data_9AU8
# 
_entry.id   9AU8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9AU8         pdb_00009au8 10.2210/pdb9au8/pdb 
WWPDB D_1000281991 ?            ?                   
EMDB  EMD-43874    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'EM metadata'     1 0 2025-03-05 ? 
3 'Half map'        1 0 2025-03-05 1 
4 'Half map'        1 0 2025-03-05 2 
5 Image             1 0 2025-03-05 ? 
6 'Primary map'     1 0 2025-03-05 ? 
7 'Structure model' 1 1 2025-05-28 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Half map'        repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 Image             repository 'Initial release' ? ? 
6 6 'Primary map'     repository 'Initial release' ? ? 
# 
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 7 'Structure model' 'Data collection'     
2 7 '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 7 'Structure model' citation        
2 7 'Structure model' citation_author 
3 7 '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  7 'Structure model' '_citation.country'                 
2  7 'Structure model' '_citation.journal_abbrev'          
3  7 'Structure model' '_citation.journal_id_CSD'          
4  7 'Structure model' '_citation.journal_id_ISSN'         
5  7 'Structure model' '_citation.journal_volume'          
6  7 'Structure model' '_citation.page_first'              
7  7 'Structure model' '_citation.page_last'               
8  7 'Structure model' '_citation.pdbx_database_id_DOI'    
9  7 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 7 'Structure model' '_citation.title'                   
11 7 'Structure model' '_citation.year'                    
12 7 'Structure model' '_citation_author.identifier_ORCID' 
13 7 '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                        9AU8 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-28 
_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 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        
'Ternary complex of human DNA polymerase theta polymerase domain with a mismatched T:T base pair' 
_pdbx_database_related.db_id          EMD-43874 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              yg60@rice.edu 
_pdbx_contact_author.name_first         Yang 
_pdbx_contact_author.name_last          Gao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4037-0431 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, C.'  1 ? 
'Gao, Y.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2063 
_citation.page_last                 2063 
_citation.title                     'Structural basis of error-prone DNA synthesis by DNA polymerase theta.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57269-9 
_citation.pdbx_database_id_PubMed   40021647 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, C.'        1 ?                   
primary 'Maksoud, L.M.' 2 ?                   
primary 'Gao, Y.'       3 0000-0002-4037-0431 
# 
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 'DNA polymerase theta'                       89585.555 1 2.7.7.7 ? ? ? 
2 polymer     syn 
;DNA (5'-D(P*CP*GP*TP*AP*GP*(DOC))-3')
;
6149.978  1 ?       ? ? ? 
3 polymer     syn 
;DNA (5'-D(P*AP*GP*TP*GP*CP*TP*AP*CP*G)-3')
;
8904.736  1 ?       ? ? ? 
4 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                  482.168   1 ?       ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                              24.305    1 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DNA polymerase eta' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)'        no no  
;GFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIG
SRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSC
LRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQS
LGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLD
AIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALH
PLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQ
AVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQV
LNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETV
KNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQS
DQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
;
;GFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIG
SRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSC
LRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQS
LGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLD
AIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALH
PLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQ
AVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQV
LNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETV
KNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQS
DQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
;
A ? 
2 polydeoxyribonucleotide no yes 
;(DT)(DG)(DC)(DT)(DG)(DT)(DG)(DA)(DG)(DG)(DC)(DA)(DT)(DC)(DC)(DG)(DT)(DA)(DG)
(DOC)
;
TGCTGTGAGGCATCCGTAGC C ? 
3 polydeoxyribonucleotide no no  
;(DG)(DC)(DA)(DG)(DT)(DC)(DA)(DG)(DT)(DG)(DC)(DT)(DA)(DC)(DG)(DG)(DA)(DT)(DG)(DC)
(DC)(DT)(DC)(DA)(DC)(DA)(DG)(DC)(DA)
;
GCAGTCAGTGCTACGGATGCCTCACAGCA D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 "THYMIDINE-5'-TRIPHOSPHATE" TTP 
5 '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   PHE n 
1 3   LYS n 
1 4   ASP n 
1 5   ASN n 
1 6   SER n 
1 7   PRO n 
1 8   ILE n 
1 9   SER n 
1 10  ASP n 
1 11  THR n 
1 12  SER n 
1 13  PHE n 
1 14  SER n 
1 15  LEU n 
1 16  GLN n 
1 17  LEU n 
1 18  SER n 
1 19  GLN n 
1 20  ASP n 
1 21  GLY n 
1 22  LEU n 
1 23  GLN n 
1 24  LEU n 
1 25  THR n 
1 26  PRO n 
1 27  ALA n 
1 28  SER n 
1 29  SER n 
1 30  SER n 
1 31  SER n 
1 32  GLU n 
1 33  SER n 
1 34  LEU n 
1 35  SER n 
1 36  ILE n 
1 37  ILE n 
1 38  ASP n 
1 39  VAL n 
1 40  ALA n 
1 41  SER n 
1 42  ASP n 
1 43  GLN n 
1 44  ASN n 
1 45  LEU n 
1 46  PHE n 
1 47  GLN n 
1 48  THR n 
1 49  PHE n 
1 50  ILE n 
1 51  LYS n 
1 52  GLU n 
1 53  TRP n 
1 54  ARG n 
1 55  CYS n 
1 56  LYS n 
1 57  LYS n 
1 58  ARG n 
1 59  PHE n 
1 60  SER n 
1 61  ILE n 
1 62  SER n 
1 63  LEU n 
1 64  ALA n 
1 65  CYS n 
1 66  GLU n 
1 67  LYS n 
1 68  ILE n 
1 69  ARG n 
1 70  SER n 
1 71  LEU n 
1 72  THR n 
1 73  SER n 
1 74  SER n 
1 75  LYS n 
1 76  THR n 
1 77  ALA n 
1 78  THR n 
1 79  ILE n 
1 80  GLY n 
1 81  SER n 
1 82  ARG n 
1 83  PHE n 
1 84  LYS n 
1 85  GLN n 
1 86  ALA n 
1 87  SER n 
1 88  SER n 
1 89  PRO n 
1 90  GLN n 
1 91  GLU n 
1 92  ILE n 
1 93  PRO n 
1 94  ILE n 
1 95  ARG n 
1 96  ASP n 
1 97  ASP n 
1 98  GLY n 
1 99  PHE n 
1 100 PRO n 
1 101 ILE n 
1 102 LYS n 
1 103 GLY n 
1 104 CYS n 
1 105 ASP n 
1 106 ASP n 
1 107 THR n 
1 108 LEU n 
1 109 VAL n 
1 110 VAL n 
1 111 GLY n 
1 112 LEU n 
1 113 ALA n 
1 114 VAL n 
1 115 CYS n 
1 116 TRP n 
1 117 GLY n 
1 118 GLY n 
1 119 ARG n 
1 120 ASP n 
1 121 ALA n 
1 122 TYR n 
1 123 TYR n 
1 124 PHE n 
1 125 SER n 
1 126 LEU n 
1 127 GLN n 
1 128 LYS n 
1 129 GLU n 
1 130 GLN n 
1 131 LYS n 
1 132 HIS n 
1 133 SER n 
1 134 GLU n 
1 135 ILE n 
1 136 SER n 
1 137 ALA n 
1 138 SER n 
1 139 LEU n 
1 140 VAL n 
1 141 PRO n 
1 142 PRO n 
1 143 SER n 
1 144 LEU n 
1 145 ASP n 
1 146 PRO n 
1 147 SER n 
1 148 LEU n 
1 149 THR n 
1 150 LEU n 
1 151 LYS n 
1 152 ASP n 
1 153 ARG n 
1 154 MET n 
1 155 TRP n 
1 156 TYR n 
1 157 LEU n 
1 158 GLN n 
1 159 SER n 
1 160 CYS n 
1 161 LEU n 
1 162 ARG n 
1 163 LYS n 
1 164 GLU n 
1 165 SER n 
1 166 ASP n 
1 167 LYS n 
1 168 GLU n 
1 169 CYS n 
1 170 SER n 
1 171 VAL n 
1 172 VAL n 
1 173 ILE n 
1 174 TYR n 
1 175 ASP n 
1 176 PHE n 
1 177 ILE n 
1 178 GLN n 
1 179 SER n 
1 180 TYR n 
1 181 LYS n 
1 182 ILE n 
1 183 LEU n 
1 184 LEU n 
1 185 LEU n 
1 186 SER n 
1 187 CYS n 
1 188 GLY n 
1 189 ILE n 
1 190 SER n 
1 191 LEU n 
1 192 GLU n 
1 193 GLN n 
1 194 SER n 
1 195 TYR n 
1 196 GLU n 
1 197 ASP n 
1 198 PRO n 
1 199 LYS n 
1 200 VAL n 
1 201 ALA n 
1 202 CYS n 
1 203 TRP n 
1 204 LEU n 
1 205 LEU n 
1 206 ASP n 
1 207 PRO n 
1 208 ASP n 
1 209 SER n 
1 210 GLN n 
1 211 GLU n 
1 212 PRO n 
1 213 THR n 
1 214 LEU n 
1 215 HIS n 
1 216 SER n 
1 217 ILE n 
1 218 VAL n 
1 219 THR n 
1 220 SER n 
1 221 PHE n 
1 222 LEU n 
1 223 PRO n 
1 224 HIS n 
1 225 GLU n 
1 226 LEU n 
1 227 PRO n 
1 228 LEU n 
1 229 LEU n 
1 230 GLU n 
1 231 GLY n 
1 232 MET n 
1 233 GLU n 
1 234 THR n 
1 235 SER n 
1 236 GLN n 
1 237 GLY n 
1 238 ILE n 
1 239 GLN n 
1 240 SER n 
1 241 LEU n 
1 242 GLY n 
1 243 LEU n 
1 244 ASN n 
1 245 ALA n 
1 246 GLY n 
1 247 SER n 
1 248 GLU n 
1 249 HIS n 
1 250 SER n 
1 251 GLY n 
1 252 ARG n 
1 253 TYR n 
1 254 ARG n 
1 255 ALA n 
1 256 SER n 
1 257 VAL n 
1 258 GLU n 
1 259 SER n 
1 260 ILE n 
1 261 LEU n 
1 262 ILE n 
1 263 PHE n 
1 264 ASN n 
1 265 SER n 
1 266 MET n 
1 267 ASN n 
1 268 GLN n 
1 269 LEU n 
1 270 ASN n 
1 271 SER n 
1 272 LEU n 
1 273 LEU n 
1 274 GLN n 
1 275 LYS n 
1 276 GLU n 
1 277 ASN n 
1 278 LEU n 
1 279 GLN n 
1 280 ASP n 
1 281 VAL n 
1 282 PHE n 
1 283 ARG n 
1 284 LYS n 
1 285 VAL n 
1 286 GLU n 
1 287 MET n 
1 288 PRO n 
1 289 SER n 
1 290 GLN n 
1 291 TYR n 
1 292 CYS n 
1 293 LEU n 
1 294 ALA n 
1 295 LEU n 
1 296 LEU n 
1 297 GLU n 
1 298 LEU n 
1 299 ASN n 
1 300 GLY n 
1 301 ILE n 
1 302 GLY n 
1 303 PHE n 
1 304 SER n 
1 305 THR n 
1 306 ALA n 
1 307 GLU n 
1 308 CYS n 
1 309 GLU n 
1 310 SER n 
1 311 GLN n 
1 312 LYS n 
1 313 HIS n 
1 314 ILE n 
1 315 MET n 
1 316 GLN n 
1 317 ALA n 
1 318 LYS n 
1 319 LEU n 
1 320 ASP n 
1 321 ALA n 
1 322 ILE n 
1 323 GLU n 
1 324 THR n 
1 325 GLN n 
1 326 ALA n 
1 327 TYR n 
1 328 GLN n 
1 329 LEU n 
1 330 ALA n 
1 331 GLY n 
1 332 HIS n 
1 333 SER n 
1 334 PHE n 
1 335 SER n 
1 336 PHE n 
1 337 THR n 
1 338 SER n 
1 339 SER n 
1 340 ASP n 
1 341 ASP n 
1 342 ILE n 
1 343 ALA n 
1 344 GLU n 
1 345 VAL n 
1 346 LEU n 
1 347 PHE n 
1 348 LEU n 
1 349 GLU n 
1 350 LEU n 
1 351 LYS n 
1 352 LEU n 
1 353 PRO n 
1 354 PRO n 
1 355 ASN n 
1 356 ARG n 
1 357 GLU n 
1 358 MET n 
1 359 LYS n 
1 360 ASN n 
1 361 GLN n 
1 362 GLY n 
1 363 SER n 
1 364 LYS n 
1 365 LYS n 
1 366 THR n 
1 367 LEU n 
1 368 GLY n 
1 369 SER n 
1 370 THR n 
1 371 ARG n 
1 372 ARG n 
1 373 GLY n 
1 374 ILE n 
1 375 ASP n 
1 376 ASN n 
1 377 GLY n 
1 378 ARG n 
1 379 LYS n 
1 380 LEU n 
1 381 ARG n 
1 382 LEU n 
1 383 GLY n 
1 384 ARG n 
1 385 GLN n 
1 386 PHE n 
1 387 SER n 
1 388 THR n 
1 389 SER n 
1 390 LYS n 
1 391 ASP n 
1 392 VAL n 
1 393 LEU n 
1 394 ASN n 
1 395 LYS n 
1 396 LEU n 
1 397 LYS n 
1 398 ALA n 
1 399 LEU n 
1 400 HIS n 
1 401 PRO n 
1 402 LEU n 
1 403 PRO n 
1 404 GLY n 
1 405 LEU n 
1 406 ILE n 
1 407 LEU n 
1 408 GLU n 
1 409 TRP n 
1 410 ARG n 
1 411 ARG n 
1 412 ILE n 
1 413 THR n 
1 414 ASN n 
1 415 ALA n 
1 416 ILE n 
1 417 THR n 
1 418 LYS n 
1 419 VAL n 
1 420 VAL n 
1 421 PHE n 
1 422 PRO n 
1 423 LEU n 
1 424 GLN n 
1 425 ARG n 
1 426 GLU n 
1 427 LYS n 
1 428 CYS n 
1 429 LEU n 
1 430 ASN n 
1 431 PRO n 
1 432 PHE n 
1 433 LEU n 
1 434 GLY n 
1 435 MET n 
1 436 GLU n 
1 437 ARG n 
1 438 ILE n 
1 439 TYR n 
1 440 PRO n 
1 441 VAL n 
1 442 SER n 
1 443 GLN n 
1 444 SER n 
1 445 HIS n 
1 446 THR n 
1 447 ALA n 
1 448 THR n 
1 449 GLY n 
1 450 ARG n 
1 451 ILE n 
1 452 THR n 
1 453 PHE n 
1 454 THR n 
1 455 GLU n 
1 456 PRO n 
1 457 ASN n 
1 458 ILE n 
1 459 GLN n 
1 460 ASN n 
1 461 VAL n 
1 462 PRO n 
1 463 ARG n 
1 464 ASP n 
1 465 PHE n 
1 466 GLU n 
1 467 ILE n 
1 468 LYS n 
1 469 MET n 
1 470 PRO n 
1 471 THR n 
1 472 LEU n 
1 473 VAL n 
1 474 GLY n 
1 475 GLU n 
1 476 SER n 
1 477 PRO n 
1 478 PRO n 
1 479 SER n 
1 480 GLN n 
1 481 ALA n 
1 482 VAL n 
1 483 GLY n 
1 484 LYS n 
1 485 GLY n 
1 486 LEU n 
1 487 LEU n 
1 488 PRO n 
1 489 MET n 
1 490 GLY n 
1 491 ARG n 
1 492 GLY n 
1 493 LYS n 
1 494 TYR n 
1 495 LYS n 
1 496 LYS n 
1 497 GLY n 
1 498 PHE n 
1 499 SER n 
1 500 VAL n 
1 501 ASN n 
1 502 PRO n 
1 503 ARG n 
1 504 CYS n 
1 505 GLN n 
1 506 ALA n 
1 507 GLN n 
1 508 MET n 
1 509 GLU n 
1 510 GLU n 
1 511 ARG n 
1 512 ALA n 
1 513 ALA n 
1 514 ASP n 
1 515 ARG n 
1 516 GLY n 
1 517 MET n 
1 518 PRO n 
1 519 PHE n 
1 520 SER n 
1 521 ILE n 
1 522 SER n 
1 523 MET n 
1 524 ARG n 
1 525 HIS n 
1 526 ALA n 
1 527 PHE n 
1 528 VAL n 
1 529 PRO n 
1 530 PHE n 
1 531 PRO n 
1 532 GLY n 
1 533 GLY n 
1 534 SER n 
1 535 ILE n 
1 536 LEU n 
1 537 ALA n 
1 538 ALA n 
1 539 ASP n 
1 540 TYR n 
1 541 SER n 
1 542 GLN n 
1 543 LEU n 
1 544 GLU n 
1 545 LEU n 
1 546 ARG n 
1 547 ILE n 
1 548 LEU n 
1 549 ALA n 
1 550 HIS n 
1 551 LEU n 
1 552 SER n 
1 553 HIS n 
1 554 ASP n 
1 555 ARG n 
1 556 ARG n 
1 557 LEU n 
1 558 ILE n 
1 559 GLN n 
1 560 VAL n 
1 561 LEU n 
1 562 ASN n 
1 563 THR n 
1 564 GLY n 
1 565 ALA n 
1 566 ASP n 
1 567 VAL n 
1 568 PHE n 
1 569 ARG n 
1 570 SER n 
1 571 ILE n 
1 572 ALA n 
1 573 ALA n 
1 574 GLU n 
1 575 TRP n 
1 576 LYS n 
1 577 MET n 
1 578 ILE n 
1 579 GLU n 
1 580 PRO n 
1 581 GLU n 
1 582 SER n 
1 583 VAL n 
1 584 GLY n 
1 585 ASP n 
1 586 ASP n 
1 587 LEU n 
1 588 ARG n 
1 589 GLN n 
1 590 GLN n 
1 591 ALA n 
1 592 LYS n 
1 593 GLN n 
1 594 ILE n 
1 595 CYS n 
1 596 TYR n 
1 597 GLY n 
1 598 ILE n 
1 599 ILE n 
1 600 TYR n 
1 601 GLY n 
1 602 MET n 
1 603 GLY n 
1 604 ALA n 
1 605 LYS n 
1 606 SER n 
1 607 LEU n 
1 608 GLY n 
1 609 GLU n 
1 610 GLN n 
1 611 MET n 
1 612 GLY n 
1 613 ILE n 
1 614 LYS n 
1 615 GLU n 
1 616 ASN n 
1 617 ASP n 
1 618 ALA n 
1 619 ALA n 
1 620 CYS n 
1 621 TYR n 
1 622 ILE n 
1 623 ASP n 
1 624 SER n 
1 625 PHE n 
1 626 LYS n 
1 627 SER n 
1 628 ARG n 
1 629 TYR n 
1 630 THR n 
1 631 GLY n 
1 632 ILE n 
1 633 ASN n 
1 634 GLN n 
1 635 PHE n 
1 636 MET n 
1 637 THR n 
1 638 GLU n 
1 639 THR n 
1 640 VAL n 
1 641 LYS n 
1 642 ASN n 
1 643 CYS n 
1 644 LYS n 
1 645 ARG n 
1 646 ASP n 
1 647 GLY n 
1 648 PHE n 
1 649 VAL n 
1 650 GLN n 
1 651 THR n 
1 652 ILE n 
1 653 LEU n 
1 654 GLY n 
1 655 ARG n 
1 656 ARG n 
1 657 ARG n 
1 658 TYR n 
1 659 LEU n 
1 660 PRO n 
1 661 GLY n 
1 662 ILE n 
1 663 LYS n 
1 664 ASP n 
1 665 ASN n 
1 666 ASN n 
1 667 PRO n 
1 668 TYR n 
1 669 ARG n 
1 670 LYS n 
1 671 ALA n 
1 672 HIS n 
1 673 ALA n 
1 674 GLU n 
1 675 ARG n 
1 676 GLN n 
1 677 ALA n 
1 678 ILE n 
1 679 ASN n 
1 680 THR n 
1 681 ILE n 
1 682 VAL n 
1 683 GLN n 
1 684 GLY n 
1 685 SER n 
1 686 ALA n 
1 687 ALA n 
1 688 ASP n 
1 689 ILE n 
1 690 VAL n 
1 691 LYS n 
1 692 ILE n 
1 693 ALA n 
1 694 THR n 
1 695 VAL n 
1 696 ASN n 
1 697 ILE n 
1 698 GLN n 
1 699 LYS n 
1 700 GLN n 
1 701 LEU n 
1 702 GLU n 
1 703 THR n 
1 704 PHE n 
1 705 HIS n 
1 706 SER n 
1 707 THR n 
1 708 PHE n 
1 709 LYS n 
1 710 SER n 
1 711 HIS n 
1 712 GLY n 
1 713 HIS n 
1 714 ARG n 
1 715 GLU n 
1 716 GLY n 
1 717 MET n 
1 718 LEU n 
1 719 GLN n 
1 720 SER n 
1 721 ASP n 
1 722 GLN n 
1 723 THR n 
1 724 GLY n 
1 725 LEU n 
1 726 SER n 
1 727 ARG n 
1 728 LYS n 
1 729 ARG n 
1 730 LYS n 
1 731 LEU n 
1 732 GLN n 
1 733 GLY n 
1 734 MET n 
1 735 PHE n 
1 736 CYS n 
1 737 PRO n 
1 738 ILE n 
1 739 ARG n 
1 740 GLY n 
1 741 GLY n 
1 742 PHE n 
1 743 PHE n 
1 744 ILE n 
1 745 LEU n 
1 746 GLN n 
1 747 LEU n 
1 748 HIS n 
1 749 ASP n 
1 750 GLU n 
1 751 LEU n 
1 752 LEU n 
1 753 TYR n 
1 754 GLU n 
1 755 VAL n 
1 756 ALA n 
1 757 GLU n 
1 758 GLU n 
1 759 ASP n 
1 760 VAL n 
1 761 VAL n 
1 762 GLN n 
1 763 VAL n 
1 764 ALA n 
1 765 GLN n 
1 766 ILE n 
1 767 VAL n 
1 768 LYS n 
1 769 ASN n 
1 770 GLU n 
1 771 MET n 
1 772 GLU n 
1 773 SER n 
1 774 ALA n 
1 775 VAL n 
1 776 LYS n 
1 777 LEU n 
1 778 SER n 
1 779 VAL n 
1 780 LYS n 
1 781 LEU n 
1 782 LYS n 
1 783 VAL n 
1 784 LYS n 
1 785 VAL n 
1 786 LYS n 
1 787 ILE n 
1 788 GLY n 
1 789 ALA n 
1 790 SER n 
1 791 TRP n 
1 792 GLY n 
1 793 GLU n 
1 794 LEU n 
1 795 LYS n 
1 796 ASP n 
1 797 PHE n 
1 798 ASP n 
1 799 VAL n 
2 1   DT  n 
2 2   DG  n 
2 3   DC  n 
2 4   DT  n 
2 5   DG  n 
2 6   DT  n 
2 7   DG  n 
2 8   DA  n 
2 9   DG  n 
2 10  DG  n 
2 11  DC  n 
2 12  DA  n 
2 13  DT  n 
2 14  DC  n 
2 15  DC  n 
2 16  DG  n 
2 17  DT  n 
2 18  DA  n 
2 19  DG  n 
2 20  DOC n 
3 1   DG  n 
3 2   DC  n 
3 3   DA  n 
3 4   DG  n 
3 5   DT  n 
3 6   DC  n 
3 7   DA  n 
3 8   DG  n 
3 9   DT  n 
3 10  DG  n 
3 11  DC  n 
3 12  DT  n 
3 13  DA  n 
3 14  DC  n 
3 15  DG  n 
3 16  DG  n 
3 17  DA  n 
3 18  DT  n 
3 19  DG  n 
3 20  DC  n 
3 21  DC  n 
3 22  DT  n 
3 23  DC  n 
3 24  DA  n 
3 25  DC  n 
3 26  DA  n 
3 27  DG  n 
3 28  DC  n 
3 29  DA  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                   799 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'POLQ, POLH' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 20 'Homo sapiens' ? 9606 ? 
3 1 sample 1 29 'Homo sapiens' ? 9606 ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                 ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                 ? 'C3 H7 N O2 S'      121.158 
DA  'DNA linking'       y "2'-DEOXYADENOSINE-5'-MONOPHOSPHATE"     ? 'C10 H14 N5 O6 P'   331.222 
DC  'DNA linking'       y "2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE"      ? 'C9 H14 N3 O7 P'    307.197 
DG  'DNA linking'       y "2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE"     ? 'C10 H14 N5 O7 P'   347.221 
DOC 'DNA linking'       n "2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE" ? 'C9 H14 N3 O6 P'    291.198 
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE"             ? 'C10 H15 N2 O8 P'   322.208 
GLN 'L-peptide linking' y GLUTAMINE                                ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                  ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                               ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                  ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                   ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                               ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                          ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                            ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                  ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                   ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                               ? 'C11 H12 N2 O2'     204.225 
TTP non-polymer         . "THYMIDINE-5'-TRIPHOSPHATE"              ? 'C10 H17 N2 O14 P3' 482.168 
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   1792 ?    ?   ?   A . n 
A 1 2   PHE 2   1793 ?    ?   ?   A . n 
A 1 3   LYS 3   1794 ?    ?   ?   A . n 
A 1 4   ASP 4   1795 ?    ?   ?   A . n 
A 1 5   ASN 5   1796 ?    ?   ?   A . n 
A 1 6   SER 6   1797 ?    ?   ?   A . n 
A 1 7   PRO 7   1798 ?    ?   ?   A . n 
A 1 8   ILE 8   1799 ?    ?   ?   A . n 
A 1 9   SER 9   1800 ?    ?   ?   A . n 
A 1 10  ASP 10  1801 ?    ?   ?   A . n 
A 1 11  THR 11  1802 ?    ?   ?   A . n 
A 1 12  SER 12  1803 ?    ?   ?   A . n 
A 1 13  PHE 13  1804 ?    ?   ?   A . n 
A 1 14  SER 14  1805 ?    ?   ?   A . n 
A 1 15  LEU 15  1806 ?    ?   ?   A . n 
A 1 16  GLN 16  1807 ?    ?   ?   A . n 
A 1 17  LEU 17  1808 ?    ?   ?   A . n 
A 1 18  SER 18  1809 ?    ?   ?   A . n 
A 1 19  GLN 19  1810 ?    ?   ?   A . n 
A 1 20  ASP 20  1811 ?    ?   ?   A . n 
A 1 21  GLY 21  1812 ?    ?   ?   A . n 
A 1 22  LEU 22  1813 ?    ?   ?   A . n 
A 1 23  GLN 23  1814 ?    ?   ?   A . n 
A 1 24  LEU 24  1815 ?    ?   ?   A . n 
A 1 25  THR 25  1816 ?    ?   ?   A . n 
A 1 26  PRO 26  1817 ?    ?   ?   A . n 
A 1 27  ALA 27  1818 ?    ?   ?   A . n 
A 1 28  SER 28  1819 ?    ?   ?   A . n 
A 1 29  SER 29  1820 ?    ?   ?   A . n 
A 1 30  SER 30  1821 ?    ?   ?   A . n 
A 1 31  SER 31  1822 ?    ?   ?   A . n 
A 1 32  GLU 32  1823 ?    ?   ?   A . n 
A 1 33  SER 33  1824 1824 SER SER A . n 
A 1 34  LEU 34  1825 1825 LEU LEU A . n 
A 1 35  SER 35  1826 1826 SER SER A . n 
A 1 36  ILE 36  1827 1827 ILE ILE A . n 
A 1 37  ILE 37  1828 1828 ILE ILE A . n 
A 1 38  ASP 38  1829 1829 ASP ASP A . n 
A 1 39  VAL 39  1830 1830 VAL VAL A . n 
A 1 40  ALA 40  1831 1831 ALA ALA A . n 
A 1 41  SER 41  1832 1832 SER SER A . n 
A 1 42  ASP 42  1833 1833 ASP ASP A . n 
A 1 43  GLN 43  1834 1834 GLN GLN A . n 
A 1 44  ASN 44  1835 1835 ASN ASN A . n 
A 1 45  LEU 45  1836 1836 LEU LEU A . n 
A 1 46  PHE 46  1837 1837 PHE PHE A . n 
A 1 47  GLN 47  1838 1838 GLN GLN A . n 
A 1 48  THR 48  1839 1839 THR THR A . n 
A 1 49  PHE 49  1840 1840 PHE PHE A . n 
A 1 50  ILE 50  1841 1841 ILE ILE A . n 
A 1 51  LYS 51  1842 1842 LYS LYS A . n 
A 1 52  GLU 52  1843 1843 GLU GLU A . n 
A 1 53  TRP 53  1844 1844 TRP TRP A . n 
A 1 54  ARG 54  1845 1845 ARG ARG A . n 
A 1 55  CYS 55  1846 1846 CYS CYS A . n 
A 1 56  LYS 56  1847 1847 LYS LYS A . n 
A 1 57  LYS 57  1848 1848 LYS LYS A . n 
A 1 58  ARG 58  1849 1849 ARG ARG A . n 
A 1 59  PHE 59  1850 1850 PHE PHE A . n 
A 1 60  SER 60  1851 1851 SER SER A . n 
A 1 61  ILE 61  1852 1852 ILE ILE A . n 
A 1 62  SER 62  1853 1853 SER SER A . n 
A 1 63  LEU 63  1854 1854 LEU LEU A . n 
A 1 64  ALA 64  1855 1855 ALA ALA A . n 
A 1 65  CYS 65  1856 1856 CYS CYS A . n 
A 1 66  GLU 66  1857 1857 GLU GLU A . n 
A 1 67  LYS 67  1858 1858 LYS LYS A . n 
A 1 68  ILE 68  1859 1859 ILE ILE A . n 
A 1 69  ARG 69  1860 1860 ARG ARG A . n 
A 1 70  SER 70  1861 1861 SER SER A . n 
A 1 71  LEU 71  1862 ?    ?   ?   A . n 
A 1 72  THR 72  1863 ?    ?   ?   A . n 
A 1 73  SER 73  1864 ?    ?   ?   A . n 
A 1 74  SER 74  1865 ?    ?   ?   A . n 
A 1 75  LYS 75  1866 ?    ?   ?   A . n 
A 1 76  THR 76  1867 ?    ?   ?   A . n 
A 1 77  ALA 77  1868 ?    ?   ?   A . n 
A 1 78  THR 78  1869 ?    ?   ?   A . n 
A 1 79  ILE 79  1870 ?    ?   ?   A . n 
A 1 80  GLY 80  1871 ?    ?   ?   A . n 
A 1 81  SER 81  1872 ?    ?   ?   A . n 
A 1 82  ARG 82  1873 ?    ?   ?   A . n 
A 1 83  PHE 83  1874 ?    ?   ?   A . n 
A 1 84  LYS 84  1875 ?    ?   ?   A . n 
A 1 85  GLN 85  1876 ?    ?   ?   A . n 
A 1 86  ALA 86  1877 ?    ?   ?   A . n 
A 1 87  SER 87  1878 ?    ?   ?   A . n 
A 1 88  SER 88  1879 ?    ?   ?   A . n 
A 1 89  PRO 89  1880 ?    ?   ?   A . n 
A 1 90  GLN 90  1881 ?    ?   ?   A . n 
A 1 91  GLU 91  1882 ?    ?   ?   A . n 
A 1 92  ILE 92  1883 ?    ?   ?   A . n 
A 1 93  PRO 93  1884 ?    ?   ?   A . n 
A 1 94  ILE 94  1885 1885 ILE ILE A . n 
A 1 95  ARG 95  1886 1886 ARG ARG A . n 
A 1 96  ASP 96  1887 1887 ASP ASP A . n 
A 1 97  ASP 97  1888 1888 ASP ASP A . n 
A 1 98  GLY 98  1889 1889 GLY GLY A . n 
A 1 99  PHE 99  1890 1890 PHE PHE A . n 
A 1 100 PRO 100 1891 1891 PRO PRO A . n 
A 1 101 ILE 101 1892 1892 ILE ILE A . n 
A 1 102 LYS 102 1893 1893 LYS LYS A . n 
A 1 103 GLY 103 1894 1894 GLY GLY A . n 
A 1 104 CYS 104 1895 1895 CYS CYS A . n 
A 1 105 ASP 105 1896 1896 ASP ASP A . n 
A 1 106 ASP 106 1897 1897 ASP ASP A . n 
A 1 107 THR 107 1898 1898 THR THR A . n 
A 1 108 LEU 108 1899 1899 LEU LEU A . n 
A 1 109 VAL 109 1900 1900 VAL VAL A . n 
A 1 110 VAL 110 1901 1901 VAL VAL A . n 
A 1 111 GLY 111 1902 1902 GLY GLY A . n 
A 1 112 LEU 112 1903 1903 LEU LEU A . n 
A 1 113 ALA 113 1904 1904 ALA ALA A . n 
A 1 114 VAL 114 1905 1905 VAL VAL A . n 
A 1 115 CYS 115 1906 1906 CYS CYS A . n 
A 1 116 TRP 116 1907 1907 TRP TRP A . n 
A 1 117 GLY 117 1908 1908 GLY GLY A . n 
A 1 118 GLY 118 1909 1909 GLY GLY A . n 
A 1 119 ARG 119 1910 1910 ARG ARG A . n 
A 1 120 ASP 120 1911 1911 ASP ASP A . n 
A 1 121 ALA 121 1912 1912 ALA ALA A . n 
A 1 122 TYR 122 1913 1913 TYR TYR A . n 
A 1 123 TYR 123 1914 1914 TYR TYR A . n 
A 1 124 PHE 124 1915 1915 PHE PHE A . n 
A 1 125 SER 125 1916 1916 SER SER A . n 
A 1 126 LEU 126 1917 1917 LEU LEU A . n 
A 1 127 GLN 127 1918 1918 GLN GLN A . n 
A 1 128 LYS 128 1919 1919 LYS LYS A . n 
A 1 129 GLU 129 1920 1920 GLU GLU A . n 
A 1 130 GLN 130 1921 ?    ?   ?   A . n 
A 1 131 LYS 131 1922 ?    ?   ?   A . n 
A 1 132 HIS 132 1923 ?    ?   ?   A . n 
A 1 133 SER 133 1924 ?    ?   ?   A . n 
A 1 134 GLU 134 1925 ?    ?   ?   A . n 
A 1 135 ILE 135 1926 ?    ?   ?   A . n 
A 1 136 SER 136 1927 ?    ?   ?   A . n 
A 1 137 ALA 137 1928 ?    ?   ?   A . n 
A 1 138 SER 138 1929 ?    ?   ?   A . n 
A 1 139 LEU 139 1930 ?    ?   ?   A . n 
A 1 140 VAL 140 1931 ?    ?   ?   A . n 
A 1 141 PRO 141 1932 ?    ?   ?   A . n 
A 1 142 PRO 142 1933 ?    ?   ?   A . n 
A 1 143 SER 143 1934 ?    ?   ?   A . n 
A 1 144 LEU 144 1935 ?    ?   ?   A . n 
A 1 145 ASP 145 1936 1936 ASP ASP A . n 
A 1 146 PRO 146 1937 1937 PRO PRO A . n 
A 1 147 SER 147 1938 1938 SER SER A . n 
A 1 148 LEU 148 1939 1939 LEU LEU A . n 
A 1 149 THR 149 1940 1940 THR THR A . n 
A 1 150 LEU 150 1941 1941 LEU LEU A . n 
A 1 151 LYS 151 1942 1942 LYS LYS A . n 
A 1 152 ASP 152 1943 1943 ASP ASP A . n 
A 1 153 ARG 153 1944 1944 ARG ARG A . n 
A 1 154 MET 154 1945 1945 MET MET A . n 
A 1 155 TRP 155 1946 1946 TRP TRP A . n 
A 1 156 TYR 156 1947 1947 TYR TYR A . n 
A 1 157 LEU 157 1948 1948 LEU LEU A . n 
A 1 158 GLN 158 1949 1949 GLN GLN A . n 
A 1 159 SER 159 1950 1950 SER SER A . n 
A 1 160 CYS 160 1951 1951 CYS CYS A . n 
A 1 161 LEU 161 1952 1952 LEU LEU A . n 
A 1 162 ARG 162 1953 1953 ARG ARG A . n 
A 1 163 LYS 163 1954 1954 LYS LYS A . n 
A 1 164 GLU 164 1955 1955 GLU GLU A . n 
A 1 165 SER 165 1956 1956 SER SER A . n 
A 1 166 ASP 166 1957 1957 ASP ASP A . n 
A 1 167 LYS 167 1958 1958 LYS LYS A . n 
A 1 168 GLU 168 1959 1959 GLU GLU A . n 
A 1 169 CYS 169 1960 1960 CYS CYS A . n 
A 1 170 SER 170 1961 1961 SER SER A . n 
A 1 171 VAL 171 1962 1962 VAL VAL A . n 
A 1 172 VAL 172 1963 1963 VAL VAL A . n 
A 1 173 ILE 173 1964 1964 ILE ILE A . n 
A 1 174 TYR 174 1965 1965 TYR TYR A . n 
A 1 175 ASP 175 1966 1966 ASP ASP A . n 
A 1 176 PHE 176 1967 1967 PHE PHE A . n 
A 1 177 ILE 177 1968 1968 ILE ILE A . n 
A 1 178 GLN 178 1969 1969 GLN GLN A . n 
A 1 179 SER 179 1970 1970 SER SER A . n 
A 1 180 TYR 180 1971 1971 TYR TYR A . n 
A 1 181 LYS 181 1972 1972 LYS LYS A . n 
A 1 182 ILE 182 1973 1973 ILE ILE A . n 
A 1 183 LEU 183 1974 1974 LEU LEU A . n 
A 1 184 LEU 184 1975 1975 LEU LEU A . n 
A 1 185 LEU 185 1976 1976 LEU LEU A . n 
A 1 186 SER 186 1977 1977 SER SER A . n 
A 1 187 CYS 187 1978 1978 CYS CYS A . n 
A 1 188 GLY 188 1979 1979 GLY GLY A . n 
A 1 189 ILE 189 1980 1980 ILE ILE A . n 
A 1 190 SER 190 1981 1981 SER SER A . n 
A 1 191 LEU 191 1982 1982 LEU LEU A . n 
A 1 192 GLU 192 1983 1983 GLU GLU A . n 
A 1 193 GLN 193 1984 1984 GLN GLN A . n 
A 1 194 SER 194 1985 1985 SER SER A . n 
A 1 195 TYR 195 1986 1986 TYR TYR A . n 
A 1 196 GLU 196 1987 1987 GLU GLU A . n 
A 1 197 ASP 197 1988 1988 ASP ASP A . n 
A 1 198 PRO 198 1989 1989 PRO PRO A . n 
A 1 199 LYS 199 1990 1990 LYS LYS A . n 
A 1 200 VAL 200 1991 1991 VAL VAL A . n 
A 1 201 ALA 201 1992 1992 ALA ALA A . n 
A 1 202 CYS 202 1993 1993 CYS CYS A . n 
A 1 203 TRP 203 1994 1994 TRP TRP A . n 
A 1 204 LEU 204 1995 1995 LEU LEU A . n 
A 1 205 LEU 205 1996 1996 LEU LEU A . n 
A 1 206 ASP 206 1997 1997 ASP ASP A . n 
A 1 207 PRO 207 1998 1998 PRO PRO A . n 
A 1 208 ASP 208 1999 1999 ASP ASP A . n 
A 1 209 SER 209 2000 2000 SER SER A . n 
A 1 210 GLN 210 2001 2001 GLN GLN A . n 
A 1 211 GLU 211 2002 2002 GLU GLU A . n 
A 1 212 PRO 212 2003 2003 PRO PRO A . n 
A 1 213 THR 213 2004 2004 THR THR A . n 
A 1 214 LEU 214 2005 2005 LEU LEU A . n 
A 1 215 HIS 215 2006 2006 HIS HIS A . n 
A 1 216 SER 216 2007 2007 SER SER A . n 
A 1 217 ILE 217 2008 2008 ILE ILE A . n 
A 1 218 VAL 218 2009 2009 VAL VAL A . n 
A 1 219 THR 219 2010 2010 THR THR A . n 
A 1 220 SER 220 2011 2011 SER SER A . n 
A 1 221 PHE 221 2012 2012 PHE PHE A . n 
A 1 222 LEU 222 2013 2013 LEU LEU A . n 
A 1 223 PRO 223 2014 2014 PRO PRO A . n 
A 1 224 HIS 224 2015 2015 HIS HIS A . n 
A 1 225 GLU 225 2016 2016 GLU GLU A . n 
A 1 226 LEU 226 2017 2017 LEU LEU A . n 
A 1 227 PRO 227 2018 2018 PRO PRO A . n 
A 1 228 LEU 228 2019 2019 LEU LEU A . n 
A 1 229 LEU 229 2020 2020 LEU LEU A . n 
A 1 230 GLU 230 2021 2021 GLU GLU A . n 
A 1 231 GLY 231 2022 2022 GLY GLY A . n 
A 1 232 MET 232 2023 2023 MET MET A . n 
A 1 233 GLU 233 2024 2024 GLU GLU A . n 
A 1 234 THR 234 2025 2025 THR THR A . n 
A 1 235 SER 235 2026 2026 SER SER A . n 
A 1 236 GLN 236 2027 2027 GLN GLN A . n 
A 1 237 GLY 237 2028 2028 GLY GLY A . n 
A 1 238 ILE 238 2029 2029 ILE ILE A . n 
A 1 239 GLN 239 2030 2030 GLN GLN A . n 
A 1 240 SER 240 2031 2031 SER SER A . n 
A 1 241 LEU 241 2032 2032 LEU LEU A . n 
A 1 242 GLY 242 2033 2033 GLY GLY A . n 
A 1 243 LEU 243 2034 2034 LEU LEU A . n 
A 1 244 ASN 244 2035 2035 ASN ASN A . n 
A 1 245 ALA 245 2036 2036 ALA ALA A . n 
A 1 246 GLY 246 2037 2037 GLY GLY A . n 
A 1 247 SER 247 2038 2038 SER SER A . n 
A 1 248 GLU 248 2039 2039 GLU GLU A . n 
A 1 249 HIS 249 2040 2040 HIS HIS A . n 
A 1 250 SER 250 2041 2041 SER SER A . n 
A 1 251 GLY 251 2042 2042 GLY GLY A . n 
A 1 252 ARG 252 2043 2043 ARG ARG A . n 
A 1 253 TYR 253 2044 2044 TYR TYR A . n 
A 1 254 ARG 254 2045 2045 ARG ARG A . n 
A 1 255 ALA 255 2046 2046 ALA ALA A . n 
A 1 256 SER 256 2047 2047 SER SER A . n 
A 1 257 VAL 257 2048 2048 VAL VAL A . n 
A 1 258 GLU 258 2049 2049 GLU GLU A . n 
A 1 259 SER 259 2050 2050 SER SER A . n 
A 1 260 ILE 260 2051 2051 ILE ILE A . n 
A 1 261 LEU 261 2052 2052 LEU LEU A . n 
A 1 262 ILE 262 2053 2053 ILE ILE A . n 
A 1 263 PHE 263 2054 2054 PHE PHE A . n 
A 1 264 ASN 264 2055 2055 ASN ASN A . n 
A 1 265 SER 265 2056 2056 SER SER A . n 
A 1 266 MET 266 2057 2057 MET MET A . n 
A 1 267 ASN 267 2058 2058 ASN ASN A . n 
A 1 268 GLN 268 2059 2059 GLN GLN A . n 
A 1 269 LEU 269 2060 2060 LEU LEU A . n 
A 1 270 ASN 270 2061 2061 ASN ASN A . n 
A 1 271 SER 271 2062 2062 SER SER A . n 
A 1 272 LEU 272 2063 2063 LEU LEU A . n 
A 1 273 LEU 273 2064 2064 LEU LEU A . n 
A 1 274 GLN 274 2065 2065 GLN GLN A . n 
A 1 275 LYS 275 2066 2066 LYS LYS A . n 
A 1 276 GLU 276 2067 2067 GLU GLU A . n 
A 1 277 ASN 277 2068 2068 ASN ASN A . n 
A 1 278 LEU 278 2069 2069 LEU LEU A . n 
A 1 279 GLN 279 2070 2070 GLN GLN A . n 
A 1 280 ASP 280 2071 2071 ASP ASP A . n 
A 1 281 VAL 281 2072 2072 VAL VAL A . n 
A 1 282 PHE 282 2073 2073 PHE PHE A . n 
A 1 283 ARG 283 2074 2074 ARG ARG A . n 
A 1 284 LYS 284 2075 2075 LYS LYS A . n 
A 1 285 VAL 285 2076 2076 VAL VAL A . n 
A 1 286 GLU 286 2077 2077 GLU GLU A . n 
A 1 287 MET 287 2078 2078 MET MET A . n 
A 1 288 PRO 288 2079 2079 PRO PRO A . n 
A 1 289 SER 289 2080 2080 SER SER A . n 
A 1 290 GLN 290 2081 2081 GLN GLN A . n 
A 1 291 TYR 291 2082 2082 TYR TYR A . n 
A 1 292 CYS 292 2083 2083 CYS CYS A . n 
A 1 293 LEU 293 2084 2084 LEU LEU A . n 
A 1 294 ALA 294 2085 2085 ALA ALA A . n 
A 1 295 LEU 295 2086 2086 LEU LEU A . n 
A 1 296 LEU 296 2087 2087 LEU LEU A . n 
A 1 297 GLU 297 2088 2088 GLU GLU A . n 
A 1 298 LEU 298 2089 2089 LEU LEU A . n 
A 1 299 ASN 299 2090 2090 ASN ASN A . n 
A 1 300 GLY 300 2091 2091 GLY GLY A . n 
A 1 301 ILE 301 2092 2092 ILE ILE A . n 
A 1 302 GLY 302 2093 2093 GLY GLY A . n 
A 1 303 PHE 303 2094 2094 PHE PHE A . n 
A 1 304 SER 304 2095 2095 SER SER A . n 
A 1 305 THR 305 2096 2096 THR THR A . n 
A 1 306 ALA 306 2097 2097 ALA ALA A . n 
A 1 307 GLU 307 2098 2098 GLU GLU A . n 
A 1 308 CYS 308 2099 2099 CYS CYS A . n 
A 1 309 GLU 309 2100 2100 GLU GLU A . n 
A 1 310 SER 310 2101 2101 SER SER A . n 
A 1 311 GLN 311 2102 2102 GLN GLN A . n 
A 1 312 LYS 312 2103 2103 LYS LYS A . n 
A 1 313 HIS 313 2104 2104 HIS HIS A . n 
A 1 314 ILE 314 2105 2105 ILE ILE A . n 
A 1 315 MET 315 2106 2106 MET MET A . n 
A 1 316 GLN 316 2107 2107 GLN GLN A . n 
A 1 317 ALA 317 2108 2108 ALA ALA A . n 
A 1 318 LYS 318 2109 2109 LYS LYS A . n 
A 1 319 LEU 319 2110 2110 LEU LEU A . n 
A 1 320 ASP 320 2111 2111 ASP ASP A . n 
A 1 321 ALA 321 2112 2112 ALA ALA A . n 
A 1 322 ILE 322 2113 2113 ILE ILE A . n 
A 1 323 GLU 323 2114 2114 GLU GLU A . n 
A 1 324 THR 324 2115 2115 THR THR A . n 
A 1 325 GLN 325 2116 2116 GLN GLN A . n 
A 1 326 ALA 326 2117 2117 ALA ALA A . n 
A 1 327 TYR 327 2118 2118 TYR TYR A . n 
A 1 328 GLN 328 2119 2119 GLN GLN A . n 
A 1 329 LEU 329 2120 2120 LEU LEU A . n 
A 1 330 ALA 330 2121 2121 ALA ALA A . n 
A 1 331 GLY 331 2122 2122 GLY GLY A . n 
A 1 332 HIS 332 2123 2123 HIS HIS A . n 
A 1 333 SER 333 2124 2124 SER SER A . n 
A 1 334 PHE 334 2125 2125 PHE PHE A . n 
A 1 335 SER 335 2126 2126 SER SER A . n 
A 1 336 PHE 336 2127 2127 PHE PHE A . n 
A 1 337 THR 337 2128 2128 THR THR A . n 
A 1 338 SER 338 2129 2129 SER SER A . n 
A 1 339 SER 339 2130 2130 SER SER A . n 
A 1 340 ASP 340 2131 2131 ASP ASP A . n 
A 1 341 ASP 341 2132 2132 ASP ASP A . n 
A 1 342 ILE 342 2133 2133 ILE ILE A . n 
A 1 343 ALA 343 2134 2134 ALA ALA A . n 
A 1 344 GLU 344 2135 2135 GLU GLU A . n 
A 1 345 VAL 345 2136 2136 VAL VAL A . n 
A 1 346 LEU 346 2137 2137 LEU LEU A . n 
A 1 347 PHE 347 2138 2138 PHE PHE A . n 
A 1 348 LEU 348 2139 2139 LEU LEU A . n 
A 1 349 GLU 349 2140 2140 GLU GLU A . n 
A 1 350 LEU 350 2141 2141 LEU LEU A . n 
A 1 351 LYS 351 2142 2142 LYS LYS A . n 
A 1 352 LEU 352 2143 2143 LEU LEU A . n 
A 1 353 PRO 353 2144 2144 PRO PRO A . n 
A 1 354 PRO 354 2145 2145 PRO PRO A . n 
A 1 355 ASN 355 2146 2146 ASN ASN A . n 
A 1 356 ARG 356 2147 2147 ARG ARG A . n 
A 1 357 GLU 357 2148 2148 GLU GLU A . n 
A 1 358 MET 358 2149 ?    ?   ?   A . n 
A 1 359 LYS 359 2150 ?    ?   ?   A . n 
A 1 360 ASN 360 2151 ?    ?   ?   A . n 
A 1 361 GLN 361 2152 ?    ?   ?   A . n 
A 1 362 GLY 362 2153 ?    ?   ?   A . n 
A 1 363 SER 363 2154 ?    ?   ?   A . n 
A 1 364 LYS 364 2155 ?    ?   ?   A . n 
A 1 365 LYS 365 2156 ?    ?   ?   A . n 
A 1 366 THR 366 2157 ?    ?   ?   A . n 
A 1 367 LEU 367 2158 ?    ?   ?   A . n 
A 1 368 GLY 368 2159 ?    ?   ?   A . n 
A 1 369 SER 369 2160 ?    ?   ?   A . n 
A 1 370 THR 370 2161 ?    ?   ?   A . n 
A 1 371 ARG 371 2162 ?    ?   ?   A . n 
A 1 372 ARG 372 2163 ?    ?   ?   A . n 
A 1 373 GLY 373 2164 ?    ?   ?   A . n 
A 1 374 ILE 374 2165 ?    ?   ?   A . n 
A 1 375 ASP 375 2166 ?    ?   ?   A . n 
A 1 376 ASN 376 2167 ?    ?   ?   A . n 
A 1 377 GLY 377 2168 ?    ?   ?   A . n 
A 1 378 ARG 378 2169 ?    ?   ?   A . n 
A 1 379 LYS 379 2170 ?    ?   ?   A . n 
A 1 380 LEU 380 2171 ?    ?   ?   A . n 
A 1 381 ARG 381 2172 ?    ?   ?   A . n 
A 1 382 LEU 382 2173 ?    ?   ?   A . n 
A 1 383 GLY 383 2174 2174 GLY GLY A . n 
A 1 384 ARG 384 2175 2175 ARG ARG A . n 
A 1 385 GLN 385 2176 2176 GLN GLN A . n 
A 1 386 PHE 386 2177 2177 PHE PHE A . n 
A 1 387 SER 387 2178 2178 SER SER A . n 
A 1 388 THR 388 2179 2179 THR THR A . n 
A 1 389 SER 389 2180 2180 SER SER A . n 
A 1 390 LYS 390 2181 2181 LYS LYS A . n 
A 1 391 ASP 391 2182 2182 ASP ASP A . n 
A 1 392 VAL 392 2183 2183 VAL VAL A . n 
A 1 393 LEU 393 2184 2184 LEU LEU A . n 
A 1 394 ASN 394 2185 2185 ASN ASN A . n 
A 1 395 LYS 395 2186 2186 LYS LYS A . n 
A 1 396 LEU 396 2187 2187 LEU LEU A . n 
A 1 397 LYS 397 2188 2188 LYS LYS A . n 
A 1 398 ALA 398 2189 2189 ALA ALA A . n 
A 1 399 LEU 399 2190 2190 LEU LEU A . n 
A 1 400 HIS 400 2191 2191 HIS HIS A . n 
A 1 401 PRO 401 2192 2192 PRO PRO A . n 
A 1 402 LEU 402 2193 2193 LEU LEU A . n 
A 1 403 PRO 403 2194 2194 PRO PRO A . n 
A 1 404 GLY 404 2195 2195 GLY GLY A . n 
A 1 405 LEU 405 2196 2196 LEU LEU A . n 
A 1 406 ILE 406 2197 2197 ILE ILE A . n 
A 1 407 LEU 407 2198 2198 LEU LEU A . n 
A 1 408 GLU 408 2199 2199 GLU GLU A . n 
A 1 409 TRP 409 2200 2200 TRP TRP A . n 
A 1 410 ARG 410 2201 2201 ARG ARG A . n 
A 1 411 ARG 411 2202 2202 ARG ARG A . n 
A 1 412 ILE 412 2203 2203 ILE ILE A . n 
A 1 413 THR 413 2204 2204 THR THR A . n 
A 1 414 ASN 414 2205 2205 ASN ASN A . n 
A 1 415 ALA 415 2206 2206 ALA ALA A . n 
A 1 416 ILE 416 2207 2207 ILE ILE A . n 
A 1 417 THR 417 2208 2208 THR THR A . n 
A 1 418 LYS 418 2209 2209 LYS LYS A . n 
A 1 419 VAL 419 2210 2210 VAL VAL A . n 
A 1 420 VAL 420 2211 2211 VAL VAL A . n 
A 1 421 PHE 421 2212 2212 PHE PHE A . n 
A 1 422 PRO 422 2213 2213 PRO PRO A . n 
A 1 423 LEU 423 2214 2214 LEU LEU A . n 
A 1 424 GLN 424 2215 2215 GLN GLN A . n 
A 1 425 ARG 425 2216 2216 ARG ARG A . n 
A 1 426 GLU 426 2217 2217 GLU GLU A . n 
A 1 427 LYS 427 2218 2218 LYS LYS A . n 
A 1 428 CYS 428 2219 2219 CYS CYS A . n 
A 1 429 LEU 429 2220 2220 LEU LEU A . n 
A 1 430 ASN 430 2221 2221 ASN ASN A . n 
A 1 431 PRO 431 2222 2222 PRO PRO A . n 
A 1 432 PHE 432 2223 2223 PHE PHE A . n 
A 1 433 LEU 433 2224 2224 LEU LEU A . n 
A 1 434 GLY 434 2225 2225 GLY GLY A . n 
A 1 435 MET 435 2226 2226 MET MET A . n 
A 1 436 GLU 436 2227 2227 GLU GLU A . n 
A 1 437 ARG 437 2228 2228 ARG ARG A . n 
A 1 438 ILE 438 2229 2229 ILE ILE A . n 
A 1 439 TYR 439 2230 2230 TYR TYR A . n 
A 1 440 PRO 440 2231 2231 PRO PRO A . n 
A 1 441 VAL 441 2232 2232 VAL VAL A . n 
A 1 442 SER 442 2233 2233 SER SER A . n 
A 1 443 GLN 443 2234 2234 GLN GLN A . n 
A 1 444 SER 444 2235 2235 SER SER A . n 
A 1 445 HIS 445 2236 2236 HIS HIS A . n 
A 1 446 THR 446 2237 2237 THR THR A . n 
A 1 447 ALA 447 2238 2238 ALA ALA A . n 
A 1 448 THR 448 2239 2239 THR THR A . n 
A 1 449 GLY 449 2240 2240 GLY GLY A . n 
A 1 450 ARG 450 2241 2241 ARG ARG A . n 
A 1 451 ILE 451 2242 2242 ILE ILE A . n 
A 1 452 THR 452 2243 2243 THR THR A . n 
A 1 453 PHE 453 2244 2244 PHE PHE A . n 
A 1 454 THR 454 2245 2245 THR THR A . n 
A 1 455 GLU 455 2246 2246 GLU GLU A . n 
A 1 456 PRO 456 2247 2247 PRO PRO A . n 
A 1 457 ASN 457 2248 2248 ASN ASN A . n 
A 1 458 ILE 458 2249 2249 ILE ILE A . n 
A 1 459 GLN 459 2250 2250 GLN GLN A . n 
A 1 460 ASN 460 2251 2251 ASN ASN A . n 
A 1 461 VAL 461 2252 2252 VAL VAL A . n 
A 1 462 PRO 462 2253 2253 PRO PRO A . n 
A 1 463 ARG 463 2254 2254 ARG ARG A . n 
A 1 464 ASP 464 2255 2255 ASP ASP A . n 
A 1 465 PHE 465 2256 2256 PHE PHE A . n 
A 1 466 GLU 466 2257 2257 GLU GLU A . n 
A 1 467 ILE 467 2258 2258 ILE ILE A . n 
A 1 468 LYS 468 2259 2259 LYS LYS A . n 
A 1 469 MET 469 2260 2260 MET MET A . n 
A 1 470 PRO 470 2261 2261 PRO PRO A . n 
A 1 471 THR 471 2262 ?    ?   ?   A . n 
A 1 472 LEU 472 2263 ?    ?   ?   A . n 
A 1 473 VAL 473 2264 ?    ?   ?   A . n 
A 1 474 GLY 474 2265 ?    ?   ?   A . n 
A 1 475 GLU 475 2266 ?    ?   ?   A . n 
A 1 476 SER 476 2267 ?    ?   ?   A . n 
A 1 477 PRO 477 2268 ?    ?   ?   A . n 
A 1 478 PRO 478 2269 ?    ?   ?   A . n 
A 1 479 SER 479 2270 ?    ?   ?   A . n 
A 1 480 GLN 480 2271 ?    ?   ?   A . n 
A 1 481 ALA 481 2272 ?    ?   ?   A . n 
A 1 482 VAL 482 2273 ?    ?   ?   A . n 
A 1 483 GLY 483 2274 ?    ?   ?   A . n 
A 1 484 LYS 484 2275 ?    ?   ?   A . n 
A 1 485 GLY 485 2276 ?    ?   ?   A . n 
A 1 486 LEU 486 2277 ?    ?   ?   A . n 
A 1 487 LEU 487 2278 ?    ?   ?   A . n 
A 1 488 PRO 488 2279 ?    ?   ?   A . n 
A 1 489 MET 489 2280 ?    ?   ?   A . n 
A 1 490 GLY 490 2281 ?    ?   ?   A . n 
A 1 491 ARG 491 2282 ?    ?   ?   A . n 
A 1 492 GLY 492 2283 ?    ?   ?   A . n 
A 1 493 LYS 493 2284 ?    ?   ?   A . n 
A 1 494 TYR 494 2285 ?    ?   ?   A . n 
A 1 495 LYS 495 2286 ?    ?   ?   A . n 
A 1 496 LYS 496 2287 ?    ?   ?   A . n 
A 1 497 GLY 497 2288 ?    ?   ?   A . n 
A 1 498 PHE 498 2289 ?    ?   ?   A . n 
A 1 499 SER 499 2290 ?    ?   ?   A . n 
A 1 500 VAL 500 2291 ?    ?   ?   A . n 
A 1 501 ASN 501 2292 ?    ?   ?   A . n 
A 1 502 PRO 502 2293 ?    ?   ?   A . n 
A 1 503 ARG 503 2294 ?    ?   ?   A . n 
A 1 504 CYS 504 2295 ?    ?   ?   A . n 
A 1 505 GLN 505 2296 ?    ?   ?   A . n 
A 1 506 ALA 506 2297 ?    ?   ?   A . n 
A 1 507 GLN 507 2298 ?    ?   ?   A . n 
A 1 508 MET 508 2299 ?    ?   ?   A . n 
A 1 509 GLU 509 2300 ?    ?   ?   A . n 
A 1 510 GLU 510 2301 ?    ?   ?   A . n 
A 1 511 ARG 511 2302 ?    ?   ?   A . n 
A 1 512 ALA 512 2303 ?    ?   ?   A . n 
A 1 513 ALA 513 2304 ?    ?   ?   A . n 
A 1 514 ASP 514 2305 ?    ?   ?   A . n 
A 1 515 ARG 515 2306 ?    ?   ?   A . n 
A 1 516 GLY 516 2307 ?    ?   ?   A . n 
A 1 517 MET 517 2308 2308 MET MET A . n 
A 1 518 PRO 518 2309 2309 PRO PRO A . n 
A 1 519 PHE 519 2310 2310 PHE PHE A . n 
A 1 520 SER 520 2311 2311 SER SER A . n 
A 1 521 ILE 521 2312 2312 ILE ILE A . n 
A 1 522 SER 522 2313 2313 SER SER A . n 
A 1 523 MET 523 2314 2314 MET MET A . n 
A 1 524 ARG 524 2315 2315 ARG ARG A . n 
A 1 525 HIS 525 2316 2316 HIS HIS A . n 
A 1 526 ALA 526 2317 2317 ALA ALA A . n 
A 1 527 PHE 527 2318 2318 PHE PHE A . n 
A 1 528 VAL 528 2319 2319 VAL VAL A . n 
A 1 529 PRO 529 2320 2320 PRO PRO A . n 
A 1 530 PHE 530 2321 2321 PHE PHE A . n 
A 1 531 PRO 531 2322 2322 PRO PRO A . n 
A 1 532 GLY 532 2323 2323 GLY GLY A . n 
A 1 533 GLY 533 2324 2324 GLY GLY A . n 
A 1 534 SER 534 2325 2325 SER SER A . n 
A 1 535 ILE 535 2326 2326 ILE ILE A . n 
A 1 536 LEU 536 2327 2327 LEU LEU A . n 
A 1 537 ALA 537 2328 2328 ALA ALA A . n 
A 1 538 ALA 538 2329 2329 ALA ALA A . n 
A 1 539 ASP 539 2330 2330 ASP ASP A . n 
A 1 540 TYR 540 2331 2331 TYR TYR A . n 
A 1 541 SER 541 2332 2332 SER SER A . n 
A 1 542 GLN 542 2333 2333 GLN GLN A . n 
A 1 543 LEU 543 2334 2334 LEU LEU A . n 
A 1 544 GLU 544 2335 2335 GLU GLU A . n 
A 1 545 LEU 545 2336 2336 LEU LEU A . n 
A 1 546 ARG 546 2337 2337 ARG ARG A . n 
A 1 547 ILE 547 2338 2338 ILE ILE A . n 
A 1 548 LEU 548 2339 2339 LEU LEU A . n 
A 1 549 ALA 549 2340 2340 ALA ALA A . n 
A 1 550 HIS 550 2341 2341 HIS HIS A . n 
A 1 551 LEU 551 2342 2342 LEU LEU A . n 
A 1 552 SER 552 2343 2343 SER SER A . n 
A 1 553 HIS 553 2344 2344 HIS HIS A . n 
A 1 554 ASP 554 2345 2345 ASP ASP A . n 
A 1 555 ARG 555 2346 2346 ARG ARG A . n 
A 1 556 ARG 556 2347 2347 ARG ARG A . n 
A 1 557 LEU 557 2348 2348 LEU LEU A . n 
A 1 558 ILE 558 2349 2349 ILE ILE A . n 
A 1 559 GLN 559 2350 2350 GLN GLN A . n 
A 1 560 VAL 560 2351 2351 VAL VAL A . n 
A 1 561 LEU 561 2352 2352 LEU LEU A . n 
A 1 562 ASN 562 2353 2353 ASN ASN A . n 
A 1 563 THR 563 2354 2354 THR THR A . n 
A 1 564 GLY 564 2355 2355 GLY GLY A . n 
A 1 565 ALA 565 2356 2356 ALA ALA A . n 
A 1 566 ASP 566 2357 2357 ASP ASP A . n 
A 1 567 VAL 567 2358 2358 VAL VAL A . n 
A 1 568 PHE 568 2359 2359 PHE PHE A . n 
A 1 569 ARG 569 2360 2360 ARG ARG A . n 
A 1 570 SER 570 2361 2361 SER SER A . n 
A 1 571 ILE 571 2362 2362 ILE ILE A . n 
A 1 572 ALA 572 2363 2363 ALA ALA A . n 
A 1 573 ALA 573 2364 2364 ALA ALA A . n 
A 1 574 GLU 574 2365 2365 GLU GLU A . n 
A 1 575 TRP 575 2366 2366 TRP TRP A . n 
A 1 576 LYS 576 2367 2367 LYS LYS A . n 
A 1 577 MET 577 2368 2368 MET MET A . n 
A 1 578 ILE 578 2369 2369 ILE ILE A . n 
A 1 579 GLU 579 2370 2370 GLU GLU A . n 
A 1 580 PRO 580 2371 2371 PRO PRO A . n 
A 1 581 GLU 581 2372 2372 GLU GLU A . n 
A 1 582 SER 582 2373 2373 SER SER A . n 
A 1 583 VAL 583 2374 2374 VAL VAL A . n 
A 1 584 GLY 584 2375 2375 GLY GLY A . n 
A 1 585 ASP 585 2376 2376 ASP ASP A . n 
A 1 586 ASP 586 2377 2377 ASP ASP A . n 
A 1 587 LEU 587 2378 2378 LEU LEU A . n 
A 1 588 ARG 588 2379 2379 ARG ARG A . n 
A 1 589 GLN 589 2380 2380 GLN GLN A . n 
A 1 590 GLN 590 2381 2381 GLN GLN A . n 
A 1 591 ALA 591 2382 2382 ALA ALA A . n 
A 1 592 LYS 592 2383 2383 LYS LYS A . n 
A 1 593 GLN 593 2384 2384 GLN GLN A . n 
A 1 594 ILE 594 2385 2385 ILE ILE A . n 
A 1 595 CYS 595 2386 2386 CYS CYS A . n 
A 1 596 TYR 596 2387 2387 TYR TYR A . n 
A 1 597 GLY 597 2388 2388 GLY GLY A . n 
A 1 598 ILE 598 2389 2389 ILE ILE A . n 
A 1 599 ILE 599 2390 2390 ILE ILE A . n 
A 1 600 TYR 600 2391 2391 TYR TYR A . n 
A 1 601 GLY 601 2392 2392 GLY GLY A . n 
A 1 602 MET 602 2393 2393 MET MET A . n 
A 1 603 GLY 603 2394 2394 GLY GLY A . n 
A 1 604 ALA 604 2395 2395 ALA ALA A . n 
A 1 605 LYS 605 2396 2396 LYS LYS A . n 
A 1 606 SER 606 2397 2397 SER SER A . n 
A 1 607 LEU 607 2398 2398 LEU LEU A . n 
A 1 608 GLY 608 2399 2399 GLY GLY A . n 
A 1 609 GLU 609 2400 2400 GLU GLU A . n 
A 1 610 GLN 610 2401 2401 GLN GLN A . n 
A 1 611 MET 611 2402 2402 MET MET A . n 
A 1 612 GLY 612 2403 2403 GLY GLY A . n 
A 1 613 ILE 613 2404 2404 ILE ILE A . n 
A 1 614 LYS 614 2405 2405 LYS LYS A . n 
A 1 615 GLU 615 2406 2406 GLU GLU A . n 
A 1 616 ASN 616 2407 2407 ASN ASN A . n 
A 1 617 ASP 617 2408 2408 ASP ASP A . n 
A 1 618 ALA 618 2409 2409 ALA ALA A . n 
A 1 619 ALA 619 2410 2410 ALA ALA A . n 
A 1 620 CYS 620 2411 2411 CYS CYS A . n 
A 1 621 TYR 621 2412 2412 TYR TYR A . n 
A 1 622 ILE 622 2413 2413 ILE ILE A . n 
A 1 623 ASP 623 2414 2414 ASP ASP A . n 
A 1 624 SER 624 2415 2415 SER SER A . n 
A 1 625 PHE 625 2416 2416 PHE PHE A . n 
A 1 626 LYS 626 2417 2417 LYS LYS A . n 
A 1 627 SER 627 2418 2418 SER SER A . n 
A 1 628 ARG 628 2419 2419 ARG ARG A . n 
A 1 629 TYR 629 2420 2420 TYR TYR A . n 
A 1 630 THR 630 2421 2421 THR THR A . n 
A 1 631 GLY 631 2422 2422 GLY GLY A . n 
A 1 632 ILE 632 2423 2423 ILE ILE A . n 
A 1 633 ASN 633 2424 2424 ASN ASN A . n 
A 1 634 GLN 634 2425 2425 GLN GLN A . n 
A 1 635 PHE 635 2426 2426 PHE PHE A . n 
A 1 636 MET 636 2427 2427 MET MET A . n 
A 1 637 THR 637 2428 2428 THR THR A . n 
A 1 638 GLU 638 2429 2429 GLU GLU A . n 
A 1 639 THR 639 2430 2430 THR THR A . n 
A 1 640 VAL 640 2431 2431 VAL VAL A . n 
A 1 641 LYS 641 2432 2432 LYS LYS A . n 
A 1 642 ASN 642 2433 2433 ASN ASN A . n 
A 1 643 CYS 643 2434 2434 CYS CYS A . n 
A 1 644 LYS 644 2435 2435 LYS LYS A . n 
A 1 645 ARG 645 2436 2436 ARG ARG A . n 
A 1 646 ASP 646 2437 2437 ASP ASP A . n 
A 1 647 GLY 647 2438 2438 GLY GLY A . n 
A 1 648 PHE 648 2439 2439 PHE PHE A . n 
A 1 649 VAL 649 2440 2440 VAL VAL A . n 
A 1 650 GLN 650 2441 2441 GLN GLN A . n 
A 1 651 THR 651 2442 2442 THR THR A . n 
A 1 652 ILE 652 2443 2443 ILE ILE A . n 
A 1 653 LEU 653 2444 2444 LEU LEU A . n 
A 1 654 GLY 654 2445 2445 GLY GLY A . n 
A 1 655 ARG 655 2446 2446 ARG ARG A . n 
A 1 656 ARG 656 2447 2447 ARG ARG A . n 
A 1 657 ARG 657 2448 2448 ARG ARG A . n 
A 1 658 TYR 658 2449 2449 TYR TYR A . n 
A 1 659 LEU 659 2450 2450 LEU LEU A . n 
A 1 660 PRO 660 2451 2451 PRO PRO A . n 
A 1 661 GLY 661 2452 2452 GLY GLY A . n 
A 1 662 ILE 662 2453 2453 ILE ILE A . n 
A 1 663 LYS 663 2454 2454 LYS LYS A . n 
A 1 664 ASP 664 2455 2455 ASP ASP A . n 
A 1 665 ASN 665 2456 2456 ASN ASN A . n 
A 1 666 ASN 666 2457 2457 ASN ASN A . n 
A 1 667 PRO 667 2458 2458 PRO PRO A . n 
A 1 668 TYR 668 2459 2459 TYR TYR A . n 
A 1 669 ARG 669 2460 2460 ARG ARG A . n 
A 1 670 LYS 670 2461 2461 LYS LYS A . n 
A 1 671 ALA 671 2462 2462 ALA ALA A . n 
A 1 672 HIS 672 2463 2463 HIS HIS A . n 
A 1 673 ALA 673 2464 2464 ALA ALA A . n 
A 1 674 GLU 674 2465 2465 GLU GLU A . n 
A 1 675 ARG 675 2466 2466 ARG ARG A . n 
A 1 676 GLN 676 2467 2467 GLN GLN A . n 
A 1 677 ALA 677 2468 2468 ALA ALA A . n 
A 1 678 ILE 678 2469 2469 ILE ILE A . n 
A 1 679 ASN 679 2470 2470 ASN ASN A . n 
A 1 680 THR 680 2471 2471 THR THR A . n 
A 1 681 ILE 681 2472 2472 ILE ILE A . n 
A 1 682 VAL 682 2473 2473 VAL VAL A . n 
A 1 683 GLN 683 2474 2474 GLN GLN A . n 
A 1 684 GLY 684 2475 2475 GLY GLY A . n 
A 1 685 SER 685 2476 2476 SER SER A . n 
A 1 686 ALA 686 2477 2477 ALA ALA A . n 
A 1 687 ALA 687 2478 2478 ALA ALA A . n 
A 1 688 ASP 688 2479 2479 ASP ASP A . n 
A 1 689 ILE 689 2480 2480 ILE ILE A . n 
A 1 690 VAL 690 2481 2481 VAL VAL A . n 
A 1 691 LYS 691 2482 2482 LYS LYS A . n 
A 1 692 ILE 692 2483 2483 ILE ILE A . n 
A 1 693 ALA 693 2484 2484 ALA ALA A . n 
A 1 694 THR 694 2485 2485 THR THR A . n 
A 1 695 VAL 695 2486 2486 VAL VAL A . n 
A 1 696 ASN 696 2487 2487 ASN ASN A . n 
A 1 697 ILE 697 2488 2488 ILE ILE A . n 
A 1 698 GLN 698 2489 2489 GLN GLN A . n 
A 1 699 LYS 699 2490 2490 LYS LYS A . n 
A 1 700 GLN 700 2491 2491 GLN GLN A . n 
A 1 701 LEU 701 2492 2492 LEU LEU A . n 
A 1 702 GLU 702 2493 2493 GLU GLU A . n 
A 1 703 THR 703 2494 2494 THR THR A . n 
A 1 704 PHE 704 2495 2495 PHE PHE A . n 
A 1 705 HIS 705 2496 2496 HIS HIS A . n 
A 1 706 SER 706 2497 2497 SER SER A . n 
A 1 707 THR 707 2498 2498 THR THR A . n 
A 1 708 PHE 708 2499 2499 PHE PHE A . n 
A 1 709 LYS 709 2500 2500 LYS LYS A . n 
A 1 710 SER 710 2501 2501 SER SER A . n 
A 1 711 HIS 711 2502 2502 HIS HIS A . n 
A 1 712 GLY 712 2503 2503 GLY GLY A . n 
A 1 713 HIS 713 2504 2504 HIS HIS A . n 
A 1 714 ARG 714 2505 2505 ARG ARG A . n 
A 1 715 GLU 715 2506 2506 GLU GLU A . n 
A 1 716 GLY 716 2507 2507 GLY GLY A . n 
A 1 717 MET 717 2508 2508 MET MET A . n 
A 1 718 LEU 718 2509 ?    ?   ?   A . n 
A 1 719 GLN 719 2510 ?    ?   ?   A . n 
A 1 720 SER 720 2511 ?    ?   ?   A . n 
A 1 721 ASP 721 2512 ?    ?   ?   A . n 
A 1 722 GLN 722 2513 ?    ?   ?   A . n 
A 1 723 THR 723 2514 ?    ?   ?   A . n 
A 1 724 GLY 724 2515 ?    ?   ?   A . n 
A 1 725 LEU 725 2516 ?    ?   ?   A . n 
A 1 726 SER 726 2517 ?    ?   ?   A . n 
A 1 727 ARG 727 2518 ?    ?   ?   A . n 
A 1 728 LYS 728 2519 ?    ?   ?   A . n 
A 1 729 ARG 729 2520 ?    ?   ?   A . n 
A 1 730 LYS 730 2521 ?    ?   ?   A . n 
A 1 731 LEU 731 2522 ?    ?   ?   A . n 
A 1 732 GLN 732 2523 ?    ?   ?   A . n 
A 1 733 GLY 733 2524 ?    ?   ?   A . n 
A 1 734 MET 734 2525 ?    ?   ?   A . n 
A 1 735 PHE 735 2526 2526 PHE PHE A . n 
A 1 736 CYS 736 2527 2527 CYS CYS A . n 
A 1 737 PRO 737 2528 2528 PRO PRO A . n 
A 1 738 ILE 738 2529 2529 ILE ILE A . n 
A 1 739 ARG 739 2530 2530 ARG ARG A . n 
A 1 740 GLY 740 2531 2531 GLY GLY A . n 
A 1 741 GLY 741 2532 2532 GLY GLY A . n 
A 1 742 PHE 742 2533 2533 PHE PHE A . n 
A 1 743 PHE 743 2534 2534 PHE PHE A . n 
A 1 744 ILE 744 2535 2535 ILE ILE A . n 
A 1 745 LEU 745 2536 2536 LEU LEU A . n 
A 1 746 GLN 746 2537 2537 GLN GLN A . n 
A 1 747 LEU 747 2538 2538 LEU LEU A . n 
A 1 748 HIS 748 2539 2539 HIS HIS A . n 
A 1 749 ASP 749 2540 2540 ASP ASP A . n 
A 1 750 GLU 750 2541 2541 GLU GLU A . n 
A 1 751 LEU 751 2542 2542 LEU LEU A . n 
A 1 752 LEU 752 2543 2543 LEU LEU A . n 
A 1 753 TYR 753 2544 2544 TYR TYR A . n 
A 1 754 GLU 754 2545 2545 GLU GLU A . n 
A 1 755 VAL 755 2546 2546 VAL VAL A . n 
A 1 756 ALA 756 2547 2547 ALA ALA A . n 
A 1 757 GLU 757 2548 2548 GLU GLU A . n 
A 1 758 GLU 758 2549 2549 GLU GLU A . n 
A 1 759 ASP 759 2550 2550 ASP ASP A . n 
A 1 760 VAL 760 2551 2551 VAL VAL A . n 
A 1 761 VAL 761 2552 2552 VAL VAL A . n 
A 1 762 GLN 762 2553 2553 GLN GLN A . n 
A 1 763 VAL 763 2554 2554 VAL VAL A . n 
A 1 764 ALA 764 2555 2555 ALA ALA A . n 
A 1 765 GLN 765 2556 2556 GLN GLN A . n 
A 1 766 ILE 766 2557 2557 ILE ILE A . n 
A 1 767 VAL 767 2558 2558 VAL VAL A . n 
A 1 768 LYS 768 2559 2559 LYS LYS A . n 
A 1 769 ASN 769 2560 2560 ASN ASN A . n 
A 1 770 GLU 770 2561 2561 GLU GLU A . n 
A 1 771 MET 771 2562 2562 MET MET A . n 
A 1 772 GLU 772 2563 2563 GLU GLU A . n 
A 1 773 SER 773 2564 2564 SER SER A . n 
A 1 774 ALA 774 2565 2565 ALA ALA A . n 
A 1 775 VAL 775 2566 2566 VAL VAL A . n 
A 1 776 LYS 776 2567 2567 LYS LYS A . n 
A 1 777 LEU 777 2568 2568 LEU LEU A . n 
A 1 778 SER 778 2569 2569 SER SER A . n 
A 1 779 VAL 779 2570 2570 VAL VAL A . n 
A 1 780 LYS 780 2571 2571 LYS LYS A . n 
A 1 781 LEU 781 2572 2572 LEU LEU A . n 
A 1 782 LYS 782 2573 2573 LYS LYS A . n 
A 1 783 VAL 783 2574 2574 VAL VAL A . n 
A 1 784 LYS 784 2575 2575 LYS LYS A . n 
A 1 785 VAL 785 2576 2576 VAL VAL A . n 
A 1 786 LYS 786 2577 2577 LYS LYS A . n 
A 1 787 ILE 787 2578 2578 ILE ILE A . n 
A 1 788 GLY 788 2579 2579 GLY GLY A . n 
A 1 789 ALA 789 2580 2580 ALA ALA A . n 
A 1 790 SER 790 2581 2581 SER SER A . n 
A 1 791 TRP 791 2582 2582 TRP TRP A . n 
A 1 792 GLY 792 2583 2583 GLY GLY A . n 
A 1 793 GLU 793 2584 2584 GLU GLU A . n 
A 1 794 LEU 794 2585 2585 LEU LEU A . n 
A 1 795 LYS 795 2586 2586 LYS LYS A . n 
A 1 796 ASP 796 2587 2587 ASP ASP A . n 
A 1 797 PHE 797 2588 2588 PHE PHE A . n 
A 1 798 ASP 798 2589 2589 ASP ASP A . n 
A 1 799 VAL 799 2590 2590 VAL VAL A . n 
B 2 1   DT  1   1    ?    ?   ?   C . n 
B 2 2   DG  2   2    ?    ?   ?   C . n 
B 2 3   DC  3   3    ?    ?   ?   C . n 
B 2 4   DT  4   4    ?    ?   ?   C . n 
B 2 5   DG  5   5    ?    ?   ?   C . n 
B 2 6   DT  6   6    ?    ?   ?   C . n 
B 2 7   DG  7   7    ?    ?   ?   C . n 
B 2 8   DA  8   8    ?    ?   ?   C . n 
B 2 9   DG  9   9    ?    ?   ?   C . n 
B 2 10  DG  10  10   ?    ?   ?   C . n 
B 2 11  DC  11  11   ?    ?   ?   C . n 
B 2 12  DA  12  12   ?    ?   ?   C . n 
B 2 13  DT  13  13   ?    ?   ?   C . n 
B 2 14  DC  14  14   ?    ?   ?   C . n 
B 2 15  DC  15  15   15   DC  DC  C . n 
B 2 16  DG  16  16   16   DG  DG  C . n 
B 2 17  DT  17  17   17   DT  DT  C . n 
B 2 18  DA  18  18   18   DA  DA  C . n 
B 2 19  DG  19  19   19   DG  DG  C . n 
B 2 20  DOC 20  20   20   DOC DOC C . n 
C 3 1   DG  1   1    ?    ?   ?   D . n 
C 3 2   DC  2   2    ?    ?   ?   D . n 
C 3 3   DA  3   3    ?    ?   ?   D . n 
C 3 4   DG  4   4    ?    ?   ?   D . n 
C 3 5   DT  5   5    ?    ?   ?   D . n 
C 3 6   DC  6   6    ?    ?   ?   D . n 
C 3 7   DA  7   7    7    DA  DA  D . n 
C 3 8   DG  8   8    8    DG  DG  D . n 
C 3 9   DT  9   9    9    DT  DT  D . n 
C 3 10  DG  10  10   10   DG  DG  D . n 
C 3 11  DC  11  11   11   DC  DC  D . n 
C 3 12  DT  12  12   12   DT  DT  D . n 
C 3 13  DA  13  13   13   DA  DA  D . n 
C 3 14  DC  14  14   14   DC  DC  D . n 
C 3 15  DG  15  15   15   DG  DG  D . n 
C 3 16  DG  16  16   ?    ?   ?   D . n 
C 3 17  DA  17  17   ?    ?   ?   D . n 
C 3 18  DT  18  18   ?    ?   ?   D . n 
C 3 19  DG  19  19   ?    ?   ?   D . n 
C 3 20  DC  20  20   ?    ?   ?   D . n 
C 3 21  DC  21  21   ?    ?   ?   D . n 
C 3 22  DT  22  22   ?    ?   ?   D . n 
C 3 23  DC  23  23   ?    ?   ?   D . n 
C 3 24  DA  24  24   ?    ?   ?   D . n 
C 3 25  DC  25  25   ?    ?   ?   D . n 
C 3 26  DA  26  26   ?    ?   ?   D . n 
C 3 27  DG  27  27   ?    ?   ?   D . n 
C 3 28  DC  28  28   ?    ?   ?   D . n 
C 3 29  DA  29  29   ?    ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 TTP ? ? TTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 4 TTP 1 2601 1 TTP TTP A . 
E 5 MG  1 2602 1 MG  MG  A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 1860 ? CG  ? A ARG 69  CG  
2  1 Y 1 A ARG 1860 ? CD  ? A ARG 69  CD  
3  1 Y 1 A ARG 1860 ? NE  ? A ARG 69  NE  
4  1 Y 1 A ARG 1860 ? CZ  ? A ARG 69  CZ  
5  1 Y 1 A ARG 1860 ? NH1 ? A ARG 69  NH1 
6  1 Y 1 A ARG 1860 ? NH2 ? A ARG 69  NH2 
7  1 Y 1 A SER 1861 ? OG  ? A SER 70  OG  
8  1 Y 1 A ASP 1896 ? CG  ? A ASP 105 CG  
9  1 Y 1 A ASP 1896 ? OD1 ? A ASP 105 OD1 
10 1 Y 1 A ASP 1896 ? OD2 ? A ASP 105 OD2 
11 1 Y 1 A LYS 1942 ? CG  ? A LYS 151 CG  
12 1 Y 1 A LYS 1942 ? CD  ? A LYS 151 CD  
13 1 Y 1 A LYS 1942 ? CE  ? A LYS 151 CE  
14 1 Y 1 A LYS 1942 ? NZ  ? A LYS 151 NZ  
15 1 Y 1 A THR 2025 ? OG1 ? A THR 234 OG1 
16 1 Y 1 A THR 2025 ? CG2 ? A THR 234 CG2 
17 1 Y 1 A SER 2026 ? OG  ? A SER 235 OG  
18 1 Y 1 A GLN 2027 ? CG  ? A GLN 236 CG  
19 1 Y 1 A GLN 2027 ? CD  ? A GLN 236 CD  
20 1 Y 1 A GLN 2027 ? OE1 ? A GLN 236 OE1 
21 1 Y 1 A GLN 2027 ? NE2 ? A GLN 236 NE2 
22 1 Y 1 A ARG 2147 ? CG  ? A ARG 356 CG  
23 1 Y 1 A ARG 2147 ? CD  ? A ARG 356 CD  
24 1 Y 1 A ARG 2147 ? NE  ? A ARG 356 NE  
25 1 Y 1 A ARG 2147 ? CZ  ? A ARG 356 CZ  
26 1 Y 1 A ARG 2147 ? NH1 ? A ARG 356 NH1 
27 1 Y 1 A ARG 2147 ? NH2 ? A ARG 356 NH2 
28 1 Y 1 A GLU 2257 ? CG  ? A GLU 466 CG  
29 1 Y 1 A GLU 2257 ? CD  ? A GLU 466 CD  
30 1 Y 1 A GLU 2257 ? OE1 ? A GLU 466 OE1 
31 1 Y 1 A GLU 2257 ? OE2 ? A GLU 466 OE2 
32 1 Y 1 A LYS 2259 ? CG  ? A LYS 468 CG  
33 1 Y 1 A LYS 2259 ? CD  ? A LYS 468 CD  
34 1 Y 1 A LYS 2259 ? CE  ? A LYS 468 CE  
35 1 Y 1 A LYS 2259 ? NZ  ? A LYS 468 NZ  
36 1 Y 1 A GLU 2370 ? CG  ? A GLU 579 CG  
37 1 Y 1 A GLU 2370 ? CD  ? A GLU 579 CD  
38 1 Y 1 A GLU 2370 ? OE1 ? A GLU 579 OE1 
39 1 Y 1 A GLU 2370 ? OE2 ? A GLU 579 OE2 
40 1 Y 1 A GLU 2372 ? CG  ? A GLU 581 CG  
41 1 Y 1 A GLU 2372 ? CD  ? A GLU 581 CD  
42 1 Y 1 A GLU 2372 ? OE1 ? A GLU 581 OE1 
43 1 Y 1 A GLU 2372 ? OE2 ? A GLU 581 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                     9AU8 
_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                         9AU8 
_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                   9AU8 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9AU8 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003  ? 5663 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.525  ? 7735 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 13.557 ? 917  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.038  ? 863  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003  ? 916  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9AU8 
_struct.title                        
'Ternary complex of human DNA polymerase theta polymerase domain with a mismatched T:T base pair' 
_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        9AU8 
_struct_keywords.text            
'DNA translesion synthesis, theta-mediated end joining, A-family DNA polymerase, DNA BINDING PROTEIN-DNA complex' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN/DNA' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP DPOLQ_HUMAN O75417 ? 1 
;GFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIG
SRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSC
LRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQS
LGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLD
AIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALH
PLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQ
AVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQV
LNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETV
KNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQS
DQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
;
1792 
2 PDB 9AU8        9AU8   ? 2 ? 1    
3 PDB 9AU8        9AU8   ? 3 ? 1    
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9AU8 A 1 ? 799 ? O75417 1792 ? 2590 ? 1792 2590 
2 2 9AU8 C 1 ? 20  ? 9AU8   1    ? 20   ? 1    20   
3 3 9AU8 D 1 ? 29  ? 9AU8   1    ? 29   ? 1    29   
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 42  ? CYS A 55  ? ASP A 1833 CYS A 1846 1 ? 14 
HELX_P HELX_P2  AA2 THR A 149 ? LEU A 161 ? THR A 1940 LEU A 1952 1 ? 13 
HELX_P HELX_P3  AA3 ASP A 175 ? SER A 186 ? ASP A 1966 SER A 1977 1 ? 12 
HELX_P HELX_P4  AA4 ASP A 197 ? ASP A 206 ? ASP A 1988 ASP A 1997 1 ? 10 
HELX_P HELX_P5  AA5 THR A 213 ? LEU A 222 ? THR A 2004 LEU A 2013 1 ? 10 
HELX_P HELX_P6  AA6 GLU A 225 ? GLU A 230 ? GLU A 2016 GLU A 2021 5 ? 6  
HELX_P HELX_P7  AA7 MET A 232 ? GLY A 237 ? MET A 2023 GLY A 2028 5 ? 6  
HELX_P HELX_P8  AA8 SER A 250 ? ASN A 277 ? SER A 2041 ASN A 2068 1 ? 28 
HELX_P HELX_P9  AA9 LEU A 278 ? LYS A 284 ? LEU A 2069 LYS A 2075 1 ? 7  
HELX_P HELX_P10 AB1 VAL A 285 ? GLY A 300 ? VAL A 2076 GLY A 2091 1 ? 16 
HELX_P HELX_P11 AB2 THR A 305 ? GLY A 331 ? THR A 2096 GLY A 2122 1 ? 27 
HELX_P HELX_P12 AB3 SER A 338 ? LEU A 348 ? SER A 2129 LEU A 2139 1 ? 11 
HELX_P HELX_P13 AB4 SER A 389 ? ALA A 398 ? SER A 2180 ALA A 2189 1 ? 10 
HELX_P HELX_P14 AB5 HIS A 400 ? VAL A 419 ? HIS A 2191 VAL A 2210 1 ? 20 
HELX_P HELX_P15 AB6 VAL A 419 ? GLU A 426 ? VAL A 2210 GLU A 2217 1 ? 8  
HELX_P HELX_P16 AB7 SER A 522 ? PHE A 527 ? SER A 2313 PHE A 2318 5 ? 6  
HELX_P HELX_P17 AB8 GLN A 542 ? HIS A 553 ? GLN A 2333 HIS A 2344 1 ? 12 
HELX_P HELX_P18 AB9 ASP A 554 ? THR A 563 ? ASP A 2345 THR A 2354 1 ? 10 
HELX_P HELX_P19 AC1 ASP A 566 ? MET A 577 ? ASP A 2357 MET A 2368 1 ? 12 
HELX_P HELX_P20 AC2 GLU A 579 ? VAL A 583 ? GLU A 2370 VAL A 2374 5 ? 5  
HELX_P HELX_P21 AC3 GLY A 584 ? GLY A 601 ? GLY A 2375 GLY A 2392 1 ? 18 
HELX_P HELX_P22 AC4 GLY A 603 ? GLY A 612 ? GLY A 2394 GLY A 2403 1 ? 10 
HELX_P HELX_P23 AC5 LYS A 614 ? TYR A 629 ? LYS A 2405 TYR A 2420 1 ? 16 
HELX_P HELX_P24 AC6 TYR A 629 ? GLY A 647 ? TYR A 2420 GLY A 2438 1 ? 19 
HELX_P HELX_P25 AC7 PRO A 660 ? ASP A 664 ? PRO A 2451 ASP A 2455 5 ? 5  
HELX_P HELX_P26 AC8 ASN A 666 ? PHE A 704 ? ASN A 2457 PHE A 2495 1 ? 39 
HELX_P HELX_P27 AC9 SER A 710 ? GLU A 715 ? SER A 2501 GLU A 2506 1 ? 6  
HELX_P HELX_P28 AD1 ASP A 759 ? MET A 771 ? ASP A 2550 MET A 2562 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? B DG  19  "O3'" ? ? ? 1_555 B DOC 20 P  ? ? C DG  19   C DOC 20   1_555 ? ? ? ? ? ? ?            1.558 ? ? 
metalc1  metalc ?    ? A ASP 539 OD1   ? ? ? 1_555 E MG  .  MG ? ? A ASP 2330 A MG  2602 1_555 ? ? ? ? ? ? ?            2.072 ? ? 
metalc2  metalc ?    ? D TTP .   O2A   ? ? ? 1_555 E MG  .  MG ? ? A TTP 2601 A MG  2602 1_555 ? ? ? ? ? ? ?            2.039 ? ? 
