B 1 239 ? 198.091 199.206 144.606 1.00 54.83  ?  258 GLU B CD    1 
ATOM   8177  O  OE1   . GLU B 1 239 ? 196.928 198.779 144.749 1.00 54.80  ?  258 GLU B OE1   1 
ATOM   8178  O  OE2   . GLU B 1 239 ? 198.584 199.480 143.492 1.00 52.21  -1 258 GLU B OE2   1 
ATOM   8179  N  N     . GLU B 1 240 ? 201.330 196.079 148.022 1.00 38.50  ?  259 GLU B N     1 
ATOM   8180  C  CA    . GLU B 1 240 ? 201.354 194.882 148.859 1.00 29.62  ?  259 GLU B CA    1 
ATOM   8181  C  C     . GLU B 1 240 ? 201.952 195.175 150.229 1.00 29.15  ?  259 GLU B C     1 
ATOM   8182  O  O     . GLU B 1 240 ? 201.403 194.763 151.259 1.00 38.43  ?  259 GLU B O     1 
ATOM   8183  C  CB    . GLU B 1 240 ? 202.135 193.766 148.165 1.00 40.53  ?  259 GLU B CB    1 
ATOM   8184  C  CG    . GLU B 1 240 ? 201.543 193.322 146.840 1.00 43.11  ?  259 GLU B CG    1 
ATOM   8185  C  CD    . GLU B 1 240 ? 200.127 192.806 146.985 1.00 49.02  ?  259 GLU B CD    1 
ATOM   8186  O  OE1   . GLU B 1 240 ? 199.949 191.699 147.534 1.00 49.44  ?  259 GLU B OE1   1 
ATOM   8187  O  OE2   . GLU B 1 240 ? 199.190 193.508 146.550 1.00 46.97  -1 259 GLU B OE2   1 
ATOM   8188  N  N     . ARG B 1 241 ? 203.073 195.897 150.266 1.00 35.40  ?  260 ARG B N     1 
ATOM   8189  C  CA    . ARG B 1 241 ? 203.678 196.225 151.551 1.00 42.84  ?  260 ARG B CA    1 
ATOM   8190  C  C     . ARG B 1 241 ? 202.782 197.163 152.351 1.00 47.33  ?  260 ARG B C     1 
ATOM   8191  O  O     . ARG B 1 241 ? 202.692 197.041 153.576 1.00 48.46  ?  260 ARG B O     1 
ATOM   8192  C  CB    . ARG B 1 241 ? 205.075 196.820 151.349 1.00 41.56  ?  260 ARG B CB    1 
ATOM   8193  C  CG    . ARG B 1 241 ? 205.114 198.180 150.682 1.00 42.86  ?  260 ARG B CG    1 
ATOM   8194  C  CD    . ARG B 1 241 ? 206.403 198.916 150.998 1.00 49.30  ?  260 ARG B CD    1 
ATOM   8195  N  NE    . ARG B 1 241 ? 207.573 198.184 150.527 1.00 53.96  ?  260 ARG B NE    1 
ATOM   8196  C  CZ    . ARG B 1 241 ? 208.133 198.352 149.337 1.00 50.35  ?  260 ARG B CZ    1 
ATOM   8197  N  NH1   . ARG B 1 241 ? 207.657 199.227 148.466 1.00 49.61  1  260 ARG B NH1   1 
ATOM   8198  N  NH2   . ARG B 1 241 ? 209.196 197.623 149.012 1.00 43.90  ?  260 ARG B NH2   1 
ATOM   8199  N  N     . GLN B 1 242 ? 202.081 198.078 151.676 1.00 42.42  ?  261 GLN B N     1 
ATOM   8200  C  CA    . GLN B 1 242 ? 201.179 198.982 152.379 1.00 39.25  ?  261 GLN B CA    1 
ATOM   8201  C  C     . GLN B 1 242 ? 199.974 198.241 152.947 1.00 45.00  ?  261 GLN B C     1 
ATOM   8202  O  O     . GLN B 1 242 ? 199.520 198.547 154.053 1.00 48.44  ?  261 GLN B O     1 
ATOM   8203  C  CB    . GLN B 1 242 ? 200.732 200.104 151.444 1.00 42.11  ?  261 GLN B CB    1 
ATOM   8204  C  CG    . GLN B 1 242 ? 201.531 201.385 151.601 1.00 40.15  ?  261 GLN B CG    1 
ATOM   8205  C  CD    . GLN B 1 242 ? 200.896 202.558 150.884 1.00 45.06  ?  261 GLN B CD    1 
ATOM   8206  O  OE1   . GLN B 1 242 ? 200.673 202.514 149.675 1.00 44.94  ?  261 GLN B OE1   1 
ATOM   8207  N  NE2   . GLN B 1 242 ? 200.603 203.617 151.629 1.00 45.96  ?  261 GLN B NE2   1 
ATOM   8208  N  N     . ILE B 1 243 ? 199.446 197.256 152.215 1.00 42.49  ?  262 ILE B N     1 
ATOM   8209  C  CA    . ILE B 1 243 ? 198.287 196.522 152.710 1.00 27.11  ?  262 ILE B CA    1 
ATOM   8210  C  C     . ILE B 1 243 ? 198.676 195.520 153.790 1.00 26.85  ?  262 ILE B C     1 
ATOM   8211  O  O     . ILE B 1 243 ? 197.843 195.184 154.641 1.00 32.56  ?  262 ILE B O     1 
ATOM   8212  C  CB    . ILE B 1 243 ? 197.539 195.823 151.558 1.00 24.73  ?  262 ILE B CB    1 
ATOM   8213  C  CG1   . ILE B 1 243 ? 196.158 195.353 152.018 1.00 30.75  ?  262 ILE B CG1   1 
ATOM   8214  C  CG2   . ILE B 1 243 ? 198.323 194.638 151.029 1.00 39.65  ?  262 ILE B CG2   1 
ATOM   8215  C  CD1   . ILE B 1 243 ? 195.216 196.477 152.367 1.00 37.76  ?  262 ILE B CD1   1 
ATOM   8216  N  N     . ARG B 1 244 ? 199.923 195.043 153.798 1.00 39.44  ?  263 ARG B N     1 
ATOM   8217  C  CA    . ARG B 1 244 ? 200.383 194.264 154.943 1.00 38.47  ?  263 ARG B CA    1 
ATOM   8218  C  C     . ARG B 1 244 ? 200.627 195.160 156.154 1.00 38.98  ?  263 ARG B C     1 
ATOM   8219  O  O     . ARG B 1 244 ? 200.292 194.789 157.287 1.00 51.93  ?  263 ARG B O     1 
ATOM   8220  C  CB    . ARG B 1 244 ? 201.652 193.490 154.585 1.00 42.01  ?  263 ARG B CB    1 
ATOM   8221  C  CG    . ARG B 1 244 ? 201.485 192.475 153.461 1.00 43.52  ?  263 ARG B CG    1 
ATOM   8222  C  CD    . ARG B 1 244 ? 200.919 191.157 153.966 1.00 47.20  ?  263 ARG B CD    1 
ATOM   8223  N  NE    . ARG B 1 244 ? 199.461 191.131 153.949 1.00 53.16  ?  263 ARG B NE    1 
ATOM   8224  C  CZ    . ARG B 1 244 ? 198.727 190.881 152.873 1.00 50.23  ?  263 ARG B CZ    1 
ATOM   8225  N  NH1   . ARG B 1 244 ? 199.284 190.630 151.699 1.00 46.94  1  263 ARG B NH1   1 
ATOM   8226  N  NH2   . ARG B 1 244 ? 197.401 190.881 152.977 1.00 48.88  ?  263 ARG B NH2   1 
ATOM   8227  N  N     . GLN B 1 245 ? 201.192 196.350 155.927 1.00 29.90  ?  264 GLN B N     1 
ATOM   8228  C  CA    . GLN B 1 245 ? 201.473 197.274 157.017 1.00 40.01  ?  264 GLN B CA    1 
ATOM   8229  C  C     . GLN B 1 245 ? 200.195 197.814 157.642 1.00 40.77  ?  264 GLN B C     1 
ATOM   8230  O  O     . GLN B 1 245 ? 200.154 198.047 158.851 1.00 41.73  ?  264 GLN B O     1 
ATOM   8231  C  CB    . GLN B 1 245 ? 202.344 198.424 156.509 1.00 39.43  ?  264 GLN B CB    1 
ATOM   8232  C  CG    . GLN B 1 245 ? 202.771 199.411 157.579 1.00 40.21  ?  264 GLN B CG    1 
ATOM   8233  C  CD    . GLN B 1 245 ? 203.929 200.282 157.135 1.00 44.85  ?  264 GLN B CD    1 
ATOM   8234  O  OE1   . GLN B 1 245 ? 204.859 199.813 156.478 1.00 39.63  ?  264 GLN B OE1   1 
ATOM   8235  N  NE2   . GLN B 1 245 ? 203.883 201.558 157.501 1.00 42.32  ?  264 GLN B NE2   1 
ATOM   8236  N  N     . LEU B 1 246 ? 199.149 198.023 156.841 1.00 35.04  ?  265 LEU B N     1 
ATOM   8237  C  CA    . LEU B 1 246 ? 197.871 198.469 157.386 1.00 23.80  ?  265 LEU B CA    1 
ATOM   8238  C  C     . LEU B 1 246 ? 197.302 197.434 158.346 1.00 27.14  ?  265 LEU B C     1 
ATOM   8239  O  O     . LEU B 1 246 ? 196.881 197.767 159.461 1.00 36.72  ?  265 LEU B O     1 
ATOM   8240  C  CB    . LEU B 1 246 ? 196.888 198.746 156.247 1.00 27.54  ?  265 LEU B CB    1 
ATOM   8241  C  CG    . LEU B 1 246 ? 195.409 198.829 156.625 1.00 29.33  ?  265 LEU B CG    1 
ATOM   8242  C  CD1   . LEU B 1 246 ? 195.108 200.125 157.356 1.00 36.86  ?  265 LEU B CD1   1 
ATOM   8243  C  CD2   . LEU B 1 246 ? 194.528 198.688 155.394 1.00 29.00  ?  265 LEU B CD2   1 
ATOM   8244  N  N     . GLU B 1 247 ? 197.297 196.165 157.932 1.00 32.02  ?  266 GLU B N     1 
ATOM   8245  C  CA    . GLU B 1 247 ? 196.807 195.102 158.801 1.00 25.44  ?  266 GLU B CA    1 
ATOM   8246  C  C     . GLU B 1 247 ? 197.655 194.997 160.060 1.00 20.21  ?  266 GLU B C     1 
ATOM   8247  O  O     . GLU B 1 247 ? 197.120 194.878 161.169 1.00 34.48  ?  266 GLU B O     1 
ATOM   8248  C  CB    . GLU B 1 247 ? 196.800 193.774 158.045 1.00 31.53  ?  266 GLU B CB    1 
ATOM   8249  C  CG    . GLU B 1 247 ? 196.033 192.657 158.731 1.00 39.53  ?  266 GLU B CG    1 
ATOM   8250  C  CD    . GLU B 1 247 ? 195.971 191.398 157.886 1.00 43.82  ?  266 GLU B CD    1 
ATOM   8251  O  OE1   . GLU B 1 247 ? 195.077 190.560 158.127 1.00 45.06  ?  266 GLU B OE1   1 
ATOM   8252  O  OE2   . GLU B 1 247 ? 196.818 191.247 156.981 1.00 37.13  -1 266 GLU B OE2   1 
ATOM   8253  N  N     . GLY B 1 248 ? 198.979 195.065 159.911 1.00 25.47  ?  267 GLY B N     1 
ATOM   8254  C  CA    . GLY B 1 248 ? 199.846 194.986 161.075 1.00 34.25  ?  267 GLY B CA    1 
ATOM   8255  C  C     . GLY B 1 248 ? 199.629 196.125 162.052 1.00 41.59  ?  267 GLY B C     1 
ATOM   8256  O  O     . GLY B 1 248 ? 199.543 195.908 163.262 1.00 46.43  ?  267 GLY B O     1 
ATOM   8257  N  N     . ASN B 1 249 ? 199.527 197.355 161.540 1.00 39.97  ?  268 ASN B N     1 
ATOM   8258  C  CA    . ASN B 1 249 ? 199.328 198.513 162.403 1.00 27.77  ?  268 ASN B CA    1 
ATOM   8259  C  C     . ASN B 1 249 ? 197.975 198.464 163.099 1.00 38.56  ?  268 ASN B C     1 
ATOM   8260  O  O     . ASN B 1 249 ? 197.878 198.766 164.295 1.00 52.21  ?  268 ASN B O     1 
ATOM   8261  C  CB    . ASN B 1 249 ? 199.469 199.801 161.592 1.00 30.70  ?  268 ASN B CB    1 
ATOM   8262  C  CG    . ASN B 1 249 ? 200.912 200.228 161.421 1.00 43.34  ?  268 ASN B CG    1 
ATOM   8263  O  OD1   . ASN B 1 249 ? 201.819 199.654 162.023 1.00 52.26  ?  268 ASN B OD1   1 
ATOM   8264  N  ND2   . ASN B 1 249 ? 201.133 201.247 160.599 1.00 41.65  ?  268 ASN B ND2   1 
ATOM   8265  N  N     . ILE B 1 250 ? 196.918 198.083 162.374 1.00 25.64  ?  269 ILE B N     1 
ATOM   8266  C  CA    . ILE B 1 250 ? 195.601 197.996 162.995 1.00 16.99  ?  269 ILE B CA    1 
ATOM   8267  C  C     . ILE B 1 250 ? 195.591 196.921 164.073 1.00 28.63  ?  269 ILE B C     1 
ATOM   8268  O  O     . ILE B 1 250 ? 195.034 197.119 165.159 1.00 38.74  ?  269 ILE B O     1 
ATOM   8269  C  CB    . ILE B 1 250 ? 194.515 197.741 161.937 1.00 15.82  ?  269 ILE B CB    1 
ATOM   8270  C  CG1   . ILE B 1 250 ? 194.395 198.934 160.994 1.00 19.21  ?  269 ILE B CG1   1 
ATOM   8271  C  CG2   . ILE B 1 250 ? 193.183 197.497 162.611 1.00 30.45  ?  269 ILE B CG2   1 
ATOM   8272  C  CD1   . ILE B 1 250 ? 193.734 200.126 161.625 1.00 37.74  ?  269 ILE B CD1   1 
ATOM   8273  N  N     . LEU B 1 251 ? 196.201 195.767 163.794 1.00 29.17  ?  270 LEU B N     1 
ATOM   8274  C  CA    . LEU B 1 251 ? 196.249 194.701 164.788 1.00 20.29  ?  270 LEU B CA    1 
ATOM   8275  C  C     . LEU B 1 251 ? 197.054 195.125 166.009 1.00 22.63  ?  270 LEU B C     1 
ATOM   8276  O  O     . LEU B 1 251 ? 196.673 194.827 167.147 1.00 41.99  ?  270 LEU B O     1 
ATOM   8277  C  CB    . LEU B 1 251 ? 196.831 193.436 164.162 1.00 24.31  ?  270 LEU B CB    1 
ATOM   8278  C  CG    . LEU B 1 251 ? 195.840 192.667 163.288 1.00 26.62  ?  270 LEU B CG    1 
ATOM   8279  C  CD1   . LEU B 1 251 ? 196.555 191.650 162.414 1.00 32.11  ?  270 LEU B CD1   1 
ATOM   8280  C  CD2   . LEU B 1 251 ? 194.776 192.001 164.147 1.00 29.62  ?  270 LEU B CD2   1 
ATOM   8281  N  N     . ALA B 1 252 ? 198.167 195.831 165.795 1.00 8.41   ?  271 ALA B N     1 
ATOM   8282  C  CA    . ALA B 1 252 ? 198.957 196.319 166.919 1.00 23.47  ?  271 ALA B CA    1 
ATOM   8283  C  C     . ALA B 1 252 ? 198.157 197.297 167.771 1.00 32.10  ?  271 ALA B C     1 
ATOM   8284  O  O     . ALA B 1 252 ? 198.170 197.214 169.005 1.00 38.74  ?  271 ALA B O     1 
ATOM   8285  C  CB    . ALA B 1 252 ? 200.242 196.974 166.413 1.00 31.84  ?  271 ALA B CB    1 
ATOM   8286  N  N     . ALA B 1 253 ? 197.442 198.222 167.131 1.00 24.33  ?  272 ALA B N     1 
ATOM   8287  C  CA    . ALA B 1 253 ? 196.628 199.169 167.885 1.00 25.67  ?  272 ALA B CA    1 
ATOM   8288  C  C     . ALA B 1 253 ? 195.520 198.458 168.650 1.00 37.93  ?  272 ALA B C     1 
ATOM   8289  O  O     . ALA B 1 253 ? 195.220 198.810 169.798 1.00 37.94  ?  272 ALA B O     1 
ATOM   8290  C  CB    . ALA B 1 253 ? 196.044 200.220 166.948 1.00 25.51  ?  272 ALA B CB    1 
ATOM   8291  N  N     . MET B 1 254 ? 194.892 197.458 168.026 1.00 39.28  ?  273 MET B N     1 
ATOM   8292  C  CA    . MET B 1 254 ? 193.847 196.694 168.697 1.00 26.35  ?  273 MET B CA    1 
ATOM   8293  C  C     . MET B 1 254 ? 194.397 195.888 169.866 1.00 29.55  ?  273 MET B C     1 
ATOM   8294  O  O     . MET B 1 254 ? 193.676 195.638 170.838 1.00 41.36  ?  273 MET B O     1 
ATOM   8295  C  CB    . MET B 1 254 ? 193.159 195.766 167.699 1.00 25.17  ?  273 MET B CB    1 
ATOM   8296  C  CG    . MET B 1 254 ? 191.647 195.760 167.794 1.00 31.78  ?  273 MET B CG    1 
ATOM   8297  S  SD    . MET B 1 254 ? 190.899 194.726 166.523 1.00 50.24  ?  273 MET B SD    1 
ATOM   8298  C  CE    . MET B 1 254 ? 191.070 195.782 165.089 1.00 36.99  ?  273 MET B CE    1 
ATOM   8299  N  N     . CYS B 1 255 ? 195.662 195.472 169.790 1.00 15.82  ?  274 CYS B N     1 
ATOM   8300  C  CA    . CYS B 1 255 ? 196.262 194.709 170.876 1.00 24.68  ?  274 CYS B CA    1 
ATOM   8301  C  C     . CYS B 1 255 ? 196.528 195.553 172.115 1.00 32.76  ?  274 CYS B C     1 
ATOM   8302  O  O     . CYS B 1 255 ? 196.845 194.991 173.168 1.00 38.92  ?  274 CYS B O     1 
ATOM   8303  C  CB    . CYS B 1 255 ? 197.565 194.060 170.403 1.00 27.27  ?  274 CYS B CB    1 
ATOM   8304  S  SG    . CYS B 1 255 ? 197.337 192.614 169.344 1.00 47.22  ?  274 CYS B SG    1 
ATOM   8305  N  N     . SER B 1 256 ? 196.402 196.875 172.021 1.00 25.21  ?  275 SER B N     1 
ATOM   8306  C  CA    . SER B 1 256 ? 196.591 197.761 173.161 1.00 31.36  ?  275 SER B CA    1 
ATOM   8307  C  C     . SER B 1 256 ? 195.308 197.995 173.947 1.00 29.35  ?  275 SER B C     1 
ATOM   8308  O  O     . SER B 1 256 ? 195.340 198.706 174.957 1.00 30.29  ?  275 SER B O     1 
ATOM   8309  C  CB    . SER B 1 256 ? 197.158 199.106 172.696 1.00 37.63  ?  275 SER B CB    1 
ATOM   8310  O  OG    . SER B 1 256 ? 196.386 199.646 171.636 1.00 40.32  ?  275 SER B OG    1 
ATOM   8311  N  N     . SER B 1 257 ? 194.195 197.409 173.514 1.00 25.27  ?  276 SER B N     1 
ATOM   8312  C  CA    . SER B 1 257 ? 192.897 197.564 174.161 1.00 31.00  ?  276 SER B CA    1 
ATOM   8313  C  C     . SER B 1 257 ? 192.527 199.034 174.393 1.00 34.25  ?  276 SER B C     1 
ATOM   8314  O  O     . SER B 1 257 ? 192.418 199.479 175.537 1.00 41.56  ?  276 SER B O     1 
ATOM   8315  C  CB    . SER B 1 257 ? 192.855 196.788 175.471 1.00 31.93  ?  276 SER B CB    1 
ATOM   8316  O  OG    . SER B 1 257 ? 193.729 197.353 176.431 1.00 40.52  ?  276 SER B OG    1 
ATOM   8317  N  N     . PRO B 1 258 ? 192.333 199.808 173.328 1.00 29.79  ?  277 PRO B N     1 
ATOM   8318  C  CA    . PRO B 1 258 ? 191.927 201.203 173.492 1.00 28.26  ?  277 PRO B CA    1 
ATOM   8319  C  C     . PRO B 1 258 ? 190.415 201.315 173.575 1.00 29.54  ?  277 PRO B C     1 
ATOM   8320  O  O     . PRO B 1 258 ? 189.700 200.334 173.321 1.00 30.48  ?  277 PRO B O     1 
ATOM   8321  C  CB    . PRO B 1 258 ? 192.472 201.883 172.223 1.00 27.06  ?  277 PRO B CB    1 
ATOM   8322  C  CG    . PRO B 1 258 ? 192.896 200.761 171.292 1.00 28.88  ?  277 PRO B CG    1 
ATOM   8323  C  CD    . PRO B 1 258 ? 192.488 199.459 171.908 1.00 25.35  ?  277 PRO B CD    1 
ATOM   8324  N  N     . PRO B 1 259 ? 189.888 202.485 173.944 1.00 33.28  ?  278 PRO B N     1 
ATOM   8325  C  CA    . PRO B 1 259 ? 188.433 202.674 173.928 1.00 30.18  ?  278 PRO B CA    1 
ATOM   8326  C  C     . PRO B 1 259 ? 187.853 202.443 172.540 1.00 25.71  ?  278 PRO B C     1 
ATOM   8327  O  O     . PRO B 1 259 ? 188.567 202.371 171.540 1.00 38.96  ?  278 PRO B O     1 
ATOM   8328  C  CB    . PRO B 1 259 ? 188.259 204.131 174.371 1.00 31.05  ?  278 PRO B CB    1 
ATOM   8329  C  CG    . PRO B 1 259 ? 189.470 204.412 175.188 1.00 34.04  ?  278 PRO B CG    1 
ATOM   8330  C  CD    . PRO B 1 259 ? 190.584 203.640 174.539 1.00 33.68  ?  278 PRO B CD    1 
ATOM   8331  N  N     . PHE B 1 260 ? 186.527 202.305 172.496 1.00 16.95  ?  279 PHE B N     1 
ATOM   8332  C  CA    . PHE B 1 260 ? 185.846 202.027 171.234 1.00 26.60  ?  279 PHE B CA    1 
ATOM   8333  C  C     . PHE B 1 260 ? 186.000 203.188 170.255 1.00 38.27  ?  279 PHE B C     1 
ATOM   8334  O  O     . PHE B 1 260 ? 186.308 202.987 169.071 1.00 39.90  ?  279 PHE B O     1 
ATOM   8335  C  CB    . PHE B 1 260 ? 184.372 201.730 171.509 1.00 32.88  ?  279 PHE B CB    1 
ATOM   8336  C  CG    . PHE B 1 260 ? 183.647 201.107 170.355 1.00 23.32  ?  279 PHE B CG    1 
ATOM   8337  C  CD1   . PHE B 1 260 ? 184.034 199.870 169.865 1.00 24.51  ?  279 PHE B CD1   1 
ATOM   8338  C  CD2   . PHE B 1 260 ? 182.561 201.742 169.777 1.00 17.43  ?  279 PHE B CD2   1 
ATOM   8339  C  CE1   . PHE B 1 260 ? 183.362 199.287 168.810 1.00 28.02  ?  279 PHE B CE1   1 
ATOM   8340  C  CE2   . PHE B 1 260 ? 181.886 201.163 168.721 1.00 14.59  ?  279 PHE B CE2   1 
ATOM   8341  C  CZ    . PHE B 1 260 ? 182.287 199.935 168.238 1.00 29.81  ?  279 PHE B CZ    1 
ATOM   8342  N  N     . HIS B 1 261 ? 185.797 204.417 170.738 1.00 38.90  ?  280 HIS B N     1 
ATOM   8343  C  CA    . HIS B 1 261 ? 185.961 205.588 169.882 1.00 35.67  ?  280 HIS B CA    1 
ATOM   8344  C  C     . HIS B 1 261 ? 187.404 205.738 169.419 1.00 42.62  ?  280 HIS B C     1 
ATOM   8345  O  O     . HIS B 1 261 ? 187.659 206.090 168.261 1.00 44.67  ?  280 HIS B O     1 
ATOM   8346  C  CB    . HIS B 1 261 ? 185.500 206.847 170.617 1.00 30.51  ?  280 HIS B CB    1 
ATOM   8347  C  CG    . HIS B 1 261 ? 184.016 206.934 170.796 1.00 43.22  ?  280 HIS B CG    1 
ATOM   8348  N  ND1   . HIS B 1 261 ? 183.126 206.585 169.803 1.00 46.59  ?  280 HIS B ND1   1 
ATOM   8349  C  CD2   . HIS B 1 261 ? 183.266 207.332 171.851 1.00 47.84  ?  280 HIS B CD2   1 
ATOM   8350  C  CE1   . HIS B 1 261 ? 181.891 206.764 170.239 1.00 42.88  ?  280 HIS B CE1   1 
ATOM   8351  N  NE2   . HIS B 1 261 ? 181.949 207.216 171.478 1.00 46.26  ?  280 HIS B NE2   1 
ATOM   8352  N  N     . GLU B 1 262 ? 188.363 205.486 170.312 1.00 41.48  ?  281 GLU B N     1 
ATOM   8353  C  CA    . GLU B 1 262 ? 189.768 205.573 169.928 1.00 37.86  ?  281 GLU B CA    1 
ATOM   8354  C  C     . GLU B 1 262 ? 190.125 204.511 168.896 1.00 33.38  ?  281 GLU B C     1 
ATOM   8355  O  O     . GLU B 1 262 ? 190.925 204.763 167.993 1.00 37.41  ?  281 GLU B O     1 
ATOM   8356  C  CB    . GLU B 1 262 ? 190.664 205.451 171.159 1.00 41.36  ?  281 GLU B CB    1 
ATOM   8357  C  CG    . GLU B 1 262 ? 192.142 205.648 170.862 1.00 44.68  ?  281 GLU B CG    1 
ATOM   8358  C  CD    . GLU B 1 262 ? 192.993 205.627 172.114 1.00 49.07  ?  281 GLU B CD    1 
ATOM   8359  O  OE1   . GLU B 1 262 ? 192.459 205.943 173.198 1.00 46.35  ?  281 GLU B OE1   1 
ATOM   8360  O  OE2   . GLU B 1 262 ? 194.193 205.298 172.014 1.00 49.22  -1 281 GLU B OE2   1 
ATOM   8361  N  N     . MET B 1 263 ? 189.555 203.311 169.021 1.00 32.33  ?  282 MET B N     1 
ATOM   8362  C  CA    . MET B 1 263 ? 189.782 202.276 168.017 1.00 30.71  ?  282 MET B CA    1 
ATOM   8363  C  C     . MET B 1 263 ? 189.216 202.690 166.666 1.00 27.63  ?  282 MET B C     1 
ATOM   8364  O  O     . MET B 1 263 ? 189.864 202.499 165.628 1.00 42.72  ?  282 MET B O     1 
ATOM   8365  C  CB    . MET B 1 263 ? 189.165 200.955 168.474 1.00 35.44  ?  282 MET B CB    1 
ATOM   8366  C  CG    . MET B 1 263 ? 190.152 199.980 169.092 1.00 36.08  ?  282 MET B CG    1 
ATOM   8367  S  SD    . MET B 1 263 ? 191.614 199.706 168.072 1.00 57.32  ?  282 MET B SD    1 
ATOM   8368  C  CE    . MET B 1 263 ? 190.867 199.183 166.529 1.00 46.76  ?  282 MET B CE    1 
ATOM   8369  N  N     . GLY B 1 264 ? 188.009 203.254 166.659 1.00 22.31  ?  283 GLY B N     1 
ATOM   8370  C  CA    . GLY B 1 264 ? 187.462 203.770 165.414 1.00 32.52  ?  283 GLY B CA    1 
ATOM   8371  C  C     . GLY B 1 264 ? 188.338 204.848 164.805 1.00 39.06  ?  283 GLY B C     1 
ATOM   8372  O  O     . GLY B 1 264 ? 188.585 204.854 163.596 1.00 39.67  ?  283 GLY B O     1 
ATOM   8373  N  N     . GLU B 1 265 ? 188.842 205.759 165.640 1.00 46.78  ?  284 GLU B N     1 
ATOM   8374  C  CA    . GLU B 1 265 ? 189.726 206.814 165.153 1.00 41.72  ?  284 GLU B CA    1 
ATOM   8375  C  C     . GLU B 1 265 ? 191.031 206.243 164.611 1.00 41.60  ?  284 GLU B C     1 
ATOM   8376  O  O     . GLU B 1 265 ? 191.571 206.745 163.622 1.00 45.52  ?  284 GLU B O     1 
ATOM   8377  C  CB    . GLU B 1 265 ? 190.005 207.823 166.267 1.00 40.66  ?  284 GLU B CB    1 
ATOM   8378  C  CG    . GLU B 1 265 ? 190.703 209.091 165.796 1.00 50.31  ?  284 GLU B CG    1 
ATOM   8379  C  CD    . GLU B 1 265 ? 189.759 210.055 165.104 1.00 54.91  ?  284 GLU B CD    1 
ATOM   8380  O  OE1   . GLU B 1 265 ? 188.530 209.902 165.263 1.00 47.02  ?  284 GLU B OE1   1 
ATOM   8381  O  OE2   . GLU B 1 265 ? 190.247 210.963 164.400 1.00 59.12  -1 284 GLU B OE2   1 
ATOM   8382  N  N     . ILE B 1 266 ? 191.565 205.208 165.262 1.00 34.88  ?  285 ILE B N     1 
ATOM   8383  C  CA    . ILE B 1 266 ? 192.808 204.595 164.804 1.00 24.75  ?  285 ILE B CA    1 
ATOM   8384  C  C     . ILE B 1 266 ? 192.610 203.940 163.444 1.00 17.58  ?  285 ILE B C     1 
ATOM   8385  O  O     . ILE B 1 266 ? 193.446 204.080 162.542 1.00 37.87  ?  285 ILE B O     1 
ATOM   8386  C  CB    . ILE B 1 266 ? 193.323 203.584 165.843 1.00 24.81  ?  285 ILE B CB    1 
ATOM   8387  C  CG1   . ILE B 1 266 ? 193.936 204.310 167.040 1.00 33.83  ?  285 ILE B CG1   1 
ATOM   8388  C  CG2   . ILE B 1 266 ? 194.335 202.659 165.207 1.00 24.41  ?  285 ILE B CG2   1 
ATOM   8389  C  CD1   . ILE B 1 266 ? 194.120 203.430 168.254 1.00 34.12  ?  285 ILE B CD1   1 
ATOM   8390  N  N     . ILE B 1 267 ? 191.513 203.196 163.285 1.00 10.17  ?  286 ILE B N     1 
ATOM   8391  C  CA    . ILE B 1 267 ? 191.200 202.626 161.978 1.00 18.29  ?  286 ILE B CA    1 
ATOM   8392  C  C     . ILE B 1 267 ? 191.062 203.736 160.946 1.00 42.08  ?  286 ILE B C     1 
ATOM   8393  O  O     . ILE B 1 267 ? 191.552 203.620 159.814 1.00 54.49  ?  286 ILE B O     1 
ATOM   8394  C  CB    . ILE B 1 267 ? 189.930 201.756 162.051 1.00 28.34  ?  286 ILE B CB    1 
ATOM   8395  C  CG1   . ILE B 1 267 ? 190.075 200.678 163.126 1.00 38.37  ?  286 ILE B CG1   1 
ATOM   8396  C  CG2   . ILE B 1 267 ? 189.645 201.114 160.706 1.00 23.87  ?  286 ILE B CG2   1 
ATOM   8397  C  CD1   . ILE B 1 267 ? 188.923 199.697 163.160 1.00 40.09  ?  286 ILE B CD1   1 
ATOM   8398  N  N     . CYS B 1 268 ? 190.417 204.840 161.330 1.00 45.49  ?  287 CYS B N     1 
ATOM   8399  C  CA    . CYS B 1 268 ? 190.270 205.977 160.429 1.00 43.63  ?  287 CYS B CA    1 
ATOM   8400  C  C     . CYS B 1 268 ? 191.624 206.507 159.972 1.00 42.63  ?  287 CYS B C     1 
ATOM   8401  O  O     . CYS B 1 268 ? 191.858 206.700 158.773 1.00 41.14  ?  287 CYS B O     1 
ATOM   8402  C  CB    . CYS B 1 268 ? 189.470 207.084 161.119 1.00 50.36  ?  287 CYS B CB    1 
ATOM   8403  S  SG    . CYS B 1 268 ? 187.682 206.831 161.151 1.00 60.92  ?  287 CYS B SG    1 
ATOM   8404  N  N     . ARG B 1 269 ? 192.529 206.752 160.921 1.00 43.50  ?  288 ARG B N     1 
ATOM   8405  C  CA    . ARG B 1 269 ? 193.826 207.333 160.584 1.00 35.57  ?  288 ARG B CA    1 
ATOM   8406  C  C     . ARG B 1 269 ? 194.668 206.376 159.753 1.00 42.71  ?  288 ARG B C     1 
ATOM   8407  O  O     . ARG B 1 269 ? 195.367 206.805 158.829 1.00 49.20  ?  288 ARG B O     1 
ATOM   8408  C  CB    . ARG B 1 269 ? 194.578 207.745 161.851 1.00 37.07  ?  288 ARG B CB    1 
ATOM   8409  C  CG    . ARG B 1 269 ? 193.824 208.683 162.789 1.00 43.77  ?  288 ARG B CG    1 
ATOM   8410  C  CD    . ARG B 1 269 ? 193.917 210.158 162.379 1.00 51.78  ?  288 ARG B CD    1 
ATOM   8411  N  NE    . ARG B 1 269 ? 193.454 210.421 161.021 1.00 52.50  ?  288 ARG B NE    1 
ATOM   8412  C  CZ    . ARG B 1 269 ? 192.181 210.424 160.648 1.00 52.72  ?  288 ARG B CZ    1 
ATOM   8413  N  NH1   . ARG B 1 269 ? 191.207 210.187 161.511 1.00 45.21  1  288 ARG B NH1   1 
ATOM   8414  N  NH2   . ARG B 1 269 ? 191.878 210.675 159.378 1.00 52.50  ?  288 ARG B NH2   1 
ATOM   8415  N  N     . ASN B 1 270 ? 194.629 205.079 160.067 1.00 42.22  ?  289 ASN B N     1 
ATOM   8416  C  CA    . ASN B 1 270 ? 195.386 204.120 159.268 1.00 28.50  ?  289 ASN B CA    1 
ATOM   8417  C  C     . ASN B 1 270 ? 194.853 204.041 157.843 1.00 27.21  ?  289 ASN B C     1 
ATOM   8418  O  O     . ASN B 1 270 ? 195.636 204.003 156.884 1.00 41.47  ?  289 ASN B O     1 
ATOM   8419  C  CB    . ASN B 1 270 ? 195.365 202.743 159.928 1.00 20.59  ?  289 ASN B CB    1 
ATOM   8420  C  CG    . ASN B 1 270 ? 196.388 202.614 161.036 1.00 29.15  ?  289 ASN B CG    1 
ATOM   8421  O  OD1   . ASN B 1 270 ? 197.584 202.484 160.780 1.00 33.84  ?  289 ASN B OD1   1 
ATOM   8422  N  ND2   . ASN B 1 270 ? 195.923 202.653 162.277 1.00 36.04  ?  289 ASN B ND2   1 
ATOM   8423  N  N     . ILE B 1 271 ? 193.526 204.029 157.680 1.00 26.70  ?  290 ILE B N     1 
ATOM   8424  C  CA    . ILE B 1 271 ? 192.956 204.003 156.336 1.00 34.57  ?  290 ILE B CA    1 
ATOM   8425  C  C     . ILE B 1 271 ? 193.319 205.273 155.577 1.00 52.51  ?  290 ILE B C     1 
ATOM   8426  O  O     . ILE B 1 271 ? 193.630 205.226 154.384 1.00 57.66  ?  290 ILE B O     1 
ATOM   8427  C  CB    . ILE B 1 271 ? 191.433 203.788 156.389 1.00 33.58  ?  290 ILE B CB    1 
ATOM   8428  C  CG1   . ILE B 1 271 ? 191.101 202.431 157.007 1.00 34.56  ?  290 ILE B CG1   1 
ATOM   8429  C  CG2   . ILE B 1 271 ? 190.834 203.882 154.996 1.00 42.12  ?  290 ILE B CG2   1 
ATOM   8430  C  CD1   . ILE B 1 271 ? 189.630 202.241 157.281 1.00 39.67  ?  290 ILE B CD1   1 
ATOM   8431  N  N     . GLU B 1 272 ? 193.285 206.426 156.250 1.00 54.75  ?  291 GLU B N     1 
ATOM   8432  C  CA    . GLU B 1 272 ? 193.629 207.677 155.577 1.00 42.94  ?  291 GLU B CA    1 
ATOM   8433  C  C     . GLU B 1 272 ? 195.102 207.713 155.180 1.00 48.01  ?  291 GLU B C     1 
ATOM   8434  O  O     . GLU B 1 272 ? 195.449 208.195 154.095 1.00 55.87  ?  291 GLU B O     1 
ATOM   8435  C  CB    . GLU B 1 272 ? 193.281 208.867 156.472 1.00 48.97  ?  291 GLU B CB    1 
ATOM   8436  C  CG    . GLU B 1 272 ? 193.757 210.209 155.935 1.00 58.87  ?  291 GLU B CG    1 
ATOM   8437  C  CD    . GLU B 1 272 ? 192.868 211.359 156.368 1.00 61.23  ?  291 GLU B CD    1 
ATOM   8438  O  OE1   . GLU B 1 272 ? 191.821 211.099 156.998 1.00 62.97  ?  291 GLU B OE1   1 
ATOM   8439  O  OE2   . GLU B 1 272 ? 193.214 212.522 156.074 1.00 57.51  -1 291 GLU B OE2   1 
ATOM   8440  N  N     . SER B 1 273 ? 195.985 207.220 156.052 1.00 41.46  ?  292 SER B N     1 
ATOM   8441  C  CA    . SER B 1 273 ? 197.406 207.171 155.725 1.00 40.60  ?  292 SER B CA    1 
ATOM   8442  C  C     . SER B 1 273 ? 197.666 206.240 154.549 1.00 39.74  ?  292 SER B C     1 
ATOM   8443  O  O     . SER B 1 273 ? 198.494 206.539 153.680 1.00 48.27  ?  292 SER B O     1 
ATOM   8444  C  CB    . SER B 1 273 ? 198.213 206.735 156.948 1.00 42.34  ?  292 SER B CB    1 
ATOM   8445  O  OG    . SER B 1 273 ? 197.915 205.398 157.310 1.00 44.25  ?  292 SER B OG    1 
ATOM   8446  N  N     . VAL B 1 274 ? 196.974 205.099 154.508 1.00 35.02  ?  293 VAL B N     1 
ATOM   8447  C  CA    . VAL B 1 274 ? 197.094 204.210 153.358 1.00 37.16  ?  293 VAL B CA    1 
ATOM   8448  C  C     . VAL B 1 274 ? 196.531 204.874 152.107 1.00 39.40  ?  293 VAL B C     1 
ATOM   8449  O  O     . VAL B 1 274 ? 197.081 204.720 151.009 1.00 47.53  ?  293 VAL B O     1 
ATOM   8450  C  CB    . VAL B 1 274 ? 196.396 202.870 153.661 1.00 46.89  ?  293 VAL B CB    1 
ATOM   8451  C  CG1   . VAL B 1 274 ? 196.140 202.087 152.384 1.00 47.23  ?  293 VAL B CG1   1 
ATOM   8452  C  CG2   . VAL B 1 274 ? 197.219 202.052 154.645 1.00 45.81  ?  293 VAL B CG2   1 
ATOM   8453  N  N     . LEU B 1 275 ? 195.452 205.643 152.253 1.00 44.51  ?  294 LEU B N     1 
ATOM   8454  C  CA    . LEU B 1 275 ? 194.764 206.309 151.150 1.00 52.92  ?  294 LEU B CA    1 
ATOM   8455  C  C     . LEU B 1 275 ? 194.702 207.793 151.502 1.00 61.97  ?  294 LEU B C     1 
ATOM   8456  O  O     . LEU B 1 275 ? 193.702 208.264 152.050 1.00 64.13  ?  294 LEU B O     1 
ATOM   8457  C  CB    . LEU B 1 275 ? 193.371 205.722 150.954 1.00 51.62  ?  294 LEU B CB    1 
ATOM   8458  C  CG    . LEU B 1 275 ? 193.274 204.247 150.565 1.00 54.01  ?  294 LEU B CG    1 
ATOM   8459  C  CD1   . LEU B 1 275 ? 191.945 203.660 151.019 1.00 54.69  ?  294 LEU B CD1   1 
ATOM   8460  C  CD2   . LEU B 1 275 ? 193.443 204.083 149.074 1.00 54.34  ?  294 LEU B CD2   1 
ATOM   8461  N  N     . ASN B 1 276 ? 195.778 208.517 151.204 1.00 59.38  ?  295 ASN B N     1 
ATOM   8462  C  CA    . ASN B 1 276 ? 195.837 209.952 151.451 1.00 59.63  ?  295 ASN B CA    1 
ATOM   8463  C  C     . ASN B 1 276 ? 194.685 210.676 150.762 1.00 62.22  ?  295 ASN B C     1 
ATOM   8464  O  O     . ASN B 1 276 ? 194.196 210.255 149.709 1.00 58.55  ?  295 ASN B O     1 
ATOM   8465  C  CB    . ASN B 1 276 ? 197.172 210.518 150.965 1.00 59.11  ?  295 ASN B CB    1 
ATOM   8466  C  CG    . ASN B 1 276 ? 197.539 210.031 149.575 1.00 63.94  ?  295 ASN B CG    1 
ATOM   8467  O  OD1   . ASN B 1 276 ? 196.807 209.254 148.962 1.00 64.06  ?  295 ASN B OD1   1 
ATOM   8468  N  ND2   . ASN B 1 276 ? 198.678 210.491 149.069 1.00 62.39  ?  295 ASN B ND2   1 
ATOM   8469  N  N     . GLU B 1 277 ? 194.249 211.776 151.380 1.00 70.64  ?  296 GLU B N     1 
ATOM   8470  C  CA    . GLU B 1 277 ? 193.116 212.573 150.908 1.00 72.48  ?  296 GLU B CA    1 
ATOM   8471  C  C     . GLU B 1 277 ? 191.836 211.734 150.872 1.00 74.54  ?  296 GLU B C     1 
ATOM   8472  O  O     . GLU B 1 277 ? 191.212 211.537 149.828 1.00 68.69  ?  296 GLU B O     1 
ATOM   8473  C  CB    . GLU B 1 277 ? 193.409 213.199 149.539 1.00 71.04  ?  296 GLU B CB    1 
ATOM   8474  C  CG    . GLU B 1 277 ? 194.602 214.144 149.521 1.00 71.96  ?  296 GLU B CG    1 
ATOM   8475  C  CD    . GLU B 1 277 ? 194.359 215.407 150.325 1.00 73.37  ?  296 GLU B CD    1 
ATOM   8476  O  OE1   . GLU B 1 277 ? 193.198 215.865 150.378 1.00 74.68  ?  296 GLU B OE1   1 
ATOM   8477  O  OE2   . GLU B 1 277 ? 195.329 215.944 150.901 1.00 73.48  -1 296 GLU B OE2   1 
ATOM   8478  N  N     . SER B 1 278 ? 191.457 211.237 152.048 1.00 75.86  ?  297 SER B N     1 
ATOM   8479  C  CA    . SER B 1 278 ? 190.255 210.432 152.198 1.00 74.43  ?  297 SER B CA    1 
ATOM   8480  C  C     . SER B 1 278 ? 189.517 210.849 153.461 1.00 69.80  ?  297 SER B C     1 
ATOM   8481  O  O     . SER B 1 278 ? 190.127 211.285 154.440 1.00 73.49  ?  297 SER B O     1 
ATOM   8482  C  CB    . SER B 1 278 ? 190.585 208.933 152.256 1.00 71.71  ?  297 SER B CB    1 
ATOM   8483  O  OG    . SER B 1 278 ? 189.415 208.142 152.144 1.00 74.78  ?  297 SER B OG    1 
ATOM   8484  N  N     . HIS B 1 279 ? 188.193 210.712 153.426 1.00 55.06  ?  298 HIS B N     1 
ATOM   8485  C  CA    . HIS B 1 279 ? 187.334 210.933 154.580 1.00 57.37  ?  298 HIS B CA    1 
ATOM   8486  C  C     . HIS B 1 279 ? 186.727 209.590 154.963 1.00 66.70  ?  298 HIS B C     1 
ATOM   8487  O  O     . HIS B 1 279 ? 185.998 208.984 154.176 1.00 62.44  ?  298 HIS B O     1 
ATOM   8488  C  CB    . HIS B 1 279 ? 186.250 211.966 154.269 1.00 55.88  ?  298 HIS B CB    1 
ATOM   8489  C  CG    . HIS B 1 279 ? 185.196 212.082 155.327 1.00 62.79  ?  298 HIS B CG    1 
ATOM   8490  N  ND1   . HIS B 1 279 ? 184.188 211.155 155.482 1.00 63.12  ?  298 HIS B ND1   1 
ATOM   8491  C  CD2   . HIS B 1 279 ? 184.993 213.020 156.282 1.00 62.63  ?  298 HIS B CD2   1 
ATOM   8492  C  CE1   . HIS B 1 279 ? 183.411 211.515 156.488 1.00 60.21  ?  298 HIS B CE1   1 
ATOM   8493  N  NE2   . HIS B 1 279 ? 183.878 212.644 156.991 1.00 62.66  ?  298 HIS B NE2   1 
ATOM   8494  N  N     . VAL B 1 280 ? 187.038 209.125 156.165 1.00 56.69  ?  299 VAL B N     1 
ATOM   8495  C  CA    . VAL B 1 280 ? 186.736 207.764 156.584 1.00 48.11  ?  299 VAL B CA    1 
ATOM   8496  C  C     . VAL B 1 280 ? 185.983 207.792 157.906 1.00 51.90  ?  299 VAL B C     1 
ATOM   8497  O  O     . VAL B 1 280 ? 186.313 208.575 158.804 1.00 55.25  ?  299 VAL B O     1 
ATOM   8498  C  CB    . VAL B 1 280 ? 188.029 206.927 156.674 1.00 50.41  ?  299 VAL B CB    1 
ATOM   8499  C  CG1   . VAL B 1 280 ? 188.965 207.533 157.675 1.00 52.72  ?  299 VAL B CG1   1 
ATOM   8500  C  CG2   . VAL B 1 280 ? 187.709 205.505 157.089 1.00 48.64  ?  299 VAL B CG2   1 
ATOM   8501  N  N     . SER B 1 281 ? 184.954 206.951 158.015 1.00 51.07  ?  300 SER B N     1 
ATOM   8502  C  CA    . SER B 1 281 ? 184.131 206.931 159.214 1.00 38.97  ?  300 SER B CA    1 
ATOM   8503  C  C     . SER B 1 281 ? 183.552 205.538 159.427 1.00 35.07  ?  300 SER B C     1 
ATOM   8504  O  O     . SER B 1 281 ? 183.450 204.729 158.498 1.00 50.79  ?  300 SER B O     1 
ATOM   8505  C  CB    . SER B 1 281 ? 183.017 207.983 159.137 1.00 39.50  ?  300 SER B CB    1 
ATOM   8506  O  OG    . SER B 1 281 ? 182.273 207.857 157.941 1.00 39.78  ?  300 SER B OG    1 
ATOM   8507  N  N     . LEU B 1 282 ? 183.179 205.276 160.678 1.00 16.76  ?  301 LEU B N     1 
ATOM   8508  C  CA    . LEU B 1 282 ? 182.661 203.989 161.115 1.00 20.97  ?  301 LEU B CA    1 
ATOM   8509  C  C     . LEU B 1 282 ? 181.418 204.199 161.967 1.00 29.05  ?  301 LEU B C     1 
ATOM   8510  O  O     . LEU B 1 282 ? 181.344 205.145 162.758 1.00 32.86  ?  301 LEU B O     1 
ATOM   8511  C  CB    . LEU B 1 282 ? 183.703 203.201 161.927 1.00 16.91  ?  301 LEU B CB    1 
ATOM   8512  C  CG    . LEU B 1 282 ? 184.949 202.681 161.208 1.00 16.98  ?  301 LEU B CG    1 
ATOM   8513  C  CD1   . LEU B 1 282 ? 186.105 203.654 161.353 1.00 33.35  ?  301 LEU B CD1   1 
ATOM   8514  C  CD2   . LEU B 1 282 ? 185.340 201.306 161.721 1.00 27.27  ?  301 LEU B CD2   1 
ATOM   8515  N  N     . PHE B 1 283 ? 180.451 203.294 161.802 1.00 33.70  ?  302 PHE B N     1 
ATOM   8516  C  CA    . PHE B 1 283 ? 179.212 203.267 162.564 1.00 20.14  ?  302 PHE B CA    1 
ATOM   8517  C  C     . PHE B 1 283 ? 179.036 201.875 163.153 1.00 22.70  ?  302 PHE B C     1 
ATOM   8518  O  O     . PHE B 1 283 ? 179.364 200.880 162.502 1.00 40.66  ?  302 PHE B O     1 
ATOM   8519  C  CB    . PHE B 1 283 ? 177.998 203.594 161.685 1.00 20.83  ?  302 PHE B CB    1 
ATOM   8520  C  CG    . PHE B 1 283 ? 178.090 204.910 160.973 1.00 30.92  ?  302 PHE B CG    1 
ATOM   8521  C  CD1   . PHE B 1 283 ? 178.178 206.097 161.678 1.00 39.15  ?  302 PHE B CD1   1 
ATOM   8522  C  CD2   . PHE B 1 283 ? 178.069 204.958 159.590 1.00 24.30  ?  302 PHE B CD2   1 
ATOM   8523  C  CE1   . PHE B 1 283 ? 178.256 207.307 161.016 1.00 37.45  ?  302 PHE B CE1   1 
ATOM   8524  C  CE2   . PHE B 1 283 ? 178.144 206.160 158.925 1.00 22.62  ?  302 PHE B CE2   1 
ATOM   8525  C  CZ    . PHE B 1 283 ? 178.239 207.338 159.638 1.00 29.50  ?  302 PHE B CZ    1 
ATOM   8526  N  N     . ALA B 1 284 ? 178.496 201.807 164.368 1.00 16.32  ?  303 ALA B N     1 
ATOM   8527  C  CA    . ALA B 1 284 ? 178.219 200.545 165.040 1.00 15.44  ?  303 ALA B CA    1 
ATOM   8528  C  C     . ALA B 1 284 ? 176.726 200.436 165.314 1.00 26.62  ?  303 ALA B C     1 
ATOM   8529  O  O     . ALA B 1 284 ? 176.121 201.372 165.847 1.00 42.81  ?  303 ALA B O     1 
ATOM   8530  C  CB    . ALA B 1 284 ? 179.009 200.431 166.347 1.00 21.32  ?  303 ALA B CB    1 
ATOM   8531  N  N     . LEU B 1 285 ? 176.132 199.302 164.945 1.00 35.05  ?  304 LEU B N     1 
ATOM   8532  C  CA    . LEU B 1 285 ? 174.702 199.096 165.124 1.00 34.44  ?  304 LEU B CA    1 
ATOM   8533  C  C     . LEU B 1 285 ? 174.353 198.963 166.601 1.00 40.29  ?  304 LEU B C     1 
ATOM   8534  O  O     . LEU B 1 285 ? 175.080 198.331 167.373 1.00 42.85  ?  304 LEU B O     1 
ATOM   8535  C  CB    . LEU B 1 285 ? 174.244 197.846 164.369 1.00 25.88  ?  304 LEU B CB    1 
ATOM   8536  C  CG    . LEU B 1 285 ? 173.710 198.023 162.946 1.00 21.28  ?  304 LEU B CG    1 
ATOM   8537  C  CD1   . LEU B 1 285 ? 172.354 198.707 162.960 1.00 37.60  ?  304 LEU B CD1   1 
ATOM   8538  C  CD2   . LEU B 1 285 ? 174.683 198.799 162.083 1.00 24.82  ?  304 LEU B CD2   1 
ATOM   8539  N  N     . ARG B 1 286 ? 173.232 199.567 166.990 1.00 39.51  ?  305 ARG B N     1 
ATOM   8540  C  CA    . ARG B 1 286 ? 172.703 199.463 168.349 1.00 44.14  ?  305 ARG B CA    1 
ATOM   8541  C  C     . ARG B 1 286 ? 171.204 199.196 168.249 1.00 43.27  ?  305 ARG B C     1 
ATOM   8542  O  O     . ARG B 1 286 ? 170.422 200.116 167.986 1.00 43.23  ?  305 ARG B O     1 
ATOM   8543  C  CB    . ARG B 1 286 ? 172.990 200.724 169.158 1.00 46.42  ?  305 ARG B CB    1 
ATOM   8544  C  CG    . ARG B 1 286 ? 174.350 200.731 169.840 1.00 43.43  ?  305 ARG B CG    1 
ATOM   8545  C  CD    . ARG B 1 286 ? 174.361 201.659 171.046 1.00 46.89  ?  305 ARG B CD    1 
ATOM   8546  N  NE    . ARG B 1 286 ? 175.715 201.921 171.520 1.00 45.86  ?  305 ARG B NE    1 
ATOM   8547  C  CZ    . ARG B 1 286 ? 176.383 201.137 172.355 1.00 48.26  ?  305 ARG B CZ    1 
ATOM   8548  N  NH1   . ARG B 1 286 ? 175.850 200.026 172.836 1.00 44.16  1  305 ARG B NH1   1 
ATOM   8549  N  NH2   . ARG B 1 286 ? 177.618 201.476 172.714 1.00 46.02  ?  305 ARG B NH2   1 
ATOM   8550  N  N     . ASN B 1 287 ? 170.812 197.938 168.463 1.00 51.09  ?  306 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 287 ? 169.411 197.517 168.394 1.00 53.42  ?  306 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 287 ? 168.787 197.871 167.046 1.00 52.44  ?  306 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 287 ? 167.623 198.267 166.964 1.00 57.67  ?  306 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 287 ? 168.596 198.117 169.543 1.00 52.53  ?  306 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 287 ? 169.263 197.928 170.890 1.00 56.55  ?  306 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 287 ? 169.933 196.924 171.129 1.00 57.44  ?  306 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 287 ? 169.080 198.896 171.781 1.00 53.51  ?  306 ASN B ND2   1 
ATOM   8558  N  N     . GLY B 1 288 ? 169.567 197.726 165.976 1.00 45.65  ?  307 GLY B N     1 
ATOM   8559  C  CA    . GLY B 1 288 ? 169.103 198.028 164.641 1.00 43.66  ?  307 GLY B CA    1 
ATOM   8560  C  C     . GLY B 1 288 ? 169.257 199.473 164.217 1.00 48.02  ?  307 GLY B C     1 
ATOM   8561  O  O     . GLY B 1 288 ? 168.953 199.797 163.062 1.00 46.81  ?  307 GLY B O     1 
ATOM   8562  N  N     . MET B 1 289 ? 169.718 200.350 165.109 1.00 46.83  ?  308 MET B N     1 
ATOM   8563  C  CA    . MET B 1 289 ? 169.904 201.754 164.779 1.00 42.68  ?  308 MET B CA    1 
ATOM   8564  C  C     . MET B 1 289 ? 171.381 202.039 164.570 1.00 45.88  ?  308 MET B C     1 
ATOM   8565  O  O     . MET B 1 289 ? 172.167 201.900 165.521 1.00 47.28  ?  308 MET B O     1 
ATOM   8566  C  CB    . MET B 1 289 ? 169.349 202.642 165.886 1.00 44.00  ?  308 MET B CB    1 
ATOM   8567  C  CG    . MET B 1 289 ? 169.396 204.127 165.572 1.00 49.03  ?  308 MET B CG    1 
ATOM   8568  S  SD    . MET B 1 289 ? 169.421 205.148 167.058 1.00 62.75  ?  308 MET B SD    1 
ATOM   8569  C  CE    . MET B 1 289 ? 167.740 204.930 167.638 1.00 44.20  ?  308 MET B CE    1 
ATOM   8570  N  N     . PRO B 1 290 ? 171.808 202.427 163.367 1.00 41.08  ?  309 PRO B N     1 
ATOM   8571  C  CA    . PRO B 1 290 ? 173.225 202.758 163.162 1.00 34.58  ?  309 PRO B CA    1 
ATOM   8572  C  C     . PRO B 1 290 ? 173.605 204.079 163.813 1.00 28.18  ?  309 PRO B C     1 
ATOM   8573  O  O     . PRO B 1 290 ? 173.171 205.148 163.372 1.00 36.87  ?  309 PRO B O     1 
ATOM   8574  C  CB    . PRO B 1 290 ? 173.354 202.822 161.635 1.00 31.92  ?  309 PRO B CB    1 
ATOM   8575  C  CG    . PRO B 1 290 ? 171.986 203.145 161.151 1.00 33.57  ?  309 PRO B CG    1 
ATOM   8576  C  CD    . PRO B 1 290 ? 171.025 202.521 162.123 1.00 33.72  ?  309 PRO B CD    1 
ATOM   8577  N  N     . ILE B 1 291 ? 174.416 204.015 164.863 1.00 16.43  ?  310 ILE B N     1 
ATOM   8578  C  CA    . ILE B 1 291 ? 174.865 205.200 165.569 1.00 25.30  ?  310 ILE B CA    1 
ATOM   8579  C  C     . ILE B 1 291 ? 176.267 205.549 165.091 1.00 31.96  ?  310 ILE B C     1 
ATOM   8580  O  O     . ILE B 1 291 ? 176.945 204.758 164.431 1.00 38.99  ?  310 ILE B O     1 
ATOM   8581  C  CB    . ILE B 1 291 ? 174.835 205.006 167.101 1.00 28.32  ?  310 ILE B CB    1 
ATOM   8582  C  CG1   . ILE B 1 291 ? 175.980 204.092 167.540 1.00 26.39  ?  310 ILE B CG1   1 
ATOM   8583  C  CG2   . ILE B 1 291 ? 173.495 204.438 167.543 1.00 31.88  ?  310 ILE B CG2   1 
ATOM   8584  C  CD1   . ILE B 1 291 ? 176.220 204.087 169.031 1.00 36.45  ?  310 ILE B CD1   1 
ATOM   8585  N  N     . HIS B 1 292 ? 176.713 206.755 165.432 1.00 39.20  ?  311 HIS B N     1 
ATOM   8586  C  CA    . HIS B 1 292 ? 178.030 207.210 165.014 1.00 32.81  ?  311 HIS B CA    1 
ATOM   8587  C  C     . HIS B 1 292 ? 179.101 206.676 165.955 1.00 32.78  ?  311 HIS B C     1 
ATOM   8588  O  O     . HIS B 1 292 ? 179.006 206.819 167.177 1.00 37.55  ?  311 HIS B O     1 
ATOM   8589  C  CB    . HIS B 1 292 ? 178.081 208.738 164.969 1.00 37.72  ?  311 HIS B CB    1 
ATOM   8590  C  CG    . HIS B 1 292 ? 179.456 209.291 164.751 1.00 42.03  ?  311 HIS B CG    1 
ATOM   8591  N  ND1   . HIS B 1 292 ? 180.350 209.491 165.781 1.00 46.13  ?  311 HIS B ND1   1 
ATOM   8592  C  CD2   . HIS B 1 292 ? 180.090 209.684 163.621 1.00 35.94  ?  311 HIS B CD2   1 
ATOM   8593  C  CE1   . HIS B 1 292 ? 181.475 209.985 165.295 1.00 44.31  ?  311 HIS B CE1   1 
ATOM   8594  N  NE2   . HIS B 1 292 ? 181.344 210.111 163.987 1.00 36.58  ?  311 HIS B NE2   1 
ATOM   8595  N  N     . TRP B 1 293 ? 180.128 206.063 165.372 1.00 28.03  ?  312 TRP B N     1 
ATOM   8596  C  CA    . TRP B 1 293 ? 181.234 205.480 166.120 1.00 34.33  ?  312 TRP B CA    1 
ATOM   8597  C  C     . TRP B 1 293 ? 182.510 206.293 165.977 1.00 31.02  ?  312 TRP B C     1 
ATOM   8598  O  O     . TRP B 1 293 ? 183.138 206.634 166.987 1.00 36.68  ?  312 TRP B O     1 
ATOM   8599  C  CB    . TRP B 1 293 ? 181.448 204.024 165.658 1.00 37.97  ?  312 TRP B CB    1 
ATOM   8600  C  CG    . TRP B 1 293 ? 182.680 203.318 166.174 1.00 35.16  ?  312 TRP B CG    1 
ATOM   8601  C  CD1   . TRP B 1 293 ? 183.508 203.715 167.186 1.00 29.83  ?  312 TRP B CD1   1 
ATOM   8602  C  CD2   . TRP B 1 293 ? 183.207 202.077 165.694 1.00 19.18  ?  312 TRP B CD2   1 
ATOM   8603  N  NE1   . TRP B 1 293 ? 184.520 202.804 167.357 1.00 32.58  ?  312 TRP B NE1   1 
ATOM   8604  C  CE2   . TRP B 1 293 ? 184.357 201.787 166.453 1.00 26.13  ?  312 TRP B CE2   1 
ATOM   8605  C  CE3   . TRP B 1 293 ? 182.818 201.182 164.693 1.00 9.39   ?  312 TRP B CE3   1 
ATOM   8606  C  CZ2   . TRP B 1 293 ? 185.121 200.642 166.244 1.00 36.16  ?  312 TRP B CZ2   1 
ATOM   8607  C  CZ3   . TRP B 1 293 ? 183.576 200.047 164.487 1.00 14.87  ?  312 TRP B CZ3   1 
ATOM   8608  C  CH2   . TRP B 1 293 ? 184.714 199.786 165.258 1.00 28.65  ?  312 TRP B CH2   1 
ATOM   8609  N  N     . ALA B 1 294 ? 182.907 206.631 164.753 1.00 37.72  ?  313 ALA B N     1 
ATOM   8610  C  CA    . ALA B 1 294 ? 184.088 207.464 164.563 1.00 33.85  ?  313 ALA B CA    1 
ATOM   8611  C  C     . ALA B 1 294 ? 184.027 208.110 163.190 1.00 36.12  ?  313 ALA B C     1 
ATOM   8612  O  O     . ALA B 1 294 ? 183.308 207.651 162.301 1.00 48.14  ?  313 ALA B O     1 
ATOM   8613  C  CB    . ALA B 1 294 ? 185.381 206.657 164.717 1.00 34.34  ?  313 ALA B CB    1 
ATOM   8614  N  N     . SER B 1 295 ? 184.814 209.170 163.024 1.00 31.80  ?  314 SER B N     1 
ATOM   8615  C  CA    . SER B 1 295 ? 184.903 209.864 161.749 1.00 34.88  ?  314 SER B CA    1 
ATOM   8616  C  C     . SER B 1 295 ? 186.228 210.607 161.681 1.00 44.99  ?  314 SER B C     1 
ATOM   8617  O  O     . SER B 1 295 ? 186.871 210.865 162.702 1.00 50.27  ?  314 SER B O     1 
ATOM   8618  C  CB    . SER B 1 295 ? 183.730 210.833 161.550 1.00 45.70  ?  314 SER B CB    1 
ATOM   8619  O  OG    . SER B 1 295 ? 183.756 211.407 160.255 1.00 43.78  ?  314 SER B OG    1 
ATOM   8620  N  N     . SER B 1 296 ? 186.632 210.943 160.459 1.00 61.71  ?  315 SER B N     1 
ATOM   8621  C  CA    . SER B 1 296 ? 187.852 211.711 160.242 1.00 68.67  ?  315 SER B CA    1 
ATOM   8622  C  C     . SER B 1 296 ? 187.578 213.190 160.491 1.00 70.29  ?  315 SER B C     1 
ATOM   8623  O  O     . SER B 1 296 ? 186.657 213.765 159.901 1.00 70.86  ?  315 SER B O     1 
ATOM   8624  C  CB    . SER B 1 296 ? 188.379 211.487 158.827 1.00 61.96  ?  315 SER B CB    1 
ATOM   8625  O  OG    . SER B 1 296 ? 187.413 211.853 157.859 1.00 59.86  ?  315 SER B OG    1 
ATOM   8626  N  N     . SER B 1 297 ? 188.375 213.802 161.371 1.00 84.74  ?  316 SER B N     1 
ATOM   8627  C  CA    . SER B 1 297 ? 188.168 215.200 161.733 1.00 86.59  ?  316 SER B CA    1 
ATOM   8628  C  C     . SER B 1 297 ? 188.453 216.158 160.583 1.00 89.25  ?  316 SER B C     1 
ATOM   8629  O  O     . SER B 1 297 ? 188.041 217.321 160.650 1.00 90.86  ?  316 SER B O     1 
ATOM   8630  C  CB    . SER B 1 297 ? 189.039 215.566 162.935 1.00 86.45  ?  316 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 297 ? 190.402 215.675 162.564 1.00 89.35  ?  316 SER B OG    1 
ATOM   8632  N  N     . HIS B 1 298 ? 189.146 215.707 159.538 1.00 93.91  ?  317 HIS B N     1 
ATOM   8633  C  CA    . HIS B 1 298 ? 189.445 216.574 158.404 1.00 94.09  ?  317 HIS B CA    1 
ATOM   8634  C  C     . HIS B 1 298 ? 188.194 216.780 157.560 1.00 93.12  ?  317 HIS B C     1 
ATOM   8635  O  O     . HIS B 1 298 ? 187.944 216.029 156.612 1.00 93.58  ?  317 HIS B O     1 
ATOM   8636  C  CB    . HIS B 1 298 ? 190.576 215.986 157.556 1.00 94.98  ?  317 HIS B CB    1 
ATOM   8637  C  CG    . HIS B 1 298 ? 191.068 216.909 156.485 1.00 97.08  ?  317 HIS B CG    1 
ATOM   8638  N  ND1   . HIS B 1 298 ? 191.600 216.455 155.297 1.00 96.99  ?  317 HIS B ND1   1 
ATOM   8639  C  CD2   . HIS B 1 298 ? 191.111 218.261 156.423 1.00 94.55  ?  317 HIS B CD2   1 
ATOM   8640  C  CE1   . HIS B 1 298 ? 191.949 217.487 154.550 1.00 94.98  ?  317 HIS B CE1   1 
ATOM   8641  N  NE2   . HIS B 1 298 ? 191.662 218.595 155.210 1.00 94.87  ?  317 HIS B NE2   1 
ATOM   8642  N  N     . GLY B 1 299 ? 187.406 217.800 157.897 1.00 97.93  ?  318 GLY B N     1 
ATOM   8643  C  CA    . GLY B 1 299 ? 186.129 218.057 157.268 1.00 97.65  ?  318 GLY B CA    1 
ATOM   8644  C  C     . GLY B 1 299 ? 186.170 218.808 155.959 1.00 98.26  ?  318 GLY B C     1 
ATOM   8645  O  O     . GLY B 1 299 ? 185.118 219.242 155.480 1.00 97.71  ?  318 GLY B O     1 
ATOM   8646  N  N     . ALA B 1 300 ? 187.349 218.989 155.368 1.00 97.64  ?  319 ALA B N     1 
ATOM   8647  C  CA    . ALA B 1 300 ? 187.440 219.658 154.077 1.00 99.34  ?  319 ALA B CA    1 
ATOM   8648  C  C     . ALA B 1 300 ? 186.691 218.865 153.013 1.00 100.54 ?  319 ALA B C     1 
ATOM   8649  O  O     . ALA B 1 300 ? 186.747 217.632 152.977 1.00 98.49  ?  319 ALA B O     1 
ATOM   8650  C  CB    . ALA B 1 300 ? 188.903 219.837 153.673 1.00 96.05  ?  319 ALA B CB    1 
ATOM   8651  N  N     . GLU B 1 301 ? 185.981 219.583 152.145 1.00 96.33  ?  320 GLU B N     1 
ATOM   8652  C  CA    . GLU B 1 301 ? 185.163 218.939 151.127 1.00 94.18  ?  320 GLU B CA    1 
ATOM   8653  C  C     . GLU B 1 301 ? 186.044 218.217 150.115 1.00 92.28  ?  320 GLU B C     1 
ATOM   8654  O  O     . GLU B 1 301 ? 186.956 218.811 149.532 1.00 92.52  ?  320 GLU B O     1 
ATOM   8655  C  CB    . GLU B 1 301 ? 184.285 219.973 150.425 1.00 95.34  ?  320 GLU B CB    1 
ATOM   8656  C  CG    . GLU B 1 301 ? 183.135 220.487 151.275 1.00 94.59  ?  320 GLU B CG    1 
ATOM   8657  C  CD    . GLU B 1 301 ? 182.155 221.330 150.483 1.00 93.78  ?  320 GLU B CD    1 
ATOM   8658  O  OE1   . GLU B 1 301 ? 182.097 221.171 149.246 1.00 91.79  ?  320 GLU B OE1   1 
ATOM   8659  O  OE2   . GLU B 1 301 ? 181.445 222.153 151.098 1.00 94.12  -1 320 GLU B OE2   1 
ATOM   8660  N  N     . ILE B 1 302 ? 185.769 216.934 149.907 1.00 83.50  ?  321 ILE B N     1 
ATOM   8661  C  CA    . ILE B 1 302 ? 186.523 216.119 148.963 1.00 85.31  ?  321 ILE B CA    1 
ATOM   8662  C  C     . ILE B 1 302 ? 185.808 216.140 147.620 1.00 84.43  ?  321 ILE B C     1 
ATOM   8663  O  O     . ILE B 1 302 ? 184.616 215.820 147.533 1.00 83.55  ?  321 ILE B O     1 
ATOM   8664  C  CB    . ILE B 1 302 ? 186.686 214.681 149.484 1.00 86.19  ?  321 ILE B CB    1 
ATOM   8665  C  CG1   . ILE B 1 302 ? 187.666 214.652 150.658 1.00 86.14  ?  321 ILE B CG1   1 
ATOM   8666  C  CG2   . ILE B 1 302 ? 187.174 213.765 148.374 1.00 82.50  ?  321 ILE B CG2   1 
ATOM   8667  C  CD1   . ILE B 1 302 ? 187.939 213.264 151.192 1.00 83.76  ?  321 ILE B CD1   1 
ATOM   8668  N  N     . GLN B 1 303 ? 186.535 216.517 146.572 1.00 80.54  ?  322 GLN B N     1 
ATOM   8669  C  CA    . GLN B 1 303 ? 185.954 216.633 145.242 1.00 80.63  ?  322 GLN B CA    1 
ATOM   8670  C  C     . GLN B 1 303 ? 185.823 215.256 144.604 1.00 79.97  ?  322 GLN B C     1 
ATOM   8671  O  O     . GLN B 1 303 ? 186.758 214.450 144.651 1.00 81.76  ?  322 GLN B O     1 
ATOM   8672  C  CB    . GLN B 1 303 ? 186.815 217.543 144.368 1.00 79.72  ?  322 GLN B CB    1 
ATOM   8673  C  CG    . GLN B 1 303 ? 187.516 218.651 145.139 1.00 80.01  ?  322 GLN B CG    1 
ATOM   8674  C  CD    . GLN B 1 303 ? 188.494 219.430 144.283 1.00 82.54  ?  322 GLN B CD    1 
ATOM   8675  O  OE1   . GLN B 1 303 ? 189.380 218.854 143.651 1.00 82.12  ?  322 GLN B OE1   1 
ATOM   8676  N  NE2   . GLN B 1 303 ? 188.340 220.749 144.259 1.00 83.12  ?  322 GLN B NE2   1 
ATOM   8677  N  N     . ASN B 1 304 ? 184.659 214.994 144.002 1.00 71.42  ?  323 ASN B N     1 
ATOM   8678  C  CA    . ASN B 1 304 ? 184.366 213.713 143.357 1.00 73.19  ?  323 ASN B CA    1 
ATOM   8679  C  C     . ASN B 1 304 ? 184.574 212.551 144.329 1.00 77.67  ?  323 ASN B C     1 
ATOM   8680  O  O     . ASN B 1 304 ? 185.190 211.535 144.001 1.00 77.49  ?  323 ASN B O     1 
ATOM   8681  C  CB    . ASN B 1 304 ? 185.204 213.529 142.090 1.00 74.96  ?  323 ASN B CB    1 
ATOM   8682  C  CG    . ASN B 1 304 ? 185.113 214.717 141.153 1.00 77.13  ?  323 ASN B CG    1 
ATOM   8683  O  OD1   . ASN B 1 304 ? 184.027 215.228 140.883 1.00 80.02  ?  323 ASN B OD1   1 
ATOM   8684  N  ND2   . ASN B 1 304 ? 186.259 215.163 140.651 1.00 75.69  ?  323 ASN B ND2   1 
ATOM   8685  N  N     . ALA B 1 305 ? 184.053 212.716 145.542 1.00 73.10  ?  324 ALA B N     1 
ATOM   8686  C  CA    . ALA B 1 305 ? 184.257 211.739 146.607 1.00 72.29  ?  324 ALA B CA    1 
ATOM   8687  C  C     . ALA B 1 305 ? 183.455 210.477 146.317 1.00 74.90  ?  324 ALA B C     1 
ATOM   8688  O  O     . ALA B 1 305 ? 182.232 210.454 146.492 1.00 75.75  ?  324 ALA B O     1 
ATOM   8689  C  CB    . ALA B 1 305 ? 183.857 212.338 147.952 1.00 71.09  ?  324 ALA B CB    1 
ATOM   8690  N  N     . GLN B 1 306 ? 184.140 209.425 145.875 1.00 71.93  ?  325 GLN B N     1 
ATOM   8691  C  CA    . GLN B 1 306 ? 183.537 208.108 145.733 1.00 67.47  ?  325 GLN B CA    1 
ATOM   8692  C  C     . GLN B 1 306 ? 183.586 207.418 147.090 1.00 61.74  ?  325 GLN B C     1 
ATOM   8693  O  O     . GLN B 1 306 ? 184.657 207.316 147.697 1.00 61.31  ?  325 GLN B O     1 
ATOM   8694  C  CB    . GLN B 1 306 ? 184.274 207.284 144.679 1.00 65.35  ?  325 GLN B CB    1 
ATOM   8695  C  CG    . GLN B 1 306 ? 184.117 207.802 143.260 1.00 71.18  ?  325 GLN B CG    1 
ATOM   8696  C  CD    . GLN B 1 306 ? 184.861 206.957 142.244 1.00 72.08  ?  325 GLN B CD    1 
ATOM   8697  O  OE1   . GLN B 1 306 ? 185.590 206.032 142.601 1.00 70.91  ?  325 GLN B OE1   1 
ATOM   8698  N  NE2   . GLN B 1 306 ? 184.680 207.273 140.967 1.00 67.19  ?  325 GLN B NE2   1 
ATOM   8699  N  N     . SER B 1 307 ? 182.433 206.961 147.567 1.00 53.29  ?  326 SER B N     1 
ATOM   8700  C  CA    . SER B 1 307 ? 182.308 206.364 148.889 1.00 50.32  ?  326 SER B CA    1 
ATOM   8701  C  C     . SER B 1 307 ? 182.126 204.858 148.761 1.00 52.55  ?  326 SER B C     1 
ATOM   8702  O  O     . SER B 1 307 ? 181.269 204.392 148.002 1.00 52.90  ?  326 SER B O     1 
ATOM   8703  C  CB    . SER B 1 307 ? 181.135 206.975 149.659 1.00 53.38  ?  326 SER B CB    1 
ATOM   8704  O  OG    . SER B 1 307 ? 181.124 208.387 149.535 1.00 51.18  ?  326 SER B OG    1 
ATOM   8705  N  N     . TRP B 1 308 ? 182.932 204.109 149.505 1.00 41.11  ?  327 TRP B N     1 
ATOM   8706  C  CA    . TRP B 1 308 ? 182.859 202.659 149.569 1.00 39.30  ?  327 TRP B CA    1 
ATOM   8707  C  C     . TRP B 1 308 ? 182.357 202.267 150.950 1.00 32.18  ?  327 TRP B C     1 
ATOM   8708  O  O     . TRP B 1 308 ? 182.921 202.697 151.962 1.00 34.93  ?  327 TRP B O     1 
ATOM   8709  C  CB    . TRP B 1 308 ? 184.229 202.032 149.309 1.00 43.82  ?  327 TRP B CB    1 
ATOM   8710  C  CG    . TRP B 1 308 ? 184.210 200.541 149.228 1.00 46.59  ?  327 TRP B CG    1 
ATOM   8711  C  CD1   . TRP B 1 308 ? 184.284 199.661 150.266 1.00 40.66  ?  327 TRP B CD1   1 
ATOM   8712  C  CD2   . TRP B 1 308 ? 184.147 199.752 148.035 1.00 44.33  ?  327 TRP B CD2   1 
ATOM   8713  N  NE1   . TRP B 1 308 ? 184.250 198.370 149.795 1.00 38.94  ?  327 TRP B NE1   1 
ATOM   8714  C  CE2   . TRP B 1 308 ? 184.170 198.400 148.428 1.00 41.36  ?  327 TRP B CE2   1 
ATOM   8715  C  CE3   . TRP B 1 308 ? 184.067 200.059 146.674 1.00 41.38  ?  327 TRP B CE3   1 
ATOM   8716  C  CZ2   . TRP B 1 308 ? 184.114 197.356 147.508 1.00 40.67  ?  327 TRP B CZ2   1 
ATOM   8717  C  CZ3   . TRP B 1 308 ? 184.012 199.021 145.762 1.00 44.88  ?  327 TRP B CZ3   1 
ATOM   8718  C  CH2   . TRP B 1 308 ? 184.036 197.687 146.183 1.00 43.85  ?  327 TRP B CH2   1 
ATOM   8719  N  N     . SER B 1 309 ? 181.298 201.464 150.990 1.00 26.99  ?  328 SER B N     1 
ATOM   8720  C  CA    . SER B 1 309 ? 180.677 201.044 152.236 1.00 28.18  ?  328 SER B CA    1 
ATOM   8721  C  C     . SER B 1 309 ? 180.843 199.543 152.416 1.00 36.61  ?  328 SER B C     1 
ATOM   8722  O  O     . SER B 1 309 ? 180.679 198.770 151.467 1.00 45.32  ?  328 SER B O     1 
ATOM   8723  C  CB    . SER B 1 309 ? 179.191 201.416 152.264 1.00 32.60  ?  328 SER B CB    1 
ATOM   8724  O  OG    . SER B 1 309 ? 178.543 200.834 153.381 1.00 33.92  ?  328 SER B OG    1 
ATOM   8725  N  N     . ALA B 1 310 ? 181.172 199.140 153.641 1.00 22.40  ?  329 ALA B N     1 
ATOM   8726  C  CA    . ALA B 1 310 ? 181.342 197.739 153.994 1.00 23.53  ?  329 ALA B CA    1 
ATOM   8727  C  C     . ALA B 1 310 ? 180.488 197.421 155.211 1.00 24.38  ?  329 ALA B C     1 
ATOM   8728  O  O     . ALA B 1 310 ? 180.395 198.228 156.142 1.00 35.91  ?  329 ALA B O     1 
ATOM   8729  C  CB    . ALA B 1 310 ? 182.812 197.405 154.279 1.00 25.56  ?  329 ALA B CB    1 
ATOM   8730  N  N     . THR B 1 311 ? 179.876 196.238 155.200 1.00 27.66  ?  330 THR B N     1 
ATOM   8731  C  CA    . THR B 1 311 ? 178.959 195.803 156.249 1.00 26.07  ?  330 THR B CA    1 
ATOM   8732  C  C     . THR B 1 311 ? 179.692 194.837 157.173 1.00 18.12  ?  330 THR B C     1 
ATOM   8733  O  O     . THR B 1 311 ? 180.087 193.744 156.756 1.00 35.34  ?  330 THR B O     1 
ATOM   8734  C  CB    . THR B 1 311 ? 177.715 195.150 155.650 1.00 37.82  ?  330 THR B CB    1 
ATOM   8735  O  OG1   . THR B 1 311 ? 177.143 196.021 154.666 1.00 43.08  ?  330 THR B OG1   1 
ATOM   8736  C  CG2   . THR B 1 311 ? 176.683 194.875 156.732 1.00 31.55  ?  330 THR B CG2   1 
ATOM   8737  N  N     . ILE B 1 312 ? 179.872 195.246 158.427 1.00 7.39   ?  331 ILE B N     1 
ATOM   8738  C  CA    . ILE B 1 312 ? 180.578 194.432 159.404 1.00 27.77  ?  331 ILE B CA    1 
ATOM   8739  C  C     . ILE B 1 312 ? 179.709 193.251 159.810 1.00 40.33  ?  331 ILE B C     1 
ATOM   8740  O  O     . ILE B 1 312 ? 178.530 193.414 160.150 1.00 46.41  ?  331 ILE B O     1 
ATOM   8741  C  CB    . ILE B 1 312 ? 180.963 195.283 160.622 1.00 28.79  ?  331 ILE B CB    1 
ATOM   8742  C  CG1   . ILE B 1 312 ? 182.073 196.268 160.254 1.00 18.17  ?  331 ILE B CG1   1 
ATOM   8743  C  CG2   . ILE B 1 312 ? 181.385 194.400 161.780 1.00 31.60  ?  331 ILE B CG2   1 
ATOM   8744  C  CD1   . ILE B 1 312 ? 181.945 197.608 160.940 1.00 20.26  ?  331 ILE B CD1   1 
ATOM   8745  N  N     . ARG B 1 313 ? 180.288 192.053 159.770 1.00 38.76  ?  332 ARG B N     1 
ATOM   8746  C  CA    . ARG B 1 313 ? 179.640 190.842 160.249 1.00 22.89  ?  332 ARG B CA    1 
ATOM   8747  C  C     . ARG B 1 313 ? 180.566 190.142 161.228 1.00 38.97  ?  332 ARG B C     1 
ATOM   8748  O  O     . ARG B 1 313 ? 181.778 190.069 161.004 1.00 53.55  ?  332 ARG B O     1 
ATOM   8749  C  CB    . ARG B 1 313 ? 179.289 189.895 159.096 1.00 33.68  ?  332 ARG B CB    1 
ATOM   8750  C  CG    . ARG B 1 313 ? 178.579 190.566 157.940 1.00 41.39  ?  332 ARG B CG    1 
ATOM   8751  C  CD    . ARG B 1 313 ? 177.622 189.609 157.259 1.00 47.09  ?  332 ARG B CD    1 
ATOM   8752  N  NE    . ARG B 1 313 ? 176.756 190.297 156.310 1.00 47.27  ?  332 ARG B NE    1 
ATOM   8753  C  CZ    . ARG B 1 313 ? 175.433 190.211 156.307 1.00 50.13  ?  332 ARG B CZ    1 
ATOM   8754  N  NH1   . ARG B 1 313 ? 174.787 189.468 157.191 1.00 44.65  1  332 ARG B NH1   1 
ATOM   8755  N  NH2   . ARG B 1 313 ? 174.741 190.891 155.398 1.00 53.04  ?  332 ARG B NH2   1 
ATOM   8756  N  N     . GLN B 1 314 ? 179.994 189.621 162.309 1.00 57.30  ?  333 GLN B N     1 
ATOM   8757  C  CA    . GLN B 1 314 ? 180.775 188.916 163.317 1.00 64.95  ?  333 GLN B CA    1 
ATOM   8758  C  C     . GLN B 1 314 ? 181.076 187.502 162.825 1.00 63.95  ?  333 GLN B C     1 
ATOM   8759  O  O     . GLN B 1 314 ? 180.911 187.177 161.646 1.00 68.75  ?  333 GLN B O     1 
ATOM   8760  C  CB    . GLN B 1 314 ? 180.047 188.920 164.659 1.00 63.90  ?  333 GLN B CB    1 
ATOM   8761  C  CG    . GLN B 1 314 ? 178.692 188.237 164.640 1.00 63.25  ?  333 GLN B CG    1 
ATOM   8762  C  CD    . GLN B 1 314 ? 177.558 189.221 164.463 1.00 64.23  ?  333 GLN B CD    1 
ATOM   8763  O  OE1   . GLN B 1 314 ? 177.782 190.396 164.172 1.00 68.55  ?  333 GLN B OE1   1 
ATOM   8764  N  NE2   . GLN B 1 314 ? 176.329 188.748 164.636 1.00 59.82  ?  333 GLN B NE2   1 
ATOM   8765  N  N     . ARG B 1 315 ? 181.543 186.643 163.735 1.00 69.68  ?  334 ARG B N     1 
ATOM   8766  C  CA    . ARG B 1 315 ? 181.921 185.285 163.356 1.00 71.32  ?  334 ARG B CA    1 
ATOM   8767  C  C     . ARG B 1 315 ? 180.755 184.520 162.743 1.00 72.13  ?  334 ARG B C     1 
ATOM   8768  O  O     . ARG B 1 315 ? 180.960 183.704 161.837 1.00 73.57  ?  334 ARG B O     1 
ATOM   8769  C  CB    . ARG B 1 315 ? 182.476 184.542 164.572 1.00 71.75  ?  334 ARG B CB    1 
ATOM   8770  C  CG    . ARG B 1 315 ? 181.668 184.742 165.843 1.00 75.08  ?  334 ARG B CG    1 
ATOM   8771  C  CD    . ARG B 1 315 ? 182.254 183.949 166.999 1.00 72.92  ?  334 ARG B CD    1 
ATOM   8772  N  NE    . ARG B 1 315 ? 181.498 184.140 168.231 1.00 75.16  ?  334 ARG B NE    1 
ATOM   8773  C  CZ    . ARG B 1 315 ? 181.776 183.543 169.382 1.00 75.41  ?  334 ARG B CZ    1 
ATOM   8774  N  NH1   . ARG B 1 315 ? 182.794 182.706 169.499 1.00 74.86  1  334 ARG B NH1   1 
ATOM   8775  N  NH2   . ARG B 1 315 ? 181.015 183.795 170.444 1.00 74.99  ?  334 ARG B NH2   1 
ATOM   8776  N  N     . ASP B 1 316 ? 179.533 184.769 163.211 1.00 70.81  ?  335 ASP B N     1 
ATOM   8777  C  CA    . ASP B 1 316 ? 178.349 184.151 162.617 1.00 71.74  ?  335 ASP B CA    1 
ATOM   8778  C  C     . ASP B 1 316 ? 177.120 184.910 163.086 1.00 72.20  ?  335 ASP B C     1 
ATOM   8779  O  O     . ASP B 1 316 ? 176.878 185.002 164.294 1.00 72.04  ?  335 ASP B O     1 
ATOM   8780  C  CB    . ASP B 1 316 ? 178.253 182.672 163.000 1.00 76.84  ?  335 ASP B CB    1 
ATOM   8781  C  CG    . ASP B 1 316 ? 177.213 181.925 162.187 1.00 79.34  ?  335 ASP B CG    1 
ATOM   8782  O  OD1   . ASP B 1 316 ? 176.728 182.484 161.181 1.00 74.62  ?  335 ASP B OD1   1 
ATOM   8783  O  OD2   . ASP B 1 316 ? 176.884 180.776 162.551 1.00 78.71  -1 335 ASP B OD2   1 
ATOM   8784  N  N     . GLY B 1 317 ? 176.344 185.448 162.146 1.00 68.25  ?  336 GLY B N     1 
ATOM   8785  C  CA    . GLY B 1 317 ? 175.094 186.093 162.501 1.00 69.65  ?  336 GLY B CA    1 
ATOM   8786  C  C     . GLY B 1 317 ? 174.781 187.398 161.794 1.00 66.67  ?  336 GLY B C     1 
ATOM   8787  O  O     . GLY B 1 317 ? 175.160 187.604 160.637 1.00 66.46  ?  336 GLY B O     1 
ATOM   8788  N  N     . ALA B 1 318 ? 174.078 188.285 162.497 1.00 52.77  ?  337 ALA B N     1 
ATOM   8789  C  CA    . ALA B 1 318 ? 173.566 189.514 161.914 1.00 54.88  ?  337 ALA B CA    1 
ATOM   8790  C  C     . ALA B 1 318 ? 174.683 190.535 161.703 1.00 51.30  ?  337 ALA B C     1 
ATOM   8791  O  O     . ALA B 1 318 ? 175.761 190.420 162.288 1.00 56.74  ?  337 ALA B O     1 
ATOM   8792  C  CB    . ALA B 1 318 ? 172.480 190.103 162.811 1.00 53.52  ?  337 ALA B CB    1 
ATOM   8793  N  N     . PRO B 1 319 ? 174.449 191.540 160.855 1.00 36.48  ?  338 PRO B N     1 
ATOM   8794  C  CA    . PRO B 1 319 ? 175.437 192.614 160.696 1.00 35.15  ?  338 PRO B CA    1 
ATOM   8795  C  C     . PRO B 1 319 ? 175.645 193.390 161.989 1.00 34.49  ?  338 PRO B C     1 
ATOM   8796  O  O     . PRO B 1 319 ? 174.753 193.485 162.835 1.00 37.92  ?  338 PRO B O     1 
ATOM   8797  C  CB    . PRO B 1 319 ? 174.821 193.502 159.611 1.00 40.17  ?  338 PRO B CB    1 
ATOM   8798  C  CG    . PRO B 1 319 ? 173.961 192.583 158.827 1.00 44.99  ?  338 PRO B CG    1 
ATOM   8799  C  CD    . PRO B 1 319 ? 173.405 191.599 159.817 1.00 43.76  ?  338 PRO B CD    1 
ATOM   8800  N  N     . ALA B 1 320 ? 176.849 193.951 162.134 1.00 25.59  ?  339 ALA B N     1 
ATOM   8801  C  CA    . ALA B 1 320 ? 177.232 194.666 163.342 1.00 16.34  ?  339 ALA B CA    1 
ATOM   8802  C  C     . ALA B 1 320 ? 177.562 196.139 163.132 1.00 17.55  ?  339 ALA B C     1 
ATOM   8803  O  O     . ALA B 1 320 ? 177.529 196.900 164.106 1.00 39.33  ?  339 ALA B O     1 
ATOM   8804  C  CB    . ALA B 1 320 ? 178.439 193.986 164.008 1.00 24.23  ?  339 ALA B CB    1 
ATOM   8805  N  N     . GLY B 1 321 ? 177.868 196.569 161.915 1.00 9.29   ?  340 GLY B N     1 
ATOM   8806  C  CA    . GLY B 1 321 ? 178.184 197.970 161.709 1.00 17.21  ?  340 GLY B CA    1 
ATOM   8807  C  C     . GLY B 1 321 ? 178.423 198.274 160.248 1.00 22.88  ?  340 GLY B C     1 
ATOM   8808  O  O     . GLY B 1 321 ? 178.265 197.418 159.373 1.00 42.68  ?  340 GLY B O     1 
ATOM   8809  N  N     . ILE B 1 322 ? 178.823 199.519 159.999 1.00 6.80   ?  341 ILE B N     1 
ATOM   8810  C  CA    . ILE B 1 322 ? 179.103 200.014 158.657 1.00 10.78  ?  341 ILE B CA    1 
ATOM   8811  C  C     . ILE B 1 322 ? 180.436 200.746 158.688 1.00 20.93  ?  341 ILE B C     1 
ATOM   8812  O  O     . ILE B 1 322 ? 180.774 201.396 159.682 1.00 31.70  ?  341 ILE B O     1 
ATOM   8813  C  CB    . ILE B 1 322 ? 177.982 200.945 158.142 1.00 22.66  ?  341 ILE B CB    1 
ATOM   8814  C  CG1   . ILE B 1 322 ? 176.627 200.237 158.170 1.00 22.60  ?  341 ILE B CG1   1 
ATOM   8815  C  CG2   . ILE B 1 322 ? 178.277 201.419 156.726 1.00 29.94  ?  341 ILE B CG2   1 
ATOM   8816  C  CD1   . ILE B 1 322 ? 175.695 200.753 159.243 1.00 31.28  ?  341 ILE B CD1   1 
ATOM   8817  N  N     . LEU B 1 323 ? 181.204 200.625 157.611 1.00 30.53  ?  342 LEU B N     1 
ATOM   8818  C  CA    . LEU B 1 323 ? 182.447 201.368 157.444 1.00 31.21  ?  342 LEU B CA    1 
ATOM   8819  C  C     . LEU B 1 323 ? 182.422 202.046 156.083 1.00 33.50  ?  342 LEU B C     1 
ATOM   8820  O  O     . LEU B 1 323 ? 182.364 201.364 155.054 1.00 44.03  ?  342 LEU B O     1 
ATOM   8821  C  CB    . LEU B 1 323 ? 183.658 200.442 157.579 1.00 28.14  ?  342 LEU B CB    1 
ATOM   8822  C  CG    . LEU B 1 323 ? 185.009 200.925 157.051 1.00 19.63  ?  342 LEU B CG    1 
ATOM   8823  C  CD1   . LEU B 1 323 ? 185.450 202.214 157.719 1.00 31.54  ?  342 LEU B CD1   1 
ATOM   8824  C  CD2   . LEU B 1 323 ? 186.046 199.840 157.259 1.00 24.22  ?  342 LEU B CD2   1 
ATOM   8825  N  N     . GLN B 1 324 ? 182.459 203.381 156.072 1.00 23.33  ?  343 GLN B N     1 
ATOM   8826  C  CA    . GLN B 1 324 ? 182.386 204.140 154.829 1.00 31.61  ?  343 GLN B CA    1 
ATOM   8827  C  C     . GLN B 1 324 ? 183.666 204.941 154.640 1.00 34.84  ?  343 GLN B C     1 
ATOM   8828  O  O     . GLN B 1 324 ? 184.055 205.724 155.515 1.00 38.62  ?  343 GLN B O     1 
ATOM   8829  C  CB    . GLN B 1 324 ? 181.168 205.067 154.804 1.00 36.40  ?  343 GLN B CB    1 
ATOM   8830  C  CG    . GLN B 1 324 ? 180.877 205.770 156.109 1.00 39.71  ?  343 GLN B CG    1 
ATOM   8831  C  CD    . GLN B 1 324 ? 179.802 206.826 155.959 1.00 43.81  ?  343 GLN B CD    1 
ATOM   8832  O  OE1   . GLN B 1 324 ? 178.969 206.755 155.056 1.00 40.92  ?  343 GLN B OE1   1 
ATOM   8833  N  NE2   . GLN B 1 324 ? 179.830 207.827 156.831 1.00 43.86  ?  343 GLN B NE2   1 
ATOM   8834  N  N     . ILE B 1 325 ? 184.305 204.751 153.489 1.00 43.87  ?  344 ILE B N     1 
ATOM   8835  C  CA    . ILE B 1 325 ? 185.548 205.422 153.131 1.00 44.24  ?  344 ILE B CA    1 
ATOM   8836  C  C     . ILE B 1 325 ? 185.312 206.134 151.807 1.00 50.61  ?  344 ILE B C     1 
ATOM   8837  O  O     . ILE B 1 325 ? 185.089 205.477 150.785 1.00 49.91  ?  344 ILE B O     1 
ATOM   8838  C  CB    . ILE B 1 325 ? 186.708 204.422 153.005 1.00 40.68  ?  344 ILE B CB    1 
ATOM   8839  C  CG1   . ILE B 1 325 ? 186.859 203.614 154.291 1.00 35.48  ?  344 ILE B CG1   1 
ATOM   8840  C  CG2   . ILE B 1 325 ? 188.005 205.145 152.675 1.00 41.58  ?  344 ILE B CG2   1 
ATOM   8841  C  CD1   . ILE B 1 325 ? 187.667 202.351 154.126 1.00 36.59  ?  344 ILE B CD1   1 
ATOM   8842  N  N     . LYS B 1 326 ? 185.353 207.464 151.814 1.00 56.19  ?  345 LYS B N     1 
ATOM   8843  C  CA    . LYS B 1 326 ? 185.166 208.241 150.598 1.00 58.24  ?  345 LYS B CA    1 
ATOM   8844  C  C     . LYS B 1 326 ? 186.487 208.883 150.203 1.00 50.40  ?  345 LYS B C     1 
ATOM   8845  O  O     . LYS B 1 326 ? 187.101 209.605 150.994 1.00 52.47  ?  345 LYS B O     1 
ATOM   8846  C  CB    . LYS B 1 326 ? 184.072 209.301 150.767 1.00 58.04  ?  345 LYS B CB    1 
ATOM   8847  C  CG    . LYS B 1 326 ? 184.158 210.124 152.036 1.00 57.86  ?  345 LYS B CG    1 
ATOM   8848  C  CD    . LYS B 1 326 ? 183.135 211.246 152.045 1.00 59.97  ?  345 LYS B CD    1 
ATOM   8849  C  CE    . LYS B 1 326 ? 181.749 210.719 152.376 1.00 56.59  ?  345 LYS B CE    1 
ATOM   8850  N  NZ    . LYS B 1 326 ? 181.669 210.232 153.780 1.00 53.27  1  345 LYS B NZ    1 
ATOM   8851  N  N     . THR B 1 327 ? 186.915 208.615 148.976 1.00 61.43  ?  346 THR B N     1 
ATOM   8852  C  CA    . THR B 1 327 ? 188.187 209.093 148.460 1.00 66.39  ?  346 THR B CA    1 
ATOM   8853  C  C     . THR B 1 327 ? 187.943 209.782 147.125 1.00 70.13  ?  346 THR B C     1 
ATOM   8854  O  O     . THR B 1 327 ? 186.976 209.475 146.422 1.00 72.62  ?  346 THR B O     1 
ATOM   8855  C  CB    . THR B 1 327 ? 189.187 207.929 148.305 1.00 68.61  ?  346 THR B CB    1 
ATOM   8856  O  OG1   . THR B 1 327 ? 189.306 207.237 149.554 1.00 69.84  ?  346 THR B OG1   1 
ATOM   8857  C  CG2   . THR B 1 327 ? 190.567 208.434 147.900 1.00 68.32  ?  346 THR B CG2   1 
ATOM   8858  N  N     . SER B 1 328 ? 188.809 210.738 146.793 1.00 72.53  ?  347 SER B N     1 
ATOM   8859  C  CA    . SER B 1 328 ? 188.706 211.420 145.511 1.00 72.68  ?  347 SER B CA    1 
ATOM   8860  C  C     . SER B 1 328 ? 188.794 210.414 144.371 1.00 73.05  ?  347 SER B C     1 
ATOM   8861  O  O     . SER B 1 328 ? 189.584 209.467 144.416 1.00 75.00  ?  347 SER B O     1 
ATOM   8862  C  CB    . SER B 1 328 ? 189.809 212.471 145.379 1.00 74.07  ?  347 SER B CB    1 
ATOM   8863  O  OG    . SER B 1 328 ? 191.083 211.906 145.633 1.00 75.46  ?  347 SER B OG    1 
ATOM   8864  N  N     . SER B 1 329 ? 187.964 210.616 143.351 1.00 66.94  ?  348 SER B N     1 
ATOM   8865  C  CA    . SER B 1 329 ? 187.894 209.667 142.248 1.00 66.89  ?  348 SER B CA    1 
ATOM   8866  C  C     . SER B 1 329 ? 189.219 209.616 141.500 1.00 72.65  ?  348 SER B C     1 
ATOM   8867  O  O     . SER B 1 329 ? 189.809 210.652 141.179 1.00 72.81  ?  348 SER B O     1 
ATOM   8868  C  CB    . SER B 1 329 ? 186.761 210.048 141.297 1.00 67.26  ?  348 SER B CB    1 
ATOM   8869  O  OG    . SER B 1 329 ? 186.747 209.201 140.161 1.00 64.41  ?  348 SER B OG    1 
ATOM   8870  N  N     . GLY B 1 330 ? 189.685 208.400 141.220 1.00 71.31  ?  349 GLY B N     1 
ATOM   8871  C  CA    . GLY B 1 330 ? 190.937 208.198 140.526 1.00 63.75  ?  349 GLY B CA    1 
ATOM   8872  C  C     . GLY B 1 330 ? 192.175 208.276 141.390 1.00 60.44  ?  349 GLY B C     1 
ATOM   8873  O  O     . GLY B 1 330 ? 193.284 208.112 140.866 1.00 61.25  ?  349 GLY B O     1 
ATOM   8874  N  N     . ALA B 1 331 ? 192.029 208.527 142.694 1.00 50.67  ?  350 ALA B N     1 
ATOM   8875  C  CA    . ALA B 1 331 ? 193.196 208.610 143.566 1.00 47.53  ?  350 ALA B CA    1 
ATOM   8876  C  C     . ALA B 1 331 ? 193.906 207.266 143.676 1.00 50.90  ?  350 ALA B C     1 
ATOM   8877  O  O     . ALA B 1 331 ? 195.141 207.203 143.640 1.00 47.53  ?  350 ALA B O     1 
ATOM   8878  C  CB    . ALA B 1 331 ? 192.784 209.113 144.949 1.00 47.59  ?  350 ALA B CB    1 
ATOM   8879  N  N     . GLU B 1 332 ? 193.146 206.181 143.808 1.00 58.06  ?  351 GLU B N     1 
ATOM   8880  C  CA    . GLU B 1 332 ? 193.725 204.858 143.980 1.00 53.65  ?  351 GLU B CA    1 
ATOM   8881  C  C     . GLU B 1 332 ? 192.880 203.822 143.254 1.00 48.83  ?  351 GLU B C     1 
ATOM   8882  O  O     . GLU B 1 332 ? 191.727 204.066 142.892 1.00 50.36  ?  351 GLU B O     1 
ATOM   8883  C  CB    . GLU B 1 332 ? 193.863 204.489 145.463 1.00 51.06  ?  351 GLU B CB    1 
ATOM   8884  C  CG    . GLU B 1 332 ? 195.161 204.970 146.090 1.00 56.38  ?  351 GLU B CG    1 
ATOM   8885  C  CD    . GLU B 1 332 ? 195.012 206.302 146.797 1.00 60.82  ?  351 GLU B CD    1 
ATOM   8886  O  OE1   . GLU B 1 332 ? 193.862 206.737 147.019 1.00 62.17  ?  351 GLU B OE1   1 
ATOM   8887  O  OE2   . GLU B 1 332 ? 196.047 206.917 147.130 1.00 57.76  -1 351 GLU B OE2   1 
ATOM   8888  N  N     . THR B 1 333 ? 193.483 202.656 143.043 1.00 49.10  ?  352 THR B N     1 
ATOM   8889  C  CA    . THR B 1 333 ? 192.842 201.580 142.304 1.00 51.30  ?  352 THR B CA    1 
ATOM   8890  C  C     . THR B 1 333 ? 191.623 201.058 143.060 1.00 52.42  ?  352 THR B C     1 
ATOM   8891  O  O     . THR B 1 333 ? 191.594 201.027 144.293 1.00 56.27  ?  352 THR B O     1 
ATOM   8892  C  CB    . THR B 1 333 ? 193.848 200.449 142.058 1.00 52.62  ?  352 THR B CB    1 
ATOM   8893  O  OG1   . THR B 1 333 ? 194.923 200.937 141.247 1.00 50.24  ?  352 THR B OG1   1 
ATOM   8894  C  CG2   . THR B 1 333 ? 193.202 199.268 141.346 1.00 47.96  ?  352 THR B CG2   1 
ATOM   8895  N  N     . SER B 1 334 ? 190.596 200.668 142.299 1.00 46.31  ?  353 SER B N     1 
ATOM   8896  C  CA    . SER B 1 334 ? 189.416 200.053 142.899 1.00 44.82  ?  353 SER B CA    1 
ATOM   8897  C  C     . SER B 1 334 ? 189.778 198.772 143.642 1.00 47.49  ?  353 SER B C     1 
ATOM   8898  O  O     . SER B 1 334 ? 189.210 198.480 144.699 1.00 45.30  ?  353 SER B O     1 
ATOM   8899  C  CB    . SER B 1 334 ? 188.366 199.769 141.825 1.00 44.29  ?  353 SER B CB    1 
ATOM   8900  O  OG    . SER B 1 334 ? 187.282 199.030 142.358 1.00 46.45  ?  353 SER B OG    1 
ATOM   8901  N  N     . ALA B 1 335 ? 190.713 197.989 143.099 1.00 44.00  ?  354 ALA B N     1 
ATOM   8902  C  CA    . ALA B 1 335 ? 191.170 196.792 143.798 1.00 35.21  ?  354 ALA B CA    1 
ATOM   8903  C  C     . ALA B 1 335 ? 191.855 197.149 145.112 1.00 32.43  ?  354 ALA B C     1 
ATOM   8904  O  O     . ALA B 1 335 ? 191.674 196.461 146.123 1.00 41.46  ?  354 ALA B O     1 
ATOM   8905  C  CB    . ALA B 1 335 ? 192.111 195.985 142.903 1.00 35.96  ?  354 ALA B CB    1 
ATOM   8906  N  N     . PHE B 1 336 ? 192.654 198.218 145.112 1.00 28.57  ?  355 PHE B N     1 
ATOM   8907  C  CA    . PHE B 1 336 ? 193.276 198.689 146.345 1.00 26.45  ?  355 PHE B CA    1 
ATOM   8908  C  C     . PHE B 1 336 ? 192.222 199.105 147.363 1.00 37.92  ?  355 PHE B C     1 
ATOM   8909  O  O     . PHE B 1 336 ? 192.318 198.764 148.551 1.00 48.34  ?  355 PHE B O     1 
ATOM   8910  C  CB    . PHE B 1 336 ? 194.214 199.851 146.022 1.00 28.48  ?  355 PHE B CB    1 
ATOM   8911  C  CG    . PHE B 1 336 ? 195.152 200.211 147.135 1.00 30.30  ?  355 PHE B CG    1 
ATOM   8912  C  CD1   . PHE B 1 336 ? 195.851 199.229 147.816 1.00 29.67  ?  355 PHE B CD1   1 
ATOM   8913  C  CD2   . PHE B 1 336 ? 195.358 201.536 147.480 1.00 40.01  ?  355 PHE B CD2   1 
ATOM   8914  C  CE1   . PHE B 1 336 ? 196.723 199.563 148.835 1.00 33.22  ?  355 PHE B CE1   1 
ATOM   8915  C  CE2   . PHE B 1 336 ? 196.228 201.874 148.496 1.00 43.29  ?  355 PHE B CE2   1 
ATOM   8916  C  CZ    . PHE B 1 336 ? 196.912 200.886 149.173 1.00 38.83  ?  355 PHE B CZ    1 
ATOM   8917  N  N     . ILE B 1 337 ? 191.198 199.831 146.906 1.00 43.57  ?  356 ILE B N     1 
ATOM   8918  C  CA    . ILE B 1 337 ? 190.101 200.237 147.780 1.00 39.86  ?  356 ILE B CA    1 
ATOM   8919  C  C     . ILE B 1 337 ? 189.407 199.016 148.367 1.00 48.20  ?  356 ILE B C     1 
ATOM   8920  O  O     . ILE B 1 337 ? 189.118 198.967 149.566 1.00 49.43  ?  356 ILE B O     1 
ATOM   8921  C  CB    . ILE B 1 337 ? 189.110 201.132 147.011 1.00 42.75  ?  356 ILE B CB    1 
ATOM   8922  C  CG1   . ILE B 1 337 ? 189.767 202.456 146.621 1.00 44.93  ?  356 ILE B CG1   1 
ATOM   8923  C  CG2   . ILE B 1 337 ? 187.849 201.370 147.833 1.00 42.30  ?  356 ILE B CG2   1 
ATOM   8924  C  CD1   . ILE B 1 337 ? 190.148 203.307 147.800 1.00 42.59  ?  356 ILE B CD1   1 
ATOM   8925  N  N     . GLU B 1 338 ? 189.134 198.011 147.531 1.00 45.84  ?  357 GLU B N     1 
ATOM   8926  C  CA    . GLU B 1 338 ? 188.428 196.822 147.997 1.00 42.75  ?  357 GLU B CA    1 
ATOM   8927  C  C     . GLU B 1 338 ? 189.265 196.026 148.992 1.00 39.25  ?  357 GLU B C     1 
ATOM   8928  O  O     . GLU B 1 338 ? 188.735 195.518 149.984 1.00 46.20  ?  357 GLU B O     1 
ATOM   8929  C  CB    . GLU B 1 338 ? 188.030 195.950 146.808 1.00 43.23  ?  357 GLU B CB    1 
ATOM   8930  C  CG    . GLU B 1 338 ? 187.144 194.772 147.169 1.00 44.65  ?  357 GLU B CG    1 
ATOM   8931  C  CD    . GLU B 1 338 ? 186.851 193.884 145.977 1.00 49.04  ?  357 GLU B CD    1 
ATOM   8932  O  OE1   . GLU B 1 338 ? 187.243 194.255 144.851 1.00 45.98  ?  357 GLU B OE1   1 
ATOM   8933  O  OE2   . GLU B 1 338 ? 186.232 192.817 146.165 1.00 53.93  -1 357 GLU B OE2   1 
ATOM   8934  N  N     . ARG B 1 339 ? 190.571 195.898 148.745 1.00 32.90  ?  358 ARG B N     1 
ATOM   8935  C  CA    . ARG B 1 339 ? 191.428 195.183 149.687 1.00 22.59  ?  358 ARG B CA    1 
ATOM   8936  C  C     . ARG B 1 339 ? 191.501 195.906 151.027 1.00 29.63  ?  358 ARG B C     1 
ATOM   8937  O  O     . ARG B 1 339 ? 191.382 195.275 152.088 1.00 48.19  ?  358 ARG B O     1 
ATOM   8938  C  CB    . ARG B 1 339 ? 192.830 195.000 149.103 1.00 33.55  ?  358 ARG B CB    1 
ATOM   8939  C  CG    . ARG B 1 339 ? 192.977 193.785 148.204 1.00 38.33  ?  358 ARG B CG    1 
ATOM   8940  C  CD    . ARG B 1 339 ? 194.360 193.721 147.578 1.00 37.46  ?  358 ARG B CD    1 
ATOM   8941  N  NE    . ARG B 1 339 ? 195.315 193.045 148.450 1.00 42.49  ?  358 ARG B NE    1 
ATOM   8942  C  CZ    . ARG B 1 339 ? 196.498 192.591 148.061 1.00 46.48  ?  358 ARG B CZ    1 
ATOM   8943  N  NH1   . ARG B 1 339 ? 196.912 192.722 146.811 1.00 47.11  1  358 ARG B NH1   1 
ATOM   8944  N  NH2   . ARG B 1 339 ? 197.285 191.987 148.947 1.00 43.15  ?  358 ARG B NH2   1 
ATOM   8945  N  N     . VAL B 1 340 ? 191.693 197.229 150.999 1.00 24.15  ?  359 VAL B N     1 
ATOM   8946  C  CA    . VAL B 1 340 ? 191.717 197.996 152.242 1.00 27.64  ?  359 VAL B CA    1 
ATOM   8947  C  C     . VAL B 1 340 ? 190.387 197.861 152.968 1.00 36.14  ?  359 VAL B C     1 
ATOM   8948  O  O     . VAL B 1 340 ? 190.345 197.690 154.193 1.00 35.04  ?  359 VAL B O     1 
ATOM   8949  C  CB    . VAL B 1 340 ? 192.062 199.470 151.958 1.00 34.72  ?  359 VAL B CB    1 
ATOM   8950  C  CG1   . VAL B 1 340 ? 191.852 200.317 153.204 1.00 39.16  ?  359 VAL B CG1   1 
ATOM   8951  C  CG2   . VAL B 1 340 ? 193.495 199.595 151.466 1.00 35.07  ?  359 VAL B CG2   1 
ATOM   8952  N  N     . ALA B 1 341 ? 189.282 197.921 152.222 1.00 36.08  ?  360 ALA B N     1 
ATOM   8953  C  CA    . ALA B 1 341 ? 187.962 197.801 152.826 1.00 28.39  ?  360 ALA B CA    1 
ATOM   8954  C  C     . ALA B 1 341 ? 187.767 196.435 153.464 1.00 27.02  ?  360 ALA B C     1 
ATOM   8955  O  O     . ALA B 1 341 ? 187.202 196.334 154.552 1.00 36.26  ?  360 ALA B O     1 
ATOM   8956  C  CB    . ALA B 1 341 ? 186.883 198.059 151.777 1.00 34.23  ?  360 ALA B CB    1 
ATOM   8957  N  N     . ASP B 1 342 ? 188.228 195.372 152.806 1.00 32.25  ?  361 ASP B N     1 
ATOM   8958  C  CA    . ASP B 1 342 ? 188.062 194.028 153.351 1.00 27.86  ?  361 ASP B CA    1 
ATOM   8959  C  C     . ASP B 1 342 ? 188.870 193.850 154.632 1.00 19.83  ?  361 ASP B C     1 
ATOM   8960  O  O     . ASP B 1 342 ? 188.357 193.342 155.642 1.00 31.35  ?  361 ASP B O     1 
ATOM   8961  C  CB    . ASP B 1 342 ? 188.470 192.991 152.304 1.00 25.82  ?  361 ASP B CB    1 
ATOM   8962  C  CG    . ASP B 1 342 ? 187.816 191.645 152.529 1.00 38.49  ?  361 ASP B CG    1 
ATOM   8963  O  OD1   . ASP B 1 342 ? 186.590 191.616 152.769 1.00 38.81  ?  361 ASP B OD1   1 
ATOM   8964  O  OD2   . ASP B 1 342 ? 188.521 190.616 152.461 1.00 40.99  -1 361 ASP B OD2   1 
ATOM   8965  N  N     . ILE B 1 343 ? 190.139 194.271 154.611 1.00 11.50  ?  362 ILE B N     1 
ATOM   8966  C  CA    . ILE B 1 343 ? 190.975 194.138 155.803 1.00 15.69  ?  362 ILE B CA    1 
ATOM   8967  C  C     . ILE B 1 343 ? 190.395 194.958 156.950 1.00 33.01  ?  362 ILE B C     1 
ATOM   8968  O  O     . ILE B 1 343 ? 190.278 194.474 158.083 1.00 41.31  ?  362 ILE B O     1 
ATOM   8969  C  CB    . ILE B 1 343 ? 192.429 194.539 155.497 1.00 17.15  ?  362 ILE B CB    1 
ATOM   8970  C  CG1   . ILE B 1 343 ? 192.950 193.783 154.274 1.00 23.81  ?  362 ILE B CG1   1 
ATOM   8971  C  CG2   . ILE B 1 343 ? 193.322 194.269 156.699 1.00 23.28  ?  362 ILE B CG2   1 
ATOM   8972  C  CD1   . ILE B 1 343 ? 192.963 192.277 154.436 1.00 32.88  ?  362 ILE B CD1   1 
ATOM   8973  N  N     . SER B 1 344 ? 189.997 196.203 156.670 1.00 30.37  ?  363 SER B N     1 
ATOM   8974  C  CA    . SER B 1 344 ? 189.450 197.052 157.721 1.00 23.25  ?  363 SER B CA    1 
ATOM   8975  C  C     . SER B 1 344 ? 188.081 196.571 158.183 1.00 26.07  ?  363 SER B C     1 
ATOM   8976  O  O     . SER B 1 344 ? 187.718 196.776 159.341 1.00 32.09  ?  363 SER B O     1 
ATOM   8977  C  CB    . SER B 1 344 ? 189.377 198.499 157.235 1.00 35.85  ?  363 SER B CB    1 
ATOM   8978  O  OG    . SER B 1 344 ? 188.719 198.580 155.984 1.00 40.71  ?  363 SER B OG    1 
ATOM   8979  N  N     . GLN B 1 345 ? 187.320 195.914 157.307 1.00 26.16  ?  364 GLN B N     1 
ATOM   8980  C  CA    . GLN B 1 345 ? 186.041 195.334 157.697 1.00 22.09  ?  364 GLN B CA    1 
ATOM   8981  C  C     . GLN B 1 345 ? 186.233 194.193 158.680 1.00 30.15  ?  364 GLN B C     1 
ATOM   8982  O  O     . GLN B 1 345 ? 185.534 194.117 159.695 1.00 37.08  ?  364 GLN B O     1 
ATOM   8983  C  CB    . GLN B 1 345 ? 185.297 194.848 156.455 1.00 21.69  ?  364 GLN B CB    1 
ATOM   8984  C  CG    . GLN B 1 345 ? 184.052 194.031 156.744 1.00 31.13  ?  364 GLN B CG    1 
ATOM   8985  C  CD    . GLN B 1 345 ? 183.355 193.580 155.476 1.00 43.92  ?  364 GLN B CD    1 
ATOM   8986  O  OE1   . GLN B 1 345 ? 183.822 193.847 154.369 1.00 41.12  ?  364 GLN B OE1   1 
ATOM   8987  N  NE2   . GLN B 1 345 ? 182.232 192.889 155.632 1.00 44.54  ?  364 GLN B NE2   1 
ATOM   8988  N  N     . HIS B 1 346 ? 187.177 193.293 158.398 1.00 28.70  ?  365 HIS B N     1 
ATOM   8989  C  CA    . HIS B 1 346 ? 187.447 192.227 159.357 1.00 20.35  ?  365 HIS B CA    1 
ATOM   8990  C  C     . HIS B 1 346 ? 188.031 192.776 160.654 1.00 19.12  ?  365 HIS B C     1 
ATOM   8991  O  O     . HIS B 1 346 ? 187.695 192.288 161.741 1.00 38.82  ?  365 HIS B O     1 
ATOM   8992  C  CB    . HIS B 1 346 ? 188.363 191.175 158.736 1.00 28.70  ?  365 HIS B CB    1 
ATOM   8993  C  CG    . HIS B 1 346 ? 187.776 190.515 157.527 1.00 44.13  ?  365 HIS B CG    1 
ATOM   8994  N  ND1   . HIS B 1 346 ? 188.048 190.934 156.243 1.00 45.57  ?  365 HIS B ND1   1 
ATOM   8995  C  CD2   . HIS B 1 346 ? 186.910 189.480 157.410 1.00 43.57  ?  365 HIS B CD2   1 
ATOM   8996  C  CE1   . HIS B 1 346 ? 187.386 190.177 155.386 1.00 44.97  ?  365 HIS B CE1   1 
ATOM   8997  N  NE2   . HIS B 1 346 ? 186.686 189.289 156.069 1.00 43.73  ?  365 HIS B NE2   1 
ATOM   8998  N  N     . MET B 1 347 ? 188.883 193.801 160.568 1.00 22.52  ?  366 MET B N     1 
ATOM   8999  C  CA    . MET B 1 347 ? 189.414 194.419 161.780 1.00 30.56  ?  366 MET B CA    1 
ATOM   9000  C  C     . MET B 1 347 ? 188.307 195.063 162.608 1.00 29.63  ?  366 MET B C     1 
ATOM   9001  O  O     . MET B 1 347 ? 188.291 194.944 163.838 1.00 36.07  ?  366 MET B O     1 
ATOM   9002  C  CB    . MET B 1 347 ? 190.487 195.445 161.416 1.00 33.39  ?  366 MET B CB    1 
ATOM   9003  C  CG    . MET B 1 347 ? 191.718 194.835 160.767 1.00 31.51  ?  366 MET B CG    1 
ATOM   9004  S  SD    . MET B 1 347 ? 192.690 193.858 161.923 1.00 56.41  ?  366 MET B SD    1 
ATOM   9005  C  CE    . MET B 1 347 ? 192.905 192.348 160.985 1.00 33.94  ?  366 MET B CE    1 
ATOM   9006  N  N     . ALA B 1 348 ? 187.364 195.742 161.951 1.00 22.06  ?  367 ALA B N     1 
ATOM   9007  C  CA    . ALA B 1 348 ? 186.254 196.359 162.666 1.00 19.50  ?  367 ALA B CA    1 
ATOM   9008  C  C     . ALA B 1 348 ? 185.304 195.315 163.231 1.00 25.66  ?  367 ALA B C     1 
ATOM   9009  O  O     . ALA B 1 348 ? 184.709 195.533 164.289 1.00 40.21  ?  367 ALA B O     1 
ATOM   9010  C  CB    . ALA B 1 348 ? 185.506 197.323 161.746 1.00 28.81  ?  367 ALA B CB    1 
ATOM   9011  N  N     . ALA B 1 349 ? 185.141 194.184 162.541 1.00 25.04  ?  368 ALA B N     1 
ATOM   9012  C  CA    . ALA B 1 349 ? 184.371 193.081 163.105 1.00 22.90  ?  368 ALA B CA    1 
ATOM   9013  C  C     . ALA B 1 349 ? 185.030 192.552 164.369 1.00 15.88  ?  368 ALA B C     1 
ATOM   9014  O  O     . ALA B 1 349 ? 184.353 192.286 165.370 1.00 30.13  ?  368 ALA B O     1 
ATOM   9015  C  CB    . ALA B 1 349 ? 184.214 191.968 162.071 1.00 21.53  ?  368 ALA B CB    1 
ATOM   9016  N  N     . LEU B 1 350 ? 186.357 192.406 164.345 1.00 11.06  ?  369 LEU B N     1 
ATOM   9017  C  CA    . LEU B 1 350 ? 187.073 191.996 165.548 1.00 13.23  ?  369 LEU B CA    1 
ATOM   9018  C  C     . LEU B 1 350 ? 186.898 193.020 166.664 1.00 15.37  ?  369 LEU B C     1 
ATOM   9019  O  O     . LEU B 1 350 ? 186.694 192.653 167.825 1.00 34.64  ?  369 LEU B O     1 
ATOM   9020  C  CB    . LEU B 1 350 ? 188.555 191.789 165.237 1.00 15.28  ?  369 LEU B CB    1 
ATOM   9021  C  CG    . LEU B 1 350 ? 188.948 190.468 164.572 1.00 17.56  ?  369 LEU B CG    1 
ATOM   9022  C  CD1   . LEU B 1 350 ? 190.313 190.591 163.913 1.00 24.07  ?  369 LEU B CD1   1 
ATOM   9023  C  CD2   . LEU B 1 350 ? 188.934 189.331 165.581 1.00 27.32  ?  369 LEU B CD2   1 
ATOM   9024  N  N     . ALA B 1 351 ? 186.972 194.309 166.326 1.00 12.53  ?  370 ALA B N     1 
ATOM   9025  C  CA    . ALA B 1 351 ? 186.816 195.358 167.332 1.00 24.76  ?  370 ALA B CA    1 
ATOM   9026  C  C     . ALA B 1 351 ? 185.415 195.352 167.935 1.00 23.69  ?  370 ALA B C     1 
ATOM   9027  O  O     . ALA B 1 351 ? 185.253 195.511 169.150 1.00 32.18  ?  370 ALA B O     1 
ATOM   9028  C  CB    . ALA B 1 351 ? 187.131 196.724 166.722 1.00 30.88  ?  370 ALA B CB    1 
ATOM   9029  N  N     . LEU B 1 352 ? 184.389 195.178 167.101 1.00 25.69  ?  371 LEU B N     1 
ATOM   9030  C  CA    . LEU B 1 352 ? 183.021 195.126 167.605 1.00 18.39  ?  371 LEU B CA    1 
ATOM   9031  C  C     . LEU B 1 352 ? 182.791 193.892 168.469 1.00 20.18  ?  371 LEU B C     1 
ATOM   9032  O  O     . LEU B 1 352 ? 182.109 193.970 169.497 1.00 28.57  ?  371 LEU B O     1 
ATOM   9033  C  CB    . LEU B 1 352 ? 182.027 195.170 166.445 1.00 17.91  ?  371 LEU B CB    1 
ATOM   9034  C  CG    . LEU B 1 352 ? 181.543 196.570 166.058 1.00 18.86  ?  371 LEU B CG    1 
ATOM   9035  C  CD1   . LEU B 1 352 ? 180.899 196.569 164.687 1.00 28.96  ?  371 LEU B CD1   1 
ATOM   9036  C  CD2   . LEU B 1 352 ? 180.565 197.087 167.097 1.00 23.18  ?  371 LEU B CD2   1 
ATOM   9037  N  N     . GLU B 1 353 ? 183.342 192.743 168.071 1.00 21.93  ?  372 GLU B N     1 
ATOM   9038  C  CA    . GLU B 1 353 ? 183.231 191.551 168.907 1.00 22.44  ?  372 GLU B CA    1 
ATOM   9039  C  C     . GLU B 1 353 ? 183.941 191.747 170.242 1.00 23.14  ?  372 GLU B C     1 
ATOM   9040  O  O     . GLU B 1 353 ? 183.431 191.341 171.294 1.00 38.78  ?  372 GLU B O     1 
ATOM   9041  C  CB    . GLU B 1 353 ? 183.792 190.338 168.163 1.00 26.04  ?  372 GLU B CB    1 
ATOM   9042  C  CG    . GLU B 1 353 ? 183.876 189.071 168.996 1.00 32.25  ?  372 GLU B CG    1 
ATOM   9043  C  CD    . GLU B 1 353 ? 185.278 188.802 169.507 1.00 43.44  ?  372 GLU B CD    1 
ATOM   9044  O  OE1   . GLU B 1 353 ? 186.246 189.198 168.824 1.00 35.25  ?  372 GLU B OE1   1 
ATOM   9045  O  OE2   . GLU B 1 353 ? 185.412 188.197 170.591 1.00 40.60  -1 372 GLU B OE2   1 
ATOM   9046  N  N     . GLN B 1 354 ? 185.118 192.377 170.219 1.00 14.06  ?  373 GLN B N     1 
ATOM   9047  C  CA    . GLN B 1 354 ? 185.839 192.654 171.456 1.00 14.49  ?  373 GLN B CA    1 
ATOM   9048  C  C     . GLN B 1 354 ? 185.060 193.611 172.349 1.00 22.04  ?  373 GLN B C     1 
ATOM   9049  O  O     . GLN B 1 354 ? 185.046 193.453 173.573 1.00 39.02  ?  373 GLN B O     1 
ATOM   9050  C  CB    . GLN B 1 354 ? 187.224 193.219 171.140 1.00 22.91  ?  373 GLN B CB    1 
ATOM   9051  C  CG    . GLN B 1 354 ? 188.201 192.198 170.581 1.00 30.85  ?  373 GLN B CG    1 
ATOM   9052  C  CD    . GLN B 1 354 ? 188.848 191.358 171.662 1.00 36.22  ?  373 GLN B CD    1 
ATOM   9053  O  OE1   . GLN B 1 354 ? 189.751 191.817 172.361 1.00 31.89  ?  373 GLN B OE1   1 
ATOM   9054  N  NE2   . GLN B 1 354 ? 188.391 190.120 171.804 1.00 40.81  ?  373 GLN B NE2   1 
ATOM   9055  N  N     . GLU B 1 355 ? 184.405 194.613 171.758 1.00 24.51  ?  374 GLU B N     1 
ATOM   9056  C  CA    . GLU B 1 355 ? 183.611 195.536 172.563 1.00 27.39  ?  374 GLU B CA    1 
ATOM   9057  C  C     . GLU B 1 355 ? 182.359 194.870 173.118 1.00 35.93  ?  374 GLU B C     1 
ATOM   9058  O  O     . GLU B 1 355 ? 181.934 195.194 174.229 1.00 38.01  ?  374 GLU B O     1 
ATOM   9059  C  CB    . GLU B 1 355 ? 183.240 196.777 171.753 1.00 34.03  ?  374 GLU B CB    1 
ATOM   9060  C  CG    . GLU B 1 355 ? 183.007 198.014 172.614 1.00 35.59  ?  374 GLU B CG    1 
ATOM   9061  C  CD    . GLU B 1 355 ? 184.288 198.597 173.193 1.00 41.77  ?  374 GLU B CD    1 
ATOM   9062  O  OE1   . GLU B 1 355 ? 184.195 199.568 173.973 1.00 45.16  ?  374 GLU B OE1   1 
ATOM   9063  O  OE2   . GLU B 1 355 ? 185.386 198.103 172.858 1.00 39.45  -1 374 GLU B OE2   1 
ATOM   9064  N  N     . LYS B 1 356 ? 181.758 193.942 172.372 1.00 40.56  ?  375 LYS B N     1 
ATOM   9065  C  CA    . LYS B 1 356 ? 180.656 193.156 172.922 1.00 31.18  ?  375 LYS B CA    1 
ATOM   9066  C  C     . LYS B 1 356 ? 181.128 192.309 174.098 1.00 26.78  ?  375 LYS B C     1 
ATOM   9067  O  O     . LYS B 1 356 ? 180.446 192.215 175.129 1.00 33.58  ?  375 LYS B O     1 
ATOM   9068  C  CB    . LYS B 1 356 ? 180.052 192.271 171.832 1.00 27.87  ?  375 LYS B CB    1 
ATOM   9069  C  CG    . LYS B 1 356 ? 179.020 192.967 170.961 1.00 33.73  ?  375 LYS B CG    1 
ATOM   9070  C  CD    . LYS B 1 356 ? 177.712 193.169 171.704 1.00 36.71  ?  375 LYS B CD    1 
ATOM   9071  C  CE    . LYS B 1 356 ? 177.109 191.838 172.125 1.00 35.57  ?  375 LYS B CE    1 
ATOM   9072  N  NZ    . LYS B 1 356 ? 177.123 190.842 171.017 1.00 31.13  1  375 LYS B NZ    1 
ATOM   9073  N  N     . SER B 1 357 ? 182.304 191.693 173.962 1.00 27.83  ?  376 SER B N     1 
ATOM   9074  C  CA    . SER B 1 357 ? 182.875 190.930 175.066 1.00 23.40  ?  376 SER B CA    1 
ATOM   9075  C  C     . SER B 1 357 ? 183.136 191.826 176.271 1.00 26.89  ?  376 SER B C     1 
ATOM   9076  O  O     . SER B 1 357 ? 182.862 191.439 177.410 1.00 46.25  ?  376 SER B O     1 
ATOM   9077  C  CB    . SER B 1 357 ? 184.163 190.242 174.617 1.00 31.87  ?  376 SER B CB    1 
ATOM   9078  O  OG    . SER B 1 357 ? 184.542 189.225 175.526 1.00 38.22  ?  376 SER B OG    1 
ATOM   9079  N  N     . ARG B 1 358 ? 183.655 193.031 176.035 1.00 23.53  ?  377 ARG B N     1 
ATOM   9080  C  CA    . ARG B 1 358 ? 183.917 193.965 177.126 1.00 28.21  ?  377 ARG B CA    1 
ATOM   9081  C  C     . ARG B 1 358 ? 182.618 194.435 177.773 1.00 36.54  ?  377 ARG B C     1 
ATOM   9082  O  O     . ARG B 1 358 ? 182.573 194.680 178.983 1.00 37.36  ?  377 ARG B O     1 
ATOM   9083  C  CB    . ARG B 1 358 ? 184.727 195.154 176.606 1.00 39.07  ?  377 ARG B CB    1 
ATOM   9084  C  CG    . ARG B 1 358 ? 185.429 195.977 177.679 1.00 43.31  ?  377 ARG B CG    1 
ATOM   9085  C  CD    . ARG B 1 358 ? 184.548 197.104 178.194 1.00 40.54  ?  377 ARG B CD    1 
ATOM   9086  N  NE    . ARG B 1 358 ? 184.282 198.106 177.169 1.00 42.73  ?  377 ARG B NE    1 
ATOM   9087  C  CZ    . ARG B 1 358 ? 183.230 198.913 177.171 1.00 43.31  ?  377 ARG B CZ    1 
ATOM   9088  N  NH1   . ARG B 1 358 ? 182.322 198.864 178.132 1.00 42.48  1  377 ARG B NH1   1 
ATOM   9089  N  NH2   . ARG B 1 358 ? 183.085 199.791 176.183 1.00 40.80  ?  377 ARG B NH2   1 
ATOM   9090  N  N     . GLN B 1 359 ? 181.556 194.579 176.979 1.00 41.76  ?  378 GLN B N     1 
ATOM   9091  C  CA    . GLN B 1 359 ? 180.252 194.906 177.541 1.00 34.87  ?  378 GLN B CA    1 
ATOM   9092  C  C     . GLN B 1 359 ? 179.767 193.790 178.452 1.00 40.91  ?  378 GLN B C     1 
ATOM   9093  O  O     . GLN B 1 359 ? 179.229 194.049 179.534 1.00 48.56  ?  378 GLN B O     1 
ATOM   9094  C  CB    . GLN B 1 359 ? 179.246 195.162 176.418 1.00 36.65  ?  378 GLN B CB    1 
ATOM   9095  C  CG    . GLN B 1 359 ? 179.087 196.628 176.048 1.00 44.71  ?  378 GLN B CG    1 
ATOM   9096  C  CD    . GLN B 1 359 ? 178.301 196.821 174.765 1.00 50.92  ?  378 GLN B CD    1 
ATOM   9097  O  OE1   . GLN B 1 359 ? 177.893 195.853 174.122 1.00 54.42  ?  378 GLN B OE1   1 
ATOM   9098  N  NE2   . GLN B 1 359 ? 178.089 198.075 174.382 1.00 43.53  ?  378 GLN B NE2   1 
ATOM   9099  N  N     . HIS B 1 360 ? 179.969 192.537 178.039 1.00 44.47  ?  379 HIS B N     1 
ATOM   9100  C  CA    . HIS B 1 360 ? 179.656 191.416 178.922 1.00 32.93  ?  379 HIS B CA    1 
ATOM   9101  C  C     . HIS B 1 360 ? 180.501 191.466 180.191 1.00 33.46  ?  379 HIS B C     1 
ATOM   9102  O  O     . HIS B 1 360 ? 180.001 191.198 181.293 1.00 48.90  ?  379 HIS B O     1 
ATOM   9103  C  CB    . HIS B 1 360 ? 179.867 190.093 178.188 1.00 42.39  ?  379 HIS B CB    1 
ATOM   9104  C  CG    . HIS B 1 360 ? 178.944 189.002 178.632 1.00 45.34  ?  379 HIS B CG    1 
ATOM   9105  N  ND1   . HIS B 1 360 ? 177.689 188.822 178.091 1.00 45.13  ?  379 HIS B ND1   1 
ATOM   9106  C  CD2   . HIS B 1 360 ? 179.094 188.031 179.564 1.00 49.85  ?  379 HIS B CD2   1 
ATOM   9107  C  CE1   . HIS B 1 360 ? 177.106 187.788 178.670 1.00 47.49  ?  379 HIS B CE1   1 
ATOM   9108  N  NE2   . HIS B 1 360 ? 177.936 187.291 179.568 1.00 48.69  ?  379 HIS B NE2   1 
ATOM   9109  N  N     . ILE B 1 361 ? 181.785 191.811 180.052 1.00 32.10  ?  380 ILE B N     1 
ATOM   9110  C  CA    . ILE B 1 361 ? 182.674 191.898 181.208 1.00 34.11  ?  380 ILE B CA    1 
ATOM   9111  C  C     . ILE B 1 361 ? 182.166 192.936 182.199 1.00 39.89  ?  380 ILE B C     1 
ATOM   9112  O  O     . ILE B 1 361 ? 182.102 192.685 183.408 1.00 40.02  ?  380 ILE B O     1 
ATOM   9113  C  CB    . ILE B 1 361 ? 184.120 192.208 180.771 1.00 42.65  ?  380 ILE B CB    1 
ATOM   9114  C  CG1   . ILE B 1 361 ? 184.656 191.156 179.795 1.00 48.63  ?  380 ILE B CG1   1 
ATOM   9115  C  CG2   . ILE B 1 361 ? 185.030 192.317 181.983 1.00 42.58  ?  380 ILE B CG2   1 
ATOM   9116  C  CD1   . ILE B 1 361 ? 184.329 189.727 180.166 1.00 42.44  ?  380 ILE B CD1   1 
ATOM   9117  N  N     . GLU B 1 362 ? 181.785 194.110 181.702 1.00 41.74  ?  381 GLU B N     1 
ATOM   9118  C  CA    . GLU B 1 362 ? 181.294 195.176 182.564 1.00 47.40  ?  381 GLU B CA    1 
ATOM   9119  C  C     . GLU B 1 362 ? 179.868 194.937 183.041 1.00 46.47  ?  381 GLU B C     1 
ATOM   9120  O  O     . GLU B 1 362 ? 179.428 195.607 183.982 1.00 48.41  ?  381 GLU B O     1 
ATOM   9121  C  CB    . GLU B 1 362 ? 181.370 196.521 181.834 1.00 53.94  ?  381 GLU B CB    1 
ATOM   9122  C  CG    . GLU B 1 362 ? 182.774 197.096 181.725 1.00 54.50  ?  381 GLU B CG    1 
ATOM   9123  C  CD    . GLU B 1 362 ? 183.461 197.237 183.070 1.00 55.49  ?  381 GLU B CD    1 
ATOM   9124  O  OE1   . GLU B 1 362 ? 182.816 197.720 184.025 1.00 52.45  ?  381 GLU B OE1   1 
ATOM   9125  O  OE2   . GLU B 1 362 ? 184.647 196.861 183.172 1.00 50.91  -1 381 GLU B OE2   1 
ATOM   9126  N  N     . GLN B 1 363 ? 179.143 194.008 182.419 1.00 38.05  ?  382 GLN B N     1 
ATOM   9127  C  CA    . GLN B 1 363 ? 177.755 193.756 182.780 1.00 36.75  ?  382 GLN B CA    1 
ATOM   9128  C  C     . GLN B 1 363 ? 177.580 192.624 183.782 1.00 37.40  ?  382 GLN B C     1 
ATOM   9129  O  O     . GLN B 1 363 ? 176.647 192.673 184.593 1.00 38.09  ?  382 GLN B O     1 
ATOM   9130  C  CB    . GLN B 1 363 ? 176.939 193.443 181.522 1.00 37.94  ?  382 GLN B CB    1 
ATOM   9131  C  CG    . GLN B 1 363 ? 175.440 193.599 181.699 1.00 41.86  ?  382 GLN B CG    1 
ATOM   9132  C  CD    . GLN B 1 363 ? 175.045 195.011 182.078 1.00 50.52  ?  382 GLN B CD    1 
ATOM   9133  O  OE1   . GLN B 1 363 ? 174.874 195.326 183.257 1.00 47.58  ?  382 GLN B OE1   1 
ATOM   9134  N  NE2   . GLN B 1 363 ? 174.900 195.873 181.079 1.00 48.43  ?  382 GLN B NE2   1 
ATOM   9135  N  N     . LEU B 1 364 ? 178.438 191.605 183.758 1.00 38.98  ?  383 LEU B N     1 
ATOM   9136  C  CA    . LEU B 1 364 ? 178.196 190.421 184.578 1.00 39.38  ?  383 LEU B CA    1 
ATOM   9137  C  C     . LEU B 1 364 ? 179.247 190.171 185.649 1.00 42.03  ?  383 LEU B C     1 
ATOM   9138  O  O     . LEU B 1 364 ? 178.895 189.751 186.754 1.00 46.06  ?  383 LEU B O     1 
ATOM   9139  C  CB    . LEU B 1 364 ? 178.071 189.180 183.687 1.00 43.76  ?  383 LEU B CB    1 
ATOM   9140  C  CG    . LEU B 1 364 ? 177.534 187.930 184.385 1.00 47.34  ?  383 LEU B CG    1 
ATOM   9141  C  CD1   . LEU B 1 364 ? 176.157 188.198 184.968 1.00 42.47  ?  383 LEU B CD1   1 
ATOM   9142  C  CD2   . LEU B 1 364 ? 177.472 186.776 183.404 1.00 43.27  ?  383 LEU B CD2   1 
ATOM   9143  N  N     . ILE B 1 365 ? 180.529 190.411 185.368 1.00 32.51  ?  384 ILE B N     1 
ATOM   9144  C  CA    . ILE B 1 365 ? 181.553 190.203 186.385 1.00 36.17  ?  384 ILE B CA    1 
ATOM   9145  C  C     . ILE B 1 365 ? 181.390 191.209 187.517 1.00 28.12  ?  384 ILE B C     1 
ATOM   9146  O  O     . ILE B 1 365 ? 181.035 192.375 187.301 1.00 30.93  ?  384 ILE B O     1 
ATOM   9147  C  CB    . ILE B 1 365 ? 182.962 190.261 185.768 1.00 39.92  ?  384 ILE B CB    1 
ATOM   9148  C  CG1   . ILE B 1 365 ? 183.182 189.091 184.803 1.00 46.32  ?  384 ILE B CG1   1 
ATOM   9149  C  CG2   . ILE B 1 365 ? 184.028 190.279 186.844 1.00 41.94  ?  384 ILE B CG2   1 
ATOM   9150  C  CD1   . ILE B 1 365 ? 182.768 189.338 183.400 1.00 47.18  ?  384 ILE B CD1   1 
ATOM   9151  N  N     . GLN B 1 366 ? 181.651 190.747 188.741 1.00 23.94  ?  385 GLN B N     1 
ATOM   9152  C  CA    . GLN B 1 366 ? 181.479 191.535 189.952 1.00 27.45  ?  385 GLN B CA    1 
ATOM   9153  C  C     . GLN B 1 366 ? 182.805 191.968 190.571 1.00 29.24  ?  385 GLN B C     1 
ATOM   9154  O  O     . GLN B 1 366 ? 182.828 192.359 191.743 1.00 35.95  ?  385 GLN B O     1 
ATOM   9155  C  CB    . GLN B 1 366 ? 180.663 190.746 190.978 1.00 26.39  ?  385 GLN B CB    1 
ATOM   9156  C  CG    . GLN B 1 366 ? 179.456 190.029 190.399 1.00 32.77  ?  385 GLN B CG    1 
ATOM   9157  C  CD    . GLN B 1 366 ? 178.308 190.969 190.100 1.00 41.48  ?  385 GLN B CD    1 
ATOM   9158  O  OE1   . GLN B 1 366 ? 177.666 191.489 191.012 1.00 36.89  ?  385 GLN B OE1   1 
ATOM   9159  N  NE2   . GLN B 1 366 ? 178.036 191.187 188.819 1.00 40.27  ?  385 GLN B NE2   1 
ATOM   9160  N  N     . PHE B 1 367 ? 183.905 191.915 189.821 1.00 20.78  ?  386 PHE B N     1 
ATOM   9161  C  CA    . PHE B 1 367 ? 185.210 192.286 190.348 1.00 20.53  ?  386 PHE B CA    1 
ATOM   9162  C  C     . PHE B 1 367 ? 185.977 193.094 189.312 1.00 25.31  ?  386 PHE B C     1 
ATOM   9163  O  O     . PHE B 1 367 ? 185.823 192.880 188.107 1.00 29.33  ?  386 PHE B O     1 
ATOM   9164  C  CB    . PHE B 1 367 ? 186.014 191.045 190.754 1.00 18.41  ?  386 PHE B CB    1 
ATOM   9165  C  CG    . PHE B 1 367 ? 185.522 190.397 192.014 1.00 25.16  ?  386 PHE B CG    1 
ATOM   9166  C  CD1   . PHE B 1 367 ? 185.574 191.074 193.220 1.00 31.21  ?  386 PHE B CD1   1 
ATOM   9167  C  CD2   . PHE B 1 367 ? 184.992 189.118 191.991 1.00 31.04  ?  386 PHE B CD2   1 
ATOM   9168  C  CE1   . PHE B 1 367 ? 185.115 190.485 194.381 1.00 32.24  ?  386 PHE B CE1   1 
ATOM   9169  C  CE2   . PHE B 1 367 ? 184.532 188.523 193.149 1.00 29.73  ?  386 PHE B CE2   1 
ATOM   9170  C  CZ    . PHE B 1 367 ? 184.595 189.207 194.346 1.00 32.22  ?  386 PHE B CZ    1 
ATOM   9171  N  N     . ASP B 1 368 ? 186.803 194.025 189.791 1.00 26.18  ?  387 ASP B N     1 
ATOM   9172  C  CA    . ASP B 1 368 ? 187.611 194.863 188.914 1.00 24.67  ?  387 ASP B CA    1 
ATOM   9173  C  C     . ASP B 1 368 ? 188.942 194.180 188.640 1.00 31.13  ?  387 ASP B C     1 
ATOM   9174  O  O     . ASP B 1 368 ? 189.652 193.831 189.592 1.00 38.16  ?  387 ASP B O     1 
ATOM   9175  C  CB    . ASP B 1 368 ? 187.847 196.227 189.540 1.00 24.62  ?  387 ASP B CB    1 
ATOM   9176  C  CG    . ASP B 1 368 ? 188.791 197.085 188.725 1.00 39.06  ?  387 ASP B CG    1 
ATOM   9177  O  OD1   . ASP B 1 368 ? 188.465 197.381 187.555 1.00 42.19  ?  387 ASP B OD1   1 
ATOM   9178  O  OD2   . ASP B 1 368 ? 189.858 197.463 189.252 1.00 39.33  -1 387 ASP B OD2   1 
ATOM   9179  N  N     . PRO B 1 369 ? 189.317 193.959 187.378 1.00 25.76  ?  388 PRO B N     1 
ATOM   9180  C  CA    . PRO B 1 369 ? 190.567 193.241 187.102 1.00 14.80  ?  388 PRO B CA    1 
ATOM   9181  C  C     . PRO B 1 369 ? 191.793 194.139 187.145 1.00 22.22  ?  388 PRO B C     1 
ATOM   9182  O  O     . PRO B 1 369 ? 192.672 194.035 186.285 1.00 31.39  ?  388 PRO B O     1 
ATOM   9183  C  CB    . PRO B 1 369 ? 190.344 192.682 185.687 1.00 21.73  ?  388 PRO B CB    1 
ATOM   9184  C  CG    . PRO B 1 369 ? 188.918 193.063 185.302 1.00 28.97  ?  388 PRO B CG    1 
ATOM   9185  C  CD    . PRO B 1 369 ? 188.565 194.235 186.148 1.00 31.33  ?  388 PRO B CD    1 
ATOM   9186  N  N     . MET B 1 370 ? 191.865 195.026 188.135 1.00 34.38  ?  389 MET B N     1 
ATOM   9187  C  CA    . MET B 1 370 ? 193.094 195.770 188.394 1.00 35.96  ?  389 MET B CA    1 
ATOM   9188  C  C     . MET B 1 370 ? 193.477 195.829 189.866 1.00 36.72  ?  389 MET B C     1 
ATOM   9189  O  O     . MET B 1 370 ? 194.673 195.897 190.170 1.00 35.16  ?  389 MET B O     1 
ATOM   9190  C  CB    . MET B 1 370 ? 192.979 197.199 187.841 1.00 36.53  ?  389 MET B CB    1 
ATOM   9191  C  CG    . MET B 1 370 ? 194.180 198.091 188.118 1.00 34.79  ?  389 MET B CG    1 
ATOM   9192  S  SD    . MET B 1 370 ? 193.844 199.836 187.823 1.00 65.60  ?  389 MET B SD    1 
ATOM   9193  C  CE    . MET B 1 370 ? 193.691 200.431 189.504 1.00 41.28  ?  389 MET B CE    1 
ATOM   9194  N  N     . THR B 1 371 ? 192.520 195.775 190.791 1.00 27.62  ?  390 THR B N     1 
ATOM   9195  C  CA    . THR B 1 371 ? 192.796 195.814 192.217 1.00 26.83  ?  390 THR B CA    1 
ATOM   9196  C  C     . THR B 1 371 ? 192.205 194.640 192.982 1.00 24.21  ?  390 THR B C     1 
ATOM   9197  O  O     . THR B 1 371 ? 192.479 194.507 194.180 1.00 29.42  ?  390 THR B O     1 
ATOM   9198  C  CB    . THR B 1 371 ? 192.269 197.122 192.830 1.00 28.37  ?  390 THR B CB    1 
ATOM   9199  O  OG1   . THR B 1 371 ? 190.937 197.367 192.361 1.00 33.69  ?  390 THR B OG1   1 
ATOM   9200  C  CG2   . THR B 1 371 ? 193.160 198.291 192.440 1.00 28.21  ?  390 THR B CG2   1 
ATOM   9201  N  N     . GLY B 1 372 ? 191.413 193.788 192.334 1.00 21.29  ?  391 GLY B N     1 
ATOM   9202  C  CA    . GLY B 1 372 ? 190.760 192.700 193.034 1.00 21.13  ?  391 GLY B CA    1 
ATOM   9203  C  C     . GLY B 1 372 ? 189.610 193.122 193.915 1.00 28.87  ?  391 GLY B C     1 
ATOM   9204  O  O     . GLY B 1 372 ? 189.232 192.379 194.825 1.00 31.55  ?  391 GLY B O     1 
ATOM   9205  N  N     . LEU B 1 373 ? 189.043 194.294 193.673 1.00 25.84  ?  392 LEU B N     1 
ATOM   9206  C  CA    . LEU B 1 373 ? 187.954 194.862 194.447 1.00 20.16  ?  392 LEU B CA    1 
ATOM   9207  C  C     . LEU B 1 373 ? 186.625 194.678 193.726 1.00 26.72  ?  392 LEU B C     1 
ATOM   9208  O  O     . LEU B 1 373 ? 186.584 194.607 192.493 1.00 40.03  ?  392 LEU B O     1 
ATOM   9209  C  CB    . LEU B 1 373 ? 188.191 196.356 194.692 1.00 15.70  ?  392 LEU B CB    1 
ATOM   9210  C  CG    . LEU B 1 373 ? 189.095 196.750 195.861 1.00 9.47   ?  392 LEU B CG    1 
ATOM   9211  C  CD1   . LEU B 1 373 ? 189.066 198.255 196.054 1.00 15.10  ?  392 LEU B CD1   1 
ATOM   9212  C  CD2   . LEU B 1 373 ? 188.671 196.036 197.135 1.00 24.74  ?  392 LEU B CD2   1 
ATOM   9213  N  N     . PRO B 1 374 ? 185.529 194.592 194.477 1.00 16.68  ?  393 PRO B N     1 
ATOM   9214  C  CA    . PRO B 1 374 ? 184.205 194.599 193.849 1.00 11.51  ?  393 PRO B CA    1 
ATOM   9215  C  C     . PRO B 1 374 ? 183.989 195.871 193.045 1.00 11.93  ?  393 PRO B C     1 
ATOM   9216  O  O     . PRO B 1 374 ? 184.491 196.943 193.389 1.00 27.27  ?  393 PRO B O     1 
ATOM   9217  C  CB    . PRO B 1 374 ? 183.249 194.526 195.041 1.00 19.43  ?  393 PRO B CB    1 
ATOM   9218  C  CG    . PRO B 1 374 ? 184.025 193.817 196.091 1.00 18.55  ?  393 PRO B CG    1 
ATOM   9219  C  CD    . PRO B 1 374 ? 185.464 194.213 195.900 1.00 18.67  ?  393 PRO B CD    1 
ATOM   9220  N  N     . ASN B 1 375 ? 183.244 195.740 191.954 1.00 9.52   ?  394 ASN B N     1 
ATOM   9221  C  CA    . ASN B 1 375 ? 182.982 196.858 191.067 1.00 16.28  ?  394 ASN B CA    1 
ATOM   9222  C  C     . ASN B 1 375 ? 181.577 197.405 191.317 1.00 30.54  ?  394 ASN B C     1 
ATOM   9223  O  O     . ASN B 1 375 ? 180.889 197.023 192.273 1.00 38.64  ?  394 ASN B O     1 
ATOM   9224  C  CB    . ASN B 1 375 ? 183.174 196.435 189.609 1.00 18.52  ?  394 ASN B CB    1 
ATOM   9225  C  CG    . ASN B 1 375 ? 182.529 195.108 189.303 1.00 25.56  ?  394 ASN B CG    1 
ATOM   9226  O  OD1   . ASN B 1 375 ? 181.675 194.642 190.054 1.00 36.66  ?  394 ASN B OD1   1 
ATOM   9227  N  ND2   . ASN B 1 375 ? 182.933 194.486 188.202 1.00 30.94  ?  394 ASN B ND2   1 
ATOM   9228  N  N     . ARG B 1 376 ? 181.145 198.317 190.443 1.00 30.41  ?  395 ARG B N     1 
ATOM   9229  C  CA    . ARG B 1 376 ? 179.859 198.981 190.619 1.00 25.87  ?  395 ARG B CA    1 
ATOM   9230  C  C     . ARG B 1 376 ? 178.696 197.997 190.578 1.00 33.50  ?  395 ARG B C     1 
ATOM   9231  O  O     . ARG B 1 376 ? 177.669 198.234 191.220 1.00 44.00  ?  395 ARG B O     1 
ATOM   9232  C  CB    . ARG B 1 376 ? 179.689 200.063 189.553 1.00 30.85  ?  395 ARG B CB    1 
ATOM   9233  C  CG    . ARG B 1 376 ? 178.800 201.218 189.976 1.00 30.92  ?  395 ARG B CG    1 
ATOM   9234  C  CD    . ARG B 1 376 ? 178.180 201.907 188.774 1.00 34.63  ?  395 ARG B CD    1 
ATOM   9235  N  NE    . ARG B 1 376 ? 179.192 202.513 187.917 1.00 40.07  ?  395 ARG B NE    1 
ATOM   9236  C  CZ    . ARG B 1 376 ? 179.627 203.760 188.038 1.00 38.65  ?  395 ARG B CZ    1 
ATOM   9237  N  NH1   . ARG B 1 376 ? 179.166 204.565 188.981 1.00 33.80  1  395 ARG B NH1   1 
ATOM   9238  N  NH2   . ARG B 1 376 ? 180.549 204.211 187.191 1.00 38.46  ?  395 ARG B NH2   1 
ATOM   9239  N  N     . ASN B 1 377 ? 178.831 196.892 189.841 1.00 22.59  ?  396 ASN B N     1 
ATOM   9240  C  CA    . ASN B 1 377 ? 177.768 195.889 189.816 1.00 23.56  ?  396 ASN B CA    1 
ATOM   9241  C  C     . ASN B 1 377 ? 177.588 195.241 191.186 1.00 26.99  ?  396 ASN B C     1 
ATOM   9242  O  O     . ASN B 1 377 ? 176.463 195.120 191.691 1.00 39.52  ?  396 ASN B O     1 
ATOM   9243  C  CB    . ASN B 1 377 ? 178.072 194.832 188.754 1.00 24.42  ?  396 ASN B CB    1 
ATOM   9244  C  CG    . ASN B 1 377 ? 178.214 195.424 187.367 1.00 28.40  ?  396 ASN B CG    1 
ATOM   9245  O  OD1   . ASN B 1 377 ? 177.595 196.438 187.045 1.00 32.38  ?  396 ASN B OD1   1 
ATOM   9246  N  ND2   . ASN B 1 377 ? 179.033 194.793 186.535 1.00 34.58  ?  396 ASN B ND2   1 
ATOM   9247  N  N     . ASN B 1 378 ? 178.693 194.809 191.800 1.00 14.29  ?  397 ASN B N     1 
ATOM   9248  C  CA    . ASN B 1 378 ? 178.617 194.239 193.140 1.00 25.80  ?  397 ASN B CA    1 
ATOM   9249  C  C     . ASN B 1 378 ? 178.137 195.275 194.146 1.00 32.86  ?  397 ASN B C     1 
ATOM   9250  O  O     . ASN B 1 378 ? 177.409 194.945 195.089 1.00 36.00  ?  397 ASN B O     1 
ATOM   9251  C  CB    . ASN B 1 378 ? 179.976 193.674 193.552 1.00 28.35  ?  397 ASN B CB    1 
ATOM   9252  C  CG    . ASN B 1 378 ? 179.862 192.602 194.619 1.00 29.56  ?  397 ASN B CG    1 
ATOM   9253  O  OD1   . ASN B 1 378 ? 178.765 192.278 195.073 1.00 32.62  ?  397 ASN B OD1   1 
ATOM   9254  N  ND2   . ASN B 1 378 ? 180.997 192.052 195.032 1.00 29.06  ?  397 ASN B ND2   1 
ATOM   9255  N  N     . LEU B 1 379 ? 178.539 196.535 193.963 1.00 32.06  ?  398 LEU B N     1 
ATOM   9256  C  CA    . LEU B 1 379 ? 178.035 197.611 194.812 1.00 27.11  ?  398 LEU B CA    1 
ATOM   9257  C  C     . LEU B 1 379 ? 176.519 197.725 194.710 1.00 22.43  ?  398 LEU B C     1 
ATOM   9258  O  O     . LEU B 1 379 ? 175.819 197.827 195.726 1.00 29.31  ?  398 LEU B O     1 
ATOM   9259  C  CB    . LEU B 1 379 ? 178.703 198.928 194.415 1.00 26.75  ?  398 LEU B CB    1 
ATOM   9260  C  CG    . LEU B 1 379 ? 178.279 200.233 195.087 1.00 24.32  ?  398 LEU B CG    1 
ATOM   9261  C  CD1   . LEU B 1 379 ? 179.487 201.119 195.218 1.00 29.65  ?  398 LEU B CD1   1 
ATOM   9262  C  CD2   . LEU B 1 379 ? 177.207 200.947 194.286 1.00 31.82  ?  398 LEU B CD2   1 
ATOM   9263  N  N     . HIS B 1 380 ? 175.997 197.722 193.483 1.00 23.33  ?  399 HIS B N     1 
ATOM   9264  C  CA    . HIS B 1 380 ? 174.558 197.814 193.278 1.00 22.53  ?  399 HIS B CA    1 
ATOM   9265  C  C     . HIS B 1 380 ? 173.845 196.651 193.946 1.00 30.34  ?  399 HIS B C     1 
ATOM   9266  O  O     . HIS B 1 380 ? 172.832 196.836 194.628 1.00 38.10  ?  399 HIS B O     1 
ATOM   9267  C  CB    . HIS B 1 380 ? 174.244 197.848 191.783 1.00 21.60  ?  399 HIS B CB    1 
ATOM   9268  C  CG    . HIS B 1 380 ? 174.649 199.121 191.109 1.00 23.94  ?  399 HIS B CG    1 
ATOM   9269  N  ND1   . HIS B 1 380 ? 175.123 200.212 191.804 1.00 29.51  ?  399 HIS B ND1   1 
ATOM   9270  C  CD2   . HIS B 1 380 ? 174.658 199.474 189.802 1.00 31.61  ?  399 HIS B CD2   1 
ATOM   9271  C  CE1   . HIS B 1 380 ? 175.401 201.185 190.955 1.00 29.79  ?  399 HIS B CE1   1 
ATOM   9272  N  NE2   . HIS B 1 380 ? 175.128 200.763 189.734 1.00 29.71  ?  399 HIS B NE2   1 
ATOM   9273  N  N     . ASN B 1 381 ? 174.377 195.439 193.776 1.00 31.57  ?  400 ASN B N     1 
ATOM   9274  C  CA    . ASN B 1 381 ? 173.746 194.270 194.379 1.00 33.55  ?  400 ASN B CA    1 
ATOM   9275  C  C     . ASN B 1 381 ? 173.763 194.351 195.903 1.00 35.78  ?  400 ASN B C     1 
ATOM   9276  O  O     . ASN B 1 381 ? 172.760 194.044 196.559 1.00 40.81  ?  400 ASN B O     1 
ATOM   9277  C  CB    . ASN B 1 381 ? 174.435 192.994 193.900 1.00 35.50  ?  400 ASN B CB    1 
ATOM   9278  C  CG    . ASN B 1 381 ? 174.224 192.741 192.423 1.00 43.46  ?  400 ASN B CG    1 
ATOM   9279  O  OD1   . ASN B 1 381 ? 175.172 192.487 191.683 1.00 46.95  ?  400 ASN B OD1   1 
ATOM   9280  N  ND2   . ASN B 1 381 ? 172.974 192.821 191.982 1.00 37.99  ?  400 ASN B ND2   1 
ATOM   9281  N  N     . TYR B 1 382 ? 174.889 194.773 196.481 1.00 28.64  ?  401 TYR B N     1 
ATOM   9282  C  CA    . TYR B 1 382 ? 175.010 194.840 197.934 1.00 27.60  ?  401 TYR B CA    1 
ATOM   9283  C  C     . TYR B 1 382 ? 174.055 195.875 198.519 1.00 33.50  ?  401 TYR B C     1 
ATOM   9284  O  O     . TYR B 1 382 ? 173.337 195.599 199.491 1.00 43.32  ?  401 TYR B O     1 
ATOM   9285  C  CB    . TYR B 1 382 ? 176.458 195.157 198.312 1.00 33.68  ?  401 TYR B CB    1 
ATOM   9286  C  CG    . TYR B 1 382 ? 176.767 195.034 199.786 1.00 32.27  ?  401 TYR B CG    1 
ATOM   9287  C  CD1   . TYR B 1 382 ? 177.097 193.807 200.345 1.00 33.71  ?  401 TYR B CD1   1 
ATOM   9288  C  CD2   . TYR B 1 382 ? 176.743 196.145 200.617 1.00 29.55  ?  401 TYR B CD2   1 
ATOM   9289  C  CE1   . TYR B 1 382 ? 177.384 193.689 201.691 1.00 35.46  ?  401 TYR B CE1   1 
ATOM   9290  C  CE2   . TYR B 1 382 ? 177.030 196.036 201.963 1.00 32.65  ?  401 TYR B CE2   1 
ATOM   9291  C  CZ    . TYR B 1 382 ? 177.349 194.807 202.495 1.00 36.43  ?  401 TYR B CZ    1 
ATOM   9292  O  OH    . TYR B 1 382 ? 177.635 194.695 203.836 1.00 40.72  ?  401 TYR B OH    1 
ATOM   9293  N  N     . LEU B 1 383 ? 174.029 197.077 197.936 1.00 36.05  ?  402 LEU B N     1 
ATOM   9294  C  CA    . LEU B 1 383 ? 173.121 198.108 198.429 1.00 37.71  ?  402 LEU B CA    1 
ATOM   9295  C  C     . LEU B 1 383 ? 171.663 197.716 198.226 1.00 36.82  ?  402 LEU B C     1 
ATOM   9296  O  O     . LEU B 1 383 ? 170.820 197.989 199.088 1.00 39.20  ?  402 LEU B O     1 
ATOM   9297  C  CB    . LEU B 1 383 ? 173.421 199.456 197.769 1.00 30.04  ?  402 LEU B CB    1 
ATOM   9298  C  CG    . LEU B 1 383 ? 174.548 200.305 198.375 1.00 31.68  ?  402 LEU B CG    1 
ATOM   9299  C  CD1   . LEU B 1 383 ? 175.930 199.734 198.119 1.00 39.63  ?  402 LEU B CD1   1 
ATOM   9300  C  CD2   . LEU B 1 383 ? 174.465 201.735 197.861 1.00 40.90  ?  402 LEU B CD2   1 
ATOM   9301  N  N     . ASP B 1 384 ? 171.339 197.079 197.096 1.00 35.58  ?  403 ASP B N     1 