hydrog1  hydrog ?    ? B DC  15  N3    ? ? ? 1_555 C DG  15 N1 ? ? C DC  15   D DG  15   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog2  hydrog ?    ? B DC  15  N4    ? ? ? 1_555 C DG  15 O6 ? ? C DC  15   D DG  15   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog3  hydrog ?    ? B DC  15  O2    ? ? ? 1_555 C DG  15 N2 ? ? C DC  15   D DG  15   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog4  hydrog ?    ? B DG  16  N1    ? ? ? 1_555 C DC  14 N3 ? ? C DG  16   D DC  14   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog5  hydrog ?    ? B DG  16  N2    ? ? ? 1_555 C DC  14 O2 ? ? C DG  16   D DC  14   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog6  hydrog ?    ? B DG  16  O6    ? ? ? 1_555 C DC  14 N4 ? ? C DG  16   D DC  14   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog7  hydrog ?    ? B DT  17  N3    ? ? ? 1_555 C DA  13 N1 ? ? C DT  17   D DA  13   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog8  hydrog ?    ? B DT  17  O4    ? ? ? 1_555 C DA  13 N6 ? ? C DT  17   D DA  13   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog9  hydrog ?    ? B DA  18  N1    ? ? ? 1_555 C DT  12 N3 ? ? C DA  18   D DT  12   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog10 hydrog ?    ? B DA  18  N6    ? ? ? 1_555 C DT  12 O4 ? ? C DA  18   D DT  12   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog11 hydrog ?    ? B DG  19  N1    ? ? ? 1_555 C DC  11 N3 ? ? C DG  19   D DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog12 hydrog ?    ? B DG  19  N2    ? ? ? 1_555 C DC  11 O2 ? ? C DG  19   D DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog13 hydrog ?    ? B DG  19  O6    ? ? ? 1_555 C DC  11 N4 ? ? C DG  19   D DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog14 hydrog ?    ? B DOC 20  N3    ? ? ? 1_555 C DG  10 N1 ? ? C DOC 20   D DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog15 hydrog ?    ? B DOC 20  N4    ? ? ? 1_555 C DG  10 O6 ? ? C DOC 20   D DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
hydrog16 hydrog ?    ? B DOC 20  O2    ? ? ? 1_555 C DG  10 N2 ? ? C DOC 20   D DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
hydrog ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OD1 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   ASP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    539 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    ASP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     2330 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     2602 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O2A 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   D 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   TTP 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    TTP 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     2601 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 103.0 
_pdbx_struct_conn_angle.value_esd             ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           455 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            2246 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    456 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     2247 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -8.70 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 35  ? ASP A 38  ? SER A 1826 ASP A 1829 
AA1 2 ASP A 120 ? SER A 125 ? ASP A 1911 SER A 1916 
AA1 3 THR A 107 ? VAL A 114 ? THR A 1898 VAL A 1905 
AA1 4 LEU A 63  ? LYS A 67  ? LEU A 1854 LYS A 1858 
AA2 1 ARG A 58  ? PHE A 59  ? ARG A 1849 PHE A 1850 
AA2 2 SER A 170 ? VAL A 171 ? SER A 1961 VAL A 1962 
AA2 3 SER A 194 ? TYR A 195 ? SER A 1985 TYR A 1986 
AA3 1 ILE A 301 ? GLY A 302 ? ILE A 2092 GLY A 2093 
AA3 2 MET A 435 ? ILE A 438 ? MET A 2226 ILE A 2229 
AA3 3 CYS A 428 ? ASN A 430 ? CYS A 2219 ASN A 2221 
AA4 1 VAL A 441 ? GLN A 443 ? VAL A 2232 GLN A 2234 
AA4 2 THR A 452 ? THR A 454 ? THR A 2243 THR A 2245 
AA5 1 PHE A 743 ? GLN A 746 ? PHE A 2534 GLN A 2537 
AA5 2 GLU A 750 ? ALA A 756 ? GLU A 2541 ALA A 2547 
AA5 3 GLY A 533 ? TYR A 540 ? GLY A 2324 TYR A 2331 
AA5 4 VAL A 783 ? GLY A 788 ? VAL A 2574 GLY A 2579 
AA5 5 LYS A 795 ? ASP A 796 ? LYS A 2586 ASP A 2587 
AA6 1 PHE A 648 ? GLN A 650 ? PHE A 2439 GLN A 2441 
AA6 2 ARG A 656 ? TYR A 658 ? ARG A 2447 TYR A 2449 
# 
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 ILE A 37  ? N ILE A 1828 O ALA A 121 ? O ALA A 1912 
AA1 2 3 O TYR A 122 ? O TYR A 1913 N VAL A 114 ? N VAL A 1905 
AA1 3 4 O LEU A 108 ? O LEU A 1899 N GLU A 66  ? N GLU A 1857 
AA2 1 2 N PHE A 59  ? N PHE A 1850 O SER A 170 ? O SER A 1961 
AA2 2 3 N VAL A 171 ? N VAL A 1962 O SER A 194 ? O SER A 1985 
AA3 1 2 N ILE A 301 ? N ILE A 2092 O ILE A 438 ? O ILE A 2229 
AA3 2 3 O ARG A 437 ? O ARG A 2228 N CYS A 428 ? N CYS A 2219 
AA4 1 2 N VAL A 441 ? N VAL A 2232 O THR A 454 ? O THR A 2245 
AA5 1 2 N LEU A 745 ? N LEU A 2536 O LEU A 752 ? O LEU A 2543 
AA5 2 3 O VAL A 755 ? O VAL A 2546 N SER A 534 ? N SER A 2325 
AA5 3 4 N ASP A 539 ? N ASP A 2330 O LYS A 784 ? O LYS A 2575 
AA5 4 5 N ILE A 787 ? N ILE A 2578 O LYS A 795 ? O LYS A 2586 
AA6 1 2 N VAL A 649 ? N VAL A 2440 O ARG A 657 ? O ARG A 2448 
# 
_pdbx_entry_details.entry_id                   9AU8 
_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 ARG A 1886 ? ? 68.37   -2.90  
2 1 VAL A 1901 ? ? -126.49 -55.65 
3 1 LEU A 2013 ? ? -160.12 68.83  
4 1 PRO A 2018 ? ? -57.92  -8.80  
5 1 ALA A 2036 ? ? -99.44  38.34  
6 1 VAL A 2210 ? ? -125.75 -51.69 
7 1 GLU A 2246 ? ? 52.98   71.54  
8 1 HIS A 2539 ? ? 72.26   -11.40 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     2202 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.084 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9AU8 
_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                    9AU8 
_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                  3.44 
_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               92385 
_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            7.6 
# 
_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                 
'Ternary complex of human DNA polymerase theta polymerase domain with a mismatched T:T base pair' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2, 3' 
# 
_em_imaging.entry_id                        9AU8 
_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              9AU8 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   295 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9AU8 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLY 1792 ? A GLY 1   
2   1 Y 1 A PHE 1793 ? A PHE 2   
3   1 Y 1 A LYS 1794 ? A LYS 3   
4   1 Y 1 A ASP 1795 ? A ASP 4   
5   1 Y 1 A ASN 1796 ? A ASN 5   
6   1 Y 1 A SER 1797 ? A SER 6   
7   1 Y 1 A PRO 1798 ? A PRO 7   
8   1 Y 1 A ILE 1799 ? A ILE 8   
9   1 Y 1 A SER 1800 ? A SER 9   
10  1 Y 1 A ASP 1801 ? A ASP 10  
11  1 Y 1 A THR 1802 ? A THR 11  
12  1 Y 1 A SER 1803 ? A SER 12  
13  1 Y 1 A PHE 1804 ? A PHE 13  
14  1 Y 1 A SER 1805 ? A SER 14  
15  1 Y 1 A LEU 1806 ? A LEU 15  
16  1 Y 1 A GLN 1807 ? A GLN 16  
17  1 Y 1 A LEU 1808 ? A LEU 17  
18  1 Y 1 A SER 1809 ? A SER 18  
19  1 Y 1 A GLN 1810 ? A GLN 19  
20  1 Y 1 A ASP 1811 ? A ASP 20  
21  1 Y 1 A GLY 1812 ? A GLY 21  
22  1 Y 1 A LEU 1813 ? A LEU 22  
23  1 Y 1 A GLN 1814 ? A GLN 23  
24  1 Y 1 A LEU 1815 ? A LEU 24  
25  1 Y 1 A THR 1816 ? A THR 25  
26  1 Y 1 A PRO 1817 ? A PRO 26  
27  1 Y 1 A ALA 1818 ? A ALA 27  
28  1 Y 1 A SER 1819 ? A SER 28  
29  1 Y 1 A SER 1820 ? A SER 29  
30  1 Y 1 A SER 1821 ? A SER 30  
31  1 Y 1 A SER 1822 ? A SER 31  
32  1 Y 1 A GLU 1823 ? A GLU 32  
33  1 Y 1 A LEU 1862 ? A LEU 71  
34  1 Y 1 A THR 1863 ? A THR 72  
35  1 Y 1 A SER 1864 ? A SER 73  
36  1 Y 1 A SER 1865 ? A SER 74  
37  1 Y 1 A LYS 1866 ? A LYS 75  
38  1 Y 1 A THR 1867 ? A THR 76  
39  1 Y 1 A ALA 1868 ? A ALA 77  
40  1 Y 1 A THR 1869 ? A THR 78  
41  1 Y 1 A ILE 1870 ? A ILE 79  
42  1 Y 1 A GLY 1871 ? A GLY 80  
43  1 Y 1 A SER 1872 ? A SER 81  
44  1 Y 1 A ARG 1873 ? A ARG 82  
45  1 Y 1 A PHE 1874 ? A PHE 83  
46  1 Y 1 A LYS 1875 ? A LYS 84  
47  1 Y 1 A GLN 1876 ? A GLN 85  
48  1 Y 1 A ALA 1877 ? A ALA 86  
49  1 Y 1 A SER 1878 ? A SER 87  
50  1 Y 1 A SER 1879 ? A SER 88  
51  1 Y 1 A PRO 1880 ? A PRO 89  
52  1 Y 1 A GLN 1881 ? A GLN 90  
53  1 Y 1 A GLU 1882 ? A GLU 91  
54  1 Y 1 A ILE 1883 ? A ILE 92  
55  1 Y 1 A PRO 1884 ? A PRO 93  
56  1 Y 1 A GLN 1921 ? A GLN 130 
57  1 Y 1 A LYS 1922 ? A LYS 131 
58  1 Y 1 A HIS 1923 ? A HIS 132 
59  1 Y 1 A SER 1924 ? A SER 133 
60  1 Y 1 A GLU 1925 ? A GLU 134 
61  1 Y 1 A ILE 1926 ? A ILE 135 
62  1 Y 1 A SER 1927 ? A SER 136 
63  1 Y 1 A ALA 1928 ? A ALA 137 
64  1 Y 1 A SER 1929 ? A SER 138 
65  1 Y 1 A LEU 1930 ? A LEU 139 
66  1 Y 1 A VAL 1931 ? A VAL 140 
67  1 Y 1 A PRO 1932 ? A PRO 141 
68  1 Y 1 A PRO 1933 ? A PRO 142 
69  1 Y 1 A SER 1934 ? A SER 143 
70  1 Y 1 A LEU 1935 ? A LEU 144 
71  1 Y 1 A MET 2149 ? A MET 358 
72  1 Y 1 A LYS 2150 ? A LYS 359 
73  1 Y 1 A ASN 2151 ? A ASN 360 
74  1 Y 1 A GLN 2152 ? A GLN 361 
75  1 Y 1 A GLY 2153 ? A GLY 362 
76  1 Y 1 A SER 2154 ? A SER 363 
77  1 Y 1 A LYS 2155 ? A LYS 364 
78  1 Y 1 A LYS 2156 ? A LYS 365 
79  1 Y 1 A THR 2157 ? A THR 366 
80  1 Y 1 A LEU 2158 ? A LEU 367 
81  1 Y 1 A GLY 2159 ? A GLY 368 
82  1 Y 1 A SER 2160 ? A SER 369 
83  1 Y 1 A THR 2161 ? A THR 370 
84  1 Y 1 A ARG 2162 ? A ARG 371 
85  1 Y 1 A ARG 2163 ? A ARG 372 
86  1 Y 1 A GLY 2164 ? A GLY 373 
87  1 Y 1 A ILE 2165 ? A ILE 374 
88  1 Y 1 A ASP 2166 ? A ASP 375 
89  1 Y 1 A ASN 2167 ? A ASN 376 
90  1 Y 1 A GLY 2168 ? A GLY 377 
91  1 Y 1 A ARG 2169 ? A ARG 378 
92  1 Y 1 A LYS 2170 ? A LYS 379 
93  1 Y 1 A LEU 2171 ? A LEU 380 
94  1 Y 1 A ARG 2172 ? A ARG 381 
95  1 Y 1 A LEU 2173 ? A LEU 382 
96  1 Y 1 A THR 2262 ? A THR 471 
97  1 Y 1 A LEU 2263 ? A LEU 472 
98  1 Y 1 A VAL 2264 ? A VAL 473 
99  1 Y 1 A GLY 2265 ? A GLY 474 
100 1 Y 1 A GLU 2266 ? A GLU 475 
101 1 Y 1 A SER 2267 ? A SER 476 
102 1 Y 1 A PRO 2268 ? A PRO 477 
103 1 Y 1 A PRO 2269 ? A PRO 478 
104 1 Y 1 A SER 2270 ? A SER 479 
105 1 Y 1 A GLN 2271 ? A GLN 480 
106 1 Y 1 A ALA 2272 ? A ALA 481 
107 1 Y 1 A VAL 2273 ? A VAL 482 
108 1 Y 1 A GLY 2274 ? A GLY 483 
109 1 Y 1 A LYS 2275 ? A LYS 484 
110 1 Y 1 A GLY 2276 ? A GLY 485 
111 1 Y 1 A LEU 2277 ? A LEU 486 
112 1 Y 1 A LEU 2278 ? A LEU 487 
113 1 Y 1 A PRO 2279 ? A PRO 488 
114 1 Y 1 A MET 2280 ? A MET 489 
115 1 Y 1 A GLY 2281 ? A GLY 490 
116 1 Y 1 A ARG 2282 ? A ARG 491 
117 1 Y 1 A GLY 2283 ? A GLY 492 
118 1 Y 1 A LYS 2284 ? A LYS 493 
119 1 Y 1 A TYR 2285 ? A TYR 494 
120 1 Y 1 A LYS 2286 ? A LYS 495 
121 1 Y 1 A LYS 2287 ? A LYS 496 
122 1 Y 1 A GLY 2288 ? A GLY 497 
123 1 Y 1 A PHE 2289 ? A PHE 498 
124 1 Y 1 A SER 2290 ? A SER 499 
125 1 Y 1 A VAL 2291 ? A VAL 500 
126 1 Y 1 A ASN 2292 ? A ASN 501 
127 1 Y 1 A PRO 2293 ? A PRO 502 
128 1 Y 1 A ARG 2294 ? A ARG 503 
129 1 Y 1 A CYS 2295 ? A CYS 504 
130 1 Y 1 A GLN 2296 ? A GLN 505 
131 1 Y 1 A ALA 2297 ? A ALA 506 
132 1 Y 1 A GLN 2298 ? A GLN 507 
133 1 Y 1 A MET 2299 ? A MET 508 
134 1 Y 1 A GLU 2300 ? A GLU 509 
135 1 Y 1 A GLU 2301 ? A GLU 510 
136 1 Y 1 A ARG 2302 ? A ARG 511 
137 1 Y 1 A ALA 2303 ? A ALA 512 
138 1 Y 1 A ALA 2304 ? A ALA 513 
139 1 Y 1 A ASP 2305 ? A ASP 514 
140 1 Y 1 A ARG 2306 ? A ARG 515 
141 1 Y 1 A GLY 2307 ? A GLY 516 
142 1 Y 1 A LEU 2509 ? A LEU 718 
143 1 Y 1 A GLN 2510 ? A GLN 719 
144 1 Y 1 A SER 2511 ? A SER 720 
145 1 Y 1 A ASP 2512 ? A ASP 721 
146 1 Y 1 A GLN 2513 ? A GLN 722 
147 1 Y 1 A THR 2514 ? A THR 723 
148 1 Y 1 A GLY 2515 ? A GLY 724 
149 1 Y 1 A LEU 2516 ? A LEU 725 
150 1 Y 1 A SER 2517 ? A SER 726 
151 1 Y 1 A ARG 2518 ? A ARG 727 
152 1 Y 1 A LYS 2519 ? A LYS 728 
153 1 Y 1 A ARG 2520 ? A ARG 729 
154 1 Y 1 A LYS 2521 ? A LYS 730 
155 1 Y 1 A LEU 2522 ? A LEU 731 
156 1 Y 1 A GLN 2523 ? A GLN 732 
157 1 Y 1 A GLY 2524 ? A GLY 733 
158 1 Y 1 A MET 2525 ? A MET 734 
159 1 Y 1 C DT  1    ? B DT  1   
160 1 Y 1 C DG  2    ? B DG  2   
161 1 Y 1 C DC  3    ? B DC  3   
162 1 Y 1 C DT  4    ? B DT  4   
163 1 Y 1 C DG  5    ? B DG  5   
164 1 Y 1 C DT  6    ? B DT  6   
165 1 Y 1 C DG  7    ? B DG  7   
166 1 Y 1 C DA  8    ? B DA  8   
167 1 Y 1 C DG  9    ? B DG  9   
168 1 Y 1 C DG  10   ? B DG  10  
169 1 Y 1 C DC  11   ? B DC  11  
170 1 Y 1 C DA  12   ? B DA  12  
171 1 Y 1 C DT  13   ? B DT  13  
172 1 Y 1 C DC  14   ? B DC  14  
173 1 Y 1 D DG  1    ? C DG  1   
174 1 Y 1 D DC  2    ? C DC  2   
175 1 Y 1 D DA  3    ? C DA  3   
176 1 Y 1 D DG  4    ? C DG  4   
177 1 Y 1 D DT  5    ? C DT  5   
178 1 Y 1 D DC  6    ? C DC  6   
179 1 Y 1 D DG  16   ? C DG  16  
180 1 Y 1 D DA  17   ? C DA  17  
181 1 Y 1 D DT  18   ? C DT  18  
182 1 Y 1 D DG  19   ? C DG  19  
183 1 Y 1 D DC  20   ? C DC  20  
184 1 Y 1 D DC  21   ? C DC  21  
185 1 Y 1 D DT  22   ? C DT  22  
186 1 Y 1 D DC  23   ? C DC  23  
187 1 Y 1 D DA  24   ? C DA  24  
188 1 Y 1 D DC  25   ? C DC  25  
189 1 Y 1 D DA  26   ? C DA  26  
190 1 Y 1 D DG  27   ? C DG  27  
191 1 Y 1 D DC  28   ? C DC  28  
192 1 Y 1 D DA  29   ? C DA  29  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
DA  OP3    O  N N 88  
DA  P      P  N N 89  
DA  OP1    O  N N 90  
DA  OP2    O  N N 91  
DA  "O5'"  O  N N 92  
DA  "C5'"  C  N N 93  
DA  "C4'"  C  N R 94  
DA  "O4'"  O  N N 95  
DA  "C3'"  C  N S 96  
DA  "O3'"  O  N N 97  
DA  "C2'"  C  N N 98  
DA  "C1'"  C  N R 99  
DA  N9     N  Y N 100 
DA  C8     C  Y N 101 
DA  N7     N  Y N 102 
DA  C5     C  Y N 103 
DA  C6     C  Y N 104 
DA  N6     N  N N 105 
DA  N1     N  Y N 106 
DA  C2     C  Y N 107 
DA  N3     N  Y N 108 
DA  C4     C  Y N 109 
DA  HOP3   H  N N 110 
DA  HOP2   H  N N 111 
DA  "H5'"  H  N N 112 
DA  "H5''" H  N N 113 
DA  "H4'"  H  N N 114 
DA  "H3'"  H  N N 115 
DA  "HO3'" H  N N 116 
DA  "H2'"  H  N N 117 
DA  "H2''" H  N N 118 
DA  "H1'"  H  N N 119 
DA  H8     H  N N 120 
DA  H61    H  N N 121 
DA  H62    H  N N 122 
DA  H2     H  N N 123 
DC  OP3    O  N N 124 
DC  P      P  N N 125 
DC  OP1    O  N N 126 
DC  OP2    O  N N 127 
DC  "O5'"  O  N N 128 
DC  "C5'"  C  N N 129 
DC  "C4'"  C  N R 130 
DC  "O4'"  O  N N 131 
DC  "C3'"  C  N S 132 
DC  "O3'"  O  N N 133 
DC  "C2'"  C  N N 134 
DC  "C1'"  C  N R 135 
DC  N1     N  N N 136 
DC  C2     C  N N 137 
DC  O2     O  N N 138 
DC  N3     N  N N 139 
DC  C4     C  N N 140 
DC  N4     N  N N 141 
DC  C5     C  N N 142 
DC  C6     C  N N 143 
DC  HOP3   H  N N 144 
DC  HOP2   H  N N 145 
DC  "H5'"  H  N N 146 
DC  "H5''" H  N N 147 
DC  "H4'"  H  N N 148 
DC  "H3'"  H  N N 149 
DC  "HO3'" H  N N 150 
DC  "H2'"  H  N N 151 
DC  "H2''" H  N N 152 
DC  "H1'"  H  N N 153 
DC  H41    H  N N 154 
DC  H42    H  N N 155 
DC  H5     H  N N 156 
DC  H6     H  N N 157 
DG  OP3    O  N N 158 
DG  P      P  N N 159 
DG  OP1    O  N N 160 
DG  OP2    O  N N 161 
DG  "O5'"  O  N N 162 
DG  "C5'"  C  N N 163 
DG  "C4'"  C  N R 164 
DG  "O4'"  O  N N 165 
DG  "C3'"  C  N S 166 
DG  "O3'"  O  N N 167 
DG  "C2'"  C  N N 168 
DG  "C1'"  C  N R 169 
DG  N9     N  Y N 170 
DG  C8     C  Y N 171 
DG  N7     N  Y N 172 
DG  C5     C  Y N 173 
DG  C6     C  N N 174 
DG  O6     O  N N 175 
DG  N1     N  N N 176 
DG  C2     C  N N 177 
DG  N2     N  N N 178 
DG  N3     N  N N 179 
DG  C4     C  Y N 180 
DG  HOP3   H  N N 181 
DG  HOP2   H  N N 182 
DG  "H5'"  H  N N 183 
DG  "H5''" H  N N 184 
DG  "H4'"  H  N N 185 
DG  "H3'"  H  N N 186 
DG  "HO3'" H  N N 187 
DG  "H2'"  H  N N 188 
DG  "H2''" H  N N 189 
DG  "H1'"  H  N N 190 
DG  H8     H  N N 191 
DG  H1     H  N N 192 
DG  H21    H  N N 193 
DG  H22    H  N N 194 
DOC N1     N  N N 195 
DOC C2     C  N N 196 
DOC N3     N  N N 197 
DOC C4     C  N N 198 
DOC C5     C  N N 199 
DOC C6     C  N N 200 
DOC O2     O  N N 201 
DOC N4     N  N N 202 
DOC "C1'"  C  N R 203 
DOC "C2'"  C  N N 204 
DOC "C3'"  C  N N 205 
DOC "C4'"  C  N S 206 
DOC "O4'"  O  N N 207 
DOC "C5'"  C  N N 208 
DOC "O5'"  O  N N 209 
DOC P      P  N N 210 
DOC OP1    O  N N 211 
DOC OP2    O  N N 212 
DOC OP3    O  N N 213 
DOC H5     H  N N 214 
DOC H6     H  N N 215 
DOC HN41   H  N N 216 
DOC HN42   H  N N 217 
DOC "H1'"  H  N N 218 
DOC "H2'"  H  N N 219 
DOC "H2''" H  N N 220 
DOC "H3'1" H  N N 221 
DOC "H3'2" H  N N 222 
DOC "H4'"  H  N N 223 
DOC "H5'"  H  N N 224 
DOC "H5''" H  N N 225 
DOC HOP2   H  N N 226 
DOC HOP3   H  N N 227 
DT  OP3    O  N N 228 
DT  P      P  N N 229 
DT  OP1    O  N N 230 
DT  OP2    O  N N 231 
DT  "O5'"  O  N N 232 
DT  "C5'"  C  N N 233 
DT  "C4'"  C  N R 234 
DT  "O4'"  O  N N 235 
DT  "C3'"  C  N S 236 
DT  "O3'"  O  N N 237 
DT  "C2'"  C  N N 238 
DT  "C1'"  C  N R 239 
DT  N1     N  N N 240 
DT  C2     C  N N 241 
DT  O2     O  N N 242 
DT  N3     N  N N 243 
DT  C4     C  N N 244 
DT  O4     O  N N 245 
DT  C5     C  N N 246 
DT  C7     C  N N 247 
DT  C6     C  N N 248 
DT  HOP3   H  N N 249 
DT  HOP2   H  N N 250 
DT  "H5'"  H  N N 251 
DT  "H5''" H  N N 252 
DT  "H4'"  H  N N 253 
DT  "H3'"  H  N N 254 
DT  "HO3'" H  N N 255 
DT  "H2'"  H  N N 256 
DT  "H2''" H  N N 257 
DT  "H1'"  H  N N 258 
DT  H3     H  N N 259 
DT  H71    H  N N 260 
DT  H72    H  N N 261 
DT  H73    H  N N 262 
DT  H6     H  N N 263 
GLN N      N  N N 264 
GLN CA     C  N S 265 
GLN C      C  N N 266 
GLN O      O  N N 267 
GLN CB     C  N N 268 
GLN CG     C  N N 269 
GLN CD     C  N N 270 
GLN OE1    O  N N 271 
GLN NE2    N  N N 272 
GLN OXT    O  N N 273 
GLN H      H  N N 274 
GLN H2     H  N N 275 
GLN HA     H  N N 276 
GLN HB2    H  N N 277 
GLN HB3    H  N N 278 
GLN HG2    H  N N 279 
GLN HG3    H  N N 280 
GLN HE21   H  N N 281 
GLN HE22   H  N N 282 
GLN HXT    H  N N 283 
GLU N      N  N N 284 
GLU CA     C  N S 285 
GLU C      C  N N 286 
GLU O      O  N N 287 
GLU CB     C  N N 288 
GLU CG     C  N N 289 
GLU CD     C  N N 290 
GLU OE1    O  N N 291 
GLU OE2    O  N N 292 
GLU OXT    O  N N 293 
GLU H      H  N N 294 
GLU H2     H  N N 295 
GLU HA     H  N N 296 
GLU HB2    H  N N 297 
GLU HB3    H  N N 298 
GLU HG2    H  N N 299 
GLU HG3    H  N N 300 
GLU HE2    H  N N 301 
GLU HXT    H  N N 302 
GLY N      N  N N 303 
GLY CA     C  N N 304 
GLY C      C  N N 305 
GLY O      O  N N 306 
GLY OXT    O  N N 307 
GLY H      H  N N 308 
GLY H2     H  N N 309 
GLY HA2    H  N N 310 
GLY HA3    H  N N 311 
GLY HXT    H  N N 312 
HIS N      N  N N 313 
HIS CA     C  N S 314 
HIS C      C  N N 315 
HIS O      O  N N 316 
HIS CB     C  N N 317 
HIS CG     C  Y N 318 
HIS ND1    N  Y N 319 
HIS CD2    C  Y N 320 
HIS CE1    C  Y N 321 
HIS NE2    N  Y N 322 
HIS OXT    O  N N 323 
HIS H      H  N N 324 
HIS H2     H  N N 325 
HIS HA     H  N N 326 
HIS HB2    H  N N 327 
HIS HB3    H  N N 328 
HIS HD1    H  N N 329 
HIS HD2    H  N N 330 
HIS HE1    H  N N 331 
HIS HE2    H  N N 332 
HIS HXT    H  N N 333 
ILE N      N  N N 334 
ILE CA     C  N S 335 
ILE C      C  N N 336 
ILE O      O  N N 337 
ILE CB     C  N S 338 
ILE CG1    C  N N 339 
ILE CG2    C  N N 340 
ILE CD1    C  N N 341 
ILE OXT    O  N N 342 
ILE H      H  N N 343 
ILE H2     H  N N 344 
ILE HA     H  N N 345 
ILE HB     H  N N 346 
ILE HG12   H  N N 347 
ILE HG13   H  N N 348 
ILE HG21   H  N N 349 
ILE HG22   H  N N 350 
ILE HG23   H  N N 351 
ILE HD11   H  N N 352 
ILE HD12   H  N N 353 
ILE HD13   H  N N 354 
ILE HXT    H  N N 355 
LEU N      N  N N 356 
LEU CA     C  N S 357 
LEU C      C  N N 358 
LEU O      O  N N 359 
LEU CB     C  N N 360 
LEU CG     C  N N 361 
LEU CD1    C  N N 362 
LEU CD2    C  N N 363 
LEU OXT    O  N N 364 
LEU H      H  N N 365 
LEU H2     H  N N 366 
LEU HA     H  N N 367 
LEU HB2    H  N N 368 
LEU HB3    H  N N 369 
LEU HG     H  N N 370 
LEU HD11   H  N N 371 
LEU HD12   H  N N 372 
LEU HD13   H  N N 373 
LEU HD21   H  N N 374 
LEU HD22   H  N N 375 
LEU HD23   H  N N 376 
LEU HXT    H  N N 377 
LYS N      N  N N 378 
LYS CA     C  N S 379 
LYS C      C  N N 380 
LYS O      O  N N 381 
LYS CB     C  N N 382 
LYS CG     C  N N 383 
LYS CD     C  N N 384 
LYS CE     C  N N 385 
LYS NZ     N  N N 386 
LYS OXT    O  N N 387 
LYS H      H  N N 388 
LYS H2     H  N N 389 
LYS HA     H  N N 390 
LYS HB2    H  N N 391 
LYS HB3    H  N N 392 
LYS HG2    H  N N 393 
LYS HG3    H  N N 394 
LYS HD2    H  N N 395 
LYS HD3    H  N N 396 
LYS HE2    H  N N 397 
LYS HE3    H  N N 398 
LYS HZ1    H  N N 399 
LYS HZ2    H  N N 400 
LYS HZ3    H  N N 401 
LYS HXT    H  N N 402 
MET N      N  N N 403 
MET CA     C  N S 404 
MET C      C  N N 405 
MET O      O  N N 406 
MET CB     C  N N 407 
MET CG     C  N N 408 
MET SD     S  N N 409 
MET CE     C  N N 410 
MET OXT    O  N N 411 
MET H      H  N N 412 
MET H2     H  N N 413 
MET HA     H  N N 414 
MET HB2    H  N N 415 
MET HB3    H  N N 416 
MET HG2    H  N N 417 
MET HG3    H  N N 418 
MET HE1    H  N N 419 
MET HE2    H  N N 420 
MET HE3    H  N N 421 
MET HXT    H  N N 422 
MG  MG     MG N N 423 
PHE N      N  N N 424 
PHE CA     C  N S 425 
PHE C      C  N N 426 
PHE O      O  N N 427 
PHE CB     C  N N 428 
PHE CG     C  Y N 429 
PHE CD1    C  Y N 430 
PHE CD2    C  Y N 431 
PHE CE1    C  Y N 432 
PHE CE2    C  Y N 433 
PHE CZ     C  Y N 434 
PHE OXT    O  N N 435 
PHE H      H  N N 436 
PHE H2     H  N N 437 
PHE HA     H  N N 438 
PHE HB2    H  N N 439 
PHE HB3    H  N N 440 
PHE HD1    H  N N 441 
PHE HD2    H  N N 442 
PHE HE1    H  N N 443 
PHE HE2    H  N N 444 
PHE HZ     H  N N 445 
PHE HXT    H  N N 446 
PRO N      N  N N 447 
PRO CA     C  N S 448 
PRO C      C  N N 449 
PRO O      O  N N 450 
PRO CB     C  N N 451 
PRO CG     C  N N 452 
PRO CD     C  N N 453 
PRO OXT    O  N N 454 
PRO H      H  N N 455 
PRO HA     H  N N 456 
PRO HB2    H  N N 457 
PRO HB3    H  N N 458 
PRO HG2    H  N N 459 
PRO HG3    H  N N 460 
PRO HD2    H  N N 461 
PRO HD3    H  N N 462 
PRO HXT    H  N N 463 
SER N      N  N N 464 
SER CA     C  N S 465 
SER C      C  N N 466 
SER O      O  N N 467 
SER CB     C  N N 468 
SER OG     O  N N 469 
SER OXT    O  N N 470 
SER H      H  N N 471 
SER H2     H  N N 472 
SER HA     H  N N 473 
SER HB2    H  N N 474 
SER HB3    H  N N 475 
SER HG     H  N N 476 
SER HXT    H  N N 477 
THR N      N  N N 478 
THR CA     C  N S 479 
THR C      C  N N 480 
THR O      O  N N 481 
THR CB     C  N R 482 
THR OG1    O  N N 483 
THR CG2    C  N N 484 
THR OXT    O  N N 485 
THR H      H  N N 486 
THR H2     H  N N 487 
THR HA     H  N N 488 
THR HB     H  N N 489 
THR HG1    H  N N 490 
THR HG21   H  N N 491 
THR HG22   H  N N 492 
THR HG23   H  N N 493 
THR HXT    H  N N 494 
TRP N      N  N N 495 
TRP CA     C  N S 496 
TRP C      C  N N 497 
TRP O      O  N N 498 
TRP CB     C  N N 499 
TRP CG     C  Y N 500 
TRP CD1    C  Y N 501 
TRP CD2    C  Y N 502 
TRP NE1    N  Y N 503 
TRP CE2    C  Y N 504 
TRP CE3    C  Y N 505 
TRP CZ2    C  Y N 506 
TRP CZ3    C  Y N 507 
TRP CH2    C  Y N 508 
TRP OXT    O  N N 509 
TRP H      H  N N 510 
TRP H2     H  N N 511 
TRP HA     H  N N 512 
TRP HB2    H  N N 513 
TRP HB3    H  N N 514 
TRP HD1    H  N N 515 
TRP HE1    H  N N 516 
TRP HE3    H  N N 517 
TRP HZ2    H  N N 518 
TRP HZ3    H  N N 519 
TRP HH2    H  N N 520 
TRP HXT    H  N N 521 
TTP PA     P  N S 522 
TTP O1A    O  N N 523 
TTP O2A    O  N N 524 
TTP O3A    O  N N 525 
TTP PB     P  N S 526 
TTP O1B    O  N N 527 
TTP O2B    O  N N 528 
TTP O3B    O  N N 529 
TTP PG     P  N N 530 
TTP O1G    O  N N 531 
TTP O2G    O  N N 532 
TTP O3G    O  N N 533 
TTP "O5'"  O  N N 534 
TTP "C5'"  C  N N 535 
TTP "C4'"  C  N R 536 
TTP "O4'"  O  N N 537 
TTP "C3'"  C  N S 538 
TTP "O3'"  O  N N 539 
TTP "C2'"  C  N N 540 
TTP "C1'"  C  N R 541 
TTP N1     N  N N 542 
TTP C2     C  N N 543 
TTP O2     O  N N 544 
TTP N3     N  N N 545 
TTP C4     C  N N 546 
TTP O4     O  N N 547 
TTP C5     C  N N 548 
TTP C5M    C  N N 549 
TTP C6     C  N N 550 
TTP HOA2   H  N N 551 
TTP HOB2   H  N N 552 
TTP HOG2   H  N N 553 
TTP HOG3   H  N N 554 
TTP "H5'1" H  N N 555 
TTP "H5'2" H  N N 556 
TTP "H4'"  H  N N 557 
TTP "H3'"  H  N N 558 
TTP "HO3'" H  N N 559 
TTP "H2'1" H  N N 560 
TTP "H2'2" H  N N 561 
TTP "H1'"  H  N N 562 
TTP HN3    H  N N 563 
TTP HM51   H  N N 564 
TTP HM52   H  N N 565 
TTP HM53   H  N N 566 
TTP H6     H  N N 567 
TYR N      N  N N 568 
TYR CA     C  N S 569 
TYR C      C  N N 570 
TYR O      O  N N 571 
TYR CB     C  N N 572 
TYR CG     C  Y N 573 
TYR CD1    C  Y N 574 
TYR CD2    C  Y N 575 
TYR CE1    C  Y N 576 
TYR CE2    C  Y N 577 
TYR CZ     C  Y N 578 
TYR OH     O  N N 579 
TYR OXT    O  N N 580 
TYR H      H  N N 581 
TYR H2     H  N N 582 
TYR HA     H  N N 583 
TYR HB2    H  N N 584 
TYR HB3    H  N N 585 
TYR HD1    H  N N 586 
TYR HD2    H  N N 587 
TYR HE1    H  N N 588 
TYR HE2    H  N N 589 
TYR HH     H  N N 590 
TYR HXT    H  N N 591 
VAL N      N  N N 592 
VAL CA     C  N S 593 
VAL C      C  N N 594 
VAL O      O  N N 595 
VAL CB     C  N N 596 
VAL CG1    C  N N 597 
VAL CG2    C  N N 598 
VAL OXT    O  N N 599 
VAL H      H  N N 600 
VAL H2     H  N N 601 
VAL HA     H  N N 602 
VAL HB     H  N N 603 
VAL HG11   H  N N 604 
VAL HG12   H  N N 605 
VAL HG13   H  N N 606 
VAL HG21   H  N N 607 
VAL HG22   H  N N 608 
VAL HG23   H  N N 609 
VAL HXT    H  N N 610 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
DA  OP3   P      sing N N 83  
DA  OP3   HOP3   sing N N 84  
DA  P     OP1    doub N N 85  
DA  P     OP2    sing N N 86  
DA  P     "O5'"  sing N N 87  
DA  OP2   HOP2   sing N N 88  
DA  "O5'" "C5'"  sing N N 89  
DA  "C5'" "C4'"  sing N N 90  
DA  "C5'" "H5'"  sing N N 91  
DA  "C5'" "H5''" sing N N 92  
DA  "C4'" "O4'"  sing N N 93  
DA  "C4'" "C3'"  sing N N 94  
DA  "C4'" "H4'"  sing N N 95  
DA  "O4'" "C1'"  sing N N 96  
DA  "C3'" "O3'"  sing N N 97  
DA  "C3'" "C2'"  sing N N 98  
DA  "C3'" "H3'"  sing N N 99  
DA  "O3'" "HO3'" sing N N 100 
DA  "C2'" "C1'"  sing N N 101 
DA  "C2'" "H2'"  sing N N 102 
DA  "C2'" "H2''" sing N N 103 
DA  "C1'" N9     sing N N 104 
DA  "C1'" "H1'"  sing N N 105 
DA  N9    C8     sing Y N 106 
DA  N9    C4     sing Y N 107 
DA  C8    N7     doub Y N 108 
DA  C8    H8     sing N N 109 
DA  N7    C5     sing Y N 110 
DA  C5    C6     sing Y N 111 
DA  C5    C4     doub Y N 112 
DA  C6    N6     sing N N 113 
DA  C6    N1     doub Y N 114 
DA  N6    H61    sing N N 115 
DA  N6    H62    sing N N 116 
DA  N1    C2     sing Y N 117 
DA  C2    N3     doub Y N 118 
DA  C2    H2     sing N N 119 
DA  N3    C4     sing Y N 120 
DC  OP3   P      sing N N 121 
DC  OP3   HOP3   sing N N 122 
DC  P     OP1    doub N N 123 
DC  P     OP2    sing N N 124 
DC  P     "O5'"  sing N N 125 
DC  OP2   HOP2   sing N N 126 
DC  "O5'" "C5'"  sing N N 127 
DC  "C5'" "C4'"  sing N N 128 
DC  "C5'" "H5'"  sing N N 129 
DC  "C5'" "H5''" sing N N 130 
DC  "C4'" "O4'"  sing N N 131 
DC  "C4'" "C3'"  sing N N 132 
DC  "C4'" "H4'"  sing N N 133 
DC  "O4'" "C1'"  sing N N 134 
DC  "C3'" "O3'"  sing N N 135 
DC  "C3'" "C2'"  sing N N 136 
DC  "C3'" "H3'"  sing N N 137 
DC  "O3'" "HO3'" sing N N 138 
DC  "C2'" "C1'"  sing N N 139 
DC  "C2'" "H2'"  sing N N 140 
DC  "C2'" "H2''" sing N N 141 
DC  "C1'" N1     sing N N 142 
DC  "C1'" "H1'"  sing N N 143 
DC  N1    C2     sing N N 144 
DC  N1    C6     sing N N 145 
DC  C2    O2     doub N N 146 
DC  C2    N3     sing N N 147 
DC  N3    C4     doub N N 148 
DC  C4    N4     sing N N 149 
DC  C4    C5     sing N N 150 
DC  N4    H41    sing N N 151 
DC  N4    H42    sing N N 152 
DC  C5    C6     doub N N 153 
DC  C5    H5     sing N N 154 
DC  C6    H6     sing N N 155 
DG  OP3   P      sing N N 156 
DG  OP3   HOP3   sing N N 157 
DG  P     OP1    doub N N 158 
DG  P     OP2    sing N N 159 
DG  P     "O5'"  sing N N 160 
DG  OP2   HOP2   sing N N 161 
DG  "O5'" "C5'"  sing N N 162 
DG  "C5'" "C4'"  sing N N 163 
DG  "C5'" "H5'"  sing N N 164 
DG  "C5'" "H5''" sing N N 165 
DG  "C4'" "O4'"  sing N N 166 
DG  "C4'" "C3'"  sing N N 167 
DG  "C4'" "H4'"  sing N N 168 
DG  "O4'" "C1'"  sing N N 169 
DG  "C3'" "O3'"  sing N N 170 
DG  "C3'" "C2'"  sing N N 171 
DG  "C3'" "H3'"  sing N N 172 
DG  "O3'" "HO3'" sing N N 173 
DG  "C2'" "C1'"  sing N N 174 
DG  "C2'" "H2'"  sing N N 175 
DG  "C2'" "H2''" sing N N 176 
DG  "C1'" N9     sing N N 177 
DG  "C1'" "H1'"  sing N N 178 
DG  N9    C8     sing Y N 179 
DG  N9    C4     sing Y N 180 
DG  C8    N7     doub Y N 181 
DG  C8    H8     sing N N 182 
DG  N7    C5     sing Y N 183 
DG  C5    C6     sing N N 184 
DG  C5    C4     doub Y N 185 
DG  C6    O6     doub N N 186 
DG  C6    N1     sing N N 187 
DG  N1    C2     sing N N 188 
DG  N1    H1     sing N N 189 
DG  C2    N2     sing N N 190 
DG  C2    N3     doub N N 191 
DG  N2    H21    sing N N 192 
DG  N2    H22    sing N N 193 
DG  N3    C4     sing N N 194 
DOC N1    C2     sing N N 195 
DOC N1    C6     sing N N 196 
DOC N1    "C1'"  sing N N 197 
DOC C2    N3     sing N N 198 
DOC C2    O2     doub N N 199 
DOC N3    C4     doub N N 200 
DOC C4    C5     sing N N 201 
DOC C4    N4     sing N N 202 
DOC C5    C6     doub N N 203 
DOC C5    H5     sing N N 204 
DOC C6    H6     sing N N 205 
DOC N4    HN41   sing N N 206 
DOC N4    HN42   sing N N 207 
DOC "C1'" "C2'"  sing N N 208 
DOC "C1'" "O4'"  sing N N 209 
DOC "C1'" "H1'"  sing N N 210 
DOC "C2'" "C3'"  sing N N 211 
DOC "C2'" "H2'"  sing N N 212 
DOC "C2'" "H2''" sing N N 213 
DOC "C3'" "C4'"  sing N N 214 
DOC "C3'" "H3'1" sing N N 215 
DOC "C3'" "H3'2" sing N N 216 
DOC "C4'" "O4'"  sing N N 217 
DOC "C4'" "C5'"  sing N N 218 
DOC "C4'" "H4'"  sing N N 219 
DOC "C5'" "O5'"  sing N N 220 
DOC "C5'" "H5'"  sing N N 221 
DOC "C5'" "H5''" sing N N 222 
DOC "O5'" P      sing N N 223 
DOC P     OP1    doub N N 224 
DOC P     OP2    sing N N 225 
DOC P     OP3    sing N N 226 
DOC OP2   HOP2   sing N N 227 
DOC OP3   HOP3   sing N N 228 
DT  OP3   P      sing N N 229 
DT  OP3   HOP3   sing N N 230 
DT  P     OP1    doub N N 231 
DT  P     OP2    sing N N 232 
DT  P     "O5'"  sing N N 233 
DT  OP2   HOP2   sing N N 234 
DT  "O5'" "C5'"  sing N N 235 
DT  "C5'" "C4'"  sing N N 236 
DT  "C5'" "H5'"  sing N N 237 
DT  "C5'" "H5''" sing N N 238 
DT  "C4'" "O4'"  sing N N 239 
DT  "C4'" "C3'"  sing N N 240 
DT  "C4'" "H4'"  sing N N 241 
DT  "O4'" "C1'"  sing N N 242 
DT  "C3'" "O3'"  sing N N 243 
DT  "C3'" "C2'"  sing N N 244 
DT  "C3'" "H3'"  sing N N 245 
DT  "O3'" "HO3'" sing N N 246 
DT  "C2'" "C1'"  sing N N 247 
DT  "C2'" "H2'"  sing N N 248 
DT  "C2'" "H2''" sing N N 249 
DT  "C1'" N1     sing N N 250 
DT  "C1'" "H1'"  sing N N 251 
DT  N1    C2     sing N N 252 
DT  N1    C6     sing N N 253 
DT  C2    O2     doub N N 254 
DT  C2    N3     sing N N 255 
DT  N3    C4     sing N N 256 
DT  N3    H3     sing N N 257 
DT  C4    O4     doub N N 258 
DT  C4    C5     sing N N 259 
DT  C5    C7     sing N N 260 
DT  C5    C6     doub N N 261 
DT  C7    H71    sing N N 262 
DT  C7    H72    sing N N 263 
DT  C7    H73    sing N N 264 
DT  C6    H6     sing N N 265 
GLN N     CA     sing N N 266 
GLN N     H      sing N N 267 
GLN N     H2     sing N N 268 
GLN CA    C      sing N N 269 
GLN CA    CB     sing N N 270 
GLN CA    HA     sing N N 271 
GLN C     O      doub N N 272 
GLN C     OXT    sing N N 273 
GLN CB    CG     sing N N 274 
GLN CB    HB2    sing N N 275 
GLN CB    HB3    sing N N 276 
GLN CG    CD     sing N N 277 
GLN CG    HG2    sing N N 278 
GLN CG    HG3    sing N N 279 
GLN CD    OE1    doub N N 280 
GLN CD    NE2    sing N N 281 
GLN NE2   HE21   sing N N 282 
GLN NE2   HE22   sing N N 283 
GLN OXT   HXT    sing N N 284 
GLU N     CA     sing N N 285 
GLU N     H      sing N N 286 
GLU N     H2     sing N N 287 
GLU CA    C      sing N N 288 
GLU CA    CB     sing N N 289 
GLU CA    HA     sing N N 290 
GLU C     O      doub N N 291 
GLU C     OXT    sing N N 292 
GLU CB    CG     sing N N 293 
GLU CB    HB2    sing N N 294 
GLU CB    HB3    sing N N 295 
GLU CG    CD     sing N N 296 
GLU CG    HG2    sing N N 297 
GLU CG    HG3    sing N N 298 
GLU CD    OE1    doub N N 299 
GLU CD    OE2    sing N N 300 
GLU OE2   HE2    sing N N 301 
GLU OXT   HXT    sing N N 302 
GLY N     CA     sing N N 303 
GLY N     H      sing N N 304 
GLY N     H2     sing N N 305 
GLY CA    C      sing N N 306 
GLY CA    HA2    sing N N 307 
GLY CA    HA3    sing N N 308 
GLY C     O      doub N N 309 
GLY C     OXT    sing N N 310 
GLY OXT   HXT    sing N N 311 
HIS N     CA     sing N N 312 
HIS N     H      sing N N 313 
HIS N     H2     sing N N 314 
HIS CA    C      sing N N 315 
HIS CA    CB     sing N N 316 
HIS CA    HA     sing N N 317 
HIS C     O      doub N N 318 
HIS C     OXT    sing N N 319 
HIS CB    CG     sing N N 320 
HIS CB    HB2    sing N N 321 
HIS CB    HB3    sing N N 322 
HIS CG    ND1    sing Y N 323 
HIS CG    CD2    doub Y N 324 
HIS ND1   CE1    doub Y N 325 
HIS ND1   HD1    sing N N 326 
HIS CD2   NE2    sing Y N 327 
HIS CD2   HD2    sing N N 328 
HIS CE1   NE2    sing Y N 329 
HIS CE1   HE1    sing N N 330 
HIS NE2   HE2    sing N N 331 
HIS OXT   HXT    sing N N 332 
ILE N     CA     sing N N 333 
ILE N     H      sing N N 334 
ILE N     H2     sing N N 335 
ILE CA    C      sing N N 336 
ILE CA    CB     sing N N 337 
ILE CA    HA     sing N N 338 
ILE C     O      doub N N 339 
ILE C     OXT    sing N N 340 
ILE CB    CG1    sing N N 341 
ILE CB    CG2    sing N N 342 
ILE CB    HB     sing N N 343 
ILE CG1   CD1    sing N N 344 
ILE CG1   HG12   sing N N 345 
ILE CG1   HG13   sing N N 346 
ILE CG2   HG21   sing N N 347 
ILE CG2   HG22   sing N N 348 
ILE CG2   HG23   sing N N 349 
ILE CD1   HD11   sing N N 350 
ILE CD1   HD12   sing N N 351 
ILE CD1   HD13   sing N N 352 
ILE OXT   HXT    sing N N 353 
LEU N     CA     sing N N 354 
LEU N     H      sing N N 355 
LEU N     H2     sing N N 356 
LEU CA    C      sing N N 357 
LEU CA    CB     sing N N 358 
LEU CA    HA     sing N N 359 
LEU C     O      doub N N 360 
LEU C     OXT    sing N N 361 
LEU CB    CG     sing N N 362 
LEU CB    HB2    sing N N 363 
LEU CB    HB3    sing N N 364 
LEU CG    CD1    sing N N 365 
LEU CG    CD2    sing N N 366 
LEU CG    HG     sing N N 367 
LEU CD1   HD11   sing N N 368 
LEU CD1   HD12   sing N N 369 
LEU CD1   HD13   sing N N 370 
LEU CD2   HD21   sing N N 371 
LEU CD2   HD22   sing N N 372 
LEU CD2   HD23   sing N N 373 
LEU OXT   HXT    sing N N 374 
LYS N     CA     sing N N 375 
LYS N     H      sing N N 376 
LYS N     H2     sing N N 377 
LYS CA    C      sing N N 378 
LYS CA    CB     sing N N 379 
LYS CA    HA     sing N N 380 
LYS C     O      doub N N 381 
LYS C     OXT    sing N N 382 
LYS CB    CG     sing N N 383 
LYS CB    HB2    sing N N 384 
LYS CB    HB3    sing N N 385 
LYS CG    CD     sing N N 386 
LYS CG    HG2    sing N N 387 
LYS CG    HG3    sing N N 388 
LYS CD    CE     sing N N 389 
LYS CD    HD2    sing N N 390 
LYS CD    HD3    sing N N 391 
LYS CE    NZ     sing N N 392 
LYS CE    HE2    sing N N 393 
LYS CE    HE3    sing N N 394 
LYS NZ    HZ1    sing N N 395 
LYS NZ    HZ2    sing N N 396 
LYS NZ    HZ3    sing N N 397 
LYS OXT   HXT    sing N N 398 
MET N     CA     sing N N 399 
MET N     H      sing N N 400 
MET N     H2     sing N N 401 
MET CA    C      sing N N 402 
MET CA    CB     sing N N 403 
MET CA    HA     sing N N 404 
MET C     O      doub N N 405 
MET C     OXT    sing N N 406 
MET CB    CG     sing N N 407 
MET CB    HB2    sing N N 408 
MET CB    HB3    sing N N 409 
MET CG    SD     sing N N 410 
MET CG    HG2    sing N N 411 
MET CG    HG3    sing N N 412 
MET SD    CE     sing N N 413 
MET CE    HE1    sing N N 414 
MET CE    HE2    sing N N 415 
MET CE    HE3    sing N N 416 
MET OXT   HXT    sing N N 417 
PHE N     CA     sing N N 418 
PHE N     H      sing N N 419 
PHE N     H2     sing N N 420 
PHE CA    C      sing N N 421 
PHE CA    CB     sing N N 422 
PHE CA    HA     sing N N 423 
PHE C     O      doub N N 424 
PHE C     OXT    sing N N 425 
PHE CB    CG     sing N N 426 
PHE CB    HB2    sing N N 427 
PHE CB    HB3    sing N N 428 
PHE CG    CD1    doub Y N 429 
PHE CG    CD2    sing Y N 430 
PHE CD1   CE1    sing Y N 431 
PHE CD1   HD1    sing N N 432 
PHE CD2   CE2    doub Y N 433 
PHE CD2   HD2    sing N N 434 
PHE CE1   CZ     doub Y N 435 
PHE CE1   HE1    sing N N 436 
PHE CE2   CZ     sing Y N 437 
PHE CE2   HE2    sing N N 438 
PHE CZ    HZ     sing N N 439 
PHE OXT   HXT    sing N N 440 
PRO N     CA     sing N N 441 
PRO N     CD     sing N N 442 
PRO N     H      sing N N 443 
PRO CA    C      sing N N 444 
PRO CA    CB     sing N N 445 
PRO CA    HA     sing N N 446 
PRO C     O      doub N N 447 
PRO C     OXT    sing N N 448 
PRO CB    CG     sing N N 449 
PRO CB    HB2    sing N N 450 
PRO CB    HB3    sing N N 451 
PRO CG    CD     sing N N 452 
PRO CG    HG2    sing N N 453 
PRO CG    HG3    sing N N 454 
PRO CD    HD2    sing N N 455 
PRO CD    HD3    sing N N 456 
PRO OXT   HXT    sing N N 457 
SER N     CA     sing N N 458 
SER N     H      sing N N 459 
SER N     H2     sing N N 460 
SER CA    C      sing N N 461 
SER CA    CB     sing N N 462 
SER CA    HA     sing N N 463 
SER C     O      doub N N 464 
SER C     OXT    sing N N 465 
SER CB    OG     sing N N 466 
SER CB    HB2    sing N N 467 
SER CB    HB3    sing N N 468 
SER OG    HG     sing N N 469 
SER OXT   HXT    sing N N 470 
THR N     CA     sing N N 471 
THR N     H      sing N N 472 
THR N     H2     sing N N 473 
THR CA    C      sing N N 474 
THR CA    CB     sing N N 475 
THR CA    HA     sing N N 476 
THR C     O      doub N N 477 
THR C     OXT    sing N N 478 
THR CB    OG1    sing N N 479 
THR CB    CG2    sing N N 480 
THR CB    HB     sing N N 481 
THR OG1   HG1    sing N N 482 
THR CG2   HG21   sing N N 483 
THR CG2   HG22   sing N N 484 
THR CG2   HG23   sing N N 485 
THR OXT   HXT    sing N N 486 
TRP N     CA     sing N N 487 
TRP N     H      sing N N 488 
TRP N     H2     sing N N 489 
TRP CA    C      sing N N 490 
TRP CA    CB     sing N N 491 
TRP CA    HA     sing N N 492 
TRP C     O      doub N N 493 
TRP C     OXT    sing N N 494 
TRP CB    CG     sing N N 495 
TRP CB    HB2    sing N N 496 
TRP CB    HB3    sing N N 497 
TRP CG    CD1    doub Y N 498 
TRP CG    CD2    sing Y N 499 
TRP CD1   NE1    sing Y N 500 
TRP CD1   HD1    sing N N 501 
TRP CD2   CE2    doub Y N 502 
TRP CD2   CE3    sing Y N 503 
TRP NE1   CE2    sing Y N 504 
TRP NE1   HE1    sing N N 505 
TRP CE2   CZ2    sing Y N 506 
TRP CE3   CZ3    doub Y N 507 
TRP CE3   HE3    sing N N 508 
TRP CZ2   CH2    doub Y N 509 
TRP CZ2   HZ2    sing N N 510 
TRP CZ3   CH2    sing Y N 511 
TRP CZ3   HZ3    sing N N 512 
TRP CH2   HH2    sing N N 513 
TRP OXT   HXT    sing N N 514 
TTP PA    O1A    doub N N 515 
TTP PA    O2A    sing N N 516 
TTP PA    O3A    sing N N 517 
TTP PA    "O5'"  sing N N 518 
TTP O2A   HOA2   sing N N 519 
TTP O3A   PB     sing N N 520 
TTP PB    O1B    doub N N 521 
TTP PB    O2B    sing N N 522 
TTP PB    O3B    sing N N 523 
TTP O2B   HOB2   sing N N 524 
TTP O3B   PG     sing N N 525 
TTP PG    O1G    doub N N 526 
TTP PG    O2G    sing N N 527 
TTP PG    O3G    sing N N 528 
TTP O2G   HOG2   sing N N 529 
TTP O3G   HOG3   sing N N 530 
TTP "O5'" "C5'"  sing N N 531 
TTP "C5'" "C4'"  sing N N 532 
TTP "C5'" "H5'1" sing N N 533 
TTP "C5'" "H5'2" sing N N 534 
TTP "C4'" "O4'"  sing N N 535 
TTP "C4'" "C3'"  sing N N 536 
TTP "C4'" "H4'"  sing N N 537 
TTP "O4'" "C1'"  sing N N 538 
TTP "C3'" "O3'"  sing N N 539 
TTP "C3'" "C2'"  sing N N 540 
TTP "C3'" "H3'"  sing N N 541 
TTP "O3'" "HO3'" sing N N 542 
TTP "C2'" "C1'"  sing N N 543 
TTP "C2'" "H2'1" sing N N 544 
TTP "C2'" "H2'2" sing N N 545 
TTP "C1'" N1     sing N N 546 
TTP "C1'" "H1'"  sing N N 547 
TTP N1    C2     sing N N 548 
TTP N1    C6     sing N N 549 
TTP C2    O2     doub N N 550 
TTP C2    N3     sing N N 551 
TTP N3    C4     sing N N 552 
TTP N3    HN3    sing N N 553 
TTP C4    O4     doub N N 554 
TTP C4    C5     sing N N 555 
TTP C5    C5M    sing N N 556 
TTP C5    C6     doub N N 557 
TTP C5M   HM51   sing N N 558 
TTP C5M   HM52   sing N N 559 
TTP C5M   HM53   sing N N 560 
TTP C6    H6     sing N N 561 
TYR N     CA     sing N N 562 
TYR N     H      sing N N 563 
TYR N     H2     sing N N 564 
TYR CA    C      sing N N 565 
TYR CA    CB     sing N N 566 
TYR CA    HA     sing N N 567 
TYR C     O      doub N N 568 
TYR C     OXT    sing N N 569 
TYR CB    CG     sing N N 570 
TYR CB    HB2    sing N N 571 
TYR CB    HB3    sing N N 572 
TYR CG    CD1    doub Y N 573 
TYR CG    CD2    sing Y N 574 
TYR CD1   CE1    sing Y N 575 
TYR CD1   HD1    sing N N 576 
TYR CD2   CE2    doub Y N 577 
TYR CD2   HD2    sing N N 578 
TYR CE1   CZ     doub Y N 579 
TYR CE1   HE1    sing N N 580 
TYR CE2   CZ     sing Y N 581 
TYR CE2   HE2    sing N N 582 
TYR CZ    OH     sing N N 583 
TYR OH    HH     sing N N 584 
TYR OXT   HXT    sing N N 585 
VAL N     CA     sing N N 586 
VAL N     H      sing N N 587 
VAL N     H2     sing N N 588 
VAL CA    C      sing N N 589 
VAL CA    CB     sing N N 590 
VAL CA    HA     sing N N 591 
VAL C     O      doub N N 592 
VAL C     OXT    sing N N 593 
VAL CB    CG1    sing N N 594 
VAL CB    CG2    sing N N 595 
VAL CB    HB     sing N N 596 
VAL CG1   HG11   sing N N 597 
VAL CG1   HG12   sing N N 598 
VAL CG1   HG13   sing N N 599 
VAL CG2   HG21   sing N N 600 
VAL CG2   HG22   sing N N 601 
VAL CG2   HG23   sing N N 602 
VAL OXT   HXT    sing N N 603 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-02-28 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9AU8 
_em_admin.last_update        2025-05-28 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              'Ternary complex of human DNA polymerase theta polymerase domain with a mismatched T:T base pair' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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          866768 
_em_entity_assembly_recombinant.organism             
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_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         1.2 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?      ?            
'MODEL REFINEMENT'         ? 2  ? ? ? PHENIX 1.21.2_5419: 
'IMAGE ACQUISITION'        ? 3  1 1 1 ?      ?            
MASKING                    ? 4  1 1 1 ?      ?            
'CTF CORRECTION'           ? 5  1 ? ? ?      ?            
'LAYERLINE INDEXING'       ? 6  1 1 1 ?      ?            
'DIFFRACTION INDEXING'     ? 7  1 1 1 ?      ?            
'MODEL FITTING'            ? 8  1 1 1 ?      ?            
OTHER                      ? 9  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?      ?            
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?      ?            
CLASSIFICATION             ? 12 1 ? ? ?      ?            
RECONSTRUCTION             ? 13 1 ? ? ?      ?            
# 
_em_specimen.concentration           0.7 
_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 
# 
_ndb_struct_conf_na.entry_id   9AU8 
_ndb_struct_conf_na.feature    'double helix' 
# 
loop_
_ndb_struct_na_base_pair.model_number 
_ndb_struct_na_base_pair.i_label_asym_id 
_ndb_struct_na_base_pair.i_label_comp_id 
_ndb_struct_na_base_pair.i_label_seq_id 
_ndb_struct_na_base_pair.i_symmetry 
_ndb_struct_na_base_pair.j_label_asym_id 
_ndb_struct_na_base_pair.j_label_comp_id 
_ndb_struct_na_base_pair.j_label_seq_id 
_ndb_struct_na_base_pair.j_symmetry 
_ndb_struct_na_base_pair.shear 
_ndb_struct_na_base_pair.stretch 
_ndb_struct_na_base_pair.stagger 
_ndb_struct_na_base_pair.buckle 
_ndb_struct_na_base_pair.propeller 
_ndb_struct_na_base_pair.opening 
_ndb_struct_na_base_pair.pair_number 
_ndb_struct_na_base_pair.pair_name 
_ndb_struct_na_base_pair.i_auth_asym_id 
_ndb_struct_na_base_pair.i_auth_seq_id 
_ndb_struct_na_base_pair.i_PDB_ins_code 
_ndb_struct_na_base_pair.j_auth_asym_id 
_ndb_struct_na_base_pair.j_auth_seq_id 
_ndb_struct_na_base_pair.j_PDB_ins_code 
_ndb_struct_na_base_pair.hbond_type_28 
_ndb_struct_na_base_pair.hbond_type_12 
1 B DC  15 1_555 C DG 15 1_555 0.189  -0.275 0.874  -2.074 -0.461 0.005  1 C_DC15:DG15_D  C 15 ? D 15 ? 19 1 
1 B DG  16 1_555 C DC 14 1_555 -0.207 -0.145 0.238  -1.618 -0.193 -0.106 2 C_DG16:DC14_D  C 16 ? D 14 ? 19 1 
1 B DT  17 1_555 C DA 13 1_555 -0.095 -0.155 -0.325 3.496  -1.481 2.915  3 C_DT17:DA13_D  C 17 ? D 13 ? 20 1 
1 B DA  18 1_555 C DT 12 1_555 0.201  -0.186 -0.713 -4.235 0.792  -0.671 4 C_DA18:DT12_D  C 18 ? D 12 ? 20 1 
1 B DG  19 1_555 C DC 11 1_555 -0.191 -0.156 -0.212 0.162  -3.246 0.005  5 C_DG19:DC11_D  C 19 ? D 11 ? 19 1 
1 B DOC 20 1_555 C DG 10 1_555 0.958  -0.421 0.528  -4.385 -5.261 -3.487 6 C_DOC20:DG10_D C 20 ? D 10 ? 19 1 
# 
loop_
_ndb_struct_na_base_pair_step.model_number 
_ndb_struct_na_base_pair_step.i_label_asym_id_1 
_ndb_struct_na_base_pair_step.i_label_comp_id_1 
_ndb_struct_na_base_pair_step.i_label_seq_id_1 
_ndb_struct_na_base_pair_step.i_symmetry_1 
_ndb_struct_na_base_pair_step.j_label_asym_id_1 
_ndb_struct_na_base_pair_step.j_label_comp_id_1 
_ndb_struct_na_base_pair_step.j_label_seq_id_1 
_ndb_struct_na_base_pair_step.j_symmetry_1 
_ndb_struct_na_base_pair_step.i_label_asym_id_2 
_ndb_struct_na_base_pair_step.i_label_comp_id_2 
_ndb_struct_na_base_pair_step.i_label_seq_id_2 
_ndb_struct_na_base_pair_step.i_symmetry_2 
_ndb_struct_na_base_pair_step.j_label_asym_id_2 
_ndb_struct_na_base_pair_step.j_label_comp_id_2 
_ndb_struct_na_base_pair_step.j_label_seq_id_2 
_ndb_struct_na_base_pair_step.j_symmetry_2 
_ndb_struct_na_base_pair_step.shift 
_ndb_struct_na_base_pair_step.slide 
_ndb_struct_na_base_pair_step.rise 
_ndb_struct_na_base_pair_step.tilt 
_ndb_struct_na_base_pair_step.roll 
_ndb_struct_na_base_pair_step.twist 
_ndb_struct_na_base_pair_step.x_displacement 
_ndb_struct_na_base_pair_step.y_displacement 
_ndb_struct_na_base_pair_step.helical_rise 
_ndb_struct_na_base_pair_step.inclination 
_ndb_struct_na_base_pair_step.tip 
_ndb_struct_na_base_pair_step.helical_twist 
_ndb_struct_na_base_pair_step.step_number 
_ndb_struct_na_base_pair_step.step_name 
_ndb_struct_na_base_pair_step.i_auth_asym_id_1 
_ndb_struct_na_base_pair_step.i_auth_seq_id_1 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.j_auth_asym_id_1 
_ndb_struct_na_base_pair_step.j_auth_seq_id_1 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_1 
_ndb_struct_na_base_pair_step.i_auth_asym_id_2 
_ndb_struct_na_base_pair_step.i_auth_seq_id_2 
_ndb_struct_na_base_pair_step.i_PDB_ins_code_2 
_ndb_struct_na_base_pair_step.j_auth_asym_id_2 
_ndb_struct_na_base_pair_step.j_auth_seq_id_2 
_ndb_struct_na_base_pair_step.j_PDB_ins_code_2 
1 B DC 15 1_555 C DG 15 1_555 B DG  16 1_555 C DC 14 1_555 -1.005 -0.432 3.308 -1.479 1.815 34.123 -1.026 1.473  3.321 3.088  
2.517  34.201 1 CC_DC15DG16:DC14DG15_DD  C 15 ? D 15 ? C 16 ? D 14 ? 
1 B DG 16 1_555 C DC 14 1_555 B DT  17 1_555 C DA 13 1_555 -0.084 -0.630 3.455 -0.430 2.349 29.918 -1.723 0.069  3.398 4.541  
0.831  30.011 2 CC_DG16DT17:DA13DC14_DD  C 16 ? D 14 ? C 17 ? D 13 ? 
1 B DT 17 1_555 C DA 13 1_555 B DA  18 1_555 C DT 12 1_555 -0.651 0.059  3.712 -6.719 6.214 43.296 -0.591 0.141  3.742 8.312  
8.987  44.207 3 CC_DT17DA18:DT12DA13_DD  C 17 ? D 13 ? C 18 ? D 12 ? 
1 B DA 18 1_555 C DT 12 1_555 B DG  19 1_555 C DC 11 1_555 -0.890 -1.228 3.409 -3.380 5.292 19.861 -5.712 0.984  3.087 14.869 
9.499  20.820 4 CC_DA18DG19:DC11DT12_DD  C 18 ? D 12 ? C 19 ? D 11 ? 
1 B DG 19 1_555 C DC 11 1_555 B DOC 20 1_555 C DG 10 1_555 0.783  -0.843 3.605 2.798  0.824 43.456 -1.224 -0.758 3.631 1.111  
-3.774 43.549 5 CC_DG19DOC20:DG10DC11_DD C 19 ? D 11 ? C 20 ? D 10 ? 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'American Cancer Society'                                   'United States' 'RSG-22-082-517 01-DMC' 1 
'Cancer Prevention and Research Institute of Texas (CPRIT)' 'United States' RR190046                2 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9AU8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
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     . SER A 1 33  ? 85.005  120.331 69.953  1.00 81.26  ? 1824 SER A N     1 
ATOM   2    C  CA    . SER A 1 33  ? 85.020  119.530 71.172  1.00 81.34  ? 1824 SER A CA    1 
ATOM   3    C  C     . SER A 1 33  ? 86.230  118.602 71.204  1.00 87.03  ? 1824 SER A C     1 
ATOM   4    O  O     . SER A 1 33  ? 87.317  118.968 70.756  1.00 85.25  ? 1824 SER A O     1 
ATOM   5    C  CB    . SER A 1 33  ? 83.729  118.717 71.294  1.00 75.74  ? 1824 SER A CB    1 
ATOM   6    O  OG    . SER A 1 33  ? 83.582  117.825 70.203  1.00 74.38  ? 1824 SER A OG    1 
ATOM   7    N  N     . LEU A 1 34  ? 86.033  117.403 71.748  1.00 88.35  ? 1825 LEU A N     1 
ATOM   8    C  CA    . LEU A 1 34  ? 87.100  116.412 71.786  1.00 81.98  ? 1825 LEU A CA    1 
ATOM   9    C  C     . LEU A 1 34  ? 87.494  116.006 70.373  1.00 81.98  ? 1825 LEU A C     1 
ATOM   10   O  O     . LEU A 1 34  ? 86.635  115.757 69.522  1.00 86.96  ? 1825 LEU A O     1 
ATOM   11   C  CB    . LEU A 1 34  ? 86.650  115.190 72.585  1.00 78.88  ? 1825 LEU A CB    1 
ATOM   12   C  CG    . LEU A 1 34  ? 87.398  113.883 72.320  1.00 68.76  ? 1825 LEU A CG    1 
ATOM   13   C  CD1   . LEU A 1 34  ? 88.687  113.838 73.116  1.00 69.42  ? 1825 LEU A CD1   1 
ATOM   14   C  CD2   . LEU A 1 34  ? 86.520  112.691 72.647  1.00 67.98  ? 1825 LEU A CD2   1 
ATOM   15   N  N     . SER A 1 35  ? 88.799  115.939 70.123  1.00 74.54  ? 1826 SER A N     1 
ATOM   16   C  CA    . SER A 1 35  ? 89.335  115.603 68.804  1.00 72.50  ? 1826 SER A CA    1 
ATOM   17   C  C     . SER A 1 35  ? 90.312  114.443 68.961  1.00 62.65  ? 1826 SER A C     1 
ATOM   18   O  O     . SER A 1 35  ? 91.488  114.650 69.278  1.00 66.29  ? 1826 SER A O     1 
ATOM   19   C  CB    . SER A 1 35  ? 90.006  116.812 68.161  1.00 71.37  ? 1826 SER A CB    1 
ATOM   20   O  OG    . SER A 1 35  ? 89.102  117.898 68.049  1.00 79.12  ? 1826 SER A OG    1 
ATOM   21   N  N     . ILE A 1 36  ? 89.823  113.228 68.737  1.00 58.68  ? 1827 ILE A N     1 
ATOM   22   C  CA    . ILE A 1 36  ? 90.648  112.028 68.797  1.00 55.77  ? 1827 ILE A CA    1 
ATOM   23   C  C     . ILE A 1 36  ? 91.159  111.717 67.398  1.00 56.21  ? 1827 ILE A C     1 
ATOM   24   O  O     . ILE A 1 36  ? 90.378  111.650 66.442  1.00 61.87  ? 1827 ILE A O     1 
ATOM   25   C  CB    . ILE A 1 36  ? 89.855  110.841 69.367  1.00 56.94  ? 1827 ILE A CB    1 
ATOM   26   C  CG1   . ILE A 1 36  ? 89.472  111.099 70.823  1.00 59.01  ? 1827 ILE A CG1   1 
ATOM   27   C  CG2   . ILE A 1 36  ? 90.662  109.559 69.251  1.00 57.34  ? 1827 ILE A CG2   1 
ATOM   28   C  CD1   . ILE A 1 36  ? 88.714  109.955 71.458  1.00 65.20  ? 1827 ILE A CD1   1 
ATOM   29   N  N     . ILE A 1 37  ? 92.468  111.527 67.277  1.00 53.03  ? 1828 ILE A N     1 
ATOM   30   C  CA    . ILE A 1 37  ? 93.108  111.191 66.011  1.00 49.33  ? 1828 ILE A CA    1 
ATOM   31   C  C     . ILE A 1 37  ? 93.559  109.740 66.087  1.00 53.13  ? 1828 ILE A C     1 
ATOM   32   O  O     . ILE A 1 37  ? 94.409  109.391 66.915  1.00 55.10  ? 1828 ILE A O     1 
ATOM   33   C  CB    . ILE A 1 37  ? 94.292  112.120 65.705  1.00 51.84  ? 1828 ILE A CB    1 
ATOM   34   C  CG1   . ILE A 1 37  ? 93.790  113.476 65.209  1.00 55.04  ? 1828 ILE A CG1   1 
ATOM   35   C  CG2   . ILE A 1 37  ? 95.214  111.491 64.673  1.00 55.73  ? 1828 ILE A CG2   1 
ATOM   36   C  CD1   . ILE A 1 37  ? 93.564  114.478 66.310  1.00 55.29  ? 1828 ILE A CD1   1 
ATOM   37   N  N     . ASP A 1 38  ? 92.992  108.898 65.229  1.00 61.12  ? 1829 ASP A N     1 
ATOM   38   C  CA    . ASP A 1 38  ? 93.381  107.492 65.156  1.00 65.05  ? 1829 ASP A CA    1 
ATOM   39   C  C     . ASP A 1 38  ? 94.656  107.403 64.331  1.00 72.12  ? 1829 ASP A C     1 
ATOM   40   O  O     . ASP A 1 38  ? 94.616  107.380 63.099  1.00 88.75  ? 1829 ASP A O     1 
ATOM   41   C  CB    . ASP A 1 38  ? 92.262  106.652 64.553  1.00 77.24  ? 1829 ASP A CB    1 
ATOM   42   C  CG    . ASP A 1 38  ? 90.977  106.735 65.352  1.00 79.53  ? 1829 ASP A CG    1 
ATOM   43   O  OD1   . ASP A 1 38  ? 91.052  106.958 66.578  1.00 68.46  ? 1829 ASP A OD1   1 
ATOM   44   O  OD2   . ASP A 1 38  ? 89.891  106.577 64.754  1.00 84.57  ? 1829 ASP A OD2   1 
ATOM   45   N  N     . VAL A 1 39  ? 95.799  107.356 65.017  1.00 60.79  ? 1830 VAL A N     1 
ATOM   46   C  CA    . VAL A 1 39  ? 97.086  107.402 64.330  1.00 65.71  ? 1830 VAL A CA    1 
ATOM   47   C  C     . VAL A 1 39  ? 97.316  106.131 63.521  1.00 80.94  ? 1830 VAL A C     1 
ATOM   48   O  O     . VAL A 1 39  ? 97.824  106.179 62.394  1.00 93.04  ? 1830 VAL A O     1 
ATOM   49   C  CB    . VAL A 1 39  ? 98.214  107.646 65.346  1.00 64.13  ? 1830 VAL A CB    1 
ATOM   50   C  CG1   . VAL A 1 39  ? 99.557  107.308 64.739  1.00 68.73  ? 1830 VAL A CG1   1 
ATOM   51   C  CG2   . VAL A 1 39  ? 98.190  109.090 65.819  1.00 62.01  ? 1830 VAL A CG2   1 
ATOM   52   N  N     . ALA A 1 40  ? 96.933  104.980 64.067  1.00 80.15  ? 1831 ALA A N     1 
ATOM   53   C  CA    . ALA A 1 40  ? 97.191  103.693 63.434  1.00 86.10  ? 1831 ALA A CA    1 
ATOM   54   C  C     . ALA A 1 40  ? 96.224  103.375 62.298  1.00 96.72  ? 1831 ALA A C     1 
ATOM   55   O  O     . ALA A 1 40  ? 96.150  102.214 61.876  1.00 105.83 ? 1831 ALA A O     1 
ATOM   56   C  CB    . ALA A 1 40  ? 97.150  102.577 64.480  1.00 75.67  ? 1831 ALA A CB    1 
ATOM   57   N  N     . SER A 1 41  ? 95.482  104.361 61.794  1.00 93.71  ? 1832 SER A N     1 
ATOM   58   C  CA    . SER A 1 41  ? 94.538  104.122 60.710  1.00 96.40  ? 1832 SER A CA    1 
ATOM   59   C  C     . SER A 1 41  ? 95.176  104.276 59.334  1.00 104.08 ? 1832 SER A C     1 
ATOM   60   O  O     . SER A 1 41  ? 94.868  103.502 58.421  1.00 109.59 ? 1832 SER A O     1 
ATOM   61   C  CB    . SER A 1 41  ? 93.342  105.069 60.835  1.00 91.86  ? 1832 SER A CB    1 
ATOM   62   O  OG    . SER A 1 41  ? 93.728  106.412 60.601  1.00 86.47  ? 1832 SER A OG    1 
ATOM   63   N  N     . ASP A 1 42  ? 96.061  105.256 59.164  1.00 100.33 ? 1833 ASP A N     1 
ATOM   64   C  CA    . ASP A 1 42  ? 96.696  105.522 57.882  1.00 106.28 ? 1833 ASP A CA    1 
ATOM   65   C  C     . ASP A 1 42  ? 98.204  105.622 58.062  1.00 107.59 ? 1833 ASP A C     1 
ATOM   66   O  O     . ASP A 1 42  ? 98.693  106.092 59.093  1.00 102.85 ? 1833 ASP A O     1 
ATOM   67   C  CB    . ASP A 1 42  ? 96.159  106.812 57.246  1.00 104.70 ? 1833 ASP A CB    1 
ATOM   68   C  CG    . ASP A 1 42  ? 94.745  106.656 56.720  1.00 103.63 ? 1833 ASP A CG    1 
ATOM   69   O  OD1   . ASP A 1 42  ? 94.377  105.530 56.324  1.00 101.02 ? 1833 ASP A OD1   1 
ATOM   70   O  OD2   . ASP A 1 42  ? 94.002  107.659 56.700  1.00 104.35 ? 1833 ASP A OD2   1 
ATOM   71   N  N     . GLN A 1 43  ? 98.937  105.169 57.042  1.00 110.84 ? 1834 GLN A N     1 
ATOM   72   C  CA    . GLN A 1 43  ? 100.395 105.174 57.115  1.00 109.64 ? 1834 GLN A CA    1 
ATOM   73   C  C     . GLN A 1 43  ? 100.951 106.593 57.114  1.00 103.94 ? 1834 GLN A C     1 
ATOM   74   O  O     . GLN A 1 43  ? 101.862 106.908 57.889  1.00 101.35 ? 1834 GLN A O     1 
ATOM   75   C  CB    . GLN A 1 43  ? 100.978 104.366 55.956  1.00 104.72 ? 1834 GLN A CB    1 
ATOM   76   C  CG    . GLN A 1 43  ? 102.252 103.611 56.299  1.00 108.99 ? 1834 GLN A CG    1 
ATOM   77   C  CD    . GLN A 1 43  ? 103.436 104.530 56.524  1.00 105.55 ? 1834 GLN A CD    1 
ATOM   78   O  OE1   . GLN A 1 43  ? 103.595 105.536 55.833  1.00 101.11 ? 1834 GLN A OE1   1 
ATOM   79   N  NE2   . GLN A 1 43  ? 104.274 104.188 57.495  1.00 101.21 ? 1834 GLN A NE2   1 
ATOM   80   N  N     . ASN A 1 44  ? 100.425 107.460 56.245  1.00 103.73 ? 1835 ASN A N     1 
ATOM   81   C  CA    . ASN A 1 44  ? 100.895 108.842 56.205  1.00 102.85 ? 1835 ASN A CA    1 
ATOM   82   C  C     . ASN A 1 44  ? 100.582 109.567 57.507  1.00 96.89  ? 1835 ASN A C     1 
ATOM   83   O  O     . ASN A 1 44  ? 101.405 110.344 58.010  1.00 93.71  ? 1835 ASN A O     1 
ATOM   84   C  CB    . ASN A 1 44  ? 100.271 109.575 55.018  1.00 107.75 ? 1835 ASN A CB    1 
ATOM   85   C  CG    . ASN A 1 44  ? 100.417 108.810 53.719  1.00 114.02 ? 1835 ASN A CG    1 
ATOM   86   O  OD1   . ASN A 1 44  ? 99.583  107.969 53.383  1.00 113.57 ? 1835 ASN A OD1   1 
ATOM   87   N  ND2   . ASN A 1 44  ? 101.481 109.099 52.978  1.00 115.39 ? 1835 ASN A ND2   1 
ATOM   88   N  N     . LEU A 1 45  ? 99.391  109.330 58.063  1.00 95.49  ? 1836 LEU A N     1 
ATOM   89   C  CA    . LEU A 1 45  ? 99.041  109.927 59.346  1.00 92.24  ? 1836 LEU A CA    1 
ATOM   90   C  C     . LEU A 1 45  ? 99.971  109.438 60.447  1.00 94.86  ? 1836 LEU A C     1 
ATOM   91   O  O     . LEU A 1 45  ? 100.415 110.225 61.291  1.00 89.96  ? 1836 LEU A O     1 
ATOM   92   C  CB    . LEU A 1 45  ? 97.584  109.613 59.689  1.00 84.83  ? 1836 LEU A CB    1 
ATOM   93   C  CG    . LEU A 1 45  ? 97.003  110.304 60.923  1.00 79.17  ? 1836 LEU A CG    1 
ATOM   94   C  CD1   . LEU A 1 45  ? 97.167  111.812 60.822  1.00 76.94  ? 1836 LEU A CD1   1 
ATOM   95   C  CD2   . LEU A 1 45  ? 95.540  109.933 61.101  1.00 74.96  ? 1836 LEU A CD2   1 
ATOM   96   N  N     . PHE A 1 46  ? 100.289 108.142 60.446  1.00 96.16  ? 1837 PHE A N     1 
ATOM   97   C  CA    . PHE A 1 46  ? 101.227 107.608 61.428  1.00 91.47  ? 1837 PHE A CA    1 
ATOM   98   C  C     . PHE A 1 46  ? 102.598 108.258 61.288  1.00 89.63  ? 1837 PHE A C     1 
ATOM   99   O  O     . PHE A 1 46  ? 103.226 108.619 62.289  1.00 85.78  ? 1837 PHE A O     1 
ATOM   100  C  CB    . PHE A 1 46  ? 101.331 106.090 61.275  1.00 93.58  ? 1837 PHE A CB    1 
ATOM   101  C  CG    . PHE A 1 46  ? 102.237 105.432 62.281  1.00 96.71  ? 1837 PHE A CG    1 
ATOM   102  C  CD1   . PHE A 1 46  ? 103.597 105.310 62.040  1.00 97.39  ? 1837 PHE A CD1   1 
ATOM   103  C  CD2   . PHE A 1 46  ? 101.728 104.927 63.464  1.00 88.40  ? 1837 PHE A CD2   1 
ATOM   104  C  CE1   . PHE A 1 46  ? 104.428 104.705 62.962  1.00 91.90  ? 1837 PHE A CE1   1 
ATOM   105  C  CE2   . PHE A 1 46  ? 102.554 104.321 64.390  1.00 81.95  ? 1837 PHE A CE2   1 
ATOM   106  C  CZ    . PHE A 1 46  ? 103.906 104.210 64.138  1.00 87.10  ? 1837 PHE A CZ    1 
ATOM   107  N  N     . GLN A 1 47  ? 103.077 108.416 60.053  1.00 93.97  ? 1838 GLN A N     1 
ATOM   108  C  CA    . GLN A 1 47  ? 104.404 108.986 59.847  1.00 88.08  ? 1838 GLN A CA    1 
ATOM   109  C  C     . GLN A 1 47  ? 104.459 110.447 60.274  1.00 83.50  ? 1838 GLN A C     1 
ATOM   110  O  O     . GLN A 1 47  ? 105.424 110.874 60.921  1.00 78.60  ? 1838 GLN A O     1 
ATOM   111  C  CB    . GLN A 1 47  ? 104.821 108.833 58.386  1.00 89.33  ? 1838 GLN A CB    1 
ATOM   112  C  CG    . GLN A 1 47  ? 105.247 107.421 58.017  1.00 92.55  ? 1838 GLN A CG    1 
ATOM   113  C  CD    . GLN A 1 47  ? 106.403 106.919 58.861  1.00 89.27  ? 1838 GLN A CD    1 
ATOM   114  O  OE1   . GLN A 1 47  ? 106.420 105.764 59.286  1.00 90.71  ? 1838 GLN A OE1   1 
ATOM   115  N  NE2   . GLN A 1 47  ? 107.381 107.785 59.103  1.00 87.53  ? 1838 GLN A NE2   1 
ATOM   116  N  N     . THR A 1 48  ? 103.436 111.235 59.929  1.00 85.17  ? 1839 THR A N     1 
ATOM   117  C  CA    . THR A 1 48  ? 103.450 112.634 60.343  1.00 84.62  ? 1839 THR A CA    1 
ATOM   118  C  C     . THR A 1 48  ? 103.267 112.771 61.851  1.00 87.25  ? 1839 THR A C     1 
ATOM   119  O  O     . THR A 1 48  ? 103.857 113.669 62.463  1.00 88.21  ? 1839 THR A O     1 
ATOM   120  C  CB    . THR A 1 48  ? 102.392 113.443 59.585  1.00 83.48  ? 1839 THR A CB    1 
ATOM   121  O  OG1   . THR A 1 48  ? 102.498 114.825 59.948  1.00 77.22  ? 1839 THR A OG1   1 
ATOM   122  C  CG2   . THR A 1 48  ? 100.990 112.957 59.897  1.00 85.68  ? 1839 THR A CG2   1 
ATOM   123  N  N     . PHE A 1 49  ? 102.485 111.881 62.472  1.00 83.64  ? 1840 PHE A N     1 
ATOM   124  C  CA    . PHE A 1 49  ? 102.375 111.885 63.926  1.00 80.71  ? 1840 PHE A CA    1 
ATOM   125  C  C     . PHE A 1 49  ? 103.715 111.567 64.575  1.00 74.53  ? 1840 PHE A C     1 
ATOM   126  O  O     . PHE A 1 49  ? 104.097 112.196 65.566  1.00 66.19  ? 1840 PHE A O     1 
ATOM   127  C  CB    . PHE A 1 49  ? 101.309 110.884 64.371  1.00 75.82  ? 1840 PHE A CB    1 
ATOM   128  C  CG    . PHE A 1 49  ? 101.432 110.460 65.808  1.00 67.91  ? 1840 PHE A CG    1 
ATOM   129  C  CD1   . PHE A 1 49  ? 100.961 111.272 66.824  1.00 57.88  ? 1840 PHE A CD1   1 
ATOM   130  C  CD2   . PHE A 1 49  ? 102.010 109.248 66.141  1.00 66.48  ? 1840 PHE A CD2   1 
ATOM   131  C  CE1   . PHE A 1 49  ? 101.070 110.885 68.144  1.00 52.80  ? 1840 PHE A CE1   1 
ATOM   132  C  CE2   . PHE A 1 49  ? 102.119 108.857 67.459  1.00 60.82  ? 1840 PHE A CE2   1 
ATOM   133  C  CZ    . PHE A 1 49  ? 101.647 109.676 68.460  1.00 57.93  ? 1840 PHE A CZ    1 
ATOM   134  N  N     . ILE A 1 50  ? 104.440 110.589 64.028  1.00 75.29  ? 1841 ILE A N     1 
ATOM   135  C  CA    . ILE A 1 50  ? 105.752 110.238 64.565  1.00 74.03  ? 1841 ILE A CA    1 
ATOM   136  C  C     . ILE A 1 50  ? 106.716 111.409 64.421  1.00 76.50  ? 1841 ILE A C     1 
ATOM   137  O  O     . ILE A 1 50  ? 107.481 111.720 65.343  1.00 76.89  ? 1841 ILE A O     1 
ATOM   138  C  CB    . ILE A 1 50  ? 106.286 108.970 63.872  1.00 75.70  ? 1841 ILE A CB    1 
ATOM   139  C  CG1   . ILE A 1 50  ? 105.591 107.727 64.430  1.00 73.75  ? 1841 ILE A CG1   1 
ATOM   140  C  CG2   . ILE A 1 50  ? 107.793 108.857 64.032  1.00 75.54  ? 1841 ILE A CG2   1 
ATOM   141  C  CD1   . ILE A 1 50  ? 105.985 107.392 65.849  1.00 75.66  ? 1841 ILE A CD1   1 
ATOM   142  N  N     . LYS A 1 51  ? 106.698 112.074 63.263  1.00 82.22  ? 1842 LYS A N     1 
ATOM   143  C  CA    . LYS A 1 51  ? 107.577 113.222 63.057  1.00 81.01  ? 1842 LYS A CA    1 
ATOM   144  C  C     . LYS A 1 51  ? 107.254 114.349 64.032  1.00 81.90  ? 1842 LYS A C     1 
ATOM   145  O  O     . LYS A 1 51  ? 108.161 114.948 64.625  1.00 81.35  ? 1842 LYS A O     1 
ATOM   146  C  CB    . LYS A 1 51  ? 107.468 113.712 61.613  1.00 76.63  ? 1842 LYS A CB    1 
ATOM   147  C  CG    . LYS A 1 51  ? 108.238 114.991 61.332  1.00 74.65  ? 1842 LYS A CG    1 
ATOM   148  C  CD    . LYS A 1 51  ? 107.700 115.700 60.100  1.00 80.14  ? 1842 LYS A CD    1 
ATOM   149  C  CE    . LYS A 1 51  ? 108.155 117.149 60.056  1.00 78.98  ? 1842 LYS A CE    1 
ATOM   150  N  NZ    . LYS A 1 51  ? 109.630 117.272 60.215  1.00 77.53  ? 1842 LYS A NZ    1 
ATOM   151  N  N     . GLU A 1 52  ? 105.965 114.644 64.221  1.00 79.45  ? 1843 GLU A N     1 
ATOM   152  C  CA    . GLU A 1 52  ? 105.578 115.691 65.162  1.00 78.31  ? 1843 GLU A CA    1 
ATOM   153  C  C     . GLU A 1 52  ? 105.961 115.318 66.589  1.00 81.51  ? 1843 GLU A C     1 
ATOM   154  O  O     . GLU A 1 52  ? 106.404 116.174 67.364  1.00 83.93  ? 1843 GLU A O     1 
ATOM   155  C  CB    . GLU A 1 52  ? 104.077 115.960 65.057  1.00 69.35  ? 1843 GLU A CB    1 
ATOM   156  C  CG    . GLU A 1 52  ? 103.555 116.973 66.061  1.00 75.27  ? 1843 GLU A CG    1 
ATOM   157  C  CD    . GLU A 1 52  ? 104.038 118.380 65.774  1.00 86.13  ? 1843 GLU A CD    1 
ATOM   158  O  OE1   . GLU A 1 52  ? 104.364 118.672 64.604  1.00 86.25  ? 1843 GLU A OE1   1 
ATOM   159  O  OE2   . GLU A 1 52  ? 104.091 119.195 66.719  1.00 87.36  ? 1843 GLU A OE2   1 
ATOM   160  N  N     . TRP A 1 53  ? 105.795 114.045 66.954  1.00 76.60  ? 1844 TRP A N     1 
ATOM   161  C  CA    . TRP A 1 53  ? 106.179 113.593 68.287  1.00 71.52  ? 1844 TRP A CA    1 
ATOM   162  C  C     . TRP A 1 53  ? 107.677 113.746 68.509  1.00 72.39  ? 1844 TRP A C     1 
ATOM   163  O  O     . TRP A 1 53  ? 108.112 114.197 69.575  1.00 70.64  ? 1844 TRP A O     1 
ATOM   164  C  CB    . TRP A 1 53  ? 105.756 112.137 68.481  1.00 66.22  ? 1844 TRP A CB    1 
ATOM   165  C  CG    . TRP A 1 53  ? 105.511 111.763 69.903  1.00 61.17  ? 1844 TRP A CG    1 
ATOM   166  C  CD1   . TRP A 1 53  ? 105.669 112.557 70.998  1.00 61.05  ? 1844 TRP A CD1   1 
ATOM   167  C  CD2   . TRP A 1 53  ? 105.061 110.493 70.388  1.00 60.28  ? 1844 TRP A CD2   1 
ATOM   168  N  NE1   . TRP A 1 53  ? 105.345 111.861 72.136  1.00 62.40  ? 1844 TRP A NE1   1 
ATOM   169  C  CE2   . TRP A 1 53  ? 104.969 110.591 71.788  1.00 61.47  ? 1844 TRP A CE2   1 
ATOM   170  C  CE3   . TRP A 1 53  ? 104.728 109.284 69.774  1.00 57.60  ? 1844 TRP A CE3   1 
ATOM   171  C  CZ2   . TRP A 1 53  ? 104.557 109.527 72.584  1.00 58.32  ? 1844 TRP A CZ2   1 
ATOM   172  C  CZ3   . TRP A 1 53  ? 104.319 108.229 70.565  1.00 56.73  ? 1844 TRP A CZ3   1 
ATOM   173  C  CH2   . TRP A 1 53  ? 104.237 108.357 71.955  1.00 56.33  ? 1844 TRP A CH2   1 
ATOM   174  N  N     . ARG A 1 54  ? 108.483 113.372 67.512  1.00 73.66  ? 1845 ARG A N     1 
ATOM   175  C  CA    . ARG A 1 54  ? 109.926 113.548 67.628  1.00 67.04  ? 1845 ARG A CA    1 
ATOM   176  C  C     . ARG A 1 54  ? 110.301 115.020 67.699  1.00 66.69  ? 1845 ARG A C     1 
ATOM   177  O  O     . ARG A 1 54  ? 111.293 115.377 68.344  1.00 65.36  ? 1845 ARG A O     1 
ATOM   178  C  CB    . ARG A 1 54  ? 110.637 112.875 66.454  1.00 64.58  ? 1845 ARG A CB    1 
ATOM   179  C  CG    . ARG A 1 54  ? 110.539 111.360 66.450  1.00 66.26  ? 1845 ARG A CG    1 
ATOM   180  C  CD    . ARG A 1 54  ? 111.305 110.770 65.279  1.00 73.35  ? 1845 ARG A CD    1 
ATOM   181  N  NE    . ARG A 1 54  ? 110.969 109.370 65.052  1.00 84.37  ? 1845 ARG A NE    1 
ATOM   182  C  CZ    . ARG A 1 54  ? 111.586 108.349 65.628  1.00 86.49  ? 1845 ARG A CZ    1 
ATOM   183  N  NH1   . ARG A 1 54  ? 112.578 108.534 66.484  1.00 77.64  ? 1845 ARG A NH1   1 
ATOM   184  N  NH2   . ARG A 1 54  ? 111.199 107.110 65.339  1.00 90.48  ? 1845 ARG A NH2   1 
ATOM   185  N  N     . CYS A 1 55  ? 109.525 115.886 67.051  1.00 72.12  ? 1846 CYS A N     1 
ATOM   186  C  CA    . CYS A 1 55  ? 109.775 117.320 67.108  1.00 78.83  ? 1846 CYS A CA    1 
ATOM   187  C  C     . CYS A 1 55  ? 109.152 117.985 68.329  1.00 79.21  ? 1846 CYS A C     1 
ATOM   188  O  O     . CYS A 1 55  ? 109.314 119.198 68.501  1.00 81.33  ? 1846 CYS A O     1 
ATOM   189  C  CB    . CYS A 1 55  ? 109.258 117.995 65.835  1.00 83.60  ? 1846 CYS A CB    1 
ATOM   190  S  SG    . CYS A 1 55  ? 110.158 117.540 64.335  1.00 101.88 ? 1846 CYS A SG    1 
ATOM   191  N  N     . LYS A 1 56  ? 108.452 117.233 69.174  1.00 77.27  ? 1847 LYS A N     1 
ATOM   192  C  CA    . LYS A 1 56  ? 107.777 117.779 70.343  1.00 72.60  ? 1847 LYS A CA    1 
ATOM   193  C  C     . LYS A 1 56  ? 108.598 117.512 71.598  1.00 67.56  ? 1847 LYS A C     1 
ATOM   194  O  O     . LYS A 1 56  ? 109.237 116.464 71.724  1.00 70.49  ? 1847 LYS A O     1 
ATOM   195  C  CB    . LYS A 1 56  ? 106.378 117.179 70.493  1.00 68.06  ? 1847 LYS A CB    1 
ATOM   196  C  CG    . LYS A 1 56  ? 105.480 117.923 71.467  1.00 63.80  ? 1847 LYS A CG    1 
ATOM   197  C  CD    . LYS A 1 56  ? 105.619 119.428 71.315  1.00 67.48  ? 1847 LYS A CD    1 
ATOM   198  C  CE    . LYS A 1 56  ? 105.187 120.148 72.582  1.00 67.06  ? 1847 LYS A CE    1 
ATOM   199  N  NZ    . LYS A 1 56  ? 105.685 121.550 72.623  1.00 73.51  ? 1847 LYS A NZ    1 
ATOM   200  N  N     . LYS A 1 57  ? 108.573 118.468 72.526  1.00 62.90  ? 1848 LYS A N     1 
ATOM   201  C  CA    . LYS A 1 57  ? 109.352 118.389 73.754  1.00 62.60  ? 1848 LYS A CA    1 
ATOM   202  C  C     . LYS A 1 57  ? 108.501 118.184 74.998  1.00 57.22  ? 1848 LYS A C     1 
ATOM   203  O  O     . LYS A 1 57  ? 109.057 118.055 76.093  1.00 49.98  ? 1848 LYS A O     1 
ATOM   204  C  CB    . LYS A 1 57  ? 110.202 119.654 73.921  1.00 61.99  ? 1848 LYS A CB    1 
ATOM   205  C  CG    . LYS A 1 57  ? 111.043 120.002 72.706  1.00 70.41  ? 1848 LYS A CG    1 
ATOM   206  C  CD    . LYS A 1 57  ? 112.233 119.069 72.574  1.00 73.34  ? 1848 LYS A CD    1 
ATOM   207  C  CE    . LYS A 1 57  ? 113.301 119.393 73.604  1.00 75.16  ? 1848 LYS A CE    1 
ATOM   208  N  NZ    . LYS A 1 57  ? 113.762 120.804 73.496  1.00 79.71  ? 1848 LYS A NZ    1 
ATOM   209  N  N     . ARG A 1 58  ? 107.176 118.152 74.868  1.00 56.73  ? 1849 ARG A N     1 
ATOM   210  C  CA    . ARG A 1 58  ? 106.296 117.986 76.023  1.00 48.05  ? 1849 ARG A CA    1 
ATOM   211  C  C     . ARG A 1 58  ? 105.050 117.242 75.569  1.00 45.11  ? 1849 ARG A C     1 
ATOM   212  O  O     . ARG A 1 58  ? 104.205 117.816 74.876  1.00 55.34  ? 1849 ARG A O     1 
ATOM   213  C  CB    . ARG A 1 58  ? 105.931 119.335 76.635  1.00 50.15  ? 1849 ARG A CB    1 
ATOM   214  C  CG    . ARG A 1 58  ? 106.959 119.883 77.607  1.00 54.14  ? 1849 ARG A CG    1 
ATOM   215  C  CD    . ARG A 1 58  ? 106.447 121.137 78.286  1.00 61.10  ? 1849 ARG A CD    1 
ATOM   216  N  NE    . ARG A 1 58  ? 105.150 120.920 78.913  1.00 64.11  ? 1849 ARG A NE    1 
ATOM   217  C  CZ    . ARG A 1 58  ? 104.934 120.980 80.219  1.00 59.54  ? 1849 ARG A CZ    1 
ATOM   218  N  NH1   . ARG A 1 58  ? 105.908 121.262 81.067  1.00 50.06  ? 1849 ARG A NH1   1 
ATOM   219  N  NH2   . ARG A 1 58  ? 103.709 120.754 80.685  1.00 56.00  ? 1849 ARG A NH2   1 
ATOM   220  N  N     . PHE A 1 59  ? 104.932 115.976 75.959  1.00 33.46  ? 1850 PHE A N     1 
ATOM   221  C  CA    . PHE A 1 59  ? 103.777 115.161 75.619  1.00 31.57  ? 1850 PHE A CA    1 
ATOM   222  C  C     . PHE A 1 59  ? 103.200 114.552 76.889  1.00 36.70  ? 1850 PHE A C     1 
ATOM   223  O  O     . PHE A 1 59  ? 103.783 114.648 77.972  1.00 47.27  ? 1850 PHE A O     1 
ATOM   224  C  CB    . PHE A 1 59  ? 104.128 114.071 74.596  1.00 33.11  ? 1850 PHE A CB    1 
ATOM   225  C  CG    . PHE A 1 59  ? 105.498 113.481 74.769  1.00 33.29  ? 1850 PHE A CG    1 
ATOM   226  C  CD1   . PHE A 1 59  ? 106.614 114.109 74.242  1.00 45.21  ? 1850 PHE A CD1   1 
ATOM   227  C  CD2   . PHE A 1 59  ? 105.666 112.281 75.432  1.00 30.83  ? 1850 PHE A CD2   1 
ATOM   228  C  CE1   . PHE A 1 59  ? 107.871 113.561 74.394  1.00 50.12  ? 1850 PHE A CE1   1 
ATOM   229  C  CE2   . PHE A 1 59  ? 106.917 111.725 75.582  1.00 40.15  ? 1850 PHE A CE2   1 
ATOM   230  C  CZ    . PHE A 1 59  ? 108.022 112.367 75.065  1.00 52.66  ? 1850 PHE A CZ    1 
ATOM   231  N  N     . SER A 1 60  ? 102.035 113.926 76.750  1.00 31.19  ? 1851 SER A N     1 
ATOM   232  C  CA    . SER A 1 60  ? 101.233 113.469 77.881  1.00 26.84  ? 1851 SER A CA    1 
ATOM   233  C  C     . SER A 1 60  ? 100.721 112.054 77.653  1.00 24.69  ? 1851 SER A C     1 
ATOM   234  O  O     . SER A 1 60  ? 99.525  111.781 77.765  1.00 33.95  ? 1851 SER A O     1 
ATOM   235  C  CB    . SER A 1 60  ? 100.071 114.420 78.133  1.00 34.79  ? 1851 SER A CB    1 
ATOM   236  O  OG    . SER A 1 60  ? 99.374  114.081 79.319  1.00 37.28  ? 1851 SER A OG    1 
ATOM   237  N  N     . ILE A 1 61  ? 101.624 111.131 77.306  1.00 23.26  ? 1852 ILE A N     1 
ATOM   238  C  CA    . ILE A 1 61  ? 101.196 109.767 77.006  1.00 27.35  ? 1852 ILE A CA    1 
ATOM   239  C  C     . ILE A 1 61  ? 100.446 109.170 78.195  1.00 26.96  ? 1852 ILE A C     1 
ATOM   240  O  O     . ILE A 1 61  ? 100.617 109.576 79.351  1.00 27.63  ? 1852 ILE A O     1 
ATOM   241  C  CB    . ILE A 1 61  ? 102.381 108.871 76.613  1.00 26.19  ? 1852 ILE A CB    1 
ATOM   242  C  CG1   . ILE A 1 61  ? 102.925 108.126 77.833  1.00 24.98  ? 1852 ILE A CG1   1 
ATOM   243  C  CG2   . ILE A 1 61  ? 103.480 109.691 75.975  1.00 31.22  ? 1852 ILE A CG2   1 
ATOM   244  C  CD1   . ILE A 1 61  ? 103.978 107.099 77.496  1.00 37.11  ? 1852 ILE A CD1   1 
ATOM   245  N  N     . SER A 1 62  ? 99.586  108.204 77.894  1.00 36.52  ? 1853 SER A N     1 
ATOM   246  C  CA    . SER A 1 62  ? 98.817  107.501 78.909  1.00 42.14  ? 1853 SER A CA    1 
ATOM   247  C  C     . SER A 1 62  ? 98.557  106.084 78.412  1.00 42.99  ? 1853 SER A C     1 
ATOM   248  O  O     . SER A 1 62  ? 99.095  105.661 77.386  1.00 51.55  ? 1853 SER A O     1 
ATOM   249  C  CB    . SER A 1 62  ? 97.521  108.252 79.230  1.00 35.63  ? 1853 SER A CB    1 
ATOM   250  O  OG    . SER A 1 62  ? 96.908  107.717 80.389  1.00 38.62  ? 1853 SER A OG    1 
ATOM   251  N  N     . LEU A 1 63  ? 97.729  105.346 79.143  1.00 33.90  ? 1854 LEU A N     1 
ATOM   252  C  CA    . LEU A 1 63  ? 97.437  103.961 78.818  1.00 39.98  ? 1854 LEU A CA    1 
ATOM   253  C  C     . LEU A 1 63  ? 95.932  103.754 78.747  1.00 56.65  ? 1854 LEU A C     1 
ATOM   254  O  O     . LEU A 1 63  ? 95.150  104.485 79.359  1.00 61.33  ? 1854 LEU A O     1 
ATOM   255  C  CB    . LEU A 1 63  ? 98.052  103.001 79.844  1.00 40.09  ? 1854 LEU A CB    1 
ATOM   256  C  CG    . LEU A 1 63  ? 99.476  102.517 79.564  1.00 45.33  ? 1854 LEU A CG    1 
ATOM   257  C  CD1   . LEU A 1 63  ? 99.589  101.960 78.155  1.00 43.66  ? 1854 LEU A CD1   1 
ATOM   258  C  CD2   . LEU A 1 63  ? 100.487 103.628 79.789  1.00 47.30  ? 1854 LEU A CD2   1 
ATOM   259  N  N     . ALA A 1 64  ? 95.538  102.742 77.979  1.00 57.25  ? 1855 ALA A N     1 
ATOM   260  C  CA    . ALA A 1 64  ? 94.146  102.343 77.834  1.00 60.71  ? 1855 ALA A CA    1 
ATOM   261  C  C     . ALA A 1 64  ? 94.028  100.868 78.182  1.00 70.53  ? 1855 ALA A C     1 
ATOM   262  O  O     . ALA A 1 64  ? 94.830  100.053 77.718  1.00 71.87  ? 1855 ALA A O     1 
ATOM   263  C  CB    . ALA A 1 64  ? 93.640  102.596 76.412  1.00 59.77  ? 1855 ALA A CB    1 
ATOM   264  N  N     . CYS A 1 65  ? 93.041  100.531 79.004  1.00 77.08  ? 1856 CYS A N     1 
ATOM   265  C  CA    . CYS A 1 65  ? 92.830  99.162  79.445  1.00 81.30  ? 1856 CYS A CA    1 
ATOM   266  C  C     . CYS A 1 65  ? 91.358  98.802  79.316  1.00 89.88  ? 1856 CYS A C     1 
ATOM   267  O  O     . CYS A 1 65  ? 90.482  99.603  79.655  1.00 90.20  ? 1856 CYS A O     1 
ATOM   268  C  CB    . CYS A 1 65  ? 93.294  98.969  80.890  1.00 76.90  ? 1856 CYS A CB    1 
ATOM   269  S  SG    . CYS A 1 65  ? 94.927  99.651  81.235  1.00 85.42  ? 1856 CYS A SG    1 
ATOM   270  N  N     . GLU A 1 66  ? 91.094  97.596  78.821  1.00 94.60  ? 1857 GLU A N     1 
ATOM   271  C  CA    . GLU A 1 66  ? 89.740  97.087  78.661  1.00 95.14  ? 1857 GLU A CA    1 
ATOM   272  C  C     . GLU A 1 66  ? 89.667  95.677  79.234  1.00 102.26 ? 1857 GLU A C     1 
ATOM   273  O  O     . GLU A 1 66  ? 90.648  95.142  79.757  1.00 102.58 ? 1857 GLU A O     1 
ATOM   274  C  CB    . GLU A 1 66  ? 89.309  97.101  77.188  1.00 95.50  ? 1857 GLU A CB    1 
ATOM   275  C  CG    . GLU A 1 66  ? 89.362  98.471  76.533  1.00 95.64  ? 1857 GLU A CG    1 
ATOM   276  C  CD    . GLU A 1 66  ? 88.955  98.431  75.074  1.00 98.23  ? 1857 GLU A CD    1 
ATOM   277  O  OE1   . GLU A 1 66  ? 88.981  97.333  74.480  1.00 101.42 ? 1857 GLU A OE1   1 
ATOM   278  O  OE2   . GLU A 1 66  ? 88.614  99.496  74.519  1.00 93.64  ? 1857 GLU A OE2   1 
ATOM   279  N  N     . LYS A 1 67  ? 88.486  95.075  79.139  1.00 103.66 ? 1858 LYS A N     1 
ATOM   280  C  CA    . LYS A 1 67  ? 88.297  93.708  79.592  1.00 106.39 ? 1858 LYS A CA    1 
ATOM   281  C  C     . LYS A 1 67  ? 88.770  92.724  78.523  1.00 108.13 ? 1858 LYS A C     1 
ATOM   282  O  O     . LYS A 1 67  ? 89.104  93.098  77.396  1.00 108.51 ? 1858 LYS A O     1 
ATOM   283  C  CB    . LYS A 1 67  ? 86.831  93.456  79.940  1.00 107.18 ? 1858 LYS A CB    1 
ATOM   284  C  CG    . LYS A 1 67  ? 86.494  93.661  81.408  1.00 100.94 ? 1858 LYS A CG    1 
ATOM   285  C  CD    . LYS A 1 67  ? 86.529  95.132  81.787  1.00 100.26 ? 1858 LYS A CD    1 
ATOM   286  C  CE    . LYS A 1 67  ? 85.655  95.968  80.866  1.00 95.51  ? 1858 LYS A CE    1 
ATOM   287  N  NZ    . LYS A 1 67  ? 85.509  97.365  81.360  1.00 94.29  ? 1858 LYS A NZ    1 
ATOM   288  N  N     . ILE A 1 68  ? 88.805  91.444  78.898  1.00 112.46 ? 1859 ILE A N     1 
ATOM   289  C  CA    . ILE A 1 68  ? 89.215  90.405  77.956  1.00 118.69 ? 1859 ILE A CA    1 
ATOM   290  C  C     . ILE A 1 68  ? 88.233  90.326  76.793  1.00 123.44 ? 1859 ILE A C     1 
ATOM   291  O  O     . ILE A 1 68  ? 88.632  90.253  75.625  1.00 122.01 ? 1859 ILE A O     1 
ATOM   292  C  CB    . ILE A 1 68  ? 89.348  89.050  78.673  1.00 122.49 ? 1859 ILE A CB    1 
ATOM   293  C  CG1   . ILE A 1 68  ? 90.300  89.168  79.863  1.00 117.69 ? 1859 ILE A CG1   1 
ATOM   294  C  CG2   . ILE A 1 68  ? 89.834  87.982  77.707  1.00 123.91 ? 1859 ILE A CG2   1 
ATOM   295  C  CD1   . ILE A 1 68  ? 91.685  89.647  79.491  1.00 115.32 ? 1859 ILE A CD1   1 
ATOM   296  N  N     . ARG A 1 69  ? 86.934  90.349  77.101  1.00 126.84 ? 1860 ARG A N     1 
ATOM   297  C  CA    . ARG A 1 69  ? 85.875  90.263  76.093  1.00 124.09 ? 1860 ARG A CA    1 
ATOM   298  C  C     . ARG A 1 69  ? 86.041  89.022  75.219  1.00 125.91 ? 1860 ARG A C     1 
ATOM   299  O  O     . ARG A 1 69  ? 85.858  89.060  74.001  1.00 125.06 ? 1860 ARG A O     1 
ATOM   300  C  CB    . ARG A 1 69  ? 85.823  91.531  75.238  1.00 117.88 ? 1860 ARG A CB    1 
ATOM   301  N  N     . SER A 1 70  ? 86.396  87.908  75.852  1.00 128.52 ? 1861 SER A N     1 
ATOM   302  C  CA    . SER A 1 70  ? 86.594  86.651  75.139  1.00 129.98 ? 1861 SER A CA    1 
ATOM   303  C  C     . SER A 1 70  ? 85.258  86.016  74.768  1.00 125.89 ? 1861 SER A C     1 
ATOM   304  O  O     . SER A 1 70  ? 85.128  85.392  73.714  1.00 120.83 ? 1861 SER A O     1 
ATOM   305  C  CB    . SER A 1 70  ? 87.422  85.681  75.984  1.00 124.58 ? 1861 SER A CB    1 