ATOM   9302  C  CA    . ASP B 1 384 ? 169.967 196.634 196.877 1.00 34.02  ?  403 ASP B CA    1 
ATOM   9303  C  C     . ASP B 1 384 ? 169.553 195.593 197.907 1.00 37.43  ?  403 ASP B C     1 
ATOM   9304  O  O     . ASP B 1 384 ? 168.442 195.651 198.443 1.00 40.66  ?  403 ASP B O     1 
ATOM   9305  C  CB    . ASP B 1 384 ? 169.811 196.081 195.461 1.00 37.95  ?  403 ASP B CB    1 
ATOM   9306  C  CG    . ASP B 1 384 ? 169.817 197.169 194.408 1.00 43.62  ?  403 ASP B CG    1 
ATOM   9307  O  OD1   . ASP B 1 384 ? 169.539 198.336 194.755 1.00 41.52  ?  403 ASP B OD1   1 
ATOM   9308  O  OD2   . ASP B 1 384 ? 170.097 196.856 193.232 1.00 47.07  -1 403 ASP B OD2   1 
ATOM   9309  N  N     . ASP B 1 385 ? 170.438 194.638 198.205 1.00 42.32  ?  404 ASP B N     1 
ATOM   9310  C  CA    . ASP B 1 385 ? 170.126 193.630 199.212 1.00 39.09  ?  404 ASP B CA    1 
ATOM   9311  C  C     . ASP B 1 385 ? 169.920 194.271 200.579 1.00 45.68  ?  404 ASP B C     1 
ATOM   9312  O  O     . ASP B 1 385 ? 168.973 193.934 201.301 1.00 47.27  ?  404 ASP B O     1 
ATOM   9313  C  CB    . ASP B 1 385 ? 171.239 192.583 199.268 1.00 39.32  ?  404 ASP B CB    1 
ATOM   9314  C  CG    . ASP B 1 385 ? 170.735 191.217 199.694 1.00 54.24  ?  404 ASP B CG    1 
ATOM   9315  O  OD1   . ASP B 1 385 ? 169.954 191.144 200.666 1.00 53.96  ?  404 ASP B OD1   1 
ATOM   9316  O  OD2   . ASP B 1 385 ? 171.123 190.215 199.058 1.00 54.98  -1 404 ASP B OD2   1 
ATOM   9317  N  N     . LEU B 1 386 ? 170.795 195.210 200.948 1.00 42.62  ?  405 LEU B N     1 
ATOM   9318  C  CA    . LEU B 1 386 ? 170.667 195.852 202.253 1.00 41.74  ?  405 LEU B CA    1 
ATOM   9319  C  C     . LEU B 1 386 ? 169.382 196.670 202.351 1.00 46.81  ?  405 LEU B C     1 
ATOM   9320  O  O     . LEU B 1 386 ? 168.665 196.593 203.357 1.00 49.11  ?  405 LEU B O     1 
ATOM   9321  C  CB    . LEU B 1 386 ? 171.889 196.727 202.527 1.00 38.71  ?  405 LEU B CB    1 
ATOM   9322  C  CG    . LEU B 1 386 ? 172.951 196.106 203.436 1.00 40.44  ?  405 LEU B CG    1 
ATOM   9323  C  CD1   . LEU B 1 386 ? 173.568 194.880 202.782 1.00 40.93  ?  405 LEU B CD1   1 
ATOM   9324  C  CD2   . LEU B 1 386 ? 174.022 197.125 203.777 1.00 47.84  ?  405 LEU B CD2   1 
ATOM   9325  N  N     . VAL B 1 387 ? 169.061 197.444 201.311 1.00 48.24  ?  406 VAL B N     1 
ATOM   9326  C  CA    . VAL B 1 387 ? 167.859 198.270 201.356 1.00 43.91  ?  406 VAL B CA    1 
ATOM   9327  C  C     . VAL B 1 387 ? 166.603 197.406 201.304 1.00 44.56  ?  406 VAL B C     1 
ATOM   9328  O  O     . VAL B 1 387 ? 165.564 197.780 201.863 1.00 48.81  ?  406 VAL B O     1 
ATOM   9329  C  CB    . VAL B 1 387 ? 167.886 199.325 200.231 1.00 47.51  ?  406 VAL B CB    1 
ATOM   9330  C  CG1   . VAL B 1 387 ? 167.588 198.701 198.875 1.00 47.05  ?  406 VAL B CG1   1 
ATOM   9331  C  CG2   . VAL B 1 387 ? 166.911 200.455 200.535 1.00 45.57  ?  406 VAL B CG2   1 
ATOM   9332  N  N     . ASP B 1 388 ? 166.664 196.246 200.643 1.00 51.23  ?  407 ASP B N     1 
ATOM   9333  C  CA    . ASP B 1 388 ? 165.527 195.332 200.658 1.00 53.55  ?  407 ASP B CA    1 
ATOM   9334  C  C     . ASP B 1 388 ? 165.349 194.705 202.034 1.00 49.83  ?  407 ASP B C     1 
ATOM   9335  O  O     . ASP B 1 388 ? 164.217 194.507 202.491 1.00 49.07  ?  407 ASP B O     1 
ATOM   9336  C  CB    . ASP B 1 388 ? 165.702 194.256 199.587 1.00 59.33  ?  407 ASP B CB    1 
ATOM   9337  C  CG    . ASP B 1 388 ? 164.383 193.648 199.155 1.00 59.02  ?  407 ASP B CG    1 
ATOM   9338  O  OD1   . ASP B 1 388 ? 163.329 194.103 199.647 1.00 57.71  ?  407 ASP B OD1   1 
ATOM   9339  O  OD2   . ASP B 1 388 ? 164.398 192.717 198.322 1.00 59.41  -1 407 ASP B OD2   1 
ATOM   9340  N  N     . LYS B 1 389 ? 166.455 194.386 202.710 1.00 49.28  ?  408 LYS B N     1 
ATOM   9341  C  CA    . LYS B 1 389 ? 166.385 193.960 204.102 1.00 55.38  ?  408 LYS B CA    1 
ATOM   9342  C  C     . LYS B 1 389 ? 166.030 195.106 205.040 1.00 56.65  ?  408 LYS B C     1 
ATOM   9343  O  O     . LYS B 1 389 ? 165.818 194.863 206.233 1.00 55.54  ?  408 LYS B O     1 
ATOM   9344  C  CB    . LYS B 1 389 ? 167.709 193.324 204.531 1.00 56.27  ?  408 LYS B CB    1 
ATOM   9345  C  CG    . LYS B 1 389 ? 168.068 192.054 203.773 1.00 55.67  ?  408 LYS B CG    1 
ATOM   9346  C  CD    . LYS B 1 389 ? 167.226 190.872 204.233 1.00 57.20  ?  408 LYS B CD    1 
ATOM   9347  C  CE    . LYS B 1 389 ? 166.173 190.500 203.198 1.00 58.78  ?  408 LYS B CE    1 
ATOM   9348  N  NZ    . LYS B 1 389 ? 165.417 189.275 203.579 1.00 58.00  1  408 LYS B NZ    1 
ATOM   9349  N  N     . ALA B 1 390 ? 165.996 196.340 204.530 1.00 58.03  ?  409 ALA B N     1 
ATOM   9350  C  CA    . ALA B 1 390 ? 165.487 197.507 205.255 1.00 54.89  ?  409 ALA B CA    1 
ATOM   9351  C  C     . ALA B 1 390 ? 166.408 197.908 206.404 1.00 55.28  ?  409 ALA B C     1 
ATOM   9352  O  O     . ALA B 1 390 ? 165.951 198.266 207.490 1.00 56.12  ?  409 ALA B O     1 
ATOM   9353  C  CB    . ALA B 1 390 ? 164.057 197.282 205.757 1.00 52.50  ?  409 ALA B CB    1 
ATOM   9354  N  N     . VAL B 1 391 ? 167.714 197.848 206.163 1.00 57.27  ?  410 VAL B N     1 
ATOM   9355  C  CA    . VAL B 1 391 ? 168.713 198.427 207.051 1.00 59.45  ?  410 VAL B CA    1 
ATOM   9356  C  C     . VAL B 1 391 ? 169.377 199.576 206.304 1.00 57.05  ?  410 VAL B C     1 
ATOM   9357  O  O     . VAL B 1 391 ? 169.770 199.424 205.141 1.00 58.87  ?  410 VAL B O     1 
ATOM   9358  C  CB    . VAL B 1 391 ? 169.741 197.380 207.527 1.00 57.75  ?  410 VAL B CB    1 
ATOM   9359  C  CG1   . VAL B 1 391 ? 170.475 196.741 206.352 1.00 55.88  ?  410 VAL B CG1   1 
ATOM   9360  C  CG2   . VAL B 1 391 ? 170.723 198.007 208.505 1.00 55.95  ?  410 VAL B CG2   1 
ATOM   9361  N  N     . SER B 1 392 ? 169.463 200.730 206.952 1.00 47.47  ?  411 SER B N     1 
ATOM   9362  C  CA    . SER B 1 392 ? 169.936 201.930 206.275 1.00 50.47  ?  411 SER B CA    1 
ATOM   9363  C  C     . SER B 1 392 ? 171.458 201.924 206.205 1.00 57.41  ?  411 SER B C     1 
ATOM   9364  O  O     . SER B 1 392 ? 172.115 201.915 207.252 1.00 58.45  ?  411 SER B O     1 
ATOM   9365  C  CB    . SER B 1 392 ? 169.448 203.180 206.996 1.00 50.28  ?  411 SER B CB    1 
ATOM   9366  O  OG    . SER B 1 392 ? 169.789 204.346 206.269 1.00 48.96  ?  411 SER B OG    1 
ATOM   9367  N  N     . PRO B 1 393 ? 172.052 201.931 205.015 1.00 47.16  ?  412 PRO B N     1 
ATOM   9368  C  CA    . PRO B 1 393 ? 173.509 201.979 204.902 1.00 38.81  ?  412 PRO B CA    1 
ATOM   9369  C  C     . PRO B 1 393 ? 174.026 203.407 204.796 1.00 38.34  ?  412 PRO B C     1 
ATOM   9370  O  O     . PRO B 1 393 ? 173.302 204.341 204.445 1.00 42.74  ?  412 PRO B O     1 
ATOM   9371  C  CB    . PRO B 1 393 ? 173.770 201.207 203.602 1.00 37.78  ?  412 PRO B CB    1 
ATOM   9372  C  CG    . PRO B 1 393 ? 172.562 201.512 202.758 1.00 39.30  ?  412 PRO B CG    1 
ATOM   9373  C  CD    . PRO B 1 393 ? 171.406 201.824 203.694 1.00 41.13  ?  412 PRO B CD    1 
ATOM   9374  N  N     . VAL B 1 394 ? 175.310 203.559 205.110 1.00 36.86  ?  413 VAL B N     1 
ATOM   9375  C  CA    . VAL B 1 394 ? 176.004 204.837 205.023 1.00 36.93  ?  413 VAL B CA    1 
ATOM   9376  C  C     . VAL B 1 394 ? 177.103 204.695 203.980 1.00 41.66  ?  413 VAL B C     1 
ATOM   9377  O  O     . VAL B 1 394 ? 177.914 203.760 204.048 1.00 53.43  ?  413 VAL B O     1 
ATOM   9378  C  CB    . VAL B 1 394 ? 176.579 205.259 206.386 1.00 37.52  ?  413 VAL B CB    1 
ATOM   9379  C  CG1   . VAL B 1 394 ? 177.183 206.646 206.297 1.00 33.04  ?  413 VAL B CG1   1 
ATOM   9380  C  CG2   . VAL B 1 394 ? 175.507 205.198 207.462 1.00 46.72  ?  413 VAL B CG2   1 
ATOM   9381  N  N     . VAL B 1 395 ? 177.128 205.614 203.015 1.00 30.05  ?  414 VAL B N     1 
ATOM   9382  C  CA    . VAL B 1 395 ? 177.966 205.495 201.825 1.00 25.08  ?  414 VAL B CA    1 
ATOM   9383  C  C     . VAL B 1 395 ? 179.025 206.588 201.845 1.00 36.35  ?  414 VAL B C     1 
ATOM   9384  O  O     . VAL B 1 395 ? 178.707 207.769 202.039 1.00 48.74  ?  414 VAL B O     1 
ATOM   9385  C  CB    . VAL B 1 395 ? 177.126 205.574 200.538 1.00 30.23  ?  414 VAL B CB    1 
ATOM   9386  C  CG1   . VAL B 1 395 ? 177.960 205.167 199.334 1.00 37.85  ?  414 VAL B CG1   1 
ATOM   9387  C  CG2   . VAL B 1 395 ? 175.891 204.698 200.656 1.00 35.87  ?  414 VAL B CG2   1 
ATOM   9388  N  N     . TYR B 1 396 ? 180.285 206.193 201.654 1.00 24.70  ?  415 TYR B N     1 
ATOM   9389  C  CA    . TYR B 1 396 ? 181.409 207.113 201.532 1.00 22.12  ?  415 TYR B CA    1 
ATOM   9390  C  C     . TYR B 1 396 ? 181.972 206.986 200.124 1.00 25.75  ?  415 TYR B C     1 
ATOM   9391  O  O     . TYR B 1 396 ? 182.351 205.886 199.708 1.00 39.56  ?  415 TYR B O     1 
ATOM   9392  C  CB    . TYR B 1 396 ? 182.500 206.793 202.555 1.00 23.13  ?  415 TYR B CB    1 
ATOM   9393  C  CG    . TYR B 1 396 ? 182.020 206.643 203.977 1.00 27.65  ?  415 TYR B CG    1 
ATOM   9394  C  CD1   . TYR B 1 396 ? 180.912 207.334 204.439 1.00 36.26  ?  415 TYR B CD1   1 
ATOM   9395  C  CD2   . TYR B 1 396 ? 182.663 205.781 204.852 1.00 35.15  ?  415 TYR B CD2   1 
ATOM   9396  C  CE1   . TYR B 1 396 ? 180.474 207.187 205.735 1.00 42.65  ?  415 TYR B CE1   1 
ATOM   9397  C  CE2   . TYR B 1 396 ? 182.227 205.623 206.147 1.00 29.35  ?  415 TYR B CE2   1 
ATOM   9398  C  CZ    . TYR B 1 396 ? 181.132 206.328 206.585 1.00 36.46  ?  415 TYR B CZ    1 
ATOM   9399  O  OH    . TYR B 1 396 ? 180.694 206.173 207.877 1.00 44.97  ?  415 TYR B OH    1 
ATOM   9400  N  N     . LEU B 1 397 ? 182.037 208.100 199.400 1.00 27.96  ?  416 LEU B N     1 
ATOM   9401  C  CA    . LEU B 1 397 ? 182.637 208.137 198.071 1.00 24.74  ?  416 LEU B CA    1 
ATOM   9402  C  C     . LEU B 1 397 ? 183.958 208.886 198.185 1.00 29.52  ?  416 LEU B C     1 
ATOM   9403  O  O     . LEU B 1 397 ? 183.976 210.082 198.493 1.00 42.31  ?  416 LEU B O     1 
ATOM   9404  C  CB    . LEU B 1 397 ? 181.703 208.793 197.055 1.00 29.01  ?  416 LEU B CB    1 
ATOM   9405  C  CG    . LEU B 1 397 ? 182.249 208.970 195.634 1.00 42.32  ?  416 LEU B CG    1 
ATOM   9406  C  CD1   . LEU B 1 397 ? 182.968 207.723 195.154 1.00 40.43  ?  416 LEU B CD1   1 
ATOM   9407  C  CD2   . LEU B 1 397 ? 181.131 209.307 194.676 1.00 44.46  ?  416 LEU B CD2   1 
ATOM   9408  N  N     . ILE B 1 398 ? 185.056 208.178 197.940 1.00 17.01  ?  417 ILE B N     1 
ATOM   9409  C  CA    . ILE B 1 398 ? 186.409 208.689 198.119 1.00 18.55  ?  417 ILE B CA    1 
ATOM   9410  C  C     . ILE B 1 398 ? 187.043 208.889 196.752 1.00 26.88  ?  417 ILE B C     1 
ATOM   9411  O  O     . ILE B 1 398 ? 186.927 208.033 195.868 1.00 38.07  ?  417 ILE B O     1 
ATOM   9412  C  CB    . ILE B 1 398 ? 187.250 207.726 198.979 1.00 15.48  ?  417 ILE B CB    1 
ATOM   9413  C  CG1   . ILE B 1 398 ? 186.554 207.447 200.313 1.00 18.89  ?  417 ILE B CG1   1 
ATOM   9414  C  CG2   . ILE B 1 398 ? 188.639 208.291 199.215 1.00 32.24  ?  417 ILE B CG2   1 
ATOM   9415  C  CD1   . ILE B 1 398 ? 185.767 206.147 200.339 1.00 31.21  ?  417 ILE B CD1   1 
ATOM   9416  N  N     . GLY B 1 399 ? 187.711 210.024 196.574 1.00 26.17  ?  418 GLY B N     1 
ATOM   9417  C  CA    . GLY B 1 399 ? 188.424 210.314 195.350 1.00 30.42  ?  418 GLY B CA    1 
ATOM   9418  C  C     . GLY B 1 399 ? 189.874 210.650 195.622 1.00 33.98  ?  418 GLY B C     1 
ATOM   9419  O  O     . GLY B 1 399 ? 190.173 211.495 196.478 1.00 37.40  ?  418 GLY B O     1 
ATOM   9420  N  N     . VAL B 1 400 ? 190.776 209.987 194.899 1.00 40.27  ?  419 VAL B N     1 
ATOM   9421  C  CA    . VAL B 1 400 ? 192.214 210.139 195.095 1.00 40.13  ?  419 VAL B CA    1 
ATOM   9422  C  C     . VAL B 1 400 ? 192.694 211.210 194.120 1.00 41.56  ?  419 VAL B C     1 
ATOM   9423  O  O     . VAL B 1 400 ? 193.023 210.920 192.968 1.00 44.24  ?  419 VAL B O     1 
ATOM   9424  C  CB    . VAL B 1 400 ? 192.958 208.818 194.890 1.00 40.43  ?  419 VAL B CB    1 
ATOM   9425  C  CG1   . VAL B 1 400 ? 194.459 209.019 195.056 1.00 42.98  ?  419 VAL B CG1   1 
ATOM   9426  C  CG2   . VAL B 1 400 ? 192.440 207.750 195.839 1.00 39.46  ?  419 VAL B CG2   1 
ATOM   9427  N  N     . ASP B 1 401 ? 192.752 212.452 194.588 1.00 46.27  ?  420 ASP B N     1 
ATOM   9428  C  CA    . ASP B 1 401 ? 193.177 213.553 193.741 1.00 47.07  ?  420 ASP B CA    1 
ATOM   9429  C  C     . ASP B 1 401 ? 194.693 213.528 193.556 1.00 50.75  ?  420 ASP B C     1 
ATOM   9430  O  O     . ASP B 1 401 ? 195.415 212.758 194.196 1.00 56.64  ?  420 ASP B O     1 
ATOM   9431  C  CB    . ASP B 1 401 ? 192.735 214.887 194.340 1.00 49.28  ?  420 ASP B CB    1 
ATOM   9432  C  CG    . ASP B 1 401 ? 191.227 215.045 194.363 1.00 53.55  ?  420 ASP B CG    1 
ATOM   9433  O  OD1   . ASP B 1 401 ? 190.554 214.463 193.487 1.00 55.56  ?  420 ASP B OD1   1 
ATOM   9434  O  OD2   . ASP B 1 401 ? 190.715 215.750 195.257 1.00 52.56  -1 420 ASP B OD2   1 
ATOM   9435  N  N     . HIS B 1 402 ? 195.168 214.385 192.650 1.00 53.67  ?  421 HIS B N     1 
ATOM   9436  C  CA    . HIS B 1 402 ? 196.598 214.571 192.399 1.00 55.19  ?  421 HIS B CA    1 
ATOM   9437  C  C     . HIS B 1 402 ? 197.257 213.283 191.910 1.00 51.73  ?  421 HIS B C     1 
ATOM   9438  O  O     . HIS B 1 402 ? 198.281 212.849 192.440 1.00 52.44  ?  421 HIS B O     1 
ATOM   9439  C  CB    . HIS B 1 402 ? 197.314 215.105 193.643 1.00 54.35  ?  421 HIS B CB    1 
ATOM   9440  C  CG    . HIS B 1 402 ? 197.060 216.555 193.910 1.00 51.98  ?  421 HIS B CG    1 
ATOM   9441  N  ND1   . HIS B 1 402 ? 195.792 217.070 194.066 1.00 53.30  ?  421 HIS B ND1   1 
ATOM   9442  C  CD2   . HIS B 1 402 ? 197.911 217.599 194.047 1.00 53.13  ?  421 HIS B CD2   1 
ATOM   9443  C  CE1   . HIS B 1 402 ? 195.872 218.370 194.289 1.00 55.16  ?  421 HIS B CE1   1 
ATOM   9444  N  NE2   . HIS B 1 402 ? 197.147 218.716 194.282 1.00 56.22  ?  421 HIS B NE2   1 
ATOM   9445  N  N     . ILE B 1 403 ? 196.662 212.661 190.893 1.00 50.60  ?  422 ILE B N     1 
ATOM   9446  C  CA    . ILE B 1 403 ? 197.262 211.475 190.292 1.00 53.58  ?  422 ILE B CA    1 
ATOM   9447  C  C     . ILE B 1 403 ? 198.030 211.806 189.015 1.00 53.17  ?  422 ILE B C     1 
ATOM   9448  O  O     . ILE B 1 403 ? 198.915 211.031 188.613 1.00 55.16  ?  422 ILE B O     1 
ATOM   9449  C  CB    . ILE B 1 403 ? 196.189 210.405 190.017 1.00 52.51  ?  422 ILE B CB    1 
ATOM   9450  C  CG1   . ILE B 1 403 ? 196.794 209.006 190.131 1.00 51.87  ?  422 ILE B CG1   1 
ATOM   9451  C  CG2   . ILE B 1 403 ? 195.549 210.610 188.650 1.00 54.17  ?  422 ILE B CG2   1 
ATOM   9452  C  CD1   . ILE B 1 403 ? 197.098 208.595 191.557 1.00 50.36  ?  422 ILE B CD1   1 
ATOM   9453  N  N     . GLN B 1 404 ? 197.727 212.939 188.376 1.00 54.35  ?  423 GLN B N     1 
ATOM   9454  C  CA    . GLN B 1 404 ? 198.431 213.325 187.162 1.00 52.87  ?  423 GLN B CA    1 
ATOM   9455  C  C     . GLN B 1 404 ? 199.911 213.568 187.411 1.00 52.17  ?  423 GLN B C     1 
ATOM   9456  O  O     . GLN B 1 404 ? 200.711 213.406 186.486 1.00 58.94  ?  423 GLN B O     1 
ATOM   9457  C  CB    . GLN B 1 404 ? 197.792 214.572 186.550 1.00 54.78  ?  423 GLN B CB    1 
ATOM   9458  C  CG    . GLN B 1 404 ? 196.380 214.355 186.038 1.00 55.91  ?  423 GLN B CG    1 
ATOM   9459  C  CD    . GLN B 1 404 ? 196.324 213.356 184.901 1.00 56.10  ?  423 GLN B CD    1 
ATOM   9460  O  OE1   . GLN B 1 404 ? 195.776 212.264 185.047 1.00 51.67  ?  423 GLN B OE1   1 
ATOM   9461  N  NE2   . GLN B 1 404 ? 196.901 213.721 183.762 1.00 56.25  ?  423 GLN B NE2   1 
ATOM   9462  N  N     . ASP B 1 405 ? 200.298 213.929 188.636 1.00 46.83  ?  424 ASP B N     1 
ATOM   9463  C  CA    . ASP B 1 405 ? 201.717 214.090 188.935 1.00 53.77  ?  424 ASP B CA    1 
ATOM   9464  C  C     . ASP B 1 405 ? 202.468 212.776 188.739 1.00 63.86  ?  424 ASP B C     1 
ATOM   9465  O  O     . ASP B 1 405 ? 203.487 212.730 188.040 1.00 67.53  ?  424 ASP B O     1 
ATOM   9466  C  CB    . ASP B 1 405 ? 201.899 214.632 190.357 1.00 52.85  ?  424 ASP B CB    1 
ATOM   9467  C  CG    . ASP B 1 405 ? 201.366 213.690 191.425 1.00 59.49  ?  424 ASP B CG    1 
ATOM   9468  O  OD1   . ASP B 1 405 ? 200.682 212.708 191.070 1.00 63.59  ?  424 ASP B OD1   1 
ATOM   9469  O  OD2   . ASP B 1 405 ? 201.632 213.933 192.621 1.00 60.33  -1 424 ASP B OD2   1 
ATOM   9470  N  N     . VAL B 1 406 ? 201.958 211.689 189.325 1.00 52.12  ?  425 VAL B N     1 
ATOM   9471  C  CA    . VAL B 1 406 ? 202.582 210.382 189.146 1.00 38.28  ?  425 VAL B CA    1 
ATOM   9472  C  C     . VAL B 1 406 ? 202.470 209.935 187.695 1.00 39.37  ?  425 VAL B C     1 
ATOM   9473  O  O     . VAL B 1 406 ? 203.422 209.386 187.125 1.00 46.15  ?  425 VAL B O     1 
ATOM   9474  C  CB    . VAL B 1 406 ? 201.959 209.351 190.106 1.00 44.27  ?  425 VAL B CB    1 
ATOM   9475  C  CG1   . VAL B 1 406 ? 202.638 207.999 189.948 1.00 48.23  ?  425 VAL B CG1   1 
ATOM   9476  C  CG2   . VAL B 1 406 ? 202.068 209.830 191.540 1.00 46.06  ?  425 VAL B CG2   1 
ATOM   9477  N  N     . ILE B 1 407 ? 201.315 210.183 187.067 1.00 37.35  ?  426 ILE B N     1 
ATOM   9478  C  CA    . ILE B 1 407 ? 201.113 209.745 185.686 1.00 41.76  ?  426 ILE B CA    1 
ATOM   9479  C  C     . ILE B 1 407 ? 202.148 210.381 184.764 1.00 50.46  ?  426 ILE B C     1 
ATOM   9480  O  O     . ILE B 1 407 ? 202.730 209.715 183.900 1.00 55.59  ?  426 ILE B O     1 
ATOM   9481  C  CB    . ILE B 1 407 ? 199.679 210.060 185.221 1.00 44.89  ?  426 ILE B CB    1 
ATOM   9482  C  CG1   . ILE B 1 407 ? 198.663 209.258 186.032 1.00 50.69  ?  426 ILE B CG1   1 
ATOM   9483  C  CG2   . ILE B 1 407 ? 199.521 209.763 183.739 1.00 50.30  ?  426 ILE B CG2   1 
ATOM   9484  C  CD1   . ILE B 1 407 ? 197.237 209.426 185.561 1.00 50.82  ?  426 ILE B CD1   1 
ATOM   9485  N  N     . ASP B 1 408 ? 202.390 211.682 184.931 1.00 48.69  ?  427 ASP B N     1 
ATOM   9486  C  CA    . ASP B 1 408 ? 203.346 212.373 184.074 1.00 46.32  ?  427 ASP B CA    1 
ATOM   9487  C  C     . ASP B 1 408 ? 204.784 212.023 184.438 1.00 46.19  ?  427 ASP B C     1 
ATOM   9488  O  O     . ASP B 1 408 ? 205.615 211.806 183.549 1.00 48.93  ?  427 ASP B O     1 
ATOM   9489  C  CB    . ASP B 1 408 ? 203.119 213.882 184.154 1.00 51.42  ?  427 ASP B CB    1 
ATOM   9490  C  CG    . ASP B 1 408 ? 201.711 214.279 183.754 1.00 56.14  ?  427 ASP B CG    1 
ATOM   9491  O  OD1   . ASP B 1 408 ? 200.960 213.405 183.271 1.00 53.51  ?  427 ASP B OD1   1 
ATOM   9492  O  OD2   . ASP B 1 408 ? 201.352 215.462 183.928 1.00 53.69  -1 427 ASP B OD2   1 
ATOM   9493  N  N     . SER B 1 409 ? 205.104 211.965 185.735 1.00 46.09  ?  428 SER B N     1 
ATOM   9494  C  CA    . SER B 1 409 ? 206.496 211.793 186.138 1.00 43.69  ?  428 SER B CA    1 
ATOM   9495  C  C     . SER B 1 409 ? 206.995 210.377 185.872 1.00 46.46  ?  428 SER B C     1 
ATOM   9496  O  O     . SER B 1 409 ? 208.117 210.194 185.384 1.00 48.35  ?  428 SER B O     1 
ATOM   9497  C  CB    . SER B 1 409 ? 206.660 212.149 187.615 1.00 43.52  ?  428 SER B CB    1 
ATOM   9498  O  OG    . SER B 1 409 ? 205.793 211.377 188.426 1.00 48.08  ?  428 SER B OG    1 
ATOM   9499  N  N     . LEU B 1 410 ? 206.187 209.361 186.182 1.00 47.32  ?  429 LEU B N     1 
ATOM   9500  C  CA    . LEU B 1 410 ? 206.644 207.981 186.107 1.00 45.05  ?  429 LEU B CA    1 
ATOM   9501  C  C     . LEU B 1 410 ? 205.867 207.123 185.118 1.00 42.79  ?  429 LEU B C     1 
ATOM   9502  O  O     . LEU B 1 410 ? 206.195 205.941 184.961 1.00 42.04  ?  429 LEU B O     1 
ATOM   9503  C  CB    . LEU B 1 410 ? 206.588 207.327 187.496 1.00 45.59  ?  429 LEU B CB    1 
ATOM   9504  C  CG    . LEU B 1 410 ? 207.777 207.483 188.453 1.00 44.92  ?  429 LEU B CG    1 
ATOM   9505  C  CD1   . LEU B 1 410 ? 209.029 206.840 187.872 1.00 45.13  ?  429 LEU B CD1   1 
ATOM   9506  C  CD2   . LEU B 1 410 ? 208.037 208.936 188.826 1.00 45.83  ?  429 LEU B CD2   1 
ATOM   9507  N  N     . GLY B 1 411 ? 204.869 207.670 184.438 1.00 38.15  ?  430 GLY B N     1 
ATOM   9508  C  CA    . GLY B 1 411 ? 204.091 206.887 183.502 1.00 32.58  ?  430 GLY B CA    1 
ATOM   9509  C  C     . GLY B 1 411 ? 202.876 206.247 184.141 1.00 38.13  ?  430 GLY B C     1 
ATOM   9510  O  O     . GLY B 1 411 ? 202.565 206.436 185.320 1.00 47.26  ?  430 GLY B O     1 
ATOM   9511  N  N     . TYR B 1 412 ? 202.174 205.460 183.324 1.00 40.47  ?  431 TYR B N     1 
ATOM   9512  C  CA    . TYR B 1 412 ? 200.922 204.854 183.763 1.00 49.86  ?  431 TYR B CA    1 
ATOM   9513  C  C     . TYR B 1 412 ? 201.146 203.673 184.700 1.00 46.49  ?  431 TYR B C     1 
ATOM   9514  O  O     . TYR B 1 412 ? 200.306 203.411 185.569 1.00 40.88  ?  431 TYR B O     1 
ATOM   9515  C  CB    . TYR B 1 412 ? 200.105 204.416 182.548 1.00 45.54  ?  431 TYR B CB    1 
ATOM   9516  C  CG    . TYR B 1 412 ? 199.135 205.469 182.066 1.00 47.50  ?  431 TYR B CG    1 
ATOM   9517  C  CD1   . TYR B 1 412 ? 197.873 205.592 182.630 1.00 49.94  ?  431 TYR B CD1   1 
ATOM   9518  C  CD2   . TYR B 1 412 ? 199.488 206.349 181.052 1.00 48.03  ?  431 TYR B CD2   1 
ATOM   9519  C  CE1   . TYR B 1 412 ? 196.986 206.558 182.191 1.00 49.86  ?  431 TYR B CE1   1 
ATOM   9520  C  CE2   . TYR B 1 412 ? 198.611 207.317 180.608 1.00 51.99  ?  431 TYR B CE2   1 
ATOM   9521  C  CZ    . TYR B 1 412 ? 197.361 207.418 181.179 1.00 52.58  ?  431 TYR B CZ    1 
ATOM   9522  O  OH    . TYR B 1 412 ? 196.485 208.383 180.737 1.00 48.47  ?  431 TYR B OH    1 
ATOM   9523  N  N     . ALA B 1 413 ? 202.260 202.953 184.541 1.00 32.10  ?  432 ALA B N     1 
ATOM   9524  C  CA    . ALA B 1 413 ? 202.509 201.778 185.371 1.00 27.36  ?  432 ALA B CA    1 
ATOM   9525  C  C     . ALA B 1 413 ? 202.667 202.151 186.841 1.00 32.44  ?  432 ALA B C     1 
ATOM   9526  O  O     . ALA B 1 413 ? 202.092 201.500 187.722 1.00 47.30  ?  432 ALA B O     1 
ATOM   9527  C  CB    . ALA B 1 413 ? 203.749 201.037 184.870 1.00 34.13  ?  432 ALA B CB    1 
ATOM   9528  N  N     . TRP B 1 414 ? 203.439 203.198 187.132 1.00 28.18  ?  433 TRP B N     1 
ATOM   9529  C  CA    . TRP B 1 414 ? 203.606 203.593 188.524 1.00 30.06  ?  433 TRP B CA    1 
ATOM   9530  C  C     . TRP B 1 414 ? 202.372 204.287 189.080 1.00 33.87  ?  433 TRP B C     1 
ATOM   9531  O  O     . TRP B 1 414 ? 202.144 204.233 190.290 1.00 36.07  ?  433 TRP B O     1 
ATOM   9532  C  CB    . TRP B 1 414 ? 204.838 204.478 188.682 1.00 38.05  ?  433 TRP B CB    1 
ATOM   9533  C  CG    . TRP B 1 414 ? 206.097 203.793 188.260 1.00 41.21  ?  433 TRP B CG    1 
ATOM   9534  C  CD1   . TRP B 1 414 ? 206.755 203.940 187.076 1.00 40.85  ?  433 TRP B CD1   1 
ATOM   9535  C  CD2   . TRP B 1 414 ? 206.833 202.823 189.011 1.00 36.27  ?  433 TRP B CD2   1 
ATOM   9536  N  NE1   . TRP B 1 414 ? 207.868 203.136 187.050 1.00 40.73  ?  433 TRP B NE1   1 
ATOM   9537  C  CE2   . TRP B 1 414 ? 207.936 202.438 188.226 1.00 38.68  ?  433 TRP B CE2   1 
ATOM   9538  C  CE3   . TRP B 1 414 ? 206.669 202.247 190.273 1.00 37.49  ?  433 TRP B CE3   1 
ATOM   9539  C  CZ2   . TRP B 1 414 ? 208.871 201.506 188.664 1.00 36.33  ?  433 TRP B CZ2   1 
ATOM   9540  C  CZ3   . TRP B 1 414 ? 207.597 201.325 190.705 1.00 32.07  ?  433 TRP B CZ3   1 
ATOM   9541  C  CH2   . TRP B 1 414 ? 208.684 200.962 189.904 1.00 32.69  ?  433 TRP B CH2   1 
ATOM   9542  N  N     . ALA B 1 415 ? 201.558 204.916 188.230 1.00 38.53  ?  434 ALA B N     1 
ATOM   9543  C  CA    . ALA B 1 415 ? 200.253 205.379 188.688 1.00 41.92  ?  434 ALA B CA    1 
ATOM   9544  C  C     . ALA B 1 415 ? 199.381 204.202 189.109 1.00 45.69  ?  434 ALA B C     1 
ATOM   9545  O  O     . ALA B 1 415 ? 198.706 204.253 190.145 1.00 45.31  ?  434 ALA B O     1 
ATOM   9546  C  CB    . ALA B 1 415 ? 199.569 206.193 187.591 1.00 36.15  ?  434 ALA B CB    1 
ATOM   9547  N  N     . ASP B 1 416 ? 199.394 203.129 188.315 1.00 42.03  ?  435 ASP B N     1 
ATOM   9548  C  CA    . ASP B 1 416 ? 198.714 201.898 188.703 1.00 32.24  ?  435 ASP B CA    1 
ATOM   9549  C  C     . ASP B 1 416 ? 199.228 201.392 190.044 1.00 23.83  ?  435 ASP B C     1 
ATOM   9550  O  O     . ASP B 1 416 ? 198.445 201.026 190.928 1.00 33.74  ?  435 ASP B O     1 
ATOM   9551  C  CB    . ASP B 1 416 ? 198.907 200.839 187.616 1.00 36.39  ?  435 ASP B CB    1 
ATOM   9552  C  CG    . ASP B 1 416 ? 198.295 199.505 187.984 1.00 45.10  ?  435 ASP B CG    1 
ATOM   9553  O  OD1   . ASP B 1 416 ? 197.077 199.331 187.775 1.00 46.87  ?  435 ASP B OD1   1 
ATOM   9554  O  OD2   . ASP B 1 416 ? 199.034 198.628 188.479 1.00 44.78  -1 435 ASP B OD2   1 
ATOM   9555  N  N     . GLN B 1 417 ? 200.550 201.371 190.213 1.00 23.52  ?  436 GLN B N     1 
ATOM   9556  C  CA    . GLN B 1 417 ? 201.121 200.914 191.474 1.00 27.14  ?  436 GLN B CA    1 
ATOM   9557  C  C     . GLN B 1 417 ? 200.700 201.806 192.636 1.00 34.85  ?  436 GLN B C     1 
ATOM   9558  O  O     . GLN B 1 417 ? 200.479 201.310 193.742 1.00 45.69  ?  436 GLN B O     1 
ATOM   9559  C  CB    . GLN B 1 417 ? 202.645 200.848 191.374 1.00 33.25  ?  436 GLN B CB    1 
ATOM   9560  C  CG    . GLN B 1 417 ? 203.141 199.889 190.307 1.00 30.64  ?  436 GLN B CG    1 
ATOM   9561  C  CD    . GLN B 1 417 ? 202.735 198.456 190.580 1.00 30.85  ?  436 GLN B CD    1 
ATOM   9562  O  OE1   . GLN B 1 417 ? 203.032 197.906 191.639 1.00 36.24  ?  436 GLN B OE1   1 
ATOM   9563  N  NE2   . GLN B 1 417 ? 202.048 197.844 189.623 1.00 35.24  ?  436 GLN B NE2   1 
ATOM   9564  N  N     . ALA B 1 418 ? 200.576 203.115 192.406 1.00 27.57  ?  437 ALA B N     1 
ATOM   9565  C  CA    . ALA B 1 418 ? 200.117 204.019 193.457 1.00 22.48  ?  437 ALA B CA    1 
ATOM   9566  C  C     . ALA B 1 418 ? 198.668 203.735 193.844 1.00 26.97  ?  437 ALA B C     1 
ATOM   9567  O  O     . ALA B 1 418 ? 198.324 203.730 195.036 1.00 40.03  ?  437 ALA B O     1 
ATOM   9568  C  CB    . ALA B 1 418 ? 200.275 205.471 193.005 1.00 30.56  ?  437 ALA B CB    1 
ATOM   9569  N  N     . LEU B 1 419 ? 197.802 203.512 192.852 1.00 27.77  ?  438 LEU B N     1 
ATOM   9570  C  CA    . LEU B 1 419 ? 196.422 203.149 193.163 1.00 29.26  ?  438 LEU B CA    1 
ATOM   9571  C  C     . LEU B 1 419 ? 196.356 201.847 193.950 1.00 32.98  ?  438 LEU B C     1 
ATOM   9572  O  O     . LEU B 1 419 ? 195.574 201.729 194.900 1.00 34.09  ?  438 LEU B O     1 
ATOM   9573  C  CB    . LEU B 1 419 ? 195.575 203.054 191.890 1.00 28.22  ?  438 LEU B CB    1 
ATOM   9574  C  CG    . LEU B 1 419 ? 194.927 204.332 191.339 1.00 37.21  ?  438 LEU B CG    1 
ATOM   9575  C  CD1   . LEU B 1 419 ? 195.918 205.273 190.683 1.00 41.31  ?  438 LEU B CD1   1 
ATOM   9576  C  CD2   . LEU B 1 419 ? 193.806 203.980 190.373 1.00 28.03  ?  438 LEU B CD2   1 
ATOM   9577  N  N     . LEU B 1 420 ? 197.168 200.855 193.577 1.00 34.37  ?  439 LEU B N     1 
ATOM   9578  C  CA    . LEU B 1 420 ? 197.193 199.622 194.360 1.00 21.18  ?  439 LEU B CA    1 
ATOM   9579  C  C     . LEU B 1 420 ? 197.779 199.826 195.754 1.00 18.98  ?  439 LEU B C     1 
ATOM   9580  O  O     . LEU B 1 420 ? 197.354 199.153 196.696 1.00 35.04  ?  439 LEU B O     1 
ATOM   9581  C  CB    . LEU B 1 420 ? 197.934 198.513 193.612 1.00 21.74  ?  439 LEU B CB    1 
ATOM   9582  C  CG    . LEU B 1 420 ? 197.140 197.742 192.545 1.00 23.42  ?  439 LEU B CG    1 
ATOM   9583  C  CD1   . LEU B 1 420 ? 196.824 198.533 191.292 1.00 26.90  ?  439 LEU B CD1   1 
ATOM   9584  C  CD2   . LEU B 1 420 ? 197.888 196.479 192.184 1.00 26.25  ?  439 LEU B CD2   1 
ATOM   9585  N  N     . GLU B 1 421 ? 198.737 200.742 195.915 1.00 14.81  ?  440 GLU B N     1 
ATOM   9586  C  CA    . GLU B 1 421 ? 199.213 201.082 197.254 1.00 21.49  ?  440 GLU B CA    1 
ATOM   9587  C  C     . GLU B 1 421 ? 198.078 201.627 198.112 1.00 35.25  ?  440 GLU B C     1 
ATOM   9588  O  O     . GLU B 1 421 ? 197.893 201.203 199.262 1.00 47.05  ?  440 GLU B O     1 
ATOM   9589  C  CB    . GLU B 1 421 ? 200.343 202.110 197.173 1.00 28.69  ?  440 GLU B CB    1 
ATOM   9590  C  CG    . GLU B 1 421 ? 201.656 201.619 196.578 1.00 40.18  ?  440 GLU B CG    1 
ATOM   9591  C  CD    . GLU B 1 421 ? 202.487 200.816 197.555 1.00 45.08  ?  440 GLU B CD    1 
ATOM   9592  O  OE1   . GLU B 1 421 ? 202.306 200.989 198.778 1.00 46.49  ?  440 GLU B OE1   1 
ATOM   9593  O  OE2   . GLU B 1 421 ? 203.341 200.030 197.096 1.00 45.18  -1 440 GLU B OE2   1 
ATOM   9594  N  N     . VAL B 1 422 ? 197.304 202.566 197.562 1.00 28.35  ?  441 VAL B N     1 
ATOM   9595  C  CA    . VAL B 1 422 ? 196.195 203.151 198.313 1.00 25.08  ?  441 VAL B CA    1 
ATOM   9596  C  C     . VAL B 1 422 ? 195.135 202.097 198.614 1.00 35.31  ?  441 VAL B C     1 
ATOM   9597  O  O     . VAL B 1 422 ? 194.552 202.072 199.707 1.00 40.75  ?  441 VAL B O     1 
ATOM   9598  C  CB    . VAL B 1 422 ? 195.609 204.353 197.550 1.00 27.00  ?  441 VAL B CB    1 
ATOM   9599  C  CG1   . VAL B 1 422 ? 194.459 204.968 198.331 1.00 35.26  ?  441 VAL B CG1   1 
ATOM   9600  C  CG2   . VAL B 1 422 ? 196.691 205.391 197.286 1.00 28.39  ?  441 VAL B CG2   1 
ATOM   9601  N  N     . VAL B 1 423 ? 194.869 201.210 197.653 1.00 31.82  ?  442 VAL B N     1 
ATOM   9602  C  CA    . VAL B 1 423 ? 193.873 200.162 197.860 1.00 19.47  ?  442 VAL B CA    1 
ATOM   9603  C  C     . VAL B 1 423 ? 194.333 199.190 198.940 1.00 23.12  ?  442 VAL B C     1 
ATOM   9604  O  O     . VAL B 1 423 ? 193.532 198.731 199.760 1.00 30.51  ?  442 VAL B O     1 
ATOM   9605  C  CB    . VAL B 1 423 ? 193.574 199.445 196.530 1.00 16.25  ?  442 VAL B CB    1 
ATOM   9606  C  CG1   . VAL B 1 423 ? 192.810 198.154 196.773 1.00 25.13  ?  442 VAL B CG1   1 
ATOM   9607  C  CG2   . VAL B 1 423 ? 192.782 200.354 195.608 1.00 16.28  ?  442 VAL B CG2   1 
ATOM   9608  N  N     . ASN B 1 424 ? 195.629 198.869 198.971 1.00 23.54  ?  443 ASN B N     1 
ATOM   9609  C  CA    . ASN B 1 424 ? 196.142 197.996 200.020 1.00 27.63  ?  443 ASN B CA    1 
ATOM   9610  C  C     . ASN B 1 424 ? 196.067 198.670 201.383 1.00 29.87  ?  443 ASN B C     1 
ATOM   9611  O  O     . ASN B 1 424 ? 195.800 198.011 202.393 1.00 38.81  ?  443 ASN B O     1 
ATOM   9612  C  CB    . ASN B 1 424 ? 197.578 197.575 199.712 1.00 24.13  ?  443 ASN B CB    1 
ATOM   9613  C  CG    . ASN B 1 424 ? 198.014 196.368 200.521 1.00 36.68  ?  443 ASN B CG    1 
ATOM   9614  O  OD1   . ASN B 1 424 ? 197.183 195.641 201.067 1.00 42.02  ?  443 ASN B OD1   1 
ATOM   9615  N  ND2   . ASN B 1 424 ? 199.319 196.153 200.611 1.00 35.41  ?  443 ASN B ND2   1 
ATOM   9616  N  N     . ARG B 1 425 ? 196.305 199.983 201.434 1.00 22.29  ?  444 ARG B N     1 
ATOM   9617  C  CA    . ARG B 1 425 ? 196.133 200.708 202.691 1.00 28.44  ?  444 ARG B CA    1 
ATOM   9618  C  C     . ARG B 1 425 ? 194.681 200.661 203.158 1.00 32.66  ?  444 ARG B C     1 
ATOM   9619  O  O     . ARG B 1 425 ? 194.404 200.449 204.349 1.00 39.06  ?  444 ARG B O     1 
ATOM   9620  C  CB    . ARG B 1 425 ? 196.605 202.151 202.526 1.00 31.28  ?  444 ARG B CB    1 
ATOM   9621  C  CG    . ARG B 1 425 ? 198.108 202.288 202.363 1.00 31.04  ?  444 ARG B CG    1 
ATOM   9622  C  CD    . ARG B 1 425 ? 198.489 203.672 201.870 1.00 34.19  ?  444 ARG B CD    1 
ATOM   9623  N  NE    . ARG B 1 425 ? 199.925 203.903 201.957 1.00 35.86  ?  444 ARG B NE    1 
ATOM   9624  C  CZ    . ARG B 1 425 ? 200.508 205.080 201.775 1.00 36.98  ?  444 ARG B CZ    1 
ATOM   9625  N  NH1   . ARG B 1 425 ? 199.804 206.163 201.495 1.00 41.30  1  444 ARG B NH1   1 
ATOM   9626  N  NH2   . ARG B 1 425 ? 201.831 205.170 201.873 1.00 34.63  ?  444 ARG B NH2   1 
ATOM   9627  N  N     . PHE B 1 426 ? 193.741 200.843 202.227 1.00 31.00  ?  445 PHE B N     1 
ATOM   9628  C  CA    . PHE B 1 426 ? 192.324 200.726 202.560 1.00 29.53  ?  445 PHE B CA    1 
ATOM   9629  C  C     . PHE B 1 426 ? 192.000 199.333 203.083 1.00 36.99  ?  445 PHE B C     1 
ATOM   9630  O  O     . PHE B 1 426 ? 191.266 199.179 204.065 1.00 46.95  ?  445 PHE B O     1 
ATOM   9631  C  CB    . PHE B 1 426 ? 191.464 201.039 201.334 1.00 33.05  ?  445 PHE B CB    1 
ATOM   9632  C  CG    . PHE B 1 426 ? 191.439 202.491 200.957 1.00 31.07  ?  445 PHE B CG    1 
ATOM   9633  C  CD1   . PHE B 1 426 ? 191.900 203.460 201.830 1.00 28.76  ?  445 PHE B CD1   1 
ATOM   9634  C  CD2   . PHE B 1 426 ? 190.941 202.887 199.726 1.00 35.76  ?  445 PHE B CD2   1 
ATOM   9635  C  CE1   . PHE B 1 426 ? 191.871 204.795 201.479 1.00 28.40  ?  445 PHE B CE1   1 
ATOM   9636  C  CE2   . PHE B 1 426 ? 190.911 204.222 199.372 1.00 34.05  ?  445 PHE B CE2   1 
ATOM   9637  C  CZ    . PHE B 1 426 ? 191.377 205.176 200.250 1.00 27.83  ?  445 PHE B CZ    1 
ATOM   9638  N  N     . ARG B 1 427 ? 192.533 198.302 202.424 1.00 28.41  ?  446 ARG B N     1 
ATOM   9639  C  CA    . ARG B 1 427 ? 192.274 196.930 202.846 1.00 27.71  ?  446 ARG B CA    1 
ATOM   9640  C  C     . ARG B 1 427 ? 192.848 196.664 204.232 1.00 27.68  ?  446 ARG B C     1 
ATOM   9641  O  O     . ARG B 1 427 ? 192.227 195.975 205.050 1.00 36.89  ?  446 ARG B O     1 
ATOM   9642  C  CB    . ARG B 1 427 ? 192.858 195.957 201.824 1.00 33.02  ?  446 ARG B CB    1 
ATOM   9643  C  CG    . ARG B 1 427 ? 192.045 195.854 200.543 1.00 33.17  ?  446 ARG B CG    1 
ATOM   9644  C  CD    . ARG B 1 427 ? 191.930 194.417 200.068 1.00 26.01  ?  446 ARG B CD    1 
ATOM   9645  N  NE    . ARG B 1 427 ? 191.431 194.333 198.701 1.00 25.10  ?  446 ARG B NE    1 
ATOM   9646  C  CZ    . ARG B 1 427 ? 192.175 194.517 197.618 1.00 36.88  ?  446 ARG B CZ    1 
ATOM   9647  N  NH1   . ARG B 1 427 ? 193.466 194.793 197.705 1.00 42.35  1  446 ARG B NH1   1 
ATOM   9648  N  NH2   . ARG B 1 427 ? 191.611 194.418 196.419 1.00 37.89  ?  446 ARG B NH2   1 
ATOM   9649  N  N     . GLU B 1 428 ? 194.039 197.196 204.509 1.00 28.58  ?  447 GLU B N     1 
ATOM   9650  C  CA    . GLU B 1 428 ? 194.640 197.029 205.827 1.00 36.84  ?  447 GLU B CA    1 
ATOM   9651  C  C     . GLU B 1 428 ? 193.803 197.702 206.906 1.00 34.40  ?  447 GLU B C     1 
ATOM   9652  O  O     . GLU B 1 428 ? 193.626 197.146 207.996 1.00 40.90  ?  447 GLU B O     1 
ATOM   9653  C  CB    . GLU B 1 428 ? 196.066 197.579 205.825 1.00 40.45  ?  447 GLU B CB    1 
ATOM   9654  C  CG    . GLU B 1 428 ? 196.947 197.006 206.918 1.00 44.91  ?  447 GLU B CG    1 
ATOM   9655  C  CD    . GLU B 1 428 ? 198.417 197.269 206.673 1.00 49.44  ?  447 GLU B CD    1 
ATOM   9656  O  OE1   . GLU B 1 428 ? 198.758 197.746 205.570 1.00 46.19  ?  447 GLU B OE1   1 
ATOM   9657  O  OE2   . GLU B 1 428 ? 199.229 196.998 207.582 1.00 45.34  -1 447 GLU B OE2   1 
ATOM   9658  N  N     . LYS B 1 429 ? 193.276 198.891 206.624 1.00 32.09  ?  448 LYS B N     1 
ATOM   9659  C  CA    . LYS B 1 429 ? 192.458 199.598 207.604 1.00 35.68  ?  448 LYS B CA    1 
ATOM   9660  C  C     . LYS B 1 429 ? 190.993 199.170 207.576 1.00 35.01  ?  448 LYS B C     1 
ATOM   9661  O  O     . LYS B 1 429 ? 190.193 199.694 208.357 1.00 36.64  ?  448 LYS B O     1 
ATOM   9662  C  CB    . LYS B 1 429 ? 192.568 201.112 207.387 1.00 36.71  ?  448 LYS B CB    1 
ATOM   9663  C  CG    . LYS B 1 429 ? 192.422 201.925 208.664 1.00 37.57  ?  448 LYS B CG    1 
ATOM   9664  C  CD    . LYS B 1 429 ? 192.791 203.379 208.439 1.00 43.77  ?  448 LYS B CD    1 
ATOM   9665  C  CE    . LYS B 1 429 ? 194.297 203.548 208.360 1.00 38.82  ?  448 LYS B CE    1 
ATOM   9666  N  NZ    . LYS B 1 429 ? 194.962 203.220 209.649 1.00 38.75  1  448 LYS B NZ    1 
ATOM   9667  N  N     . LEU B 1 430 ? 190.630 198.235 206.703 1.00 35.32  ?  449 LEU B N     1 
ATOM   9668  C  CA    . LEU B 1 430 ? 189.241 197.830 206.535 1.00 32.09  ?  449 LEU B CA    1 
ATOM   9669  C  C     . LEU B 1 430 ? 188.752 197.010 207.728 1.00 38.88  ?  449 LEU B C     1 
ATOM   9670  O  O     . LEU B 1 430 ? 189.519 196.298 208.382 1.00 42.89  ?  449 LEU B O     1 
ATOM   9671  C  CB    . LEU B 1 430 ? 189.097 197.051 205.220 1.00 36.89  ?  449 LEU B CB    1 
ATOM   9672  C  CG    . LEU B 1 430 ? 187.740 196.623 204.658 1.00 35.38  ?  449 LEU B CG    1 
ATOM   9673  C  CD1   . LEU B 1 430 ? 187.821 196.501 203.146 1.00 37.96  ?  449 LEU B CD1   1 
ATOM   9674  C  CD2   . LEU B 1 430 ? 187.327 195.277 205.237 1.00 39.59  ?  449 LEU B CD2   1 
ATOM   9675  N  N     . LYS B 1 431 ? 187.442 197.123 208.010 1.00 43.95  ?  450 LYS B N     1 
ATOM   9676  C  CA    . LYS B 1 431 ? 186.787 196.458 209.128 1.00 42.30  ?  450 LYS B CA    1 
ATOM   9677  C  C     . LYS B 1 431 ? 185.807 195.401 208.625 1.00 45.25  ?  450 LYS B C     1 
ATOM   9678  O  O     . LYS B 1 431 ? 185.267 195.525 207.521 1.00 47.07  ?  450 LYS B O     1 
ATOM   9679  C  CB    . LYS B 1 431 ? 186.037 197.463 210.012 1.00 41.00  ?  450 LYS B CB    1 
ATOM   9680  C  CG    . LYS B 1 431 ? 186.928 198.287 210.931 1.00 46.29  ?  450 LYS B CG    1 
ATOM   9681  C  CD    . LYS B 1 431 ? 186.089 199.210 211.804 1.00 48.25  ?  450 LYS B CD    1 
ATOM   9682  C  CE    . LYS B 1 431 ? 186.954 200.133 212.651 1.00 47.31  ?  450 LYS B CE    1 
ATOM   9683  N  NZ    . LYS B 1 431 ? 188.100 200.691 211.885 1.00 44.93  1  450 LYS B NZ    1 
ATOM   9684  N  N     . PRO B 1 432 ? 185.550 194.355 209.418 1.00 50.10  ?  451 PRO B N     1 
ATOM   9685  C  CA    . PRO B 1 432 ? 184.714 193.246 208.919 1.00 48.11  ?  451 PRO B CA    1 
ATOM   9686  C  C     . PRO B 1 432 ? 183.328 193.667 208.457 1.00 43.11  ?  451 PRO B C     1 
ATOM   9687  O  O     . PRO B 1 432 ? 182.816 193.109 207.478 1.00 42.81  ?  451 PRO B O     1 
ATOM   9688  C  CB    . PRO B 1 432 ? 184.650 192.298 210.126 1.00 41.02  ?  451 PRO B CB    1 
ATOM   9689  C  CG    . PRO B 1 432 ? 185.876 192.616 210.920 1.00 41.05  ?  451 PRO B CG    1 
ATOM   9690  C  CD    . PRO B 1 432 ? 186.093 194.083 210.760 1.00 45.81  ?  451 PRO B CD    1 
ATOM   9691  N  N     . ASP B 1 433 ? 182.703 194.638 209.126 1.00 36.82  ?  452 ASP B N     1 
ATOM   9692  C  CA    . ASP B 1 433 ? 181.367 195.061 208.719 1.00 37.97  ?  452 ASP B CA    1 
ATOM   9693  C  C     . ASP B 1 433 ? 181.404 195.917 207.460 1.00 45.61  ?  452 ASP B C     1 
ATOM   9694  O  O     . ASP B 1 433 ? 180.447 195.906 206.677 1.00 42.89  ?  452 ASP B O     1 
ATOM   9695  C  CB    . ASP B 1 433 ? 180.686 195.823 209.856 1.00 46.84  ?  452 ASP B CB    1 
ATOM   9696  C  CG    . ASP B 1 433 ? 179.216 196.079 209.588 1.00 51.60  ?  452 ASP B CG    1 
ATOM   9697  O  OD1   . ASP B 1 433 ? 178.898 197.012 208.821 1.00 52.47  ?  452 ASP B OD1   1 
ATOM   9698  O  OD2   . ASP B 1 433 ? 178.377 195.344 210.149 1.00 48.87  -1 452 ASP B OD2   1 
ATOM   9699  N  N     . GLN B 1 434 ? 182.485 196.663 207.254 1.00 45.00  ?  453 GLN B N     1 
ATOM   9700  C  CA    . GLN B 1 434 ? 182.585 197.566 206.117 1.00 34.84  ?  453 GLN B CA    1 
ATOM   9701  C  C     . GLN B 1 434 ? 182.741 196.789 204.815 1.00 30.03  ?  453 GLN B C     1 
ATOM   9702  O  O     . GLN B 1 434 ? 183.259 195.669 204.788 1.00 30.07  ?  453 GLN B O     1 
ATOM   9703  C  CB    . GLN B 1 434 ? 183.767 198.513 206.305 1.00 30.97  ?  453 GLN B CB    1 
ATOM   9704  C  CG    . GLN B 1 434 ? 183.753 199.230 207.640 1.00 25.84  ?  453 GLN B CG    1 
ATOM   9705  C  CD    . GLN B 1 434 ? 184.698 200.408 207.679 1.00 37.59  ?  453 GLN B CD    1 
ATOM   9706  O  OE1   . GLN B 1 434 ? 185.681 200.457 206.940 1.00 44.79  ?  453 GLN B OE1   1 
ATOM   9707  N  NE2   . GLN B 1 434 ? 184.409 201.368 208.549 1.00 44.08  ?  453 GLN B NE2   1 
ATOM   9708  N  N     . TYR B 1 435 ? 182.291 197.402 203.723 1.00 20.27  ?  454 TYR B N     1 
ATOM   9709  C  CA    . TYR B 1 435 ? 182.380 196.806 202.397 1.00 16.79  ?  454 TYR B CA    1 
ATOM   9710  C  C     . TYR B 1 435 ? 183.057 197.798 201.463 1.00 22.65  ?  454 TYR B C     1 
ATOM   9711  O  O     . TYR B 1 435 ? 182.671 198.969 201.417 1.00 33.78  ?  454 TYR B O     1 
ATOM   9712  C  CB    . TYR B 1 435 ? 180.987 196.415 201.882 1.00 26.71  ?  454 TYR B CB    1 
ATOM   9713  C  CG    . TYR B 1 435 ? 180.883 196.221 200.385 1.00 26.59  ?  454 TYR B CG    1 
ATOM   9714  C  CD1   . TYR B 1 435 ? 181.089 194.975 199.810 1.00 20.67  ?  454 TYR B CD1   1 
ATOM   9715  C  CD2   . TYR B 1 435 ? 180.537 197.276 199.550 1.00 32.65  ?  454 TYR B CD2   1 
ATOM   9716  C  CE1   . TYR B 1 435 ? 180.985 194.793 198.445 1.00 23.80  ?  454 TYR B CE1   1 
ATOM   9717  C  CE2   . TYR B 1 435 ? 180.431 197.103 198.186 1.00 32.60  ?  454 TYR B CE2   1 
ATOM   9718  C  CZ    . TYR B 1 435 ? 180.654 195.859 197.639 1.00 27.51  ?  454 TYR B CZ    1 
ATOM   9719  O  OH    . TYR B 1 435 ? 180.545 195.682 196.280 1.00 32.49  ?  454 TYR B OH    1 
ATOM   9720  N  N     . LEU B 1 436 ? 184.064 197.335 200.727 1.00 27.18  ?  455 LEU B N     1 
ATOM   9721  C  CA    . LEU B 1 436 ? 184.874 198.194 199.875 1.00 20.43  ?  455 LEU B CA    1 
ATOM   9722  C  C     . LEU B 1 436 ? 184.622 197.877 198.407 1.00 9.61   ?  455 LEU B C     1 
ATOM   9723  O  O     . LEU B 1 436 ? 184.518 196.709 198.022 1.00 26.79  ?  455 LEU B O     1 
ATOM   9724  C  CB    . LEU B 1 436 ? 186.363 198.040 200.198 1.00 27.49  ?  455 LEU B CB    1 
ATOM   9725  C  CG    . LEU B 1 436 ? 187.317 198.994 199.476 1.00 32.06  ?  455 LEU B CG    1 
ATOM   9726  C  CD1   . LEU B 1 436 ? 186.973 200.438 199.793 1.00 20.41  ?  455 LEU B CD1   1 
ATOM   9727  C  CD2   . LEU B 1 436 ? 188.759 198.692 199.850 1.00 31.79  ?  455 LEU B CD2   1 
ATOM   9728  N  N     . CYS B 1 437 ? 184.524 198.927 197.592 1.00 3.44   ?  456 CYS B N     1 
ATOM   9729  C  CA    . CYS B 1 437 ? 184.255 198.786 196.170 1.00 14.38  ?  456 CYS B CA    1 
ATOM   9730  C  C     . CYS B 1 437 ? 184.999 199.876 195.413 1.00 31.13  ?  456 CYS B C     1 
ATOM   9731  O  O     . CYS B 1 437 ? 185.352 200.915 195.974 1.00 49.38  ?  456 CYS B O     1 
ATOM   9732  C  CB    . CYS B 1 437 ? 182.753 198.863 195.880 1.00 25.34  ?  456 CYS B CB    1 
ATOM   9733  S  SG    . CYS B 1 437 ? 182.342 199.100 194.142 1.00 57.08  ?  456 CYS B SG    1 
ATOM   9734  N  N     . ARG B 1 438 ? 185.216 199.637 194.124 1.00 22.72  ?  457 ARG B N     1 
ATOM   9735  C  CA    . ARG B 1 438 ? 185.878 200.591 193.237 1.00 22.69  ?  457 ARG B CA    1 
ATOM   9736  C  C     . ARG B 1 438 ? 184.928 200.869 192.077 1.00 28.40  ?  457 ARG B C     1 
ATOM   9737  O  O     . ARG B 1 438 ? 184.818 200.062 191.149 1.00 40.35  ?  457 ARG B O     1 
ATOM   9738  C  CB    . ARG B 1 438 ? 187.220 200.049 192.752 1.00 21.72  ?  457 ARG B CB    1 
ATOM   9739  C  CG    . ARG B 1 438 ? 187.894 200.884 191.671 1.00 26.80  ?  457 ARG B CG    1 
ATOM   9740  C  CD    . ARG B 1 438 ? 189.397 200.649 191.672 1.00 29.77  ?  457 ARG B CD    1 
ATOM   9741  N  NE    . ARG B 1 438 ? 190.102 201.503 190.724 1.00 36.25  ?  457 ARG B NE    1 
ATOM   9742  C  CZ    . ARG B 1 438 ? 190.238 201.237 189.432 1.00 32.98  ?  457 ARG B CZ    1 
ATOM   9743  N  NH1   . ARG B 1 438 ? 189.726 200.143 188.893 1.00 34.01  1  457 ARG B NH1   1 
ATOM   9744  N  NH2   . ARG B 1 438 ? 190.914 202.086 188.662 1.00 25.61  ?  457 ARG B NH2   1 
ATOM   9745  N  N     . ILE B 1 439 ? 184.229 202.004 192.136 1.00 20.83  ?  458 ILE B N     1 
ATOM   9746  C  CA    . ILE B 1 439 ? 183.234 202.309 191.111 1.00 33.07  ?  458 ILE B CA    1 
ATOM   9747  C  C     . ILE B 1 439 ? 183.912 202.631 189.782 1.00 36.90  ?  458 ILE B C     1 
ATOM   9748  O  O     . ILE B 1 439 ? 183.567 202.059 188.742 1.00 46.81  ?  458 ILE B O     1 
ATOM   9749  C  CB    . ILE B 1 439 ? 182.299 203.440 191.584 1.00 31.35  ?  458 ILE B CB    1 
ATOM   9750  C  CG1   . ILE B 1 439 ? 183.079 204.695 191.977 1.00 40.64  ?  458 ILE B CG1   1 
ATOM   9751  C  CG2   . ILE B 1 439 ? 181.451 202.971 192.751 1.00 31.24  ?  458 ILE B CG2   1 
ATOM   9752  C  CD1   . ILE B 1 439 ? 182.274 205.968 191.851 1.00 40.46  ?  458 ILE B CD1   1 
ATOM   9753  N  N     . GLU B 1 440 ? 184.901 203.528 189.798 1.00 30.98  ?  459 GLU B N     1 
ATOM   9754  C  CA    . GLU B 1 440 ? 185.680 203.831 188.602 1.00 34.30  ?  459 GLU B CA    1 
ATOM   9755  C  C     . GLU B 1 440 ? 186.923 204.651 188.931 1.00 35.68  ?  459 GLU B C     1 
ATOM   9756  O  O     . GLU B 1 440 ? 186.836 205.687 189.599 1.00 41.53  ?  459 GLU B O     1 
ATOM   9757  C  CB    . GLU B 1 440 ? 184.817 204.563 187.564 1.00 34.56  ?  459 GLU B CB    1 
ATOM   9758  C  CG    . GLU B 1 440 ? 184.203 205.878 188.030 1.00 35.46  ?  459 GLU B CG    1 
ATOM   9759  C  CD    . GLU B 1 440 ? 185.026 207.086 187.617 1.00 43.74  ?  459 GLU B CD    1 
ATOM   9760  O  OE1   . GLU B 1 440 ? 185.846 206.957 186.685 1.00 42.10  ?  459 GLU B OE1   1 
ATOM   9761  O  OE2   . GLU B 1 440 ? 184.852 208.164 188.223 1.00 41.88  -1 459 GLU B OE2   1 
ATOM   9762  N  N     . GLY B 1 441 ? 188.083 204.177 188.478 1.00 28.87  ?  460 GLY B N     1 
ATOM   9763  C  CA    . GLY B 1 441 ? 189.312 204.951 188.486 1.00 30.03  ?  460 GLY B CA    1 
ATOM   9764  C  C     . GLY B 1 441 ? 189.669 205.642 189.786 1.00 32.75  ?  460 GLY B C     1 
ATOM   9765  O  O     . GLY B 1 441 ? 189.993 205.000 190.789 1.00 38.29  ?  460 GLY B O     1 
ATOM   9766  N  N     . THR B 1 442 ? 189.602 206.974 189.758 1.00 30.31  ?  461 THR B N     1 
ATOM   9767  C  CA    . THR B 1 442 ? 189.989 207.807 190.891 1.00 36.14  ?  461 THR B CA    1 
ATOM   9768  C  C     . THR B 1 442 ? 189.121 207.558 192.122 1.00 37.05  ?  461 THR B C     1 
ATOM   9769  O  O     . THR B 1 442 ? 189.523 207.914 193.237 1.00 35.02  ?  461 THR B O     1 
ATOM   9770  C  CB    . THR B 1 442 ? 189.914 209.280 190.459 1.00 46.11  ?  461 THR B CB    1 
ATOM   9771  O  OG1   . THR B 1 442 ? 190.774 209.489 189.331 1.00 46.35  ?  461 THR B OG1   1 
ATOM   9772  C  CG2   . THR B 1 442 ? 190.335 210.225 191.570 1.00 38.97  ?  461 THR B CG2   1 
ATOM   9773  N  N     . GLN B 1 443 ? 187.958 206.932 191.951 1.00 30.75  ?  462 GLN B N     1 
ATOM   9774  C  CA    . GLN B 1 443 ? 186.937 206.879 192.984 1.00 21.81  ?  462 GLN B CA    1 
ATOM   9775  C  C     . GLN B 1 443 ? 186.751 205.470 193.535 1.00 28.91  ?  462 GLN B C     1 
ATOM   9776  O  O     . GLN B 1 443 ? 186.908 204.472 192.826 1.00 46.30  ?  462 GLN B O     1 
ATOM   9777  C  CB    . GLN B 1 443 ? 185.602 207.399 192.444 1.00 22.81  ?  462 GLN B CB    1 
ATOM   9778  C  CG    . GLN B 1 443 ? 185.554 208.909 192.309 1.00 32.97  ?  462 GLN B CG    1 
ATOM   9779  C  CD    . GLN B 1 443 ? 184.683 209.364 191.156 1.00 44.07  ?  462 GLN B CD    1 
ATOM   9780  O  OE1   . GLN B 1 443 ? 183.740 208.677 190.767 1.00 44.13  ?  462 GLN B OE1   1 
ATOM   9781  N  NE2   . GLN B 1 443 ? 184.994 210.531 190.605 1.00 42.09  ?  462 GLN B NE2   1 
ATOM   9782  N  N     . PHE B 1 444 ? 186.410 205.416 194.821 1.00 23.31  ?  463 PHE B N     1 
ATOM   9783  C  CA    . PHE B 1 444 ? 186.093 204.190 195.540 1.00 16.06  ?  463 PHE B CA    1 
ATOM   9784  C  C     . PHE B 1 444 ? 184.907 204.470 196.449 1.00 26.45  ?  463 PHE B C     1 
ATOM   9785  O  O     . PHE B 1 444 ? 184.595 205.621 196.750 1.00 34.54  ?  463 PHE B O     1 
ATOM   9786  C  CB    . PHE B 1 444 ? 187.274 203.679 196.378 1.00 12.61  ?  463 PHE B CB    1 
ATOM   9787  C  CG    . PHE B 1 444 ? 188.589 203.700 195.658 1.00 21.14  ?  463 PHE B CG    1 
ATOM   9788  C  CD1   . PHE B 1 444 ? 189.342 204.860 195.594 1.00 28.34  ?  463 PHE B CD1   1 
ATOM   9789  C  CD2   . PHE B 1 444 ? 189.077 202.557 195.052 1.00 26.52  ?  463 PHE B CD2   1 
ATOM   9790  C  CE1   . PHE B 1 444 ? 190.551 204.880 194.932 1.00 27.06  ?  463 PHE B CE1   1 
ATOM   9791  C  CE2   . PHE B 1 444 ? 190.287 202.571 194.392 1.00 28.86  ?  463 PHE B CE2   1 
ATOM   9792  C  CZ    . PHE B 1 444 ? 191.026 203.734 194.330 1.00 26.16  ?  463 PHE B CZ    1 
ATOM   9793  N  N     . VAL B 1 445 ? 184.234 203.411 196.884 1.00 29.61  ?  464 VAL B N     1 
ATOM   9794  C  CA    . VAL B 1 445 ? 183.071 203.543 197.752 1.00 24.65  ?  464 VAL B CA    1 
ATOM   9795  C  C     . VAL B 1 445 ? 183.208 202.579 198.920 1.00 27.90  ?  464 VAL B C     1 
ATOM   9796  O  O     . VAL B 1 445 ? 183.468 201.387 198.725 1.00 38.50  ?  464 VAL B O     1 
ATOM   9797  C  CB    . VAL B 1 445 ? 181.753 203.290 196.996 1.00 19.53  ?  464 VAL B CB    1 
ATOM   9798  C  CG1   . VAL B 1 445 ? 180.633 202.970 197.977 1.00 23.43  ?  464 VAL B CG1   1 
ATOM   9799  C  CG2   . VAL B 1 445 ? 181.394 204.493 196.144 1.00 30.18  ?  464 VAL B CG2   1 
ATOM   9800  N  N     . LEU B 1 446 ? 183.029 203.096 200.131 1.00 30.17  ?  465 LEU B N     1 
ATOM   9801  C  CA    . LEU B 1 446 ? 182.976 202.280 201.335 1.00 23.01  ?  465 LEU B CA    1 
ATOM   9802  C  C     . LEU B 1 446 ? 181.568 202.341 201.913 1.00 29.69  ?  465 LEU B C     1 
ATOM   9803  O  O     . LEU B 1 446 ? 181.016 203.429 202.108 1.00 42.62  ?  465 LEU B O     1 
ATOM   9804  C  CB    . LEU B 1 446 ? 184.005 202.745 202.367 1.00 22.92  ?  465 LEU B CB    1 
ATOM   9805  C  CG    . LEU B 1 446 ? 184.163 201.847 203.597 1.00 22.41  ?  465 LEU B CG    1 
ATOM   9806  C  CD1   . LEU B 1 446 ? 185.634 201.636 203.914 1.00 31.27  ?  465 LEU B CD1   1 
ATOM   9807  C  CD2   . LEU B 1 446 ? 183.436 202.421 204.797 1.00 27.42  ?  465 LEU B CD2   1 
ATOM   9808  N  N     . VAL B 1 447 ? 180.995 201.174 202.187 1.00 27.95  ?  466 VAL B N     1 
ATOM   9809  C  CA    . VAL B 1 447 ? 179.631 201.050 202.684 1.00 22.39  ?  466 VAL B CA    1 
ATOM   9810  C  C     . VAL B 1 447 ? 179.695 200.521 204.108 1.00 26.86  ?  466 VAL B C     1 
ATOM   9811  O  O     . VAL B 1 447 ? 180.343 199.499 204.369 1.00 43.45  ?  466 VAL B O     1 
ATOM   9812  C  CB    . VAL B 1 447 ? 178.789 200.126 201.788 1.00 27.03  ?  466 VAL B CB    1 
ATOM   9813  C  CG1   . VAL B 1 447 ? 177.452 199.814 202.442 1.00 28.86  ?  466 VAL B CG1   1 
ATOM   9814  C  CG2   . VAL B 1 447 ? 178.583 200.759 200.423 1.00 34.63  ?  466 VAL B CG2   1 
ATOM   9815  N  N     . SER B 1 448 ? 179.034 201.222 205.027 1.00 29.37  ?  467 SER B N     1 
ATOM   9816  C  CA    . SER B 1 448 ? 179.023 200.841 206.430 1.00 33.43  ?  467 SER B CA    1 
ATOM   9817  C  C     . SER B 1 448 ? 177.588 200.798 206.936 1.00 45.29  ?  467 SER B C     1 
ATOM   9818  O  O     . SER B 1 448 ? 176.661 201.287 206.286 1.00 52.04  ?  467 SER B O     1 
ATOM   9819  C  CB    . SER B 1 448 ? 179.856 201.809 207.281 1.00 44.02  ?  467 SER B CB    1 
ATOM   9820  O  OG    . SER B 1 448 ? 179.515 203.157 207.006 1.00 49.97  ?  467 SER B OG    1 
ATOM   9821  N  N     . LEU B 1 449 ? 177.416 200.197 208.112 1.00 54.37  ?  468 LEU B N     1 
ATOM   9822  C  CA    . LEU B 1 449 ? 176.105 200.100 208.741 1.00 52.83  ?  468 LEU B CA    1 
ATOM   9823  C  C     . LEU B 1 449 ? 175.949 201.015 209.947 1.00 53.33  ?  468 LEU B C     1 
ATOM   9824  O  O     . LEU B 1 449 ? 174.820 201.389 210.281 1.00 56.90  ?  468 LEU B O     1 
ATOM   9825  C  CB    . LEU B 1 449 ? 175.823 198.654 209.164 1.00 50.06  ?  468 LEU B CB    1 
ATOM   9826  C  CG    . LEU B 1 449 ? 175.463 197.696 208.027 1.00 51.97  ?  468 LEU B CG    1 
ATOM   9827  C  CD1   . LEU B 1 449 ? 175.342 196.267 208.539 1.00 54.00  ?  468 LEU B CD1   1 
ATOM   9828  C  CD2   . LEU B 1 449 ? 174.183 198.141 207.338 1.00 52.26  ?  468 LEU B CD2   1 
ATOM   9829  N  N     . GLU B 1 450 ? 177.046 201.379 210.608 1.00 55.75  ?  469 GLU B N     1 
ATOM   9830  C  CA    . GLU B 1 450 ? 176.970 202.321 211.717 1.00 59.94  ?  469 GLU B CA    1 
ATOM   9831  C  C     . GLU B 1 450 ? 176.507 203.679 211.209 1.00 63.63  ?  469 GLU B C     1 
ATOM   9832  O  O     . GLU B 1 450 ? 177.052 204.210 210.238 1.00 68.70  ?  469 GLU B O     1 
ATOM   9833  C  CB    . GLU B 1 450 ? 178.332 202.446 212.399 1.00 58.45  ?  469 GLU B CB    1 
ATOM   9834  C  CG    . GLU B 1 450 ? 178.760 201.213 213.177 1.00 62.56  ?  469 GLU B CG    1 
ATOM   9835  C  CD    . GLU B 1 450 ? 179.475 200.196 212.307 1.00 64.65  ?  469 GLU B CD    1 
ATOM   9836  O  OE1   . GLU B 1 450 ? 179.752 200.511 211.130 1.00 63.65  ?  469 GLU B OE1   1 
ATOM   9837  O  OE2   . GLU B 1 450 ? 179.763 199.086 212.800 1.00 61.01  -1 469 GLU B OE2   1 
ATOM   9838  N  N     . ASN B 1 451 ? 175.493 204.243 211.866 1.00 62.55  ?  470 ASN B N     1 
ATOM   9839  C  CA    . ASN B 1 451 ? 174.892 205.511 211.448 1.00 59.11  ?  470 ASN B CA    1 
ATOM   9840  C  C     . ASN B 1 451 ? 174.779 206.447 212.650 1.00 60.50  ?  470 ASN B C     1 
ATOM   9841  O  O     . ASN B 1 451 ? 173.735 206.511 213.305 1.00 61.70  ?  470 ASN B O     1 
ATOM   9842  C  CB    . ASN B 1 451 ? 173.536 205.268 210.790 1.00 53.55  ?  470 ASN B CB    1 
ATOM   9843  C  CG    . ASN B 1 451 ? 172.681 204.283 211.561 1.00 63.18  ?  470 ASN B CG    1 
ATOM   9844  O  OD1   . ASN B 1 451 ? 173.067 203.814 212.631 1.00 67.94  ?  470 ASN B OD1   1 
ATOM   9845  N  ND2   . ASN B 1 451 ? 171.508 203.968 211.023 1.00 64.78  ?  470 ASN B ND2   1 
ATOM   9846  N  N     . ASP B 1 452 ? 175.857 207.178 212.924 1.00 60.92  ?  471 ASP B N     1 
ATOM   9847  C  CA    . ASP B 1 452 ? 175.860 208.247 213.912 1.00 62.05  ?  471 ASP B CA    1 
ATOM   9848  C  C     . ASP B 1 452 ? 177.114 209.091 213.721 1.00 63.76  ?  471 ASP B C     1 
ATOM   9849  O  O     . ASP B 1 452 ? 178.178 208.567 213.381 1.00 67.84  ?  471 ASP B O     1 
ATOM   9850  C  CB    . ASP B 1 452 ? 175.745 207.709 215.351 1.00 66.39  ?  471 ASP B CB    1 
ATOM   9851  C  CG    . ASP B 1 452 ? 176.882 206.778 215.740 1.00 71.42  ?  471 ASP B CG    1 
ATOM   9852  O  OD1   . ASP B 1 452 ? 177.746 206.475 214.897 1.00 69.87  ?  471 ASP B OD1   1 
ATOM   9853  O  OD2   . ASP B 1 452 ? 176.909 206.345 216.911 1.00 70.02  -1 471 ASP B OD2   1 
ATOM   9854  N  N     . VAL B 1 453 ? 176.972 210.400 213.947 1.00 55.47  ?  472 VAL B N     1 
ATOM   9855  C  CA    . VAL B 1 453 ? 177.994 211.358 213.531 1.00 55.81  ?  472 VAL B CA    1 
ATOM   9856  C  C     . VAL B 1 453 ? 179.333 211.049 214.191 1.00 55.50  ?  472 VAL B C     1 
ATOM   9857  O  O     . VAL B 1 453 ? 180.391 211.148 213.555 1.00 57.43  ?  472 VAL B O     1 
ATOM   9858  C  CB    . VAL B 1 453 ? 177.527 212.795 213.836 1.00 56.72  ?  472 VAL B CB    1 
ATOM   9859  C  CG1   . VAL B 1 453 ? 178.670 213.783 213.663 1.00 55.92  ?  472 VAL B CG1   1 
ATOM   9860  C  CG2   . VAL B 1 453 ? 176.350 213.169 212.946 1.00 55.45  ?  472 VAL B CG2   1 
ATOM   9861  N  N     . SER B 1 454 ? 179.310 210.655 215.467 1.00 54.54  ?  473 SER B N     1 
ATOM   9862  C  CA    . SER B 1 454 ? 180.553 210.405 216.191 1.00 55.07  ?  473 SER B CA    1 
ATOM   9863  C  C     . SER B 1 454 ? 181.386 209.308 215.537 1.00 54.24  ?  473 SER B C     1 
ATOM   9864  O  O     . SER B 1 454 ? 182.618 209.324 215.638 1.00 57.18  ?  473 SER B O     1 
ATOM   9865  C  CB    . SER B 1 454 ? 180.250 210.045 217.646 1.00 62.15  ?  473 SER B CB    1 
ATOM   9866  O  OG    . SER B 1 454 ? 179.494 208.850 217.729 1.00 60.40  ?  473 SER B OG    1 
ATOM   9867  N  N     . ASN B 1 455 ? 180.742 208.355 214.863 1.00 52.69  ?  474 ASN B N     1 
ATOM   9868  C  CA    . ASN B 1 455 ? 181.476 207.305 214.166 1.00 53.84  ?  474 ASN B CA    1 
ATOM   9869  C  C     . ASN B 1 455 ? 181.720 207.638 212.699 1.00 53.66  ?  474 ASN B C     1 
ATOM   9870  O  O     . ASN B 1 455 ? 182.772 207.280 212.157 1.00 58.83  ?  474 ASN B O     1 
ATOM   9871  C  CB    . ASN B 1 455 ? 180.733 205.971 214.274 1.00 56.14  ?  474 ASN B CB    1 
ATOM   9872  C  CG    . ASN B 1 455 ? 180.945 205.294 215.612 1.00 58.27  ?  474 ASN B CG    1 
ATOM   9873  O  OD1   . ASN B 1 455 ? 180.167 205.481 216.548 1.00 56.49  ?  474 ASN B OD1   1 
ATOM   9874  N  ND2   . ASN B 1 455 ? 182.002 204.496 215.710 1.00 56.83  ?  474 ASN B ND2   1 
ATOM   9875  N  N     . ILE B 1 456 ? 180.765 208.303 212.040 1.00 41.88  ?  475 ILE B N     1 
ATOM   9876  C  CA    . ILE B 1 456 ? 180.955 208.669 210.637 1.00 34.59  ?  475 ILE B CA    1 
ATOM   9877  C  C     . ILE B 1 456 ? 182.151 209.601 210.492 1.00 37.13  ?  475 ILE B C     1 
ATOM   9878  O  O     . ILE B 1 456 ? 182.999 209.422 209.609 1.00 40.40  ?  475 ILE B O     1 
ATOM   9879  C  CB    . ILE B 1 456 ? 179.679 209.305 210.055 1.00 34.30  ?  475 ILE B CB    1 
ATOM   9880  C  CG1   . ILE B 1 456 ? 178.439 208.479 210.396 1.00 39.28  ?  475 ILE B CG1   1 
ATOM   9881  C  CG2   . ILE B 1 456 ? 179.810 209.456 208.550 1.00 41.77  ?  475 ILE B CG2   1 
ATOM   9882  C  CD1   . ILE B 1 456 ? 178.470 207.069 209.882 1.00 42.95  ?  475 ILE B CD1   1 
ATOM   9883  N  N     . THR B 1 457 ? 182.239 210.612 211.362 1.00 39.83  ?  476 THR B N     1 
ATOM   9884  C  CA    . THR B 1 457 ? 183.371 211.530 211.313 1.00 37.35  ?  476 THR B CA    1 
ATOM   9885  C  C     . THR B 1 457 ? 184.681 210.804 211.584 1.00 44.32  ?  476 THR B C     1 
ATOM   9886  O  O     . THR B 1 457 ? 185.693 211.073 210.929 1.00 51.23  ?  476 THR B O     1 
ATOM   9887  C  CB    . THR B 1 457 ? 183.171 212.666 212.317 1.00 39.11  ?  476 THR B CB    1 
ATOM   9888  O  OG1   . THR B 1 457 ? 181.912 213.306 212.074 1.00 44.40  ?  476 THR B OG1   1 
ATOM   9889  C  CG2   . THR B 1 457 ? 184.289 213.693 212.197 1.00 42.80  ?  476 THR B CG2   1 
ATOM   9890  N  N     . GLN B 1 458 ? 184.682 209.877 212.545 1.00 43.59  ?  477 GLN B N     1 
ATOM   9891  C  CA    . GLN B 1 458 ? 185.904 209.154 212.882 1.00 42.53  ?  477 GLN B CA    1 
ATOM   9892  C  C     . GLN B 1 458 ? 186.388 208.302 211.713 1.00 46.43  ?  477 GLN B C     1 
ATOM   9893  O  O     . GLN B 1 458 ? 187.580 208.299 211.384 1.00 54.38  ?  477 GLN B O     1 
ATOM   9894  C  CB    . GLN B 1 458 ? 185.670 208.290 214.121 1.00 44.05  ?  477 GLN B CB    1 
ATOM   9895  C  CG    . GLN B 1 458 ? 186.798 207.321 214.431 1.00 51.00  ?  477 GLN B CG    1 
ATOM   9896  C  CD    . GLN B 1 458 ? 186.511 206.465 215.649 1.00 52.16  ?  477 GLN B CD    1 
ATOM   9897  O  OE1   . GLN B 1 458 ? 185.427 206.535 216.229 1.00 48.02  ?  477 GLN B OE1   1 
ATOM   9898  N  NE2   . GLN B 1 458 ? 187.481 205.646 216.040 1.00 50.12  ?  477 GLN B NE2   1 
ATOM   9899  N  N     . ILE B 1 459 ? 185.476 207.568 211.071 1.00 37.10  ?  478 ILE B N     1 
ATOM   9900  C  CA    . ILE B 1 459 ? 185.902 206.716 209.964 1.00 37.01  ?  478 ILE B CA    1 
ATOM   9901  C  C     . ILE B 1 459 ? 186.305 207.558 208.758 1.00 46.36  ?  478 ILE B C     1 
ATOM   9902  O  O     . ILE B 1 459 ? 187.248 207.207 208.037 1.00 56.38  ?  478 ILE B O     1 
ATOM   9903  C  CB    . ILE B 1 459 ? 184.819 205.680 209.608 1.00 37.73  ?  478 ILE B CB    1 
ATOM   9904  C  CG1   . ILE B 1 459 ? 185.273 204.814 208.431 1.00 44.39  ?  478 ILE B CG1   1 
ATOM   9905  C  CG2   . ILE B 1 459 ? 183.512 206.354 209.277 1.00 41.14  ?  478 ILE B CG2   1 
ATOM   9906  C  CD1   . ILE B 1 459 ? 186.506 203.984 208.725 1.00 42.87  ?  478 ILE B CD1   1 
ATOM   9907  N  N     . ALA B 1 460 ? 185.620 208.682 208.518 1.00 37.89  ?  479 ALA B N     1 
ATOM   9908  C  CA    . ALA B 1 460 ? 186.041 209.577 207.445 1.00 35.52  ?  479 ALA B CA    1 
ATOM   9909  C  C     . ALA B 1 460 ? 187.429 210.140 207.717 1.00 33.65  ?  479 ALA B C     1 
ATOM   9910  O  O     . ALA B 1 460 ? 188.251 210.257 206.802 1.00 40.54  ?  479 ALA B O     1 
ATOM   9911  C  CB    . ALA B 1 460 ? 185.027 210.706 207.271 1.00 39.45  ?  479 ALA B CB    1 
ATOM   9912  N  N     . ASP B 1 461 ? 187.708 210.493 208.974 1.00 37.33  ?  480 ASP B N     1 
ATOM   9913  C  CA    . ASP B 1 461 ? 189.032 210.986 209.334 1.00 44.36  ?  480 ASP B CA    1 
ATOM   9914  C  C     . ASP B 1 461 ? 190.092 209.910 209.142 1.00 45.37  ?  480 ASP B C     1 
ATOM   9915  O  O     . ASP B 1 461 ? 191.198 210.201 208.677 1.00 47.96  ?  480 ASP B O     1 
ATOM   9916  C  CB    . ASP B 1 461 ? 189.030 211.486 210.779 1.00 44.34  ?  480 ASP B CB    1 
ATOM   9917  C  CG    . ASP B 1 461 ? 188.548 212.918 210.900 1.00 50.65  ?  480 ASP B CG    1 
ATOM   9918  O  OD1   . ASP B 1 461 ? 188.798 213.712 209.968 1.00 52.44  ?  480 ASP B OD1   1 
ATOM   9919  O  OD2   . ASP B 1 461 ? 187.918 213.251 211.925 1.00 50.24  -1 480 ASP B OD2   1 
ATOM   9920  N  N     . GLU B 1 462 ? 189.779 208.663 209.503 1.00 43.11  ?  481 GLU B N     1 
ATOM   9921  C  CA    . GLU B 1 462 ? 190.724 207.572 209.276 1.00 40.55  ?  481 GLU B CA    1 
ATOM   9922  C  C     . GLU B 1 462 ? 191.000 207.379 207.789 1.00 47.35  ?  481 GLU B C     1 
ATOM   9923  O  O     . GLU B 1 462 ? 192.156 207.203 207.378 1.00 53.46  ?  481 GLU B O     1 
ATOM   9924  C  CB    . GLU B 1 462 ? 190.190 206.277 209.890 1.00 41.17  ?  481 GLU B CB    1 
ATOM   9925  C  CG    . GLU B 1 462 ? 190.106 206.290 211.407 1.00 47.97  ?  481 GLU B CG    1 
ATOM   9926  C  CD    . GLU B 1 462 ? 191.468 206.348 212.067 1.00 55.22  ?  481 GLU B CD    1 
ATOM   9927  O  OE1   . GLU B 1 462 ? 192.427 205.777 211.508 1.00 53.46  ?  481 GLU B OE1   1 
ATOM   9928  O  OE2   . GLU B 1 462 ? 191.580 206.965 213.148 1.00 53.47  -1 481 GLU B OE2   1 
ATOM   9929  N  N     . LEU B 1 463 ? 189.947 207.406 206.968 1.00 43.50  ?  482 LEU B N     1 
ATOM   9930  C  CA    . LEU B 1 463 ? 190.125 207.259 205.527 1.00 39.01  ?  482 LEU B CA    1 
ATOM   9931  C  C     . LEU B 1 463 ? 190.963 208.397 204.957 1.00 42.90  ?  482 LEU B C     1 
ATOM   9932  O  O     . LEU B 1 463 ? 191.828 208.173 204.106 1.00 43.37  ?  482 LEU B O     1 
ATOM   9933  C  CB    . LEU B 1 463 ? 188.765 207.191 204.832 1.00 36.93  ?  482 LEU B CB    1 
ATOM   9934  C  CG    . LEU B 1 463 ? 188.112 205.809 204.742 1.00 40.69  ?  482 LEU B CG    1 
ATOM   9935  C  CD1   . LEU B 1 463 ? 186.948 205.829 203.766 1.00 40.66  ?  482 LEU B CD1   1 
ATOM   9936  C  CD2   . LEU B 1 463 ? 189.132 204.754 204.342 1.00 46.18  ?  482 LEU B CD2   1 
ATOM   9937  N  N     . ARG B 1 464 ? 190.717 209.625 205.414 1.00 46.80  ?  483 ARG B N     1 
ATOM   9938  C  CA    . ARG B 1 464 ? 191.495 210.766 204.941 1.00 47.32  ?  483 ARG B CA    1 
ATOM   9939  C  C     . ARG B 1 464 ? 192.941 210.709 205.422 1.00 42.57  ?  483 ARG B C     1 
ATOM   9940  O  O     . ARG B 1 464 ? 193.848 211.139 204.702 1.00 43.23  ?  483 ARG B O     1 
ATOM   9941  C  CB    . ARG B 1 464 ? 190.825 212.065 205.393 1.00 49.50  ?  483 ARG B CB    1 
ATOM   9942  C  CG    . ARG B 1 464 ? 191.500 213.335 204.912 1.00 50.08  ?  483 ARG B CG    1 
ATOM   9943  C  CD    . ARG B 1 464 ? 191.013 214.532 205.714 1.00 46.80  ?  483 ARG B CD    1 
ATOM   9944  N  NE    . ARG B 1 464 ? 191.783 215.737 205.436 1.00 52.36  ?  483 ARG B NE    1 
ATOM   9945  C  CZ    . ARG B 1 464 ? 192.977 215.999 205.949 1.00 51.64  ?  483 ARG B CZ    1 
ATOM   9946  N  NH1   . ARG B 1 464 ? 193.574 215.157 206.778 1.00 50.65  1  483 ARG B NH1   1 
ATOM   9947  N  NH2   . ARG B 1 464 ? 193.588 217.135 205.625 1.00 47.46  ?  483 ARG B NH2   1 
ATOM   9948  N  N     . ASN B 1 465 ? 193.175 210.185 206.623 1.00 37.48  ?  484 ASN B N     1 
ATOM   9949  C  CA    . ASN B 1 465 ? 194.498 210.156 207.228 1.00 46.06  ?  484 ASN B CA    1 
ATOM   9950  C  C     . ASN B 1 465 ? 195.337 208.962 206.794 1.00 48.12  ?  484 ASN B C     1 
ATOM   9951  O  O     . ASN B 1 465 ? 196.545 208.951 207.056 1.00 49.98  ?  484 ASN B O     1 
ATOM   9952  C  CB    . ASN B 1 465 ? 194.371 210.153 208.756 1.00 45.49  ?  484 ASN B CB    1 
ATOM   9953  C  CG    . ASN B 1 465 ? 195.617 210.666 209.446 1.00 50.39  ?  484 ASN B CG    1 
ATOM   9954  O  OD1   . ASN B 1 465 ? 196.474 211.288 208.821 1.00 50.85  ?  484 ASN B OD1   1 
ATOM   9955  N  ND2   . ASN B 1 465 ? 195.725 210.403 210.744 1.00 46.59  ?  484 ASN B ND2   1 
ATOM   9956  N  N     . VAL B 1 466 ? 194.733 207.958 206.151 1.00 47.36  ?  485 VAL B N     1 
ATOM   9957  C  CA    . VAL B 1 466 ? 195.519 206.812 205.696 1.00 44.46  ?  485 VAL B CA    1 
ATOM   9958  C  C     . VAL B 1 466 ? 196.576 207.239 204.683 1.00 42.63  ?  485 VAL B C     1 
ATOM   9959  O  O     . VAL B 1 466 ? 197.591 206.553 204.508 1.00 44.81  ?  485 VAL B O     1 
ATOM   9960  C  CB    . VAL B 1 466 ? 194.598 205.719 205.117 1.00 41.02  ?  485 VAL B CB    1 
ATOM   9961  C  CG1   . VAL B 1 466 ? 194.106 206.109 203.740 1.00 44.11  ?  485 VAL B CG1   1 
ATOM   9962  C  CG2   . VAL B 1 466 ? 195.323 204.387 205.064 1.00 40.59  ?  485 VAL B CG2   1 
ATOM   9963  N  N     . VAL B 1 467 ? 196.370 208.367 204.009 1.00 42.66  ?  486 VAL B N     1 
ATOM   9964  C  CA    . VAL B 1 467 ? 197.305 208.847 203.000 1.00 43.26  ?  486 VAL B CA    1 
ATOM   9965  C  C     . VAL B 1 467 ? 198.186 209.974 203.542 1.00 52.05  ?  486 VAL B C     1 
ATOM   9966  O  O     . VAL B 1 467 ? 198.715 210.769 202.767 1.00 52.47  ?  486 VAL B O     1 
ATOM   9967  C  CB    . VAL B 1 467 ? 196.578 209.287 201.720 1.00 41.07  ?  486 VAL B CB    1 
ATOM   9968  C  CG1   . VAL B 1 467 ? 196.073 208.077 200.949 1.00 46.10  ?  486 VAL B CG1   1 
ATOM   9969  C  CG2   . VAL B 1 467 ? 195.447 210.241 202.053 1.00 46.65  ?  486 VAL B CG2   1 
ATOM   9970  N  N     . SER B 1 468 ? 198.342 210.063 204.866 1.00 55.52  ?  487 SER B N     1 
ATOM   9971  C  CA    . SER B 1 468 ? 199.193 211.102 205.438 1.00 51.36  ?  487 SER B CA    1 
ATOM   9972  C  C     . SER B 1 468 ? 200.636 210.950 204.972 1.00 54.99  ?  487 SER B C     1 
ATOM   9973  O  O     . SER B 1 468 ? 201.291 211.939 204.624 1.00 54.30  ?  487 SER B O     1 
ATOM   9974  C  CB    . SER B 1 468 ? 199.116 211.063 206.964 1.00 52.16  ?  487 SER B CB    1 
ATOM   9975  O  OG    . SER B 1 468 ? 199.737 209.897 207.478 1.00 56.88  ?  487 SER B OG    1 
ATOM   9976  N  N     . LYS B 1 469 ? 201.143 209.726 204.956 1.00 56.41  ?  488 LYS B N     1 
ATOM   9977  C  CA    . LYS B 1 469 ? 202.488 209.476 204.455 1.00 51.07  ?  488 LYS B CA    1 
ATOM   9978  C  C     . LYS B 1 469 ? 202.468 209.420 202.932 1.00 46.07  ?  488 LYS B C     1 
ATOM   9979  O  O     . LYS B 1 469 ? 201.600 208.757 202.355 1.00 49.67  ?  488 LYS B O     1 
ATOM   9980  C  CB    . LYS B 1 469 ? 203.040 208.170 205.016 1.00 50.20  ?  488 LYS B CB    1 
ATOM   9981  C  CG    . LYS B 1 469 ? 202.847 208.003 206.511 1.00 52.98  ?  488 LYS B CG    1 
ATOM   9982  C  CD    . LYS B 1 469 ? 203.654 206.829 207.039 1.00 53.58  ?  488 LYS B CD    1 
ATOM   9983  C  CE    . LYS B 1 469 ? 203.253 205.532 206.356 1.00 55.16  ?  488 LYS B CE    1 
ATOM   9984  N  NZ    . LYS B 1 469 ? 201.782 205.302 206.414 1.00 56.16  1  488 LYS B NZ    1 
ATOM   9985  N  N     . PRO B 1 470 ? 203.388 210.103 202.252 1.00 52.67  ?  489 PRO B N     1 
ATOM   9986  C  CA    . PRO B 1 470 ? 203.416 210.034 200.788 1.00 57.42  ?  489 PRO B CA    1 
ATOM   9987  C  C     . PRO B 1 470 ? 203.735 208.626 200.310 1.00 56.01  ?  489 PRO B C     1 
ATOM   9988  O  O     . PRO B 1 470 ? 204.494 207.886 200.941 1.00 61.38  ?  489 PRO B O     1 
ATOM   9989  C  CB    . PRO B 1 470 ? 204.523 211.023 200.406 1.00 56.44  ?  489 PRO B CB    1 
ATOM   9990  C  CG    . PRO B 1 470 ? 205.402 211.084 201.610 1.00 57.60  ?  489 PRO B CG    1 
ATOM   9991  C  CD    . PRO B 1 470 ? 204.490 210.916 202.793 1.00 58.05  ?  489 PRO B CD    1 
ATOM   9992  N  N     . ILE B 1 471 ? 203.141 208.259 199.175 1.00 50.01  ?  490 ILE B N     1 
ATOM   9993  C  CA    . ILE B 1 471 ? 203.329 206.921 198.627 1.00 53.31  ?  490 ILE B CA    1 
ATOM   9994  C  C     . ILE B 1 471 ? 204.720 206.812 198.019 1.00 59.98  ?  490 ILE B C     1 
ATOM   9995  O  O     . ILE B 1 471 ? 205.112 207.624 197.170 1.00 61.28  ?  490 ILE B O     1 
ATOM   9996  C  CB    . ILE B 1 471 ? 202.233 206.595 197.600 1.00 50.38  ?  490 ILE B CB    1 
ATOM   9997  C  CG1   . ILE B 1 471 ? 200.858 206.540 198.276 1.00 52.89  ?  490 ILE B CG1   1 
ATOM   9998  C  CG2   . ILE B 1 471 ? 202.530 205.276 196.903 1.00 53.37  ?  490 ILE B CG2   1 
ATOM   9999  C  CD1   . ILE B 1 471 ? 200.118 207.858 198.326 1.00 54.16  ?  490 ILE B CD1   1 
ATOM   10000 N  N     . MET B 1 472 ? 205.471 205.803 198.453 1.00 68.03  ?  491 MET B N     1 
ATOM   10001 C  CA    . MET B 1 472 ? 206.858 205.618 198.034 1.00 62.67  ?  491 MET B CA    1 
ATOM   10002 C  C     . MET B 1 472 ? 206.873 204.876 196.705 1.00 63.22  ?  491 MET B C     1 
ATOM   10003 O  O     . MET B 1 472 ? 206.704 203.656 196.656 1.00 68.66  ?  491 MET B O     1 
ATOM   10004 C  CB    . MET B 1 472 ? 207.638 204.861 199.101 1.00 67.25  ?  491 MET B CB    1 
ATOM   10005 C  CG    . MET B 1 472 ? 209.147 204.950 198.953 1.00 72.58  ?  491 MET B CG    1 
ATOM   10006 S  SD    . MET B 1 472 ? 209.815 206.448 199.703 1.00 88.90  ?  491 MET B SD    1 
ATOM   10007 C  CE    . MET B 1 472 ? 211.558 206.043 199.779 1.00 72.37  ?  491 MET B CE    1 
ATOM   10008 N  N     . ILE B 1 473 ? 207.075 205.615 195.620 1.00 56.11  ?  492 ILE B N     1 
ATOM   10009 C  CA    . ILE B 1 473 ? 207.119 205.059 194.273 1.00 55.81  ?  492 ILE B CA    1 
ATOM   10010 C  C     . ILE B 1 473 ? 208.538 205.225 193.749 1.00 66.07  ?  492 ILE B C     1 
ATOM   10011 O  O     . ILE B 1 473 ? 208.988 206.352 193.505 1.00 70.12  ?  492 ILE B O     1 
ATOM   10012 C  CB    . ILE B 1 473 ? 206.102 205.736 193.345 1.00 54.86  ?  492 ILE B CB    1 
ATOM   10013 C  CG1   . ILE B 1 473 ? 204.679 205.509 193.859 1.00 58.20  ?  492 ILE B CG1   1 
ATOM   10014 C  CG2   . ILE B 1 473 ? 206.256 205.231 191.926 1.00 56.27  ?  492 ILE B CG2   1 
ATOM   10015 C  CD1   . ILE B 1 473 ? 204.279 204.053 193.913 1.00 58.88  ?  492 ILE B CD1   1 
ATOM   10016 N  N     . ASP B 1 474 ? 209.237 204.104 193.566 1.00 67.98  ?  493 ASP B N     1 
ATOM   10017 C  CA    . ASP B 1 474 ? 210.604 204.089 193.044 1.00 62.00  ?  493 ASP B CA    1 
ATOM   10018 C  C     . ASP B 1 474 ? 211.511 205.025 193.840 1.00 66.40  ?  493 ASP B C     1 
ATOM   10019 O  O     . ASP B 1 474 ? 212.237 205.852 193.285 1.00 67.30  ?  493 ASP B O     1 
ATOM   10020 C  CB    . ASP B 1 474 ? 210.624 204.438 191.554 1.00 62.03  ?  493 ASP B CB    1 
ATOM   10021 C  CG    . ASP B 1 474 ? 211.847 203.891 190.843 1.00 70.69  ?  493 ASP B CG    1 
ATOM   10022 O  OD1   . ASP B 1 474 ? 212.666 203.211 191.498 1.00 72.36  ?  493 ASP B OD1   1 
ATOM   10023 O  OD2   . ASP B 1 474 ? 211.989 204.137 189.627 1.00 73.14  -1 493 ASP B OD2   1 
ATOM   10024 N  N     . ASP B 1 475 ? 211.459 204.883 195.167 1.00 68.60  ?  494 ASP B N     1 
ATOM   10025 C  CA    . ASP B 1 475 ? 212.246 205.708 196.087 1.00 69.28  ?  494 ASP B CA    1 
ATOM   10026 C  C     . ASP B 1 475 ? 211.982 207.197 195.866 1.00 69.20  ?  494 ASP B C     1 
ATOM   10027 O  O     . ASP B 1 475 ? 212.899 208.020 195.885 1.00 69.63  ?  494 ASP B O     1 
ATOM   10028 C  CB    . ASP B 1 475 ? 213.741 205.398 195.967 1.00 69.60  ?  494 ASP B CB    1 
ATOM   10029 C  CG    . ASP B 1 475 ? 214.081 203.987 196.407 1.00 70.57  ?  494 ASP B CG    1 
ATOM   10030 O  OD1   . ASP B 1 475 ? 213.381 203.452 197.292 1.00 70.78  ?  494 ASP B OD1   1 
ATOM   10031 O  OD2   . ASP B 1 475 ? 215.048 203.411 195.865 1.00 70.61  -1 494 ASP B OD2   1 
ATOM   10032 N  N     . LYS B 1 476 ? 210.714 207.546 195.653 1.00 65.71  ?  495 LYS B N     1 
ATOM   10033 C  CA    . LYS B 1 476 ? 210.333 208.930 195.406 1.00 65.42  ?  495 LYS B CA    1 
ATOM   10034 C  C     . LYS B 1 476 ? 208.948 209.199 195.981 1.00 66.34  ?  495 LYS B C     1 
ATOM   10035 O  O     . LYS B 1 476 ? 207.975 208.537 195.597 1.00 65.73  ?  495 LYS B O     1 
ATOM   10036 C  CB    . LYS B 1 476 ? 210.362 209.235 193.907 1.00 64.51  ?  495 LYS B CB    1 
ATOM   10037 C  CG    . LYS B 1 476 ? 210.229 210.709 193.563 1.00 67.59  ?  495 LYS B CG    1 
ATOM   10038 C  CD    . LYS B 1 476 ? 210.320 210.929 192.062 1.00 67.85  ?  495 LYS B CD    1 
ATOM   10039 C  CE    . LYS B 1 476 ? 211.746 210.755 191.566 1.00 66.14  ?  495 LYS B CE    1 
ATOM   10040 N  NZ    . LYS B 1 476 ? 212.637 211.851 192.037 1.00 64.97  1  495 LYS B NZ    1 
ATOM   10041 N  N     . PRO B 1 477 ? 208.818 210.152 196.901 1.00 59.45  ?  496 PRO B N     1 
ATOM   10042 C  CA    . PRO B 1 477 ? 207.512 210.418 197.511 1.00 64.55  ?  496 PRO B CA    1 
ATOM   10043 C  C     . PRO B 1 477 ? 206.552 211.085 196.538 1.00 67.71  ?  496 PRO B C     1 
ATOM   10044 O  O     . PRO B 1 477 ? 206.946 211.777 195.596 1.00 65.32  ?  496 PRO B O     1 
ATOM   10045 C  CB    . PRO B 1 477 ? 207.854 211.348 198.678 1.00 63.39  ?  496 PRO B CB    1 
ATOM   10046 C  CG    . PRO B 1 477 ? 209.078 212.067 198.218 1.00 58.98  ?  496 PRO B CG    1 
ATOM   10047 C  CD    . PRO B 1 477 ? 209.859 211.067 197.400 1.00 59.31  ?  496 PRO B CD    1 
ATOM   10048 N  N     . PHE B 1 478 ? 205.261 210.865 196.791 1.00 65.59  ?  497 PHE B N     1 
ATOM   10049 C  CA    . PHE B 1 478 ? 204.183 211.466 196.014 1.00 58.11  ?  497 PHE B CA    1 
ATOM   10050 C  C     . PHE B 1 478 ? 202.980 211.702 196.918 1.00 60.10  ?  497 PHE B C     1 
ATOM   10051 O  O     . PHE B 1 478 ? 202.261 210.754 197.261 1.00 62.97  ?  497 PHE B O     1 
ATOM   10052 C  CB    . PHE B 1 478 ? 203.803 210.577 194.830 1.00 56.78  ?  497 PHE B CB    1 
ATOM   10053 C  CG    . PHE B 1 478 ? 204.815 210.582 193.721 1.00 57.84  ?  497 PHE B CG    1 
ATOM   10054 C  CD1   . PHE B 1 478 ? 204.896 211.651 192.845 1.00 60.35  ?  497 PHE B CD1   1 
ATOM   10055 C  CD2   . PHE B 1 478 ? 205.687 209.519 193.557 1.00 56.20  ?  497 PHE B CD2   1 
ATOM   10056 C  CE1   . PHE B 1 478 ? 205.827 211.660 191.825 1.00 62.19  ?  497 PHE B CE1   1 
ATOM   10057 C  CE2   . PHE B 1 478 ? 206.620 209.522 192.538 1.00 56.22  ?  497 PHE B CE2   1 
ATOM   10058 C  CZ    . PHE B 1 478 ? 206.690 210.594 191.672 1.00 60.42  ?  497 PHE B CZ    1 
ATOM   10059 N  N     . PRO B 1 479 ? 202.728 212.947 197.325 1.00 54.02  ?  498 PRO B N     1 
ATOM   10060 C  CA    . PRO B 1 479 ? 201.658 213.251 198.301 1.00 54.10  ?  498 PRO B CA    1 
ATOM   10061 C  C     . PRO B 1 479 ? 200.259 213.312 197.689 1.00 55.93  ?  498 PRO B C     1 
ATOM   10062 O  O     . PRO B 1 479 ? 199.733 214.363 197.323 1.00 58.34  ?  498 PRO B O     1 
ATOM   10063 C  CB    . PRO B 1 479 ? 202.088 214.611 198.861 1.00 53.27  ?  498 PRO B CB    1 
ATOM   10064 C  CG    . PRO B 1 479 ? 203.432 214.939 198.222 1.00 51.69  ?  498 PRO B CG    1 
ATOM   10065 C  CD    . PRO B 1 479 ? 203.492 214.148 196.967 1.00 51.57  ?  498 PRO B CD    1 
ATOM   10066 N  N     . LEU B 1 480 ? 199.628 212.147 197.567 1.00 55.85  ?  499 LEU B N     1 
ATOM   10067 C  CA    . LEU B 1 480 ? 198.245 212.106 197.121 1.00 53.33  ?  499 LEU B CA    1 
ATOM   10068 C  C     . LEU B 1 480 ? 197.314 212.562 198.244 1.00 54.91  ?  499 LEU B C     1 
ATOM   10069 O  O     . LEU B 1 480 ? 197.684 212.595 199.421 1.00 54.69  ?  499 LEU B O     1 
ATOM   10070 C  CB    . LEU B 1 480 ? 197.865 210.702 196.647 1.00 46.94  ?  499 LEU B CB    1 
ATOM   10071 C  CG    . LEU B 1 480 ? 198.840 209.959 195.728 1.00 50.74  ?  499 LEU B CG    1 
ATOM   10072 C  CD1   . LEU B 1 480 ? 198.167 208.741 195.115 1.00 52.74  ?  499 LEU B CD1   1 
ATOM   10073 C  CD2   . LEU B 1 480 ? 199.386 210.867 194.638 1.00 51.76  ?  499 LEU B CD2   1 
ATOM   10074 N  N     . THR B 1 481 ? 196.088 212.919 197.865 1.00 51.21  ?  500 THR B N     1 
ATOM   10075 C  CA    . THR B 1 481 ? 195.152 213.556 198.779 1.00 46.04  ?  500 THR B CA    1 
ATOM   10076 C  C     . THR B 1 481 ? 193.748 213.040 198.472 1.00 41.25  ?  500 THR B C     1 
ATOM   10077 O  O     . THR B 1 481 ? 193.484 212.536 197.379 1.00 42.53  ?  500 THR B O     1 
ATOM   10078 C  CB    . THR B 1 481 ? 195.251 215.086 198.654 1.00 46.31  ?  500 THR B CB    1 
ATOM   10079 O  OG1   . THR B 1 481 ? 196.589 215.497 198.957 1.00 50.15  ?  500 THR B OG1   1 
ATOM   10080 C  CG2   . THR B 1 481 ? 194.340 215.771 199.633 1.00 44.96  ?  500 THR B CG2   1 
ATOM   10081 N  N     . LEU B 1 482 ? 192.847 213.141 199.453 1.00 33.21  ?  501 LEU B N     1 
ATOM   10082 C  CA    . LEU B 1 482 ? 191.537 212.510 199.367 1.00 33.79  ?  501 LEU B CA    1 
ATOM   10083 C  C     . LEU B 1 482 ? 190.395 213.509 199.516 1.00 31.66  ?  501 LEU B C     1 
ATOM   10084 O  O     . LEU B 1 482 ? 190.441 214.417 200.359 1.00 40.83  ?  501 LEU B O     1 
ATOM   10085 C  CB    . LEU B 1 482 ? 191.392 211.410 200.419 1.00 37.94  ?  501 LEU B CB    1 
ATOM   10086 C  CG    . LEU B 1 482 ? 192.277 210.198 200.145 1.00 43.27  ?  501 LEU B CG    1 
ATOM   10087 C  CD1   . LEU B 1 482 ? 192.089 209.141 201.206 1.00 40.83  ?  501 LEU B CD1   1 
ATOM   10088 C  CD2   . LEU B 1 482 ? 191.960 209.642 198.776 1.00 37.77  ?  501 LEU B CD2   1 
ATOM   10089 N  N     . SER B 1 483 ? 189.365 213.313 198.690 1.00 29.55  ?  502 SER B N     1 
ATOM   10090 C  CA    . SER B 1 483 ? 188.118 214.068 198.764 1.00 30.56  ?  502 SER B CA    1 
ATOM   10091 C  C     . SER B 1 483 ? 186.970 213.087 198.961 1.00 39.61  ?  502 SER B C     1 
ATOM   10092 O  O     . SER B 1 483 ? 186.756 212.208 198.123 1.00 49.64  ?  502 SER B O     1 
ATOM   10093 C  CB    . SER B 1 483 ? 187.906 214.895 197.495 1.00 40.60  ?  502 SER B CB    1 
ATOM   10094 O  OG    . SER B 1 483 ? 189.073 215.623 197.159 1.00 46.78  ?  502 SER B OG    1 
ATOM   10095 N  N     . ILE B 1 484 ? 186.225 213.240 200.053 1.00 32.86  ?  503 ILE B N     1 
ATOM   10096 C  CA    . ILE B 1 484 ? 185.234 212.252 200.469 1.00 24.01  ?  503 ILE B CA    1 
ATOM   10097 C  C     . ILE B 1 484 ? 183.867 212.913 200.588 1.00 25.07  ?  503 ILE B C     1 
ATOM   10098 O  O     . ILE B 1 484 ? 183.737 213.996 201.169 1.00 35.78  ?  503 ILE B O     1 
ATOM   10099 C  CB    . ILE B 1 484 ? 185.629 211.574 201.793 1.00 21.59  ?  503 ILE B CB    1 
ATOM   10100 C  CG1   . ILE B 1 484 ? 187.108 211.188 201.778 1.00 27.46  ?  503 ILE B CG1   1 
ATOM   10101 C  CG2   . ILE B 1 484 ? 184.766 210.351 202.042 1.00 30.30  ?  503 ILE B CG2   1 
ATOM   10102 C  CD1   . ILE B 1 484 ? 187.555 210.451 203.012 1.00 33.25  ?  503 ILE B CD1   1 
ATOM   10103 N  N     . GLY B 1 485 ? 182.854 212.258 200.029 1.00 26.07  ?  504 GLY B N     1 
ATOM   10104 C  CA    . GLY B 1 485 ? 181.470 212.655 200.201 1.00 25.99  ?  504 GLY B CA    1 
ATOM   10105 C  C     . GLY B 1 485 ? 180.679 211.591 200.935 1.00 31.36  ?  504 GLY B C     1 
ATOM   10106 O  O     . GLY B 1 485 ? 180.764 210.408 200.594 1.00 42.63  ?  504 GLY B O     1 
ATOM   10107 N  N     . ILE B 1 486 ? 179.908 211.988 201.944 1.00 33.12  ?  505 ILE B N     1 
ATOM   10108 C  CA    . ILE B 1 486 ? 179.216 211.048 202.818 1.00 24.70  ?  505 ILE B CA    1 
ATOM   10109 C  C     . ILE B 1 486 ? 177.713 211.220 202.651 1.00 33.76  ?  505 ILE B C     1 
ATOM   10110 O  O     . ILE B 1 486 ? 177.192 212.341 202.738 1.00 47.39  ?  505 ILE B O     1 
ATOM   10111 C  CB    . ILE B 1 486 ? 179.626 211.228 204.290 1.00 28.50  ?  505 ILE B CB    1 
ATOM   10112 C  CG1   . ILE B 1 486 ? 181.101 210.871 204.474 1.00 28.66  ?  505 ILE B CG1   1 
ATOM   10113 C  CG2   . ILE B 1 486 ? 178.763 210.366 205.189 1.00 35.89  ?  505 ILE B CG2   1 
ATOM   10114 C  CD1   . ILE B 1 486 ? 181.688 211.373 205.761 1.00 36.14  ?  505 ILE B CD1   1 
ATOM   10115 N  N     . SER B 1 487 ? 177.017 210.103 202.435 1.00 29.40  ?  506 SER B N     1 
ATOM   10116 C  CA    . SER B 1 487 ? 175.573 210.091 202.266 1.00 24.62  ?  506 SER B CA    1 
ATOM   10117 C  C     . SER B 1 487 ? 174.940 209.108 203.240 1.00 40.54  ?  506 SER B C     1 
ATOM   10118 O  O     . SER B 1 487 ? 175.414 207.977 203.402 1.00 49.79  ?  506 SER B O     1 
ATOM   10119 C  CB    . SER B 1 487 ? 175.183 209.720 200.833 1.00 35.59  ?  506 SER B CB    1 
ATOM   10120 O  OG    . SER B 1 487 ? 173.831 210.053 200.574 1.00 40.68  ?  506 SER B OG    1 
ATOM   10121 N  N     . TYR B 1 488 ? 173.862 209.554 203.884 1.00 61.76  ?  507 TYR B N     1 
ATOM   10122 C  CA    . TYR B 1 488 ? 173.075 208.707 204.776 1.00 55.48  ?  507 TYR B CA    1 
ATOM   10123 C  C     . TYR B 1 488 ? 171.701 209.332 204.951 1.00 54.54  ?  507 TYR B C     1 
ATOM   10124 O  O     . TYR B 1 488 ? 171.593 210.462 205.438 1.00 57.57  ?  507 TYR B O     1 
ATOM   10125 C  CB    . TYR B 1 488 ? 173.760 208.531 206.130 1.00 52.51  ?  507 TYR B CB    1 
ATOM   10126 C  CG    . TYR B 1 488 ? 172.836 207.985 207.193 1.00 49.95  ?  507 TYR B CG    1 
ATOM   10127 C  CD1   . TYR B 1 488 ? 172.361 206.683 207.122 1.00 60.90  ?  507 TYR B CD1   1 
ATOM   10128 C  CD2   . TYR B 1 488 ? 172.435 208.769 208.265 1.00 55.71  ?  507 TYR B CD2   1 
ATOM   10129 C  CE1   . TYR B 1 488 ? 171.514 206.179 208.087 1.00 63.41  ?  507 TYR B CE1   1 
ATOM   10130 C  CE2   . TYR B 1 488 ? 171.588 208.273 209.237 1.00 59.65  ?  507 TYR B CE2   1 
ATOM   10131 C  CZ    . TYR B 1 488 ? 171.130 206.976 209.141 1.00 63.07  ?  507 TYR B CZ    1 
ATOM   10132 O  OH    . TYR B 1 488 ? 170.288 206.469 210.104 1.00 62.44  ?  507 TYR B OH    1 
ATOM   10133 N  N     . ASP B 1 489 ? 170.659 208.604 204.557 1.00 68.28  ?  508 ASP B N     1 
ATOM   10134 C  CA    . ASP B 1 489 ? 169.286 209.054 204.748 1.00 71.69  ?  508 ASP B CA    1 
ATOM   10135 C  C     . ASP B 1 489 ? 168.393 207.830 204.881 1.00 72.66  ?  508 ASP B C     1 
ATOM   10136 O  O     . ASP B 1 489 ? 168.381 206.972 203.993 1.00 71.43  ?  508 ASP B O     1 
ATOM   10137 C  CB    . ASP B 1 489 ? 168.821 209.942 203.590 1.00 69.37  ?  508 ASP B CB    1 
ATOM   10138 C  CG    . ASP B 1 489 ? 167.534 210.679 203.904 1.00 73.86  ?  508 ASP B CG    1 
ATOM   10139 O  OD1   . ASP B 1 489 ? 167.272 210.939 205.097 1.00 72.94  ?  508 ASP B OD1   1 
ATOM   10140 O  OD2   . ASP B 1 489 ? 166.789 211.011 202.959 1.00 75.29  -1 508 ASP B OD2   1 
ATOM   10141 N  N     . LEU B 1 490 ? 167.658 207.756 205.988 1.00 78.11  ?  509 LEU B N     1 
ATOM   10142 C  CA    . LEU B 1 490 ? 166.863 206.573 206.290 1.00 76.35  ?  509 LEU B CA    1 
ATOM   10143 C  C     . LEU B 1 490 ? 165.787 206.350 205.234 1.00 75.07  ?  509 LEU B C     1 
ATOM   10144 O  O     . LEU B 1 490 ? 165.091 207.286 204.830 1.00 73.99  ?  509 LEU B O     1 
ATOM   10145 C  CB    . LEU B 1 490 ? 166.223 206.714 207.671 1.00 74.66  ?  509 LEU B CB    1 
ATOM   10146 C  CG    . LEU B 1 490 ? 167.168 206.640 208.872 1.00 76.60  ?  509 LEU B CG    1 
ATOM   10147 C  CD1   . LEU B 1 490 ? 167.571 208.039 209.319 1.00 76.17  ?  509 LEU B CD1   1 
ATOM   10148 C  CD2   . LEU B 1 490 ? 166.529 205.870 210.016 1.00 74.62  ?  509 LEU B CD2   1 
ATOM   10149 N  N     . GLY B 1 491 ? 165.656 205.102 204.788 1.00 76.20  ?  510 GLY B N     1 
ATOM   10150 C  CA    . GLY B 1 491 ? 164.601 204.714 203.877 1.00 75.13  ?  510 GLY B CA    1 
ATOM   10151 C  C     . GLY B 1 491 ? 164.840 205.028 202.417 1.00 76.67  ?  510 GLY B C     1 
ATOM   10152 O  O     . GLY B 1 491 ? 163.961 204.747 201.593 1.00 80.69  ?  510 GLY B O     1 
ATOM   10153 N  N     . LYS B 1 492 ? 165.988 205.596 202.064 1.00 73.11  ?  511 LYS B N     1 
ATOM   10154 C  CA    . LYS B 1 492 ? 166.256 205.948 200.679 1.00 71.85  ?  511 LYS B CA    1 
ATOM   10155 C  C     . LYS B 1 492 ? 166.970 204.806 199.961 1.00 71.02  ?  511 LYS B C     1 
ATOM   10156 O  O     . LYS B 1 492 ? 167.377 203.811 200.563 1.00 71.78  ?  511 LYS B O     1 
ATOM   10157 C  CB    . LYS B 1 492 ? 167.074 207.235 200.600 1.00 71.00  ?  511 LYS B CB    1 
ATOM   10158 C  CG    . LYS B 1 492 ? 166.364 208.440 201.192 1.00 72.92  ?  511 LYS B CG    1 
ATOM   10159 C  CD    . LYS B 1 492 ? 165.056 208.732 200.470 1.00 73.29  ?  511 LYS B CD    1 
ATOM   10160 C  CE    . LYS B 1 492 ? 165.293 209.252 199.063 1.00 73.78  ?  511 LYS B CE    1 
ATOM   10161 N  NZ    . LYS B 1 492 ? 164.017 209.609 198.383 1.00 71.55  1  511 LYS B NZ    1 
ATOM   10162 N  N     . ASN B 1 493 ? 167.121 204.963 198.650 1.00 63.02  ?  512 ASN B N     1 
ATOM   10163 C  CA    . ASN B 1 493 ? 167.611 203.898 197.792 1.00 59.63  ?  512 ASN B CA    1 
ATOM   10164 C  C     . ASN B 1 493 ? 169.050 204.158 197.348 1.00 59.89  ?  512 ASN B C     1 
ATOM   10165 O  O     . ASN B 1 493 ? 169.643 205.213 197.606 1.00 62.00  ?  512 ASN B O     1 
ATOM   10166 C  CB    . ASN B 1 493 ? 166.683 203.726 196.587 1.00 57.92  ?  512 ASN B CB    1 
ATOM   10167 C  CG    . ASN B 1 493 ? 166.414 205.031 195.866 1.00 61.10  ?  512 ASN B CG    1 
ATOM   10168 O  OD1   . ASN B 1 493 ? 167.334 205.691 195.386 1.00 60.97  ?  512 ASN B OD1   1 
ATOM   10169 N  ND2   . ASN B 1 493 ? 165.144 205.412 195.790 1.00 61.35  ?  512 ASN B ND2   1 
ATOM   10170 N  N     . ARG B 1 494 ? 169.609 203.162 196.653 1.00 51.16  ?  513 ARG B N     1 
ATOM   10171 C  CA    . ARG B 1 494 ? 171.010 203.217 196.249 1.00 54.34  ?  513 ARG B CA    1 
ATOM   10172 C  C     . ARG B 1 494 ? 171.265 204.359 195.274 1.00 53.41  ?  513 ARG B C     1 
ATOM   10173 O  O     . ARG B 1 494 ? 172.320 204.999 195.326 1.00 53.62  ?  513 ARG B O     1 
ATOM   10174 C  CB    . ARG B 1 494 ? 171.436 201.876 195.642 1.00 52.68  ?  513 ARG B CB    1 
ATOM   10175 C  CG    . ARG B 1 494 ? 170.910 201.615 194.236 1.00 50.42  ?  513 ARG B CG    1 
ATOM   10176 C  CD    . ARG B 1 494 ? 171.742 200.580 193.499 1.00 48.05  ?  513 ARG B CD    1 
ATOM   10177 N  NE    . ARG B 1 494 ? 171.554 200.668 192.055 1.00 49.63  ?  513 ARG B NE    1 
ATOM   10178 C  CZ    . ARG B 1 494 ? 171.185 199.657 191.282 1.00 51.87  ?  513 ARG B CZ    1 
ATOM   10179 N  NH1   . ARG B 1 494 ? 170.950 198.455 191.780 1.00 51.83  1  513 ARG B NH1   1 
ATOM   10180 N  NH2   . ARG B 1 494 ? 171.045 199.857 189.974 1.00 49.80  ?  513 ARG B NH2   1 
ATOM   10181 N  N     . ASP B 1 495 ? 170.314 204.632 194.377 1.00 54.30  ?  514 ASP B N     1 
ATOM   10182 C  CA    . ASP B 1 495 ? 170.503 205.706 193.408 1.00 55.92  ?  514 ASP B CA    1 
ATOM   10183 C  C     . ASP B 1 495 ? 170.619 207.053 194.107 1.00 54.46  ?  514 ASP B C     1 
ATOM   10184 O  O     . ASP B 1 495 ? 171.535 207.836 193.826 1.00 55.46  ?  514 ASP B O     1 
ATOM   10185 C  CB    . ASP B 1 495 ? 169.351 205.714 192.404 1.00 56.29  ?  514 ASP B CB    1 
ATOM   10186 C  CG    . ASP B 1 495 ? 169.461 204.601 191.383 1.00 58.75  ?  514 ASP B CG    1 
ATOM   10187 O  OD1   . ASP B 1 495 ? 170.563 204.031 191.241 1.00 61.34  ?  514 ASP B OD1   1 
ATOM   10188 O  OD2   . ASP B 1 495 ? 168.446 204.295 190.722 1.00 55.21  -1 514 ASP B OD2   1 
ATOM   10189 N  N     . TYR B 1 496 ? 169.704 207.331 195.038 1.00 54.39  ?  515 TYR B N     1 
ATOM   10190 C  CA    . TYR B 1 496 ? 169.759 208.581 195.787 1.00 55.56  ?  515 TYR B CA    1 
ATOM   10191 C  C     . TYR B 1 496 ? 171.038 208.668 196.609 1.00 56.23  ?  515 TYR B C     1 
ATOM   10192 O  O     . TYR B 1 496 ? 171.708 209.708 196.626 1.00 59.21  ?  515 TYR B O     1 
ATOM   10193 C  CB    . TYR B 1 496 ? 168.526 208.706 196.683 1.00 57.15  ?  515 TYR B CB    1 
ATOM   10194 C  CG    . TYR B 1 496 ? 168.446 210.009 197.446 1.00 56.97  ?  515 TYR B CG    1 
ATOM   10195 C  CD1   . TYR B 1 496 ? 168.116 211.195 196.803 1.00 55.78  ?  515 TYR B CD1   1 
ATOM   10196 C  CD2   . TYR B 1 496 ? 168.697 210.053 198.811 1.00 58.02  ?  515 TYR B CD2   1 
ATOM   10197 C  CE1   . TYR B 1 496 ? 168.042 212.387 197.499 1.00 56.97  ?  515 TYR B CE1   1 
ATOM   10198 C  CE2   . TYR B 1 496 ? 168.624 211.239 199.514 1.00 55.82  ?  515 TYR B CE2   1 
ATOM   10199 C  CZ    . TYR B 1 496 ? 168.297 212.403 198.853 1.00 56.96  ?  515 TYR B CZ    1 
ATOM   10200 O  OH    . TYR B 1 496 ? 168.225 213.586 199.553 1.00 59.50  ?  515 TYR B OH    1 
ATOM   10201 N  N     . LEU B 1 497 ? 171.402 207.576 197.287 1.00 46.51  ?  516 LEU B N     1 
ATOM   10202 C  CA    . LEU B 1 497 ? 172.599 207.596 198.123 1.00 50.26  ?  516 LEU B CA    1 
ATOM   10203 C  C     . LEU B 1 497 ? 173.847 207.879 197.291 1.00 50.84  ?  516 LEU B C     1 
ATOM   10204 O  O     . LEU B 1 497 ? 174.664 208.740 197.645 1.00 54.08  ?  516 LEU B O     1 
ATOM   10205 C  CB    . LEU B 1 497 ? 172.733 206.269 198.870 1.00 47.50  ?  516 LEU B CB    1 
ATOM   10206 C  CG    . LEU B 1 497 ? 171.954 206.148 200.182 1.00 47.27  ?  516 LEU B CG    1 
ATOM   10207 C  CD1   . LEU B 1 497 ? 172.106 204.757 200.776 1.00 46.17  ?  516 LEU B CD1   1 
ATOM   10208 C  CD2   . LEU B 1 497 ? 172.399 207.209 201.176 1.00 48.70  ?  516 LEU B CD2   1 
ATOM   10209 N  N     . LEU B 1 498 ? 174.001 207.171 196.168 1.00 44.65  ?  517 LEU B N     1 
ATOM   10210 C  CA    . LEU B 1 498 ? 175.171 207.359 195.317 1.00 43.97  ?  517 LEU B CA    1 
ATOM   10211 C  C     . LEU B 1 498 ? 175.201 208.756 194.714 1.00 48.78  ?  517 LEU B C     1 
ATOM   10212 O  O     . LEU B 1 498 ? 176.260 209.392 194.666 1.00 55.97  ?  517 LEU B O     1 
ATOM   10213 C  CB    . LEU B 1 498 ? 175.196 206.302 194.213 1.00 45.38  ?  517 LEU B CB    1 
ATOM   10214 C  CG    . LEU B 1 498 ? 175.506 204.866 194.639 1.00 50.56  ?  517 LEU B CG    1 
ATOM   10215 C  CD1   . LEU B 1 498 ? 175.177 203.900 193.512 1.00 52.02  ?  517 LEU B CD1   1 
ATOM   10216 C  CD2   . LEU B 1 498 ? 176.964 204.735 195.055 1.00 44.88  ?  517 LEU B CD2   1 
ATOM   10217 N  N     . SER B 1 499 ? 174.052 209.253 194.243 1.00 49.43  ?  518 SER B N     1 
ATOM   10218 C  CA    . SER B 1 499 ? 174.019 210.584 193.648 1.00 48.77  ?  518 SER B CA    1 
ATOM   10219 C  C     . SER B 1 499 ? 174.393 211.652 194.667 1.00 46.12  ?  518 SER B C     1 
ATOM   10220 O  O     . SER B 1 499 ? 175.154 212.575 194.358 1.00 51.76  ?  518 SER B O     1 
ATOM   10221 C  CB    . SER B 1 499 ? 172.636 210.863 193.060 1.00 49.58  ?  518 SER B CB    1 
ATOM   10222 O  OG    . SER B 1 499 ? 171.622 210.680 194.032 1.00 50.61  ?  518 SER B OG    1 
ATOM   10223 N  N     . THR B 1 500 ? 173.881 211.534 195.893 1.00 34.72  ?  519 THR B N     1 
ATOM   10224 C  CA    . THR B 1 500 ? 174.181 212.531 196.915 1.00 40.43  ?  519 THR B CA    1 
ATOM   10225 C  C     . THR B 1 500 ? 175.645 212.470 197.344 1.00 47.87  ?  519 THR B C     1 
ATOM   10226 O  O     . THR B 1 500 ? 176.292 213.513 197.524 1.00 56.62  ?  519 THR B O     1 
ATOM   10227 C  CB    . THR B 1 500 ? 173.252 212.330 198.108 1.00 45.85  ?  519 THR B CB    1 
ATOM   10228 O  OG1   . THR B 1 500 ? 173.339 210.972 198.555 1.00 51.32  ?  519 THR B OG1   1 
ATOM   10229 C  CG2   . THR B 1 500 ? 171.818 212.615 197.696 1.00 47.42  ?  519 THR B CG2   1 
ATOM   10230 N  N     . ALA B 1 501 ? 176.189 211.259 197.503 1.00 39.64  ?  520 ALA B N     1 
ATOM   10231 C  CA    . ALA B 1 501 ? 177.601 211.137 197.848 1.00 37.27  ?  520 ALA B CA    1 
ATOM   10232 C  C     . ALA B 1 501 ? 178.484 211.697 196.742 1.00 40.50  ?  520 ALA B C     1 
ATOM   10233 O  O     . ALA B 1 501 ? 179.491 212.362 197.016 1.00 45.68  ?  520 ALA B O     1 
ATOM   10234 C  CB    . ALA B 1 501 ? 177.952 209.677 198.132 1.00 34.61  ?  520 ALA B CB    1 
ATOM   10235 N  N     . HIS B 1 502 ? 178.120 211.446 195.481 1.00 45.70  ?  521 HIS B N     1 
ATOM   10236 C  CA    . HIS B 1 502 ? 178.903 211.979 194.373 1.00 44.05  ?  521 HIS B CA    1 
ATOM   10237 C  C     . HIS B 1 502 ? 178.796 213.494 194.304 1.00 49.63  ?  521 HIS B C     1 
ATOM   10238 O  O     . HIS B 1 502 ? 179.766 214.174 193.961 1.00 51.85  ?  521 HIS B O     1 
ATOM   10239 C  CB    . HIS B 1 502 ? 178.459 211.345 193.056 1.00 39.66  ?  521 HIS B CB    1 
ATOM   10240 C  CG    . HIS B 1 502 ? 179.366 211.652 191.905 1.00 47.15  ?  521 HIS B CG    1 
ATOM   10241 N  ND1   . HIS B 1 502 ? 180.592 211.044 191.745 1.00 54.38  ?  521 HIS B ND1   1 
ATOM   10242 C  CD2   . HIS B 1 502 ? 179.231 212.506 190.864 1.00 47.49  ?  521 HIS B CD2   1 
ATOM   10243 C  CE1   . HIS B 1 502 ? 181.171 211.507 190.652 1.00 47.83  ?  521 HIS B CE1   1 
ATOM   10244 N  NE2   . HIS B 1 502 ? 180.366 212.396 190.099 1.00 48.06  ?  521 HIS B NE2   1 
ATOM   10245 N  N     . ASN B 1 503 ? 177.622 214.044 194.625 1.00 43.74  ?  522 ASN B N     1 
ATOM   10246 C  CA    . ASN B 1 503 ? 177.480 215.495 194.681 1.00 37.47  ?  522 ASN B CA    1 
ATOM   10247 C  C     . ASN B 1 503 ? 178.404 216.096 195.732 1.00 39.74  ?  522 ASN B C     1 
ATOM   10248 O  O     . ASN B 1 503 ? 179.110 217.076 195.462 1.00 47.66  ?  522 ASN B O     1 
ATOM   10249 C  CB    . ASN B 1 503 ? 176.025 215.867 194.968 1.00 40.53  ?  522 ASN B CB    1 
ATOM   10250 C  CG    . ASN B 1 503 ? 175.622 217.181 194.327 1.00 47.30  ?  522 ASN B CG    1 
ATOM   10251 O  OD1   . ASN B 1 503 ? 176.403 217.798 193.603 1.00 49.36  ?  522 ASN B OD1   1 
ATOM   10252 N  ND2   . ASN B 1 503 ? 174.395 217.615 194.591 1.00 44.72  ?  522 ASN B ND2   1 
ATOM   10253 N  N     . ALA B 1 504 ? 178.427 215.510 196.933 1.00 26.88  ?  523 ALA B N     1 
ATOM   10254 C  CA    . ALA B 1 504 ? 179.303 216.025 197.984 1.00 32.12  ?  523 ALA B CA    1 
ATOM   10255 C  C     . ALA B 1 504 ? 180.774 215.907 197.592 1.00 39.04  ?  523 ALA B C     1 
ATOM   10256 O  O     . ALA B 1 504 ? 181.557 216.851 197.779 1.00 43.56  ?  523 ALA B O     1 
ATOM   10257 C  CB    . ALA B 1 504 ? 179.037 215.290 199.298 1.00 37.08  ?  523 ALA B CB    1 
ATOM   10258 N  N     . MET B 1 505 ? 181.164 214.755 197.038 1.00 49.70  ?  524 MET B N     1 
ATOM   10259 C  CA    . MET B 1 505 ? 182.553 214.548 196.640 1.00 45.82  ?  524 MET B CA    1 
ATOM   10260 C  C     . MET B 1 505 ? 182.962 215.504 195.526 1.00 44.95  ?  524 MET B C     1 
ATOM   10261 O  O     . MET B 1 505 ? 184.070 216.050 195.543 1.00 44.37  ?  524 MET B O     1 
ATOM   10262 C  CB    . MET B 1 505 ? 182.755 213.100 196.202 1.00 46.53  ?  524 MET B CB    1 
ATOM   10263 C  CG    . MET B 1 505 ? 184.200 212.643 196.201 1.00 42.50  ?  524 MET B CG    1 
ATOM   10264 S  SD    . MET B 1 505 ? 184.929 212.741 194.559 1.00 57.97  ?  524 MET B SD    1 
ATOM   10265 C  CE    . MET B 1 505 ? 183.809 211.692 193.639 1.00 49.19  ?  524 MET B CE    1 
ATOM   10266 N  N     . ASP B 1 506 ? 182.085 215.716 194.543 1.00 53.25  ?  525 ASP B N     1 
ATOM   10267 C  CA    . ASP B 1 506 ? 182.390 216.644 193.462 1.00 50.05  ?  525 ASP B CA    1 
ATOM   10268 C  C     . ASP B 1 506 ? 182.505 218.068 193.982 1.00 43.63  ?  525 ASP B C     1 
ATOM   10269 O  O     . ASP B 1 506 ? 183.376 218.826 193.542 1.00 50.29  ?  525 ASP B O     1 
ATOM   10270 C  CB    . ASP B 1 506 ? 181.320 216.551 192.374 1.00 52.24  ?  525 ASP B CB    1 
ATOM   10271 C  CG    . ASP B 1 506 ? 181.666 215.538 191.303 1.00 57.18  ?  525 ASP B CG    1 
ATOM   10272 O  OD1   . ASP B 1 506 ? 182.799 215.013 191.325 1.00 57.03  ?  525 ASP B OD1   1 
ATOM   10273 O  OD2   . ASP B 1 506 ? 180.807 215.268 190.439 1.00 56.12  -1 525 ASP B OD2   1 
ATOM   10274 N  N     . TYR B 1 507 ? 181.632 218.452 194.916 1.00 42.74  ?  526 TYR B N     1 
ATOM   10275 C  CA    . TYR B 1 507 ? 181.713 219.795 195.478 1.00 52.58  ?  526 TYR B CA    1 
ATOM   10276 C  C     . TYR B 1 507 ? 183.029 220.008 196.214 1.00 50.66  ?  526 TYR B C     1 
ATOM   10277 O  O     . TYR B 1 507 ? 183.677 221.049 196.048 1.00 52.45  ?  526 TYR B O     1 
ATOM   10278 C  CB    . TYR B 1 507 ? 180.531 220.055 196.409 1.00 51.37  ?  526 TYR B CB    1 
ATOM   10279 C  CG    . TYR B 1 507 ? 180.411 221.502 196.828 1.00 50.29  ?  526 TYR B CG    1 
ATOM   10280 C  CD1   . TYR B 1 507 ? 180.786 222.525 195.969 1.00 53.03  ?  526 TYR B CD1   1 
ATOM   10281 C  CD2   . TYR B 1 507 ? 179.926 221.846 198.082 1.00 47.86  ?  526 TYR B CD2   1 
ATOM   10282 C  CE1   . TYR B 1 507 ? 180.682 223.849 196.345 1.00 55.34  ?  526 TYR B CE1   1 
ATOM   10283 C  CE2   . TYR B 1 507 ? 179.817 223.169 198.467 1.00 50.60  ?  526 TYR B CE2   1 
ATOM   10284 C  CZ    . TYR B 1 507 ? 180.196 224.166 197.595 1.00 52.95  ?  526 TYR B CZ    1 
ATOM   10285 O  OH    . TYR B 1 507 ? 180.089 225.484 197.975 1.00 53.44  ?  526 TYR B OH    1 
ATOM   10286 N  N     . ILE B 1 508 ? 183.448 219.034 197.027 1.00 46.73  ?  527 ILE B N     1 
ATOM   10287 C  CA    . ILE B 1 508 ? 184.707 219.216 197.749 1.00 46.22  ?  527 ILE B CA    1 
ATOM   10288 C  C     . ILE B 1 508 ? 185.898 219.179 196.790 1.00 50.20  ?  527 ILE B C     1 
ATOM   10289 O  O     . ILE B 1 508 ? 186.872 219.923 196.974 1.00 52.74  ?  527 ILE B O     1 
ATOM   10290 C  CB    . ILE B 1 508 ? 184.843 218.193 198.897 1.00 50.46  ?  527 ILE B CB    1 
ATOM   10291 C  CG1   . ILE B 1 508 ? 186.047 218.534 199.779 1.00 51.04  ?  527 ILE B CG1   1 
ATOM   10292 C  CG2   . ILE B 1 508 ? 184.947 216.774 198.380 1.00 55.29  ?  527 ILE B CG2   1 
ATOM   10293 C  CD1   . ILE B 1 508 ? 186.044 219.959 200.293 1.00 53.97  ?  527 ILE B CD1   1 
ATOM   10294 N  N     . ARG B 1 509 ? 185.840 218.347 195.743 1.00 54.25  ?  528 ARG B N     1 
ATOM   10295 C  CA    . ARG B 1 509 ? 186.908 218.341 194.746 1.00 49.92  ?  528 ARG B CA    1 
ATOM   10296 C  C     . ARG B 1 509 ? 187.013 219.686 194.039 1.00 54.95  ?  528 ARG B C     1 
ATOM   10297 O  O     . ARG B 1 509 ? 188.118 220.195 193.817 1.00 52.43  ?  528 ARG B O     1 
ATOM   10298 C  CB    . ARG B 1 509 ? 186.678 217.225 193.727 1.00 52.19  ?  528 ARG B CB    1 
ATOM   10299 C  CG    . ARG B 1 509 ? 187.262 215.881 194.120 1.00 56.78  ?  528 ARG B CG    1 
ATOM   10300 C  CD    . ARG B 1 509 ? 187.261 214.917 192.945 1.00 54.02  ?  528 ARG B CD    1 
ATOM   10301 N  NE    . ARG B 1 509 ? 188.028 215.430 191.817 1.00 57.44  ?  528 ARG B NE    1 
ATOM   10302 C  CZ    . ARG B 1 509 ? 187.722 215.220 190.544 1.00 58.53  ?  528 ARG B CZ    1 
ATOM   10303 N  NH1   . ARG B 1 509 ? 186.663 214.507 190.196 1.00 58.21  1  528 ARG B NH1   1 
ATOM   10304 N  NH2   . ARG B 1 509 ? 188.498 215.737 189.596 1.00 55.22  ?  528 ARG B NH2   1 
ATOM   10305 N  N     . LYS B 1 510 ? 185.872 220.272 193.669 1.00 62.02  ?  529 LYS B N     1 
ATOM   10306 C  CA    . LYS B 1 510 ? 185.887 221.578 193.019 1.00 55.77  ?  529 LYS B CA    1 
ATOM   10307 C  C     . LYS B 1 510 ? 186.405 222.654 193.965 1.00 55.94  ?  529 LYS B C     1 
ATOM   10308 O  O     . LYS B 1 510 ? 187.172 223.533 193.556 1.00 59.55  ?  529 LYS B O     1 
ATOM   10309 C  CB    . LYS B 1 510 ? 184.487 221.930 192.516 1.00 56.32  ?  529 LYS B CB    1 
ATOM   10310 C  CG    . LYS B 1 510 ? 184.375 223.319 191.912 1.00 60.54  ?  529 LYS B CG    1 
ATOM   10311 C  CD    . LYS B 1 510 ? 185.291 223.462 190.706 1.00 62.54  ?  529 LYS B CD    1 
ATOM   10312 C  CE    . LYS B 1 510 ? 184.922 224.676 189.873 1.00 58.68  ?  529 LYS B CE    1 
ATOM   10313 N  NZ    . LYS B 1 510 ? 185.171 225.942 190.614 1.00 56.83  1  529 LYS B NZ    1 
ATOM   10314 N  N     . ASN B 1 511 ? 185.999 222.598 195.236 1.00 54.65  ?  530 ASN B N     1 
ATOM   10315 C  CA    . ASN B 1 511 ? 186.484 223.568 196.210 1.00 56.47  ?  530 ASN B CA    1 
ATOM   10316 C  C     . ASN B 1 511 ? 187.970 223.407 196.498 1.00 57.84  ?  530 ASN B C     1 
ATOM   10317 O  O     . ASN B 1 511 ? 188.604 224.362 196.958 1.00 60.62  ?  530 ASN B O     1 
ATOM   10318 C  CB    . ASN B 1 511 ? 185.689 223.454 197.512 1.00 58.73  ?  530 ASN B CB    1 
ATOM   10319 C  CG    . ASN B 1 511 ? 184.246 223.887 197.353 1.00 60.67  ?  530 ASN B CG    1 
ATOM   10320 O  OD1   . ASN B 1 511 ? 183.926 224.725 196.511 1.00 56.12  ?  530 ASN B OD1   1 
ATOM   10321 N  ND2   . ASN B 1 511 ? 183.365 223.318 198.168 1.00 62.00  ?  530 ASN B ND2   1 
ATOM   10322 N  N     . GLY B 1 512 ? 188.538 222.232 196.241 1.00 60.58  ?  531 GLY B N     1 
ATOM   10323 C  CA    . GLY B 1 512 ? 189.969 222.064 196.402 1.00 61.63  ?  531 GLY B CA    1 
ATOM   10324 C  C     . GLY B 1 512 ? 190.378 220.716 196.951 1.00 67.12  ?  531 GLY B C     1 
ATOM   10325 O  O     . GLY B 1 512 ? 191.569 220.392 196.995 1.00 67.67  ?  531 GLY B O     1 
ATOM   10326 N  N     . GLY B 1 513 ? 189.402 219.919 197.369 1.00 62.23  ?  532 GLY B N     1 
ATOM   10327 C  CA    . GLY B 1 513 ? 189.703 218.617 197.921 1.00 56.06  ?  532 GLY B CA    1 
ATOM   10328 C  C     . GLY B 1 513 ? 190.308 218.710 199.311 1.00 53.25  ?  532 GLY B C     1 
ATOM   10329 O  O     . GLY B 1 513 ? 190.112 219.681 200.051 1.00 57.71  ?  532 GLY B O     1 
ATOM   10330 N  N     . ASN B 1 514 ? 191.060 217.666 199.661 1.00 35.00  ?  533 ASN B N     1 
ATOM   10331 C  CA    . ASN B 1 514 ? 191.719 217.562 200.963 1.00 35.53  ?  533 ASN B CA    1 
ATOM   10332 C  C     . ASN B 1 514 ? 190.705 217.632 202.101 1.00 42.41  ?  533 ASN B C     1 
ATOM   10333 O  O     . ASN B 1 514 ? 190.825 218.444 203.021 1.00 49.57  ?  533 ASN B O     1 
ATOM   10334 C  CB    . ASN B 1 514 ? 192.800 218.636 201.123 1.00 42.12  ?  533 ASN B CB    1 
ATOM   10335 C  CG    . ASN B 1 514 ? 193.861 218.248 202.134 1.00 45.59  ?  533 ASN B CG    1 
ATOM   10336 O  OD1   . ASN B 1 514 ? 193.652 217.360 202.961 1.00 44.12  ?  533 ASN B OD1   1 
ATOM   10337 N  ND2   . ASN B 1 514 ? 195.004 218.921 202.080 1.00 48.22  ?  533 ASN B ND2   1 
ATOM   10338 N  N     . GLY B 1 515 ? 189.693 216.777 202.033 1.00 44.13  ?  534 GLY B N     1 
ATOM   10339 C  CA    . GLY B 1 515 ? 188.665 216.823 203.052 1.00 42.39  ?  534 GLY B CA    1 
ATOM   10340 C  C     . GLY B 1 515 ? 187.441 216.032 202.651 1.00 39.28  ?  534 GLY B C     1 
ATOM   10341 O  O     . GLY B 1 515 ? 187.444 215.278 201.675 1.00 46.05  ?  534 GLY B O     1 
ATOM   10342 N  N     . TRP B 1 516 ? 186.385 216.219 203.440 1.00 31.69  ?  535 TRP B N     1 
ATOM   10343 C  CA    . TRP B 1 516 ? 185.160 215.456 203.270 1.00 37.53  ?  535 TRP B CA    1 
ATOM   10344 C  C     . TRP B 1 516 ? 183.963 216.315 203.649 1.00 34.25  ?  535 TRP B C     1 
ATOM   10345 O  O     . TRP B 1 516 ? 184.087 217.313 204.362 1.00 37.56  ?  535 TRP B O     1 
ATOM   10346 C  CB    . TRP B 1 516 ? 185.191 214.167 204.099 1.00 42.82  ?  535 TRP B CB    1 
ATOM   10347 C  CG    . TRP B 1 516 ? 185.297 214.398 205.567 1.00 35.79  ?  535 TRP B CG    1 
ATOM   10348 C  CD1   . TRP B 1 516 ? 186.443 214.479 206.297 1.00 36.56  ?  535 TRP B CD1   1 
ATOM   10349 C  CD2   . TRP B 1 516 ? 184.218 214.572 206.491 1.00 26.08  ?  535 TRP B CD2   1 
ATOM   10350 N  NE1   . TRP B 1 516 ? 186.149 214.694 207.620 1.00 34.99  ?  535 TRP B NE1   1 
ATOM   10351 C  CE2   . TRP B 1 516 ? 184.788 214.756 207.766 1.00 32.55  ?  535 TRP B CE2   1 
ATOM   10352 C  CE3   . TRP B 1 516 ? 182.827 214.593 206.366 1.00 28.50  ?  535 TRP B CE3   1 
ATOM   10353 C  CZ2   . TRP B 1 516 ? 184.016 214.957 208.907 1.00 39.57  ?  535 TRP B CZ2   1 
ATOM   10354 C  CZ3   . TRP B 1 516 ? 182.063 214.792 207.500 1.00 37.95  ?  535 TRP B CZ3   1 
ATOM   10355 C  CH2   . TRP B 1 516 ? 182.658 214.971 208.753 1.00 39.52  ?  535 TRP B CH2   1 
ATOM   10356 N  N     . GLN B 1 517 ? 182.798 215.907 203.154 1.00 47.41  ?  536 GLN B N     1 
ATOM   10357 C  CA    . GLN B 1 517 ? 181.572 216.661 203.376 1.00 42.19  ?  536 GLN B CA    1 
ATOM   10358 C  C     . GLN B 1 517 ? 180.364 215.734 203.358 1.00 47.76  ?  536 GLN B C     1 
ATOM   10359 O  O     . GLN B 1 517 ? 180.296 214.798 202.557 1.00 50.40  ?  536 GLN B O     1 
ATOM   10360 C  CB    . GLN B 1 517 ? 181.391 217.760 202.322 1.00 38.93  ?  536 GLN B CB    1 
ATOM   10361 C  CG    . GLN B 1 517 ? 180.270 218.736 202.641 1.00 43.33  ?  536 GLN B CG    1 
ATOM   10362 C  CD    . GLN B 1 517 ? 180.053 219.760 201.547 1.00 47.36  ?  536 GLN B CD    1 
ATOM   10363 O  OE1   . GLN B 1 517 ? 180.019 219.424 200.363 1.00 49.00  ?  536 GLN B OE1   1 
ATOM   10364 N  NE2   . GLN B 1 517 ? 179.897 221.019 201.938 1.00 48.74  ?  536 GLN B NE2   1 
ATOM   10365 N  N     . PHE B 1 518 ? 179.418 216.008 204.252 1.00 46.38  ?  537 PHE B N     1 
ATOM   10366 C  CA    . PHE B 1 518 ? 178.110 215.373 204.213 1.00 37.90  ?  537 PHE B CA    1 
ATOM   10367 C  C     . PHE B 1 518 ? 177.265 215.958 203.088 1.00 40.84  ?  537 PHE B C     1 
ATOM   10368 O  O     . PHE B 1 518 ? 177.454 217.099 202.659 1.00 49.90  ?  537 PHE B O     1 
ATOM   10369 C  CB    . PHE B 1 518 ? 177.374 215.567 205.538 1.00 38.92  ?  537 PHE B CB    1 
ATOM   10370 C  CG    . PHE B 1 518 ? 177.661 214.511 206.559 1.00 34.03  ?  537 PHE B CG    1 
ATOM   10371 C  CD1   . PHE B 1 518 ? 178.699 214.660 207.459 1.00 36.47  ?  537 PHE B CD1   1 
ATOM   10372 C  CD2   . PHE B 1 518 ? 176.874 213.375 206.634 1.00 38.84  ?  537 PHE B CD2   1 
ATOM   10373 C  CE1   . PHE B 1 518 ? 178.958 213.688 208.405 1.00 39.61  ?  537 PHE B CE1   1 
ATOM   10374 C  CE2   . PHE B 1 518 ? 177.126 212.402 207.578 1.00 42.56  ?  537 PHE B CE2   1 
ATOM   10375 C  CZ    . PHE B 1 518 ? 178.169 212.559 208.464 1.00 42.73  ?  537 PHE B CZ    1 
ATOM   10376 N  N     . PHE B 1 519 ? 176.320 215.158 202.606 1.00 43.96  ?  538 PHE B N     1 
ATOM   10377 C  CA    . PHE B 1 519 ? 175.299 215.734 201.747 1.00 45.50  ?  538 PHE B CA    1 
ATOM   10378 C  C     . PHE B 1 519 ? 174.200 216.367 202.601 1.00 54.15  ?  538 PHE B C     1 
ATOM   10379 O  O     . PHE B 1 519 ? 174.051 216.065 203.789 1.00 56.15  ?  538 PHE B O     1 
ATOM   10380 C  CB    . PHE B 1 519 ? 174.692 214.682 200.818 1.00 44.61  ?  538 PHE B CB    1 
ATOM   10381 C  CG    . PHE B 1 519 ? 173.583 215.215 199.955 1.00 47.54  ?  538 PHE B CG    1 
ATOM   10382 C  CD1   . PHE B 1 519 ? 173.862 216.058 198.892 1.00 48.57  ?  538 PHE B CD1   1 
ATOM   10383 C  CD2   . PHE B 1 519 ? 172.260 214.924 200.242 1.00 47.31  ?  538 PHE B CD2   1 
ATOM   10384 C  CE1   . PHE B 1 519 ? 172.847 216.566 198.106 1.00 51.71  ?  538 PHE B CE1   1 
ATOM   10385 C  CE2   . PHE B 1 519 ? 171.238 215.437 199.464 1.00 47.33  ?  538 PHE B CE2   1 
ATOM   10386 C  CZ    . PHE B 1 519 ? 171.533 216.255 198.392 1.00 51.56  ?  538 PHE B CZ    1 
ATOM   10387 N  N     . SER B 1 520 ? 173.442 217.282 201.977 1.00 60.61  ?  539 SER B N     1 
ATOM   10388 C  CA    . SER B 1 520 ? 172.204 217.859 202.498 1.00 60.90  ?  539 SER B CA    1 
ATOM   10389 C  C     . SER B 1 520 ? 172.474 218.847 203.626 1.00 56.10  ?  539 SER B C     1 
ATOM   10390 O  O     . SER B 1 520 ? 173.433 218.681 204.390 1.00 57.20  ?  539 SER B O     1 
ATOM   10391 C  CB    . SER B 1 520 ? 171.246 216.762 202.972 1.00 59.32  ?  539 SER B CB    1 
ATOM   10392 O  OG    . SER B 1 520 ? 171.522 216.389 204.310 1.00 51.19  ?  539 SER B OG    1 
ATOM   10393 N  N     . PRO B 1 521 ? 171.657 219.890 203.755 1.00 58.53  ?  540 PRO B N     1 
ATOM   10394 C  CA    . PRO B 1 521 ? 171.867 220.864 204.830 1.00 61.77  ?  540 PRO B CA    1 
ATOM   10395 C  C     . PRO B 1 521 ? 171.551 220.274 206.197 1.00 66.09  ?  540 PRO B C     1 
ATOM   10396 O  O     . PRO B 1 521 ? 170.943 219.210 206.338 1.00 65.35  ?  540 PRO B O     1 
ATOM   10397 C  CB    . PRO B 1 521 ? 170.909 222.005 204.476 1.00 62.46  ?  540 PRO B CB    1 
ATOM   10398 C  CG    . PRO B 1 521 ? 169.864 221.371 203.628 1.00 63.39  ?  540 PRO B CG    1 
ATOM   10399 C  CD    . PRO B 1 521 ? 170.559 220.286 202.857 1.00 60.45  ?  540 PRO B CD    1 
ATOM   10400 N  N     . ALA B 1 522 ? 172.024 220.997 207.212 1.00 67.06  ?  541 ALA B N     1 
ATOM   10401 C  CA    . ALA B 1 522 ? 171.881 220.724 208.640 1.00 64.49  ?  541 ALA B CA    1 
ATOM   10402 C  C     . ALA B 1 522 ? 172.761 219.566 209.097 1.00 60.65  ?  541 ALA B C     1 
ATOM   10403 O  O     . ALA B 1 522 ? 173.100 219.485 210.280 1.00 62.60  ?  541 ALA B O     1 
ATOM   10404 C  CB    . ALA B 1 522 ? 170.418 220.451 209.004 1.00 65.25  ?  541 ALA B CB    1 
ATOM   10405 N  N     . MET B 1 523 ? 173.289 218.779 208.161 1.00 56.62  ?  542 MET B N     1 
ATOM   10406 C  CA    . MET B 1 523 ? 174.250 217.749 208.543 1.00 58.49  ?  542 MET B CA    1 
ATOM   10407 C  C     . MET B 1 523 ? 175.635 218.356 208.716 1.00 55.54  ?  542 MET B C     1 
ATOM   10408 O  O     . MET B 1 523 ? 176.280 218.186 209.760 1.00 58.95  ?  542 MET B O     1 
ATOM   10409 C  CB    . MET B 1 523 ? 174.273 216.633 207.498 1.00 59.04  ?  542 MET B CB    1 
ATOM   10410 C  CG    . MET B 1 523 ? 173.042 215.745 207.513 1.00 61.47  ?  542 MET B CG    1 
ATOM   10411 S  SD    . MET B 1 523 ? 173.006 214.636 208.935 1.00 78.21  ?  542 MET B SD    1 
ATOM   10412 C  CE    . MET B 1 523 ? 173.512 213.094 208.173 1.00 58.44  ?  542 MET B CE    1 
ATOM   10413 N  N     . ASN B 1 524 ? 176.092 219.092 207.703 1.00 52.31  ?  543 ASN B N     1 
ATOM   10414 C  CA    . ASN B 1 524 ? 177.297 219.890 207.865 1.00 54.89  ?  543 ASN B CA    1 
ATOM   10415 C  C     . ASN B 1 524 ? 177.108 220.954 208.936 1.00 60.10  ?  543 ASN B C     1 
ATOM   10416 O  O     . ASN B 1 524 ? 178.083 221.385 209.554 1.00 61.46  ?  543 ASN B O     1 
ATOM   10417 C  CB    . ASN B 1 524 ? 177.689 220.526 206.532 1.00 57.92  ?  543 ASN B CB    1 
ATOM   10418 C  CG    . ASN B 1 524 ? 178.100 219.496 205.499 1.00 56.87  ?  543 ASN B CG    1 
ATOM   10419 O  OD1   . ASN B 1 524 ? 179.038 218.728 205.712 1.00 60.47  ?  543 ASN B OD1   1 
ATOM   10420 N  ND2   . ASN B 1 524 ? 177.399 219.475 204.372 1.00 54.38  ?  543 ASN B ND2   1 
ATOM   10421 N  N     . GLU B 1 525 ? 175.865 221.367 209.194 1.00 64.15  ?  544 GLU B N     1 
ATOM   10422 C  CA    . GLU B 1 525 ? 175.614 222.316 210.275 1.00 61.82  ?  544 GLU B CA    1 
ATOM   10423 C  C     . GLU B 1 525 ? 175.841 221.672 211.639 1.00 60.04  ?  544 GLU B C     1 
ATOM   10424 O  O     . GLU B 1 525 ? 176.443 222.282 212.527 1.00 59.65  ?  544 GLU B O     1 
ATOM   10425 C  CB    . GLU B 1 525 ? 174.197 222.877 210.171 1.00 60.68  ?  544 GLU B CB    1 
ATOM   10426 N  N     . MET B 1 526 ? 175.364 220.437 211.827 1.00 59.26  ?  545 MET B N     1 
ATOM   10427 C  CA    . MET B 1 526 ? 175.665 219.715 213.060 1.00 57.65  ?  545 MET B CA    1 