ATOM   306  N  N     . ILE A 1 94  ? 94.148  88.169  74.750  1.00 127.64 ? 1885 ILE A N     1 
ATOM   307  C  CA    . ILE A 1 94  ? 95.540  87.761  74.883  1.00 129.71 ? 1885 ILE A CA    1 
ATOM   308  C  C     . ILE A 1 94  ? 96.174  87.607  73.506  1.00 127.89 ? 1885 ILE A C     1 
ATOM   309  O  O     . ILE A 1 94  ? 95.710  86.815  72.685  1.00 129.89 ? 1885 ILE A O     1 
ATOM   310  C  CB    . ILE A 1 94  ? 95.663  86.458  75.691  1.00 135.33 ? 1885 ILE A CB    1 
ATOM   311  C  CG1   . ILE A 1 94  ? 94.918  86.586  77.021  1.00 131.65 ? 1885 ILE A CG1   1 
ATOM   312  C  CG2   . ILE A 1 94  ? 97.125  86.112  75.924  1.00 128.85 ? 1885 ILE A CG2   1 
ATOM   313  C  CD1   . ILE A 1 94  ? 94.931  85.321  77.851  1.00 128.93 ? 1885 ILE A CD1   1 
ATOM   314  N  N     . ARG A 1 95  ? 97.226  88.389  73.259  1.00 123.26 ? 1886 ARG A N     1 
ATOM   315  C  CA    . ARG A 1 95  ? 98.018  88.413  72.032  1.00 122.01 ? 1886 ARG A CA    1 
ATOM   316  C  C     . ARG A 1 95  ? 97.248  88.963  70.837  1.00 123.87 ? 1886 ARG A C     1 
ATOM   317  O  O     . ARG A 1 95  ? 97.828  89.085  69.750  1.00 120.29 ? 1886 ARG A O     1 
ATOM   318  C  CB    . ARG A 1 95  ? 98.580  87.031  71.667  1.00 119.13 ? 1886 ARG A CB    1 
ATOM   319  C  CG    . ARG A 1 95  ? 99.502  86.439  72.721  1.00 116.78 ? 1886 ARG A CG    1 
ATOM   320  C  CD    . ARG A 1 95  ? 100.064 85.097  72.276  1.00 116.52 ? 1886 ARG A CD    1 
ATOM   321  N  NE    . ARG A 1 95  ? 100.975 84.533  73.264  1.00 125.23 ? 1886 ARG A NE    1 
ATOM   322  C  CZ    . ARG A 1 95  ? 100.611 83.702  74.231  1.00 128.46 ? 1886 ARG A CZ    1 
ATOM   323  N  NH1   . ARG A 1 95  ? 99.353  83.315  74.373  1.00 127.54 ? 1886 ARG A NH1   1 
ATOM   324  N  NH2   . ARG A 1 95  ? 101.531 83.249  75.078  1.00 124.97 ? 1886 ARG A NH2   1 
ATOM   325  N  N     . ASP A 1 96  ? 95.969  89.299  70.992  1.00 123.86 ? 1887 ASP A N     1 
ATOM   326  C  CA    . ASP A 1 96  ? 95.180  89.897  69.922  1.00 119.42 ? 1887 ASP A CA    1 
ATOM   327  C  C     . ASP A 1 96  ? 94.662  91.277  70.290  1.00 115.62 ? 1887 ASP A C     1 
ATOM   328  O  O     . ASP A 1 96  ? 94.822  92.223  69.510  1.00 110.22 ? 1887 ASP A O     1 
ATOM   329  C  CB    . ASP A 1 96  ? 94.006  88.977  69.551  1.00 124.40 ? 1887 ASP A CB    1 
ATOM   330  C  CG    . ASP A 1 96  ? 94.463  87.651  68.975  1.00 128.74 ? 1887 ASP A CG    1 
ATOM   331  O  OD1   . ASP A 1 96  ? 94.930  86.792  69.751  1.00 133.28 ? 1887 ASP A OD1   1 
ATOM   332  O  OD2   . ASP A 1 96  ? 94.355  87.468  67.744  1.00 126.97 ? 1887 ASP A OD2   1 
ATOM   333  N  N     . ASP A 1 97  ? 94.044  91.422  71.464  1.00 114.17 ? 1888 ASP A N     1 
ATOM   334  C  CA    . ASP A 1 97  ? 93.587  92.736  71.898  1.00 113.50 ? 1888 ASP A CA    1 
ATOM   335  C  C     . ASP A 1 97  ? 94.748  93.608  72.356  1.00 109.67 ? 1888 ASP A C     1 
ATOM   336  O  O     . ASP A 1 97  ? 94.688  94.836  72.229  1.00 103.87 ? 1888 ASP A O     1 
ATOM   337  C  CB    . ASP A 1 97  ? 92.556  92.592  73.017  1.00 110.25 ? 1888 ASP A CB    1 
ATOM   338  C  CG    . ASP A 1 97  ? 91.583  93.755  73.067  1.00 111.54 ? 1888 ASP A CG    1 
ATOM   339  O  OD1   . ASP A 1 97  ? 91.809  94.752  72.350  1.00 109.86 ? 1888 ASP A OD1   1 
ATOM   340  O  OD2   . ASP A 1 97  ? 90.593  93.671  73.823  1.00 110.11 ? 1888 ASP A OD2   1 
ATOM   341  N  N     . GLY A 1 98  ? 95.801  93.000  72.886  1.00 107.95 ? 1889 GLY A N     1 
ATOM   342  C  CA    . GLY A 1 98  ? 96.956  93.752  73.335  1.00 100.27 ? 1889 GLY A CA    1 
ATOM   343  C  C     . GLY A 1 98  ? 97.831  92.893  74.231  1.00 100.65 ? 1889 GLY A C     1 
ATOM   344  O  O     . GLY A 1 98  ? 97.722  91.669  74.239  1.00 104.66 ? 1889 GLY A O     1 
ATOM   345  N  N     . PHE A 1 99  ? 98.702  93.570  74.974  1.00 96.01  ? 1890 PHE A N     1 
ATOM   346  C  CA    . PHE A 1 99  ? 99.577  92.902  75.926  1.00 93.56  ? 1890 PHE A CA    1 
ATOM   347  C  C     . PHE A 1 99  ? 98.854  92.738  77.256  1.00 91.54  ? 1890 PHE A C     1 
ATOM   348  O  O     . PHE A 1 99  ? 98.373  93.735  77.811  1.00 90.58  ? 1890 PHE A O     1 
ATOM   349  C  CB    . PHE A 1 99  ? 100.858 93.694  76.123  1.00 85.65  ? 1890 PHE A CB    1 
ATOM   350  C  CG    . PHE A 1 99  ? 101.463 94.195  74.842  1.00 85.12  ? 1890 PHE A CG    1 
ATOM   351  C  CD1   . PHE A 1 99  ? 102.309 93.389  74.099  1.00 86.44  ? 1890 PHE A CD1   1 
ATOM   352  C  CD2   . PHE A 1 99  ? 101.188 95.471  74.382  1.00 86.99  ? 1890 PHE A CD2   1 
ATOM   353  C  CE1   . PHE A 1 99  ? 102.867 93.846  72.922  1.00 83.42  ? 1890 PHE A CE1   1 
ATOM   354  C  CE2   . PHE A 1 99  ? 101.742 95.933  73.205  1.00 90.83  ? 1890 PHE A CE2   1 
ATOM   355  C  CZ    . PHE A 1 99  ? 102.583 95.119  72.474  1.00 89.45  ? 1890 PHE A CZ    1 
ATOM   356  N  N     . PRO A 1 100 ? 98.740  91.523  77.790  1.00 93.35  ? 1891 PRO A N     1 
ATOM   357  C  CA    . PRO A 1 100 ? 98.058  91.348  79.079  1.00 92.34  ? 1891 PRO A CA    1 
ATOM   358  C  C     . PRO A 1 100 ? 98.789  92.071  80.200  1.00 86.72  ? 1891 PRO A C     1 
ATOM   359  O  O     . PRO A 1 100 ? 100.020 92.128  80.232  1.00 78.84  ? 1891 PRO A O     1 
ATOM   360  C  CB    . PRO A 1 100 ? 98.072  89.829  79.283  1.00 95.11  ? 1891 PRO A CB    1 
ATOM   361  C  CG    . PRO A 1 100 ? 99.211  89.344  78.449  1.00 102.31 ? 1891 PRO A CG    1 
ATOM   362  C  CD    . PRO A 1 100 ? 99.263  90.254  77.259  1.00 97.98  ? 1891 PRO A CD    1 
ATOM   363  N  N     . ILE A 1 101 ? 98.014  92.620  81.129  1.00 84.77  ? 1892 ILE A N     1 
ATOM   364  C  CA    . ILE A 1 101 ? 98.555  93.357  82.265  1.00 75.91  ? 1892 ILE A CA    1 
ATOM   365  C  C     . ILE A 1 101 ? 98.867  92.374  83.384  1.00 84.18  ? 1892 ILE A C     1 
ATOM   366  O  O     . ILE A 1 101 ? 98.025  91.543  83.746  1.00 89.72  ? 1892 ILE A O     1 
ATOM   367  C  CB    . ILE A 1 101 ? 97.571  94.439  82.738  1.00 72.67  ? 1892 ILE A CB    1 
ATOM   368  C  CG1   . ILE A 1 101 ? 97.585  95.627  81.776  1.00 74.50  ? 1892 ILE A CG1   1 
ATOM   369  C  CG2   . ILE A 1 101 ? 97.904  94.889  84.151  1.00 72.11  ? 1892 ILE A CG2   1 
ATOM   370  C  CD1   . ILE A 1 101 ? 96.935  96.870  82.336  1.00 70.12  ? 1892 ILE A CD1   1 
ATOM   371  N  N     . LYS A 1 102 ? 100.079 92.463  83.928  1.00 84.67  ? 1893 LYS A N     1 
ATOM   372  C  CA    . LYS A 1 102 ? 100.468 91.591  85.027  1.00 85.55  ? 1893 LYS A CA    1 
ATOM   373  C  C     . LYS A 1 102 ? 99.611  91.870  86.256  1.00 88.67  ? 1893 LYS A C     1 
ATOM   374  O  O     . LYS A 1 102 ? 99.257  93.017  86.542  1.00 90.43  ? 1893 LYS A O     1 
ATOM   375  C  CB    . LYS A 1 102 ? 101.948 91.784  85.360  1.00 68.82  ? 1893 LYS A CB    1 
ATOM   376  C  CG    . LYS A 1 102 ? 102.869 91.715  84.154  1.00 65.60  ? 1893 LYS A CG    1 
ATOM   377  C  CD    . LYS A 1 102 ? 102.648 90.437  83.361  1.00 71.73  ? 1893 LYS A CD    1 
ATOM   378  C  CE    . LYS A 1 102 ? 103.905 90.023  82.614  1.00 68.10  ? 1893 LYS A CE    1 
ATOM   379  N  NZ    . LYS A 1 102 ? 103.587 89.393  81.304  1.00 75.87  ? 1893 LYS A NZ    1 
ATOM   380  N  N     . GLY A 1 103 ? 99.277  90.809  86.985  1.00 86.17  ? 1894 GLY A N     1 
ATOM   381  C  CA    . GLY A 1 103 ? 98.423  90.935  88.148  1.00 91.17  ? 1894 GLY A CA    1 
ATOM   382  C  C     . GLY A 1 103 ? 96.955  90.771  87.818  1.00 101.30 ? 1894 GLY A C     1 
ATOM   383  O  O     . GLY A 1 103 ? 96.331  89.780  88.209  1.00 102.62 ? 1894 GLY A O     1 
ATOM   384  N  N     . CYS A 1 104 ? 96.390  91.737  87.096  1.00 103.94 ? 1895 CYS A N     1 
ATOM   385  C  CA    . CYS A 1 104 ? 94.992  91.677  86.671  1.00 102.07 ? 1895 CYS A CA    1 
ATOM   386  C  C     . CYS A 1 104 ? 94.936  90.931  85.345  1.00 101.10 ? 1895 CYS A C     1 
ATOM   387  O  O     . CYS A 1 104 ? 95.078  91.515  84.270  1.00 101.89 ? 1895 CYS A O     1 
ATOM   388  C  CB    . CYS A 1 104 ? 94.398  93.075  86.558  1.00 103.85 ? 1895 CYS A CB    1 
ATOM   389  S  SG    . CYS A 1 104 ? 94.479  94.049  88.078  1.00 126.54 ? 1895 CYS A SG    1 
ATOM   390  N  N     . ASP A 1 105 ? 94.725  89.615  85.422  1.00 99.10  ? 1896 ASP A N     1 
ATOM   391  C  CA    . ASP A 1 105 ? 94.664  88.798  84.216  1.00 102.86 ? 1896 ASP A CA    1 
ATOM   392  C  C     . ASP A 1 105 ? 93.411  89.069  83.395  1.00 104.59 ? 1896 ASP A C     1 
ATOM   393  O  O     . ASP A 1 105 ? 93.367  88.704  82.216  1.00 97.41  ? 1896 ASP A O     1 
ATOM   394  C  CB    . ASP A 1 105 ? 94.736  87.315  84.581  1.00 93.19  ? 1896 ASP A CB    1 
ATOM   395  N  N     . ASP A 1 106 ? 92.398  89.696  83.987  1.00 107.26 ? 1897 ASP A N     1 
ATOM   396  C  CA    . ASP A 1 106 ? 91.160  90.016  83.290  1.00 102.01 ? 1897 ASP A CA    1 
ATOM   397  C  C     . ASP A 1 106 ? 91.213  91.355  82.567  1.00 103.51 ? 1897 ASP A C     1 
ATOM   398  O  O     . ASP A 1 106 ? 90.225  91.739  81.934  1.00 102.56 ? 1897 ASP A O     1 
ATOM   399  C  CB    . ASP A 1 106 ? 89.981  90.007  84.271  1.00 101.94 ? 1897 ASP A CB    1 
ATOM   400  C  CG    . ASP A 1 106 ? 90.093  91.083  85.337  1.00 103.15 ? 1897 ASP A CG    1 
ATOM   401  O  OD1   . ASP A 1 106 ? 91.143  91.161  86.008  1.00 109.19 ? 1897 ASP A OD1   1 
ATOM   402  O  OD2   . ASP A 1 106 ? 89.125  91.855  85.504  1.00 92.29  ? 1897 ASP A OD2   1 
ATOM   403  N  N     . THR A 1 107 ? 92.332  92.069  82.643  1.00 106.33 ? 1898 THR A N     1 
ATOM   404  C  CA    . THR A 1 107 ? 92.485  93.369  82.007  1.00 107.24 ? 1898 THR A CA    1 
ATOM   405  C  C     . THR A 1 107 ? 93.545  93.290  80.916  1.00 103.18 ? 1898 THR A C     1 
ATOM   406  O  O     . THR A 1 107 ? 94.574  92.629  81.085  1.00 100.43 ? 1898 THR A O     1 
ATOM   407  C  CB    . THR A 1 107 ? 92.866  94.442  83.031  1.00 101.06 ? 1898 THR A CB    1 
ATOM   408  O  OG1   . THR A 1 107 ? 92.112  94.246  84.233  1.00 101.61 ? 1898 THR A OG1   1 
ATOM   409  C  CG2   . THR A 1 107 ? 92.568  95.824  82.483  1.00 87.74  ? 1898 THR A CG2   1 
ATOM   410  N  N     . LEU A 1 108 ? 93.286  93.966  79.800  1.00 101.67 ? 1899 LEU A N     1 
ATOM   411  C  CA    . LEU A 1 108 ? 94.160  93.939  78.636  1.00 99.64  ? 1899 LEU A CA    1 
ATOM   412  C  C     . LEU A 1 108 ? 94.443  95.360  78.177  1.00 95.33  ? 1899 LEU A C     1 
ATOM   413  O  O     . LEU A 1 108 ? 93.528  96.185  78.086  1.00 98.01  ? 1899 LEU A O     1 
ATOM   414  C  CB    . LEU A 1 108 ? 93.524  93.141  77.490  1.00 103.96 ? 1899 LEU A CB    1 
ATOM   415  C  CG    . LEU A 1 108 ? 94.087  91.750  77.200  1.00 109.99 ? 1899 LEU A CG    1 
ATOM   416  C  CD1   . LEU A 1 108 ? 93.123  90.959  76.332  1.00 116.42 ? 1899 LEU A CD1   1 
ATOM   417  C  CD2   . LEU A 1 108 ? 95.444  91.851  76.535  1.00 102.40 ? 1899 LEU A CD2   1 
ATOM   418  N  N     . VAL A 1 109 ? 95.714  95.643  77.883  1.00 88.45  ? 1900 VAL A N     1 
ATOM   419  C  CA    . VAL A 1 109 ? 96.076  96.957  77.367  1.00 83.18  ? 1900 VAL A CA    1 
ATOM   420  C  C     . VAL A 1 109 ? 95.605  97.082  75.921  1.00 87.64  ? 1900 VAL A C     1 
ATOM   421  O  O     . VAL A 1 109 ? 95.512  96.092  75.181  1.00 88.66  ? 1900 VAL A O     1 
ATOM   422  C  CB    . VAL A 1 109 ? 97.592  97.203  77.494  1.00 69.59  ? 1900 VAL A CB    1 
ATOM   423  C  CG1   . VAL A 1 109 ? 98.345  96.606  76.317  1.00 72.83  ? 1900 VAL A CG1   1 
ATOM   424  C  CG2   . VAL A 1 109 ? 97.880  98.690  77.616  1.00 62.78  ? 1900 VAL A CG2   1 
ATOM   425  N  N     . VAL A 1 110 ? 95.274  98.308  75.521  1.00 83.19  ? 1901 VAL A N     1 
ATOM   426  C  CA    . VAL A 1 110 ? 94.705  98.548  74.200  1.00 80.26  ? 1901 VAL A CA    1 
ATOM   427  C  C     . VAL A 1 110 ? 95.505  99.611  73.457  1.00 78.37  ? 1901 VAL A C     1 
ATOM   428  O  O     . VAL A 1 110 ? 95.985  99.372  72.344  1.00 79.72  ? 1901 VAL A O     1 
ATOM   429  C  CB    . VAL A 1 110 ? 93.223  98.948  74.307  1.00 81.09  ? 1901 VAL A CB    1 
ATOM   430  C  CG1   . VAL A 1 110 ? 92.738  99.550  73.003  1.00 78.60  ? 1901 VAL A CG1   1 
ATOM   431  C  CG2   . VAL A 1 110 ? 92.384  97.739  74.679  1.00 83.18  ? 1901 VAL A CG2   1 
ATOM   432  N  N     . GLY A 1 111 ? 95.657  100.787 74.061  1.00 72.15  ? 1902 GLY A N     1 
ATOM   433  C  CA    . GLY A 1 111 ? 96.299  101.876 73.354  1.00 63.68  ? 1902 GLY A CA    1 
ATOM   434  C  C     . GLY A 1 111 ? 96.896  102.907 74.287  1.00 59.46  ? 1902 GLY A C     1 
ATOM   435  O  O     . GLY A 1 111 ? 96.769  102.828 75.509  1.00 65.27  ? 1902 GLY A O     1 
ATOM   436  N  N     . LEU A 1 112 ? 97.568  103.875 73.675  1.00 48.13  ? 1903 LEU A N     1 
ATOM   437  C  CA    . LEU A 1 112 ? 98.115  105.047 74.338  1.00 44.90  ? 1903 LEU A CA    1 
ATOM   438  C  C     . LEU A 1 112 ? 97.351  106.286 73.895  1.00 46.48  ? 1903 LEU A C     1 
ATOM   439  O  O     . LEU A 1 112 ? 96.656  106.281 72.877  1.00 54.03  ? 1903 LEU A O     1 
ATOM   440  C  CB    . LEU A 1 112 ? 99.604  105.221 74.018  1.00 41.94  ? 1903 LEU A CB    1 
ATOM   441  C  CG    . LEU A 1 112 ? 100.631 104.404 74.800  1.00 56.12  ? 1903 LEU A CG    1 
ATOM   442  C  CD1   . LEU A 1 112 ? 100.656 102.966 74.324  1.00 56.50  ? 1903 LEU A CD1   1 
ATOM   443  C  CD2   . LEU A 1 112 ? 102.006 105.035 74.667  1.00 47.78  ? 1903 LEU A CD2   1 
ATOM   444  N  N     . ALA A 1 113 ? 97.503  107.364 74.658  1.00 41.43  ? 1904 ALA A N     1 
ATOM   445  C  CA    . ALA A 1 113 ? 96.862  108.631 74.329  1.00 41.80  ? 1904 ALA A CA    1 
ATOM   446  C  C     . ALA A 1 113 ? 97.845  109.757 74.596  1.00 40.44  ? 1904 ALA A C     1 
ATOM   447  O  O     . ALA A 1 113 ? 98.213  109.999 75.749  1.00 49.98  ? 1904 ALA A O     1 
ATOM   448  C  CB    . ALA A 1 113 ? 95.581  108.829 75.139  1.00 44.42  ? 1904 ALA A CB    1 
ATOM   449  N  N     . VAL A 1 114 ? 98.257  110.450 73.538  1.00 33.45  ? 1905 VAL A N     1 
ATOM   450  C  CA    . VAL A 1 114 ? 99.264  111.500 73.615  1.00 27.37  ? 1905 VAL A CA    1 
ATOM   451  C  C     . VAL A 1 114 ? 98.619  112.819 73.218  1.00 36.47  ? 1905 VAL A C     1 
ATOM   452  O  O     . VAL A 1 114 ? 98.020  112.922 72.143  1.00 50.02  ? 1905 VAL A O     1 
ATOM   453  C  CB    . VAL A 1 114 ? 100.468 111.191 72.709  1.00 30.68  ? 1905 VAL A CB    1 
ATOM   454  C  CG1   . VAL A 1 114 ? 101.558 112.222 72.911  1.00 36.90  ? 1905 VAL A CG1   1 
ATOM   455  C  CG2   . VAL A 1 114 ? 100.988 109.791 72.980  1.00 36.16  ? 1905 VAL A CG2   1 
ATOM   456  N  N     . CYS A 1 115 ? 98.746  113.824 74.080  1.00 36.38  ? 1906 CYS A N     1 
ATOM   457  C  CA    . CYS A 1 115 ? 98.201  115.152 73.823  1.00 44.97  ? 1906 CYS A CA    1 
ATOM   458  C  C     . CYS A 1 115 ? 99.250  116.190 74.186  1.00 52.91  ? 1906 CYS A C     1 
ATOM   459  O  O     . CYS A 1 115 ? 99.654  116.284 75.349  1.00 58.52  ? 1906 CYS A O     1 
ATOM   460  C  CB    . CYS A 1 115 ? 96.916  115.387 74.620  1.00 49.83  ? 1906 CYS A CB    1 
ATOM   461  S  SG    . CYS A 1 115 ? 96.510  117.129 74.870  1.00 65.01  ? 1906 CYS A SG    1 
ATOM   462  N  N     . TRP A 1 116 ? 99.686  116.970 73.197  1.00 55.47  ? 1907 TRP A N     1 
ATOM   463  C  CA    . TRP A 1 116 ? 100.710 117.987 73.396  1.00 64.61  ? 1907 TRP A CA    1 
ATOM   464  C  C     . TRP A 1 116 ? 100.163 119.400 73.217  1.00 70.44  ? 1907 TRP A C     1 
ATOM   465  O  O     . TRP A 1 116 ? 100.864 120.284 72.719  1.00 70.57  ? 1907 TRP A O     1 
ATOM   466  C  CB    . TRP A 1 116 ? 101.889 117.753 72.453  1.00 61.31  ? 1907 TRP A CB    1 
ATOM   467  C  CG    . TRP A 1 116 ? 101.487 117.535 71.031  1.00 63.60  ? 1907 TRP A CG    1 
ATOM   468  C  CD1   . TRP A 1 116 ? 101.003 118.468 70.162  1.00 65.39  ? 1907 TRP A CD1   1 
ATOM   469  C  CD2   . TRP A 1 116 ? 101.540 116.302 70.306  1.00 61.57  ? 1907 TRP A CD2   1 
ATOM   470  N  NE1   . TRP A 1 116 ? 100.748 117.892 68.942  1.00 61.88  ? 1907 TRP A NE1   1 
ATOM   471  C  CE2   . TRP A 1 116 ? 101.070 116.563 69.005  1.00 58.64  ? 1907 TRP A CE2   1 
ATOM   472  C  CE3   . TRP A 1 116 ? 101.938 115.003 70.632  1.00 60.28  ? 1907 TRP A CE3   1 
ATOM   473  C  CZ2   . TRP A 1 116 ? 100.987 115.573 68.031  1.00 55.67  ? 1907 TRP A CZ2   1 
ATOM   474  C  CZ3   . TRP A 1 116 ? 101.855 114.023 69.664  1.00 63.24  ? 1907 TRP A CZ3   1 
ATOM   475  C  CH2   . TRP A 1 116 ? 101.383 114.312 68.379  1.00 58.53  ? 1907 TRP A CH2   1 
ATOM   476  N  N     . GLY A 1 117 ? 98.921  119.626 73.615  1.00 67.61  ? 1908 GLY A N     1 
ATOM   477  C  CA    . GLY A 1 117 ? 98.318  120.947 73.563  1.00 70.25  ? 1908 GLY A CA    1 
ATOM   478  C  C     . GLY A 1 117 ? 96.882  120.903 73.085  1.00 68.96  ? 1908 GLY A C     1 
ATOM   479  O  O     . GLY A 1 117 ? 96.499  120.086 72.247  1.00 67.42  ? 1908 GLY A O     1 
ATOM   480  N  N     . GLY A 1 118 ? 96.066  121.807 73.626  1.00 70.49  ? 1909 GLY A N     1 
ATOM   481  C  CA    . GLY A 1 118 ? 94.676  121.891 73.225  1.00 75.84  ? 1909 GLY A CA    1 
ATOM   482  C  C     . GLY A 1 118 ? 93.890  120.649 73.611  1.00 74.24  ? 1909 GLY A C     1 
ATOM   483  O  O     . GLY A 1 118 ? 94.176  119.974 74.605  1.00 74.56  ? 1909 GLY A O     1 
ATOM   484  N  N     . ARG A 1 119 ? 92.877  120.344 72.801  1.00 67.47  ? 1910 ARG A N     1 
ATOM   485  C  CA    . ARG A 1 119 ? 92.015  119.188 73.009  1.00 62.62  ? 1910 ARG A CA    1 
ATOM   486  C  C     . ARG A 1 119 ? 92.252  118.110 71.956  1.00 62.84  ? 1910 ARG A C     1 
ATOM   487  O  O     . ARG A 1 119 ? 91.339  117.357 71.613  1.00 68.30  ? 1910 ARG A O     1 
ATOM   488  C  CB    . ARG A 1 119 ? 90.548  119.613 73.011  1.00 69.35  ? 1910 ARG A CB    1 
ATOM   489  C  CG    . ARG A 1 119 ? 90.223  120.720 73.998  1.00 69.17  ? 1910 ARG A CG    1 
ATOM   490  C  CD    . ARG A 1 119 ? 88.820  121.253 73.771  1.00 73.61  ? 1910 ARG A CD    1 
ATOM   491  N  NE    . ARG A 1 119 ? 87.837  120.179 73.703  1.00 80.44  ? 1910 ARG A NE    1 
ATOM   492  C  CZ    . ARG A 1 119 ? 86.776  120.083 74.492  1.00 80.30  ? 1910 ARG A CZ    1 
ATOM   493  N  NH1   . ARG A 1 119 ? 86.518  120.994 75.415  1.00 76.95  ? 1910 ARG A NH1   1 
ATOM   494  N  NH2   . ARG A 1 119 ? 85.953  119.049 74.349  1.00 80.34  ? 1910 ARG A NH2   1 
ATOM   495  N  N     . ASP A 1 120 ? 93.473  118.028 71.435  1.00 63.08  ? 1911 ASP A N     1 
ATOM   496  C  CA    . ASP A 1 120 ? 93.819  117.089 70.374  1.00 61.50  ? 1911 ASP A CA    1 
ATOM   497  C  C     . ASP A 1 120 ? 94.505  115.881 71.000  1.00 52.86  ? 1911 ASP A C     1 
ATOM   498  O  O     . ASP A 1 120 ? 95.660  115.969 71.427  1.00 56.73  ? 1911 ASP A O     1 
ATOM   499  C  CB    . ASP A 1 120 ? 94.722  117.758 69.340  1.00 63.80  ? 1911 ASP A CB    1 
ATOM   500  C  CG    . ASP A 1 120 ? 93.995  118.082 68.052  1.00 67.05  ? 1911 ASP A CG    1 
ATOM   501  O  OD1   . ASP A 1 120 ? 93.118  117.293 67.648  1.00 64.51  ? 1911 ASP A OD1   1 
ATOM   502  O  OD2   . ASP A 1 120 ? 94.302  119.128 67.443  1.00 67.37  ? 1911 ASP A OD2   1 
ATOM   503  N  N     . ALA A 1 121 ? 93.799  114.753 71.052  1.00 48.55  ? 1912 ALA A N     1 
ATOM   504  C  CA    . ALA A 1 121 ? 94.327  113.522 71.630  1.00 41.33  ? 1912 ALA A CA    1 
ATOM   505  C  C     . ALA A 1 121 ? 94.670  112.564 70.498  1.00 45.69  ? 1912 ALA A C     1 
ATOM   506  O  O     . ALA A 1 121 ? 93.777  112.071 69.802  1.00 59.89  ? 1912 ALA A O     1 
ATOM   507  C  CB    . ALA A 1 121 ? 93.324  112.895 72.592  1.00 43.91  ? 1912 ALA A CB    1 
ATOM   508  N  N     . TYR A 1 122 ? 95.960  112.296 70.320  1.00 37.99  ? 1913 TYR A N     1 
ATOM   509  C  CA    . TYR A 1 122 ? 96.436  111.415 69.255  1.00 42.55  ? 1913 TYR A CA    1 
ATOM   510  C  C     . TYR A 1 122 ? 96.504  110.000 69.811  1.00 40.66  ? 1913 TYR A C     1 
ATOM   511  O  O     . TYR A 1 122 ? 97.500  109.589 70.405  1.00 43.23  ? 1913 TYR A O     1 
ATOM   512  C  CB    . TYR A 1 122 ? 97.788  111.880 68.726  1.00 47.44  ? 1913 TYR A CB    1 
ATOM   513  C  CG    . TYR A 1 122 ? 97.784  113.259 68.098  1.00 51.16  ? 1913 TYR A CG    1 
ATOM   514  C  CD1   . TYR A 1 122 ? 97.579  114.399 68.865  1.00 54.41  ? 1913 TYR A CD1   1 
ATOM   515  C  CD2   . TYR A 1 122 ? 97.987  113.419 66.734  1.00 57.28  ? 1913 TYR A CD2   1 
ATOM   516  C  CE1   . TYR A 1 122 ? 97.574  115.655 68.292  1.00 61.96  ? 1913 TYR A CE1   1 
ATOM   517  C  CE2   . TYR A 1 122 ? 97.984  114.671 66.152  1.00 59.39  ? 1913 TYR A CE2   1 
ATOM   518  C  CZ    . TYR A 1 122 ? 97.778  115.785 66.936  1.00 66.78  ? 1913 TYR A CZ    1 
ATOM   519  O  OH    . TYR A 1 122 ? 97.775  117.035 66.360  1.00 73.74  ? 1913 TYR A OH    1 
ATOM   520  N  N     . TYR A 1 123 ? 95.429  109.243 69.614  1.00 39.27  ? 1914 TYR A N     1 
ATOM   521  C  CA    . TYR A 1 123 ? 95.374  107.884 70.129  1.00 43.61  ? 1914 TYR A CA    1 
ATOM   522  C  C     . TYR A 1 123 ? 96.299  106.979 69.326  1.00 49.55  ? 1914 TYR A C     1 
ATOM   523  O  O     . TYR A 1 123 ? 96.309  107.013 68.093  1.00 61.10  ? 1914 TYR A O     1 
ATOM   524  C  CB    . TYR A 1 123 ? 93.941  107.357 70.082  1.00 53.87  ? 1914 TYR A CB    1 
ATOM   525  C  CG    . TYR A 1 123 ? 93.832  105.863 70.280  1.00 58.52  ? 1914 TYR A CG    1 
ATOM   526  C  CD1   . TYR A 1 123 ? 93.930  105.302 71.545  1.00 58.49  ? 1914 TYR A CD1   1 
ATOM   527  C  CD2   . TYR A 1 123 ? 93.627  105.014 69.202  1.00 62.59  ? 1914 TYR A CD2   1 
ATOM   528  C  CE1   . TYR A 1 123 ? 93.830  103.938 71.730  1.00 60.39  ? 1914 TYR A CE1   1 
ATOM   529  C  CE2   . TYR A 1 123 ? 93.526  103.649 69.378  1.00 61.79  ? 1914 TYR A CE2   1 
ATOM   530  C  CZ    . TYR A 1 123 ? 93.627  103.117 70.643  1.00 62.84  ? 1914 TYR A CZ    1 
ATOM   531  O  OH    . TYR A 1 123 ? 93.526  101.758 70.818  1.00 65.50  ? 1914 TYR A OH    1 
ATOM   532  N  N     . PHE A 1 124 ? 97.074  106.168 70.035  1.00 48.36  ? 1915 PHE A N     1 
ATOM   533  C  CA    . PHE A 1 124 ? 98.029  105.237 69.452  1.00 46.93  ? 1915 PHE A CA    1 
ATOM   534  C  C     . PHE A 1 124 ? 97.537  103.823 69.721  1.00 55.57  ? 1915 PHE A C     1 
ATOM   535  O  O     . PHE A 1 124 ? 97.221  103.486 70.864  1.00 67.40  ? 1915 PHE A O     1 
ATOM   536  C  CB    . PHE A 1 124 ? 99.415  105.454 70.063  1.00 48.35  ? 1915 PHE A CB    1 
ATOM   537  C  CG    . PHE A 1 124 ? 100.539 104.860 69.270  1.00 48.02  ? 1915 PHE A CG    1 
ATOM   538  C  CD1   . PHE A 1 124 ? 100.777 103.498 69.290  1.00 51.36  ? 1915 PHE A CD1   1 
ATOM   539  C  CD2   . PHE A 1 124 ? 101.375 105.670 68.525  1.00 52.64  ? 1915 PHE A CD2   1 
ATOM   540  C  CE1   . PHE A 1 124 ? 101.817 102.954 68.569  1.00 54.49  ? 1915 PHE A CE1   1 
ATOM   541  C  CE2   . PHE A 1 124 ? 102.417 105.131 67.801  1.00 61.71  ? 1915 PHE A CE2   1 
ATOM   542  C  CZ    . PHE A 1 124 ? 102.639 103.772 67.824  1.00 61.68  ? 1915 PHE A CZ    1 
ATOM   543  N  N     . SER A 1 125 ? 97.464  103.002 68.680  1.00 55.81  ? 1916 SER A N     1 
ATOM   544  C  CA    . SER A 1 125 ? 96.902  101.663 68.798  1.00 67.91  ? 1916 SER A CA    1 
ATOM   545  C  C     . SER A 1 125 ? 98.004  100.615 68.724  1.00 71.30  ? 1916 SER A C     1 
ATOM   546  O  O     . SER A 1 125 ? 98.822  100.630 67.799  1.00 73.62  ? 1916 SER A O     1 
ATOM   547  C  CB    . SER A 1 125 ? 95.864  101.411 67.703  1.00 69.33  ? 1916 SER A CB    1 
ATOM   548  O  OG    . SER A 1 125 ? 95.438  100.060 67.708  1.00 76.85  ? 1916 SER A OG    1 
ATOM   549  N  N     . LEU A 1 126 ? 98.021  99.708  69.703  1.00 68.85  ? 1917 LEU A N     1 
ATOM   550  C  CA    . LEU A 1 126 ? 98.899  98.547  69.683  1.00 73.12  ? 1917 LEU A CA    1 
ATOM   551  C  C     . LEU A 1 126 ? 98.153  97.269  69.317  1.00 81.73  ? 1917 LEU A C     1 
ATOM   552  O  O     . LEU A 1 126 ? 98.675  96.170  69.528  1.00 89.67  ? 1917 LEU A O     1 
ATOM   553  C  CB    . LEU A 1 126 ? 99.601  98.375  71.031  1.00 74.37  ? 1917 LEU A CB    1 
ATOM   554  C  CG    . LEU A 1 126 ? 100.139 99.624  71.728  1.00 66.68  ? 1917 LEU A CG    1 
ATOM   555  C  CD1   . LEU A 1 126 ? 99.196  100.041 72.830  1.00 59.17  ? 1917 LEU A CD1   1 
ATOM   556  C  CD2   . LEU A 1 126 ? 101.528 99.387  72.286  1.00 62.68  ? 1917 LEU A CD2   1 
ATOM   557  N  N     . GLN A 1 127 ? 96.940  97.394  68.784  1.00 87.15  ? 1918 GLN A N     1 
ATOM   558  C  CA    . GLN A 1 127 ? 96.162  96.233  68.387  1.00 96.09  ? 1918 GLN A CA    1 
ATOM   559  C  C     . GLN A 1 127 ? 96.815  95.529  67.200  1.00 102.90 ? 1918 GLN A C     1 
ATOM   560  O  O     . GLN A 1 127 ? 97.591  96.117  66.442  1.00 100.69 ? 1918 GLN A O     1 
ATOM   561  C  CB    . GLN A 1 127 ? 94.734  96.643  68.027  1.00 97.79  ? 1918 GLN A CB    1 
ATOM   562  C  CG    . GLN A 1 127 ? 94.017  97.432  69.108  1.00 91.90  ? 1918 GLN A CG    1 
ATOM   563  C  CD    . GLN A 1 127 ? 93.072  96.572  69.921  1.00 99.08  ? 1918 GLN A CD    1 
ATOM   564  O  OE1   . GLN A 1 127 ? 93.131  95.345  69.867  1.00 106.11 ? 1918 GLN A OE1   1 
ATOM   565  N  NE2   . GLN A 1 127 ? 92.189  97.214  70.676  1.00 96.09  ? 1918 GLN A NE2   1 
ATOM   566  N  N     . LYS A 1 128 ? 96.490  94.244  67.047  1.00 108.02 ? 1919 LYS A N     1 
ATOM   567  C  CA    . LYS A 1 128 ? 97.029  93.471  65.935  1.00 114.35 ? 1919 LYS A CA    1 
ATOM   568  C  C     . LYS A 1 128 ? 96.517  93.960  64.586  1.00 117.27 ? 1919 LYS A C     1 
ATOM   569  O  O     . LYS A 1 128 ? 97.178  93.732  63.567  1.00 119.92 ? 1919 LYS A O     1 
ATOM   570  C  CB    . LYS A 1 128 ? 96.695  91.988  66.111  1.00 117.43 ? 1919 LYS A CB    1 
ATOM   571  C  CG    . LYS A 1 128 ? 95.217  91.701  66.334  1.00 117.23 ? 1919 LYS A CG    1 
ATOM   572  C  CD    . LYS A 1 128 ? 94.542  91.223  65.057  1.00 111.40 ? 1919 LYS A CD    1 
ATOM   573  C  CE    . LYS A 1 128 ? 93.377  90.296  65.362  1.00 105.92 ? 1919 LYS A CE    1 
ATOM   574  N  NZ    . LYS A 1 128 ? 92.957  89.523  64.161  1.00 100.82 ? 1919 LYS A NZ    1 
ATOM   575  N  N     . GLU A 1 129 ? 95.365  94.622  64.556  1.00 113.42 ? 1920 GLU A N     1 
ATOM   576  C  CA    . GLU A 1 129 ? 94.808  95.133  63.310  1.00 111.84 ? 1920 GLU A CA    1 
ATOM   577  C  C     . GLU A 1 129 ? 95.475  96.445  62.911  1.00 112.42 ? 1920 GLU A C     1 
ATOM   578  O  O     . GLU A 1 129 ? 95.027  97.125  61.988  1.00 115.61 ? 1920 GLU A O     1 
ATOM   579  C  CB    . GLU A 1 129 ? 93.295  95.328  63.435  1.00 109.89 ? 1920 GLU A CB    1 
ATOM   580  C  CG    . GLU A 1 129 ? 92.861  96.083  64.681  1.00 110.60 ? 1920 GLU A CG    1 
ATOM   581  C  CD    . GLU A 1 129 ? 92.392  95.161  65.790  1.00 112.93 ? 1920 GLU A CD    1 
ATOM   582  O  OE1   . GLU A 1 129 ? 92.831  93.992  65.822  1.00 110.85 ? 1920 GLU A OE1   1 
ATOM   583  O  OE2   . GLU A 1 129 ? 91.581  95.605  66.629  1.00 111.76 ? 1920 GLU A OE2   1 
ATOM   584  N  N     . ASP A 1 145 ? 94.972  99.315  59.959  1.00 105.71 ? 1936 ASP A N     1 
ATOM   585  C  CA    . ASP A 1 145 ? 95.939  99.365  58.869  1.00 116.80 ? 1936 ASP A CA    1 
ATOM   586  C  C     . ASP A 1 145 ? 96.824  98.122  58.864  1.00 120.07 ? 1936 ASP A C     1 
ATOM   587  O  O     . ASP A 1 145 ? 97.760  98.020  59.658  1.00 119.01 ? 1936 ASP A O     1 
ATOM   588  C  CB    . ASP A 1 145 ? 96.801  100.625 58.974  1.00 117.05 ? 1936 ASP A CB    1 
ATOM   589  C  CG    . ASP A 1 145 ? 97.476  100.980 57.664  1.00 116.77 ? 1936 ASP A CG    1 
ATOM   590  O  OD1   . ASP A 1 145 ? 97.266  100.255 56.669  1.00 117.00 ? 1936 ASP A OD1   1 
ATOM   591  O  OD2   . ASP A 1 145 ? 98.215  101.986 57.629  1.00 112.47 ? 1936 ASP A OD2   1 
ATOM   592  N  N     . PRO A 1 146 ? 96.524  97.176  57.971  1.00 122.58 ? 1937 PRO A N     1 
ATOM   593  C  CA    . PRO A 1 146 ? 97.346  95.957  57.890  1.00 123.04 ? 1937 PRO A CA    1 
ATOM   594  C  C     . PRO A 1 146 ? 98.789  96.221  57.501  1.00 123.81 ? 1937 PRO A C     1 
ATOM   595  O  O     . PRO A 1 146 ? 99.659  95.403  57.824  1.00 120.93 ? 1937 PRO A O     1 
ATOM   596  C  CB    . PRO A 1 146 ? 96.624  95.116  56.828  1.00 121.67 ? 1937 PRO A CB    1 
ATOM   597  C  CG    . PRO A 1 146 ? 95.855  96.107  56.016  1.00 120.78 ? 1937 PRO A CG    1 
ATOM   598  C  CD    . PRO A 1 146 ? 95.442  97.187  56.972  1.00 119.26 ? 1937 PRO A CD    1 
ATOM   599  N  N     . SER A 1 147 ? 99.071  97.331  56.813  1.00 124.76 ? 1938 SER A N     1 
ATOM   600  C  CA    . SER A 1 147 ? 100.447 97.639  56.434  1.00 122.83 ? 1938 SER A CA    1 
ATOM   601  C  C     . SER A 1 147 ? 101.317 97.875  57.662  1.00 125.39 ? 1938 SER A C     1 
ATOM   602  O  O     . SER A 1 147 ? 102.473 97.438  57.706  1.00 120.34 ? 1938 SER A O     1 
ATOM   603  C  CB    . SER A 1 147 ? 100.477 98.856  55.511  1.00 113.37 ? 1938 SER A CB    1 
ATOM   604  O  OG    . SER A 1 147 ? 100.141 100.040 56.214  1.00 110.18 ? 1938 SER A OG    1 
ATOM   605  N  N     . LEU A 1 148 ? 100.781 98.563  58.666  1.00 125.52 ? 1939 LEU A N     1 
ATOM   606  C  CA    . LEU A 1 148 ? 101.513 98.844  59.899  1.00 117.27 ? 1939 LEU A CA    1 
ATOM   607  C  C     . LEU A 1 148 ? 101.406 97.631  60.814  1.00 111.68 ? 1939 LEU A C     1 
ATOM   608  O  O     . LEU A 1 148 ? 100.434 97.481  61.556  1.00 110.91 ? 1939 LEU A O     1 
ATOM   609  C  CB    . LEU A 1 148 ? 100.966 100.094 60.576  1.00 112.00 ? 1939 LEU A CB    1 
ATOM   610  C  CG    . LEU A 1 148 ? 101.475 101.436 60.051  1.00 107.20 ? 1939 LEU A CG    1 
ATOM   611  C  CD1   . LEU A 1 148 ? 100.751 102.576 60.742  1.00 101.14 ? 1939 LEU A CD1   1 
ATOM   612  C  CD2   . LEU A 1 148 ? 102.977 101.553 60.246  1.00 101.86 ? 1939 LEU A CD2   1 
ATOM   613  N  N     . THR A 1 149 ? 102.410 96.761  60.764  1.00 108.40 ? 1940 THR A N     1 
ATOM   614  C  CA    . THR A 1 149 ? 102.436 95.590  61.624  1.00 110.43 ? 1940 THR A CA    1 
ATOM   615  C  C     . THR A 1 149 ? 102.784 96.005  63.053  1.00 109.45 ? 1940 THR A C     1 
ATOM   616  O  O     . THR A 1 149 ? 103.038 97.176  63.347  1.00 108.03 ? 1940 THR A O     1 
ATOM   617  C  CB    . THR A 1 149 ? 103.421 94.553  61.085  1.00 109.22 ? 1940 THR A CB    1 
ATOM   618  O  OG1   . THR A 1 149 ? 103.165 93.282  61.697  1.00 113.08 ? 1940 THR A OG1   1 
ATOM   619  C  CG2   . THR A 1 149 ? 104.854 94.971  61.376  1.00 105.52 ? 1940 THR A CG2   1 
ATOM   620  N  N     . LEU A 1 150 ? 102.782 95.032  63.963  1.00 108.81 ? 1941 LEU A N     1 
ATOM   621  C  CA    . LEU A 1 150 ? 103.072 95.338  65.358  1.00 100.67 ? 1941 LEU A CA    1 
ATOM   622  C  C     . LEU A 1 150 ? 104.553 95.607  65.594  1.00 100.29 ? 1941 LEU A C     1 
ATOM   623  O  O     . LEU A 1 150 ? 104.896 96.424  66.455  1.00 96.41  ? 1941 LEU A O     1 
ATOM   624  C  CB    . LEU A 1 150 ? 102.597 94.196  66.257  1.00 101.94 ? 1941 LEU A CB    1 
ATOM   625  C  CG    . LEU A 1 150 ? 102.418 94.546  67.734  1.00 100.87 ? 1941 LEU A CG    1 
ATOM   626  C  CD1   . LEU A 1 150 ? 101.526 95.766  67.884  1.00 94.73  ? 1941 LEU A CD1   1 
ATOM   627  C  CD2   . LEU A 1 150 ? 101.847 93.363  68.501  1.00 101.31 ? 1941 LEU A CD2   1 
ATOM   628  N  N     . LYS A 1 151 ? 105.437 94.944  64.846  1.00 105.20 ? 1942 LYS A N     1 
ATOM   629  C  CA    . LYS A 1 151 ? 106.868 95.051  65.117  1.00 105.51 ? 1942 LYS A CA    1 
ATOM   630  C  C     . LYS A 1 151 ? 107.390 96.458  64.840  1.00 105.44 ? 1942 LYS A C     1 
ATOM   631  O  O     . LYS A 1 151 ? 108.046 97.065  65.695  1.00 97.78  ? 1942 LYS A O     1 
ATOM   632  C  CB    . LYS A 1 151 ? 107.635 94.019  64.290  1.00 100.04 ? 1942 LYS A CB    1 
ATOM   633  N  N     . ASP A 1 152 ? 107.106 96.999  63.652  1.00 107.08 ? 1943 ASP A N     1 
ATOM   634  C  CA    . ASP A 1 152 ? 107.624 98.323  63.324  1.00 102.11 ? 1943 ASP A CA    1 
ATOM   635  C  C     . ASP A 1 152 ? 106.916 99.413  64.118  1.00 99.85  ? 1943 ASP A C     1 
ATOM   636  O  O     . ASP A 1 152 ? 107.532 100.430 64.454  1.00 100.50 ? 1943 ASP A O     1 
ATOM   637  C  CB    . ASP A 1 152 ? 107.522 98.591  61.818  1.00 99.77  ? 1943 ASP A CB    1 
ATOM   638  C  CG    . ASP A 1 152 ? 106.089 98.715  61.327  1.00 105.99 ? 1943 ASP A CG    1 
ATOM   639  O  OD1   . ASP A 1 152 ? 105.184 98.100  61.923  1.00 105.45 ? 1943 ASP A OD1   1 
ATOM   640  O  OD2   . ASP A 1 152 ? 105.869 99.437  60.332  1.00 107.09 ? 1943 ASP A OD2   1 
ATOM   641  N  N     . ARG A 1 153 ? 105.637 99.214  64.440  1.00 97.68  ? 1944 ARG A N     1 
ATOM   642  C  CA    . ARG A 1 153 ? 104.936 100.158 65.304  1.00 89.65  ? 1944 ARG A CA    1 
ATOM   643  C  C     . ARG A 1 153 ? 105.562 100.195 66.692  1.00 87.64  ? 1944 ARG A C     1 
ATOM   644  O  O     . ARG A 1 153 ? 105.770 101.273 67.263  1.00 81.77  ? 1944 ARG A O     1 
ATOM   645  C  CB    . ARG A 1 153 ? 103.458 99.782  65.386  1.00 86.38  ? 1944 ARG A CB    1 
ATOM   646  C  CG    . ARG A 1 153 ? 102.549 100.896 65.865  1.00 78.44  ? 1944 ARG A CG    1 
ATOM   647  C  CD    . ARG A 1 153 ? 101.145 100.718 65.316  1.00 86.11  ? 1944 ARG A CD    1 
ATOM   648  N  NE    . ARG A 1 153 ? 100.775 99.310  65.247  1.00 92.94  ? 1944 ARG A NE    1 
ATOM   649  C  CZ    . ARG A 1 153 ? 99.625  98.858  64.767  1.00 92.63  ? 1944 ARG A CZ    1 
ATOM   650  N  NH1   . ARG A 1 153 ? 98.695  99.680  64.313  1.00 82.86  ? 1944 ARG A NH1   1 
ATOM   651  N  NH2   . ARG A 1 153 ? 99.404  97.547  64.739  1.00 100.02 ? 1944 ARG A NH2   1 
ATOM   652  N  N     . MET A 1 154 ? 105.878 99.021  67.247  1.00 94.62  ? 1945 MET A N     1 
ATOM   653  C  CA    . MET A 1 154 ? 106.551 98.960  68.539  1.00 96.84  ? 1945 MET A CA    1 
ATOM   654  C  C     . MET A 1 154 ? 107.928 99.605  68.472  1.00 93.33  ? 1945 MET A C     1 
ATOM   655  O  O     . MET A 1 154 ? 108.333 100.319 69.397  1.00 91.60  ? 1945 MET A O     1 
ATOM   656  C  CB    . MET A 1 154 ? 106.666 97.505  68.999  1.00 98.25  ? 1945 MET A CB    1 
ATOM   657  C  CG    . MET A 1 154 ? 105.438 96.919  69.711  1.00 102.28 ? 1945 MET A CG    1 
ATOM   658  S  SD    . MET A 1 154 ? 104.188 98.057  70.352  1.00 105.92 ? 1945 MET A SD    1 
ATOM   659  C  CE    . MET A 1 154 ? 105.105 98.985  71.587  1.00 84.50  ? 1945 MET A CE    1 
ATOM   660  N  N     . TRP A 1 155 ? 108.664 99.357  67.386  1.00 90.68  ? 1946 TRP A N     1 
ATOM   661  C  CA    . TRP A 1 155 ? 109.977 99.973  67.227  1.00 90.00  ? 1946 TRP A CA    1 
ATOM   662  C  C     . TRP A 1 155 ? 109.871 101.492 67.188  1.00 89.02  ? 1946 TRP A C     1 
ATOM   663  O  O     . TRP A 1 155 ? 110.650 102.192 67.845  1.00 92.34  ? 1946 TRP A O     1 
ATOM   664  C  CB    . TRP A 1 155 ? 110.653 99.450  65.960  1.00 90.06  ? 1946 TRP A CB    1 
ATOM   665  C  CG    . TRP A 1 155 ? 111.529 100.464 65.292  1.00 90.97  ? 1946 TRP A CG    1 
ATOM   666  C  CD1   . TRP A 1 155 ? 111.277 101.121 64.124  1.00 88.50  ? 1946 TRP A CD1   1 
ATOM   667  C  CD2   . TRP A 1 155 ? 112.799 100.937 65.754  1.00 96.21  ? 1946 TRP A CD2   1 
ATOM   668  N  NE1   . TRP A 1 155 ? 112.312 101.975 63.829  1.00 91.96  ? 1946 TRP A NE1   1 
ATOM   669  C  CE2   . TRP A 1 155 ? 113.259 101.881 64.814  1.00 96.61  ? 1946 TRP A CE2   1 
ATOM   670  C  CE3   . TRP A 1 155 ? 113.592 100.655 66.870  1.00 98.53  ? 1946 TRP A CE3   1 
ATOM   671  C  CZ2   . TRP A 1 155 ? 114.476 102.543 64.957  1.00 94.67  ? 1946 TRP A CZ2   1 
ATOM   672  C  CZ3   . TRP A 1 155 ? 114.800 101.313 67.009  1.00 95.14  ? 1946 TRP A CZ3   1 
ATOM   673  C  CH2   . TRP A 1 155 ? 115.230 102.246 66.058  1.00 93.77  ? 1946 TRP A CH2   1 
ATOM   674  N  N     . TYR A 1 156 ? 108.904 102.018 66.434  1.00 89.07  ? 1947 TYR A N     1 
ATOM   675  C  CA    . TYR A 1 156 ? 108.711 103.463 66.373  1.00 88.03  ? 1947 TYR A CA    1 
ATOM   676  C  C     . TYR A 1 156 ? 108.353 104.026 67.742  1.00 83.59  ? 1947 TYR A C     1 
ATOM   677  O  O     . TYR A 1 156 ? 108.922 105.034 68.179  1.00 85.37  ? 1947 TYR A O     1 
ATOM   678  C  CB    . TYR A 1 156 ? 107.623 103.804 65.353  1.00 92.70  ? 1947 TYR A CB    1 
ATOM   679  C  CG    . TYR A 1 156 ? 108.147 104.159 63.981  1.00 94.60  ? 1947 TYR A CG    1 
ATOM   680  C  CD1   . TYR A 1 156 ? 109.008 105.233 63.803  1.00 90.41  ? 1947 TYR A CD1   1 
ATOM   681  C  CD2   . TYR A 1 156 ? 107.775 103.425 62.863  1.00 95.51  ? 1947 TYR A CD2   1 
ATOM   682  C  CE1   . TYR A 1 156 ? 109.488 105.564 62.551  1.00 94.60  ? 1947 TYR A CE1   1 
ATOM   683  C  CE2   . TYR A 1 156 ? 108.249 103.748 61.607  1.00 100.99 ? 1947 TYR A CE2   1 
ATOM   684  C  CZ    . TYR A 1 156 ? 109.105 104.818 61.456  1.00 103.71 ? 1947 TYR A CZ    1 
ATOM   685  O  OH    . TYR A 1 156 ? 109.581 105.145 60.207  1.00 104.51 ? 1947 TYR A OH    1 
ATOM   686  N  N     . LEU A 1 157 ? 107.418 103.373 68.440  1.00 79.55  ? 1948 LEU A N     1 
ATOM   687  C  CA    . LEU A 1 157 ? 106.993 103.857 69.750  1.00 77.27  ? 1948 LEU A CA    1 
ATOM   688  C  C     . LEU A 1 157 ? 108.154 103.870 70.734  1.00 76.67  ? 1948 LEU A C     1 
ATOM   689  O  O     . LEU A 1 157 ? 108.310 104.821 71.509  1.00 73.89  ? 1948 LEU A O     1 
ATOM   690  C  CB    . LEU A 1 157 ? 105.846 102.996 70.281  1.00 76.81  ? 1948 LEU A CB    1 
ATOM   691  C  CG    . LEU A 1 157 ? 105.270 103.392 71.642  1.00 66.51  ? 1948 LEU A CG    1 
ATOM   692  C  CD1   . LEU A 1 157 ? 104.847 104.850 71.641  1.00 61.26  ? 1948 LEU A CD1   1 
ATOM   693  C  CD2   . LEU A 1 157 ? 104.100 102.495 72.013  1.00 55.84  ? 1948 LEU A CD2   1 
ATOM   694  N  N     . GLN A 1 158 ? 108.979 102.822 70.719  1.00 79.79  ? 1949 GLN A N     1 
ATOM   695  C  CA    . GLN A 1 158 ? 110.173 102.810 71.555  1.00 79.61  ? 1949 GLN A CA    1 
ATOM   696  C  C     . GLN A 1 158 ? 111.131 103.926 71.155  1.00 79.82  ? 1949 GLN A C     1 
ATOM   697  O  O     . GLN A 1 158 ? 111.757 104.555 72.016  1.00 76.78  ? 1949 GLN A O     1 
ATOM   698  C  CB    . GLN A 1 158 ? 110.858 101.445 71.464  1.00 87.35  ? 1949 GLN A CB    1 
ATOM   699  C  CG    . GLN A 1 158 ? 112.317 101.436 71.891  1.00 95.58  ? 1949 GLN A CG    1 
ATOM   700  C  CD    . GLN A 1 158 ? 113.049 100.189 71.430  1.00 100.80 ? 1949 GLN A CD    1 
ATOM   701  O  OE1   . GLN A 1 158 ? 114.274 100.182 71.312  1.00 101.40 ? 1949 GLN A OE1   1 
ATOM   702  N  NE2   . GLN A 1 158 ? 112.299 99.126  71.166  1.00 100.06 ? 1949 GLN A NE2   1 
ATOM   703  N  N     . SER A 1 159 ? 111.251 104.189 69.851  1.00 81.44  ? 1950 SER A N     1 
ATOM   704  C  CA    . SER A 1 159 ? 112.171 105.219 69.383  1.00 80.20  ? 1950 SER A CA    1 
ATOM   705  C  C     . SER A 1 159 ? 111.764 106.604 69.873  1.00 76.08  ? 1950 SER A C     1 
ATOM   706  O  O     . SER A 1 159 ? 112.617 107.389 70.303  1.00 80.05  ? 1950 SER A O     1 
ATOM   707  C  CB    . SER A 1 159 ? 112.252 105.194 67.857  1.00 82.08  ? 1950 SER A CB    1 
ATOM   708  O  OG    . SER A 1 159 ? 112.883 104.010 67.399  1.00 88.91  ? 1950 SER A OG    1 
ATOM   709  N  N     . CYS A 1 160 ? 110.470 106.928 69.819  1.00 72.36  ? 1951 CYS A N     1 
ATOM   710  C  CA    . CYS A 1 160 ? 110.060 108.265 70.238  1.00 66.38  ? 1951 CYS A CA    1 
ATOM   711  C  C     . CYS A 1 160 ? 109.884 108.390 71.746  1.00 62.22  ? 1951 CYS A C     1 
ATOM   712  O  O     . CYS A 1 160 ? 109.659 109.503 72.233  1.00 54.55  ? 1951 CYS A O     1 
ATOM   713  C  CB    . CYS A 1 160 ? 108.759 108.690 69.550  1.00 76.59  ? 1951 CYS A CB    1 
ATOM   714  S  SG    . CYS A 1 160 ? 107.535 107.396 69.303  1.00 87.47  ? 1951 CYS A SG    1 
ATOM   715  N  N     . LEU A 1 161 ? 109.981 107.289 72.493  1.00 65.53  ? 1952 LEU A N     1 
ATOM   716  C  CA    . LEU A 1 161 ? 109.819 107.308 73.941  1.00 63.36  ? 1952 LEU A CA    1 
ATOM   717  C  C     . LEU A 1 161 ? 111.141 107.124 74.678  1.00 68.49  ? 1952 LEU A C     1 
ATOM   718  O  O     . LEU A 1 161 ? 111.146 106.698 75.837  1.00 66.79  ? 1952 LEU A O     1 
ATOM   719  C  CB    . LEU A 1 161 ? 108.821 106.237 74.380  1.00 56.42  ? 1952 LEU A CB    1 
ATOM   720  C  CG    . LEU A 1 161 ? 107.390 106.708 74.639  1.00 50.07  ? 1952 LEU A CG    1 
ATOM   721  C  CD1   . LEU A 1 161 ? 106.581 105.609 75.303  1.00 45.80  ? 1952 LEU A CD1   1 
ATOM   722  C  CD2   . LEU A 1 161 ? 107.382 107.969 75.486  1.00 46.75  ? 1952 LEU A CD2   1 
ATOM   723  N  N     . ARG A 1 162 ? 112.262 107.432 74.032  1.00 72.69  ? 1953 ARG A N     1 
ATOM   724  C  CA    . ARG A 1 162 ? 113.576 107.317 74.646  1.00 75.84  ? 1953 ARG A CA    1 
ATOM   725  C  C     . ARG A 1 162 ? 114.337 108.619 74.463  1.00 73.59  ? 1953 ARG A C     1 
ATOM   726  O  O     . ARG A 1 162 ? 114.219 109.277 73.425  1.00 69.99  ? 1953 ARG A O     1 
ATOM   727  C  CB    . ARG A 1 162 ? 114.374 106.155 74.044  1.00 84.95  ? 1953 ARG A CB    1 
ATOM   728  C  CG    . ARG A 1 162 ? 115.166 105.353 75.062  1.00 81.45  ? 1953 ARG A CG    1 
ATOM   729  C  CD    . ARG A 1 162 ? 116.211 104.479 74.388  1.00 77.16  ? 1953 ARG A CD    1 
ATOM   730  N  NE    . ARG A 1 162 ? 115.635 103.638 73.346  1.00 89.02  ? 1953 ARG A NE    1 
ATOM   731  C  CZ    . ARG A 1 162 ? 115.862 103.791 72.049  1.00 94.68  ? 1953 ARG A CZ    1 
ATOM   732  N  NH1   . ARG A 1 162 ? 116.654 104.748 71.594  1.00 88.76  ? 1953 ARG A NH1   1 
ATOM   733  N  NH2   . ARG A 1 162 ? 115.279 102.963 71.186  1.00 95.30  ? 1953 ARG A NH2   1 
ATOM   734  N  N     . LYS A 1 163 ? 115.119 108.986 75.474  1.00 75.98  ? 1954 LYS A N     1 
ATOM   735  C  CA    . LYS A 1 163 ? 115.914 110.204 75.426  1.00 84.21  ? 1954 LYS A CA    1 
ATOM   736  C  C     . LYS A 1 163 ? 117.294 109.901 74.856  1.00 94.10  ? 1954 LYS A C     1 
ATOM   737  O  O     . LYS A 1 163 ? 117.877 108.846 75.127  1.00 93.92  ? 1954 LYS A O     1 
ATOM   738  C  CB    . LYS A 1 163 ? 116.029 110.831 76.819  1.00 75.18  ? 1954 LYS A CB    1 
ATOM   739  C  CG    . LYS A 1 163 ? 117.408 110.752 77.457  1.00 76.12  ? 1954 LYS A CG    1 
ATOM   740  C  CD    . LYS A 1 163 ? 117.478 111.579 78.731  1.00 72.87  ? 1954 LYS A CD    1 
ATOM   741  C  CE    . LYS A 1 163 ? 117.071 113.022 78.480  1.00 72.88  ? 1954 LYS A CE    1 
ATOM   742  N  NZ    . LYS A 1 163 ? 116.967 113.797 79.747  1.00 71.77  ? 1954 LYS A NZ    1 
ATOM   743  N  N     . GLU A 1 164 ? 117.797 110.822 74.039  1.00 100.06 ? 1955 GLU A N     1 
ATOM   744  C  CA    . GLU A 1 164 ? 119.103 110.682 73.409  1.00 102.29 ? 1955 GLU A CA    1 
ATOM   745  C  C     . GLU A 1 164 ? 119.497 112.020 72.804  1.00 113.44 ? 1955 GLU A C     1 
ATOM   746  O  O     . GLU A 1 164 ? 118.634 112.809 72.407  1.00 111.34 ? 1955 GLU A O     1 
ATOM   747  C  CB    . GLU A 1 164 ? 119.098 109.591 72.331  1.00 103.82 ? 1955 GLU A CB    1 
ATOM   748  C  CG    . GLU A 1 164 ? 118.085 109.816 71.220  1.00 98.50  ? 1955 GLU A CG    1 
ATOM   749  C  CD    . GLU A 1 164 ? 116.790 109.064 71.452  1.00 92.59  ? 1955 GLU A CD    1 
ATOM   750  O  OE1   . GLU A 1 164 ? 116.771 108.163 72.317  1.00 94.13  ? 1955 GLU A OE1   1 
ATOM   751  O  OE2   . GLU A 1 164 ? 115.791 109.372 70.770  1.00 86.99  ? 1955 GLU A OE2   1 
ATOM   752  N  N     . SER A 1 165 ? 120.808 112.259 72.742  1.00 121.72 ? 1956 SER A N     1 
ATOM   753  C  CA    . SER A 1 165 ? 121.382 113.473 72.158  1.00 130.85 ? 1956 SER A CA    1 
ATOM   754  C  C     . SER A 1 165 ? 120.736 114.732 72.737  1.00 131.74 ? 1956 SER A C     1 
ATOM   755  O  O     . SER A 1 165 ? 120.326 115.644 72.015  1.00 132.35 ? 1956 SER A O     1 
ATOM   756  C  CB    . SER A 1 165 ? 121.283 113.448 70.629  1.00 125.99 ? 1956 SER A CB    1 
ATOM   757  O  OG    . SER A 1 165 ? 119.949 113.608 70.178  1.00 115.74 ? 1956 SER A OG    1 
ATOM   758  N  N     . ASP A 1 166 ? 120.651 114.769 74.069  1.00 125.47 ? 1957 ASP A N     1 
ATOM   759  C  CA    . ASP A 1 166 ? 120.110 115.914 74.806  1.00 123.35 ? 1957 ASP A CA    1 
ATOM   760  C  C     . ASP A 1 166 ? 118.665 116.208 74.400  1.00 114.36 ? 1957 ASP A C     1 
ATOM   761  O  O     . ASP A 1 166 ? 118.298 117.345 74.094  1.00 105.76 ? 1957 ASP A O     1 
ATOM   762  C  CB    . ASP A 1 166 ? 120.993 117.152 74.628  1.00 125.12 ? 1957 ASP A CB    1 
ATOM   763  C  CG    . ASP A 1 166 ? 122.343 117.008 75.303  1.00 127.13 ? 1957 ASP A CG    1 
ATOM   764  O  OD1   . ASP A 1 166 ? 122.582 115.962 75.943  1.00 130.08 ? 1957 ASP A OD1   1 
ATOM   765  O  OD2   . ASP A 1 166 ? 123.166 117.942 75.194  1.00 130.16 ? 1957 ASP A OD2   1 
ATOM   766  N  N     . LYS A 1 167 ? 117.839 115.163 74.401  1.00 113.30 ? 1958 LYS A N     1 
ATOM   767  C  CA    . LYS A 1 167 ? 116.411 115.298 74.114  1.00 110.61 ? 1958 LYS A CA    1 
ATOM   768  C  C     . LYS A 1 167 ? 115.698 115.578 75.431  1.00 103.75 ? 1958 LYS A C     1 
ATOM   769  O  O     . LYS A 1 167 ? 115.326 114.665 76.170  1.00 92.18  ? 1958 LYS A O     1 
ATOM   770  C  CB    . LYS A 1 167 ? 115.873 114.046 73.434  1.00 107.39 ? 1958 LYS A CB    1 
ATOM   771  C  CG    . LYS A 1 167 ? 114.528 114.235 72.750  1.00 94.54  ? 1958 LYS A CG    1 
ATOM   772  C  CD    . LYS A 1 167 ? 114.679 114.955 71.419  1.00 97.34  ? 1958 LYS A CD    1 
ATOM   773  C  CE    . LYS A 1 167 ? 115.404 114.087 70.402  1.00 100.83 ? 1958 LYS A CE    1 
ATOM   774  N  NZ    . LYS A 1 167 ? 115.448 114.723 69.056  1.00 88.42  ? 1958 LYS A NZ    1 
ATOM   775  N  N     . GLU A 1 168 ? 115.506 116.864 75.730  1.00 99.72  ? 1959 GLU A N     1 
ATOM   776  C  CA    . GLU A 1 168 ? 114.881 117.289 76.982  1.00 89.60  ? 1959 GLU A CA    1 
ATOM   777  C  C     . GLU A 1 168 ? 113.364 117.260 76.810  1.00 83.67  ? 1959 GLU A C     1 
ATOM   778  O  O     . GLU A 1 168 ? 112.700 118.283 76.626  1.00 86.09  ? 1959 GLU A O     1 
ATOM   779  C  CB    . GLU A 1 168 ? 115.375 118.673 77.386  1.00 92.34  ? 1959 GLU A CB    1 
ATOM   780  C  CG    . GLU A 1 168 ? 114.997 119.079 78.800  1.00 106.28 ? 1959 GLU A CG    1 
ATOM   781  C  CD    . GLU A 1 168 ? 115.487 120.469 79.158  1.00 115.96 ? 1959 GLU A CD    1 
ATOM   782  O  OE1   . GLU A 1 168 ? 116.216 121.071 78.343  1.00 118.31 ? 1959 GLU A OE1   1 
ATOM   783  O  OE2   . GLU A 1 168 ? 115.142 120.959 80.254  1.00 118.84 ? 1959 GLU A OE2   1 
ATOM   784  N  N     . CYS A 1 169 ? 112.809 116.054 76.880  1.00 77.57  ? 1960 CYS A N     1 
ATOM   785  C  CA    . CYS A 1 169 ? 111.376 115.841 76.741  1.00 62.50  ? 1960 CYS A CA    1 
ATOM   786  C  C     . CYS A 1 169 ? 110.750 115.592 78.106  1.00 60.05  ? 1960 CYS A C     1 
ATOM   787  O  O     . CYS A 1 169 ? 111.311 114.872 78.937  1.00 62.78  ? 1960 CYS A O     1 
ATOM   788  C  CB    . CYS A 1 169 ? 111.085 114.661 75.813  1.00 54.88  ? 1960 CYS A CB    1 
ATOM   789  S  SG    . CYS A 1 169 ? 111.218 115.044 74.054  1.00 79.75  ? 1960 CYS A SG    1 
ATOM   790  N  N     . SER A 1 170 ? 109.586 116.193 78.332  1.00 56.96  ? 1961 SER A N     1 
ATOM   791  C  CA    . SER A 1 170 ? 108.829 116.015 79.564  1.00 45.73  ? 1961 SER A CA    1 
ATOM   792  C  C     . SER A 1 170 ? 107.583 115.197 79.257  1.00 41.93  ? 1961 SER A C     1 
ATOM   793  O  O     . SER A 1 170 ? 106.773 115.587 78.410  1.00 50.84  ? 1961 SER A O     1 
ATOM   794  C  CB    . SER A 1 170 ? 108.454 117.362 80.179  1.00 46.05  ? 1961 SER A CB    1 
ATOM   795  O  OG    . SER A 1 170 ? 109.602 118.040 80.657  1.00 54.75  ? 1961 SER A OG    1 
ATOM   796  N  N     . VAL A 1 171 ? 107.432 114.072 79.947  1.00 32.08  ? 1962 VAL A N     1 
ATOM   797  C  CA    . VAL A 1 171 ? 106.305 113.167 79.764  1.00 26.59  ? 1962 VAL A CA    1 
ATOM   798  C  C     . VAL A 1 171 ? 105.381 113.334 80.959  1.00 32.14  ? 1962 VAL A C     1 
ATOM   799  O  O     . VAL A 1 171 ? 105.790 113.104 82.103  1.00 46.83  ? 1962 VAL A O     1 
ATOM   800  C  CB    . VAL A 1 171 ? 106.766 111.709 79.628  1.00 24.64  ? 1962 VAL A CB    1 
ATOM   801  C  CG1   . VAL A 1 171 ? 105.684 110.868 78.978  1.00 29.54  ? 1962 VAL A CG1   1 
ATOM   802  C  CG2   . VAL A 1 171 ? 108.061 111.636 78.846  1.00 32.48  ? 1962 VAL A CG2   1 
ATOM   803  N  N     . VAL A 1 172 ? 104.141 113.726 80.699  1.00 25.12  ? 1963 VAL A N     1 
ATOM   804  C  CA    . VAL A 1 172 ? 103.149 113.933 81.745  1.00 28.62  ? 1963 VAL A CA    1 
ATOM   805  C  C     . VAL A 1 172 ? 102.280 112.687 81.810  1.00 34.92  ? 1963 VAL A C     1 
ATOM   806  O  O     . VAL A 1 172 ? 101.469 112.436 80.914  1.00 48.97  ? 1963 VAL A O     1 
ATOM   807  C  CB    . VAL A 1 172 ? 102.302 115.182 81.481  1.00 30.49  ? 1963 VAL A CB    1 
ATOM   808  C  CG1   . VAL A 1 172 ? 101.201 115.285 82.514  1.00 34.77  ? 1963 VAL A CG1   1 
ATOM   809  C  CG2   . VAL A 1 172 ? 103.173 116.424 81.484  1.00 29.13  ? 1963 VAL A CG2   1 
ATOM   810  N  N     . ILE A 1 173 ? 102.442 111.899 82.869  1.00 27.63  ? 1964 ILE A N     1 
ATOM   811  C  CA    . ILE A 1 173 ? 101.665 110.683 83.062  1.00 27.27  ? 1964 ILE A CA    1 
ATOM   812  C  C     . ILE A 1 173 ? 101.016 110.739 84.435  1.00 34.27  ? 1964 ILE A C     1 
ATOM   813  O  O     . ILE A 1 173 ? 101.689 111.013 85.434  1.00 40.77  ? 1964 ILE A O     1 
ATOM   814  C  CB    . ILE A 1 173 ? 102.528 109.414 82.932  1.00 23.24  ? 1964 ILE A CB    1 
ATOM   815  C  CG1   . ILE A 1 173 ? 103.707 109.651 81.992  1.00 22.24  ? 1964 ILE A CG1   1 
ATOM   816  C  CG2   . ILE A 1 173 ? 101.688 108.264 82.422  1.00 27.18  ? 1964 ILE A CG2   1 
ATOM   817  C  CD1   . ILE A 1 173 ? 104.656 108.481 81.910  1.00 23.02  ? 1964 ILE A CD1   1 
ATOM   818  N  N     . TYR A 1 174 ? 99.713  110.482 84.484  1.00 32.71  ? 1965 TYR A N     1 
ATOM   819  C  CA    . TYR A 1 174 ? 99.009  110.359 85.752  1.00 38.36  ? 1965 TYR A CA    1 
ATOM   820  C  C     . TYR A 1 174 ? 99.223  108.958 86.309  1.00 39.60  ? 1965 TYR A C     1 
ATOM   821  O  O     . TYR A 1 174 ? 99.116  107.970 85.575  1.00 39.20  ? 1965 TYR A O     1 
ATOM   822  C  CB    . TYR A 1 174 ? 97.522  110.645 85.562  1.00 40.75  ? 1965 TYR A CB    1 
ATOM   823  C  CG    . TYR A 1 174 ? 96.709  110.569 86.829  1.00 39.77  ? 1965 TYR A CG    1 
ATOM   824  C  CD1   . TYR A 1 174 ? 96.669  111.633 87.718  1.00 42.15  ? 1965 TYR A CD1   1 
ATOM   825  C  CD2   . TYR A 1 174 ? 95.975  109.435 87.134  1.00 41.40  ? 1965 TYR A CD2   1 
ATOM   826  C  CE1   . TYR A 1 174 ? 95.924  111.564 88.875  1.00 42.38  ? 1965 TYR A CE1   1 
ATOM   827  C  CE2   . TYR A 1 174 ? 95.228  109.357 88.286  1.00 51.39  ? 1965 TYR A CE2   1 
ATOM   828  C  CZ    . TYR A 1 174 ? 95.206  110.423 89.153  1.00 48.96  ? 1965 TYR A CZ    1 
ATOM   829  O  OH    . TYR A 1 174 ? 94.460  110.343 90.303  1.00 58.94  ? 1965 TYR A OH    1 
ATOM   830  N  N     . ASP A 1 175 ? 99.529  108.875 87.606  1.00 39.79  ? 1966 ASP A N     1 
ATOM   831  C  CA    . ASP A 1 175 ? 99.914  107.622 88.259  1.00 34.68  ? 1966 ASP A CA    1 
ATOM   832  C  C     . ASP A 1 175 ? 101.136 107.017 87.559  1.00 33.94  ? 1966 ASP A C     1 
ATOM   833  O  O     . ASP A 1 175 ? 101.085 105.952 86.941  1.00 30.26  ? 1966 ASP A O     1 
ATOM   834  C  CB    . ASP A 1 175 ? 98.742  106.634 88.299  1.00 42.99  ? 1966 ASP A CB    1 
ATOM   835  C  CG    . ASP A 1 175 ? 98.758  105.764 89.539  1.00 42.61  ? 1966 ASP A CG    1 
ATOM   836  O  OD1   . ASP A 1 175 ? 99.318  106.200 90.566  1.00 39.43  ? 1966 ASP A OD1   1 
ATOM   837  O  OD2   . ASP A 1 175 ? 98.210  104.643 89.487  1.00 49.40  ? 1966 ASP A OD2   1 
ATOM   838  N  N     . PHE A 1 176 ? 102.244 107.754 87.672  1.00 34.37  ? 1967 PHE A N     1 
ATOM   839  C  CA    . PHE A 1 176 ? 103.442 107.437 86.902  1.00 34.67  ? 1967 PHE A CA    1 
ATOM   840  C  C     . PHE A 1 176 ? 104.022 106.078 87.267  1.00 30.75  ? 1967 PHE A C     1 
ATOM   841  O  O     . PHE A 1 176 ? 104.561 105.389 86.397  1.00 32.83  ? 1967 PHE A O     1 
ATOM   842  C  CB    . PHE A 1 176 ? 104.497 108.526 87.094  1.00 24.40  ? 1967 PHE A CB    1 
ATOM   843  C  CG    . PHE A 1 176 ? 105.880 108.103 86.701  1.00 22.12  ? 1967 PHE A CG    1 
ATOM   844  C  CD1   . PHE A 1 176 ? 106.177 107.800 85.386  1.00 21.85  ? 1967 PHE A CD1   1 
ATOM   845  C  CD2   . PHE A 1 176 ? 106.881 108.002 87.647  1.00 25.51  ? 1967 PHE A CD2   1 
ATOM   846  C  CE1   . PHE A 1 176 ? 107.445 107.404 85.023  1.00 24.04  ? 1967 PHE A CE1   1 
ATOM   847  C  CE2   . PHE A 1 176 ? 108.151 107.608 87.289  1.00 25.52  ? 1967 PHE A CE2   1 
ATOM   848  C  CZ    . PHE A 1 176 ? 108.433 107.310 85.975  1.00 27.57  ? 1967 PHE A CZ    1 
ATOM   849  N  N     . ILE A 1 177 ? 103.943 105.677 88.536  1.00 23.01  ? 1968 ILE A N     1 
ATOM   850  C  CA    . ILE A 1 177 ? 104.530 104.400 88.939  1.00 21.37  ? 1968 ILE A CA    1 
ATOM   851  C  C     . ILE A 1 177 ? 103.840 103.246 88.222  1.00 25.62  ? 1968 ILE A C     1 
ATOM   852  O  O     . ILE A 1 177 ? 104.491 102.388 87.610  1.00 30.54  ? 1968 ILE A O     1 
ATOM   853  C  CB    . ILE A 1 177 ? 104.459 104.235 90.467  1.00 24.38  ? 1968 ILE A CB    1 
ATOM   854  C  CG1   . ILE A 1 177 ? 105.443 105.182 91.152  1.00 22.49  ? 1968 ILE A CG1   1 
ATOM   855  C  CG2   . ILE A 1 177 ? 104.735 102.796 90.858  1.00 28.39  ? 1968 ILE A CG2   1 
ATOM   856  C  CD1   . ILE A 1 177 ? 104.778 106.345 91.843  1.00 20.71  ? 1968 ILE A CD1   1 
ATOM   857  N  N     . GLN A 1 178 ? 102.507 103.216 88.273  1.00 26.57  ? 1969 GLN A N     1 
ATOM   858  C  CA    . GLN A 1 178 ? 101.772 102.126 87.643  1.00 26.86  ? 1969 GLN A CA    1 
ATOM   859  C  C     . GLN A 1 178 ? 101.903 102.174 86.126  1.00 32.85  ? 1969 GLN A C     1 
ATOM   860  O  O     . GLN A 1 178 ? 101.994 101.127 85.475  1.00 41.00  ? 1969 GLN A O     1 
ATOM   861  C  CB    . GLN A 1 178 ? 100.303 102.171 88.060  1.00 25.64  ? 1969 GLN A CB    1 
ATOM   862  C  CG    . GLN A 1 178 ? 99.524  100.923 87.683  1.00 29.83  ? 1969 GLN A CG    1 
ATOM   863  C  CD    . GLN A 1 178 ? 99.945  99.707  88.483  1.00 38.87  ? 1969 GLN A CD    1 
ATOM   864  O  OE1   . GLN A 1 178 ? 100.488 99.828  89.580  1.00 45.78  ? 1969 GLN A OE1   1 
ATOM   865  N  NE2   . GLN A 1 178 ? 99.695  98.524  87.935  1.00 41.15  ? 1969 GLN A NE2   1 
ATOM   866  N  N     . SER A 1 179 ? 101.907 103.378 85.546  1.00 28.53  ? 1970 SER A N     1 
ATOM   867  C  CA    . SER A 1 179 ? 102.082 103.501 84.103  1.00 29.32  ? 1970 SER A CA    1 
ATOM   868  C  C     . SER A 1 179 ? 103.449 102.988 83.669  1.00 32.67  ? 1970 SER A C     1 
ATOM   869  O  O     . SER A 1 179 ? 103.565 102.280 82.662  1.00 34.67  ? 1970 SER A O     1 
ATOM   870  C  CB    . SER A 1 179 ? 101.894 104.954 83.673  1.00 26.74  ? 1970 SER A CB    1 
ATOM   871  O  OG    . SER A 1 179 ? 100.554 105.372 83.865  1.00 30.58  ? 1970 SER A OG    1 
ATOM   872  N  N     . TYR A 1 180 ? 104.494 103.331 84.423  1.00 32.15  ? 1971 TYR A N     1 
ATOM   873  C  CA    . TYR A 1 180 ? 105.828 102.816 84.140  1.00 31.21  ? 1971 TYR A CA    1 
ATOM   874  C  C     . TYR A 1 180 ? 105.853 101.298 84.239  1.00 31.66  ? 1971 TYR A C     1 
ATOM   875  O  O     . TYR A 1 180 ? 106.422 100.619 83.375  1.00 36.90  ? 1971 TYR A O     1 
ATOM   876  C  CB    . TYR A 1 180 ? 106.829 103.440 85.114  1.00 27.51  ? 1971 TYR A CB    1 
ATOM   877  C  CG    . TYR A 1 180 ? 108.290 103.257 84.764  1.00 25.19  ? 1971 TYR A CG    1 
ATOM   878  C  CD1   . TYR A 1 180 ? 108.938 102.054 84.999  1.00 25.99  ? 1971 TYR A CD1   1 
ATOM   879  C  CD2   . TYR A 1 180 ? 109.028 104.301 84.226  1.00 30.11  ? 1971 TYR A CD2   1 
ATOM   880  C  CE1   . TYR A 1 180 ? 110.273 101.889 84.690  1.00 31.51  ? 1971 TYR A CE1   1 
ATOM   881  C  CE2   . TYR A 1 180 ? 110.364 104.146 83.915  1.00 35.23  ? 1971 TYR A CE2   1 
ATOM   882  C  CZ    . TYR A 1 180 ? 110.981 102.938 84.150  1.00 35.66  ? 1971 TYR A CZ    1 
ATOM   883  O  OH    . TYR A 1 180 ? 112.311 102.778 83.841  1.00 36.45  ? 1971 TYR A OH    1 
ATOM   884  N  N     . LYS A 1 181 ? 105.219 100.745 85.276  1.00 28.65  ? 1972 LYS A N     1 
ATOM   885  C  CA    . LYS A 1 181 ? 105.220 99.297  85.454  1.00 30.81  ? 1972 LYS A CA    1 
ATOM   886  C  C     . LYS A 1 181 ? 104.523 98.596  84.293  1.00 37.04  ? 1972 LYS A C     1 
ATOM   887  O  O     . LYS A 1 181 ? 105.043 97.618  83.745  1.00 46.64  ? 1972 LYS A O     1 
ATOM   888  C  CB    . LYS A 1 181 ? 104.560 98.931  86.783  1.00 30.75  ? 1972 LYS A CB    1 
ATOM   889  C  CG    . LYS A 1 181 ? 105.396 99.273  88.003  1.00 29.52  ? 1972 LYS A CG    1 
ATOM   890  C  CD    . LYS A 1 181 ? 104.637 98.993  89.286  1.00 27.23  ? 1972 LYS A CD    1 
ATOM   891  C  CE    . LYS A 1 181 ? 104.087 97.577  89.303  1.00 32.53  ? 1972 LYS A CE    1 
ATOM   892  N  NZ    . LYS A 1 181 ? 103.293 97.302  90.532  1.00 31.71  ? 1972 LYS A NZ    1 
ATOM   893  N  N     . ILE A 1 182 ? 103.344 99.084  83.897  1.00 33.55  ? 1973 ILE A N     1 
ATOM   894  C  CA    . ILE A 1 182 ? 102.623 98.407  82.822  1.00 38.66  ? 1973 ILE A CA    1 
ATOM   895  C  C     . ILE A 1 182 ? 103.344 98.591  81.494  1.00 48.82  ? 1973 ILE A C     1 
ATOM   896  O  O     . ILE A 1 182 ? 103.391 97.665  80.677  1.00 51.46  ? 1973 ILE A O     1 
ATOM   897  C  CB    . ILE A 1 182 ? 101.160 98.878  82.732  1.00 33.75  ? 1973 ILE A CB    1 
ATOM   898  C  CG1   . ILE A 1 182 ? 101.080 100.398 82.645  1.00 39.15  ? 1973 ILE A CG1   1 
ATOM   899  C  CG2   . ILE A 1 182 ? 100.370 98.366  83.925  1.00 40.43  ? 1973 ILE A CG2   1 
ATOM   900  C  CD1   . ILE A 1 182 ? 99.714  100.956 82.934  1.00 39.59  ? 1973 ILE A CD1   1 
ATOM   901  N  N     . LEU A 1 183 ? 103.920 99.772  81.250  1.00 47.98  ? 1974 LEU A N     1 
ATOM   902  C  CA    . LEU A 1 183 ? 104.669 99.974  80.016  1.00 47.02  ? 1974 LEU A CA    1 
ATOM   903  C  C     . LEU A 1 183 ? 105.895 99.075  79.955  1.00 51.88  ? 1974 LEU A C     1 
ATOM   904  O  O     . LEU A 1 183 ? 106.290 98.642  78.867  1.00 58.06  ? 1974 LEU A O     1 
ATOM   905  C  CB    . LEU A 1 183 ? 105.075 101.442 79.884  1.00 39.29  ? 1974 LEU A CB    1 
ATOM   906  C  CG    . LEU A 1 183 ? 104.012 102.387 79.321  1.00 38.70  ? 1974 LEU A CG    1 
ATOM   907  C  CD1   . LEU A 1 183 ? 104.493 103.827 79.367  1.00 40.61  ? 1974 LEU A CD1   1 
ATOM   908  C  CD2   . LEU A 1 183 ? 103.634 101.992 77.903  1.00 35.93  ? 1974 LEU A CD2   1 
ATOM   909  N  N     . LEU A 1 184 ? 106.500 98.772  81.104  1.00 46.96  ? 1975 LEU A N     1 
ATOM   910  C  CA    . LEU A 1 184 ? 107.695 97.938  81.105  1.00 43.45  ? 1975 LEU A CA    1 
ATOM   911  C  C     . LEU A 1 184 ? 107.358 96.456  80.970  1.00 52.81  ? 1975 LEU A C     1 
ATOM   912  O  O     . LEU A 1 184 ? 107.869 95.779  80.072  1.00 62.27  ? 1975 LEU A O     1 
ATOM   913  C  CB    . LEU A 1 184 ? 108.502 98.181  82.378  1.00 41.38  ? 1975 LEU A CB    1 
ATOM   914  C  CG    . LEU A 1 184 ? 109.879 97.524  82.395  1.00 46.91  ? 1975 LEU A CG    1 
ATOM   915  C  CD1   . LEU A 1 184 ? 110.599 97.748  81.075  1.00 49.41  ? 1975 LEU A CD1   1 
ATOM   916  C  CD2   . LEU A 1 184 ? 110.694 98.054  83.553  1.00 45.56  ? 1975 LEU A CD2   1 
ATOM   917  N  N     . LEU A 1 185 ? 106.510 95.930  81.858  1.00 49.20  ? 1976 LEU A N     1 
ATOM   918  C  CA    . LEU A 1 185 ? 106.303 94.483  81.895  1.00 47.76  ? 1976 LEU A CA    1 
ATOM   919  C  C     . LEU A 1 185 ? 105.518 93.981  80.688  1.00 49.08  ? 1976 LEU A C     1 
ATOM   920  O  O     . LEU A 1 185 ? 105.881 92.959  80.095  1.00 59.73  ? 1976 LEU A O     1 
ATOM   921  C  CB    . LEU A 1 185 ? 105.613 94.072  83.197  1.00 47.96  ? 1976 LEU A CB    1 
ATOM   922  C  CG    . LEU A 1 185 ? 106.030 94.785  84.482  1.00 42.42  ? 1976 LEU A CG    1 
ATOM   923  C  CD1   . LEU A 1 185 ? 105.298 94.202  85.676  1.00 35.51  ? 1976 LEU A CD1   1 
ATOM   924  C  CD2   . LEU A 1 185 ? 107.531 94.671  84.679  1.00 42.83  ? 1976 LEU A CD2   1 
ATOM   925  N  N     . SER A 1 186 ? 104.444 94.671  80.306  1.00 45.11  ? 1977 SER A N     1 
ATOM   926  C  CA    . SER A 1 186 ? 103.591 94.175  79.230  1.00 60.64  ? 1977 SER A CA    1 
ATOM   927  C  C     . SER A 1 186 ? 103.956 94.753  77.867  1.00 64.36  ? 1977 SER A C     1 
ATOM   928  O  O     . SER A 1 186 ? 104.143 93.999  76.909  1.00 68.45  ? 1977 SER A O     1 
ATOM   929  C  CB    . SER A 1 186 ? 102.116 94.457  79.544  1.00 71.58  ? 1977 SER A CB    1 
ATOM   930  O  OG    . SER A 1 186 ? 101.830 95.842  79.526  1.00 72.27  ? 1977 SER A OG    1 
ATOM   931  N  N     . CYS A 1 187 ? 104.060 96.079  77.756  1.00 62.18  ? 1978 CYS A N     1 
ATOM   932  C  CA    . CYS A 1 187 ? 104.384 96.686  76.470  1.00 64.88  ? 1978 CYS A CA    1 
ATOM   933  C  C     . CYS A 1 187 ? 105.855 96.538  76.108  1.00 61.72  ? 1978 CYS A C     1 
ATOM   934  O  O     . CYS A 1 187 ? 106.204 96.659  74.929  1.00 65.25  ? 1978 CYS A O     1 
ATOM   935  C  CB    . CYS A 1 187 ? 103.992 98.163  76.472  1.00 68.21  ? 1978 CYS A CB    1 
ATOM   936  S  SG    . CYS A 1 187 ? 102.557 98.544  77.500  1.00 82.95  ? 1978 CYS A SG    1 
ATOM   937  N  N     . GLY A 1 188 ? 106.722 96.282  77.084  1.00 60.47  ? 1979 GLY A N     1 
ATOM   938  C  CA    . GLY A 1 188 ? 108.129 96.082  76.809  1.00 60.27  ? 1979 GLY A CA    1 
ATOM   939  C  C     . GLY A 1 188 ? 108.922 97.337  76.532  1.00 61.57  ? 1979 GLY A C     1 
ATOM   940  O  O     . GLY A 1 188 ? 110.085 97.235  76.126  1.00 67.24  ? 1979 GLY A O     1 
ATOM   941  N  N     . ILE A 1 189 ? 108.341 98.515  76.738  1.00 58.60  ? 1980 ILE A N     1 
ATOM   942  C  CA    . ILE A 1 189 ? 109.022 99.778  76.486  1.00 53.66  ? 1980 ILE A CA    1 
ATOM   943  C  C     . ILE A 1 189 ? 109.169 100.534 77.798  1.00 52.44  ? 1980 ILE A C     1 
ATOM   944  O  O     . ILE A 1 189 ? 108.238 100.612 78.606  1.00 55.64  ? 1980 ILE A O     1 
ATOM   945  C  CB    . ILE A 1 189 ? 108.280 100.634 75.435  1.00 54.75  ? 1980 ILE A CB    1 
ATOM   946  C  CG1   . ILE A 1 189 ? 106.838 100.896 75.870  1.00 56.79  ? 1980 ILE A CG1   1 
ATOM   947  C  CG2   . ILE A 1 189 ? 108.317 99.959  74.074  1.00 66.42  ? 1980 ILE A CG2   1 
ATOM   948  C  CD1   . ILE A 1 189 ? 106.157 101.989 75.086  1.00 64.33  ? 1980 ILE A CD1   1 
ATOM   949  N  N     . SER A 1 190 ? 110.361 101.083 78.014  1.00 48.85  ? 1981 SER A N     1 
ATOM   950  C  CA    . SER A 1 190 ? 110.674 101.818 79.231  1.00 45.65  ? 1981 SER A CA    1 
ATOM   951  C  C     . SER A 1 190 ? 111.017 103.255 78.873  1.00 44.07  ? 1981 SER A C     1 
ATOM   952  O  O     . SER A 1 190 ? 111.861 103.497 78.005  1.00 49.71  ? 1981 SER A O     1 
ATOM   953  C  CB    . SER A 1 190 ? 111.834 101.166 79.990  1.00 45.57  ? 1981 SER A CB    1 
ATOM   954  O  OG    . SER A 1 190 ? 112.994 101.086 79.181  1.00 35.13  ? 1981 SER A OG    1 
ATOM   955  N  N     . LEU A 1 191 ? 110.362 104.201 79.539  1.00 40.73  ? 1982 LEU A N     1 
ATOM   956  C  CA    . LEU A 1 191 ? 110.625 105.609 79.290  1.00 49.01  ? 1982 LEU A CA    1 
ATOM   957  C  C     . LEU A 1 191 ? 111.978 106.013 79.864  1.00 57.85  ? 1982 LEU A C     1 
ATOM   958  O  O     . LEU A 1 191 ? 112.478 105.414 80.819  1.00 60.42  ? 1982 LEU A O     1 
ATOM   959  C  CB    . LEU A 1 191 ? 109.525 106.480 79.897  1.00 39.74  ? 1982 LEU A CB    1 
ATOM   960  C  CG    . LEU A 1 191 ? 108.081 105.992 79.779  1.00 32.47  ? 1982 LEU A CG    1 
ATOM   961  C  CD1   . LEU A 1 191 ? 107.669 105.203 81.008  1.00 34.61  ? 1982 LEU A CD1   1 
ATOM   962  C  CD2   . LEU A 1 191 ? 107.149 107.167 79.561  1.00 29.64  ? 1982 LEU A CD2   1 
ATOM   963  N  N     . GLU A 1 192 ? 112.576 107.044 79.262  1.00 56.15  ? 1983 GLU A N     1 
ATOM   964  C  CA    . GLU A 1 192 ? 113.843 107.565 79.760  1.00 59.64  ? 1983 GLU A CA    1 
ATOM   965  C  C     . GLU A 1 192 ? 113.894 109.089 79.729  1.00 65.36  ? 1983 GLU A C     1 
ATOM   966  O  O     . GLU A 1 192 ? 114.989 109.663 79.759  1.00 75.84  ? 1983 GLU A O     1 
ATOM   967  C  CB    . GLU A 1 192 ? 115.018 106.993 78.963  1.00 64.00  ? 1983 GLU A CB    1 
ATOM   968  C  CG    . GLU A 1 192 ? 115.846 105.987 79.740  1.00 72.92  ? 1983 GLU A CG    1 
ATOM   969  C  CD    . GLU A 1 192 ? 116.362 106.552 81.050  1.00 83.64  ? 1983 GLU A CD    1 
ATOM   970  O  OE1   . GLU A 1 192 ? 116.997 107.627 81.027  1.00 84.92  ? 1983 GLU A OE1   1 
ATOM   971  O  OE2   . GLU A 1 192 ? 116.127 105.924 82.104  1.00 77.03  ? 1983 GLU A OE2   1 
ATOM   972  N  N     . GLN A 1 193 ? 112.747 109.757 79.673  1.00 52.81  ? 1984 GLN A N     1 
ATOM   973  C  CA    . GLN A 1 193 ? 112.685 111.208 79.651  1.00 45.86  ? 1984 GLN A CA    1 
ATOM   974  C  C     . GLN A 1 193 ? 112.277 111.731 81.025  1.00 44.74  ? 1984 GLN A C     1 
ATOM   975  O  O     . GLN A 1 193 ? 111.980 110.969 81.948  1.00 51.55  ? 1984 GLN A O     1 
ATOM   976  C  CB    . GLN A 1 193 ? 111.712 111.684 78.572  1.00 51.28  ? 1984 GLN A CB    1 
ATOM   977  C  CG    . GLN A 1 193 ? 112.127 111.327 77.158  1.00 59.72  ? 1984 GLN A CG    1 
ATOM   978  C  CD    . GLN A 1 193 ? 111.351 110.151 76.607  1.00 58.18  ? 1984 GLN A CD    1 
ATOM   979  O  OE1   . GLN A 1 193 ? 111.058 109.196 77.324  1.00 57.79  ? 1984 GLN A OE1   1 
ATOM   980  N  NE2   . GLN A 1 193 ? 111.010 110.215 75.326  1.00 60.40  ? 1984 GLN A NE2   1 
ATOM   981  N  N     . SER A 1 194 ? 112.272 113.053 81.162  1.00 43.42  ? 1985 SER A N     1 
ATOM   982  C  CA    . SER A 1 194 ? 111.785 113.671 82.386  1.00 44.77  ? 1985 SER A CA    1 
ATOM   983  C  C     . SER A 1 194 ? 110.295 113.401 82.551  1.00 44.53  ? 1985 SER A C     1 
ATOM   984  O  O     . SER A 1 194 ? 109.550 113.296 81.574  1.00 46.77  ? 1985 SER A O     1 
ATOM   985  C  CB    . SER A 1 194 ? 112.048 115.176 82.369  1.00 43.03  ? 1985 SER A CB    1 
ATOM   986  O  OG    . SER A 1 194 ? 113.431 115.455 82.492  1.00 46.77  ? 1985 SER A OG    1 
ATOM   987  N  N     . TYR A 1 195 ? 109.863 113.276 83.801  1.00 36.13  ? 1986 TYR A N     1 
ATOM   988  C  CA    . TYR A 1 195 ? 108.478 112.968 84.120  1.00 30.72  ? 1986 TYR A CA    1 
ATOM   989  C  C     . TYR A 1 195 ? 107.839 114.128 84.872  1.00 32.67  ? 1986 TYR A C     1 
ATOM   990  O  O     . TYR A 1 195 ? 108.503 114.846 85.623  1.00 44.78  ? 1986 TYR A O     1 
ATOM   991  C  CB    . TYR A 1 195 ? 108.380 111.686 84.947  1.00 29.96  ? 1986 TYR A CB    1 
ATOM   992  C  CG    . TYR A 1 195 ? 109.277 110.581 84.446  1.00 30.04  ? 1986 TYR A CG    1 
ATOM   993  C  CD1   . TYR A 1 195 ? 108.966 109.880 83.290  1.00 27.08  ? 1986 TYR A CD1   1 
ATOM   994  C  CD2   . TYR A 1 195 ? 110.439 110.243 85.124  1.00 30.81  ? 1986 TYR A CD2   1 
ATOM   995  C  CE1   . TYR A 1 195 ? 109.783 108.870 82.827  1.00 33.04  ? 1986 TYR A CE1   1 
ATOM   996  C  CE2   . TYR A 1 195 ? 111.263 109.235 84.668  1.00 31.91  ? 1986 TYR A CE2   1 
ATOM   997  C  CZ    . TYR A 1 195 ? 110.930 108.552 83.520  1.00 40.86  ? 1986 TYR A CZ    1 
ATOM   998  O  OH    . TYR A 1 195 ? 111.750 107.547 83.062  1.00 47.75  ? 1986 TYR A OH    1 
ATOM   999  N  N     . GLU A 1 196 ? 106.545 114.317 84.639  1.00 29.80  ? 1987 GLU A N     1 
ATOM   1000 C  CA    . GLU A 1 196 ? 105.799 115.444 85.189  1.00 34.28  ? 1987 GLU A CA    1 
ATOM   1001 C  C     . GLU A 1 196 ? 104.443 114.979 85.712  1.00 41.52  ? 1987 GLU A C     1 
ATOM   1002 O  O     . GLU A 1 196 ? 103.394 115.498 85.327  1.00 52.30  ? 1987 GLU A O     1 
ATOM   1003 C  CB    . GLU A 1 196 ? 105.650 116.554 84.153  1.00 42.58  ? 1987 GLU A CB    1 
ATOM   1004 C  CG    . GLU A 1 196 ? 106.876 117.440 84.033  1.00 43.38  ? 1987 GLU A CG    1 
ATOM   1005 C  CD    . GLU A 1 196 ? 106.609 118.700 83.238  1.00 60.71  ? 1987 GLU A CD    1 
ATOM   1006 O  OE1   . GLU A 1 196 ? 105.802 118.644 82.287  1.00 56.11  ? 1987 GLU A OE1   1 
ATOM   1007 O  OE2   . GLU A 1 196 ? 107.210 119.745 83.562  1.00 67.67  ? 1987 GLU A OE2   1 
ATOM   1008 N  N     . ASP A 1 197 ? 104.455 113.959 86.565  1.00 38.24  ? 1988 ASP A N     1 
ATOM   1009 C  CA    . ASP A 1 197 ? 103.227 113.413 87.128  1.00 37.99  ? 1988 ASP A CA    1 
ATOM   1010 C  C     . ASP A 1 197 ? 102.383 114.529 87.746  1.00 37.68  ? 1988 ASP A C     1 
ATOM   1011 O  O     . ASP A 1 197 ? 102.889 115.292 88.580  1.00 43.39  ? 1988 ASP A O     1 
ATOM   1012 C  CB    . ASP A 1 197 ? 103.571 112.365 88.189  1.00 33.65  ? 1988 ASP A CB    1 
ATOM   1013 C  CG    . ASP A 1 197 ? 102.380 111.516 88.595  1.00 33.49  ? 1988 ASP A CG    1 
ATOM   1014 O  OD1   . ASP A 1 197 ? 101.277 112.063 88.786  1.00 36.90  ? 1988 ASP A OD1   1 
ATOM   1015 O  OD2   . ASP A 1 197 ? 102.552 110.293 88.749  1.00 29.17  ? 1988 ASP A OD2   1 
ATOM   1016 N  N     . PRO A 1 198 ? 101.107 114.659 87.366  1.00 29.76  ? 1989 PRO A N     1 
ATOM   1017 C  CA    . PRO A 1 198 ? 100.278 115.738 87.919  1.00 31.52  ? 1989 PRO A CA    1 
ATOM   1018 C  C     . PRO A 1 198 ? 99.816  115.456 89.338  1.00 37.36  ? 1989 PRO A C     1 
ATOM   1019 O  O     . PRO A 1 198 ? 99.602  116.382 90.125  1.00 42.83  ? 1989 PRO A O     1 
ATOM   1020 C  CB    . PRO A 1 198 ? 99.094  115.798 86.948  1.00 36.67  ? 1989 PRO A CB    1 
ATOM   1021 C  CG    . PRO A 1 198 ? 98.981  114.414 86.426  1.00 37.50  ? 1989 PRO A CG    1 
ATOM   1022 C  CD    . PRO A 1 198 ? 100.383 113.869 86.355  1.00 35.33  ? 1989 PRO A CD    1 
ATOM   1023 N  N     . LYS A 1 199 ? 99.651  114.175 89.672  1.00 36.77  ? 1990 LYS A N     1 
ATOM   1024 C  CA    . LYS A 1 199 ? 99.283  113.808 91.035  1.00 32.23  ? 1990 LYS A CA    1 
ATOM   1025 C  C     . LYS A 1 199 ? 100.370 114.214 92.021  1.00 35.09  ? 1990 LYS A C     1 
ATOM   1026 O  O     . LYS A 1 199 ? 100.077 114.689 93.125  1.00 47.01  ? 1990 LYS A O     1 
ATOM   1027 C  CB    . LYS A 1 199 ? 99.011  112.306 91.111  1.00 28.95  ? 1990 LYS A CB    1 
ATOM   1028 C  CG    . LYS A 1 199 ? 98.995  111.741 92.516  1.00 32.38  ? 1990 LYS A CG    1 
ATOM   1029 C  CD    . LYS A 1 199 ? 98.751  110.242 92.499  1.00 42.78  ? 1990 LYS A CD    1 
ATOM   1030 C  CE    . LYS A 1 199 ? 97.463  109.903 91.770  1.00 39.15  ? 1990 LYS A CE    1 
ATOM   1031 N  NZ    . LYS A 1 199 ? 97.118  108.462 91.900  1.00 45.46  ? 1990 LYS A NZ    1 
ATOM   1032 N  N     . VAL A 1 200 ? 101.635 114.049 91.632  1.00 34.35  ? 1991 VAL A N     1 
ATOM   1033 C  CA    . VAL A 1 200 ? 102.742 114.446 92.497  1.00 30.97  ? 1991 VAL A CA    1 
ATOM   1034 C  C     . VAL A 1 200 ? 102.750 115.956 92.702  1.00 31.43  ? 1991 VAL A C     1 
ATOM   1035 O  O     . VAL A 1 200 ? 102.987 116.443 93.812  1.00 35.17  ? 1991 VAL A O     1 
ATOM   1036 C  CB    . VAL A 1 200 ? 104.073 113.940 91.916  1.00 28.42  ? 1991 VAL A CB    1 
ATOM   1037 C  CG1   . VAL A 1 200 ? 105.236 114.662 92.555  1.00 29.67  ? 1991 VAL A CG1   1 
ATOM   1038 C  CG2   . VAL A 1 200 ? 104.193 112.443 92.121  1.00 26.27  ? 1991 VAL A CG2   1 
ATOM   1039 N  N     . ALA A 1 201 ? 102.495 116.722 91.639  1.00 32.07  ? 1992 ALA A N     1 
ATOM   1040 C  CA    . ALA A 1 201 ? 102.426 118.174 91.782  1.00 35.74  ? 1992 ALA A CA    1 
ATOM   1041 C  C     . ALA A 1 201 ? 101.263 118.586 92.676  1.00 33.02  ? 1992 ALA A C     1 
ATOM   1042 O  O     . ALA A 1 201 ? 101.395 119.500 93.501  1.00 34.74  ? 1992 ALA A O     1 
ATOM   1043 C  CB    . ALA A 1 201 ? 102.309 118.833 90.409  1.00 44.37  ? 1992 ALA A CB    1 
ATOM   1044 N  N     . CYS A 1 202 ? 100.114 117.924 92.524  1.00 32.96  ? 1993 CYS A N     1 
ATOM   1045 C  CA    . CYS A 1 202 ? 98.976  118.208 93.391  1.00 36.91  ? 1993 CYS A CA    1 
ATOM   1046 C  C     . CYS A 1 202 ? 99.313  117.912 94.845  1.00 36.14  ? 1993 CYS A C     1 
ATOM   1047 O  O     . CYS A 1 202 ? 98.897  118.646 95.749  1.00 41.07  ? 1993 CYS A O     1 
ATOM   1048 C  CB    . CYS A 1 202 ? 97.760  117.399 92.945  1.00 38.36  ? 1993 CYS A CB    1 
ATOM   1049 S  SG    . CYS A 1 202 ? 96.264  117.729 93.900  1.00 50.32  ? 1993 CYS A SG    1 
ATOM   1050 N  N     . TRP A 1 203 ? 100.058 116.833 95.090  1.00 34.04  ? 1994 TRP A N     1 
ATOM   1051 C  CA    . TRP A 1 203 ? 100.535 116.562 96.442  1.00 29.47  ? 1994 TRP A CA    1 
ATOM   1052 C  C     . TRP A 1 203 ? 101.469 117.664 96.924  1.00 29.67  ? 1994 TRP A C     1 
ATOM   1053 O  O     . TRP A 1 203 ? 101.393 118.090 98.081  1.00 34.38  ? 1994 TRP A O     1 
ATOM   1054 C  CB    . TRP A 1 203 ? 101.245 115.212 96.497  1.00 27.72  ? 1994 TRP A CB    1 
ATOM   1055 C  CG    . TRP A 1 203 ? 102.040 115.041 97.749  1.00 29.89  ? 1994 TRP A CG    1 
ATOM   1056 C  CD1   . TRP A 1 203 ? 101.566 115.065 99.024  1.00 34.28  ? 1994 TRP A CD1   1 
ATOM   1057 C  CD2   . TRP A 1 203 ? 103.452 114.835 97.850  1.00 25.03  ? 1994 TRP A CD2   1 
ATOM   1058 N  NE1   . TRP A 1 203 ? 102.593 114.884 99.916  1.00 28.93  ? 1994 TRP A NE1   1 
ATOM   1059 C  CE2   . TRP A 1 203 ? 103.762 114.740 99.220  1.00 22.85  ? 1994 TRP A CE2   1 
ATOM   1060 C  CE3   . TRP A 1 203 ? 104.483 114.718 96.917  1.00 27.74  ? 1994 TRP A CE3   1 
ATOM   1061 C  CZ2   . TRP A 1 203 ? 105.057 114.534 99.677  1.00 22.28  ? 1994 TRP A CZ2   1 
ATOM   1062 C  CZ3   . TRP A 1 203 ? 105.768 114.514 97.373  1.00 30.76  ? 1994 TRP A CZ3   1 
ATOM   1063 C  CH2   . TRP A 1 203 ? 106.045 114.423 98.741  1.00 26.86  ? 1994 TRP A CH2   1 
ATOM   1064 N  N     . LEU A 1 204 ? 102.359 118.135 96.048  1.00 29.36  ? 1995 LEU A N     1 
ATOM   1065 C  CA    . LEU A 1 204 ? 103.288 119.195 96.428  1.00 28.56  ? 1995 LEU A CA    1 
ATOM   1066 C  C     . LEU A 1 204 ? 102.544 120.458 96.836  1.00 32.24  ? 1995 LEU A C     1 
ATOM   1067 O  O     . LEU A 1 204 ? 102.974 121.173 97.748  1.00 30.57  ? 1995 LEU A O     1 
ATOM   1068 C  CB    . LEU A 1 204 ? 104.249 119.497 95.279  1.00 31.02  ? 1995 LEU A CB    1 
ATOM   1069 C  CG    . LEU A 1 204 ? 105.683 118.993 95.428  1.00 25.17  ? 1995 LEU A CG    1 
ATOM   1070 C  CD1   . LEU A 1 204 ? 106.224 119.344 96.800  1.00 32.19  ? 1995 LEU A CD1   1 
ATOM   1071 C  CD2   . LEU A 1 204 ? 105.752 117.503 95.189  1.00 27.15  ? 1995 LEU A CD2   1 
ATOM   1072 N  N     . LEU A 1 205 ? 101.433 120.756 96.162  1.00 37.65  ? 1996 LEU A N     1 
ATOM   1073 C  CA    . LEU A 1 205 ? 100.643 121.926 96.532  1.00 41.97  ? 1996 LEU A CA    1 
ATOM   1074 C  C     . LEU A 1 205 ? 100.095 121.796 97.949  1.00 47.29  ? 1996 LEU A C     1 
ATOM   1075 O  O     . LEU A 1 205 ? 100.279 122.689 98.783  1.00 42.57  ? 1996 LEU A O     1 
ATOM   1076 C  CB    . LEU A 1 205 ? 99.508  122.132 95.529  1.00 39.12  ? 1996 LEU A CB    1 
ATOM   1077 C  CG    . LEU A 1 205 ? 99.755  123.151 94.416  1.00 39.31  ? 1996 LEU A CG    1 
ATOM   1078 C  CD1   . LEU A 1 205 ? 100.117 124.503 95.006  1.00 41.29  ? 1996 LEU A CD1   1 
ATOM   1079 C  CD2   . LEU A 1 205 ? 100.838 122.672 93.469  1.00 37.33  ? 1996 LEU A CD2   1 
ATOM   1080 N  N     . ASP A 1 206 ? 99.423  120.682 98.242  1.00 48.39  ? 1997 ASP A N     1 
ATOM   1081 C  CA    . ASP A 1 206 ? 98.810  120.440 99.549  1.00 46.05  ? 1997 ASP A CA    1 
ATOM   1082 C  C     . ASP A 1 206 ? 99.194  119.046 100.027 1.00 41.63  ? 1997 ASP A C     1 
ATOM   1083 O  O     . ASP A 1 206 ? 98.468  118.073 99.780  1.00 44.22  ? 1997 ASP A O     1 
ATOM   1084 C  CB    . ASP A 1 206 ? 97.293  120.597 99.482  1.00 46.82  ? 1997 ASP A CB    1 
ATOM   1085 C  CG    . ASP A 1 206 ? 96.820  121.923 100.043 1.00 57.37  ? 1997 ASP A CG    1 
ATOM   1086 O  OD1   . ASP A 1 206 ? 97.318  122.329 101.114 1.00 63.42  ? 1997 ASP A OD1   1 
ATOM   1087 O  OD2   . ASP A 1 206 ? 95.948  122.559 99.414  1.00 60.76  ? 1997 ASP A OD2   1 
ATOM   1088 N  N     . PRO A 1 207 ? 100.333 118.909 100.711 1.00 36.66  ? 1998 PRO A N     1 
ATOM   1089 C  CA    . PRO A 1 207 ? 100.766 117.571 101.147 1.00 34.57  ? 1998 PRO A CA    1 
ATOM   1090 C  C     . PRO A 1 207 ? 99.796  116.889 102.094 1.00 39.51  ? 1998 PRO A C     1 
ATOM   1091 O  O     . PRO A 1 207 ? 99.699  115.656 102.083 1.00 40.89  ? 1998 PRO A O     1 
ATOM   1092 C  CB    . PRO A 1 207 ? 102.117 117.843 101.820 1.00 29.26  ? 1998 PRO A CB    1 
ATOM   1093 C  CG    . PRO A 1 207 ? 102.064 119.273 102.214 1.00 33.23  ? 1998 PRO A CG    1 
ATOM   1094 C  CD    . PRO A 1 207 ? 101.253 119.964 101.162 1.00 39.23  ? 1998 PRO A CD    1 
ATOM   1095 N  N     . ASP A 1 208 ? 99.072  117.649 102.913 1.00 42.06  ? 1999 ASP A N     1 
ATOM   1096 C  CA    . ASP A 1 208 ? 98.152  117.063 103.879 1.00 45.46  ? 1999 ASP A CA    1 
ATOM   1097 C  C     . ASP A 1 208 ? 96.787  116.746 103.286 1.00 50.42  ? 1999 ASP A C     1 
ATOM   1098 O  O     . ASP A 1 208 ? 95.949  116.166 103.985 1.00 55.12  ? 1999 ASP A O     1 
ATOM   1099 C  CB    . ASP A 1 208 ? 97.986  118.004 105.073 1.00 51.80  ? 1999 ASP A CB    1 
ATOM   1100 C  CG    . ASP A 1 208 ? 97.584  119.404 104.657 1.00 64.02  ? 1999 ASP A CG    1 
ATOM   1101 O  OD1   . ASP A 1 208 ? 96.459  119.580 104.144 1.00 62.41  ? 1999 ASP A OD1   1 
ATOM   1102 O  OD2   . ASP A 1 208 ? 98.402  120.328 104.827 1.00 66.50  ? 1999 ASP A OD2   1 
ATOM   1103 N  N     . SER A 1 209 ? 96.543  117.108 102.030 1.00 48.55  ? 2000 SER A N     1 
ATOM   1104 C  CA    . SER A 1 209 ? 95.244  116.883 101.420 1.00 45.83  ? 2000 SER A CA    1 
ATOM   1105 C  C     . SER A 1 209 ? 95.025  115.396 101.154 1.00 47.74  ? 2000 SER A C     1 
ATOM   1106 O  O     . SER A 1 209 ? 95.945  114.576 101.229 1.00 44.82  ? 2000 SER A O     1 
ATOM   1107 C  CB    . SER A 1 209 ? 95.118  117.674 100.119 1.00 39.66  ? 2000 SER A CB    1 
ATOM   1108 O  OG    . SER A 1 209 ? 95.872  117.069 99.084  1.00 37.57  ? 2000 SER A OG    1 
ATOM   1109 N  N     . GLN A 1 210 ? 93.779  115.054 100.840 1.00 53.39  ? 2001 GLN A N     1 
ATOM   1110 C  CA    . GLN A 1 210 ? 93.430  113.680 100.523 1.00 53.40  ? 2001 GLN A CA    1 
ATOM   1111 C  C     . GLN A 1 210 ? 94.111  113.253 99.224  1.00 53.53  ? 2001 GLN A C     1 
ATOM   1112 O  O     . GLN A 1 210 ? 94.548  114.082 98.421  1.00 49.34  ? 2001 GLN A O     1 
ATOM   1113 C  CB    . GLN A 1 210 ? 91.911  113.534 100.411 1.00 50.33  ? 2001 GLN A CB    1 
ATOM   1114 C  CG    . GLN A 1 210 ? 91.401  112.102 100.437 1.00 54.92  ? 2001 GLN A CG    1 
ATOM   1115 C  CD    . GLN A 1 210 ? 90.178  111.906 99.565  1.00 56.07  ? 2001 GLN A CD    1 