ATOM   10428 C  C     . MET B 1 526 ? 177.164 219.483 213.204 1.00 58.24  ?  545 MET B C     1 
ATOM   10429 O  O     . MET B 1 526 ? 177.721 219.617 214.302 1.00 60.73  ?  545 MET B O     1 
ATOM   10430 C  CB    . MET B 1 526 ? 174.911 218.386 213.091 1.00 63.96  ?  545 MET B CB    1 
ATOM   10431 C  CG    . MET B 1 526 ? 173.428 218.518 213.383 1.00 65.26  ?  545 MET B CG    1 
ATOM   10432 S  SD    . MET B 1 526 ? 172.622 216.917 213.565 1.00 77.80  ?  545 MET B SD    1 
ATOM   10433 C  CE    . MET B 1 526 ? 173.200 216.431 215.189 1.00 63.60  ?  545 MET B CE    1 
ATOM   10434 N  N     . VAL B 1 527 ? 177.834 219.139 212.101 1.00 61.74  ?  546 VAL B N     1 
ATOM   10435 C  CA    . VAL B 1 527 ? 179.282 218.938 212.144 1.00 58.48  ?  546 VAL B CA    1 
ATOM   10436 C  C     . VAL B 1 527 ? 179.993 220.230 212.540 1.00 61.90  ?  546 VAL B C     1 
ATOM   10437 O  O     . VAL B 1 527 ? 180.916 220.221 213.363 1.00 61.29  ?  546 VAL B O     1 
ATOM   10438 C  CB    . VAL B 1 527 ? 179.787 218.403 210.792 1.00 57.51  ?  546 VAL B CB    1 
ATOM   10439 C  CG1   . VAL B 1 527 ? 181.307 218.417 210.745 1.00 61.29  ?  546 VAL B CG1   1 
ATOM   10440 C  CG2   . VAL B 1 527 ? 179.257 216.998 210.547 1.00 60.02  ?  546 VAL B CG2   1 
ATOM   10441 N  N     . LYS B 1 528 ? 179.570 221.359 211.967 1.00 64.60  ?  547 LYS B N     1 
ATOM   10442 C  CA    . LYS B 1 528 ? 180.192 222.642 212.277 1.00 60.65  ?  547 LYS B CA    1 
ATOM   10443 C  C     . LYS B 1 528 ? 179.917 223.059 213.715 1.00 59.50  ?  547 LYS B C     1 
ATOM   10444 O  O     . LYS B 1 528 ? 180.779 223.653 214.372 1.00 63.66  ?  547 LYS B O     1 
ATOM   10445 C  CB    . LYS B 1 528 ? 179.693 223.711 211.305 1.00 64.77  ?  547 LYS B CB    1 
ATOM   10446 C  CG    . LYS B 1 528 ? 180.638 224.886 211.126 1.00 66.47  ?  547 LYS B CG    1 
ATOM   10447 C  CD    . LYS B 1 528 ? 182.056 224.413 210.856 1.00 65.53  ?  547 LYS B CD    1 
ATOM   10448 C  CE    . LYS B 1 528 ? 182.978 225.581 210.550 1.00 67.56  ?  547 LYS B CE    1 
ATOM   10449 N  NZ    . LYS B 1 528 ? 184.357 225.125 210.226 1.00 64.92  1  547 LYS B NZ    1 
ATOM   10450 N  N     . GLU B 1 529 ? 178.712 222.777 214.216 1.00 59.53  ?  548 GLU B N     1 
ATOM   10451 C  CA    . GLU B 1 529 ? 178.408 223.062 215.614 1.00 61.25  ?  548 GLU B CA    1 
ATOM   10452 C  C     . GLU B 1 529 ? 179.290 222.240 216.541 1.00 59.24  ?  548 GLU B C     1 
ATOM   10453 O  O     . GLU B 1 529 ? 179.810 222.757 217.536 1.00 61.83  ?  548 GLU B O     1 
ATOM   10454 C  CB    . GLU B 1 529 ? 176.930 222.798 215.899 1.00 66.22  ?  548 GLU B CB    1 
ATOM   10455 C  CG    . GLU B 1 529 ? 175.988 223.846 215.330 1.00 66.28  ?  548 GLU B CG    1 
ATOM   10456 C  CD    . GLU B 1 529 ? 174.616 223.806 215.973 1.00 65.94  ?  548 GLU B CD    1 
ATOM   10457 O  OE1   . GLU B 1 529 ? 174.010 222.714 216.014 1.00 64.70  ?  548 GLU B OE1   1 
ATOM   10458 O  OE2   . GLU B 1 529 ? 174.143 224.864 216.438 1.00 64.11  -1 548 GLU B OE2   1 
ATOM   10459 N  N     . ARG B 1 530 ? 179.484 220.957 216.224 1.00 54.47  ?  549 ARG B N     1 
ATOM   10460 C  CA    . ARG B 1 530 ? 180.388 220.137 217.023 1.00 53.82  ?  549 ARG B CA    1 
ATOM   10461 C  C     . ARG B 1 530 ? 181.815 220.670 216.958 1.00 57.43  ?  549 ARG B C     1 
ATOM   10462 O  O     . ARG B 1 530 ? 182.520 220.701 217.972 1.00 59.85  ?  549 ARG B O     1 
ATOM   10463 C  CB    . ARG B 1 530 ? 180.333 218.681 216.559 1.00 55.99  ?  549 ARG B CB    1 
ATOM   10464 C  CG    . ARG B 1 530 ? 181.050 217.721 217.493 1.00 56.58  ?  549 ARG B CG    1 
ATOM   10465 C  CD    . ARG B 1 530 ? 180.648 216.277 217.246 1.00 60.33  ?  549 ARG B CD    1 
ATOM   10466 N  NE    . ARG B 1 530 ? 181.270 215.370 218.204 1.00 62.24  ?  549 ARG B NE    1 
ATOM   10467 C  CZ    . ARG B 1 530 ? 180.823 215.155 219.433 1.00 58.64  ?  549 ARG B CZ    1 
ATOM   10468 N  NH1   . ARG B 1 530 ? 179.745 215.768 219.894 1.00 52.20  1  549 ARG B NH1   1 
ATOM   10469 N  NH2   . ARG B 1 530 ? 181.473 214.303 220.221 1.00 62.34  ?  549 ARG B NH2   1 
ATOM   10470 N  N     . LEU B 1 531 ? 182.254 221.102 215.773 1.00 61.44  ?  550 LEU B N     1 
ATOM   10471 C  CA    . LEU B 1 531 ? 183.612 221.623 215.625 1.00 60.16  ?  550 LEU B CA    1 
ATOM   10472 C  C     . LEU B 1 531 ? 183.813 222.908 216.422 1.00 66.66  ?  550 LEU B C     1 
ATOM   10473 O  O     . LEU B 1 531 ? 184.842 223.077 217.089 1.00 68.96  ?  550 LEU B O     1 
ATOM   10474 C  CB    . LEU B 1 531 ? 183.923 221.857 214.147 1.00 62.30  ?  550 LEU B CB    1 
ATOM   10475 C  CG    . LEU B 1 531 ? 185.400 221.858 213.751 1.00 66.76  ?  550 LEU B CG    1 
ATOM   10476 C  CD1   . LEU B 1 531 ? 186.059 220.537 214.121 1.00 64.78  ?  550 LEU B CD1   1 
ATOM   10477 C  CD2   . LEU B 1 531 ? 185.556 222.140 212.264 1.00 66.46  ?  550 LEU B CD2   1 
ATOM   10478 N  N     . VAL B 1 532 ? 182.851 223.832 216.359 1.00 65.45  ?  551 VAL B N     1 
ATOM   10479 C  CA    . VAL B 1 532 ? 182.989 225.086 217.094 1.00 58.91  ?  551 VAL B CA    1 
ATOM   10480 C  C     . VAL B 1 532 ? 182.884 224.839 218.595 1.00 55.41  ?  551 VAL B C     1 
ATOM   10481 O  O     . VAL B 1 532 ? 183.566 225.495 219.390 1.00 58.67  ?  551 VAL B O     1 
ATOM   10482 C  CB    . VAL B 1 532 ? 181.966 226.129 216.598 1.00 60.07  ?  551 VAL B CB    1 
ATOM   10483 C  CG1   . VAL B 1 532 ? 180.543 225.724 216.935 1.00 61.32  ?  551 VAL B CG1   1 
ATOM   10484 C  CG2   . VAL B 1 532 ? 182.283 227.503 217.178 1.00 58.18  ?  551 VAL B CG2   1 
ATOM   10485 N  N     . LEU B 1 533 ? 182.049 223.880 219.008 1.00 49.98  ?  552 LEU B N     1 
ATOM   10486 C  CA    . LEU B 1 533 ? 181.999 223.502 220.415 1.00 51.68  ?  552 LEU B CA    1 
ATOM   10487 C  C     . LEU B 1 533 ? 183.333 222.927 220.872 1.00 52.96  ?  552 LEU B C     1 
ATOM   10488 O  O     . LEU B 1 533 ? 183.795 223.216 221.981 1.00 56.34  ?  552 LEU B O     1 
ATOM   10489 C  CB    . LEU B 1 533 ? 180.870 222.496 220.644 1.00 55.37  ?  552 LEU B CB    1 
ATOM   10490 C  CG    . LEU B 1 533 ? 180.871 221.701 221.952 1.00 49.98  ?  552 LEU B CG    1 
ATOM   10491 C  CD1   . LEU B 1 533 ? 180.751 222.621 223.157 1.00 49.75  ?  552 LEU B CD1   1 
ATOM   10492 C  CD2   . LEU B 1 533 ? 179.757 220.667 221.946 1.00 53.29  ?  552 LEU B CD2   1 
ATOM   10493 N  N     . GLY B 1 534 ? 183.968 222.111 220.030 1.00 55.39  ?  553 GLY B N     1 
ATOM   10494 C  CA    . GLY B 1 534 ? 185.273 221.576 220.378 1.00 54.79  ?  553 GLY B CA    1 
ATOM   10495 C  C     . GLY B 1 534 ? 186.340 222.649 220.472 1.00 55.12  ?  553 GLY B C     1 
ATOM   10496 O  O     . GLY B 1 534 ? 187.191 222.615 221.364 1.00 58.13  ?  553 GLY B O     1 
ATOM   10497 N  N     . ALA B 1 535 ? 186.316 223.610 219.546 1.00 60.07  ?  554 ALA B N     1 
ATOM   10498 C  CA    . ALA B 1 535 ? 187.257 224.724 219.617 1.00 61.56  ?  554 ALA B CA    1 
ATOM   10499 C  C     . ALA B 1 535 ? 187.035 225.550 220.879 1.00 60.09  ?  554 ALA B C     1 
ATOM   10500 O  O     . ALA B 1 535 ? 187.998 225.971 221.537 1.00 61.84  ?  554 ALA B O     1 
ATOM   10501 C  CB    . ALA B 1 535 ? 187.129 225.599 218.370 1.00 58.58  ?  554 ALA B CB    1 
ATOM   10502 N  N     . ALA B 1 536 ? 185.770 225.791 221.232 1.00 53.68  ?  555 ALA B N     1 
ATOM   10503 C  CA    . ALA B 1 536 ? 185.463 226.511 222.462 1.00 51.89  ?  555 ALA B CA    1 
ATOM   10504 C  C     . ALA B 1 536 ? 185.948 225.742 223.683 1.00 53.15  ?  555 ALA B C     1 
ATOM   10505 O  O     . ALA B 1 536 ? 186.477 226.334 224.628 1.00 57.83  ?  555 ALA B O     1 
ATOM   10506 C  CB    . ALA B 1 536 ? 183.962 226.779 222.555 1.00 55.22  ?  555 ALA B CB    1 
ATOM   10507 N  N     . LEU B 1 537 ? 185.774 224.419 223.682 1.00 52.47  ?  556 LEU B N     1 
ATOM   10508 C  CA    . LEU B 1 537 ? 186.264 223.606 224.791 1.00 50.91  ?  556 LEU B CA    1 
ATOM   10509 C  C     . LEU B 1 537 ? 187.782 223.677 224.893 1.00 52.94  ?  556 LEU B C     1 
ATOM   10510 O  O     . LEU B 1 537 ? 188.332 223.793 225.994 1.00 55.11  ?  556 LEU B O     1 
ATOM   10511 C  CB    . LEU B 1 537 ? 185.804 222.159 224.623 1.00 53.26  ?  556 LEU B CB    1 
ATOM   10512 C  CG    . LEU B 1 537 ? 186.405 221.132 225.584 1.00 50.40  ?  556 LEU B CG    1 
ATOM   10513 C  CD1   . LEU B 1 537 ? 186.014 221.445 227.020 1.00 51.42  ?  556 LEU B CD1   1 
ATOM   10514 C  CD2   . LEU B 1 537 ? 185.977 219.724 225.201 1.00 54.87  ?  556 LEU B CD2   1 
ATOM   10515 N  N     . LYS B 1 538 ? 188.473 223.610 223.754 1.00 61.93  ?  557 LYS B N     1 
ATOM   10516 C  CA    . LYS B 1 538 ? 189.930 223.697 223.760 1.00 60.34  ?  557 LYS B CA    1 
ATOM   10517 C  C     . LYS B 1 538 ? 190.402 225.031 224.324 1.00 62.93  ?  557 LYS B C     1 
ATOM   10518 O  O     . LYS B 1 538 ? 191.294 225.073 225.182 1.00 63.58  ?  557 LYS B O     1 
ATOM   10519 C  CB    . LYS B 1 538 ? 190.471 223.493 222.345 1.00 58.61  ?  557 LYS B CB    1 
ATOM   10520 C  CG    . LYS B 1 538 ? 191.972 223.690 222.218 1.00 61.48  ?  557 LYS B CG    1 
ATOM   10521 C  CD    . LYS B 1 538 ? 192.383 223.861 220.764 1.00 60.01  ?  557 LYS B CD    1 
ATOM   10522 C  CE    . LYS B 1 538 ? 192.049 222.626 219.946 1.00 60.16  ?  557 LYS B CE    1 
ATOM   10523 N  NZ    . LYS B 1 538 ? 193.043 221.539 220.157 1.00 58.42  1  557 LYS B NZ    1 
ATOM   10524 N  N     . GLU B 1 539 ? 189.803 226.135 223.867 1.00 63.97  ?  558 GLU B N     1 
ATOM   10525 C  CA    . GLU B 1 539 ? 190.231 227.439 224.363 1.00 61.34  ?  558 GLU B CA    1 
ATOM   10526 C  C     . GLU B 1 539 ? 189.851 227.637 225.826 1.00 63.53  ?  558 GLU B C     1 
ATOM   10527 O  O     . GLU B 1 539 ? 190.593 228.285 226.571 1.00 65.96  ?  558 GLU B O     1 
ATOM   10528 C  CB    . GLU B 1 539 ? 189.662 228.562 223.490 1.00 62.25  ?  558 GLU B CB    1 
ATOM   10529 C  CG    . GLU B 1 539 ? 188.151 228.694 223.497 1.00 65.08  ?  558 GLU B CG    1 
ATOM   10530 C  CD    . GLU B 1 539 ? 187.658 229.711 224.508 1.00 66.47  ?  558 GLU B CD    1 
ATOM   10531 O  OE1   . GLU B 1 539 ? 188.483 230.510 224.999 1.00 65.60  ?  558 GLU B OE1   1 
ATOM   10532 O  OE2   . GLU B 1 539 ? 186.447 229.711 224.812 1.00 65.98  -1 558 GLU B OE2   1 
ATOM   10533 N  N     . ALA B 1 540 ? 188.719 227.077 226.264 1.00 62.86  ?  559 ALA B N     1 
ATOM   10534 C  CA    . ALA B 1 540 ? 188.348 227.161 227.673 1.00 59.31  ?  559 ALA B CA    1 
ATOM   10535 C  C     . ALA B 1 540 ? 189.321 226.382 228.548 1.00 57.94  ?  559 ALA B C     1 
ATOM   10536 O  O     . ALA B 1 540 ? 189.677 226.835 229.641 1.00 63.89  ?  559 ALA B O     1 
ATOM   10537 C  CB    . ALA B 1 540 ? 186.920 226.655 227.872 1.00 59.04  ?  559 ALA B CB    1 
ATOM   10538 N  N     . ILE B 1 541 ? 189.752 225.204 228.092 1.00 59.31  ?  560 ILE B N     1 
ATOM   10539 C  CA    . ILE B 1 541 ? 190.761 224.447 228.829 1.00 62.70  ?  560 ILE B CA    1 
ATOM   10540 C  C     . ILE B 1 541 ? 192.066 225.227 228.890 1.00 63.52  ?  560 ILE B C     1 
ATOM   10541 O  O     . ILE B 1 541 ? 192.731 225.277 229.932 1.00 62.35  ?  560 ILE B O     1 
ATOM   10542 C  CB    . ILE B 1 541 ? 190.961 223.057 228.197 1.00 65.15  ?  560 ILE B CB    1 
ATOM   10543 C  CG1   . ILE B 1 541 ? 189.680 222.230 228.305 1.00 68.17  ?  560 ILE B CG1   1 
ATOM   10544 C  CG2   . ILE B 1 541 ? 192.115 222.325 228.866 1.00 62.72  ?  560 ILE B CG2   1 
ATOM   10545 C  CD1   . ILE B 1 541 ? 189.676 221.003 227.425 1.00 62.56  ?  560 ILE B CD1   1 
ATOM   10546 N  N     . SER B 1 542 ? 192.454 225.848 227.773 1.00 65.89  ?  561 SER B N     1 
ATOM   10547 C  CA    . SER B 1 542 ? 193.686 226.631 227.753 1.00 66.39  ?  561 SER B CA    1 
ATOM   10548 C  C     . SER B 1 542 ? 193.612 227.817 228.710 1.00 65.40  ?  561 SER B C     1 
ATOM   10549 O  O     . SER B 1 542 ? 194.582 228.116 229.416 1.00 64.88  ?  561 SER B O     1 
ATOM   10550 C  CB    . SER B 1 542 ? 193.980 227.107 226.331 1.00 68.31  ?  561 SER B CB    1 
ATOM   10551 O  OG    . SER B 1 542 ? 195.005 228.086 226.323 1.00 69.67  ?  561 SER B OG    1 
ATOM   10552 N  N     . ASN B 1 543 ? 192.471 228.502 228.749 1.00 64.19  ?  562 ASN B N     1 
ATOM   10553 C  CA    . ASN B 1 543 ? 192.308 229.714 229.542 1.00 63.05  ?  562 ASN B CA    1 
ATOM   10554 C  C     . ASN B 1 543 ? 191.763 229.451 230.942 1.00 62.92  ?  562 ASN B C     1 
ATOM   10555 O  O     . ASN B 1 543 ? 191.484 230.410 231.670 1.00 63.45  ?  562 ASN B O     1 
ATOM   10556 C  CB    . ASN B 1 543 ? 191.392 230.698 228.808 1.00 64.16  ?  562 ASN B CB    1 
ATOM   10557 C  CG    . ASN B 1 543 ? 191.869 231.000 227.401 1.00 68.97  ?  562 ASN B CG    1 
ATOM   10558 O  OD1   . ASN B 1 543 ? 193.069 231.109 227.151 1.00 68.76  ?  562 ASN B OD1   1 
ATOM   10559 N  ND2   . ASN B 1 543 ? 190.928 231.137 226.474 1.00 67.30  ?  562 ASN B ND2   1 
ATOM   10560 N  N     . ASN B 1 544 ? 191.589 228.184 231.324 1.00 61.55  ?  563 ASN B N     1 
ATOM   10561 C  CA    . ASN B 1 544 ? 191.135 227.810 232.667 1.00 63.70  ?  563 ASN B CA    1 
ATOM   10562 C  C     . ASN B 1 544 ? 189.733 228.347 232.956 1.00 65.05  ?  563 ASN B C     1 
ATOM   10563 O  O     . ASN B 1 544 ? 189.492 228.989 233.980 1.00 62.72  ?  563 ASN B O     1 
ATOM   10564 C  CB    . ASN B 1 544 ? 192.128 228.275 233.737 1.00 62.24  ?  563 ASN B CB    1 
ATOM   10565 C  CG    . ASN B 1 544 ? 191.942 227.556 235.060 1.00 67.53  ?  563 ASN B CG    1 
ATOM   10566 O  OD1   . ASN B 1 544 ? 191.007 226.773 235.231 1.00 66.19  ?  563 ASN B OD1   1 
ATOM   10567 N  ND2   . ASN B 1 544 ? 192.836 227.821 236.005 1.00 66.83  ?  563 ASN B ND2   1 
ATOM   10568 N  N     . GLN B 1 545 ? 188.796 228.086 232.043 1.00 64.36  ?  564 GLN B N     1 
ATOM   10569 C  CA    . GLN B 1 545 ? 187.401 228.459 232.240 1.00 60.98  ?  564 GLN B CA    1 
ATOM   10570 C  C     . GLN B 1 545 ? 186.560 227.344 232.845 1.00 61.73  ?  564 GLN B C     1 
ATOM   10571 O  O     . GLN B 1 545 ? 185.390 227.579 233.170 1.00 64.28  ?  564 GLN B O     1 
ATOM   10572 C  CB    . GLN B 1 545 ? 186.770 228.899 230.913 1.00 62.11  ?  564 GLN B CB    1 
ATOM   10573 C  CG    . GLN B 1 545 ? 187.330 230.195 230.353 1.00 63.71  ?  564 GLN B CG    1 
ATOM   10574 C  CD    . GLN B 1 545 ? 186.688 230.584 229.035 1.00 66.81  ?  564 GLN B CD    1 
ATOM   10575 O  OE1   . GLN B 1 545 ? 185.860 229.850 228.494 1.00 68.62  ?  564 GLN B OE1   1 
ATOM   10576 N  NE2   . GLN B 1 545 ? 187.063 231.746 228.515 1.00 65.08  ?  564 GLN B NE2   1 
ATOM   10577 N  N     . LEU B 1 546 ? 187.118 226.148 233.001 1.00 50.93  ?  565 LEU B N     1 
ATOM   10578 C  CA    . LEU B 1 546 ? 186.369 225.032 233.555 1.00 43.57  ?  565 LEU B CA    1 
ATOM   10579 C  C     . LEU B 1 546 ? 186.376 225.083 235.081 1.00 48.62  ?  565 LEU B C     1 
ATOM   10580 O  O     . LEU B 1 546 ? 187.167 225.794 235.706 1.00 59.50  ?  565 LEU B O     1 
ATOM   10581 C  CB    . LEU B 1 546 ? 186.944 223.702 233.069 1.00 40.51  ?  565 LEU B CB    1 
ATOM   10582 C  CG    . LEU B 1 546 ? 186.372 223.107 231.778 1.00 43.26  ?  565 LEU B CG    1 
ATOM   10583 C  CD1   . LEU B 1 546 ? 186.359 224.113 230.639 1.00 49.15  ?  565 LEU B CD1   1 
ATOM   10584 C  CD2   . LEU B 1 546 ? 187.151 221.865 231.380 1.00 44.25  ?  565 LEU B CD2   1 
ATOM   10585 N  N     . LYS B 1 547 ? 185.466 224.317 235.680 1.00 38.17  ?  566 LYS B N     1 
ATOM   10586 C  CA    . LYS B 1 547 ? 185.339 224.249 237.127 1.00 38.38  ?  566 LYS B CA    1 
ATOM   10587 C  C     . LYS B 1 547 ? 185.175 222.799 237.557 1.00 38.93  ?  566 LYS B C     1 
ATOM   10588 O  O     . LYS B 1 547 ? 184.878 221.922 236.742 1.00 48.64  ?  566 LYS B O     1 
ATOM   10589 C  CB    . LYS B 1 547 ? 184.150 225.078 237.629 1.00 40.30  ?  566 LYS B CB    1 
ATOM   10590 C  CG    . LYS B 1 547 ? 184.412 226.572 237.673 1.00 42.87  ?  566 LYS B CG    1 
ATOM   10591 C  CD    . LYS B 1 547 ? 183.161 227.336 238.071 1.00 48.35  ?  566 LYS B CD    1 
ATOM   10592 C  CE    . LYS B 1 547 ? 183.418 228.832 238.081 1.00 52.06  ?  566 LYS B CE    1 
ATOM   10593 N  NZ    . LYS B 1 547 ? 184.816 229.152 238.486 1.00 51.78  1  566 LYS B NZ    1 
ATOM   10594 N  N     . LEU B 1 548 ? 185.373 222.559 238.851 1.00 33.19  ?  567 LEU B N     1 
ATOM   10595 C  CA    . LEU B 1 548 ? 185.206 221.243 239.446 1.00 33.12  ?  567 LEU B CA    1 
ATOM   10596 C  C     . LEU B 1 548 ? 184.124 221.292 240.516 1.00 39.73  ?  567 LEU B C     1 
ATOM   10597 O  O     . LEU B 1 548 ? 183.982 222.284 241.237 1.00 39.89  ?  567 LEU B O     1 
ATOM   10598 C  CB    . LEU B 1 548 ? 186.517 220.735 240.061 1.00 37.33  ?  567 LEU B CB    1 
ATOM   10599 C  CG    . LEU B 1 548 ? 187.612 220.281 239.094 1.00 39.72  ?  567 LEU B CG    1 
ATOM   10600 C  CD1   . LEU B 1 548 ? 188.671 219.480 239.833 1.00 42.09  ?  567 LEU B CD1   1 
ATOM   10601 C  CD2   . LEU B 1 548 ? 187.021 219.465 237.957 1.00 42.80  ?  567 LEU B CD2   1 
ATOM   10602 N  N     . VAL B 1 549 ? 183.362 220.205 240.613 1.00 43.56  ?  568 VAL B N     1 
ATOM   10603 C  CA    . VAL B 1 549 ? 182.294 220.064 241.595 1.00 35.36  ?  568 VAL B CA    1 
ATOM   10604 C  C     . VAL B 1 549 ? 182.447 218.707 242.268 1.00 28.14  ?  568 VAL B C     1 
ATOM   10605 O  O     . VAL B 1 549 ? 182.767 217.711 241.610 1.00 37.62  ?  568 VAL B O     1 
ATOM   10606 C  CB    . VAL B 1 549 ? 180.902 220.221 240.944 1.00 42.44  ?  568 VAL B CB    1 
ATOM   10607 C  CG1   . VAL B 1 549 ? 179.808 219.985 241.953 1.00 49.45  ?  568 VAL B CG1   1 
ATOM   10608 C  CG2   . VAL B 1 549 ? 180.754 221.612 240.352 1.00 43.68  ?  568 VAL B CG2   1 
ATOM   10609 N  N     . TYR B 1 550 ? 182.218 218.668 243.579 1.00 28.27  ?  569 TYR B N     1 
ATOM   10610 C  CA    . TYR B 1 550 ? 182.593 217.535 244.414 1.00 32.19  ?  569 TYR B CA    1 
ATOM   10611 C  C     . TYR B 1 550 ? 181.365 216.872 245.023 1.00 39.68  ?  569 TYR B C     1 
ATOM   10612 O  O     . TYR B 1 550 ? 180.497 217.544 245.587 1.00 44.95  ?  569 TYR B O     1 
ATOM   10613 C  CB    . TYR B 1 550 ? 183.545 217.983 245.525 1.00 41.01  ?  569 TYR B CB    1 
ATOM   10614 C  CG    . TYR B 1 550 ? 184.784 218.678 245.010 1.00 40.94  ?  569 TYR B CG    1 
ATOM   10615 C  CD1   . TYR B 1 550 ? 185.899 217.953 244.616 1.00 39.63  ?  569 TYR B CD1   1 
ATOM   10616 C  CD2   . TYR B 1 550 ? 184.830 220.059 244.900 1.00 37.98  ?  569 TYR B CD2   1 
ATOM   10617 C  CE1   . TYR B 1 550 ? 187.030 218.584 244.140 1.00 36.33  ?  569 TYR B CE1   1 
ATOM   10618 C  CE2   . TYR B 1 550 ? 185.956 220.699 244.420 1.00 34.76  ?  569 TYR B CE2   1 
ATOM   10619 C  CZ    . TYR B 1 550 ? 187.053 219.957 244.045 1.00 35.24  ?  569 TYR B CZ    1 
ATOM   10620 O  OH    . TYR B 1 550 ? 188.177 220.591 243.570 1.00 51.56  ?  569 TYR B OH    1 
ATOM   10621 N  N     . GLN B 1 551 ? 181.309 215.549 244.914 1.00 46.33  ?  570 GLN B N     1 
ATOM   10622 C  CA    . GLN B 1 551 ? 180.214 214.751 245.467 1.00 37.29  ?  570 GLN B CA    1 
ATOM   10623 C  C     . GLN B 1 551 ? 180.714 213.924 246.643 1.00 33.79  ?  570 GLN B C     1 
ATOM   10624 O  O     . GLN B 1 551 ? 181.582 213.050 246.457 1.00 44.12  ?  570 GLN B O     1 
ATOM   10625 C  CB    . GLN B 1 551 ? 179.614 213.840 244.398 1.00 29.52  ?  570 GLN B CB    1 
ATOM   10626 C  CG    . GLN B 1 551 ? 178.530 212.915 244.920 1.00 35.10  ?  570 GLN B CG    1 
ATOM   10627 C  CD    . GLN B 1 551 ? 177.776 212.223 243.807 1.00 43.57  ?  570 GLN B CD    1 
ATOM   10628 O  OE1   . GLN B 1 551 ? 178.374 211.720 242.854 1.00 49.00  ?  570 GLN B OE1   1 
ATOM   10629 N  NE2   . GLN B 1 551 ? 176.454 212.193 243.918 1.00 47.18  ?  570 GLN B NE2   1 
ATOM   10630 N  N     . PRO B 1 552 ? 180.216 214.155 247.857 1.00 34.52  ?  571 PRO B N     1 
ATOM   10631 C  CA    . PRO B 1 552 ? 180.696 213.385 249.010 1.00 36.89  ?  571 PRO B CA    1 
ATOM   10632 C  C     . PRO B 1 552 ? 180.266 211.926 248.954 1.00 45.16  ?  571 PRO B C     1 
ATOM   10633 O  O     . PRO B 1 552 ? 179.224 211.578 248.394 1.00 56.27  ?  571 PRO B O     1 
ATOM   10634 C  CB    . PRO B 1 552 ? 180.063 214.106 250.208 1.00 46.48  ?  571 PRO B CB    1 
ATOM   10635 C  CG    . PRO B 1 552 ? 179.603 215.439 249.673 1.00 50.13  ?  571 PRO B CG    1 
ATOM   10636 C  CD    . PRO B 1 552 ? 179.240 215.181 248.251 1.00 47.50  ?  571 PRO B CD    1 
ATOM   10637 N  N     . GLN B 1 553 ? 181.094 211.071 249.548 1.00 45.33  ?  572 GLN B N     1 
ATOM   10638 C  CA    . GLN B 1 553 ? 180.790 209.662 249.744 1.00 46.39  ?  572 GLN B CA    1 
ATOM   10639 C  C     . GLN B 1 553 ? 180.820 209.351 251.234 1.00 50.86  ?  572 GLN B C     1 
ATOM   10640 O  O     . GLN B 1 553 ? 181.768 209.721 251.934 1.00 56.50  ?  572 GLN B O     1 
ATOM   10641 C  CB    . GLN B 1 553 ? 181.783 208.770 248.995 1.00 46.54  ?  572 GLN B CB    1 
ATOM   10642 C  CG    . GLN B 1 553 ? 182.348 209.399 247.736 1.00 47.14  ?  572 GLN B CG    1 
ATOM   10643 C  CD    . GLN B 1 553 ? 183.180 208.431 246.924 1.00 49.44  ?  572 GLN B CD    1 
ATOM   10644 O  OE1   . GLN B 1 553 ? 183.912 207.608 247.474 1.00 51.76  ?  572 GLN B OE1   1 
ATOM   10645 N  NE2   . GLN B 1 553 ? 183.077 208.526 245.605 1.00 51.20  ?  572 GLN B NE2   1 
ATOM   10646 N  N     . ILE B 1 554 ? 179.785 208.669 251.715 1.00 55.46  ?  573 ILE B N     1 
ATOM   10647 C  CA    . ILE B 1 554 ? 179.563 208.499 253.144 1.00 54.61  ?  573 ILE B CA    1 
ATOM   10648 C  C     . ILE B 1 554 ? 179.727 207.032 253.522 1.00 66.21  ?  573 ILE B C     1 
ATOM   10649 O  O     . ILE B 1 554 ? 179.570 206.129 252.693 1.00 68.99  ?  573 ILE B O     1 
ATOM   10650 C  CB    . ILE B 1 554 ? 178.169 209.025 253.553 1.00 52.00  ?  573 ILE B CB    1 
ATOM   10651 C  CG1   . ILE B 1 554 ? 178.184 209.506 255.003 1.00 61.41  ?  573 ILE B CG1   1 
ATOM   10652 C  CG2   . ILE B 1 554 ? 177.104 207.963 253.342 1.00 58.27  ?  573 ILE B CG2   1 
ATOM   10653 C  CD1   . ILE B 1 554 ? 179.046 210.724 255.218 1.00 64.04  ?  573 ILE B CD1   1 
ATOM   10654 N  N     . PHE B 1 555 ? 180.071 206.804 254.789 1.00 69.07  ?  574 PHE B N     1 
ATOM   10655 C  CA    . PHE B 1 555 ? 180.136 205.459 255.340 1.00 58.65  ?  574 PHE B CA    1 
ATOM   10656 C  C     . PHE B 1 555 ? 178.737 204.925 255.620 1.00 57.24  ?  574 PHE B C     1 
ATOM   10657 O  O     . PHE B 1 555 ? 177.802 205.682 255.897 1.00 60.63  ?  574 PHE B O     1 
ATOM   10658 C  CB    . PHE B 1 555 ? 180.962 205.438 256.627 1.00 56.28  ?  574 PHE B CB    1 
ATOM   10659 C  CG    . PHE B 1 555 ? 182.446 205.375 256.400 1.00 58.45  ?  574 PHE B CG    1 
ATOM   10660 C  CD1   . PHE B 1 555 ? 183.021 204.266 255.803 1.00 58.73  ?  574 PHE B CD1   1 
ATOM   10661 C  CD2   . PHE B 1 555 ? 183.268 206.414 256.800 1.00 65.34  ?  574 PHE B CD2   1 
ATOM   10662 C  CE1   . PHE B 1 555 ? 184.386 204.201 255.598 1.00 62.47  ?  574 PHE B CE1   1 
ATOM   10663 C  CE2   . PHE B 1 555 ? 184.633 206.355 256.598 1.00 65.87  ?  574 PHE B CE2   1 
ATOM   10664 C  CZ    . PHE B 1 555 ? 185.193 205.247 255.997 1.00 61.78  ?  574 PHE B CZ    1 
ATOM   10665 N  N     . ALA B 1 556 ? 178.599 203.601 255.532 1.00 69.09  ?  575 ALA B N     1 
ATOM   10666 C  CA    . ALA B 1 556 ? 177.302 202.975 255.770 1.00 71.93  ?  575 ALA B CA    1 
ATOM   10667 C  C     . ALA B 1 556 ? 176.857 203.141 257.218 1.00 75.02  ?  575 ALA B C     1 
ATOM   10668 O  O     . ALA B 1 556 ? 175.701 203.492 257.480 1.00 79.47  ?  575 ALA B O     1 
ATOM   10669 C  CB    . ALA B 1 556 ? 177.359 201.494 255.394 1.00 74.31  ?  575 ALA B CB    1 
ATOM   10670 N  N     . GLU B 1 557 ? 177.756 202.899 258.170 1.00 79.95  ?  576 GLU B N     1 
ATOM   10671 C  CA    . GLU B 1 557 ? 177.403 202.907 259.585 1.00 81.25  ?  576 GLU B CA    1 
ATOM   10672 C  C     . GLU B 1 557 ? 177.687 204.241 260.266 1.00 80.23  ?  576 GLU B C     1 
ATOM   10673 O  O     . GLU B 1 557 ? 176.768 204.877 260.790 1.00 77.80  ?  576 GLU B O     1 
ATOM   10674 C  CB    . GLU B 1 557 ? 178.151 201.784 260.314 1.00 82.84  ?  576 GLU B CB    1 
ATOM   10675 C  CG    . GLU B 1 557 ? 178.278 200.499 259.511 1.00 81.25  ?  576 GLU B CG    1 
ATOM   10676 C  CD    . GLU B 1 557 ? 176.948 199.798 259.322 1.00 83.35  ?  576 GLU B CD    1 
ATOM   10677 O  OE1   . GLU B 1 557 ? 176.106 199.865 260.242 1.00 82.27  ?  576 GLU B OE1   1 
ATOM   10678 O  OE2   . GLU B 1 557 ? 176.744 199.180 258.256 1.00 83.62  -1 576 GLU B OE2   1 
ATOM   10679 N  N     . THR B 1 558 ? 178.944 204.680 260.265 1.00 74.45  ?  577 THR B N     1 
ATOM   10680 C  CA    . THR B 1 558 ? 179.365 205.847 261.031 1.00 72.35  ?  577 THR B CA    1 
ATOM   10681 C  C     . THR B 1 558 ? 178.859 207.167 260.465 1.00 75.44  ?  577 THR B C     1 
ATOM   10682 O  O     . THR B 1 558 ? 178.817 208.158 261.202 1.00 78.28  ?  577 THR B O     1 
ATOM   10683 C  CB    . THR B 1 558 ? 180.894 205.898 261.117 1.00 72.09  ?  577 THR B CB    1 
ATOM   10684 O  OG1   . THR B 1 558 ? 181.437 206.165 259.818 1.00 74.15  ?  577 THR B OG1   1 
ATOM   10685 C  CG2   . THR B 1 558 ? 181.442 204.575 261.626 1.00 75.32  ?  577 THR B CG2   1 
ATOM   10686 N  N     . GLY B 1 559 ? 178.478 207.212 259.191 1.00 76.51  ?  578 GLY B N     1 
ATOM   10687 C  CA    . GLY B 1 559 ? 178.096 208.466 258.573 1.00 74.67  ?  578 GLY B CA    1 
ATOM   10688 C  C     . GLY B 1 559 ? 179.243 209.454 258.507 1.00 75.43  ?  578 GLY B C     1 
ATOM   10689 O  O     . GLY B 1 559 ? 179.066 210.647 258.770 1.00 74.46  ?  578 GLY B O     1 
ATOM   10690 N  N     . GLU B 1 560 ? 180.427 208.961 258.152 1.00 66.06  ?  579 GLU B N     1 
ATOM   10691 C  CA    . GLU B 1 560 ? 181.629 209.772 258.038 1.00 62.67  ?  579 GLU B CA    1 
ATOM   10692 C  C     . GLU B 1 560 ? 182.048 209.829 256.574 1.00 61.96  ?  579 GLU B C     1 
ATOM   10693 O  O     . GLU B 1 560 ? 181.787 208.902 255.804 1.00 69.39  ?  579 GLU B O     1 
ATOM   10694 C  CB    . GLU B 1 560 ? 182.764 209.197 258.905 1.00 65.61  ?  579 GLU B CB    1 
ATOM   10695 C  CG    . GLU B 1 560 ? 184.088 209.945 258.826 1.00 67.78  ?  579 GLU B CG    1 
ATOM   10696 C  CD    . GLU B 1 560 ? 183.971 211.392 259.261 1.00 73.19  ?  579 GLU B CD    1 
ATOM   10697 O  OE1   . GLU B 1 560 ? 184.617 212.257 258.633 1.00 72.79  ?  579 GLU B OE1   1 
ATOM   10698 O  OE2   . GLU B 1 560 ? 183.236 211.666 260.233 1.00 72.13  -1 579 GLU B OE2   1 
ATOM   10699 N  N     . LEU B 1 561 ? 182.681 210.933 256.187 1.00 57.68  ?  580 LEU B N     1 
ATOM   10700 C  CA    . LEU B 1 561 ? 183.031 211.161 254.789 1.00 59.49  ?  580 LEU B CA    1 
ATOM   10701 C  C     . LEU B 1 561 ? 184.284 210.366 254.442 1.00 59.57  ?  580 LEU B C     1 
ATOM   10702 O  O     . LEU B 1 561 ? 185.378 210.663 254.934 1.00 67.56  ?  580 LEU B O     1 
ATOM   10703 C  CB    . LEU B 1 561 ? 183.215 212.653 254.523 1.00 62.10  ?  580 LEU B CB    1 
ATOM   10704 C  CG    . LEU B 1 561 ? 183.435 213.097 253.075 1.00 63.70  ?  580 LEU B CG    1 
ATOM   10705 C  CD1   . LEU B 1 561 ? 182.862 214.477 252.865 1.00 62.34  ?  580 LEU B CD1   1 
ATOM   10706 C  CD2   . LEU B 1 561 ? 184.916 213.119 252.740 1.00 62.49  ?  580 LEU B CD2   1 
ATOM   10707 N  N     . TYR B 1 562 ? 184.119 209.349 253.592 1.00 52.31  ?  581 TYR B N     1 
ATOM   10708 C  CA    . TYR B 1 562 ? 185.265 208.590 253.100 1.00 57.26  ?  581 TYR B CA    1 
ATOM   10709 C  C     . TYR B 1 562 ? 186.081 209.405 252.106 1.00 60.27  ?  581 TYR B C     1 
ATOM   10710 O  O     . TYR B 1 562 ? 187.316 209.382 252.140 1.00 64.31  ?  581 TYR B O     1 
ATOM   10711 C  CB    . TYR B 1 562 ? 184.785 207.288 252.462 1.00 63.84  ?  581 TYR B CB    1 
ATOM   10712 C  CG    . TYR B 1 562 ? 185.859 206.510 251.737 1.00 63.80  ?  581 TYR B CG    1 
ATOM   10713 C  CD1   . TYR B 1 562 ? 186.980 206.040 252.407 1.00 61.85  ?  581 TYR B CD1   1 
ATOM   10714 C  CD2   . TYR B 1 562 ? 185.743 206.232 250.380 1.00 62.70  ?  581 TYR B CD2   1 
ATOM   10715 C  CE1   . TYR B 1 562 ? 187.961 205.325 251.744 1.00 62.31  ?  581 TYR B CE1   1 
ATOM   10716 C  CE2   . TYR B 1 562 ? 186.717 205.518 249.710 1.00 65.27  ?  581 TYR B CE2   1 
ATOM   10717 C  CZ    . TYR B 1 562 ? 187.823 205.067 250.396 1.00 64.37  ?  581 TYR B CZ    1 
ATOM   10718 O  OH    . TYR B 1 562 ? 188.794 204.355 249.729 1.00 61.83  ?  581 TYR B OH    1 
ATOM   10719 N  N     . GLY B 1 563 ? 185.409 210.130 251.223 1.00 54.59  ?  582 GLY B N     1 
ATOM   10720 C  CA    . GLY B 1 563 ? 186.098 210.937 250.234 1.00 56.36  ?  582 GLY B CA    1 
ATOM   10721 C  C     . GLY B 1 563 ? 185.092 211.689 249.395 1.00 52.98  ?  582 GLY B C     1 
ATOM   10722 O  O     . GLY B 1 563 ? 183.876 211.522 249.535 1.00 57.65  ?  582 GLY B O     1 
ATOM   10723 N  N     . ILE B 1 564 ? 185.621 212.538 248.520 1.00 40.18  ?  583 ILE B N     1 
ATOM   10724 C  CA    . ILE B 1 564 ? 184.808 213.264 247.551 1.00 38.89  ?  583 ILE B CA    1 
ATOM   10725 C  C     . ILE B 1 564 ? 185.381 213.009 246.166 1.00 42.57  ?  583 ILE B C     1 
ATOM   10726 O  O     . ILE B 1 564 ? 186.581 212.766 246.016 1.00 51.60  ?  583 ILE B O     1 
ATOM   10727 C  CB    . ILE B 1 564 ? 184.754 214.777 247.846 1.00 40.46  ?  583 ILE B CB    1 
ATOM   10728 C  CG1   . ILE B 1 564 ? 186.138 215.320 248.178 1.00 40.49  ?  583 ILE B CG1   1 
ATOM   10729 C  CG2   . ILE B 1 564 ? 183.816 215.066 248.999 1.00 48.29  ?  583 ILE B CG2   1 
ATOM   10730 C  CD1   . ILE B 1 564 ? 186.171 216.826 248.227 1.00 42.92  ?  583 ILE B CD1   1 
ATOM   10731 N  N     . GLU B 1 565 ? 184.521 213.063 245.154 1.00 34.21  ?  584 GLU B N     1 
ATOM   10732 C  CA    . GLU B 1 565 ? 184.924 212.863 243.769 1.00 30.74  ?  584 GLU B CA    1 
ATOM   10733 C  C     . GLU B 1 565 ? 184.854 214.187 243.023 1.00 36.50  ?  584 GLU B C     1 
ATOM   10734 O  O     . GLU B 1 565 ? 183.855 214.906 243.122 1.00 46.91  ?  584 GLU B O     1 
ATOM   10735 C  CB    . GLU B 1 565 ? 184.029 211.828 243.088 1.00 32.81  ?  584 GLU B CB    1 
ATOM   10736 C  CG    . GLU B 1 565 ? 184.365 211.586 241.626 1.00 36.27  ?  584 GLU B CG    1 
ATOM   10737 C  CD    . GLU B 1 565 ? 184.018 210.184 241.171 1.00 44.81  ?  584 GLU B CD    1 
ATOM   10738 O  OE1   . GLU B 1 565 ? 184.294 209.227 241.925 1.00 50.92  ?  584 GLU B OE1   1 
ATOM   10739 O  OE2   . GLU B 1 565 ? 183.468 210.038 240.059 1.00 46.03  -1 584 GLU B OE2   1 
ATOM   10740 N  N     . ALA B 1 566 ? 185.907 214.503 242.271 1.00 34.72  ?  585 ALA B N     1 
ATOM   10741 C  CA    . ALA B 1 566 ? 185.955 215.730 241.483 1.00 39.05  ?  585 ALA B CA    1 
ATOM   10742 C  C     . ALA B 1 566 ? 185.324 215.458 240.123 1.00 37.13  ?  585 ALA B C     1 
ATOM   10743 O  O     . ALA B 1 566 ? 185.768 214.570 239.389 1.00 40.68  ?  585 ALA B O     1 
ATOM   10744 C  CB    . ALA B 1 566 ? 187.393 216.223 241.338 1.00 42.51  ?  585 ALA B CB    1 
ATOM   10745 N  N     . LEU B 1 567 ? 184.290 216.223 239.788 1.00 34.08  ?  586 LEU B N     1 
ATOM   10746 C  CA    . LEU B 1 567 ? 183.573 216.077 238.529 1.00 31.01  ?  586 LEU B CA    1 
ATOM   10747 C  C     . LEU B 1 567 ? 183.683 217.369 237.729 1.00 35.78  ?  586 LEU B C     1 
ATOM   10748 O  O     . LEU B 1 567 ? 183.358 218.449 238.235 1.00 48.11  ?  586 LEU B O     1 
ATOM   10749 C  CB    . LEU B 1 567 ? 182.105 215.723 238.777 1.00 34.49  ?  586 LEU B CB    1 
ATOM   10750 C  CG    . LEU B 1 567 ? 181.845 214.536 239.707 1.00 33.66  ?  586 LEU B CG    1 
ATOM   10751 C  CD1   . LEU B 1 567 ? 180.449 214.608 240.303 1.00 33.29  ?  586 LEU B CD1   1 
ATOM   10752 C  CD2   . LEU B 1 567 ? 182.039 213.227 238.958 1.00 41.81  ?  586 LEU B CD2   1 
ATOM   10753 N  N     . ALA B 1 568 ? 184.140 217.252 236.486 1.00 36.71  ?  587 ALA B N     1 
ATOM   10754 C  CA    . ALA B 1 568 ? 184.367 218.421 235.651 1.00 33.61  ?  587 ALA B CA    1 
ATOM   10755 C  C     . ALA B 1 568 ? 183.051 219.092 235.275 1.00 37.45  ?  587 ALA B C     1 
ATOM   10756 O  O     . ALA B 1 568 ? 182.062 218.434 234.941 1.00 44.89  ?  587 ALA B O     1 
ATOM   10757 C  CB    . ALA B 1 568 ? 185.134 218.032 234.389 1.00 42.91  ?  587 ALA B CB    1 
ATOM   10758 N  N     . ARG B 1 569 ? 183.051 220.422 235.333 1.00 35.03  ?  588 ARG B N     1 
ATOM   10759 C  CA    . ARG B 1 569 ? 181.909 221.224 234.925 1.00 30.26  ?  588 ARG B CA    1 
ATOM   10760 C  C     . ARG B 1 569 ? 182.408 222.391 234.087 1.00 33.49  ?  588 ARG B C     1 
ATOM   10761 O  O     . ARG B 1 569 ? 183.523 222.884 234.274 1.00 52.39  ?  588 ARG B O     1 
ATOM   10762 C  CB    . ARG B 1 569 ? 181.110 221.741 236.129 1.00 37.26  ?  588 ARG B CB    1 
ATOM   10763 C  CG    . ARG B 1 569 ? 180.456 220.656 236.966 1.00 39.88  ?  588 ARG B CG    1 
ATOM   10764 C  CD    . ARG B 1 569 ? 179.290 219.998 236.248 1.00 33.96  ?  588 ARG B CD    1 
ATOM   10765 N  NE    . ARG B 1 569 ? 178.528 219.136 237.144 1.00 28.36  ?  588 ARG B NE    1 
ATOM   10766 C  CZ    . ARG B 1 569 ? 178.714 217.830 237.272 1.00 34.92  ?  588 ARG B CZ    1 
ATOM   10767 N  NH1   . ARG B 1 569 ? 179.645 217.193 236.583 1.00 39.14  1  588 ARG B NH1   1 
ATOM   10768 N  NH2   . ARG B 1 569 ? 177.945 217.145 238.114 1.00 40.59  ?  588 ARG B NH2   1 
ATOM   10769 N  N     . TRP B 1 570 ? 181.566 222.833 233.157 1.00 33.06  ?  589 TRP B N     1 
ATOM   10770 C  CA    . TRP B 1 570 ? 181.943 223.895 232.237 1.00 35.36  ?  589 TRP B CA    1 
ATOM   10771 C  C     . TRP B 1 570 ? 180.748 224.810 232.021 1.00 40.75  ?  589 TRP B C     1 
ATOM   10772 O  O     . TRP B 1 570 ? 179.624 224.339 231.825 1.00 46.79  ?  589 TRP B O     1 
ATOM   10773 C  CB    . TRP B 1 570 ? 182.427 223.312 230.904 1.00 37.70  ?  589 TRP B CB    1 
ATOM   10774 C  CG    . TRP B 1 570 ? 182.757 224.324 229.848 1.00 40.77  ?  589 TRP B CG    1 
ATOM   10775 C  CD1   . TRP B 1 570 ? 183.122 225.626 230.034 1.00 45.19  ?  589 TRP B CD1   1 
ATOM   10776 C  CD2   . TRP B 1 570 ? 182.745 224.110 228.433 1.00 29.06  ?  589 TRP B CD2   1 
ATOM   10777 N  NE1   . TRP B 1 570 ? 183.340 226.234 228.821 1.00 49.46  ?  589 TRP B NE1   1 
ATOM   10778 C  CE2   . TRP B 1 570 ? 183.115 225.324 227.823 1.00 36.17  ?  589 TRP B CE2   1 
ATOM   10779 C  CE3   . TRP B 1 570 ? 182.458 223.008 227.623 1.00 29.44  ?  589 TRP B CE3   1 
ATOM   10780 C  CZ2   . TRP B 1 570 ? 183.206 225.466 226.442 1.00 40.66  ?  589 TRP B CZ2   1 
ATOM   10781 C  CZ3   . TRP B 1 570 ? 182.549 223.151 226.253 1.00 32.04  ?  589 TRP B CZ3   1 
ATOM   10782 C  CH2   . TRP B 1 570 ? 182.919 224.370 225.676 1.00 39.72  ?  589 TRP B CH2   1 
ATOM   10783 N  N     . HIS B 1 571 ? 180.998 226.118 232.054 1.00 46.26  ?  590 HIS B N     1 
ATOM   10784 C  CA    . HIS B 1 571 ? 179.954 227.106 231.792 1.00 47.61  ?  590 HIS B CA    1 
ATOM   10785 C  C     . HIS B 1 571 ? 180.468 228.042 230.702 1.00 51.56  ?  590 HIS B C     1 
ATOM   10786 O  O     . HIS B 1 571 ? 181.318 228.896 230.968 1.00 58.65  ?  590 HIS B O     1 
ATOM   10787 C  CB    . HIS B 1 571 ? 179.585 227.873 233.053 1.00 51.02  ?  590 HIS B CB    1 
ATOM   10788 C  CG    . HIS B 1 571 ? 178.536 228.918 232.834 1.00 55.28  ?  590 HIS B CG    1 
ATOM   10789 N  ND1   . HIS B 1 571 ? 177.198 228.689 233.071 1.00 56.36  ?  590 HIS B ND1   1 
ATOM   10790 C  CD2   . HIS B 1 571 ? 178.627 230.193 232.390 1.00 53.77  ?  590 HIS B CD2   1 
ATOM   10791 C  CE1   . HIS B 1 571 ? 176.510 229.780 232.787 1.00 55.69  ?  590 HIS B CE1   1 
ATOM   10792 N  NE2   . HIS B 1 571 ? 177.353 230.708 232.371 1.00 57.80  ?  590 HIS B NE2   1 
ATOM   10793 N  N     . ASP B 1 572 ? 179.947 227.877 229.489 1.00 55.40  ?  591 ASP B N     1 
ATOM   10794 C  CA    . ASP B 1 572 ? 180.324 228.747 228.382 1.00 57.49  ?  591 ASP B CA    1 
ATOM   10795 C  C     . ASP B 1 572 ? 179.183 229.709 228.059 1.00 60.53  ?  591 ASP B C     1 
ATOM   10796 O  O     . ASP B 1 572 ? 178.016 229.306 228.052 1.00 62.84  ?  591 ASP B O     1 
ATOM   10797 C  CB    . ASP B 1 572 ? 180.671 227.925 227.144 1.00 55.16  ?  591 ASP B CB    1 
ATOM   10798 C  CG    . ASP B 1 572 ? 181.216 228.774 226.013 1.00 60.67  ?  591 ASP B CG    1 
ATOM   10799 O  OD1   . ASP B 1 572 ? 182.432 229.062 226.016 1.00 61.53  ?  591 ASP B OD1   1 
ATOM   10800 O  OD2   . ASP B 1 572 ? 180.431 229.154 225.119 1.00 64.12  -1 591 ASP B OD2   1 
ATOM   10801 N  N     . PRO B 1 573 ? 179.499 230.983 227.804 1.00 59.20  ?  592 PRO B N     1 
ATOM   10802 C  CA    . PRO B 1 573 ? 178.427 231.967 227.567 1.00 57.98  ?  592 PRO B CA    1 
ATOM   10803 C  C     . PRO B 1 573 ? 177.516 231.617 226.403 1.00 58.10  ?  592 PRO B C     1 
ATOM   10804 O  O     . PRO B 1 573 ? 176.308 231.878 226.469 1.00 62.97  ?  592 PRO B O     1 
ATOM   10805 C  CB    . PRO B 1 573 ? 179.204 233.265 227.309 1.00 57.87  ?  592 PRO B CB    1 
ATOM   10806 C  CG    . PRO B 1 573 ? 180.498 233.074 228.026 1.00 61.99  ?  592 PRO B CG    1 
ATOM   10807 C  CD    . PRO B 1 573 ? 180.827 231.616 227.882 1.00 59.68  ?  592 PRO B CD    1 
ATOM   10808 N  N     . LEU B 1 574 ? 178.057 231.030 225.335 1.00 55.62  ?  593 LEU B N     1 
ATOM   10809 C  CA    . LEU B 1 574 ? 177.242 230.735 224.161 1.00 54.32  ?  593 LEU B CA    1 
ATOM   10810 C  C     . LEU B 1 574 ? 176.455 229.440 224.334 1.00 57.32  ?  593 LEU B C     1 
ATOM   10811 O  O     . LEU B 1 574 ? 175.264 229.383 224.011 1.00 58.22  ?  593 LEU B O     1 
ATOM   10812 C  CB    . LEU B 1 574 ? 178.123 230.665 222.911 1.00 59.34  ?  593 LEU B CB    1 
ATOM   10813 C  CG    . LEU B 1 574 ? 178.460 231.989 222.219 1.00 62.70  ?  593 LEU B CG    1 
ATOM   10814 C  CD1   . LEU B 1 574 ? 179.523 232.761 222.988 1.00 59.45  ?  593 LEU B CD1   1 
ATOM   10815 C  CD2   . LEU B 1 574 ? 178.904 231.746 220.782 1.00 60.00  ?  593 LEU B CD2   1 
ATOM   10816 N  N     . HIS B 1 575 ? 177.101 228.393 224.842 1.00 57.94  ?  594 HIS B N     1 
ATOM   10817 C  CA    . HIS B 1 575 ? 176.483 227.078 224.960 1.00 57.42  ?  594 HIS B CA    1 
ATOM   10818 C  C     . HIS B 1 575 ? 175.865 226.819 226.328 1.00 56.48  ?  594 HIS B C     1 
ATOM   10819 O  O     . HIS B 1 575 ? 175.330 225.728 226.549 1.00 58.57  ?  594 HIS B O     1 
ATOM   10820 C  CB    . HIS B 1 575 ? 177.512 225.986 224.649 1.00 53.43  ?  594 HIS B CB    1 
ATOM   10821 C  CG    . HIS B 1 575 ? 178.291 226.229 223.395 1.00 54.07  ?  594 HIS B CG    1 
ATOM   10822 N  ND1   . HIS B 1 575 ? 179.403 227.042 223.357 1.00 54.18  ?  594 HIS B ND1   1 
ATOM   10823 C  CD2   . HIS B 1 575 ? 178.119 225.767 222.134 1.00 57.23  ?  594 HIS B CD2   1 
ATOM   10824 C  CE1   . HIS B 1 575 ? 179.883 227.071 222.127 1.00 55.71  ?  594 HIS B CE1   1 
ATOM   10825 N  NE2   . HIS B 1 575 ? 179.122 226.306 221.365 1.00 58.36  ?  594 HIS B NE2   1 
ATOM   10826 N  N     . GLY B 1 576 ? 175.914 227.786 227.242 1.00 51.72  ?  595 GLY B N     1 
ATOM   10827 C  CA    . GLY B 1 576 ? 175.369 227.559 228.572 1.00 47.83  ?  595 GLY B CA    1 
ATOM   10828 C  C     . GLY B 1 576 ? 176.136 226.483 229.317 1.00 48.46  ?  595 GLY B C     1 
ATOM   10829 O  O     . GLY B 1 576 ? 177.369 226.508 229.403 1.00 50.39  ?  595 GLY B O     1 
ATOM   10830 N  N     . HIS B 1 577 ? 175.399 225.525 229.872 1.00 40.39  ?  596 HIS B N     1 
ATOM   10831 C  CA    . HIS B 1 577 ? 175.979 224.420 230.624 1.00 40.04  ?  596 HIS B CA    1 
ATOM   10832 C  C     . HIS B 1 577 ? 176.155 223.225 229.697 1.00 41.81  ?  596 HIS B C     1 
ATOM   10833 O  O     . HIS B 1 577 ? 175.190 222.769 229.075 1.00 42.52  ?  596 HIS B O     1 
ATOM   10834 C  CB    . HIS B 1 577 ? 175.101 224.050 231.818 1.00 35.25  ?  596 HIS B CB    1 
ATOM   10835 C  CG    . HIS B 1 577 ? 174.990 225.133 232.845 1.00 43.90  ?  596 HIS B CG    1 
ATOM   10836 N  ND1   . HIS B 1 577 ? 174.162 226.224 232.688 1.00 48.58  ?  596 HIS B ND1   1 
ATOM   10837 C  CD2   . HIS B 1 577 ? 175.604 225.295 234.041 1.00 50.00  ?  596 HIS B CD2   1 
ATOM   10838 C  CE1   . HIS B 1 577 ? 174.269 227.010 233.744 1.00 48.57  ?  596 HIS B CE1   1 
ATOM   10839 N  NE2   . HIS B 1 577 ? 175.138 226.470 234.580 1.00 51.02  ?  596 HIS B NE2   1 
ATOM   10840 N  N     . VAL B 1 578 ? 177.384 222.724 229.604 1.00 32.51  ?  597 VAL B N     1 
ATOM   10841 C  CA    . VAL B 1 578 ? 177.715 221.585 228.753 1.00 31.71  ?  597 VAL B CA    1 
ATOM   10842 C  C     . VAL B 1 578 ? 177.932 220.376 229.659 1.00 34.05  ?  597 VAL B C     1 
ATOM   10843 O  O     . VAL B 1 578 ? 178.855 220.398 230.492 1.00 42.30  ?  597 VAL B O     1 
ATOM   10844 C  CB    . VAL B 1 578 ? 178.951 221.863 227.889 1.00 37.99  ?  597 VAL B CB    1 
ATOM   10845 C  CG1   . VAL B 1 578 ? 179.290 220.646 227.045 1.00 39.07  ?  597 VAL B CG1   1 
ATOM   10846 C  CG2   . VAL B 1 578 ? 178.721 223.082 227.009 1.00 39.47  ?  597 VAL B CG2   1 
ATOM   10847 N  N     . PRO B 1 579 ? 177.127 219.319 229.543 1.00 32.78  ?  598 PRO B N     1 
ATOM   10848 C  CA    . PRO B 1 579 ? 177.268 218.190 230.460 1.00 29.35  ?  598 PRO B CA    1 
ATOM   10849 C  C     . PRO B 1 579 ? 178.582 217.463 230.244 1.00 38.65  ?  598 PRO B C     1 
ATOM   10850 O  O     . PRO B 1 579 ? 179.139 217.465 229.130 1.00 49.44  ?  598 PRO B O     1 
ATOM   10851 C  CB    . PRO B 1 579 ? 176.067 217.293 230.106 1.00 33.52  ?  598 PRO B CB    1 
ATOM   10852 C  CG    . PRO B 1 579 ? 175.132 218.171 229.341 1.00 39.43  ?  598 PRO B CG    1 
ATOM   10853 C  CD    . PRO B 1 579 ? 175.995 219.147 228.620 1.00 42.14  ?  598 PRO B CD    1 
ATOM   10854 N  N     . PRO B 1 580 ? 179.132 216.843 231.292 1.00 21.64  ?  599 PRO B N     1 
ATOM   10855 C  CA    . PRO B 1 580 ? 180.321 216.001 231.100 1.00 18.24  ?  599 PRO B CA    1 
ATOM   10856 C  C     . PRO B 1 580 ? 180.106 214.888 230.098 1.00 20.08  ?  599 PRO B C     1 
ATOM   10857 O  O     . PRO B 1 580 ? 181.000 214.615 229.288 1.00 32.43  ?  599 PRO B O     1 
ATOM   10858 C  CB    . PRO B 1 580 ? 180.590 215.449 232.506 1.00 25.43  ?  599 PRO B CB    1 
ATOM   10859 C  CG    . PRO B 1 580 ? 179.965 216.427 233.424 1.00 27.69  ?  599 PRO B CG    1 
ATOM   10860 C  CD    . PRO B 1 580 ? 178.769 216.981 232.712 1.00 22.35  ?  599 PRO B CD    1 
ATOM   10861 N  N     . SER B 1 581 ? 178.934 214.261 230.099 1.00 28.66  ?  600 SER B N     1 
ATOM   10862 C  CA    . SER B 1 581 ? 178.629 213.218 229.126 1.00 31.64  ?  600 SER B CA    1 
ATOM   10863 C  C     . SER B 1 581 ? 178.591 213.742 227.709 1.00 28.14  ?  600 SER B C     1 
ATOM   10864 O  O     . SER B 1 581 ? 178.622 212.953 226.755 1.00 37.58  ?  600 SER B O     1 
ATOM   10865 C  CB    . SER B 1 581 ? 177.297 212.552 229.473 1.00 38.61  ?  600 SER B CB    1 
ATOM   10866 O  OG    . SER B 1 581 ? 177.028 211.468 228.601 1.00 45.80  ?  600 SER B OG    1 
ATOM   10867 N  N     . ARG B 1 582 ? 178.522 215.059 227.564 1.00 24.40  ?  601 ARG B N     1 
ATOM   10868 C  CA    . ARG B 1 582 ? 178.517 215.720 226.268 1.00 34.23  ?  601 ARG B CA    1 
ATOM   10869 C  C     . ARG B 1 582 ? 179.888 216.215 225.836 1.00 43.79  ?  601 ARG B C     1 
ATOM   10870 O  O     . ARG B 1 582 ? 180.187 216.201 224.639 1.00 45.70  ?  601 ARG B O     1 
ATOM   10871 C  CB    . ARG B 1 582 ? 177.530 216.898 226.287 1.00 40.53  ?  601 ARG B CB    1 
ATOM   10872 C  CG    . ARG B 1 582 ? 177.364 217.615 224.956 1.00 43.83  ?  601 ARG B CG    1 
ATOM   10873 C  CD    . ARG B 1 582 ? 176.279 218.677 225.049 1.00 40.83  ?  601 ARG B CD    1 
ATOM   10874 N  NE    . ARG B 1 582 ? 176.310 219.600 223.921 1.00 44.03  ?  601 ARG B NE    1 
ATOM   10875 C  CZ    . ARG B 1 582 ? 175.792 219.343 222.728 1.00 49.09  ?  601 ARG B CZ    1 
ATOM   10876 N  NH1   . ARG B 1 582 ? 175.187 218.195 222.469 1.00 45.18  1  601 ARG B NH1   1 
ATOM   10877 N  NH2   . ARG B 1 582 ? 175.878 220.264 221.772 1.00 48.46  ?  601 ARG B NH2   1 
ATOM   10878 N  N     . PHE B 1 583 ? 180.743 216.645 226.768 1.00 37.56  ?  602 PHE B N     1 
ATOM   10879 C  CA    . PHE B 1 583 ? 182.028 217.215 226.373 1.00 22.90  ?  602 PHE B CA    1 
ATOM   10880 C  C     . PHE B 1 583 ? 183.218 216.291 226.622 1.00 34.57  ?  602 PHE B C     1 
ATOM   10881 O  O     . PHE B 1 583 ? 184.322 216.602 226.163 1.00 51.00  ?  602 PHE B O     1 
ATOM   10882 C  CB    . PHE B 1 583 ? 182.248 218.581 227.054 1.00 28.28  ?  602 PHE B CB    1 
ATOM   10883 C  CG    . PHE B 1 583 ? 182.880 218.517 228.423 1.00 33.38  ?  602 PHE B CG    1 
ATOM   10884 C  CD1   . PHE B 1 583 ? 184.260 218.468 228.572 1.00 43.05  ?  602 PHE B CD1   1 
ATOM   10885 C  CD2   . PHE B 1 583 ? 182.096 218.560 229.560 1.00 34.97  ?  602 PHE B CD2   1 
ATOM   10886 C  CE1   . PHE B 1 583 ? 184.836 218.425 229.825 1.00 44.75  ?  602 PHE B CE1   1 
ATOM   10887 C  CE2   . PHE B 1 583 ? 182.670 218.520 230.816 1.00 36.14  ?  602 PHE B CE2   1 
ATOM   10888 C  CZ    . PHE B 1 583 ? 184.040 218.452 230.947 1.00 38.92  ?  602 PHE B CZ    1 
ATOM   10889 N  N     . ILE B 1 584 ? 183.037 215.166 227.309 1.00 40.43  ?  603 ILE B N     1 
ATOM   10890 C  CA    . ILE B 1 584 ? 184.142 214.231 227.516 1.00 38.50  ?  603 ILE B CA    1 
ATOM   10891 C  C     . ILE B 1 584 ? 184.345 213.369 226.270 1.00 39.25  ?  603 ILE B C     1 
ATOM   10892 O  O     . ILE B 1 584 ? 185.492 213.219 225.823 1.00 47.20  ?  603 ILE B O     1 
ATOM   10893 C  CB    . ILE B 1 584 ? 183.923 213.374 228.776 1.00 38.47  ?  603 ILE B CB    1 
ATOM   10894 C  CG1   . ILE B 1 584 ? 184.148 214.210 230.037 1.00 45.05  ?  603 ILE B CG1   1 
ATOM   10895 C  CG2   . ILE B 1 584 ? 184.848 212.170 228.773 1.00 41.98  ?  603 ILE B CG2   1 
ATOM   10896 C  CD1   . ILE B 1 584 ? 185.490 214.897 230.086 1.00 41.07  ?  603 ILE B CD1   1 
ATOM   10897 N  N     . PRO B 1 585 ? 183.298 212.776 225.674 1.00 37.24  ?  604 PRO B N     1 
ATOM   10898 C  CA    . PRO B 1 585 ? 183.514 212.096 224.384 1.00 46.36  ?  604 PRO B CA    1 
ATOM   10899 C  C     . PRO B 1 585 ? 184.041 213.028 223.308 1.00 53.19  ?  604 PRO B C     1 
ATOM   10900 O  O     . PRO B 1 585 ? 184.807 212.600 222.437 1.00 58.61  ?  604 PRO B O     1 
ATOM   10901 C  CB    . PRO B 1 585 ? 182.120 211.554 224.041 1.00 49.61  ?  604 PRO B CB    1 
ATOM   10902 C  CG    . PRO B 1 585 ? 181.476 211.363 225.353 1.00 48.57  ?  604 PRO B CG    1 
ATOM   10903 C  CD    . PRO B 1 585 ? 181.932 212.531 226.175 1.00 46.48  ?  604 PRO B CD    1 
ATOM   10904 N  N     . LEU B 1 586 ? 183.645 214.301 223.348 1.00 47.80  ?  605 LEU B N     1 
ATOM   10905 C  CA    . LEU B 1 586 ? 184.198 215.282 222.421 1.00 47.95  ?  605 LEU B CA    1 
ATOM   10906 C  C     . LEU B 1 586 ? 185.699 215.446 222.630 1.00 48.00  ?  605 LEU B C     1 
ATOM   10907 O  O     . LEU B 1 586 ? 186.467 215.528 221.662 1.00 55.07  ?  605 LEU B O     1 
ATOM   10908 C  CB    . LEU B 1 586 ? 183.472 216.615 222.592 1.00 45.39  ?  605 LEU B CB    1 
ATOM   10909 C  CG    . LEU B 1 586 ? 183.903 217.781 221.708 1.00 45.81  ?  605 LEU B CG    1 
ATOM   10910 C  CD1   . LEU B 1 586 ? 183.196 217.722 220.368 1.00 49.67  ?  605 LEU B CD1   1 
ATOM   10911 C  CD2   . LEU B 1 586 ? 183.615 219.097 222.408 1.00 46.66  ?  605 LEU B CD2   1 
ATOM   10912 N  N     . ALA B 1 587 ? 186.135 215.491 223.891 1.00 38.87  ?  606 ALA B N     1 
ATOM   10913 C  CA    . ALA B 1 587 ? 187.563 215.550 224.179 1.00 44.03  ?  606 ALA B CA    1 
ATOM   10914 C  C     . ALA B 1 587 ? 188.273 214.292 223.697 1.00 51.13  ?  606 ALA B C     1 
ATOM   10915 O  O     . ALA B 1 587 ? 189.397 214.362 223.190 1.00 55.36  ?  606 ALA B O     1 
ATOM   10916 C  CB    . ALA B 1 587 ? 187.788 215.758 225.676 1.00 46.00  ?  606 ALA B CB    1 
ATOM   10917 N  N     . GLU B 1 588 ? 187.637 213.129 223.855 1.00 52.92  ?  607 GLU B N     1 
ATOM   10918 C  CA    . GLU B 1 588 ? 188.229 211.891 223.355 1.00 48.79  ?  607 GLU B CA    1 
ATOM   10919 C  C     . GLU B 1 588 ? 188.396 211.934 221.841 1.00 53.45  ?  607 GLU B C     1 
ATOM   10920 O  O     . GLU B 1 588 ? 189.425 211.505 221.308 1.00 60.01  ?  607 GLU B O     1 
ATOM   10921 C  CB    . GLU B 1 588 ? 187.371 210.694 223.763 1.00 50.28  ?  607 GLU B CB    1 
ATOM   10922 C  CG    . GLU B 1 588 ? 187.511 210.286 225.218 1.00 56.40  ?  607 GLU B CG    1 
ATOM   10923 C  CD    . GLU B 1 588 ? 186.484 209.251 225.631 1.00 59.90  ?  607 GLU B CD    1 
ATOM   10924 O  OE1   . GLU B 1 588 ? 186.044 208.468 224.762 1.00 58.95  ?  607 GLU B OE1   1 
ATOM   10925 O  OE2   . GLU B 1 588 ? 186.115 209.223 226.823 1.00 61.27  -1 607 GLU B OE2   1 
ATOM   10926 N  N     . GLU B 1 589 ? 187.389 212.449 221.135 1.00 53.43  ?  608 GLU B N     1 
ATOM   10927 C  CA    . GLU B 1 589 ? 187.451 212.515 219.679 1.00 56.23  ?  608 GLU B CA    1 
ATOM   10928 C  C     . GLU B 1 589 ? 188.514 213.504 219.213 1.00 57.13  ?  608 GLU B C     1 
ATOM   10929 O  O     . GLU B 1 589 ? 189.227 213.248 218.235 1.00 58.29  ?  608 GLU B O     1 
ATOM   10930 C  CB    . GLU B 1 589 ? 186.081 212.892 219.114 1.00 55.54  ?  608 GLU B CB    1 
ATOM   10931 C  CG    . GLU B 1 589 ? 186.005 212.863 217.596 1.00 58.78  ?  608 GLU B CG    1 
ATOM   10932 C  CD    . GLU B 1 589 ? 184.583 212.971 217.083 1.00 62.03  ?  608 GLU B CD    1 
ATOM   10933 O  OE1   . GLU B 1 589 ? 183.667 213.172 217.908 1.00 60.72  ?  608 GLU B OE1   1 
ATOM   10934 O  OE2   . GLU B 1 589 ? 184.381 212.853 215.856 1.00 62.25  -1 608 GLU B OE2   1 
ATOM   10935 N  N     . ILE B 1 590 ? 188.639 214.642 219.900 1.00 51.62  ?  609 ILE B N     1 
ATOM   10936 C  CA    . ILE B 1 590 ? 189.537 215.689 219.420 1.00 50.90  ?  609 ILE B CA    1 
ATOM   10937 C  C     . ILE B 1 590 ? 190.978 215.404 219.825 1.00 52.70  ?  609 ILE B C     1 
ATOM   10938 O  O     . ILE B 1 590 ? 191.884 215.403 218.983 1.00 56.64  ?  609 ILE B O     1 
ATOM   10939 C  CB    . ILE B 1 590 ? 189.071 217.064 219.927 1.00 54.48  ?  609 ILE B CB    1 
ATOM   10940 C  CG1   . ILE B 1 590 ? 187.746 217.444 219.271 1.00 54.51  ?  609 ILE B CG1   1 
ATOM   10941 C  CG2   . ILE B 1 590 ? 190.132 218.119 219.658 1.00 54.70  ?  609 ILE B CG2   1 
ATOM   10942 C  CD1   . ILE B 1 590 ? 187.007 218.521 220.003 1.00 55.70  ?  609 ILE B CD1   1 
ATOM   10943 N  N     . GLY B 1 591 ? 191.216 215.156 221.110 1.00 58.38  ?  610 GLY B N     1 
ATOM   10944 C  CA    . GLY B 1 591 ? 192.563 214.986 221.616 1.00 60.59  ?  610 GLY B CA    1 
ATOM   10945 C  C     . GLY B 1 591 ? 192.846 215.873 222.810 1.00 61.76  ?  610 GLY B C     1 
ATOM   10946 O  O     . GLY B 1 591 ? 194.006 216.111 223.158 1.00 63.93  ?  610 GLY B O     1 
ATOM   10947 N  N     . GLU B 1 592 ? 191.786 216.369 223.446 1.00 65.36  ?  611 GLU B N     1 
ATOM   10948 C  CA    . GLU B 1 592 ? 191.894 217.227 224.618 1.00 67.26  ?  611 GLU B CA    1 
ATOM   10949 C  C     . GLU B 1 592 ? 191.828 216.446 225.924 1.00 67.71  ?  611 GLU B C     1 
ATOM   10950 O  O     . GLU B 1 592 ? 191.778 217.057 226.997 1.00 73.37  ?  611 GLU B O     1 
ATOM   10951 C  CB    . GLU B 1 592 ? 190.799 218.295 224.593 1.00 70.17  ?  611 GLU B CB    1 
ATOM   10952 C  CG    . GLU B 1 592 ? 190.747 219.099 223.304 1.00 70.85  ?  611 GLU B CG    1 
ATOM   10953 C  CD    . GLU B 1 592 ? 192.093 219.684 222.926 1.00 71.74  ?  611 GLU B CD    1 
ATOM   10954 O  OE1   . GLU B 1 592 ? 192.713 220.353 223.779 1.00 70.80  ?  611 GLU B OE1   1 
ATOM   10955 O  OE2   . GLU B 1 592 ? 192.531 219.475 221.775 1.00 71.69  -1 611 GLU B OE2   1 
ATOM   10956 N  N     . ILE B 1 593 ? 191.812 215.112 225.856 1.00 57.50  ?  612 ILE B N     1 
ATOM   10957 C  CA    . ILE B 1 593 ? 191.755 214.297 227.068 1.00 56.77  ?  612 ILE B CA    1 
ATOM   10958 C  C     . ILE B 1 593 ? 192.980 214.544 227.938 1.00 57.14  ?  612 ILE B C     1 
ATOM   10959 O  O     . ILE B 1 593 ? 192.875 214.652 229.166 1.00 57.54  ?  612 ILE B O     1 
ATOM   10960 C  CB    . ILE B 1 593 ? 191.606 212.808 226.705 1.00 59.51  ?  612 ILE B CB    1 
ATOM   10961 C  CG1   . ILE B 1 593 ? 190.163 212.504 226.305 1.00 59.80  ?  612 ILE B CG1   1 
ATOM   10962 C  CG2   . ILE B 1 593 ? 192.032 211.917 227.866 1.00 63.93  ?  612 ILE B CG2   1 
ATOM   10963 C  CD1   . ILE B 1 593 ? 189.159 212.765 227.406 1.00 59.31  ?  612 ILE B CD1   1 
ATOM   10964 N  N     . GLU B 1 594 ? 194.160 214.631 227.322 1.00 70.50  ?  613 GLU B N     1 
ATOM   10965 C  CA    . GLU B 1 594 ? 195.374 214.884 228.092 1.00 72.94  ?  613 GLU B CA    1 
ATOM   10966 C  C     . GLU B 1 594 ? 195.305 216.232 228.800 1.00 70.39  ?  613 GLU B C     1 
ATOM   10967 O  O     . GLU B 1 594 ? 195.619 216.336 229.991 1.00 72.04  ?  613 GLU B O     1 
ATOM   10968 C  CB    . GLU B 1 594 ? 196.599 214.815 227.178 1.00 76.19  ?  613 GLU B CB    1 
ATOM   10969 C  CG    . GLU B 1 594 ? 196.622 213.603 226.262 1.00 75.68  ?  613 GLU B CG    1 
ATOM   10970 C  CD    . GLU B 1 594 ? 196.565 212.294 227.026 1.00 75.45  ?  613 GLU B CD    1 
ATOM   10971 O  OE1   . GLU B 1 594 ? 197.308 212.151 228.019 1.00 74.92  ?  613 GLU B OE1   1 
ATOM   10972 O  OE2   . GLU B 1 594 ? 195.775 211.410 226.633 1.00 75.49  -1 613 GLU B OE2   1 
ATOM   10973 N  N     . ASN B 1 595 ? 194.886 217.276 228.081 1.00 64.49  ?  614 ASN B N     1 
ATOM   10974 C  CA    . ASN B 1 595 ? 194.790 218.600 228.688 1.00 66.77  ?  614 ASN B CA    1 
ATOM   10975 C  C     . ASN B 1 595 ? 193.779 218.605 229.826 1.00 72.68  ?  614 ASN B C     1 
ATOM   10976 O  O     . ASN B 1 595 ? 194.019 219.211 230.878 1.00 72.15  ?  614 ASN B O     1 
ATOM   10977 C  CB    . ASN B 1 595 ? 194.412 219.639 227.633 1.00 68.68  ?  614 ASN B CB    1 
ATOM   10978 C  CG    . ASN B 1 595 ? 195.367 219.651 226.458 1.00 71.33  ?  614 ASN B CG    1 
ATOM   10979 O  OD1   . ASN B 1 595 ? 194.973 219.396 225.320 1.00 71.82  ?  614 ASN B OD1   1 
ATOM   10980 N  ND2   . ASN B 1 595 ? 196.634 219.945 226.728 1.00 71.07  ?  614 ASN B ND2   1 
ATOM   10981 N  N     . ILE B 1 596 ? 192.644 217.929 229.633 1.00 73.79  ?  615 ILE B N     1 
ATOM   10982 C  CA    . ILE B 1 596 ? 191.656 217.811 230.701 1.00 68.23  ?  615 ILE B CA    1 
ATOM   10983 C  C     . ILE B 1 596 ? 192.266 217.117 231.911 1.00 64.56  ?  615 ILE B C     1 
ATOM   10984 O  O     . ILE B 1 596 ? 192.047 217.529 233.054 1.00 64.44  ?  615 ILE B O     1 
ATOM   10985 C  CB    . ILE B 1 596 ? 190.401 217.076 230.196 1.00 64.63  ?  615 ILE B CB    1 
ATOM   10986 C  CG1   . ILE B 1 596 ? 189.463 218.053 229.489 1.00 63.96  ?  615 ILE B CG1   1 
ATOM   10987 C  CG2   . ILE B 1 596 ? 189.676 216.380 231.341 1.00 66.90  ?  615 ILE B CG2   1 
ATOM   10988 C  CD1   . ILE B 1 596 ? 188.245 217.399 228.889 1.00 64.58  ?  615 ILE B CD1   1 
ATOM   10989 N  N     . GLY B 1 597 ? 193.041 216.055 231.680 1.00 65.59  ?  616 GLY B N     1 
ATOM   10990 C  CA    . GLY B 1 597 ? 193.656 215.348 232.793 1.00 67.69  ?  616 GLY B CA    1 
ATOM   10991 C  C     . GLY B 1 597 ? 194.626 216.217 233.572 1.00 67.10  ?  616 GLY B C     1 