ATOM   1116 O  OE1   . GLN A 1 210 ? 89.379  112.824 99.381  1.00 55.66  ? 2001 GLN A OE1   1 
ATOM   1117 N  NE2   . GLN A 1 210 ? 90.026  110.704 99.021  1.00 55.41  ? 2001 GLN A NE2   1 
ATOM   1118 N  N     . GLU A 1 211 ? 94.211  111.941 99.032  1.00 53.05  ? 2002 GLU A N     1 
ATOM   1119 C  CA    . GLU A 1 211 ? 94.877  111.408 97.853  1.00 45.59  ? 2002 GLU A CA    1 
ATOM   1120 C  C     . GLU A 1 211 ? 94.182  111.918 96.595  1.00 46.02  ? 2002 GLU A C     1 
ATOM   1121 O  O     . GLU A 1 211 ? 92.963  111.750 96.454  1.00 56.79  ? 2002 GLU A O     1 
ATOM   1122 C  CB    . GLU A 1 211 ? 94.874  109.882 97.879  1.00 42.67  ? 2002 GLU A CB    1 
ATOM   1123 C  CG    . GLU A 1 211 ? 95.987  109.249 97.066  1.00 45.79  ? 2002 GLU A CG    1 
ATOM   1124 C  CD    . GLU A 1 211 ? 96.567  108.021 97.735  1.00 54.59  ? 2002 GLU A CD    1 
ATOM   1125 O  OE1   . GLU A 1 211 ? 96.049  107.623 98.799  1.00 53.26  ? 2002 GLU A OE1   1 
ATOM   1126 O  OE2   . GLU A 1 211 ? 97.540  107.453 97.198  1.00 70.82  ? 2002 GLU A OE2   1 
ATOM   1127 N  N     . PRO A 1 212 ? 94.907  112.538 95.667  1.00 37.63  ? 2003 PRO A N     1 
ATOM   1128 C  CA    . PRO A 1 212 ? 94.264  113.224 94.540  1.00 37.37  ? 2003 PRO A CA    1 
ATOM   1129 C  C     . PRO A 1 212 ? 93.853  112.242 93.456  1.00 48.30  ? 2003 PRO A C     1 
ATOM   1130 O  O     . PRO A 1 212 ? 94.697  111.657 92.770  1.00 55.24  ? 2003 PRO A O     1 
ATOM   1131 C  CB    . PRO A 1 212 ? 95.358  114.189 94.052  1.00 38.49  ? 2003 PRO A CB    1 
ATOM   1132 C  CG    . PRO A 1 212 ? 96.563  113.953 94.940  1.00 44.78  ? 2003 PRO A CG    1 
ATOM   1133 C  CD    . PRO A 1 212 ? 96.369  112.627 95.586  1.00 44.35  ? 2003 PRO A CD    1 
ATOM   1134 N  N     . THR A 1 213 ? 92.547  112.052 93.307  1.00 53.67  ? 2004 THR A N     1 
ATOM   1135 C  CA    . THR A 1 213 ? 92.014  111.328 92.168  1.00 53.26  ? 2004 THR A CA    1 
ATOM   1136 C  C     . THR A 1 213 ? 91.994  112.244 90.946  1.00 49.12  ? 2004 THR A C     1 
ATOM   1137 O  O     . THR A 1 213 ? 92.221  113.452 91.042  1.00 47.35  ? 2004 THR A O     1 
ATOM   1138 C  CB    . THR A 1 213 ? 90.615  110.798 92.481  1.00 60.35  ? 2004 THR A CB    1 
ATOM   1139 O  OG1   . THR A 1 213 ? 90.135  110.016 91.381  1.00 72.28  ? 2004 THR A OG1   1 
ATOM   1140 C  CG2   . THR A 1 213 ? 89.655  111.947 92.739  1.00 62.50  ? 2004 THR A CG2   1 
ATOM   1141 N  N     . LEU A 1 214 ? 91.732  111.656 89.778  1.00 51.84  ? 2005 LEU A N     1 
ATOM   1142 C  CA    . LEU A 1 214 ? 91.653  112.461 88.563  1.00 53.46  ? 2005 LEU A CA    1 
ATOM   1143 C  C     . LEU A 1 214 ? 90.546  113.500 88.669  1.00 56.76  ? 2005 LEU A C     1 
ATOM   1144 O  O     . LEU A 1 214 ? 90.726  114.655 88.266  1.00 55.16  ? 2005 LEU A O     1 
ATOM   1145 C  CB    . LEU A 1 214 ? 91.434  111.566 87.345  1.00 48.64  ? 2005 LEU A CB    1 
ATOM   1146 C  CG    . LEU A 1 214 ? 91.322  112.290 86.001  1.00 39.07  ? 2005 LEU A CG    1 
ATOM   1147 C  CD1   . LEU A 1 214 ? 92.478  113.252 85.801  1.00 40.62  ? 2005 LEU A CD1   1 
ATOM   1148 C  CD2   . LEU A 1 214 ? 91.262  111.294 84.864  1.00 50.61  ? 2005 LEU A CD2   1 
ATOM   1149 N  N     . HIS A 1 215 ? 89.398  113.111 89.226  1.00 61.64  ? 2006 HIS A N     1 
ATOM   1150 C  CA    . HIS A 1 215 ? 88.287  114.045 89.365  1.00 62.68  ? 2006 HIS A CA    1 
ATOM   1151 C  C     . HIS A 1 215 ? 88.664  115.228 90.248  1.00 61.95  ? 2006 HIS A C     1 
ATOM   1152 O  O     . HIS A 1 215 ? 88.311  116.373 89.945  1.00 65.16  ? 2006 HIS A O     1 
ATOM   1153 C  CB    . HIS A 1 215 ? 87.065  113.322 89.930  1.00 64.18  ? 2006 HIS A CB    1 
ATOM   1154 C  CG    . HIS A 1 215 ? 85.787  114.085 89.777  1.00 66.01  ? 2006 HIS A CG    1 
ATOM   1155 N  ND1   . HIS A 1 215 ? 85.703  115.261 89.064  1.00 70.23  ? 2006 HIS A ND1   1 
ATOM   1156 C  CD2   . HIS A 1 215 ? 84.541  113.840 90.247  1.00 67.63  ? 2006 HIS A CD2   1 
ATOM   1157 C  CE1   . HIS A 1 215 ? 84.461  115.708 89.100  1.00 77.70  ? 2006 HIS A CE1   1 
ATOM   1158 N  NE2   . HIS A 1 215 ? 83.735  114.864 89.812  1.00 75.50  ? 2006 HIS A NE2   1 
ATOM   1159 N  N     . SER A 1 216 ? 89.385  114.973 91.342  1.00 59.20  ? 2007 SER A N     1 
ATOM   1160 C  CA    . SER A 1 216 ? 89.733  116.051 92.264  1.00 62.90  ? 2007 SER A CA    1 
ATOM   1161 C  C     . SER A 1 216 ? 90.684  117.052 91.616  1.00 63.49  ? 2007 SER A C     1 
ATOM   1162 O  O     . SER A 1 216 ? 90.490  118.269 91.730  1.00 63.07  ? 2007 SER A O     1 
ATOM   1163 C  CB    . SER A 1 216 ? 90.341  115.476 93.544  1.00 56.61  ? 2007 SER A CB    1 
ATOM   1164 O  OG    . SER A 1 216 ? 91.624  114.926 93.307  1.00 59.30  ? 2007 SER A OG    1 
ATOM   1165 N  N     . ILE A 1 217 ? 91.720  116.561 90.929  1.00 64.53  ? 2008 ILE A N     1 
ATOM   1166 C  CA    . ILE A 1 217 ? 92.654  117.476 90.280  1.00 62.82  ? 2008 ILE A CA    1 
ATOM   1167 C  C     . ILE A 1 217 ? 91.975  118.213 89.134  1.00 62.75  ? 2008 ILE A C     1 
ATOM   1168 O  O     . ILE A 1 217 ? 92.270  119.388 88.885  1.00 62.66  ? 2008 ILE A O     1 
ATOM   1169 C  CB    . ILE A 1 217 ? 93.928  116.739 89.818  1.00 54.13  ? 2008 ILE A CB    1 
ATOM   1170 C  CG1   . ILE A 1 217 ? 93.674  115.907 88.559  1.00 46.73  ? 2008 ILE A CG1   1 
ATOM   1171 C  CG2   . ILE A 1 217 ? 94.471  115.865 90.936  1.00 59.31  ? 2008 ILE A CG2   1 
ATOM   1172 C  CD1   . ILE A 1 217 ? 94.724  114.853 88.304  1.00 40.55  ? 2008 ILE A CD1   1 
ATOM   1173 N  N     . VAL A 1 218 ? 91.055  117.553 88.426  1.00 61.75  ? 2009 VAL A N     1 
ATOM   1174 C  CA    . VAL A 1 218 ? 90.328  118.228 87.356  1.00 65.62  ? 2009 VAL A CA    1 
ATOM   1175 C  C     . VAL A 1 218 ? 89.459  119.343 87.921  1.00 68.25  ? 2009 VAL A C     1 
ATOM   1176 O  O     . VAL A 1 218 ? 89.408  120.449 87.372  1.00 67.74  ? 2009 VAL A O     1 
ATOM   1177 C  CB    . VAL A 1 218 ? 89.500  117.211 86.552  1.00 68.34  ? 2009 VAL A CB    1 
ATOM   1178 C  CG1   . VAL A 1 218 ? 88.467  117.924 85.697  1.00 74.77  ? 2009 VAL A CG1   1 
ATOM   1179 C  CG2   . VAL A 1 218 ? 90.412  116.357 85.694  1.00 63.01  ? 2009 VAL A CG2   1 
ATOM   1180 N  N     . THR A 1 219 ? 88.765  119.075 89.028  1.00 69.99  ? 2010 THR A N     1 
ATOM   1181 C  CA    . THR A 1 219 ? 87.911  120.094 89.629  1.00 68.02  ? 2010 THR A CA    1 
ATOM   1182 C  C     . THR A 1 219 ? 88.729  121.256 90.179  1.00 68.46  ? 2010 THR A C     1 
ATOM   1183 O  O     . THR A 1 219 ? 88.342  122.420 90.026  1.00 74.08  ? 2010 THR A O     1 
ATOM   1184 C  CB    . THR A 1 219 ? 87.052  119.475 90.732  1.00 68.73  ? 2010 THR A CB    1 
ATOM   1185 O  OG1   . THR A 1 219 ? 86.297  118.383 90.196  1.00 71.79  ? 2010 THR A OG1   1 
ATOM   1186 C  CG2   . THR A 1 219 ? 86.095  120.508 91.306  1.00 69.97  ? 2010 THR A CG2   1 
ATOM   1187 N  N     . SER A 1 220 ? 89.863  120.966 90.817  1.00 67.87  ? 2011 SER A N     1 
ATOM   1188 C  CA    . SER A 1 220 ? 90.631  121.997 91.500  1.00 68.18  ? 2011 SER A CA    1 
ATOM   1189 C  C     . SER A 1 220 ? 91.629  122.721 90.604  1.00 66.05  ? 2011 SER A C     1 
ATOM   1190 O  O     . SER A 1 220 ? 92.155  123.761 91.013  1.00 62.49  ? 2011 SER A O     1 
ATOM   1191 C  CB    . SER A 1 220 ? 91.375  121.391 92.694  1.00 68.33  ? 2011 SER A CB    1 
ATOM   1192 O  OG    . SER A 1 220 ? 90.612  121.509 93.882  1.00 85.69  ? 2011 SER A OG    1 
ATOM   1193 N  N     . PHE A 1 221 ? 91.903  122.214 89.400  1.00 63.57  ? 2012 PHE A N     1 
ATOM   1194 C  CA    . PHE A 1 221 ? 92.918  122.812 88.545  1.00 60.24  ? 2012 PHE A CA    1 
ATOM   1195 C  C     . PHE A 1 221 ? 92.497  122.957 87.090  1.00 67.79  ? 2012 PHE A C     1 
ATOM   1196 O  O     . PHE A 1 221 ? 93.286  123.467 86.288  1.00 69.03  ? 2012 PHE A O     1 
ATOM   1197 C  CB    . PHE A 1 221 ? 94.217  121.993 88.612  1.00 55.41  ? 2012 PHE A CB    1 
ATOM   1198 C  CG    . PHE A 1 221 ? 94.820  121.931 89.985  1.00 60.80  ? 2012 PHE A CG    1 
ATOM   1199 C  CD1   . PHE A 1 221 ? 95.222  123.087 90.633  1.00 59.59  ? 2012 PHE A CD1   1 
ATOM   1200 C  CD2   . PHE A 1 221 ? 94.974  120.718 90.634  1.00 63.67  ? 2012 PHE A CD2   1 
ATOM   1201 C  CE1   . PHE A 1 221 ? 95.772  123.033 91.898  1.00 57.99  ? 2012 PHE A CE1   1 
ATOM   1202 C  CE2   . PHE A 1 221 ? 95.522  120.658 91.900  1.00 60.74  ? 2012 PHE A CE2   1 
ATOM   1203 C  CZ    . PHE A 1 221 ? 95.923  121.818 92.532  1.00 57.73  ? 2012 PHE A CZ    1 
ATOM   1204 N  N     . LEU A 1 222 ? 91.291  122.529 86.725  1.00 70.25  ? 2013 LEU A N     1 
ATOM   1205 C  CA    . LEU A 1 222 ? 90.823  122.646 85.350  1.00 72.39  ? 2013 LEU A CA    1 
ATOM   1206 C  C     . LEU A 1 222 ? 89.303  122.552 85.300  1.00 76.64  ? 2013 LEU A C     1 
ATOM   1207 O  O     . LEU A 1 222 ? 88.759  121.564 84.791  1.00 77.56  ? 2013 LEU A O     1 
ATOM   1208 C  CB    . LEU A 1 222 ? 91.452  121.558 84.480  1.00 66.40  ? 2013 LEU A CB    1 
ATOM   1209 C  CG    . LEU A 1 222 ? 91.471  121.819 82.976  1.00 67.53  ? 2013 LEU A CG    1 
ATOM   1210 C  CD1   . LEU A 1 222 ? 92.579  122.794 82.621  1.00 63.74  ? 2013 LEU A CD1   1 
ATOM   1211 C  CD2   . LEU A 1 222 ? 91.638  120.514 82.227  1.00 67.51  ? 2013 LEU A CD2   1 
ATOM   1212 N  N     . PRO A 1 223 ? 88.581  123.551 85.816  1.00 79.21  ? 2014 PRO A N     1 
ATOM   1213 C  CA    . PRO A 1 223 ? 87.116  123.429 85.865  1.00 81.58  ? 2014 PRO A CA    1 
ATOM   1214 C  C     . PRO A 1 223 ? 86.448  123.581 84.511  1.00 79.79  ? 2014 PRO A C     1 
ATOM   1215 O  O     . PRO A 1 223 ? 85.430  122.923 84.263  1.00 79.57  ? 2014 PRO A O     1 
ATOM   1216 C  CB    . PRO A 1 223 ? 86.698  124.555 86.827  1.00 81.76  ? 2014 PRO A CB    1 
ATOM   1217 C  CG    . PRO A 1 223 ? 87.983  125.085 87.427  1.00 77.42  ? 2014 PRO A CG    1 
ATOM   1218 C  CD    . PRO A 1 223 ? 89.045  124.808 86.419  1.00 73.95  ? 2014 PRO A CD    1 
ATOM   1219 N  N     . HIS A 1 224 ? 86.994  124.417 83.623  1.00 78.43  ? 2015 HIS A N     1 
ATOM   1220 C  CA    . HIS A 1 224 ? 86.324  124.696 82.356  1.00 82.49  ? 2015 HIS A CA    1 
ATOM   1221 C  C     . HIS A 1 224 ? 86.192  123.438 81.508  1.00 83.09  ? 2015 HIS A C     1 
ATOM   1222 O  O     . HIS A 1 224 ? 85.163  123.225 80.856  1.00 84.18  ? 2015 HIS A O     1 
ATOM   1223 C  CB    . HIS A 1 224 ? 87.078  125.787 81.593  1.00 83.63  ? 2015 HIS A CB    1 
ATOM   1224 C  CG    . HIS A 1 224 ? 88.460  125.391 81.176  1.00 84.00  ? 2015 HIS A CG    1 
ATOM   1225 N  ND1   . HIS A 1 224 ? 88.715  124.686 80.020  1.00 79.93  ? 2015 HIS A ND1   1 
ATOM   1226 C  CD2   . HIS A 1 224 ? 89.662  125.604 81.760  1.00 84.44  ? 2015 HIS A CD2   1 
ATOM   1227 C  CE1   . HIS A 1 224 ? 90.015  124.480 79.910  1.00 79.83  ? 2015 HIS A CE1   1 
ATOM   1228 N  NE2   . HIS A 1 224 ? 90.613  125.028 80.953  1.00 84.31  ? 2015 HIS A NE2   1 
ATOM   1229 N  N     . GLU A 1 225 ? 87.219  122.596 81.502  1.00 81.82  ? 2016 GLU A N     1 
ATOM   1230 C  CA    . GLU A 1 225 ? 87.191  121.333 80.779  1.00 82.53  ? 2016 GLU A CA    1 
ATOM   1231 C  C     . GLU A 1 225 ? 86.589  120.212 81.624  1.00 83.51  ? 2016 GLU A C     1 
ATOM   1232 O  O     . GLU A 1 225 ? 86.358  119.111 81.112  1.00 83.25  ? 2016 GLU A O     1 
ATOM   1233 C  CB    . GLU A 1 225 ? 88.619  121.003 80.303  1.00 79.98  ? 2016 GLU A CB    1 
ATOM   1234 C  CG    . GLU A 1 225 ? 88.918  119.574 79.881  1.00 77.38  ? 2016 GLU A CG    1 
ATOM   1235 C  CD    . GLU A 1 225 ? 88.571  119.301 78.431  1.00 79.62  ? 2016 GLU A CD    1 
ATOM   1236 O  OE1   . GLU A 1 225 ? 89.109  118.329 77.862  1.00 74.99  ? 2016 GLU A OE1   1 
ATOM   1237 O  OE2   . GLU A 1 225 ? 87.760  120.057 77.858  1.00 83.23  ? 2016 GLU A OE2   1 
ATOM   1238 N  N     . LEU A 1 226 ? 86.266  120.497 82.884  1.00 81.64  ? 2017 LEU A N     1 
ATOM   1239 C  CA    . LEU A 1 226 ? 85.657  119.503 83.767  1.00 85.34  ? 2017 LEU A CA    1 
ATOM   1240 C  C     . LEU A 1 226 ? 84.408  118.836 83.190  1.00 88.67  ? 2017 LEU A C     1 
ATOM   1241 O  O     . LEU A 1 226 ? 84.266  117.614 83.368  1.00 83.51  ? 2017 LEU A O     1 
ATOM   1242 C  CB    . LEU A 1 226 ? 85.348  120.163 85.121  1.00 88.62  ? 2017 LEU A CB    1 
ATOM   1243 C  CG    . LEU A 1 226 ? 84.352  119.543 86.110  1.00 93.06  ? 2017 LEU A CG    1 
ATOM   1244 C  CD1   . LEU A 1 226 ? 84.677  118.087 86.426  1.00 84.16  ? 2017 LEU A CD1   1 
ATOM   1245 C  CD2   . LEU A 1 226 ? 84.290  120.369 87.386  1.00 89.17  ? 2017 LEU A CD2   1 
ATOM   1246 N  N     . PRO A 1 227 ? 83.480  119.536 82.521  1.00 94.34  ? 2018 PRO A N     1 
ATOM   1247 C  CA    . PRO A 1 227 ? 82.304  118.843 81.961  1.00 94.35  ? 2018 PRO A CA    1 
ATOM   1248 C  C     . PRO A 1 227 ? 82.630  117.722 80.981  1.00 91.41  ? 2018 PRO A C     1 
ATOM   1249 O  O     . PRO A 1 227 ? 81.711  116.991 80.591  1.00 91.85  ? 2018 PRO A O     1 
ATOM   1250 C  CB    . PRO A 1 227 ? 81.530  119.970 81.268  1.00 90.22  ? 2018 PRO A CB    1 
ATOM   1251 C  CG    . PRO A 1 227 ? 81.898  121.183 82.026  1.00 87.07  ? 2018 PRO A CG    1 
ATOM   1252 C  CD    . PRO A 1 227 ? 83.339  121.000 82.404  1.00 87.55  ? 2018 PRO A CD    1 
ATOM   1253 N  N     . LEU A 1 228 ? 83.889  117.563 80.566  1.00 86.87  ? 2019 LEU A N     1 
ATOM   1254 C  CA    . LEU A 1 228 ? 84.255  116.426 79.729  1.00 82.32  ? 2019 LEU A CA    1 
ATOM   1255 C  C     . LEU A 1 228 ? 84.105  115.100 80.463  1.00 85.58  ? 2019 LEU A C     1 
ATOM   1256 O  O     . LEU A 1 228 ? 84.069  114.047 79.817  1.00 83.70  ? 2019 LEU A O     1 
ATOM   1257 C  CB    . LEU A 1 228 ? 85.691  116.578 79.227  1.00 77.29  ? 2019 LEU A CB    1 
ATOM   1258 C  CG    . LEU A 1 228 ? 85.859  116.942 77.752  1.00 80.41  ? 2019 LEU A CG    1 
ATOM   1259 C  CD1   . LEU A 1 228 ? 85.547  115.744 76.871  1.00 77.56  ? 2019 LEU A CD1   1 
ATOM   1260 C  CD2   . LEU A 1 228 ? 84.976  118.125 77.388  1.00 82.25  ? 2019 LEU A CD2   1 
ATOM   1261 N  N     . LEU A 1 229 ? 84.020  115.127 81.793  1.00 87.27  ? 2020 LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 229 ? 83.857  113.927 82.605  1.00 89.78  ? 2020 LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 229 ? 82.400  113.679 82.983  1.00 92.89  ? 2020 LEU A C     1 
ATOM   1264 O  O     . LEU A 1 229 ? 82.125  113.041 84.005  1.00 88.53  ? 2020 LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 229 ? 84.720  114.019 83.863  1.00 85.57  ? 2020 LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 229 ? 86.237  114.023 83.669  1.00 75.29  ? 2020 LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 229 ? 86.931  114.510 84.928  1.00 71.01  ? 2020 LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 229 ? 86.732  112.641 83.285  1.00 67.85  ? 2020 LEU A CD2   1 
ATOM   1269 N  N     . GLU A 1 230 ? 81.460  114.180 82.185  1.00 97.11  ? 2021 GLU A N     1 
ATOM   1270 C  CA    . GLU A 1 230 ? 80.048  113.981 82.480  1.00 94.30  ? 2021 GLU A CA    1 
ATOM   1271 C  C     . GLU A 1 230 ? 79.676  112.511 82.336  1.00 96.29  ? 2021 GLU A C     1 
ATOM   1272 O  O     . GLU A 1 230 ? 80.040  111.852 81.358  1.00 95.15  ? 2021 GLU A O     1 
ATOM   1273 C  CB    . GLU A 1 230 ? 79.183  114.843 81.560  1.00 93.89  ? 2021 GLU A CB    1 
ATOM   1274 C  CG    . GLU A 1 230 ? 79.480  114.677 80.077  1.00 96.07  ? 2021 GLU A CG    1 
ATOM   1275 C  CD    . GLU A 1 230 ? 78.968  115.839 79.247  1.00 100.68 ? 2021 GLU A CD    1 
ATOM   1276 O  OE1   . GLU A 1 230 ? 78.251  116.698 79.801  1.00 102.33 ? 2021 GLU A OE1   1 
ATOM   1277 O  OE2   . GLU A 1 230 ? 79.285  115.894 78.040  1.00 99.63  ? 2021 GLU A OE2   1 
ATOM   1278 N  N     . GLY A 1 231 ? 78.949  111.997 83.326  1.00 100.26 ? 2022 GLY A N     1 
ATOM   1279 C  CA    . GLY A 1 231 ? 78.585  110.591 83.328  1.00 102.80 ? 2022 GLY A CA    1 
ATOM   1280 C  C     . GLY A 1 231 ? 79.773  109.657 83.359  1.00 102.57 ? 2022 GLY A C     1 
ATOM   1281 O  O     . GLY A 1 231 ? 79.734  108.591 82.735  1.00 99.76  ? 2022 GLY A O     1 
ATOM   1282 N  N     . MET A 1 232 ? 80.833  110.030 84.070  1.00 104.72 ? 2023 MET A N     1 
ATOM   1283 C  CA    . MET A 1 232 ? 82.077  109.266 84.115  1.00 105.76 ? 2023 MET A CA    1 
ATOM   1284 C  C     . MET A 1 232 ? 82.364  108.940 85.578  1.00 105.90 ? 2023 MET A C     1 
ATOM   1285 O  O     . MET A 1 232 ? 83.075  109.678 86.263  1.00 106.95 ? 2023 MET A O     1 
ATOM   1286 C  CB    . MET A 1 232 ? 83.216  110.054 83.476  1.00 101.97 ? 2023 MET A CB    1 
ATOM   1287 C  CG    . MET A 1 232 ? 84.139  109.230 82.600  1.00 98.55  ? 2023 MET A CG    1 
ATOM   1288 S  SD    . MET A 1 232 ? 84.780  110.211 81.231  1.00 110.01 ? 2023 MET A SD    1 
ATOM   1289 C  CE    . MET A 1 232 ? 85.581  108.948 80.251  1.00 81.12  ? 2023 MET A CE    1 
ATOM   1290 N  N     . GLU A 1 233 ? 81.808  107.826 86.053  1.00 107.19 ? 2024 GLU A N     1 
ATOM   1291 C  CA    . GLU A 1 233 ? 81.983  107.421 87.441  1.00 104.68 ? 2024 GLU A CA    1 
ATOM   1292 C  C     . GLU A 1 233 ? 83.332  106.766 87.704  1.00 100.13 ? 2024 GLU A C     1 
ATOM   1293 O  O     . GLU A 1 233 ? 83.679  106.550 88.870  1.00 93.07  ? 2024 GLU A O     1 
ATOM   1294 C  CB    . GLU A 1 233 ? 80.861  106.465 87.856  1.00 103.32 ? 2024 GLU A CB    1 
ATOM   1295 C  CG    . GLU A 1 233 ? 80.503  105.428 86.803  1.00 109.05 ? 2024 GLU A CG    1 
ATOM   1296 C  CD    . GLU A 1 233 ? 79.360  105.873 85.911  1.00 112.64 ? 2024 GLU A CD    1 
ATOM   1297 O  OE1   . GLU A 1 233 ? 78.879  107.013 86.082  1.00 111.18 ? 2024 GLU A OE1   1 
ATOM   1298 O  OE2   . GLU A 1 233 ? 78.943  105.083 85.037  1.00 110.29 ? 2024 GLU A OE2   1 
ATOM   1299 N  N     . THR A 1 234 ? 84.095  106.444 86.659  1.00 100.41 ? 2025 THR A N     1 
ATOM   1300 C  CA    . THR A 1 234 ? 85.406  105.833 86.832  1.00 96.94  ? 2025 THR A CA    1 
ATOM   1301 C  C     . THR A 1 234 ? 86.496  106.847 87.155  1.00 91.61  ? 2025 THR A C     1 
ATOM   1302 O  O     . THR A 1 234 ? 87.584  106.445 87.582  1.00 84.23  ? 2025 THR A O     1 
ATOM   1303 C  CB    . THR A 1 234 ? 85.795  105.054 85.574  1.00 93.12  ? 2025 THR A CB    1 
ATOM   1304 N  N     . SER A 1 235 ? 86.235  108.142 86.963  1.00 91.30  ? 2026 SER A N     1 
ATOM   1305 C  CA    . SER A 1 235 ? 87.245  109.155 87.240  1.00 81.43  ? 2026 SER A CA    1 
ATOM   1306 C  C     . SER A 1 235 ? 87.461  109.369 88.731  1.00 78.51  ? 2026 SER A C     1 
ATOM   1307 O  O     . SER A 1 235 ? 88.457  109.991 89.115  1.00 71.06  ? 2026 SER A O     1 
ATOM   1308 C  CB    . SER A 1 235 ? 86.858  110.478 86.578  1.00 77.08  ? 2026 SER A CB    1 
ATOM   1309 N  N     . GLN A 1 236 ? 86.558  108.876 89.577  1.00 80.09  ? 2027 GLN A N     1 
ATOM   1310 C  CA    . GLN A 1 236 ? 86.685  109.034 91.019  1.00 76.11  ? 2027 GLN A CA    1 
ATOM   1311 C  C     . GLN A 1 236 ? 87.547  107.958 91.667  1.00 75.29  ? 2027 GLN A C     1 
ATOM   1312 O  O     . GLN A 1 236 ? 87.846  108.064 92.861  1.00 68.59  ? 2027 GLN A O     1 
ATOM   1313 C  CB    . GLN A 1 236 ? 85.299  109.037 91.673  1.00 70.54  ? 2027 GLN A CB    1 
ATOM   1314 N  N     . GLY A 1 237 ? 87.952  106.934 90.919  1.00 78.46  ? 2028 GLY A N     1 
ATOM   1315 C  CA    . GLY A 1 237 ? 88.785  105.896 91.485  1.00 78.86  ? 2028 GLY A CA    1 
ATOM   1316 C  C     . GLY A 1 237 ? 90.214  106.354 91.705  1.00 86.45  ? 2028 GLY A C     1 
ATOM   1317 O  O     . GLY A 1 237 ? 90.679  107.346 91.144  1.00 87.74  ? 2028 GLY A O     1 
ATOM   1318 N  N     . ILE A 1 238 ? 90.925  105.601 92.548  1.00 89.11  ? 2029 ILE A N     1 
ATOM   1319 C  CA    . ILE A 1 238 ? 92.311  105.940 92.860  1.00 87.51  ? 2029 ILE A CA    1 
ATOM   1320 C  C     . ILE A 1 238 ? 93.178  105.850 91.612  1.00 83.19  ? 2029 ILE A C     1 
ATOM   1321 O  O     . ILE A 1 238 ? 94.022  106.718 91.359  1.00 76.27  ? 2029 ILE A O     1 
ATOM   1322 C  CB    . ILE A 1 238 ? 92.845  105.035 93.985  1.00 90.50  ? 2029 ILE A CB    1 
ATOM   1323 C  CG1   . ILE A 1 238 ? 91.773  104.821 95.055  1.00 94.28  ? 2029 ILE A CG1   1 
ATOM   1324 C  CG2   . ILE A 1 238 ? 94.102  105.633 94.596  1.00 77.19  ? 2029 ILE A CG2   1 
ATOM   1325 C  CD1   . ILE A 1 238 ? 92.149  103.790 96.098  1.00 86.09  ? 2029 ILE A CD1   1 
ATOM   1326 N  N     . GLN A 1 239 ? 92.987  104.802 90.815  1.00 84.19  ? 2030 GLN A N     1 
ATOM   1327 C  CA    . GLN A 1 239 ? 93.769  104.620 89.603  1.00 81.82  ? 2030 GLN A CA    1 
ATOM   1328 C  C     . GLN A 1 239 ? 93.357  105.647 88.549  1.00 78.96  ? 2030 GLN A C     1 
ATOM   1329 O  O     . GLN A 1 239 ? 92.397  106.405 88.714  1.00 67.86  ? 2030 GLN A O     1 
ATOM   1330 C  CB    . GLN A 1 239 ? 93.603  103.198 89.073  1.00 76.47  ? 2030 GLN A CB    1 
ATOM   1331 C  CG    . GLN A 1 239 ? 93.175  102.190 90.124  1.00 73.29  ? 2030 GLN A CG    1 
ATOM   1332 C  CD    . GLN A 1 239 ? 92.737  100.872 89.518  1.00 78.27  ? 2030 GLN A CD    1 
ATOM   1333 O  OE1   . GLN A 1 239 ? 93.402  100.330 88.635  1.00 77.05  ? 2030 GLN A OE1   1 
ATOM   1334 N  NE2   . GLN A 1 239 ? 91.612  100.349 89.991  1.00 86.23  ? 2030 GLN A NE2   1 
ATOM   1335 N  N     . SER A 1 240 ? 94.101  105.670 87.447  1.00 78.42  ? 2031 SER A N     1 
ATOM   1336 C  CA    . SER A 1 240 ? 93.808  106.607 86.375  1.00 72.37  ? 2031 SER A CA    1 
ATOM   1337 C  C     . SER A 1 240 ? 92.541  106.196 85.633  1.00 72.12  ? 2031 SER A C     1 
ATOM   1338 O  O     . SER A 1 240 ? 92.028  105.083 85.782  1.00 73.04  ? 2031 SER A O     1 
ATOM   1339 C  CB    . SER A 1 240 ? 94.978  106.695 85.396  1.00 65.74  ? 2031 SER A CB    1 
ATOM   1340 O  OG    . SER A 1 240 ? 95.488  105.413 85.087  1.00 60.68  ? 2031 SER A OG    1 
ATOM   1341 N  N     . LEU A 1 241 ? 92.033  107.126 84.824  1.00 71.70  ? 2032 LEU A N     1 
ATOM   1342 C  CA    . LEU A 1 241 ? 90.822  106.863 84.056  1.00 66.79  ? 2032 LEU A CA    1 
ATOM   1343 C  C     . LEU A 1 241 ? 91.039  105.741 83.049  1.00 64.18  ? 2032 LEU A C     1 
ATOM   1344 O  O     . LEU A 1 241 ? 90.152  104.906 82.838  1.00 70.87  ? 2032 LEU A O     1 
ATOM   1345 C  CB    . LEU A 1 241 ? 90.369  108.140 83.353  1.00 62.06  ? 2032 LEU A CB    1 
ATOM   1346 C  CG    . LEU A 1 241 ? 88.929  108.190 82.851  1.00 69.19  ? 2032 LEU A CG    1 
ATOM   1347 C  CD1   . LEU A 1 241 ? 87.973  107.705 83.924  1.00 76.02  ? 2032 LEU A CD1   1 
ATOM   1348 C  CD2   . LEU A 1 241 ? 88.578  109.599 82.413  1.00 70.79  ? 2032 LEU A CD2   1 
ATOM   1349 N  N     . GLY A 1 242 ? 92.208  105.704 82.419  1.00 58.97  ? 2033 GLY A N     1 
ATOM   1350 C  CA    . GLY A 1 242 ? 92.512  104.685 81.438  1.00 62.13  ? 2033 GLY A CA    1 
ATOM   1351 C  C     . GLY A 1 242 ? 92.984  103.361 81.988  1.00 63.72  ? 2033 GLY A C     1 
ATOM   1352 O  O     . GLY A 1 242 ? 93.246  102.440 81.211  1.00 63.84  ? 2033 GLY A O     1 
ATOM   1353 N  N     . LEU A 1 243 ? 93.102  103.230 83.308  1.00 67.69  ? 2034 LEU A N     1 
ATOM   1354 C  CA    . LEU A 1 243 ? 93.569  101.999 83.935  1.00 76.72  ? 2034 LEU A CA    1 
ATOM   1355 C  C     . LEU A 1 243 ? 92.442  101.122 84.461  1.00 79.64  ? 2034 LEU A C     1 
ATOM   1356 O  O     . LEU A 1 243 ? 92.522  99.895  84.354  1.00 80.67  ? 2034 LEU A O     1 
ATOM   1357 C  CB    . LEU A 1 243 ? 94.531  102.321 85.082  1.00 78.15  ? 2034 LEU A CB    1 
ATOM   1358 C  CG    . LEU A 1 243 ? 96.019  102.313 84.737  1.00 66.73  ? 2034 LEU A CG    1 
ATOM   1359 C  CD1   . LEU A 1 243 ? 96.848  102.631 85.967  1.00 63.17  ? 2034 LEU A CD1   1 
ATOM   1360 C  CD2   . LEU A 1 243 ? 96.397  100.959 84.179  1.00 62.04  ? 2034 LEU A CD2   1 
ATOM   1361 N  N     . ASN A 1 244 ? 91.400  101.717 85.033  1.00 80.18  ? 2035 ASN A N     1 
ATOM   1362 C  CA    . ASN A 1 244 ? 90.329  100.932 85.627  1.00 85.78  ? 2035 ASN A CA    1 
ATOM   1363 C  C     . ASN A 1 244 ? 89.547  100.176 84.557  1.00 92.83  ? 2035 ASN A C     1 
ATOM   1364 O  O     . ASN A 1 244 ? 89.443  100.606 83.406  1.00 85.89  ? 2035 ASN A O     1 
ATOM   1365 C  CB    . ASN A 1 244 ? 89.388  101.830 86.431  1.00 88.72  ? 2035 ASN A CB    1 
ATOM   1366 C  CG    . ASN A 1 244 ? 88.580  102.764 85.554  1.00 92.51  ? 2035 ASN A CG    1 
ATOM   1367 O  OD1   . ASN A 1 244 ? 87.545  102.383 85.006  1.00 92.62  ? 2035 ASN A OD1   1 
ATOM   1368 N  ND2   . ASN A 1 244 ? 89.046  103.999 85.420  1.00 89.62  ? 2035 ASN A ND2   1 
ATOM   1369 N  N     . ALA A 1 245 ? 88.996  99.032  84.957  1.00 96.47  ? 2036 ALA A N     1 
ATOM   1370 C  CA    . ALA A 1 245 ? 88.178  98.183  84.094  1.00 93.52  ? 2036 ALA A CA    1 
ATOM   1371 C  C     . ALA A 1 245 ? 86.693  98.403  84.345  1.00 94.99  ? 2036 ALA A C     1 
ATOM   1372 O  O     . ALA A 1 245 ? 85.898  97.459  84.327  1.00 98.45  ? 2036 ALA A O     1 
ATOM   1373 C  CB    . ALA A 1 245 ? 88.548  96.717  84.292  1.00 96.93  ? 2036 ALA A CB    1 
ATOM   1374 N  N     . GLY A 1 246 ? 86.298  99.651  84.583  1.00 93.81  ? 2037 GLY A N     1 
ATOM   1375 C  CA    . GLY A 1 246 ? 84.964  99.963  85.054  1.00 89.45  ? 2037 GLY A CA    1 
ATOM   1376 C  C     . GLY A 1 246 ? 83.997  100.444 83.993  1.00 94.01  ? 2037 GLY A C     1 
ATOM   1377 O  O     . GLY A 1 246 ? 83.390  99.633  83.287  1.00 98.90  ? 2037 GLY A O     1 
ATOM   1378 N  N     . SER A 1 247 ? 83.841  101.765 83.887  1.00 97.55  ? 2038 SER A N     1 
ATOM   1379 C  CA    . SER A 1 247 ? 82.771  102.397 83.121  1.00 107.91 ? 2038 SER A CA    1 
ATOM   1380 C  C     . SER A 1 247 ? 82.656  101.888 81.688  1.00 107.77 ? 2038 SER A C     1 
ATOM   1381 O  O     . SER A 1 247 ? 83.624  101.379 81.113  1.00 100.03 ? 2038 SER A O     1 
ATOM   1382 C  CB    . SER A 1 247 ? 82.967  103.915 83.111  1.00 107.97 ? 2038 SER A CB    1 
ATOM   1383 O  OG    . SER A 1 247 ? 82.762  104.463 84.401  1.00 102.07 ? 2038 SER A OG    1 
ATOM   1384 N  N     . GLU A 1 248 ? 81.463  102.041 81.107  1.00 109.44 ? 2039 GLU A N     1 
ATOM   1385 C  CA    . GLU A 1 248 ? 81.164  101.494 79.789  1.00 110.18 ? 2039 GLU A CA    1 
ATOM   1386 C  C     . GLU A 1 248 ? 81.949  102.175 78.674  1.00 109.08 ? 2039 GLU A C     1 
ATOM   1387 O  O     . GLU A 1 248 ? 82.010  101.638 77.563  1.00 112.11 ? 2039 GLU A O     1 
ATOM   1388 C  CB    . GLU A 1 248 ? 79.660  101.607 79.519  1.00 112.50 ? 2039 GLU A CB    1 
ATOM   1389 C  CG    . GLU A 1 248 ? 79.148  100.761 78.362  1.00 120.10 ? 2039 GLU A CG    1 
ATOM   1390 C  CD    . GLU A 1 248 ? 78.921  101.574 77.103  1.00 118.42 ? 2039 GLU A CD    1 
ATOM   1391 O  OE1   . GLU A 1 248 ? 78.908  102.820 77.192  1.00 111.31 ? 2039 GLU A OE1   1 
ATOM   1392 O  OE2   . GLU A 1 248 ? 78.754  100.969 76.023  1.00 120.79 ? 2039 GLU A OE2   1 
ATOM   1393 N  N     . HIS A 1 249 ? 82.551  103.333 78.941  1.00 104.30 ? 2040 HIS A N     1 
ATOM   1394 C  CA    . HIS A 1 249 ? 83.288  104.044 77.905  1.00 96.43  ? 2040 HIS A CA    1 
ATOM   1395 C  C     . HIS A 1 249 ? 84.448  103.199 77.393  1.00 94.20  ? 2040 HIS A C     1 
ATOM   1396 O  O     . HIS A 1 249 ? 85.095  102.473 78.153  1.00 89.98  ? 2040 HIS A O     1 
ATOM   1397 C  CB    . HIS A 1 249 ? 83.804  105.379 78.441  1.00 94.07  ? 2040 HIS A CB    1 
ATOM   1398 C  CG    . HIS A 1 249 ? 82.771  106.173 79.178  1.00 97.75  ? 2040 HIS A CG    1 
ATOM   1399 N  ND1   . HIS A 1 249 ? 82.537  106.021 80.527  1.00 100.29 ? 2040 HIS A ND1   1 
ATOM   1400 C  CD2   . HIS A 1 249 ? 81.911  107.129 78.752  1.00 92.87  ? 2040 HIS A CD2   1 
ATOM   1401 C  CE1   . HIS A 1 249 ? 81.577  106.848 80.901  1.00 98.16  ? 2040 HIS A CE1   1 
ATOM   1402 N  NE2   . HIS A 1 249 ? 81.180  107.531 79.843  1.00 95.83  ? 2040 HIS A NE2   1 
ATOM   1403 N  N     . SER A 1 250 ? 84.700  103.292 76.090  1.00 89.99  ? 2041 SER A N     1 
ATOM   1404 C  CA    . SER A 1 250 ? 85.751  102.511 75.460  1.00 87.39  ? 2041 SER A CA    1 
ATOM   1405 C  C     . SER A 1 250 ? 87.122  102.939 75.973  1.00 90.29  ? 2041 SER A C     1 
ATOM   1406 O  O     . SER A 1 250 ? 87.321  104.066 76.435  1.00 89.21  ? 2041 SER A O     1 
ATOM   1407 C  CB    . SER A 1 250 ? 85.689  102.659 73.939  1.00 81.14  ? 2041 SER A CB    1 
ATOM   1408 O  OG    . SER A 1 250 ? 86.730  101.932 73.311  1.00 76.57  ? 2041 SER A OG    1 
ATOM   1409 N  N     . GLY A 1 251 ? 88.077  102.011 75.891  1.00 90.91  ? 2042 GLY A N     1 
ATOM   1410 C  CA    . GLY A 1 251 ? 89.419  102.298 76.369  1.00 79.63  ? 2042 GLY A CA    1 
ATOM   1411 C  C     . GLY A 1 251 ? 90.076  103.448 75.629  1.00 74.43  ? 2042 GLY A C     1 
ATOM   1412 O  O     . GLY A 1 251 ? 90.743  104.288 76.237  1.00 72.02  ? 2042 GLY A O     1 
ATOM   1413 N  N     . ARG A 1 252 ? 89.894  103.503 74.308  1.00 72.56  ? 2043 ARG A N     1 
ATOM   1414 C  CA    . ARG A 1 252 ? 90.522  104.554 73.514  1.00 68.24  ? 2043 ARG A CA    1 
ATOM   1415 C  C     . ARG A 1 252 ? 89.993  105.930 73.900  1.00 68.12  ? 2043 ARG A C     1 
ATOM   1416 O  O     . ARG A 1 252 ? 90.770  106.855 74.163  1.00 71.86  ? 2043 ARG A O     1 
ATOM   1417 C  CB    . ARG A 1 252 ? 90.295  104.286 72.026  1.00 68.09  ? 2043 ARG A CB    1 
ATOM   1418 C  CG    . ARG A 1 252 ? 90.395  105.520 71.146  1.00 69.27  ? 2043 ARG A CG    1 
ATOM   1419 C  CD    . ARG A 1 252 ? 89.912  105.233 69.734  1.00 71.98  ? 2043 ARG A CD    1 
ATOM   1420 N  NE    . ARG A 1 252 ? 89.378  106.427 69.091  1.00 66.15  ? 2043 ARG A NE    1 
ATOM   1421 C  CZ    . ARG A 1 252 ? 88.159  106.907 69.298  1.00 68.49  ? 2043 ARG A CZ    1 
ATOM   1422 N  NH1   . ARG A 1 252 ? 87.315  106.315 70.127  1.00 71.81  ? 2043 ARG A NH1   1 
ATOM   1423 N  NH2   . ARG A 1 252 ? 87.778  108.007 68.656  1.00 70.02  ? 2043 ARG A NH2   1 
ATOM   1424 N  N     . TYR A 1 253 ? 88.668  106.082 73.943  1.00 66.29  ? 2044 TYR A N     1 
ATOM   1425 C  CA    . TYR A 1 253 ? 88.076  107.372 74.287  1.00 67.97  ? 2044 TYR A CA    1 
ATOM   1426 C  C     . TYR A 1 253 ? 88.409  107.771 75.719  1.00 72.31  ? 2044 TYR A C     1 
ATOM   1427 O  O     . TYR A 1 253 ? 88.718  108.940 75.990  1.00 74.12  ? 2044 TYR A O     1 
ATOM   1428 C  CB    . TYR A 1 253 ? 86.563  107.321 74.080  1.00 71.43  ? 2044 TYR A CB    1 
ATOM   1429 C  CG    . TYR A 1 253 ? 85.795  108.365 74.857  1.00 68.27  ? 2044 TYR A CG    1 
ATOM   1430 C  CD1   . TYR A 1 253 ? 85.787  109.692 74.453  1.00 64.32  ? 2044 TYR A CD1   1 
ATOM   1431 C  CD2   . TYR A 1 253 ? 85.070  108.021 75.989  1.00 71.48  ? 2044 TYR A CD2   1 
ATOM   1432 C  CE1   . TYR A 1 253 ? 85.084  110.647 75.158  1.00 69.80  ? 2044 TYR A CE1   1 
ATOM   1433 C  CE2   . TYR A 1 253 ? 84.365  108.969 76.701  1.00 74.34  ? 2044 TYR A CE2   1 
ATOM   1434 C  CZ    . TYR A 1 253 ? 84.375  110.281 76.281  1.00 73.55  ? 2044 TYR A CZ    1 
ATOM   1435 O  OH    . TYR A 1 253 ? 83.673  111.232 76.986  1.00 72.59  ? 2044 TYR A OH    1 
ATOM   1436 N  N     . ARG A 1 254 ? 88.340  106.815 76.648  1.00 73.76  ? 2045 ARG A N     1 
ATOM   1437 C  CA    . ARG A 1 254 ? 88.662  107.100 78.041  1.00 72.40  ? 2045 ARG A CA    1 
ATOM   1438 C  C     . ARG A 1 254 ? 90.104  107.568 78.179  1.00 67.88  ? 2045 ARG A C     1 
ATOM   1439 O  O     . ARG A 1 254 ? 90.385  108.578 78.837  1.00 65.44  ? 2045 ARG A O     1 
ATOM   1440 C  CB    . ARG A 1 254 ? 88.414  105.853 78.891  1.00 72.20  ? 2045 ARG A CB    1 
ATOM   1441 C  CG    . ARG A 1 254 ? 87.735  106.120 80.220  1.00 76.40  ? 2045 ARG A CG    1 
ATOM   1442 C  CD    . ARG A 1 254 ? 87.066  104.873 80.783  1.00 81.21  ? 2045 ARG A CD    1 
ATOM   1443 N  NE    . ARG A 1 254 ? 88.031  103.848 81.162  1.00 79.01  ? 2045 ARG A NE    1 
ATOM   1444 C  CZ    . ARG A 1 254 ? 88.376  102.821 80.397  1.00 75.92  ? 2045 ARG A CZ    1 
ATOM   1445 N  NH1   . ARG A 1 254 ? 87.837  102.636 79.204  1.00 76.11  ? 2045 ARG A NH1   1 
ATOM   1446 N  NH2   . ARG A 1 254 ? 89.282  101.956 80.843  1.00 75.13  ? 2045 ARG A NH2   1 
ATOM   1447 N  N     . ALA A 1 255 ? 91.033  106.853 77.541  1.00 66.97  ? 2046 ALA A N     1 
ATOM   1448 C  CA    . ALA A 1 255 ? 92.436  107.237 77.602  1.00 62.83  ? 2046 ALA A CA    1 
ATOM   1449 C  C     . ALA A 1 255 ? 92.662  108.602 76.969  1.00 61.16  ? 2046 ALA A C     1 
ATOM   1450 O  O     . ALA A 1 255 ? 93.434  109.410 77.491  1.00 60.83  ? 2046 ALA A O     1 
ATOM   1451 C  CB    . ALA A 1 255 ? 93.301  106.179 76.920  1.00 63.85  ? 2046 ALA A CB    1 
ATOM   1452 N  N     . SER A 1 256 ? 91.998  108.880 75.845  1.00 60.20  ? 2047 SER A N     1 
ATOM   1453 C  CA    . SER A 1 256 ? 92.194  110.156 75.164  1.00 58.90  ? 2047 SER A CA    1 
ATOM   1454 C  C     . SER A 1 256 ? 91.712  111.322 76.019  1.00 60.58  ? 2047 SER A C     1 
ATOM   1455 O  O     . SER A 1 256 ? 92.422  112.325 76.185  1.00 64.52  ? 2047 SER A O     1 
ATOM   1456 C  CB    . SER A 1 256 ? 91.474  110.140 73.817  1.00 63.00  ? 2047 SER A CB    1 
ATOM   1457 O  OG    . SER A 1 256 ? 91.992  109.125 72.976  1.00 66.80  ? 2047 SER A OG    1 
ATOM   1458 N  N     . VAL A 1 257 ? 90.500  111.213 76.569  1.00 59.97  ? 2048 VAL A N     1 
ATOM   1459 C  CA    . VAL A 1 257 ? 89.982  112.302 77.389  1.00 60.22  ? 2048 VAL A CA    1 
ATOM   1460 C  C     . VAL A 1 257 ? 90.820  112.461 78.652  1.00 62.78  ? 2048 VAL A C     1 
ATOM   1461 O  O     . VAL A 1 257 ? 91.114  113.585 79.079  1.00 66.00  ? 2048 VAL A O     1 
ATOM   1462 C  CB    . VAL A 1 257 ? 88.487  112.094 77.701  1.00 61.09  ? 2048 VAL A CB    1 
ATOM   1463 C  CG1   . VAL A 1 257 ? 88.257  110.844 78.528  1.00 61.77  ? 2048 VAL A CG1   1 
ATOM   1464 C  CG2   . VAL A 1 257 ? 87.921  113.314 78.410  1.00 61.26  ? 2048 VAL A CG2   1 
ATOM   1465 N  N     . GLU A 1 258 ? 91.254  111.348 79.250  1.00 59.33  ? 2049 GLU A N     1 
ATOM   1466 C  CA    . GLU A 1 258 ? 92.096  111.442 80.436  1.00 58.30  ? 2049 GLU A CA    1 
ATOM   1467 C  C     . GLU A 1 258 ? 93.433  112.096 80.115  1.00 52.90  ? 2049 GLU A C     1 
ATOM   1468 O  O     . GLU A 1 258 ? 93.942  112.890 80.909  1.00 56.18  ? 2049 GLU A O     1 
ATOM   1469 C  CB    . GLU A 1 258 ? 92.299  110.055 81.042  1.00 64.55  ? 2049 GLU A CB    1 
ATOM   1470 C  CG    . GLU A 1 258 ? 93.339  109.997 82.143  1.00 55.12  ? 2049 GLU A CG    1 
ATOM   1471 C  CD    . GLU A 1 258 ? 94.669  109.495 81.639  1.00 56.61  ? 2049 GLU A CD    1 
ATOM   1472 O  OE1   . GLU A 1 258 ? 94.833  109.423 80.406  1.00 59.27  ? 2049 GLU A OE1   1 
ATOM   1473 O  OE2   . GLU A 1 258 ? 95.543  109.170 82.469  1.00 57.47  ? 2049 GLU A OE2   1 
ATOM   1474 N  N     . SER A 1 259 ? 94.020  111.772 78.960  1.00 50.97  ? 2050 SER A N     1 
ATOM   1475 C  CA    . SER A 1 259 ? 95.300  112.366 78.590  1.00 52.66  ? 2050 SER A CA    1 
ATOM   1476 C  C     . SER A 1 259 ? 95.166  113.864 78.362  1.00 51.85  ? 2050 SER A C     1 
ATOM   1477 O  O     . SER A 1 259 ? 96.017  114.642 78.809  1.00 52.19  ? 2050 SER A O     1 
ATOM   1478 C  CB    . SER A 1 259 ? 95.864  111.679 77.347  1.00 47.94  ? 2050 SER A CB    1 
ATOM   1479 O  OG    . SER A 1 259 ? 95.211  112.119 76.172  1.00 42.18  ? 2050 SER A OG    1 
ATOM   1480 N  N     . ILE A 1 260 ? 94.099  114.290 77.682  1.00 54.76  ? 2051 ILE A N     1 
ATOM   1481 C  CA    . ILE A 1 260 ? 93.874  115.723 77.500  1.00 56.42  ? 2051 ILE A CA    1 
ATOM   1482 C  C     . ILE A 1 260 ? 93.731  116.407 78.854  1.00 58.95  ? 2051 ILE A C     1 
ATOM   1483 O  O     . ILE A 1 260 ? 94.343  117.455 79.116  1.00 62.79  ? 2051 ILE A O     1 
ATOM   1484 C  CB    . ILE A 1 260 ? 92.637  115.968 76.618  1.00 58.41  ? 2051 ILE A CB    1 
ATOM   1485 C  CG1   . ILE A 1 260 ? 92.844  115.390 75.221  1.00 55.80  ? 2051 ILE A CG1   1 
ATOM   1486 C  CG2   . ILE A 1 260 ? 92.329  117.455 76.537  1.00 58.86  ? 2051 ILE A CG2   1 
ATOM   1487 C  CD1   . ILE A 1 260 ? 91.659  115.594 74.314  1.00 47.86  ? 2051 ILE A CD1   1 
ATOM   1488 N  N     . LEU A 1 261 ? 92.924  115.813 79.739  1.00 52.47  ? 2052 LEU A N     1 
ATOM   1489 C  CA    . LEU A 1 261 ? 92.681  116.419 81.041  1.00 52.55  ? 2052 LEU A CA    1 
ATOM   1490 C  C     . LEU A 1 261 ? 93.965  116.522 81.853  1.00 61.84  ? 2052 LEU A C     1 
ATOM   1491 O  O     . LEU A 1 261 ? 94.245  117.568 82.449  1.00 61.10  ? 2052 LEU A O     1 
ATOM   1492 C  CB    . LEU A 1 261 ? 91.626  115.618 81.806  1.00 52.87  ? 2052 LEU A CB    1 
ATOM   1493 C  CG    . LEU A 1 261 ? 90.151  115.997 81.639  1.00 60.57  ? 2052 LEU A CG    1 
ATOM   1494 C  CD1   . LEU A 1 261 ? 89.854  117.285 82.375  1.00 70.13  ? 2052 LEU A CD1   1 
ATOM   1495 C  CD2   . LEU A 1 261 ? 89.743  116.118 80.182  1.00 61.15  ? 2052 LEU A CD2   1 
ATOM   1496 N  N     . ILE A 1 262 ? 94.766  115.453 81.880  1.00 64.43  ? 2053 ILE A N     1 
ATOM   1497 C  CA    . ILE A 1 262 ? 95.980  115.471 82.690  1.00 53.52  ? 2053 ILE A CA    1 
ATOM   1498 C  C     . ILE A 1 262 ? 97.007  116.425 82.099  1.00 56.05  ? 2053 ILE A C     1 
ATOM   1499 O  O     . ILE A 1 262 ? 97.730  117.094 82.839  1.00 57.91  ? 2053 ILE A O     1 
ATOM   1500 C  CB    . ILE A 1 262 ? 96.558  114.054 82.880  1.00 43.27  ? 2053 ILE A CB    1 
ATOM   1501 C  CG1   . ILE A 1 262 ? 97.014  113.450 81.553  1.00 43.78  ? 2053 ILE A CG1   1 
ATOM   1502 C  CG2   . ILE A 1 262 ? 95.557  113.156 83.591  1.00 47.29  ? 2053 ILE A CG2   1 
ATOM   1503 C  CD1   . ILE A 1 262 ? 97.595  112.062 81.688  1.00 43.04  ? 2053 ILE A CD1   1 
ATOM   1504 N  N     . PHE A 1 263 ? 97.084  116.527 80.769  1.00 53.51  ? 2054 PHE A N     1 
ATOM   1505 C  CA    . PHE A 1 263 ? 98.033  117.466 80.176  1.00 52.06  ? 2054 PHE A CA    1 
ATOM   1506 C  C     . PHE A 1 263 ? 97.668  118.906 80.515  1.00 56.59  ? 2054 PHE A C     1 
ATOM   1507 O  O     . PHE A 1 263 ? 98.529  119.700 80.914  1.00 65.37  ? 2054 PHE A O     1 
ATOM   1508 C  CB    . PHE A 1 263 ? 98.103  117.280 78.663  1.00 48.47  ? 2054 PHE A CB    1 
ATOM   1509 C  CG    . PHE A 1 263 ? 99.131  118.153 78.001  1.00 49.58  ? 2054 PHE A CG    1 
ATOM   1510 C  CD1   . PHE A 1 263 ? 100.476 117.844 78.084  1.00 46.02  ? 2054 PHE A CD1   1 
ATOM   1511 C  CD2   . PHE A 1 263 ? 98.753  119.290 77.310  1.00 55.63  ? 2054 PHE A CD2   1 
ATOM   1512 C  CE1   . PHE A 1 263 ? 101.424 118.645 77.482  1.00 48.66  ? 2054 PHE A CE1   1 
ATOM   1513 C  CE2   . PHE A 1 263 ? 99.699  120.096 76.707  1.00 52.36  ? 2054 PHE A CE2   1 
ATOM   1514 C  CZ    . PHE A 1 263 ? 101.035 119.773 76.793  1.00 52.25  ? 2054 PHE A CZ    1 
ATOM   1515 N  N     . ASN A 1 264 ? 96.391  119.267 80.357  1.00 51.47  ? 2055 ASN A N     1 
ATOM   1516 C  CA    . ASN A 1 264 ? 95.994  120.636 80.675  1.00 56.14  ? 2055 ASN A CA    1 
ATOM   1517 C  C     . ASN A 1 264 ? 96.145  120.926 82.166  1.00 62.05  ? 2055 ASN A C     1 
ATOM   1518 O  O     . ASN A 1 264 ? 96.646  121.993 82.556  1.00 71.95  ? 2055 ASN A O     1 
ATOM   1519 C  CB    . ASN A 1 264 ? 94.562  120.885 80.207  1.00 61.00  ? 2055 ASN A CB    1 
ATOM   1520 C  CG    . ASN A 1 264 ? 94.479  121.167 78.720  1.00 65.86  ? 2055 ASN A CG    1 
ATOM   1521 O  OD1   . ASN A 1 264 ? 94.598  122.312 78.286  1.00 72.15  ? 2055 ASN A OD1   1 
ATOM   1522 N  ND2   . ASN A 1 264 ? 94.279  120.119 77.930  1.00 64.81  ? 2055 ASN A ND2   1 
ATOM   1523 N  N     . SER A 1 265 ? 95.737  119.979 83.017  1.00 51.59  ? 2056 SER A N     1 
ATOM   1524 C  CA    . SER A 1 265 ? 95.890  120.164 84.453  1.00 52.25  ? 2056 SER A CA    1 
ATOM   1525 C  C     . SER A 1 265 ? 97.354  120.261 84.847  1.00 53.92  ? 2056 SER A C     1 
ATOM   1526 O  O     . SER A 1 265 ? 97.695  121.004 85.769  1.00 54.99  ? 2056 SER A O     1 
ATOM   1527 C  CB    . SER A 1 265 ? 95.209  119.022 85.205  1.00 53.18  ? 2056 SER A CB    1 
ATOM   1528 O  OG    . SER A 1 265 ? 95.829  117.784 84.915  1.00 49.07  ? 2056 SER A OG    1 
ATOM   1529 N  N     . MET A 1 266 ? 98.238  119.540 84.155  1.00 53.65  ? 2057 MET A N     1 
ATOM   1530 C  CA    . MET A 1 266 ? 99.654  119.610 84.482  1.00 54.13  ? 2057 MET A CA    1 
ATOM   1531 C  C     . MET A 1 266 ? 100.274 120.911 84.000  1.00 55.08  ? 2057 MET A C     1 
ATOM   1532 O  O     . MET A 1 266 ? 101.197 121.420 84.636  1.00 64.23  ? 2057 MET A O     1 
ATOM   1533 C  CB    . MET A 1 266 ? 100.395 118.416 83.889  1.00 43.80  ? 2057 MET A CB    1 
ATOM   1534 C  CG    . MET A 1 266 ? 101.865 118.375 84.250  1.00 47.66  ? 2057 MET A CG    1 
ATOM   1535 S  SD    . MET A 1 266 ? 102.114 118.231 86.028  1.00 50.03  ? 2057 MET A SD    1 
ATOM   1536 C  CE    . MET A 1 266 ? 103.714 119.007 86.206  1.00 39.48  ? 2057 MET A CE    1 
ATOM   1537 N  N     . ASN A 1 267 ? 99.789  121.464 82.889  1.00 48.29  ? 2058 ASN A N     1 
ATOM   1538 C  CA    . ASN A 1 267 ? 100.214 122.811 82.519  1.00 49.10  ? 2058 ASN A CA    1 
ATOM   1539 C  C     . ASN A 1 267 ? 99.818  123.814 83.596  1.00 54.00  ? 2058 ASN A C     1 
ATOM   1540 O  O     . ASN A 1 267 ? 100.625 124.665 84.000  1.00 64.54  ? 2058 ASN A O     1 
ATOM   1541 C  CB    . ASN A 1 267 ? 99.614  123.203 81.170  1.00 51.63  ? 2058 ASN A CB    1 
ATOM   1542 C  CG    . ASN A 1 267 ? 100.607 123.078 80.034  1.00 57.09  ? 2058 ASN A CG    1 
ATOM   1543 O  OD1   . ASN A 1 267 ? 101.818 123.077 80.252  1.00 61.18  ? 2058 ASN A OD1   1 
ATOM   1544 N  ND2   . ASN A 1 267 ? 100.099 122.975 78.812  1.00 52.99  ? 2058 ASN A ND2   1 
ATOM   1545 N  N     . GLN A 1 268 ? 98.583  123.706 84.095  1.00 48.30  ? 2059 GLN A N     1 
ATOM   1546 C  CA    . GLN A 1 268 ? 98.149  124.581 85.183  1.00 54.74  ? 2059 GLN A CA    1 
ATOM   1547 C  C     . GLN A 1 268 ? 99.001  124.379 86.433  1.00 60.95  ? 2059 GLN A C     1 
ATOM   1548 O  O     . GLN A 1 268 ? 99.397  125.349 87.093  1.00 59.94  ? 2059 GLN A O     1 
ATOM   1549 C  CB    . GLN A 1 268 ? 96.673  124.334 85.493  1.00 59.60  ? 2059 GLN A CB    1 
ATOM   1550 C  CG    . GLN A 1 268 ? 96.139  125.137 86.665  1.00 65.51  ? 2059 GLN A CG    1 
ATOM   1551 C  CD    . GLN A 1 268 ? 95.934  126.597 86.321  1.00 67.26  ? 2059 GLN A CD    1 
ATOM   1552 O  OE1   . GLN A 1 268 ? 95.744  126.951 85.158  1.00 65.75  ? 2059 GLN A OE1   1 
ATOM   1553 N  NE2   . GLN A 1 268 ? 95.967  127.453 87.335  1.00 68.32  ? 2059 GLN A NE2   1 
ATOM   1554 N  N     . LEU A 1 269 ? 99.295  123.121 86.770  1.00 58.70  ? 2060 LEU A N     1 
ATOM   1555 C  CA    . LEU A 1 269 ? 100.101 122.820 87.949  1.00 53.85  ? 2060 LEU A CA    1 
ATOM   1556 C  C     . LEU A 1 269 ? 101.524 123.336 87.799  1.00 51.84  ? 2060 LEU A C     1 
ATOM   1557 O  O     . LEU A 1 269 ? 102.123 123.799 88.772  1.00 54.22  ? 2060 LEU A O     1 
ATOM   1558 C  CB    . LEU A 1 269 ? 100.104 121.315 88.213  1.00 42.79  ? 2060 LEU A CB    1 
ATOM   1559 C  CG    . LEU A 1 269 ? 98.787  120.727 88.710  1.00 39.87  ? 2060 LEU A CG    1 
ATOM   1560 C  CD1   . LEU A 1 269 ? 98.841  119.211 88.713  1.00 39.40  ? 2060 LEU A CD1   1 
ATOM   1561 C  CD2   . LEU A 1 269 ? 98.475  121.258 90.094  1.00 47.08  ? 2060 LEU A CD2   1 
ATOM   1562 N  N     . ASN A 1 270 ? 102.093 123.238 86.598  1.00 47.20  ? 2061 ASN A N     1 
ATOM   1563 C  CA    . ASN A 1 270 ? 103.428 123.771 86.363  1.00 48.55  ? 2061 ASN A CA    1 
ATOM   1564 C  C     . ASN A 1 270 ? 103.443 125.283 86.519  1.00 55.30  ? 2061 ASN A C     1 
ATOM   1565 O  O     . ASN A 1 270 ? 104.385 125.845 87.090  1.00 64.90  ? 2061 ASN A O     1 
ATOM   1566 C  CB    . ASN A 1 270 ? 103.916 123.366 84.975  1.00 47.39  ? 2061 ASN A CB    1 
ATOM   1567 C  CG    . ASN A 1 270 ? 104.804 122.143 85.008  1.00 46.84  ? 2061 ASN A CG    1 
ATOM   1568 O  OD1   . ASN A 1 270 ? 105.357 121.792 86.048  1.00 47.44  ? 2061 ASN A OD1   1 
ATOM   1569 N  ND2   . ASN A 1 270 ? 104.941 121.481 83.867  1.00 47.33  ? 2061 ASN A ND2   1 
ATOM   1570 N  N     . SER A 1 271 ? 102.407 125.960 86.019  1.00 54.64  ? 2062 SER A N     1 
ATOM   1571 C  CA    . SER A 1 271 ? 102.313 127.400 86.241  1.00 60.04  ? 2062 SER A CA    1 
ATOM   1572 C  C     . SER A 1 271 ? 102.231 127.720 87.730  1.00 66.34  ? 2062 SER A C     1 
ATOM   1573 O  O     . SER A 1 271 ? 102.907 128.637 88.218  1.00 71.49  ? 2062 SER A O     1 
ATOM   1574 C  CB    . SER A 1 271 ? 101.104 127.969 85.499  1.00 65.64  ? 2062 SER A CB    1 
ATOM   1575 O  OG    . SER A 1 271 ? 101.328 127.989 84.100  1.00 76.67  ? 2062 SER A OG    1 
ATOM   1576 N  N     . LEU A 1 272 ? 101.422 126.959 88.471  1.00 66.12  ? 2063 LEU A N     1 
ATOM   1577 C  CA    . LEU A 1 272 ? 101.297 127.186 89.909  1.00 67.01  ? 2063 LEU A CA    1 
ATOM   1578 C  C     . LEU A 1 272 ? 102.620 126.947 90.630  1.00 67.65  ? 2063 LEU A C     1 
ATOM   1579 O  O     . LEU A 1 272 ? 102.995 127.713 91.525  1.00 67.50  ? 2063 LEU A O     1 
ATOM   1580 C  CB    . LEU A 1 272 ? 100.204 126.289 90.487  1.00 57.82  ? 2063 LEU A CB    1 
ATOM   1581 C  CG    . LEU A 1 272 ? 98.789  126.864 90.462  1.00 56.27  ? 2063 LEU A CG    1 
ATOM   1582 C  CD1   . LEU A 1 272 ? 97.771  125.791 90.801  1.00 59.53  ? 2063 LEU A CD1   1 
ATOM   1583 C  CD2   . LEU A 1 272 ? 98.680  128.033 91.426  1.00 55.99  ? 2063 LEU A CD2   1 
ATOM   1584 N  N     . LEU A 1 273 ? 103.334 125.883 90.260  1.00 64.46  ? 2064 LEU A N     1 
ATOM   1585 C  CA    . LEU A 1 273 ? 104.610 125.573 90.896  1.00 60.98  ? 2064 LEU A CA    1 
ATOM   1586 C  C     . LEU A 1 273 ? 105.655 126.634 90.583  1.00 64.86  ? 2064 LEU A C     1 
ATOM   1587 O  O     . LEU A 1 273 ? 106.455 126.997 91.452  1.00 67.04  ? 2064 LEU A O     1 
ATOM   1588 C  CB    . LEU A 1 273 ? 105.095 124.193 90.453  1.00 53.29  ? 2064 LEU A CB    1 
ATOM   1589 C  CG    . LEU A 1 273 ? 104.321 122.995 91.006  1.00 51.95  ? 2064 LEU A CG    1 
ATOM   1590 C  CD1   . LEU A 1 273 ? 104.870 121.692 90.451  1.00 45.65  ? 2064 LEU A CD1   1 
ATOM   1591 C  CD2   . LEU A 1 273 ? 104.363 122.993 92.520  1.00 52.51  ? 2064 LEU A CD2   1 
ATOM   1592 N  N     . GLN A 1 274 ? 105.671 127.137 89.347  1.00 66.12  ? 2065 GLN A N     1 
ATOM   1593 C  CA    . GLN A 1 274 ? 106.572 128.234 89.012  1.00 62.45  ? 2065 GLN A CA    1 
ATOM   1594 C  C     . GLN A 1 274 ? 106.239 129.476 89.826  1.00 68.01  ? 2065 GLN A C     1 
ATOM   1595 O  O     . GLN A 1 274 ? 107.140 130.202 90.263  1.00 70.93  ? 2065 GLN A O     1 
ATOM   1596 C  CB    . GLN A 1 274 ? 106.504 128.536 87.516  1.00 63.11  ? 2065 GLN A CB    1 
ATOM   1597 C  CG    . GLN A 1 274 ? 107.783 128.216 86.759  1.00 61.08  ? 2065 GLN A CG    1 
ATOM   1598 C  CD    . GLN A 1 274 ? 107.531 127.901 85.298  1.00 63.79  ? 2065 GLN A CD    1 
ATOM   1599 O  OE1   . GLN A 1 274 ? 106.532 128.330 84.722  1.00 59.02  ? 2065 GLN A OE1   1 
ATOM   1600 N  NE2   . GLN A 1 274 ? 108.440 127.147 84.690  1.00 60.90  ? 2065 GLN A NE2   1 
ATOM   1601 N  N     . LYS A 1 275 ? 104.947 129.739 90.036  1.00 71.68  ? 2066 LYS A N     1 
ATOM   1602 C  CA    . LYS A 1 275 ? 104.554 130.853 90.894  1.00 76.31  ? 2066 LYS A CA    1 
ATOM   1603 C  C     . LYS A 1 275 ? 105.039 130.645 92.325  1.00 74.12  ? 2066 LYS A C     1 
ATOM   1604 O  O     . LYS A 1 275 ? 105.517 131.585 92.970  1.00 74.96  ? 2066 LYS A O     1 
ATOM   1605 C  CB    . LYS A 1 275 ? 103.035 131.027 90.862  1.00 71.91  ? 2066 LYS A CB    1 
ATOM   1606 C  CG    . LYS A 1 275 ? 102.490 131.977 91.917  1.00 70.48  ? 2066 LYS A CG    1 
ATOM   1607 C  CD    . LYS A 1 275 ? 101.738 131.226 93.005  1.00 67.55  ? 2066 LYS A CD    1 
ATOM   1608 C  CE    . LYS A 1 275 ? 101.547 132.090 94.241  1.00 65.91  ? 2066 LYS A CE    1 
ATOM   1609 N  NZ    . LYS A 1 275 ? 101.103 131.291 95.417  1.00 72.53  ? 2066 LYS A NZ    1 
ATOM   1610 N  N     . GLU A 1 276 ? 104.929 129.418 92.832  1.00 69.11  ? 2067 GLU A N     1 
ATOM   1611 C  CA    . GLU A 1 276 ? 105.283 129.101 94.210  1.00 68.51  ? 2067 GLU A CA    1 
ATOM   1612 C  C     . GLU A 1 276 ? 106.779 128.869 94.401  1.00 71.27  ? 2067 GLU A C     1 
ATOM   1613 O  O     . GLU A 1 276 ? 107.232 128.751 95.546  1.00 69.18  ? 2067 GLU A O     1 
ATOM   1614 C  CB    . GLU A 1 276 ? 104.483 127.870 94.661  1.00 64.27  ? 2067 GLU A CB    1 
ATOM   1615 C  CG    . GLU A 1 276 ? 104.637 127.472 96.121  1.00 69.60  ? 2067 GLU A CG    1 
ATOM   1616 C  CD    . GLU A 1 276 ? 103.520 126.568 96.598  1.00 82.92  ? 2067 GLU A CD    1 
ATOM   1617 O  OE1   . GLU A 1 276 ? 102.411 126.643 96.030  1.00 84.94  ? 2067 GLU A OE1   1 
ATOM   1618 O  OE2   . GLU A 1 276 ? 103.752 125.782 97.540  1.00 77.90  ? 2067 GLU A OE2   1 
ATOM   1619 N  N     . ASN A 1 277 ? 107.556 128.838 93.316  1.00 75.84  ? 2068 ASN A N     1 
ATOM   1620 C  CA    . ASN A 1 277 ? 108.981 128.498 93.362  1.00 75.66  ? 2068 ASN A CA    1 
ATOM   1621 C  C     . ASN A 1 277 ? 109.182 127.101 93.948  1.00 67.44  ? 2068 ASN A C     1 
ATOM   1622 O  O     . ASN A 1 277 ? 109.957 126.895 94.884  1.00 55.12  ? 2068 ASN A O     1 
ATOM   1623 C  CB    . ASN A 1 277 ? 109.784 129.547 94.136  1.00 76.35  ? 2068 ASN A CB    1 
ATOM   1624 C  CG    . ASN A 1 277 ? 111.243 129.585 93.724  1.00 76.82  ? 2068 ASN A CG    1 
ATOM   1625 O  OD1   . ASN A 1 277 ? 111.832 128.559 93.383  1.00 80.29  ? 2068 ASN A OD1   1 
ATOM   1626 N  ND2   . ASN A 1 277 ? 111.834 130.774 93.754  1.00 72.43  ? 2068 ASN A ND2   1 
ATOM   1627 N  N     . LEU A 1 278 ? 108.465 126.133 93.378  1.00 67.56  ? 2069 LEU A N     1 
ATOM   1628 C  CA    . LEU A 1 278 ? 108.526 124.750 93.819  1.00 56.63  ? 2069 LEU A CA    1 
ATOM   1629 C  C     . LEU A 1 278 ? 108.832 123.776 92.690  1.00 59.69  ? 2069 LEU A C     1 
ATOM   1630 O  O     . LEU A 1 278 ? 108.919 122.570 92.945  1.00 59.38  ? 2069 LEU A O     1 
ATOM   1631 C  CB    . LEU A 1 278 ? 107.202 124.347 94.487  1.00 51.28  ? 2069 LEU A CB    1 
ATOM   1632 C  CG    . LEU A 1 278 ? 107.252 123.324 95.621  1.00 42.92  ? 2069 LEU A CG    1 
ATOM   1633 C  CD1   . LEU A 1 278 ? 108.072 123.857 96.779  1.00 50.79  ? 2069 LEU A CD1   1 
ATOM   1634 C  CD2   . LEU A 1 278 ? 105.847 122.971 96.073  1.00 40.20  ? 2069 LEU A CD2   1 
ATOM   1635 N  N     . GLN A 1 279 ? 108.995 124.257 91.456  1.00 64.31  ? 2070 GLN A N     1 
ATOM   1636 C  CA    . GLN A 1 279 ? 109.221 123.348 90.338  1.00 57.48  ? 2070 GLN A CA    1 
ATOM   1637 C  C     . GLN A 1 279 ? 110.615 122.736 90.376  1.00 53.44  ? 2070 GLN A C     1 
ATOM   1638 O  O     . GLN A 1 279 ? 110.807 121.614 89.894  1.00 49.84  ? 2070 GLN A O     1 
ATOM   1639 C  CB    . GLN A 1 279 ? 108.998 124.073 89.012  1.00 54.77  ? 2070 GLN A CB    1 
ATOM   1640 C  CG    . GLN A 1 279 ? 108.880 123.140 87.820  1.00 52.41  ? 2070 GLN A CG    1 
ATOM   1641 C  CD    . GLN A 1 279 ? 108.470 123.861 86.555  1.00 60.42  ? 2070 GLN A CD    1 
ATOM   1642 O  OE1   . GLN A 1 279 ? 107.971 124.985 86.602  1.00 64.26  ? 2070 GLN A OE1   1 
ATOM   1643 N  NE2   . GLN A 1 279 ? 108.681 123.219 85.413  1.00 61.30  ? 2070 GLN A NE2   1 
ATOM   1644 N  N     . ASP A 1 280 ? 111.597 123.450 90.928  1.00 56.46  ? 2071 ASP A N     1 
ATOM   1645 C  CA    . ASP A 1 280 ? 112.942 122.893 91.028  1.00 58.15  ? 2071 ASP A CA    1 
ATOM   1646 C  C     . ASP A 1 280 ? 112.956 121.660 91.923  1.00 54.22  ? 2071 ASP A C     1 
ATOM   1647 O  O     . ASP A 1 280 ? 113.528 120.623 91.566  1.00 54.95  ? 2071 ASP A O     1 
ATOM   1648 C  CB    . ASP A 1 280 ? 113.913 123.952 91.548  1.00 58.41  ? 2071 ASP A CB    1 
ATOM   1649 C  CG    . ASP A 1 280 ? 115.186 124.026 90.730  1.00 59.10  ? 2071 ASP A CG    1 
ATOM   1650 O  OD1   . ASP A 1 280 ? 115.321 123.243 89.767  1.00 57.32  ? 2071 ASP A OD1   1 
ATOM   1651 O  OD2   . ASP A 1 280 ? 116.052 124.868 91.050  1.00 59.73  ? 2071 ASP A OD2   1 
ATOM   1652 N  N     . VAL A 1 281 ? 112.312 121.751 93.090  1.00 48.08  ? 2072 VAL A N     1 
ATOM   1653 C  CA    . VAL A 1 281 ? 112.221 120.609 93.992  1.00 42.03  ? 2072 VAL A CA    1 
ATOM   1654 C  C     . VAL A 1 281 ? 111.253 119.552 93.489  1.00 39.22  ? 2072 VAL A C     1 
ATOM   1655 O  O     . VAL A 1 281 ? 111.253 118.429 94.004  1.00 43.46  ? 2072 VAL A O     1 
ATOM   1656 C  CB    . VAL A 1 281 ? 111.809 121.069 95.406  1.00 49.39  ? 2072 VAL A CB    1 
ATOM   1657 C  CG1   . VAL A 1 281 ? 110.300 121.190 95.512  1.00 42.43  ? 2072 VAL A CG1   1 
ATOM   1658 C  CG2   . VAL A 1 281 ? 112.353 120.121 96.459  1.00 48.82  ? 2072 VAL A CG2   1 
ATOM   1659 N  N     . PHE A 1 282 ? 110.427 119.879 92.497  1.00 41.07  ? 2073 PHE A N     1 
ATOM   1660 C  CA    . PHE A 1 282 ? 109.515 118.908 91.908  1.00 41.81  ? 2073 PHE A CA    1 
ATOM   1661 C  C     . PHE A 1 282 ? 110.147 118.139 90.758  1.00 39.66  ? 2073 PHE A C     1 
ATOM   1662 O  O     . PHE A 1 282 ? 109.778 116.984 90.516  1.00 42.24  ? 2073 PHE A O     1 
ATOM   1663 C  CB    . PHE A 1 282 ? 108.243 119.611 91.423  1.00 40.26  ? 2073 PHE A CB    1 
ATOM   1664 C  CG    . PHE A 1 282 ? 107.441 118.809 90.438  1.00 34.19  ? 2073 PHE A CG    1 
ATOM   1665 C  CD1   . PHE A 1 282 ? 106.762 117.673 90.838  1.00 37.42  ? 2073 PHE A CD1   1 
ATOM   1666 C  CD2   . PHE A 1 282 ? 107.364 119.195 89.113  1.00 38.72  ? 2073 PHE A CD2   1 
ATOM   1667 C  CE1   . PHE A 1 282 ? 106.025 116.937 89.934  1.00 34.16  ? 2073 PHE A CE1   1 
ATOM   1668 C  CE2   . PHE A 1 282 ? 106.629 118.461 88.207  1.00 43.59  ? 2073 PHE A CE2   1 
ATOM   1669 C  CZ    . PHE A 1 282 ? 105.958 117.331 88.618  1.00 35.17  ? 2073 PHE A CZ    1 
ATOM   1670 N  N     . ARG A 1 283 ? 111.100 118.745 90.054  1.00 37.81  ? 2074 ARG A N     1 
ATOM   1671 C  CA    . ARG A 1 283 ? 111.728 118.112 88.903  1.00 34.33  ? 2074 ARG A CA    1 
ATOM   1672 C  C     . ARG A 1 283 ? 113.107 117.543 89.197  1.00 32.65  ? 2074 ARG A C     1 
ATOM   1673 O  O     . ARG A 1 283 ? 113.538 116.617 88.504  1.00 29.22  ? 2074 ARG A O     1 
ATOM   1674 C  CB    . ARG A 1 283 ? 111.843 119.110 87.746  1.00 42.69  ? 2074 ARG A CB    1 
ATOM   1675 C  CG    . ARG A 1 283 ? 110.544 119.351 86.998  1.00 47.91  ? 2074 ARG A CG    1 
ATOM   1676 C  CD    . ARG A 1 283 ? 110.753 120.263 85.798  1.00 46.43  ? 2074 ARG A CD    1 
ATOM   1677 N  NE    . ARG A 1 283 ? 111.641 121.379 86.100  1.00 52.97  ? 2074 ARG A NE    1 
ATOM   1678 C  CZ    . ARG A 1 283 ? 112.850 121.539 85.577  1.00 54.29  ? 2074 ARG A CZ    1 
ATOM   1679 N  NH1   . ARG A 1 283 ? 113.351 120.667 84.718  1.00 57.21  ? 2074 ARG A NH1   1 
ATOM   1680 N  NH2   . ARG A 1 283 ? 113.573 122.598 85.927  1.00 56.75  ? 2074 ARG A NH2   1 
ATOM   1681 N  N     . LYS A 1 284 ? 113.812 118.067 90.201  1.00 33.05  ? 2075 LYS A N     1 
ATOM   1682 C  CA    . LYS A 1 284 ? 115.181 117.630 90.447  1.00 32.40  ? 2075 LYS A CA    1 
ATOM   1683 C  C     . LYS A 1 284 ? 115.265 116.468 91.427  1.00 34.53  ? 2075 LYS A C     1 
ATOM   1684 O  O     . LYS A 1 284 ? 116.127 115.596 91.273  1.00 35.29  ? 2075 LYS A O     1 
ATOM   1685 C  CB    . LYS A 1 284 ? 116.023 118.801 90.958  1.00 35.89  ? 2075 LYS A CB    1 
ATOM   1686 C  CG    . LYS A 1 284 ? 116.333 119.844 89.897  1.00 37.71  ? 2075 LYS A CG    1 
ATOM   1687 C  CD    . LYS A 1 284 ? 117.828 120.086 89.773  1.00 38.88  ? 2075 LYS A CD    1 
ATOM   1688 C  CE    . LYS A 1 284 ? 118.417 120.590 91.080  1.00 40.33  ? 2075 LYS A CE    1 
ATOM   1689 N  NZ    . LYS A 1 284 ? 119.903 120.489 91.094  1.00 28.10  ? 2075 LYS A NZ    1 
ATOM   1690 N  N     . VAL A 1 285 ? 114.395 116.431 92.438  1.00 34.13  ? 2076 VAL A N     1 
ATOM   1691 C  CA    . VAL A 1 285 ? 114.417 115.383 93.447  1.00 33.38  ? 2076 VAL A CA    1 
ATOM   1692 C  C     . VAL A 1 285 ? 113.106 114.609 93.506  1.00 30.73  ? 2076 VAL A C     1 
ATOM   1693 O  O     . VAL A 1 285 ? 113.117 113.380 93.614  1.00 33.98  ? 2076 VAL A O     1 
ATOM   1694 C  CB    . VAL A 1 285 ? 114.780 115.943 94.840  1.00 34.97  ? 2076 VAL A CB    1 
ATOM   1695 C  CG1   . VAL A 1 285 ? 113.801 117.015 95.271  1.00 33.40  ? 2076 VAL A CG1   1 
ATOM   1696 C  CG2   . VAL A 1 285 ? 114.795 114.818 95.857  1.00 32.56  ? 2076 VAL A CG2   1 
ATOM   1697 N  N     . GLU A 1 286 ? 111.967 115.298 93.434  1.00 28.16  ? 2077 GLU A N     1 
ATOM   1698 C  CA    . GLU A 1 286 ? 110.692 114.641 93.703  1.00 22.87  ? 2077 GLU A CA    1 
ATOM   1699 C  C     . GLU A 1 286 ? 110.335 113.651 92.601  1.00 25.08  ? 2077 GLU A C     1 
ATOM   1700 O  O     . GLU A 1 286 ? 110.104 112.467 92.864  1.00 27.02  ? 2077 GLU A O     1 
ATOM   1701 C  CB    . GLU A 1 286 ? 109.593 115.687 93.871  1.00 24.80  ? 2077 GLU A CB    1 
ATOM   1702 C  CG    . GLU A 1 286 ? 108.263 115.116 94.301  1.00 24.95  ? 2077 GLU A CG    1 
ATOM   1703 C  CD    . GLU A 1 286 ? 108.410 113.962 95.271  1.00 33.72  ? 2077 GLU A CD    1 
ATOM   1704 O  OE1   . GLU A 1 286 ? 108.254 112.799 94.848  1.00 30.08  ? 2077 GLU A OE1   1 
ATOM   1705 O  OE2   . GLU A 1 286 ? 108.699 114.218 96.457  1.00 45.42  ? 2077 GLU A OE2   1 
ATOM   1706 N  N     . MET A 1 287 ? 110.266 114.123 91.358  1.00 28.93  ? 2078 MET A N     1 
ATOM   1707 C  CA    . MET A 1 287 ? 109.972 113.219 90.249  1.00 24.30  ? 2078 MET A CA    1 
ATOM   1708 C  C     . MET A 1 287 ? 111.043 112.150 90.048  1.00 28.02  ? 2078 MET A C     1 
ATOM   1709 O  O     . MET A 1 287 ? 110.675 110.993 89.774  1.00 32.92  ? 2078 MET A O     1 
ATOM   1710 C  CB    . MET A 1 287 ? 109.743 114.030 88.967  1.00 21.46  ? 2078 MET A CB    1 
ATOM   1711 C  CG    . MET A 1 287 ? 108.296 114.478 88.744  1.00 25.28  ? 2078 MET A CG    1 
ATOM   1712 S  SD    . MET A 1 287 ? 106.970 113.370 89.278  1.00 30.36  ? 2078 MET A SD    1 
ATOM   1713 C  CE    . MET A 1 287 ? 107.412 111.828 88.480  1.00 32.54  ? 2078 MET A CE    1 
ATOM   1714 N  N     . PRO A 1 288 ? 112.346 112.443 90.131  1.00 24.22  ? 2079 PRO A N     1 
ATOM   1715 C  CA    . PRO A 1 288 ? 113.321 111.343 90.150  1.00 25.61  ? 2079 PRO A CA    1 
ATOM   1716 C  C     . PRO A 1 288 ? 113.119 110.387 91.312  1.00 28.62  ? 2079 PRO A C     1 
ATOM   1717 O  O     . PRO A 1 288 ? 113.405 109.193 91.175  1.00 31.06  ? 2079 PRO A O     1 
ATOM   1718 C  CB    . PRO A 1 288 ? 114.667 112.073 90.233  1.00 29.42  ? 2079 PRO A CB    1 
ATOM   1719 C  CG    . PRO A 1 288 ? 114.409 113.388 89.611  1.00 28.89  ? 2079 PRO A CG    1 
ATOM   1720 C  CD    . PRO A 1 288 ? 113.016 113.752 90.026  1.00 26.73  ? 2079 PRO A CD    1 
ATOM   1721 N  N     . SER A 1 289 ? 112.630 110.869 92.457  1.00 25.90  ? 2080 SER A N     1 
ATOM   1722 C  CA    . SER A 1 289 ? 112.300 109.960 93.551  1.00 21.21  ? 2080 SER A CA    1 
ATOM   1723 C  C     . SER A 1 289 ? 111.125 109.065 93.184  1.00 24.38  ? 2080 SER A C     1 
ATOM   1724 O  O     . SER A 1 289 ? 111.090 107.894 93.571  1.00 28.43  ? 2080 SER A O     1 
ATOM   1725 C  CB    . SER A 1 289 ? 111.993 110.741 94.825  1.00 24.45  ? 2080 SER A CB    1 
ATOM   1726 O  OG    . SER A 1 289 ? 111.641 109.860 95.875  1.00 24.47  ? 2080 SER A OG    1 
ATOM   1727 N  N     . GLN A 1 290 ? 110.146 109.601 92.453  1.00 26.34  ? 2081 GLN A N     1 
ATOM   1728 C  CA    . GLN A 1 290 ? 109.059 108.765 91.954  1.00 22.38  ? 2081 GLN A CA    1 
ATOM   1729 C  C     . GLN A 1 290 ? 109.585 107.715 90.987  1.00 22.16  ? 2081 GLN A C     1 
ATOM   1730 O  O     . GLN A 1 290 ? 109.120 106.571 90.984  1.00 25.98  ? 2081 GLN A O     1 
ATOM   1731 C  CB    . GLN A 1 290 ? 107.997 109.626 91.277  1.00 22.32  ? 2081 GLN A CB    1 
ATOM   1732 C  CG    . GLN A 1 290 ? 107.293 110.586 92.209  1.00 28.46  ? 2081 GLN A CG    1 
ATOM   1733 C  CD    . GLN A 1 290 ? 106.361 109.881 93.166  1.00 26.36  ? 2081 GLN A CD    1 
ATOM   1734 O  OE1   . GLN A 1 290 ? 105.307 109.387 92.771  1.00 19.72  ? 2081 GLN A OE1   1 
ATOM   1735 N  NE2   . GLN A 1 290 ? 106.744 109.832 94.434  1.00 27.58  ? 2081 GLN A NE2   1 
ATOM   1736 N  N     . TYR A 1 291 ? 110.551 108.094 90.152  1.00 20.54  ? 2082 TYR A N     1 
ATOM   1737 C  CA    . TYR A 1 291 ? 111.186 107.128 89.259  1.00 23.51  ? 2082 TYR A CA    1 
ATOM   1738 C  C     . TYR A 1 291 ? 111.902 106.034 90.049  1.00 27.60  ? 2082 TYR A C     1 
ATOM   1739 O  O     . TYR A 1 291 ? 111.800 104.843 89.722  1.00 35.88  ? 2082 TYR A O     1 
ATOM   1740 C  CB    . TYR A 1 291 ? 112.158 107.858 88.334  1.00 25.74  ? 2082 TYR A CB    1 
ATOM   1741 C  CG    . TYR A 1 291 ? 113.018 106.963 87.481  1.00 24.52  ? 2082 TYR A CG    1 
ATOM   1742 C  CD1   . TYR A 1 291 ? 112.521 106.398 86.318  1.00 30.65  ? 2082 TYR A CD1   1 
ATOM   1743 C  CD2   . TYR A 1 291 ? 114.334 106.699 87.828  1.00 20.48  ? 2082 TYR A CD2   1 
ATOM   1744 C  CE1   . TYR A 1 291 ? 113.305 105.587 85.531  1.00 36.21  ? 2082 TYR A CE1   1 
ATOM   1745 C  CE2   . TYR A 1 291 ? 115.126 105.889 87.047  1.00 28.78  ? 2082 TYR A CE2   1 
ATOM   1746 C  CZ    . TYR A 1 291 ? 114.606 105.336 85.900  1.00 40.36  ? 2082 TYR A CZ    1 
ATOM   1747 O  OH    . TYR A 1 291 ? 115.390 104.528 85.114  1.00 51.70  ? 2082 TYR A OH    1 
ATOM   1748 N  N     . CYS A 1 292 ? 112.625 106.424 91.100  1.00 24.84  ? 2083 CYS A N     1 
ATOM   1749 C  CA    . CYS A 1 292 ? 113.306 105.450 91.945  1.00 20.15  ? 2083 CYS A CA    1 
ATOM   1750 C  C     . CYS A 1 292 ? 112.309 104.533 92.640  1.00 17.88  ? 2083 CYS A C     1 
ATOM   1751 O  O     . CYS A 1 292 ? 112.557 103.334 92.791  1.00 20.22  ? 2083 CYS A O     1 
ATOM   1752 C  CB    . CYS A 1 292 ? 114.177 106.167 92.973  1.00 21.33  ? 2083 CYS A CB    1 
ATOM   1753 S  SG    . CYS A 1 292 ? 115.595 107.039 92.279  1.00 41.86  ? 2083 CYS A SG    1 
ATOM   1754 N  N     . LEU A 1 293 ? 111.179 105.083 93.083  1.00 19.79  ? 2084 LEU A N     1 
ATOM   1755 C  CA    . LEU A 1 293 ? 110.146 104.263 93.706  1.00 19.65  ? 2084 LEU A CA    1 
ATOM   1756 C  C     . LEU A 1 293 ? 109.504 103.317 92.703  1.00 21.91  ? 2084 LEU A C     1 
ATOM   1757 O  O     . LEU A 1 293 ? 109.122 102.202 93.066  1.00 28.27  ? 2084 LEU A O     1 
ATOM   1758 C  CB    . LEU A 1 293 ? 109.088 105.151 94.355  1.00 19.41  ? 2084 LEU A CB    1 
ATOM   1759 C  CG    . LEU A 1 293 ? 109.502 105.783 95.682  1.00 13.26  ? 2084 LEU A CG    1 
ATOM   1760 C  CD1   . LEU A 1 293 ? 108.351 106.566 96.270  1.00 14.25  ? 2084 LEU A CD1   1 
ATOM   1761 C  CD2   . LEU A 1 293 ? 109.975 104.719 96.652  1.00 12.16  ? 2084 LEU A CD2   1 
ATOM   1762 N  N     . ALA A 1 294 ? 109.364 103.742 91.447  1.00 18.78  ? 2085 ALA A N     1 
ATOM   1763 C  CA    . ALA A 1 294 ? 108.903 102.825 90.411  1.00 19.39  ? 2085 ALA A CA    1 
ATOM   1764 C  C     . ALA A 1 294 ? 109.889 101.681 90.228  1.00 27.39  ? 2085 ALA A C     1 
ATOM   1765 O  O     . ALA A 1 294 ? 109.488 100.519 90.081  1.00 33.41  ? 2085 ALA A O     1 
ATOM   1766 C  CB    . ALA A 1 294 ? 108.695 103.574 89.097  1.00 19.01  ? 2085 ALA A CB    1 
ATOM   1767 N  N     . LEU A 1 295 ? 111.187 101.991 90.247  1.00 28.57  ? 2086 LEU A N     1 
ATOM   1768 C  CA    . LEU A 1 295 ? 112.200 100.939 90.177  1.00 25.28  ? 2086 LEU A CA    1 
ATOM   1769 C  C     . LEU A 1 295 ? 112.117 100.010 91.383  1.00 27.56  ? 2086 LEU A C     1 
ATOM   1770 O  O     . LEU A 1 295 ? 112.290 98.793  91.255  1.00 32.31  ? 2086 LEU A O     1 
ATOM   1771 C  CB    . LEU A 1 295 ? 113.593 101.556 90.073  1.00 18.36  ? 2086 LEU A CB    1 
ATOM   1772 C  CG    . LEU A 1 295 ? 113.938 102.171 88.719  1.00 30.11  ? 2086 LEU A CG    1 
ATOM   1773 C  CD1   . LEU A 1 295 ? 115.433 102.393 88.600  1.00 32.88  ? 2086 LEU A CD1   1 
ATOM   1774 C  CD2   . LEU A 1 295 ? 113.436 101.282 87.598  1.00 35.29  ? 2086 LEU A CD2   1 
ATOM   1775 N  N     . LEU A 1 296 ? 111.868 100.572 92.567  1.00 22.53  ? 2087 LEU A N     1 
ATOM   1776 C  CA    . LEU A 1 296 ? 111.715 99.761  93.771  1.00 18.55  ? 2087 LEU A CA    1 
ATOM   1777 C  C     . LEU A 1 296 ? 110.506 98.841  93.671  1.00 19.56  ? 2087 LEU A C     1 
ATOM   1778 O  O     . LEU A 1 296 ? 110.569 97.672  94.069  1.00 24.17  ? 2087 LEU A O     1 
ATOM   1779 C  CB    . LEU A 1 296 ? 111.605 100.673 94.994  1.00 18.14  ? 2087 LEU A CB    1 
ATOM   1780 C  CG    . LEU A 1 296 ? 110.733 100.257 96.179  1.00 16.35  ? 2087 LEU A CG    1 
ATOM   1781 C  CD1   . LEU A 1 296 ? 111.376 100.717 97.464  1.00 21.62  ? 2087 LEU A CD1   1 
ATOM   1782 C  CD2   . LEU A 1 296 ? 109.348 100.860 96.062  1.00 20.86  ? 2087 LEU A CD2   1 
ATOM   1783 N  N     . GLU A 1 297 ? 109.392 99.359  93.157  1.00 17.84  ? 2088 GLU A N     1 
ATOM   1784 C  CA    . GLU A 1 297 ? 108.196 98.544  92.986  1.00 18.07  ? 2088 GLU A CA    1 
ATOM   1785 C  C     . GLU A 1 297 ? 108.435 97.433  91.975  1.00 23.62  ? 2088 GLU A C     1 
ATOM   1786 O  O     . GLU A 1 297 ? 107.944 96.311  92.145  1.00 30.75  ? 2088 GLU A O     1 
ATOM   1787 C  CB    . GLU A 1 297 ? 107.026 99.423  92.554  1.00 19.39  ? 2088 GLU A CB    1 
ATOM   1788 C  CG    . GLU A 1 297 ? 105.664 98.814  92.803  1.00 26.76  ? 2088 GLU A CG    1 
ATOM   1789 C  CD    . GLU A 1 297 ? 104.614 99.861  93.100  1.00 34.41  ? 2088 GLU A CD    1 
ATOM   1790 O  OE1   . GLU A 1 297 ? 104.990 100.961 93.554  1.00 30.16  ? 2088 GLU A OE1   1 
ATOM   1791 O  OE2   . GLU A 1 297 ? 103.417 99.589  92.873  1.00 35.90  ? 2088 GLU A OE2   1 
ATOM   1792 N  N     . LEU A 1 298 ? 109.174 97.732  90.906  1.00 21.07  ? 2089 LEU A N     1 
ATOM   1793 C  CA    . LEU A 1 298 ? 109.524 96.696  89.941  1.00 21.29  ? 2089 LEU A CA    1 
ATOM   1794 C  C     . LEU A 1 298 ? 110.409 95.629  90.574  1.00 27.82  ? 2089 LEU A C     1 
ATOM   1795 O  O     . LEU A 1 298 ? 110.213 94.430  90.341  1.00 35.60  ? 2089 LEU A O     1 
ATOM   1796 C  CB    . LEU A 1 298 ? 110.220 97.320  88.734  1.00 21.35  ? 2089 LEU A CB    1 
ATOM   1797 C  CG    . LEU A 1 298 ? 109.354 98.204  87.838  1.00 26.07  ? 2089 LEU A CG    1 
ATOM   1798 C  CD1   . LEU A 1 298 ? 110.225 99.144  87.028  1.00 28.37  ? 2089 LEU A CD1   1 
ATOM   1799 C  CD2   . LEU A 1 298 ? 108.491 97.355  86.929  1.00 36.10  ? 2089 LEU A CD2   1 
ATOM   1800 N  N     . ASN A 1 299 ? 111.393 96.046  91.375  1.00 24.21  ? 2090 ASN A N     1 
ATOM   1801 C  CA    . ASN A 1 299 ? 112.314 95.094  91.988  1.00 23.86  ? 2090 ASN A CA    1 
ATOM   1802 C  C     . ASN A 1 299 ? 111.610 94.215  93.012  1.00 26.33  ? 2090 ASN A C     1 
ATOM   1803 O  O     . ASN A 1 299 ? 111.716 92.984  92.968  1.00 34.26  ? 2090 ASN A O     1 
ATOM   1804 C  CB    . ASN A 1 299 ? 113.474 95.839  92.645  1.00 23.81  ? 2090 ASN A CB    1 
ATOM   1805 C  CG    . ASN A 1 299 ? 114.488 96.331  91.645  1.00 31.75  ? 2090 ASN A CG    1 
ATOM   1806 O  OD1   . ASN A 1 299 ? 114.881 95.604  90.736  1.00 43.13  ? 2090 ASN A OD1   1 
ATOM   1807 N  ND2   . ASN A 1 299 ? 114.923 97.575  91.807  1.00 29.56  ? 2090 ASN A ND2   1 
ATOM   1808 N  N     . GLY A 1 300 ? 110.883 94.828  93.941  1.00 25.75  ? 2091 GLY A N     1 
ATOM   1809 C  CA    . GLY A 1 300 ? 110.337 94.103  95.066  1.00 20.86  ? 2091 GLY A CA    1 
ATOM   1810 C  C     . GLY A 1 300 ? 111.405 93.787  96.094  1.00 24.73  ? 2091 GLY A C     1 
ATOM   1811 O  O     . GLY A 1 300 ? 112.570 94.163  95.972  1.00 34.12  ? 2091 GLY A O     1 
ATOM   1812 N  N     . ILE A 1 301 ? 110.989 93.067  97.131  1.00 27.71  ? 2092 ILE A N     1 
ATOM   1813 C  CA    . ILE A 1 301 ? 111.868 92.660  98.219  1.00 23.07  ? 2092 ILE A CA    1 
ATOM   1814 C  C     . ILE A 1 301 ? 111.953 91.144  98.217  1.00 30.41  ? 2092 ILE A C     1 
ATOM   1815 O  O     . ILE A 1 301 ? 110.923 90.461  98.228  1.00 41.01  ? 2092 ILE A O     1 
ATOM   1816 C  CB    . ILE A 1 301 ? 111.366 93.174  99.580  1.00 15.81  ? 2092 ILE A CB    1 
ATOM   1817 C  CG1   . ILE A 1 301 ? 110.917 94.629  99.460  1.00 28.01  ? 2092 ILE A CG1   1 
ATOM   1818 C  CG2   . ILE A 1 301 ? 112.448 93.032  100.631 1.00 17.33  ? 2092 ILE A CG2   1 
ATOM   1819 C  CD1   . ILE A 1 301 ? 110.319 95.183  100.722 1.00 19.79  ? 2092 ILE A CD1   1 
ATOM   1820 N  N     . GLY A 1 302 ? 113.174 90.620  98.197  1.00 33.98  ? 2093 GLY A N     1 
ATOM   1821 C  CA    . GLY A 1 302 ? 113.363 89.184  98.187  1.00 46.66  ? 2093 GLY A CA    1 
ATOM   1822 C  C     . GLY A 1 302 ? 112.864 88.529  99.456  1.00 48.21  ? 2093 GLY A C     1 
ATOM   1823 O  O     . GLY A 1 302 ? 113.469 88.687  100.518 1.00 44.57  ? 2093 GLY A O     1 
ATOM   1824 N  N     . PHE A 1 303 ? 111.764 87.790  99.361  1.00 52.14  ? 2094 PHE A N     1 
ATOM   1825 C  CA    . PHE A 1 303 ? 111.131 87.161  100.512 1.00 52.42  ? 2094 PHE A CA    1 
ATOM   1826 C  C     . PHE A 1 303 ? 111.271 85.651  100.403 1.00 57.29  ? 2094 PHE A C     1 
ATOM   1827 O  O     . PHE A 1 303 ? 110.878 85.059  99.393  1.00 64.43  ? 2094 PHE A O     1 
ATOM   1828 C  CB    . PHE A 1 303 ? 109.655 87.551  100.602 1.00 50.63  ? 2094 PHE A CB    1 
ATOM   1829 C  CG    . PHE A 1 303 ? 108.989 87.126  101.878 1.00 51.85  ? 2094 PHE A CG    1 
ATOM   1830 C  CD1   . PHE A 1 303 ? 109.038 87.932  103.001 1.00 49.83  ? 2094 PHE A CD1   1 
ATOM   1831 C  CD2   . PHE A 1 303 ? 108.304 85.926  101.950 1.00 58.99  ? 2094 PHE A CD2   1 
ATOM   1832 C  CE1   . PHE A 1 303 ? 108.422 87.545  104.175 1.00 52.06  ? 2094 PHE A CE1   1 
ATOM   1833 C  CE2   . PHE A 1 303 ? 107.687 85.533  103.121 1.00 62.25  ? 2094 PHE A CE2   1 
ATOM   1834 C  CZ    . PHE A 1 303 ? 107.746 86.344  104.234 1.00 52.41  ? 2094 PHE A CZ    1 
ATOM   1835 N  N     . SER A 1 304 ? 111.824 85.032  101.441 1.00 52.93  ? 2095 SER A N     1 
ATOM   1836 C  CA    . SER A 1 304 ? 112.014 83.590  101.486 1.00 60.76  ? 2095 SER A CA    1 
ATOM   1837 C  C     . SER A 1 304 ? 111.110 82.997  102.556 1.00 62.76  ? 2095 SER A C     1 
ATOM   1838 O  O     . SER A 1 304 ? 111.124 83.445  103.707 1.00 67.60  ? 2095 SER A O     1 
ATOM   1839 C  CB    . SER A 1 304 ? 113.478 83.237  101.763 1.00 66.27  ? 2095 SER A CB    1 
ATOM   1840 O  OG    . SER A 1 304 ? 113.793 83.372  103.137 1.00 61.23  ? 2095 SER A OG    1 
ATOM   1841 N  N     . THR A 1 305 ? 110.315 82.000  102.170 1.00 60.08  ? 2096 THR A N     1 
ATOM   1842 C  CA    . THR A 1 305 ? 109.441 81.323  103.117 1.00 63.05  ? 2096 THR A CA    1 
ATOM   1843 C  C     . THR A 1 305 ? 110.167 80.271  103.942 1.00 68.84  ? 2096 THR A C     1 
ATOM   1844 O  O     . THR A 1 305 ? 109.612 79.799  104.940 1.00 71.47  ? 2096 THR A O     1 
ATOM   1845 C  CB    . THR A 1 305 ? 108.267 80.673  102.380 1.00 59.30  ? 2096 THR A CB    1 
ATOM   1846 O  OG1   . THR A 1 305 ? 108.712 80.181  101.110 1.00 58.31  ? 2096 THR A OG1   1 
ATOM   1847 C  CG2   . THR A 1 305 ? 107.154 81.682  102.164 1.00 58.78  ? 2096 THR A CG2   1 
ATOM   1848 N  N     . ALA A 1 306 ? 111.386 79.891  103.551 1.00 68.76  ? 2097 ALA A N     1 
ATOM   1849 C  CA    . ALA A 1 306 ? 112.146 78.923  104.335 1.00 76.02  ? 2097 ALA A CA    1 
ATOM   1850 C  C     . ALA A 1 306 ? 112.497 79.481  105.708 1.00 73.05  ? 2097 ALA A C     1 
ATOM   1851 O  O     . ALA A 1 306 ? 112.427 78.765  106.714 1.00 73.21  ? 2097 ALA A O     1 
ATOM   1852 C  CB    . ALA A 1 306 ? 113.410 78.513  103.581 1.00 73.78  ? 2097 ALA A CB    1 
ATOM   1853 N  N     . GLU A 1 307 ? 112.876 80.756  105.769 1.00 68.02  ? 2098 GLU A N     1 
ATOM   1854 C  CA    . GLU A 1 307 ? 113.235 81.408  107.019 1.00 67.28  ? 2098 GLU A CA    1 
ATOM   1855 C  C     . GLU A 1 307 ? 112.083 82.201  107.620 1.00 63.29  ? 2098 GLU A C     1 
ATOM   1856 O  O     . GLU A 1 307 ? 112.291 82.942  108.585 1.00 63.42  ? 2098 GLU A O     1 
ATOM   1857 C  CB    . GLU A 1 307 ? 114.446 82.320  106.811 1.00 65.14  ? 2098 GLU A CB    1 
ATOM   1858 C  CG    . GLU A 1 307 ? 115.794 81.632  106.999 1.00 69.35  ? 2098 GLU A CG    1 
ATOM   1859 C  CD    . GLU A 1 307 ? 115.884 80.824  108.284 1.00 72.74  ? 2098 GLU A CD    1 
ATOM   1860 O  OE1   . GLU A 1 307 ? 116.552 79.769  108.274 1.00 77.64  ? 2098 GLU A OE1   1 
ATOM   1861 O  OE2   . GLU A 1 307 ? 115.312 81.252  109.309 1.00 71.17  ? 2098 GLU A OE2   1 
ATOM   1862 N  N     . CYS A 1 308 ? 110.880 82.074  107.066 1.00 61.97  ? 2099 CYS A N     1 
ATOM   1863 C  CA    . CYS A 1 308 ? 109.684 82.681  107.637 1.00 66.48  ? 2099 CYS A CA    1 
ATOM   1864 C  C     . CYS A 1 308 ? 108.723 81.662  108.223 1.00 74.89  ? 2099 CYS A C     1 
ATOM   1865 O  O     . CYS A 1 308 ? 108.137 81.911  109.279 1.00 78.86  ? 2099 CYS A O     1 
ATOM   1866 C  CB    . CYS A 1 308 ? 108.952 83.513  106.578 1.00 66.11  ? 2099 CYS A CB    1 
ATOM   1867 S  SG    . CYS A 1 308 ? 107.405 84.249  107.152 1.00 71.43  ? 2099 CYS A SG    1 
ATOM   1868 N  N     . GLU A 1 309 ? 108.550 80.513  107.564 1.00 74.40  ? 2100 GLU A N     1 
ATOM   1869 C  CA    . GLU A 1 309 ? 107.694 79.465  108.112 1.00 73.18  ? 2100 GLU A CA    1 
ATOM   1870 C  C     . GLU A 1 309 ? 108.250 78.929  109.424 1.00 72.50  ? 2100 GLU A C     1 
ATOM   1871 O  O     . GLU A 1 309 ? 107.491 78.642  110.357 1.00 73.60  ? 2100 GLU A O     1 
ATOM   1872 C  CB    . GLU A 1 309 ? 107.532 78.334  107.096 1.00 73.21  ? 2100 GLU A CB    1 
ATOM   1873 C  CG    . GLU A 1 309 ? 106.417 78.555  106.087 1.00 74.52  ? 2100 GLU A CG    1 
ATOM   1874 C  CD    . GLU A 1 309 ? 105.091 77.989  106.552 1.00 81.82  ? 2100 GLU A CD    1 
ATOM   1875 O  OE1   . GLU A 1 309 ? 105.042 77.423  107.664 1.00 82.71  ? 2100 GLU A OE1   1 
ATOM   1876 O  OE2   . GLU A 1 309 ? 104.096 78.108  105.806 1.00 79.70  ? 2100 GLU A OE2   1 
ATOM   1877 N  N     . SER A 1 310 ? 109.574 78.775  109.511 1.00 68.91  ? 2101 SER A N     1 
ATOM   1878 C  CA    . SER A 1 310 ? 110.184 78.310  110.753 1.00 71.23  ? 2101 SER A CA    1 
ATOM   1879 C  C     . SER A 1 310 ? 109.940 79.295  111.888 1.00 71.30  ? 2101 SER A C     1 
ATOM   1880 O  O     . SER A 1 310 ? 109.592 78.894  113.007 1.00 76.22  ? 2101 SER A O     1 
ATOM   1881 C  CB    . SER A 1 310 ? 111.682 78.086  110.548 1.00 67.75  ? 2101 SER A CB    1 
ATOM   1882 O  OG    . SER A 1 310 ? 112.358 77.996  111.789 1.00 71.63  ? 2101 SER A OG    1 
ATOM   1883 N  N     . GLN A 1 311 ? 110.111 80.591  111.618 1.00 65.82  ? 2102 GLN A N     1 
ATOM   1884 C  CA    . GLN A 1 311 ? 109.834 81.597  112.636 1.00 63.43  ? 2102 GLN A CA    1 
ATOM   1885 C  C     . GLN A 1 311 ? 108.366 81.579  113.036 1.00 69.29  ? 2102 GLN A C     1 
ATOM   1886 O  O     . GLN A 1 311 ? 108.039 81.684  114.223 1.00 76.04  ? 2102 GLN A O     1 
ATOM   1887 C  CB    . GLN A 1 311 ? 110.238 82.982  112.133 1.00 56.92  ? 2102 GLN A CB    1 
ATOM   1888 C  CG    . GLN A 1 311 ? 111.699 83.098  111.735 1.00 60.84  ? 2102 GLN A CG    1 
ATOM   1889 C  CD    . GLN A 1 311 ? 112.576 83.593  112.866 1.00 59.21  ? 2102 GLN A CD    1 
ATOM   1890 O  OE1   . GLN A 1 311 ? 112.107 84.270  113.780 1.00 60.69  ? 2102 GLN A OE1   1 
ATOM   1891 N  NE2   . GLN A 1 311 ? 113.860 83.257  112.810 1.00 56.05  ? 2102 GLN A NE2   1 
ATOM   1892 N  N     . LYS A 1 312 ? 107.467 81.441  112.060 1.00 66.63  ? 2103 LYS A N     1 
ATOM   1893 C  CA    . LYS A 1 312 ? 106.041 81.394  112.368 1.00 67.68  ? 2103 LYS A CA    1 
ATOM   1894 C  C     . LYS A 1 312 ? 105.712 80.204  113.260 1.00 74.26  ? 2103 LYS A C     1 
ATOM   1895 O  O     . LYS A 1 312 ? 104.944 80.332  114.220 1.00 75.66  ? 2103 LYS A O     1 
ATOM   1896 C  CB    . LYS A 1 312 ? 105.231 81.339  111.073 1.00 62.68  ? 2103 LYS A CB    1 
ATOM   1897 C  CG    . LYS A 1 312 ? 103.778 80.942  111.256 1.00 61.48  ? 2103 LYS A CG    1 
ATOM   1898 C  CD    . LYS A 1 312 ? 103.033 80.983  109.932 1.00 63.70  ? 2103 LYS A CD    1 
ATOM   1899 C  CE    . LYS A 1 312 ? 101.645 80.382  110.059 1.00 61.52  ? 2103 LYS A CE    1 
ATOM   1900 N  NZ    . LYS A 1 312 ? 100.923 80.381  108.758 1.00 53.49  ? 2103 LYS A NZ    1 
ATOM   1901 N  N     . HIS A 1 313 ? 106.295 79.041  112.965 1.00 76.29  ? 2104 HIS A N     1 
ATOM   1902 C  CA    . HIS A 1 313 ? 106.069 77.866  113.799 1.00 73.71  ? 2104 HIS A CA    1 
ATOM   1903 C  C     . HIS A 1 313 ? 106.627 78.069  115.202 1.00 75.14  ? 2104 HIS A C     1 
ATOM   1904 O  O     . HIS A 1 313 ? 106.013 77.646  116.189 1.00 82.46  ? 2104 HIS A O     1 
ATOM   1905 C  CB    . HIS A 1 313 ? 106.687 76.630  113.146 1.00 70.90  ? 2104 HIS A CB    1 
ATOM   1906 C  CG    . HIS A 1 313 ? 106.001 76.210  111.884 1.00 79.97  ? 2104 HIS A CG    1 
ATOM   1907 N  ND1   . HIS A 1 313 ? 104.705 76.571  111.586 1.00 82.16  ? 2104 HIS A ND1   1 
ATOM   1908 C  CD2   . HIS A 1 313 ? 106.432 75.460  110.842 1.00 83.30  ? 2104 HIS A CD2   1 
ATOM   1909 C  CE1   . HIS A 1 313 ? 104.366 76.062  110.415 1.00 83.71  ? 2104 HIS A CE1   1 
ATOM   1910 N  NE2   . HIS A 1 313 ? 105.396 75.383  109.943 1.00 87.89  ? 2104 HIS A NE2   1 
ATOM   1911 N  N     . ILE A 1 314 ? 107.792 78.712  115.312 1.00 72.59  ? 2105 ILE A N     1 
ATOM   1912 C  CA    . ILE A 1 314 ? 108.382 78.956  116.627 1.00 75.73  ? 2105 ILE A CA    1 
ATOM   1913 C  C     . ILE A 1 314 ? 107.478 79.861  117.458 1.00 79.81  ? 2105 ILE A C     1 
ATOM   1914 O  O     . ILE A 1 314 ? 107.217 79.597  118.639 1.00 81.72  ? 2105 ILE A O     1 
ATOM   1915 C  CB    . ILE A 1 314 ? 109.796 79.544  116.482 1.00 72.37  ? 2105 ILE A CB    1 
ATOM   1916 C  CG1   . ILE A 1 314 ? 110.814 78.424  116.261 1.00 67.71  ? 2105 ILE A CG1   1 
ATOM   1917 C  CG2   . ILE A 1 314 ? 110.166 80.362  117.708 1.00 68.78  ? 2105 ILE A CG2   1 
ATOM   1918 C  CD1   . ILE A 1 314 ? 112.155 78.907  115.760 1.00 60.45  ? 2105 ILE A CD1   1 
ATOM   1919 N  N     . MET A 1 315 ? 106.975 80.939  116.850 1.00 76.81  ? 2106 MET A N     1 
ATOM   1920 C  CA    . MET A 1 315 ? 106.091 81.827  117.600 1.00 73.64  ? 2106 MET A CA    1 
ATOM   1921 C  C     . MET A 1 315 ? 104.744 81.179  117.899 1.00 82.73  ? 2106 MET A C     1 
ATOM   1922 O  O     . MET A 1 315 ? 104.144 81.475  118.933 1.00 89.95  ? 2106 MET A O     1 
ATOM   1923 C  CB    . MET A 1 315 ? 105.899 83.162  116.879 1.00 66.16  ? 2106 MET A CB    1 
ATOM   1924 C  CG    . MET A 1 315 ? 107.116 83.670  116.139 1.00 72.65  ? 2106 MET A CG    1 
ATOM   1925 S  SD    . MET A 1 315 ? 106.710 84.625  114.669 1.00 90.05  ? 2106 MET A SD    1 
ATOM   1926 C  CE    . MET A 1 315 ? 105.670 85.890  115.386 1.00 65.84  ? 2106 MET A CE    1 
ATOM   1927 N  N     . GLN A 1 316 ? 104.255 80.288  117.034 1.00 80.39  ? 2107 GLN A N     1 
ATOM   1928 C  CA    . GLN A 1 316 ? 103.026 79.568  117.363 1.00 82.05  ? 2107 GLN A CA    1 
ATOM   1929 C  C     . GLN A 1 316 ? 103.240 78.617  118.537 1.00 86.69  ? 2107 GLN A C     1 
ATOM   1930 O  O     . GLN A 1 316 ? 102.366 78.477  119.405 1.00 89.12  ? 2107 GLN A O     1 
ATOM   1931 C  CB    . GLN A 1 316 ? 102.513 78.812  116.138 1.00 79.15  ? 2107 GLN A CB    1 
ATOM   1932 C  CG    . GLN A 1 316 ? 101.001 78.841  115.990 1.00 71.05  ? 2107 GLN A CG    1 
ATOM   1933 C  CD    . GLN A 1 316 ? 100.556 78.839  114.542 1.00 77.03  ? 2107 GLN A CD    1 
ATOM   1934 O  OE1   . GLN A 1 316 ? 100.235 79.886  113.979 1.00 75.39  ? 2107 GLN A OE1   1 
ATOM   1935 N  NE2   . GLN A 1 316 ? 100.533 77.661  113.930 1.00 83.20  ? 2107 GLN A NE2   1 
ATOM   1936 N  N     . ALA A 1 317 ? 104.399 77.953  118.577 1.00 89.36  ? 2108 ALA A N     1 
ATOM   1937 C  CA    . ALA A 1 317 ? 104.734 77.117  119.724 1.00 92.20  ? 2108 ALA A CA    1 
ATOM   1938 C  C     . ALA A 1 317 ? 104.806 77.946  120.998 1.00 92.93  ? 2108 ALA A C     1 
ATOM   1939 O  O     . ALA A 1 317 ? 104.300 77.533  122.049 1.00 97.75  ? 2108 ALA A O     1 
ATOM   1940 C  CB    . ALA A 1 317 ? 106.055 76.389  119.478 1.00 88.43  ? 2108 ALA A CB    1 
ATOM   1941 N  N     . LYS A 1 318 ? 105.426 79.125  120.920 1.00 88.78  ? 2109 LYS A N     1 
ATOM   1942 C  CA    . LYS A 1 318 ? 105.465 80.012  122.077 1.00 89.50  ? 2109 LYS A CA    1 
ATOM   1943 C  C     . LYS A 1 318 ? 104.062 80.447  122.482 1.00 89.92  ? 2109 LYS A C     1 
ATOM   1944 O  O     . LYS A 1 318 ? 103.756 80.548  123.676 1.00 97.63  ? 2109 LYS A O     1 
ATOM   1945 C  CB    . LYS A 1 318 ? 106.343 81.227  121.778 1.00 93.22  ? 2109 LYS A CB    1 
ATOM   1946 C  CG    . LYS A 1 318 ? 106.249 82.335  122.812 1.00 91.50  ? 2109 LYS A CG    1 
ATOM   1947 C  CD    . LYS A 1 318 ? 106.650 81.843  124.191 1.00 87.76  ? 2109 LYS A CD    1 
ATOM   1948 C  CE    . LYS A 1 318 ? 108.154 81.728  124.321 1.00 96.48  ? 2109 LYS A CE    1 
ATOM   1949 N  NZ    . LYS A 1 318 ? 108.576 81.748  125.748 1.00 103.98 ? 2109 LYS A NZ    1 
ATOM   1950 N  N     . LEU A 1 319 ? 103.197 80.713  121.501 1.00 81.17  ? 2110 LEU A N     1 
ATOM   1951 C  CA    . LEU A 1 319 ? 101.818 81.086  121.798 1.00 86.92  ? 2110 LEU A CA    1 
ATOM   1952 C  C     . LEU A 1 319 ? 101.106 79.995  122.583 1.00 99.91  ? 2110 LEU A C     1 
ATOM   1953 O  O     . LEU A 1 319 ? 100.477 80.268  123.610 1.00 102.41 ? 2110 LEU A O     1 
ATOM   1954 C  CB    . LEU A 1 319 ? 101.058 81.390  120.507 1.00 86.62  ? 2110 LEU A CB    1 
ATOM   1955 C  CG    . LEU A 1 319 ? 100.779 82.858  120.188 1.00 81.18  ? 2110 LEU A CG    1 
ATOM   1956 C  CD1   . LEU A 1 319 ? 102.065 83.621  120.009 1.00 78.25  ? 2110 LEU A CD1   1 
ATOM   1957 C  CD2   . LEU A 1 319 ? 99.908  82.976  118.946 1.00 77.21  ? 2110 LEU A CD2   1 
ATOM   1958 N  N     . ASP A 1 320 ? 101.187 78.748  122.113 1.00 102.91 ? 2111 ASP A N     1 
ATOM   1959 C  CA    . ASP A 1 320 ? 100.472 77.692  122.825 1.00 102.49 ? 2111 ASP A CA    1 
ATOM   1960 C  C     . ASP A 1 320 ? 101.103 77.406  124.184 1.00 102.32 ? 2111 ASP A C     1 
ATOM   1961 O  O     . ASP A 1 320 ? 100.386 77.087  125.141 1.00 106.20 ? 2111 ASP A O     1 
ATOM   1962 C  CB    . ASP A 1 320 ? 100.371 76.416  121.979 1.00 98.63  ? 2111 ASP A CB    1 
ATOM   1963 C  CG    . ASP A 1 320 ? 101.717 75.870  121.553 1.00 102.21 ? 2111 ASP A CG    1 
ATOM   1964 O  OD1   . ASP A 1 320 ? 102.502 75.440  122.423 1.00 105.75 ? 2111 ASP A OD1   1 
ATOM   1965 O  OD2   . ASP A 1 320 ? 101.972 75.837  120.333 1.00 100.71 ? 2111 ASP A OD2   1 
ATOM   1966 N  N     . ALA A 1 321 ? 102.428 77.542  124.302 1.00 100.35 ? 2112 ALA A N     1 
ATOM   1967 C  CA    . ALA A 1 321 ? 103.066 77.376  125.605 1.00 99.20  ? 2112 ALA A CA    1 
ATOM   1968 C  C     . ALA A 1 321 ? 102.595 78.439  126.590 1.00 99.77  ? 2112 ALA A C     1 
ATOM   1969 O  O     . ALA A 1 321 ? 102.283 78.131  127.747 1.00 100.09 ? 2112 ALA A O     1 
ATOM   1970 C  CB    . ALA A 1 321 ? 104.586 77.418  125.455 1.00 95.59  ? 2112 ALA A CB    1 
ATOM   1971 N  N     . ILE A 1 322 ? 102.529 79.696  126.148 1.00 101.16 ? 2113 ILE A N     1 
ATOM   1972 C  CA    . ILE A 1 322 ? 102.052 80.768  127.015 1.00 102.13 ? 2113 ILE A CA    1 
ATOM   1973 C  C     . ILE A 1 322 ? 100.585 80.555  127.364 1.00 106.90 ? 2113 ILE A C     1 
ATOM   1974 O  O     . ILE A 1 322 ? 100.161 80.809  128.497 1.00 110.81 ? 2113 ILE A O     1 
ATOM   1975 C  CB    . ILE A 1 322 ? 102.291 82.137  126.350 1.00 100.28 ? 2113 ILE A CB    1 
ATOM   1976 C  CG1   . ILE A 1 322 ? 103.774 82.506  126.413 1.00 105.04 ? 2113 ILE A CG1   1 
ATOM   1977 C  CG2   . ILE A 1 322 ? 101.451 83.218  127.012 1.00 91.40  ? 2113 ILE A CG2   1 
ATOM   1978 C  CD1   . ILE A 1 322 ? 104.086 83.881  125.864 1.00 97.61  ? 2113 ILE A CD1   1 
ATOM   1979 N  N     . GLU A 1 323 ? 99.790  80.083  126.402 1.00 104.39 ? 2114 GLU A N     1 
ATOM   1980 C  CA    . GLU A 1 323 ? 98.380  79.818  126.666 1.00 109.81 ? 2114 GLU A CA    1 
ATOM   1981 C  C     . GLU A 1 323 ? 98.216  78.757  127.747 1.00 115.04 ? 2114 GLU A C     1 
ATOM   1982 O  O     . GLU A 1 323 ? 97.432  78.930  128.687 1.00 116.54 ? 2114 GLU A O     1 
ATOM   1983 C  CB    . GLU A 1 323 ? 97.678  79.387  125.377 1.00 110.30 ? 2114 GLU A CB    1 
ATOM   1984 C  CG    . GLU A 1 323 ? 97.416  80.516  124.390 1.00 104.46 ? 2114 GLU A CG    1 
ATOM   1985 C  CD    . GLU A 1 323 ? 96.096  81.219  124.637 1.00 110.29 ? 2114 GLU A CD    1 
ATOM   1986 O  OE1   . GLU A 1 323 ? 95.347  80.784  125.536 1.00 120.88 ? 2114 GLU A OE1   1 
ATOM   1987 O  OE2   . GLU A 1 323 ? 95.805  82.203  123.925 1.00 100.43 ? 2114 GLU A OE2   1 
ATOM   1988 N  N     . THR A 1 324 ? 98.959  77.652  127.635 1.00 115.18 ? 2115 THR A N     1 
ATOM   1989 C  CA    . THR A 1 324 ? 98.865  76.600  128.644 1.00 114.94 ? 2115 THR A CA    1 
ATOM   1990 C  C     . THR A 1 324 ? 99.369  77.082  130.000 1.00 114.40 ? 2115 THR A C     1 
ATOM   1991 O  O     . THR A 1 324 ? 98.780  76.755  131.038 1.00 117.74 ? 2115 THR A O     1 
ATOM   1992 C  CB    . THR A 1 324 ? 99.636  75.357  128.198 1.00 115.96 ? 2115 THR A CB    1 
ATOM   1993 O  OG1   . THR A 1 324 ? 100.999 75.704  127.925 1.00 116.39 ? 2115 THR A OG1   1 
ATOM   1994 C  CG2   . THR A 1 324 ? 99.005  74.756  126.950 1.00 116.36 ? 2115 THR A CG2   1 
ATOM   1995 N  N     . GLN A 1 325 ? 100.458 77.856  130.014 1.00 110.25 ? 2116 GLN A N     1 
ATOM   1996 C  CA    . GLN A 1 325 ? 100.980 78.369  131.277 1.00 109.53 ? 2116 GLN A CA    1 
ATOM   1997 C  C     . GLN A 1 325 ? 99.968  79.283  131.958 1.00 115.59 ? 2116 GLN A C     1 
ATOM   1998 O  O     . GLN A 1 325 ? 99.727  79.172  133.166 1.00 117.83 ? 2116 GLN A O     1 
ATOM   1999 C  CB    . GLN A 1 325 ? 102.297 79.107  131.037 1.00 101.97 ? 2116 GLN A CB    1 
ATOM   2000 C  CG    . GLN A 1 325 ? 102.840 79.818  132.264 1.00 94.73  ? 2116 GLN A CG    1 
ATOM   2001 C  CD    . GLN A 1 325 ? 104.352 79.790  132.331 1.00 89.21  ? 2116 GLN A CD    1 
ATOM   2002 O  OE1   . GLN A 1 325 ? 104.990 78.861  131.836 1.00 86.35  ? 2116 GLN A OE1   1 
ATOM   2003 N  NE2   . GLN A 1 325 ? 104.936 80.813  132.943 1.00 87.63  ? 2116 GLN A NE2   1 
ATOM   2004 N  N     . ALA A 1 326 ? 99.353  80.188  131.195 1.00 114.30 ? 2117 ALA A N     1 
ATOM   2005 C  CA    . ALA A 1 326 ? 98.356  81.083  131.772 1.00 115.89 ? 2117 ALA A CA    1 
ATOM   2006 C  C     . ALA A 1 326 ? 97.122  80.316  132.224 1.00 120.60 ? 2117 ALA A C     1 
ATOM   2007 O  O     . ALA A 1 326 ? 96.517  80.653  133.249 1.00 120.17 ? 2117 ALA A O     1 
ATOM   2008 C  CB    . ALA A 1 326 ? 97.978  82.168  130.765 1.00 109.67 ? 2117 ALA A CB    1 
ATOM   2009 N  N     . TYR A 1 327 ? 96.731  79.284  131.473 1.00 121.92 ? 2118 TYR A N     1 
ATOM   2010 C  CA    . TYR A 1 327 ? 95.581  78.479  131.866 1.00 123.08 ? 2118 TYR A CA    1 
ATOM   2011 C  C     . TYR A 1 327 ? 95.841  77.753  133.178 1.00 123.37 ? 2118 TYR A C     1 
ATOM   2012 O  O     . TYR A 1 327 ? 94.957  77.676  134.039 1.00 124.54 ? 2118 TYR A O     1 
ATOM   2013 C  CB    . TYR A 1 327 ? 95.235  77.481  130.762 1.00 122.96 ? 2118 TYR A CB    1 
ATOM   2014 C  CG    . TYR A 1 327 ? 94.567  78.099  129.554 1.00 122.87 ? 2118 TYR A CG    1 
ATOM   2015 C  CD1   . TYR A 1 327 ? 94.239  79.448  129.530 1.00 121.67 ? 2118 TYR A CD1   1 
ATOM   2016 C  CD2   . TYR A 1 327 ? 94.265  77.331  128.437 1.00 123.41 ? 2118 TYR A CD2   1 
ATOM   2017 C  CE1   . TYR A 1 327 ? 93.631  80.014  128.427 1.00 121.65 ? 2118 TYR A CE1   1 
ATOM   2018 C  CE2   . TYR A 1 327 ? 93.656  77.889  127.330 1.00 121.92 ? 2118 TYR A CE2   1 
ATOM   2019 C  CZ    . TYR A 1 327 ? 93.341  79.230  127.331 1.00 121.47 ? 2118 TYR A CZ    1 
ATOM   2020 O  OH    . TYR A 1 327 ? 92.734  79.790  126.230 1.00 119.93 ? 2118 TYR A OH    1 
ATOM   2021 N  N     . GLN A 1 328 ? 97.049  77.209  133.351 1.00 119.66 ? 2119 GLN A N     1 
ATOM   2022 C  CA    . GLN A 1 328 ? 97.342  76.497  134.590 1.00 119.09 ? 2119 GLN A CA    1 
ATOM   2023 C  C     . GLN A 1 328 ? 97.565  77.459  135.750 1.00 122.95 ? 2119 GLN A C     1 
ATOM   2024 O  O     . GLN A 1 328 ? 97.318  77.095  136.906 1.00 123.01 ? 2119 GLN A O     1 
ATOM   2025 C  CB    . GLN A 1 328 ? 98.534  75.544  134.384 1.00 115.07 ? 2119 GLN A CB    1 
ATOM   2026 C  CG    . GLN A 1 328 ? 99.960  76.124  134.259 1.00 117.82 ? 2119 GLN A CG    1 
ATOM   2027 C  CD    . GLN A 1 328 ? 100.469 76.827  135.511 1.00 122.07 ? 2119 GLN A CD    1 
ATOM   2028 O  OE1   . GLN A 1 328 ? 100.396 76.281  136.612 1.00 118.84 ? 2119 GLN A OE1   1 
ATOM   2029 N  NE2   . GLN A 1 328 ? 101.002 78.030  135.343 1.00 118.90 ? 2119 GLN A NE2   1 
ATOM   2030 N  N     . LEU A 1 329 ? 98.022  78.682  135.469 1.00 120.75 ? 2120 LEU A N     1 
ATOM   2031 C  CA    . LEU A 1 329 ? 98.199  79.664  136.534 1.00 120.85 ? 2120 LEU A CA    1 
ATOM   2032 C  C     . LEU A 1 329 ? 96.853  80.188  137.022 1.00 123.75 ? 2120 LEU A C     1 
ATOM   2033 O  O     . LEU A 1 329 ? 96.618  80.295  138.231 1.00 126.40 ? 2120 LEU A O     1 
ATOM   2034 C  CB    . LEU A 1 329 ? 99.101  80.804  136.044 1.00 116.15 ? 2120 LEU A CB    1 
ATOM   2035 C  CG    . LEU A 1 329 ? 99.304  82.125  136.804 1.00 113.40 ? 2120 LEU A CG    1 
ATOM   2036 C  CD1   . LEU A 1 329 ? 100.554 82.806  136.274 1.00 110.58 ? 2120 LEU A CD1   1 
ATOM   2037 C  CD2   . LEU A 1 329 ? 98.127  83.088  136.682 1.00 109.71 ? 2120 LEU A CD2   1 
ATOM   2038 N  N     . ALA A 1 330 ? 95.954  80.522  136.094 1.00 121.30 ? 2121 ALA A N     1 
ATOM   2039 C  CA    . ALA A 1 330 ? 94.651  81.052  136.470 1.00 120.36 ? 2121 ALA A CA    1 
ATOM   2040 C  C     . ALA A 1 330 ? 93.662  79.964  136.861 1.00 124.11 ? 2121 ALA A C     1 
ATOM   2041 O  O     . ALA A 1 330 ? 92.625  80.274  137.458 1.00 123.80 ? 2121 ALA A O     1 
ATOM   2042 C  CB    . ALA A 1 330 ? 94.071  81.886  135.325 1.00 118.49 ? 2121 ALA A CB    1 
ATOM   2043 N  N     . GLY A 1 331 ? 93.954  78.706  136.541 1.00 124.49 ? 2122 GLY A N     1 
ATOM   2044 C  CA    . GLY A 1 331 ? 93.081  77.604  136.881 1.00 123.57 ? 2122 GLY A CA    1 
ATOM   2045 C  C     . GLY A 1 331 ? 91.954  77.343  135.906 1.00 123.81 ? 2122 GLY A C     1 
ATOM   2046 O  O     . GLY A 1 331 ? 91.194  76.388  136.108 1.00 124.56 ? 2122 GLY A O     1 
ATOM   2047 N  N     . HIS A 1 332 ? 91.818  78.154  134.858 1.00 123.81 ? 2123 HIS A N     1 
ATOM   2048 C  CA    . HIS A 1 332 ? 90.750  77.968  133.888 1.00 124.67 ? 2123 HIS A CA    1 
ATOM   2049 C  C     . HIS A 1 332 ? 91.188  78.534  132.546 1.00 127.00 ? 2123 HIS A C     1 
ATOM   2050 O  O     . HIS A 1 332 ? 92.122  79.335  132.461 1.00 123.96 ? 2123 HIS A O     1 
ATOM   2051 C  CB    . HIS A 1 332 ? 89.443  78.627  134.348 1.00 121.06 ? 2123 HIS A CB    1 
ATOM   2052 C  CG    . HIS A 1 332 ? 89.563  80.096  134.612 1.00 124.03 ? 2123 HIS A CG    1 
ATOM   2053 N  ND1   . HIS A 1 332 ? 90.372  80.612  135.601 1.00 126.99 ? 2123 HIS A ND1   1 
ATOM   2054 C  CD2   . HIS A 1 332 ? 88.972  81.159  134.017 1.00 122.17 ? 2123 HIS A CD2   1 
ATOM   2055 C  CE1   . HIS A 1 332 ? 90.277  81.929  135.602 1.00 126.68 ? 2123 HIS A CE1   1 
ATOM   2056 N  NE2   . HIS A 1 332 ? 89.433  82.287  134.651 1.00 124.19 ? 2123 HIS A NE2   1 
ATOM   2057 N  N     . SER A 1 333 ? 90.498  78.103  131.493 1.00 130.89 ? 2124 SER A N     1 
ATOM   2058 C  CA    . SER A 1 333 ? 90.787  78.548  130.138 1.00 128.85 ? 2124 SER A CA    1 
ATOM   2059 C  C     . SER A 1 333 ? 89.976  79.797  129.819 1.00 127.16 ? 2124 SER A C     1 
ATOM   2060 O  O     . SER A 1 333 ? 88.753  79.814  129.993 1.00 124.38 ? 2124 SER A O     1 
ATOM   2061 C  CB    . SER A 1 333 ? 90.477  77.442  129.128 1.00 125.67 ? 2124 SER A CB    1 
ATOM   2062 O  OG    . SER A 1 333 ? 91.307  76.313  129.338 1.00 118.62 ? 2124 SER A OG    1 
ATOM   2063 N  N     . PHE A 1 334 ? 90.660  80.839  129.353 1.00 126.39 ? 2125 PHE A N     1 
ATOM   2064 C  CA    . PHE A 1 334 ? 90.030  82.106  129.019 1.00 125.35 ? 2125 PHE A CA    1 
ATOM   2065 C  C     . PHE A 1 334 ? 90.559  82.603  127.682 1.00 124.92 ? 2125 PHE A C     1 
ATOM   2066 O  O     . PHE A 1 334 ? 91.670  82.262  127.270 1.00 120.91 ? 2125 PHE A O     1 
ATOM   2067 C  CB    . PHE A 1 334 ? 90.276  83.163  130.109 1.00 124.32 ? 2125 PHE A CB    1 
ATOM   2068 C  CG    . PHE A 1 334 ? 91.729  83.403  130.408 1.00 124.66 ? 2125 PHE A CG    1 
ATOM   2069 C  CD1   . PHE A 1 334 ? 92.407  82.600  131.310 1.00 125.39 ? 2125 PHE A CD1   1 
ATOM   2070 C  CD2   . PHE A 1 334 ? 92.416  84.437  129.793 1.00 119.87 ? 2125 PHE A CD2   1 
ATOM   2071 C  CE1   . PHE A 1 334 ? 93.743  82.819  131.588 1.00 125.24 ? 2125 PHE A CE1   1 
ATOM   2072 C  CE2   . PHE A 1 334 ? 93.751  84.661  130.068 1.00 117.39 ? 2125 PHE A CE2   1 
ATOM   2073 C  CZ    . PHE A 1 334 ? 94.415  83.852  130.966 1.00 118.54 ? 2125 PHE A CZ    1 
ATOM   2074 N  N     . SER A 1 335 ? 89.749  83.416  127.008 1.00 126.23 ? 2126 SER A N     1 
ATOM   2075 C  CA    . SER A 1 335 ? 90.115  83.950  125.703 1.00 120.42 ? 2126 SER A CA    1 
ATOM   2076 C  C     . SER A 1 335 ? 90.966  85.201  125.882 1.00 119.17 ? 2126 SER A C     1 
ATOM   2077 O  O     . SER A 1 335 ? 90.541  86.162  126.532 1.00 125.90 ? 2126 SER A O     1 
ATOM   2078 C  CB    . SER A 1 335 ? 88.863  84.261  124.885 1.00 114.87 ? 2126 SER A CB    1 
ATOM   2079 O  OG    . SER A 1 335 ? 89.201  84.829  123.632 1.00 113.42 ? 2126 SER A OG    1 
ATOM   2080 N  N     . PHE A 1 336 ? 92.169  85.187  125.304 1.00 114.14 ? 2127 PHE A N     1 
ATOM   2081 C  CA    . PHE A 1 336 ? 93.069  86.328  125.433 1.00 114.22 ? 2127 PHE A CA    1 
ATOM   2082 C  C     . PHE A 1 336 ? 92.589  87.528  124.626 1.00 113.90 ? 2127 PHE A C     1 
ATOM   2083 O  O     . PHE A 1 336 ? 92.839  88.674  125.017 1.00 110.33 ? 2127 PHE A O     1 
ATOM   2084 C  CB    . PHE A 1 336 ? 94.479  85.936  124.995 1.00 108.05 ? 2127 PHE A CB    1 
ATOM   2085 C  CG    . PHE A 1 336 ? 95.299  85.301  126.078 1.00 108.33 ? 2127 PHE A CG    1 
ATOM   2086 C  CD1   . PHE A 1 336 ? 95.094  83.980  126.435 1.00 116.54 ? 2127 PHE A CD1   1 
ATOM   2087 C  CD2   . PHE A 1 336 ? 96.282  86.023  126.731 1.00 100.37 ? 2127 PHE A CD2   1 
ATOM   2088 C  CE1   . PHE A 1 336 ? 95.851  83.393  127.429 1.00 116.45 ? 2127 PHE A CE1   1 
ATOM   2089 C  CE2   . PHE A 1 336 ? 97.041  85.441  127.725 1.00 102.74 ? 2127 PHE A CE2   1 
ATOM   2090 C  CZ    . PHE A 1 336 ? 96.826  84.125  128.074 1.00 111.88 ? 2127 PHE A CZ    1 
ATOM   2091 N  N     . THR A 1 337 ? 91.911  87.288  123.501 1.00 114.77 ? 2128 THR A N     1 
ATOM   2092 C  CA    . THR A 1 337 ? 91.525  88.386  122.619 1.00 117.18 ? 2128 THR A CA    1 
ATOM   2093 C  C     . THR A 1 337 ? 90.533  89.325  123.296 1.00 123.47 ? 2128 THR A C     1 
ATOM   2094 O  O     . THR A 1 337 ? 90.607  90.547  123.121 1.00 126.71 ? 2128 THR A O     1 
ATOM   2095 C  CB    . THR A 1 337 ? 90.941  87.836  121.316 1.00 114.29 ? 2128 THR A CB    1 
ATOM   2096 O  OG1   . THR A 1 337 ? 89.531  87.629  121.465 1.00 116.26 ? 2128 THR A OG1   1 
ATOM   2097 C  CG2   . THR A 1 337 ? 91.605  86.518  120.951 1.00 109.72 ? 2128 THR A CG2   1 
ATOM   2098 N  N     . SER A 1 338 ? 89.601  88.777  124.072 1.00 122.58 ? 2129 SER A N     1 
ATOM   2099 C  CA    . SER A 1 338 ? 88.583  89.596  124.717 1.00 122.47 ? 2129 SER A CA    1 
ATOM   2100 C  C     . SER A 1 338 ? 89.203  90.399  125.854 1.00 123.15 ? 2129 SER A C     1 
ATOM   2101 O  O     . SER A 1 338 ? 89.752  89.827  126.802 1.00 122.83 ? 2129 SER A O     1 
ATOM   2102 C  CB    . SER A 1 338 ? 87.448  88.715  125.232 1.00 122.41 ? 2129 SER A CB    1 
ATOM   2103 O  OG    . SER A 1 338 ? 87.937  87.720  126.113 1.00 122.66 ? 2129 SER A OG    1 
ATOM   2104 N  N     . SER A 1 339 ? 89.113  91.728  125.758 1.00 122.76 ? 2130 SER A N     1 
ATOM   2105 C  CA    . SER A 1 339 ? 89.703  92.586  126.780 1.00 123.47 ? 2130 SER A CA    1 
ATOM   2106 C  C     . SER A 1 339 ? 88.932  92.518  128.091 1.00 127.54 ? 2130 SER A C     1 
ATOM   2107 O  O     . SER A 1 339 ? 89.534  92.629  129.166 1.00 126.84 ? 2130 SER A O     1 
ATOM   2108 C  CB    . SER A 1 339 ? 89.769  94.029  126.279 1.00 119.48 ? 2130 SER A CB    1 
ATOM   2109 O  OG    . SER A 1 339 ? 90.231  94.084  124.941 1.00 118.09 ? 2130 SER A OG    1 
ATOM   2110 N  N     . ASP A 1 340 ? 87.609  92.349  128.026 1.00 129.75 ? 2131 ASP A N     1 
ATOM   2111 C  CA    . ASP A 1 340 ? 86.811  92.286  129.247 1.00 129.73 ? 2131 ASP A CA    1 
ATOM   2112 C  C     . ASP A 1 340 ? 87.182  91.074  130.094 1.00 127.14 ? 2131 ASP A C     1 
ATOM   2113 O  O     . ASP A 1 340 ? 87.279  91.174  131.323 1.00 124.52 ? 2131 ASP A O     1 
ATOM   2114 C  CB    . ASP A 1 340 ? 85.320  92.277  128.901 1.00 129.02 ? 2131 ASP A CB    1 
ATOM   2115 C  CG    . ASP A 1 340 ? 85.016  91.511  127.625 1.00 123.92 ? 2131 ASP A CG    1 
ATOM   2116 O  OD1   . ASP A 1 340 ? 85.497  90.370  127.473 1.00 123.25 ? 2131 ASP A OD1   1 
ATOM   2117 O  OD2   . ASP A 1 340 ? 84.290  92.057  126.767 1.00 117.74 ? 2131 ASP A OD2   1 
ATOM   2118 N  N     . ASP A 1 341 ? 87.398  89.921  129.457 1.00 126.73 ? 2132 ASP A N     1 
ATOM   2119 C  CA    . ASP A 1 341 ? 87.791  88.729  130.202 1.00 131.16 ? 2132 ASP A CA    1 
ATOM   2120 C  C     . ASP A 1 341 ? 89.160  88.906  130.846 1.00 132.64 ? 2132 ASP A C     1 
ATOM   2121 O  O     . ASP A 1 341 ? 89.370  88.496  131.993 1.00 133.69 ? 2132 ASP A O     1 
ATOM   2122 C  CB    . ASP A 1 341 ? 87.784  87.509  129.284 1.00 129.05 ? 2132 ASP A CB    1 
ATOM   2123 C  CG    . ASP A 1 341 ? 88.671  86.392  129.795 1.00 130.21 ? 2132 ASP A CG    1 
ATOM   2124 O  OD1   . ASP A 1 341 ? 88.226  85.638  130.685 1.00 133.40 ? 2132 ASP A OD1   1 
ATOM   2125 O  OD2   . ASP A 1 341 ? 89.814  86.271  129.308 1.00 125.61 ? 2132 ASP A OD2   1 
ATOM   2126 N  N     . ILE A 1 342 ? 90.104  89.512  130.122 1.00 130.69 ? 2133 ILE A N     1 
ATOM   2127 C  CA    . ILE A 1 342 ? 91.429  89.759  130.683 1.00 128.93 ? 2133 ILE A CA    1 
ATOM   2128 C  C     . ILE A 1 342 ? 91.332  90.704  131.873 1.00 133.53 ? 2133 ILE A C     1 
ATOM   2129 O  O     . ILE A 1 342 ? 91.986  90.499  132.903 1.00 133.74 ? 2133 ILE A O     1 
ATOM   2130 C  CB    . ILE A 1 342 ? 92.377  90.305  129.599 1.00 127.84 ? 2133 ILE A CB    1 
ATOM   2131 C  CG1   . ILE A 1 342 ? 92.545  89.285  128.473 1.00 127.27 ? 2133 ILE A CG1   1 
ATOM   2132 C  CG2   . ILE A 1 342 ? 93.728  90.657  130.199 1.00 122.21 ? 2133 ILE A CG2   1 
ATOM   2133 C  CD1   . ILE A 1 342 ? 93.300  88.042  128.885 1.00 119.15 ? 2133 ILE A CD1   1 
ATOM   2134 N  N     . ALA A 1 343 ? 90.519  91.756  131.749 1.00 134.90 ? 2134 ALA A N     1 
ATOM   2135 C  CA    . ALA A 1 343 ? 90.347  92.694  132.854 1.00 132.99 ? 2134 ALA A CA    1 
ATOM   2136 C  C     . ALA A 1 343 ? 89.720  92.015  134.065 1.00 133.58 ? 2134 ALA A C     1 
ATOM   2137 O  O     . ALA A 1 343 ? 90.122  92.269  135.206 1.00 131.42 ? 2134 ALA A O     1 
ATOM   2138 C  CB    . ALA A 1 343 ? 89.500  93.884  132.405 1.00 128.79 ? 2134 ALA A CB    1 
ATOM   2139 N  N     . GLU A 1 344 ? 88.726  91.154  133.837 1.00 133.94 ? 2135 GLU A N     1 
ATOM   2140 C  CA    . GLU A 1 344 ? 88.091  90.448  134.946 1.00 133.71 ? 2135 GLU A CA    1 
ATOM   2141 C  C     . GLU A 1 344 ? 89.060  89.486  135.622 1.00 130.93 ? 2135 GLU A C     1 
ATOM   2142 O  O     . GLU A 1 344 ? 89.075  89.373  136.853 1.00 130.88 ? 2135 GLU A O     1 
ATOM   2143 C  CB    . GLU A 1 344 ? 86.852  89.702  134.452 1.00 134.24 ? 2135 GLU A CB    1 
ATOM   2144 C  CG    . GLU A 1 344 ? 85.673  90.604  134.122 1.00 135.93 ? 2135 GLU A CG    1 
ATOM   2145 C  CD    . GLU A 1 344 ? 84.463  89.829  133.640 1.00 134.41 ? 2135 GLU A CD    1 
ATOM   2146 O  OE1   . GLU A 1 344 ? 84.494  88.582  133.695 1.00 134.93 ? 2135 GLU A OE1   1 
ATOM   2147 O  OE2   . GLU A 1 344 ? 83.481  90.467  133.204 1.00 132.08 ? 2135 GLU A OE2   1 
ATOM   2148 N  N     . VAL A 1 345 ? 89.873  88.779  134.836 1.00 130.05 ? 2136 VAL A N     1 
ATOM   2149 C  CA    . VAL A 1 345 ? 90.799  87.803  135.401 1.00 134.11 ? 2136 VAL A CA    1 
ATOM   2150 C  C     . VAL A 1 345 ? 91.930  88.493  136.156 1.00 137.05 ? 2136 VAL A C     1 
ATOM   2151 O  O     . VAL A 1 345 ? 92.319  88.059  137.246 1.00 136.58 ? 2136 VAL A O     1 
ATOM   2152 C  CB    . VAL A 1 345 ? 91.331  86.882  134.287 1.00 130.83 ? 2136 VAL A CB    1 
ATOM   2153 C  CG1   . VAL A 1 345 ? 92.701  86.325  134.650 1.00 125.49 ? 2136 VAL A CG1   1 
ATOM   2154 C  CG2   . VAL A 1 345 ? 90.345  85.756  134.017 1.00 127.23 ? 2136 VAL A CG2   1 
ATOM   2155 N  N     . LEU A 1 346 ? 92.466  89.580  135.604 1.00 135.34 ? 2137 LEU A N     1 
ATOM   2156 C  CA    . LEU A 1 346 ? 93.644  90.223  136.174 1.00 134.64 ? 2137 LEU A CA    1 
ATOM   2157 C  C     . LEU A 1 346 ? 93.292  91.202  137.290 1.00 138.41 ? 2137 LEU A C     1 
ATOM   2158 O  O     . LEU A 1 346 ? 93.827  91.101  138.399 1.00 139.34 ? 2137 LEU A O     1 
ATOM   2159 C  CB    . LEU A 1 346 ? 94.427  90.941  135.070 1.00 132.56 ? 2137 LEU A CB    1 
ATOM   2160 C  CG    . LEU A 1 346 ? 95.794  91.512  135.452 1.00 132.30 ? 2137 LEU A CG    1 
ATOM   2161 C  CD1   . LEU A 1 346 ? 96.785  90.391  135.721 1.00 129.77 ? 2137 LEU A CD1   1 
ATOM   2162 C  CD2   . LEU A 1 346 ? 96.310  92.439  134.364 1.00 125.05 ? 2137 LEU A CD2   1 
ATOM   2163 N  N     . PHE A 1 347 ? 92.399  92.154  137.015 1.00 138.46 ? 2138 PHE A N     1 
ATOM   2164 C  CA    . PHE A 1 347 ? 92.097  93.195  137.993 1.00 140.22 ? 2138 PHE A CA    1 
ATOM   2165 C  C     . PHE A 1 347 ? 91.236  92.675  139.139 1.00 140.74 ? 2138 PHE A C     1 
ATOM   2166 O  O     . PHE A 1 347 ? 91.452  93.048  140.297 1.00 137.27 ? 2138 PHE A O     1 
ATOM   2167 C  CB    . PHE A 1 347 ? 91.409  94.374  137.307 1.00 137.83 ? 2138 PHE A CB    1 
ATOM   2168 C  CG    . PHE A 1 347 ? 92.297  95.126  136.358 1.00 139.70 ? 2138 PHE A CG    1 
ATOM   2169 C  CD1   . PHE A 1 347 ? 93.103  96.156  136.811 1.00 139.87 ? 2138 PHE A CD1   1 
ATOM   2170 C  CD2   . PHE A 1 347 ? 92.324  94.803  135.012 1.00 138.30 ? 2138 PHE A CD2   1 
ATOM   2171 C  CE1   . PHE A 1 347 ? 93.921  96.851  135.940 1.00 140.03 ? 2138 PHE A CE1   1 
ATOM   2172 C  CE2   . PHE A 1 347 ? 93.140  95.494  134.135 1.00 134.82 ? 2138 PHE A CE2   1 
ATOM   2173 C  CZ    . PHE A 1 347 ? 93.939  96.519  134.600 1.00 137.34 ? 2138 PHE A CZ    1 
ATOM   2174 N  N     . LEU A 1 348 ? 90.258  91.819  138.842 1.00 139.43 ? 2139 LEU A N     1 
ATOM   2175 C  CA    . LEU A 1 348 ? 89.312  91.368  139.859 1.00 134.35 ? 2139 LEU A CA    1 
ATOM   2176 C  C     . LEU A 1 348 ? 89.765  90.073  140.528 1.00 133.88 ? 2139 LEU A C     1 
ATOM   2177 O  O     . LEU A 1 348 ? 89.951  90.031  141.749 1.00 132.92 ? 2139 LEU A O     1 
ATOM   2178 C  CB    . LEU A 1 348 ? 87.921  91.192  139.239 1.00 131.01 ? 2139 LEU A CB    1 
ATOM   2179 C  CG    . LEU A 1 348 ? 87.173  92.472  138.861 1.00 129.66 ? 2139 LEU A CG    1 
ATOM   2180 C  CD1   . LEU A 1 348 ? 85.858  92.140  138.174 1.00 123.53 ? 2139 LEU A CD1   1 
ATOM   2181 C  CD2   . LEU A 1 348 ? 86.936  93.335  140.089 1.00 129.13 ? 2139 LEU A CD2   1 
ATOM   2182 N  N     . GLU A 1 349 ? 89.939  89.009  139.741 1.00 134.75 ? 2140 GLU A N     1 
ATOM   2183 C  CA    . GLU A 1 349 ? 90.291  87.714  140.316 1.00 135.82 ? 2140 GLU A CA    1 
ATOM   2184 C  C     . GLU A 1 349 ? 91.665  87.749  140.973 1.00 135.73 ? 2140 GLU A C     1 
ATOM   2185 O  O     . GLU A 1 349 ? 91.853  87.201  142.065 1.00 139.19 ? 2140 GLU A O     1 
ATOM   2186 C  CB    . GLU A 1 349 ? 90.239  86.629  139.241 1.00 134.62 ? 2140 GLU A CB    1 
ATOM   2187 C  CG    . GLU A 1 349 ? 88.841  86.332  138.725 1.00 137.13 ? 2140 GLU A CG    1 
ATOM   2188 C  CD    . GLU A 1 349 ? 88.744  84.973  138.060 1.00 137.38 ? 2140 GLU A CD    1 
ATOM   2189 O  OE1   . GLU A 1 349 ? 89.763  84.252  138.027 1.00 134.13 ? 2140 GLU A OE1   1 
ATOM   2190 O  OE2   . GLU A 1 349 ? 87.649  84.625  137.571 1.00 134.97 ? 2140 GLU A OE2   1 
ATOM   2191 N  N     . LEU A 1 350 ? 92.637  88.388  140.327 1.00 132.80 ? 2141 LEU A N     1 
ATOM   2192 C  CA    . LEU A 1 350 ? 93.999  88.436  140.843 1.00 136.53 ? 2141 LEU A CA    1 
ATOM   2193 C  C     . LEU A 1 350 ? 94.281  89.684  141.670 1.00 138.26 ? 2141 LEU A C     1 
ATOM   2194 O  O     . LEU A 1 350 ? 95.397  89.830  142.179 1.00 135.98 ? 2141 LEU A O     1 
ATOM   2195 C  CB    . LEU A 1 350 ? 95.002  88.339  139.690 1.00 135.23 ? 2141 LEU A CB    1 
ATOM   2196 C  CG    . LEU A 1 350 ? 95.570  86.947  139.396 1.00 128.56 ? 2141 LEU A CG    1 
ATOM   2197 C  CD1   . LEU A 1 350 ? 96.522  86.518  140.501 1.00 123.42 ? 2141 LEU A CD1   1 
ATOM   2198 C  CD2   . LEU A 1 350 ? 94.462  85.921  139.209 1.00 131.22 ? 2141 LEU A CD2   1 
ATOM   2199 N  N     . LYS A 1 351 ? 93.302  90.581  141.811 1.00 138.47 ? 2142 LYS A N     1 
ATOM   2200 C  CA    . LYS A 1 351 ? 93.402  91.748  142.691 1.00 141.38 ? 2142 LYS A CA    1 
ATOM   2201 C  C     . LYS A 1 351 ? 94.586  92.643  142.326 1.00 142.29 ? 2142 LYS A C     1 
ATOM   2202 O  O     . LYS A 1 351 ? 95.251  93.207  143.197 1.00 140.50 ? 2142 LYS A O     1 
ATOM   2203 C  CB    . LYS A 1 351 ? 93.480  91.322  144.159 1.00 142.40 ? 2142 LYS A CB    1 
ATOM   2204 C  CG    . LYS A 1 351 ? 92.366  90.387  144.594 1.00 137.25 ? 2142 LYS A CG    1 
ATOM   2205 C  CD    . LYS A 1 351 ? 92.785  89.555  145.795 1.00 129.37 ? 2142 LYS A CD    1 
ATOM   2206 C  CE    . LYS A 1 351 ? 94.016  88.719  145.485 1.00 126.33 ? 2142 LYS A CE    1 
ATOM   2207 N  NZ    . LYS A 1 351 ? 93.813  87.851  144.292 1.00 127.70 ? 2142 LYS A NZ    1 
ATOM   2208 N  N     . LEU A 1 352 ? 94.855  92.776  141.032 1.00 141.99 ? 2143 LEU A N     1 
ATOM   2209 C  CA    . LEU A 1 352 ? 95.885  93.703  140.590 1.00 139.44 ? 2143 LEU A CA    1 
ATOM   2210 C  C     . LEU A 1 352 ? 95.389  95.140  140.753 1.00 139.24 ? 2143 LEU A C     1 
ATOM   2211 O  O     . LEU A 1 352 ? 94.195  95.407  140.580 1.00 134.03 ? 2143 LEU A O     1 
ATOM   2212 C  CB    . LEU A 1 352 ? 96.261  93.436  139.132 1.00 136.06 ? 2143 LEU A CB    1 
ATOM   2213 C  CG    . LEU A 1 352 ? 97.471  92.532  138.863 1.00 129.10 ? 2143 LEU A CG    1 
ATOM   2214 C  CD1   . LEU A 1 352 ? 98.737  93.087  139.497 1.00 123.46 ? 2143 LEU A CD1   1 
ATOM   2215 C  CD2   . LEU A 1 352 ? 97.211  91.119  139.352 1.00 128.22 ? 2143 LEU A CD2   1 
ATOM   2216 N  N     . PRO A 1 353 ? 96.269  96.079  141.088 1.00 141.97 ? 2144 PRO A N     1 
ATOM   2217 C  CA    . PRO A 1 353 ? 95.835  97.466  141.308 1.00 144.52 ? 2144 PRO A CA    1 
ATOM   2218 C  C     . PRO A 1 353 ? 95.348  98.100  140.018 1.00 144.41 ? 2144 PRO A C     1 
ATOM   2219 O  O     . PRO A 1 353 ? 96.116  98.240  139.054 1.00 141.60 ? 2144 PRO A O     1 
ATOM   2220 C  CB    . PRO A 1 353 ? 97.105  98.161  141.825 1.00 139.97 ? 2144 PRO A CB    1 
ATOM   2221 C  CG    . PRO A 1 353 ? 98.003  97.055  142.277 1.00 132.66 ? 2144 PRO A CG    1 
ATOM   2222 C  CD    . PRO A 1 353 ? 97.699  95.898  141.384 1.00 132.98 ? 2144 PRO A CD    1 
ATOM   2223 N  N     . PRO A 1 354 ? 94.080  98.496  139.960 1.00 146.04 ? 2145 PRO A N     1 
ATOM   2224 C  CA    . PRO A 1 354 ? 93.557  99.128  138.745 1.00 146.51 ? 2145 PRO A CA    1 
ATOM   2225 C  C     . PRO A 1 354 ? 94.092  100.541 138.572 1.00 144.27 ? 2145 PRO A C     1 
ATOM   2226 O  O     . PRO A 1 354 ? 94.524  101.200 139.520 1.00 139.42 ? 2145 PRO A O     1 
ATOM   2227 C  CB    . PRO A 1 354 ? 92.038  99.136  138.965 1.00 144.35 ? 2145 PRO A CB    1 
ATOM   2228 C  CG    . PRO A 1 354 ? 91.794  98.294  140.196 1.00 143.24 ? 2145 PRO A CG    1 
ATOM   2229 C  CD    . PRO A 1 354 ? 93.048  98.367  140.999 1.00 142.40 ? 2145 PRO A CD    1 
ATOM   2230 N  N     . ASN A 1 355 ? 94.059  101.001 137.326 1.00 144.41 ? 2146 ASN A N     1 
ATOM   2231 C  CA    . ASN A 1 355 ? 94.464  102.356 136.989 1.00 142.69 ? 2146 ASN A CA    1 
ATOM   2232 C  C     . ASN A 1 355 ? 93.256  103.289 136.991 1.00 144.09 ? 2146 ASN A C     1 
ATOM   2233 O  O     . ASN A 1 355 ? 92.105  102.858 136.889 1.00 144.86 ? 2146 ASN A O     1 
ATOM   2234 C  CB    . ASN A 1 355 ? 95.158  102.389 135.626 1.00 142.42 ? 2146 ASN A CB    1 
ATOM   2235 C  CG    . ASN A 1 355 ? 94.195  102.174 134.473 1.00 142.59 ? 2146 ASN A CG    1 
ATOM   2236 O  OD1   . ASN A 1 355 ? 93.243  101.400 134.576 1.00 140.82 ? 2146 ASN A OD1   1 
ATOM   2237 N  ND2   . ASN A 1 355 ? 94.444  102.857 133.362 1.00 138.28 ? 2146 ASN A ND2   1 
ATOM   2238 N  N     . ARG A 1 356 ? 93.538  104.588 137.116 1.00 139.74 ? 2147 ARG A N     1 
ATOM   2239 C  CA    . ARG A 1 356 ? 92.467  105.580 137.166 1.00 135.63 ? 2147 ARG A CA    1 
ATOM   2240 C  C     . ARG A 1 356 ? 91.700  105.634 135.850 1.00 139.93 ? 2147 ARG A C     1 
ATOM   2241 O  O     . ARG A 1 356 ? 90.463  105.646 135.840 1.00 139.37 ? 2147 ARG A O     1 
ATOM   2242 C  CB    . ARG A 1 356 ? 93.041  106.953 137.514 1.00 123.73 ? 2147 ARG A CB    1 
ATOM   2243 N  N     . GLU A 1 357 ? 92.415  105.663 134.730 1.00 142.44 ? 2148 GLU A N     1 
ATOM   2244 C  CA    . GLU A 1 357 ? 91.785  105.719 133.415 1.00 140.27 ? 2148 GLU A CA    1 
ATOM   2245 C  C     . GLU A 1 357 ? 92.761  105.298 132.321 1.00 140.76 ? 2148 GLU A C     1 
ATOM   2246 O  O     . GLU A 1 357 ? 92.515  104.337 131.593 1.00 140.41 ? 2148 GLU A O     1 
ATOM   2247 C  CB    . GLU A 1 357 ? 91.255  107.127 133.130 1.00 136.93 ? 2148 GLU A CB    1 
ATOM   2248 C  CG    . GLU A 1 357 ? 90.718  107.314 131.719 1.00 133.07 ? 2148 GLU A CG    1 
ATOM   2249 C  CD    . GLU A 1 357 ? 89.445  106.528 131.469 1.00 129.46 ? 2148 GLU A CD    1 
ATOM   2250 O  OE1   . GLU A 1 357 ? 88.679  106.310 132.431 1.00 130.69 ? 2148 GLU A OE1   1 
ATOM   2251 O  OE2   . GLU A 1 357 ? 89.211  106.127 130.309 1.00 123.91 ? 2148 GLU A OE2   1 
ATOM   2252 N  N     . GLY A 1 383 ? 81.005  96.381  130.212 1.00 117.58 ? 2174 GLY A N     1 
ATOM   2253 C  CA    . GLY A 1 383 ? 82.054  96.818  129.310 1.00 130.75 ? 2174 GLY A CA    1 
ATOM   2254 C  C     . GLY A 1 383 ? 82.786  98.054  129.795 1.00 139.19 ? 2174 GLY A C     1 
ATOM   2255 O  O     . GLY A 1 383 ? 82.224  98.867  130.530 1.00 140.25 ? 2174 GLY A O     1 
ATOM   2256 N  N     . ARG A 1 384 ? 84.048  98.185  129.383 1.00 141.08 ? 2175 ARG A N     1 
ATOM   2257 C  CA    . ARG A 1 384 ? 84.908  99.317  129.730 1.00 136.03 ? 2175 ARG A CA    1 
ATOM   2258 C  C     . ARG A 1 384 ? 85.088  99.473  131.236 1.00 135.79 ? 2175 ARG A C     1 
ATOM   2259 O  O     . ARG A 1 384 ? 85.360  100.577 131.719 1.00 133.39 ? 2175 ARG A O     1 
ATOM   2260 C  CB    . ARG A 1 384 ? 84.379  100.624 129.126 1.00 136.35 ? 2175 ARG A CB    1 
ATOM   2261 C  CG    . ARG A 1 384 ? 83.970  100.514 127.668 1.00 137.76 ? 2175 ARG A CG    1 
ATOM   2262 C  CD    . ARG A 1 384 ? 84.994  101.165 126.754 1.00 139.27 ? 2175 ARG A CD    1 
ATOM   2263 N  NE    . ARG A 1 384 ? 84.412  101.549 125.474 1.00 136.69 ? 2175 ARG A NE    1 
ATOM   2264 C  CZ    . ARG A 1 384 ? 84.152  100.704 124.486 1.00 139.74 ? 2175 ARG A CZ    1 
ATOM   2265 N  NH1   . ARG A 1 384 ? 84.419  99.413  124.592 1.00 146.11 ? 2175 ARG A NH1   1 
ATOM   2266 N  NH2   . ARG A 1 384 ? 83.614  101.167 123.361 1.00 136.10 ? 2175 ARG A NH2   1 
ATOM   2267 N  N     . GLN A 1 385 ? 84.934  98.384  131.993 1.00 138.59 ? 2176 GLN A N     1 
ATOM   2268 C  CA    . GLN A 1 385 ? 85.114  98.458  133.440 1.00 135.54 ? 2176 GLN A CA    1 
ATOM   2269 C  C     . GLN A 1 385 ? 86.557  98.788  133.803 1.00 134.87 ? 2176 GLN A C     1 
ATOM   2270 O  O     . GLN A 1 385 ? 86.807  99.589  134.711 1.00 135.97 ? 2176 GLN A O     1 
ATOM   2271 C  CB    . GLN A 1 385 ? 84.678  97.145  134.090 1.00 134.01 ? 2176 GLN A CB    1 
ATOM   2272 C  CG    . GLN A 1 385 ? 85.224  95.898  133.412 1.00 134.28 ? 2176 GLN A CG    1 
ATOM   2273 C  CD    . GLN A 1 385 ? 84.196  95.215  132.531 1.00 129.52 ? 2176 GLN A CD    1 
ATOM   2274 O  OE1   . GLN A 1 385 ? 83.114  95.750  132.290 1.00 133.91 ? 2176 GLN A OE1   1 
ATOM   2275 N  NE2   . GLN A 1 385 ? 84.530  94.025  132.045 1.00 119.95 ? 2176 GLN A NE2   1 
ATOM   2276 N  N     . PHE A 1 386 ? 87.517  98.185  133.105 1.00 132.65 ? 2177 PHE A N     1 
ATOM   2277 C  CA    . PHE A 1 386 ? 88.930  98.432  133.345 1.00 130.84 ? 2177 PHE A CA    1 
ATOM   2278 C  C     . PHE A 1 386 ? 89.653  98.546  132.012 1.00 131.97 ? 2177 PHE A C     1 
ATOM   2279 O  O     . PHE A 1 386 ? 89.214  97.992  131.000 1.00 135.77 ? 2177 PHE A O     1 
ATOM   2280 C  CB    . PHE A 1 386 ? 89.564  97.322  134.194 1.00 134.05 ? 2177 PHE A CB    1 
ATOM   2281 C  CG    . PHE A 1 386 ? 89.099  97.309  135.621 1.00 139.54 ? 2177 PHE A CG    1 
ATOM   2282 C  CD1   . PHE A 1 386 ? 89.213  98.440  136.412 1.00 137.12 ? 2177 PHE A CD1   1 
ATOM   2283 C  CD2   . PHE A 1 386 ? 88.545  96.165  136.173 1.00 139.41 ? 2177 PHE A CD2   1 
ATOM   2284 C  CE1   . PHE A 1 386 ? 88.785  98.431  137.726 1.00 134.90 ? 2177 PHE A CE1   1 
ATOM   2285 C  CE2   . PHE A 1 386 ? 88.115  96.150  137.486 1.00 134.72 ? 2177 PHE A CE2   1 
ATOM   2286 C  CZ    . PHE A 1 386 ? 88.236  97.284  138.264 1.00 134.00 ? 2177 PHE A CZ    1 
ATOM   2287 N  N     . SER A 1 387 ? 90.768  99.270  132.021 1.00 133.60 ? 2178 SER A N     1 
ATOM   2288 C  CA    . SER A 1 387 ? 91.598  99.452  130.838 1.00 128.33 ? 2178 SER A CA    1 
ATOM   2289 C  C     . SER A 1 387 ? 92.743  98.449  130.865 1.00 122.67 ? 2178 SER A C     1 
ATOM   2290 O  O     . SER A 1 387 ? 93.402  98.278  131.896 1.00 125.53 ? 2178 SER A O     1 
ATOM   2291 C  CB    . SER A 1 387 ? 92.143  100.879 130.766 1.00 129.41 ? 2178 SER A CB    1 
ATOM   2292 O  OG    . SER A 1 387 ? 91.097  101.815 130.569 1.00 128.39 ? 2178 SER A OG    1 
ATOM   2293 N  N     . THR A 1 388 ? 92.975  97.790  129.731 1.00 114.95 ? 2179 THR A N     1 
ATOM   2294 C  CA    . THR A 1 388 ? 94.004  96.763  129.640 1.00 111.23 ? 2179 THR A CA    1 
ATOM   2295 C  C     . THR A 1 388 ? 95.026  97.165  128.581 1.00 107.22 ? 2179 THR A C     1 
ATOM   2296 O  O     . THR A 1 388 ? 95.406  96.361  127.724 1.00 98.66  ? 2179 THR A O     1 
ATOM   2297 C  CB    . THR A 1 388 ? 93.372  95.404  129.322 1.00 103.58 ? 2179 THR A CB    1 
ATOM   2298 O  OG1   . THR A 1 388 ? 92.213  95.221  130.143 1.00 111.40 ? 2179 THR A OG1   1 
ATOM   2299 C  CG2   . THR A 1 388 ? 94.343  94.273  129.631 1.00 99.71  ? 2179 THR A CG2   1 
ATOM   2300 N  N     . SER A 1 389 ? 95.461  98.422  128.623 1.00 110.55 ? 2180 SER A N     1 
ATOM   2301 C  CA    . SER A 1 389 ? 96.386  98.942  127.628 1.00 103.79 ? 2180 SER A CA    1 
ATOM   2302 C  C     . SER A 1 389 ? 97.787  98.369  127.850 1.00 103.05 ? 2180 SER A C     1 
ATOM   2303 O  O     . SER A 1 389 ? 98.054  97.644  128.812 1.00 107.13 ? 2180 SER A O     1 
ATOM   2304 C  CB    . SER A 1 389 ? 96.404  100.468 127.671 1.00 104.24 ? 2180 SER A CB    1 
ATOM   2305 O  OG    . SER A 1 389 ? 95.143  101.003 127.307 1.00 101.48 ? 2180 SER A OG    1 
ATOM   2306 N  N     . LYS A 1 390 ? 98.693  98.698  126.927 1.00 100.82 ? 2181 LYS A N     1 
ATOM   2307 C  CA    . LYS A 1 390 ? 100.060 98.194  127.012 1.00 99.18  ? 2181 LYS A CA    1 
ATOM   2308 C  C     . LYS A 1 390 ? 100.801 98.783  128.206 1.00 105.33 ? 2181 LYS A C     1 
ATOM   2309 O  O     . LYS A 1 390 ? 101.549 98.073  128.889 1.00 102.42 ? 2181 LYS A O     1 
ATOM   2310 C  CB    . LYS A 1 390 ? 100.807 98.496  125.713 1.00 93.28  ? 2181 LYS A CB    1 
ATOM   2311 C  CG    . LYS A 1 390 ? 102.321 98.438  125.827 1.00 92.41  ? 2181 LYS A CG    1 
ATOM   2312 C  CD    . LYS A 1 390 ? 102.854 97.092  125.367 1.00 91.50  ? 2181 LYS A CD    1 
ATOM   2313 C  CE    . LYS A 1 390 ? 104.155 97.244  124.599 1.00 88.83  ? 2181 LYS A CE    1 
ATOM   2314 N  NZ    . LYS A 1 390 ? 104.761 95.923  124.278 1.00 84.43  ? 2181 LYS A NZ    1 
ATOM   2315 N  N     . ASP A 1 391 ? 100.614 100.079 128.470 1.00 110.25 ? 2182 ASP A N     1 
ATOM   2316 C  CA    . ASP A 1 391 ? 101.372 100.736 129.533 1.00 111.82 ? 2182 ASP A CA    1 
ATOM   2317 C  C     . ASP A 1 391 ? 100.993 100.207 130.914 1.00 112.26 ? 2182 ASP A C     1 
ATOM   2318 O  O     . ASP A 1 391 ? 101.869 99.996  131.762 1.00 107.37 ? 2182 ASP A O     1 
ATOM   2319 C  CB    . ASP A 1 391 ? 101.193 102.257 129.458 1.00 106.95 ? 2182 ASP A CB    1 
ATOM   2320 C  CG    . ASP A 1 391 ? 99.754  102.684 129.186 1.00 105.40 ? 2182 ASP A CG    1 
ATOM   2321 O  OD1   . ASP A 1 391 ? 98.818  101.881 129.372 1.00 106.74 ? 2182 ASP A OD1   1 
ATOM   2322 O  OD2   . ASP A 1 391 ? 99.561  103.848 128.777 1.00 102.96 ? 2182 ASP A OD2   1 
ATOM   2323 N  N     . VAL A 1 392 ? 99.701  99.982  131.162 1.00 113.04 ? 2183 VAL A N     1 
ATOM   2324 C  CA    . VAL A 1 392 ? 99.291  99.464  132.464 1.00 110.85 ? 2183 VAL A CA    1 
ATOM   2325 C  C     . VAL A 1 392 ? 99.791  98.036  132.651 1.00 108.66 ? 2183 VAL A C     1 
ATOM   2326 O  O     . VAL A 1 392 ? 100.194 97.645  133.752 1.00 108.31 ? 2183 VAL A O     1 
ATOM   2327 C  CB    . VAL A 1 392 ? 97.763  99.576  132.638 1.00 109.46 ? 2183 VAL A CB    1 
ATOM   2328 C  CG1   . VAL A 1 392 ? 97.321  101.023 132.485 1.00 114.75 ? 2183 VAL A CG1   1 
ATOM   2329 C  CG2   . VAL A 1 392 ? 97.026  98.692  131.646 1.00 101.62 ? 2183 VAL A CG2   1 
ATOM   2330 N  N     . LEU A 1 393 ? 99.794  97.243  131.577 1.00 107.23 ? 2184 LEU A N     1 
ATOM   2331 C  CA    . LEU A 1 393 ? 100.337 95.891  131.656 1.00 105.69 ? 2184 LEU A CA    1 
ATOM   2332 C  C     . LEU A 1 393 ? 101.834 95.918  131.940 1.00 107.77 ? 2184 LEU A C     1 
ATOM   2333 O  O     . LEU A 1 393 ? 102.337 95.113  132.734 1.00 110.60 ? 2184 LEU A O     1 
ATOM   2334 C  CB    . LEU A 1 393 ? 100.046 95.135  130.360 1.00 104.25 ? 2184 LEU A CB    1 
ATOM   2335 C  CG    . LEU A 1 393 ? 98.776  94.280  130.296 1.00 97.71  ? 2184 LEU A CG    1 
ATOM   2336 C  CD1   . LEU A 1 393 ? 99.039  92.887  130.830 1.00 94.58  ? 2184 LEU A CD1   1 
ATOM   2337 C  CD2   . LEU A 1 393 ? 97.629  94.931  131.054 1.00 97.91  ? 2184 LEU A CD2   1 
ATOM   2338 N  N     . ASN A 1 394 ? 102.560 96.839  131.302 1.00 103.57 ? 2185 ASN A N     1 
ATOM   2339 C  CA    . ASN A 1 394 ? 103.988 96.977  131.569 1.00 102.09 ? 2185 ASN A CA    1 
ATOM   2340 C  C     . ASN A 1 394 ? 104.238 97.380  133.016 1.00 102.47 ? 2185 ASN A C     1 
ATOM   2341 O  O     . ASN A 1 394 ? 105.165 96.874  133.659 1.00 105.50 ? 2185 ASN A O     1 
ATOM   2342 C  CB    . ASN A 1 394 ? 104.603 98.000  130.614 1.00 104.60 ? 2185 ASN A CB    1 
ATOM   2343 C  CG    . ASN A 1 394 ? 105.253 97.354  129.407 1.00 106.01 ? 2185 ASN A CG    1 
ATOM   2344 O  OD1   . ASN A 1 394 ? 105.953 96.350  129.526 1.00 104.68 ? 2185 ASN A OD1   1 
ATOM   2345 N  ND2   . ASN A 1 394 ? 105.021 97.929  128.232 1.00 109.00 ? 2185 ASN A ND2   1 
ATOM   2346 N  N     . LYS A 1 395 ? 103.421 98.294  133.544 1.00 101.93 ? 2186 LYS A N     1 
ATOM   2347 C  CA    . LYS A 1 395 ? 103.555 98.685  134.943 1.00 109.54 ? 2186 LYS A CA    1 
ATOM   2348 C  C     . LYS A 1 395 ? 103.263 97.514  135.873 1.00 111.17 ? 2186 LYS A C     1 
ATOM   2349 O  O     . LYS A 1 395 ? 103.918 97.354  136.909 1.00 103.57 ? 2186 LYS A O     1 
ATOM   2350 C  CB    . LYS A 1 395 ? 102.627 99.859  135.254 1.00 106.56 ? 2186 LYS A CB    1 
ATOM   2351 C  CG    . LYS A 1 395 ? 103.056 101.177 134.629 1.00 103.24 ? 2186 LYS A CG    1 
ATOM   2352 C  CD    . LYS A 1 395 ? 102.409 102.357 135.334 1.00 99.21  ? 2186 LYS A CD    1 
ATOM   2353 C  CE    . LYS A 1 395 ? 100.899 102.196 135.406 1.00 99.60  ? 2186 LYS A CE    1 
ATOM   2354 N  NZ    . LYS A 1 395 ? 100.263 103.278 136.207 1.00 94.86  ? 2186 LYS A NZ    1 
ATOM   2355 N  N     . LEU A 1 396 ? 102.284 96.684  135.518 1.00 114.59 ? 2187 LEU A N     1 
ATOM   2356 C  CA    . LEU A 1 396 ? 101.898 95.543  136.338 1.00 110.46 ? 2187 LEU A CA    1 
ATOM   2357 C  C     . LEU A 1 396 ? 102.778 94.320  136.113 1.00 109.92 ? 2187 LEU A C     1 
ATOM   2358 O  O     . LEU A 1 396 ? 102.581 93.307  136.792 1.00 110.68 ? 2187 LEU A O     1 
ATOM   2359 C  CB    . LEU A 1 396 ? 100.436 95.177  136.065 1.00 109.49 ? 2187 LEU A CB    1 
ATOM   2360 C  CG    . LEU A 1 396 ? 99.365  95.789  136.972 1.00 107.31 ? 2187 LEU A CG    1 
ATOM   2361 C  CD1   . LEU A 1 396 ? 99.494  97.303  137.041 1.00 101.71 ? 2187 LEU A CD1   1 
ATOM   2362 C  CD2   . LEU A 1 396 ? 97.980  95.393  136.488 1.00 117.17 ? 2187 LEU A CD2   1 
ATOM   2363 N  N     . LYS A 1 397 ? 103.732 94.386  135.179 1.00 110.15 ? 2188 LYS A N     1 
ATOM   2364 C  CA    . LYS A 1 397 ? 104.591 93.235  134.909 1.00 105.84 ? 2188 LYS A CA    1 
ATOM   2365 C  C     . LYS A 1 397 ? 105.386 92.826  136.143 1.00 106.21 ? 2188 LYS A C     1 
ATOM   2366 O  O     . LYS A 1 397 ? 105.515 91.633  136.440 1.00 108.76 ? 2188 LYS A O     1 
ATOM   2367 C  CB    . LYS A 1 397 ? 105.541 93.548  133.753 1.00 104.88 ? 2188 LYS A CB    1 
ATOM   2368 C  CG    . LYS A 1 397 ? 104.957 93.315  132.370 1.00 108.01 ? 2188 LYS A CG    1 
ATOM   2369 C  CD    . LYS A 1 397 ? 106.054 93.176  131.323 1.00 101.76 ? 2188 LYS A CD    1 
ATOM   2370 C  CE    . LYS A 1 397 ? 107.184 94.167  131.558 1.00 87.86  ? 2188 LYS A CE    1 
ATOM   2371 N  NZ    . LYS A 1 397 ? 108.288 93.991  130.576 1.00 71.44  ? 2188 LYS A NZ    1 
ATOM   2372 N  N     . ALA A 1 398 ? 105.938 93.802  136.867 1.00 109.66 ? 2189 ALA A N     1 
ATOM   2373 C  CA    . ALA A 1 398 ? 106.752 93.487  138.036 1.00 110.76 ? 2189 ALA A CA    1 
ATOM   2374 C  C     . ALA A 1 398 ? 105.916 92.870  139.151 1.00 114.52 ? 2189 ALA A C     1 
ATOM   2375 O  O     . ALA A 1 398 ? 106.379 91.961  139.849 1.00 113.22 ? 2189 ALA A O     1 
ATOM   2376 C  CB    . ALA A 1 398 ? 107.464 94.745  138.532 1.00 104.81 ? 2189 ALA A CB    1 
ATOM   2377 N  N     . LEU A 1 399 ? 104.687 93.356  139.337 1.00 115.06 ? 2190 LEU A N     1 
ATOM   2378 C  CA    . LEU A 1 399 ? 103.866 92.897  140.454 1.00 109.01 ? 2190 LEU A CA    1 
ATOM   2379 C  C     . LEU A 1 399 ? 103.506 91.421  140.323 1.00 101.06 ? 2190 LEU A C     1 
ATOM   2380 O  O     . LEU A 1 399 ? 103.575 90.673  141.305 1.00 92.24  ? 2190 LEU A O     1 
ATOM   2381 C  CB    . LEU A 1 399 ? 102.600 93.748  140.556 1.00 108.74 ? 2190 LEU A CB    1 
ATOM   2382 C  CG    . LEU A 1 399 ? 102.727 95.079  141.300 1.00 107.61 ? 2190 LEU A CG    1 
ATOM   2383 C  CD1   . LEU A 1 399 ? 103.309 96.155  140.395 1.00 105.66 ? 2190 LEU A CD1   1 
ATOM   2384 C  CD2   . LEU A 1 399 ? 101.379 95.513  141.853 1.00 111.20 ? 2190 LEU A CD2   1 
ATOM   2385 N  N     . HIS A 1 400 ? 103.121 90.982  139.125 1.00 104.79 ? 2191 HIS A N     1 
ATOM   2386 C  CA    . HIS A 1 400 ? 102.681 89.611  138.916 1.00 106.43 ? 2191 HIS A CA    1 
ATOM   2387 C  C     . HIS A 1 400 ? 103.245 89.069  137.610 1.00 113.64 ? 2191 HIS A C     1 
ATOM   2388 O  O     . HIS A 1 400 ? 103.344 89.810  136.621 1.00 114.62 ? 2191 HIS A O     1 
ATOM   2389 C  CB    . HIS A 1 400 ? 101.149 89.523  138.901 1.00 108.42 ? 2191 HIS A CB    1 
ATOM   2390 C  CG    . HIS A 1 400 ? 100.617 88.161  139.224 1.00 110.73 ? 2191 HIS A CG    1 
ATOM   2391 N  ND1   . HIS A 1 400 ? 100.577 87.140  138.300 1.00 113.72 ? 2191 HIS A ND1   1 
ATOM   2392 C  CD2   . HIS A 1 400 ? 100.111 87.651  140.371 1.00 111.23 ? 2191 HIS A CD2   1 
ATOM   2393 C  CE1   . HIS A 1 400 ? 100.066 86.060  138.862 1.00 116.16 ? 2191 HIS A CE1   1 
ATOM   2394 N  NE2   . HIS A 1 400 ? 99.775  86.343  140.119 1.00 115.22 ? 2191 HIS A NE2   1 
ATOM   2395 N  N     . PRO A 1 401 ? 103.644 87.795  137.581 1.00 115.90 ? 2192 PRO A N     1 
ATOM   2396 C  CA    . PRO A 1 401 ? 104.136 87.213  136.321 1.00 115.10 ? 2192 PRO A CA    1 
ATOM   2397 C  C     . PRO A 1 401 ? 103.094 87.152  135.216 1.00 109.17 ? 2192 PRO A C     1 
ATOM   2398 O  O     . PRO A 1 401 ? 103.455 87.257  134.038 1.00 105.25 ? 2192 PRO A O     1 
ATOM   2399 C  CB    . PRO A 1 401 ? 104.593 85.807  136.740 1.00 118.40 ? 2192 PRO A CB    1 
ATOM   2400 C  CG    . PRO A 1 401 ? 103.881 85.535  138.030 1.00 112.85 ? 2192 PRO A CG    1 
ATOM   2401 C  CD    . PRO A 1 401 ? 103.771 86.860  138.710 1.00 110.69 ? 2192 PRO A CD    1 
ATOM   2402 N  N     . LEU A 1 402 ? 101.816 86.977  135.558 1.00 112.14 ? 2193 LEU A N     1 
ATOM   2403 C  CA    . LEU A 1 402 ? 100.791 86.764  134.535 1.00 112.20 ? 2193 LEU A CA    1 
ATOM   2404 C  C     . LEU A 1 402 ? 100.649 87.930  133.563 1.00 105.97 ? 2193 LEU A C     1 
ATOM   2405 O  O     . LEU A 1 402 ? 100.563 87.678  132.348 1.00 98.51  ? 2193 LEU A O     1 
ATOM   2406 C  CB    . LEU A 1 402 ? 99.453  86.433  135.204 1.00 113.79 ? 2193 LEU A CB    1 
ATOM   2407 C  CG    . LEU A 1 402 ? 98.237  86.422  134.274 1.00 105.55 ? 2193 LEU A CG    1 
ATOM   2408 C  CD1   . LEU A 1 402 ? 98.319  85.260  133.296 1.00 100.25 ? 2193 LEU A CD1   1 
ATOM   2409 C  CD2   . LEU A 1 402 ? 96.944  86.369  135.071 1.00 114.34 ? 2193 LEU A CD2   1 
ATOM   2410 N  N     . PRO A 1 403 ? 100.587 89.197  133.996 1.00 108.54 ? 2194 PRO A N     1 
ATOM   2411 C  CA    . PRO A 1 403 ? 100.505 90.286  133.008 1.00 103.88 ? 2194 PRO A CA    1 
ATOM   2412 C  C     . PRO A 1 403 ? 101.678 90.321  132.047 1.00 97.07  ? 2194 PRO A C     1 
ATOM   2413 O  O     . PRO A 1 403 ? 101.497 90.695  130.882 1.00 92.26  ? 2194 PRO A O     1 
ATOM   2414 C  CB    . PRO A 1 403 ? 100.446 91.553  133.876 1.00 105.95 ? 2194 PRO A CB    1 
ATOM   2415 C  CG    . PRO A 1 403 ? 100.832 91.128  135.243 1.00 106.05 ? 2194 PRO A CG    1 
ATOM   2416 C  CD    . PRO A 1 403 ? 100.415 89.707  135.366 1.00 110.94 ? 2194 PRO A CD    1 
ATOM   2417 N  N     . GLY A 1 404 ? 102.877 89.941  132.491 1.00 102.13 ? 2195 GLY A N     1 
ATOM   2418 C  CA    . GLY A 1 404 ? 103.998 89.863  131.570 1.00 101.25 ? 2195 GLY A CA    1 
ATOM   2419 C  C     . GLY A 1 404 ? 103.780 88.834  130.477 1.00 92.45  ? 2195 GLY A C     1 
ATOM   2420 O  O     . GLY A 1 404 ? 104.057 89.091  129.302 1.00 91.74  ? 2195 GLY A O     1 
ATOM   2421 N  N     . LEU A 1 405 ? 103.269 87.658  130.848 1.00 91.39  ? 2196 LEU A N     1 
ATOM   2422 C  CA    . LEU A 1 405 ? 102.958 86.639  129.851 1.00 84.07  ? 2196 LEU A CA    1 
ATOM   2423 C  C     . LEU A 1 405 ? 101.846 87.102  128.919 1.00 83.79  ? 2196 LEU A C     1 
ATOM   2424 O  O     . LEU A 1 405 ? 101.887 86.828  127.715 1.00 87.06  ? 2196 LEU A O     1 
ATOM   2425 C  CB    . LEU A 1 405 ? 102.577 85.328  130.537 1.00 87.49  ? 2196 LEU A CB    1 
ATOM   2426 C  CG    . LEU A 1 405 ? 103.425 84.930  131.746 1.00 93.38  ? 2196 LEU A CG    1 
ATOM   2427 C  CD1   . LEU A 1 405 ? 102.615 84.086  132.718 1.00 98.57  ? 2196 LEU A CD1   1 
ATOM   2428 C  CD2   . LEU A 1 405 ? 104.679 84.192  131.305 1.00 86.88  ? 2196 LEU A CD2   1 
ATOM   2429 N  N     . ILE A 1 406 ? 100.846 87.803  129.457 1.00 83.30  ? 2197 ILE A N     1 
ATOM   2430 C  CA    . ILE A 1 406 ? 99.767  88.320  128.617 1.00 82.32  ? 2197 ILE A CA    1 
ATOM   2431 C  C     . ILE A 1 406 ? 100.312 89.319  127.604 1.00 82.36  ? 2197 ILE A C     1 
ATOM   2432 O  O     . ILE A 1 406 ? 99.961  89.279  126.419 1.00 82.04  ? 2197 ILE A O     1 
ATOM   2433 C  CB    . ILE A 1 406 ? 98.662  88.943  129.489 1.00 89.95  ? 2197 ILE A CB    1 
ATOM   2434 C  CG1   . ILE A 1 406 ? 97.887  87.851  130.229 1.00 104.81 ? 2197 ILE A CG1   1 
ATOM   2435 C  CG2   . ILE A 1 406 ? 97.722  89.787  128.642 1.00 81.90  ? 2197 ILE A CG2   1 
ATOM   2436 C  CD1   . ILE A 1 406 ? 96.691  88.366  131.001 1.00 112.94 ? 2197 ILE A CD1   1 
ATOM   2437 N  N     . LEU A 1 407 ? 101.179 90.228  128.054 1.00 84.11  ? 2198 LEU A N     1 
ATOM   2438 C  CA    . LEU A 1 407 ? 101.754 91.218  127.150 1.00 79.89  ? 2198 LEU A CA    1 
ATOM   2439 C  C     . LEU A 1 407 ? 102.634 90.562  126.093 1.00 73.86  ? 2198 LEU A C     1 
ATOM   2440 O  O     . LEU A 1 407 ? 102.603 90.952  124.919 1.00 76.52  ? 2198 LEU A O     1 
ATOM   2441 C  CB    . LEU A 1 407 ? 102.550 92.252  127.945 1.00 84.77  ? 2198 LEU A CB    1 
ATOM   2442 C  CG    . LEU A 1 407 ? 102.689 93.623  127.286 1.00 90.29  ? 2198 LEU A CG    1 
ATOM   2443 C  CD1   . LEU A 1 407 ? 101.319 94.218  127.017 1.00 88.19  ? 2198 LEU A CD1   1 
ATOM   2444 C  CD2   . LEU A 1 407 ? 103.515 94.549  128.160 1.00 94.66  ? 2198 LEU A CD2   1 
ATOM   2445 N  N     . GLU A 1 408 ? 103.433 89.569  126.491 1.00 70.99  ? 2199 GLU A N     1 
ATOM   2446 C  CA    . GLU A 1 408 ? 104.262 88.867  125.517 1.00 66.74  ? 2199 GLU A CA    1 
ATOM   2447 C  C     . GLU A 1 408 ? 103.407 88.134  124.494 1.00 66.25  ? 2199 GLU A C     1 
ATOM   2448 O  O     . GLU A 1 408 ? 103.713 88.147  123.296 1.00 69.17  ? 2199 GLU A O     1 
ATOM   2449 C  CB    . GLU A 1 408 ? 105.207 87.897  126.226 1.00 71.42  ? 2199 GLU A CB    1 
ATOM   2450 C  CG    . GLU A 1 408 ? 106.407 88.571  126.870 1.00 83.73  ? 2199 GLU A CG    1 
ATOM   2451 C  CD    . GLU A 1 408 ? 107.374 89.141  125.849 1.00 91.44  ? 2199 GLU A CD    1 
ATOM   2452 O  OE1   . GLU A 1 408 ? 107.381 88.659  124.697 1.00 95.40  ? 2199 GLU A OE1   1 
ATOM   2453 O  OE2   . GLU A 1 408 ? 108.126 90.076  126.197 1.00 96.14  ? 2199 GLU A OE2   1 
ATOM   2454 N  N     . TRP A 1 409 ? 102.327 87.490  124.943 1.00 72.35  ? 2200 TRP A N     1 
ATOM   2455 C  CA    . TRP A 1 409 ? 101.434 86.821  124.006 1.00 75.23  ? 2200 TRP A CA    1 
ATOM   2456 C  C     . TRP A 1 409 ? 100.801 87.821  123.053 1.00 69.59  ? 2200 TRP A C     1 
ATOM   2457 O  O     . TRP A 1 409 ? 100.668 87.548  121.857 1.00 67.93  ? 2200 TRP A O     1 
ATOM   2458 C  CB    . TRP A 1 409 ? 100.350 86.047  124.754 1.00 79.75  ? 2200 TRP A CB    1 
ATOM   2459 C  CG    . TRP A 1 409 ? 99.392  85.351  123.835 1.00 77.00  ? 2200 TRP A CG    1 
ATOM   2460 C  CD1   . TRP A 1 409 ? 99.476  84.066  123.389 1.00 80.52  ? 2200 TRP A CD1   1 
ATOM   2461 C  CD2   . TRP A 1 409 ? 98.218  85.909  123.230 1.00 77.58  ? 2200 TRP A CD2   1 
ATOM   2462 N  NE1   . TRP A 1 409 ? 98.423  83.784  122.554 1.00 88.76  ? 2200 TRP A NE1   1 
ATOM   2463 C  CE2   . TRP A 1 409 ? 97.637  84.900  122.439 1.00 85.37  ? 2200 TRP A CE2   1 
ATOM   2464 C  CE3   . TRP A 1 409 ? 97.600  87.162  123.284 1.00 75.87  ? 2200 TRP A CE3   1 
ATOM   2465 C  CZ2   . TRP A 1 409 ? 96.469  85.104  121.708 1.00 84.98  ? 2200 TRP A CZ2   1 
ATOM   2466 C  CZ3   . TRP A 1 409 ? 96.443  87.364  122.556 1.00 81.66  ? 2200 TRP A CZ3   1 
ATOM   2467 C  CH2   . TRP A 1 409 ? 95.888  86.340  121.780 1.00 86.78  ? 2200 TRP A CH2   1 
ATOM   2468 N  N     . ARG A 1 410 ? 100.396 88.985  123.567 1.00 69.28  ? 2201 ARG A N     1 
ATOM   2469 C  CA    . ARG A 1 410 ? 99.816  90.010  122.706 1.00 66.17  ? 2201 ARG A CA    1 
ATOM   2470 C  C     . ARG A 1 410 ? 100.813 90.474  121.653 1.00 63.10  ? 2201 ARG A C     1 
ATOM   2471 O  O     . ARG A 1 410 ? 100.466 90.603  120.474 1.00 63.21  ? 2201 ARG A O     1 
ATOM   2472 C  CB    . ARG A 1 410 ? 99.340  91.194  123.546 1.00 64.54  ? 2201 ARG A CB    1 
ATOM   2473 C  CG    . ARG A 1 410 ? 97.902  91.091  124.014 1.00 58.29  ? 2201 ARG A CG    1 
ATOM   2474 C  CD    . ARG A 1 410 ? 97.247  92.458  124.021 1.00 53.98  ? 2201 ARG A CD    1 
ATOM   2475 N  NE    . ARG A 1 410 ? 96.075  92.503  124.885 1.00 54.80  ? 2201 ARG A NE    1 
ATOM   2476 C  CZ    . ARG A 1 410 ? 95.773  93.521  125.679 1.00 65.50  ? 2201 ARG A CZ    1 
ATOM   2477 N  NH1   . ARG A 1 410 ? 96.546  94.592  125.751 1.00 72.28  ? 2201 ARG A NH1   1 
ATOM   2478 N  NH2   . ARG A 1 410 ? 94.670  93.462  126.419 1.00 77.87  ? 2201 ARG A NH2   1 
ATOM   2479 N  N     . ARG A 1 411 ? 102.043 90.744  122.026 1.00 60.25  ? 2202 ARG A N     1 
ATOM   2480 C  CA    . ARG A 1 411 ? 102.980 91.112  120.963 1.00 55.85  ? 2202 ARG A CA    1 
ATOM   2481 C  C     . ARG A 1 411 ? 103.078 89.970  119.992 1.00 55.09  ? 2202 ARG A C     1 
ATOM   2482 O  O     . ARG A 1 411 ? 102.641 90.089  118.879 1.00 62.53  ? 2202 ARG A O     1 
ATOM   2483 C  CB    . ARG A 1 411 ? 104.396 91.254  121.491 1.00 58.35  ? 2202 ARG A CB    1 
ATOM   2484 C  CG    . ARG A 1 411 ? 105.472 91.013  120.447 1.00 63.04  ? 2202 ARG A CG    1 
ATOM   2485 C  CD    . ARG A 1 411 ? 106.854 90.938  121.055 1.00 70.65  ? 2202 ARG A CD    1 
ATOM   2486 N  NE    . ARG A 1 411 ? 107.555 92.200  120.892 1.00 79.89  ? 2202 ARG A NE    1 
ATOM   2487 C  CZ    . ARG A 1 411 ? 108.020 92.664  119.741 1.00 73.81  ? 2202 ARG A CZ    1 
ATOM   2488 N  NH1   . ARG A 1 411 ? 107.586 92.165  118.598 1.00 69.53  ? 2202 ARG A NH1   1 
ATOM   2489 N  NH2   . ARG A 1 411 ? 108.922 93.626  119.740 1.00 71.90  ? 2202 ARG A NH2   1 
ATOM   2490 N  N     . ILE A 1 412 ? 103.508 88.850  120.457 1.00 51.70  ? 2203 ILE A N     1 
ATOM   2491 C  CA    . ILE A 1 412 ? 103.829 87.813  119.485 1.00 52.57  ? 2203 ILE A CA    1 
ATOM   2492 C  C     . ILE A 1 412 ? 102.637 87.523  118.580 1.00 59.69  ? 2203 ILE A C     1 
ATOM   2493 O  O     . ILE A 1 412 ? 102.814 87.231  117.393 1.00 66.56  ? 2203 ILE A O     1 
ATOM   2494 C  CB    . ILE A 1 412 ? 104.339 86.544  120.188 1.00 47.76  ? 2203 ILE A CB    1 
ATOM   2495 C  CG1   . ILE A 1 412 ? 105.483 86.894  121.140 1.00 60.23  ? 2203 ILE A CG1   1 
ATOM   2496 C  CG2   . ILE A 1 412 ? 104.843 85.557  119.165 1.00 45.56  ? 2203 ILE A CG2   1 
ATOM   2497 C  CD1   . ILE A 1 412 ? 106.422 85.744  121.434 1.00 64.48  ? 2203 ILE A CD1   1 
ATOM   2498 N  N     . THR A 1 413 ? 101.409 87.613  119.097 1.00 60.01  ? 2204 THR A N     1 
ATOM   2499 C  CA    . THR A 1 413 ? 100.254 87.390  118.235 1.00 60.19  ? 2204 THR A CA    1 
ATOM   2500 C  C     . THR A 1 413 ? 100.029 88.564  117.289 1.00 58.57  ? 2204 THR A C     1 
ATOM   2501 O  O     . THR A 1 413 ? 99.534  88.367  116.174 1.00 55.73  ? 2204 THR A O     1 
ATOM   2502 C  CB    . THR A 1 413 ? 99.001  87.104  119.071 1.00 66.76  ? 2204 THR A CB    1 
ATOM   2503 O  OG1   . THR A 1 413 ? 98.050  86.386  118.275 1.00 61.29  ? 2204 THR A OG1   1 
ATOM   2504 C  CG2   . THR A 1 413 ? 98.357  88.387  119.578 1.00 67.60  ? 2204 THR A CG2   1 
ATOM   2505 N  N     . ASN A 1 414 ? 100.403 89.780  117.697 1.00 57.83  ? 2205 ASN A N     1 
ATOM   2506 C  CA    . ASN A 1 414 ? 100.392 90.900  116.763 1.00 50.79  ? 2205 ASN A CA    1 
ATOM   2507 C  C     . ASN A 1 414 ? 101.406 90.677  115.652 1.00 51.58  ? 2205 ASN A C     1 
ATOM   2508 O  O     . ASN A 1 414 ? 101.148 91.003  114.488 1.00 59.42  ? 2205 ASN A O     1 
ATOM   2509 C  CB    . ASN A 1 414 ? 100.672 92.207  117.508 1.00 44.85  ? 2205 ASN A CB    1 
ATOM   2510 C  CG    . ASN A 1 414 ? 101.303 93.267  116.623 1.00 45.40  ? 2205 ASN A CG    1 
ATOM   2511 O  OD1   . ASN A 1 414 ? 102.507 93.244  116.362 1.00 41.68  ? 2205 ASN A OD1   1 
ATOM   2512 N  ND2   . ASN A 1 414 ? 100.490 94.206  116.157 1.00 53.92  ? 2205 ASN A ND2   1 
ATOM   2513 N  N     . ALA A 1 415 ? 102.570 90.126  115.997 1.00 49.47  ? 2206 ALA A N     1 
ATOM   2514 C  CA    . ALA A 1 415 ? 103.558 89.795  114.974 1.00 50.36  ? 2206 ALA A CA    1 
ATOM   2515 C  C     . ALA A 1 415 ? 103.060 88.684  114.054 1.00 54.02  ? 2206 ALA A C     1 
ATOM   2516 O  O     . ALA A 1 415 ? 103.340 88.693  112.850 1.00 57.18  ? 2206 ALA A O     1 
ATOM   2517 C  CB    . ALA A 1 415 ? 104.881 89.399  115.629 1.00 45.80  ? 2206 ALA A CB    1 
ATOM   2518 N  N     . ILE A 1 416 ? 102.327 87.714  114.602 1.00 53.38  ? 2207 ILE A N     1 
ATOM   2519 C  CA    . ILE A 1 416 ? 101.907 86.555  113.818 1.00 53.55  ? 2207 ILE A CA    1 
ATOM   2520 C  C     . ILE A 1 416 ? 100.629 86.786  113.016 1.00 57.49  ? 2207 ILE A C     1 
ATOM   2521 O  O     . ILE A 1 416 ? 100.349 86.016  112.086 1.00 62.99  ? 2207 ILE A O     1 
ATOM   2522 C  CB    . ILE A 1 416 ? 101.727 85.319  114.721 1.00 55.39  ? 2207 ILE A CB    1 
ATOM   2523 C  CG1   . ILE A 1 416 ? 101.940 84.030  113.924 1.00 55.72  ? 2207 ILE A CG1   1 
ATOM   2524 C  CG2   . ILE A 1 416 ? 100.345 85.300  115.340 1.00 57.64  ? 2207 ILE A CG2   1 
ATOM   2525 C  CD1   . ILE A 1 416 ? 103.383 83.679  113.695 1.00 58.60  ? 2207 ILE A CD1   1 
ATOM   2526 N  N     . THR A 1 417 ? 99.845  87.814  113.339 1.00 56.34  ? 2208 THR A N     1 
ATOM   2527 C  CA    . THR A 1 417 ? 98.622  88.097  112.597 1.00 55.06  ? 2208 THR A CA    1 
ATOM   2528 C  C     . THR A 1 417 ? 98.730  89.340  111.728 1.00 52.01  ? 2208 THR A C     1 
ATOM   2529 O  O     . THR A 1 417 ? 98.367  89.302  110.549 1.00 53.52  ? 2208 THR A O     1 
ATOM   2530 C  CB    . THR A 1 417 ? 97.428  88.244  113.552 1.00 55.98  ? 2208 THR A CB    1 
ATOM   2531 O  OG1   . THR A 1 417 ? 97.641  89.356  114.430 1.00 55.34  ? 2208 THR A OG1   1 
ATOM   2532 C  CG2   . THR A 1 417 ? 97.234  86.977  114.369 1.00 62.21  ? 2208 THR A CG2   1 
ATOM   2533 N  N     . LYS A 1 418 ? 99.221  90.449  112.280 1.00 50.38  ? 2209 LYS A N     1 
ATOM   2534 C  CA    . LYS A 1 418 ? 99.316  91.691  111.527 1.00 45.53  ? 2209 LYS A CA    1 
ATOM   2535 C  C     . LYS A 1 418 ? 100.541 91.753  110.626 1.00 48.70  ? 2209 LYS A C     1 
ATOM   2536 O  O     . LYS A 1 418 ? 100.645 92.682  109.818 1.00 55.00  ? 2209 LYS A O     1 
ATOM   2537 C  CB    . LYS A 1 418 ? 99.333  92.886  112.483 1.00 47.78  ? 2209 LYS A CB    1 
ATOM   2538 C  CG    . LYS A 1 418 ? 97.992  93.195  113.121 1.00 59.05  ? 2209 LYS A CG    1 
ATOM   2539 C  CD    . LYS A 1 418 ? 97.899  94.660  113.513 1.00 71.49  ? 2209 LYS A CD    1 
ATOM   2540 C  CE    . LYS A 1 418 ? 96.734  94.908  114.456 1.00 85.36  ? 2209 LYS A CE    1 
ATOM   2541 N  NZ    . LYS A 1 418 ? 96.091  93.639  114.895 1.00 76.63  ? 2209 LYS A NZ    1 
ATOM   2542 N  N     . VAL A 1 419 ? 101.468 90.804  110.742 1.00 44.15  ? 2210 VAL A N     1 
ATOM   2543 C  CA    . VAL A 1 419 ? 102.696 90.841  109.956 1.00 40.00  ? 2210 VAL A CA    1 
ATOM   2544 C  C     . VAL A 1 419 ? 102.879 89.538  109.190 1.00 47.37  ? 2210 VAL A C     1 
ATOM   2545 O  O     . VAL A 1 419 ? 103.106 89.549  107.976 1.00 55.45  ? 2210 VAL A O     1 
ATOM   2546 C  CB    . VAL A 1 419 ? 103.914 91.128  110.849 1.00 34.72  ? 2210 VAL A CB    1 
ATOM   2547 C  CG1   . VAL A 1 419 ? 105.200 90.845  110.092 1.00 38.72  ? 2210 VAL A CG1   1 
ATOM   2548 C  CG2   . VAL A 1 419 ? 103.877 92.566  111.334 1.00 35.96  ? 2210 VAL A CG2   1 
ATOM   2549 N  N     . VAL A 1 420 ? 102.794 88.408  109.894 1.00 48.68  ? 2211 VAL A N     1 
ATOM   2550 C  CA    . VAL A 1 420 ? 103.031 87.114  109.255 1.00 50.14  ? 2211 VAL A CA    1 
ATOM   2551 C  C     . VAL A 1 420 ? 101.988 86.854  108.175 1.00 57.07  ? 2211 VAL A C     1 
ATOM   2552 O  O     . VAL A 1 420 ? 102.317 86.454  107.052 1.00 59.54  ? 2211 VAL A O     1 
ATOM   2553 C  CB    . VAL A 1 420 ? 103.045 85.992  110.308 1.00 49.99  ? 2211 VAL A CB    1 
ATOM   2554 C  CG1   . VAL A 1 420 ? 102.612 84.668  109.692 1.00 53.07  ? 2211 VAL A CG1   1 
ATOM   2555 C  CG2   . VAL A 1 420 ? 104.417 85.870  110.930 1.00 53.17  ? 2211 VAL A CG2   1 
ATOM   2556 N  N     . PHE A 1 421 ? 100.715 87.075  108.499 1.00 54.67  ? 2212 PHE A N     1 
ATOM   2557 C  CA    . PHE A 1 421 ? 99.656  86.837  107.521 1.00 54.01  ? 2212 PHE A CA    1 
ATOM   2558 C  C     . PHE A 1 421 ? 99.742  87.760  106.312 1.00 54.20  ? 2212 PHE A C     1 
ATOM   2559 O  O     . PHE A 1 421 ? 99.641  87.258  105.180 1.00 63.21  ? 2212 PHE A O     1 
ATOM   2560 C  CB    . PHE A 1 421 ? 98.287  86.928  108.205 1.00 58.30  ? 2212 PHE A CB    1 
ATOM   2561 C  CG    . PHE A 1 421 ? 97.618  85.599  108.395 1.00 63.05  ? 2212 PHE A CG    1 
ATOM   2562 C  CD1   . PHE A 1 421 ? 96.800  85.075  107.409 1.00 59.18  ? 2212 PHE A CD1   1 
ATOM   2563 C  CD2   . PHE A 1 421 ? 97.810  84.871  109.558 1.00 64.24  ? 2212 PHE A CD2   1 
ATOM   2564 C  CE1   . PHE A 1 421 ? 96.182  83.852  107.580 1.00 64.64  ? 2212 PHE A CE1   1 
ATOM   2565 C  CE2   . PHE A 1 421 ? 97.195  83.647  109.735 1.00 61.58  ? 2212 PHE A CE2   1 
ATOM   2566 C  CZ    . PHE A 1 421 ? 96.380  83.137  108.744 1.00 62.99  ? 2212 PHE A CZ    1 
ATOM   2567 N  N     . PRO A 1 422 ? 99.897  89.084  106.454 1.00 47.69  ? 2213 PRO A N     1 
ATOM   2568 C  CA    . PRO A 1 422 ? 100.023 89.915  105.244 1.00 51.20  ? 2213 PRO A CA    1 
ATOM   2569 C  C     . PRO A 1 422 ? 101.205 89.541  104.367 1.00 52.29  ? 2213 PRO A C     1 
ATOM   2570 O  O     . PRO A 1 422 ? 101.091 89.587  103.137 1.00 58.46  ? 2213 PRO A O     1 
ATOM   2571 C  CB    . PRO A 1 422 ? 100.159 91.334  105.811 1.00 46.05  ? 2213 PRO A CB    1 
ATOM   2572 C  CG    . PRO A 1 422 ? 99.477  91.271  107.122 1.00 47.17  ? 2213 PRO A CG    1 
ATOM   2573 C  CD    . PRO A 1 422 ? 99.817  89.918  107.666 1.00 47.58  ? 2213 PRO A CD    1 
ATOM   2574 N  N     . LEU A 1 423 ? 102.340 89.167  104.960 1.00 41.69  ? 2214 LEU A N     1 
ATOM   2575 C  CA    . LEU A 1 423 ? 103.497 88.798  104.151 1.00 43.37  ? 2214 LEU A CA    1 
ATOM   2576 C  C     . LEU A 1 423 ? 103.270 87.478  103.427 1.00 47.97  ? 2214 LEU A C     1 
ATOM   2577 O  O     . LEU A 1 423 ? 103.569 87.358  102.234 1.00 54.62  ? 2214 LEU A O     1 
ATOM   2578 C  CB    . LEU A 1 423 ? 104.749 88.720  105.024 1.00 43.94  ? 2214 LEU A CB    1 
ATOM   2579 C  CG    . LEU A 1 423 ? 105.261 90.034  105.614 1.00 44.15  ? 2214 LEU A CG    1 
ATOM   2580 C  CD1   . LEU A 1 423 ? 106.639 89.844  106.225 1.00 35.78  ? 2214 LEU A CD1   1 
ATOM   2581 C  CD2   . LEU A 1 423 ? 105.285 91.122  104.559 1.00 46.36  ? 2214 LEU A CD2   1 
ATOM   2582 N  N     . GLN A 1 424 ? 102.738 86.477  104.131 1.00 46.48  ? 2215 GLN A N     1 
ATOM   2583 C  CA    . GLN A 1 424 ? 102.541 85.166  103.521 1.00 53.66  ? 2215 GLN A CA    1 
ATOM   2584 C  C     . GLN A 1 424 ? 101.412 85.181  102.500 1.00 53.63  ? 2215 GLN A C     1 
ATOM   2585 O  O     . GLN A 1 424 ? 101.419 84.381  101.559 1.00 58.47  ? 2215 GLN A O     1 
ATOM   2586 C  CB    . GLN A 1 424 ? 102.260 84.125  104.604 1.00 61.44  ? 2215 GLN A CB    1 
ATOM   2587 C  CG    . GLN A 1 424 ? 103.487 83.695  105.388 1.00 64.11  ? 2215 GLN A CG    1 
ATOM   2588 C  CD    . GLN A 1 424 ? 104.243 82.571  104.713 1.00 73.32  ? 2215 GLN A CD    1 
ATOM   2589 O  OE1   . GLN A 1 424 ? 103.696 81.854  103.876 1.00 75.86  ? 2215 GLN A OE1   1 
ATOM   2590 N  NE2   . GLN A 1 424 ? 105.510 82.411  105.074 1.00 71.28  ? 2215 GLN A NE2   1 
ATOM   2591 N  N     . ARG A 1 425 ? 100.436 86.075  102.670 1.00 50.57  ? 2216 ARG A N     1 
ATOM   2592 C  CA    . ARG A 1 425 ? 99.284  86.097  101.776 1.00 51.06  ? 2216 ARG A CA    1 
ATOM   2593 C  C     . ARG A 1 425 ? 99.672  86.548  100.374 1.00 56.73  ? 2216 ARG A C     1 
ATOM   2594 O  O     . ARG A 1 425 ? 99.196  85.984  99.382  1.00 56.88  ? 2216 ARG A O     1 
ATOM   2595 C  CB    . ARG A 1 425 ? 98.199  87.003  102.357 1.00 50.17  ? 2216 ARG A CB    1 
ATOM   2596 C  CG    . ARG A 1 425 ? 97.299  87.656  101.325 1.00 51.63  ? 2216 ARG A CG    1 
ATOM   2597 C  CD    . ARG A 1 425 ? 96.218  88.486  101.995 1.00 55.49  ? 2216 ARG A CD    1 
ATOM   2598 N  NE    . ARG A 1 425 ? 96.739  89.750  102.501 1.00 62.23  ? 2216 ARG A NE    1 
ATOM   2599 C  CZ    . ARG A 1 425 ? 96.016  90.651  103.150 1.00 73.11  ? 2216 ARG A CZ    1 
ATOM   2600 N  NH1   . ARG A 1 425 ? 94.730  90.458  103.397 1.00 71.36  ? 2216 ARG A NH1   1 
ATOM   2601 N  NH2   . ARG A 1 425 ? 96.596  91.775  103.561 1.00 79.73  ? 2216 ARG A NH2   1 
ATOM   2602 N  N     . GLU A 1 426 ? 100.539 87.552  100.268 1.00 58.27  ? 2217 GLU A N     1 
ATOM   2603 C  CA    . GLU A 1 426 ? 100.908 88.144  98.984  1.00 56.24  ? 2217 GLU A CA    1 
ATOM   2604 C  C     . GLU A 1 426 ? 102.416 88.014  98.774  1.00 45.50  ? 2217 GLU A C     1 
ATOM   2605 O  O     . GLU A 1 426 ? 103.197 88.886  99.160  1.00 34.75  ? 2217 GLU A O     1 
ATOM   2606 C  CB    . GLU A 1 426 ? 100.443 89.599  98.911  1.00 54.82  ? 2217 GLU A CB    1 
ATOM   2607 C  CG    . GLU A 1 426 ? 100.775 90.431  100.133 1.00 54.67  ? 2217 GLU A CG    1 
ATOM   2608 C  CD    . GLU A 1 426 ? 100.176 91.813  100.063 1.00 57.25  ? 2217 GLU A CD    1 
ATOM   2609 O  OE1   . GLU A 1 426 ? 99.250  92.106  100.848 1.00 57.15  ? 2217 GLU A OE1   1 
ATOM   2610 O  OE2   . GLU A 1 426 ? 100.621 92.601  99.206  1.00 56.59  ? 2217 GLU A OE2   1 
ATOM   2611 N  N     . LYS A 1 427 ? 102.820 86.910  98.154  1.00 49.21  ? 2218 LYS A N     1 
ATOM   2612 C  CA    . LYS A 1 427 ? 104.195 86.713  97.718  1.00 46.10  ? 2218 LYS A CA    1 
ATOM   2613 C  C     . LYS A 1 427 ? 104.165 86.162  96.302  1.00 48.33  ? 2218 LYS A C     1 
ATOM   2614 O  O     . LYS A 1 427 ? 103.440 85.203  96.023  1.00 54.74  ? 2218 LYS A O     1 
ATOM   2615 C  CB    . LYS A 1 427 ? 104.953 85.766  98.655  1.00 49.53  ? 2218 LYS A CB    1 
ATOM   2616 C  CG    . LYS A 1 427 ? 104.182 84.517  99.040  1.00 54.55  ? 2218 LYS A CG    1 
ATOM   2617 C  CD    . LYS A 1 427 ? 105.105 83.452  99.601  1.00 55.74  ? 2218 LYS A CD    1 
ATOM   2618 C  CE    . LYS A 1 427 ? 104.421 82.096  99.631  1.00 66.13  ? 2218 LYS A CE    1 
ATOM   2619 N  NZ    . LYS A 1 427 ? 103.190 82.116  100.467 1.00 70.25  ? 2218 LYS A NZ    1 
ATOM   2620 N  N     . CYS A 1 428 ? 104.942 86.771  95.413  1.00 46.00  ? 2219 CYS A N     1 
ATOM   2621 C  CA    . CYS A 1 428 ? 104.951 86.416  94.000  1.00 47.96  ? 2219 CYS A CA    1 
ATOM   2622 C  C     . CYS A 1 428 ? 106.186 85.579  93.701  1.00 54.46  ? 2219 CYS A C     1 
ATOM   2623 O  O     . CYS A 1 428 ? 107.315 86.059  93.842  1.00 59.04  ? 2219 CYS A O     1 
ATOM   2624 C  CB    . CYS A 1 428 ? 104.922 87.669  93.126  1.00 48.71  ? 2219 CYS A CB    1 
ATOM   2625 S  SG    . CYS A 1 428 ? 103.839 88.975  93.750  1.00 60.96  ? 2219 CYS A SG    1 
ATOM   2626 N  N     . LEU A 1 429 ? 105.968 84.334  93.285  1.00 59.80  ? 2220 LEU A N     1 
ATOM   2627 C  CA    . LEU A 1 429 ? 107.050 83.431  92.911  1.00 69.27  ? 2220 LEU A CA    1 
ATOM   2628 C  C     . LEU A 1 429 ? 107.318 83.596  91.420  1.00 73.19  ? 2220 LEU A C     1 
ATOM   2629 O  O     . LEU A 1 429 ? 106.546 83.112  90.586  1.00 82.72  ? 2220 LEU A O     1 
ATOM   2630 C  CB    . LEU A 1 429 ? 106.690 81.987  93.255  1.00 76.27  ? 2220 LEU A CB    1 
ATOM   2631 C  CG    . LEU A 1 429 ? 107.690 80.885  92.894  1.00 82.42  ? 2220 LEU A CG    1 
ATOM   2632 C  CD1   . LEU A 1 429 ? 107.838 79.903  94.046  1.00 76.07  ? 2220 LEU A CD1   1 
ATOM   2633 C  CD2   . LEU A 1 429 ? 107.266 80.152  91.629  1.00 76.57  ? 2220 LEU A CD2   1 
ATOM   2634 N  N     . ASN A 1 430 ? 108.405 84.284  91.084  1.00 67.51  ? 2221 ASN A N     1 
ATOM   2635 C  CA    . ASN A 1 430 ? 108.766 84.507  89.695  1.00 74.57  ? 2221 ASN A CA    1 
ATOM   2636 C  C     . ASN A 1 430 ? 109.992 83.685  89.333  1.00 84.47  ? 2221 ASN A C     1 
ATOM   2637 O  O     . ASN A 1 430 ? 111.014 83.764  90.028  1.00 82.39  ? 2221 ASN A O     1 
ATOM   2638 C  CB    . ASN A 1 430 ? 109.030 85.996  89.433  1.00 70.63  ? 2221 ASN A CB    1 
ATOM   2639 C  CG    . ASN A 1 430 ? 109.971 86.611  90.448  1.00 69.38  ? 2221 ASN A CG    1 
ATOM   2640 O  OD1   . ASN A 1 430 ? 111.186 86.433  90.378  1.00 71.30  ? 2221 ASN A OD1   1 
ATOM   2641 N  ND2   . ASN A 1 430 ? 109.410 87.340  91.404  1.00 62.81  ? 2221 ASN A ND2   1 
ATOM   2642 N  N     . PRO A 1 431 ? 109.923 82.872  88.276  1.00 91.60  ? 2222 PRO A N     1 
ATOM   2643 C  CA    . PRO A 1 431 ? 111.084 82.043  87.915  1.00 89.14  ? 2222 PRO A CA    1 
ATOM   2644 C  C     . PRO A 1 431 ? 112.270 82.843  87.406  1.00 84.12  ? 2222 PRO A C     1 
ATOM   2645 O  O     . PRO A 1 431 ? 113.380 82.300  87.356  1.00 83.49  ? 2222 PRO A O     1 
ATOM   2646 C  CB    . PRO A 1 431 ? 110.533 81.112  86.823  1.00 91.01  ? 2222 PRO A CB    1 
ATOM   2647 C  CG    . PRO A 1 431 ? 109.035 81.281  86.856  1.00 92.32  ? 2222 PRO A CG    1 
ATOM   2648 C  CD    . PRO A 1 431 ? 108.784 82.657  87.372  1.00 91.01  ? 2222 PRO A CD    1 
ATOM   2649 N  N     . PHE A 1 432 ? 112.073 84.106  87.023  1.00 81.91  ? 2223 PHE A N     1 
ATOM   2650 C  CA    . PHE A 1 432 ? 113.163 84.880  86.434  1.00 80.35  ? 2223 PHE A CA    1 
ATOM   2651 C  C     . PHE A 1 432 ? 114.271 85.128  87.450  1.00 78.91  ? 2223 PHE A C     1 
ATOM   2652 O  O     . PHE A 1 432 ? 115.459 84.988  87.134  1.00 77.60  ? 2223 PHE A O     1 
ATOM   2653 C  CB    . PHE A 1 432 ? 112.643 86.206  85.866  1.00 75.97  ? 2223 PHE A CB    1 
ATOM   2654 C  CG    . PHE A 1 432 ? 111.618 86.062  84.755  1.00 81.60  ? 2223 PHE A CG    1 
ATOM   2655 C  CD1   . PHE A 1 432 ? 110.928 84.878  84.536  1.00 86.59  ? 2223 PHE A CD1   1 
ATOM   2656 C  CD2   . PHE A 1 432 ? 111.360 87.131  83.917  1.00 76.93  ? 2223 PHE A CD2   1 
ATOM   2657 C  CE1   . PHE A 1 432 ? 110.001 84.772  83.517  1.00 87.44  ? 2223 PHE A CE1   1 
ATOM   2658 C  CE2   . PHE A 1 432 ? 110.434 87.031  82.896  1.00 82.20  ? 2223 PHE A CE2   1 
ATOM   2659 C  CZ    . PHE A 1 432 ? 109.755 85.850  82.696  1.00 85.12  ? 2223 PHE A CZ    1 
ATOM   2660 N  N     . LEU A 1 433 ? 113.906 85.498  88.675  1.00 78.99  ? 2224 LEU A N     1 
ATOM   2661 C  CA    . LEU A 1 433 ? 114.879 85.636  89.749  1.00 79.52  ? 2224 LEU A CA    1 
ATOM   2662 C  C     . LEU A 1 433 ? 115.123 84.332  90.495  1.00 80.04  ? 2224 LEU A C     1 
ATOM   2663 O  O     . LEU A 1 433 ? 116.045 84.269  91.314  1.00 77.55  ? 2224 LEU A O     1 
ATOM   2664 C  CB    . LEU A 1 433 ? 114.429 86.715  90.740  1.00 75.60  ? 2224 LEU A CB    1 
ATOM   2665 C  CG    . LEU A 1 433 ? 114.626 88.164  90.293  1.00 69.61  ? 2224 LEU A CG    1 
ATOM   2666 C  CD1   . LEU A 1 433 ? 113.323 88.757  89.785  1.00 68.08  ? 2224 LEU A CD1   1 
ATOM   2667 C  CD2   . LEU A 1 433 ? 115.189 88.998  91.430  1.00 54.02  ? 2224 LEU A CD2   1 
ATOM   2668 N  N     . GLY A 1 434 ? 114.325 83.299  90.234  1.00 79.58  ? 2225 GLY A N     1 
ATOM   2669 C  CA    . GLY A 1 434 ? 114.534 82.008  90.855  1.00 76.00  ? 2225 GLY A CA    1 
ATOM   2670 C  C     . GLY A 1 434 ? 114.126 81.910  92.305  1.00 65.85  ? 2225 GLY A C     1 
ATOM   2671 O  O     . GLY A 1 434 ? 114.453 80.914  92.956  1.00 60.55  ? 2225 GLY A O     1 
ATOM   2672 N  N     . MET A 1 435 ? 113.422 82.906  92.836  1.00 64.27  ? 2226 MET A N     1 
ATOM   2673 C  CA    . MET A 1 435 ? 113.031 82.883  94.238  1.00 56.85  ? 2226 MET A CA    1 
ATOM   2674 C  C     . MET A 1 435 ? 111.818 83.778  94.434  1.00 54.42  ? 2226 MET A C     1 
ATOM   2675 O  O     . MET A 1 435 ? 111.521 84.645  93.609  1.00 56.73  ? 2226 MET A O     1 
ATOM   2676 C  CB    . MET A 1 435 ? 114.181 83.328  95.144  1.00 60.24  ? 2226 MET A CB    1 
ATOM   2677 C  CG    . MET A 1 435 ? 115.002 84.469  94.575  1.00 67.22  ? 2226 MET A CG    1 
ATOM   2678 S  SD    . MET A 1 435 ? 114.260 86.074  94.908  1.00 71.40  ? 2226 MET A SD    1 
ATOM   2679 C  CE    . MET A 1 435 ? 114.845 86.356  96.573  1.00 54.48  ? 2226 MET A CE    1 
ATOM   2680 N  N     . GLU A 1 436 ? 111.124 83.555  95.546  1.00 57.42  ? 2227 GLU A N     1 
ATOM   2681 C  CA    . GLU A 1 436 ? 109.944 84.342  95.868  1.00 58.93  ? 2227 GLU A CA    1 
ATOM   2682 C  C     . GLU A 1 436 ? 110.330 85.765  96.251  1.00 51.05  ? 2227 GLU A C     1 
ATOM   2683 O  O     . GLU A 1 436 ? 111.395 86.015  96.822  1.00 49.16  ? 2227 GLU A O     1 
ATOM   2684 C  CB    . GLU A 1 436 ? 109.161 83.690  97.007  1.00 62.09  ? 2227 GLU A CB    1 
ATOM   2685 C  CG    . GLU A 1 436 ? 108.553 82.348  96.652  1.00 63.15  ? 2227 GLU A CG    1 
ATOM   2686 C  CD    . GLU A 1 436 ? 107.838 81.706  97.822  1.00 72.10  ? 2227 GLU A CD    1 
ATOM   2687 O  OE1   . GLU A 1 436 ? 108.071 82.136  98.970  1.00 72.11  ? 2227 GLU A OE1   1 
ATOM   2688 O  OE2   . GLU A 1 436 ? 107.041 80.772  97.594  1.00 70.41  ? 2227 GLU A OE2   1 
ATOM   2689 N  N     . ARG A 1 437 ? 109.452 86.707  95.915  1.00 48.38  ? 2228 ARG A N     1 
ATOM   2690 C  CA    . ARG A 1 437 ? 109.621 88.109  96.265  1.00 38.92  ? 2228 ARG A CA    1 
ATOM   2691 C  C     . ARG A 1 437 ? 108.273 88.657  96.711  1.00 37.29  ? 2228 ARG A C     1 
ATOM   2692 O  O     . ARG A 1 437 ? 107.251 87.967  96.659  1.00 46.81  ? 2228 ARG A O     1 
ATOM   2693 C  CB    . ARG A 1 437 ? 110.179 88.924  95.090  1.00 40.83  ? 2228 ARG A CB    1 
ATOM   2694 C  CG    . ARG A 1 437 ? 111.317 88.258  94.336  1.00 53.19  ? 2228 ARG A CG    1 
ATOM   2695 C  CD    . ARG A 1 437 ? 112.013 89.239  93.412  1.00 58.31  ? 2228 ARG A CD    1 
ATOM   2696 N  NE    . ARG A 1 437 ? 112.479 90.416  94.132  1.00 48.04  ? 2228 ARG A NE    1 
ATOM   2697 C  CZ    . ARG A 1 437 ? 113.599 90.466  94.838  1.00 38.50  ? 2228 ARG A CZ    1 
ATOM   2698 N  NH1   . ARG A 1 437 ? 114.404 89.421  94.931  1.00 41.38  ? 2228 ARG A NH1   1 
ATOM   2699 N  NH2   . ARG A 1 437 ? 113.920 91.593  95.466  1.00 40.39  ? 2228 ARG A NH2   1 
ATOM   2700 N  N     . ILE A 1 438 ? 108.273 89.908  97.161  1.00 30.38  ? 2229 ILE A N     1 
ATOM   2701 C  CA    . ILE A 1 438 ? 107.050 90.609  97.533  1.00 22.20  ? 2229 ILE A CA    1 
ATOM   2702 C  C     . ILE A 1 438 ? 107.123 92.021  96.973  1.00 25.63  ? 2229 ILE A C     1 
ATOM   2703 O  O     . ILE A 1 438 ? 108.121 92.720  97.172  1.00 33.45  ? 2229 ILE A O     1 
ATOM   2704 C  CB    . ILE A 1 438 ? 106.842 90.633  99.059  1.00 19.30  ? 2229 ILE A CB    1 
ATOM   2705 C  CG1   . ILE A 1 438 ? 105.807 91.686  99.443  1.00 19.77  ? 2229 ILE A CG1   1 
ATOM   2706 C  CG2   . ILE A 1 438 ? 108.151 90.885  99.777  1.00 31.05  ? 2229 ILE A CG2   1 
ATOM   2707 C  CD1   . ILE A 1 438 ? 105.578 91.780  100.924 1.00 31.02  ? 2229 ILE A CD1   1 
ATOM   2708 N  N     . TYR A 1 439 ? 106.071 92.441  96.271  1.00 27.94  ? 2230 TYR A N     1 
ATOM   2709 C  CA    . TYR A 1 439 ? 106.050 93.749  95.624  1.00 26.55  ? 2230 TYR A CA    1 
ATOM   2710 C  C     . TYR A 1 439 ? 105.068 94.664  96.340  1.00 25.12  ? 2230 TYR A C     1 
ATOM   2711 O  O     . TYR A 1 439 ? 103.855 94.588  96.091  1.00 31.38  ? 2230 TYR A O     1 
ATOM   2712 C  CB    . TYR A 1 439 ? 105.673 93.614  94.146  1.00 23.06  ? 2230 TYR A CB    1 
ATOM   2713 C  CG    . TYR A 1 439 ? 106.588 92.709  93.353  1.00 30.10  ? 2230 TYR A CG    1 
ATOM   2714 C  CD1   . TYR A 1 439 ? 107.802 93.171  92.871  1.00 32.76  ? 2230 TYR A CD1   1 
ATOM   2715 C  CD2   . TYR A 1 439 ? 106.235 91.396  93.082  1.00 33.25  ? 2230 TYR A CD2   1 
ATOM   2716 C  CE1   . TYR A 1 439 ? 108.642 92.350  92.146  1.00 33.47  ? 2230 TYR A CE1   1 
ATOM   2717 C  CE2   . TYR A 1 439 ? 107.068 90.567  92.357  1.00 39.61  ? 2230 TYR A CE2   1 
ATOM   2718 C  CZ    . TYR A 1 439 ? 108.270 91.051  91.892  1.00 39.77  ? 2230 TYR A CZ    1 
ATOM   2719 O  OH    . TYR A 1 439 ? 109.106 90.233  91.169  1.00 43.21  ? 2230 TYR A OH    1 
ATOM   2720 N  N     . PRO A 1 440 ? 105.529 95.540  97.225  1.00 20.23  ? 2231 PRO A N     1 
ATOM   2721 C  CA    . PRO A 1 440 ? 104.623 96.479  97.889  1.00 21.19  ? 2231 PRO A CA    1 
ATOM   2722 C  C     . PRO A 1 440 ? 104.254 97.623  96.956  1.00 20.63  ? 2231 PRO A C     1 
ATOM   2723 O  O     . PRO A 1 440 ? 104.859 97.824  95.904  1.00 21.65  ? 2231 PRO A O     1 
ATOM   2724 C  CB    . PRO A 1 440 ? 105.447 96.976  99.077  1.00 21.41  ? 2231 PRO A CB    1 
ATOM   2725 C  CG    . PRO A 1 440 ? 106.850 96.892  98.597  1.00 18.78  ? 2231 PRO A CG    1 
ATOM   2726 C  CD    . PRO A 1 440 ? 106.924 95.716  97.660  1.00 21.62  ? 2231 PRO A CD    1 
ATOM   2727 N  N     . VAL A 1 441 ? 103.238 98.378  97.360  1.00 25.96  ? 2232 VAL A N     1 
ATOM   2728 C  CA    . VAL A 1 441 ? 102.799 99.547  96.608  1.00 26.86  ? 2232 VAL A CA    1 
ATOM   2729 C  C     . VAL A 1 441 ? 103.324 100.780 97.330  1.00 26.96  ? 2232 VAL A C     1 
ATOM   2730 O  O     . VAL A 1 441 ? 102.980 101.024 98.491  1.00 34.42  ? 2232 VAL A O     1 
ATOM   2731 C  CB    . VAL A 1 441 ? 101.270 99.582  96.459  1.00 30.27  ? 2232 VAL A CB    1 
ATOM   2732 C  CG1   . VAL A 1 441 ? 100.769 101.014 96.322  1.00 29.34  ? 2232 VAL A CG1   1 
ATOM   2733 C  CG2   . VAL A 1 441 ? 100.836 98.743  95.268  1.00 31.30  ? 2232 VAL A CG2   1 