ATOM   10992 O  O     . GLY B 1 597 ? 194.577 216.270 234.807 1.00 70.37  ?  616 GLY B O     1 
ATOM   10993 N  N     . ARG B 1 598 ? 195.515 216.920 232.861 1.00 69.88  ?  617 ARG B N     1 
ATOM   10994 C  CA    . ARG B 1 598 ? 196.451 217.808 233.547 1.00 70.46  ?  617 ARG B CA    1 
ATOM   10995 C  C     . ARG B 1 598 ? 195.707 218.883 234.327 1.00 67.10  ?  617 ARG B C     1 
ATOM   10996 O  O     . ARG B 1 598 ? 196.036 219.162 235.488 1.00 69.06  ?  617 ARG B O     1 
ATOM   10997 C  CB    . ARG B 1 598 ? 197.438 218.469 232.572 1.00 71.75  ?  617 ARG B CB    1 
ATOM   10998 C  CG    . ARG B 1 598 ? 198.633 217.631 232.093 1.00 72.30  ?  617 ARG B CG    1 
ATOM   10999 C  CD    . ARG B 1 598 ? 198.350 216.866 230.819 1.00 73.96  ?  617 ARG B CD    1 
ATOM   11000 N  NE    . ARG B 1 598 ? 199.548 216.281 230.227 1.00 75.63  ?  617 ARG B NE    1 
ATOM   11001 C  CZ    . ARG B 1 598 ? 199.946 215.030 230.411 1.00 75.05  ?  617 ARG B CZ    1 
ATOM   11002 N  NH1   . ARG B 1 598 ? 199.230 214.175 231.122 1.00 74.33  1  617 ARG B NH1   1 
ATOM   11003 N  NH2   . ARG B 1 598 ? 201.081 214.620 229.850 1.00 73.99  ?  617 ARG B NH2   1 
ATOM   11004 N  N     . TRP B 1 599 ? 194.690 219.495 233.709 1.00 57.78  ?  618 TRP B N     1 
ATOM   11005 C  CA    . TRP B 1 599 ? 193.957 220.555 234.392 1.00 58.76  ?  618 TRP B CA    1 
ATOM   11006 C  C     . TRP B 1 599 ? 193.250 220.030 235.631 1.00 59.33  ?  618 TRP B C     1 
ATOM   11007 O  O     . TRP B 1 599 ? 193.276 220.674 236.683 1.00 57.52  ?  618 TRP B O     1 
ATOM   11008 C  CB    . TRP B 1 599 ? 192.940 221.207 233.457 1.00 59.34  ?  618 TRP B CB    1 
ATOM   11009 C  CG    . TRP B 1 599 ? 192.259 222.369 234.113 1.00 60.07  ?  618 TRP B CG    1 
ATOM   11010 C  CD1   . TRP B 1 599 ? 192.688 223.663 234.132 1.00 59.64  ?  618 TRP B CD1   1 
ATOM   11011 C  CD2   . TRP B 1 599 ? 191.052 222.336 234.887 1.00 56.42  ?  618 TRP B CD2   1 
ATOM   11012 N  NE1   . TRP B 1 599 ? 191.815 224.441 234.850 1.00 59.26  ?  618 TRP B NE1   1 
ATOM   11013 C  CE2   . TRP B 1 599 ? 190.802 223.651 235.325 1.00 58.39  ?  618 TRP B CE2   1 
ATOM   11014 C  CE3   . TRP B 1 599 ? 190.154 221.324 235.242 1.00 56.69  ?  618 TRP B CE3   1 
ATOM   11015 C  CZ2   . TRP B 1 599 ? 189.693 223.981 236.100 1.00 59.06  ?  618 TRP B CZ2   1 
ATOM   11016 C  CZ3   . TRP B 1 599 ? 189.054 221.655 236.012 1.00 59.25  ?  618 TRP B CZ3   1 
ATOM   11017 C  CH2   . TRP B 1 599 ? 188.833 222.972 236.432 1.00 59.91  ?  618 TRP B CH2   1 
ATOM   11018 N  N     . VAL B 1 600 ? 192.593 218.872 235.521 1.00 65.08  ?  619 VAL B N     1 
ATOM   11019 C  CA    . VAL B 1 600 ? 191.857 218.336 236.659 1.00 60.13  ?  619 VAL B CA    1 
ATOM   11020 C  C     . VAL B 1 600 ? 192.807 218.000 237.798 1.00 59.79  ?  619 VAL B C     1 
ATOM   11021 O  O     . VAL B 1 600 ? 192.540 218.335 238.956 1.00 68.78  ?  619 VAL B O     1 
ATOM   11022 C  CB    . VAL B 1 600 ? 191.013 217.119 236.240 1.00 64.60  ?  619 VAL B CB    1 
ATOM   11023 C  CG1   . VAL B 1 600 ? 190.395 216.462 237.464 1.00 63.18  ?  619 VAL B CG1   1 
ATOM   11024 C  CG2   . VAL B 1 600 ? 189.914 217.544 235.286 1.00 65.98  ?  619 VAL B CG2   1 
ATOM   11025 N  N     . ILE B 1 601 ? 193.939 217.357 237.495 1.00 63.33  ?  620 ILE B N     1 
ATOM   11026 C  CA    . ILE B 1 601 ? 194.881 217.014 238.559 1.00 65.33  ?  620 ILE B CA    1 
ATOM   11027 C  C     . ILE B 1 601 ? 195.426 218.275 239.222 1.00 64.68  ?  620 ILE B C     1 
ATOM   11028 O  O     . ILE B 1 601 ? 195.468 218.378 240.458 1.00 64.82  ?  620 ILE B O     1 
ATOM   11029 C  CB    . ILE B 1 601 ? 196.014 216.125 238.015 1.00 63.38  ?  620 ILE B CB    1 
ATOM   11030 C  CG1   . ILE B 1 601 ? 195.456 214.802 237.491 1.00 62.62  ?  620 ILE B CG1   1 
ATOM   11031 C  CG2   . ILE B 1 601 ? 197.044 215.857 239.096 1.00 65.12  ?  620 ILE B CG2   1 
ATOM   11032 C  CD1   . ILE B 1 601 ? 196.345 214.131 236.468 1.00 64.08  ?  620 ILE B CD1   1 
ATOM   11033 N  N     . ALA B 1 602 ? 195.837 219.260 238.417 1.00 63.79  ?  621 ALA B N     1 
ATOM   11034 C  CA    . ALA B 1 602 ? 196.420 220.476 238.974 1.00 64.78  ?  621 ALA B CA    1 
ATOM   11035 C  C     . ALA B 1 602 ? 195.406 221.240 239.816 1.00 64.17  ?  621 ALA B C     1 
ATOM   11036 O  O     . ALA B 1 602 ? 195.719 221.694 240.923 1.00 66.31  ?  621 ALA B O     1 
ATOM   11037 C  CB    . ALA B 1 602 ? 196.964 221.357 237.850 1.00 65.78  ?  621 ALA B CB    1 
ATOM   11038 N  N     . GLU B 1 603 ? 194.180 221.388 239.310 1.00 65.37  ?  622 GLU B N     1 
ATOM   11039 C  CA    . GLU B 1 603 ? 193.159 222.131 240.040 1.00 68.14  ?  622 GLU B CA    1 
ATOM   11040 C  C     . GLU B 1 603 ? 192.735 221.389 241.299 1.00 65.78  ?  622 GLU B C     1 
ATOM   11041 O  O     . GLU B 1 603 ? 192.456 222.013 242.328 1.00 63.45  ?  622 GLU B O     1 
ATOM   11042 C  CB    . GLU B 1 603 ? 191.958 222.396 239.131 1.00 67.59  ?  622 GLU B CB    1 
ATOM   11043 C  CG    . GLU B 1 603 ? 190.694 222.818 239.861 1.00 70.81  ?  622 GLU B CG    1 
ATOM   11044 C  CD    . GLU B 1 603 ? 190.732 224.271 240.289 1.00 72.69  ?  622 GLU B CD    1 
ATOM   11045 O  OE1   . GLU B 1 603 ? 191.604 225.015 239.791 1.00 70.19  ?  622 GLU B OE1   1 
ATOM   11046 O  OE2   . GLU B 1 603 ? 189.895 224.668 241.126 1.00 71.40  -1 622 GLU B OE2   1 
ATOM   11047 N  N     . ALA B 1 604 ? 192.686 220.056 241.243 1.00 65.16  ?  623 ALA B N     1 
ATOM   11048 C  CA    . ALA B 1 604 ? 192.368 219.278 242.432 1.00 58.57  ?  623 ALA B CA    1 
ATOM   11049 C  C     . ALA B 1 604 ? 193.424 219.479 243.507 1.00 63.71  ?  623 ALA B C     1 
ATOM   11050 O  O     . ALA B 1 604 ? 193.097 219.691 244.678 1.00 73.01  ?  623 ALA B O     1 
ATOM   11051 C  CB    . ALA B 1 604 ? 192.235 217.799 242.069 1.00 63.98  ?  623 ALA B CB    1 
ATOM   11052 N  N     . CYS B 1 605 ? 194.703 219.435 243.123 1.00 75.88  ?  624 CYS B N     1 
ATOM   11053 C  CA    . CYS B 1 605 ? 195.765 219.665 244.099 1.00 81.15  ?  624 CYS B CA    1 
ATOM   11054 C  C     . CYS B 1 605 ? 195.727 221.092 244.639 1.00 80.95  ?  624 CYS B C     1 
ATOM   11055 O  O     . CYS B 1 605 ? 195.963 221.318 245.833 1.00 79.39  ?  624 CYS B O     1 
ATOM   11056 C  CB    . CYS B 1 605 ? 197.124 219.353 243.478 1.00 80.08  ?  624 CYS B CB    1 
ATOM   11057 S  SG    . CYS B 1 605 ? 197.404 217.593 243.197 1.00 93.35  ?  624 CYS B SG    1 
ATOM   11058 N  N     . ARG B 1 606 ? 195.427 222.067 243.777 1.00 73.25  ?  625 ARG B N     1 
ATOM   11059 C  CA    . ARG B 1 606 ? 195.309 223.450 244.227 1.00 69.80  ?  625 ARG B CA    1 
ATOM   11060 C  C     . ARG B 1 606 ? 194.184 223.610 245.241 1.00 67.87  ?  625 ARG B C     1 
ATOM   11061 O  O     . ARG B 1 606 ? 194.348 224.286 246.263 1.00 68.99  ?  625 ARG B O     1 
ATOM   11062 C  CB    . ARG B 1 606 ? 195.080 224.372 243.030 1.00 70.78  ?  625 ARG B CB    1 
ATOM   11063 C  CG    . ARG B 1 606 ? 194.966 225.842 243.393 1.00 71.30  ?  625 ARG B CG    1 
ATOM   11064 C  CD    . ARG B 1 606 ? 194.268 226.627 242.293 1.00 69.24  ?  625 ARG B CD    1 
ATOM   11065 N  NE    . ARG B 1 606 ? 192.835 226.750 242.537 1.00 71.93  ?  625 ARG B NE    1 
ATOM   11066 C  CZ    . ARG B 1 606 ? 192.290 227.551 243.442 1.00 75.59  ?  625 ARG B CZ    1 
ATOM   11067 N  NH1   . ARG B 1 606 ? 193.030 228.339 244.206 1.00 72.63  1  625 ARG B NH1   1 
ATOM   11068 N  NH2   . ARG B 1 606 ? 190.967 227.564 243.585 1.00 74.38  ?  625 ARG B NH2   1 
ATOM   11069 N  N     . GLN B 1 607 ? 193.029 222.999 244.974 1.00 71.23  ?  626 GLN B N     1 
ATOM   11070 C  CA    . GLN B 1 607 ? 191.913 223.095 245.907 1.00 69.37  ?  626 GLN B CA    1 
ATOM   11071 C  C     . GLN B 1 607 ? 192.196 222.334 247.195 1.00 66.57  ?  626 GLN B C     1 
ATOM   11072 O  O     . GLN B 1 607 ? 191.753 222.754 248.268 1.00 71.81  ?  626 GLN B O     1 
ATOM   11073 C  CB    . GLN B 1 607 ? 190.631 222.583 245.253 1.00 69.01  ?  626 GLN B CB    1 
ATOM   11074 C  CG    . GLN B 1 607 ? 189.372 223.227 245.803 1.00 69.34  ?  626 GLN B CG    1 
ATOM   11075 C  CD    . GLN B 1 607 ? 189.356 224.730 245.608 1.00 74.78  ?  626 GLN B CD    1 
ATOM   11076 O  OE1   . GLN B 1 607 ? 189.563 225.493 246.552 1.00 76.29  ?  626 GLN B OE1   1 
ATOM   11077 N  NE2   . GLN B 1 607 ? 189.104 225.165 244.379 1.00 73.53  ?  626 GLN B NE2   1 
ATOM   11078 N  N     . LEU B 1 608 ? 192.933 221.224 247.111 1.00 62.75  ?  627 LEU B N     1 
ATOM   11079 C  CA    . LEU B 1 608 ? 193.355 220.524 248.320 1.00 68.91  ?  627 LEU B CA    1 
ATOM   11080 C  C     . LEU B 1 608 ? 194.260 221.402 249.174 1.00 73.01  ?  627 LEU B C     1 
ATOM   11081 O  O     . LEU B 1 608 ? 194.115 221.446 250.400 1.00 70.51  ?  627 LEU B O     1 
ATOM   11082 C  CB    . LEU B 1 608 ? 194.056 219.214 247.954 1.00 70.20  ?  627 LEU B CB    1 
ATOM   11083 C  CG    . LEU B 1 608 ? 193.173 218.154 247.292 1.00 68.74  ?  627 LEU B CG    1 
ATOM   11084 C  CD1   . LEU B 1 608 ? 193.977 216.953 246.833 1.00 68.93  ?  627 LEU B CD1   1 
ATOM   11085 C  CD2   . LEU B 1 608 ? 192.084 217.719 248.239 1.00 69.27  ?  627 LEU B CD2   1 
ATOM   11086 N  N     . ALA B 1 609 ? 195.197 222.115 248.543 1.00 81.16  ?  628 ALA B N     1 
ATOM   11087 C  CA    . ALA B 1 609 ? 196.043 223.043 249.290 1.00 81.22  ?  628 ALA B CA    1 
ATOM   11088 C  C     . ALA B 1 609 ? 195.222 224.179 249.893 1.00 80.06  ?  628 ALA B C     1 
ATOM   11089 O  O     . ALA B 1 609 ? 195.452 224.584 251.040 1.00 81.97  ?  628 ALA B O     1 
ATOM   11090 C  CB    . ALA B 1 609 ? 197.142 223.598 248.386 1.00 77.41  ?  628 ALA B CB    1 
ATOM   11091 N  N     . GLU B 1 610 ? 194.261 224.706 249.131 1.00 76.55  ?  629 GLU B N     1 
ATOM   11092 C  CA    . GLU B 1 610 ? 193.424 225.791 249.635 1.00 75.62  ?  629 GLU B CA    1 
ATOM   11093 C  C     . GLU B 1 610 ? 192.604 225.342 250.838 1.00 72.24  ?  629 GLU B C     1 
ATOM   11094 O  O     . GLU B 1 610 ? 192.450 226.091 251.810 1.00 75.90  ?  629 GLU B O     1 
ATOM   11095 C  CB    . GLU B 1 610 ? 192.508 226.304 248.523 1.00 78.21  ?  629 GLU B CB    1 
ATOM   11096 C  CG    . GLU B 1 610 ? 193.212 227.154 247.476 1.00 78.40  ?  629 GLU B CG    1 
ATOM   11097 C  CD    . GLU B 1 610 ? 193.700 228.478 248.028 1.00 79.44  ?  629 GLU B CD    1 
ATOM   11098 O  OE1   . GLU B 1 610 ? 193.036 229.029 248.931 1.00 77.62  ?  629 GLU B OE1   1 
ATOM   11099 O  OE2   . GLU B 1 610 ? 194.748 228.970 247.559 1.00 78.74  -1 629 GLU B OE2   1 
ATOM   11100 N  N     . TRP B 1 611 ? 192.065 224.122 250.789 1.00 69.64  ?  630 TRP B N     1 
ATOM   11101 C  CA    . TRP B 1 611 ? 191.328 223.580 251.923 1.00 76.64  ?  630 TRP B CA    1 
ATOM   11102 C  C     . TRP B 1 611 ? 192.233 223.261 253.105 1.00 79.53  ?  630 TRP B C     1 
ATOM   11103 O  O     . TRP B 1 611 ? 191.810 223.431 254.253 1.00 84.42  ?  630 TRP B O     1 
ATOM   11104 C  CB    . TRP B 1 611 ? 190.559 222.326 251.504 1.00 78.64  ?  630 TRP B CB    1 
ATOM   11105 C  CG    . TRP B 1 611 ? 189.318 222.614 250.718 1.00 75.68  ?  630 TRP B CG    1 
ATOM   11106 C  CD1   . TRP B 1 611 ? 188.441 223.639 250.918 1.00 76.87  ?  630 TRP B CD1   1 
ATOM   11107 C  CD2   . TRP B 1 611 ? 188.816 221.868 249.604 1.00 73.06  ?  630 TRP B CD2   1 
ATOM   11108 N  NE1   . TRP B 1 611 ? 187.421 223.576 249.999 1.00 78.19  ?  630 TRP B NE1   1 
ATOM   11109 C  CE2   . TRP B 1 611 ? 187.630 222.497 249.180 1.00 74.11  ?  630 TRP B CE2   1 
ATOM   11110 C  CE3   . TRP B 1 611 ? 189.256 220.731 248.922 1.00 76.76  ?  630 TRP B CE3   1 
ATOM   11111 C  CZ2   . TRP B 1 611 ? 186.877 222.025 248.108 1.00 73.89  ?  630 TRP B CZ2   1 
ATOM   11112 C  CZ3   . TRP B 1 611 ? 188.507 220.263 247.859 1.00 75.91  ?  630 TRP B CZ3   1 
ATOM   11113 C  CH2   . TRP B 1 611 ? 187.331 220.908 247.463 1.00 75.63  ?  630 TRP B CH2   1 
ATOM   11114 N  N     . ARG B 1 612 ? 193.459 222.801 252.852 1.00 80.69  ?  631 ARG B N     1 
ATOM   11115 C  CA    . ARG B 1 612 ? 194.406 222.554 253.933 1.00 82.48  ?  631 ARG B CA    1 
ATOM   11116 C  C     . ARG B 1 612 ? 194.854 223.848 254.597 1.00 82.00  ?  631 ARG B C     1 
ATOM   11117 O  O     . ARG B 1 612 ? 195.267 223.830 255.762 1.00 83.68  ?  631 ARG B O     1 
ATOM   11118 C  CB    . ARG B 1 612 ? 195.620 221.789 253.401 1.00 81.44  ?  631 ARG B CB    1 
ATOM   11119 C  CG    . ARG B 1 612 ? 196.542 221.245 254.480 1.00 81.26  ?  631 ARG B CG    1 
ATOM   11120 C  CD    . ARG B 1 612 ? 197.784 220.614 253.873 1.00 80.95  ?  631 ARG B CD    1 
ATOM   11121 N  NE    . ARG B 1 612 ? 198.497 221.549 253.012 1.00 80.69  ?  631 ARG B NE    1 
ATOM   11122 C  CZ    . ARG B 1 612 ? 199.399 221.197 252.107 1.00 80.57  ?  631 ARG B CZ    1 
ATOM   11123 N  NH1   . ARG B 1 612 ? 199.731 219.930 251.918 1.00 80.24  1  631 ARG B NH1   1 
ATOM   11124 N  NH2   . ARG B 1 612 ? 199.982 222.139 251.371 1.00 79.59  ?  631 ARG B NH2   1 
ATOM   11125 N  N     . SER B 1 613 ? 194.791 224.966 253.869 1.00 82.68  ?  632 SER B N     1 
ATOM   11126 C  CA    . SER B 1 613 ? 195.124 226.259 254.462 1.00 83.59  ?  632 SER B CA    1 
ATOM   11127 C  C     . SER B 1 613 ? 194.287 226.518 255.711 1.00 82.80  ?  632 SER B C     1 
ATOM   11128 O  O     . SER B 1 613 ? 194.801 226.993 256.730 1.00 82.49  ?  632 SER B O     1 
ATOM   11129 C  CB    . SER B 1 613 ? 194.924 227.374 253.435 1.00 81.16  ?  632 SER B CB    1 
ATOM   11130 O  OG    . SER B 1 613 ? 195.915 227.325 252.424 1.00 81.85  ?  632 SER B OG    1 
ATOM   11131 N  N     . GLN B 1 614 ? 192.993 226.218 255.647 1.00 78.07  ?  633 GLN B N     1 
ATOM   11132 C  CA    . GLN B 1 614 ? 192.120 226.263 256.807 1.00 75.99  ?  633 GLN B CA    1 
ATOM   11133 C  C     . GLN B 1 614 ? 191.861 224.842 257.315 1.00 74.97  ?  633 GLN B C     1 
ATOM   11134 O  O     . GLN B 1 614 ? 192.484 223.873 256.876 1.00 75.09  ?  633 GLN B O     1 
ATOM   11135 C  CB    . GLN B 1 614 ? 190.827 227.013 256.475 1.00 77.19  ?  633 GLN B CB    1 
ATOM   11136 C  CG    . GLN B 1 614 ? 190.217 226.684 255.123 1.00 79.01  ?  633 GLN B CG    1 
ATOM   11137 C  CD    . GLN B 1 614 ? 189.309 225.476 255.169 1.00 84.08  ?  633 GLN B CD    1 
ATOM   11138 O  OE1   . GLN B 1 614 ? 188.779 225.124 256.222 1.00 84.75  ?  633 GLN B OE1   1 
ATOM   11139 N  NE2   . GLN B 1 614 ? 189.110 224.844 254.019 1.00 81.95  ?  633 GLN B NE2   1 
ATOM   11140 N  N     . ASN B 1 615 ? 190.940 224.721 258.272 1.00 85.88  ?  634 ASN B N     1 
ATOM   11141 C  CA    . ASN B 1 615 ? 190.733 223.466 259.000 1.00 90.79  ?  634 ASN B CA    1 
ATOM   11142 C  C     . ASN B 1 615 ? 189.729 222.585 258.259 1.00 89.97  ?  634 ASN B C     1 
ATOM   11143 O  O     . ASN B 1 615 ? 188.522 222.602 258.514 1.00 93.13  ?  634 ASN B O     1 
ATOM   11144 C  CB    . ASN B 1 615 ? 190.277 223.747 260.425 1.00 95.32  ?  634 ASN B CB    1 
ATOM   11145 C  CG    . ASN B 1 615 ? 191.292 224.549 261.214 1.00 93.26  ?  634 ASN B CG    1 
ATOM   11146 O  OD1   . ASN B 1 615 ? 192.327 224.952 260.684 1.00 92.15  ?  634 ASN B OD1   1 
ATOM   11147 N  ND2   . ASN B 1 615 ? 191.001 224.784 262.488 1.00 91.30  ?  634 ASN B ND2   1 
ATOM   11148 N  N     . ILE B 1 616 ? 190.251 221.791 257.324 1.00 80.76  ?  635 ILE B N     1 
ATOM   11149 C  CA    . ILE B 1 616 ? 189.489 220.748 256.647 1.00 83.27  ?  635 ILE B CA    1 
ATOM   11150 C  C     . ILE B 1 616 ? 190.359 219.503 256.546 1.00 83.81  ?  635 ILE B C     1 
ATOM   11151 O  O     . ILE B 1 616 ? 191.511 219.574 256.102 1.00 85.22  ?  635 ILE B O     1 
ATOM   11152 C  CB    . ILE B 1 616 ? 189.007 221.194 255.249 1.00 82.68  ?  635 ILE B CB    1 
ATOM   11153 C  CG1   . ILE B 1 616 ? 187.864 222.201 255.376 1.00 83.15  ?  635 ILE B CG1   1 
ATOM   11154 C  CG2   . ILE B 1 616 ? 188.563 219.998 254.423 1.00 86.02  ?  635 ILE B CG2   1 
ATOM   11155 C  CD1   . ILE B 1 616 ? 186.615 221.635 256.017 1.00 83.59  ?  635 ILE B CD1   1 
ATOM   11156 N  N     . HIS B 1 617 ? 189.808 218.360 256.961 1.00 83.79  ?  636 HIS B N     1 
ATOM   11157 C  CA    . HIS B 1 617 ? 190.570 217.115 256.933 1.00 85.46  ?  636 HIS B CA    1 
ATOM   11158 C  C     . HIS B 1 617 ? 190.578 216.483 255.545 1.00 87.12  ?  636 HIS B C     1 
ATOM   11159 O  O     . HIS B 1 617 ? 191.637 216.061 255.067 1.00 89.58  ?  636 HIS B O     1 
ATOM   11160 C  CB    . HIS B 1 617 ? 190.013 216.134 257.966 1.00 86.43  ?  636 HIS B CB    1 
ATOM   11161 C  CG    . HIS B 1 617 ? 188.518 216.094 258.019 1.00 87.75  ?  636 HIS B CG    1 
ATOM   11162 N  ND1   . HIS B 1 617 ? 187.772 217.036 258.694 1.00 87.97  ?  636 HIS B ND1   1 
ATOM   11163 C  CD2   . HIS B 1 617 ? 187.629 215.223 257.485 1.00 88.43  ?  636 HIS B CD2   1 
ATOM   11164 C  CE1   . HIS B 1 617 ? 186.488 216.748 258.571 1.00 87.58  ?  636 HIS B CE1   1 
ATOM   11165 N  NE2   . HIS B 1 617 ? 186.375 215.653 257.842 1.00 89.46  ?  636 HIS B NE2   1 
ATOM   11166 N  N     . ILE B 1 618 ? 189.413 216.410 254.899 1.00 80.68  ?  637 ILE B N     1 
ATOM   11167 C  CA    . ILE B 1 618 ? 189.210 215.896 253.539 1.00 79.90  ?  637 ILE B CA    1 
ATOM   11168 C  C     . ILE B 1 618 ? 190.031 214.628 253.307 1.00 82.11  ?  637 ILE B C     1 
ATOM   11169 O  O     . ILE B 1 618 ? 191.081 214.665 252.648 1.00 82.69  ?  637 ILE B O     1 
ATOM   11170 C  CB    . ILE B 1 618 ? 189.459 216.982 252.468 1.00 80.08  ?  637 ILE B CB    1 
ATOM   11171 C  CG1   . ILE B 1 618 ? 189.154 216.431 251.074 1.00 80.12  ?  637 ILE B CG1   1 
ATOM   11172 C  CG2   . ILE B 1 618 ? 190.859 217.620 252.534 1.00 82.25  ?  637 ILE B CG2   1 
ATOM   11173 C  CD1   . ILE B 1 618 ? 189.117 217.481 250.017 1.00 80.95  ?  637 ILE B CD1   1 
ATOM   11174 N  N     . PRO B 1 619 ? 189.604 213.490 253.863 1.00 79.10  ?  638 PRO B N     1 
ATOM   11175 C  CA    . PRO B 1 619 ? 190.449 212.282 253.811 1.00 76.75  ?  638 PRO B CA    1 
ATOM   11176 C  C     . PRO B 1 619 ? 190.834 211.826 252.410 1.00 77.60  ?  638 PRO B C     1 
ATOM   11177 O  O     . PRO B 1 619 ? 191.965 211.361 252.220 1.00 78.06  ?  638 PRO B O     1 
ATOM   11178 C  CB    . PRO B 1 619 ? 189.591 211.228 254.529 1.00 72.59  ?  638 PRO B CB    1 
ATOM   11179 C  CG    . PRO B 1 619 ? 188.619 212.008 255.351 1.00 75.59  ?  638 PRO B CG    1 
ATOM   11180 C  CD    . PRO B 1 619 ? 188.343 213.260 254.586 1.00 78.08  ?  638 PRO B CD    1 
ATOM   11181 N  N     . ALA B 1 620 ? 189.947 211.935 251.422 1.00 63.76  ?  639 ALA B N     1 
ATOM   11182 C  CA    . ALA B 1 620 ? 190.251 211.369 250.114 1.00 60.10  ?  639 ALA B CA    1 
ATOM   11183 C  C     . ALA B 1 620 ? 189.585 212.175 249.008 1.00 60.47  ?  639 ALA B C     1 
ATOM   11184 O  O     . ALA B 1 620 ? 188.465 212.674 249.153 1.00 63.42  ?  639 ALA B O     1 
ATOM   11185 C  CB    . ALA B 1 620 ? 189.818 209.901 250.026 1.00 63.01  ?  639 ALA B CB    1 
ATOM   11186 N  N     . LEU B 1 621 ? 190.286 212.263 247.877 1.00 52.25  ?  640 LEU B N     1 
ATOM   11187 C  CA    . LEU B 1 621 ? 189.777 212.922 246.678 1.00 49.58  ?  640 LEU B CA    1 
ATOM   11188 C  C     . LEU B 1 621 ? 189.992 211.988 245.495 1.00 47.13  ?  640 LEU B C     1 
ATOM   11189 O  O     . LEU B 1 621 ? 191.094 211.465 245.304 1.00 58.06  ?  640 LEU B O     1 
ATOM   11190 C  CB    . LEU B 1 621 ? 190.464 214.268 246.443 1.00 55.01  ?  640 LEU B CB    1 
ATOM   11191 C  CG    . LEU B 1 621 ? 189.966 215.058 245.231 1.00 54.62  ?  640 LEU B CG    1 
ATOM   11192 C  CD1   . LEU B 1 621 ? 188.494 215.397 245.372 1.00 53.84  ?  640 LEU B CD1   1 
ATOM   11193 C  CD2   . LEU B 1 621 ? 190.786 216.319 245.040 1.00 55.43  ?  640 LEU B CD2   1 
ATOM   11194 N  N     . SER B 1 622 ? 188.939 211.779 244.709 1.00 40.53  ?  641 SER B N     1 
ATOM   11195 C  CA    . SER B 1 622 ? 188.984 210.905 243.544 1.00 40.11  ?  641 SER B CA    1 
ATOM   11196 C  C     . SER B 1 622 ? 188.949 211.758 242.282 1.00 40.53  ?  641 SER B C     1 
ATOM   11197 O  O     . SER B 1 622 ? 188.226 212.758 242.223 1.00 55.30  ?  641 SER B O     1 
ATOM   11198 C  CB    . SER B 1 622 ? 187.817 209.922 243.566 1.00 47.15  ?  641 SER B CB    1 
ATOM   11199 O  OG    . SER B 1 622 ? 187.759 209.232 244.802 1.00 52.50  ?  641 SER B OG    1 
ATOM   11200 N  N     . VAL B 1 623 ? 189.735 211.369 241.281 1.00 41.05  ?  642 VAL B N     1 
ATOM   11201 C  CA    . VAL B 1 623 ? 189.872 212.124 240.041 1.00 44.05  ?  642 VAL B CA    1 
ATOM   11202 C  C     . VAL B 1 623 ? 189.763 211.153 238.874 1.00 43.80  ?  642 VAL B C     1 
ATOM   11203 O  O     . VAL B 1 623 ? 190.465 210.136 238.838 1.00 58.46  ?  642 VAL B O     1 
ATOM   11204 C  CB    . VAL B 1 623 ? 191.203 212.898 240.000 1.00 52.27  ?  642 VAL B CB    1 
ATOM   11205 C  CG1   . VAL B 1 623 ? 191.579 213.246 238.575 1.00 53.62  ?  642 VAL B CG1   1 
ATOM   11206 C  CG2   . VAL B 1 623 ? 191.113 214.153 240.853 1.00 54.00  ?  642 VAL B CG2   1 
ATOM   11207 N  N     . ASN B 1 624 ? 188.882 211.465 237.926 1.00 36.10  ?  643 ASN B N     1 
ATOM   11208 C  CA    . ASN B 1 624 ? 188.615 210.572 236.806 1.00 38.10  ?  643 ASN B CA    1 
ATOM   11209 C  C     . ASN B 1 624 ? 189.681 210.726 235.728 1.00 50.67  ?  643 ASN B C     1 
ATOM   11210 O  O     . ASN B 1 624 ? 190.059 211.846 235.371 1.00 56.03  ?  643 ASN B O     1 
ATOM   11211 C  CB    . ASN B 1 624 ? 187.233 210.856 236.218 1.00 40.35  ?  643 ASN B CB    1 
ATOM   11212 C  CG    . ASN B 1 624 ? 186.113 210.533 237.184 1.00 46.83  ?  643 ASN B CG    1 
ATOM   11213 O  OD1   . ASN B 1 624 ? 185.507 209.464 237.117 1.00 53.63  ?  643 ASN B OD1   1 
ATOM   11214 N  ND2   . ASN B 1 624 ? 185.830 211.460 238.091 1.00 49.10  ?  643 ASN B ND2   1 
ATOM   11215 N  N     . LEU B 1 625 ? 190.159 209.597 235.208 1.00 66.84  ?  644 LEU B N     1 
ATOM   11216 C  CA    . LEU B 1 625 ? 191.097 209.571 234.096 1.00 66.71  ?  644 LEU B CA    1 
ATOM   11217 C  C     . LEU B 1 625 ? 190.592 208.600 233.036 1.00 67.64  ?  644 LEU B C     1 
ATOM   11218 O  O     . LEU B 1 625 ? 189.761 207.730 233.307 1.00 73.25  ?  644 LEU B O     1 
ATOM   11219 C  CB    . LEU B 1 625 ? 192.513 209.166 234.534 1.00 67.62  ?  644 LEU B CB    1 
ATOM   11220 C  CG    . LEU B 1 625 ? 193.454 210.229 235.117 1.00 69.71  ?  644 LEU B CG    1 
ATOM   11221 C  CD1   . LEU B 1 625 ? 193.760 211.313 234.088 1.00 72.39  ?  644 LEU B CD1   1 
ATOM   11222 C  CD2   . LEU B 1 625 ? 192.958 210.822 236.423 1.00 67.98  ?  644 LEU B CD2   1 
ATOM   11223 N  N     . SER B 1 626 ? 191.105 208.758 231.819 1.00 68.02  ?  645 SER B N     1 
ATOM   11224 C  CA    . SER B 1 626 ? 190.699 207.948 230.680 1.00 72.16  ?  645 SER B CA    1 
ATOM   11225 C  C     . SER B 1 626 ? 191.819 206.988 230.288 1.00 77.21  ?  645 SER B C     1 
ATOM   11226 O  O     . SER B 1 626 ? 192.902 206.976 230.879 1.00 80.21  ?  645 SER B O     1 
ATOM   11227 C  CB    . SER B 1 626 ? 190.301 208.839 229.502 1.00 73.90  ?  645 SER B CB    1 
ATOM   11228 O  OG    . SER B 1 626 ? 189.947 208.060 228.372 1.00 75.44  ?  645 SER B OG    1 
ATOM   11229 N  N     . ALA B 1 627 ? 191.541 206.170 229.269 1.00 88.37  ?  646 ALA B N     1 
ATOM   11230 C  CA    . ALA B 1 627 ? 192.519 205.185 228.817 1.00 86.51  ?  646 ALA B CA    1 
ATOM   11231 C  C     . ALA B 1 627 ? 193.682 205.845 228.087 1.00 88.14  ?  646 ALA B C     1 
ATOM   11232 O  O     . ALA B 1 627 ? 194.846 205.499 228.325 1.00 87.33  ?  646 ALA B O     1 
ATOM   11233 C  CB    . ALA B 1 627 ? 191.843 204.152 227.916 1.00 86.05  ?  646 ALA B CB    1 
ATOM   11234 N  N     . LEU B 1 628 ? 193.389 206.789 227.190 1.00 89.54  ?  647 LEU B N     1 
ATOM   11235 C  CA    . LEU B 1 628 ? 194.437 207.434 226.409 1.00 89.03  ?  647 LEU B CA    1 
ATOM   11236 C  C     . LEU B 1 628 ? 195.376 208.268 227.270 1.00 87.89  ?  647 LEU B C     1 
ATOM   11237 O  O     . LEU B 1 628 ? 196.504 208.543 226.847 1.00 90.50  ?  647 LEU B O     1 
ATOM   11238 C  CB    . LEU B 1 628 ? 193.814 208.309 225.320 1.00 88.56  ?  647 LEU B CB    1 
ATOM   11239 C  CG    . LEU B 1 628 ? 192.893 207.596 224.328 1.00 90.77  ?  647 LEU B CG    1 
ATOM   11240 C  CD1   . LEU B 1 628 ? 192.501 208.525 223.189 1.00 88.09  ?  647 LEU B CD1   1 
ATOM   11241 C  CD2   . LEU B 1 628 ? 193.549 206.333 223.792 1.00 87.61  ?  647 LEU B CD2   1 
ATOM   11242 N  N     . HIS B 1 629 ? 194.938 208.679 228.461 1.00 80.21  ?  648 HIS B N     1 
ATOM   11243 C  CA    . HIS B 1 629 ? 195.798 209.470 229.332 1.00 80.40  ?  648 HIS B CA    1 
ATOM   11244 C  C     . HIS B 1 629 ? 196.957 208.648 229.881 1.00 84.10  ?  648 HIS B C     1 
ATOM   11245 O  O     . HIS B 1 629 ? 198.060 209.178 230.058 1.00 86.73  ?  648 HIS B O     1 
ATOM   11246 C  CB    . HIS B 1 629 ? 194.979 210.063 230.479 1.00 78.27  ?  648 HIS B CB    1 
ATOM   11247 C  CG    . HIS B 1 629 ? 195.595 211.279 231.097 1.00 79.43  ?  648 HIS B CG    1 
ATOM   11248 N  ND1   . HIS B 1 629 ? 196.595 211.210 232.043 1.00 81.57  ?  648 HIS B ND1   1 
ATOM   11249 C  CD2   . HIS B 1 629 ? 195.351 212.597 230.904 1.00 81.41  ?  648 HIS B CD2   1 
ATOM   11250 C  CE1   . HIS B 1 629 ? 196.939 212.432 232.407 1.00 84.15  ?  648 HIS B CE1   1 
ATOM   11251 N  NE2   . HIS B 1 629 ? 196.200 213.292 231.731 1.00 85.13  ?  648 HIS B NE2   1 
ATOM   11252 N  N     . PHE B 1 630 ? 196.734 207.365 230.156 1.00 95.48  ?  649 PHE B N     1 
ATOM   11253 C  CA    . PHE B 1 630 ? 197.742 206.516 230.778 1.00 96.73  ?  649 PHE B CA    1 
ATOM   11254 C  C     . PHE B 1 630 ? 198.597 205.764 229.769 1.00 99.29  ?  649 PHE B C     1 
ATOM   11255 O  O     . PHE B 1 630 ? 199.551 205.089 230.169 1.00 101.06 ?  649 PHE B O     1 
ATOM   11256 C  CB    . PHE B 1 630 ? 197.083 205.512 231.731 1.00 94.16  ?  649 PHE B CB    1 
ATOM   11257 C  CG    . PHE B 1 630 ? 196.524 206.129 232.986 1.00 94.85  ?  649 PHE B CG    1 
ATOM   11258 C  CD1   . PHE B 1 630 ? 196.447 207.503 233.134 1.00 98.55  ?  649 PHE B CD1   1 
ATOM   11259 C  CD2   . PHE B 1 630 ? 196.087 205.326 234.026 1.00 95.99  ?  649 PHE B CD2   1 
ATOM   11260 C  CE1   . PHE B 1 630 ? 195.937 208.060 234.285 1.00 96.97  ?  649 PHE B CE1   1 
ATOM   11261 C  CE2   . PHE B 1 630 ? 195.576 205.880 235.182 1.00 97.10  ?  649 PHE B CE2   1 
ATOM   11262 C  CZ    . PHE B 1 630 ? 195.502 207.249 235.311 1.00 96.00  ?  649 PHE B CZ    1 
ATOM   11263 N  N     . ARG B 1 631 ? 198.288 205.861 228.479 1.00 103.55 ?  650 ARG B N     1 
ATOM   11264 C  CA    . ARG B 1 631 ? 199.039 205.153 227.451 1.00 103.14 ?  650 ARG B CA    1 
ATOM   11265 C  C     . ARG B 1 631 ? 200.301 205.893 227.025 1.00 102.60 ?  650 ARG B C     1 
ATOM   11266 O  O     . ARG B 1 631 ? 201.075 205.358 226.224 1.00 101.85 ?  650 ARG B O     1 
ATOM   11267 C  CB    . ARG B 1 631 ? 198.150 204.897 226.230 1.00 103.60 ?  650 ARG B CB    1 
ATOM   11268 C  CG    . ARG B 1 631 ? 198.005 206.088 225.299 1.00 104.41 ?  650 ARG B CG    1 
ATOM   11269 C  CD    . ARG B 1 631 ? 197.187 205.723 224.071 1.00 103.32 ?  650 ARG B CD    1 
ATOM   11270 N  NE    . ARG B 1 631 ? 197.578 204.433 223.515 1.00 103.15 ?  650 ARG B NE    1 
ATOM   11271 C  CZ    . ARG B 1 631 ? 198.646 204.235 222.755 1.00 102.14 ?  650 ARG B CZ    1 
ATOM   11272 N  NH1   . ARG B 1 631 ? 199.460 205.228 222.435 1.00 101.50 1  650 ARG B NH1   1 
ATOM   11273 N  NH2   . ARG B 1 631 ? 198.904 203.011 222.304 1.00 100.96 ?  650 ARG B NH2   1 
ATOM   11274 N  N     . SER B 1 632 ? 200.528 207.096 227.540 1.00 106.43 ?  651 SER B N     1 
ATOM   11275 C  CA    . SER B 1 632 ? 201.727 207.864 227.246 1.00 106.62 ?  651 SER B CA    1 
ATOM   11276 C  C     . SER B 1 632 ? 202.672 207.837 228.442 1.00 109.37 ?  651 SER B C     1 
ATOM   11277 O  O     . SER B 1 632 ? 202.241 207.829 229.598 1.00 109.13 ?  651 SER B O     1 
ATOM   11278 C  CB    . SER B 1 632 ? 201.378 209.311 226.890 1.00 105.42 ?  651 SER B CB    1 
ATOM   11279 O  OG    . SER B 1 632 ? 200.666 209.938 227.942 1.00 107.76 ?  651 SER B OG    1 
ATOM   11280 N  N     . ASN B 1 633 ? 203.969 207.823 228.151 1.00 113.83 ?  652 ASN B N     1 
ATOM   11281 C  CA    . ASN B 1 633 ? 204.999 207.765 229.189 1.00 112.44 ?  652 ASN B CA    1 
ATOM   11282 C  C     . ASN B 1 633 ? 205.288 209.141 229.786 1.00 112.43 ?  652 ASN B C     1 
ATOM   11283 O  O     . ASN B 1 633 ? 206.431 209.590 229.863 1.00 112.62 ?  652 ASN B O     1 
ATOM   11284 C  CB    . ASN B 1 633 ? 206.264 207.122 228.626 1.00 111.77 ?  652 ASN B CB    1 
ATOM   11285 C  CG    . ASN B 1 633 ? 206.855 207.897 227.454 1.00 113.04 ?  652 ASN B CG    1 
ATOM   11286 O  OD1   . ASN B 1 633 ? 206.393 208.984 227.107 1.00 115.46 ?  652 ASN B OD1   1 
ATOM   11287 N  ND2   . ASN B 1 633 ? 207.889 207.332 226.841 1.00 109.54 ?  652 ASN B ND2   1 
ATOM   11288 N  N     . GLN B 1 634 ? 204.231 209.818 230.233 1.00 104.83 ?  653 GLN B N     1 
ATOM   11289 C  CA    . GLN B 1 634 ? 204.356 211.131 230.851 1.00 103.67 ?  653 GLN B CA    1 
ATOM   11290 C  C     . GLN B 1 634 ? 203.567 211.291 232.140 1.00 105.03 ?  653 GLN B C     1 
ATOM   11291 O  O     . GLN B 1 634 ? 203.893 212.194 232.920 1.00 106.01 ?  653 GLN B O     1 
ATOM   11292 C  CB    . GLN B 1 634 ? 203.921 212.232 229.872 1.00 105.20 ?  653 GLN B CB    1 
ATOM   11293 C  CG    . GLN B 1 634 ? 205.044 212.765 229.000 1.00 106.42 ?  653 GLN B CG    1 
ATOM   11294 C  CD    . GLN B 1 634 ? 204.772 214.169 228.495 1.00 106.57 ?  653 GLN B CD    1 
ATOM   11295 O  OE1   . GLN B 1 634 ? 203.755 214.775 228.830 1.00 105.29 ?  653 GLN B OE1   1 
ATOM   11296 N  NE2   . GLN B 1 634 ? 205.686 214.694 227.688 1.00 106.73 ?  653 GLN B NE2   1 
ATOM   11297 N  N     . LEU B 1 635 ? 202.562 210.450 232.396 1.00 104.45 ?  654 LEU B N     1 
ATOM   11298 C  CA    . LEU B 1 635 ? 201.688 210.598 233.561 1.00 105.36 ?  654 LEU B CA    1 
ATOM   11299 C  C     . LEU B 1 635 ? 202.424 210.795 234.882 1.00 104.55 ?  654 LEU B C     1 
ATOM   11300 O  O     . LEU B 1 635 ? 202.123 211.777 235.585 1.00 103.82 ?  654 LEU B O     1 
ATOM   11301 C  CB    . LEU B 1 635 ? 200.767 209.372 233.650 1.00 105.17 ?  654 LEU B CB    1 
ATOM   11302 C  CG    . LEU B 1 635 ? 199.809 209.329 234.842 1.00 106.65 ?  654 LEU B CG    1 
ATOM   11303 C  CD1   . LEU B 1 635 ? 198.673 210.329 234.674 1.00 104.45 ?  654 LEU B CD1   1 
ATOM   11304 C  CD2   . LEU B 1 635 ? 199.291 207.919 235.082 1.00 106.43 ?  654 LEU B CD2   1 
ATOM   11305 N  N     . PRO B 1 636 ? 203.377 209.936 235.277 1.00 108.32 ?  655 PRO B N     1 
ATOM   11306 C  CA    . PRO B 1 636 ? 203.993 210.106 236.601 1.00 109.47 ?  655 PRO B CA    1 
ATOM   11307 C  C     . PRO B 1 636 ? 204.686 211.438 236.772 1.00 108.76 ?  655 PRO B C     1 
ATOM   11308 O  O     . PRO B 1 636 ? 204.721 211.957 237.891 1.00 108.22 ?  655 PRO B O     1 
ATOM   11309 C  CB    . PRO B 1 636 ? 204.986 208.936 236.684 1.00 109.97 ?  655 PRO B CB    1 
ATOM   11310 C  CG    . PRO B 1 636 ? 204.520 207.959 235.665 1.00 109.19 ?  655 PRO B CG    1 
ATOM   11311 C  CD    . PRO B 1 636 ? 203.973 208.795 234.558 1.00 109.25 ?  655 PRO B CD    1 
ATOM   11312 N  N     . ASN B 1 637 ? 205.221 212.021 235.697 1.00 109.31 ?  656 ASN B N     1 
ATOM   11313 C  CA    . ASN B 1 637 ? 205.914 213.299 235.825 1.00 108.74 ?  656 ASN B CA    1 
ATOM   11314 C  C     . ASN B 1 637 ? 204.977 214.385 236.343 1.00 108.47 ?  656 ASN B C     1 
ATOM   11315 O  O     . ASN B 1 637 ? 205.251 215.015 237.374 1.00 108.73 ?  656 ASN B O     1 
ATOM   11316 C  CB    . ASN B 1 637 ? 206.521 213.699 234.480 1.00 108.63 ?  656 ASN B CB    1 
ATOM   11317 C  CG    . ASN B 1 637 ? 207.396 212.609 233.889 1.00 108.84 ?  656 ASN B CG    1 
ATOM   11318 O  OD1   . ASN B 1 637 ? 206.904 211.685 233.241 1.00 107.58 ?  656 ASN B OD1   1 
ATOM   11319 N  ND2   . ASN B 1 637 ? 208.701 212.712 234.113 1.00 106.80 ?  656 ASN B ND2   1 
ATOM   11320 N  N     . GLN B 1 638 ? 203.836 214.586 235.674 1.00 104.39 ?  657 GLN B N     1 
ATOM   11321 C  CA    . GLN B 1 638 ? 202.950 215.654 236.122 1.00 105.95 ?  657 GLN B CA    1 
ATOM   11322 C  C     . GLN B 1 638 ? 202.225 215.274 237.404 1.00 104.42 ?  657 GLN B C     1 
ATOM   11323 O  O     . GLN B 1 638 ? 201.897 216.156 238.202 1.00 102.00 ?  657 GLN B O     1 
ATOM   11324 C  CB    . GLN B 1 638 ? 201.928 216.047 235.048 1.00 103.66 ?  657 GLN B CB    1 
ATOM   11325 C  CG    . GLN B 1 638 ? 200.670 215.197 235.020 1.00 102.56 ?  657 GLN B CG    1 
ATOM   11326 C  CD    . GLN B 1 638 ? 200.771 214.041 234.066 1.00 102.65 ?  657 GLN B CD    1 
ATOM   11327 O  OE1   . GLN B 1 638 ? 201.848 213.731 233.571 1.00 102.51 ?  657 GLN B OE1   1 
ATOM   11328 N  NE2   . GLN B 1 638 ? 199.651 213.372 233.827 1.00 103.84 ?  657 GLN B NE2   1 
ATOM   11329 N  N     . VAL B 1 639 ? 201.981 213.980 237.644 1.00 104.80 ?  658 VAL B N     1 
ATOM   11330 C  CA    . VAL B 1 639 ? 201.307 213.616 238.889 1.00 103.88 ?  658 VAL B CA    1 
ATOM   11331 C  C     . VAL B 1 639 ? 202.228 213.853 240.086 1.00 104.94 ?  658 VAL B C     1 
ATOM   11332 O  O     . VAL B 1 639 ? 201.804 214.390 241.119 1.00 105.92 ?  658 VAL B O     1 
ATOM   11333 C  CB    . VAL B 1 639 ? 200.793 212.167 238.820 1.00 103.88 ?  658 VAL B CB    1 
ATOM   11334 C  CG1   . VAL B 1 639 ? 200.046 211.809 240.081 1.00 101.19 ?  658 VAL B CG1   1 
ATOM   11335 C  CG2   . VAL B 1 639 ? 199.860 212.004 237.636 1.00 104.28 ?  658 VAL B CG2   1 
ATOM   11336 N  N     . SER B 1 640 ? 203.508 213.490 239.957 1.00 106.21 ?  659 SER B N     1 
ATOM   11337 C  CA    . SER B 1 640 ? 204.478 213.775 241.008 1.00 106.36 ?  659 SER B CA    1 
ATOM   11338 C  C     . SER B 1 640 ? 204.664 215.275 241.188 1.00 106.13 ?  659 SER B C     1 
ATOM   11339 O  O     . SER B 1 640 ? 204.816 215.757 242.318 1.00 106.83 ?  659 SER B O     1 
ATOM   11340 C  CB    . SER B 1 640 ? 205.814 213.109 240.680 1.00 107.86 ?  659 SER B CB    1 
ATOM   11341 O  OG    . SER B 1 640 ? 205.629 211.772 240.249 1.00 109.49 ?  659 SER B OG    1 
ATOM   11342 N  N     . ASP B 1 641 ? 204.673 216.029 240.083 1.00 101.69 ?  660 ASP B N     1 
ATOM   11343 C  CA    . ASP B 1 641 ? 204.742 217.481 240.193 1.00 102.10 ?  660 ASP B CA    1 
ATOM   11344 C  C     . ASP B 1 641 ? 203.551 218.022 240.972 1.00 100.79 ?  660 ASP B C     1 
ATOM   11345 O  O     . ASP B 1 641 ? 203.708 218.887 241.841 1.00 100.95 ?  660 ASP B O     1 
ATOM   11346 C  CB    . ASP B 1 641 ? 204.807 218.112 238.802 1.00 101.18 ?  660 ASP B CB    1 
ATOM   11347 C  CG    . ASP B 1 641 ? 206.132 217.860 238.108 1.00 101.99 ?  660 ASP B CG    1 
ATOM   11348 O  OD1   . ASP B 1 641 ? 207.150 217.685 238.808 1.00 103.03 ?  660 ASP B OD1   1 
ATOM   11349 O  OD2   . ASP B 1 641 ? 206.155 217.836 236.859 1.00 101.12 -1 660 ASP B OD2   1 
ATOM   11350 N  N     . ALA B 1 642 ? 202.355 217.503 240.687 1.00 97.02  ?  661 ALA B N     1 
ATOM   11351 C  CA    . ALA B 1 642 ? 201.156 217.953 241.382 1.00 97.15  ?  661 ALA B CA    1 
ATOM   11352 C  C     . ALA B 1 642 ? 201.225 217.646 242.872 1.00 96.64  ?  661 ALA B C     1 
ATOM   11353 O  O     . ALA B 1 642 ? 200.837 218.480 243.699 1.00 98.73  ?  661 ALA B O     1 
ATOM   11354 C  CB    . ALA B 1 642 ? 199.921 217.310 240.754 1.00 98.24  ?  661 ALA B CB    1 
ATOM   11355 N  N     . MET B 1 643 ? 201.702 216.453 243.241 1.00 94.33  ?  662 MET B N     1 
ATOM   11356 C  CA    . MET B 1 643 ? 201.840 216.158 244.667 1.00 96.40  ?  662 MET B CA    1 
ATOM   11357 C  C     . MET B 1 643 ? 202.868 217.064 245.336 1.00 97.23  ?  662 MET B C     1 
ATOM   11358 O  O     . MET B 1 643 ? 202.575 217.696 246.358 1.00 95.33  ?  662 MET B O     1 
ATOM   11359 C  CB    . MET B 1 643 ? 202.200 214.692 244.921 1.00 97.28  ?  662 MET B CB    1 
ATOM   11360 C  CG    . MET B 1 643 ? 201.017 213.737 245.027 1.00 97.88  ?  662 MET B CG    1 
ATOM   11361 S  SD    . MET B 1 643 ? 200.362 213.120 243.479 1.00 102.81 ?  662 MET B SD    1 
ATOM   11362 C  CE    . MET B 1 643 ? 201.618 211.890 243.137 1.00 97.71  ?  662 MET B CE    1 
ATOM   11363 N  N     . HIS B 1 644 ? 204.077 217.143 244.782 1.00 101.26 ?  663 HIS B N     1 
ATOM   11364 C  CA    . HIS B 1 644 ? 205.171 217.783 245.503 1.00 102.54 ?  663 HIS B CA    1 
ATOM   11365 C  C     . HIS B 1 644 ? 205.226 219.293 245.304 1.00 101.50 ?  663 HIS B C     1 
ATOM   11366 O  O     . HIS B 1 644 ? 206.095 219.944 245.892 1.00 101.31 ?  663 HIS B O     1 
ATOM   11367 C  CB    . HIS B 1 644 ? 206.517 217.154 245.116 1.00 102.00 ?  663 HIS B CB    1 
ATOM   11368 C  CG    . HIS B 1 644 ? 207.163 217.771 243.914 1.00 101.62 ?  663 HIS B CG    1 
ATOM   11369 N  ND1   . HIS B 1 644 ? 206.951 217.309 242.633 1.00 102.62 ?  663 HIS B ND1   1 
ATOM   11370 C  CD2   . HIS B 1 644 ? 208.034 218.803 243.803 1.00 99.78  ?  663 HIS B CD2   1 
ATOM   11371 C  CE1   . HIS B 1 644 ? 207.657 218.036 241.785 1.00 101.68 ?  663 HIS B CE1   1 
ATOM   11372 N  NE2   . HIS B 1 644 ? 208.320 218.950 242.468 1.00 100.91 ?  663 HIS B NE2   1 
ATOM   11373 N  N     . ALA B 1 645 ? 204.328 219.872 244.502 1.00 95.85  ?  664 ALA B N     1 
ATOM   11374 C  CA    . ALA B 1 645 ? 204.254 221.326 244.439 1.00 95.04  ?  664 ALA B CA    1 
ATOM   11375 C  C     . ALA B 1 645 ? 203.284 221.891 245.467 1.00 95.84  ?  664 ALA B C     1 
ATOM   11376 O  O     . ALA B 1 645 ? 203.193 223.115 245.618 1.00 95.66  ?  664 ALA B O     1 
ATOM   11377 C  CB    . ALA B 1 645 ? 203.849 221.776 243.034 1.00 91.96  ?  664 ALA B CB    1 
ATOM   11378 N  N     . TRP B 1 646 ? 202.555 221.029 246.177 1.00 87.19  ?  665 TRP B N     1 
ATOM   11379 C  CA    . TRP B 1 646 ? 201.589 221.468 247.175 1.00 84.95  ?  665 TRP B CA    1 
ATOM   11380 C  C     . TRP B 1 646 ? 201.608 220.612 248.437 1.00 83.50  ?  665 TRP B C     1 
ATOM   11381 O  O     . TRP B 1 646 ? 200.795 220.847 249.340 1.00 83.52  ?  665 TRP B O     1 
ATOM   11382 C  CB    . TRP B 1 646 ? 200.179 221.482 246.574 1.00 83.61  ?  665 TRP B CB    1 
ATOM   11383 C  CG    . TRP B 1 646 ? 199.890 222.700 245.746 1.00 83.42  ?  665 TRP B CG    1 
ATOM   11384 C  CD1   . TRP B 1 646 ? 199.772 223.985 246.190 1.00 84.26  ?  665 TRP B CD1   1 
ATOM   11385 C  CD2   . TRP B 1 646 ? 199.680 222.746 244.328 1.00 85.52  ?  665 TRP B CD2   1 
ATOM   11386 N  NE1   . TRP B 1 646 ? 199.502 224.827 245.138 1.00 83.20  ?  665 TRP B NE1   1 
ATOM   11387 C  CE2   . TRP B 1 646 ? 199.441 224.091 243.984 1.00 84.15  ?  665 TRP B CE2   1 
ATOM   11388 C  CE3   . TRP B 1 646 ? 199.673 221.780 243.317 1.00 85.06  ?  665 TRP B CE3   1 
ATOM   11389 C  CZ2   . TRP B 1 646 ? 199.197 224.495 242.673 1.00 82.29  ?  665 TRP B CZ2   1 
ATOM   11390 C  CZ3   . TRP B 1 646 ? 199.429 222.183 242.016 1.00 84.68  ?  665 TRP B CZ3   1 
ATOM   11391 C  CH2   . TRP B 1 646 ? 199.195 223.528 241.706 1.00 82.00  ?  665 TRP B CH2   1 
ATOM   11392 N  N     . GLY B 1 647 ? 202.509 219.635 248.531 1.00 88.43  ?  666 GLY B N     1 
ATOM   11393 C  CA    . GLY B 1 647 ? 202.597 218.807 249.720 1.00 90.92  ?  666 GLY B CA    1 
ATOM   11394 C  C     . GLY B 1 647 ? 201.342 217.995 249.963 1.00 92.31  ?  666 GLY B C     1 
ATOM   11395 O  O     . GLY B 1 647 ? 200.834 217.934 251.087 1.00 92.12  ?  666 GLY B O     1 
ATOM   11396 N  N     . ILE B 1 648 ? 200.834 217.368 248.906 1.00 91.62  ?  667 ILE B N     1 
ATOM   11397 C  CA    . ILE B 1 648 ? 199.543 216.689 248.929 1.00 92.40  ?  667 ILE B CA    1 
ATOM   11398 C  C     . ILE B 1 648 ? 199.750 215.208 248.615 1.00 92.44  ?  667 ILE B C     1 
ATOM   11399 O  O     . ILE B 1 648 ? 198.940 214.582 247.920 1.00 93.61  ?  667 ILE B O     1 
ATOM   11400 C  CB    . ILE B 1 648 ? 198.546 217.381 247.974 1.00 92.66  ?  667 ILE B CB    1 
ATOM   11401 C  CG1   . ILE B 1 648 ? 197.111 216.935 248.268 1.00 92.91  ?  667 ILE B CG1   1 
ATOM   11402 C  CG2   . ILE B 1 648 ? 198.944 217.213 246.505 1.00 91.63  ?  667 ILE B CG2   1 
ATOM   11403 C  CD1   . ILE B 1 648 ? 196.661 217.212 249.688 1.00 91.83  ?  667 ILE B CD1   1 
ATOM   11404 N  N     . ASP B 1 649 ? 200.854 214.652 249.128 1.00 91.18  ?  668 ASP B N     1 
ATOM   11405 C  CA    . ASP B 1 649 ? 201.314 213.298 248.818 1.00 93.10  ?  668 ASP B CA    1 
ATOM   11406 C  C     . ASP B 1 649 ? 200.169 212.296 248.726 1.00 93.72  ?  668 ASP B C     1 
ATOM   11407 O  O     . ASP B 1 649 ? 199.200 212.356 249.487 1.00 92.94  ?  668 ASP B O     1 
ATOM   11408 C  CB    . ASP B 1 649 ? 202.318 212.836 249.880 1.00 93.79  ?  668 ASP B CB    1 
ATOM   11409 C  CG    . ASP B 1 649 ? 201.821 213.070 251.294 1.00 95.58  ?  668 ASP B CG    1 
ATOM   11410 O  OD1   . ASP B 1 649 ? 200.776 213.734 251.457 1.00 92.51  ?  668 ASP B OD1   1 
ATOM   11411 O  OD2   . ASP B 1 649 ? 202.475 212.586 252.243 1.00 96.39  -1 668 ASP B OD2   1 
ATOM   11412 N  N     . GLY B 1 650 ? 200.316 211.356 247.793 1.00 86.65  ?  669 GLY B N     1 
ATOM   11413 C  CA    . GLY B 1 650 ? 199.243 210.517 247.290 1.00 84.87  ?  669 GLY B CA    1 
ATOM   11414 C  C     . GLY B 1 650 ? 198.402 209.735 248.279 1.00 86.81  ?  669 GLY B C     1 
ATOM   11415 O  O     . GLY B 1 650 ? 197.442 209.074 247.873 1.00 86.72  ?  669 GLY B O     1 
ATOM   11416 N  N     . HIS B 1 651 ? 198.735 209.785 249.570 1.00 86.97  ?  670 HIS B N     1 
ATOM   11417 C  CA    . HIS B 1 651 ? 197.903 209.103 250.558 1.00 84.62  ?  670 HIS B CA    1 
ATOM   11418 C  C     . HIS B 1 651 ? 196.518 209.727 250.696 1.00 85.90  ?  670 HIS B C     1 
ATOM   11419 O  O     . HIS B 1 651 ? 195.716 209.237 251.499 1.00 83.71  ?  670 HIS B O     1 
ATOM   11420 C  CB    . HIS B 1 651 ? 198.601 209.086 251.920 1.00 84.94  ?  670 HIS B CB    1 
ATOM   11421 C  CG    . HIS B 1 651 ? 198.397 210.332 252.724 1.00 88.35  ?  670 HIS B CG    1 
ATOM   11422 N  ND1   . HIS B 1 651 ? 199.197 211.446 252.588 1.00 88.22  ?  670 HIS B ND1   1 
ATOM   11423 C  CD2   . HIS B 1 651 ? 197.486 210.637 253.679 1.00 87.32  ?  670 HIS B CD2   1 
ATOM   11424 C  CE1   . HIS B 1 651 ? 198.786 212.385 253.422 1.00 87.93  ?  670 HIS B CE1   1 
ATOM   11425 N  NE2   . HIS B 1 651 ? 197.749 211.920 254.095 1.00 89.34  ?  670 HIS B NE2   1 
ATOM   11426 N  N     . GLN B 1 652 ? 196.220 210.783 249.942 1.00 84.10  ?  671 GLN B N     1 
ATOM   11427 C  CA    . GLN B 1 652 ? 194.902 211.404 249.905 1.00 81.70  ?  671 GLN B CA    1 
ATOM   11428 C  C     . GLN B 1 652 ? 194.273 211.384 248.521 1.00 79.91  ?  671 GLN B C     1 
ATOM   11429 O  O     . GLN B 1 652 ? 193.057 211.216 248.404 1.00 81.31  ?  671 GLN B O     1 
ATOM   11430 C  CB    . GLN B 1 652 ? 194.988 212.855 250.394 1.00 80.10  ?  671 GLN B CB    1 
ATOM   11431 C  CG    . GLN B 1 652 ? 194.734 213.032 251.882 1.00 81.91  ?  671 GLN B CG    1 
ATOM   11432 C  CD    . GLN B 1 652 ? 194.783 214.485 252.310 1.00 82.38  ?  671 GLN B CD    1 
ATOM   11433 O  OE1   . GLN B 1 652 ? 195.836 215.122 252.263 1.00 82.36  ?  671 GLN B OE1   1 
ATOM   11434 N  NE2   . GLN B 1 652 ? 193.642 215.019 252.729 1.00 81.98  ?  671 GLN B NE2   1 
ATOM   11435 N  N     . LEU B 1 653 ? 195.072 211.554 247.472 1.00 65.81  ?  672 LEU B N     1 
ATOM   11436 C  CA    . LEU B 1 653 ? 194.551 211.552 246.114 1.00 60.66  ?  672 LEU B CA    1 
ATOM   11437 C  C     . LEU B 1 653 ? 194.195 210.134 245.676 1.00 63.01  ?  672 LEU B C     1 
ATOM   11438 O  O     . LEU B 1 653 ? 194.785 209.151 246.133 1.00 68.86  ?  672 LEU B O     1 
ATOM   11439 C  CB    . LEU B 1 653 ? 195.576 212.163 245.157 1.00 67.04  ?  672 LEU B CB    1 
ATOM   11440 C  CG    . LEU B 1 653 ? 195.196 212.342 243.685 1.00 66.48  ?  672 LEU B CG    1 
ATOM   11441 C  CD1   . LEU B 1 653 ? 194.027 213.302 243.545 1.00 66.41  ?  672 LEU B CD1   1 
ATOM   11442 C  CD2   . LEU B 1 653 ? 196.391 212.829 242.879 1.00 65.08  ?  672 LEU B CD2   1 
ATOM   11443 N  N     . THR B 1 654 ? 193.215 210.035 244.781 1.00 58.80  ?  673 THR B N     1 
ATOM   11444 C  CA    . THR B 1 654 ? 192.777 208.756 244.243 1.00 58.63  ?  673 THR B CA    1 
ATOM   11445 C  C     . THR B 1 654 ? 192.494 208.917 242.756 1.00 55.35  ?  673 THR B C     1 
ATOM   11446 O  O     . THR B 1 654 ? 192.082 209.986 242.299 1.00 66.34  ?  673 THR B O     1 
ATOM   11447 C  CB    . THR B 1 654 ? 191.526 208.240 244.974 1.00 62.09  ?  673 THR B CB    1 
ATOM   11448 O  OG1   . THR B 1 654 ? 191.733 208.322 246.390 1.00 61.31  ?  673 THR B OG1   1 
ATOM   11449 C  CG2   . THR B 1 654 ? 191.241 206.791 244.605 1.00 60.17  ?  673 THR B CG2   1 
ATOM   11450 N  N     . VAL B 1 655 ? 192.719 207.842 242.003 1.00 47.98  ?  674 VAL B N     1 
ATOM   11451 C  CA    . VAL B 1 655 ? 192.511 207.824 240.561 1.00 47.58  ?  674 VAL B CA    1 
ATOM   11452 C  C     . VAL B 1 655 ? 191.591 206.659 240.226 1.00 50.34  ?  674 VAL B C     1 
ATOM   11453 O  O     . VAL B 1 655 ? 191.830 205.529 240.663 1.00 65.92  ?  674 VAL B O     1 
ATOM   11454 C  CB    . VAL B 1 655 ? 193.842 207.702 239.794 1.00 53.89  ?  674 VAL B CB    1 
ATOM   11455 C  CG1   . VAL B 1 655 ? 193.600 207.242 238.366 1.00 58.70  ?  674 VAL B CG1   1 
ATOM   11456 C  CG2   . VAL B 1 655 ? 194.589 209.027 239.814 1.00 55.04  ?  674 VAL B CG2   1 
ATOM   11457 N  N     . GLU B 1 656 ? 190.536 206.934 239.461 1.00 47.00  ?  675 GLU B N     1 
ATOM   11458 C  CA    . GLU B 1 656 ? 189.621 205.906 238.978 1.00 54.59  ?  675 GLU B CA    1 
ATOM   11459 C  C     . GLU B 1 656 ? 189.807 205.756 237.476 1.00 52.19  ?  675 GLU B C     1 
ATOM   11460 O  O     . GLU B 1 656 ? 189.893 206.756 236.755 1.00 54.79  ?  675 GLU B O     1 
ATOM   11461 C  CB    . GLU B 1 656 ? 188.168 206.243 239.321 1.00 59.19  ?  675 GLU B CB    1 
ATOM   11462 C  CG    . GLU B 1 656 ? 187.715 207.627 238.892 1.00 64.63  ?  675 GLU B CG    1 
ATOM   11463 C  CD    . GLU B 1 656 ? 187.901 208.657 239.985 1.00 68.06  ?  675 GLU B CD    1 
ATOM   11464 O  OE1   . GLU B 1 656 ? 188.674 208.389 240.928 1.00 70.69  ?  675 GLU B OE1   1 
ATOM   11465 O  OE2   . GLU B 1 656 ? 187.269 209.731 239.907 1.00 65.11  -1 675 GLU B OE2   1 
ATOM   11466 N  N     . ILE B 1 657 ? 189.877 204.515 237.011 1.00 70.96  ?  676 ILE B N     1 
ATOM   11467 C  CA    . ILE B 1 657 ? 190.153 204.238 235.610 1.00 73.03  ?  676 ILE B CA    1 
ATOM   11468 C  C     . ILE B 1 657 ? 188.920 203.633 234.952 1.00 74.47  ?  676 ILE B C     1 
ATOM   11469 O  O     . ILE B 1 657 ? 187.936 203.283 235.607 1.00 74.97  ?  676 ILE B O     1 
ATOM   11470 C  CB    . ILE B 1 657 ? 191.374 203.311 235.450 1.00 75.10  ?  676 ILE B CB    1 
ATOM   11471 C  CG1   . ILE B 1 657 ? 191.131 201.982 236.168 1.00 77.35  ?  676 ILE B CG1   1 
ATOM   11472 C  CG2   . ILE B 1 657 ? 192.627 203.989 235.975 1.00 73.91  ?  676 ILE B CG2   1 
ATOM   11473 C  CD1   . ILE B 1 657 ? 192.268 200.995 236.023 1.00 76.47  ?  676 ILE B CD1   1 
ATOM   11474 N  N     . THR B 1 658 ? 188.983 203.509 233.629 1.00 98.99  ?  677 THR B N     1 
ATOM   11475 C  CA    . THR B 1 658 ? 187.900 202.896 232.873 1.00 102.75 ?  677 THR B CA    1 
ATOM   11476 C  C     . THR B 1 658 ? 188.072 201.381 232.844 1.00 104.43 ?  677 THR B C     1 
ATOM   11477 O  O     . THR B 1 658 ? 189.195 200.868 232.828 1.00 105.92 ?  677 THR B O     1 
ATOM   11478 C  CB    . THR B 1 658 ? 187.870 203.458 231.449 1.00 101.81 ?  677 THR B CB    1 
ATOM   11479 O  OG1   . THR B 1 658 ? 187.856 204.890 231.502 1.00 101.49 ?  677 THR B OG1   1 
ATOM   11480 C  CG2   . THR B 1 658 ? 186.634 202.980 230.699 1.00 101.18 ?  677 THR B CG2   1 
ATOM   11481 N  N     . GLU B 1 659 ? 186.945 200.663 232.853 1.00 120.48 ?  678 GLU B N     1 
ATOM   11482 C  CA    . GLU B 1 659 ? 186.988 199.204 232.791 1.00 123.44 ?  678 GLU B CA    1 
ATOM   11483 C  C     . GLU B 1 659 ? 187.667 198.717 231.516 1.00 124.13 ?  678 GLU B C     1 
ATOM   11484 O  O     . GLU B 1 659 ? 188.269 197.635 231.505 1.00 122.40 ?  678 GLU B O     1 
ATOM   11485 C  CB    . GLU B 1 659 ? 185.569 198.638 232.902 1.00 122.72 ?  678 GLU B CB    1 
ATOM   11486 C  CG    . GLU B 1 659 ? 185.463 197.130 232.723 1.00 123.48 ?  678 GLU B CG    1 
ATOM   11487 C  CD    . GLU B 1 659 ? 185.075 196.735 231.311 1.00 124.61 ?  678 GLU B CD    1 
ATOM   11488 O  OE1   . GLU B 1 659 ? 184.517 197.587 230.587 1.00 125.03 ?  678 GLU B OE1   1 
ATOM   11489 O  OE2   . GLU B 1 659 ? 185.330 195.576 230.923 1.00 124.67 -1 678 GLU B OE2   1 
ATOM   11490 N  N     . SER B 1 660 ? 187.583 199.497 230.434 1.00 127.40 ?  679 SER B N     1 
ATOM   11491 C  CA    . SER B 1 660 ? 188.263 199.127 229.198 1.00 127.22 ?  679 SER B CA    1 
ATOM   11492 C  C     . SER B 1 660 ? 189.772 199.053 229.387 1.00 127.39 ?  679 SER B C     1 
ATOM   11493 O  O     . SER B 1 660 ? 190.444 198.271 228.706 1.00 127.52 ?  679 SER B O     1 
ATOM   11494 C  CB    . SER B 1 660 ? 187.915 200.120 228.089 1.00 126.34 ?  679 SER B CB    1 
ATOM   11495 O  OG    . SER B 1 660 ? 186.514 200.200 227.895 1.00 125.93 ?  679 SER B OG    1 
ATOM   11496 N  N     . MET B 1 661 ? 190.323 199.850 230.306 1.00 120.67 ?  680 MET B N     1 
ATOM   11497 C  CA    . MET B 1 661 ? 191.758 199.787 230.564 1.00 120.58 ?  680 MET B CA    1 
ATOM   11498 C  C     . MET B 1 661 ? 192.163 198.424 231.111 1.00 119.46 ?  680 MET B C     1 
ATOM   11499 O  O     . MET B 1 661 ? 193.165 197.844 230.675 1.00 119.00 ?  680 MET B O     1 
ATOM   11500 C  CB    . MET B 1 661 ? 192.170 200.892 231.534 1.00 119.35 ?  680 MET B CB    1 
ATOM   11501 C  CG    . MET B 1 661 ? 191.970 202.291 230.994 1.00 118.24 ?  680 MET B CG    1 
ATOM   11502 S  SD    . MET B 1 661 ? 192.655 203.529 232.103 1.00 120.94 ?  680 MET B SD    1 
ATOM   11503 C  CE    . MET B 1 661 ? 194.392 203.115 231.984 1.00 117.52 ?  680 MET B CE    1 
ATOM   11504 N  N     . MET B 1 662 ? 191.397 197.895 232.068 1.00 126.86 ?  681 MET B N     1 
ATOM   11505 C  CA    . MET B 1 662 ? 191.703 196.571 232.596 1.00 128.73 ?  681 MET B CA    1 
ATOM   11506 C  C     . MET B 1 662 ? 191.327 195.477 231.608 1.00 128.43 ?  681 MET B C     1 
ATOM   11507 O  O     . MET B 1 662 ? 191.915 194.390 231.636 1.00 127.65 ?  681 MET B O     1 
ATOM   11508 C  CB    . MET B 1 662 ? 190.996 196.358 233.933 1.00 128.07 ?  681 MET B CB    1 
ATOM   11509 C  CG    . MET B 1 662 ? 191.666 197.079 235.090 1.00 128.12 ?  681 MET B CG    1 
ATOM   11510 S  SD    . MET B 1 662 ? 193.417 196.668 235.238 1.00 131.76 ?  681 MET B SD    1 
ATOM   11511 C  CE    . MET B 1 662 ? 193.351 194.878 235.298 1.00 126.24 ?  681 MET B CE    1 
ATOM   11512 N  N     . MET B 1 663 ? 190.348 195.738 230.739 1.00 133.32 ?  682 MET B N     1 
ATOM   11513 C  CA    . MET B 1 663 ? 190.070 194.811 229.647 1.00 133.06 ?  682 MET B CA    1 
ATOM   11514 C  C     . MET B 1 663 ? 191.276 194.686 228.725 1.00 134.53 ?  682 MET B C     1 
ATOM   11515 O  O     . MET B 1 663 ? 191.622 193.584 228.282 1.00 134.76 ?  682 MET B O     1 
ATOM   11516 C  CB    . MET B 1 663 ? 188.836 195.271 228.869 1.00 133.30 ?  682 MET B CB    1 
ATOM   11517 C  CG    . MET B 1 663 ? 188.468 194.378 227.694 1.00 133.39 ?  682 MET B CG    1 
ATOM   11518 S  SD    . MET B 1 663 ? 189.048 195.026 226.114 1.00 133.29 ?  682 MET B SD    1 
ATOM   11519 C  CE    . MET B 1 663 ? 187.962 196.435 225.905 1.00 131.96 ?  682 MET B CE    1 
ATOM   11520 N  N     . GLU B 1 664 ? 191.925 195.807 228.425 1.00 132.19 ?  683 GLU B N     1 
ATOM   11521 C  CA    . GLU B 1 664 ? 193.167 195.790 227.667 1.00 130.68 ?  683 GLU B CA    1 
ATOM   11522 C  C     . GLU B 1 664 ? 194.282 195.148 228.487 1.00 130.73 ?  683 GLU B C     1 
ATOM   11523 O  O     . GLU B 1 664 ? 194.273 195.174 229.720 1.00 130.06 ?  683 GLU B O     1 
ATOM   11524 C  CB    . GLU B 1 664 ? 193.568 197.209 227.262 1.00 130.11 ?  683 GLU B CB    1 
ATOM   11525 C  CG    . GLU B 1 664 ? 192.621 197.870 226.274 1.00 130.86 ?  683 GLU B CG    1 
ATOM   11526 C  CD    . GLU B 1 664 ? 192.903 199.350 226.100 1.00 131.71 ?  683 GLU B CD    1 
ATOM   11527 O  OE1   . GLU B 1 664 ? 193.848 199.856 226.741 1.00 131.31 ?  683 GLU B OE1   1 
ATOM   11528 O  OE2   . GLU B 1 664 ? 192.181 200.008 225.321 1.00 130.94 -1 683 GLU B OE2   1 
ATOM   11529 N  N     . HIS B 1 665 ? 195.251 194.565 227.785 1.00 129.26 ?  684 HIS B N     1 
ATOM   11530 C  CA    . HIS B 1 665 ? 196.375 193.860 228.400 1.00 128.72 ?  684 HIS B CA    1 
ATOM   11531 C  C     . HIS B 1 665 ? 197.668 194.434 227.825 1.00 128.87 ?  684 HIS B C     1 
ATOM   11532 O  O     . HIS B 1 665 ? 198.157 193.974 226.790 1.00 128.37 ?  684 HIS B O     1 
ATOM   11533 C  CB    . HIS B 1 665 ? 196.276 192.350 228.156 1.00 129.57 ?  684 HIS B CB    1 
ATOM   11534 C  CG    . HIS B 1 665 ? 195.234 191.667 228.987 1.00 130.64 ?  684 HIS B CG    1 
ATOM   11535 N  ND1   . HIS B 1 665 ? 193.938 192.128 229.086 1.00 130.65 ?  684 HIS B ND1   1 
ATOM   11536 C  CD2   . HIS B 1 665 ? 195.295 190.551 229.751 1.00 129.84 ?  684 HIS B CD2   1 
ATOM   11537 C  CE1   . HIS B 1 665 ? 193.248 191.328 229.880 1.00 129.18 ?  684 HIS B CE1   1 
ATOM   11538 N  NE2   . HIS B 1 665 ? 194.048 190.363 230.296 1.00 130.57 ?  684 HIS B NE2   1 
ATOM   11539 N  N     . ASP B 1 666 ? 198.223 195.439 228.500 1.00 122.82 ?  685 ASP B N     1 
ATOM   11540 C  CA    . ASP B 1 666 ? 199.458 196.087 228.077 1.00 121.41 ?  685 ASP B CA    1 
ATOM   11541 C  C     . ASP B 1 666 ? 200.467 196.061 229.216 1.00 119.45 ?  685 ASP B C     1 
ATOM   11542 O  O     . ASP B 1 666 ? 200.197 196.583 230.304 1.00 119.05 ?  685 ASP B O     1 
ATOM   11543 C  CB    . ASP B 1 666 ? 199.194 197.526 227.627 1.00 119.96 ?  685 ASP B CB    1 
ATOM   11544 C  CG    . ASP B 1 666 ? 198.308 197.597 226.397 1.00 121.28 ?  685 ASP B CG    1 
ATOM   11545 O  OD1   . ASP B 1 666 ? 198.327 196.641 225.595 1.00 121.82 ?  685 ASP B OD1   1 
ATOM   11546 O  OD2   . ASP B 1 666 ? 197.591 198.607 226.234 1.00 120.63 -1 685 ASP B OD2   1 
ATOM   11547 N  N     . THR B 1 667 ? 201.632 195.462 228.956 1.00 119.08 ?  686 THR B N     1 
ATOM   11548 C  CA    . THR B 1 667 ? 202.649 195.328 229.994 1.00 119.66 ?  686 THR B CA    1 
ATOM   11549 C  C     . THR B 1 667 ? 203.187 196.686 230.430 1.00 119.30 ?  686 THR B C     1 
ATOM   11550 O  O     . THR B 1 667 ? 203.398 196.921 231.625 1.00 119.58 ?  686 THR B O     1 
ATOM   11551 C  CB    . THR B 1 667 ? 203.790 194.435 229.503 1.00 121.76 ?  686 THR B CB    1 
ATOM   11552 O  OG1   . THR B 1 667 ? 204.423 195.044 228.371 1.00 121.25 ?  686 THR B OG1   1 
ATOM   11553 C  CG2   . THR B 1 667 ? 203.260 193.065 229.108 1.00 120.65 ?  686 THR B CG2   1 
ATOM   11554 N  N     . GLU B 1 668 ? 203.424 197.590 229.476 1.00 121.80 ?  687 GLU B N     1 
ATOM   11555 C  CA    . GLU B 1 668 ? 203.926 198.915 229.826 1.00 122.00 ?  687 GLU B CA    1 
ATOM   11556 C  C     . GLU B 1 668 ? 202.906 199.694 230.649 1.00 121.92 ?  687 GLU B C     1 
ATOM   11557 O  O     . GLU B 1 668 ? 203.267 200.370 231.621 1.00 119.86 ?  687 GLU B O     1 
ATOM   11558 C  CB    . GLU B 1 668 ? 204.311 199.686 228.561 1.00 122.22 ?  687 GLU B CB    1 
ATOM   11559 C  CG    . GLU B 1 668 ? 203.209 199.788 227.514 1.00 123.13 ?  687 GLU B CG    1 
ATOM   11560 C  CD    . GLU B 1 668 ? 203.217 198.625 226.542 1.00 122.25 ?  687 GLU B CD    1 
ATOM   11561 O  OE1   . GLU B 1 668 ? 202.250 198.491 225.763 1.00 122.18 ?  687 GLU B OE1   1 
ATOM   11562 O  OE2   . GLU B 1 668 ? 204.192 197.844 226.556 1.00 120.85 -1 687 GLU B OE2   1 
ATOM   11563 N  N     . ILE B 1 669 ? 201.626 199.604 230.281 1.00 123.89 ?  688 ILE B N     1 
ATOM   11564 C  CA    . ILE B 1 669 ? 200.581 200.275 231.048 1.00 122.02 ?  688 ILE B CA    1 
ATOM   11565 C  C     . ILE B 1 669 ? 200.505 199.701 232.456 1.00 120.76 ?  688 ILE B C     1 
ATOM   11566 O  O     . ILE B 1 669 ? 200.369 200.441 233.437 1.00 121.04 ?  688 ILE B O     1 
ATOM   11567 C  CB    . ILE B 1 669 ? 199.229 200.174 230.316 1.00 122.23 ?  688 ILE B CB    1 
ATOM   11568 C  CG1   . ILE B 1 669 ? 199.247 201.023 229.044 1.00 121.77 ?  688 ILE B CG1   1 
ATOM   11569 C  CG2   . ILE B 1 669 ? 198.088 200.603 231.229 1.00 121.34 ?  688 ILE B CG2   1 
ATOM   11570 C  CD1   . ILE B 1 669 ? 197.914 201.088 228.331 1.00 122.64 ?  688 ILE B CD1   1 
ATOM   11571 N  N     . PHE B 1 670 ? 200.594 198.374 232.580 1.00 118.17 ?  689 PHE B N     1 
ATOM   11572 C  CA    . PHE B 1 670 ? 200.555 197.751 233.900 1.00 117.18 ?  689 PHE B CA    1 
ATOM   11573 C  C     . PHE B 1 670 ? 201.749 198.168 234.751 1.00 116.45 ?  689 PHE B C     1 
ATOM   11574 O  O     . PHE B 1 670 ? 201.605 198.410 235.955 1.00 115.89 ?  689 PHE B O     1 
ATOM   11575 C  CB    . PHE B 1 670 ? 200.495 196.230 233.761 1.00 117.89 ?  689 PHE B CB    1 
ATOM   11576 C  CG    . PHE B 1 670 ? 199.116 195.698 233.484 1.00 118.39 ?  689 PHE B CG    1 
ATOM   11577 C  CD1   . PHE B 1 670 ? 198.247 196.376 232.644 1.00 119.08 ?  689 PHE B CD1   1 
ATOM   11578 C  CD2   . PHE B 1 670 ? 198.690 194.515 234.061 1.00 117.81 ?  689 PHE B CD2   1 
ATOM   11579 C  CE1   . PHE B 1 670 ? 196.981 195.887 232.389 1.00 118.13 ?  689 PHE B CE1   1 
ATOM   11580 C  CE2   . PHE B 1 670 ? 197.427 194.022 233.808 1.00 118.81 ?  689 PHE B CE2   1 
ATOM   11581 C  CZ    . PHE B 1 670 ? 196.571 194.708 232.972 1.00 118.26 ?  689 PHE B CZ    1 
ATOM   11582 N  N     . LYS B 1 671 ? 202.937 198.249 234.148 1.00 115.26 ?  690 LYS B N     1 
ATOM   11583 C  CA    . LYS B 1 671 ? 204.113 198.699 234.888 1.00 114.72 ?  690 LYS B CA    1 
ATOM   11584 C  C     . LYS B 1 671 ? 203.963 200.148 235.334 1.00 114.31 ?  690 LYS B C     1 
ATOM   11585 O  O     . LYS B 1 671 ? 204.345 200.502 236.456 1.00 112.94 ?  690 LYS B O     1 
ATOM   11586 C  CB    . LYS B 1 671 ? 205.370 198.523 234.037 1.00 113.81 ?  690 LYS B CB    1 
ATOM   11587 C  CG    . LYS B 1 671 ? 205.757 197.073 233.800 1.00 114.76 ?  690 LYS B CG    1 
ATOM   11588 C  CD    . LYS B 1 671 ? 205.843 196.308 235.112 1.00 114.50 ?  690 LYS B CD    1 
ATOM   11589 C  CE    . LYS B 1 671 ? 206.233 194.857 234.885 1.00 113.53 ?  690 LYS B CE    1 
ATOM   11590 N  NZ    . LYS B 1 671 ? 205.304 194.176 233.941 1.00 112.33 1  690 LYS B NZ    1 
ATOM   11591 N  N     . ARG B 1 672 ? 203.413 201.003 234.468 1.00 110.29 ?  691 ARG B N     1 
ATOM   11592 C  CA    . ARG B 1 672 ? 203.168 202.389 234.857 1.00 109.02 ?  691 ARG B CA    1 
ATOM   11593 C  C     . ARG B 1 672 ? 202.168 202.470 236.004 1.00 108.61 ?  691 ARG B C     1 
ATOM   11594 O  O     . ARG B 1 672 ? 202.337 203.272 236.932 1.00 106.94 ?  691 ARG B O     1 
ATOM   11595 C  CB    . ARG B 1 672 ? 202.678 203.193 233.653 1.00 107.99 ?  691 ARG B CB    1 
ATOM   11596 C  CG    . ARG B 1 672 ? 202.549 204.684 233.912 1.00 108.88 ?  691 ARG B CG    1 
ATOM   11597 C  CD    . ARG B 1 672 ? 202.171 205.435 232.645 1.00 110.53 ?  691 ARG B CD    1 
ATOM   11598 N  NE    . ARG B 1 672 ? 203.182 205.292 231.604 1.00 111.64 ?  691 ARG B NE    1 
ATOM   11599 C  CZ    . ARG B 1 672 ? 203.013 204.610 230.480 1.00 110.26 ?  691 ARG B CZ    1 
ATOM   11600 N  NH1   . ARG B 1 672 ? 201.874 203.993 230.210 1.00 108.64 1  691 ARG B NH1   1 
ATOM   11601 N  NH2   . ARG B 1 672 ? 204.011 204.545 229.603 1.00 108.27 ?  691 ARG B NH2   1 
ATOM   11602 N  N     . ILE B 1 673 ? 201.117 201.647 235.956 1.00 109.33 ?  692 ILE B N     1 
ATOM   11603 C  CA    . ILE B 1 673 ? 200.139 201.614 237.041 1.00 106.75 ?  692 ILE B CA    1 
ATOM   11604 C  C     . ILE B 1 673 ? 200.792 201.163 238.340 1.00 106.27 ?  692 ILE B C     1 
ATOM   11605 O  O     . ILE B 1 673 ? 200.520 201.716 239.411 1.00 105.14 ?  692 ILE B O     1 
ATOM   11606 C  CB    . ILE B 1 673 ? 198.946 200.714 236.665 1.00 107.94 ?  692 ILE B CB    1 
ATOM   11607 C  CG1   . ILE B 1 673 ? 198.190 201.297 235.472 1.00 109.54 ?  692 ILE B CG1   1 
ATOM   11608 C  CG2   . ILE B 1 673 ? 198.015 200.536 237.851 1.00 106.95 ?  692 ILE B CG2   1 
ATOM   11609 C  CD1   . ILE B 1 673 ? 197.597 202.660 235.738 1.00 107.19 ?  692 ILE B CD1   1 
ATOM   11610 N  N     . GLN B 1 674 ? 201.650 200.142 238.272 1.00 107.70 ?  693 GLN B N     1 
ATOM   11611 C  CA    . GLN B 1 674 ? 202.335 199.672 239.474 1.00 107.97 ?  693 GLN B CA    1 
ATOM   11612 C  C     . GLN B 1 674 ? 203.250 200.750 240.042 1.00 107.25 ?  693 GLN B C     1 
ATOM   11613 O  O     . GLN B 1 674 ? 203.311 200.946 241.263 1.00 106.84 ?  693 GLN B O     1 
ATOM   11614 C  CB    . GLN B 1 674 ? 203.130 198.403 239.163 1.00 108.49 ?  693 GLN B CB    1 
ATOM   11615 C  CG    . GLN B 1 674 ? 203.943 197.877 240.335 1.00 107.86 ?  693 GLN B CG    1 
ATOM   11616 C  CD    . GLN B 1 674 ? 205.432 198.097 240.158 1.00 108.33 ?  693 GLN B CD    1 
ATOM   11617 O  OE1   . GLN B 1 674 ? 205.944 198.096 239.038 1.00 107.18 ?  693 GLN B OE1   1 
ATOM   11618 N  NE2   . GLN B 1 674 ? 206.138 198.286 241.267 1.00 107.12 ?  693 GLN B NE2   1 
ATOM   11619 N  N     . ILE B 1 675 ? 203.964 201.464 239.169 1.00 102.97 ?  694 ILE B N     1 
ATOM   11620 C  CA    . ILE B 1 675 ? 204.828 202.551 239.621 1.00 104.18 ?  694 ILE B CA    1 
ATOM   11621 C  C     . ILE B 1 675 ? 204.005 203.640 240.298 1.00 101.64 ?  694 ILE B C     1 
ATOM   11622 O  O     . ILE B 1 675 ? 204.375 204.147 241.363 1.00 99.70  ?  694 ILE B O     1 
ATOM   11623 C  CB    . ILE B 1 675 ? 205.647 203.105 238.440 1.00 103.01 ?  694 ILE B CB    1 
ATOM   11624 C  CG1   . ILE B 1 675 ? 206.742 202.114 238.039 1.00 103.87 ?  694 ILE B CG1   1 
ATOM   11625 C  CG2   . ILE B 1 675 ? 206.251 204.458 238.789 1.00 102.65 ?  694 ILE B CG2   1 
ATOM   11626 C  CD1   . ILE B 1 675 ? 207.590 201.635 239.199 1.00 102.33 ?  694 ILE B CD1   1 
ATOM   11627 N  N     . LEU B 1 676 ? 202.871 204.009 239.695 1.00 98.27  ?  695 LEU B N     1 
ATOM   11628 C  CA    . LEU B 1 676 ? 202.011 205.029 240.288 1.00 96.93  ?  695 LEU B CA    1 
ATOM   11629 C  C     . LEU B 1 676 ? 201.456 204.573 241.633 1.00 96.69  ?  695 LEU B C     1 
ATOM   11630 O  O     . LEU B 1 676 ? 201.375 205.363 242.581 1.00 96.75  ?  695 LEU B O     1 
ATOM   11631 C  CB    . LEU B 1 676 ? 200.876 205.378 239.325 1.00 100.49 ?  695 LEU B CB    1 
ATOM   11632 C  CG    . LEU B 1 676 ? 200.156 206.704 239.571 1.00 100.47 ?  695 LEU B CG    1 
ATOM   11633 C  CD1   . LEU B 1 676 ? 200.990 207.871 239.067 1.00 100.30 ?  695 LEU B CD1   1 
ATOM   11634 C  CD2   . LEU B 1 676 ? 198.785 206.699 238.913 1.00 98.28  ?  695 LEU B CD2   1 
ATOM   11635 N  N     . ARG B 1 677 ? 201.063 203.300 241.732 1.00 91.67  ?  696 ARG B N     1 
ATOM   11636 C  CA    . ARG B 1 677 ? 200.569 202.755 242.992 1.00 91.42  ?  696 ARG B CA    1 
ATOM   11637 C  C     . ARG B 1 677 ? 201.648 202.760 244.066 1.00 94.02  ?  696 ARG B C     1 
ATOM   11638 O  O     . ARG B 1 677 ? 201.344 202.966 245.247 1.00 94.96  ?  696 ARG B O     1 
ATOM   11639 C  CB    . ARG B 1 677 ? 200.040 201.337 242.773 1.00 91.93  ?  696 ARG B CB    1 
ATOM   11640 C  CG    . ARG B 1 677 ? 199.498 200.658 244.023 1.00 91.94  ?  696 ARG B CG    1 
ATOM   11641 C  CD    . ARG B 1 677 ? 198.124 201.190 244.398 1.00 91.60  ?  696 ARG B CD    1 
ATOM   11642 N  NE    . ARG B 1 677 ? 197.729 200.798 245.746 1.00 91.32  ?  696 ARG B NE    1 
ATOM   11643 C  CZ    . ARG B 1 677 ? 198.176 201.370 246.856 1.00 92.33  ?  696 ARG B CZ    1 
ATOM   11644 N  NH1   . ARG B 1 677 ? 199.037 202.374 246.820 1.00 91.20  1  696 ARG B NH1   1 
ATOM   11645 N  NH2   . ARG B 1 677 ? 197.745 200.925 248.033 1.00 95.06  ?  696 ARG B NH2   1 
ATOM   11646 N  N     . ASP B 1 678 ? 202.906 202.537 243.679 1.00 102.35 ?  697 ASP B N     1 
ATOM   11647 C  CA    . ASP B 1 678 ? 204.000 202.602 244.641 1.00 102.60 ?  697 ASP B CA    1 
ATOM   11648 C  C     . ASP B 1 678 ? 204.144 203.986 245.263 1.00 100.69 ?  697 ASP B C     1 
ATOM   11649 O  O     . ASP B 1 678 ? 204.756 204.113 246.329 1.00 100.95 ?  697 ASP B O     1 
ATOM   11650 C  CB    . ASP B 1 678 ? 205.316 202.191 243.978 1.00 101.20 ?  697 ASP B CB    1 
ATOM   11651 C  CG    . ASP B 1 678 ? 205.348 200.722 243.608 1.00 101.54 ?  697 ASP B CG    1 
ATOM   11652 O  OD1   . ASP B 1 678 ? 204.677 199.921 244.292 1.00 99.93  ?  697 ASP B OD1   1 
ATOM   11653 O  OD2   . ASP B 1 678 ? 206.049 200.367 242.637 1.00 101.09 -1 697 ASP B OD2   1 
ATOM   11654 N  N     . MET B 1 679 ? 203.600 205.023 244.624 1.00 97.88  ?  698 MET B N     1 
ATOM   11655 C  CA    . MET B 1 679 ? 203.655 206.371 245.174 1.00 97.40  ?  698 MET B CA    1 
ATOM   11656 C  C     . MET B 1 679 ? 202.574 206.636 246.214 1.00 96.47  ?  698 MET B C     1 
ATOM   11657 O  O     . MET B 1 679 ? 202.579 207.709 246.826 1.00 96.96  ?  698 MET B O     1 
ATOM   11658 C  CB    . MET B 1 679 ? 203.548 207.402 244.050 1.00 97.88  ?  698 MET B CB    1 
ATOM   11659 C  CG    . MET B 1 679 ? 204.275 207.003 242.780 1.00 99.17  ?  698 MET B CG    1 
ATOM   11660 S  SD    . MET B 1 679 ? 204.028 208.194 241.454 1.00 103.93 ?  698 MET B SD    1 
ATOM   11661 C  CE    . MET B 1 679 ? 204.410 209.713 242.318 1.00 98.50  ?  698 MET B CE    1 
ATOM   11662 N  N     . GLY B 1 680 ? 201.652 205.698 246.425 1.00 87.67  ?  699 GLY B N     1 
ATOM   11663 C  CA    . GLY B 1 680 ? 200.641 205.823 247.452 1.00 89.40  ?  699 GLY B CA    1 
ATOM   11664 C  C     . GLY B 1 680 ? 199.264 206.224 246.966 1.00 88.63  ?  699 GLY B C     1 
ATOM   11665 O  O     . GLY B 1 680 ? 198.295 206.066 247.720 1.00 90.11  ?  699 GLY B O     1 
ATOM   11666 N  N     . VAL B 1 681 ? 199.142 206.736 245.742 1.00 75.91  ?  700 VAL B N     1 
ATOM   11667 C  CA    . VAL B 1 681 ? 197.834 207.131 245.231 1.00 71.66  ?  700 VAL B CA    1 
ATOM   11668 C  C     . VAL B 1 681 ? 197.002 205.886 244.947 1.00 75.62  ?  700 VAL B C     1 
ATOM   11669 O  O     . VAL B 1 681 ? 197.477 204.924 244.329 1.00 79.20  ?  700 VAL B O     1 
ATOM   11670 C  CB    . VAL B 1 681 ? 197.984 208.020 243.986 1.00 76.03  ?  700 VAL B CB    1 
ATOM   11671 C  CG1   . VAL B 1 681 ? 198.771 207.309 242.895 1.00 78.88  ?  700 VAL B CG1   1 
ATOM   11672 C  CG2   . VAL B 1 681 ? 196.615 208.443 243.469 1.00 75.14  ?  700 VAL B CG2   1 
ATOM   11673 N  N     . GLY B 1 682 ? 195.760 205.892 245.418 1.00 70.28  ?  701 GLY B N     1 
ATOM   11674 C  CA    . GLY B 1 682 ? 194.891 204.746 245.272 1.00 70.21  ?  701 GLY B CA    1 
ATOM   11675 C  C     . GLY B 1 682 ? 194.378 204.577 243.854 1.00 64.39  ?  701 GLY B C     1 
ATOM   11676 O  O     . GLY B 1 682 ? 194.553 205.422 242.976 1.00 68.96  ?  701 GLY B O     1 
ATOM   11677 N  N     . LEU B 1 683 ? 193.716 203.443 243.637 1.00 58.13  ?  702 LEU B N     1 
ATOM   11678 C  CA    . LEU B 1 683 ? 193.155 203.121 242.332 1.00 58.28  ?  702 LEU B CA    1 
ATOM   11679 C  C     . LEU B 1 683 ? 191.761 202.545 242.526 1.00 67.27  ?  702 LEU B C     1 
ATOM   11680 O  O     . LEU B 1 683 ? 191.515 201.818 243.495 1.00 73.38  ?  702 LEU B O     1 
ATOM   11681 C  CB    . LEU B 1 683 ? 194.047 202.134 241.571 1.00 62.85  ?  702 LEU B CB    1 
ATOM   11682 C  CG    . LEU B 1 683 ? 193.785 202.002 240.069 1.00 65.20  ?  702 LEU B CG    1 
ATOM   11683 C  CD1   . LEU B 1 683 ? 193.828 203.363 239.400 1.00 66.79  ?  702 LEU B CD1   1 
ATOM   11684 C  CD2   . LEU B 1 683 ? 194.797 201.071 239.430 1.00 65.81  ?  702 LEU B CD2   1 
ATOM   11685 N  N     . SER B 1 684 ? 190.857 202.874 241.608 1.00 65.59  ?  703 SER B N     1 
ATOM   11686 C  CA    . SER B 1 684 ? 189.474 202.436 241.680 1.00 65.50  ?  703 SER B CA    1 
ATOM   11687 C  C     . SER B 1 684 ? 189.033 201.911 240.322 1.00 60.76  ?  703 SER B C     1 
ATOM   11688 O  O     . SER B 1 684 ? 189.514 202.349 239.274 1.00 59.22  ?  703 SER B O     1 
ATOM   11689 C  CB    . SER B 1 684 ? 188.545 203.570 242.131 1.00 65.47  ?  703 SER B CB    1 
ATOM   11690 O  OG    . SER B 1 684 ? 187.194 203.145 242.144 1.00 69.36  ?  703 SER B OG    1 
ATOM   11691 N  N     . VAL B 1 685 ? 188.107 200.959 240.356 1.00 68.59  ?  704 VAL B N     1 
ATOM   11692 C  CA    . VAL B 1 685 ? 187.563 200.342 239.151 1.00 68.90  ?  704 VAL B CA    1 
ATOM   11693 C  C     . VAL B 1 685 ? 186.047 200.470 239.194 1.00 72.99  ?  704 VAL B C     1 
ATOM   11694 O  O     . VAL B 1 685 ? 185.404 199.998 240.142 1.00 74.54  ?  704 VAL B O     1 
ATOM   11695 C  CB    . VAL B 1 685 ? 187.984 198.875 239.008 1.00 73.51  ?  704 VAL B CB    1 
ATOM   11696 C  CG1   . VAL B 1 685 ? 187.294 198.238 237.811 1.00 74.15  ?  704 VAL B CG1   1 
ATOM   11697 C  CG2   . VAL B 1 685 ? 189.491 198.784 238.856 1.00 75.99  ?  704 VAL B CG2   1 
ATOM   11698 N  N     . ASP B 1 686 ? 185.477 201.106 238.174 1.00 81.28  ?  705 ASP B N     1 
ATOM   11699 C  CA    . ASP B 1 686 ? 184.035 201.231 238.044 1.00 82.55  ?  705 ASP B CA    1 
ATOM   11700 C  C     . ASP B 1 686 ? 183.510 200.232 237.016 1.00 84.81  ?  705 ASP B C     1 
ATOM   11701 O  O     . ASP B 1 686 ? 184.239 199.772 236.132 1.00 87.08  ?  705 ASP B O     1 
ATOM   11702 C  CB    . ASP B 1 686 ? 183.651 202.656 237.643 1.00 84.68  ?  705 ASP B CB    1 
ATOM   11703 C  CG    . ASP B 1 686 ? 182.212 202.993 237.989 1.00 83.77  ?  705 ASP B CG    1 
ATOM   11704 O  OD1   . ASP B 1 686 ? 181.512 202.121 238.544 1.00 83.78  ?  705 ASP B OD1   1 
ATOM   11705 O  OD2   . ASP B 1 686 ? 181.783 204.131 237.707 1.00 82.23  -1 705 ASP B OD2   1 
ATOM   11706 N  N     . ASP B 1 687 ? 182.227 199.889 237.157 1.00 91.70  ?  706 ASP B N     1 
ATOM   11707 C  CA    . ASP B 1 687 ? 181.543 198.922 236.301 1.00 93.77  ?  706 ASP B CA    1 
ATOM   11708 C  C     . ASP B 1 687 ? 182.138 197.525 236.450 1.00 93.17  ?  706 ASP B C     1 
ATOM   11709 O  O     . ASP B 1 687 ? 183.209 197.354 237.042 1.00 94.84  ?  706 ASP B O     1 
ATOM   11710 C  CB    . ASP B 1 687 ? 181.580 199.364 234.833 1.00 95.28  ?  706 ASP B CB    1 
ATOM   11711 C  CG    . ASP B 1 687 ? 180.954 200.726 234.619 1.00 94.35  ?  706 ASP B CG    1 
ATOM   11712 O  OD1   . ASP B 1 687 ? 180.565 201.367 235.618 1.00 92.57  ?  706 ASP B OD1   1 
ATOM   11713 O  OD2   . ASP B 1 687 ? 180.850 201.157 233.451 1.00 92.69  -1 706 ASP B OD2   1 
ATOM   11714 N  N     . PHE B 1 688 ? 181.446 196.516 235.923 1.00 94.84  ?  707 PHE B N     1 
ATOM   11715 C  CA    . PHE B 1 688 ? 181.868 195.127 236.055 1.00 97.02  ?  707 PHE B CA    1 
ATOM   11716 C  C     . PHE B 1 688 ? 181.931 194.424 234.703 1.00 98.38  ?  707 PHE B C     1 
ATOM   11717 O  O     . PHE B 1 688 ? 181.588 193.246 234.592 1.00 94.16  ?  707 PHE B O     1 
ATOM   11718 C  CB    . PHE B 1 688 ? 180.943 194.376 237.012 1.00 96.00  ?  707 PHE B CB    1 
ATOM   11719 C  CG    . PHE B 1 688 ? 180.812 195.028 238.357 1.00 95.64  ?  707 PHE B CG    1 
ATOM   11720 C  CD1   . PHE B 1 688 ? 181.938 195.381 239.081 1.00 93.54  ?  707 PHE B CD1   1 
ATOM   11721 C  CD2   . PHE B 1 688 ? 179.565 195.300 238.893 1.00 94.59  ?  707 PHE B CD2   1 
ATOM   11722 C  CE1   . PHE B 1 688 ? 181.824 195.986 240.316 1.00 93.31  ?  707 PHE B CE1   1 
ATOM   11723 C  CE2   . PHE B 1 688 ? 179.444 195.906 240.128 1.00 92.47  ?  707 PHE B CE2   1 
ATOM   11724 C  CZ    . PHE B 1 688 ? 180.576 196.250 240.840 1.00 94.08  ?  707 PHE B CZ    1 
ATOM   11725 N  N     . GLY B 1 689 ? 182.364 195.142 233.665 1.00 122.66 ?  708 GLY B N     1 
ATOM   11726 C  CA    . GLY B 1 689 ? 182.567 194.506 232.376 1.00 123.98 ?  708 GLY B CA    1 
ATOM   11727 C  C     . GLY B 1 689 ? 183.670 193.467 232.401 1.00 124.96 ?  708 GLY B C     1 
ATOM   11728 O  O     . GLY B 1 689 ? 183.535 192.397 231.801 1.00 122.92 ?  708 GLY B O     1 
ATOM   11729 N  N     . THR B 1 690 ? 184.769 193.763 233.090 1.00 127.56 ?  709 THR B N     1 
ATOM   11730 C  CA    . THR B 1 690 ? 185.845 192.795 233.240 1.00 126.69 ?  709 THR B CA    1 
ATOM   11731 C  C     . THR B 1 690 ? 185.401 191.645 234.135 1.00 125.87 ?  709 THR B C     1 
ATOM   11732 O  O     . THR B 1 690 ? 184.603 191.825 235.059 1.00 125.84 ?  709 THR B O     1 
ATOM   11733 C  CB    . THR B 1 690 ? 187.091 193.463 233.823 1.00 124.73 ?  709 THR B CB    1 
ATOM   11734 O  OG1   . THR B 1 690 ? 186.710 194.350 234.882 1.00 123.08 ?  709 THR B OG1   1 
ATOM   11735 C  CG2   . THR B 1 690 ? 187.828 194.248 232.748 1.00 123.28 ?  709 THR B CG2   1 
ATOM   11736 N  N     . GLY B 1 691 ? 185.926 190.457 233.856 1.00 117.41 ?  710 GLY B N     1 
ATOM   11737 C  CA    . GLY B 1 691 ? 185.522 189.274 234.584 1.00 117.09 ?  710 GLY B CA    1 
ATOM   11738 C  C     . GLY B 1 691 ? 186.172 189.166 235.949 1.00 118.19 ?  710 GLY B C     1 
ATOM   11739 O  O     . GLY B 1 691 ? 186.998 189.983 236.355 1.00 118.37 ?  710 GLY B O     1 
ATOM   11740 N  N     . PHE B 1 692 ? 185.774 188.122 236.682 1.00 113.40 ?  711 PHE B N     1 
ATOM   11741 C  CA    . PHE B 1 692 ? 186.342 187.889 238.005 1.00 112.30 ?  711 PHE B CA    1 
ATOM   11742 C  C     . PHE B 1 692 ? 187.783 187.398 237.930 1.00 110.25 ?  711 PHE B C     1 
ATOM   11743 O  O     . PHE B 1 692 ? 188.567 187.668 238.845 1.00 110.54 ?  711 PHE B O     1 
ATOM   11744 C  CB    . PHE B 1 692 ? 185.476 186.897 238.785 1.00 111.87 ?  711 PHE B CB    1 
ATOM   11745 C  CG    . PHE B 1 692 ? 185.852 186.771 240.235 1.00 112.91 ?  711 PHE B CG    1 
ATOM   11746 C  CD1   . PHE B 1 692 ? 186.402 187.844 240.919 1.00 112.60 ?  711 PHE B CD1   1 
ATOM   11747 C  CD2   . PHE B 1 692 ? 185.640 185.586 240.920 1.00 110.99 ?  711 PHE B CD2   1 
ATOM   11748 C  CE1   . PHE B 1 692 ? 186.751 187.733 242.249 1.00 111.28 ?  711 PHE B CE1   1 
ATOM   11749 C  CE2   . PHE B 1 692 ? 185.983 185.471 242.254 1.00 110.93 ?  711 PHE B CE2   1 
ATOM   11750 C  CZ    . PHE B 1 692 ? 186.538 186.546 242.919 1.00 111.20 ?  711 PHE B CZ    1 
ATOM   11751 N  N     . SER B 1 693 ? 188.158 186.691 236.862 1.00 116.62 ?  712 SER B N     1 
ATOM   11752 C  CA    . SER B 1 693 ? 189.574 186.426 236.630 1.00 119.44 ?  712 SER B CA    1 
ATOM   11753 C  C     . SER B 1 693 ? 190.335 187.730 236.430 1.00 120.11 ?  712 SER B C     1 
ATOM   11754 O  O     . SER B 1 693 ? 191.455 187.896 236.933 1.00 119.37 ?  712 SER B O     1 
ATOM   11755 C  CB    . SER B 1 693 ? 189.747 185.507 235.421 1.00 120.93 ?  712 SER B CB    1 
ATOM   11756 O  OG    . SER B 1 693 ? 191.117 185.255 235.163 1.00 120.66 ?  712 SER B OG    1 
ATOM   11757 N  N     . GLY B 1 694 ? 189.734 188.672 235.700 1.00 123.80 ?  713 GLY B N     1 
ATOM   11758 C  CA    . GLY B 1 694 ? 190.324 189.993 235.585 1.00 122.83 ?  713 GLY B CA    1 
ATOM   11759 C  C     . GLY B 1 694 ? 190.422 190.701 236.922 1.00 124.87 ?  713 GLY B C     1 
ATOM   11760 O  O     . GLY B 1 694 ? 191.383 191.422 237.180 1.00 124.59 ?  713 GLY B O     1 
ATOM   11761 N  N     . LEU B 1 695 ? 189.436 190.493 237.797 1.00 124.59 ?  714 LEU B N     1 
ATOM   11762 C  CA    . LEU B 1 695 ? 189.495 191.088 239.130 1.00 122.95 ?  714 LEU B CA    1 
ATOM   11763 C  C     . LEU B 1 695 ? 190.586 190.455 239.987 1.00 121.87 ?  714 LEU B C     1 
ATOM   11764 O  O     . LEU B 1 695 ? 191.208 191.141 240.801 1.00 119.64 ?  714 LEU B O     1 
ATOM   11765 C  CB    . LEU B 1 695 ? 188.138 190.972 239.824 1.00 122.84 ?  714 LEU B CB    1 
ATOM   11766 C  CG    . LEU B 1 695 ? 186.960 191.635 239.108 1.00 122.20 ?  714 LEU B CG    1 
ATOM   11767 C  CD1   . LEU B 1 695 ? 185.704 191.568 239.962 1.00 120.96 ?  714 LEU B CD1   1 
ATOM   11768 C  CD2   . LEU B 1 695 ? 187.292 193.075 238.747 1.00 120.70 ?  714 LEU B CD2   1 
ATOM   11769 N  N     . SER B 1 696 ? 190.826 189.155 239.833 1.00 123.05 ?  715 SER B N     1 
ATOM   11770 C  CA    . SER B 1 696 ? 191.930 188.525 240.552 1.00 121.64 ?  715 SER B CA    1 
ATOM   11771 C  C     . SER B 1 696 ? 193.277 189.027 240.042 1.00 121.85 ?  715 SER B C     1 
ATOM   11772 O  O     . SER B 1 696 ? 194.196 189.286 240.831 1.00 119.99 ?  715 SER B O     1 
ATOM   11773 C  CB    . SER B 1 696 ? 191.836 187.007 240.430 1.00 122.14 ?  715 SER B CB    1 
ATOM   11774 O  OG    . SER B 1 696 ? 190.621 186.545 240.989 1.00 123.44 ?  715 SER B OG    1 
ATOM   11775 N  N     . ARG B 1 697 ? 193.413 189.175 238.723 1.00 127.17 ?  716 ARG B N     1 
ATOM   11776 C  CA    . ARG B 1 697 ? 194.608 189.814 238.183 1.00 127.89 ?  716 ARG B CA    1 
ATOM   11777 C  C     . ARG B 1 697 ? 194.712 191.262 238.653 1.00 127.63 ?  716 ARG B C     1 
ATOM   11778 O  O     . ARG B 1 697 ? 195.817 191.795 238.804 1.00 126.26 ?  716 ARG B O     1 
ATOM   11779 C  CB    . ARG B 1 697 ? 194.598 189.726 236.656 1.00 126.71 ?  716 ARG B CB    1 
ATOM   11780 C  CG    . ARG B 1 697 ? 195.925 190.048 235.995 1.00 126.25 ?  716 ARG B CG    1 
ATOM   11781 C  CD    . ARG B 1 697 ? 195.983 191.498 235.564 1.00 127.76 ?  716 ARG B CD    1 
ATOM   11782 N  NE    . ARG B 1 697 ? 194.757 191.912 234.892 1.00 129.41 ?  716 ARG B NE    1 
ATOM   11783 C  CZ    . ARG B 1 697 ? 194.523 191.754 233.597 1.00 128.96 ?  716 ARG B CZ    1 
ATOM   11784 N  NH1   . ARG B 1 697 ? 193.387 192.147 233.046 1.00 128.21 1  716 ARG B NH1   1 
ATOM   11785 N  NH2   . ARG B 1 697 ? 195.455 191.187 232.835 1.00 127.36 ?  716 ARG B NH2   1 
ATOM   11786 N  N     . LEU B 1 698 ? 193.571 191.903 238.902 1.00 123.45 ?  717 LEU B N     1 
ATOM   11787 C  CA    . LEU B 1 698 ? 193.548 193.237 239.489 1.00 123.65 ?  717 LEU B CA    1 
ATOM   11788 C  C     . LEU B 1 698 ? 194.043 193.223 240.930 1.00 124.68 ?  717 LEU B C     1 
ATOM   11789 O  O     . LEU B 1 698 ? 194.657 194.190 241.385 1.00 124.04 ?  717 LEU B O     1 
ATOM   11790 C  CB    . LEU B 1 698 ? 192.126 193.791 239.423 1.00 123.48 ?  717 LEU B CB    1 
ATOM   11791 C  CG    . LEU B 1 698 ? 191.874 195.267 239.700 1.00 122.86 ?  717 LEU B CG    1 
ATOM   11792 C  CD1   . LEU B 1 698 ? 192.473 196.122 238.602 1.00 122.40 ?  717 LEU B CD1   1 
ATOM   11793 C  CD2   . LEU B 1 698 ? 190.383 195.512 239.840 1.00 121.01 ?  717 LEU B CD2   1 
ATOM   11794 N  N     . VAL B 1 699 ? 193.741 192.160 241.672 1.00 124.24 ?  718 VAL B N     1 
ATOM   11795 C  CA    . VAL B 1 699 ? 194.315 192.001 243.005 1.00 124.59 ?  718 VAL B CA    1 
ATOM   11796 C  C     . VAL B 1 699 ? 195.823 191.821 242.908 1.00 123.24 ?  718 VAL B C     1 
ATOM   11797 O  O     . VAL B 1 699 ? 196.584 192.354 243.725 1.00 122.46 ?  718 VAL B O     1 
ATOM   11798 C  CB    . VAL B 1 699 ? 193.651 190.825 243.742 1.00 123.48 ?  718 VAL B CB    1 
ATOM   11799 C  CG1   . VAL B 1 699 ? 194.161 190.742 245.172 1.00 122.46 ?  718 VAL B CG1   1 
ATOM   11800 C  CG2   . VAL B 1 699 ? 192.146 190.982 243.725 1.00 122.16 ?  718 VAL B CG2   1 
ATOM   11801 N  N     . SER B 1 700 ? 196.276 191.064 241.908 1.00 123.35 ?  719 SER B N     1 
ATOM   11802 C  CA    . SER B 1 700 ? 197.706 190.912 241.656 1.00 123.61 ?  719 SER B CA    1 
ATOM   11803 C  C     . SER B 1 700 ? 198.383 192.238 241.329 1.00 124.17 ?  719 SER B C     1 
ATOM   11804 O  O     . SER B 1 700 ? 199.499 192.484 241.802 1.00 123.16 ?  719 SER B O     1 
ATOM   11805 C  CB    . SER B 1 700 ? 197.940 189.919 240.516 1.00 123.34 ?  719 SER B CB    1 
ATOM   11806 O  OG    . SER B 1 700 ? 199.316 189.827 240.193 1.00 123.99 ?  719 SER B OG    1 
ATOM   11807 N  N     . LEU B 1 701 ? 197.735 193.090 240.533 1.00 119.49 ?  720 LEU B N     1 
ATOM   11808 C  CA    . LEU B 1 701 ? 198.198 194.448 240.249 1.00 119.31 ?  720 LEU B CA    1 
ATOM   11809 C  C     . LEU B 1 701 ? 197.369 195.397 241.106 1.00 116.84 ?  720 LEU B C     1 
ATOM   11810 O  O     . LEU B 1 701 ? 196.362 195.947 240.637 1.00 113.67 ?  720 LEU B O     1 
ATOM   11811 C  CB    . LEU B 1 701 ? 198.055 194.778 238.761 1.00 120.72 ?  720 LEU B CB    1 
ATOM   11812 C  CG    . LEU B 1 701 ? 198.503 196.163 238.290 1.00 120.00 ?  720 LEU B CG    1 
ATOM   11813 C  CD1   . LEU B 1 701 ? 200.018 196.230 238.189 1.00 118.24 ?  720 LEU B CD1   1 
ATOM   11814 C  CD2   . LEU B 1 701 ? 197.859 196.504 236.955 1.00 119.50 ?  720 LEU B CD2   1 
ATOM   11815 N  N     . PRO B 1 702 ? 197.796 195.680 242.338 1.00 108.82 ?  721 PRO B N     1 
ATOM   11816 C  CA    . PRO B 1 702 ? 196.847 196.049 243.400 1.00 107.60 ?  721 PRO B CA    1 
ATOM   11817 C  C     . PRO B 1 702 ? 196.048 197.314 243.112 1.00 107.46 ?  721 PRO B C     1 
ATOM   11818 O  O     . PRO B 1 702 ? 196.520 198.243 242.453 1.00 109.13 ?  721 PRO B O     1 
ATOM   11819 C  CB    . PRO B 1 702 ? 197.749 196.230 244.626 1.00 107.49 ?  721 PRO B CB    1 
ATOM   11820 C  CG    . PRO B 1 702 ? 199.113 196.480 244.072 1.00 107.01 ?  721 PRO B CG    1 
ATOM   11821 C  CD    . PRO B 1 702 ? 199.190 195.687 242.808 1.00 108.22 ?  721 PRO B CD    1 
ATOM   11822 N  N     . VAL B 1 703 ? 194.815 197.330 243.624 1.00 86.13  ?  722 VAL B N     1 
ATOM   11823 C  CA    . VAL B 1 703 ? 193.930 198.487 243.592 1.00 83.85  ?  722 VAL B CA    1 
ATOM   11824 C  C     . VAL B 1 703 ? 193.419 198.728 245.007 1.00 83.35  ?  722 VAL B C     1 
ATOM   11825 O  O     . VAL B 1 703 ? 193.808 198.047 245.957 1.00 89.75  ?  722 VAL B O     1 
ATOM   11826 C  CB    . VAL B 1 703 ? 192.744 198.299 242.625 1.00 83.60  ?  722 VAL B CB    1 
ATOM   11827 C  CG1   . VAL B 1 703 ? 193.211 198.412 241.192 1.00 86.11  ?  722 VAL B CG1   1 
ATOM   11828 C  CG2   . VAL B 1 703 ? 192.067 196.963 242.876 1.00 80.42  ?  722 VAL B CG2   1 
ATOM   11829 N  N     . THR B 1 704 ? 192.534 199.718 245.141 1.00 65.85  ?  723 THR B N     1 
ATOM   11830 C  CA    . THR B 1 704 ? 191.950 200.049 246.433 1.00 67.58  ?  723 THR B CA    1 
ATOM   11831 C  C     . THR B 1 704 ? 190.429 200.040 246.459 1.00 70.16  ?  723 THR B C     1 
ATOM   11832 O  O     . THR B 1 704 ? 189.857 199.635 247.479 1.00 72.36  ?  723 THR B O     1 
ATOM   11833 C  CB    . THR B 1 704 ? 192.429 201.431 246.910 1.00 70.48  ?  723 THR B CB    1 
ATOM   11834 O  OG1   . THR B 1 704 ? 191.766 202.457 246.160 1.00 75.05  ?  723 THR B OG1   1 
ATOM   11835 C  CG2   . THR B 1 704 ? 193.937 201.573 246.748 1.00 68.91  ?  723 THR B CG2   1 
ATOM   11836 N  N     . GLU B 1 705 ? 189.759 200.459 245.386 1.00 67.82  ?  724 GLU B N     1 
ATOM   11837 C  CA    . GLU B 1 705 ? 188.318 200.661 245.427 1.00 66.29  ?  724 GLU B CA    1 
ATOM   11838 C  C     . GLU B 1 705 ? 187.636 199.987 244.245 1.00 64.24  ?  724 GLU B C     1 
ATOM   11839 O  O     . GLU B 1 705 ? 188.129 200.013 243.114 1.00 72.51  ?  724 GLU B O     1 
ATOM   11840 C  CB    . GLU B 1 705 ? 187.963 202.155 245.437 1.00 70.94  ?  724 GLU B CB    1 
ATOM   11841 C  CG    . GLU B 1 705 ? 188.472 202.909 246.655 1.00 70.86  ?  724 GLU B CG    1 
ATOM   11842 C  CD    . GLU B 1 705 ? 188.455 204.412 246.458 1.00 75.72  ?  724 GLU B CD    1 
ATOM   11843 O  OE1   . GLU B 1 705 ? 187.877 204.874 245.452 1.00 75.98  ?  724 GLU B OE1   1 
ATOM   11844 O  OE2   . GLU B 1 705 ? 189.020 205.130 247.309 1.00 76.37  -1 724 GLU B OE2   1 
ATOM   11845 N  N     . ILE B 1 706 ? 186.477 199.398 244.526 1.00 53.51  ?  725 ILE B N     1 
ATOM   11846 C  CA    . ILE B 1 706 ? 185.590 198.847 243.508 1.00 60.64  ?  725 ILE B CA    1 
ATOM   11847 C  C     . ILE B 1 706 ? 184.242 199.540 243.637 1.00 61.49  ?  725 ILE B C     1 
ATOM   11848 O  O     . ILE B 1 706 ? 183.678 199.621 244.733 1.00 65.51  ?  725 ILE B O     1 
ATOM   11849 C  CB    . ILE B 1 706 ? 185.437 197.317 243.644 1.00 71.74  ?  725 ILE B CB    1 
ATOM   11850 C  CG1   . ILE B 1 706 ? 186.695 196.605 243.146 1.00 72.75  ?  725 ILE B CG1   1 
ATOM   11851 C  CG2   . ILE B 1 706 ? 184.213 196.830 242.887 1.00 70.65  ?  725 ILE B CG2   1 
ATOM   11852 C  CD1   . ILE B 1 706 ? 186.601 195.096 243.210 1.00 68.59  ?  725 ILE B CD1   1 
ATOM   11853 N  N     . LYS B 1 707 ? 183.722 200.043 242.521 1.00 61.20  ?  726 LYS B N     1 
ATOM   11854 C  CA    . LYS B 1 707 ? 182.490 200.816 242.524 1.00 64.79  ?  726 LYS B CA    1 
ATOM   11855 C  C     . LYS B 1 707 ? 181.377 200.056 241.814 1.00 62.97  ?  726 LYS B C     1 
ATOM   11856 O  O     . LYS B 1 707 ? 181.512 199.682 240.645 1.00 66.39  ?  726 LYS B O     1 
ATOM   11857 C  CB    . LYS B 1 707 ? 182.704 202.180 241.862 1.00 69.87  ?  726 LYS B CB    1 
ATOM   11858 C  CG    . LYS B 1 707 ? 183.301 203.215 242.798 1.00 64.36  ?  726 LYS B CG    1 
ATOM   11859 C  CD    . LYS B 1 707 ? 183.845 204.415 242.048 1.00 63.80  ?  726 LYS B CD    1 
ATOM   11860 C  CE    . LYS B 1 707 ? 184.081 205.581 242.995 1.00 67.29  ?  726 LYS B CE    1 
ATOM   11861 N  NZ    . LYS B 1 707 ? 183.465 206.841 242.497 1.00 66.48  1  726 LYS B NZ    1 
ATOM   11862 N  N     . ILE B 1 708 ? 180.278 199.840 242.530 1.00 60.50  ?  727 ILE B N     1 
ATOM   11863 C  CA    . ILE B 1 708 ? 179.075 199.229 241.979 1.00 60.52  ?  727 ILE B CA    1 
ATOM   11864 C  C     . ILE B 1 708 ? 178.285 200.315 241.266 1.00 59.97  ?  727 ILE B C     1 
ATOM   11865 O  O     . ILE B 1 708 ? 177.857 201.296 241.890 1.00 63.43  ?  727 ILE B O     1 
ATOM   11866 C  CB    . ILE B 1 708 ? 178.230 198.552 243.070 1.00 64.45  ?  727 ILE B CB    1 
ATOM   11867 C  CG1   . ILE B 1 708 ? 179.105 197.654 243.946 1.00 65.23  ?  727 ILE B CG1   1 
ATOM   11868 C  CG2   . ILE B 1 708 ? 177.099 197.751 242.445 1.00 67.65  ?  727 ILE B CG2   1 
ATOM   11869 C  CD1   . ILE B 1 708 ? 178.382 197.077 245.141 1.00 68.65  ?  727 ILE B CD1   1 
ATOM   11870 N  N     . ASP B 1 709 ? 178.087 200.128 239.963 1.00 69.57  ?  728 ASP B N     1 
ATOM   11871 C  CA    . ASP B 1 709 ? 177.530 201.163 239.106 1.00 71.69  ?  728 ASP B CA    1 
ATOM   11872 C  C     . ASP B 1 709 ? 176.054 201.404 239.402 1.00 71.93  ?  728 ASP B C     1 
ATOM   11873 O  O     . ASP B 1 709 ? 175.317 200.504 239.821 1.00 78.17  ?  728 ASP B O     1 
ATOM   11874 C  CB    . ASP B 1 709 ? 177.706 200.782 237.634 1.00 74.76  ?  728 ASP B CB    1 
ATOM   11875 C  CG    . ASP B 1 709 ? 177.563 201.970 236.700 1.00 80.25  ?  728 ASP B CG    1 
ATOM   11876 O  OD1   . ASP B 1 709 ? 177.390 203.104 237.194 1.00 81.66  ?  728 ASP B OD1   1 
ATOM   11877 O  OD2   . ASP B 1 709 ? 177.623 201.769 235.469 1.00 79.09  -1 728 ASP B OD2   1 
ATOM   11878 N  N     . LYS B 1 710 ? 175.624 202.645 239.154 1.00 67.03  ?  729 LYS B N     1 
ATOM   11879 C  CA    . LYS B 1 710 ? 174.227 203.012 239.350 1.00 71.01  ?  729 LYS B CA    1 
ATOM   11880 C  C     . LYS B 1 710 ? 173.301 202.167 238.484 1.00 77.09  ?  729 LYS B C     1 
ATOM   11881 O  O     . LYS B 1 710 ? 172.162 201.896 238.879 1.00 81.49  ?  729 LYS B O     1 
ATOM   11882 C  CB    . LYS B 1 710 ? 174.038 204.501 239.053 1.00 69.84  ?  729 LYS B CB    1 
ATOM   11883 C  CG    . LYS B 1 710 ? 172.591 204.950 238.918 1.00 69.58  ?  729 LYS B CG    1 
ATOM   11884 C  CD    . LYS B 1 710 ? 172.494 206.456 238.744 1.00 72.98  ?  729 LYS B CD    1 
ATOM   11885 C  CE    . LYS B 1 710 ? 171.084 206.876 238.358 1.00 74.53  ?  729 LYS B CE    1 
ATOM   11886 N  NZ    . LYS B 1 710 ? 170.079 206.437 239.364 1.00 74.34  1  729 LYS B NZ    1 
ATOM   11887 N  N     . SER B 1 711 ? 173.775 201.721 237.318 1.00 74.61  ?  730 SER B N     1 
ATOM   11888 C  CA    . SER B 1 711 ? 172.956 200.857 236.474 1.00 71.23  ?  730 SER B CA    1 
ATOM   11889 C  C     . SER B 1 711 ? 172.610 199.552 237.178 1.00 72.09  ?  730 SER B C     1 
ATOM   11890 O  O     . SER B 1 711 ? 171.472 199.079 237.085 1.00 73.85  ?  730 SER B O     1 
ATOM   11891 C  CB    . SER B 1 711 ? 173.674 200.577 235.155 1.00 71.49  ?  730 SER B CB    1 
ATOM   11892 O  OG    . SER B 1 711 ? 173.894 201.775 234.431 1.00 72.44  ?  730 SER B OG    1 
ATOM   11893 N  N     . PHE B 1 712 ? 173.572 198.956 237.885 1.00 77.43  ?  731 PHE B N     1 
ATOM   11894 C  CA    . PHE B 1 712 ? 173.290 197.737 238.634 1.00 74.17  ?  731 PHE B CA    1 
ATOM   11895 C  C     . PHE B 1 712 ? 172.513 198.028 239.912 1.00 76.92  ?  731 PHE B C     1 
ATOM   11896 O  O     . PHE B 1 712 ? 171.644 197.240 240.305 1.00 84.03  ?  731 PHE B O     1 
ATOM   11897 C  CB    . PHE B 1 712 ? 174.592 197.003 238.958 1.00 76.93  ?  731 PHE B CB    1 
ATOM   11898 C  CG    . PHE B 1 712 ? 175.119 196.172 237.823 1.00 79.61  ?  731 PHE B CG    1 
ATOM   11899 C  CD1   . PHE B 1 712 ? 174.481 196.165 236.593 1.00 80.94  ?  731 PHE B CD1   1 
ATOM   11900 C  CD2   . PHE B 1 712 ? 176.250 195.391 237.988 1.00 79.88  ?  731 PHE B CD2   1 
ATOM   11901 C  CE1   . PHE B 1 712 ? 174.964 195.399 235.550 1.00 81.19  ?  731 PHE B CE1   1 
ATOM   11902 C  CE2   . PHE B 1 712 ? 176.738 194.623 236.949 1.00 80.15  ?  731 PHE B CE2   1 
ATOM   11903 C  CZ    . PHE B 1 712 ? 176.094 194.627 235.728 1.00 79.12  ?  731 PHE B CZ    1 
ATOM   11904 N  N     . VAL B 1 713 ? 172.806 199.150 240.575 1.00 73.79  ?  732 VAL B N     1 
ATOM   11905 C  CA    . VAL B 1 713 ? 172.090 199.468 241.809 1.00 75.81  ?  732 VAL B CA    1 
ATOM   11906 C  C     . VAL B 1 713 ? 170.613 199.737 241.532 1.00 75.09  ?  732 VAL B C     1 
ATOM   11907 O  O     . VAL B 1 713 ? 169.753 199.424 242.364 1.00 78.76  ?  732 VAL B O     1 
ATOM   11908 C  CB    . VAL B 1 713 ? 172.761 200.649 242.535 1.00 76.72  ?  732 VAL B CB    1 
ATOM   11909 C  CG1   . VAL B 1 713 ? 172.129 200.863 243.898 1.00 75.61  ?  732 VAL B CG1   1 
ATOM   11910 C  CG2   . VAL B 1 713 ? 174.243 200.384 242.705 1.00 77.08  ?  732 VAL B CG2   1 
ATOM   11911 N  N     . ASP B 1 714 ? 170.290 200.315 240.373 1.00 73.53  ?  733 ASP B N     1 
ATOM   11912 C  CA    . ASP B 1 714 ? 168.891 200.546 240.026 1.00 74.98  ?  733 ASP B CA    1 
ATOM   11913 C  C     . ASP B 1 714 ? 168.147 199.233 239.819 1.00 81.18  ?  733 ASP B C     1 
ATOM   11914 O  O     . ASP B 1 714 ? 167.028 199.060 240.316 1.00 84.81  ?  733 ASP B O     1 
ATOM   11915 C  CB    . ASP B 1 714 ? 168.795 201.419 238.774 1.00 79.73  ?  733 ASP B CB    1 
ATOM   11916 C  CG    . ASP B 1 714 ? 169.257 202.840 239.019 1.00 82.59  ?  733 ASP B CG    1 
ATOM   11917 O  OD1   . ASP B 1 714 ? 169.171 203.305 240.176 1.00 82.99  ?  733 ASP B OD1   1 
ATOM   11918 O  OD2   . ASP B 1 714 ? 169.707 203.494 238.054 1.00 81.59  -1 733 ASP B OD2   1 
ATOM   11919 N  N     . ARG B 1 715 ? 168.751 198.294 239.089 1.00 87.59  ?  734 ARG B N     1 
ATOM   11920 C  CA    . ARG B 1 715 ? 168.135 196.990 238.880 1.00 87.04  ?  734 ARG B CA    1 
ATOM   11921 C  C     . ARG B 1 715 ? 168.169 196.116 240.124 1.00 89.89  ?  734 ARG B C     1 
ATOM   11922 O  O     . ARG B 1 715 ? 167.496 195.080 240.153 1.00 91.88  ?  734 ARG B O     1 
ATOM   11923 C  CB    . ARG B 1 715 ? 168.816 196.259 237.720 1.00 85.73  ?  734 ARG B CB    1 
ATOM   11924 C  CG    . ARG B 1 715 ? 168.900 197.076 236.441 1.00 88.56  ?  734 ARG B CG    1 
ATOM   11925 C  CD    . ARG B 1 715 ? 169.622 196.314 235.342 1.00 90.82  ?  734 ARG B CD    1 
ATOM   11926 N  NE    . ARG B 1 715 ? 170.775 195.583 235.852 1.00 92.62  ?  734 ARG B NE    1 
ATOM   11927 C  CZ    . ARG B 1 715 ? 171.056 194.323 235.550 1.00 89.77  ?  734 ARG B CZ    1 
ATOM   11928 N  NH1   . ARG B 1 715 ? 170.283 193.617 234.741 1.00 89.04  1  734 ARG B NH1   1 
ATOM   11929 N  NH2   . ARG B 1 715 ? 172.139 193.757 236.074 1.00 86.88  ?  734 ARG B NH2   1 
ATOM   11930 N  N     . CYS B 1 716 ? 168.951 196.495 241.138 1.00 90.80  ?  735 CYS B N     1 
ATOM   11931 C  CA    . CYS B 1 716 ? 168.921 195.770 242.405 1.00 88.05  ?  735 CYS B CA    1 
ATOM   11932 C  C     . CYS B 1 716 ? 167.519 195.758 243.003 1.00 88.07  ?  735 CYS B C     1 
ATOM   11933 O  O     . CYS B 1 716 ? 167.156 194.830 243.736 1.00 86.10  ?  735 CYS B O     1 
ATOM   11934 C  CB    . CYS B 1 716 ? 169.919 196.392 243.382 1.00 91.07  ?  735 CYS B CB    1 
ATOM   11935 S  SG    . CYS B 1 716 ? 170.321 195.366 244.808 1.00 102.24 ?  735 CYS B SG    1 
ATOM   11936 N  N     . LEU B 1 717 ? 166.720 196.786 242.709 1.00 98.38  ?  736 LEU B N     1 
ATOM   11937 C  CA    . LEU B 1 717 ? 165.351 196.839 243.212 1.00 101.71 ?  736 LEU B CA    1 
ATOM   11938 C  C     . LEU B 1 717 ? 164.497 195.722 242.620 1.00 99.98  ?  736 LEU B C     1 
ATOM   11939 O  O     . LEU B 1 717 ? 163.853 194.963 243.354 1.00 97.65  ?  736 LEU B O     1 
ATOM   11940 C  CB    . LEU B 1 717 ? 164.737 198.205 242.900 1.00 100.96 ?  736 LEU B CB    1 
ATOM   11941 C  CG    . LEU B 1 717 ? 165.339 199.434 243.585 1.00 100.78 ?  736 LEU B CG    1 
ATOM   11942 C  CD1   . LEU B 1 717 ? 164.705 200.705 243.050 1.00 98.68  ?  736 LEU B CD1   1 
ATOM   11943 C  CD2   . LEU B 1 717 ? 165.149 199.356 245.081 1.00 100.05 ?  736 LEU B CD2   1 
ATOM   11944 N  N     . THR B 1 718 ? 164.488 195.597 241.291 1.00 103.44 ?  737 THR B N     1 
ATOM   11945 C  CA    . THR B 1 718 ? 163.583 194.657 240.635 1.00 101.94 ?  737 THR B CA    1 
ATOM   11946 C  C     . THR B 1 718 ? 164.204 193.270 240.502 1.00 101.67 ?  737 THR B C     1 
ATOM   11947 O  O     . THR B 1 718 ? 163.657 192.282 241.002 1.00 100.42 ?  737 THR B O     1 
ATOM   11948 C  CB    . THR B 1 718 ? 163.175 195.191 239.258 1.00 103.06 ?  737 THR B CB    1 
ATOM   11949 O  OG1   . THR B 1 718 ? 164.314 195.197 238.387 1.00 103.19 ?  737 THR B OG1   1 
ATOM   11950 C  CG2   . THR B 1 718 ? 162.618 196.602 239.375 1.00 102.68 ?  737 THR B CG2   1 
ATOM   11951 N  N     . GLU B 1 719 ? 165.345 193.176 239.823 1.00 102.67 ?  738 GLU B N     1 
ATOM   11952 C  CA    . GLU B 1 719 ? 165.991 191.888 239.578 1.00 101.67 ?  738 GLU B CA    1 
ATOM   11953 C  C     . GLU B 1 719 ? 166.660 191.423 240.864 1.00 102.80 ?  738 GLU B C     1 
ATOM   11954 O  O     . GLU B 1 719 ? 167.758 191.867 241.208 1.00 102.79 ?  738 GLU B O     1 
ATOM   11955 C  CB    . GLU B 1 719 ? 166.993 191.996 238.433 1.00 100.81 ?  738 GLU B CB    1 
ATOM   11956 C  CG    . GLU B 1 719 ? 166.417 192.610 237.165 1.00 103.44 ?  738 GLU B CG    1 
ATOM   11957 C  CD    . GLU B 1 719 ? 167.426 192.678 236.036 1.00 103.20 ?  738 GLU B CD    1 
ATOM   11958 O  OE1   . GLU B 1 719 ? 168.570 192.218 236.233 1.00 101.78 ?  738 GLU B OE1   1 
ATOM   11959 O  OE2   . GLU B 1 719 ? 167.076 193.191 234.952 1.00 102.58 -1 738 GLU B OE2   1 
ATOM   11960 N  N     . LYS B 1 720 ? 165.996 190.514 241.580 1.00 103.04 ?  739 LYS B N     1 
ATOM   11961 C  CA    . LYS B 1 720 ? 166.507 190.016 242.850 1.00 102.16 ?  739 LYS B CA    1 
ATOM   11962 C  C     . LYS B 1 720 ? 167.695 189.078 242.685 1.00 98.68  ?  739 LYS B C     1 
ATOM   11963 O  O     . LYS B 1 720 ? 168.332 188.734 243.687 1.00 96.52  ?  739 LYS B O     1 
ATOM   11964 C  CB    . LYS B 1 720 ? 165.390 189.304 243.614 1.00 102.07 ?  739 LYS B CB    1 
ATOM   11965 C  CG    . LYS B 1 720 ? 164.158 190.164 243.841 1.00 101.49 ?  739 LYS B CG    1 
ATOM   11966 C  CD    . LYS B 1 720 ? 163.069 189.395 244.571 1.00 101.24 ?  739 LYS B CD    1 
ATOM   11967 C  CE    . LYS B 1 720 ? 161.839 190.263 244.788 1.00 103.10 ?  739 LYS B CE    1 
ATOM   11968 N  NZ    . LYS B 1 720 ? 160.756 189.535 245.507 1.00 101.74 1  739 LYS B NZ    1 
ATOM   11969 N  N     . ARG B 1 721 ? 168.003 188.652 241.458 1.00 98.53  ?  740 ARG B N     1 
ATOM   11970 C  CA    . ARG B 1 721 ? 169.133 187.753 241.250 1.00 100.40 ?  740 ARG B CA    1 
ATOM   11971 C  C     . ARG B 1 721 ? 170.464 188.450 241.504 1.00 98.56  ?  740 ARG B C     1 
ATOM   11972 O  O     . ARG B 1 721 ? 171.399 187.828 242.022 1.00 98.45  ?  740 ARG B O     1 
ATOM   11973 C  CB    . ARG B 1 721 ? 169.101 187.184 239.831 1.00 100.51 ?  740 ARG B CB    1 
ATOM   11974 C  CG    . ARG B 1 721 ? 168.822 188.219 238.751 1.00 102.39 ?  740 ARG B CG    1 
ATOM   11975 C  CD    . ARG B 1 721 ? 168.544 187.568 237.404 1.00 101.85 ?  740 ARG B CD    1 
ATOM   11976 N  NE    . ARG B 1 721 ? 167.248 186.902 237.362 1.00 103.35 ?  740 ARG B NE    1 
ATOM   11977 C  CZ    . ARG B 1 721 ? 166.123 187.481 236.966 1.00 102.11 ?  740 ARG B CZ    1 
ATOM   11978 N  NH1   . ARG B 1 721 ? 166.098 188.744 236.572 1.00 100.26 1  740 ARG B NH1   1 
ATOM   11979 N  NH2   . ARG B 1 721 ? 164.996 186.776 236.962 1.00 100.78 ?  740 ARG B NH2   1 
ATOM   11980 N  N     . ILE B 1 722 ? 170.570 189.734 241.152 1.00 92.88  ?  741 ILE B N     1 
ATOM   11981 C  CA    . ILE B 1 722 ? 171.852 190.428 241.189 1.00 91.34  ?  741 ILE B CA    1 
ATOM   11982 C  C     . ILE B 1 722 ? 172.264 190.869 242.584 1.00 91.24  ?  741 ILE B C     1 
ATOM   11983 O  O     . ILE B 1 722 ? 173.296 191.535 242.729 1.00 94.35  ?  741 ILE B O     1 
ATOM   11984 C  CB    . ILE B 1 722 ? 171.830 191.643 240.240 1.00 94.70  ?  741 ILE B CB    1 
ATOM   11985 C  CG1   . ILE B 1 722 ? 170.917 192.739 240.787 1.00 94.57  ?  741 ILE B CG1   1 
ATOM   11986 C  CG2   . ILE B 1 722 ? 171.380 191.223 238.850 1.00 94.44  ?  741 ILE B CG2   1 
ATOM   11987 C  CD1   . ILE B 1 722 ? 170.965 194.013 239.979 1.00 92.65  ?  741 ILE B CD1   1 
ATOM   11988 N  N     . LEU B 1 723 ? 171.487 190.531 243.616 1.00 88.34  ?  742 LEU B N     1 
ATOM   11989 C  CA    . LEU B 1 723 ? 171.948 190.754 244.984 1.00 86.63  ?  742 LEU B CA    1 
ATOM   11990 C  C     . LEU B 1 723 ? 173.203 189.938 245.266 1.00 86.31  ?  742 LEU B C     1 
ATOM   11991 O  O     . LEU B 1 723 ? 174.063 190.345 246.059 1.00 84.30  ?  742 LEU B O     1 
ATOM   11992 C  CB    . LEU B 1 723 ? 170.842 190.396 245.979 1.00 88.45  ?  742 LEU B CB    1 
ATOM   11993 C  CG    . LEU B 1 723 ? 169.841 191.484 246.381 1.00 90.18  ?  742 LEU B CG    1 
ATOM   11994 C  CD1   . LEU B 1 723 ? 170.540 192.612 247.126 1.00 89.52  ?  742 LEU B CD1   1 
ATOM   11995 C  CD2   . LEU B 1 723 ? 169.073 192.014 245.176 1.00 91.71  ?  742 LEU B CD2   1 
ATOM   11996 N  N     . ALA B 1 724 ? 173.324 188.781 244.613 1.00 90.17  ?  743 ALA B N     1 
ATOM   11997 C  CA    . ALA B 1 724 ? 174.505 187.942 244.777 1.00 89.84  ?  743 ALA B CA    1 
ATOM   11998 C  C     . ALA B 1 724 ? 175.751 188.636 244.246 1.00 88.54  ?  743 ALA B C     1 
ATOM   11999 O  O     . ALA B 1 724 ? 176.852 188.436 244.766 1.00 87.57  ?  743 ALA B O     1 
ATOM   12000 C  CB    . ALA B 1 724 ? 174.294 186.604 244.072 1.00 92.56  ?  743 ALA B CB    1 
ATOM   12001 N  N     . LEU B 1 725 ? 175.597 189.446 243.195 1.00 92.63  ?  744 LEU B N     1 
ATOM   12002 C  CA    . LEU B 1 725 ? 176.709 190.242 242.690 1.00 95.52  ?  744 LEU B CA    1 
ATOM   12003 C  C     . LEU B 1 725 ? 177.308 191.102 243.796 1.00 94.39  ?  744 LEU B C     1 
ATOM   12004 O  O     . LEU B 1 725 ? 178.514 191.053 244.066 1.00 91.65  ?  744 LEU B O     1 
ATOM   12005 C  CB    . LEU B 1 725 ? 176.231 191.128 241.534 1.00 96.31  ?  744 LEU B CB    1 
ATOM   12006 C  CG    . LEU B 1 725 ? 176.289 190.597 240.103 1.00 94.47  ?  744 LEU B CG    1 
ATOM   12007 C  CD1   . LEU B 1 725 ? 175.420 191.441 239.186 1.00 93.54  ?  744 LEU B CD1   1 
ATOM   12008 C  CD2   . LEU B 1 725 ? 177.721 190.576 239.600 1.00 94.96  ?  744 LEU B CD2   1 
ATOM   12009 N  N     . LEU B 1 726 ? 176.451 191.880 244.461 1.00 89.58  ?  745 LEU B N     1 
ATOM   12010 C  CA    . LEU B 1 726 ? 176.904 192.759 245.532 1.00 87.33  ?  745 LEU B CA    1 
ATOM   12011 C  C     . LEU B 1 726 ? 177.460 191.956 246.700 1.00 90.69  ?  745 LEU B C     1 
ATOM   12012 O  O     . LEU B 1 726 ? 178.484 192.321 247.289 1.00 94.17  ?  745 LEU B O     1 
ATOM   12013 C  CB    . LEU B 1 726 ? 175.752 193.654 245.990 1.00 89.90  ?  745 LEU B CB    1 
ATOM   12014 C  CG    . LEU B 1 726 ? 175.381 194.808 245.055 1.00 90.08  ?  745 LEU B CG    1 
ATOM   12015 C  CD1   . LEU B 1 726 ? 174.329 194.377 244.045 1.00 87.01  ?  745 LEU B CD1   1 
ATOM   12016 C  CD2   . LEU B 1 726 ? 174.897 196.003 245.855 1.00 90.14  ?  745 LEU B CD2   1 
ATOM   12017 N  N     . GLU B 1 727 ? 176.790 190.855 247.050 1.00 92.47  ?  746 GLU B N     1 
ATOM   12018 C  CA    . GLU B 1 727 ? 177.249 190.035 248.167 1.00 90.82  ?  746 GLU B CA    1 
ATOM   12019 C  C     . GLU B 1 727 ? 178.650 189.492 247.910 1.00 89.02  ?  746 GLU B C     1 
ATOM   12020 O  O     . GLU B 1 727 ? 179.534 189.585 248.770 1.00 89.10  ?  746 GLU B O     1 
ATOM   12021 C  CB    . GLU B 1 727 ? 176.264 188.892 248.416 1.00 90.99  ?  746 GLU B CB    1 
ATOM   12022 C  CG    . GLU B 1 727 ? 176.808 187.788 249.306 1.00 92.04  ?  746 GLU B CG    1 
ATOM   12023 C  CD    . GLU B 1 727 ? 176.764 188.153 250.776 1.00 93.35  ?  746 GLU B CD    1 
ATOM   12024 O  OE1   . GLU B 1 727 ? 175.926 188.997 251.156 1.00 92.27  ?  746 GLU B OE1   1 
ATOM   12025 O  OE2   . GLU B 1 727 ? 177.572 187.599 251.551 1.00 93.80  -1 746 GLU B OE2   1 
ATOM   12026 N  N     . ALA B 1 728 ? 178.880 188.947 246.714 1.00 86.26  ?  747 ALA B N     1 
ATOM   12027 C  CA    . ALA B 1 728 ? 180.185 188.387 246.385 1.00 88.14  ?  747 ALA B CA    1 
ATOM   12028 C  C     . ALA B 1 728 ? 181.250 189.470 246.286 1.00 88.56  ?  747 ALA B C     1 
ATOM   12029 O  O     . ALA B 1 728 ? 182.390 189.267 246.719 1.00 88.50  ?  747 ALA B O     1 
ATOM   12030 C  CB    . ALA B 1 728 ? 180.101 187.597 245.079 1.00 90.55  ?  747 ALA B CB    1 
ATOM   12031 N  N     . ILE B 1 729 ? 180.904 190.626 245.713 1.00 89.61  ?  748 ILE B N     1 
ATOM   12032 C  CA    . ILE B 1 729 ? 181.877 191.710 245.596 1.00 90.83  ?  748 ILE B CA    1 
ATOM   12033 C  C     . ILE B 1 729 ? 182.301 192.193 246.978 1.00 89.28  ?  748 ILE B C     1 
ATOM   12034 O  O     . ILE B 1 729 ? 183.491 192.397 247.247 1.00 88.38  ?  748 ILE B O     1 
ATOM   12035 C  CB    . ILE B 1 729 ? 181.309 192.853 244.736 1.00 91.65  ?  748 ILE B CB    1 
ATOM   12036 C  CG1   . ILE B 1 729 ? 181.266 192.433 243.266 1.00 89.49  ?  748 ILE B CG1   1 
ATOM   12037 C  CG2   . ILE B 1 729 ? 182.140 194.118 244.904 1.00 90.96  ?  748 ILE B CG2   1 
ATOM   12038 C  CD1   . ILE B 1 729 ? 180.281 193.215 242.438 1.00 89.16  ?  748 ILE B CD1   1 
ATOM   12039 N  N     . THR B 1 730 ? 181.335 192.363 247.884 1.00 87.64  ?  749 THR B N     1 
ATOM   12040 C  CA    . THR B 1 730 ? 181.673 192.740 249.253 1.00 88.41  ?  749 THR B CA    1 
ATOM   12041 C  C     . THR B 1 730 ? 182.490 191.653 249.939 1.00 90.16  ?  749 THR B C     1 
ATOM   12042 O  O     . THR B 1 730 ? 183.391 191.953 250.732 1.00 91.66  ?  749 THR B O     1 
ATOM   12043 C  CB    . THR B 1 730 ? 180.404 193.037 250.050 1.00 88.75  ?  749 THR B CB    1 
ATOM   12044 O  OG1   . THR B 1 730 ? 179.486 191.946 249.912 1.00 88.99  ?  749 THR B OG1   1 
ATOM   12045 C  CG2   . THR B 1 730 ? 179.753 194.322 249.558 1.00 89.11  ?  749 THR B CG2   1 
ATOM   12046 N  N     . SER B 1 731 ? 182.174 190.382 249.666 1.00 91.35  ?  750 SER B N     1 
ATOM   12047 C  CA    . SER B 1 731 ? 182.959 189.291 250.234 1.00 91.03  ?  750 SER B CA    1 
ATOM   12048 C  C     . SER B 1 731 ? 184.414 189.371 249.798 1.00 89.35  ?  750 SER B C     1 
ATOM   12049 O  O     . SER B 1 731 ? 185.316 189.226 250.629 1.00 89.25  ?  750 SER B O     1 
ATOM   12050 C  CB    . SER B 1 731 ? 182.355 187.946 249.833 1.00 91.85  ?  750 SER B CB    1 
ATOM   12051 O  OG    . SER B 1 731 ? 182.726 187.594 248.512 1.00 92.02  ?  750 SER B OG    1 
ATOM   12052 N  N     . ILE B 1 732 ? 184.660 189.623 248.511 1.00 87.19  ?  751 ILE B N     1 
ATOM   12053 C  CA    . ILE B 1 732 ? 186.027 189.848 248.044 1.00 88.04  ?  751 ILE B CA    1 
ATOM   12054 C  C     . ILE B 1 732 ? 186.629 191.062 248.742 1.00 91.35  ?  751 ILE B C     1 
ATOM   12055 O  O     . ILE B 1 732 ? 187.823 191.081 249.075 1.00 90.24  ?  751 ILE B O     1 
ATOM   12056 C  CB    . ILE B 1 732 ? 186.058 190.009 246.513 1.00 88.17  ?  751 ILE B CB    1 
ATOM   12057 C  CG1   . ILE B 1 732 ? 185.337 188.850 245.828 1.00 91.81  ?  751 ILE B CG1   1 
ATOM   12058 C  CG2   . ILE B 1 732 ? 187.489 190.107 246.014 1.00 88.15  ?  751 ILE B CG2   1 
ATOM   12059 C  CD1   . ILE B 1 732 ? 184.651 189.244 244.536 1.00 90.38  ?  751 ILE B CD1   1 
ATOM   12060 N  N     . GLY B 1 733 ? 185.813 192.090 248.969 1.00 91.17  ?  752 GLY B N     1 
ATOM   12061 C  CA    . GLY B 1 733 ? 186.258 193.291 249.646 1.00 89.80  ?  752 GLY B CA    1 
ATOM   12062 C  C     . GLY B 1 733 ? 186.814 193.031 251.030 1.00 88.94  ?  752 GLY B C     1 
ATOM   12063 O  O     . GLY B 1 733 ? 187.933 193.453 251.332 1.00 91.43  ?  752 GLY B O     1 
ATOM   12064 N  N     . GLN B 1 734 ? 186.061 192.329 251.879 1.00 86.63  ?  753 GLN B N     1 
ATOM   12065 C  CA    . GLN B 1 734 ? 186.614 192.023 253.199 1.00 90.30  ?  753 GLN B CA    1 
ATOM   12066 C  C     . GLN B 1 734 ? 187.635 190.893 253.150 1.00 91.49  ?  753 GLN B C     1 
ATOM   12067 O  O     . GLN B 1 734 ? 188.416 190.742 254.096 1.00 91.97  ?  753 GLN B O     1 
ATOM   12068 C  CB    . GLN B 1 734 ? 185.550 191.668 254.254 1.00 92.22  ?  753 GLN B CB    1 
ATOM   12069 C  CG    . GLN B 1 734 ? 184.861 190.319 254.103 1.00 91.57  ?  753 GLN B CG    1 
ATOM   12070 C  CD    . GLN B 1 734 ? 183.448 190.424 253.573 1.00 92.21  ?  753 GLN B CD    1 
ATOM   12071 O  OE1   . GLN B 1 734 ? 183.004 191.489 253.161 1.00 92.57  ?  753 GLN B OE1   1 
ATOM   12072 N  NE2   . GLN B 1 734 ? 182.731 189.307 253.587 1.00 93.01  ?  753 GLN B NE2   1 
ATOM   12073 N  N     . SER B 1 735 ? 187.650 190.093 252.081 1.00 90.33  ?  754 SER B N     1 
ATOM   12074 C  CA    . SER B 1 735 ? 188.644 189.031 251.977 1.00 90.15  ?  754 SER B CA    1 
ATOM   12075 C  C     . SER B 1 735 ? 190.030 189.595 251.694 1.00 87.59  ?  754 SER B C     1 
ATOM   12076 O  O     . SER B 1 735 ? 191.031 189.079 252.205 1.00 88.49  ?  754 SER B O     1 
ATOM   12077 C  CB    . SER B 1 735 ? 188.237 188.035 250.889 1.00 89.90  ?  754 SER B CB    1 
ATOM   12078 O  OG    . SER B 1 735 ? 186.968 187.471 251.164 1.00 89.53  ?  754 SER B OG    1 
ATOM   12079 N  N     . LEU B 1 736 ? 190.113 190.653 250.881 1.00 88.12  ?  755 LEU B N     1 
ATOM   12080 C  CA    . LEU B 1 736 ? 191.426 191.150 250.479 1.00 92.98  ?  755 LEU B CA    1 
ATOM   12081 C  C     . LEU B 1 736 ? 191.538 192.671 250.589 1.00 91.90  ?  755 LEU B C     1 
ATOM   12082 O  O     . LEU B 1 736 ? 192.318 193.293 249.859 1.00 92.17  ?  755 LEU B O     1 
ATOM   12083 C  CB    . LEU B 1 736 ? 191.770 190.650 249.070 1.00 93.76  ?  755 LEU B CB    1 
ATOM   12084 C  CG    . LEU B 1 736 ? 190.902 190.969 247.848 1.00 91.86  ?  755 LEU B CG    1 
ATOM   12085 C  CD1   . LEU B 1 736 ? 191.226 192.304 247.205 1.00 90.11  ?  755 LEU B CD1   1 
ATOM   12086 C  CD2   . LEU B 1 736 ? 191.028 189.851 246.841 1.00 92.33  ?  755 LEU B CD2   1 
ATOM   12087 N  N     . ASN B 1 737 ? 190.804 193.276 251.527 1.00 85.74  ?  756 ASN B N     1 
ATOM   12088 C  CA    . ASN B 1 737 ? 190.988 194.675 251.917 1.00 85.76  ?  756 ASN B CA    1 
ATOM   12089 C  C     . ASN B 1 737 ? 190.775 195.631 250.738 1.00 87.87  ?  756 ASN B C     1 
ATOM   12090 O  O     . ASN B 1 737 ? 191.685 196.332 250.292 1.00 88.16  ?  756 ASN B O     1 
ATOM   12091 C  CB    . ASN B 1 737 ? 192.369 194.881 252.552 1.00 88.22  ?  756 ASN B CB    1 
ATOM   12092 C  CG    . ASN B 1 737 ? 192.464 196.177 253.334 1.00 90.16  ?  756 ASN B CG    1 
ATOM   12093 O  OD1   . ASN B 1 737 ? 191.476 196.891 253.498 1.00 89.85  ?  756 ASN B OD1   1 
ATOM   12094 N  ND2   . ASN B 1 737 ? 193.660 196.485 253.824 1.00 87.19  ?  756 ASN B ND2   1 
ATOM   12095 N  N     . LEU B 1 738 ? 189.542 195.645 250.237 1.00 83.58  ?  757 LEU B N     1 
ATOM   12096 C  CA    . LEU B 1 738 ? 189.109 196.605 249.232 1.00 81.64  ?  757 LEU B CA    1 
ATOM   12097 C  C     . LEU B 1 738 ? 187.915 197.391 249.752 1.00 81.74  ?  757 LEU B C     1 
ATOM   12098 O  O     . LEU B 1 738 ? 187.115 196.884 250.544 1.00 78.49  ?  757 LEU B O     1 
ATOM   12099 C  CB    . LEU B 1 738 ? 188.733 195.919 247.912 1.00 79.69  ?  757 LEU B CB    1 
ATOM   12100 C  CG    . LEU B 1 738 ? 189.879 195.511 246.987 1.00 78.22  ?  757 LEU B CG    1 
ATOM   12101 C  CD1   . LEU B 1 738 ? 189.366 195.228 245.582 1.00 77.41  ?  757 LEU B CD1   1 
ATOM   12102 C  CD2   . LEU B 1 738 ? 190.968 196.570 246.961 1.00 81.43  ?  757 LEU B CD2   1 
ATOM   12103 N  N     . THR B 1 739 ? 187.799 198.638 249.302 1.00 77.95  ?  758 THR B N     1 
ATOM   12104 C  CA    . THR B 1 739 ? 186.680 199.500 249.652 1.00 72.30  ?  758 THR B CA    1 
ATOM   12105 C  C     . THR B 1 739 ? 185.657 199.455 248.526 1.00 72.68  ?  758 THR B C     1 
ATOM   12106 O  O     . THR B 1 739 ? 185.993 199.725 247.368 1.00 78.01  ?  758 THR B O     1 
ATOM   12107 C  CB    . THR B 1 739 ? 187.146 200.939 249.887 1.00 73.83  ?  758 THR B CB    1 
ATOM   12108 O  OG1   . THR B 1 739 ? 187.929 201.001 251.086 1.00 74.43  ?  758 THR B OG1   1 
ATOM   12109 C  CG2   . THR B 1 739 ? 185.951 201.873 250.022 1.00 73.93  ?  758 THR B CG2   1 
ATOM   12110 N  N     . VAL B 1 740 ? 184.415 199.121 248.861 1.00 57.50  ?  759 VAL B N     1 
ATOM   12111 C  CA    . VAL B 1 740 ? 183.348 199.013 247.874 1.00 58.30  ?  759 VAL B CA    1 
ATOM   12112 C  C     . VAL B 1 740 ? 182.427 200.218 248.007 1.00 65.41  ?  759 VAL B C     1 
ATOM   12113 O  O     . VAL B 1 740 ? 181.950 200.541 249.106 1.00 68.97  ?  759 VAL B O     1 
ATOM   12114 C  CB    . VAL B 1 740 ? 182.584 197.682 248.008 1.00 62.52  ?  759 VAL B CB    1 
ATOM   12115 C  CG1   . VAL B 1 740 ? 181.963 197.522 249.385 1.00 69.98  ?  759 VAL B CG1   1 
ATOM   12116 C  CG2   . VAL B 1 740 ? 181.522 197.573 246.924 1.00 67.02  ?  759 VAL B CG2   1 
ATOM   12117 N  N     . VAL B 1 741 ? 182.200 200.894 246.883 1.00 66.84  ?  760 VAL B N     1 