ATOM   2734 N  N     . SER A 1 442 ? 104.174 101.548 96.657  1.00 20.01  ? 2233 SER A N     1 
ATOM   2735 C  CA    . SER A 1 442 ? 104.810 102.698 97.284  1.00 19.67  ? 2233 SER A CA    1 
ATOM   2736 C  C     . SER A 1 442 ? 103.871 103.894 97.234  1.00 19.53  ? 2233 SER A C     1 
ATOM   2737 O  O     . SER A 1 442 ? 103.468 104.326 96.149  1.00 29.53  ? 2233 SER A O     1 
ATOM   2738 C  CB    . SER A 1 442 ? 106.127 103.020 96.586  1.00 23.52  ? 2233 SER A CB    1 
ATOM   2739 O  OG    . SER A 1 442 ? 105.962 103.033 95.180  1.00 21.58  ? 2233 SER A OG    1 
ATOM   2740 N  N     . GLN A 1 443 ? 103.524 104.430 98.400  1.00 19.01  ? 2234 GLN A N     1 
ATOM   2741 C  CA    . GLN A 1 443 ? 102.683 105.613 98.506  1.00 23.43  ? 2234 GLN A CA    1 
ATOM   2742 C  C     . GLN A 1 443 ? 103.538 106.768 99.004  1.00 31.30  ? 2234 GLN A C     1 
ATOM   2743 O  O     . GLN A 1 443 ? 104.155 106.673 100.071 1.00 38.62  ? 2234 GLN A O     1 
ATOM   2744 C  CB    . GLN A 1 443 ? 101.505 105.372 99.448  1.00 32.16  ? 2234 GLN A CB    1 
ATOM   2745 C  CG    . GLN A 1 443 ? 100.851 106.649 99.940  1.00 40.94  ? 2234 GLN A CG    1 
ATOM   2746 C  CD    . GLN A 1 443 ? 99.783  106.393 100.981 1.00 59.16  ? 2234 GLN A CD    1 
ATOM   2747 O  OE1   . GLN A 1 443 ? 99.360  105.256 101.185 1.00 68.11  ? 2234 GLN A OE1   1 
ATOM   2748 N  NE2   . GLN A 1 443 ? 99.341  107.453 101.648 1.00 54.84  ? 2234 GLN A NE2   1 
ATOM   2749 N  N     . SER A 1 444 ? 103.575 107.849 98.229  1.00 28.25  ? 2235 SER A N     1 
ATOM   2750 C  CA    . SER A 1 444 ? 104.355 109.032 98.563  1.00 27.23  ? 2235 SER A CA    1 
ATOM   2751 C  C     . SER A 1 444 ? 103.482 110.209 98.966  1.00 31.68  ? 2235 SER A C     1 
ATOM   2752 O  O     . SER A 1 444 ? 103.983 111.333 99.069  1.00 34.79  ? 2235 SER A O     1 
ATOM   2753 C  CB    . SER A 1 444 ? 105.246 109.426 97.386  1.00 24.35  ? 2235 SER A CB    1 
ATOM   2754 O  OG    . SER A 1 444 ? 105.733 108.279 96.716  1.00 26.27  ? 2235 SER A OG    1 
ATOM   2755 N  N     . HIS A 1 445 ? 102.187 109.983 99.193  1.00 35.92  ? 2236 HIS A N     1 
ATOM   2756 C  CA    . HIS A 1 445 ? 101.260 111.056 99.529  1.00 36.20  ? 2236 HIS A CA    1 
ATOM   2757 C  C     . HIS A 1 445 ? 101.151 111.289 101.029 1.00 32.59  ? 2236 HIS A C     1 
ATOM   2758 O  O     . HIS A 1 445 ? 100.116 111.774 101.506 1.00 36.12  ? 2236 HIS A O     1 
ATOM   2759 C  CB    . HIS A 1 445 ? 99.882  110.770 98.932  1.00 35.16  ? 2236 HIS A CB    1 
ATOM   2760 C  CG    . HIS A 1 445 ? 99.033  111.991 98.772  1.00 34.00  ? 2236 HIS A CG    1 
ATOM   2761 N  ND1   . HIS A 1 445 ? 99.300  112.964 97.833  1.00 29.74  ? 2236 HIS A ND1   1 
ATOM   2762 C  CD2   . HIS A 1 445 ? 97.933  112.407 99.442  1.00 39.93  ? 2236 HIS A CD2   1 
ATOM   2763 C  CE1   . HIS A 1 445 ? 98.398  113.924 97.928  1.00 35.60  ? 2236 HIS A CE1   1 
ATOM   2764 N  NE2   . HIS A 1 445 ? 97.555  113.609 98.895  1.00 43.37  ? 2236 HIS A NE2   1 
ATOM   2765 N  N     . THR A 1 446 ? 102.188 110.955 101.789 1.00 24.24  ? 2237 THR A N     1 
ATOM   2766 C  CA    . THR A 1 446 ? 102.173 111.239 103.213 1.00 26.33  ? 2237 THR A CA    1 
ATOM   2767 C  C     . THR A 1 446 ? 102.269 112.742 103.450 1.00 26.58  ? 2237 THR A C     1 
ATOM   2768 O  O     . THR A 1 446 ? 102.653 113.517 102.570 1.00 27.25  ? 2237 THR A O     1 
ATOM   2769 C  CB    . THR A 1 446 ? 103.320 110.523 103.919 1.00 31.30  ? 2237 THR A CB    1 
ATOM   2770 O  OG1   . THR A 1 446 ? 104.544 111.218 103.661 1.00 34.71  ? 2237 THR A OG1   1 
ATOM   2771 C  CG2   . THR A 1 446 ? 103.437 109.097 103.416 1.00 29.79  ? 2237 THR A CG2   1 
ATOM   2772 N  N     . ALA A 1 447 ? 101.911 113.152 104.662 1.00 27.31  ? 2238 ALA A N     1 
ATOM   2773 C  CA    . ALA A 1 447 ? 101.810 114.567 104.991 1.00 31.29  ? 2238 ALA A CA    1 
ATOM   2774 C  C     . ALA A 1 447 ? 103.152 115.213 105.304 1.00 30.69  ? 2238 ALA A C     1 
ATOM   2775 O  O     . ALA A 1 447 ? 103.201 116.432 105.497 1.00 40.74  ? 2238 ALA A O     1 
ATOM   2776 C  CB    . ALA A 1 447 ? 100.860 114.758 106.174 1.00 35.97  ? 2238 ALA A CB    1 
ATOM   2777 N  N     . THR A 1 448 ? 104.237 114.443 105.359 1.00 22.17  ? 2239 THR A N     1 
ATOM   2778 C  CA    . THR A 1 448 ? 105.547 114.978 105.708 1.00 22.85  ? 2239 THR A CA    1 
ATOM   2779 C  C     . THR A 1 448 ? 106.597 114.719 104.635 1.00 24.33  ? 2239 THR A C     1 
ATOM   2780 O  O     . THR A 1 448 ? 107.780 115.000 104.859 1.00 32.92  ? 2239 THR A O     1 
ATOM   2781 C  CB    . THR A 1 448 ? 106.008 114.403 107.051 1.00 31.67  ? 2239 THR A CB    1 
ATOM   2782 O  OG1   . THR A 1 448 ? 106.997 115.261 107.631 1.00 36.91  ? 2239 THR A OG1   1 
ATOM   2783 C  CG2   . THR A 1 448 ? 106.575 113.001 106.880 1.00 28.15  ? 2239 THR A CG2   1 
ATOM   2784 N  N     . GLY A 1 449 ? 106.199 114.222 103.468 1.00 23.83  ? 2240 GLY A N     1 
ATOM   2785 C  CA    . GLY A 1 449 ? 107.145 113.863 102.435 1.00 25.17  ? 2240 GLY A CA    1 
ATOM   2786 C  C     . GLY A 1 449 ? 107.728 112.478 102.572 1.00 25.67  ? 2240 GLY A C     1 
ATOM   2787 O  O     . GLY A 1 449 ? 108.526 112.071 101.719 1.00 27.28  ? 2240 GLY A O     1 
ATOM   2788 N  N     . ARG A 1 450 ? 107.352 111.743 103.612 1.00 21.13  ? 2241 ARG A N     1 
ATOM   2789 C  CA    . ARG A 1 450 ? 107.831 110.389 103.821 1.00 18.88  ? 2241 ARG A CA    1 
ATOM   2790 C  C     . ARG A 1 450 ? 107.268 109.458 102.751 1.00 28.05  ? 2241 ARG A C     1 
ATOM   2791 O  O     . ARG A 1 450 ? 106.306 109.781 102.052 1.00 39.05  ? 2241 ARG A O     1 
ATOM   2792 C  CB    . ARG A 1 450 ? 107.427 109.908 105.213 1.00 20.78  ? 2241 ARG A CB    1 
ATOM   2793 C  CG    . ARG A 1 450 ? 108.313 108.843 105.812 1.00 27.28  ? 2241 ARG A CG    1 
ATOM   2794 C  CD    . ARG A 1 450 ? 108.207 108.856 107.328 1.00 30.13  ? 2241 ARG A CD    1 
ATOM   2795 N  NE    . ARG A 1 450 ? 109.340 109.528 107.951 1.00 31.51  ? 2241 ARG A NE    1 
ATOM   2796 C  CZ    . ARG A 1 450 ? 109.829 109.218 109.144 1.00 31.68  ? 2241 ARG A CZ    1 
ATOM   2797 N  NH1   . ARG A 1 450 ? 109.292 108.263 109.883 1.00 32.45  ? 2241 ARG A NH1   1 
ATOM   2798 N  NH2   . ARG A 1 450 ? 110.887 109.879 109.603 1.00 29.92  ? 2241 ARG A NH2   1 
ATOM   2799 N  N     . ILE A 1 451 ? 107.892 108.293 102.617 1.00 23.17  ? 2242 ILE A N     1 
ATOM   2800 C  CA    . ILE A 1 451 ? 107.462 107.272 101.671 1.00 22.92  ? 2242 ILE A CA    1 
ATOM   2801 C  C     . ILE A 1 451 ? 107.013 106.058 102.467 1.00 23.04  ? 2242 ILE A C     1 
ATOM   2802 O  O     . ILE A 1 451 ? 107.809 105.461 103.203 1.00 28.27  ? 2242 ILE A O     1 
ATOM   2803 C  CB    . ILE A 1 451 ? 108.579 106.905 100.684 1.00 18.04  ? 2242 ILE A CB    1 
ATOM   2804 C  CG1   . ILE A 1 451 ? 108.836 108.062 99.719  1.00 25.20  ? 2242 ILE A CG1   1 
ATOM   2805 C  CG2   . ILE A 1 451 ? 108.220 105.642 99.924  1.00 21.08  ? 2242 ILE A CG2   1 
ATOM   2806 C  CD1   . ILE A 1 451 ? 110.211 108.038 99.093  1.00 28.29  ? 2242 ILE A CD1   1 
ATOM   2807 N  N     . THR A 1 452 ? 105.745 105.691 102.324 1.00 22.89  ? 2243 THR A N     1 
ATOM   2808 C  CA    . THR A 1 452 ? 105.183 104.541 103.014 1.00 24.36  ? 2243 THR A CA    1 
ATOM   2809 C  C     . THR A 1 452 ? 104.878 103.443 102.007 1.00 30.31  ? 2243 THR A C     1 
ATOM   2810 O  O     . THR A 1 452 ? 104.940 103.643 100.793 1.00 38.44  ? 2243 THR A O     1 
ATOM   2811 C  CB    . THR A 1 452 ? 103.915 104.920 103.786 1.00 39.69  ? 2243 THR A CB    1 
ATOM   2812 O  OG1   . THR A 1 452 ? 102.994 105.570 102.903 1.00 46.96  ? 2243 THR A OG1   1 
ATOM   2813 C  CG2   . THR A 1 452 ? 104.250 105.850 104.938 1.00 43.51  ? 2243 THR A CG2   1 
ATOM   2814 N  N     . PHE A 1 453 ? 104.542 102.266 102.525 1.00 26.70  ? 2244 PHE A N     1 
ATOM   2815 C  CA    . PHE A 1 453 ? 104.237 101.117 101.687 1.00 31.11  ? 2244 PHE A CA    1 
ATOM   2816 C  C     . PHE A 1 453 ? 102.892 100.538 102.090 1.00 33.96  ? 2244 PHE A C     1 
ATOM   2817 O  O     . PHE A 1 453 ? 102.638 100.312 103.277 1.00 43.52  ? 2244 PHE A O     1 
ATOM   2818 C  CB    . PHE A 1 453 ? 105.334 100.056 101.784 1.00 29.83  ? 2244 PHE A CB    1 
ATOM   2819 C  CG    . PHE A 1 453 ? 106.633 100.484 101.173 1.00 22.65  ? 2244 PHE A CG    1 
ATOM   2820 C  CD1   . PHE A 1 453 ? 107.536 101.240 101.895 1.00 20.02  ? 2244 PHE A CD1   1 
ATOM   2821 C  CD2   . PHE A 1 453 ? 106.945 100.145 99.871  1.00 20.19  ? 2244 PHE A CD2   1 
ATOM   2822 C  CE1   . PHE A 1 453 ? 108.727 101.643 101.334 1.00 20.14  ? 2244 PHE A CE1   1 
ATOM   2823 C  CE2   . PHE A 1 453 ? 108.135 100.544 99.307  1.00 19.05  ? 2244 PHE A CE2   1 
ATOM   2824 C  CZ    . PHE A 1 453 ? 109.026 101.295 100.039 1.00 19.10  ? 2244 PHE A CZ    1 
ATOM   2825 N  N     . THR A 1 454 ? 102.039 100.304 101.100 1.00 33.43  ? 2245 THR A N     1 
ATOM   2826 C  CA    . THR A 1 454 ? 100.723 99.725  101.295 1.00 40.85  ? 2245 THR A CA    1 
ATOM   2827 C  C     . THR A 1 454 ? 100.667 98.367  100.615 1.00 47.72  ? 2245 THR A C     1 
ATOM   2828 O  O     . THR A 1 454 ? 101.329 98.134  99.596  1.00 51.54  ? 2245 THR A O     1 
ATOM   2829 C  CB    . THR A 1 454 ? 99.621  100.625 100.723 1.00 45.17  ? 2245 THR A CB    1 
ATOM   2830 O  OG1   . THR A 1 454 ? 99.985  101.046 99.404  1.00 45.51  ? 2245 THR A OG1   1 
ATOM   2831 C  CG2   . THR A 1 454 ? 99.430  101.850 101.588 1.00 44.97  ? 2245 THR A CG2   1 
ATOM   2832 N  N     . GLU A 1 455 ? 99.863  97.477  101.194 1.00 49.13  ? 2246 GLU A N     1 
ATOM   2833 C  CA    . GLU A 1 455 ? 99.625  96.135  100.681 1.00 53.69  ? 2246 GLU A CA    1 
ATOM   2834 C  C     . GLU A 1 455 ? 100.931 95.387  100.443 1.00 47.47  ? 2246 GLU A C     1 
ATOM   2835 O  O     . GLU A 1 455 ? 101.329 95.193  99.287  1.00 47.84  ? 2246 GLU A O     1 
ATOM   2836 C  CB    . GLU A 1 455 ? 98.811  96.196  99.386  1.00 53.25  ? 2246 GLU A CB    1 
ATOM   2837 C  CG    . GLU A 1 455 ? 97.590  97.098  99.463  1.00 50.69  ? 2246 GLU A CG    1 
ATOM   2838 C  CD    . GLU A 1 455 ? 97.193  97.658  98.112  1.00 58.21  ? 2246 GLU A CD    1 
ATOM   2839 O  OE1   . GLU A 1 455 ? 97.889  97.364  97.117  1.00 55.43  ? 2246 GLU A OE1   1 
ATOM   2840 O  OE2   . GLU A 1 455 ? 96.186  98.392  98.044  1.00 72.10  ? 2246 GLU A OE2   1 
ATOM   2841 N  N     . PRO A 1 456 ? 101.643 94.973  101.500 1.00 43.96  ? 2247 PRO A N     1 
ATOM   2842 C  CA    . PRO A 1 456 ? 101.442 95.280  102.918 1.00 46.94  ? 2247 PRO A CA    1 
ATOM   2843 C  C     . PRO A 1 456 ? 102.300 96.467  103.327 1.00 45.66  ? 2247 PRO A C     1 
ATOM   2844 O  O     . PRO A 1 456 ? 102.794 97.194  102.472 1.00 45.07  ? 2247 PRO A O     1 
ATOM   2845 C  CB    . PRO A 1 456 ? 101.879 93.986  103.599 1.00 49.20  ? 2247 PRO A CB    1 
ATOM   2846 C  CG    . PRO A 1 456 ? 103.035 93.529  102.744 1.00 49.03  ? 2247 PRO A CG    1 
ATOM   2847 C  CD    . PRO A 1 456 ? 102.725 93.987  101.326 1.00 42.19  ? 2247 PRO A CD    1 
ATOM   2848 N  N     . ASN A 1 457 ? 102.497 96.699  104.621 1.00 42.68  ? 2248 ASN A N     1 
ATOM   2849 C  CA    . ASN A 1 457 ? 103.474 97.670  105.099 1.00 34.60  ? 2248 ASN A CA    1 
ATOM   2850 C  C     . ASN A 1 457 ? 104.723 96.907  105.519 1.00 31.59  ? 2248 ASN A C     1 
ATOM   2851 O  O     . ASN A 1 457 ? 104.744 96.275  106.579 1.00 39.74  ? 2248 ASN A O     1 
ATOM   2852 C  CB    . ASN A 1 457 ? 102.923 98.501  106.254 1.00 39.81  ? 2248 ASN A CB    1 
ATOM   2853 C  CG    . ASN A 1 457 ? 103.612 99.844  106.376 1.00 39.46  ? 2248 ASN A CG    1 
ATOM   2854 O  OD1   . ASN A 1 457 ? 103.232 100.681 107.190 1.00 44.44  ? 2248 ASN A OD1   1 
ATOM   2855 N  ND2   . ASN A 1 457 ? 104.634 100.057 105.558 1.00 36.96  ? 2248 ASN A ND2   1 
ATOM   2856 N  N     . ILE A 1 458 ? 105.758 96.961  104.682 1.00 26.67  ? 2249 ILE A N     1 
ATOM   2857 C  CA    . ILE A 1 458 ? 106.980 96.217  104.967 1.00 28.40  ? 2249 ILE A CA    1 
ATOM   2858 C  C     . ILE A 1 458 ? 107.727 96.836  106.141 1.00 27.98  ? 2249 ILE A C     1 
ATOM   2859 O  O     . ILE A 1 458 ? 108.267 96.122  106.994 1.00 34.78  ? 2249 ILE A O     1 
ATOM   2860 C  CB    . ILE A 1 458 ? 107.859 96.141  103.708 1.00 26.72  ? 2249 ILE A CB    1 
ATOM   2861 C  CG1   . ILE A 1 458 ? 107.339 95.054  102.773 1.00 31.13  ? 2249 ILE A CG1   1 
ATOM   2862 C  CG2   . ILE A 1 458 ? 109.293 95.848  104.082 1.00 24.54  ? 2249 ILE A CG2   1 
ATOM   2863 C  CD1   . ILE A 1 458 ? 107.623 93.660  103.267 1.00 34.94  ? 2249 ILE A CD1   1 
ATOM   2864 N  N     . GLN A 1 459 ? 107.765 98.168  106.213 1.00 21.66  ? 2250 GLN A N     1 
ATOM   2865 C  CA    . GLN A 1 459 ? 108.500 98.826  107.288 1.00 28.35  ? 2250 GLN A CA    1 
ATOM   2866 C  C     . GLN A 1 459 ? 107.936 98.474  108.659 1.00 40.01  ? 2250 GLN A C     1 
ATOM   2867 O  O     . GLN A 1 459 ? 108.659 98.531  109.660 1.00 36.50  ? 2250 GLN A O     1 
ATOM   2868 C  CB    . GLN A 1 459 ? 108.484 100.338 107.084 1.00 22.62  ? 2250 GLN A CB    1 
ATOM   2869 C  CG    . GLN A 1 459 ? 108.657 100.764 105.644 1.00 19.56  ? 2250 GLN A CG    1 
ATOM   2870 C  CD    . GLN A 1 459 ? 107.958 102.068 105.348 1.00 22.43  ? 2250 GLN A CD    1 
ATOM   2871 O  OE1   . GLN A 1 459 ? 106.944 102.393 105.962 1.00 29.01  ? 2250 GLN A OE1   1 
ATOM   2872 N  NE2   . GLN A 1 459 ? 108.499 102.828 104.407 1.00 21.20  ? 2250 GLN A NE2   1 
ATOM   2873 N  N     . ASN A 1 460 ? 106.658 98.110  108.727 1.00 44.20  ? 2251 ASN A N     1 
ATOM   2874 C  CA    . ASN A 1 460 ? 106.034 97.704  109.986 1.00 39.88  ? 2251 ASN A CA    1 
ATOM   2875 C  C     . ASN A 1 460 ? 106.205 96.199  110.200 1.00 38.64  ? 2251 ASN A C     1 
ATOM   2876 O  O     . ASN A 1 460 ? 105.247 95.436  110.307 1.00 48.24  ? 2251 ASN A O     1 
ATOM   2877 C  CB    . ASN A 1 460 ? 104.564 98.106  110.001 1.00 45.10  ? 2251 ASN A CB    1 
ATOM   2878 C  CG    . ASN A 1 460 ? 104.368 99.610  110.039 1.00 54.95  ? 2251 ASN A CG    1 
ATOM   2879 O  OD1   . ASN A 1 460 ? 105.334 100.370 110.007 1.00 53.04  ? 2251 ASN A OD1   1 
ATOM   2880 N  ND2   . ASN A 1 460 ? 103.115 100.047 110.088 1.00 59.07  ? 2251 ASN A ND2   1 
ATOM   2881 N  N     . VAL A 1 461 ? 107.461 95.783  110.250 1.00 29.30  ? 2252 VAL A N     1 
ATOM   2882 C  CA    . VAL A 1 461 ? 107.843 94.401  110.527 1.00 27.56  ? 2252 VAL A CA    1 
ATOM   2883 C  C     . VAL A 1 461 ? 108.577 94.381  111.861 1.00 32.41  ? 2252 VAL A C     1 
ATOM   2884 O  O     . VAL A 1 461 ? 109.471 95.208  112.072 1.00 39.84  ? 2252 VAL A O     1 
ATOM   2885 C  CB    . VAL A 1 461 ? 108.724 93.812  109.409 1.00 22.86  ? 2252 VAL A CB    1 
ATOM   2886 C  CG1   . VAL A 1 461 ? 109.623 92.722  109.952 1.00 30.75  ? 2252 VAL A CG1   1 
ATOM   2887 C  CG2   . VAL A 1 461 ? 107.857 93.260  108.296 1.00 26.31  ? 2252 VAL A CG2   1 
ATOM   2888 N  N     . PRO A 1 462 ? 108.223 93.487  112.785 1.00 28.89  ? 2253 PRO A N     1 
ATOM   2889 C  CA    . PRO A 1 462 ? 108.879 93.485  114.097 1.00 31.57  ? 2253 PRO A CA    1 
ATOM   2890 C  C     . PRO A 1 462 ? 110.377 93.254  113.970 1.00 36.33  ? 2253 PRO A C     1 
ATOM   2891 O  O     . PRO A 1 462 ? 110.837 92.457  113.152 1.00 46.78  ? 2253 PRO A O     1 
ATOM   2892 C  CB    . PRO A 1 462 ? 108.192 92.331  114.836 1.00 33.67  ? 2253 PRO A CB    1 
ATOM   2893 C  CG    . PRO A 1 462 ? 106.909 92.116  114.108 1.00 36.88  ? 2253 PRO A CG    1 
ATOM   2894 C  CD    . PRO A 1 462 ? 107.199 92.437  112.680 1.00 29.11  ? 2253 PRO A CD    1 
ATOM   2895 N  N     . ARG A 1 463 ? 111.135 93.963  114.799 1.00 34.67  ? 2254 ARG A N     1 
ATOM   2896 C  CA    . ARG A 1 463 ? 112.588 93.896  114.761 1.00 42.40  ? 2254 ARG A CA    1 
ATOM   2897 C  C     . ARG A 1 463 ? 113.069 92.708  115.589 1.00 42.19  ? 2254 ARG A C     1 
ATOM   2898 O  O     . ARG A 1 463 ? 112.297 91.822  115.965 1.00 40.57  ? 2254 ARG A O     1 
ATOM   2899 C  CB    . ARG A 1 463 ? 113.189 95.207  115.252 1.00 43.66  ? 2254 ARG A CB    1 
ATOM   2900 C  CG    . ARG A 1 463 ? 112.502 95.765  116.474 1.00 41.89  ? 2254 ARG A CG    1 
ATOM   2901 C  CD    . ARG A 1 463 ? 112.679 97.262  116.548 1.00 44.31  ? 2254 ARG A CD    1 
ATOM   2902 N  NE    . ARG A 1 463 ? 114.081 97.640  116.451 1.00 48.59  ? 2254 ARG A NE    1 
ATOM   2903 C  CZ    . ARG A 1 463 ? 114.561 98.814  116.834 1.00 57.48  ? 2254 ARG A CZ    1 
ATOM   2904 N  NH1   . ARG A 1 463 ? 113.772 99.749  117.338 1.00 60.16  ? 2254 ARG A NH1   1 
ATOM   2905 N  NH2   . ARG A 1 463 ? 115.862 99.056  116.709 1.00 59.73  ? 2254 ARG A NH2   1 
ATOM   2906 N  N     . ASP A 1 464 ? 114.368 92.678  115.875 1.00 43.62  ? 2255 ASP A N     1 
ATOM   2907 C  CA    . ASP A 1 464 ? 114.957 91.590  116.641 1.00 51.00  ? 2255 ASP A CA    1 
ATOM   2908 C  C     . ASP A 1 464 ? 114.551 91.671  118.107 1.00 56.90  ? 2255 ASP A C     1 
ATOM   2909 O  O     . ASP A 1 464 ? 115.190 92.374  118.896 1.00 62.22  ? 2255 ASP A O     1 
ATOM   2910 C  CB    . ASP A 1 464 ? 116.482 91.616  116.512 1.00 49.73  ? 2255 ASP A CB    1 
ATOM   2911 C  CG    . ASP A 1 464 ? 116.954 91.326  115.099 1.00 49.52  ? 2255 ASP A CG    1 
ATOM   2912 O  OD1   . ASP A 1 464 ? 116.753 90.190  114.623 1.00 48.17  ? 2255 ASP A OD1   1 
ATOM   2913 O  OD2   . ASP A 1 464 ? 117.525 92.237  114.464 1.00 49.66  ? 2255 ASP A OD2   1 
ATOM   2914 N  N     . PHE A 1 465 ? 113.490 90.961  118.478 1.00 54.22  ? 2256 PHE A N     1 
ATOM   2915 C  CA    . PHE A 1 465 ? 113.078 90.819  119.868 1.00 50.74  ? 2256 PHE A CA    1 
ATOM   2916 C  C     . PHE A 1 465 ? 113.282 89.371  120.288 1.00 56.94  ? 2256 PHE A C     1 
ATOM   2917 O  O     . PHE A 1 465 ? 112.903 88.449  119.559 1.00 61.13  ? 2256 PHE A O     1 
ATOM   2918 C  CB    . PHE A 1 465 ? 111.621 91.252  120.068 1.00 55.95  ? 2256 PHE A CB    1 
ATOM   2919 C  CG    . PHE A 1 465 ? 110.609 90.302  119.485 1.00 56.24  ? 2256 PHE A CG    1 
ATOM   2920 C  CD1   . PHE A 1 465 ? 110.315 90.325  118.132 1.00 51.49  ? 2256 PHE A CD1   1 
ATOM   2921 C  CD2   . PHE A 1 465 ? 109.940 89.398  120.293 1.00 54.35  ? 2256 PHE A CD2   1 
ATOM   2922 C  CE1   . PHE A 1 465 ? 109.383 89.458  117.596 1.00 45.16  ? 2256 PHE A CE1   1 
ATOM   2923 C  CE2   . PHE A 1 465 ? 109.008 88.529  119.761 1.00 50.13  ? 2256 PHE A CE2   1 
ATOM   2924 C  CZ    . PHE A 1 465 ? 108.730 88.559  118.412 1.00 43.42  ? 2256 PHE A CZ    1 
ATOM   2925 N  N     . GLU A 1 466 ? 113.892 89.174  121.451 1.00 60.25  ? 2257 GLU A N     1 
ATOM   2926 C  CA    . GLU A 1 466 ? 114.310 87.854  121.898 1.00 63.59  ? 2257 GLU A CA    1 
ATOM   2927 C  C     . GLU A 1 466 ? 113.366 87.336  122.972 1.00 63.91  ? 2257 GLU A C     1 
ATOM   2928 O  O     . GLU A 1 466 ? 113.124 88.015  123.975 1.00 72.58  ? 2257 GLU A O     1 
ATOM   2929 C  CB    . GLU A 1 466 ? 115.743 87.892  122.432 1.00 65.56  ? 2257 GLU A CB    1 
ATOM   2930 N  N     . ILE A 1 467 ? 112.835 86.136  122.756 1.00 62.75  ? 2258 ILE A N     1 
ATOM   2931 C  CA    . ILE A 1 467 ? 112.019 85.444  123.744 1.00 74.42  ? 2258 ILE A CA    1 
ATOM   2932 C  C     . ILE A 1 467 ? 112.436 83.980  123.756 1.00 92.60  ? 2258 ILE A C     1 
ATOM   2933 O  O     . ILE A 1 467 ? 112.704 83.390  122.703 1.00 93.83  ? 2258 ILE A O     1 
ATOM   2934 C  CB    . ILE A 1 467 ? 110.509 85.605  123.459 1.00 74.04  ? 2258 ILE A CB    1 
ATOM   2935 C  CG1   . ILE A 1 467 ? 109.684 84.997  124.594 1.00 93.82  ? 2258 ILE A CG1   1 
ATOM   2936 C  CG2   . ILE A 1 467 ? 110.133 84.992  122.116 1.00 56.07  ? 2258 ILE A CG2   1 
ATOM   2937 C  CD1   . ILE A 1 467 ? 108.242 85.448  124.609 1.00 101.03 ? 2258 ILE A CD1   1 
ATOM   2938 N  N     . LYS A 1 468 ? 112.518 83.400  124.951 1.00 98.81  ? 2259 LYS A N     1 
ATOM   2939 C  CA    . LYS A 1 468 ? 112.994 82.036  125.132 1.00 99.33  ? 2259 LYS A CA    1 
ATOM   2940 C  C     . LYS A 1 468 ? 111.938 81.202  125.840 1.00 103.15 ? 2259 LYS A C     1 
ATOM   2941 O  O     . LYS A 1 468 ? 111.248 81.690  126.741 1.00 100.03 ? 2259 LYS A O     1 
ATOM   2942 C  CB    . LYS A 1 468 ? 114.301 82.010  125.932 1.00 93.38  ? 2259 LYS A CB    1 
ATOM   2943 N  N     . MET A 1 469 ? 111.824 79.942  125.433 1.00 110.88 ? 2260 MET A N     1 
ATOM   2944 C  CA    . MET A 1 469 ? 110.890 78.996  126.019 1.00 119.98 ? 2260 MET A CA    1 
ATOM   2945 C  C     . MET A 1 469 ? 111.634 77.745  126.459 1.00 122.29 ? 2260 MET A C     1 
ATOM   2946 O  O     . MET A 1 469 ? 112.662 77.390  125.873 1.00 119.67 ? 2260 MET A O     1 
ATOM   2947 C  CB    . MET A 1 469 ? 109.789 78.610  125.020 1.00 114.13 ? 2260 MET A CB    1 
ATOM   2948 C  CG    . MET A 1 469 ? 110.287 78.369  123.605 1.00 110.71 ? 2260 MET A CG    1 
ATOM   2949 S  SD    . MET A 1 469 ? 108.986 77.781  122.504 1.00 123.93 ? 2260 MET A SD    1 
ATOM   2950 C  CE    . MET A 1 469 ? 109.957 77.096  121.164 1.00 96.47  ? 2260 MET A CE    1 
ATOM   2951 N  N     . PRO A 1 470 ? 111.140 77.054  127.499 1.00 120.72 ? 2261 PRO A N     1 
ATOM   2952 C  CA    . PRO A 1 470 ? 111.765 75.817  127.979 1.00 121.19 ? 2261 PRO A CA    1 
ATOM   2953 C  C     . PRO A 1 470 ? 111.753 74.706  126.933 1.00 120.51 ? 2261 PRO A C     1 
ATOM   2954 O  O     . PRO A 1 470 ? 112.773 74.037  126.761 1.00 118.85 ? 2261 PRO A O     1 
ATOM   2955 C  CB    . PRO A 1 470 ? 110.903 75.432  129.187 1.00 119.84 ? 2261 PRO A CB    1 
ATOM   2956 C  CG    . PRO A 1 470 ? 110.261 76.705  129.619 1.00 119.35 ? 2261 PRO A CG    1 
ATOM   2957 C  CD    . PRO A 1 470 ? 110.019 77.473  128.358 1.00 118.36 ? 2261 PRO A CD    1 
ATOM   2958 N  N     . MET A 1 517 ? 120.289 81.175  125.267 1.00 103.57 ? 2308 MET A N     1 
ATOM   2959 C  CA    . MET A 1 517 ? 118.920 80.748  125.541 1.00 110.00 ? 2308 MET A CA    1 
ATOM   2960 C  C     . MET A 1 517 ? 117.858 81.513  124.728 1.00 104.06 ? 2308 MET A C     1 
ATOM   2961 O  O     . MET A 1 517 ? 116.966 80.882  124.162 1.00 97.73  ? 2308 MET A O     1 
ATOM   2962 C  CB    . MET A 1 517 ? 118.618 80.858  127.042 1.00 109.63 ? 2308 MET A CB    1 
ATOM   2963 C  CG    . MET A 1 517 ? 117.456 79.993  127.503 1.00 105.83 ? 2308 MET A CG    1 
ATOM   2964 S  SD    . MET A 1 517 ? 116.619 80.666  128.951 1.00 106.58 ? 2308 MET A SD    1 
ATOM   2965 C  CE    . MET A 1 517 ? 115.269 79.504  129.129 1.00 91.00  ? 2308 MET A CE    1 
ATOM   2966 N  N     . PRO A 1 518 ? 117.926 82.850  124.668 1.00 100.47 ? 2309 PRO A N     1 
ATOM   2967 C  CA    . PRO A 1 518 ? 116.969 83.577  123.825 1.00 96.20  ? 2309 PRO A CA    1 
ATOM   2968 C  C     . PRO A 1 518 ? 117.143 83.222  122.356 1.00 94.13  ? 2309 PRO A C     1 
ATOM   2969 O  O     . PRO A 1 518 ? 118.250 82.951  121.883 1.00 96.52  ? 2309 PRO A O     1 
ATOM   2970 C  CB    . PRO A 1 518 ? 117.303 85.050  124.091 1.00 93.99  ? 2309 PRO A CB    1 
ATOM   2971 C  CG    . PRO A 1 518 ? 118.696 85.039  124.589 1.00 95.16  ? 2309 PRO A CG    1 
ATOM   2972 C  CD    . PRO A 1 518 ? 118.803 83.788  125.394 1.00 98.80  ? 2309 PRO A CD    1 
ATOM   2973 N  N     . PHE A 1 519 ? 116.025 83.227  121.630 1.00 84.71  ? 2310 PHE A N     1 
ATOM   2974 C  CA    . PHE A 1 519 ? 116.027 82.852  120.221 1.00 76.78  ? 2310 PHE A CA    1 
ATOM   2975 C  C     . PHE A 1 519 ? 116.228 84.034  119.284 1.00 73.83  ? 2310 PHE A C     1 
ATOM   2976 O  O     . PHE A 1 519 ? 116.629 83.825  118.132 1.00 77.44  ? 2310 PHE A O     1 
ATOM   2977 C  CB    . PHE A 1 519 ? 114.716 82.146  119.845 1.00 74.14  ? 2310 PHE A CB    1 
ATOM   2978 C  CG    . PHE A 1 519 ? 114.408 80.921  120.669 1.00 85.20  ? 2310 PHE A CG    1 
ATOM   2979 C  CD1   . PHE A 1 519 ? 113.167 80.314  120.573 1.00 92.32  ? 2310 PHE A CD1   1 
ATOM   2980 C  CD2   . PHE A 1 519 ? 115.361 80.351  121.499 1.00 91.22  ? 2310 PHE A CD2   1 
ATOM   2981 C  CE1   . PHE A 1 519 ? 112.871 79.186  121.313 1.00 98.77  ? 2310 PHE A CE1   1 
ATOM   2982 C  CE2   . PHE A 1 519 ? 115.069 79.223  122.242 1.00 94.47  ? 2310 PHE A CE2   1 
ATOM   2983 C  CZ    . PHE A 1 519 ? 113.823 78.639  122.147 1.00 99.14  ? 2310 PHE A CZ    1 
ATOM   2984 N  N     . SER A 1 520 ? 115.965 85.256  119.744 1.00 66.99  ? 2311 SER A N     1 
ATOM   2985 C  CA    . SER A 1 520 ? 116.018 86.454  118.908 1.00 60.74  ? 2311 SER A CA    1 
ATOM   2986 C  C     . SER A 1 520 ? 115.119 86.292  117.682 1.00 59.93  ? 2311 SER A C     1 
ATOM   2987 O  O     . SER A 1 520 ? 115.566 86.299  116.534 1.00 62.81  ? 2311 SER A O     1 
ATOM   2988 C  CB    . SER A 1 520 ? 117.459 86.783  118.506 1.00 61.91  ? 2311 SER A CB    1 
ATOM   2989 O  OG    . SER A 1 520 ? 117.514 87.940  117.690 1.00 56.01  ? 2311 SER A OG    1 
ATOM   2990 N  N     . ILE A 1 521 ? 113.828 86.132  117.954 1.00 60.13  ? 2312 ILE A N     1 
ATOM   2991 C  CA    . ILE A 1 521 ? 112.843 85.903  116.904 1.00 54.01  ? 2312 ILE A CA    1 
ATOM   2992 C  C     . ILE A 1 521 ? 112.547 87.215  116.195 1.00 53.26  ? 2312 ILE A C     1 
ATOM   2993 O  O     . ILE A 1 521 ? 112.207 88.219  116.831 1.00 50.91  ? 2312 ILE A O     1 
ATOM   2994 C  CB    . ILE A 1 521 ? 111.563 85.285  117.486 1.00 54.04  ? 2312 ILE A CB    1 
ATOM   2995 C  CG1   . ILE A 1 521 ? 111.839 83.867  117.987 1.00 68.44  ? 2312 ILE A CG1   1 
ATOM   2996 C  CG2   . ILE A 1 521 ? 110.449 85.289  116.453 1.00 50.06  ? 2312 ILE A CG2   1 
ATOM   2997 C  CD1   . ILE A 1 521 ? 112.616 83.017  117.005 1.00 65.06  ? 2312 ILE A CD1   1 
ATOM   2998 N  N     . SER A 1 522 ? 112.675 87.208  114.871 1.00 55.17  ? 2313 SER A N     1 
ATOM   2999 C  CA    . SER A 1 522 ? 112.403 88.386  114.063 1.00 44.00  ? 2313 SER A CA    1 
ATOM   3000 C  C     . SER A 1 522 ? 112.077 87.937  112.649 1.00 40.14  ? 2313 SER A C     1 
ATOM   3001 O  O     . SER A 1 522 ? 112.674 86.983  112.145 1.00 47.90  ? 2313 SER A O     1 
ATOM   3002 C  CB    . SER A 1 522 ? 113.598 89.343  114.050 1.00 43.08  ? 2313 SER A CB    1 
ATOM   3003 O  OG    . SER A 1 522 ? 114.698 88.760  113.373 1.00 47.34  ? 2313 SER A OG    1 
ATOM   3004 N  N     . MET A 1 523 ? 111.132 88.626  112.016 1.00 36.40  ? 2314 MET A N     1 
ATOM   3005 C  CA    . MET A 1 523 ? 110.776 88.338  110.635 1.00 43.78  ? 2314 MET A CA    1 
ATOM   3006 C  C     . MET A 1 523 ? 111.615 89.118  109.635 1.00 42.28  ? 2314 MET A C     1 
ATOM   3007 O  O     . MET A 1 523 ? 111.457 88.919  108.427 1.00 40.75  ? 2314 MET A O     1 
ATOM   3008 C  CB    . MET A 1 523 ? 109.290 88.618  110.400 1.00 32.53  ? 2314 MET A CB    1 
ATOM   3009 C  CG    . MET A 1 523 ? 108.426 88.404  111.624 1.00 37.25  ? 2314 MET A CG    1 
ATOM   3010 S  SD    . MET A 1 523 ? 108.513 86.691  112.173 1.00 64.06  ? 2314 MET A SD    1 
ATOM   3011 C  CE    . MET A 1 523 ? 107.936 85.841  110.708 1.00 62.54  ? 2314 MET A CE    1 
ATOM   3012 N  N     . ARG A 1 524 ? 112.501 89.996  110.106 1.00 31.73  ? 2315 ARG A N     1 
ATOM   3013 C  CA    . ARG A 1 524 ? 113.405 90.691  109.201 1.00 29.45  ? 2315 ARG A CA    1 
ATOM   3014 C  C     . ARG A 1 524 ? 114.402 89.743  108.552 1.00 41.95  ? 2315 ARG A C     1 
ATOM   3015 O  O     . ARG A 1 524 ? 114.904 90.042  107.464 1.00 52.69  ? 2315 ARG A O     1 
ATOM   3016 C  CB    . ARG A 1 524 ? 114.138 91.802  109.950 1.00 28.35  ? 2315 ARG A CB    1 
ATOM   3017 C  CG    . ARG A 1 524 ? 113.210 92.864  110.503 1.00 27.21  ? 2315 ARG A CG    1 
ATOM   3018 C  CD    . ARG A 1 524 ? 113.930 94.179  110.723 1.00 34.73  ? 2315 ARG A CD    1 
ATOM   3019 N  NE    . ARG A 1 524 ? 113.007 95.305  110.677 1.00 29.72  ? 2315 ARG A NE    1 
ATOM   3020 C  CZ    . ARG A 1 524 ? 113.311 96.540  111.049 1.00 28.33  ? 2315 ARG A CZ    1 
ATOM   3021 N  NH1   . ARG A 1 524 ? 114.508 96.845  111.520 1.00 33.83  ? 2315 ARG A NH1   1 
ATOM   3022 N  NH2   . ARG A 1 524 ? 112.391 97.494  110.945 1.00 26.12  ? 2315 ARG A NH2   1 
ATOM   3023 N  N     . HIS A 1 525 ? 114.700 88.611  109.191 1.00 45.14  ? 2316 HIS A N     1 
ATOM   3024 C  CA    . HIS A 1 525 ? 115.578 87.617  108.587 1.00 47.97  ? 2316 HIS A CA    1 
ATOM   3025 C  C     . HIS A 1 525 ? 114.951 86.966  107.362 1.00 44.68  ? 2316 HIS A C     1 
ATOM   3026 O  O     . HIS A 1 525 ? 115.677 86.454  106.505 1.00 52.32  ? 2316 HIS A O     1 
ATOM   3027 C  CB    . HIS A 1 525 ? 115.947 86.552  109.624 1.00 45.73  ? 2316 HIS A CB    1 
ATOM   3028 C  CG    . HIS A 1 525 ? 116.876 85.497  109.108 1.00 53.88  ? 2316 HIS A CG    1 
ATOM   3029 N  ND1   . HIS A 1 525 ? 117.815 85.744  108.131 1.00 51.00  ? 2316 HIS A ND1   1 
ATOM   3030 C  CD2   . HIS A 1 525 ? 117.009 84.191  109.436 1.00 63.39  ? 2316 HIS A CD2   1 
ATOM   3031 C  CE1   . HIS A 1 525 ? 118.484 84.634  107.876 1.00 58.76  ? 2316 HIS A CE1   1 
ATOM   3032 N  NE2   . HIS A 1 525 ? 118.017 83.677  108.657 1.00 66.80  ? 2316 HIS A NE2   1 
ATOM   3033 N  N     . ALA A 1 526 ? 113.623 86.991  107.250 1.00 34.46  ? 2317 ALA A N     1 
ATOM   3034 C  CA    . ALA A 1 526 ? 112.945 86.346  106.134 1.00 42.13  ? 2317 ALA A CA    1 
ATOM   3035 C  C     . ALA A 1 526 ? 113.191 87.040  104.802 1.00 50.19  ? 2317 ALA A C     1 
ATOM   3036 O  O     . ALA A 1 526 ? 112.839 86.477  103.761 1.00 58.46  ? 2317 ALA A O     1 
ATOM   3037 C  CB    . ALA A 1 526 ? 111.442 86.276  106.405 1.00 50.59  ? 2317 ALA A CB    1 
ATOM   3038 N  N     . PHE A 1 527 ? 113.777 88.237  104.805 1.00 43.74  ? 2318 PHE A N     1 
ATOM   3039 C  CA    . PHE A 1 527 ? 113.970 89.007  103.575 1.00 43.48  ? 2318 PHE A CA    1 
ATOM   3040 C  C     . PHE A 1 527 ? 115.324 88.663  102.949 1.00 43.27  ? 2318 PHE A C     1 
ATOM   3041 O  O     . PHE A 1 527 ? 116.258 89.465  102.898 1.00 36.62  ? 2318 PHE A O     1 
ATOM   3042 C  CB    . PHE A 1 527 ? 113.832 90.496  103.860 1.00 30.23  ? 2318 PHE A CB    1 
ATOM   3043 C  CG    . PHE A 1 527 ? 112.462 90.888  104.326 1.00 29.44  ? 2318 PHE A CG    1 
ATOM   3044 C  CD1   . PHE A 1 527 ? 111.395 90.895  103.447 1.00 37.80  ? 2318 PHE A CD1   1 
ATOM   3045 C  CD2   . PHE A 1 527 ? 112.236 91.231  105.645 1.00 28.11  ? 2318 PHE A CD2   1 
ATOM   3046 C  CE1   . PHE A 1 527 ? 110.132 91.247  103.872 1.00 31.91  ? 2318 PHE A CE1   1 
ATOM   3047 C  CE2   . PHE A 1 527 ? 110.976 91.589  106.076 1.00 31.06  ? 2318 PHE A CE2   1 
ATOM   3048 C  CZ    . PHE A 1 527 ? 109.922 91.596  105.188 1.00 32.01  ? 2318 PHE A CZ    1 
ATOM   3049 N  N     . VAL A 1 528 ? 115.402 87.436  102.454 1.00 49.09  ? 2319 VAL A N     1 
ATOM   3050 C  CA    . VAL A 1 528 ? 116.627 86.932  101.828 1.00 48.66  ? 2319 VAL A CA    1 
ATOM   3051 C  C     . VAL A 1 528 ? 116.678 87.414  100.381 1.00 49.81  ? 2319 VAL A C     1 
ATOM   3052 O  O     . VAL A 1 528 ? 115.691 87.250  99.648  1.00 51.15  ? 2319 VAL A O     1 
ATOM   3053 C  CB    . VAL A 1 528 ? 116.675 85.409  101.900 1.00 52.05  ? 2319 VAL A CB    1 
ATOM   3054 C  CG1   . VAL A 1 528 ? 117.914 84.880  101.192 1.00 56.64  ? 2319 VAL A CG1   1 
ATOM   3055 C  CG2   . VAL A 1 528 ? 116.646 84.946  103.349 1.00 46.48  ? 2319 VAL A CG2   1 
ATOM   3056 N  N     . PRO A 1 529 ? 117.792 87.998  99.933  1.00 48.81  ? 2320 PRO A N     1 
ATOM   3057 C  CA    . PRO A 1 529 ? 117.879 88.461  98.542  1.00 50.05  ? 2320 PRO A CA    1 
ATOM   3058 C  C     . PRO A 1 529 ? 118.022 87.320  97.546  1.00 52.64  ? 2320 PRO A C     1 
ATOM   3059 O  O     . PRO A 1 529 ? 117.962 86.145  97.923  1.00 58.01  ? 2320 PRO A O     1 
ATOM   3060 C  CB    . PRO A 1 529 ? 119.127 89.349  98.553  1.00 43.35  ? 2320 PRO A CB    1 
ATOM   3061 C  CG    . PRO A 1 529 ? 119.967 88.783  99.634  1.00 39.95  ? 2320 PRO A CG    1 
ATOM   3062 C  CD    . PRO A 1 529 ? 119.016 88.298  100.691 1.00 44.43  ? 2320 PRO A CD    1 
ATOM   3063 N  N     . PHE A 1 530 ? 118.209 87.657  96.273  1.00 47.83  ? 2321 PHE A N     1 
ATOM   3064 C  CA    . PHE A 1 530 ? 118.360 86.638  95.249  1.00 49.19  ? 2321 PHE A CA    1 
ATOM   3065 C  C     . PHE A 1 530 ? 119.681 85.892  95.437  1.00 54.15  ? 2321 PHE A C     1 
ATOM   3066 O  O     . PHE A 1 530 ? 120.623 86.426  96.029  1.00 52.92  ? 2321 PHE A O     1 
ATOM   3067 C  CB    . PHE A 1 530 ? 118.301 87.263  93.855  1.00 54.99  ? 2321 PHE A CB    1 
ATOM   3068 C  CG    . PHE A 1 530 ? 119.374 88.283  93.592  1.00 52.18  ? 2321 PHE A CG    1 
ATOM   3069 C  CD1   . PHE A 1 530 ? 120.587 87.910  93.042  1.00 59.13  ? 2321 PHE A CD1   1 
ATOM   3070 C  CD2   . PHE A 1 530 ? 119.162 89.618  93.877  1.00 47.71  ? 2321 PHE A CD2   1 
ATOM   3071 C  CE1   . PHE A 1 530 ? 121.571 88.847  92.797  1.00 60.82  ? 2321 PHE A CE1   1 
ATOM   3072 C  CE2   . PHE A 1 530 ? 120.141 90.560  93.632  1.00 46.27  ? 2321 PHE A CE2   1 
ATOM   3073 C  CZ    . PHE A 1 530 ? 121.347 90.173  93.091  1.00 53.47  ? 2321 PHE A CZ    1 
ATOM   3074 N  N     . PRO A 1 531 ? 119.769 84.649  94.960  1.00 55.94  ? 2322 PRO A N     1 
ATOM   3075 C  CA    . PRO A 1 531 ? 121.017 83.892  95.109  1.00 57.05  ? 2322 PRO A CA    1 
ATOM   3076 C  C     . PRO A 1 531 ? 122.184 84.614  94.452  1.00 61.37  ? 2322 PRO A C     1 
ATOM   3077 O  O     . PRO A 1 531 ? 122.052 85.199  93.375  1.00 62.30  ? 2322 PRO A O     1 
ATOM   3078 C  CB    . PRO A 1 531 ? 120.712 82.563  94.411  1.00 56.76  ? 2322 PRO A CB    1 
ATOM   3079 C  CG    . PRO A 1 531 ? 119.229 82.440  94.469  1.00 55.41  ? 2322 PRO A CG    1 
ATOM   3080 C  CD    . PRO A 1 531 ? 118.701 83.837  94.351  1.00 52.46  ? 2322 PRO A CD    1 
ATOM   3081 N  N     . GLY A 1 532 ? 123.337 84.555  95.108  1.00 60.78  ? 2323 GLY A N     1 
ATOM   3082 C  CA    . GLY A 1 532 ? 124.478 85.341  94.674  1.00 59.77  ? 2323 GLY A CA    1 
ATOM   3083 C  C     . GLY A 1 532 ? 124.281 86.828  94.870  1.00 58.44  ? 2323 GLY A C     1 
ATOM   3084 O  O     . GLY A 1 532 ? 124.684 87.623  94.012  1.00 56.63  ? 2323 GLY A O     1 
ATOM   3085 N  N     . GLY A 1 533 ? 123.662 87.224  95.979  1.00 57.43  ? 2324 GLY A N     1 
ATOM   3086 C  CA    . GLY A 1 533 ? 123.440 88.626  96.272  1.00 53.45  ? 2324 GLY A CA    1 
ATOM   3087 C  C     . GLY A 1 533 ? 123.254 88.829  97.757  1.00 43.27  ? 2324 GLY A C     1 
ATOM   3088 O  O     . GLY A 1 533 ? 122.865 87.910  98.484  1.00 48.11  ? 2324 GLY A O     1 
ATOM   3089 N  N     . SER A 1 534 ? 123.540 90.049  98.204  1.00 34.50  ? 2325 SER A N     1 
ATOM   3090 C  CA    . SER A 1 534 ? 123.487 90.387  99.618  1.00 32.95  ? 2325 SER A CA    1 
ATOM   3091 C  C     . SER A 1 534 ? 122.776 91.716  99.813  1.00 30.73  ? 2325 SER A C     1 
ATOM   3092 O  O     . SER A 1 534 ? 123.006 92.669  99.064  1.00 33.76  ? 2325 SER A O     1 
ATOM   3093 C  CB    . SER A 1 534 ? 124.894 90.457  100.223 1.00 34.94  ? 2325 SER A CB    1 
ATOM   3094 O  OG    . SER A 1 534 ? 125.630 91.537  99.676  1.00 33.65  ? 2325 SER A OG    1 
ATOM   3095 N  N     . ILE A 1 535 ? 121.913 91.773  100.828 1.00 29.38  ? 2326 ILE A N     1 
ATOM   3096 C  CA    . ILE A 1 535 ? 121.246 93.020  101.176 1.00 23.43  ? 2326 ILE A CA    1 
ATOM   3097 C  C     . ILE A 1 535 ? 122.273 94.010  101.703 1.00 22.33  ? 2326 ILE A C     1 
ATOM   3098 O  O     . ILE A 1 535 ? 123.140 93.664  102.518 1.00 29.44  ? 2326 ILE A O     1 
ATOM   3099 C  CB    . ILE A 1 535 ? 120.136 92.773  102.211 1.00 28.72  ? 2326 ILE A CB    1 
ATOM   3100 C  CG1   . ILE A 1 535 ? 119.166 91.703  101.712 1.00 36.59  ? 2326 ILE A CG1   1 
ATOM   3101 C  CG2   . ILE A 1 535 ? 119.403 94.068  102.523 1.00 24.77  ? 2326 ILE A CG2   1 
ATOM   3102 C  CD1   . ILE A 1 535 ? 118.142 92.207  100.726 1.00 25.19  ? 2326 ILE A CD1   1 
ATOM   3103 N  N     . LEU A 1 536 ? 122.180 95.254  101.236 1.00 21.82  ? 2327 LEU A N     1 
ATOM   3104 C  CA    . LEU A 1 536 ? 123.124 96.316  101.584 1.00 24.72  ? 2327 LEU A CA    1 
ATOM   3105 C  C     . LEU A 1 536 ? 122.327 97.529  102.050 1.00 29.68  ? 2327 LEU A C     1 
ATOM   3106 O  O     . LEU A 1 536 ? 121.997 98.411  101.254 1.00 34.81  ? 2327 LEU A O     1 
ATOM   3107 C  CB    . LEU A 1 536 ? 124.019 96.652  100.399 1.00 24.62  ? 2327 LEU A CB    1 
ATOM   3108 C  CG    . LEU A 1 536 ? 125.291 97.443  100.694 1.00 30.07  ? 2327 LEU A CG    1 
ATOM   3109 C  CD1   . LEU A 1 536 ? 126.436 96.906  99.858  1.00 36.62  ? 2327 LEU A CD1   1 
ATOM   3110 C  CD2   . LEU A 1 536 ? 125.078 98.921  100.424 1.00 29.56  ? 2327 LEU A CD2   1 
ATOM   3111 N  N     . ALA A 1 537 ? 122.031 97.578  103.344 1.00 29.17  ? 2328 ALA A N     1 
ATOM   3112 C  CA    . ALA A 1 537 ? 121.324 98.720  103.894 1.00 24.76  ? 2328 ALA A CA    1 
ATOM   3113 C  C     . ALA A 1 537 ? 122.302 99.848  104.194 1.00 23.73  ? 2328 ALA A C     1 
ATOM   3114 O  O     . ALA A 1 537 ? 123.502 99.633  104.380 1.00 36.27  ? 2328 ALA A O     1 
ATOM   3115 C  CB    . ALA A 1 537 ? 120.566 98.329  105.160 1.00 29.21  ? 2328 ALA A CB    1 
ATOM   3116 N  N     . ALA A 1 538 ? 121.775 101.068 104.245 1.00 17.47  ? 2329 ALA A N     1 
ATOM   3117 C  CA    . ALA A 1 538 ? 122.593 102.253 104.508 1.00 21.38  ? 2329 ALA A CA    1 
ATOM   3118 C  C     . ALA A 1 538 ? 121.810 103.156 105.457 1.00 22.23  ? 2329 ALA A C     1 
ATOM   3119 O  O     . ALA A 1 538 ? 121.025 104.001 105.023 1.00 22.77  ? 2329 ALA A O     1 
ATOM   3120 C  CB    . ALA A 1 538 ? 122.957 102.964 103.215 1.00 17.25  ? 2329 ALA A CB    1 
ATOM   3121 N  N     . ASP A 1 539 ? 122.047 102.983 106.753 1.00 30.27  ? 2330 ASP A N     1 
ATOM   3122 C  CA    . ASP A 1 539 ? 121.287 103.685 107.777 1.00 34.65  ? 2330 ASP A CA    1 
ATOM   3123 C  C     . ASP A 1 539 ? 121.940 105.022 108.094 1.00 36.89  ? 2330 ASP A C     1 
ATOM   3124 O  O     . ASP A 1 539 ? 123.132 105.080 108.405 1.00 45.96  ? 2330 ASP A O     1 
ATOM   3125 C  CB    . ASP A 1 539 ? 121.184 102.833 109.043 1.00 47.29  ? 2330 ASP A CB    1 
ATOM   3126 C  CG    . ASP A 1 539 ? 120.433 103.532 110.161 1.00 57.38  ? 2330 ASP A CG    1 
ATOM   3127 O  OD1   . ASP A 1 539 ? 119.220 103.785 110.002 1.00 56.39  ? 2330 ASP A OD1   1 
ATOM   3128 O  OD2   . ASP A 1 539 ? 121.057 103.823 111.203 1.00 57.30  ? 2330 ASP A OD2   1 
ATOM   3129 N  N     . TYR A 1 540 ? 121.158 106.092 108.010 1.00 31.71  ? 2331 TYR A N     1 
ATOM   3130 C  CA    . TYR A 1 540 ? 121.639 107.392 108.452 1.00 35.69  ? 2331 TYR A CA    1 
ATOM   3131 C  C     . TYR A 1 540 ? 121.892 107.361 109.953 1.00 41.58  ? 2331 TYR A C     1 
ATOM   3132 O  O     . TYR A 1 540 ? 121.053 106.887 110.725 1.00 51.40  ? 2331 TYR A O     1 
ATOM   3133 C  CB    . TYR A 1 540 ? 120.627 108.480 108.109 1.00 32.47  ? 2331 TYR A CB    1 
ATOM   3134 C  CG    . TYR A 1 540 ? 121.012 109.332 106.924 1.00 28.93  ? 2331 TYR A CG    1 
ATOM   3135 C  CD1   . TYR A 1 540 ? 122.229 109.996 106.890 1.00 29.60  ? 2331 TYR A CD1   1 
ATOM   3136 C  CD2   . TYR A 1 540 ? 120.153 109.484 105.846 1.00 30.51  ? 2331 TYR A CD2   1 
ATOM   3137 C  CE1   . TYR A 1 540 ? 122.582 110.779 105.811 1.00 34.52  ? 2331 TYR A CE1   1 
ATOM   3138 C  CE2   . TYR A 1 540 ? 120.496 110.267 104.766 1.00 30.56  ? 2331 TYR A CE2   1 
ATOM   3139 C  CZ    . TYR A 1 540 ? 121.712 110.910 104.752 1.00 36.52  ? 2331 TYR A CZ    1 
ATOM   3140 O  OH    . TYR A 1 540 ? 122.060 111.689 103.674 1.00 36.89  ? 2331 TYR A OH    1 
ATOM   3141 N  N     . SER A 1 541 ? 123.051 107.867 110.367 1.00 41.10  ? 2332 SER A N     1 
ATOM   3142 C  CA    . SER A 1 541 ? 123.430 107.881 111.778 1.00 44.97  ? 2332 SER A CA    1 
ATOM   3143 C  C     . SER A 1 541 ? 122.820 109.121 112.415 1.00 44.32  ? 2332 SER A C     1 
ATOM   3144 O  O     . SER A 1 541 ? 123.418 110.198 112.429 1.00 42.28  ? 2332 SER A O     1 
ATOM   3145 C  CB    . SER A 1 541 ? 124.944 107.850 111.932 1.00 52.19  ? 2332 SER A CB    1 
ATOM   3146 O  OG    . SER A 1 541 ? 125.439 106.529 111.808 1.00 53.90  ? 2332 SER A OG    1 
ATOM   3147 N  N     . GLN A 1 542 ? 121.610 108.961 112.950 1.00 46.28  ? 2333 GLN A N     1 
ATOM   3148 C  CA    . GLN A 1 542 ? 120.863 110.044 113.586 1.00 41.75  ? 2333 GLN A CA    1 
ATOM   3149 C  C     . GLN A 1 542 ? 120.702 111.229 112.632 1.00 36.18  ? 2333 GLN A C     1 
ATOM   3150 O  O     . GLN A 1 542 ? 121.148 112.346 112.899 1.00 38.10  ? 2333 GLN A O     1 
ATOM   3151 C  CB    . GLN A 1 542 ? 121.529 110.473 114.898 1.00 42.31  ? 2333 GLN A CB    1 
ATOM   3152 C  CG    . GLN A 1 542 ? 122.004 109.315 115.758 1.00 43.90  ? 2333 GLN A CG    1 
ATOM   3153 C  CD    . GLN A 1 542 ? 123.285 109.630 116.502 1.00 52.32  ? 2333 GLN A CD    1 
ATOM   3154 O  OE1   . GLN A 1 542 ? 123.480 110.747 116.979 1.00 53.54  ? 2333 GLN A OE1   1 
ATOM   3155 N  NE2   . GLN A 1 542 ? 124.167 108.644 116.605 1.00 58.00  ? 2333 GLN A NE2   1 
ATOM   3156 N  N     . LEU A 1 543 ? 120.050 110.959 111.498 1.00 32.45  ? 2334 LEU A N     1 
ATOM   3157 C  CA    . LEU A 1 543 ? 119.808 112.012 110.518 1.00 32.84  ? 2334 LEU A CA    1 
ATOM   3158 C  C     . LEU A 1 543 ? 118.955 113.123 111.108 1.00 36.45  ? 2334 LEU A C     1 
ATOM   3159 O  O     . LEU A 1 543 ? 119.196 114.307 110.849 1.00 47.45  ? 2334 LEU A O     1 
ATOM   3160 C  CB    . LEU A 1 543 ? 119.133 111.438 109.275 1.00 23.72  ? 2334 LEU A CB    1 
ATOM   3161 C  CG    . LEU A 1 543 ? 118.773 112.475 108.210 1.00 23.83  ? 2334 LEU A CG    1 
ATOM   3162 C  CD1   . LEU A 1 543 ? 120.026 113.129 107.667 1.00 26.08  ? 2334 LEU A CD1   1 
ATOM   3163 C  CD2   . LEU A 1 543 ? 117.961 111.857 107.088 1.00 30.72  ? 2334 LEU A CD2   1 
ATOM   3164 N  N     . GLU A 1 544 ? 117.945 112.757 111.895 1.00 29.60  ? 2335 GLU A N     1 
ATOM   3165 C  CA    . GLU A 1 544 ? 117.050 113.756 112.465 1.00 31.11  ? 2335 GLU A CA    1 
ATOM   3166 C  C     . GLU A 1 544 ? 117.792 114.699 113.401 1.00 35.94  ? 2335 GLU A C     1 
ATOM   3167 O  O     . GLU A 1 544 ? 117.608 115.920 113.338 1.00 41.43  ? 2335 GLU A O     1 
ATOM   3168 C  CB    . GLU A 1 544 ? 115.907 113.054 113.188 1.00 35.25  ? 2335 GLU A CB    1 
ATOM   3169 C  CG    . GLU A 1 544 ? 114.556 113.620 112.861 1.00 35.82  ? 2335 GLU A CG    1 
ATOM   3170 C  CD    . GLU A 1 544 ? 114.136 113.299 111.445 1.00 38.57  ? 2335 GLU A CD    1 
ATOM   3171 O  OE1   . GLU A 1 544 ? 113.515 114.166 110.802 1.00 32.58  ? 2335 GLU A OE1   1 
ATOM   3172 O  OE2   . GLU A 1 544 ? 114.465 112.200 110.957 1.00 45.36  ? 2335 GLU A OE2   1 
ATOM   3173 N  N     . LEU A 1 545 ? 118.649 114.154 114.265 1.00 33.10  ? 2336 LEU A N     1 
ATOM   3174 C  CA    . LEU A 1 545 ? 119.403 114.999 115.185 1.00 37.35  ? 2336 LEU A CA    1 
ATOM   3175 C  C     . LEU A 1 545 ? 120.392 115.889 114.440 1.00 40.56  ? 2336 LEU A C     1 
ATOM   3176 O  O     . LEU A 1 545 ? 120.551 117.065 114.782 1.00 44.01  ? 2336 LEU A O     1 
ATOM   3177 C  CB    . LEU A 1 545 ? 120.123 114.135 116.217 1.00 35.87  ? 2336 LEU A CB    1 
ATOM   3178 C  CG    . LEU A 1 545 ? 119.286 113.774 117.444 1.00 33.18  ? 2336 LEU A CG    1 
ATOM   3179 C  CD1   . LEU A 1 545 ? 119.829 112.526 118.108 1.00 36.63  ? 2336 LEU A CD1   1 
ATOM   3180 C  CD2   . LEU A 1 545 ? 119.255 114.934 118.423 1.00 34.52  ? 2336 LEU A CD2   1 
ATOM   3181 N  N     . ARG A 1 546 ? 121.066 115.347 113.423 1.00 38.33  ? 2337 ARG A N     1 
ATOM   3182 C  CA    . ARG A 1 546 ? 122.004 116.155 112.649 1.00 32.30  ? 2337 ARG A CA    1 
ATOM   3183 C  C     . ARG A 1 546 ? 121.290 117.288 111.927 1.00 36.35  ? 2337 ARG A C     1 
ATOM   3184 O  O     . ARG A 1 546 ? 121.772 118.426 111.909 1.00 43.04  ? 2337 ARG A O     1 
ATOM   3185 C  CB    . ARG A 1 546 ? 122.756 115.274 111.655 1.00 29.57  ? 2337 ARG A CB    1 
ATOM   3186 C  CG    . ARG A 1 546 ? 123.628 114.232 112.317 1.00 34.92  ? 2337 ARG A CG    1 
ATOM   3187 C  CD    . ARG A 1 546 ? 124.422 113.436 111.305 1.00 40.93  ? 2337 ARG A CD    1 
ATOM   3188 N  NE    . ARG A 1 546 ? 125.213 112.400 111.955 1.00 52.33  ? 2337 ARG A NE    1 
ATOM   3189 C  CZ    . ARG A 1 546 ? 126.373 112.615 112.559 1.00 59.20  ? 2337 ARG A CZ    1 
ATOM   3190 N  NH1   . ARG A 1 546 ? 126.919 113.818 112.598 1.00 61.09  ? 2337 ARG A NH1   1 
ATOM   3191 N  NH2   . ARG A 1 546 ? 127.001 111.596 113.139 1.00 56.50  ? 2337 ARG A NH2   1 
ATOM   3192 N  N     . ILE A 1 547 ? 120.132 117.001 111.334 1.00 36.45  ? 2338 ILE A N     1 
ATOM   3193 C  CA    . ILE A 1 547 ? 119.375 118.038 110.642 1.00 34.32  ? 2338 ILE A CA    1 
ATOM   3194 C  C     . ILE A 1 547 ? 118.886 119.093 111.626 1.00 43.24  ? 2338 ILE A C     1 
ATOM   3195 O  O     . ILE A 1 547 ? 118.931 120.299 111.342 1.00 48.33  ? 2338 ILE A O     1 
ATOM   3196 C  CB    . ILE A 1 547 ? 118.216 117.401 109.856 1.00 24.76  ? 2338 ILE A CB    1 
ATOM   3197 C  CG1   . ILE A 1 547 ? 118.767 116.599 108.677 1.00 25.08  ? 2338 ILE A CG1   1 
ATOM   3198 C  CG2   . ILE A 1 547 ? 117.250 118.456 109.374 1.00 25.61  ? 2338 ILE A CG2   1 
ATOM   3199 C  CD1   . ILE A 1 547 ? 117.760 116.332 107.595 1.00 28.48  ? 2338 ILE A CD1   1 
ATOM   3200 N  N     . LEU A 1 548 ? 118.412 118.663 112.797 1.00 40.59  ? 2339 LEU A N     1 
ATOM   3201 C  CA    . LEU A 1 548 ? 117.968 119.620 113.803 1.00 40.77  ? 2339 LEU A CA    1 
ATOM   3202 C  C     . LEU A 1 548 ? 119.118 120.502 114.264 1.00 43.51  ? 2339 LEU A C     1 
ATOM   3203 O  O     . LEU A 1 548 ? 118.943 121.708 114.460 1.00 50.08  ? 2339 LEU A O     1 
ATOM   3204 C  CB    . LEU A 1 548 ? 117.339 118.889 114.985 1.00 34.08  ? 2339 LEU A CB    1 
ATOM   3205 C  CG    . LEU A 1 548 ? 116.594 119.818 115.937 1.00 40.85  ? 2339 LEU A CG    1 
ATOM   3206 C  CD1   . LEU A 1 548 ? 115.598 120.647 115.168 1.00 36.15  ? 2339 LEU A CD1   1 
ATOM   3207 C  CD2   . LEU A 1 548 ? 115.889 119.020 117.002 1.00 46.50  ? 2339 LEU A CD2   1 
ATOM   3208 N  N     . ALA A 1 549 ? 120.304 119.917 114.442 1.00 39.33  ? 2340 ALA A N     1 
ATOM   3209 C  CA    . ALA A 1 549 ? 121.481 120.716 114.758 1.00 46.86  ? 2340 ALA A CA    1 
ATOM   3210 C  C     . ALA A 1 549 ? 121.830 121.665 113.622 1.00 46.12  ? 2340 ALA A C     1 
ATOM   3211 O  O     . ALA A 1 549 ? 122.364 122.753 113.864 1.00 56.61  ? 2340 ALA A O     1 
ATOM   3212 C  CB    . ALA A 1 549 ? 122.667 119.805 115.070 1.00 56.12  ? 2340 ALA A CB    1 
ATOM   3213 N  N     . HIS A 1 550 ? 121.552 121.268 112.380 1.00 43.39  ? 2341 HIS A N     1 
ATOM   3214 C  CA    . HIS A 1 550 ? 121.832 122.144 111.247 1.00 45.47  ? 2341 HIS A CA    1 
ATOM   3215 C  C     . HIS A 1 550 ? 120.948 123.384 111.277 1.00 49.48  ? 2341 HIS A C     1 
ATOM   3216 O  O     . HIS A 1 550 ? 121.441 124.512 111.170 1.00 56.53  ? 2341 HIS A O     1 
ATOM   3217 C  CB    . HIS A 1 550 ? 121.643 121.391 109.933 1.00 41.35  ? 2341 HIS A CB    1 
ATOM   3218 C  CG    . HIS A 1 550 ? 121.482 122.291 108.748 1.00 43.32  ? 2341 HIS A CG    1 
ATOM   3219 N  ND1   . HIS A 1 550 ? 122.555 122.833 108.074 1.00 49.49  ? 2341 HIS A ND1   1 
ATOM   3220 C  CD2   . HIS A 1 550 ? 120.374 122.754 108.124 1.00 49.78  ? 2341 HIS A CD2   1 
ATOM   3221 C  CE1   . HIS A 1 550 ? 122.115 123.586 107.083 1.00 50.59  ? 2341 HIS A CE1   1 
ATOM   3222 N  NE2   . HIS A 1 550 ? 120.795 123.555 107.090 1.00 54.25  ? 2341 HIS A NE2   1 
ATOM   3223 N  N     . LEU A 1 551 ? 119.634 123.200 111.419 1.00 46.89  ? 2342 LEU A N     1 
ATOM   3224 C  CA    . LEU A 1 551 ? 118.778 124.387 111.442 1.00 50.43  ? 2342 LEU A CA    1 
ATOM   3225 C  C     . LEU A 1 551 ? 118.676 125.034 112.817 1.00 54.26  ? 2342 LEU A C     1 
ATOM   3226 O  O     . LEU A 1 551 ? 117.982 126.047 112.950 1.00 59.05  ? 2342 LEU A O     1 
ATOM   3227 C  CB    . LEU A 1 551 ? 117.356 124.118 110.923 1.00 45.24  ? 2342 LEU A CB    1 
ATOM   3228 C  CG    . LEU A 1 551 ? 116.968 123.255 109.721 1.00 45.98  ? 2342 LEU A CG    1 
ATOM   3229 C  CD1   . LEU A 1 551 ? 116.751 121.824 110.109 1.00 41.25  ? 2342 LEU A CD1   1 
ATOM   3230 C  CD2   . LEU A 1 551 ? 115.724 123.816 109.047 1.00 47.90  ? 2342 LEU A CD2   1 
ATOM   3231 N  N     . SER A 1 552 ? 119.339 124.492 113.839 1.00 49.08  ? 2343 SER A N     1 
ATOM   3232 C  CA    . SER A 1 552 ? 119.367 125.126 115.148 1.00 53.44  ? 2343 SER A CA    1 
ATOM   3233 C  C     . SER A 1 552 ? 120.697 125.783 115.475 1.00 62.99  ? 2343 SER A C     1 
ATOM   3234 O  O     . SER A 1 552 ? 120.734 126.663 116.341 1.00 68.61  ? 2343 SER A O     1 
ATOM   3235 C  CB    . SER A 1 552 ? 119.042 124.103 116.245 1.00 57.67  ? 2343 SER A CB    1 
ATOM   3236 O  OG    . SER A 1 552 ? 120.109 123.187 116.412 1.00 59.57  ? 2343 SER A OG    1 
ATOM   3237 N  N     . HIS A 1 553 ? 121.778 125.381 114.805 1.00 64.06  ? 2344 HIS A N     1 
ATOM   3238 C  CA    . HIS A 1 553 ? 123.114 125.932 115.032 1.00 63.78  ? 2344 HIS A CA    1 
ATOM   3239 C  C     . HIS A 1 553 ? 123.532 125.814 116.496 1.00 67.47  ? 2344 HIS A C     1 
ATOM   3240 O  O     . HIS A 1 553 ? 124.120 126.733 117.070 1.00 70.03  ? 2344 HIS A O     1 
ATOM   3241 C  CB    . HIS A 1 553 ? 123.201 127.382 114.552 1.00 58.59  ? 2344 HIS A CB    1 
ATOM   3242 C  CG    . HIS A 1 553 ? 122.609 127.602 113.195 1.00 60.81  ? 2344 HIS A CG    1 
ATOM   3243 N  ND1   . HIS A 1 553 ? 121.366 128.169 113.007 1.00 64.97  ? 2344 HIS A ND1   1 
ATOM   3244 C  CD2   . HIS A 1 553 ? 123.086 127.324 111.959 1.00 60.52  ? 2344 HIS A CD2   1 
ATOM   3245 C  CE1   . HIS A 1 553 ? 121.106 128.234 111.713 1.00 61.96  ? 2344 HIS A CE1   1 
ATOM   3246 N  NE2   . HIS A 1 553 ? 122.134 127.728 111.055 1.00 61.52  ? 2344 HIS A NE2   1 
ATOM   3247 N  N     . ASP A 1 554 ? 123.224 124.673 117.107 1.00 65.78  ? 2345 ASP A N     1 
ATOM   3248 C  CA    . ASP A 1 554 ? 123.689 124.382 118.457 1.00 71.81  ? 2345 ASP A CA    1 
ATOM   3249 C  C     . ASP A 1 554 ? 125.153 123.974 118.401 1.00 78.72  ? 2345 ASP A C     1 
ATOM   3250 O  O     . ASP A 1 554 ? 125.491 122.953 117.795 1.00 80.16  ? 2345 ASP A O     1 
ATOM   3251 C  CB    . ASP A 1 554 ? 122.861 123.266 119.089 1.00 65.59  ? 2345 ASP A CB    1 
ATOM   3252 C  CG    . ASP A 1 554 ? 121.602 123.773 119.748 1.00 63.84  ? 2345 ASP A CG    1 
ATOM   3253 O  OD1   . ASP A 1 554 ? 120.575 123.875 119.052 1.00 62.07  ? 2345 ASP A OD1   1 
ATOM   3254 O  OD2   . ASP A 1 554 ? 121.639 124.063 120.962 1.00 65.12  ? 2345 ASP A OD2   1 
ATOM   3255 N  N     . ARG A 1 555 ? 126.023 124.764 119.033 1.00 79.81  ? 2346 ARG A N     1 
ATOM   3256 C  CA    . ARG A 1 555 ? 127.442 124.422 119.040 1.00 84.18  ? 2346 ARG A CA    1 
ATOM   3257 C  C     . ARG A 1 555 ? 127.682 123.092 119.743 1.00 84.80  ? 2346 ARG A C     1 
ATOM   3258 O  O     . ARG A 1 555 ? 128.471 122.264 119.270 1.00 87.31  ? 2346 ARG A O     1 
ATOM   3259 C  CB    . ARG A 1 555 ? 128.251 125.542 119.697 1.00 83.40  ? 2346 ARG A CB    1 
ATOM   3260 C  CG    . ARG A 1 555 ? 127.715 126.000 121.044 1.00 86.37  ? 2346 ARG A CG    1 
ATOM   3261 C  CD    . ARG A 1 555 ? 128.831 126.528 121.932 1.00 88.26  ? 2346 ARG A CD    1 
ATOM   3262 N  NE    . ARG A 1 555 ? 129.646 125.452 122.484 1.00 88.48  ? 2346 ARG A NE    1 
ATOM   3263 C  CZ    . ARG A 1 555 ? 129.298 124.702 123.520 1.00 90.29  ? 2346 ARG A CZ    1 
ATOM   3264 N  NH1   . ARG A 1 555 ? 128.149 124.884 124.151 1.00 93.64  ? 2346 ARG A NH1   1 
ATOM   3265 N  NH2   . ARG A 1 555 ? 130.124 123.746 123.936 1.00 87.21  ? 2346 ARG A NH2   1 
ATOM   3266 N  N     . ARG A 1 556 ? 127.001 122.863 120.867 1.00 79.04  ? 2347 ARG A N     1 
ATOM   3267 C  CA    . ARG A 1 556 ? 127.170 121.608 121.591 1.00 80.29  ? 2347 ARG A CA    1 
ATOM   3268 C  C     . ARG A 1 556 ? 126.659 120.425 120.780 1.00 76.31  ? 2347 ARG A C     1 
ATOM   3269 O  O     . ARG A 1 556 ? 127.318 119.382 120.711 1.00 78.22  ? 2347 ARG A O     1 
ATOM   3270 C  CB    . ARG A 1 556 ? 126.468 121.689 122.946 1.00 81.64  ? 2347 ARG A CB    1 
ATOM   3271 C  CG    . ARG A 1 556 ? 126.457 120.386 123.725 1.00 78.21  ? 2347 ARG A CG    1 
ATOM   3272 C  CD    . ARG A 1 556 ? 126.433 120.653 125.220 1.00 79.60  ? 2347 ARG A CD    1 
ATOM   3273 N  NE    . ARG A 1 556 ? 125.742 121.895 125.545 1.00 84.37  ? 2347 ARG A NE    1 
ATOM   3274 C  CZ    . ARG A 1 556 ? 125.751 122.465 126.742 1.00 87.70  ? 2347 ARG A CZ    1 
ATOM   3275 N  NH1   . ARG A 1 556 ? 126.407 121.928 127.758 1.00 84.57  ? 2347 ARG A NH1   1 
ATOM   3276 N  NH2   . ARG A 1 556 ? 125.092 123.605 126.923 1.00 85.76  ? 2347 ARG A NH2   1 
ATOM   3277 N  N     . LEU A 1 557 ? 125.491 120.567 120.149 1.00 75.10  ? 2348 LEU A N     1 
ATOM   3278 C  CA    . LEU A 1 557 ? 124.966 119.480 119.328 1.00 78.29  ? 2348 LEU A CA    1 
ATOM   3279 C  C     . LEU A 1 557 ? 125.859 119.212 118.123 1.00 81.32  ? 2348 LEU A C     1 
ATOM   3280 O  O     . LEU A 1 557 ? 126.099 118.052 117.769 1.00 81.03  ? 2348 LEU A O     1 
ATOM   3281 C  CB    . LEU A 1 557 ? 123.540 119.795 118.878 1.00 70.18  ? 2348 LEU A CB    1 
ATOM   3282 C  CG    . LEU A 1 557 ? 122.627 118.594 118.623 1.00 52.15  ? 2348 LEU A CG    1 
ATOM   3283 C  CD1   . LEU A 1 557 ? 122.772 117.565 119.729 1.00 63.25  ? 2348 LEU A CD1   1 
ATOM   3284 C  CD2   . LEU A 1 557 ? 121.183 119.042 118.497 1.00 46.96  ? 2348 LEU A CD2   1 
ATOM   3285 N  N     . ILE A 1 558 ? 126.360 120.268 117.478 1.00 83.45  ? 2349 ILE A N     1 
ATOM   3286 C  CA    . ILE A 1 558 ? 127.240 120.082 116.328 1.00 82.77  ? 2349 ILE A CA    1 
ATOM   3287 C  C     . ILE A 1 558 ? 128.523 119.376 116.746 1.00 80.94  ? 2349 ILE A C     1 
ATOM   3288 O  O     . ILE A 1 558 ? 128.985 118.445 116.075 1.00 80.24  ? 2349 ILE A O     1 
ATOM   3289 C  CB    . ILE A 1 558 ? 127.529 121.433 115.646 1.00 83.89  ? 2349 ILE A CB    1 
ATOM   3290 C  CG1   . ILE A 1 558 ? 126.284 121.945 114.920 1.00 76.88  ? 2349 ILE A CG1   1 
ATOM   3291 C  CG2   . ILE A 1 558 ? 128.689 121.305 114.672 1.00 80.53  ? 2349 ILE A CG2   1 
ATOM   3292 C  CD1   . ILE A 1 558 ? 126.266 123.445 114.718 1.00 73.55  ? 2349 ILE A CD1   1 
ATOM   3293 N  N     . GLN A 1 559 ? 129.114 119.796 117.868 1.00 80.90  ? 2350 GLN A N     1 
ATOM   3294 C  CA    . GLN A 1 559 ? 130.359 119.186 118.318 1.00 82.25  ? 2350 GLN A CA    1 
ATOM   3295 C  C     . GLN A 1 559 ? 130.155 117.779 118.869 1.00 79.22  ? 2350 GLN A C     1 
ATOM   3296 O  O     . GLN A 1 559 ? 131.107 116.993 118.887 1.00 79.96  ? 2350 GLN A O     1 
ATOM   3297 C  CB    . GLN A 1 559 ? 131.031 120.074 119.368 1.00 84.34  ? 2350 GLN A CB    1 
ATOM   3298 C  CG    . GLN A 1 559 ? 130.587 119.813 120.796 1.00 89.17  ? 2350 GLN A CG    1 
ATOM   3299 C  CD    . GLN A 1 559 ? 131.335 120.666 121.800 1.00 91.87  ? 2350 GLN A CD    1 
ATOM   3300 O  OE1   . GLN A 1 559 ? 132.010 121.628 121.434 1.00 88.08  ? 2350 GLN A OE1   1 
ATOM   3301 N  NE2   . GLN A 1 559 ? 131.221 120.316 123.076 1.00 95.04  ? 2350 GLN A NE2   1 
ATOM   3302 N  N     . VAL A 1 560 ? 128.943 117.442 119.314 1.00 76.37  ? 2351 VAL A N     1 
ATOM   3303 C  CA    . VAL A 1 560 ? 128.678 116.088 119.786 1.00 72.87  ? 2351 VAL A CA    1 
ATOM   3304 C  C     . VAL A 1 560 ? 128.230 115.161 118.660 1.00 77.19  ? 2351 VAL A C     1 
ATOM   3305 O  O     . VAL A 1 560 ? 128.297 113.934 118.818 1.00 79.56  ? 2351 VAL A O     1 
ATOM   3306 C  CB    . VAL A 1 560 ? 127.633 116.103 120.918 1.00 67.07  ? 2351 VAL A CB    1 
ATOM   3307 C  CG1   . VAL A 1 560 ? 126.223 116.114 120.357 1.00 65.61  ? 2351 VAL A CG1   1 
ATOM   3308 C  CG2   . VAL A 1 560 ? 127.835 114.918 121.850 1.00 58.94  ? 2351 VAL A CG2   1 
ATOM   3309 N  N     . LEU A 1 561 ? 127.778 115.708 117.532 1.00 79.41  ? 2352 LEU A N     1 
ATOM   3310 C  CA    . LEU A 1 561 ? 127.447 114.887 116.374 1.00 76.67  ? 2352 LEU A CA    1 
ATOM   3311 C  C     . LEU A 1 561 ? 128.626 114.698 115.430 1.00 81.66  ? 2352 LEU A C     1 
ATOM   3312 O  O     . LEU A 1 561 ? 128.729 113.648 114.786 1.00 74.27  ? 2352 LEU A O     1 
ATOM   3313 C  CB    . LEU A 1 561 ? 126.276 115.501 115.602 1.00 64.98  ? 2352 LEU A CB    1 
ATOM   3314 C  CG    . LEU A 1 561 ? 124.896 114.910 115.884 1.00 60.65  ? 2352 LEU A CG    1 
ATOM   3315 C  CD1   . LEU A 1 561 ? 124.929 113.401 115.713 1.00 60.37  ? 2352 LEU A CD1   1 
ATOM   3316 C  CD2   . LEU A 1 561 ? 124.413 115.284 117.272 1.00 68.54  ? 2352 LEU A CD2   1 
ATOM   3317 N  N     . ASN A 1 562 ? 129.518 115.689 115.334 1.00 85.10  ? 2353 ASN A N     1 
ATOM   3318 C  CA    . ASN A 1 562 ? 130.680 115.553 114.461 1.00 86.08  ? 2353 ASN A CA    1 
ATOM   3319 C  C     . ASN A 1 562 ? 131.581 114.410 114.906 1.00 90.95  ? 2353 ASN A C     1 
ATOM   3320 O  O     . ASN A 1 562 ? 132.235 113.773 114.072 1.00 94.37  ? 2353 ASN A O     1 
ATOM   3321 C  CB    . ASN A 1 562 ? 131.462 116.865 114.421 1.00 85.93  ? 2353 ASN A CB    1 
ATOM   3322 C  CG    . ASN A 1 562 ? 131.064 117.744 113.252 1.00 88.47  ? 2353 ASN A CG    1 
ATOM   3323 O  OD1   . ASN A 1 562 ? 130.845 117.260 112.142 1.00 81.43  ? 2353 ASN A OD1   1 
ATOM   3324 N  ND2   . ASN A 1 562 ? 130.967 119.045 113.497 1.00 94.00  ? 2353 ASN A ND2   1 
ATOM   3325 N  N     . THR A 1 563 ? 131.632 114.137 116.205 1.00 89.77  ? 2354 THR A N     1 
ATOM   3326 C  CA    . THR A 1 563 ? 132.370 113.002 116.730 1.00 89.22  ? 2354 THR A CA    1 
ATOM   3327 C  C     . THR A 1 563 ? 131.462 111.777 116.810 1.00 94.73  ? 2354 THR A C     1 
ATOM   3328 O  O     . THR A 1 563 ? 130.240 111.864 116.677 1.00 88.81  ? 2354 THR A O     1 
ATOM   3329 C  CB    . THR A 1 563 ? 132.947 113.326 118.107 1.00 82.16  ? 2354 THR A CB    1 
ATOM   3330 O  OG1   . THR A 1 563 ? 131.906 113.260 119.090 1.00 83.48  ? 2354 THR A OG1   1 
ATOM   3331 C  CG2   . THR A 1 563 ? 133.552 114.721 118.114 1.00 77.47  ? 2354 THR A CG2   1 
ATOM   3332 N  N     . GLY A 1 564 ? 132.079 110.619 117.029 1.00 97.63  ? 2355 GLY A N     1 
ATOM   3333 C  CA    . GLY A 1 564 ? 131.327 109.392 117.204 1.00 93.80  ? 2355 GLY A CA    1 
ATOM   3334 C  C     . GLY A 1 564 ? 130.799 109.239 118.615 1.00 96.82  ? 2355 GLY A C     1 
ATOM   3335 O  O     . GLY A 1 564 ? 130.973 108.192 119.245 1.00 105.48 ? 2355 GLY A O     1 
ATOM   3336 N  N     . ALA A 1 565 ? 130.148 110.288 119.123 1.00 90.37  ? 2356 ALA A N     1 
ATOM   3337 C  CA    . ALA A 1 565 ? 129.700 110.284 120.510 1.00 91.91  ? 2356 ALA A CA    1 
ATOM   3338 C  C     . ALA A 1 565 ? 128.519 109.348 120.729 1.00 93.41  ? 2356 ALA A C     1 
ATOM   3339 O  O     . ALA A 1 565 ? 128.398 108.757 121.809 1.00 92.98  ? 2356 ALA A O     1 
ATOM   3340 C  CB    . ALA A 1 565 ? 129.339 111.702 120.949 1.00 84.60  ? 2356 ALA A CB    1 
ATOM   3341 N  N     . ASP A 1 566 ? 127.644 109.199 119.731 1.00 85.20  ? 2357 ASP A N     1 
ATOM   3342 C  CA    . ASP A 1 566 ? 126.444 108.369 119.839 1.00 78.54  ? 2357 ASP A CA    1 
ATOM   3343 C  C     . ASP A 1 566 ? 125.568 108.845 121.003 1.00 81.98  ? 2357 ASP A C     1 
ATOM   3344 O  O     . ASP A 1 566 ? 125.430 108.188 122.036 1.00 84.76  ? 2357 ASP A O     1 
ATOM   3345 C  CB    . ASP A 1 566 ? 126.807 106.885 119.979 1.00 83.29  ? 2357 ASP A CB    1 
ATOM   3346 C  CG    . ASP A 1 566 ? 125.679 105.968 119.555 1.00 84.66  ? 2357 ASP A CG    1 
ATOM   3347 O  OD1   . ASP A 1 566 ? 124.666 106.476 119.029 1.00 76.52  ? 2357 ASP A OD1   1 
ATOM   3348 O  OD2   . ASP A 1 566 ? 125.804 104.741 119.744 1.00 89.62  ? 2357 ASP A OD2   1 
ATOM   3349 N  N     . VAL A 1 567 ? 125.006 110.042 120.805 1.00 73.53  ? 2358 VAL A N     1 
ATOM   3350 C  CA    . VAL A 1 567 ? 124.274 110.752 121.854 1.00 67.04  ? 2358 VAL A CA    1 
ATOM   3351 C  C     . VAL A 1 567 ? 123.182 109.892 122.480 1.00 66.15  ? 2358 VAL A C     1 
ATOM   3352 O  O     . VAL A 1 567 ? 122.856 110.055 123.662 1.00 69.35  ? 2358 VAL A O     1 
ATOM   3353 C  CB    . VAL A 1 567 ? 123.705 112.070 121.283 1.00 51.13  ? 2358 VAL A CB    1 
ATOM   3354 C  CG1   . VAL A 1 567 ? 122.820 111.792 120.082 1.00 51.38  ? 2358 VAL A CG1   1 
ATOM   3355 C  CG2   . VAL A 1 567 ? 122.948 112.850 122.349 1.00 48.65  ? 2358 VAL A CG2   1 
ATOM   3356 N  N     . PHE A 1 568 ? 122.602 108.964 121.715 1.00 67.41  ? 2359 PHE A N     1 
ATOM   3357 C  CA    . PHE A 1 568 ? 121.594 108.074 122.284 1.00 67.06  ? 2359 PHE A CA    1 
ATOM   3358 C  C     . PHE A 1 568 ? 122.193 107.179 123.363 1.00 73.57  ? 2359 PHE A C     1 
ATOM   3359 O  O     . PHE A 1 568 ? 121.593 106.985 124.427 1.00 76.24  ? 2359 PHE A O     1 
ATOM   3360 C  CB    . PHE A 1 568 ? 120.953 107.233 121.182 1.00 65.07  ? 2359 PHE A CB    1 
ATOM   3361 C  CG    . PHE A 1 568 ? 119.981 107.995 120.333 1.00 52.64  ? 2359 PHE A CG    1 
ATOM   3362 C  CD1   . PHE A 1 568 ? 119.352 109.124 120.825 1.00 46.65  ? 2359 PHE A CD1   1 
ATOM   3363 C  CD2   . PHE A 1 568 ? 119.702 107.587 119.042 1.00 51.56  ? 2359 PHE A CD2   1 
ATOM   3364 C  CE1   . PHE A 1 568 ? 118.461 109.828 120.048 1.00 44.66  ? 2359 PHE A CE1   1 
ATOM   3365 C  CE2   . PHE A 1 568 ? 118.812 108.288 118.261 1.00 47.26  ? 2359 PHE A CE2   1 
ATOM   3366 C  CZ    . PHE A 1 568 ? 118.191 109.409 118.765 1.00 45.52  ? 2359 PHE A CZ    1 
ATOM   3367 N  N     . ARG A 1 569 ? 123.381 106.631 123.108 1.00 76.46  ? 2360 ARG A N     1 
ATOM   3368 C  CA    . ARG A 1 569 ? 124.060 105.839 124.127 1.00 83.94  ? 2360 ARG A CA    1 
ATOM   3369 C  C     . ARG A 1 569 ? 124.396 106.688 125.346 1.00 84.80  ? 2360 ARG A C     1 
ATOM   3370 O  O     . ARG A 1 569 ? 124.275 106.225 126.485 1.00 86.78  ? 2360 ARG A O     1 
ATOM   3371 C  CB    . ARG A 1 569 ? 125.324 105.208 123.544 1.00 87.35  ? 2360 ARG A CB    1 
ATOM   3372 C  CG    . ARG A 1 569 ? 125.444 103.715 123.796 1.00 88.15  ? 2360 ARG A CG    1 
ATOM   3373 C  CD    . ARG A 1 569 ? 126.406 103.064 122.818 1.00 87.20  ? 2360 ARG A CD    1 
ATOM   3374 N  NE    . ARG A 1 569 ? 125.716 102.519 121.655 1.00 87.89  ? 2360 ARG A NE    1 
ATOM   3375 C  CZ    . ARG A 1 569 ? 125.349 101.251 121.526 1.00 88.16  ? 2360 ARG A CZ    1 
ATOM   3376 N  NH1   . ARG A 1 569 ? 125.593 100.362 122.473 1.00 88.67  ? 2360 ARG A NH1   1 
ATOM   3377 N  NH2   . ARG A 1 569 ? 124.723 100.866 120.417 1.00 81.16  ? 2360 ARG A NH2   1 
ATOM   3378 N  N     . SER A 1 570 ? 124.816 107.936 125.125 1.00 84.11  ? 2361 SER A N     1 
ATOM   3379 C  CA    . SER A 1 570 ? 125.143 108.820 126.239 1.00 85.46  ? 2361 SER A CA    1 
ATOM   3380 C  C     . SER A 1 570 ? 123.918 109.095 127.105 1.00 84.05  ? 2361 SER A C     1 
ATOM   3381 O  O     . SER A 1 570 ? 123.992 109.045 128.338 1.00 85.81  ? 2361 SER A O     1 
ATOM   3382 C  CB    . SER A 1 570 ? 125.733 110.130 125.714 1.00 81.50  ? 2361 SER A CB    1 
ATOM   3383 O  OG    . SER A 1 570 ? 126.938 109.903 125.005 1.00 83.41  ? 2361 SER A OG    1 
ATOM   3384 N  N     . ILE A 1 571 ? 122.778 109.393 126.476 1.00 78.30  ? 2362 ILE A N     1 
ATOM   3385 C  CA    . ILE A 1 571 ? 121.579 109.682 127.256 1.00 74.26  ? 2362 ILE A CA    1 
ATOM   3386 C  C     . ILE A 1 571 ? 121.073 108.425 127.952 1.00 80.88  ? 2362 ILE A C     1 
ATOM   3387 O  O     . ILE A 1 571 ? 120.567 108.497 129.078 1.00 87.54  ? 2362 ILE A O     1 
ATOM   3388 C  CB    . ILE A 1 571 ? 120.491 110.342 126.384 1.00 76.72  ? 2362 ILE A CB    1 
ATOM   3389 C  CG1   . ILE A 1 571 ? 119.375 110.902 127.268 1.00 80.20  ? 2362 ILE A CG1   1 
ATOM   3390 C  CG2   . ILE A 1 571 ? 119.912 109.372 125.373 1.00 73.12  ? 2362 ILE A CG2   1 
ATOM   3391 C  CD1   . ILE A 1 571 ? 118.578 112.011 126.621 1.00 72.96  ? 2362 ILE A CD1   1 
ATOM   3392 N  N     . ALA A 1 572 ? 121.211 107.255 127.320 1.00 80.47  ? 2363 ALA A N     1 
ATOM   3393 C  CA    . ALA A 1 572 ? 120.842 106.013 127.993 1.00 83.29  ? 2363 ALA A CA    1 
ATOM   3394 C  C     . ALA A 1 572 ? 121.718 105.766 129.215 1.00 90.81  ? 2363 ALA A C     1 
ATOM   3395 O  O     . ALA A 1 572 ? 121.223 105.358 130.273 1.00 92.19  ? 2363 ALA A O     1 
ATOM   3396 C  CB    . ALA A 1 572 ? 120.938 104.840 127.020 1.00 77.15  ? 2363 ALA A CB    1 
ATOM   3397 N  N     . ALA A 1 573 ? 123.025 106.005 129.085 1.00 89.03  ? 2364 ALA A N     1 
ATOM   3398 C  CA    . ALA A 1 573 ? 123.932 105.825 130.213 1.00 88.01  ? 2364 ALA A CA    1 
ATOM   3399 C  C     . ALA A 1 573 ? 123.625 106.812 131.330 1.00 89.62  ? 2364 ALA A C     1 
ATOM   3400 O  O     . ALA A 1 573 ? 123.700 106.465 132.514 1.00 94.58  ? 2364 ALA A O     1 
ATOM   3401 C  CB    . ALA A 1 573 ? 125.380 105.971 129.749 1.00 90.50  ? 2364 ALA A CB    1 
ATOM   3402 N  N     . GLU A 1 574 ? 123.293 108.054 130.975 1.00 87.69  ? 2365 GLU A N     1 
ATOM   3403 C  CA    . GLU A 1 574 ? 122.916 109.035 131.987 1.00 84.13  ? 2365 GLU A CA    1 
ATOM   3404 C  C     . GLU A 1 574 ? 121.626 108.631 132.690 1.00 81.04  ? 2365 GLU A C     1 
ATOM   3405 O  O     . GLU A 1 574 ? 121.491 108.808 133.907 1.00 83.76  ? 2365 GLU A O     1 
ATOM   3406 C  CB    . GLU A 1 574 ? 122.772 110.417 131.350 1.00 85.93  ? 2365 GLU A CB    1 
ATOM   3407 C  CG    . GLU A 1 574 ? 124.092 111.049 130.935 1.00 88.84  ? 2365 GLU A CG    1 
ATOM   3408 C  CD    . GLU A 1 574 ? 124.677 111.939 132.013 1.00 85.27  ? 2365 GLU A CD    1 
ATOM   3409 O  OE1   . GLU A 1 574 ? 124.105 111.988 133.122 1.00 86.37  ? 2365 GLU A OE1   1 
ATOM   3410 O  OE2   . GLU A 1 574 ? 125.711 112.589 131.753 1.00 80.08  ? 2365 GLU A OE2   1 
ATOM   3411 N  N     . TRP A 1 575 ? 120.665 108.089 131.940 1.00 79.99  ? 2366 TRP A N     1 
ATOM   3412 C  CA    . TRP A 1 575 ? 119.391 107.694 132.531 1.00 80.30  ? 2366 TRP A CA    1 
ATOM   3413 C  C     . TRP A 1 575 ? 119.558 106.503 133.468 1.00 85.57  ? 2366 TRP A C     1 
ATOM   3414 O  O     . TRP A 1 575 ? 119.043 106.511 134.592 1.00 89.72  ? 2366 TRP A O     1 
ATOM   3415 C  CB    . TRP A 1 575 ? 118.384 107.379 131.422 1.00 80.84  ? 2366 TRP A CB    1 
ATOM   3416 C  CG    . TRP A 1 575 ? 117.097 106.782 131.907 1.00 83.07  ? 2366 TRP A CG    1 
ATOM   3417 C  CD1   . TRP A 1 575 ? 116.481 107.017 133.102 1.00 86.20  ? 2366 TRP A CD1   1 
ATOM   3418 C  CD2   . TRP A 1 575 ? 116.266 105.851 131.204 1.00 84.00  ? 2366 TRP A CD2   1 
ATOM   3419 N  NE1   . TRP A 1 575 ? 115.321 106.288 133.187 1.00 92.07  ? 2366 TRP A NE1   1 
ATOM   3420 C  CE2   . TRP A 1 575 ? 115.165 105.564 132.034 1.00 89.34  ? 2366 TRP A CE2   1 
ATOM   3421 C  CE3   . TRP A 1 575 ? 116.347 105.231 129.953 1.00 77.87  ? 2366 TRP A CE3   1 
ATOM   3422 C  CZ2   . TRP A 1 575 ? 114.154 104.685 131.656 1.00 86.19  ? 2366 TRP A CZ2   1 
ATOM   3423 C  CZ3   . TRP A 1 575 ? 115.341 104.359 129.579 1.00 82.25  ? 2366 TRP A CZ3   1 
ATOM   3424 C  CH2   . TRP A 1 575 ? 114.260 104.094 130.427 1.00 86.50  ? 2366 TRP A CH2   1 
ATOM   3425 N  N     . LYS A 1 576 ? 120.274 105.472 133.028 1.00 85.78  ? 2367 LYS A N     1 
ATOM   3426 C  CA    . LYS A 1 576 ? 120.396 104.244 133.803 1.00 87.87  ? 2367 LYS A CA    1 
ATOM   3427 C  C     . LYS A 1 576 ? 121.610 104.224 134.724 1.00 93.82  ? 2367 LYS A C     1 
ATOM   3428 O  O     . LYS A 1 576 ? 121.800 103.237 135.443 1.00 93.95  ? 2367 LYS A O     1 
ATOM   3429 C  CB    . LYS A 1 576 ? 120.441 103.033 132.867 1.00 84.05  ? 2367 LYS A CB    1 
ATOM   3430 C  CG    . LYS A 1 576 ? 119.075 102.586 132.370 1.00 83.21  ? 2367 LYS A CG    1 
ATOM   3431 C  CD    . LYS A 1 576 ? 118.053 102.568 133.496 1.00 79.18  ? 2367 LYS A CD    1 
ATOM   3432 C  CE    . LYS A 1 576 ? 116.670 102.212 132.980 1.00 75.38  ? 2367 LYS A CE    1 
ATOM   3433 N  NZ    . LYS A 1 576 ? 116.602 100.796 132.524 1.00 69.26  ? 2367 LYS A NZ    1 
ATOM   3434 N  N     . MET A 1 577 ? 122.424 105.281 134.725 1.00 97.70  ? 2368 MET A N     1 
ATOM   3435 C  CA    . MET A 1 577 ? 123.605 105.375 135.587 1.00 94.61  ? 2368 MET A CA    1 
ATOM   3436 C  C     . MET A 1 577 ? 124.541 104.184 135.392 1.00 95.97  ? 2368 MET A C     1 
ATOM   3437 O  O     . MET A 1 577 ? 125.101 103.646 136.349 1.00 93.68  ? 2368 MET A O     1 
ATOM   3438 C  CB    . MET A 1 577 ? 123.201 105.516 137.059 1.00 91.81  ? 2368 MET A CB    1 
ATOM   3439 C  CG    . MET A 1 577 ? 122.139 106.581 137.343 1.00 93.26  ? 2368 MET A CG    1 
ATOM   3440 S  SD    . MET A 1 577 ? 122.544 108.325 137.049 1.00 98.08  ? 2368 MET A SD    1 
ATOM   3441 C  CE    . MET A 1 577 ? 124.337 108.346 137.039 1.00 76.47  ? 2368 MET A CE    1 
ATOM   3442 N  N     . ILE A 1 578 ? 124.714 103.767 134.139 1.00 101.33 ? 2369 ILE A N     1 
ATOM   3443 C  CA    . ILE A 1 578 ? 125.575 102.646 133.795 1.00 103.44 ? 2369 ILE A CA    1 
ATOM   3444 C  C     . ILE A 1 578 ? 126.553 103.097 132.719 1.00 103.45 ? 2369 ILE A C     1 
ATOM   3445 O  O     . ILE A 1 578 ? 126.484 104.216 132.211 1.00 103.72 ? 2369 ILE A O     1 
ATOM   3446 C  CB    . ILE A 1 578 ? 124.777 101.415 133.319 1.00 100.93 ? 2369 ILE A CB    1 
ATOM   3447 C  CG1   . ILE A 1 578 ? 123.910 101.777 132.112 1.00 90.99  ? 2369 ILE A CG1   1 
ATOM   3448 C  CG2   . ILE A 1 578 ? 123.924 100.861 134.451 1.00 94.70  ? 2369 ILE A CG2   1 
ATOM   3449 C  CD1   . ILE A 1 578 ? 123.050 100.638 131.614 1.00 88.03  ? 2369 ILE A CD1   1 
ATOM   3450 N  N     . GLU A 1 579 ? 127.481 102.206 132.384 1.00 106.50 ? 2370 GLU A N     1 
ATOM   3451 C  CA    . GLU A 1 579 ? 128.433 102.494 131.328 1.00 105.67 ? 2370 GLU A CA    1 
ATOM   3452 C  C     . GLU A 1 579 ? 127.725 102.526 129.974 1.00 108.56 ? 2370 GLU A C     1 
ATOM   3453 O  O     . GLU A 1 579 ? 126.772 101.777 129.745 1.00 109.87 ? 2370 GLU A O     1 
ATOM   3454 C  CB    . GLU A 1 579 ? 129.546 101.449 131.310 1.00 106.75 ? 2370 GLU A CB    1 
ATOM   3455 N  N     . PRO A 1 580 ? 128.164 103.401 129.063 1.00 106.37 ? 2371 PRO A N     1 
ATOM   3456 C  CA    . PRO A 1 580 ? 127.530 103.443 127.734 1.00 104.29 ? 2371 PRO A CA    1 
ATOM   3457 C  C     . PRO A 1 580 ? 127.611 102.124 126.987 1.00 104.35 ? 2371 PRO A C     1 
ATOM   3458 O  O     . PRO A 1 580 ? 126.674 101.767 126.263 1.00 98.32  ? 2371 PRO A O     1 
ATOM   3459 C  CB    . PRO A 1 580 ? 128.306 104.556 127.015 1.00 100.24 ? 2371 PRO A CB    1 
ATOM   3460 C  CG    . PRO A 1 580 ? 128.874 105.395 128.109 1.00 100.56 ? 2371 PRO A CG    1 
ATOM   3461 C  CD    . PRO A 1 580 ? 129.187 104.446 129.225 1.00 98.63  ? 2371 PRO A CD    1 
ATOM   3462 N  N     . GLU A 1 581 ? 128.710 101.383 127.145 1.00 107.60 ? 2372 GLU A N     1 
ATOM   3463 C  CA    . GLU A 1 581 ? 128.839 100.094 126.478 1.00 109.17 ? 2372 GLU A CA    1 
ATOM   3464 C  C     . GLU A 1 581 ? 127.961 99.025  127.113 1.00 113.03 ? 2372 GLU A C     1 
ATOM   3465 O  O     . GLU A 1 581 ? 127.723 97.985  126.489 1.00 115.22 ? 2372 GLU A O     1 
ATOM   3466 C  CB    . GLU A 1 581 ? 130.300 99.640  126.486 1.00 100.89 ? 2372 GLU A CB    1 
ATOM   3467 N  N     . SER A 1 582 ? 127.475 99.255  128.332 1.00 110.03 ? 2373 SER A N     1 
ATOM   3468 C  CA    . SER A 1 582 ? 126.621 98.292  129.015 1.00 107.80 ? 2373 SER A CA    1 
ATOM   3469 C  C     . SER A 1 582 ? 125.171 98.355  128.556 1.00 104.55 ? 2373 SER A C     1 
ATOM   3470 O  O     . SER A 1 582 ? 124.374 97.499  128.956 1.00 103.93 ? 2373 SER A O     1 
ATOM   3471 C  CB    . SER A 1 582 ? 126.693 98.516  130.529 1.00 99.94  ? 2373 SER A CB    1 
ATOM   3472 O  OG    . SER A 1 582 ? 125.950 97.535  131.232 1.00 97.71  ? 2373 SER A OG    1 
ATOM   3473 N  N     . VAL A 1 583 ? 124.812 99.336  127.727 1.00 100.65 ? 2374 VAL A N     1 
ATOM   3474 C  CA    . VAL A 1 583 ? 123.429 99.483  127.295 1.00 99.27  ? 2374 VAL A CA    1 
ATOM   3475 C  C     . VAL A 1 583 ? 123.058 98.361  126.331 1.00 100.02 ? 2374 VAL A C     1 
ATOM   3476 O  O     . VAL A 1 583 ? 123.911 97.795  125.632 1.00 103.26 ? 2374 VAL A O     1 
ATOM   3477 C  CB    . VAL A 1 583 ? 123.209 100.867 126.655 1.00 94.00  ? 2374 VAL A CB    1 
ATOM   3478 C  CG1   . VAL A 1 583 ? 123.668 100.870 125.206 1.00 86.80  ? 2374 VAL A CG1   1 
ATOM   3479 C  CG2   . VAL A 1 583 ? 121.750 101.274 126.756 1.00 88.20  ? 2374 VAL A CG2   1 
ATOM   3480 N  N     . GLY A 1 584 ? 121.769 98.017  126.311 1.00 97.78  ? 2375 GLY A N     1 
ATOM   3481 C  CA    . GLY A 1 584 ? 121.242 97.044  125.383 1.00 97.04  ? 2375 GLY A CA    1 
ATOM   3482 C  C     . GLY A 1 584 ? 120.534 97.705  124.208 1.00 91.90  ? 2375 GLY A C     1 
ATOM   3483 O  O     . GLY A 1 584 ? 120.427 98.924  124.107 1.00 85.31  ? 2375 GLY A O     1 
ATOM   3484 N  N     . ASP A 1 585 ? 120.046 96.858  123.300 1.00 95.94  ? 2376 ASP A N     1 
ATOM   3485 C  CA    . ASP A 1 585 ? 119.346 97.370  122.126 1.00 98.23  ? 2376 ASP A CA    1 
ATOM   3486 C  C     . ASP A 1 585 ? 118.000 97.978  122.509 1.00 95.42  ? 2376 ASP A C     1 
ATOM   3487 O  O     . ASP A 1 585 ? 117.661 99.083  122.069 1.00 93.67  ? 2376 ASP A O     1 
ATOM   3488 C  CB    . ASP A 1 585 ? 119.174 96.260  121.084 1.00 105.54 ? 2376 ASP A CB    1 
ATOM   3489 C  CG    . ASP A 1 585 ? 118.211 95.173  121.529 1.00 105.18 ? 2376 ASP A CG    1 
ATOM   3490 O  OD1   . ASP A 1 585 ? 118.411 94.605  122.623 1.00 112.37 ? 2376 ASP A OD1   1 
ATOM   3491 O  OD2   . ASP A 1 585 ? 117.250 94.889  120.784 1.00 87.14  ? 2376 ASP A OD2   1 
ATOM   3492 N  N     . ASP A 1 586 ? 117.224 97.277  123.340 1.00 91.24  ? 2377 ASP A N     1 
ATOM   3493 C  CA    . ASP A 1 586 ? 115.916 97.790  123.732 1.00 84.23  ? 2377 ASP A CA    1 
ATOM   3494 C  C     . ASP A 1 586 ? 116.049 99.014  124.628 1.00 85.29  ? 2377 ASP A C     1 
ATOM   3495 O  O     . ASP A 1 586 ? 115.266 99.963  124.512 1.00 85.16  ? 2377 ASP A O     1 
ATOM   3496 C  CB    . ASP A 1 586 ? 115.108 96.698  124.431 1.00 83.98  ? 2377 ASP A CB    1 
ATOM   3497 C  CG    . ASP A 1 586 ? 113.629 96.775  124.110 1.00 88.99  ? 2377 ASP A CG    1 
ATOM   3498 O  OD1   . ASP A 1 586 ? 113.285 96.908  122.917 1.00 84.90  ? 2377 ASP A OD1   1 
ATOM   3499 O  OD2   . ASP A 1 586 ? 112.810 96.705  125.051 1.00 88.91  ? 2377 ASP A OD2   1 
ATOM   3500 N  N     . LEU A 1 587 ? 117.031 99.008  125.532 1.00 89.98  ? 2378 LEU A N     1 
ATOM   3501 C  CA    . LEU A 1 587 ? 117.256 100.173 126.381 1.00 87.91  ? 2378 LEU A CA    1 
ATOM   3502 C  C     . LEU A 1 587 ? 117.664 101.384 125.553 1.00 85.10  ? 2378 LEU A C     1 
ATOM   3503 O  O     . LEU A 1 587 ? 117.187 102.499 125.791 1.00 84.44  ? 2378 LEU A O     1 
ATOM   3504 C  CB    . LEU A 1 587 ? 118.317 99.855  127.433 1.00 88.80  ? 2378 LEU A CB    1 
ATOM   3505 C  CG    . LEU A 1 587 ? 118.543 100.910 128.515 1.00 89.24  ? 2378 LEU A CG    1 
ATOM   3506 C  CD1   . LEU A 1 587 ? 117.228 101.294 129.169 1.00 83.59  ? 2378 LEU A CD1   1 
ATOM   3507 C  CD2   . LEU A 1 587 ? 119.529 100.395 129.549 1.00 94.83  ? 2378 LEU A CD2   1 
ATOM   3508 N  N     . ARG A 1 588 ? 118.543 101.183 124.567 1.00 87.91  ? 2379 ARG A N     1 
ATOM   3509 C  CA    . ARG A 1 588 ? 118.933 102.284 123.694 1.00 86.46  ? 2379 ARG A CA    1 
ATOM   3510 C  C     . ARG A 1 588 ? 117.754 102.781 122.870 1.00 77.20  ? 2379 ARG A C     1 
ATOM   3511 O  O     . ARG A 1 588 ? 117.609 103.988 122.648 1.00 74.28  ? 2379 ARG A O     1 
ATOM   3512 C  CB    . ARG A 1 588 ? 120.081 101.858 122.781 1.00 86.07  ? 2379 ARG A CB    1 
ATOM   3513 C  CG    . ARG A 1 588 ? 120.544 102.956 121.842 1.00 74.51  ? 2379 ARG A CG    1 
ATOM   3514 C  CD    . ARG A 1 588 ? 121.882 102.628 121.212 1.00 83.07  ? 2379 ARG A CD    1 
ATOM   3515 N  NE    . ARG A 1 588 ? 122.305 103.671 120.287 1.00 82.18  ? 2379 ARG A NE    1 
ATOM   3516 C  CZ    . ARG A 1 588 ? 121.934 103.734 119.016 1.00 77.88  ? 2379 ARG A CZ    1 
ATOM   3517 N  NH1   . ARG A 1 588 ? 121.141 102.819 118.484 1.00 78.49  ? 2379 ARG A NH1   1 
ATOM   3518 N  NH2   . ARG A 1 588 ? 122.371 104.737 118.261 1.00 58.56  ? 2379 ARG A NH2   1 
ATOM   3519 N  N     . GLN A 1 589 ? 116.906 101.866 122.395 1.00 73.33  ? 2380 GLN A N     1 
ATOM   3520 C  CA    . GLN A 1 589 ? 115.730 102.282 121.639 1.00 69.63  ? 2380 GLN A CA    1 
ATOM   3521 C  C     . GLN A 1 589 ? 114.775 103.091 122.506 1.00 73.29  ? 2380 GLN A C     1 
ATOM   3522 O  O     . GLN A 1 589 ? 114.222 104.100 122.057 1.00 66.57  ? 2380 GLN A O     1 
ATOM   3523 C  CB    . GLN A 1 589 ? 115.021 101.065 121.052 1.00 69.23  ? 2380 GLN A CB    1 
ATOM   3524 C  CG    . GLN A 1 589 ? 115.721 100.482 119.843 1.00 70.64  ? 2380 GLN A CG    1 
ATOM   3525 C  CD    . GLN A 1 589 ? 115.877 101.490 118.721 1.00 82.64  ? 2380 GLN A CD    1 
ATOM   3526 O  OE1   . GLN A 1 589 ? 116.916 101.548 118.065 1.00 87.95  ? 2380 GLN A OE1   1 
ATOM   3527 N  NE2   . GLN A 1 589 ? 114.838 102.285 118.489 1.00 86.14  ? 2380 GLN A NE2   1 
ATOM   3528 N  N     . GLN A 1 590 ? 114.571 102.665 123.754 1.00 79.93  ? 2381 GLN A N     1 
ATOM   3529 C  CA    . GLN A 1 590 ? 113.733 103.433 124.669 1.00 74.28  ? 2381 GLN A CA    1 
ATOM   3530 C  C     . GLN A 1 590 ? 114.334 104.806 124.936 1.00 68.49  ? 2381 GLN A C     1 
ATOM   3531 O  O     . GLN A 1 590 ? 113.613 105.810 124.993 1.00 66.58  ? 2381 GLN A O     1 
ATOM   3532 C  CB    . GLN A 1 590 ? 113.543 102.665 125.976 1.00 68.54  ? 2381 GLN A CB    1 
ATOM   3533 C  CG    . GLN A 1 590 ? 112.229 102.950 126.679 1.00 66.76  ? 2381 GLN A CG    1 
ATOM   3534 C  CD    . GLN A 1 590 ? 111.887 101.895 127.711 1.00 79.52  ? 2381 GLN A CD    1 
ATOM   3535 O  OE1   . GLN A 1 590 ? 112.662 100.968 127.947 1.00 81.13  ? 2381 GLN A OE1   1 
ATOM   3536 N  NE2   . GLN A 1 590 ? 110.721 102.030 128.331 1.00 84.36  ? 2381 GLN A NE2   1 
ATOM   3537 N  N     . ALA A 1 591 ? 115.657 104.870 125.099 1.00 67.73  ? 2382 ALA A N     1 
ATOM   3538 C  CA    . ALA A 1 591 ? 116.317 106.152 125.314 1.00 62.71  ? 2382 ALA A CA    1 
ATOM   3539 C  C     . ALA A 1 591 ? 116.153 107.068 124.110 1.00 57.21  ? 2382 ALA A C     1 
ATOM   3540 O  O     . ALA A 1 591 ? 115.938 108.274 124.264 1.00 59.41  ? 2382 ALA A O     1 
ATOM   3541 C  CB    . ALA A 1 591 ? 117.796 105.938 125.624 1.00 72.36  ? 2382 ALA A CB    1 
ATOM   3542 N  N     . LYS A 1 592 ? 116.264 106.517 122.900 1.00 57.17  ? 2383 LYS A N     1 
ATOM   3543 C  CA    . LYS A 1 592 ? 116.100 107.336 121.703 1.00 52.34  ? 2383 LYS A CA    1 