ATOM   12118 C  CA    . VAL B 1 741 ? 181.452 202.144 246.822 1.00 64.25  ?  760 VAL B CA    1 
ATOM   12119 C  C     . VAL B 1 741 ? 180.219 201.898 245.967 1.00 62.55  ?  760 VAL B C     1 
ATOM   12120 O  O     . VAL B 1 741 ? 180.338 201.622 244.768 1.00 71.17  ?  760 VAL B O     1 
ATOM   12121 C  CB    . VAL B 1 741 ? 182.296 203.281 246.222 1.00 64.07  ?  760 VAL B CB    1 
ATOM   12122 C  CG1   . VAL B 1 741 ? 181.648 204.637 246.481 1.00 64.65  ?  760 VAL B CG1   1 
ATOM   12123 C  CG2   . VAL B 1 741 ? 183.738 203.225 246.718 1.00 65.13  ?  760 VAL B CG2   1 
ATOM   12124 N  N     . ALA B 1 742 ? 179.042 202.020 246.566 1.00 48.99  ?  761 ALA B N     1 
ATOM   12125 C  CA    . ALA B 1 742 ? 177.784 201.818 245.854 1.00 53.36  ?  761 ALA B CA    1 
ATOM   12126 C  C     . ALA B 1 742 ? 177.320 203.163 245.306 1.00 54.59  ?  761 ALA B C     1 
ATOM   12127 O  O     . ALA B 1 742 ? 177.039 204.085 246.078 1.00 64.27  ?  761 ALA B O     1 
ATOM   12128 C  CB    . ALA B 1 742 ? 176.732 201.204 246.773 1.00 62.85  ?  761 ALA B CB    1 
ATOM   12129 N  N     . GLU B 1 743 ? 177.234 203.278 243.981 1.00 59.97  ?  762 GLU B N     1 
ATOM   12130 C  CA    . GLU B 1 743 ? 176.891 204.542 243.349 1.00 60.85  ?  762 GLU B CA    1 
ATOM   12131 C  C     . GLU B 1 743 ? 175.402 204.606 243.009 1.00 64.09  ?  762 GLU B C     1 
ATOM   12132 O  O     . GLU B 1 743 ? 174.715 203.590 242.886 1.00 67.02  ?  762 GLU B O     1 
ATOM   12133 C  CB    . GLU B 1 743 ? 177.726 204.747 242.085 1.00 63.17  ?  762 GLU B CB    1 
ATOM   12134 C  CG    . GLU B 1 743 ? 179.213 204.946 242.333 1.00 65.46  ?  762 GLU B CG    1 
ATOM   12135 C  CD    . GLU B 1 743 ? 179.941 205.458 241.104 1.00 68.30  ?  762 GLU B CD    1 
ATOM   12136 O  OE1   . GLU B 1 743 ? 179.366 205.385 239.999 1.00 65.92  ?  762 GLU B OE1   1 
ATOM   12137 O  OE2   . GLU B 1 743 ? 181.087 205.934 241.243 1.00 70.91  -1 762 GLU B OE2   1 
ATOM   12138 N  N     . GLY B 1 744 ? 174.909 205.833 242.860 1.00 65.34  ?  763 GLY B N     1 
ATOM   12139 C  CA    . GLY B 1 744 ? 173.574 206.079 242.350 1.00 66.05  ?  763 GLY B CA    1 
ATOM   12140 C  C     . GLY B 1 744 ? 172.416 205.624 243.215 1.00 66.36  ?  763 GLY B C     1 
ATOM   12141 O  O     . GLY B 1 744 ? 171.453 205.042 242.707 1.00 71.74  ?  763 GLY B O     1 
ATOM   12142 N  N     . VAL B 1 745 ? 172.488 205.880 244.518 1.00 59.24  ?  764 VAL B N     1 
ATOM   12143 C  CA    . VAL B 1 745 ? 171.370 205.647 245.427 1.00 61.23  ?  764 VAL B CA    1 
ATOM   12144 C  C     . VAL B 1 745 ? 170.448 206.856 245.368 1.00 60.26  ?  764 VAL B C     1 
ATOM   12145 O  O     . VAL B 1 745 ? 170.913 207.998 245.254 1.00 63.06  ?  764 VAL B O     1 
ATOM   12146 C  CB    . VAL B 1 745 ? 171.855 205.381 246.862 1.00 59.49  ?  764 VAL B CB    1 
ATOM   12147 C  CG1   . VAL B 1 745 ? 172.710 204.126 246.900 1.00 61.26  ?  764 VAL B CG1   1 
ATOM   12148 C  CG2   . VAL B 1 745 ? 172.630 206.573 247.394 1.00 61.53  ?  764 VAL B CG2   1 
ATOM   12149 N  N     . GLU B 1 746 ? 169.139 206.610 245.414 1.00 62.22  ?  765 GLU B N     1 
ATOM   12150 C  CA    . GLU B 1 746 ? 168.171 207.690 245.271 1.00 64.85  ?  765 GLU B CA    1 
ATOM   12151 C  C     . GLU B 1 746 ? 167.085 207.634 246.340 1.00 73.96  ?  765 GLU B C     1 
ATOM   12152 O  O     . GLU B 1 746 ? 166.482 208.662 246.666 1.00 75.39  ?  765 GLU B O     1 
ATOM   12153 C  CB    . GLU B 1 746 ? 167.538 207.654 243.877 1.00 65.43  ?  765 GLU B CB    1 
ATOM   12154 C  CG    . GLU B 1 746 ? 168.542 207.650 242.734 1.00 65.80  ?  765 GLU B CG    1 
ATOM   12155 C  CD    . GLU B 1 746 ? 168.024 208.350 241.496 1.00 70.89  ?  765 GLU B CD    1 
ATOM   12156 O  OE1   . GLU B 1 746 ? 167.417 209.433 241.633 1.00 71.67  ?  765 GLU B OE1   1 
ATOM   12157 O  OE2   . GLU B 1 746 ? 168.226 207.819 240.384 1.00 73.26  -1 765 GLU B OE2   1 
ATOM   12158 N  N     . THR B 1 747 ? 166.826 206.451 246.894 1.00 81.95  ?  766 THR B N     1 
ATOM   12159 C  CA    . THR B 1 747 ? 165.730 206.262 247.833 1.00 79.69  ?  766 THR B CA    1 
ATOM   12160 C  C     . THR B 1 747 ? 166.207 205.554 249.096 1.00 79.58  ?  766 THR B C     1 
ATOM   12161 O  O     . THR B 1 747 ? 167.220 204.842 249.094 1.00 78.72  ?  766 THR B O     1 
ATOM   12162 C  CB    . THR B 1 747 ? 164.577 205.465 247.200 1.00 77.52  ?  766 THR B CB    1 
ATOM   12163 O  OG1   . THR B 1 747 ? 165.061 204.200 246.734 1.00 78.44  ?  766 THR B OG1   1 
ATOM   12164 C  CG2   . THR B 1 747 ? 163.966 206.233 246.034 1.00 76.12  ?  766 THR B CG2   1 
ATOM   12165 N  N     . LYS B 1 748 ? 165.453 205.762 250.179 1.00 77.56  ?  767 LYS B N     1 
ATOM   12166 C  CA    . LYS B 1 748 ? 165.809 205.169 251.464 1.00 76.08  ?  767 LYS B CA    1 
ATOM   12167 C  C     . LYS B 1 748 ? 165.730 203.649 251.416 1.00 75.94  ?  767 LYS B C     1 
ATOM   12168 O  O     . LYS B 1 748 ? 166.549 202.962 252.033 1.00 78.58  ?  767 LYS B O     1 
ATOM   12169 C  CB    . LYS B 1 748 ? 164.904 205.719 252.566 1.00 79.57  ?  767 LYS B CB    1 
ATOM   12170 C  CG    . LYS B 1 748 ? 165.433 205.485 253.972 1.00 80.00  ?  767 LYS B CG    1 
ATOM   12171 C  CD    . LYS B 1 748 ? 164.651 206.288 254.999 1.00 80.32  ?  767 LYS B CD    1 
ATOM   12172 C  CE    . LYS B 1 748 ? 165.294 206.200 256.375 1.00 77.63  ?  767 LYS B CE    1 
ATOM   12173 N  NZ    . LYS B 1 748 ? 165.083 204.870 257.011 1.00 75.11  1  767 LYS B NZ    1 
ATOM   12174 N  N     . GLU B 1 749 ? 164.742 203.104 250.703 1.00 80.36  ?  768 GLU B N     1 
ATOM   12175 C  CA    . GLU B 1 749 ? 164.663 201.654 250.554 1.00 78.15  ?  768 GLU B CA    1 
ATOM   12176 C  C     . GLU B 1 749 ? 165.856 201.117 249.770 1.00 76.28  ?  768 GLU B C     1 
ATOM   12177 O  O     . GLU B 1 749 ? 166.394 200.051 250.094 1.00 78.25  ?  768 GLU B O     1 
ATOM   12178 C  CB    . GLU B 1 749 ? 163.343 201.261 249.886 1.00 81.53  ?  768 GLU B CB    1 
ATOM   12179 C  CG    . GLU B 1 749 ? 163.127 201.844 248.498 1.00 83.36  ?  768 GLU B CG    1 
ATOM   12180 C  CD    . GLU B 1 749 ? 162.290 203.108 248.521 1.00 83.98  ?  768 GLU B CD    1 
ATOM   12181 O  OE1   . GLU B 1 749 ? 162.310 203.818 249.548 1.00 83.44  ?  768 GLU B OE1   1 
ATOM   12182 O  OE2   . GLU B 1 749 ? 161.613 203.392 247.511 1.00 83.58  -1 768 GLU B OE2   1 
ATOM   12183 N  N     . GLN B 1 750 ? 166.287 201.849 248.740 1.00 78.45  ?  769 GLN B N     1 
ATOM   12184 C  CA    . GLN B 1 750 ? 167.462 201.442 247.977 1.00 80.17  ?  769 GLN B CA    1 
ATOM   12185 C  C     . GLN B 1 750 ? 168.711 201.465 248.847 1.00 79.68  ?  769 GLN B C     1 
ATOM   12186 O  O     . GLN B 1 750 ? 169.583 200.598 248.719 1.00 77.37  ?  769 GLN B O     1 
ATOM   12187 C  CB    . GLN B 1 750 ? 167.626 202.353 246.760 1.00 81.34  ?  769 GLN B CB    1 
ATOM   12188 C  CG    . GLN B 1 750 ? 168.693 201.925 245.770 1.00 82.32  ?  769 GLN B CG    1 
ATOM   12189 C  CD    . GLN B 1 750 ? 168.716 202.812 244.539 1.00 83.62  ?  769 GLN B CD    1 
ATOM   12190 O  OE1   . GLN B 1 750 ? 169.501 202.598 243.617 1.00 84.32  ?  769 GLN B OE1   1 
ATOM   12191 N  NE2   . GLN B 1 750 ? 167.846 203.814 244.518 1.00 80.72  ?  769 GLN B NE2   1 
ATOM   12192 N  N     . PHE B 1 751 ? 168.818 202.455 249.737 1.00 80.35  ?  770 PHE B N     1 
ATOM   12193 C  CA    . PHE B 1 751 ? 169.932 202.480 250.681 1.00 77.76  ?  770 PHE B CA    1 
ATOM   12194 C  C     . PHE B 1 751 ? 169.860 201.318 251.667 1.00 80.33  ?  770 PHE B C     1 
ATOM   12195 O  O     . PHE B 1 751 ? 170.871 200.656 251.935 1.00 83.48  ?  770 PHE B O     1 
ATOM   12196 C  CB    . PHE B 1 751 ? 169.952 203.815 251.426 1.00 74.55  ?  770 PHE B CB    1 
ATOM   12197 C  CG    . PHE B 1 751 ? 170.731 203.783 252.711 1.00 74.30  ?  770 PHE B CG    1 
ATOM   12198 C  CD1   . PHE B 1 751 ? 172.108 203.639 252.700 1.00 74.40  ?  770 PHE B CD1   1 
ATOM   12199 C  CD2   . PHE B 1 751 ? 170.084 203.903 253.930 1.00 78.08  ?  770 PHE B CD2   1 
ATOM   12200 C  CE1   . PHE B 1 751 ? 172.825 203.611 253.883 1.00 73.10  ?  770 PHE B CE1   1 
ATOM   12201 C  CE2   . PHE B 1 751 ? 170.795 203.877 255.114 1.00 80.73  ?  770 PHE B CE2   1 
ATOM   12202 C  CZ    . PHE B 1 751 ? 172.167 203.730 255.090 1.00 76.28  ?  770 PHE B CZ    1 
ATOM   12203 N  N     . GLU B 1 752 ? 168.671 201.047 252.210 1.00 89.01  ?  771 GLU B N     1 
ATOM   12204 C  CA    . GLU B 1 752 ? 168.556 200.050 253.268 1.00 87.28  ?  771 GLU B CA    1 
ATOM   12205 C  C     . GLU B 1 752 ? 168.730 198.633 252.736 1.00 89.20  ?  771 GLU B C     1 
ATOM   12206 O  O     . GLU B 1 752 ? 169.209 197.759 253.467 1.00 90.69  ?  771 GLU B O     1 
ATOM   12207 C  CB    . GLU B 1 752 ? 167.213 200.193 253.988 1.00 87.33  ?  771 GLU B CB    1 
ATOM   12208 C  CG    . GLU B 1 752 ? 166.022 199.610 253.245 1.00 87.99  ?  771 GLU B CG    1 
ATOM   12209 C  CD    . GLU B 1 752 ? 164.697 200.155 253.740 1.00 91.08  ?  771 GLU B CD    1 
ATOM   12210 O  OE1   . GLU B 1 752 ? 164.651 201.333 254.152 1.00 90.97  ?  771 GLU B OE1   1 
ATOM   12211 O  OE2   . GLU B 1 752 ? 163.699 199.403 253.719 1.00 91.04  -1 771 GLU B OE2   1 
ATOM   12212 N  N     . MET B 1 753 ? 168.359 198.379 251.478 1.00 91.57  ?  772 MET B N     1 
ATOM   12213 C  CA    . MET B 1 753 ? 168.537 197.034 250.946 1.00 92.07  ?  772 MET B CA    1 
ATOM   12214 C  C     . MET B 1 753 ? 169.999 196.735 250.644 1.00 90.05  ?  772 MET B C     1 
ATOM   12215 O  O     . MET B 1 753 ? 170.404 195.569 250.677 1.00 91.72  ?  772 MET B O     1 
ATOM   12216 C  CB    . MET B 1 753 ? 167.675 196.830 249.699 1.00 91.90  ?  772 MET B CB    1 
ATOM   12217 C  CG    . MET B 1 753 ? 168.225 197.455 248.438 1.00 92.70  ?  772 MET B CG    1 
ATOM   12218 S  SD    . MET B 1 753 ? 167.020 197.441 247.107 1.00 95.37  ?  772 MET B SD    1 
ATOM   12219 C  CE    . MET B 1 753 ? 166.754 195.682 246.914 1.00 91.39  ?  772 MET B CE    1 
ATOM   12220 N  N     . LEU B 1 754 ? 170.801 197.759 250.349 1.00 85.86  ?  773 LEU B N     1 
ATOM   12221 C  CA    . LEU B 1 754 ? 172.242 197.583 250.235 1.00 86.88  ?  773 LEU B CA    1 
ATOM   12222 C  C     . LEU B 1 754 ? 172.953 197.677 251.578 1.00 83.34  ?  773 LEU B C     1 
ATOM   12223 O  O     . LEU B 1 754 ? 174.124 197.291 251.671 1.00 82.67  ?  773 LEU B O     1 
ATOM   12224 C  CB    . LEU B 1 754 ? 172.833 198.618 249.273 1.00 87.37  ?  773 LEU B CB    1 
ATOM   12225 C  CG    . LEU B 1 754 ? 172.795 198.323 247.771 1.00 88.00  ?  773 LEU B CG    1 
ATOM   12226 C  CD1   . LEU B 1 754 ? 171.396 198.447 247.202 1.00 87.38  ?  773 LEU B CD1   1 
ATOM   12227 C  CD2   . LEU B 1 754 ? 173.745 199.253 247.041 1.00 85.29  ?  773 LEU B CD2   1 
ATOM   12228 N  N     . ARG B 1 755 ? 172.278 198.187 252.610 1.00 83.39  ?  774 ARG B N     1 
ATOM   12229 C  CA    . ARG B 1 755 ? 172.874 198.228 253.943 1.00 85.62  ?  774 ARG B CA    1 
ATOM   12230 C  C     . ARG B 1 755 ? 173.149 196.826 254.478 1.00 89.33  ?  774 ARG B C     1 
ATOM   12231 O  O     . ARG B 1 755 ? 174.178 196.592 255.122 1.00 89.03  ?  774 ARG B O     1 
ATOM   12232 C  CB    . ARG B 1 755 ? 171.957 198.994 254.896 1.00 86.68  ?  774 ARG B CB    1 
ATOM   12233 C  CG    . ARG B 1 755 ? 172.452 199.077 256.332 1.00 86.97  ?  774 ARG B CG    1 
ATOM   12234 C  CD    . ARG B 1 755 ? 173.835 199.690 256.423 1.00 84.25  ?  774 ARG B CD    1 
ATOM   12235 N  NE    . ARG B 1 755 ? 174.173 200.039 257.797 1.00 81.73  ?  774 ARG B NE    1 
ATOM   12236 C  CZ    . ARG B 1 755 ? 173.801 201.160 258.400 1.00 86.75  ?  774 ARG B CZ    1 
ATOM   12237 N  NH1   . ARG B 1 755 ? 173.077 202.075 257.776 1.00 88.46  1  774 ARG B NH1   1 
ATOM   12238 N  NH2   . ARG B 1 755 ? 174.165 201.368 259.662 1.00 87.86  ?  774 ARG B NH2   1 
ATOM   12239 N  N     . LYS B 1 756 ? 172.239 195.880 254.225 1.00 99.46  ?  775 LYS B N     1 
ATOM   12240 C  CA    . LYS B 1 756 ? 172.372 194.550 254.813 1.00 99.63  ?  775 LYS B CA    1 
ATOM   12241 C  C     . LYS B 1 756 ? 173.588 193.803 254.276 1.00 99.45  ?  775 LYS B C     1 
ATOM   12242 O  O     . LYS B 1 756 ? 174.209 193.029 255.014 1.00 101.61 ?  775 LYS B O     1 
ATOM   12243 C  CB    . LYS B 1 756 ? 171.096 193.737 254.582 1.00 99.03  ?  775 LYS B CB    1 
ATOM   12244 C  CG    . LYS B 1 756 ? 170.693 193.578 253.127 1.00 98.73  ?  775 LYS B CG    1 
ATOM   12245 C  CD    . LYS B 1 756 ? 169.303 192.969 253.007 1.00 98.39  ?  775 LYS B CD    1 
ATOM   12246 C  CE    . LYS B 1 756 ? 168.845 192.898 251.558 1.00 98.88  ?  775 LYS B CE    1 
ATOM   12247 N  NZ    . LYS B 1 756 ? 169.734 192.032 250.735 1.00 98.89  1  775 LYS B NZ    1 
ATOM   12248 N  N     . ILE B 1 757 ? 173.943 194.011 253.004 1.00 89.89  ?  776 ILE B N     1 
ATOM   12249 C  CA    . ILE B 1 757 ? 175.171 193.429 252.462 1.00 90.18  ?  776 ILE B CA    1 
ATOM   12250 C  C     . ILE B 1 757 ? 176.410 194.050 253.092 1.00 91.71  ?  776 ILE B C     1 
ATOM   12251 O  O     . ILE B 1 757 ? 177.502 193.472 253.002 1.00 89.42  ?  776 ILE B O     1 
ATOM   12252 C  CB    . ILE B 1 757 ? 175.184 193.563 250.923 1.00 92.10  ?  776 ILE B CB    1 
ATOM   12253 C  CG1   . ILE B 1 757 ? 174.018 192.796 250.292 1.00 92.79  ?  776 ILE B CG1   1 
ATOM   12254 C  CG2   . ILE B 1 757 ? 176.458 193.013 250.310 1.00 93.47  ?  776 ILE B CG2   1 
ATOM   12255 C  CD1   . ILE B 1 757 ? 172.752 193.594 250.120 1.00 93.12  ?  776 ILE B CD1   1 
ATOM   12256 N  N     . HIS B 1 758 ? 176.257 195.191 253.771 1.00 98.20  ?  777 HIS B N     1 
ATOM   12257 C  CA    . HIS B 1 758 ? 177.361 195.912 254.408 1.00 99.19  ?  777 HIS B CA    1 
ATOM   12258 C  C     . HIS B 1 758 ? 178.344 196.446 253.367 1.00 101.46 ?  777 HIS B C     1 
ATOM   12259 O  O     . HIS B 1 758 ? 179.554 196.223 253.444 1.00 100.87 ?  777 HIS B O     1 
ATOM   12260 C  CB    . HIS B 1 758 ? 178.082 195.045 255.447 1.00 97.37  ?  777 HIS B CB    1 
ATOM   12261 C  CG    . HIS B 1 758 ? 177.197 194.561 256.553 1.00 97.99  ?  777 HIS B CG    1 
ATOM   12262 N  ND1   . HIS B 1 758 ? 176.446 193.409 256.458 1.00 99.94  ?  777 HIS B ND1   1 
ATOM   12263 C  CD2   . HIS B 1 758 ? 176.945 195.073 257.781 1.00 97.48  ?  777 HIS B CD2   1 
ATOM   12264 C  CE1   . HIS B 1 758 ? 175.771 193.231 257.580 1.00 98.69  ?  777 HIS B CE1   1 
ATOM   12265 N  NE2   . HIS B 1 758 ? 176.055 194.227 258.398 1.00 99.66  ?  777 HIS B NE2   1 
ATOM   12266 N  N     . CYS B 1 759 ? 177.806 197.153 252.375 1.00 91.82  ?  778 CYS B N     1 
ATOM   12267 C  CA    . CYS B 1 759 ? 178.647 197.894 251.447 1.00 86.67  ?  778 CYS B CA    1 
ATOM   12268 C  C     . CYS B 1 759 ? 179.432 198.958 252.204 1.00 82.23  ?  778 CYS B C     1 
ATOM   12269 O  O     . CYS B 1 759 ? 178.892 199.646 253.074 1.00 80.57  ?  778 CYS B O     1 
ATOM   12270 C  CB    . CYS B 1 759 ? 177.798 198.535 250.350 1.00 83.37  ?  778 CYS B CB    1 
ATOM   12271 S  SG    . CYS B 1 759 ? 177.352 197.414 249.000 1.00 86.73  ?  778 CYS B SG    1 
ATOM   12272 N  N     . ARG B 1 760 ? 180.720 199.081 251.877 1.00 74.35  ?  779 ARG B N     1 
ATOM   12273 C  CA    . ARG B 1 760 ? 181.614 199.907 252.683 1.00 75.78  ?  779 ARG B CA    1 
ATOM   12274 C  C     . ARG B 1 760 ? 181.184 201.369 252.681 1.00 75.22  ?  779 ARG B C     1 
ATOM   12275 O  O     . ARG B 1 760 ? 181.016 201.973 253.746 1.00 76.53  ?  779 ARG B O     1 
ATOM   12276 C  CB    . ARG B 1 760 ? 183.055 199.768 252.191 1.00 77.61  ?  779 ARG B CB    1 
ATOM   12277 C  CG    . ARG B 1 760 ? 184.062 200.463 253.092 1.00 75.88  ?  779 ARG B CG    1 
ATOM   12278 C  CD    . ARG B 1 760 ? 184.540 199.536 254.198 1.00 74.25  ?  779 ARG B CD    1 
ATOM   12279 N  NE    . ARG B 1 760 ? 185.592 200.142 255.005 1.00 76.65  ?  779 ARG B NE    1 
ATOM   12280 C  CZ    . ARG B 1 760 ? 186.876 200.164 254.674 1.00 79.98  ?  779 ARG B CZ    1 
ATOM   12281 N  NH1   . ARG B 1 760 ? 187.312 199.608 253.556 1.00 80.80  1  779 ARG B NH1   1 
ATOM   12282 N  NH2   . ARG B 1 760 ? 187.744 200.758 255.488 1.00 78.56  ?  779 ARG B NH2   1 
ATOM   12283 N  N     . VAL B 1 761 ? 180.996 201.959 251.498 1.00 65.37  ?  780 VAL B N     1 
ATOM   12284 C  CA    . VAL B 1 761 ? 180.580 203.352 251.405 1.00 60.72  ?  780 VAL B CA    1 
ATOM   12285 C  C     . VAL B 1 761 ? 179.523 203.498 250.319 1.00 62.33  ?  780 VAL B C     1 
ATOM   12286 O  O     . VAL B 1 761 ? 179.434 202.698 249.384 1.00 70.01  ?  780 VAL B O     1 
ATOM   12287 C  CB    . VAL B 1 761 ? 181.764 204.308 251.137 1.00 66.92  ?  780 VAL B CB    1 
ATOM   12288 C  CG1   . VAL B 1 761 ? 182.711 204.336 252.322 1.00 67.57  ?  780 VAL B CG1   1 
ATOM   12289 C  CG2   . VAL B 1 761 ? 182.506 203.886 249.900 1.00 65.67  ?  780 VAL B CG2   1 
ATOM   12290 N  N     . ILE B 1 762 ? 178.717 204.547 250.457 1.00 52.44  ?  781 ILE B N     1 
ATOM   12291 C  CA    . ILE B 1 762 ? 177.598 204.813 249.564 1.00 55.80  ?  781 ILE B CA    1 
ATOM   12292 C  C     . ILE B 1 762 ? 177.714 206.238 249.043 1.00 56.83  ?  781 ILE B C     1 
ATOM   12293 O  O     . ILE B 1 762 ? 177.881 207.183 249.822 1.00 63.15  ?  781 ILE B O     1 
ATOM   12294 C  CB    . ILE B 1 762 ? 176.243 204.601 250.272 1.00 55.92  ?  781 ILE B CB    1 
ATOM   12295 C  CG1   . ILE B 1 762 ? 176.058 203.136 250.678 1.00 59.72  ?  781 ILE B CG1   1 
ATOM   12296 C  CG2   . ILE B 1 762 ? 175.108 205.035 249.381 1.00 55.69  ?  781 ILE B CG2   1 
ATOM   12297 C  CD1   . ILE B 1 762 ? 176.554 202.811 252.073 1.00 62.43  ?  781 ILE B CD1   1 
ATOM   12298 N  N     . GLN B 1 763 ? 177.627 206.392 247.722 1.00 56.02  ?  782 GLN B N     1 
ATOM   12299 C  CA    . GLN B 1 763 ? 177.677 207.692 247.066 1.00 50.81  ?  782 GLN B CA    1 
ATOM   12300 C  C     . GLN B 1 763 ? 176.465 207.823 246.157 1.00 54.96  ?  782 GLN B C     1 
ATOM   12301 O  O     . GLN B 1 763 ? 176.218 206.950 245.320 1.00 62.10  ?  782 GLN B O     1 
ATOM   12302 C  CB    . GLN B 1 763 ? 178.972 207.852 246.262 1.00 52.74  ?  782 GLN B CB    1 
ATOM   12303 C  CG    . GLN B 1 763 ? 178.878 208.826 245.100 1.00 53.09  ?  782 GLN B CG    1 
ATOM   12304 C  CD    . GLN B 1 763 ? 180.043 208.697 244.139 1.00 51.37  ?  782 GLN B CD    1 
ATOM   12305 O  OE1   . GLN B 1 763 ? 181.064 208.087 244.459 1.00 54.81  ?  782 GLN B OE1   1 
ATOM   12306 N  NE2   . GLN B 1 763 ? 179.893 209.266 242.950 1.00 47.85  ?  782 GLN B NE2   1 
ATOM   12307 N  N     . GLY B 1 764 ? 175.711 208.899 246.324 1.00 56.57  ?  783 GLY B N     1 
ATOM   12308 C  CA    . GLY B 1 764 ? 174.520 209.100 245.526 1.00 57.40  ?  783 GLY B CA    1 
ATOM   12309 C  C     . GLY B 1 764 ? 173.750 210.319 245.997 1.00 55.22  ?  783 GLY B C     1 
ATOM   12310 O  O     . GLY B 1 764 ? 174.211 211.083 246.844 1.00 55.09  ?  783 GLY B O     1 
ATOM   12311 N  N     . TYR B 1 765 ? 172.557 210.477 245.417 1.00 47.84  ?  784 TYR B N     1 
ATOM   12312 C  CA    . TYR B 1 765 ? 171.718 211.630 245.721 1.00 46.22  ?  784 TYR B CA    1 
ATOM   12313 C  C     . TYR B 1 765 ? 171.017 211.505 247.067 1.00 45.78  ?  784 TYR B C     1 
ATOM   12314 O  O     . TYR B 1 765 ? 170.473 212.498 247.561 1.00 41.37  ?  784 TYR B O     1 
ATOM   12315 C  CB    . TYR B 1 765 ? 170.674 211.828 244.619 1.00 46.82  ?  784 TYR B CB    1 
ATOM   12316 C  CG    . TYR B 1 765 ? 171.218 212.447 243.351 1.00 41.76  ?  784 TYR B CG    1 
ATOM   12317 C  CD1   . TYR B 1 765 ? 172.532 212.886 243.276 1.00 40.10  ?  784 TYR B CD1   1 
ATOM   12318 C  CD2   . TYR B 1 765 ? 170.417 212.587 242.227 1.00 47.19  ?  784 TYR B CD2   1 
ATOM   12319 C  CE1   . TYR B 1 765 ? 173.031 213.449 242.118 1.00 46.91  ?  784 TYR B CE1   1 
ATOM   12320 C  CE2   . TYR B 1 765 ? 170.907 213.149 241.066 1.00 45.16  ?  784 TYR B CE2   1 
ATOM   12321 C  CZ    . TYR B 1 765 ? 172.214 213.578 241.016 1.00 47.47  ?  784 TYR B CZ    1 
ATOM   12322 O  OH    . TYR B 1 765 ? 172.704 214.137 239.859 1.00 49.49  ?  784 TYR B OH    1 
ATOM   12323 N  N     . PHE B 1 766 ? 171.016 210.314 247.670 1.00 63.82  ?  785 PHE B N     1 
ATOM   12324 C  CA    . PHE B 1 766 ? 170.368 210.145 248.965 1.00 64.95  ?  785 PHE B CA    1 
ATOM   12325 C  C     . PHE B 1 766 ? 171.120 210.849 250.085 1.00 60.85  ?  785 PHE B C     1 
ATOM   12326 O  O     . PHE B 1 766 ? 170.520 211.160 251.120 1.00 66.82  ?  785 PHE B O     1 
ATOM   12327 C  CB    . PHE B 1 766 ? 170.223 208.659 249.295 1.00 71.31  ?  785 PHE B CB    1 
ATOM   12328 C  CG    . PHE B 1 766 ? 169.401 208.391 250.523 1.00 68.29  ?  785 PHE B CG    1 
ATOM   12329 C  CD1   . PHE B 1 766 ? 168.051 208.698 250.552 1.00 65.78  ?  785 PHE B CD1   1 
ATOM   12330 C  CD2   . PHE B 1 766 ? 169.983 207.836 251.652 1.00 66.08  ?  785 PHE B CD2   1 
ATOM   12331 C  CE1   . PHE B 1 766 ? 167.296 208.457 251.684 1.00 65.61  ?  785 PHE B CE1   1 
ATOM   12332 C  CE2   . PHE B 1 766 ? 169.232 207.591 252.786 1.00 66.76  ?  785 PHE B CE2   1 
ATOM   12333 C  CZ    . PHE B 1 766 ? 167.887 207.902 252.802 1.00 68.26  ?  785 PHE B CZ    1 
ATOM   12334 N  N     . PHE B 1 767 ? 172.410 211.113 249.903 1.00 52.76  ?  786 PHE B N     1 
ATOM   12335 C  CA    . PHE B 1 767 ? 173.223 211.762 250.922 1.00 54.08  ?  786 PHE B CA    1 
ATOM   12336 C  C     . PHE B 1 767 ? 173.642 213.173 250.547 1.00 55.99  ?  786 PHE B C     1 
ATOM   12337 O  O     . PHE B 1 767 ? 173.537 214.079 251.377 1.00 59.31  ?  786 PHE B O     1 
ATOM   12338 C  CB    . PHE B 1 767 ? 174.469 210.918 251.214 1.00 59.57  ?  786 PHE B CB    1 
ATOM   12339 C  CG    . PHE B 1 767 ? 174.170 209.640 251.945 1.00 58.23  ?  786 PHE B CG    1 
ATOM   12340 C  CD1   . PHE B 1 767 ? 173.893 209.651 253.301 1.00 56.31  ?  786 PHE B CD1   1 
ATOM   12341 C  CD2   . PHE B 1 767 ? 174.151 208.430 251.272 1.00 59.38  ?  786 PHE B CD2   1 
ATOM   12342 C  CE1   . PHE B 1 767 ? 173.613 208.477 253.976 1.00 59.00  ?  786 PHE B CE1   1 
ATOM   12343 C  CE2   . PHE B 1 767 ? 173.871 207.253 251.941 1.00 59.33  ?  786 PHE B CE2   1 
ATOM   12344 C  CZ    . PHE B 1 767 ? 173.601 207.277 253.296 1.00 59.93  ?  786 PHE B CZ    1 
ATOM   12345 N  N     . SER B 1 768 ? 174.101 213.387 249.314 1.00 54.59  ?  787 SER B N     1 
ATOM   12346 C  CA    . SER B 1 768 ? 174.482 214.724 248.875 1.00 54.16  ?  787 SER B CA    1 
ATOM   12347 C  C     . SER B 1 768 ? 174.624 214.803 247.360 1.00 45.40  ?  787 SER B C     1 
ATOM   12348 O  O     . SER B 1 768 ? 175.296 213.967 246.747 1.00 48.73  ?  787 SER B O     1 
ATOM   12349 C  CB    . SER B 1 768 ? 175.792 215.153 249.539 1.00 57.13  ?  787 SER B CB    1 
ATOM   12350 O  OG    . SER B 1 768 ? 176.327 216.302 248.908 1.00 55.89  ?  787 SER B OG    1 
ATOM   12351 N  N     . ARG B 1 769 ? 173.997 215.808 246.753 1.00 37.45  ?  788 ARG B N     1 
ATOM   12352 C  CA    . ARG B 1 769 ? 174.228 216.109 245.353 1.00 40.23  ?  788 ARG B CA    1 
ATOM   12353 C  C     . ARG B 1 769 ? 175.621 216.707 245.172 1.00 48.26  ?  788 ARG B C     1 
ATOM   12354 O  O     . ARG B 1 769 ? 176.243 217.154 246.137 1.00 54.55  ?  788 ARG B O     1 
ATOM   12355 C  CB    . ARG B 1 769 ? 173.171 217.081 244.833 1.00 44.60  ?  788 ARG B CB    1 
ATOM   12356 C  CG    . ARG B 1 769 ? 171.922 216.421 244.282 1.00 47.77  ?  788 ARG B CG    1 
ATOM   12357 C  CD    . ARG B 1 769 ? 171.015 217.449 243.628 1.00 44.24  ?  788 ARG B CD    1 
ATOM   12358 N  NE    . ARG B 1 769 ? 169.786 216.851 243.122 1.00 52.70  ?  788 ARG B NE    1 
ATOM   12359 C  CZ    . ARG B 1 769 ? 169.622 216.424 241.878 1.00 52.73  ?  788 ARG B CZ    1 
ATOM   12360 N  NH1   . ARG B 1 769 ? 170.594 216.508 240.984 1.00 50.14  1  788 ARG B NH1   1 
ATOM   12361 N  NH2   . ARG B 1 769 ? 168.454 215.897 241.521 1.00 50.49  ?  788 ARG B NH2   1 
ATOM   12362 N  N     . PRO B 1 770 ? 176.149 216.694 243.940 1.00 45.31  ?  789 PRO B N     1 
ATOM   12363 C  CA    . PRO B 1 770 ? 177.408 217.404 243.674 1.00 35.93  ?  789 PRO B CA    1 
ATOM   12364 C  C     . PRO B 1 770 ? 177.332 218.873 244.065 1.00 35.88  ?  789 PRO B C     1 
ATOM   12365 O  O     . PRO B 1 770 ? 176.451 219.601 243.598 1.00 43.80  ?  789 PRO B O     1 
ATOM   12366 C  CB    . PRO B 1 770 ? 177.589 217.231 242.161 1.00 37.07  ?  789 PRO B CB    1 
ATOM   12367 C  CG    . PRO B 1 770 ? 176.913 215.943 241.861 1.00 41.56  ?  789 PRO B CG    1 
ATOM   12368 C  CD    . PRO B 1 770 ? 175.732 215.867 242.793 1.00 45.94  ?  789 PRO B CD    1 
ATOM   12369 N  N     . LEU B 1 771 ? 178.259 219.322 244.927 1.00 32.71  ?  790 LEU B N     1 
ATOM   12370 C  CA    . LEU B 1 771 ? 178.214 220.682 245.453 1.00 37.49  ?  790 LEU B CA    1 
ATOM   12371 C  C     . LEU B 1 771 ? 179.427 221.474 244.995 1.00 40.02  ?  790 LEU B C     1 
ATOM   12372 O  O     . LEU B 1 771 ? 180.546 220.940 245.001 1.00 51.50  ?  790 LEU B O     1 
ATOM   12373 C  CB    . LEU B 1 771 ? 178.160 220.667 246.979 1.00 43.62  ?  790 LEU B CB    1 
ATOM   12374 C  CG    . LEU B 1 771 ? 177.049 219.851 247.639 1.00 47.41  ?  790 LEU B CG    1 
ATOM   12375 C  CD1   . LEU B 1 771 ? 177.426 219.483 249.065 1.00 45.43  ?  790 LEU B CD1   1 
ATOM   12376 C  CD2   . LEU B 1 771 ? 175.733 220.611 247.606 1.00 45.30  ?  790 LEU B CD2   1 
ATOM   12377 N  N     . PRO B 1 772 ? 179.247 222.730 244.587 1.00 40.55  ?  791 PRO B N     1 
ATOM   12378 C  CA    . PRO B 1 772 ? 180.400 223.574 244.259 1.00 36.57  ?  791 PRO B CA    1 
ATOM   12379 C  C     . PRO B 1 772 ? 181.321 223.754 245.457 1.00 41.10  ?  791 PRO B C     1 
ATOM   12380 O  O     . PRO B 1 772 ? 180.900 223.728 246.615 1.00 48.92  ?  791 PRO B O     1 
ATOM   12381 C  CB    . PRO B 1 772 ? 179.759 224.901 243.844 1.00 40.59  ?  791 PRO B CB    1 
ATOM   12382 C  CG    . PRO B 1 772 ? 178.425 224.512 243.312 1.00 45.64  ?  791 PRO B CG    1 
ATOM   12383 C  CD    . PRO B 1 772 ? 177.979 223.316 244.115 1.00 47.07  ?  791 PRO B CD    1 
ATOM   12384 N  N     . ALA B 1 773 ? 182.608 223.938 245.154 1.00 44.34  ?  792 ALA B N     1 
ATOM   12385 C  CA    . ALA B 1 773 ? 183.637 223.953 246.187 1.00 49.43  ?  792 ALA B CA    1 
ATOM   12386 C  C     . ALA B 1 773 ? 183.532 225.148 247.128 1.00 50.40  ?  792 ALA B C     1 
ATOM   12387 O  O     . ALA B 1 773 ? 184.158 225.131 248.193 1.00 52.84  ?  792 ALA B O     1 
ATOM   12388 C  CB    . ALA B 1 773 ? 185.023 223.929 245.543 1.00 52.15  ?  792 ALA B CB    1 
ATOM   12389 N  N     . GLU B 1 774 ? 182.762 226.180 246.773 1.00 47.99  ?  793 GLU B N     1 
ATOM   12390 C  CA    . GLU B 1 774 ? 182.729 227.379 247.606 1.00 48.76  ?  793 GLU B CA    1 
ATOM   12391 C  C     . GLU B 1 774 ? 181.970 227.153 248.909 1.00 49.51  ?  793 GLU B C     1 
ATOM   12392 O  O     . GLU B 1 774 ? 182.182 227.891 249.879 1.00 54.54  ?  793 GLU B O     1 
ATOM   12393 C  CB    . GLU B 1 774 ? 182.122 228.551 246.832 1.00 50.22  ?  793 GLU B CB    1 
ATOM   12394 C  CG    . GLU B 1 774 ? 180.651 228.393 246.494 1.00 51.96  ?  793 GLU B CG    1 
ATOM   12395 C  CD    . GLU B 1 774 ? 180.424 228.068 245.033 1.00 57.59  ?  793 GLU B CD    1 
ATOM   12396 O  OE1   . GLU B 1 774 ? 181.411 227.778 244.325 1.00 55.55  ?  793 GLU B OE1   1 
ATOM   12397 O  OE2   . GLU B 1 774 ? 179.256 228.106 244.591 1.00 58.60  -1 793 GLU B OE2   1 
ATOM   12398 N  N     . GLU B 1 775 ? 181.089 226.154 248.961 1.00 46.70  ?  794 GLU B N     1 
ATOM   12399 C  CA    . GLU B 1 775 ? 180.340 225.847 250.173 1.00 50.74  ?  794 GLU B CA    1 
ATOM   12400 C  C     . GLU B 1 775 ? 180.558 224.417 250.657 1.00 45.57  ?  794 GLU B C     1 
ATOM   12401 O  O     . GLU B 1 775 ? 179.861 223.970 251.575 1.00 51.98  ?  794 GLU B O     1 
ATOM   12402 C  CB    . GLU B 1 775 ? 178.846 226.121 249.961 1.00 55.03  ?  794 GLU B CB    1 
ATOM   12403 C  CG    . GLU B 1 775 ? 178.067 224.995 249.304 1.00 53.86  ?  794 GLU B CG    1 
ATOM   12404 C  CD    . GLU B 1 775 ? 178.231 224.974 247.802 1.00 52.12  ?  794 GLU B CD    1 
ATOM   12405 O  OE1   . GLU B 1 775 ? 178.429 226.054 247.208 1.00 54.65  ?  794 GLU B OE1   1 
ATOM   12406 O  OE2   . GLU B 1 775 ? 178.159 223.876 247.216 1.00 49.23  -1 794 GLU B OE2   1 
ATOM   12407 N  N     . ILE B 1 776 ? 181.514 223.694 250.067 1.00 51.10  ?  795 ILE B N     1 
ATOM   12408 C  CA    . ILE B 1 776 ? 181.846 222.354 250.561 1.00 61.08  ?  795 ILE B CA    1 
ATOM   12409 C  C     . ILE B 1 776 ? 182.216 222.367 252.042 1.00 62.08  ?  795 ILE B C     1 
ATOM   12410 O  O     . ILE B 1 776 ? 181.713 221.510 252.788 1.00 68.39  ?  795 ILE B O     1 
ATOM   12411 C  CB    . ILE B 1 776 ? 182.934 221.721 249.678 1.00 61.75  ?  795 ILE B CB    1 
ATOM   12412 C  CG1   . ILE B 1 776 ? 182.327 221.186 248.378 1.00 59.40  ?  795 ILE B CG1   1 
ATOM   12413 C  CG2   . ILE B 1 776 ? 183.666 220.615 250.422 1.00 57.42  ?  795 ILE B CG2   1 
ATOM   12414 C  CD1   . ILE B 1 776 ? 181.365 220.036 248.581 1.00 58.80  ?  795 ILE B CD1   1 
ATOM   12415 N  N     . PRO B 1 777 ? 183.059 223.285 252.535 1.00 57.55  ?  796 PRO B N     1 
ATOM   12416 C  CA    . PRO B 1 777 ? 183.285 223.337 253.989 1.00 59.45  ?  796 PRO B CA    1 
ATOM   12417 C  C     . PRO B 1 777 ? 182.016 223.576 254.785 1.00 57.21  ?  796 PRO B C     1 
ATOM   12418 O  O     . PRO B 1 777 ? 181.914 223.100 255.922 1.00 57.46  ?  796 PRO B O     1 
ATOM   12419 C  CB    . PRO B 1 777 ? 184.281 224.494 254.147 1.00 62.59  ?  796 PRO B CB    1 
ATOM   12420 C  CG    . PRO B 1 777 ? 184.998 224.538 252.850 1.00 58.85  ?  796 PRO B CG    1 
ATOM   12421 C  CD    . PRO B 1 777 ? 183.956 224.216 251.823 1.00 55.59  ?  796 PRO B CD    1 
ATOM   12422 N  N     . GLY B 1 778 ? 181.043 224.297 254.225 1.00 60.15  ?  797 GLY B N     1 
ATOM   12423 C  CA    . GLY B 1 778 ? 179.764 224.438 254.901 1.00 60.54  ?  797 GLY B CA    1 
ATOM   12424 C  C     . GLY B 1 778 ? 179.072 223.105 255.110 1.00 59.95  ?  797 GLY B C     1 
ATOM   12425 O  O     . GLY B 1 778 ? 178.575 222.817 256.201 1.00 62.62  ?  797 GLY B O     1 
ATOM   12426 N  N     . TRP B 1 779 ? 179.041 222.269 254.069 1.00 62.34  ?  798 TRP B N     1 
ATOM   12427 C  CA    . TRP B 1 779 ? 178.504 220.920 254.217 1.00 62.31  ?  798 TRP B CA    1 
ATOM   12428 C  C     . TRP B 1 779 ? 179.299 220.111 255.231 1.00 64.22  ?  798 TRP B C     1 
ATOM   12429 O  O     . TRP B 1 779 ? 178.707 219.411 256.062 1.00 72.34  ?  798 TRP B O     1 
ATOM   12430 C  CB    . TRP B 1 779 ? 178.490 220.205 252.865 1.00 61.80  ?  798 TRP B CB    1 
ATOM   12431 C  CG    . TRP B 1 779 ? 177.455 219.125 252.756 1.00 63.72  ?  798 TRP B CG    1 
ATOM   12432 C  CD1   . TRP B 1 779 ? 176.161 219.264 252.344 1.00 65.19  ?  798 TRP B CD1   1 
ATOM   12433 C  CD2   . TRP B 1 779 ? 177.633 217.734 253.053 1.00 66.54  ?  798 TRP B CD2   1 
ATOM   12434 N  NE1   . TRP B 1 779 ? 175.522 218.047 252.372 1.00 65.55  ?  798 TRP B NE1   1 
ATOM   12435 C  CE2   . TRP B 1 779 ? 176.404 217.092 252.803 1.00 67.36  ?  798 TRP B CE2   1 
ATOM   12436 C  CE3   . TRP B 1 779 ? 178.711 216.971 253.510 1.00 68.72  ?  798 TRP B CE3   1 
ATOM   12437 C  CZ2   . TRP B 1 779 ? 176.226 215.723 252.993 1.00 68.02  ?  798 TRP B CZ2   1 
ATOM   12438 C  CZ3   . TRP B 1 779 ? 178.532 215.613 253.698 1.00 71.51  ?  798 TRP B CZ3   1 
ATOM   12439 C  CH2   . TRP B 1 779 ? 177.299 215.003 253.441 1.00 71.32  ?  798 TRP B CH2   1 
ATOM   12440 N  N     . MET B 1 780 ? 180.631 220.206 255.187 1.00 63.56  ?  799 MET B N     1 
ATOM   12441 C  CA    . MET B 1 780 ? 181.458 219.455 256.127 1.00 64.75  ?  799 MET B CA    1 
ATOM   12442 C  C     . MET B 1 780 ? 181.146 219.836 257.570 1.00 67.09  ?  799 MET B C     1 
ATOM   12443 O  O     . MET B 1 780 ? 181.029 218.964 258.439 1.00 70.09  ?  799 MET B O     1 
ATOM   12444 C  CB    . MET B 1 780 ? 182.939 219.686 255.829 1.00 67.37  ?  799 MET B CB    1 
ATOM   12445 C  CG    . MET B 1 780 ? 183.345 219.402 254.396 1.00 70.41  ?  799 MET B CG    1 
ATOM   12446 S  SD    . MET B 1 780 ? 182.789 217.785 253.839 1.00 83.77  ?  799 MET B SD    1 
ATOM   12447 C  CE    . MET B 1 780 ? 181.805 218.230 252.411 1.00 69.86  ?  799 MET B CE    1 
ATOM   12448 N  N     . SER B 1 781 ? 181.007 221.131 257.842 1.00 66.21  ?  800 SER B N     1 
ATOM   12449 C  CA    . SER B 1 781 ? 180.800 221.628 259.194 1.00 67.88  ?  800 SER B CA    1 
ATOM   12450 C  C     . SER B 1 781 ? 179.346 221.576 259.646 1.00 64.57  ?  800 SER B C     1 
ATOM   12451 O  O     . SER B 1 781 ? 179.084 221.705 260.846 1.00 67.52  ?  800 SER B O     1 
ATOM   12452 C  CB    . SER B 1 781 ? 181.320 223.065 259.310 1.00 68.44  ?  800 SER B CB    1 
ATOM   12453 O  OG    . SER B 1 781 ? 182.701 223.131 259.000 1.00 67.42  ?  800 SER B OG    1 
ATOM   12454 N  N     . SER B 1 782 ? 178.394 221.395 258.731 1.00 61.60  ?  801 SER B N     1 
ATOM   12455 C  CA    . SER B 1 782 ? 176.987 221.431 259.100 1.00 64.06  ?  801 SER B CA    1 
ATOM   12456 C  C     . SER B 1 782 ? 176.269 220.094 259.007 1.00 64.03  ?  801 SER B C     1 
ATOM   12457 O  O     . SER B 1 782 ? 175.233 219.930 259.655 1.00 63.44  ?  801 SER B O     1 
ATOM   12458 C  CB    . SER B 1 782 ? 176.235 222.447 258.226 1.00 67.17  ?  801 SER B CB    1 
ATOM   12459 O  OG    . SER B 1 782 ? 174.841 222.401 258.474 1.00 70.34  ?  801 SER B OG    1 
ATOM   12460 N  N     . VAL B 1 783 ? 176.771 219.139 258.230 1.00 69.63  ?  802 VAL B N     1 
ATOM   12461 C  CA    . VAL B 1 783 ? 176.067 217.891 257.969 1.00 72.13  ?  802 VAL B CA    1 
ATOM   12462 C  C     . VAL B 1 783 ? 176.701 216.721 258.713 1.00 70.59  ?  802 VAL B C     1 
ATOM   12463 O  O     . VAL B 1 783 ? 176.007 215.945 259.370 1.00 68.75  ?  802 VAL B O     1 
ATOM   12464 C  CB    . VAL B 1 783 ? 175.990 217.608 256.452 1.00 73.45  ?  802 VAL B CB    1 
ATOM   12465 C  CG1   . VAL B 1 783 ? 175.130 216.387 256.192 1.00 70.54  ?  802 VAL B CG1   1 
ATOM   12466 C  CG2   . VAL B 1 783 ? 175.444 218.820 255.716 1.00 70.20  ?  802 VAL B CG2   1 
ATOM   12467 N  N     . LEU B 1 784 ? 178.019 216.576 258.615 1.00 72.77  ?  803 LEU B N     1 
ATOM   12468 C  CA    . LEU B 1 784 ? 178.690 215.439 259.229 1.00 73.63  ?  803 LEU B CA    1 
ATOM   12469 C  C     . LEU B 1 784 ? 178.610 215.529 260.752 1.00 72.40  ?  803 LEU B C     1 
ATOM   12470 O  O     . LEU B 1 784 ? 178.766 216.615 261.319 1.00 77.40  ?  803 LEU B O     1 
ATOM   12471 C  CB    . LEU B 1 784 ? 180.152 215.383 258.788 1.00 75.71  ?  803 LEU B CB    1 
ATOM   12472 C  CG    . LEU B 1 784 ? 180.411 215.148 257.299 1.00 75.89  ?  803 LEU B CG    1 
ATOM   12473 C  CD1   . LEU B 1 784 ? 181.749 215.743 256.889 1.00 73.03  ?  803 LEU B CD1   1 
ATOM   12474 C  CD2   . LEU B 1 784 ? 180.364 213.665 256.978 1.00 74.93  ?  803 LEU B CD2   1 
ATOM   12475 N  N     . PRO B 1 785 ? 178.362 214.405 261.446 1.00 67.57  ?  804 PRO B N     1 
ATOM   12476 C  CA    . PRO B 1 785 ? 178.037 213.090 260.880 1.00 69.59  ?  804 PRO B CA    1 
ATOM   12477 C  C     . PRO B 1 785 ? 176.564 212.980 260.488 1.00 74.64  ?  804 PRO B C     1 
ATOM   12478 O  O     . PRO B 1 785 ? 175.748 213.764 260.971 1.00 75.50  ?  804 PRO B O     1 
ATOM   12479 C  CB    . PRO B 1 785 ? 178.367 212.118 262.024 1.00 69.44  ?  804 PRO B CB    1 
ATOM   12480 C  CG    . PRO B 1 785 ? 179.082 212.945 263.072 1.00 70.75  ?  804 PRO B CG    1 
ATOM   12481 C  CD    . PRO B 1 785 ? 178.554 214.326 262.901 1.00 71.03  ?  804 PRO B CD    1 
ATOM   12482 N  N     . LEU B 1 786 ? 176.227 212.008 259.642 1.00 72.96  ?  805 LEU B N     1 
ATOM   12483 C  CA    . LEU B 1 786 ? 174.877 211.877 259.102 1.00 69.23  ?  805 LEU B CA    1 
ATOM   12484 C  C     . LEU B 1 786 ? 174.041 210.810 259.789 1.00 72.18  ?  805 LEU B C     1 
ATOM   12485 O  O     . LEU B 1 786 ? 172.915 211.096 260.204 1.00 71.32  ?  805 LEU B O     1 
ATOM   12486 C  CB    . LEU B 1 786 ? 174.933 211.572 257.600 1.00 69.00  ?  805 LEU B CB    1 
ATOM   12487 C  CG    . LEU B 1 786 ? 175.208 212.743 256.654 1.00 71.29  ?  805 LEU B CG    1 
ATOM   12488 C  CD1   . LEU B 1 786 ? 176.681 213.125 256.657 1.00 70.40  ?  805 LEU B CD1   1 
ATOM   12489 C  CD2   . LEU B 1 786 ? 174.736 212.423 255.245 1.00 72.32  ?  805 LEU B CD2   1 
ATOM   12490 N  N     . LYS B 1 787 ? 174.563 209.592 259.919 1.00 81.13  ?  806 LYS B N     1 
ATOM   12491 C  CA    . LYS B 1 787 ? 173.818 208.465 260.482 1.00 79.28  ?  806 LYS B CA    1 
ATOM   12492 C  C     . LYS B 1 787 ? 172.490 208.250 259.762 1.00 75.33  ?  806 LYS B C     1 
ATOM   12493 O  O     . LYS B 1 787 ? 172.290 207.233 259.099 1.00 74.74  ?  806 LYS B O     1 
ATOM   12494 C  CB    . LYS B 1 787 ? 173.574 208.668 261.981 1.00 79.11  ?  806 LYS B CB    1 
ATOM   12495 C  CG    . LYS B 1 787 ? 174.829 208.974 262.779 1.00 81.11  ?  806 LYS B CG    1 
ATOM   12496 C  CD    . LYS B 1 787 ? 175.788 207.795 262.771 1.00 79.87  ?  806 LYS B CD    1 
ATOM   12497 C  CE    . LYS B 1 787 ? 175.280 206.668 263.656 1.00 79.59  ?  806 LYS B CE    1 
ATOM   12498 N  NZ    . LYS B 1 787 ? 175.245 207.064 265.091 1.00 80.95  1  806 LYS B NZ    1 
HETATM 12499 C  CHA   . HEM C 2 .   ? 185.837 173.306 99.454  1.00 77.54  ?  901 HEM A CHA   1 
HETATM 12500 C  CHB   . HEM C 2 .   ? 189.047 176.435 101.275 1.00 70.61  ?  901 HEM A CHB   1 
HETATM 12501 C  CHC   . HEM C 2 .   ? 187.503 179.818 98.179  1.00 70.13  ?  901 HEM A CHC   1 
HETATM 12502 C  CHD   . HEM C 2 .   ? 184.383 176.648 96.250  1.00 73.87  ?  901 HEM A CHD   1 
HETATM 12503 C  C1A   . HEM C 2 .   ? 186.732 173.909 100.304 1.00 74.44  ?  901 HEM A C1A   1 
HETATM 12504 C  C2A   . HEM C 2 .   ? 187.124 173.431 101.612 1.00 71.94  ?  901 HEM A C2A   1 
HETATM 12505 C  C3A   . HEM C 2 .   ? 188.009 174.292 102.118 1.00 72.16  ?  901 HEM A C3A   1 
HETATM 12506 C  C4A   . HEM C 2 .   ? 188.213 175.347 101.145 1.00 71.64  ?  901 HEM A C4A   1 
HETATM 12507 C  CMA   . HEM C 2 .   ? 188.700 174.188 103.494 1.00 73.45  ?  901 HEM A CMA   1 
HETATM 12508 C  CAA   . HEM C 2 .   ? 186.600 172.150 102.294 1.00 73.49  ?  901 HEM A CAA   1 
HETATM 12509 C  CBA   . HEM C 2 .   ? 187.595 171.015 102.076 1.00 79.45  ?  901 HEM A CBA   1 
HETATM 12510 C  CGA   . HEM C 2 .   ? 187.090 169.770 102.755 1.00 79.58  ?  901 HEM A CGA   1 
HETATM 12511 O  O1A   . HEM C 2 .   ? 187.804 168.735 102.722 1.00 75.40  ?  901 HEM A O1A   1 
HETATM 12512 O  O2A   . HEM C 2 .   ? 185.972 169.813 103.331 1.00 77.42  ?  901 HEM A O2A   1 
HETATM 12513 C  C1B   . HEM C 2 .   ? 188.838 177.655 100.671 1.00 71.37  ?  901 HEM A C1B   1 
HETATM 12514 C  C2B   . HEM C 2 .   ? 189.342 178.937 101.123 1.00 73.45  ?  901 HEM A C2B   1 
HETATM 12515 C  C3B   . HEM C 2 .   ? 188.915 179.877 100.259 1.00 73.06  ?  901 HEM A C3B   1 
HETATM 12516 C  C4B   . HEM C 2 .   ? 188.125 179.209 99.245  1.00 70.46  ?  901 HEM A C4B   1 
HETATM 12517 C  CMB   . HEM C 2 .   ? 190.219 179.106 102.385 1.00 72.47  ?  901 HEM A CMB   1 
HETATM 12518 C  CAB   . HEM C 2 .   ? 189.148 181.411 100.252 1.00 74.46  ?  901 HEM A CAB   1 
HETATM 12519 C  CBB   . HEM C 2 .   ? 189.786 182.088 101.213 1.00 74.89  ?  901 HEM A CBB   1 
HETATM 12520 C  C1C   . HEM C 2 .   ? 186.480 179.285 97.428  1.00 69.97  ?  901 HEM A C1C   1 
HETATM 12521 C  C2C   . HEM C 2 .   ? 185.623 180.013 96.519  1.00 69.70  ?  901 HEM A C2C   1 
HETATM 12522 C  C3C   . HEM C 2 .   ? 184.753 179.156 95.977  1.00 70.52  ?  901 HEM A C3C   1 
HETATM 12523 C  C4C   . HEM C 2 .   ? 185.030 177.835 96.528  1.00 73.80  ?  901 HEM A C4C   1 
HETATM 12524 C  CMC   . HEM C 2 .   ? 185.704 181.528 96.230  1.00 75.07  ?  901 HEM A CMC   1 
HETATM 12525 C  CAC   . HEM C 2 .   ? 183.669 179.563 94.949  1.00 70.00  ?  901 HEM A CAC   1 
HETATM 12526 C  CBC   . HEM C 2 .   ? 182.798 178.691 94.427  1.00 68.84  ?  901 HEM A CBC   1 
HETATM 12527 C  C1D   . HEM C 2 .   ? 184.483 175.472 96.962  1.00 69.22  ?  901 HEM A C1D   1 
HETATM 12528 C  C2D   . HEM C 2 .   ? 183.680 174.281 96.769  1.00 71.11  ?  901 HEM A C2D   1 
HETATM 12529 C  C3D   . HEM C 2 .   ? 184.078 173.364 97.654  1.00 69.70  ?  901 HEM A C3D   1 
HETATM 12530 C  C4D   . HEM C 2 .   ? 185.152 173.934 98.438  1.00 71.81  ?  901 HEM A C4D   1 
HETATM 12531 C  CMD   . HEM C 2 .   ? 182.557 174.107 95.726  1.00 72.46  ?  901 HEM A CMD   1 
HETATM 12532 C  CAD   . HEM C 2 .   ? 183.511 171.939 97.819  1.00 72.05  ?  901 HEM A CAD   1 
HETATM 12533 C  CBD   . HEM C 2 .   ? 182.802 171.827 99.165  1.00 73.43  ?  901 HEM A CBD   1 
HETATM 12534 C  CGD   . HEM C 2 .   ? 182.615 170.376 99.520  1.00 77.76  ?  901 HEM A CGD   1 
HETATM 12535 O  O1D   . HEM C 2 .   ? 181.966 170.092 100.560 1.00 79.39  ?  901 HEM A O1D   1 
HETATM 12536 O  O2D   . HEM C 2 .   ? 183.116 169.504 98.765  1.00 76.12  ?  901 HEM A O2D   1 
HETATM 12537 N  NA    . HEM C 2 .   ? 187.414 175.081 100.049 1.00 73.13  ?  901 HEM A NA    1 
HETATM 12538 N  NB    . HEM C 2 .   ? 188.099 177.859 99.525  1.00 69.71  ?  901 HEM A NB    1 
HETATM 12539 N  NC    . HEM C 2 .   ? 186.090 177.961 97.408  1.00 74.36  ?  901 HEM A NC    1 
HETATM 12540 N  ND    . HEM C 2 .   ? 185.371 175.221 97.989  1.00 65.38  ?  901 HEM A ND    1 
HETATM 12541 FE FE    . HEM C 2 .   ? 186.752 176.526 98.731  1.00 74.10  ?  901 HEM A FE    1 
HETATM 12542 P  P1    . C2E D 3 .   ? 188.108 166.973 233.181 1.00 63.55  ?  902 C2E A P1    1 
HETATM 12543 O  O2P   . C2E D 3 .   ? 186.700 167.456 232.981 1.00 50.66  ?  902 C2E A O2P   1 
HETATM 12544 O  O1P   . C2E D 3 .   ? 188.924 167.642 234.249 1.00 56.72  -1 902 C2E A O1P   1 
HETATM 12545 O  "O5'" . C2E D 3 .   ? 188.052 165.402 233.504 1.00 60.91  ?  902 C2E A "O5'" 1 
HETATM 12546 C  "C5'" . C2E D 3 .   ? 188.676 164.920 234.719 1.00 56.10  ?  902 C2E A "C5'" 1 
HETATM 12547 C  "C4'" . C2E D 3 .   ? 190.145 164.693 234.463 1.00 50.53  ?  902 C2E A "C4'" 1 
HETATM 12548 O  "O4'" . C2E D 3 .   ? 190.898 165.145 235.616 1.00 44.84  ?  902 C2E A "O4'" 1 
HETATM 12549 C  "C3'" . C2E D 3 .   ? 190.542 163.238 234.240 1.00 48.38  ?  902 C2E A "C3'" 1 
HETATM 12550 O  "O3'" . C2E D 3 .   ? 191.539 163.147 233.234 1.00 49.82  ?  902 C2E A "O3'" 1 
HETATM 12551 C  "C2'" . C2E D 3 .   ? 191.086 162.828 235.606 1.00 49.36  ?  902 C2E A "C2'" 1 
HETATM 12552 O  "O2'" . C2E D 3 .   ? 192.010 161.764 235.530 1.00 53.55  ?  902 C2E A "O2'" 1 
HETATM 12553 C  "C1'" . C2E D 3 .   ? 191.753 164.120 236.051 1.00 47.76  ?  902 C2E A "C1'" 1 
HETATM 12554 N  N9    . C2E D 3 .   ? 191.893 164.234 237.492 1.00 51.92  ?  902 C2E A N9    1 
HETATM 12555 C  C8    . C2E D 3 .   ? 190.880 164.218 238.414 1.00 56.90  ?  902 C2E A C8    1 
HETATM 12556 N  N7    . C2E D 3 .   ? 191.303 164.334 239.648 1.00 57.36  ?  902 C2E A N7    1 
HETATM 12557 C  C5    . C2E D 3 .   ? 192.682 164.434 239.527 1.00 49.22  ?  902 C2E A C5    1 
HETATM 12558 C  C6    . C2E D 3 .   ? 193.671 164.580 240.523 1.00 51.41  ?  902 C2E A C6    1 
HETATM 12559 O  O6    . C2E D 3 .   ? 193.516 164.652 241.747 1.00 58.75  ?  902 C2E A O6    1 
HETATM 12560 N  N1    . C2E D 3 .   ? 194.947 164.643 239.969 1.00 56.74  ?  902 C2E A N1    1 
HETATM 12561 C  C2    . C2E D 3 .   ? 195.233 164.574 238.629 1.00 52.71  ?  902 C2E A C2    1 
HETATM 12562 N  N2    . C2E D 3 .   ? 196.526 164.648 238.287 1.00 55.42  ?  902 C2E A N2    1 
HETATM 12563 N  N3    . C2E D 3 .   ? 194.306 164.434 237.686 1.00 44.33  ?  902 C2E A N3    1 
HETATM 12564 C  C4    . C2E D 3 .   ? 193.059 164.372 238.205 1.00 46.37  ?  902 C2E A C4    1 
HETATM 12565 P  P11   . C2E D 3 .   ? 190.964 162.335 231.975 1.00 52.11  ?  902 C2E A P11   1 
HETATM 12566 O  O21   . C2E D 3 .   ? 190.082 161.223 232.460 1.00 53.24  ?  902 C2E A O21   1 
HETATM 12567 O  O11   . C2E D 3 .   ? 192.100 162.004 231.051 1.00 46.50  -1 902 C2E A O11   1 
HETATM 12568 O  O5A   . C2E D 3 .   ? 190.068 163.443 231.243 1.00 51.75  ?  902 C2E A O5A   1 
HETATM 12569 C  C5A   . C2E D 3 .   ? 190.762 164.574 230.684 1.00 48.11  ?  902 C2E A C5A   1 
HETATM 12570 C  C4A   . C2E D 3 .   ? 189.755 165.513 230.075 1.00 48.53  ?  902 C2E A C4A   1 
HETATM 12571 O  O4A   . C2E D 3 .   ? 189.122 164.853 228.956 1.00 47.24  ?  902 C2E A O4A   1 
HETATM 12572 C  C3A   . C2E D 3 .   ? 188.598 165.905 230.971 1.00 46.03  ?  902 C2E A C3A   1 
HETATM 12573 O  O3A   . C2E D 3 .   ? 188.931 167.006 231.804 1.00 50.36  ?  902 C2E A O3A   1 
HETATM 12574 C  C2A   . C2E D 3 .   ? 187.568 166.334 229.931 1.00 49.39  ?  902 C2E A C2A   1 
HETATM 12575 O  O2A   . C2E D 3 .   ? 187.774 167.657 229.490 1.00 52.61  ?  902 C2E A O2A   1 
HETATM 12576 C  C1A   . C2E D 3 .   ? 187.807 165.328 228.809 1.00 46.30  ?  902 C2E A C1A   1 
HETATM 12577 N  N91   . C2E D 3 .   ? 186.898 164.194 228.857 1.00 45.32  ?  902 C2E A N91   1 
HETATM 12578 C  C81   . C2E D 3 .   ? 186.989 163.107 229.685 1.00 49.11  ?  902 C2E A C81   1 
HETATM 12579 N  N71   . C2E D 3 .   ? 186.014 162.250 229.523 1.00 51.50  ?  902 C2E A N71   1 
HETATM 12580 C  C51   . C2E D 3 .   ? 185.230 162.811 228.528 1.00 45.07  ?  902 C2E A C51   1 
HETATM 12581 C  C61   . C2E D 3 .   ? 184.039 162.333 227.940 1.00 43.60  ?  902 C2E A C61   1 
HETATM 12582 O  O61   . C2E D 3 .   ? 183.431 161.286 228.190 1.00 51.79  ?  902 C2E A O61   1 
HETATM 12583 N  N11   . C2E D 3 .   ? 183.565 163.210 226.967 1.00 43.22  ?  902 C2E A N11   1 
HETATM 12584 C  C21   . C2E D 3 .   ? 184.158 164.394 226.611 1.00 48.44  ?  902 C2E A C21   1 
HETATM 12585 N  N21   . C2E D 3 .   ? 183.550 165.104 225.653 1.00 48.82  ?  902 C2E A N21   1 
HETATM 12586 N  N31   . C2E D 3 .   ? 185.280 164.850 227.165 1.00 51.12  ?  902 C2E A N31   1 
HETATM 12587 C  C41   . C2E D 3 .   ? 185.760 164.008 228.111 1.00 48.02  ?  902 C2E A C41   1 
HETATM 12588 MG MG    . MG  E 4 .   ? 184.992 167.280 234.120 1.00 35.42  ?  903 MG  A MG    1 
HETATM 12589 MG MG    . MG  F 4 .   ? 188.706 170.232 235.176 1.00 53.67  ?  904 MG  A MG    1 
HETATM 12590 P  P1    . C2E G 3 .   ? 180.873 208.748 236.507 1.00 46.92  ?  901 C2E B P1    1 
HETATM 12591 O  O2P   . C2E G 3 .   ? 182.270 208.521 237.011 1.00 53.22  ?  901 C2E B O2P   1 
HETATM 12592 O  O1P   . C2E G 3 .   ? 179.899 207.613 236.635 1.00 57.27  -1 901 C2E B O1P   1 
HETATM 12593 O  "O5'" . C2E G 3 .   ? 180.278 210.008 237.297 1.00 46.99  ?  901 C2E B "O5'" 1 
HETATM 12594 C  "C5'" . C2E G 3 .   ? 179.156 209.780 238.175 1.00 49.46  ?  901 C2E B "C5'" 1 
HETATM 12595 C  "C4'" . C2E G 3 .   ? 177.996 210.601 237.676 1.00 54.74  ?  901 C2E B "C4'" 1 
HETATM 12596 O  "O4'" . C2E G 3 .   ? 176.779 210.137 238.312 1.00 54.30  ?  901 C2E B "O4'" 1 
HETATM 12597 C  "C3'" . C2E G 3 .   ? 178.080 212.089 237.990 1.00 51.85  ?  901 C2E B "C3'" 1 
HETATM 12598 O  "O3'" . C2E G 3 .   ? 177.365 212.825 237.005 1.00 51.38  ?  901 C2E B "O3'" 1 
HETATM 12599 C  "C2'" . C2E G 3 .   ? 177.335 212.146 239.320 1.00 52.55  ?  901 C2E B "C2'" 1 
HETATM 12600 O  "O2'" . C2E G 3 .   ? 176.879 213.439 239.645 1.00 58.29  ?  901 C2E B "O2'" 1 
HETATM 12601 C  "C1'" . C2E G 3 .   ? 176.181 211.211 238.991 1.00 52.94  ?  901 C2E B "C1'" 1 
HETATM 12602 N  N9    . C2E G 3 .   ? 175.461 210.683 240.140 1.00 50.68  ?  901 C2E B N9    1 
HETATM 12603 C  C8    . C2E G 3 .   ? 175.969 210.345 241.366 1.00 53.00  ?  901 C2E B C8    1 
HETATM 12604 N  N7    . C2E G 3 .   ? 175.061 209.887 242.191 1.00 52.05  ?  901 C2E B N7    1 
HETATM 12605 C  C5    . C2E G 3 .   ? 173.885 209.916 241.454 1.00 48.93  ?  901 C2E B C5    1 
HETATM 12606 C  C6    . C2E G 3 .   ? 172.574 209.536 241.818 1.00 52.72  ?  901 C2E B C6    1 
HETATM 12607 O  O6    . C2E G 3 .   ? 172.178 209.088 242.901 1.00 58.25  ?  901 C2E B O6    1 
HETATM 12608 N  N1    . C2E G 3 .   ? 171.680 209.729 240.769 1.00 52.66  ?  901 C2E B N1    1 
HETATM 12609 C  C2    . C2E G 3 .   ? 172.004 210.225 239.533 1.00 52.59  ?  901 C2E B C2    1 
HETATM 12610 N  N2    . C2E G 3 .   ? 171.002 210.346 238.653 1.00 54.42  ?  901 C2E B N2    1 
HETATM 12611 N  N3    . C2E G 3 .   ? 173.235 210.583 239.183 1.00 54.64  ?  901 C2E B N3    1 
HETATM 12612 C  C4    . C2E G 3 .   ? 174.119 210.401 240.190 1.00 48.88  ?  901 C2E B C4    1 
HETATM 12613 P  P11   . C2E G 3 .   ? 178.231 213.536 235.853 1.00 40.28  ?  901 C2E B P11   1 
HETATM 12614 O  O21   . C2E G 3 .   ? 178.984 214.689 236.448 1.00 55.53  ?  901 C2E B O21   1 
HETATM 12615 O  O11   . C2E G 3 .   ? 177.372 213.786 234.649 1.00 42.19  -1 901 C2E B O11   1 
HETATM 12616 O  O5A   . C2E G 3 .   ? 179.296 212.418 235.426 1.00 58.06  ?  901 C2E B O5A   1 
HETATM 12617 C  C5A   . C2E G 3 .   ? 179.151 211.854 234.106 1.00 53.95  ?  901 C2E B C5A   1 
HETATM 12618 C  C4A   . C2E G 3 .   ? 180.464 211.258 233.668 1.00 54.01  ?  901 C2E B C4A   1 
HETATM 12619 O  O4A   . C2E G 3 .   ? 181.332 212.311 233.187 1.00 52.21  ?  901 C2E B O4A   1 
HETATM 12620 C  C3A   . C2E G 3 .   ? 181.286 210.589 234.754 1.00 54.59  ?  901 C2E B C3A   1 
HETATM 12621 O  O3A   . C2E G 3 .   ? 180.859 209.251 234.982 1.00 53.87  ?  901 C2E B O3A   1 
HETATM 12622 C  C2A   . C2E G 3 .   ? 182.655 210.576 234.082 1.00 58.06  ?  901 C2E B C2A   1 
HETATM 12623 O  O2A   . C2E G 3 .   ? 182.797 209.488 233.195 1.00 58.53  ?  901 C2E B O2A   1 
HETATM 12624 C  C1A   . C2E G 3 .   ? 182.672 211.902 233.325 1.00 51.89  ?  901 C2E B C1A   1 
HETATM 12625 N  N91   . C2E G 3 .   ? 183.423 212.938 234.020 1.00 47.46  ?  901 C2E B N91   1 
HETATM 12626 C  C81   . C2E G 3 .   ? 182.946 213.857 234.915 1.00 49.08  ?  901 C2E B C81   1 
HETATM 12627 N  N71   . C2E G 3 .   ? 183.881 214.638 235.395 1.00 54.03  ?  901 C2E B N71   1 
HETATM 12628 C  C51   . C2E G 3 .   ? 185.047 214.194 234.788 1.00 49.10  ?  901 C2E B C51   1 
HETATM 12629 C  C61   . C2E G 3 .   ? 186.379 214.655 234.920 1.00 51.77  ?  901 C2E B C61   1 
HETATM 12630 O  O61   . C2E G 3 .   ? 186.807 215.579 235.622 1.00 56.49  ?  901 C2E B O61   1 
HETATM 12631 N  N11   . C2E G 3 .   ? 187.252 213.925 234.115 1.00 50.91  ?  901 C2E B N11   1 
HETATM 12632 C  C21   . C2E G 3 .   ? 186.892 212.886 233.295 1.00 51.53  ?  901 C2E B C21   1 
HETATM 12633 N  N21   . C2E G 3 .   ? 187.877 212.301 232.603 1.00 53.72  ?  901 C2E B N21   1 
HETATM 12634 N  N31   . C2E G 3 .   ? 185.643 212.449 233.168 1.00 53.00  ?  901 C2E B N31   1 
HETATM 12635 C  C41   . C2E G 3 .   ? 184.778 213.147 233.940 1.00 48.56  ?  901 C2E B C41   1 
HETATM 12636 C  CHA   . HEM H 2 .   ? 164.074 199.970 108.205 1.00 73.50  ?  902 HEM B CHA   1 
HETATM 12637 C  CHB   . HEM H 2 .   ? 163.023 196.990 111.889 1.00 79.61  ?  902 HEM B CHB   1 
HETATM 12638 C  CHC   . HEM H 2 .   ? 162.045 193.452 108.731 1.00 76.23  ?  902 HEM B CHC   1 
HETATM 12639 C  CHD   . HEM H 2 .   ? 162.585 196.577 105.069 1.00 79.08  ?  902 HEM B CHD   1 
HETATM 12640 C  C1A   . HEM H 2 .   ? 163.989 199.433 109.471 1.00 75.03  ?  902 HEM B C1A   1 
HETATM 12641 C  C2A   . HEM H 2 .   ? 164.534 200.008 110.684 1.00 76.24  ?  902 HEM B C2A   1 
HETATM 12642 C  C3A   . HEM H 2 .   ? 164.245 199.191 111.701 1.00 77.65  ?  902 HEM B C3A   1 
HETATM 12643 C  C4A   . HEM H 2 .   ? 163.506 198.063 111.172 1.00 79.81  ?  902 HEM B C4A   1 
HETATM 12644 C  CMA   . HEM H 2 .   ? 164.627 199.403 113.182 1.00 78.23  ?  902 HEM B CMA   1 
HETATM 12645 C  CAA   . HEM H 2 .   ? 165.309 201.340 110.775 1.00 79.62  ?  902 HEM B CAA   1 
HETATM 12646 C  CBA   . HEM H 2 .   ? 166.807 201.053 110.806 1.00 82.99  ?  902 HEM B CBA   1 
HETATM 12647 C  CGA   . HEM H 2 .   ? 167.565 202.346 110.946 1.00 82.43  ?  902 HEM B CGA   1 
HETATM 12648 O  O1A   . HEM H 2 .   ? 168.821 202.300 111.009 1.00 82.07  ?  902 HEM B O1A   1 
HETATM 12649 O  O2A   . HEM H 2 .   ? 166.915 203.421 110.995 1.00 78.70  ?  902 HEM B O2A   1 
HETATM 12650 C  C1B   . HEM H 2 .   ? 162.762 195.744 111.362 1.00 77.53  ?  902 HEM B C1B   1 
HETATM 12651 C  C2B   . HEM H 2 .   ? 162.689 194.496 112.095 1.00 76.19  ?  902 HEM B C2B   1 
HETATM 12652 C  C3B   . HEM H 2 .   ? 162.417 193.514 111.214 1.00 73.42  ?  902 HEM B C3B   1 
HETATM 12653 C  C4B   . HEM H 2 .   ? 162.314 194.121 109.904 1.00 74.81  ?  902 HEM B C4B   1 
HETATM 12654 C  CMB   . HEM H 2 .   ? 162.898 194.396 113.624 1.00 78.56  ?  902 HEM B CMB   1 
HETATM 12655 C  CAB   . HEM H 2 .   ? 162.228 191.990 111.431 1.00 77.61  ?  902 HEM B CAB   1 
HETATM 12656 C  CBB   . HEM H 2 .   ? 162.326 191.368 112.610 1.00 80.14  ?  902 HEM B CBB   1 
HETATM 12657 C  C1C   . HEM H 2 .   ? 162.168 193.972 107.461 1.00 75.88  ?  902 HEM B C1C   1 
HETATM 12658 C  C2C   . HEM H 2 .   ? 162.142 193.212 106.229 1.00 73.21  ?  902 HEM B C2C   1 
HETATM 12659 C  C3C   . HEM H 2 .   ? 162.293 194.076 105.208 1.00 73.85  ?  902 HEM B C3C   1 
HETATM 12660 C  C4C   . HEM H 2 .   ? 162.416 195.405 105.775 1.00 77.47  ?  902 HEM B C4C   1 
HETATM 12661 C  CMC   . HEM H 2 .   ? 161.969 191.676 106.188 1.00 76.94  ?  902 HEM B CMC   1 
HETATM 12662 C  CAC   . HEM H 2 .   ? 162.338 193.816 103.679 1.00 76.00  ?  902 HEM B CAC   1 
HETATM 12663 C  CBC   . HEM H 2 .   ? 162.203 192.618 103.100 1.00 77.34  ?  902 HEM B CBC   1 
HETATM 12664 C  C1D   . HEM H 2 .   ? 163.032 197.773 105.588 1.00 73.74  ?  902 HEM B C1D   1 
HETATM 12665 C  C2D   . HEM H 2 .   ? 163.316 198.980 104.842 1.00 73.30  ?  902 HEM B C2D   1 
HETATM 12666 C  C3D   . HEM H 2 .   ? 163.730 199.914 105.701 1.00 75.08  ?  902 HEM B C3D   1 
HETATM 12667 C  C4D   . HEM H 2 .   ? 163.720 199.339 107.032 1.00 72.15  ?  902 HEM B C4D   1 
HETATM 12668 C  CMD   . HEM H 2 .   ? 163.171 199.153 103.315 1.00 74.35  ?  902 HEM B CMD   1 
HETATM 12669 C  CAD   . HEM H 2 .   ? 164.137 201.356 105.327 1.00 79.85  ?  902 HEM B CAD   1 
HETATM 12670 C  CBD   . HEM H 2 .   ? 165.622 201.560 105.610 1.00 80.79  ?  902 HEM B CBD   1 
HETATM 12671 C  CGD   . HEM H 2 .   ? 166.065 202.884 105.050 1.00 79.87  ?  902 HEM B CGD   1 
HETATM 12672 O  O1D   . HEM H 2 .   ? 167.226 203.289 105.312 1.00 77.35  ?  902 HEM B O1D   1 
HETATM 12673 O  O2D   . HEM H 2 .   ? 165.255 203.537 104.342 1.00 79.62  ?  902 HEM B O2D   1 
HETATM 12674 N  NA    . HEM H 2 .   ? 163.370 198.245 109.808 1.00 79.43  ?  902 HEM B NA    1 
HETATM 12675 N  NB    . HEM H 2 .   ? 162.528 195.478 110.029 1.00 78.99  ?  902 HEM B NB    1 
HETATM 12676 N  NC    . HEM H 2 .   ? 162.336 195.304 107.148 1.00 77.76  ?  902 HEM B NC    1 
HETATM 12677 N  ND    . HEM H 2 .   ? 163.289 198.030 106.921 1.00 70.66  ?  902 HEM B ND    1 
HETATM 12678 FE FE    . HEM H 2 .   ? 162.808 196.793 108.476 1.00 84.72  ?  902 HEM B FE    1 
HETATM 12679 MG MG    . MG  I 4 .   ? 183.952 208.095 238.128 1.00 18.68  ?  903 MG  B MG    1 
HETATM 12680 MG MG    . MG  J 4 .   ? 179.602 204.672 236.160 1.00 59.34  ?  904 MG  B MG    1 
# 