ATOM   3544 C  C     . LYS A 1 592 ? 114.655 107.796 121.547 1.00 46.50  ? 2383 LYS A C     1 
ATOM   3545 O  O     . LYS A 1 592 ? 114.403 108.930 121.122 1.00 44.26  ? 2383 LYS A O     1 
ATOM   3546 C  CB    . LYS A 1 592 ? 116.581 106.572 120.466 1.00 48.33  ? 2383 LYS A CB    1 
ATOM   3547 C  CG    . LYS A 1 592 ? 115.494 105.902 119.642 1.00 45.19  ? 2383 LYS A CG    1 
ATOM   3548 C  CD    . LYS A 1 592 ? 115.857 105.867 118.171 1.00 44.99  ? 2383 LYS A CD    1 
ATOM   3549 C  CE    . LYS A 1 592 ? 116.916 104.817 117.895 1.00 51.29  ? 2383 LYS A CE    1 
ATOM   3550 N  NZ    . LYS A 1 592 ? 116.887 104.362 116.478 1.00 54.02  ? 2383 LYS A NZ    1 
ATOM   3551 N  N     . GLN A 1 593 ? 113.719 106.957 121.927 1.00 46.40  ? 2384 GLN A N     1 
ATOM   3552 C  CA    . GLN A 1 593 ? 112.298 107.365 121.902 1.00 50.20  ? 2384 GLN A CA    1 
ATOM   3553 C  C     . GLN A 1 593 ? 112.085 108.512 122.876 1.00 52.98  ? 2384 GLN A C     1 
ATOM   3554 O  O     . GLN A 1 593 ? 111.407 109.454 122.527 1.00 48.88  ? 2384 GLN A O     1 
ATOM   3555 C  CB    . GLN A 1 593 ? 111.357 106.189 122.139 1.00 54.91  ? 2384 GLN A CB    1 
ATOM   3556 C  CG    . GLN A 1 593 ? 111.620 105.017 121.210 1.00 58.83  ? 2384 GLN A CG    1 
ATOM   3557 C  CD    . GLN A 1 593 ? 110.345 104.425 120.668 1.00 60.69  ? 2384 GLN A CD    1 
ATOM   3558 O  OE1   . GLN A 1 593 ? 110.356 103.620 119.741 1.00 60.87  ? 2384 GLN A OE1   1 
ATOM   3559 N  NE2   . GLN A 1 593 ? 109.229 104.832 121.250 1.00 56.53  ? 2384 GLN A NE2   1 
ATOM   3560 N  N     . ILE A 1 594 ? 112.664 108.406 124.073 1.00 59.09  ? 2385 ILE A N     1 
ATOM   3561 C  CA    . ILE A 1 594 ? 112.556 109.479 125.057 1.00 54.32  ? 2385 ILE A CA    1 
ATOM   3562 C  C     . ILE A 1 594 ? 113.162 110.764 124.508 1.00 54.18  ? 2385 ILE A C     1 
ATOM   3563 O  O     . ILE A 1 594 ? 112.532 111.830 124.539 1.00 53.08  ? 2385 ILE A O     1 
ATOM   3564 C  CB    . ILE A 1 594 ? 113.230 109.063 126.377 1.00 48.40  ? 2385 ILE A CB    1 
ATOM   3565 C  CG1   . ILE A 1 594 ? 112.439 107.946 127.058 1.00 60.13  ? 2385 ILE A CG1   1 
ATOM   3566 C  CG2   . ILE A 1 594 ? 113.371 110.255 127.304 1.00 46.86  ? 2385 ILE A CG2   1 
ATOM   3567 C  CD1   . ILE A 1 594 ? 111.089 108.381 127.562 1.00 71.77  ? 2385 ILE A CD1   1 
ATOM   3568 N  N     . CYS A 1 595 ? 114.389 110.675 123.988 1.00 55.83  ? 2386 CYS A N     1 
ATOM   3569 C  CA    . CYS A 1 595 ? 115.098 111.862 123.522 1.00 52.25  ? 2386 CYS A CA    1 
ATOM   3570 C  C     . CYS A 1 595 ? 114.343 112.549 122.395 1.00 49.53  ? 2386 CYS A C     1 
ATOM   3571 O  O     . CYS A 1 595 ? 114.184 113.775 122.404 1.00 55.95  ? 2386 CYS A O     1 
ATOM   3572 C  CB    . CYS A 1 595 ? 116.509 111.490 123.068 1.00 49.06  ? 2386 CYS A CB    1 
ATOM   3573 S  SG    . CYS A 1 595 ? 117.345 112.777 122.117 1.00 50.31  ? 2386 CYS A SG    1 
ATOM   3574 N  N     . TYR A 1 596 ? 113.855 111.778 121.422 1.00 41.96  ? 2387 TYR A N     1 
ATOM   3575 C  CA    . TYR A 1 596 ? 113.034 112.372 120.375 1.00 40.67  ? 2387 TYR A CA    1 
ATOM   3576 C  C     . TYR A 1 596 ? 111.727 112.913 120.937 1.00 49.41  ? 2387 TYR A C     1 
ATOM   3577 O  O     . TYR A 1 596 ? 111.166 113.865 120.386 1.00 54.49  ? 2387 TYR A O     1 
ATOM   3578 C  CB    . TYR A 1 596 ? 112.770 111.351 119.272 1.00 40.72  ? 2387 TYR A CB    1 
ATOM   3579 C  CG    . TYR A 1 596 ? 113.896 111.252 118.272 1.00 32.02  ? 2387 TYR A CG    1 
ATOM   3580 C  CD1   . TYR A 1 596 ? 114.515 112.391 117.781 1.00 32.91  ? 2387 TYR A CD1   1 
ATOM   3581 C  CD2   . TYR A 1 596 ? 114.346 110.020 117.826 1.00 32.53  ? 2387 TYR A CD2   1 
ATOM   3582 C  CE1   . TYR A 1 596 ? 115.545 112.305 116.871 1.00 30.08  ? 2387 TYR A CE1   1 
ATOM   3583 C  CE2   . TYR A 1 596 ? 115.375 109.925 116.918 1.00 29.08  ? 2387 TYR A CE2   1 
ATOM   3584 C  CZ    . TYR A 1 596 ? 115.970 111.070 116.443 1.00 28.46  ? 2387 TYR A CZ    1 
ATOM   3585 O  OH    . TYR A 1 596 ? 116.997 110.975 115.536 1.00 44.03  ? 2387 TYR A OH    1 
ATOM   3586 N  N     . GLY A 1 597 ? 111.234 112.330 122.031 1.00 50.30  ? 2388 GLY A N     1 
ATOM   3587 C  CA    . GLY A 1 597 ? 110.043 112.868 122.663 1.00 49.89  ? 2388 GLY A CA    1 
ATOM   3588 C  C     . GLY A 1 597 ? 110.250 114.272 123.194 1.00 50.89  ? 2388 GLY A C     1 
ATOM   3589 O  O     . GLY A 1 597 ? 109.434 115.164 122.953 1.00 55.69  ? 2388 GLY A O     1 
ATOM   3590 N  N     . ILE A 1 598 ? 111.351 114.493 123.921 1.00 41.10  ? 2389 ILE A N     1 
ATOM   3591 C  CA    . ILE A 1 598 ? 111.622 115.874 124.332 1.00 37.00  ? 2389 ILE A CA    1 
ATOM   3592 C  C     . ILE A 1 598 ? 111.928 116.735 123.114 1.00 41.39  ? 2389 ILE A C     1 
ATOM   3593 O  O     . ILE A 1 598 ? 111.571 117.920 123.079 1.00 43.24  ? 2389 ILE A O     1 
ATOM   3594 C  CB    . ILE A 1 598 ? 112.741 116.046 125.388 1.00 43.00  ? 2389 ILE A CB    1 
ATOM   3595 C  CG1   . ILE A 1 598 ? 112.693 115.039 126.539 1.00 49.69  ? 2389 ILE A CG1   1 
ATOM   3596 C  CG2   . ILE A 1 598 ? 112.738 117.464 125.943 1.00 62.24  ? 2389 ILE A CG2   1 
ATOM   3597 C  CD1   . ILE A 1 598 ? 113.460 113.801 126.331 1.00 52.36  ? 2389 ILE A CD1   1 
ATOM   3598 N  N     . ILE A 1 599 ? 112.582 116.166 122.100 1.00 44.07  ? 2390 ILE A N     1 
ATOM   3599 C  CA    . ILE A 1 599 ? 113.004 116.957 120.948 1.00 46.14  ? 2390 ILE A CA    1 
ATOM   3600 C  C     . ILE A 1 599 ? 111.789 117.531 120.226 1.00 47.87  ? 2390 ILE A C     1 
ATOM   3601 O  O     . ILE A 1 599 ? 111.766 118.709 119.851 1.00 49.76  ? 2390 ILE A O     1 
ATOM   3602 C  CB    . ILE A 1 599 ? 113.876 116.101 120.011 1.00 46.29  ? 2390 ILE A CB    1 
ATOM   3603 C  CG1   . ILE A 1 599 ? 115.334 116.140 120.471 1.00 43.09  ? 2390 ILE A CG1   1 
ATOM   3604 C  CG2   . ILE A 1 599 ? 113.748 116.567 118.569 1.00 44.17  ? 2390 ILE A CG2   1 
ATOM   3605 C  CD1   . ILE A 1 599 ? 116.066 117.401 120.114 1.00 43.43  ? 2390 ILE A CD1   1 
ATOM   3606 N  N     . TYR A 1 600 ? 110.759 116.709 120.032 1.00 47.94  ? 2391 TYR A N     1 
ATOM   3607 C  CA    . TYR A 1 600 ? 109.529 117.139 119.379 1.00 41.46  ? 2391 TYR A CA    1 
ATOM   3608 C  C     . TYR A 1 600 ? 108.530 117.771 120.337 1.00 43.50  ? 2391 TYR A C     1 
ATOM   3609 O  O     . TYR A 1 600 ? 107.510 118.299 119.882 1.00 37.11  ? 2391 TYR A O     1 
ATOM   3610 C  CB    . TYR A 1 600 ? 108.862 115.955 118.674 1.00 35.54  ? 2391 TYR A CB    1 
ATOM   3611 C  CG    . TYR A 1 600 ? 109.640 115.423 117.495 1.00 34.91  ? 2391 TYR A CG    1 
ATOM   3612 C  CD1   . TYR A 1 600 ? 110.476 116.250 116.760 1.00 35.00  ? 2391 TYR A CD1   1 
ATOM   3613 C  CD2   . TYR A 1 600 ? 109.538 114.093 117.118 1.00 34.04  ? 2391 TYR A CD2   1 
ATOM   3614 C  CE1   . TYR A 1 600 ? 111.188 115.767 115.684 1.00 31.97  ? 2391 TYR A CE1   1 
ATOM   3615 C  CE2   . TYR A 1 600 ? 110.245 113.601 116.043 1.00 31.76  ? 2391 TYR A CE2   1 
ATOM   3616 C  CZ    . TYR A 1 600 ? 111.069 114.441 115.331 1.00 31.50  ? 2391 TYR A CZ    1 
ATOM   3617 O  OH    . TYR A 1 600 ? 111.773 113.952 114.258 1.00 39.70  ? 2391 TYR A OH    1 
ATOM   3618 N  N     . GLY A 1 601 ? 108.790 117.730 121.642 1.00 51.72  ? 2392 GLY A N     1 
ATOM   3619 C  CA    . GLY A 1 601 ? 107.869 118.282 122.615 1.00 50.70  ? 2392 GLY A CA    1 
ATOM   3620 C  C     . GLY A 1 601 ? 106.982 117.227 123.241 1.00 54.05  ? 2392 GLY A C     1 
ATOM   3621 O  O     . GLY A 1 601 ? 106.051 116.730 122.600 1.00 61.56  ? 2392 GLY A O     1 
ATOM   3622 N  N     . MET A 1 602 ? 107.260 116.877 124.493 1.00 46.93  ? 2393 MET A N     1 
ATOM   3623 C  CA    . MET A 1 602 ? 106.527 115.845 125.210 1.00 42.84  ? 2393 MET A CA    1 
ATOM   3624 C  C     . MET A 1 602 ? 105.957 116.415 126.499 1.00 49.36  ? 2393 MET A C     1 
ATOM   3625 O  O     . MET A 1 602 ? 106.616 117.202 127.186 1.00 54.04  ? 2393 MET A O     1 
ATOM   3626 C  CB    . MET A 1 602 ? 107.427 114.650 125.535 1.00 45.27  ? 2393 MET A CB    1 
ATOM   3627 C  CG    . MET A 1 602 ? 107.223 113.451 124.636 1.00 39.68  ? 2393 MET A CG    1 
ATOM   3628 S  SD    . MET A 1 602 ? 107.856 111.926 125.355 1.00 43.27  ? 2393 MET A SD    1 
ATOM   3629 C  CE    . MET A 1 602 ? 106.327 111.123 125.820 1.00 67.95  ? 2393 MET A CE    1 
ATOM   3630 N  N     . GLY A 1 603 ? 104.732 116.014 126.823 1.00 56.18  ? 2394 GLY A N     1 
ATOM   3631 C  CA    . GLY A 1 603 ? 104.158 116.384 128.099 1.00 71.50  ? 2394 GLY A CA    1 
ATOM   3632 C  C     . GLY A 1 603 ? 104.863 115.694 129.251 1.00 75.49  ? 2394 GLY A C     1 
ATOM   3633 O  O     . GLY A 1 603 ? 105.443 114.618 129.106 1.00 73.96  ? 2394 GLY A O     1 
ATOM   3634 N  N     . ALA A 1 604 ? 104.817 116.339 130.418 1.00 78.11  ? 2395 ALA A N     1 
ATOM   3635 C  CA    . ALA A 1 604 ? 105.466 115.775 131.597 1.00 81.90  ? 2395 ALA A CA    1 
ATOM   3636 C  C     . ALA A 1 604 ? 104.831 114.448 131.995 1.00 82.33  ? 2395 ALA A C     1 
ATOM   3637 O  O     . ALA A 1 604 ? 105.535 113.504 132.370 1.00 79.84  ? 2395 ALA A O     1 
ATOM   3638 C  CB    . ALA A 1 604 ? 105.408 116.768 132.757 1.00 85.79  ? 2395 ALA A CB    1 
ATOM   3639 N  N     . LYS A 1 605 ? 103.502 114.358 131.919 1.00 83.66  ? 2396 LYS A N     1 
ATOM   3640 C  CA    . LYS A 1 605 ? 102.812 113.143 132.338 1.00 79.01  ? 2396 LYS A CA    1 
ATOM   3641 C  C     . LYS A 1 605 ? 103.180 111.957 131.453 1.00 80.77  ? 2396 LYS A C     1 
ATOM   3642 O  O     . LYS A 1 605 ? 103.464 110.862 131.953 1.00 81.17  ? 2396 LYS A O     1 
ATOM   3643 C  CB    . LYS A 1 605 ? 101.302 113.374 132.326 1.00 79.99  ? 2396 LYS A CB    1 
ATOM   3644 C  CG    . LYS A 1 605 ? 100.487 112.200 132.831 1.00 81.26  ? 2396 LYS A CG    1 
ATOM   3645 C  CD    . LYS A 1 605 ? 99.091  112.214 132.237 1.00 82.28  ? 2396 LYS A CD    1 
ATOM   3646 C  CE    . LYS A 1 605 ? 98.293  113.409 132.730 1.00 86.95  ? 2396 LYS A CE    1 
ATOM   3647 N  NZ    . LYS A 1 605 ? 96.920  113.425 132.155 1.00 80.77  ? 2396 LYS A NZ    1 
ATOM   3648 N  N     . SER A 1 606 ? 103.169 112.154 130.131 1.00 78.62  ? 2397 SER A N     1 
ATOM   3649 C  CA    . SER A 1 606 ? 103.482 111.057 129.219 1.00 75.16  ? 2397 SER A CA    1 
ATOM   3650 C  C     . SER A 1 606 ? 104.932 110.617 129.361 1.00 77.59  ? 2397 SER A C     1 
ATOM   3651 O  O     . SER A 1 606 ? 105.232 109.415 129.336 1.00 78.07  ? 2397 SER A O     1 
ATOM   3652 C  CB    . SER A 1 606 ? 103.184 111.469 127.778 1.00 68.92  ? 2397 SER A CB    1 
ATOM   3653 O  OG    . SER A 1 606 ? 103.257 110.354 126.907 1.00 71.59  ? 2397 SER A OG    1 
ATOM   3654 N  N     . LEU A 1 607 ? 105.846 111.578 129.507 1.00 77.24  ? 2398 LEU A N     1 
ATOM   3655 C  CA    . LEU A 1 607 ? 107.244 111.236 129.740 1.00 77.35  ? 2398 LEU A CA    1 
ATOM   3656 C  C     . LEU A 1 607 ? 107.404 110.474 131.046 1.00 85.48  ? 2398 LEU A C     1 
ATOM   3657 O  O     . LEU A 1 607 ? 108.225 109.556 131.140 1.00 87.31  ? 2398 LEU A O     1 
ATOM   3658 C  CB    . LEU A 1 607 ? 108.106 112.498 129.748 1.00 69.11  ? 2398 LEU A CB    1 
ATOM   3659 C  CG    . LEU A 1 607 ? 109.610 112.244 129.860 1.00 73.37  ? 2398 LEU A CG    1 
ATOM   3660 C  CD1   . LEU A 1 607 ? 110.155 111.761 128.532 1.00 60.04  ? 2398 LEU A CD1   1 
ATOM   3661 C  CD2   . LEU A 1 607 ? 110.346 113.487 130.321 1.00 85.54  ? 2398 LEU A CD2   1 
ATOM   3662 N  N     . GLY A 1 608 ? 106.631 110.842 132.068 1.00 87.21  ? 2399 GLY A N     1 
ATOM   3663 C  CA    . GLY A 1 608 ? 106.677 110.102 133.317 1.00 91.41  ? 2399 GLY A CA    1 
ATOM   3664 C  C     . GLY A 1 608 ? 106.182 108.676 133.172 1.00 89.22  ? 2399 GLY A C     1 
ATOM   3665 O  O     . GLY A 1 608 ? 106.796 107.741 133.691 1.00 91.62  ? 2399 GLY A O     1 
ATOM   3666 N  N     . GLU A 1 609 ? 105.064 108.489 132.463 1.00 82.37  ? 2400 GLU A N     1 
ATOM   3667 C  CA    . GLU A 1 609 ? 104.534 107.139 132.285 1.00 78.84  ? 2400 GLU A CA    1 
ATOM   3668 C  C     . GLU A 1 609 ? 105.491 106.269 131.478 1.00 79.95  ? 2400 GLU A C     1 
ATOM   3669 O  O     . GLU A 1 609 ? 105.684 105.090 131.799 1.00 75.25  ? 2400 GLU A O     1 
ATOM   3670 C  CB    . GLU A 1 609 ? 103.156 107.164 131.618 1.00 79.68  ? 2400 GLU A CB    1 
ATOM   3671 C  CG    . GLU A 1 609 ? 102.028 107.737 132.468 1.00 81.23  ? 2400 GLU A CG    1 
ATOM   3672 C  CD    . GLU A 1 609 ? 100.990 108.486 131.647 1.00 80.35  ? 2400 GLU A CD    1 
ATOM   3673 O  OE1   . GLU A 1 609 ? 99.858  107.974 131.518 1.00 69.21  ? 2400 GLU A OE1   1 
ATOM   3674 O  OE2   . GLU A 1 609 ? 101.296 109.574 131.122 1.00 85.28  ? 2400 GLU A OE2   1 
ATOM   3675 N  N     . GLN A 1 610 ? 106.097 106.828 130.428 1.00 83.83  ? 2401 GLN A N     1 
ATOM   3676 C  CA    . GLN A 1 610 ? 107.008 106.040 129.601 1.00 83.43  ? 2401 GLN A CA    1 
ATOM   3677 C  C     . GLN A 1 610 ? 108.324 105.768 130.321 1.00 81.20  ? 2401 GLN A C     1 
ATOM   3678 O  O     . GLN A 1 610 ? 108.858 104.654 130.254 1.00 87.82  ? 2401 GLN A O     1 
ATOM   3679 C  CB    . GLN A 1 610 ? 107.262 106.755 128.274 1.00 80.32  ? 2401 GLN A CB    1 
ATOM   3680 C  CG    . GLN A 1 610 ? 108.304 106.080 127.402 1.00 76.50  ? 2401 GLN A CG    1 
ATOM   3681 C  CD    . GLN A 1 610 ? 108.119 106.384 125.932 1.00 76.90  ? 2401 GLN A CD    1 
ATOM   3682 O  OE1   . GLN A 1 610 ? 107.948 107.539 125.542 1.00 69.92  ? 2401 GLN A OE1   1 
ATOM   3683 N  NE2   . GLN A 1 610 ? 108.155 105.347 125.105 1.00 78.02  ? 2401 GLN A NE2   1 
ATOM   3684 N  N     . MET A 1 611 ? 108.863 106.770 131.012 1.00 78.57  ? 2402 MET A N     1 
ATOM   3685 C  CA    . MET A 1 611 ? 110.154 106.643 131.673 1.00 89.53  ? 2402 MET A CA    1 
ATOM   3686 C  C     . MET A 1 611 ? 110.066 105.888 132.992 1.00 97.13  ? 2402 MET A C     1 
ATOM   3687 O  O     . MET A 1 611 ? 111.105 105.520 133.550 1.00 96.20  ? 2402 MET A O     1 
ATOM   3688 C  CB    . MET A 1 611 ? 110.746 108.036 131.904 1.00 90.95  ? 2402 MET A CB    1 
ATOM   3689 C  CG    . MET A 1 611 ? 112.261 108.091 131.981 1.00 86.94  ? 2402 MET A CG    1 
ATOM   3690 S  SD    . MET A 1 611 ? 112.829 109.802 131.937 1.00 91.02  ? 2402 MET A SD    1 
ATOM   3691 C  CE    . MET A 1 611 ? 114.604 109.587 131.892 1.00 78.16  ? 2402 MET A CE    1 
ATOM   3692 N  N     . GLY A 1 612 ? 108.860 105.649 133.502 1.00 95.64  ? 2403 GLY A N     1 
ATOM   3693 C  CA    . GLY A 1 612 ? 108.717 104.982 134.779 1.00 92.10  ? 2403 GLY A CA    1 
ATOM   3694 C  C     . GLY A 1 612 ? 109.078 105.832 135.972 1.00 88.34  ? 2403 GLY A C     1 
ATOM   3695 O  O     . GLY A 1 612 ? 109.403 105.289 137.032 1.00 89.69  ? 2403 GLY A O     1 
ATOM   3696 N  N     . ILE A 1 613 ? 109.044 107.155 135.830 1.00 87.36  ? 2404 ILE A N     1 
ATOM   3697 C  CA    . ILE A 1 613 ? 109.392 108.077 136.899 1.00 91.69  ? 2404 ILE A CA    1 
ATOM   3698 C  C     . ILE A 1 613 ? 108.188 108.968 137.190 1.00 97.38  ? 2404 ILE A C     1 
ATOM   3699 O  O     . ILE A 1 613 ? 107.176 108.935 136.490 1.00 90.99  ? 2404 ILE A O     1 
ATOM   3700 C  CB    . ILE A 1 613 ? 110.639 108.918 136.559 1.00 90.93  ? 2404 ILE A CB    1 
ATOM   3701 C  CG1   . ILE A 1 613 ? 110.260 110.124 135.696 1.00 96.31  ? 2404 ILE A CG1   1 
ATOM   3702 C  CG2   . ILE A 1 613 ? 111.687 108.064 135.862 1.00 88.55  ? 2404 ILE A CG2   1 
ATOM   3703 C  CD1   . ILE A 1 613 ? 111.450 110.905 135.187 1.00 95.73  ? 2404 ILE A CD1   1 
ATOM   3704 N  N     . LYS A 1 614 ? 108.312 109.765 138.248 1.00 102.61 ? 2405 LYS A N     1 
ATOM   3705 C  CA    . LYS A 1 614 ? 107.227 110.637 138.669 1.00 102.73 ? 2405 LYS A CA    1 
ATOM   3706 C  C     . LYS A 1 614 ? 107.039 111.789 137.685 1.00 97.96  ? 2405 LYS A C     1 
ATOM   3707 O  O     . LYS A 1 614 ? 107.906 112.090 136.861 1.00 97.71  ? 2405 LYS A O     1 
ATOM   3708 C  CB    . LYS A 1 614 ? 107.496 111.183 140.071 1.00 99.09  ? 2405 LYS A CB    1 
ATOM   3709 C  CG    . LYS A 1 614 ? 107.333 110.155 141.179 1.00 93.25  ? 2405 LYS A CG    1 
ATOM   3710 C  CD    . LYS A 1 614 ? 107.556 110.778 142.547 1.00 92.46  ? 2405 LYS A CD    1 
ATOM   3711 C  CE    . LYS A 1 614 ? 106.695 112.015 142.739 1.00 91.14  ? 2405 LYS A CE    1 
ATOM   3712 N  NZ    . LYS A 1 614 ? 105.249 111.728 142.533 1.00 92.15  ? 2405 LYS A NZ    1 
ATOM   3713 N  N     . GLU A 1 615 ? 105.873 112.433 137.778 1.00 96.35  ? 2406 GLU A N     1 
ATOM   3714 C  CA    . GLU A 1 615 ? 105.568 113.551 136.890 1.00 96.06  ? 2406 GLU A CA    1 
ATOM   3715 C  C     . GLU A 1 615 ? 106.508 114.726 137.130 1.00 95.88  ? 2406 GLU A C     1 
ATOM   3716 O  O     . GLU A 1 615 ? 106.969 115.365 136.177 1.00 94.57  ? 2406 GLU A O     1 
ATOM   3717 C  CB    . GLU A 1 615 ? 104.113 113.982 137.069 1.00 97.76  ? 2406 GLU A CB    1 
ATOM   3718 C  CG    . GLU A 1 615 ? 103.660 115.057 136.094 1.00 96.71  ? 2406 GLU A CG    1 
ATOM   3719 C  CD    . GLU A 1 615 ? 102.151 115.173 136.012 1.00 99.09  ? 2406 GLU A CD    1 
ATOM   3720 O  OE1   . GLU A 1 615 ? 101.467 114.733 136.959 1.00 105.06 ? 2406 GLU A OE1   1 
ATOM   3721 O  OE2   . GLU A 1 615 ? 101.647 115.704 135.000 1.00 92.16  ? 2406 GLU A OE2   1 
ATOM   3722 N  N     . ASN A 1 616 ? 106.793 115.037 138.397 1.00 100.45 ? 2407 ASN A N     1 
ATOM   3723 C  CA    . ASN A 1 616 ? 107.716 116.127 138.698 1.00 98.54  ? 2407 ASN A CA    1 
ATOM   3724 C  C     . ASN A 1 616 ? 109.124 115.810 138.211 1.00 93.55  ? 2407 ASN A C     1 
ATOM   3725 O  O     . ASN A 1 616 ? 109.826 116.692 137.701 1.00 90.52  ? 2407 ASN A O     1 
ATOM   3726 C  CB    . ASN A 1 616 ? 107.717 116.416 140.199 1.00 102.91 ? 2407 ASN A CB    1 
ATOM   3727 C  CG    . ASN A 1 616 ? 106.396 116.980 140.683 1.00 104.89 ? 2407 ASN A CG    1 
ATOM   3728 O  OD1   . ASN A 1 616 ? 105.723 117.719 139.965 1.00 108.13 ? 2407 ASN A OD1   1 
ATOM   3729 N  ND2   . ASN A 1 616 ? 106.019 116.634 141.908 1.00 103.67 ? 2407 ASN A ND2   1 
ATOM   3730 N  N     . ASP A 1 617 ? 109.556 114.557 138.364 1.00 91.90  ? 2408 ASP A N     1 
ATOM   3731 C  CA    . ASP A 1 617 ? 110.864 114.161 137.853 1.00 94.92  ? 2408 ASP A CA    1 
ATOM   3732 C  C     . ASP A 1 617 ? 110.913 114.264 136.333 1.00 98.71  ? 2408 ASP A C     1 
ATOM   3733 O  O     . ASP A 1 617 ? 111.923 114.691 135.764 1.00 98.95  ? 2408 ASP A O     1 
ATOM   3734 C  CB    . ASP A 1 617 ? 111.196 112.741 138.311 1.00 94.38  ? 2408 ASP A CB    1 
ATOM   3735 C  CG    . ASP A 1 617 ? 111.488 112.662 139.797 1.00 103.56 ? 2408 ASP A CG    1 
ATOM   3736 O  OD1   . ASP A 1 617 ? 111.459 113.715 140.467 1.00 103.78 ? 2408 ASP A OD1   1 
ATOM   3737 O  OD2   . ASP A 1 617 ? 111.746 111.546 140.294 1.00 113.23 ? 2408 ASP A OD2   1 
ATOM   3738 N  N     . ALA A 1 618 ? 109.827 113.878 135.659 1.00 99.69  ? 2409 ALA A N     1 
ATOM   3739 C  CA    . ALA A 1 618 ? 109.770 114.026 134.208 1.00 91.89  ? 2409 ALA A CA    1 
ATOM   3740 C  C     . ALA A 1 618 ? 109.830 115.492 133.801 1.00 88.33  ? 2409 ALA A C     1 
ATOM   3741 O  O     . ALA A 1 618 ? 110.492 115.844 132.820 1.00 87.95  ? 2409 ALA A O     1 
ATOM   3742 C  CB    . ALA A 1 618 ? 108.506 113.365 133.662 1.00 88.74  ? 2409 ALA A CB    1 
ATOM   3743 N  N     . ALA A 1 619 ? 109.138 116.361 134.540 1.00 91.31  ? 2410 ALA A N     1 
ATOM   3744 C  CA    . ALA A 1 619 ? 109.182 117.788 134.237 1.00 85.62  ? 2410 ALA A CA    1 
ATOM   3745 C  C     . ALA A 1 619 ? 110.585 118.351 134.432 1.00 86.61  ? 2410 ALA A C     1 
ATOM   3746 O  O     . ALA A 1 619 ? 111.053 119.166 133.628 1.00 86.57  ? 2410 ALA A O     1 
ATOM   3747 C  CB    . ALA A 1 619 ? 108.175 118.542 135.104 1.00 88.82  ? 2410 ALA A CB    1 
ATOM   3748 N  N     . CYS A 1 620 ? 111.271 117.931 135.498 1.00 87.74  ? 2411 CYS A N     1 
ATOM   3749 C  CA    . CYS A 1 620 ? 112.639 118.393 135.708 1.00 85.50  ? 2411 CYS A CA    1 
ATOM   3750 C  C     . CYS A 1 620 ? 113.576 117.861 134.630 1.00 85.43  ? 2411 CYS A C     1 
ATOM   3751 O  O     . CYS A 1 620 ? 114.502 118.566 134.215 1.00 86.50  ? 2411 CYS A O     1 
ATOM   3752 C  CB    . CYS A 1 620 ? 113.128 117.999 137.104 1.00 85.77  ? 2411 CYS A CB    1 
ATOM   3753 S  SG    . CYS A 1 620 ? 114.050 116.446 137.215 1.00 89.07  ? 2411 CYS A SG    1 
ATOM   3754 N  N     . TYR A 1 621 ? 113.345 116.634 134.156 1.00 83.63  ? 2412 TYR A N     1 
ATOM   3755 C  CA    . TYR A 1 621 ? 114.123 116.110 133.037 1.00 82.82  ? 2412 TYR A CA    1 
ATOM   3756 C  C     . TYR A 1 621 ? 113.880 116.925 131.773 1.00 81.38  ? 2412 TYR A C     1 
ATOM   3757 O  O     . TYR A 1 621 ? 114.819 117.219 131.022 1.00 79.50  ? 2412 TYR A O     1 
ATOM   3758 C  CB    . TYR A 1 621 ? 113.773 114.641 132.804 1.00 79.05  ? 2412 TYR A CB    1 
ATOM   3759 C  CG    . TYR A 1 621 ? 114.808 113.874 132.015 1.00 79.21  ? 2412 TYR A CG    1 
ATOM   3760 C  CD1   . TYR A 1 621 ? 114.795 113.876 130.628 1.00 72.49  ? 2412 TYR A CD1   1 
ATOM   3761 C  CD2   . TYR A 1 621 ? 115.796 113.143 132.659 1.00 78.07  ? 2412 TYR A CD2   1 
ATOM   3762 C  CE1   . TYR A 1 621 ? 115.738 113.174 129.904 1.00 70.27  ? 2412 TYR A CE1   1 
ATOM   3763 C  CE2   . TYR A 1 621 ? 116.743 112.438 131.945 1.00 76.53  ? 2412 TYR A CE2   1 
ATOM   3764 C  CZ    . TYR A 1 621 ? 116.709 112.457 130.568 1.00 74.71  ? 2412 TYR A CZ    1 
ATOM   3765 O  OH    . TYR A 1 621 ? 117.652 111.756 129.854 1.00 73.43  ? 2412 TYR A OH    1 
ATOM   3766 N  N     . ILE A 1 622 ? 112.623 117.295 131.522 1.00 83.46  ? 2413 ILE A N     1 
ATOM   3767 C  CA    . ILE A 1 622 ? 112.299 118.133 130.370 1.00 78.04  ? 2413 ILE A CA    1 
ATOM   3768 C  C     . ILE A 1 622 ? 113.022 119.468 130.474 1.00 79.02  ? 2413 ILE A C     1 
ATOM   3769 O  O     . ILE A 1 622 ? 113.606 119.958 129.501 1.00 77.82  ? 2413 ILE A O     1 
ATOM   3770 C  CB    . ILE A 1 622 ? 110.776 118.333 130.264 1.00 79.03  ? 2413 ILE A CB    1 
ATOM   3771 C  CG1   . ILE A 1 622 ? 110.079 117.026 129.886 1.00 72.46  ? 2413 ILE A CG1   1 
ATOM   3772 C  CG2   . ILE A 1 622 ? 110.448 119.427 129.259 1.00 69.45  ? 2413 ILE A CG2   1 
ATOM   3773 C  CD1   . ILE A 1 622 ? 110.160 116.686 128.424 1.00 59.15  ? 2413 ILE A CD1   1 
ATOM   3774 N  N     . ASP A 1 623 ? 112.993 120.075 131.663 1.00 83.31  ? 2414 ASP A N     1 
ATOM   3775 C  CA    . ASP A 1 623 ? 113.644 121.367 131.856 1.00 82.87  ? 2414 ASP A CA    1 
ATOM   3776 C  C     . ASP A 1 623 ? 115.153 121.263 131.673 1.00 82.06  ? 2414 ASP A C     1 
ATOM   3777 O  O     . ASP A 1 623 ? 115.772 122.147 131.072 1.00 84.41  ? 2414 ASP A O     1 
ATOM   3778 C  CB    . ASP A 1 623 ? 113.306 121.923 133.239 1.00 88.61  ? 2414 ASP A CB    1 
ATOM   3779 C  CG    . ASP A 1 623 ? 111.830 122.223 133.401 1.00 97.33  ? 2414 ASP A CG    1 
ATOM   3780 O  OD1   . ASP A 1 623 ? 111.113 122.257 132.379 1.00 94.01  ? 2414 ASP A OD1   1 
ATOM   3781 O  OD2   . ASP A 1 623 ? 111.387 122.428 134.550 1.00 100.18 ? 2414 ASP A OD2   1 
ATOM   3782 N  N     . SER A 1 624 ? 115.765 120.195 132.192 1.00 81.54  ? 2415 SER A N     1 
ATOM   3783 C  CA    . SER A 1 624 ? 117.205 120.022 132.029 1.00 80.15  ? 2415 SER A CA    1 
ATOM   3784 C  C     . SER A 1 624 ? 117.575 119.813 130.565 1.00 75.94  ? 2415 SER A C     1 
ATOM   3785 O  O     . SER A 1 624 ? 118.565 120.378 130.084 1.00 78.07  ? 2415 SER A O     1 
ATOM   3786 C  CB    . SER A 1 624 ? 117.697 118.854 132.883 1.00 78.58  ? 2415 SER A CB    1 
ATOM   3787 O  OG    . SER A 1 624 ? 117.180 117.621 132.418 1.00 82.34  ? 2415 SER A OG    1 
ATOM   3788 N  N     . PHE A 1 625 ? 116.793 119.008 129.841 1.00 74.07  ? 2416 PHE A N     1 
ATOM   3789 C  CA    . PHE A 1 625 ? 117.051 118.810 128.418 1.00 73.66  ? 2416 PHE A CA    1 
ATOM   3790 C  C     . PHE A 1 625 ? 116.899 120.114 127.646 1.00 74.76  ? 2416 PHE A C     1 
ATOM   3791 O  O     . PHE A 1 625 ? 117.690 120.406 126.742 1.00 72.92  ? 2416 PHE A O     1 
ATOM   3792 C  CB    . PHE A 1 625 ? 116.109 117.742 127.859 1.00 71.33  ? 2416 PHE A CB    1 
ATOM   3793 C  CG    . PHE A 1 625 ? 116.580 117.129 126.571 1.00 65.19  ? 2416 PHE A CG    1 
ATOM   3794 C  CD1   . PHE A 1 625 ? 116.388 117.782 125.364 1.00 56.47  ? 2416 PHE A CD1   1 
ATOM   3795 C  CD2   . PHE A 1 625 ? 117.211 115.897 126.566 1.00 64.14  ? 2416 PHE A CD2   1 
ATOM   3796 C  CE1   . PHE A 1 625 ? 116.819 117.219 124.179 1.00 54.65  ? 2416 PHE A CE1   1 
ATOM   3797 C  CE2   . PHE A 1 625 ? 117.644 115.329 125.384 1.00 63.59  ? 2416 PHE A CE2   1 
ATOM   3798 C  CZ    . PHE A 1 625 ? 117.448 115.991 124.189 1.00 58.62  ? 2416 PHE A CZ    1 
ATOM   3799 N  N     . LYS A 1 626 ? 115.881 120.906 127.985 1.00 78.75  ? 2417 LYS A N     1 
ATOM   3800 C  CA    . LYS A 1 626 ? 115.668 122.177 127.302 1.00 76.81  ? 2417 LYS A CA    1 
ATOM   3801 C  C     . LYS A 1 626 ? 116.794 123.162 127.592 1.00 74.25  ? 2417 LYS A C     1 
ATOM   3802 O  O     . LYS A 1 626 ? 117.258 123.867 126.688 1.00 72.78  ? 2417 LYS A O     1 
ATOM   3803 C  CB    . LYS A 1 626 ? 114.317 122.762 127.712 1.00 78.63  ? 2417 LYS A CB    1 
ATOM   3804 C  CG    . LYS A 1 626 ? 113.125 122.047 127.094 1.00 73.13  ? 2417 LYS A CG    1 
ATOM   3805 C  CD    . LYS A 1 626 ? 111.892 122.933 127.071 1.00 65.78  ? 2417 LYS A CD    1 
ATOM   3806 C  CE    . LYS A 1 626 ? 110.661 122.146 126.652 1.00 67.00  ? 2417 LYS A CE    1 
ATOM   3807 N  NZ    . LYS A 1 626 ? 110.912 121.324 125.436 1.00 74.25  ? 2417 LYS A NZ    1 
ATOM   3808 N  N     . SER A 1 627 ? 117.249 123.224 128.845 1.00 77.33  ? 2418 SER A N     1 
ATOM   3809 C  CA    . SER A 1 627 ? 118.308 124.160 129.205 1.00 78.20  ? 2418 SER A CA    1 
ATOM   3810 C  C     . SER A 1 627 ? 119.654 123.740 128.631 1.00 75.94  ? 2418 SER A C     1 
ATOM   3811 O  O     . SER A 1 627 ? 120.476 124.599 128.294 1.00 73.70  ? 2418 SER A O     1 
ATOM   3812 C  CB    . SER A 1 627 ? 118.398 124.291 130.725 1.00 74.83  ? 2418 SER A CB    1 
ATOM   3813 O  OG    . SER A 1 627 ? 118.616 123.029 131.332 1.00 78.96  ? 2418 SER A OG    1 
ATOM   3814 N  N     . ARG A 1 628 ? 119.902 122.432 128.521 1.00 76.10  ? 2419 ARG A N     1 
ATOM   3815 C  CA    . ARG A 1 628 ? 121.173 121.967 127.977 1.00 73.87  ? 2419 ARG A CA    1 
ATOM   3816 C  C     . ARG A 1 628 ? 121.345 122.399 126.527 1.00 79.15  ? 2419 ARG A C     1 
ATOM   3817 O  O     . ARG A 1 628 ? 122.442 122.797 126.116 1.00 83.58  ? 2419 ARG A O     1 
ATOM   3818 C  CB    . ARG A 1 628 ? 121.276 120.447 128.105 1.00 73.59  ? 2419 ARG A CB    1 
ATOM   3819 C  CG    . ARG A 1 628 ? 121.902 119.982 129.409 1.00 74.55  ? 2419 ARG A CG    1 
ATOM   3820 C  CD    . ARG A 1 628 ? 122.063 118.472 129.446 1.00 72.35  ? 2419 ARG A CD    1 
ATOM   3821 N  NE    . ARG A 1 628 ? 120.844 117.779 129.047 1.00 73.24  ? 2419 ARG A NE    1 
ATOM   3822 C  CZ    . ARG A 1 628 ? 120.527 116.548 129.425 1.00 71.55  ? 2419 ARG A CZ    1 
ATOM   3823 N  NH1   . ARG A 1 628 ? 121.317 115.845 130.220 1.00 59.44  ? 2419 ARG A NH1   1 
ATOM   3824 N  NH2   . ARG A 1 628 ? 119.389 116.010 128.998 1.00 71.47  ? 2419 ARG A NH2   1 
ATOM   3825 N  N     . TYR A 1 629 ? 120.278 122.327 125.736 1.00 74.25  ? 2420 TYR A N     1 
ATOM   3826 C  CA    . TYR A 1 629 ? 120.305 122.725 124.330 1.00 66.22  ? 2420 TYR A CA    1 
ATOM   3827 C  C     . TYR A 1 629 ? 119.348 123.901 124.160 1.00 70.88  ? 2420 TYR A C     1 
ATOM   3828 O  O     . TYR A 1 629 ? 118.176 123.717 123.824 1.00 76.28  ? 2420 TYR A O     1 
ATOM   3829 C  CB    . TYR A 1 629 ? 119.925 121.559 123.419 1.00 59.66  ? 2420 TYR A CB    1 
ATOM   3830 C  CG    . TYR A 1 629 ? 120.668 120.275 123.708 1.00 60.02  ? 2420 TYR A CG    1 
ATOM   3831 C  CD1   . TYR A 1 629 ? 122.024 120.283 124.001 1.00 63.77  ? 2420 TYR A CD1   1 
ATOM   3832 C  CD2   . TYR A 1 629 ? 120.012 119.052 123.680 1.00 66.71  ? 2420 TYR A CD2   1 
ATOM   3833 C  CE1   . TYR A 1 629 ? 122.703 119.109 124.265 1.00 64.60  ? 2420 TYR A CE1   1 
ATOM   3834 C  CE2   . TYR A 1 629 ? 120.683 117.875 123.940 1.00 64.73  ? 2420 TYR A CE2   1 
ATOM   3835 C  CZ    . TYR A 1 629 ? 122.028 117.908 124.232 1.00 59.79  ? 2420 TYR A CZ    1 
ATOM   3836 O  OH    . TYR A 1 629 ? 122.697 116.736 124.492 1.00 58.86  ? 2420 TYR A OH    1 
ATOM   3837 N  N     . THR A 1 630 ? 119.852 125.115 124.392 1.00 72.14  ? 2421 THR A N     1 
ATOM   3838 C  CA    . THR A 1 630 ? 119.012 126.298 124.234 1.00 75.71  ? 2421 THR A CA    1 
ATOM   3839 C  C     . THR A 1 630 ? 118.774 126.626 122.766 1.00 70.98  ? 2421 THR A C     1 
ATOM   3840 O  O     . THR A 1 630 ? 117.762 127.251 122.427 1.00 69.23  ? 2421 THR A O     1 
ATOM   3841 C  CB    . THR A 1 630 ? 119.635 127.494 124.959 1.00 75.15  ? 2421 THR A CB    1 
ATOM   3842 O  OG1   . THR A 1 630 ? 118.699 128.579 124.987 1.00 78.50  ? 2421 THR A OG1   1 
ATOM   3843 C  CG2   . THR A 1 630 ? 120.914 127.947 124.267 1.00 67.12  ? 2421 THR A CG2   1 
ATOM   3844 N  N     . GLY A 1 631 ? 119.687 126.215 121.883 1.00 68.53  ? 2422 GLY A N     1 
ATOM   3845 C  CA    . GLY A 1 631 ? 119.477 126.427 120.463 1.00 69.10  ? 2422 GLY A CA    1 
ATOM   3846 C  C     . GLY A 1 631 ? 118.303 125.643 119.916 1.00 69.09  ? 2422 GLY A C     1 
ATOM   3847 O  O     . GLY A 1 631 ? 117.613 126.110 119.006 1.00 67.07  ? 2422 GLY A O     1 
ATOM   3848 N  N     . ILE A 1 632 ? 118.062 124.444 120.453 1.00 67.47  ? 2423 ILE A N     1 
ATOM   3849 C  CA    . ILE A 1 632 ? 116.889 123.674 120.049 1.00 55.77  ? 2423 ILE A CA    1 
ATOM   3850 C  C     . ILE A 1 632 ? 115.617 124.428 120.406 1.00 63.03  ? 2423 ILE A C     1 
ATOM   3851 O  O     . ILE A 1 632 ? 114.676 124.501 119.607 1.00 66.20  ? 2423 ILE A O     1 
ATOM   3852 C  CB    . ILE A 1 632 ? 116.917 122.275 120.691 1.00 50.23  ? 2423 ILE A CB    1 
ATOM   3853 C  CG1   . ILE A 1 632 ? 118.146 121.493 120.225 1.00 50.26  ? 2423 ILE A CG1   1 
ATOM   3854 C  CG2   . ILE A 1 632 ? 115.648 121.510 120.360 1.00 51.75  ? 2423 ILE A CG2   1 
ATOM   3855 C  CD1   . ILE A 1 632 ? 118.304 121.445 118.729 1.00 42.86  ? 2423 ILE A CD1   1 
ATOM   3856 N  N     . ASN A 1 633 ? 115.569 125.006 121.608 1.00 67.76  ? 2424 ASN A N     1 
ATOM   3857 C  CA    . ASN A 1 633 ? 114.412 125.803 122.002 1.00 72.89  ? 2424 ASN A CA    1 
ATOM   3858 C  C     . ASN A 1 633 ? 114.266 127.036 121.123 1.00 73.44  ? 2424 ASN A C     1 
ATOM   3859 O  O     . ASN A 1 633 ? 113.149 127.416 120.754 1.00 69.86  ? 2424 ASN A O     1 
ATOM   3860 C  CB    . ASN A 1 633 ? 114.529 126.211 123.467 1.00 74.23  ? 2424 ASN A CB    1 
ATOM   3861 C  CG    . ASN A 1 633 ? 113.986 125.163 124.403 1.00 78.39  ? 2424 ASN A CG    1 
ATOM   3862 O  OD1   . ASN A 1 633 ? 112.809 124.808 124.348 1.00 77.16  ? 2424 ASN A OD1   1 
ATOM   3863 N  ND2   . ASN A 1 633 ? 114.846 124.654 125.270 1.00 77.51  ? 2424 ASN A ND2   1 
ATOM   3864 N  N     . GLN A 1 634 ? 115.385 127.686 120.794 1.00 71.51  ? 2425 GLN A N     1 
ATOM   3865 C  CA    . GLN A 1 634 ? 115.326 128.851 119.918 1.00 68.61  ? 2425 GLN A CA    1 
ATOM   3866 C  C     . GLN A 1 634 ? 114.764 128.481 118.552 1.00 69.63  ? 2425 GLN A C     1 
ATOM   3867 O  O     . GLN A 1 634 ? 113.897 129.183 118.017 1.00 75.63  ? 2425 GLN A O     1 
ATOM   3868 C  CB    . GLN A 1 634 ? 116.716 129.473 119.783 1.00 71.56  ? 2425 GLN A CB    1 
ATOM   3869 C  CG    . GLN A 1 634 ? 116.954 130.208 118.475 1.00 77.39  ? 2425 GLN A CG    1 
ATOM   3870 C  CD    . GLN A 1 634 ? 118.256 130.984 118.474 1.00 86.77  ? 2425 GLN A CD    1 
ATOM   3871 O  OE1   . GLN A 1 634 ? 118.640 131.576 119.482 1.00 93.72  ? 2425 GLN A OE1   1 
ATOM   3872 N  NE2   . GLN A 1 634 ? 118.943 130.986 117.337 1.00 82.67  ? 2425 GLN A NE2   1 
ATOM   3873 N  N     . PHE A 1 635 ? 115.229 127.366 117.983 1.00 67.30  ? 2426 PHE A N     1 
ATOM   3874 C  CA    . PHE A 1 635 ? 114.717 126.925 116.690 1.00 71.72  ? 2426 PHE A CA    1 
ATOM   3875 C  C     . PHE A 1 635 ? 113.242 126.558 116.776 1.00 67.21  ? 2426 PHE A C     1 
ATOM   3876 O  O     . PHE A 1 635 ? 112.466 126.866 115.865 1.00 64.39  ? 2426 PHE A O     1 
ATOM   3877 C  CB    . PHE A 1 635 ? 115.525 125.736 116.174 1.00 68.94  ? 2426 PHE A CB    1 
ATOM   3878 C  CG    . PHE A 1 635 ? 114.881 125.030 115.014 1.00 64.40  ? 2426 PHE A CG    1 
ATOM   3879 C  CD1   . PHE A 1 635 ? 114.963 125.556 113.737 1.00 66.16  ? 2426 PHE A CD1   1 
ATOM   3880 C  CD2   . PHE A 1 635 ? 114.181 123.850 115.203 1.00 50.76  ? 2426 PHE A CD2   1 
ATOM   3881 C  CE1   . PHE A 1 635 ? 114.369 124.914 112.668 1.00 61.06  ? 2426 PHE A CE1   1 
ATOM   3882 C  CE2   . PHE A 1 635 ? 113.582 123.207 114.137 1.00 46.93  ? 2426 PHE A CE2   1 
ATOM   3883 C  CZ    . PHE A 1 635 ? 113.679 123.738 112.869 1.00 55.28  ? 2426 PHE A CZ    1 
ATOM   3884 N  N     . MET A 1 636 ? 112.840 125.882 117.854 1.00 61.06  ? 2427 MET A N     1 
ATOM   3885 C  CA    . MET A 1 636 ? 111.444 125.485 118.000 1.00 60.26  ? 2427 MET A CA    1 
ATOM   3886 C  C     . MET A 1 636 ? 110.536 126.705 118.097 1.00 67.97  ? 2427 MET A C     1 
ATOM   3887 O  O     . MET A 1 636 ? 109.491 126.769 117.440 1.00 68.75  ? 2427 MET A O     1 
ATOM   3888 C  CB    . MET A 1 636 ? 111.282 124.587 119.226 1.00 58.02  ? 2427 MET A CB    1 
ATOM   3889 C  CG    . MET A 1 636 ? 111.523 123.112 118.945 1.00 56.54  ? 2427 MET A CG    1 
ATOM   3890 S  SD    . MET A 1 636 ? 111.519 122.084 120.428 1.00 80.46  ? 2427 MET A SD    1 
ATOM   3891 C  CE    . MET A 1 636 ? 110.687 123.157 121.596 1.00 69.48  ? 2427 MET A CE    1 
ATOM   3892 N  N     . THR A 1 637 ? 110.928 127.693 118.903 1.00 71.75  ? 2428 THR A N     1 
ATOM   3893 C  CA    . THR A 1 637 ? 110.128 128.908 119.013 1.00 70.11  ? 2428 THR A CA    1 
ATOM   3894 C  C     . THR A 1 637 ? 110.088 129.661 117.690 1.00 69.38  ? 2428 THR A C     1 
ATOM   3895 O  O     . THR A 1 637 ? 109.033 130.164 117.285 1.00 70.02  ? 2428 THR A O     1 
ATOM   3896 C  CB    . THR A 1 637 ? 110.673 129.806 120.125 1.00 74.19  ? 2428 THR A CB    1 
ATOM   3897 O  OG1   . THR A 1 637 ? 112.092 129.937 119.988 1.00 74.18  ? 2428 THR A OG1   1 
ATOM   3898 C  CG2   . THR A 1 637 ? 110.354 129.215 121.490 1.00 72.25  ? 2428 THR A CG2   1 
ATOM   3899 N  N     . GLU A 1 638 ? 111.227 129.741 116.995 1.00 70.35  ? 2429 GLU A N     1 
ATOM   3900 C  CA    . GLU A 1 638 ? 111.265 130.446 115.719 1.00 72.44  ? 2429 GLU A CA    1 
ATOM   3901 C  C     . GLU A 1 638 ? 110.369 129.775 114.686 1.00 76.21  ? 2429 GLU A C     1 
ATOM   3902 O  O     . GLU A 1 638 ? 109.627 130.452 113.967 1.00 75.80  ? 2429 GLU A O     1 
ATOM   3903 C  CB    . GLU A 1 638 ? 112.706 130.529 115.213 1.00 68.86  ? 2429 GLU A CB    1 
ATOM   3904 C  CG    . GLU A 1 638 ? 112.833 130.833 113.731 1.00 67.72  ? 2429 GLU A CG    1 
ATOM   3905 C  CD    . GLU A 1 638 ? 114.100 130.260 113.128 1.00 70.57  ? 2429 GLU A CD    1 
ATOM   3906 O  OE1   . GLU A 1 638 ? 114.778 129.467 113.813 1.00 70.33  ? 2429 GLU A OE1   1 
ATOM   3907 O  OE2   . GLU A 1 638 ? 114.417 130.603 111.970 1.00 70.75  ? 2429 GLU A OE2   1 
ATOM   3908 N  N     . THR A 1 639 ? 110.408 128.442 114.607 1.00 72.67  ? 2430 THR A N     1 
ATOM   3909 C  CA    . THR A 1 639 ? 109.589 127.753 113.617 1.00 71.12  ? 2430 THR A CA    1 
ATOM   3910 C  C     . THR A 1 639 ? 108.113 127.771 113.998 1.00 70.97  ? 2430 THR A C     1 
ATOM   3911 O  O     . THR A 1 639 ? 107.254 127.820 113.112 1.00 76.50  ? 2430 THR A O     1 
ATOM   3912 C  CB    . THR A 1 639 ? 110.087 126.320 113.405 1.00 62.63  ? 2430 THR A CB    1 
ATOM   3913 O  OG1   . THR A 1 639 ? 109.512 125.785 112.207 1.00 57.34  ? 2430 THR A OG1   1 
ATOM   3914 C  CG2   . THR A 1 639 ? 109.725 125.425 114.573 1.00 59.58  ? 2430 THR A CG2   1 
ATOM   3915 N  N     . VAL A 1 640 ? 107.794 127.769 115.295 1.00 66.92  ? 2431 VAL A N     1 
ATOM   3916 C  CA    . VAL A 1 640 ? 106.403 127.921 115.705 1.00 71.70  ? 2431 VAL A CA    1 
ATOM   3917 C  C     . VAL A 1 640 ? 105.886 129.302 115.322 1.00 77.58  ? 2431 VAL A C     1 
ATOM   3918 O  O     . VAL A 1 640 ? 104.769 129.443 114.806 1.00 79.24  ? 2431 VAL A O     1 
ATOM   3919 C  CB    . VAL A 1 640 ? 106.261 127.654 117.214 1.00 68.37  ? 2431 VAL A CB    1 
ATOM   3920 C  CG1   . VAL A 1 640 ? 105.023 128.340 117.769 1.00 70.23  ? 2431 VAL A CG1   1 
ATOM   3921 C  CG2   . VAL A 1 640 ? 106.212 126.159 117.480 1.00 65.56  ? 2431 VAL A CG2   1 
ATOM   3922 N  N     . LYS A 1 641 ? 106.693 130.341 115.554 1.00 75.29  ? 2432 LYS A N     1 
ATOM   3923 C  CA    . LYS A 1 641 ? 106.297 131.688 115.158 1.00 74.07  ? 2432 LYS A CA    1 
ATOM   3924 C  C     . LYS A 1 641 ? 106.138 131.793 113.646 1.00 74.44  ? 2432 LYS A C     1 
ATOM   3925 O  O     . LYS A 1 641 ? 105.202 132.435 113.156 1.00 78.72  ? 2432 LYS A O     1 
ATOM   3926 C  CB    . LYS A 1 641 ? 107.321 132.704 115.664 1.00 67.03  ? 2432 LYS A CB    1 
ATOM   3927 C  CG    . LYS A 1 641 ? 106.989 134.147 115.326 1.00 67.08  ? 2432 LYS A CG    1 
ATOM   3928 C  CD    . LYS A 1 641 ? 108.217 134.891 114.827 1.00 70.52  ? 2432 LYS A CD    1 
ATOM   3929 C  CE    . LYS A 1 641 ? 109.365 134.787 115.817 1.00 67.16  ? 2432 LYS A CE    1 
ATOM   3930 N  NZ    . LYS A 1 641 ? 110.582 135.496 115.335 1.00 61.94  ? 2432 LYS A NZ    1 
ATOM   3931 N  N     . ASN A 1 642 ? 107.044 131.168 112.891 1.00 71.62  ? 2433 ASN A N     1 
ATOM   3932 C  CA    . ASN A 1 642 ? 106.947 131.200 111.435 1.00 76.73  ? 2433 ASN A CA    1 
ATOM   3933 C  C     . ASN A 1 642 ? 105.692 130.487 110.947 1.00 77.51  ? 2433 ASN A C     1 
ATOM   3934 O  O     . ASN A 1 642 ? 105.022 130.957 110.020 1.00 77.02  ? 2433 ASN A O     1 
ATOM   3935 C  CB    . ASN A 1 642 ? 108.196 130.579 110.813 1.00 73.23  ? 2433 ASN A CB    1 
ATOM   3936 C  CG    . ASN A 1 642 ? 109.416 131.468 110.946 1.00 76.24  ? 2433 ASN A CG    1 
ATOM   3937 O  OD1   . ASN A 1 642 ? 109.361 132.527 111.571 1.00 76.08  ? 2433 ASN A OD1   1 
ATOM   3938 N  ND2   . ASN A 1 642 ? 110.526 131.041 110.357 1.00 78.09  ? 2433 ASN A ND2   1 
ATOM   3939 N  N     . CYS A 1 643 ? 105.361 129.344 111.553 1.00 72.19  ? 2434 CYS A N     1 
ATOM   3940 C  CA    . CYS A 1 643 ? 104.139 128.637 111.182 1.00 68.17  ? 2434 CYS A CA    1 
ATOM   3941 C  C     . CYS A 1 643 ? 102.904 129.461 111.518 1.00 72.82  ? 2434 CYS A C     1 
ATOM   3942 O  O     . CYS A 1 643 ? 101.933 129.478 110.753 1.00 72.75  ? 2434 CYS A O     1 
ATOM   3943 C  CB    . CYS A 1 643 ? 104.086 127.280 111.880 1.00 69.47  ? 2434 CYS A CB    1 
ATOM   3944 S  SG    . CYS A 1 643 ? 102.531 126.390 111.657 1.00 80.57  ? 2434 CYS A SG    1 
ATOM   3945 N  N     . LYS A 1 644 ? 102.918 130.146 112.664 1.00 76.20  ? 2435 LYS A N     1 
ATOM   3946 C  CA    . LYS A 1 644 ? 101.781 130.983 113.035 1.00 82.53  ? 2435 LYS A CA    1 
ATOM   3947 C  C     . LYS A 1 644 ? 101.633 132.170 112.090 1.00 79.61  ? 2435 LYS A C     1 
ATOM   3948 O  O     . LYS A 1 644 ? 100.512 132.570 111.758 1.00 80.04  ? 2435 LYS A O     1 
ATOM   3949 C  CB    . LYS A 1 644 ? 101.932 131.463 114.478 1.00 78.20  ? 2435 LYS A CB    1 
ATOM   3950 C  CG    . LYS A 1 644 ? 100.633 131.924 115.118 1.00 71.52  ? 2435 LYS A CG    1 
ATOM   3951 C  CD    . LYS A 1 644 ? 100.772 132.033 116.628 1.00 73.95  ? 2435 LYS A CD    1 
ATOM   3952 C  CE    . LYS A 1 644 ? 101.348 130.758 117.224 1.00 72.09  ? 2435 LYS A CE    1 
ATOM   3953 N  NZ    . LYS A 1 644 ? 101.656 130.908 118.672 1.00 67.49  ? 2435 LYS A NZ    1 
ATOM   3954 N  N     . ARG A 1 645 ? 102.752 132.744 111.648 1.00 71.59  ? 2436 ARG A N     1 
ATOM   3955 C  CA    . ARG A 1 645 ? 102.703 133.938 110.812 1.00 70.80  ? 2436 ARG A CA    1 
ATOM   3956 C  C     . ARG A 1 645 ? 102.359 133.597 109.366 1.00 76.53  ? 2436 ARG A C     1 
ATOM   3957 O  O     . ARG A 1 645 ? 101.345 134.058 108.832 1.00 82.03  ? 2436 ARG A O     1 
ATOM   3958 C  CB    . ARG A 1 645 ? 104.040 134.679 110.888 1.00 73.63  ? 2436 ARG A CB    1 
ATOM   3959 C  CG    . ARG A 1 645 ? 104.184 135.813 109.891 1.00 71.83  ? 2436 ARG A CG    1 
ATOM   3960 C  CD    . ARG A 1 645 ? 105.439 136.623 110.166 1.00 68.94  ? 2436 ARG A CD    1 
ATOM   3961 N  NE    . ARG A 1 645 ? 106.606 135.770 110.355 1.00 68.95  ? 2436 ARG A NE    1 
ATOM   3962 C  CZ    . ARG A 1 645 ? 107.436 135.412 109.385 1.00 65.49  ? 2436 ARG A CZ    1 
ATOM   3963 N  NH1   . ARG A 1 645 ? 107.259 135.818 108.139 1.00 65.86  ? 2436 ARG A NH1   1 
ATOM   3964 N  NH2   . ARG A 1 645 ? 108.470 134.627 109.673 1.00 61.21  ? 2436 ARG A NH2   1 
ATOM   3965 N  N     . ASP A 1 646 ? 103.197 132.787 108.716 1.00 76.52  ? 2437 ASP A N     1 
ATOM   3966 C  CA    . ASP A 1 646 ? 102.994 132.479 107.305 1.00 76.95  ? 2437 ASP A CA    1 
ATOM   3967 C  C     . ASP A 1 646 ? 101.851 131.499 107.077 1.00 80.24  ? 2437 ASP A C     1 
ATOM   3968 O  O     . ASP A 1 646 ? 101.366 131.387 105.947 1.00 75.51  ? 2437 ASP A O     1 
ATOM   3969 C  CB    . ASP A 1 646 ? 104.280 131.917 106.697 1.00 72.28  ? 2437 ASP A CB    1 
ATOM   3970 C  CG    . ASP A 1 646 ? 105.426 132.908 106.738 1.00 79.49  ? 2437 ASP A CG    1 
ATOM   3971 O  OD1   . ASP A 1 646 ? 105.913 133.212 107.846 1.00 79.93  ? 2437 ASP A OD1   1 
ATOM   3972 O  OD2   . ASP A 1 646 ? 105.843 133.382 105.660 1.00 83.52  ? 2437 ASP A OD2   1 
ATOM   3973 N  N     . GLY A 1 647 ? 101.412 130.791 108.114 1.00 81.56  ? 2438 GLY A N     1 
ATOM   3974 C  CA    . GLY A 1 647 ? 100.381 129.789 107.966 1.00 75.59  ? 2438 GLY A CA    1 
ATOM   3975 C  C     . GLY A 1 647 ? 100.872 128.429 107.525 1.00 75.83  ? 2438 GLY A C     1 
ATOM   3976 O  O     . GLY A 1 647 ? 100.058 127.507 107.398 1.00 73.83  ? 2438 GLY A O     1 
ATOM   3977 N  N     . PHE A 1 648 ? 102.172 128.273 107.291 1.00 77.14  ? 2439 PHE A N     1 
ATOM   3978 C  CA    . PHE A 1 648 ? 102.742 127.004 106.863 1.00 64.46  ? 2439 PHE A CA    1 
ATOM   3979 C  C     . PHE A 1 648 ? 104.177 126.930 107.366 1.00 68.29  ? 2439 PHE A C     1 
ATOM   3980 O  O     . PHE A 1 648 ? 104.678 127.852 108.014 1.00 77.77  ? 2439 PHE A O     1 
ATOM   3981 C  CB    . PHE A 1 648 ? 102.673 126.854 105.340 1.00 59.34  ? 2439 PHE A CB    1 
ATOM   3982 C  CG    . PHE A 1 648 ? 103.444 127.904 104.590 1.00 67.06  ? 2439 PHE A CG    1 
ATOM   3983 C  CD1   . PHE A 1 648 ? 102.849 129.104 104.244 1.00 76.49  ? 2439 PHE A CD1   1 
ATOM   3984 C  CD2   . PHE A 1 648 ? 104.763 127.688 104.226 1.00 64.49  ? 2439 PHE A CD2   1 
ATOM   3985 C  CE1   . PHE A 1 648 ? 103.555 130.069 103.554 1.00 78.98  ? 2439 PHE A CE1   1 
ATOM   3986 C  CE2   . PHE A 1 648 ? 105.473 128.650 103.536 1.00 64.39  ? 2439 PHE A CE2   1 
ATOM   3987 C  CZ    . PHE A 1 648 ? 104.868 129.842 103.200 1.00 72.04  ? 2439 PHE A CZ    1 
ATOM   3988 N  N     . VAL A 1 649 ? 104.842 125.818 107.061 1.00 58.51  ? 2440 VAL A N     1 
ATOM   3989 C  CA    . VAL A 1 649 ? 106.237 125.625 107.427 1.00 56.97  ? 2440 VAL A CA    1 
ATOM   3990 C  C     . VAL A 1 649 ? 107.027 125.307 106.166 1.00 57.75  ? 2440 VAL A C     1 
ATOM   3991 O  O     . VAL A 1 649 ? 106.486 124.839 105.161 1.00 56.05  ? 2440 VAL A O     1 
ATOM   3992 C  CB    . VAL A 1 649 ? 106.422 124.516 108.478 1.00 49.34  ? 2440 VAL A CB    1 
ATOM   3993 C  CG1   . VAL A 1 649 ? 105.392 124.657 109.575 1.00 55.79  ? 2440 VAL A CG1   1 
ATOM   3994 C  CG2   . VAL A 1 649 ? 106.325 123.156 107.828 1.00 46.78  ? 2440 VAL A CG2   1 
ATOM   3995 N  N     . GLN A 1 650 ? 108.329 125.571 106.230 1.00 54.48  ? 2441 GLN A N     1 
ATOM   3996 C  CA    . GLN A 1 650 ? 109.213 125.429 105.081 1.00 46.82  ? 2441 GLN A CA    1 
ATOM   3997 C  C     . GLN A 1 650 ? 110.229 124.332 105.355 1.00 48.95  ? 2441 GLN A C     1 
ATOM   3998 O  O     . GLN A 1 650 ? 111.026 124.438 106.292 1.00 55.64  ? 2441 GLN A O     1 
ATOM   3999 C  CB    . GLN A 1 650 ? 109.923 126.749 104.772 1.00 46.36  ? 2441 GLN A CB    1 
ATOM   4000 C  CG    . GLN A 1 650 ? 109.196 127.620 103.765 1.00 51.64  ? 2441 GLN A CG    1 
ATOM   4001 C  CD    . GLN A 1 650 ? 109.745 127.465 102.364 1.00 58.42  ? 2441 GLN A CD    1 
ATOM   4002 O  OE1   . GLN A 1 650 ? 110.718 126.745 102.143 1.00 56.80  ? 2441 GLN A OE1   1 
ATOM   4003 N  NE2   . GLN A 1 650 ? 109.120 128.138 101.406 1.00 62.22  ? 2441 GLN A NE2   1 
ATOM   4004 N  N     . THR A 1 651 ? 110.198 123.287 104.536 1.00 43.61  ? 2442 THR A N     1 
ATOM   4005 C  CA    . THR A 1 651 ? 111.264 122.301 104.524 1.00 45.43  ? 2442 THR A CA    1 
ATOM   4006 C  C     . THR A 1 651 ? 112.542 122.936 103.979 1.00 51.75  ? 2442 THR A C     1 
ATOM   4007 O  O     . THR A 1 651 ? 112.507 123.919 103.234 1.00 59.12  ? 2442 THR A O     1 
ATOM   4008 C  CB    . THR A 1 651 ? 110.856 121.093 103.679 1.00 38.67  ? 2442 THR A CB    1 
ATOM   4009 O  OG1   . THR A 1 651 ? 109.535 120.680 104.048 1.00 32.00  ? 2442 THR A OG1   1 
ATOM   4010 C  CG2   . THR A 1 651 ? 111.804 119.935 103.886 1.00 37.55  ? 2442 THR A CG2   1 
ATOM   4011 N  N     . ILE A 1 652 ? 113.688 122.374 104.373 1.00 43.09  ? 2443 ILE A N     1 
ATOM   4012 C  CA    . ILE A 1 652 ? 114.970 122.942 103.969 1.00 48.71  ? 2443 ILE A CA    1 
ATOM   4013 C  C     . ILE A 1 652 ? 115.247 122.786 102.478 1.00 50.30  ? 2443 ILE A C     1 
ATOM   4014 O  O     . ILE A 1 652 ? 116.182 123.414 101.968 1.00 48.32  ? 2443 ILE A O     1 
ATOM   4015 C  CB    . ILE A 1 652 ? 116.105 122.339 104.826 1.00 49.56  ? 2443 ILE A CB    1 
ATOM   4016 C  CG1   . ILE A 1 652 ? 117.332 123.258 104.836 1.00 51.52  ? 2443 ILE A CG1   1 
ATOM   4017 C  CG2   . ILE A 1 652 ? 116.473 120.950 104.360 1.00 43.21  ? 2443 ILE A CG2   1 
ATOM   4018 C  CD1   . ILE A 1 652 ? 117.031 124.684 105.235 1.00 53.46  ? 2443 ILE A CD1   1 
ATOM   4019 N  N     . LEU A 1 653 ? 114.461 121.984 101.757 1.00 49.97  ? 2444 LEU A N     1 
ATOM   4020 C  CA    . LEU A 1 653 ? 114.512 121.962 100.299 1.00 46.31  ? 2444 LEU A CA    1 
ATOM   4021 C  C     . LEU A 1 653 ? 113.381 122.749 99.648  1.00 47.65  ? 2444 LEU A C     1 
ATOM   4022 O  O     . LEU A 1 653 ? 113.257 122.728 98.420  1.00 46.95  ? 2444 LEU A O     1 
ATOM   4023 C  CB    . LEU A 1 653 ? 114.512 120.530 99.752  1.00 41.83  ? 2444 LEU A CB    1 
ATOM   4024 C  CG    . LEU A 1 653 ? 115.689 119.567 99.954  1.00 44.60  ? 2444 LEU A CG    1 
ATOM   4025 C  CD1   . LEU A 1 653 ? 116.888 120.034 99.137  1.00 47.64  ? 2444 LEU A CD1   1 
ATOM   4026 C  CD2   . LEU A 1 653 ? 116.077 119.329 101.395 1.00 39.24  ? 2444 LEU A CD2   1 
ATOM   4027 N  N     . GLY A 1 654 ? 112.558 123.438 100.433 1.00 45.70  ? 2445 GLY A N     1 
ATOM   4028 C  CA    . GLY A 1 654 ? 111.572 124.355 99.911  1.00 39.11  ? 2445 GLY A CA    1 
ATOM   4029 C  C     . GLY A 1 654 ? 110.142 123.852 99.913  1.00 40.40  ? 2445 GLY A C     1 
ATOM   4030 O  O     . GLY A 1 654 ? 109.223 124.663 99.756  1.00 47.20  ? 2445 GLY A O     1 
ATOM   4031 N  N     . ARG A 1 655 ? 109.924 122.549 100.080 1.00 41.53  ? 2446 ARG A N     1 
ATOM   4032 C  CA    . ARG A 1 655 ? 108.561 122.037 100.126 1.00 44.84  ? 2446 ARG A CA    1 
ATOM   4033 C  C     . ARG A 1 655 ? 107.832 122.588 101.346 1.00 48.18  ? 2446 ARG A C     1 
ATOM   4034 O  O     . ARG A 1 655 ? 108.424 122.808 102.404 1.00 54.01  ? 2446 ARG A O     1 
ATOM   4035 C  CB    . ARG A 1 655 ? 108.555 120.508 100.158 1.00 39.44  ? 2446 ARG A CB    1 
ATOM   4036 C  CG    . ARG A 1 655 ? 109.329 119.854 99.030  1.00 35.03  ? 2446 ARG A CG    1 
ATOM   4037 C  CD    . ARG A 1 655 ? 109.091 118.354 98.997  1.00 25.64  ? 2446 ARG A CD    1 
ATOM   4038 N  NE    . ARG A 1 655 ? 109.389 117.726 100.277 1.00 33.56  ? 2446 ARG A NE    1 
ATOM   4039 C  CZ    . ARG A 1 655 ? 108.474 117.225 101.094 1.00 38.13  ? 2446 ARG A CZ    1 
ATOM   4040 N  NH1   . ARG A 1 655 ? 107.187 117.254 100.792 1.00 33.12  ? 2446 ARG A NH1   1 
ATOM   4041 N  NH2   . ARG A 1 655 ? 108.860 116.683 102.245 1.00 37.82  ? 2446 ARG A NH2   1 
ATOM   4042 N  N     . ARG A 1 656 ? 106.532 122.817 101.192 1.00 33.88  ? 2447 ARG A N     1 
ATOM   4043 C  CA    . ARG A 1 656 ? 105.734 123.450 102.230 1.00 38.45  ? 2447 ARG A CA    1 
ATOM   4044 C  C     . ARG A 1 656 ? 104.594 122.539 102.660 1.00 45.83  ? 2447 ARG A C     1 
ATOM   4045 O  O     . ARG A 1 656 ? 104.029 121.796 101.852 1.00 46.49  ? 2447 ARG A O     1 
ATOM   4046 C  CB    . ARG A 1 656 ? 105.170 124.792 101.751 1.00 45.52  ? 2447 ARG A CB    1 
ATOM   4047 C  CG    . ARG A 1 656 ? 106.200 125.692 101.092 1.00 48.04  ? 2447 ARG A CG    1 
ATOM   4048 C  CD    . ARG A 1 656 ? 105.541 126.736 100.207 1.00 54.30  ? 2447 ARG A CD    1 
ATOM   4049 N  NE    . ARG A 1 656 ? 106.341 127.951 100.113 1.00 61.26  ? 2447 ARG A NE    1 
ATOM   4050 C  CZ    . ARG A 1 656 ? 105.840 129.165 99.927  1.00 69.76  ? 2447 ARG A CZ    1 
ATOM   4051 N  NH1   . ARG A 1 656 ? 104.538 129.364 99.807  1.00 73.77  ? 2447 ARG A NH1   1 
ATOM   4052 N  NH2   . ARG A 1 656 ? 106.667 130.204 99.858  1.00 65.72  ? 2447 ARG A NH2   1 
ATOM   4053 N  N     . ARG A 1 657 ? 104.267 122.601 103.950 1.00 52.95  ? 2448 ARG A N     1 
ATOM   4054 C  CA    . ARG A 1 657 ? 103.123 121.901 104.518 1.00 48.99  ? 2448 ARG A CA    1 
ATOM   4055 C  C     . ARG A 1 657 ? 102.249 122.915 105.238 1.00 58.76  ? 2448 ARG A C     1 
ATOM   4056 O  O     . ARG A 1 657 ? 102.750 123.714 106.035 1.00 61.51  ? 2448 ARG A O     1 
ATOM   4057 C  CB    . ARG A 1 657 ? 103.562 120.796 105.481 1.00 36.77  ? 2448 ARG A CB    1 
ATOM   4058 C  CG    . ARG A 1 657 ? 102.454 119.828 105.855 1.00 39.52  ? 2448 ARG A CG    1 
ATOM   4059 C  CD    . ARG A 1 657 ? 102.356 119.658 107.358 1.00 38.62  ? 2448 ARG A CD    1 
ATOM   4060 N  NE    . ARG A 1 657 ? 101.227 118.822 107.746 1.00 39.60  ? 2448 ARG A NE    1 
ATOM   4061 C  CZ    . ARG A 1 657 ? 101.330 117.575 108.182 1.00 32.34  ? 2448 ARG A CZ    1 
ATOM   4062 N  NH1   . ARG A 1 657 ? 102.502 116.973 108.283 1.00 28.05  ? 2448 ARG A NH1   1 
ATOM   4063 N  NH2   . ARG A 1 657 ? 100.228 116.916 108.527 1.00 32.74  ? 2448 ARG A NH2   1 
ATOM   4064 N  N     . TYR A 1 658 ? 100.949 122.881 104.963 1.00 56.82  ? 2449 TYR A N     1 
ATOM   4065 C  CA    . TYR A 1 658 ? 100.014 123.869 105.480 1.00 58.65  ? 2449 TYR A CA    1 
ATOM   4066 C  C     . TYR A 1 658 ? 99.337  123.336 106.735 1.00 57.70  ? 2449 TYR A C     1 
ATOM   4067 O  O     . TYR A 1 658 ? 98.810  122.220 106.737 1.00 60.16  ? 2449 TYR A O     1 
ATOM   4068 C  CB    . TYR A 1 658 ? 98.970  124.230 104.423 1.00 56.11  ? 2449 TYR A CB    1 
ATOM   4069 C  CG    . TYR A 1 658 ? 99.548  124.936 103.218 1.00 58.43  ? 2449 TYR A CG    1 
ATOM   4070 C  CD1   . TYR A 1 658 ? 100.029 124.217 102.132 1.00 58.94  ? 2449 TYR A CD1   1 
ATOM   4071 C  CD2   . TYR A 1 658 ? 99.617  126.320 103.167 1.00 63.24  ? 2449 TYR A CD2   1 
ATOM   4072 C  CE1   . TYR A 1 658 ? 100.561 124.857 101.031 1.00 59.56  ? 2449 TYR A CE1   1 
ATOM   4073 C  CE2   . TYR A 1 658 ? 100.146 126.969 102.069 1.00 69.58  ? 2449 TYR A CE2   1 
ATOM   4074 C  CZ    . TYR A 1 658 ? 100.616 126.233 101.004 1.00 68.08  ? 2449 TYR A CZ    1 
ATOM   4075 O  OH    . TYR A 1 658 ? 101.144 126.875 99.909  1.00 74.00  ? 2449 TYR A OH    1 
ATOM   4076 N  N     . LEU A 1 659 ? 99.357  124.134 107.800 1.00 55.69  ? 2450 LEU A N     1 
ATOM   4077 C  CA    . LEU A 1 659 ? 98.769  123.766 109.087 1.00 49.56  ? 2450 LEU A CA    1 
ATOM   4078 C  C     . LEU A 1 659 ? 97.875  124.897 109.574 1.00 56.77  ? 2450 LEU A C     1 
ATOM   4079 O  O     . LEU A 1 659 ? 98.301  125.740 110.372 1.00 63.08  ? 2450 LEU A O     1 
ATOM   4080 C  CB    . LEU A 1 659 ? 99.850  123.447 110.118 1.00 51.99  ? 2450 LEU A CB    1 
ATOM   4081 C  CG    . LEU A 1 659 ? 100.807 122.317 109.756 1.00 52.13  ? 2450 LEU A CG    1 
ATOM   4082 C  CD1   . LEU A 1 659 ? 102.040 122.377 110.626 1.00 45.55  ? 2450 LEU A CD1   1 
ATOM   4083 C  CD2   . LEU A 1 659 ? 100.103 120.986 109.927 1.00 56.15  ? 2450 LEU A CD2   1 
ATOM   4084 N  N     . PRO A 1 660 ? 96.627  124.952 109.105 1.00 58.49  ? 2451 PRO A N     1 
ATOM   4085 C  CA    . PRO A 1 660 ? 95.688  125.944 109.653 1.00 60.12  ? 2451 PRO A CA    1 
ATOM   4086 C  C     . PRO A 1 660 ? 95.387  125.732 111.126 1.00 65.41  ? 2451 PRO A C     1 
ATOM   4087 O  O     . PRO A 1 660 ? 94.975  126.683 111.805 1.00 73.17  ? 2451 PRO A O     1 
ATOM   4088 C  CB    . PRO A 1 660 ? 94.434  125.754 108.790 1.00 54.12  ? 2451 PRO A CB    1 
ATOM   4089 C  CG    . PRO A 1 660 ? 94.534  124.349 108.287 1.00 53.35  ? 2451 PRO A CG    1 
ATOM   4090 C  CD    . PRO A 1 660 ? 95.998  124.085 108.095 1.00 58.60  ? 2451 PRO A CD    1 
ATOM   4091 N  N     . GLY A 1 661 ? 95.605  124.522 111.645 1.00 64.12  ? 2452 GLY A N     1 
ATOM   4092 C  CA    . GLY A 1 661 ? 95.242  124.208 113.015 1.00 67.52  ? 2452 GLY A CA    1 
ATOM   4093 C  C     . GLY A 1 661 ? 95.987  125.010 114.060 1.00 69.96  ? 2452 GLY A C     1 
ATOM   4094 O  O     . GLY A 1 661 ? 95.575  125.024 115.224 1.00 76.25  ? 2452 GLY A O     1 
ATOM   4095 N  N     . ILE A 1 662 ? 97.081  125.673 113.681 1.00 64.79  ? 2453 ILE A N     1 
ATOM   4096 C  CA    . ILE A 1 662 ? 97.780  126.515 114.645 1.00 68.48  ? 2453 ILE A CA    1 
ATOM   4097 C  C     . ILE A 1 662 ? 96.919  127.716 115.013 1.00 76.47  ? 2453 ILE A C     1 
ATOM   4098 O  O     . ILE A 1 662 ? 97.020  128.247 116.126 1.00 81.03  ? 2453 ILE A O     1 
ATOM   4099 C  CB    . ILE A 1 662 ? 99.157  126.932 114.095 1.00 62.56  ? 2453 ILE A CB    1 
ATOM   4100 C  CG1   . ILE A 1 662 ? 99.862  127.888 115.056 1.00 74.10  ? 2453 ILE A CG1   1 
ATOM   4101 C  CG2   . ILE A 1 662 ? 99.009  127.607 112.750 1.00 62.18  ? 2453 ILE A CG2   1 
ATOM   4102 C  CD1   . ILE A 1 662 ? 101.364 127.892 114.905 1.00 76.60  ? 2453 ILE A CD1   1 
ATOM   4103 N  N     . LYS A 1 663 ? 96.040  128.147 114.108 1.00 79.22  ? 2454 LYS A N     1 
ATOM   4104 C  CA    . LYS A 1 663 ? 95.133  129.249 114.399 1.00 81.20  ? 2454 LYS A CA    1 
ATOM   4105 C  C     . LYS A 1 663 ? 93.889  128.806 115.159 1.00 85.75  ? 2454 LYS A C     1 
ATOM   4106 O  O     . LYS A 1 663 ? 93.053  129.653 115.491 1.00 91.49  ? 2454 LYS A O     1 
ATOM   4107 C  CB    . LYS A 1 663 ? 94.721  129.952 113.102 1.00 76.87  ? 2454 LYS A CB    1 
ATOM   4108 C  CG    . LYS A 1 663 ? 95.888  130.422 112.246 1.00 71.77  ? 2454 LYS A CG    1 
ATOM   4109 C  CD    . LYS A 1 663 ? 96.917  131.182 113.069 1.00 77.25  ? 2454 LYS A CD    1 
ATOM   4110 C  CE    . LYS A 1 663 ? 96.403  132.552 113.476 1.00 80.42  ? 2454 LYS A CE    1 
ATOM   4111 N  NZ    . LYS A 1 663 ? 97.383  133.273 114.335 1.00 75.93  ? 2454 LYS A NZ    1 
ATOM   4112 N  N     . ASP A 1 664 ? 93.746  127.512 115.435 1.00 85.67  ? 2455 ASP A N     1 
ATOM   4113 C  CA    . ASP A 1 664 ? 92.589  127.022 116.170 1.00 92.99  ? 2455 ASP A CA    1 
ATOM   4114 C  C     . ASP A 1 664 ? 92.599  127.549 117.600 1.00 97.07  ? 2455 ASP A C     1 
ATOM   4115 O  O     . ASP A 1 664 ? 93.654  127.675 118.227 1.00 90.26  ? 2455 ASP A O     1 
ATOM   4116 C  CB    . ASP A 1 664 ? 92.571  125.493 116.172 1.00 94.07  ? 2455 ASP A CB    1 
ATOM   4117 C  CG    . ASP A 1 664 ? 91.168  124.924 116.257 1.00 96.70  ? 2455 ASP A CG    1 
ATOM   4118 O  OD1   . ASP A 1 664 ? 90.433  125.282 117.200 1.00 95.24  ? 2455 ASP A OD1   1 
ATOM   4119 O  OD2   . ASP A 1 664 ? 90.800  124.115 115.379 1.00 90.71  ? 2455 ASP A OD2   1 
ATOM   4120 N  N     . ASN A 1 665 ? 91.407  127.859 118.113 1.00 101.84 ? 2456 ASN A N     1 
ATOM   4121 C  CA    . ASN A 1 665 ? 91.287  128.401 119.461 1.00 101.49 ? 2456 ASN A CA    1 
ATOM   4122 C  C     . ASN A 1 665 ? 91.539  127.352 120.536 1.00 100.29 ? 2456 ASN A C     1 
ATOM   4123 O  O     . ASN A 1 665 ? 91.890  127.714 121.665 1.00 102.84 ? 2456 ASN A O     1 
ATOM   4124 C  CB    . ASN A 1 665 ? 89.900  129.016 119.655 1.00 103.61 ? 2456 ASN A CB    1 
ATOM   4125 C  CG    . ASN A 1 665 ? 89.500  129.925 118.510 1.00 105.29 ? 2456 ASN A CG    1 
ATOM   4126 O  OD1   . ASN A 1 665 ? 90.346  130.552 117.873 1.00 102.22 ? 2456 ASN A OD1   1 
ATOM   4127 N  ND2   . ASN A 1 665 ? 88.202  129.997 118.239 1.00 102.75 ? 2456 ASN A ND2   1 
ATOM   4128 N  N     . ASN A 1 666 ? 91.368  126.076 120.218 1.00 97.10  ? 2457 ASN A N     1 
ATOM   4129 C  CA    . ASN A 1 666 ? 91.563  125.024 121.208 1.00 96.68  ? 2457 ASN A CA    1 
ATOM   4130 C  C     . ASN A 1 666 ? 93.034  124.947 121.602 1.00 95.61  ? 2457 ASN A C     1 
ATOM   4131 O  O     . ASN A 1 666 ? 93.900  124.855 120.724 1.00 95.41  ? 2457 ASN A O     1 
ATOM   4132 C  CB    . ASN A 1 666 ? 91.093  123.683 120.651 1.00 90.47  ? 2457 ASN A CB    1 
ATOM   4133 C  CG    . ASN A 1 666 ? 90.823  122.661 121.737 1.00 92.80  ? 2457 ASN A CG    1 
ATOM   4134 O  OD1   . ASN A 1 666 ? 91.652  122.439 122.619 1.00 88.99  ? 2457 ASN A OD1   1 
ATOM   4135 N  ND2   . ASN A 1 666 ? 89.656  122.030 121.677 1.00 98.18  ? 2457 ASN A ND2   1 
ATOM   4136 N  N     . PRO A 1 667 ? 93.360  125.000 122.897 1.00 97.66  ? 2458 PRO A N     1 
ATOM   4137 C  CA    . PRO A 1 667 ? 94.770  124.851 123.296 1.00 95.36  ? 2458 PRO A CA    1 
ATOM   4138 C  C     . PRO A 1 667 ? 95.376  123.529 122.861 1.00 97.27  ? 2458 PRO A C     1 
ATOM   4139 O  O     . PRO A 1 667 ? 96.555  123.484 122.483 1.00 96.15  ? 2458 PRO A O     1 
ATOM   4140 C  CB    . PRO A 1 667 ? 94.717  124.978 124.826 1.00 93.02  ? 2458 PRO A CB    1 
ATOM   4141 C  CG    . PRO A 1 667 ? 93.431  125.685 125.113 1.00 97.24  ? 2458 PRO A CG    1 
ATOM   4142 C  CD    . PRO A 1 667 ? 92.477  125.243 124.049 1.00 100.72 ? 2458 PRO A CD    1 
ATOM   4143 N  N     . TYR A 1 668 ? 94.594  122.447 122.903 1.00 100.08 ? 2459 TYR A N     1 
ATOM   4144 C  CA    . TYR A 1 668 ? 95.080  121.161 122.413 1.00 98.12  ? 2459 TYR A CA    1 
ATOM   4145 C  C     . TYR A 1 668 ? 95.455  121.275 120.941 1.00 89.46  ? 2459 TYR A C     1 
ATOM   4146 O  O     . TYR A 1 668 ? 96.548  120.867 120.536 1.00 90.64  ? 2459 TYR A O     1 
ATOM   4147 C  CB    . TYR A 1 668 ? 94.006  120.085 122.635 1.00 99.12  ? 2459 TYR A CB    1 
ATOM   4148 C  CG    . TYR A 1 668 ? 94.295  118.660 122.149 1.00 103.81 ? 2459 TYR A CG    1 
ATOM   4149 C  CD1   . TYR A 1 668 ? 95.437  118.337 121.422 1.00 96.05  ? 2459 TYR A CD1   1 
ATOM   4150 C  CD2   . TYR A 1 668 ? 93.395  117.636 122.415 1.00 113.45 ? 2459 TYR A CD2   1 
ATOM   4151 C  CE1   . TYR A 1 668 ? 95.677  117.051 120.985 1.00 94.95  ? 2459 TYR A CE1   1 
ATOM   4152 C  CE2   . TYR A 1 668 ? 93.628  116.344 121.981 1.00 119.26 ? 2459 TYR A CE2   1 
ATOM   4153 C  CZ    . TYR A 1 668 ? 94.770  116.057 121.267 1.00 111.85 ? 2459 TYR A CZ    1 
ATOM   4154 O  OH    . TYR A 1 668 ? 95.004  114.772 120.835 1.00 111.08 ? 2459 TYR A OH    1 
ATOM   4155 N  N     . ARG A 1 669 ? 94.563  121.844 120.129 1.00 83.15  ? 2460 ARG A N     1 
ATOM   4156 C  CA    . ARG A 1 669 ? 94.844  121.975 118.704 1.00 80.74  ? 2460 ARG A CA    1 
ATOM   4157 C  C     . ARG A 1 669 ? 96.052  122.868 118.459 1.00 78.63  ? 2460 ARG A C     1 
ATOM   4158 O  O     . ARG A 1 669 ? 96.872  122.583 117.582 1.00 79.34  ? 2460 ARG A O     1 
ATOM   4159 C  CB    . ARG A 1 669 ? 93.618  122.518 117.973 1.00 85.63  ? 2460 ARG A CB    1 
ATOM   4160 C  CG    . ARG A 1 669 ? 92.428  121.576 117.976 1.00 85.33  ? 2460 ARG A CG    1 
ATOM   4161 C  CD    . ARG A 1 669 ? 92.778  120.244 117.325 1.00 76.90  ? 2460 ARG A CD    1 
ATOM   4162 N  NE    . ARG A 1 669 ? 91.711  119.726 116.476 1.00 74.72  ? 2460 ARG A NE    1 
ATOM   4163 C  CZ    . ARG A 1 669 ? 90.486  119.420 116.887 1.00 76.81  ? 2460 ARG A CZ    1 
ATOM   4164 N  NH1   . ARG A 1 669 ? 90.136  119.513 118.160 1.00 76.58  ? 2460 ARG A NH1   1 
ATOM   4165 N  NH2   . ARG A 1 669 ? 89.593  118.993 115.999 1.00 79.81  ? 2460 ARG A NH2   1 
ATOM   4166 N  N     . LYS A 1 670 ? 96.183  123.951 119.227 1.00 81.91  ? 2461 LYS A N     1 
ATOM   4167 C  CA    . LYS A 1 670 ? 97.314  124.856 119.047 1.00 80.39  ? 2461 LYS A CA    1 
ATOM   4168 C  C     . LYS A 1 670 ? 98.636  124.159 119.352 1.00 76.32  ? 2461 LYS A C     1 
ATOM   4169 O  O     . LYS A 1 670 ? 99.588  124.233 118.564 1.00 72.89  ? 2461 LYS A O     1 
ATOM   4170 C  CB    . LYS A 1 670 ? 97.137  126.089 119.932 1.00 87.08  ? 2461 LYS A CB    1 
ATOM   4171 C  CG    . LYS A 1 670 ? 98.362  126.980 120.009 1.00 79.35  ? 2461 LYS A CG    1 
ATOM   4172 C  CD    . LYS A 1 670 ? 98.215  128.196 119.114 1.00 77.05  ? 2461 LYS A CD    1 
ATOM   4173 C  CE    . LYS A 1 670 ? 97.016  129.037 119.520 1.00 78.60  ? 2461 LYS A CE    1 
ATOM   4174 N  NZ    . LYS A 1 670 ? 96.665  130.039 118.477 1.00 77.20  ? 2461 LYS A NZ    1 
ATOM   4175 N  N     . ALA A 1 671 ? 98.713  123.472 120.495 1.00 81.34  ? 2462 ALA A N     1 
ATOM   4176 C  CA    . ALA A 1 671 ? 99.945  122.772 120.848 1.00 80.63  ? 2462 ALA A CA    1 
ATOM   4177 C  C     . ALA A 1 671 ? 100.239 121.645 119.866 1.00 74.84  ? 2462 ALA A C     1 
ATOM   4178 O  O     . ALA A 1 671 ? 101.398 121.426 119.483 1.00 71.80  ? 2462 ALA A O     1 
ATOM   4179 C  CB    . ALA A 1 671 ? 99.852  122.232 122.275 1.00 77.77  ? 2462 ALA A CB    1 
ATOM   4180 N  N     . HIS A 1 672 ? 99.200  120.917 119.450 1.00 71.72  ? 2463 HIS A N     1 
ATOM   4181 C  CA    . HIS A 1 672 ? 99.383  119.837 118.492 1.00 64.24  ? 2463 HIS A CA    1 
ATOM   4182 C  C     . HIS A 1 672 ? 99.897  120.367 117.167 1.00 62.16  ? 2463 HIS A C     1 
ATOM   4183 O  O     . HIS A 1 672 ? 100.774 119.760 116.552 1.00 63.25  ? 2463 HIS A O     1 
ATOM   4184 C  CB    . HIS A 1 672 ? 98.073  119.079 118.291 1.00 65.10  ? 2463 HIS A CB    1 
ATOM   4185 C  CG    . HIS A 1 672 ? 98.176  117.942 117.325 1.00 57.17  ? 2463 HIS A CG    1 
ATOM   4186 N  ND1   . HIS A 1 672 ? 99.058  116.897 117.498 1.00 54.50  ? 2463 HIS A ND1   1 
ATOM   4187 C  CD2   . HIS A 1 672 ? 97.510  117.685 116.175 1.00 47.82  ? 2463 HIS A CD2   1 
ATOM   4188 C  CE1   . HIS A 1 672 ? 98.930  116.045 116.497 1.00 49.10  ? 2463 HIS A CE1   1 
ATOM   4189 N  NE2   . HIS A 1 672 ? 97.997  116.499 115.681 1.00 45.52  ? 2463 HIS A NE2   1 
ATOM   4190 N  N     . ALA A 1 673 ? 99.376  121.509 116.717 1.00 63.50  ? 2464 ALA A N     1 
ATOM   4191 C  CA    . ALA A 1 673 ? 99.844  122.087 115.465 1.00 60.72  ? 2464 ALA A CA    1 
ATOM   4192 C  C     . ALA A 1 673 ? 101.257 122.636 115.591 1.00 58.59  ? 2464 ALA A C     1 
ATOM   4193 O  O     . ALA A 1 673 ? 102.023 122.574 114.629 1.00 66.39  ? 2464 ALA A O     1 
ATOM   4194 C  CB    . ALA A 1 673 ? 98.886  123.179 115.000 1.00 64.90  ? 2464 ALA A CB    1 
ATOM   4195 N  N     . GLU A 1 674 ? 101.629 123.164 116.758 1.00 56.58  ? 2465 GLU A N     1 
ATOM   4196 C  CA    . GLU A 1 674 ? 103.003 123.626 116.945 1.00 59.33  ? 2465 GLU A CA    1 
ATOM   4197 C  C     . GLU A 1 674 ? 103.989 122.464 116.870 1.00 56.96  ? 2465 GLU A C     1 
ATOM   4198 O  O     . GLU A 1 674 ? 104.987 122.516 116.134 1.00 54.76  ? 2465 GLU A O     1 
ATOM   4199 C  CB    . GLU A 1 674 ? 103.130 124.357 118.280 1.00 71.73  ? 2465 GLU A CB    1 
ATOM   4200 C  CG    . GLU A 1 674 ? 102.457 125.716 118.309 1.00 85.09  ? 2465 GLU A CG    1 
ATOM   4201 C  CD    . GLU A 1 674 ? 102.101 126.159 119.712 1.00 95.13  ? 2465 GLU A CD    1 
ATOM   4202 O  OE1   . GLU A 1 674 ? 102.362 125.392 120.663 1.00 89.33  ? 2465 GLU A OE1   1 
ATOM   4203 O  OE2   . GLU A 1 674 ? 101.563 127.275 119.866 1.00 100.10 ? 2465 GLU A OE2   1 
ATOM   4204 N  N     . ARG A 1 675 ? 103.721 121.398 117.630 1.00 57.84  ? 2466 ARG A N     1 
ATOM   4205 C  CA    . ARG A 1 675 ? 104.592 120.229 117.574 1.00 52.03  ? 2466 ARG A CA    1 
ATOM   4206 C  C     . ARG A 1 675 ? 104.549 119.570 116.201 1.00 46.92  ? 2466 ARG A C     1 
ATOM   4207 O  O     . ARG A 1 675 ? 105.569 119.053 115.724 1.00 52.90  ? 2466 ARG A O     1 
ATOM   4208 C  CB    . ARG A 1 675 ? 104.210 119.239 118.674 1.00 55.02  ? 2466 ARG A CB    1 
ATOM   4209 C  CG    . ARG A 1 675 ? 104.471 119.775 120.079 1.00 58.09  ? 2466 ARG A CG    1 
ATOM   4210 C  CD    . ARG A 1 675 ? 103.903 118.905 121.203 1.00 55.76  ? 2466 ARG A CD    1 
ATOM   4211 N  NE    . ARG A 1 675 ? 102.456 118.718 121.149 1.00 61.00  ? 2466 ARG A NE    1 
ATOM   4212 C  CZ    . ARG A 1 675 ? 101.842 117.728 120.517 1.00 61.12  ? 2466 ARG A CZ    1 
ATOM   4213 N  NH1   . ARG A 1 675 ? 102.517 116.820 119.834 1.00 57.31  ? 2466 ARG A NH1   1 
ATOM   4214 N  NH2   . ARG A 1 675 ? 100.517 117.642 120.578 1.00 62.91  ? 2466 ARG A NH2   1 
ATOM   4215 N  N     . GLN A 1 676 ? 103.390 119.606 115.542 1.00 45.48  ? 2467 GLN A N     1 
ATOM   4216 C  CA    . GLN A 1 676 ? 103.276 119.106 114.181 1.00 45.16  ? 2467 GLN A CA    1 
ATOM   4217 C  C     . GLN A 1 676 ? 104.151 119.907 113.233 1.00 46.12  ? 2467 GLN A C     1 
ATOM   4218 O  O     . GLN A 1 676 ? 104.788 119.340 112.349 1.00 48.34  ? 2467 GLN A O     1 
ATOM   4219 C  CB    . GLN A 1 676 ? 101.816 119.154 113.733 1.00 43.08  ? 2467 GLN A CB    1 
ATOM   4220 C  CG    . GLN A 1 676 ? 101.410 118.043 112.790 1.00 40.54  ? 2467 GLN A CG    1 
ATOM   4221 C  CD    . GLN A 1 676 ? 99.906  117.889 112.693 1.00 46.02  ? 2467 GLN A CD    1 
ATOM   4222 O  OE1   . GLN A 1 676 ? 99.198  118.823 112.319 1.00 48.16  ? 2467 GLN A OE1   1 
ATOM   4223 N  NE2   . GLN A 1 676 ? 99.410  116.704 113.029 1.00 50.11  ? 2467 GLN A NE2   1 
ATOM   4224 N  N     . ALA A 1 677 ? 104.195 121.227 113.405 1.00 48.14  ? 2468 ALA A N     1 
ATOM   4225 C  CA    . ALA A 1 677 ? 105.038 122.064 112.559 1.00 42.75  ? 2468 ALA A CA    1 
ATOM   4226 C  C     . ALA A 1 677 ? 106.510 121.738 112.760 1.00 42.85  ? 2468 ALA A C     1 
ATOM   4227 O  O     . ALA A 1 677 ? 107.269 121.607 111.790 1.00 52.54  ? 2468 ALA A O     1 
ATOM   4228 C  CB    . ALA A 1 677 ? 104.767 123.538 112.856 1.00 51.30  ? 2468 ALA A CB    1 
ATOM   4229 N  N     . ILE A 1 678 ? 106.931 121.600 114.019 1.00 38.41  ? 2469 ILE A N     1 
ATOM   4230 C  CA    . ILE A 1 678 ? 108.339 121.309 114.294 1.00 35.89  ? 2469 ILE A CA    1 
ATOM   4231 C  C     . ILE A 1 678 ? 108.731 119.964 113.689 1.00 35.68  ? 2469 ILE A C     1 
ATOM   4232 O  O     . ILE A 1 678 ? 109.727 119.849 112.953 1.00 33.90  ? 2469 ILE A O     1 
ATOM   4233 C  CB    . ILE A 1 678 ? 108.612 121.343 115.807 1.00 39.47  ? 2469 ILE A CB    1 
ATOM   4234 C  CG1   . ILE A 1 678 ? 108.175 122.683 116.400 1.00 50.80  ? 2469 ILE A CG1   1 
ATOM   4235 C  CG2   . ILE A 1 678 ? 110.082 121.089 116.083 1.00 37.35  ? 2469 ILE A CG2   1 
ATOM   4236 C  CD1   . ILE A 1 678 ? 108.055 122.674 117.906 1.00 51.82  ? 2469 ILE A CD1   1 
ATOM   4237 N  N     . ASN A 1 679 ? 107.942 118.926 113.973 1.00 39.67  ? 2470 ASN A N     1 
ATOM   4238 C  CA    . ASN A 1 679 ? 108.269 117.627 113.405 1.00 35.68  ? 2470 ASN A CA    1 
ATOM   4239 C  C     . ASN A 1 679 ? 108.114 117.624 111.895 1.00 31.62  ? 2470 ASN A C     1 
ATOM   4240 O  O     . ASN A 1 679 ? 108.837 116.903 111.213 1.00 35.29  ? 2470 ASN A O     1 
ATOM   4241 C  CB    . ASN A 1 679 ? 107.413 116.521 114.004 1.00 39.80  ? 2470 ASN A CB    1 
ATOM   4242 C  CG    . ASN A 1 679 ? 107.925 115.147 113.633 1.00 40.14  ? 2470 ASN A CG    1 
ATOM   4243 O  OD1   . ASN A 1 679 ? 109.045 115.002 113.149 1.00 38.68  ? 2470 ASN A OD1   1 
ATOM   4244 N  ND2   . ASN A 1 679 ? 107.102 114.138 113.827 1.00 42.05  ? 2470 ASN A ND2   1 
ATOM   4245 N  N     . THR A 1 680 ? 107.200 118.423 111.350 1.00 29.80  ? 2471 THR A N     1 
ATOM   4246 C  CA    . THR A 1 680 ? 107.014 118.436 109.909 1.00 29.45  ? 2471 THR A CA    1 
ATOM   4247 C  C     . THR A 1 680 ? 108.238 119.004 109.215 1.00 29.78  ? 2471 THR A C     1 
ATOM   4248 O  O     . THR A 1 680 ? 108.743 118.409 108.262 1.00 34.15  ? 2471 THR A O     1 
ATOM   4249 C  CB    . THR A 1 680 ? 105.765 119.232 109.537 1.00 36.20  ? 2471 THR A CB    1 
ATOM   4250 O  OG1   . THR A 1 680 ? 104.608 118.403 109.694 1.00 46.39  ? 2471 THR A OG1   1 
ATOM   4251 C  CG2   . THR A 1 680 ? 105.846 119.682 108.093 1.00 29.90  ? 2471 THR A CG2   1 
ATOM   4252 N  N     . ILE A 1 681 ? 108.755 120.136 109.696 1.00 33.87  ? 2472 ILE A N     1 
ATOM   4253 C  CA    . ILE A 1 681 ? 109.946 120.694 109.057 1.00 33.00  ? 2472 ILE A CA    1 
ATOM   4254 C  C     . ILE A 1 681 ? 111.120 119.732 109.202 1.00 25.17  ? 2472 ILE A C     1 
ATOM   4255 O  O     . ILE A 1 681 ? 111.810 119.421 108.222 1.00 29.66  ? 2472 ILE A O     1 
ATOM   4256 C  CB    . ILE A 1 681 ? 110.275 122.098 109.601 1.00 30.29  ? 2472 ILE A CB    1 
ATOM   4257 C  CG1   . ILE A 1 681 ? 111.631 122.564 109.069 1.00 28.15  ? 2472 ILE A CG1   1 
ATOM   4258 C  CG2   . ILE A 1 681 ? 110.284 122.139 111.105 1.00 31.28  ? 2472 ILE A CG2   1 
ATOM   4259 C  CD1   . ILE A 1 681 ? 112.003 123.964 109.498 1.00 31.25  ? 2472 ILE A CD1   1 
ATOM   4260 N  N     . VAL A 1 682 ? 111.329 119.191 110.408 1.00 23.74  ? 2473 VAL A N     1 
ATOM   4261 C  CA    . VAL A 1 682 ? 112.503 118.343 110.619 1.00 28.56  ? 2473 VAL A CA    1 
ATOM   4262 C  C     . VAL A 1 682 ? 112.392 117.048 109.812 1.00 29.07  ? 2473 VAL A C     1 
ATOM   4263 O  O     . VAL A 1 682 ? 113.335 116.639 109.120 1.00 32.45  ? 2473 VAL A O     1 
ATOM   4264 C  CB    . VAL A 1 682 ? 112.695 118.067 112.120 1.00 32.08  ? 2473 VAL A CB    1 
ATOM   4265 C  CG1   . VAL A 1 682 ? 113.688 116.951 112.327 1.00 23.03  ? 2473 VAL A CG1   1 
ATOM   4266 C  CG2   . VAL A 1 682 ? 113.152 119.327 112.830 1.00 40.19  ? 2473 VAL A CG2   1 
ATOM   4267 N  N     . GLN A 1 683 ? 111.231 116.393 109.869 1.00 30.08  ? 2474 GLN A N     1 
ATOM   4268 C  CA    . GLN A 1 683 ? 111.034 115.118 109.194 1.00 29.02  ? 2474 GLN A CA    1 
ATOM   4269 C  C     . GLN A 1 683 ? 110.961 115.276 107.683 1.00 28.96  ? 2474 GLN A C     1 
ATOM   4270 O  O     . GLN A 1 683 ? 111.413 114.391 106.953 1.00 31.13  ? 2474 GLN A O     1 
ATOM   4271 C  CB    . GLN A 1 683 ? 109.765 114.453 109.721 1.00 31.32  ? 2474 GLN A CB    1 
ATOM   4272 C  CG    . GLN A 1 683 ? 109.807 112.946 109.715 1.00 33.42  ? 2474 GLN A CG    1 
ATOM   4273 C  CD    . GLN A 1 683 ? 108.612 112.338 110.411 1.00 36.59  ? 2474 GLN A CD    1 
ATOM   4274 O  OE1   . GLN A 1 683 ? 108.396 112.555 111.603 1.00 29.24  ? 2474 GLN A OE1   1 
ATOM   4275 N  NE2   . GLN A 1 683 ? 107.823 111.575 109.669 1.00 46.68  ? 2474 GLN A NE2   1 
ATOM   4276 N  N     . GLY A 1 684 ? 110.388 116.375 107.190 1.00 31.01  ? 2475 GLY A N     1 
ATOM   4277 C  CA    . GLY A 1 684 ? 110.426 116.635 105.766 1.00 32.24  ? 2475 GLY A CA    1 
ATOM   4278 C  C     . GLY A 1 684 ? 111.836 116.876 105.274 1.00 33.22  ? 2475 GLY A C     1 
ATOM   4279 O  O     . GLY A 1 684 ? 112.199 116.437 104.182 1.00 35.13  ? 2475 GLY A O     1 
ATOM   4280 N  N     . SER A 1 685 ? 112.653 117.573 106.070 1.00 31.92  ? 2476 SER A N     1 
ATOM   4281 C  CA    . SER A 1 685 ? 114.058 117.711 105.708 1.00 33.57  ? 2476 SER A CA    1 
ATOM   4282 C  C     . SER A 1 685 ? 114.740 116.352 105.649 1.00 33.32  ? 2476 SER A C     1 
ATOM   4283 O  O     . SER A 1 685 ? 115.487 116.068 104.707 1.00 37.31  ? 2476 SER A O     1 
ATOM   4284 C  CB    . SER A 1 685 ? 114.770 118.633 106.695 1.00 32.09  ? 2476 SER A CB    1 
ATOM   4285 O  OG    . SER A 1 685 ? 114.112 119.883 106.785 1.00 44.91  ? 2476 SER A OG    1 
ATOM   4286 N  N     . ALA A 1 686 ? 114.477 115.490 106.634 1.00 31.87  ? 2477 ALA A N     1 
ATOM   4287 C  CA    . ALA A 1 686 ? 115.081 114.158 106.623 1.00 30.75  ? 2477 ALA A CA    1 
ATOM   4288 C  C     . ALA A 1 686 ? 114.633 113.348 105.409 1.00 30.30  ? 2477 ALA A C     1 
ATOM   4289 O  O     . ALA A 1 686 ? 115.451 112.692 104.749 1.00 32.08  ? 2477 ALA A O     1 
ATOM   4290 C  CB    . ALA A 1 686 ? 114.738 113.416 107.913 1.00 33.57  ? 2477 ALA A CB    1 
ATOM   4291 N  N     . ALA A 1 687 ? 113.336 113.383 105.100 1.00 25.89  ? 2478 ALA A N     1 
ATOM   4292 C  CA    . ALA A 1 687 ? 112.813 112.624 103.970 1.00 22.49  ? 2478 ALA A CA    1 
ATOM   4293 C  C     . ALA A 1 687 ? 113.343 113.163 102.649 1.00 28.85  ? 2478 ALA A C     1 
ATOM   4294 O  O     . ALA A 1 687 ? 113.632 112.391 101.731 1.00 31.51  ? 2478 ALA A O     1 
ATOM   4295 C  CB    . ALA A 1 687 ? 111.287 112.643 103.986 1.00 22.23  ? 2478 ALA A CB    1 
ATOM   4296 N  N     . ASP A 1 688 ? 113.486 114.483 102.531 1.00 30.82  ? 2479 ASP A N     1 
ATOM   4297 C  CA    . ASP A 1 688 ? 114.042 115.038 101.305 1.00 32.42  ? 2479 ASP A CA    1 
ATOM   4298 C  C     . ASP A 1 688 ? 115.522 114.713 101.172 1.00 29.74  ? 2479 ASP A C     1 
ATOM   4299 O  O     . ASP A 1 688 ? 116.003 114.483 100.058 1.00 33.04  ? 2479 ASP A O     1 
ATOM   4300 C  CB    . ASP A 1 688 ? 113.818 116.546 101.254 1.00 37.60  ? 2479 ASP A CB    1 
ATOM   4301 C  CG    . ASP A 1 688 ? 113.409 117.021 99.876  1.00 49.96  ? 2479 ASP A CG    1 
ATOM   4302 O  OD1   . ASP A 1 688 ? 114.245 116.961 98.951  1.00 54.38  ? 2479 ASP A OD1   1 
ATOM   4303 O  OD2   . ASP A 1 688 ? 112.249 117.454 99.715  1.00 50.69  ? 2479 ASP A OD2   1 
ATOM   4304 N  N     . ILE A 1 689 ? 116.258 114.676 102.286 1.00 25.58  ? 2480 ILE A N     1 
ATOM   4305 C  CA    . ILE A 1 689 ? 117.654 114.252 102.229 1.00 25.60  ? 2480 ILE A CA    1 
ATOM   4306 C  C     . ILE A 1 689 ? 117.747 112.811 101.750 1.00 25.78  ? 2480 ILE A C     1 
ATOM   4307 O  O     . ILE A 1 689 ? 118.568 112.479 100.885 1.00 30.18  ? 2480 ILE A O     1 
ATOM   4308 C  CB    . ILE A 1 689 ? 118.334 114.432 103.599 1.00 23.63  ? 2480 ILE A CB    1 
ATOM   4309 C  CG1   . ILE A 1 689 ? 118.422 115.908 103.984 1.00 25.58  ? 2480 ILE A CG1   1 
ATOM   4310 C  CG2   . ILE A 1 689 ? 119.719 113.828 103.581 1.00 21.17  ? 2480 ILE A CG2   1 
ATOM   4311 C  CD1   . ILE A 1 689 ? 118.772 116.817 102.851 1.00 32.85  ? 2480 ILE A CD1   1 
ATOM   4312 N  N     . VAL A 1 690 ? 116.900 111.932 102.292 1.00 23.46  ? 2481 VAL A N     1 
ATOM   4313 C  CA    . VAL A 1 690 ? 116.964 110.535 101.873 1.00 22.90  ? 2481 VAL A CA    1 
ATOM   4314 C  C     . VAL A 1 690 ? 116.501 110.380 100.427 1.00 27.94  ? 2481 VAL A C     1 
ATOM   4315 O  O     . VAL A 1 690 ? 116.995 109.508 99.707  1.00 32.89  ? 2481 VAL A O     1 
ATOM   4316 C  CB    . VAL A 1 690 ? 116.173 109.626 102.835 1.00 20.74  ? 2481 VAL A CB    1 
ATOM   4317 C  CG1   . VAL A 1 690 ? 114.704 109.580 102.478 1.00 23.32  ? 2481 VAL A CG1   1 
ATOM   4318 C  CG2   . VAL A 1 690 ? 116.757 108.226 102.827 1.00 13.87  ? 2481 VAL A CG2   1 
ATOM   4319 N  N     . LYS A 1 691 ? 115.579 111.227 99.962  1.00 27.03  ? 2482 LYS A N     1 
ATOM   4320 C  CA    . LYS A 1 691 ? 115.148 111.152 98.568  1.00 25.65  ? 2482 LYS A CA    1 
ATOM   4321 C  C     . LYS A 1 691 ? 116.244 111.631 97.622  1.00 25.31  ? 2482 LYS A C     1 
ATOM   4322 O  O     . LYS A 1 691 ? 116.445 111.050 96.547  1.00 28.81  ? 2482 LYS A O     1 
ATOM   4323 C  CB    . LYS A 1 691 ? 113.869 111.965 98.373  1.00 26.81  ? 2482 LYS A CB    1 
ATOM   4324 C  CG    . LYS A 1 691 ? 112.599 111.169 98.625  1.00 27.98  ? 2482 LYS A CG    1 
ATOM   4325 C  CD    . LYS A 1 691 ? 111.351 111.977 98.309  1.00 28.34  ? 2482 LYS A CD    1 
ATOM   4326 C  CE    . LYS A 1 691 ? 111.147 113.090 99.317  1.00 29.69  ? 2482 LYS A CE    1 
ATOM   4327 N  NZ    . LYS A 1 691 ? 109.859 113.797 99.099  1.00 29.81  ? 2482 LYS A NZ    1 
ATOM   4328 N  N     . ILE A 1 692 ? 116.957 112.693 98.003  1.00 24.51  ? 2483 ILE A N     1 
ATOM   4329 C  CA    . ILE A 1 692 ? 118.116 113.126 97.230  1.00 24.62  ? 2483 ILE A CA    1 
ATOM   4330 C  C     . ILE A 1 692 ? 119.159 112.021 97.190  1.00 27.65  ? 2483 ILE A C     1 
ATOM   4331 O  O     . ILE A 1 692 ? 119.783 111.772 96.152  1.00 30.45  ? 2483 ILE A O     1 
ATOM   4332 C  CB    . ILE A 1 692 ? 118.694 114.429 97.810  1.00 22.56  ? 2483 ILE A CB    1 
ATOM   4333 C  CG1   . ILE A 1 692 ? 117.717 115.584 97.610  1.00 20.31  ? 2483 ILE A CG1   1 
ATOM   4334 C  CG2   . ILE A 1 692 ? 120.021 114.761 97.156  1.00 25.60  ? 2483 ILE A CG2   1 
ATOM   4335 C  CD1   . ILE A 1 692 ? 118.244 116.908 98.077  1.00 24.67  ? 2483 ILE A CD1   1 
ATOM   4336 N  N     . ALA A 1 693 ? 119.361 111.337 98.318  1.00 22.72  ? 2484 ALA A N     1 
ATOM   4337 C  CA    . ALA A 1 693 ? 120.282 110.207 98.335  1.00 21.39  ? 2484 ALA A CA    1 
ATOM   4338 C  C     . ALA A 1 693 ? 119.824 109.108 97.385  1.00 24.45  ? 2484 ALA A C     1 
ATOM   4339 O  O     . ALA A 1 693 ? 120.639 108.530 96.659  1.00 28.25  ? 2484 ALA A O     1 
ATOM   4340 C  CB    . ALA A 1 693 ? 120.423 109.665 99.755  1.00 27.66  ? 2484 ALA A CB    1 
ATOM   4341 N  N     . THR A 1 694 ? 118.522 108.810 97.373  1.00 23.23  ? 2485 THR A N     1 
ATOM   4342 C  CA    . THR A 1 694 ? 117.999 107.778 96.481  1.00 23.46  ? 2485 THR A CA    1 
ATOM   4343 C  C     . THR A 1 694 ? 118.253 108.132 95.022  1.00 28.24  ? 2485 THR A C     1 
ATOM   4344 O  O     . THR A 1 694 ? 118.741 107.302 94.245  1.00 32.67  ? 2485 THR A O     1 
ATOM   4345 C  CB    . THR A 1 694 ? 116.500 107.579 96.708  1.00 22.52  ? 2485 THR A CB    1 
ATOM   4346 O  OG1   . THR A 1 694 ? 116.216 107.547 98.109  1.00 22.51  ? 2485 THR A OG1   1 
ATOM   4347 C  CG2   . THR A 1 694 ? 116.044 106.278 96.079  1.00 24.73  ? 2485 THR A CG2   1 
ATOM   4348 N  N     . VAL A 1 695 ? 117.926 109.365 94.632  1.00 29.49  ? 2486 VAL A N     1 
ATOM   4349 C  CA    . VAL A 1 695 ? 118.073 109.745 93.229  1.00 28.38  ? 2486 VAL A CA    1 
ATOM   4350 C  C     . VAL A 1 695 ? 119.547 109.816 92.842  1.00 31.97  ? 2486 VAL A C     1 
ATOM   4351 O  O     . VAL A 1 695 ? 119.926 109.422 91.733  1.00 37.55  ? 2486 VAL A O     1 
ATOM   4352 C  CB    . VAL A 1 695 ? 117.325 111.060 92.935  1.00 26.54  ? 2486 VAL A CB    1 
ATOM   4353 C  CG1   . VAL A 1 695 ? 115.888 110.954 93.398  1.00 30.55  ? 2486 VAL A CG1   1 
ATOM   4354 C  CG2   . VAL A 1 695 ? 118.003 112.249 93.588  1.00 29.24  ? 2486 VAL A CG2   1 
ATOM   4355 N  N     . ASN A 1 696 ? 120.407 110.288 93.750  1.00 26.81  ? 2487 ASN A N     1 
ATOM   4356 C  CA    . ASN A 1 696 ? 121.834 110.339 93.454  1.00 30.31  ? 2487 ASN A CA    1 
ATOM   4357 C  C     . ASN A 1 696 ? 122.418 108.942 93.297  1.00 35.21  ? 2487 ASN A C     1 
ATOM   4358 O  O     . ASN A 1 696 ? 123.210 108.695 92.380  1.00 41.70  ? 2487 ASN A O     1 
ATOM   4359 C  CB    . ASN A 1 696 ? 122.570 111.108 94.549  1.00 30.66  ? 2487 ASN A CB    1 
ATOM   4360 C  CG    . ASN A 1 696 ? 122.302 112.597 94.497  1.00 28.24  ? 2487 ASN A CG    1 
ATOM   4361 O  OD1   . ASN A 1 696 ? 121.339 113.045 93.877  1.00 23.74  ? 2487 ASN A OD1   1 
ATOM   4362 N  ND2   . ASN A 1 696 ? 123.158 113.375 95.150  1.00 35.19  ? 2487 ASN A ND2   1 
ATOM   4363 N  N     . ILE A 1 697 ? 122.042 108.014 94.179  1.00 30.02  ? 2488 ILE A N     1 
ATOM   4364 C  CA    . ILE A 1 697 ? 122.549 106.651 94.077  1.00 28.58  ? 2488 ILE A CA    1 
ATOM   4365 C  C     . ILE A 1 697 ? 122.046 105.990 92.803  1.00 33.11  ? 2488 ILE A C     1 
ATOM   4366 O  O     . ILE A 1 697 ? 122.788 105.262 92.132  1.00 39.68  ? 2488 ILE A O     1 
ATOM   4367 C  CB    . ILE A 1 697 ? 122.167 105.841 95.328  1.00 25.39  ? 2488 ILE A CB    1 
ATOM   4368 C  CG1   . ILE A 1 697 ? 122.918 106.368 96.548  1.00 39.15  ? 2488 ILE A CG1   1 
ATOM   4369 C  CG2   . ILE A 1 697 ? 122.486 104.374 95.127  1.00 29.56  ? 2488 ILE A CG2   1 
ATOM   4370 C  CD1   . ILE A 1 697 ? 122.299 105.960 97.861  1.00 43.18  ? 2488 ILE A CD1   1 
ATOM   4371 N  N     . GLN A 1 698 ? 120.779 106.222 92.449  1.00 37.44  ? 2489 GLN A N     1 
ATOM   4372 C  CA    . GLN A 1 698 ? 120.260 105.663 91.206  1.00 43.34  ? 2489 GLN A CA    1 
ATOM   4373 C  C     . GLN A 1 698 ? 121.001 106.225 90.001  1.00 51.36  ? 2489 GLN A C     1 
ATOM   4374 O  O     . GLN A 1 698 ? 121.334 105.484 89.073  1.00 56.08  ? 2489 GLN A O     1 
ATOM   4375 C  CB    . GLN A 1 698 ? 118.760 105.926 91.088  1.00 34.82  ? 2489 GLN A CB    1 
ATOM   4376 C  CG    . GLN A 1 698 ? 118.013 104.843 90.333  1.00 29.42  ? 2489 GLN A CG    1 
ATOM   4377 C  CD    . GLN A 1 698 ? 118.054 103.507 91.046  1.00 27.18  ? 2489 GLN A CD    1 
ATOM   4378 O  OE1   . GLN A 1 698 ? 117.843 103.430 92.255  1.00 22.18  ? 2489 GLN A OE1   1 
ATOM   4379 N  NE2   . GLN A 1 698 ? 118.329 102.445 90.299  1.00 30.43  ? 2489 GLN A NE2   1 
ATOM   4380 N  N     . LYS A 1 699 ? 121.291 107.529 90.007  1.00 52.38  ? 2490 LYS A N     1 
ATOM   4381 C  CA    . LYS A 1 699 ? 122.073 108.113 88.921  1.00 50.87  ? 2490 LYS A CA    1 
ATOM   4382 C  C     . LYS A 1 699 ? 123.461 107.490 88.845  1.00 48.15  ? 2490 LYS A C     1 
ATOM   4383 O  O     . LYS A 1 699 ? 123.953 107.178 87.753  1.00 55.94  ? 2490 LYS A O     1 
ATOM   4384 C  CB    . LYS A 1 699 ? 122.182 109.626 89.107  1.00 44.82  ? 2490 LYS A CB    1 
ATOM   4385 C  CG    . LYS A 1 699 ? 120.933 110.404 88.734  1.00 45.36  ? 2490 LYS A CG    1 
ATOM   4386 C  CD    . LYS A 1 699 ? 121.115 111.888 89.013  1.00 46.61  ? 2490 LYS A CD    1 
ATOM   4387 C  CE    . LYS A 1 699 ? 119.825 112.658 88.789  1.00 47.37  ? 2490 LYS A CE    1 
ATOM   4388 N  NZ    . LYS A 1 699 ? 119.938 114.075 89.233  1.00 46.45  ? 2490 LYS A NZ    1 
ATOM   4389 N  N     . GLN A 1 700 ? 124.105 107.296 89.998  1.00 39.57  ? 2491 GLN A N     1 
ATOM   4390 C  CA    . GLN A 1 700 ? 125.479 106.805 90.001  1.00 46.41  ? 2491 GLN A CA    1 
ATOM   4391 C  C     . GLN A 1 700 ? 125.557 105.349 89.559  1.00 52.02  ? 2491 GLN A C     1 
ATOM   4392 O  O     . GLN A 1 700 ? 126.480 104.968 88.831  1.00 59.09  ? 2491 GLN A O     1 
ATOM   4393 C  CB    . GLN A 1 700 ? 126.098 106.983 91.385  1.00 47.31  ? 2491 GLN A CB    1 
ATOM   4394 C  CG    . GLN A 1 700 ? 127.607 107.142 91.364  1.00 43.19  ? 2491 GLN A CG    1 
ATOM   4395 C  CD    . GLN A 1 700 ? 128.052 108.440 90.719  1.00 42.80  ? 2491 GLN A CD    1 
ATOM   4396 O  OE1   . GLN A 1 700 ? 127.261 109.368 90.550  1.00 39.41  ? 2491 GLN A OE1   1 
ATOM   4397 N  NE2   . GLN A 1 700 ? 129.326 108.511 90.353  1.00 43.88  ? 2491 GLN A NE2   1 
ATOM   4398 N  N     . LEU A 1 701 ? 124.607 104.518 89.986  1.00 47.86  ? 2492 LEU A N     1 
ATOM   4399 C  CA    . LEU A 1 701 ? 124.584 103.138 89.516  1.00 50.80  ? 2492 LEU A CA    1 
ATOM   4400 C  C     . LEU A 1 701 ? 123.892 102.997 88.167  1.00 55.15  ? 2492 LEU A C     1 
ATOM   4401 O  O     . LEU A 1 701 ? 123.820 101.885 87.636  1.00 63.54  ? 2492 LEU A O     1 
ATOM   4402 C  CB    . LEU A 1 701 ? 123.921 102.223 90.551  1.00 47.48  ? 2492 LEU A CB    1 
ATOM   4403 C  CG    . LEU A 1 701 ? 122.412 102.282 90.780  1.00 51.52  ? 2492 LEU A CG    1 
ATOM   4404 C  CD1   . LEU A 1 701 ? 121.707 101.169 90.020  1.00 50.74  ? 2492 LEU A CD1   1 
ATOM   4405 C  CD2   . LEU A 1 701 ? 122.119 102.173 92.263  1.00 43.86  ? 2492 LEU A CD2   1 
ATOM   4406 N  N     . GLU A 1 702 ? 123.363 104.091 87.620  1.00 56.59  ? 2493 GLU A N     1 
ATOM   4407 C  CA    . GLU A 1 702 ? 122.935 104.114 86.229  1.00 64.13  ? 2493 GLU A CA    1 
ATOM   4408 C  C     . GLU A 1 702 ? 124.116 104.388 85.308  1.00 65.02  ? 2493 GLU A C     1 
ATOM   4409 O  O     . GLU A 1 702 ? 124.291 103.711 84.289  1.00 67.02  ? 2493 GLU A O     1 
ATOM   4410 C  CB    . GLU A 1 702 ? 121.851 105.177 86.042  1.00 66.85  ? 2493 GLU A CB    1 
ATOM   4411 C  CG    . GLU A 1 702 ? 120.609 104.714 85.307  1.00 67.21  ? 2493 GLU A CG    1 
ATOM   4412 C  CD    . GLU A 1 702 ? 119.516 105.767 85.317  1.00 78.56  ? 2493 GLU A CD    1 
ATOM   4413 O  OE1   . GLU A 1 702 ? 119.840 106.956 85.519  1.00 77.84  ? 2493 GLU A OE1   1 
ATOM   4414 O  OE2   . GLU A 1 702 ? 118.336 105.410 85.130  1.00 83.72  ? 2493 GLU A OE2   1 
ATOM   4415 N  N     . THR A 1 703 ? 124.936 105.385 85.656  1.00 62.32  ? 2494 THR A N     1 
ATOM   4416 C  CA    . THR A 1 703 ? 126.130 105.671 84.866  1.00 63.28  ? 2494 THR A CA    1 
ATOM   4417 C  C     . THR A 1 703 ? 127.107 104.503 84.916  1.00 62.40  ? 2494 THR A C     1 
ATOM   4418 O  O     . THR A 1 703 ? 127.630 104.070 83.883  1.00 67.79  ? 2494 THR A O     1 
ATOM   4419 C  CB    . THR A 1 703 ? 126.798 106.954 85.363  1.00 60.21  ? 2494 THR A CB    1 
ATOM   4420 O  OG1   . THR A 1 703 ? 127.171 106.803 86.737  1.00 58.59  ? 2494 THR A OG1   1 
ATOM   4421 C  CG2   . THR A 1 703 ? 125.850 108.136 85.228  1.00 49.93  ? 2494 THR A CG2   1 
ATOM   4422 N  N     . PHE A 1 704 ? 127.361 103.978 86.108  1.00 58.31  ? 2495 PHE A N     1 
ATOM   4423 C  CA    . PHE A 1 704 ? 128.170 102.782 86.265  1.00 65.59  ? 2495 PHE A CA    1 
ATOM   4424 C  C     . PHE A 1 704 ? 127.288 101.544 86.143  1.00 66.57  ? 2495 PHE A C     1 
ATOM   4425 O  O     . PHE A 1 704 ? 126.060 101.629 86.107  1.00 66.02  ? 2495 PHE A O     1 
ATOM   4426 C  CB    . PHE A 1 704 ? 128.896 102.791 87.612  1.00 68.30  ? 2495 PHE A CB    1 
ATOM   4427 C  CG    . PHE A 1 704 ? 129.916 103.886 87.748  1.00 71.91  ? 2495 PHE A CG    1 
ATOM   4428 C  CD1   . PHE A 1 704 ? 130.420 104.530 86.630  1.00 73.80  ? 2495 PHE A CD1   1 
ATOM   4429 C  CD2   . PHE A 1 704 ? 130.371 104.272 88.997  1.00 68.34  ? 2495 PHE A CD2   1 
ATOM   4430 C  CE1   . PHE A 1 704 ? 131.358 105.538 86.756  1.00 71.80  ? 2495 PHE A CE1   1 
ATOM   4431 C  CE2   . PHE A 1 704 ? 131.309 105.278 89.130  1.00 67.85  ? 2495 PHE A CE2   1 
ATOM   4432 C  CZ    . PHE A 1 704 ? 131.803 105.912 88.008  1.00 71.83  ? 2495 PHE A CZ    1 
ATOM   4433 N  N     . HIS A 1 705 ? 127.934 100.380 86.075  1.00 69.90  ? 2496 HIS A N     1 
ATOM   4434 C  CA    . HIS A 1 705 ? 127.246 99.090  86.024  1.00 71.97  ? 2496 HIS A CA    1 
ATOM   4435 C  C     . HIS A 1 705 ? 126.204 99.072  84.901  1.00 71.14  ? 2496 HIS A C     1 
ATOM   4436 O  O     . HIS A 1 705 ? 124.997 99.018  85.130  1.00 67.64  ? 2496 HIS A O     1 
ATOM   4437 C  CB    . HIS A 1 705 ? 126.605 98.760  87.376  1.00 69.27  ? 2496 HIS A CB    1 
ATOM   4438 C  CG    . HIS A 1 705 ? 127.379 99.267  88.552  1.00 64.56  ? 2496 HIS A CG    1 
ATOM   4439 N  ND1   . HIS A 1 705 ? 127.026 100.408 89.240  1.00 60.19  ? 2496 HIS A ND1   1 
ATOM   4440 C  CD2   . HIS A 1 705 ? 128.485 98.786  89.166  1.00 68.83  ? 2496 HIS A CD2   1 
ATOM   4441 C  CE1   . HIS A 1 705 ? 127.882 100.610 90.225  1.00 66.04  ? 2496 HIS A CE1   1 
ATOM   4442 N  NE2   . HIS A 1 705 ? 128.778 99.640  90.202  1.00 71.17  ? 2496 HIS A NE2   1 
ATOM   4443 N  N     . SER A 1 706 ? 126.717 99.148  83.672  1.00 76.55  ? 2497 SER A N     1 
ATOM   4444 C  CA    . SER A 1 706 ? 125.879 99.219  82.474  1.00 86.65  ? 2497 SER A CA    1 
ATOM   4445 C  C     . SER A 1 706 ? 125.262 97.847  82.211  1.00 85.92  ? 2497 SER A C     1 
ATOM   4446 O  O     . SER A 1 706 ? 125.690 97.085  81.341  1.00 80.31  ? 2497 SER A O     1 
ATOM   4447 C  CB    . SER A 1 706 ? 126.689 99.705  81.278  1.00 86.29  ? 2497 SER A CB    1 
ATOM   4448 O  OG    . SER A 1 706 ? 127.009 101.079 81.401  1.00 77.32  ? 2497 SER A OG    1 
ATOM   4449 N  N     . THR A 1 707 ? 124.230 97.534  82.994  1.00 84.13  ? 2498 THR A N     1 
ATOM   4450 C  CA    . THR A 1 707 ? 123.466 96.301  82.862  1.00 80.08  ? 2498 THR A CA    1 
ATOM   4451 C  C     . THR A 1 707 ? 121.981 96.626  82.931  1.00 79.27  ? 2498 THR A C     1 
ATOM   4452 O  O     . THR A 1 707 ? 121.592 97.794  82.832  1.00 87.22  ? 2498 THR A O     1 
ATOM   4453 C  CB    . THR A 1 707 ? 123.830 95.294  83.959  1.00 73.76  ? 2498 THR A CB    1 
ATOM   4454 O  OG1   . THR A 1 707 ? 123.318 95.750  85.216  1.00 57.70  ? 2498 THR A OG1   1 
ATOM   4455 C  CG2   . THR A 1 707 ? 125.339 95.108  84.063  1.00 80.90  ? 2498 THR A CG2   1 
ATOM   4456 N  N     . PHE A 1 708 ? 121.146 95.603  83.093  1.00 73.78  ? 2499 PHE A N     1 
ATOM   4457 C  CA    . PHE A 1 708 ? 119.716 95.828  83.243  1.00 63.91  ? 2499 PHE A CA    1 
ATOM   4458 C  C     . PHE A 1 708 ? 119.443 96.597  84.529  1.00 55.27  ? 2499 PHE A C     1 
ATOM   4459 O  O     . PHE A 1 708 ? 119.979 96.269  85.592  1.00 58.21  ? 2499 PHE A O     1 
ATOM   4460 C  CB    . PHE A 1 708 ? 118.977 94.492  83.234  1.00 63.79  ? 2499 PHE A CB    1 
ATOM   4461 C  CG    . PHE A 1 708 ? 119.174 93.712  81.968  1.00 80.17  ? 2499 PHE A CG    1 
ATOM   4462 C  CD1   . PHE A 1 708 ? 119.214 94.359  80.744  1.00 86.24  ? 2499 PHE A CD1   1 
ATOM   4463 C  CD2   . PHE A 1 708 ? 119.350 92.340  81.999  1.00 83.70  ? 2499 PHE A CD2   1 
ATOM   4464 C  CE1   . PHE A 1 708 ? 119.405 93.651  79.575  1.00 86.63  ? 2499 PHE A CE1   1 
ATOM   4465 C  CE2   . PHE A 1 708 ? 119.542 91.625  80.833  1.00 94.38  ? 2499 PHE A CE2   1 
ATOM   4466 C  CZ    . PHE A 1 708 ? 119.572 92.282  79.620  1.00 97.09  ? 2499 PHE A CZ    1 
ATOM   4467 N  N     . LYS A 1 709 ? 118.606 97.630  84.424  1.00 46.21  ? 2500 LYS A N     1 
ATOM   4468 C  CA    . LYS A 1 709 ? 118.475 98.597  85.509  1.00 41.22  ? 2500 LYS A CA    1 
ATOM   4469 C  C     . LYS A 1 709 ? 117.758 98.003  86.715  1.00 36.73  ? 2500 LYS A C     1 
ATOM   4470 O  O     . LYS A 1 709 ? 118.103 98.308  87.862  1.00 35.54  ? 2500 LYS A O     1 
ATOM   4471 C  CB    . LYS A 1 709 ? 117.742 99.834  85.002  1.00 39.84  ? 2500 LYS A CB    1 
ATOM   4472 C  CG    . LYS A 1 709 ? 117.583 100.937 86.025  1.00 36.05  ? 2500 LYS A CG    1 
ATOM   4473 C  CD    . LYS A 1 709 ? 117.616 102.304 85.358  1.00 43.43  ? 2500 LYS A CD    1 
ATOM   4474 C  CE    . LYS A 1 709 ? 117.234 102.225 83.884  1.00 46.79  ? 2500 LYS A CE    1 
ATOM   4475 N  NZ    . LYS A 1 709 ? 117.429 103.515 83.172  1.00 47.63  ? 2500 LYS A NZ    1 
ATOM   4476 N  N     . SER A 1 710 ? 116.758 97.158  86.479  1.00 43.29  ? 2501 SER A N     1 
ATOM   4477 C  CA    . SER A 1 710 ? 115.965 96.591  87.558  1.00 42.54  ? 2501 SER A CA    1 
ATOM   4478 C  C     . SER A 1 710 ? 115.409 95.251  87.102  1.00 47.80  ? 2501 SER A C     1 
ATOM   4479 O  O     . SER A 1 710 ? 115.377 94.947  85.907  1.00 58.36  ? 2501 SER A O     1 
ATOM   4480 C  CB    . SER A 1 710 ? 114.838 97.545  87.975  1.00 39.27  ? 2501 SER A CB    1 
ATOM   4481 O  OG    . SER A 1 710 ? 113.718 96.846  88.484  1.00 44.40  ? 2501 SER A OG    1 
ATOM   4482 N  N     . HIS A 1 711 ? 114.980 94.441  88.073  1.00 40.82  ? 2502 HIS A N     1 
ATOM   4483 C  CA    . HIS A 1 711 ? 114.380 93.153  87.745  1.00 43.77  ? 2502 HIS A CA    1 
ATOM   4484 C  C     . HIS A 1 711 ? 113.143 93.321  86.875  1.00 49.88  ? 2502 HIS A C     1 
ATOM   4485 O  O     . HIS A 1 711 ? 112.824 92.436  86.071  1.00 62.16  ? 2502 HIS A O     1 
ATOM   4486 C  CB    . HIS A 1 711 ? 114.034 92.394  89.024  1.00 43.75  ? 2502 HIS A CB    1 
ATOM   4487 C  CG    . HIS A 1 711 ? 115.185 92.253  89.968  1.00 48.04  ? 2502 HIS A CG    1 
ATOM   4488 N  ND1   . HIS A 1 711 ? 115.075 92.506  91.318  1.00 45.87  ? 2502 HIS A ND1   1 
ATOM   4489 C  CD2   . HIS A 1 711 ? 116.472 91.889  89.757  1.00 55.97  ? 2502 HIS A CD2   1 
ATOM   4490 C  CE1   . HIS A 1 711 ? 116.244 92.302  91.898  1.00 52.66  ? 2502 HIS A CE1   1 
ATOM   4491 N  NE2   . HIS A 1 711 ? 117.108 91.926  90.973  1.00 64.39  ? 2502 HIS A NE2   1 
ATOM   4492 N  N     . GLY A 1 712 ? 112.436 94.443  87.015  1.00 43.48  ? 2503 GLY A N     1 
ATOM   4493 C  CA    . GLY A 1 712 ? 111.336 94.726  86.109  1.00 47.35  ? 2503 GLY A CA    1 
ATOM   4494 C  C     . GLY A 1 712 ? 111.799 94.867  84.673  1.00 49.66  ? 2503 GLY A C     1 
ATOM   4495 O  O     . GLY A 1 712 ? 111.163 94.352  83.750  1.00 54.73  ? 2503 GLY A O     1 
ATOM   4496 N  N     . HIS A 1 713 ? 112.918 95.562  84.463  1.00 39.89  ? 2504 HIS A N     1 
ATOM   4497 C  CA    . HIS A 1 713 ? 113.490 95.641  83.125  1.00 43.76  ? 2504 HIS A CA    1 
ATOM   4498 C  C     . HIS A 1 713 ? 113.985 94.282  82.651  1.00 53.58  ? 2504 HIS A C     1 
ATOM   4499 O  O     . HIS A 1 713 ? 113.925 93.986  81.452  1.00 69.66  ? 2504 HIS A O     1 
ATOM   4500 C  CB    . HIS A 1 713 ? 114.623 96.664  83.099  1.00 43.70  ? 2504 HIS A CB    1 
ATOM   4501 C  CG    . HIS A 1 713 ? 114.170 98.073  83.323  1.00 44.79  ? 2504 HIS A CG    1 
ATOM   4502 N  ND1   . HIS A 1 713 ? 113.806 98.549  84.564  1.00 46.10  ? 2504 HIS A ND1   1 
ATOM   4503 C  CD2   . HIS A 1 713 ? 114.020 99.108  82.464  1.00 43.49  ? 2504 HIS A CD2   1 
ATOM   4504 C  CE1   . HIS A 1 713 ? 113.454 99.818  84.460  1.00 43.09  ? 2504 HIS A CE1   1 
ATOM   4505 N  NE2   . HIS A 1 713 ? 113.573 100.181 83.196  1.00 37.73  ? 2504 HIS A NE2   1 
ATOM   4506 N  N     . ARG A 1 714 ? 114.479 93.448  83.569  1.00 52.51  ? 2505 ARG A N     1 
ATOM   4507 C  CA    . ARG A 1 714 ? 114.895 92.099  83.199  1.00 57.85  ? 2505 ARG A CA    1 
ATOM   4508 C  C     . ARG A 1 714 ? 113.714 91.276  82.703  1.00 61.84  ? 2505 ARG A C     1 
ATOM   4509 O  O     . ARG A 1 714 ? 113.833 90.532  81.723  1.00 68.76  ? 2505 ARG A O     1 
ATOM   4510 C  CB    . ARG A 1 714 ? 115.563 91.410  84.389  1.00 61.70  ? 2505 ARG A CB    1 
ATOM   4511 C  CG    . ARG A 1 714 ? 117.054 91.665  84.499  1.00 63.80  ? 2505 ARG A CG    1 
ATOM   4512 C  CD    . ARG A 1 714 ? 117.647 90.981  85.721  1.00 67.18  ? 2505 ARG A CD    1 
ATOM   4513 N  NE    . ARG A 1 714 ? 117.028 89.688  85.981  1.00 75.58  ? 2505 ARG A NE    1 
ATOM   4514 C  CZ    . ARG A 1 714 ? 117.320 88.571  85.329  1.00 83.22  ? 2505 ARG A CZ    1 
ATOM   4515 N  NH1   . ARG A 1 714 ? 118.229 88.549  84.368  1.00 90.87  ? 2505 ARG A NH1   1 
ATOM   4516 N  NH2   . ARG A 1 714 ? 116.686 87.447  85.651  1.00 79.19  ? 2505 ARG A NH2   1 
ATOM   4517 N  N     . GLU A 1 715 ? 112.566 91.396  83.364  1.00 59.43  ? 2506 GLU A N     1 
ATOM   4518 C  CA    . GLU A 1 715 ? 111.368 90.670  82.965  1.00 62.88  ? 2506 GLU A CA    1 
ATOM   4519 C  C     . GLU A 1 715 ? 110.557 91.403  81.906  1.00 70.63  ? 2506 GLU A C     1 
ATOM   4520 O  O     . GLU A 1 715 ? 109.507 90.899  81.493  1.00 74.66  ? 2506 GLU A O     1 
ATOM   4521 C  CB    . GLU A 1 715 ? 110.487 90.381  84.186  1.00 62.42  ? 2506 GLU A CB    1 
ATOM   4522 C  CG    . GLU A 1 715 ? 109.932 91.604  84.885  1.00 61.45  ? 2506 GLU A CG    1 
ATOM   4523 C  CD    . GLU A 1 715 ? 109.535 91.314  86.320  1.00 58.58  ? 2506 GLU A CD    1 
ATOM   4524 O  OE1   . GLU A 1 715 ? 110.427 91.298  87.194  1.00 44.36  ? 2506 GLU A OE1   1 
ATOM   4525 O  OE2   . GLU A 1 715 ? 108.332 91.094  86.572  1.00 58.34  ? 2506 GLU A OE2   1 
ATOM   4526 N  N     . GLY A 1 716 ? 111.012 92.576  81.462  1.00 68.18  ? 2507 GLY A N     1 
ATOM   4527 C  CA    . GLY A 1 716 ? 110.323 93.286  80.399  1.00 69.71  ? 2507 GLY A CA    1 
ATOM   4528 C  C     . GLY A 1 716 ? 110.343 92.574  79.063  1.00 81.36  ? 2507 GLY A C     1 
ATOM   4529 O  O     . GLY A 1 716 ? 109.540 92.906  78.185  1.00 82.28  ? 2507 GLY A O     1 
ATOM   4530 N  N     . MET A 1 717 ? 111.239 91.608  78.888  1.00 81.72  ? 2508 MET A N     1 
ATOM   4531 C  CA    . MET A 1 717 ? 111.306 90.839  77.651  1.00 88.61  ? 2508 MET A CA    1 
ATOM   4532 C  C     . MET A 1 717 ? 110.111 89.900  77.523  1.00 87.40  ? 2508 MET A C     1 
ATOM   4533 O  O     . MET A 1 717 ? 110.181 88.736  77.917  1.00 78.62  ? 2508 MET A O     1 
ATOM   4534 C  CB    . MET A 1 717 ? 112.608 90.041  77.585  1.00 75.72  ? 2508 MET A CB    1 
ATOM   4535 C  CG    . MET A 1 717 ? 113.858 90.893  77.664  1.00 70.79  ? 2508 MET A CG    1 
ATOM   4536 S  SD    . MET A 1 717 ? 115.193 90.072  78.550  1.00 75.88  ? 2508 MET A SD    1 
ATOM   4537 C  CE    . MET A 1 717 ? 116.378 91.406  78.657  1.00 70.05  ? 2508 MET A CE    1 
ATOM   4538 N  N     . PHE A 1 735 ? 125.427 89.977  81.658  1.00 91.67  ? 2526 PHE A N     1 
ATOM   4539 C  CA    . PHE A 1 735 ? 124.182 89.708  80.948  1.00 108.61 ? 2526 PHE A CA    1 
ATOM   4540 C  C     . PHE A 1 735 ? 123.262 88.815  81.775  1.00 112.75 ? 2526 PHE A C     1 
ATOM   4541 O  O     . PHE A 1 735 ? 122.465 89.302  82.577  1.00 111.88 ? 2526 PHE A O     1 
ATOM   4542 C  CB    . PHE A 1 735 ? 124.467 89.058  79.593  1.00 108.59 ? 2526 PHE A CB    1 
ATOM   4543 C  CG    . PHE A 1 735 ? 123.384 89.278  78.576  1.00 105.66 ? 2526 PHE A CG    1 
ATOM   4544 C  CD1   . PHE A 1 735 ? 122.274 88.451  78.536  1.00 102.92 ? 2526 PHE A CD1   1 
ATOM   4545 C  CD2   . PHE A 1 735 ? 123.476 90.313  77.660  1.00 106.96 ? 2526 PHE A CD2   1 
ATOM   4546 C  CE1   . PHE A 1 735 ? 121.276 88.651  77.602  1.00 106.55 ? 2526 PHE A CE1   1 
ATOM   4547 C  CE2   . PHE A 1 735 ? 122.481 90.518  76.723  1.00 109.02 ? 2526 PHE A CE2   1 
ATOM   4548 C  CZ    . PHE A 1 735 ? 121.379 89.686  76.694  1.00 109.67 ? 2526 PHE A CZ    1 
ATOM   4549 N  N     . CYS A 1 736 ? 123.377 87.504  81.564  1.00 112.56 ? 2527 CYS A N     1 
ATOM   4550 C  CA    . CYS A 1 736 ? 122.559 86.554  82.316  1.00 109.35 ? 2527 CYS A CA    1 
ATOM   4551 C  C     . CYS A 1 736 ? 122.788 86.628  83.822  1.00 107.78 ? 2527 CYS A C     1 
ATOM   4552 O  O     . CYS A 1 736 ? 121.795 86.607  84.571  1.00 105.53 ? 2527 CYS A O     1 
ATOM   4553 C  CB    . CYS A 1 736 ? 122.793 85.136  81.782  1.00 108.15 ? 2527 CYS A CB    1 
ATOM   4554 S  SG    . CYS A 1 736 ? 121.710 83.882  82.505  1.00 92.32  ? 2527 CYS A SG    1 
ATOM   4555 N  N     . PRO A 1 737 ? 124.021 86.690  84.337  1.00 107.94 ? 2528 PRO A N     1 
ATOM   4556 C  CA    . PRO A 1 737 ? 124.189 86.839  85.788  1.00 103.14 ? 2528 PRO A CA    1 
ATOM   4557 C  C     . PRO A 1 737 ? 123.569 88.135  86.291  1.00 97.25  ? 2528 PRO A C     1 
ATOM   4558 O  O     . PRO A 1 737 ? 123.617 89.170  85.624  1.00 93.21  ? 2528 PRO A O     1 
ATOM   4559 C  CB    . PRO A 1 737 ? 125.710 86.834  85.975  1.00 100.17 ? 2528 PRO A CB    1 
ATOM   4560 C  CG    . PRO A 1 737 ? 126.234 86.130  84.783  1.00 101.05 ? 2528 PRO A CG    1 
ATOM   4561 C  CD    . PRO A 1 737 ? 125.323 86.522  83.665  1.00 103.52 ? 2528 PRO A CD    1 
ATOM   4562 N  N     . ILE A 1 738 ? 122.984 88.066  87.481  1.00 94.23  ? 2529 ILE A N     1 
ATOM   4563 C  CA    . ILE A 1 738 ? 122.357 89.231  88.093  1.00 84.92  ? 2529 ILE A CA    1 
ATOM   4564 C  C     . ILE A 1 738 ? 123.444 90.134  88.657  1.00 79.73  ? 2529 ILE A C     1 
ATOM   4565 O  O     . ILE A 1 738 ? 124.300 89.688  89.431  1.00 77.31  ? 2529 ILE A O     1 
ATOM   4566 C  CB    . ILE A 1 738 ? 121.363 88.808  89.187  1.00 78.55  ? 2529 ILE A CB    1 
ATOM   4567 C  CG1   . ILE A 1 738 ? 120.596 87.550  88.769  1.00 79.76  ? 2529 ILE A CG1   1 
ATOM   4568 C  CG2   . ILE A 1 738 ? 120.399 89.942  89.495  1.00 69.27  ? 2529 ILE A CG2   1 
ATOM   4569 C  CD1   . ILE A 1 738 ? 121.129 86.265  89.380  1.00 71.09  ? 2529 ILE A CD1   1 
ATOM   4570 N  N     . ARG A 1 739 ? 123.415 91.406  88.271  1.00 73.79  ? 2530 ARG A N     1 
ATOM   4571 C  CA    . ARG A 1 739 ? 124.438 92.354  88.703  1.00 77.28  ? 2530 ARG A CA    1 
ATOM   4572 C  C     . ARG A 1 739 ? 123.849 93.753  88.654  1.00 71.09  ? 2530 ARG A C     1 
ATOM   4573 O  O     . ARG A 1 739 ? 123.339 94.170  87.609  1.00 75.77  ? 2530 ARG A O     1 
ATOM   4574 C  CB    . ARG A 1 739 ? 125.679 92.254  87.816  1.00 77.91  ? 2530 ARG A CB    1 
ATOM   4575 C  CG    . ARG A 1 739 ? 126.856 93.091  88.284  1.00 74.72  ? 2530 ARG A CG    1 
ATOM   4576 C  CD    . ARG A 1 739 ? 128.172 92.395  87.981  1.00 91.60  ? 2530 ARG A CD    1 
ATOM   4577 N  NE    . ARG A 1 739 ? 129.308 93.303  88.079  1.00 99.34  ? 2530 ARG A NE    1 
ATOM   4578 C  CZ    . ARG A 1 739 ? 130.475 93.110  87.479  1.00 97.79  ? 2530 ARG A CZ    1 
ATOM   4579 N  NH1   . ARG A 1 739 ? 130.698 92.044  86.728  1.00 98.17  ? 2530 ARG A NH1   1 
ATOM   4580 N  NH2   . ARG A 1 739 ? 131.443 94.008  87.639  1.00 93.42  ? 2530 ARG A NH2   1 
ATOM   4581 N  N     . GLY A 1 740 ? 123.913 94.471  89.767  1.00 58.56  ? 2531 GLY A N     1 
ATOM   4582 C  CA    . GLY A 1 740 ? 123.405 95.826  89.801  1.00 46.18  ? 2531 GLY A CA    1 
ATOM   4583 C  C     . GLY A 1 740 ? 123.273 96.324  91.223  1.00 48.40  ? 2531 GLY A C     1 
ATOM   4584 O  O     . GLY A 1 740 ? 123.657 95.655  92.187  1.00 56.00  ? 2531 GLY A O     1 
ATOM   4585 N  N     . GLY A 1 741 ? 122.718 97.527  91.329  1.00 49.28  ? 2532 GLY A N     1 
ATOM   4586 C  CA    . GLY A 1 741 ? 122.495 98.175  92.606  1.00 47.09  ? 2532 GLY A CA    1 
ATOM   4587 C  C     . GLY A 1 741 ? 121.029 98.438  92.879  1.00 50.32  ? 2532 GLY A C     1 
ATOM   4588 O  O     . GLY A 1 741 ? 120.666 99.535  93.309  1.00 53.00  ? 2532 GLY A O     1 
ATOM   4589 N  N     . PHE A 1 742 ? 120.179 97.448  92.609  1.00 41.47  ? 2533 PHE A N     1 
ATOM   4590 C  CA    . PHE A 1 742 ? 118.735 97.642  92.680  1.00 29.73  ? 2533 PHE A CA    1 
ATOM   4591 C  C     . PHE A 1 742 ? 118.301 98.127  94.059  1.00 32.28  ? 2533 PHE A C     1 
ATOM   4592 O  O     . PHE A 1 742 ? 118.770 97.636  95.087  1.00 41.07  ? 2533 PHE A O     1 
ATOM   4593 C  CB    . PHE A 1 742 ? 118.014 96.340  92.337  1.00 31.89  ? 2533 PHE A CB    1 
ATOM   4594 C  CG    . PHE A 1 742 ? 118.782 95.450  91.406  1.00 38.45  ? 2533 PHE A CG    1 
ATOM   4595 C  CD1   . PHE A 1 742 ? 119.015 95.830  90.097  1.00 42.63  ? 2533 PHE A CD1   1 
ATOM   4596 C  CD2   . PHE A 1 742 ? 119.270 94.230  91.840  1.00 40.37  ? 2533 PHE A CD2   1 
ATOM   4597 C  CE1   . PHE A 1 742 ? 119.720 95.011  89.238  1.00 47.22  ? 2533 PHE A CE1   1 
ATOM   4598 C  CE2   . PHE A 1 742 ? 119.975 93.408  90.986  1.00 47.01  ? 2533 PHE A CE2   1 
ATOM   4599 C  CZ    . PHE A 1 742 ? 120.201 93.799  89.684  1.00 44.84  ? 2533 PHE A CZ    1 
ATOM   4600 N  N     . PHE A 1 743 ? 117.392 99.097  94.067  1.00 23.97  ? 2534 PHE A N     1 
ATOM   4601 C  CA    . PHE A 1 743 ? 116.874 99.709  95.284  1.00 19.22  ? 2534 PHE A CA    1 
ATOM   4602 C  C     . PHE A 1 743 ? 115.541 99.051  95.616  1.00 19.99  ? 2534 PHE A C     1 
ATOM   4603 O  O     . PHE A 1 743 ? 114.619 99.074  94.795  1.00 21.60  ? 2534 PHE A O     1 
ATOM   4604 C  CB    . PHE A 1 743 ? 116.724 101.218 95.079  1.00 13.30  ? 2534 PHE A CB    1 
ATOM   4605 C  CG    . PHE A 1 743 ? 115.808 101.894 96.057  1.00 10.70  ? 2534 PHE A CG    1 
ATOM   4606 C  CD1   . PHE A 1 743 ? 115.992 101.760 97.418  1.00 14.97  ? 2534 PHE A CD1   1 
ATOM   4607 C  CD2   . PHE A 1 743 ? 114.782 102.702 95.606  1.00 11.22  ? 2534 PHE A CD2   1 
ATOM   4608 C  CE1   . PHE A 1 743 ? 115.155 102.399 98.307  1.00 11.63  ? 2534 PHE A CE1   1 
ATOM   4609 C  CE2   . PHE A 1 743 ? 113.944 103.342 96.492  1.00 9.98   ? 2534 PHE A CE2   1 
ATOM   4610 C  CZ    . PHE A 1 743 ? 114.131 103.190 97.843  1.00 8.87   ? 2534 PHE A CZ    1 
ATOM   4611 N  N     . ILE A 1 744 ? 115.438 98.458  96.804  1.00 17.84  ? 2535 ILE A N     1 
ATOM   4612 C  CA    . ILE A 1 744 ? 114.317 97.580  97.110  1.00 18.74  ? 2535 ILE A CA    1 
ATOM   4613 C  C     . ILE A 1 744 ? 113.464 98.051  98.281  1.00 21.22  ? 2535 ILE A C     1 
ATOM   4614 O  O     . ILE A 1 744 ? 112.311 97.606  98.396  1.00 33.62  ? 2535 ILE A O     1 
ATOM   4615 C  CB    . ILE A 1 744 ? 114.799 96.137  97.360  1.00 14.82  ? 2535 ILE A CB    1 
ATOM   4616 C  CG1   . ILE A 1 744 ? 115.681 96.078  98.605  1.00 15.88  ? 2535 ILE A CG1   1 
ATOM   4617 C  CG2   . ILE A 1 744 ? 115.545 95.610  96.152  1.00 22.50  ? 2535 ILE A CG2   1 
ATOM   4618 C  CD1   . ILE A 1 744 ? 116.290 94.721  98.849  1.00 22.38  ? 2535 ILE A CD1   1 
ATOM   4619 N  N     . LEU A 1 745 ? 113.955 98.924  99.157  1.00 14.76  ? 2536 LEU A N     1 
ATOM   4620 C  CA    . LEU A 1 745 ? 113.170 99.287  100.328 1.00 13.06  ? 2536 LEU A CA    1 
ATOM   4621 C  C     . LEU A 1 745 ? 113.674 100.598 100.911 1.00 17.15  ? 2536 LEU A C     1 
ATOM   4622 O  O     . LEU A 1 745 ? 114.877 100.859 100.915 1.00 20.42  ? 2536 LEU A O     1 
ATOM   4623 C  CB    . LEU A 1 745 ? 113.231 98.186  101.391 1.00 11.63  ? 2536 LEU A CB    1 
ATOM   4624 C  CG    . LEU A 1 745 ? 112.405 98.398  102.657 1.00 12.30  ? 2536 LEU A CG    1 
ATOM   4625 C  CD1   . LEU A 1 745 ? 110.950 98.641  102.308 1.00 14.51  ? 2536 LEU A CD1   1 
ATOM   4626 C  CD2   . LEU A 1 745 ? 112.552 97.208  103.584 1.00 20.61  ? 2536 LEU A CD2   1 
ATOM   4627 N  N     . GLN A 1 746 ? 112.744 101.409 101.409 1.00 16.89  ? 2537 GLN A N     1 
ATOM   4628 C  CA    . GLN A 1 746 ? 113.057 102.619 102.156 1.00 15.68  ? 2537 GLN A CA    1 
ATOM   4629 C  C     . GLN A 1 746 ? 112.394 102.532 103.522 1.00 15.48  ? 2537 GLN A C     1 
ATOM   4630 O  O     . GLN A 1 746 ? 111.222 102.155 103.621 1.00 17.56  ? 2537 GLN A O     1 
ATOM   4631 C  CB    . GLN A 1 746 ? 112.584 103.872 101.416 1.00 10.89  ? 2537 GLN A CB    1 
ATOM   4632 C  CG    . GLN A 1 746 ? 112.250 105.033 102.333 1.00 11.71  ? 2537 GLN A CG    1 
ATOM   4633 C  CD    . GLN A 1 746 ? 112.442 106.375 101.668 1.00 15.33  ? 2537 GLN A CD    1 
ATOM   4634 O  OE1   . GLN A 1 746 ? 112.885 106.456 100.524 1.00 19.64  ? 2537 GLN A OE1   1 
ATOM   4635 N  NE2   . GLN A 1 746 ? 112.110 107.442 102.384 1.00 17.09  ? 2537 GLN A NE2   1 
ATOM   4636 N  N     . LEU A 1 747 ? 113.142 102.877 104.570 1.00 16.48  ? 2538 LEU A N     1 
ATOM   4637 C  CA    . LEU A 1 747 ? 112.655 102.791 105.942 1.00 20.55  ? 2538 LEU A CA    1 
ATOM   4638 C  C     . LEU A 1 747 ? 112.609 104.158 106.614 1.00 22.95  ? 2538 LEU A C     1 
ATOM   4639 O  O     . LEU A 1 747 ? 112.855 104.270 107.815 1.00 23.33  ? 2538 LEU A O     1 
ATOM   4640 C  CB    . LEU A 1 747 ? 113.515 101.828 106.755 1.00 17.15  ? 2538 LEU A CB    1 
ATOM   4641 C  CG    . LEU A 1 747 ? 113.245 100.352 106.489 1.00 17.40  ? 2538 LEU A CG    1 
ATOM   4642 C  CD1   . LEU A 1 747 ? 114.554 99.629  106.280 1.00 19.93  ? 2538 LEU A CD1   1 
ATOM   4643 C  CD2   . LEU A 1 747 ? 112.466 99.742  107.639 1.00 18.95  ? 2538 LEU A CD2   1 
ATOM   4644 N  N     . HIS A 1 748 ? 112.339 105.204 105.833 1.00 19.07  ? 2539 HIS A N     1 
ATOM   4645 C  CA    . HIS A 1 748 ? 112.136 106.570 106.308 1.00 20.55  ? 2539 HIS A CA    1 
ATOM   4646 C  C     . HIS A 1 748 ? 113.438 107.215 106.767 1.00 26.73  ? 2539 HIS A C     1 
ATOM   4647 O  O     . HIS A 1 748 ? 113.485 108.426 107.007 1.00 35.02  ? 2539 HIS A O     1 
ATOM   4648 C  CB    . HIS A 1 748 ? 111.125 106.609 107.458 1.00 26.64  ? 2539 HIS A CB    1 
ATOM   4649 C  CG    . HIS A 1 748 ? 109.815 105.956 107.147 1.00 34.34  ? 2539 HIS A CG    1 
ATOM   4650 N  ND1   . HIS A 1 748 ? 108.873 105.690 108.117 1.00 36.96  ? 2539 HIS A ND1   1 
ATOM   4651 C  CD2   . HIS A 1 748 ? 109.280 105.532 105.978 1.00 29.33  ? 2539 HIS A CD2   1 
ATOM   4652 C  CE1   . HIS A 1 748 ? 107.819 105.122 107.561 1.00 32.36  ? 2539 HIS A CE1   1 
ATOM   4653 N  NE2   . HIS A 1 748 ? 108.039 105.017 106.263 1.00 28.77  ? 2539 HIS A NE2   1 
ATOM   4654 N  N     . ASP A 1 749 ? 114.490 106.423 106.900 1.00 23.92  ? 2540 ASP A N     1 
ATOM   4655 C  CA    . ASP A 1 749 ? 115.804 106.968 107.211 1.00 22.10  ? 2540 ASP A CA    1 
ATOM   4656 C  C     . ASP A 1 749 ? 116.937 106.208 106.542 1.00 20.56  ? 2540 ASP A C     1 
ATOM   4657 O  O     . ASP A 1 749 ? 118.098 106.547 106.780 1.00 28.17  ? 2540 ASP A O     1 
ATOM   4658 C  CB    . ASP A 1 749 ? 116.021 106.988 108.730 1.00 30.99  ? 2540 ASP A CB    1 
ATOM   4659 C  CG    . ASP A 1 749 ? 116.472 108.339 109.229 1.00 41.17  ? 2540 ASP A CG    1 
ATOM   4660 O  OD1   . ASP A 1 749 ? 116.854 109.178 108.390 1.00 49.64  ? 2540 ASP A OD1   1 
ATOM   4661 O  OD2   . ASP A 1 749 ? 116.445 108.564 110.456 1.00 44.01  ? 2540 ASP A OD2   1 
ATOM   4662 N  N     . GLU A 1 750 ? 116.650 105.202 105.724 1.00 16.17  ? 2541 GLU A N     1 
ATOM   4663 C  CA    . GLU A 1 750 ? 117.689 104.335 105.194 1.00 17.62  ? 2541 GLU A CA    1 
ATOM   4664 C  C     . GLU A 1 750 ? 117.171 103.666 103.934 1.00 15.61  ? 2541 GLU A C     1 
ATOM   4665 O  O     . GLU A 1 750 ? 115.967 103.638 103.672 1.00 23.49  ? 2541 GLU A O     1 
ATOM   4666 C  CB    . GLU A 1 750 ? 118.122 103.292 106.228 1.00 25.59  ? 2541 GLU A CB    1 
ATOM   4667 C  CG    . GLU A 1 750 ? 117.318 102.006 106.206 1.00 28.20  ? 2541 GLU A CG    1 
ATOM   4668 C  CD    . GLU A 1 750 ? 117.911 100.941 107.107 1.00 40.25  ? 2541 GLU A CD    1 
ATOM   4669 O  OE1   . GLU A 1 750 ? 119.114 100.640 106.960 1.00 45.37  ? 2541 GLU A OE1   1 
ATOM   4670 O  OE2   . GLU A 1 750 ? 117.179 100.409 107.967 1.00 34.61  ? 2541 GLU A OE2   1 
ATOM   4671 N  N     . LEU A 1 751 ? 118.101 103.125 103.158 1.00 14.49  ? 2542 LEU A N     1 
ATOM   4672 C  CA    . LEU A 1 751 ? 117.788 102.494 101.888 1.00 11.25  ? 2542 LEU A CA    1 
ATOM   4673 C  C     . LEU A 1 751 ? 118.363 101.089 101.862 1.00 17.74  ? 2542 LEU A C     1 
ATOM   4674 O  O     . LEU A 1 751 ? 119.486 100.861 102.318 1.00 32.69  ? 2542 LEU A O     1 
ATOM   4675 C  CB    . LEU A 1 751 ? 118.349 103.297 100.719 1.00 8.18   ? 2542 LEU A CB    1 
ATOM   4676 C  CG    . LEU A 1 751 ? 117.918 104.753 100.582 1.00 10.61  ? 2542 LEU A CG    1 
ATOM   4677 C  CD1   . LEU A 1 751 ? 118.890 105.667 101.289 1.00 14.35  ? 2542 LEU A CD1   1 
ATOM   4678 C  CD2   . LEU A 1 751 ? 117.842 105.104 99.120  1.00 18.36  ? 2542 LEU A CD2   1 
ATOM   4679 N  N     . LEU A 1 752 ? 117.593 100.152 101.324 1.00 13.77  ? 2543 LEU A N     1 
ATOM   4680 C  CA    . LEU A 1 752 ? 118.037 98.781  101.137 1.00 15.13  ? 2543 LEU A CA    1 
ATOM   4681 C  C     . LEU A 1 752 ? 118.342 98.559  99.664  1.00 17.38  ? 2543 LEU A C     1 
ATOM   4682 O  O     . LEU A 1 752 ? 117.526 98.894  98.799  1.00 26.87  ? 2543 LEU A O     1 
ATOM   4683 C  CB    . LEU A 1 752 ? 116.981 97.787  101.618 1.00 16.16  ? 2543 LEU A CB    1 
ATOM   4684 C  CG    . LEU A 1 752 ? 117.234 97.155  102.985 1.00 19.10  ? 2543 LEU A CG    1 
ATOM   4685 C  CD1   . LEU A 1 752 ? 117.080 98.193  104.078 1.00 19.91  ? 2543 LEU A CD1   1 
ATOM   4686 C  CD2   . LEU A 1 752 ? 116.295 95.986  103.213 1.00 22.38  ? 2543 LEU A CD2   1 
ATOM   4687 N  N     . TYR A 1 753 ? 119.515 98.005  99.382  1.00 15.35  ? 2544 TYR A N     1 
ATOM   4688 C  CA    . TYR A 1 753 ? 119.951 97.752  98.017  1.00 20.29  ? 2544 TYR A CA    1 
ATOM   4689 C  C     . TYR A 1 753 ? 120.308 96.282  97.877  1.00 26.55  ? 2544 TYR A C     1 
ATOM   4690 O  O     . TYR A 1 753 ? 121.168 95.776  98.605  1.00 29.61  ? 2544 TYR A O     1 
ATOM   4691 C  CB    . TYR A 1 753 ? 121.140 98.638  97.650  1.00 24.82  ? 2544 TYR A CB    1 
ATOM   4692 C  CG    . TYR A 1 753 ? 120.761 100.078 97.415  1.00 19.38  ? 2544 TYR A CG    1 
ATOM   4693 C  CD1   . TYR A 1 753 ? 120.351 100.510 96.165  1.00 18.34  ? 2544 TYR A CD1   1 
ATOM   4694 C  CD2   . TYR A 1 753 ? 120.810 101.005 98.443  1.00 17.58  ? 2544 TYR A CD2   1 
ATOM   4695 C  CE1   . TYR A 1 753 ? 120.005 101.823 95.943  1.00 20.43  ? 2544 TYR A CE1   1 
ATOM   4696 C  CE2   . TYR A 1 753 ? 120.466 102.321 98.229  1.00 17.15  ? 2544 TYR A CE2   1 
ATOM   4697 C  CZ    . TYR A 1 753 ? 120.060 102.723 96.978  1.00 17.67  ? 2544 TYR A CZ    1 
ATOM   4698 O  OH    . TYR A 1 753 ? 119.715 104.033 96.759  1.00 19.32  ? 2544 TYR A OH    1 
ATOM   4699 N  N     . GLU A 1 754 ? 119.655 95.603  96.936  1.00 31.79  ? 2545 GLU A N     1 
ATOM   4700 C  CA    . GLU A 1 754 ? 119.892 94.183  96.686  1.00 34.60  ? 2545 GLU A CA    1 
ATOM   4701 C  C     . GLU A 1 754 ? 121.089 94.002  95.750  1.00 35.84  ? 2545 GLU A C     1 
ATOM   4702 O  O     . GLU A 1 754 ? 120.980 93.509  94.628  1.00 43.53  ? 2545 GLU A O     1 
ATOM   4703 C  CB    . GLU A 1 754 ? 118.636 93.544  96.112  1.00 27.34  ? 2545 GLU A CB    1 
ATOM   4704 C  CG    . GLU A 1 754 ? 118.515 92.067  96.385  1.00 30.92  ? 2545 GLU A CG    1 
ATOM   4705 C  CD    . GLU A 1 754 ? 117.271 91.475  95.769  1.00 38.58  ? 2545 GLU A CD    1 
ATOM   4706 O  OE1   . GLU A 1 754 ? 116.662 92.145  94.912  1.00 43.91  ? 2545 GLU A OE1   1 
ATOM   4707 O  OE2   . GLU A 1 754 ? 116.906 90.340  96.135  1.00 47.21  ? 2545 GLU A OE2   1 
ATOM   4708 N  N     . VAL A 1 755 ? 122.256 94.412  96.246  1.00 25.74  ? 2546 VAL A N     1 
ATOM   4709 C  CA    . VAL A 1 755 ? 123.463 94.405  95.432  1.00 29.64  ? 2546 VAL A CA    1 
ATOM   4710 C  C     . VAL A 1 755 ? 123.923 92.975  95.189  1.00 40.12  ? 2546 VAL A C     1 
ATOM   4711 O  O     . VAL A 1 755 ? 123.785 92.100  96.055  1.00 48.30  ? 2546 VAL A O     1 
ATOM   4712 C  CB    . VAL A 1 755 ? 124.565 95.236  96.108  1.00 35.75  ? 2546 VAL A CB    1 
ATOM   4713 C  CG1   . VAL A 1 755 ? 125.613 95.635  95.094  1.00 47.92  ? 2546 VAL A CG1   1 
ATOM   4714 C  CG2   . VAL A 1 755 ? 123.965 96.462  96.766  1.00 30.28  ? 2546 VAL A CG2   1 
ATOM   4715 N  N     . ALA A 1 756 ? 124.475 92.733  94.003  1.00 37.94  ? 2547 ALA A N     1 
ATOM   4716 C  CA    . ALA A 1 756 ? 124.970 91.411  93.655  1.00 48.73  ? 2547 ALA A CA    1 
ATOM   4717 C  C     . ALA A 1 756 ? 126.234 91.084  94.445  1.00 62.35  ? 2547 ALA A C     1 
ATOM   4718 O  O     . ALA A 1 756 ? 126.906 91.963  94.990  1.00 54.66  ? 2547 ALA A O     1 
ATOM   4719 C  CB    . ALA A 1 756 ? 125.249 91.321  92.156  1.00 47.88  ? 2547 ALA A CB    1 
ATOM   4720 N  N     . GLU A 1 757 ? 126.556 89.789  94.494  1.00 67.52  ? 2548 GLU A N     1 
ATOM   4721 C  CA    . GLU A 1 757 ? 127.686 89.313  95.282  1.00 65.32  ? 2548 GLU A CA    1 
ATOM   4722 C  C     . GLU A 1 757 ? 129.034 89.744  94.720  1.00 68.84  ? 2548 GLU A C     1 
ATOM   4723 O  O     . GLU A 1 757 ? 130.048 89.582  95.406  1.00 68.05  ? 2548 GLU A O     1 
ATOM   4724 C  CB    . GLU A 1 757 ? 127.646 87.788  95.395  1.00 64.98  ? 2548 GLU A CB    1 
ATOM   4725 C  CG    . GLU A 1 757 ? 128.125 87.059  94.151  1.00 73.22  ? 2548 GLU A CG    1 
ATOM   4726 C  CD    . GLU A 1 757 ? 128.685 85.684  94.462  1.00 82.49  ? 2548 GLU A CD    1 
ATOM   4727 O  OE1   . GLU A 1 757 ? 128.922 85.393  95.653  1.00 92.05  ? 2548 GLU A OE1   1 
ATOM   4728 O  OE2   . GLU A 1 757 ? 128.887 84.895  93.515  1.00 78.26  ? 2548 GLU A OE2   1 
ATOM   4729 N  N     . GLU A 1 758 ? 129.076 90.279  93.501  1.00 71.49  ? 2549 GLU A N     1 
ATOM   4730 C  CA    . GLU A 1 758 ? 130.335 90.728  92.921  1.00 73.10  ? 2549 GLU A CA    1 
ATOM   4731 C  C     . GLU A 1 758 ? 130.585 92.214  93.135  1.00 72.24  ? 2549 GLU A C     1 
ATOM   4732 O  O     . GLU A 1 758 ? 131.744 92.631  93.240  1.00 74.98  ? 2549 GLU A O     1 
ATOM   4733 C  CB    . GLU A 1 758 ? 130.369 90.415  91.423  1.00 76.07  ? 2549 GLU A CB    1 
ATOM   4734 C  CG    . GLU A 1 758 ? 131.752 90.067  90.893  1.00 82.39  ? 2549 GLU A CG    1 
ATOM   4735 C  CD    . GLU A 1 758 ? 132.608 91.293  90.642  1.00 88.85  ? 2549 GLU A CD    1 
ATOM   4736 O  OE1   . GLU A 1 758 ? 132.224 92.126  89.796  1.00 85.61  ? 2549 GLU A OE1   1 
ATOM   4737 O  OE2   . GLU A 1 758 ? 133.666 91.424  91.293  1.00 91.03  ? 2549 GLU A OE2   1 
ATOM   4738 N  N     . ASP A 1 759 ? 129.527 93.022  93.209  1.00 66.12  ? 2550 ASP A N     1 
ATOM   4739 C  CA    . ASP A 1 759 ? 129.646 94.465  93.371  1.00 63.15  ? 2550 ASP A CA    1 
ATOM   4740 C  C     . ASP A 1 759 ? 129.294 94.911  94.787  1.00 60.50  ? 2550 ASP A C     1 
ATOM   4741 O  O     . ASP A 1 759 ? 128.791 96.019  94.986  1.00 56.45  ? 2550 ASP A O     1 
ATOM   4742 C  CB    . ASP A 1 759 ? 128.765 95.190  92.355  1.00 63.08  ? 2550 ASP A CB    1 
ATOM   4743 C  CG    . ASP A 1 759 ? 129.199 94.942  90.924  1.00 70.54  ? 2550 ASP A CG    1 
ATOM   4744 O  OD1   . ASP A 1 759 ? 130.255 94.308  90.720  1.00 75.31  ? 2550 ASP A OD1   1 
ATOM   4745 O  OD2   . ASP A 1 759 ? 128.482 95.382  90.001  1.00 70.02  ? 2550 ASP A OD2   1 
ATOM   4746 N  N     . VAL A 1 760 ? 129.556 94.058  95.780  1.00 61.99  ? 2551 VAL A N     1 
ATOM   4747 C  CA    . VAL A 1 760 ? 129.171 94.370  97.155  1.00 60.78  ? 2551 VAL A CA    1 
ATOM   4748 C  C     . VAL A 1 760 ? 129.910 95.605  97.653  1.00 67.40  ? 2551 VAL A C     1 
ATOM   4749 O  O     . VAL A 1 760 ? 129.312 96.510  98.245  1.00 70.68  ? 2551 VAL A O     1 
ATOM   4750 C  CB    . VAL A 1 760 ? 129.427 93.163  98.075  1.00 62.54  ? 2551 VAL A CB    1 
ATOM   4751 C  CG1   . VAL A 1 760 ? 128.721 93.356  99.400  1.00 51.42  ? 2551 VAL A CG1   1 
ATOM   4752 C  CG2   . VAL A 1 760 ? 128.966 91.887  97.415  1.00 63.89  ? 2551 VAL A CG2   1 
ATOM   4753 N  N     . VAL A 1 761 ? 131.220 95.661  97.422  1.00 68.16  ? 2552 VAL A N     1 
ATOM   4754 C  CA    . VAL A 1 761 ? 132.030 96.735  97.991  1.00 70.15  ? 2552 VAL A CA    1 
ATOM   4755 C  C     . VAL A 1 761 ? 131.853 98.028  97.203  1.00 68.46  ? 2552 VAL A C     1 
ATOM   4756 O  O     . VAL A 1 761 ? 131.468 99.061  97.763  1.00 65.47  ? 2552 VAL A O     1 
ATOM   4757 C  CB    . VAL A 1 761 ? 133.509 96.311  98.075  1.00 64.39  ? 2552 VAL A CB    1 
ATOM   4758 C  CG1   . VAL A 1 761 ? 133.963 95.639  96.784  1.00 65.66  ? 2552 VAL A CG1   1 
ATOM   4759 C  CG2   . VAL A 1 761 ? 134.383 97.514  98.392  1.00 60.82  ? 2552 VAL A CG2   1 
ATOM   4760 N  N     . GLN A 1 762 ? 132.104 97.981  95.890  1.00 69.69  ? 2553 GLN A N     1 
ATOM   4761 C  CA    . GLN A 1 762 ? 132.107 99.199  95.082  1.00 70.05  ? 2553 GLN A CA    1 
ATOM   4762 C  C     . GLN A 1 762 ? 130.791 99.953  95.212  1.00 67.92  ? 2553 GLN A C     1 
ATOM   4763 O  O     . GLN A 1 762 ? 130.775 101.141 95.557  1.00 62.39  ? 2553 GLN A O     1 
ATOM   4764 C  CB    . GLN A 1 762 ? 132.382 98.854  93.618  1.00 69.26  ? 2553 GLN A CB    1 
ATOM   4765 C  CG    . GLN A 1 762 ? 131.974 99.945  92.643  1.00 67.95  ? 2553 GLN A CG    1 
ATOM   4766 C  CD    . GLN A 1 762 ? 131.868 99.440  91.219  1.00 77.36  ? 2553 GLN A CD    1 
ATOM   4767 O  OE1   . GLN A 1 762 ? 131.878 98.234  90.974  1.00 80.31  ? 2553 GLN A OE1   1 
ATOM   4768 N  NE2   . GLN A 1 762 ? 131.761 100.362 90.270  1.00 78.00  ? 2553 GLN A NE2   1 
ATOM   4769 N  N     . VAL A 1 763 ? 129.672 99.260  94.981  1.00 68.83  ? 2554 VAL A N     1 
ATOM   4770 C  CA    . VAL A 1 763 ? 128.363 99.893  95.115  1.00 62.10  ? 2554 VAL A CA    1 
ATOM   4771 C  C     . VAL A 1 763 ? 128.208 100.488 96.505  1.00 59.59  ? 2554 VAL A C     1 
ATOM   4772 O  O     . VAL A 1 763 ? 127.754 101.630 96.659  1.00 56.35  ? 2554 VAL A O     1 
ATOM   4773 C  CB    . VAL A 1 763 ? 127.244 98.884  94.802  1.00 51.91  ? 2554 VAL A CB    1 
ATOM   4774 C  CG1   . VAL A 1 763 ? 125.894 99.441  95.223  1.00 44.73  ? 2554 VAL A CG1   1 
ATOM   4775 C  CG2   . VAL A 1 763 ? 127.244 98.536  93.323  1.00 56.67  ? 2554 VAL A CG2   1 
ATOM   4776 N  N     . ALA A 1 764 ? 128.614 99.740  97.536  1.00 58.32  ? 2555 ALA A N     1 
ATOM   4777 C  CA    . ALA A 1 764 ? 128.558 100.264 98.895  1.00 51.51  ? 2555 ALA A CA    1 
ATOM   4778 C  C     . ALA A 1 764 ? 129.293 101.591 98.983  1.00 51.38  ? 2555 ALA A C     1 
ATOM   4779 O  O     . ALA A 1 764 ? 128.745 102.586 99.473  1.00 53.43  ? 2555 ALA A O     1 
ATOM   4780 C  CB    . ALA A 1 764 ? 129.152 99.254  99.877  1.00 47.99  ? 2555 ALA A CB    1 
ATOM   4781 N  N     . GLN A 1 765 ? 130.519 101.634 98.454  1.00 48.30  ? 2556 GLN A N     1 
ATOM   4782 C  CA    . GLN A 1 765 ? 131.277 102.879 98.456  1.00 50.20  ? 2556 GLN A CA    1 
ATOM   4783 C  C     . GLN A 1 765 ? 130.480 103.992 97.796  1.00 52.93  ? 2556 GLN A C     1 
ATOM   4784 O  O     . GLN A 1 765 ? 130.381 105.099 98.340  1.00 50.02  ? 2556 GLN A O     1 
ATOM   4785 C  CB    . GLN A 1 765 ? 132.617 102.680 97.750  1.00 53.97  ? 2556 GLN A CB    1 
ATOM   4786 C  CG    . GLN A 1 765 ? 133.747 103.525 98.311  1.00 49.49  ? 2556 GLN A CG    1 
ATOM   4787 C  CD    . GLN A 1 765 ? 135.111 103.048 97.853  1.00 51.37  ? 2556 GLN A CD    1 
ATOM   4788 O  OE1   . GLN A 1 765 ? 135.457 103.161 96.677  1.00 48.45  ? 2556 GLN A OE1   1 
ATOM   4789 N  NE2   . GLN A 1 765 ? 135.893 102.511 98.781  1.00 56.83  ? 2556 GLN A NE2   1 
ATOM   4790 N  N     . ILE A 1 766 ? 129.853 103.692 96.655  1.00 57.94  ? 2557 ILE A N     1 
ATOM   4791 C  CA    . ILE A 1 766 ? 129.043 104.691 95.965  1.00 60.90  ? 2557 ILE A CA    1 
ATOM   4792 C  C     . ILE A 1 766 ? 127.990 105.248 96.909  1.00 59.58  ? 2557 ILE A C     1 
ATOM   4793 O  O     . ILE A 1 766 ? 127.846 106.468 97.057  1.00 59.59  ? 2557 ILE A O     1 
ATOM   4794 C  CB    . ILE A 1 766 ? 128.406 104.087 94.701  1.00 54.29  ? 2557 ILE A CB    1 
ATOM   4795 C  CG1   . ILE A 1 766 ? 129.451 103.946 93.593  1.00 58.83  ? 2557 ILE A CG1   1 
ATOM   4796 C  CG2   . ILE A 1 766 ? 127.233 104.932 94.238  1.00 43.23  ? 2557 ILE A CG2   1 
ATOM   4797 C  CD1   . ILE A 1 766 ? 130.179 105.233 93.273  1.00 60.87  ? 2557 ILE A CD1   1 
ATOM   4798 N  N     . VAL A 1 767 ? 127.276 104.361 97.607  1.00 55.95  ? 2558 VAL A N     1 
ATOM   4799 C  CA    . VAL A 1 767 ? 126.280 104.819 98.569  1.00 44.02  ? 2558 VAL A CA    1 
ATOM   4800 C  C     . VAL A 1 767 ? 126.945 105.694 99.620  1.00 47.97  ? 2558 VAL A C     1 
ATOM   4801 O  O     . VAL A 1 767 ? 126.521 106.832 99.865  1.00 50.19  ? 2558 VAL A O     1 
ATOM   4802 C  CB    . VAL A 1 767 ? 125.551 103.622 99.203  1.00 34.80  ? 2558 VAL A CB    1 
ATOM   4803 C  CG1   . VAL A 1 767 ? 124.479 104.107 100.153 1.00 27.30  ? 2558 VAL A CG1   1 
ATOM   4804 C  CG2   . VAL A 1 767 ? 124.948 102.739 98.125  1.00 33.01  ? 2558 VAL A CG2   1 
ATOM   4805 N  N     . LYS A 1 768 ? 128.058 105.214 100.184 1.00 45.39  ? 2559 LYS A N     1 
ATOM   4806 C  CA    . LYS A 1 768 ? 128.737 105.957 101.236 1.00 44.23  ? 2559 LYS A CA    1 
ATOM   4807 C  C     . LYS A 1 768 ? 129.248 107.296 100.735 1.00 48.47  ? 2559 LYS A C     1 
ATOM   4808 O  O     . LYS A 1 768 ? 129.586 108.163 101.547 1.00 57.87  ? 2559 LYS A O     1 
ATOM   4809 C  CB    . LYS A 1 768 ? 129.889 105.131 101.811 1.00 48.21  ? 2559 LYS A CB    1 
ATOM   4810 C  CG    . LYS A 1 768 ? 130.269 105.502 103.238 1.00 48.70  ? 2559 LYS A CG    1 
ATOM   4811 C  CD    . LYS A 1 768 ? 131.009 104.369 103.931 1.00 51.44  ? 2559 LYS A CD    1 
ATOM   4812 C  CE    . LYS A 1 768 ? 132.251 103.961 103.154 1.00 61.82  ? 2559 LYS A CE    1 
ATOM   4813 N  NZ    . LYS A 1 768 ? 132.867 102.719 103.698 1.00 60.40  ? 2559 LYS A NZ    1 
ATOM   4814 N  N     . ASN A 1 769 ? 129.314 107.483 99.417  1.00 41.29  ? 2560 ASN A N     1 
ATOM   4815 C  CA    . ASN A 1 769 ? 129.583 108.807 98.878  1.00 42.91  ? 2560 ASN A CA    1 
ATOM   4816 C  C     . ASN A 1 769 ? 128.295 109.615 98.776  1.00 48.82  ? 2560 ASN A C     1 
ATOM   4817 O  O     . ASN A 1 769 ? 128.174 110.694 99.368  1.00 47.13  ? 2560 ASN A O     1 
ATOM   4818 C  CB    . ASN A 1 769 ? 130.263 108.688 97.512  1.00 50.50  ? 2560 ASN A CB    1 
ATOM   4819 C  CG    . ASN A 1 769 ? 130.859 109.997 97.043  1.00 60.39  ? 2560 ASN A CG    1 
ATOM   4820 O  OD1   . ASN A 1 769 ? 131.045 110.924 97.830  1.00 64.20  ? 2560 ASN A OD1   1 
ATOM   4821 N  ND2   . ASN A 1 769 ? 131.163 110.080 95.753  1.00 55.44  ? 2560 ASN A ND2   1 
ATOM   4822 N  N     . GLU A 1 770 ? 127.301 109.077 98.064  1.00 48.26  ? 2561 GLU A N     1 
ATOM   4823 C  CA    . GLU A 1 770 ? 126.143 109.881 97.687  1.00 43.99  ? 2561 GLU A CA    1 
ATOM   4824 C  C     . GLU A 1 770 ? 125.294 110.238 98.898  1.00 43.32  ? 2561 GLU A C     1 
ATOM   4825 O  O     . GLU A 1 770 ? 124.733 111.337 98.968  1.00 42.22  ? 2561 GLU A O     1 
ATOM   4826 C  CB    . GLU A 1 770 ? 125.314 109.145 96.638  1.00 37.44  ? 2561 GLU A CB    1 
ATOM   4827 C  CG    . GLU A 1 770 ? 126.104 108.756 95.401  1.00 35.63  ? 2561 GLU A CG    1 
ATOM   4828 C  CD    . GLU A 1 770 ? 126.218 109.888 94.394  1.00 43.05  ? 2561 GLU A CD    1 
ATOM   4829 O  OE1   . GLU A 1 770 ? 126.131 111.067 94.796  1.00 45.43  ? 2561 GLU A OE1   1 
ATOM   4830 O  OE2   . GLU A 1 770 ? 126.399 109.598 93.194  1.00 43.27  ? 2561 GLU A OE2   1 
ATOM   4831 N  N     . MET A 1 771 ? 125.185 109.323 99.857  1.00 41.01  ? 2562 MET A N     1 
ATOM   4832 C  CA    . MET A 1 771 ? 124.472 109.634 101.087 1.00 39.03  ? 2562 MET A CA    1 
ATOM   4833 C  C     . MET A 1 771 ? 125.251 110.623 101.943 1.00 42.83  ? 2562 MET A C     1 
ATOM   4834 O  O     . MET A 1 771 ? 124.649 111.396 102.696 1.00 49.08  ? 2562 MET A O     1 
ATOM   4835 C  CB    . MET A 1 771 ? 124.193 108.347 101.858 1.00 35.09  ? 2562 MET A CB    1 
ATOM   4836 C  CG    . MET A 1 771 ? 123.025 107.556 101.302 1.00 31.57  ? 2562 MET A CG    1 
ATOM   4837 S  SD    . MET A 1 771 ? 122.436 106.286 102.425 1.00 11.55  ? 2562 MET A SD    1 
ATOM   4838 C  CE    . MET A 1 771 ? 121.333 107.235 103.455 1.00 18.60  ? 2562 MET A CE    1 
ATOM   4839 N  N     . GLU A 1 772 ? 126.583 110.620 101.842 1.00 42.45  ? 2563 GLU A N     1 
ATOM   4840 C  CA    . GLU A 1 772 ? 127.377 111.556 102.630 1.00 43.18  ? 2563 GLU A CA    1 
ATOM   4841 C  C     . GLU A 1 772 ? 127.292 112.969 102.067 1.00 48.24  ? 2563 GLU A C     1 
ATOM   4842 O  O     . GLU A 1 772 ? 127.190 113.940 102.826 1.00 52.01  ? 2563 GLU A O     1 
ATOM   4843 C  CB    . GLU A 1 772 ? 128.831 111.090 102.694 1.00 50.15  ? 2563 GLU A CB    1 
ATOM   4844 C  CG    . GLU A 1 772 ? 129.171 110.284 103.938 1.00 53.58  ? 2563 GLU A CG    1 
ATOM   4845 C  CD    . GLU A 1 772 ? 129.658 111.151 105.082 1.00 56.17  ? 2563 GLU A CD    1 
ATOM   4846 O  OE1   . GLU A 1 772 ? 129.107 112.255 105.275 1.00 55.64  ? 2563 GLU A OE1   1 
ATOM   4847 O  OE2   . GLU A 1 772 ? 130.595 110.728 105.791 1.00 54.65  ? 2563 GLU A OE2   1 
ATOM   4848 N  N     . SER A 1 773 ? 127.327 113.104 100.742 1.00 46.37  ? 2564 SER A N     1 
ATOM   4849 C  CA    . SER A 1 773 ? 127.325 114.402 100.081 1.00 42.12  ? 2564 SER A CA    1 
ATOM   4850 C  C     . SER A 1 773 ? 125.988 114.702 99.409  1.00 46.09  ? 2564 SER A C     1 
ATOM   4851 O  O     . SER A 1 773 ? 125.943 115.401 98.394  1.00 48.17  ? 2564 SER A O     1 
ATOM   4852 C  CB    . SER A 1 773 ? 128.461 114.480 99.063  1.00 42.20  ? 2564 SER A CB    1 
ATOM   4853 O  OG    . SER A 1 773 ? 128.156 113.732 97.899  1.00 52.10  ? 2564 SER A OG    1 
ATOM   4854 N  N     . ALA A 1 774 ? 124.892 114.177 99.962  1.00 44.75  ? 2565 ALA A N     1 
ATOM   4855 C  CA    . ALA A 1 774 ? 123.576 114.458 99.399  1.00 38.04  ? 2565 ALA A CA    1 
ATOM   4856 C  C     . ALA A 1 774 ? 123.258 115.945 99.476  1.00 36.13  ? 2565 ALA A C     1 
ATOM   4857 O  O     . ALA A 1 774 ? 122.907 116.572 98.471  1.00 36.48  ? 2565 ALA A O     1 
ATOM   4858 C  CB    . ALA A 1 774 ? 122.509 113.638 100.123 1.00 33.71  ? 2565 ALA A CB    1 
ATOM   4859 N  N     . VAL A 1 775 ? 123.382 116.528 100.666 1.00 35.82  ? 2566 VAL A N     1 
ATOM   4860 C  CA    . VAL A 1 775 ? 123.265 117.969 100.862 1.00 37.88  ? 2566 VAL A CA    1 
ATOM   4861 C  C     . VAL A 1 775 ? 124.363 118.409 101.818 1.00 45.68  ? 2566 VAL A C     1 
ATOM   4862 O  O     . VAL A 1 775 ? 124.541 117.810 102.884 1.00 42.91  ? 2566 VAL A O     1 
ATOM   4863 C  CB    . VAL A 1 775 ? 121.879 118.373 101.400 1.00 30.13  ? 2566 VAL A CB    1 
ATOM   4864 C  CG1   . VAL A 1 775 ? 121.878 119.830 101.820 1.00 36.20  ? 2566 VAL A CG1   1 
ATOM   4865 C  CG2   . VAL A 1 775 ? 120.824 118.150 100.338 1.00 28.59  ? 2566 VAL A CG2   1 
ATOM   4866 N  N     . LYS A 1 776 ? 125.100 119.450 101.439 1.00 51.66  ? 2567 LYS A N     1 
ATOM   4867 C  CA    . LYS A 1 776 ? 126.172 119.982 102.276 1.00 52.85  ? 2567 LYS A CA    1 
ATOM   4868 C  C     . LYS A 1 776 ? 125.550 120.743 103.439 1.00 46.07  ? 2567 LYS A C     1 
ATOM   4869 O  O     . LYS A 1 776 ? 125.224 121.926 103.323 1.00 45.73  ? 2567 LYS A O     1 
ATOM   4870 C  CB    . LYS A 1 776 ? 127.093 120.879 101.458 1.00 59.19  ? 2567 LYS A CB    1 
ATOM   4871 C  CG    . LYS A 1 776 ? 128.326 120.174 100.919 1.00 62.11  ? 2567 LYS A CG    1 
ATOM   4872 C  CD    . LYS A 1 776 ? 129.157 119.580 102.044 1.00 67.04  ? 2567 LYS A CD    1 
ATOM   4873 C  CE    . LYS A 1 776 ? 130.132 118.540 101.520 1.00 62.16  ? 2567 LYS A CE    1 
ATOM   4874 N  NZ    . LYS A 1 776 ? 130.539 117.577 102.580 1.00 53.83  ? 2567 LYS A NZ    1 
ATOM   4875 N  N     . LEU A 1 777 ? 125.383 120.063 104.566 1.00 47.59  ? 2568 LEU A N     1 
ATOM   4876 C  CA    . LEU A 1 777 ? 124.769 120.658 105.741 1.00 49.90  ? 2568 LEU A CA    1 
ATOM   4877 C  C     . LEU A 1 777 ? 125.842 121.237 106.660 1.00 54.76  ? 2568 LEU A C     1 
ATOM   4878 O  O     . LEU A 1 777 ? 127.043 121.141 106.399 1.00 53.12  ? 2568 LEU A O     1 
ATOM   4879 C  CB    . LEU A 1 777 ? 123.933 119.619 106.489 1.00 39.60  ? 2568 LEU A CB    1 
ATOM   4880 C  CG    . LEU A 1 777 ? 122.590 119.219 105.872 1.00 42.99  ? 2568 LEU A CG    1 
ATOM   4881 C  CD1   . LEU A 1 777 ? 122.118 117.897 106.451 1.00 39.11  ? 2568 LEU A CD1   1 
ATOM   4882 C  CD2   . LEU A 1 777 ? 121.539 120.294 106.054 1.00 50.93  ? 2568 LEU A CD2   1 
ATOM   4883 N  N     . SER A 1 778 ? 125.391 121.851 107.756 1.00 56.87  ? 2569 SER A N     1 
ATOM   4884 C  CA    . SER A 1 778 ? 126.324 122.329 108.769 1.00 49.97  ? 2569 SER A CA    1 
ATOM   4885 C  C     . SER A 1 778 ? 126.962 121.185 109.544 1.00 48.39  ? 2569 SER A C     1 
ATOM   4886 O  O     . SER A 1 778 ? 127.978 121.396 110.214 1.00 51.18  ? 2569 SER A O     1 
ATOM   4887 C  CB    . SER A 1 778 ? 125.615 123.278 109.736 1.00 49.73  ? 2569 SER A CB    1 
ATOM   4888 O  OG    . SER A 1 778 ? 125.038 124.372 109.046 1.00 53.34  ? 2569 SER A OG    1 
ATOM   4889 N  N     . VAL A 1 779 ? 126.391 119.985 109.468 1.00 47.36  ? 2570 VAL A N     1 
ATOM   4890 C  CA    . VAL A 1 779 ? 126.891 118.814 110.175 1.00 40.62  ? 2570 VAL A CA    1 
ATOM   4891 C  C     . VAL A 1 779 ? 127.082 117.694 109.164 1.00 45.08  ? 2570 VAL A C     1 
ATOM   4892 O  O     . VAL A 1 779 ? 126.189 117.430 108.351 1.00 55.43  ? 2570 VAL A O     1 
ATOM   4893 C  CB    . VAL A 1 779 ? 125.929 118.374 111.295 1.00 40.14  ? 2570 VAL A CB    1 
ATOM   4894 C  CG1   . VAL A 1 779 ? 126.263 116.971 111.764 1.00 50.36  ? 2570 VAL A CG1   1 
ATOM   4895 C  CG2   . VAL A 1 779 ? 125.983 119.353 112.449 1.00 51.10  ? 2570 VAL A CG2   1 
ATOM   4896 N  N     . LYS A 1 780 ? 128.244 117.046 109.207 1.00 46.97  ? 2571 LYS A N     1 
ATOM   4897 C  CA    . LYS A 1 780 ? 128.511 115.930 108.309 1.00 46.63  ? 2571 LYS A CA    1 
ATOM   4898 C  C     . LYS A 1 780 ? 127.497 114.817 108.536 1.00 47.53  ? 2571 LYS A C     1 
ATOM   4899 O  O     . LYS A 1 780 ? 127.225 114.430 109.675 1.00 49.03  ? 2571 LYS A O     1 
ATOM   4900 C  CB    . LYS A 1 780 ? 129.933 115.410 108.527 1.00 61.21  ? 2571 LYS A CB    1 
ATOM   4901 C  CG    . LYS A 1 780 ? 130.195 114.036 107.931 1.00 64.87  ? 2571 LYS A CG    1 
ATOM   4902 C  CD    . LYS A 1 780 ? 131.596 113.945 107.347 1.00 68.41  ? 2571 LYS A CD    1 
ATOM   4903 C  CE    . LYS A 1 780 ? 132.629 113.677 108.429 1.00 64.22  ? 2571 LYS A CE    1 
ATOM   4904 N  NZ    . LYS A 1 780 ? 132.553 112.278 108.931 1.00 73.07  ? 2571 LYS A NZ    1 
ATOM   4905 N  N     . LEU A 1 781 ? 126.936 114.303 107.443 1.00 49.63  ? 2572 LEU A N     1 
ATOM   4906 C  CA    . LEU A 1 781 ? 125.882 113.291 107.509 1.00 47.67  ? 2572 LEU A CA    1 
ATOM   4907 C  C     . LEU A 1 781 ? 126.525 111.912 107.523 1.00 49.86  ? 2572 LEU A C     1 
ATOM   4908 O  O     . LEU A 1 781 ? 126.799 111.319 106.480 1.00 59.26  ? 2572 LEU A O     1 
ATOM   4909 C  CB    . LEU A 1 781 ? 124.918 113.442 106.340 1.00 41.67  ? 2572 LEU A CB    1 
ATOM   4910 C  CG    . LEU A 1 781 ? 123.970 114.637 106.393 1.00 38.90  ? 2572 LEU A CG    1 
ATOM   4911 C  CD1   . LEU A 1 781 ? 122.928 114.528 105.296 1.00 35.74  ? 2572 LEU A CD1   1 
ATOM   4912 C  CD2   . LEU A 1 781 ? 123.312 114.732 107.758 1.00 43.62  ? 2572 LEU A CD2   1 
ATOM   4913 N  N     . LYS A 1 782 ? 126.765 111.391 108.722 1.00 44.23  ? 2573 LYS A N     1 
ATOM   4914 C  CA    . LYS A 1 782 ? 127.309 110.048 108.847 1.00 44.40  ? 2573 LYS A CA    1 
ATOM   4915 C  C     . LYS A 1 782 ? 126.285 109.018 108.393 1.00 39.78  ? 2573 LYS A C     1 
ATOM   4916 O  O     . LYS A 1 782 ? 125.096 109.121 108.704 1.00 41.10  ? 2573 LYS A O     1 
ATOM   4917 C  CB    . LYS A 1 782 ? 127.729 109.772 110.290 1.00 46.80  ? 2573 LYS A CB    1 
ATOM   4918 C  CG    . LYS A 1 782 ? 129.198 110.034 110.572 1.00 55.74  ? 2573 LYS A CG    1 
ATOM   4919 C  CD    . LYS A 1 782 ? 129.525 109.814 112.040 1.00 68.42  ? 2573 LYS A CD    1 
ATOM   4920 C  CE    . LYS A 1 782 ? 128.999 108.472 112.527 1.00 64.03  ? 2573 LYS A CE    1 
ATOM   4921 N  NZ    . LYS A 1 782 ? 129.112 108.329 114.005 1.00 66.25  ? 2573 LYS A NZ    1 
ATOM   4922 N  N     . VAL A 1 783 ? 126.751 108.024 107.644 1.00 35.36  ? 2574 VAL A N     1 
ATOM   4923 C  CA    . VAL A 1 783 ? 125.913 106.931 107.167 1.00 33.21  ? 2574 VAL A CA    1 
ATOM   4924 C  C     . VAL A 1 783 ? 126.641 105.625 107.441 1.00 33.09  ? 2574 VAL A C     1 
ATOM   4925 O  O     . VAL A 1 783 ? 127.788 105.448 107.013 1.00 43.49  ? 2574 VAL A O     1 
ATOM   4926 C  CB    . VAL A 1 783 ? 125.583 107.067 105.671 1.00 34.33  ? 2574 VAL A CB    1 
ATOM   4927 C  CG1   . VAL A 1 783 ? 126.780 107.604 104.908 1.00 33.44  ? 2574 VAL A CG1   1 
ATOM   4928 C  CG2   . VAL A 1 783 ? 125.150 105.727 105.102 1.00 33.87  ? 2574 VAL A CG2   1 
ATOM   4929 N  N     . LYS A 1 784 ? 125.986 104.717 108.158 1.00 32.41  ? 2575 LYS A N     1 
ATOM   4930 C  CA    . LYS A 1 784 ? 126.533 103.393 108.415 1.00 35.60  ? 2575 LYS A CA    1 
ATOM   4931 C  C     . LYS A 1 784 ? 126.014 102.437 107.351 1.00 37.80  ? 2575 LYS A C     1 
ATOM   4932 O  O     . LYS A 1 784 ? 124.806 102.193 107.265 1.00 45.92  ? 2575 LYS A O     1 
ATOM   4933 C  CB    . LYS A 1 784 ? 126.152 102.908 109.812 1.00 42.44  ? 2575 LYS A CB    1 
ATOM   4934 C  CG    . LYS A 1 784 ? 127.026 103.460 110.925 1.00 49.45  ? 2575 LYS A CG    1 
ATOM   4935 C  CD    . LYS A 1 784 ? 126.689 102.818 112.261 1.00 56.05  ? 2575 LYS A CD    1 
ATOM   4936 C  CE    . LYS A 1 784 ? 126.448 103.865 113.335 1.00 54.75  ? 2575 LYS A CE    1 
ATOM   4937 N  NZ    . LYS A 1 784 ? 127.491 104.928 113.319 1.00 53.82  ? 2575 LYS A NZ    1 
ATOM   4938 N  N     . VAL A 1 785 ? 126.921 101.908 106.539 1.00 33.81  ? 2576 VAL A N     1 
ATOM   4939 C  CA    . VAL A 1 785 ? 126.577 100.968 105.481 1.00 30.67  ? 2576 VAL A CA    1 
ATOM   4940 C  C     . VAL A 1 785 ? 126.763 99.561  106.027 1.00 33.98  ? 2576 VAL A C     1 
ATOM   4941 O  O     . VAL A 1 785 ? 127.881 99.164  106.374 1.00 45.27  ? 2576 VAL A O     1 
ATOM   4942 C  CB    . VAL A 1 785 ? 127.435 101.193 104.226 1.00 29.98  ? 2576 VAL A CB    1 
ATOM   4943 C  CG1   . VAL A 1 785 ? 127.229 100.062 103.236 1.00 38.28  ? 2576 VAL A CG1   1 
ATOM   4944 C  CG2   . VAL A 1 785 ? 127.100 102.531 103.591 1.00 32.72  ? 2576 VAL A CG2   1 
ATOM   4945 N  N     . LYS A 1 786 ? 125.672 98.809  106.107 1.00 27.97  ? 2577 LYS A N     1 
ATOM   4946 C  CA    . LYS A 1 786 ? 125.688 97.449  106.619 1.00 31.79  ? 2577 LYS A CA    1 
ATOM   4947 C  C     . LYS A 1 786 ? 125.330 96.487  105.498 1.00 33.89  ? 2577 LYS A C     1 
ATOM   4948 O  O     . LYS A 1 786 ? 124.488 96.795  104.650 1.00 38.77  ? 2577 LYS A O     1 
ATOM   4949 C  CB    . LYS A 1 786 ? 124.706 97.290  107.780 1.00 37.70  ? 2577 LYS A CB    1 
ATOM   4950 C  CG    . LYS A 1 786 ? 124.754 98.423  108.789 1.00 42.37  ? 2577 LYS A CG    1 
ATOM   4951 C  CD    . LYS A 1 786 ? 123.531 98.413  109.690 1.00 51.81  ? 2577 LYS A CD    1 
ATOM   4952 C  CE    . LYS A 1 786 ? 123.896 98.757  111.124 1.00 53.80  ? 2577 LYS A CE    1 
ATOM   4953 N  NZ    . LYS A 1 786 ? 124.314 97.553  111.893 1.00 46.80  ? 2577 LYS A NZ    1 
ATOM   4954 N  N     . ILE A 1 787 ? 125.982 95.329  105.482 1.00 33.46  ? 2578 ILE A N     1 
ATOM   4955 C  CA    . ILE A 1 787 ? 125.717 94.313  104.472 1.00 34.42  ? 2578 ILE A CA    1 
ATOM   4956 C  C     . ILE A 1 787 ? 125.429 92.996  105.172 1.00 35.70  ? 2578 ILE A C     1 
ATOM   4957 O  O     . ILE A 1 787 ? 125.876 92.761  106.298 1.00 44.44  ? 2578 ILE A O     1 
ATOM   4958 C  CB    . ILE A 1 787 ? 126.882 94.147  103.472 1.00 32.13  ? 2578 ILE A CB    1 
ATOM   4959 C  CG1   . ILE A 1 787 ? 127.591 95.479  103.235 1.00 36.04  ? 2578 ILE A CG1   1 
ATOM   4960 C  CG2   . ILE A 1 787 ? 126.381 93.576  102.158 1.00 39.68  ? 2578 ILE A CG2   1 
ATOM   4961 C  CD1   . ILE A 1 787 ? 128.853 95.348  102.425 1.00 47.47  ? 2578 ILE A CD1   1 
ATOM   4962 N  N     . GLY A 1 788 ? 124.664 92.142  104.510 1.00 30.65  ? 2579 GLY A N     1 
ATOM   4963 C  CA    . GLY A 1 788 ? 124.361 90.848  105.086 1.00 31.60  ? 2579 GLY A CA    1 
ATOM   4964 C  C     . GLY A 1 788 ? 123.657 89.953  104.097 1.00 33.93  ? 2579 GLY A C     1 
ATOM   4965 O  O     . GLY A 1 788 ? 123.075 90.416  103.111 1.00 38.91  ? 2579 GLY A O     1 
ATOM   4966 N  N     . ALA A 1 789 ? 123.717 88.652  104.381 1.00 35.37  ? 2580 ALA A N     1 
ATOM   4967 C  CA    . ALA A 1 789 ? 122.974 87.678  103.595 1.00 35.58  ? 2580 ALA A CA    1 
ATOM   4968 C  C     . ALA A 1 789 ? 121.471 87.814  103.779 1.00 34.79  ? 2580 ALA A C     1 
ATOM   4969 O  O     . ALA A 1 789 ? 120.714 87.202  103.021 1.00 37.80  ? 2580 ALA A O     1 
ATOM   4970 C  CB    . ALA A 1 789 ? 123.414 86.259  103.959 1.00 32.87  ? 2580 ALA A CB    1 
ATOM   4971 N  N     . SER A 1 790 ? 121.030 88.582  104.772 1.00 35.34  ? 2581 SER A N     1 
ATOM   4972 C  CA    . SER A 1 790 ? 119.620 88.866  104.982 1.00 39.10  ? 2581 SER A CA    1 
ATOM   4973 C  C     . SER A 1 790 ? 119.501 90.182  105.733 1.00 40.25  ? 2581 SER A C     1 
ATOM   4974 O  O     . SER A 1 790 ? 120.459 90.658  106.347 1.00 49.14  ? 2581 SER A O     1 
ATOM   4975 C  CB    . SER A 1 790 ? 118.920 87.745  105.757 1.00 45.67  ? 2581 SER A CB    1 
ATOM   4976 O  OG    . SER A 1 790 ? 118.938 86.527  105.035 1.00 46.76  ? 2581 SER A OG    1 
ATOM   4977 N  N     . TRP A 1 791 ? 118.306 90.771  105.673 1.00 29.31  ? 2582 TRP A N     1 
ATOM   4978 C  CA    . TRP A 1 791 ? 118.053 92.002  106.413 1.00 26.47  ? 2582 TRP A CA    1 
ATOM   4979 C  C     . TRP A 1 791 ? 118.081 91.762  107.918 1.00 35.71  ? 2582 TRP A C     1 
ATOM   4980 O  O     . TRP A 1 791 ? 118.434 92.667  108.682 1.00 43.90  ? 2582 TRP A O     1 
ATOM   4981 C  CB    . TRP A 1 791 ? 116.712 92.593  105.975 1.00 29.23  ? 2582 TRP A CB    1 
ATOM   4982 C  CG    . TRP A 1 791 ? 116.345 93.904  106.609 1.00 30.70  ? 2582 TRP A CG    1 
ATOM   4983 C  CD1   . TRP A 1 791 ? 117.180 94.782  107.231 1.00 33.13  ? 2582 TRP A CD1   1 
ATOM   4984 C  CD2   . TRP A 1 791 ? 115.037 94.483  106.673 1.00 31.10  ? 2582 TRP A CD2   1 
ATOM   4985 N  NE1   . TRP A 1 791 ? 116.473 95.867  107.686 1.00 35.91  ? 2582 TRP A NE1   1 
ATOM   4986 C  CE2   . TRP A 1 791 ? 115.154 95.707  107.354 1.00 29.25  ? 2582 TRP A CE2   1 
ATOM   4987 C  CE3   . TRP A 1 791 ? 113.778 94.082  106.221 1.00 29.09  ? 2582 TRP A CE3   1 
ATOM   4988 C  CZ2   . TRP A 1 791 ? 114.061 96.531  107.596 1.00 26.80  ? 2582 TRP A CZ2   1 
ATOM   4989 C  CZ3   . TRP A 1 791 ? 112.694 94.903  106.461 1.00 24.87  ? 2582 TRP A CZ3   1 
ATOM   4990 C  CH2   . TRP A 1 791 ? 112.843 96.113  107.140 1.00 25.95  ? 2582 TRP A CH2   1 
ATOM   4991 N  N     . GLY A 1 792 ? 117.733 90.554  108.361 1.00 40.16  ? 2583 GLY A N     1 
ATOM   4992 C  CA    . GLY A 1 792 ? 117.650 90.298  109.791 1.00 47.21  ? 2583 GLY A CA    1 
ATOM   4993 C  C     . GLY A 1 792 ? 118.995 90.366  110.493 1.00 50.83  ? 2583 GLY A C     1 
ATOM   4994 O  O     . GLY A 1 792 ? 119.119 90.975  111.559 1.00 50.04  ? 2583 GLY A O     1 
ATOM   4995 N  N     . GLU A 1 793 ? 120.018 89.749  109.908 1.00 48.07  ? 2584 GLU A N     1 
ATOM   4996 C  CA    . GLU A 1 793 ? 121.331 89.649  110.535 1.00 44.03  ? 2584 GLU A CA    1 
ATOM   4997 C  C     . GLU A 1 793 ? 122.394 90.375  109.723 1.00 43.37  ? 2584 GLU A C     1 
ATOM   4998 O  O     . GLU A 1 793 ? 123.500 89.871  109.521 1.00 48.08  ? 2584 GLU A O     1 
ATOM   4999 C  CB    . GLU A 1 793 ? 121.734 88.192  110.748 1.00 48.03  ? 2584 GLU A CB    1 
ATOM   5000 C  CG    . GLU A 1 793 ? 121.472 87.284  109.564 1.00 53.42  ? 2584 GLU A CG    1 
ATOM   5001 C  CD    . GLU A 1 793 ? 120.528 86.153  109.907 1.00 57.94  ? 2584 GLU A CD    1 
ATOM   5002 O  OE1   . GLU A 1 793 ? 119.432 86.433  110.436 1.00 58.13  ? 2584 GLU A OE1   1 
ATOM   5003 O  OE2   . GLU A 1 793 ? 120.884 84.983  109.656 1.00 56.70  ? 2584 GLU A OE2   1 
ATOM   5004 N  N     . LEU A 1 794 ? 122.069 91.569  109.241 1.00 41.02  ? 2585 LEU A N     1 
ATOM   5005 C  CA    . LEU A 1 794 ? 123.060 92.381  108.552 1.00 43.40  ? 2585 LEU A CA    1 
ATOM   5006 C  C     . LEU A 1 794 ? 124.115 92.871  109.539 1.00 47.70  ? 2585 LEU A C     1 
ATOM   5007 O  O     . LEU A 1 794 ? 123.803 93.268  110.665 1.00 54.08  ? 2585 LEU A O     1 
ATOM   5008 C  CB    . LEU A 1 794 ? 122.385 93.559  107.843 1.00 36.62  ? 2585 LEU A CB    1 
ATOM   5009 C  CG    . LEU A 1 794 ? 121.981 94.828  108.601 1.00 39.28  ? 2585 LEU A CG    1 
ATOM   5010 C  CD1   . LEU A 1 794 ? 121.360 95.818  107.636 1.00 33.86  ? 2585 LEU A CD1   1 
ATOM   5011 C  CD2   . LEU A 1 794 ? 121.021 94.541  109.746 1.00 47.01  ? 2585 LEU A CD2   1 
ATOM   5012 N  N     . LYS A 1 795 ? 125.376 92.816  109.120 1.00 43.69  ? 2586 LYS A N     1 
ATOM   5013 C  CA    . LYS A 1 795 ? 126.500 93.231  109.940 1.00 40.27  ? 2586 LYS A CA    1 
ATOM   5014 C  C     . LYS A 1 795 ? 127.140 94.480  109.349 1.00 42.34  ? 2586 LYS A C     1 
ATOM   5015 O  O     . LYS A 1 795 ? 127.073 94.723  108.139 1.00 46.79  ? 2586 LYS A O     1 
ATOM   5016 C  CB    . LYS A 1 795 ? 127.542 92.115  110.050 1.00 39.89  ? 2586 LYS A CB    1 
ATOM   5017 C  CG    . LYS A 1 795 ? 126.953 90.745  110.341 1.00 43.78  ? 2586 LYS A CG    1 
ATOM   5018 C  CD    . LYS A 1 795 ? 126.479 90.641  111.780 1.00 46.15  ? 2586 LYS A CD    1 
ATOM   5019 C  CE    . LYS A 1 795 ? 125.779 89.317  112.037 1.00 48.39  ? 2586 LYS A CE    1 
ATOM   5020 N  NZ    . LYS A 1 795 ? 126.576 88.158  111.550 1.00 45.84  ? 2586 LYS A NZ    1 
ATOM   5021 N  N     . ASP A 1 796 ? 127.764 95.267  110.220 1.00 43.19  ? 2587 ASP A N     1 
ATOM   5022 C  CA    . ASP A 1 796 ? 128.374 96.520  109.807 1.00 45.69  ? 2587 ASP A CA    1 
ATOM   5023 C  C     . ASP A 1 796 ? 129.533 96.274  108.848 1.00 42.34  ? 2587 ASP A C     1 
ATOM   5024 O  O     . ASP A 1 796 ? 130.263 95.286  108.956 1.00 42.84  ? 2587 ASP A O     1 
ATOM   5025 C  CB    . ASP A 1 796 ? 128.863 97.302  111.026 1.00 45.33  ? 2587 ASP A CB    1 
ATOM   5026 C  CG    . ASP A 1 796 ? 128.596 98.789  110.909 1.00 53.15  ? 2587 ASP A CG    1 
ATOM   5027 O  OD1   . ASP A 1 796 ? 128.777 99.341  109.804 1.00 53.32  ? 2587 ASP A OD1   1 
ATOM   5028 O  OD2   . ASP A 1 796 ? 128.203 99.405  111.921 1.00 50.28  ? 2587 ASP A OD2   1 
ATOM   5029 N  N     . PHE A 1 797 ? 129.688 97.189  107.895 1.00 45.20  ? 2588 PHE A N     1 
ATOM   5030 C  CA    . PHE A 1 797 ? 130.760 97.137  106.910 1.00 49.43  ? 2588 PHE A CA    1 
ATOM   5031 C  C     . PHE A 1 797 ? 131.356 98.531  106.806 1.00 57.38  ? 2588 PHE A C     1 
ATOM   5032 O  O     . PHE A 1 797 ? 130.649 99.487  106.469 1.00 56.81  ? 2588 PHE A O     1 
ATOM   5033 C  CB    . PHE A 1 797 ? 130.233 96.629  105.559 1.00 48.10  ? 2588 PHE A CB    1 
ATOM   5034 C  CG    . PHE A 1 797 ? 131.142 96.897  104.383 1.00 52.35  ? 2588 PHE A CG    1 
ATOM   5035 C  CD1   . PHE A 1 797 ? 131.178 98.140  103.766 1.00 61.10  ? 2588 PHE A CD1   1 
ATOM   5036 C  CD2   . PHE A 1 797 ? 131.956 95.892  103.889 1.00 55.17  ? 2588 PHE A CD2   1 
ATOM   5037 C  CE1   . PHE A 1 797 ? 132.009 98.372  102.689 1.00 69.17  ? 2588 PHE A CE1   1 
ATOM   5038 C  CE2   . PHE A 1 797 ? 132.788 96.119  102.810 1.00 68.17  ? 2588 PHE A CE2   1 
ATOM   5039 C  CZ    . PHE A 1 797 ? 132.815 97.361  102.210 1.00 70.54  ? 2588 PHE A CZ    1 
ATOM   5040 N  N     . ASP A 1 798 ? 132.648 98.648  107.108 1.00 63.06  ? 2589 ASP A N     1 
ATOM   5041 C  CA    . ASP A 1 798 ? 133.333 99.935  107.122 1.00 68.09  ? 2589 ASP A CA    1 
ATOM   5042 C  C     . ASP A 1 798 ? 134.546 99.966  106.204 1.00 69.59  ? 2589 ASP A C     1 
ATOM   5043 O  O     . ASP A 1 798 ? 135.320 100.930 106.250 1.00 72.71  ? 2589 ASP A O     1 
ATOM   5044 C  CB    . ASP A 1 798 ? 133.747 100.299 108.552 1.00 70.13  ? 2589 ASP A CB    1 
ATOM   5045 C  CG    . ASP A 1 798 ? 134.254 99.103  109.337 1.00 73.06  ? 2589 ASP A CG    1 
ATOM   5046 O  OD1   . ASP A 1 798 ? 134.922 98.232  108.742 1.00 70.35  ? 2589 ASP A OD1   1 
ATOM   5047 O  OD2   . ASP A 1 798 ? 133.980 99.034  110.554 1.00 79.74  ? 2589 ASP A OD2   1 
ATOM   5048 N  N     . VAL A 1 799 ? 134.735 98.946  105.374 1.00 69.91  ? 2590 VAL A N     1 
ATOM   5049 C  CA    . VAL A 1 799 ? 135.870 98.902  104.463 1.00 76.14  ? 2590 VAL A CA    1 
ATOM   5050 C  C     . VAL A 1 799 ? 135.680 99.916  103.340 1.00 70.30  ? 2590 VAL A C     1 
ATOM   5051 O  O     . VAL A 1 799 ? 134.554 100.258 102.980 1.00 57.73  ? 2590 VAL A O     1 
ATOM   5052 C  CB    . VAL A 1 799 ? 136.070 97.486  103.894 1.00 72.37  ? 2590 VAL A CB    1 
ATOM   5053 C  CG1   . VAL A 1 799 ? 137.468 97.339  103.311 1.00 70.26  ? 2590 VAL A CG1   1 
ATOM   5054 C  CG2   . VAL A 1 799 ? 135.822 96.442  104.972 1.00 61.79  ? 2590 VAL A CG2   1 
ATOM   5055 O  OXT   . VAL A 1 799 ? 136.646 100.420 102.767 1.00 72.15  ? 2590 VAL A OXT   1 
ATOM   5056 P  P     . DC  B 2 15  ? 89.192  107.753 118.359 1.00 155.50 ? 15   DC  C P     1 
ATOM   5057 O  OP1   . DC  B 2 15  ? 88.514  108.539 119.414 1.00 157.78 ? 15   DC  C OP1   1 
ATOM   5058 O  OP2   . DC  B 2 15  ? 90.117  108.427 117.421 1.00 145.38 ? 15   DC  C OP2   1 
ATOM   5059 O  "O5'" . DC  B 2 15  ? 89.986  106.546 119.046 1.00 147.42 ? 15   DC  C "O5'" 1 
ATOM   5060 C  "C5'" . DC  B 2 15  ? 89.366  105.779 120.073 1.00 145.78 ? 15   DC  C "C5'" 1 
ATOM   5061 C  "C4'" . DC  B 2 15  ? 90.055  104.435 120.242 1.00 139.09 ? 15   DC  C "C4'" 1 
ATOM   5062 O  "O4'" . DC  B 2 15  ? 90.020  103.710 118.984 1.00 139.28 ? 15   DC  C "O4'" 1 
ATOM   5063 C  "C3'" . DC  B 2 15  ? 91.528  104.500 120.647 1.00 130.98 ? 15   DC  C "C3'" 1 
ATOM   5064 O  "O3'" . DC  B 2 15  ? 91.830  103.435 121.542 1.00 130.10 ? 15   DC  C "O3'" 1 
ATOM   5065 C  "C2'" . DC  B 2 15  ? 92.250  104.329 119.316 1.00 124.90 ? 15   DC  C "C2'" 1 
ATOM   5066 C  "C1'" . DC  B 2 15  ? 91.331  103.345 118.612 1.00 128.20 ? 15   DC  C "C1'" 1 
ATOM   5067 N  N1    . DC  B 2 15  ? 91.430  103.392 117.131 1.00 132.20 ? 15   DC  C N1    1 
ATOM   5068 C  C2    . DC  B 2 15  ? 91.901  102.276 116.438 1.00 129.60 ? 15   DC  C C2    1 
ATOM   5069 O  O2    . DC  B 2 15  ? 92.230  101.268 117.075 1.00 125.25 ? 15   DC  C O2    1 
ATOM   5070 N  N3    . DC  B 2 15  ? 91.985  102.327 115.087 1.00 128.36 ? 15   DC  C N3    1 
ATOM   5071 C  C4    . DC  B 2 15  ? 91.621  103.435 114.439 1.00 130.71 ? 15   DC  C C4    1 
ATOM   5072 N  N4    . DC  B 2 15  ? 91.720  103.442 113.107 1.00 128.86 ? 15   DC  C N4    1 
ATOM   5073 C  C5    . DC  B 2 15  ? 91.138  104.585 115.130 1.00 137.48 ? 15   DC  C C5    1 
ATOM   5074 C  C6    . DC  B 2 15  ? 91.058  104.519 116.462 1.00 136.34 ? 15   DC  C C6    1 
ATOM   5075 P  P     . DG  B 2 16  ? 93.129  103.513 122.484 1.00 134.03 ? 16   DG  C P     1 
ATOM   5076 O  OP1   . DG  B 2 16  ? 92.679  103.316 123.879 1.00 122.09 ? 16   DG  C OP1   1 
ATOM   5077 O  OP2   . DG  B 2 16  ? 93.880  104.734 122.117 1.00 133.00 ? 16   DG  C OP2   1 
ATOM   5078 O  "O5'" . DG  B 2 16  ? 94.005  102.248 122.042 1.00 125.30 ? 16   DG  C "O5'" 1 
ATOM   5079 C  "C5'" . DG  B 2 16  ? 93.566  100.931 122.361 1.00 119.06 ? 16   DG  C "C5'" 1 
ATOM   5080 C  "C4'" . DG  B 2 16  ? 94.522  99.883  121.811 1.00 107.74 ? 16   DG  C "C4'" 1 
ATOM   5081 O  "O4'" . DG  B 2 16  ? 94.416  99.833  120.364 1.00 107.14 ? 16   DG  C "O4'" 1 
ATOM   5082 C  "C3'" . DG  B 2 16  ? 95.998  100.119 122.118 1.00 99.64  ? 16   DG  C "C3'" 1 
ATOM   5083 O  "O3'" . DG  B 2 16  ? 96.645  98.876  122.350 1.00 92.20  ? 16   DG  C "O3'" 1 
ATOM   5084 C  "C2'" . DG  B 2 16  ? 96.510  100.787 120.846 1.00 102.16 ? 16   DG  C "C2'" 1 
ATOM   5085 C  "C1'" . DG  B 2 16  ? 95.673  100.102 119.775 1.00 105.02 ? 16   DG  C "C1'" 1 
ATOM   5086 N  N9    . DG  B 2 16  ? 95.445  100.927 118.592 1.00 107.31 ? 16   DG  C N9    1 
ATOM   5087 C  C8    . DG  B 2 16  ? 94.918  102.195 118.560 1.00 111.48 ? 16   DG  C C8    1 
ATOM   5088 N  N7    . DG  B 2 16  ? 94.818  102.686 117.356 1.00 112.75 ? 16   DG  C N7    1 
ATOM   5089 C  C5    . DG  B 2 16  ? 95.299  101.675 116.535 1.00 106.78 ? 16   DG  C C5    1 
ATOM   5090 C  C6    . DG  B 2 16  ? 95.431  101.633 115.127 1.00 101.95 ? 16   DG  C C6    1 
ATOM   5091 O  O6    . DG  B 2 16  ? 95.138  102.511 114.304 1.00 96.20  ? 16   DG  C O6    1 
ATOM   5092 N  N1    . DG  B 2 16  ? 95.964  100.420 114.695 1.00 103.66 ? 16   DG  C N1    1 
ATOM   5093 C  C2    . DG  B 2 16  ? 96.323  99.382  115.523 1.00 105.28 ? 16   DG  C C2    1 
ATOM   5094 N  N2    . DG  B 2 16  ? 96.821  98.290  114.927 1.00 100.92 ? 16   DG  C N2    1 
ATOM   5095 N  N3    . DG  B 2 16  ? 96.204  99.411  116.845 1.00 105.16 ? 16   DG  C N3    1 
ATOM   5096 C  C4    . DG  B 2 16  ? 95.687  100.584 117.279 1.00 104.93 ? 16   DG  C C4    1 
ATOM   5097 P  P     . DT  B 2 17  ? 98.138  98.837  122.939 1.00 85.32  ? 17   DT  C P     1 
ATOM   5098 O  OP1   . DT  B 2 17  ? 98.210  97.714  123.900 1.00 94.42  ? 17   DT  C OP1   1 
ATOM   5099 O  OP2   . DT  B 2 17  ? 98.493  100.206 123.372 1.00 86.01  ? 17   DT  C OP2   1 
ATOM   5100 O  "O5'" . DT  B 2 17  ? 99.039  98.476  121.671 1.00 83.32  ? 17   DT  C "O5'" 1 
ATOM   5101 C  "C5'" . DT  B 2 17  ? 98.838  97.248  120.985 1.00 82.30  ? 17   DT  C "C5'" 1 
ATOM   5102 C  "C4'" . DT  B 2 17  ? 99.702  97.182  119.740 1.00 80.02  ? 17   DT  C "C4'" 1 
ATOM   5103 O  "O4'" . DT  B 2 17  ? 99.129  98.026  118.706 1.00 82.95  ? 17   DT  C "O4'" 1 
ATOM   5104 C  "C3'" . DT  B 2 17  ? 101.145 97.661  119.934 1.00 70.64  ? 17   DT  C "C3'" 1 
ATOM   5105 O  "O3'" . DT  B 2 17  ? 102.058 96.714  119.388 1.00 66.00  ? 17   DT  C "O3'" 1 
ATOM   5106 C  "C2'" . DT  B 2 17  ? 101.188 98.987  119.175 1.00 71.16  ? 17   DT  C "C2'" 1 
ATOM   5107 C  "C1'" . DT  B 2 17  ? 100.163 98.740  118.083 1.00 77.00  ? 17   DT  C "C1'" 1 
ATOM   5108 N  N1    . DT  B 2 17  ? 99.609  99.992  117.491 1.00 83.28  ? 17   DT  C N1    1 
ATOM   5109 C  C2    . DT  B 2 17  ? 99.597  100.138 116.126 1.00 83.44  ? 17   DT  C C2    1 
ATOM   5110 O  O2    . DT  B 2 17  ? 100.010 99.286  115.361 1.00 78.26  ? 17   DT  C O2    1 
ATOM   5111 N  N3    . DT  B 2 17  ? 99.080  101.324 115.681 1.00 87.51  ? 17   DT  C N3    1 
ATOM   5112 C  C4    . DT  B 2 17  ? 98.585  102.360 116.447 1.00 88.51  ? 17   DT  C C4    1 
ATOM   5113 O  O4    . DT  B 2 17  ? 98.139  103.389 115.950 1.00 92.72  ? 17   DT  C O4    1 
ATOM   5114 C  C5    . DT  B 2 17  ? 98.630  102.147 117.873 1.00 87.91  ? 17   DT  C C5    1 
ATOM   5115 C  C7    . DT  B 2 17  ? 98.123  103.206 118.806 1.00 91.02  ? 17   DT  C C7    1 
ATOM   5116 C  C6    . DT  B 2 17  ? 99.136  100.987 118.322 1.00 87.27  ? 17   DT  C C6    1 
ATOM   5117 P  P     . DA  B 2 18  ? 103.586 96.686  119.888 1.00 73.22  ? 18   DA  C P     1 
ATOM   5118 O  OP1   . DA  B 2 18  ? 103.839 95.359  120.487 1.00 68.85  ? 18   DA  C OP1   1 
ATOM   5119 O  OP2   . DA  B 2 18  ? 103.818 97.906  120.691 1.00 64.96  ? 18   DA  C OP2   1 
ATOM   5120 O  "O5'" . DA  B 2 18  ? 104.440 96.816  118.541 1.00 75.28  ? 18   DA  C "O5'" 1 
ATOM   5121 C  "C5'" . DA  B 2 18  ? 104.475 95.737  117.615 1.00 60.55  ? 18   DA  C "C5'" 1 
ATOM   5122 C  "C4'" . DA  B 2 18  ? 104.968 96.199  116.253 1.00 53.31  ? 18   DA  C "C4'" 1 
ATOM   5123 O  "O4'" . DA  B 2 18  ? 103.867 96.763  115.501 1.00 57.34  ? 18   DA  C "O4'" 1 
ATOM   5124 C  "C3'" . DA  B 2 18  ? 106.016 97.296  116.280 1.00 50.85  ? 18   DA  C "C3'" 1 
ATOM   5125 O  "O3'" . DA  B 2 18  ? 107.306 96.740  116.429 1.00 51.23  ? 18   DA  C "O3'" 1 
ATOM   5126 C  "C2'" . DA  B 2 18  ? 105.842 97.917  114.904 1.00 50.55  ? 18   DA  C "C2'" 1 
ATOM   5127 C  "C1'" . DA  B 2 18  ? 104.330 97.859  114.728 1.00 55.02  ? 18   DA  C "C1'" 1 
ATOM   5128 N  N9    . DA  B 2 18  ? 103.651 99.068  115.181 1.00 56.27  ? 18   DA  C N9    1 
ATOM   5129 C  C8    . DA  B 2 18  ? 103.182 99.329  116.435 1.00 61.41  ? 18   DA  C C8    1 
ATOM   5130 N  N7    . DA  B 2 18  ? 102.612 100.503 116.553 1.00 62.18  ? 18   DA  C N7    1 
ATOM   5131 C  C5    . DA  B 2 18  ? 102.716 101.050 115.288 1.00 60.45  ? 18   DA  C C5    1 
ATOM   5132 C  C6    . DA  B 2 18  ? 102.302 102.284 114.752 1.00 65.46  ? 18   DA  C C6    1 
ATOM   5133 N  N6    . DA  B 2 18  ? 101.672 103.220 115.467 1.00 64.48  ? 18   DA  C N6    1 
ATOM   5134 N  N1    . DA  B 2 18  ? 102.562 102.519 113.448 1.00 69.03  ? 18   DA  C N1    1 
ATOM   5135 C  C2    . DA  B 2 18  ? 103.193 101.578 112.740 1.00 67.75  ? 18   DA  C C2    1 
ATOM   5136 N  N3    . DA  B 2 18  ? 103.627 100.382 113.133 1.00 66.64  ? 18   DA  C N3    1 
ATOM   5137 C  C4    . DA  B 2 18  ? 103.355 100.180 114.430 1.00 60.36  ? 18   DA  C C4    1 
ATOM   5138 P  P     . DG  B 2 19  ? 108.536 97.678  116.859 1.00 57.39  ? 19   DG  C P     1 
ATOM   5139 O  OP1   . DG  B 2 19  ? 109.636 96.788  117.279 1.00 52.92  ? 19   DG  C OP1   1 
ATOM   5140 O  OP2   . DG  B 2 19  ? 108.018 98.696  117.798 1.00 58.96  ? 19   DG  C OP2   1 
ATOM   5141 O  "O5'" . DG  B 2 19  ? 108.945 98.431  115.508 1.00 42.74  ? 19   DG  C "O5'" 1 
ATOM   5142 C  "C5'" . DG  B 2 19  ? 109.410 97.685  114.389 1.00 43.52  ? 19   DG  C "C5'" 1 
ATOM   5143 C  "C4'" . DG  B 2 19  ? 109.427 98.542  113.133 1.00 45.30  ? 19   DG  C "C4'" 1 
ATOM   5144 O  "O4'" . DG  B 2 19  ? 108.093 99.032  112.864 1.00 50.92  ? 19   DG  C "O4'" 1 
ATOM   5145 C  "C3'" . DG  B 2 19  ? 110.290 99.789  113.210 1.00 37.16  ? 19   DG  C "C3'" 1 
ATOM   5146 O  "O3'" . DG  B 2 19  ? 111.628 99.477  112.861 1.00 35.23  ? 19   DG  C "O3'" 1 
ATOM   5147 C  "C2'" . DG  B 2 19  ? 109.641 100.685 112.164 1.00 36.82  ? 19   DG  C "C2'" 1 
ATOM   5148 C  "C1'" . DG  B 2 19  ? 108.163 100.338 112.317 1.00 43.48  ? 19   DG  C "C1'" 1 
ATOM   5149 N  N9    . DG  B 2 19  ? 107.438 101.250 113.193 1.00 51.66  ? 19   DG  C N9    1 
ATOM   5150 C  C8    . DG  B 2 19  ? 107.086 101.036 114.501 1.00 54.63  ? 19   DG  C C8    1 
ATOM   5151 N  N7    . DG  B 2 19  ? 106.437 102.032 115.033 1.00 49.67  ? 19   DG  C N7    1 
ATOM   5152 C  C5    . DG  B 2 19  ? 106.357 102.967 114.013 1.00 47.88  ? 19   DG  C C5    1 
ATOM   5153 C  C6    . DG  B 2 19  ? 105.766 104.249 114.000 1.00 51.41  ? 19   DG  C C6    1 
ATOM   5154 O  O6    . DG  B 2 19  ? 105.177 104.827 114.922 1.00 56.23  ? 19   DG  C O6    1 
ATOM   5155 N  N1    . DG  B 2 19  ? 105.906 104.869 112.762 1.00 54.86  ? 19   DG  C N1    1 
ATOM   5156 C  C2    . DG  B 2 19  ? 106.540 104.316 111.676 1.00 55.09  ? 19   DG  C C2    1 
ATOM   5157 N  N2    . DG  B 2 19  ? 106.579 105.062 110.563 1.00 58.85  ? 19   DG  C N2    1 
ATOM   5158 N  N3    . DG  B 2 19  ? 107.098 103.114 111.677 1.00 50.03  ? 19   DG  C N3    1 
ATOM   5159 C  C4    . DG  B 2 19  ? 106.968 102.500 112.874 1.00 47.78  ? 19   DG  C C4    1 
HETATM 5160 N  N1    . DOC B 2 20  ? 110.462 104.858 112.968 1.00 40.40  ? 20   DOC C N1    1 
HETATM 5161 C  C2    . DOC B 2 20  ? 109.723 105.985 113.423 1.00 39.13  ? 20   DOC C C2    1 
HETATM 5162 N  N3    . DOC B 2 20  ? 109.251 106.064 114.694 1.00 39.28  ? 20   DOC C N3    1 
HETATM 5163 C  C4    . DOC B 2 20  ? 109.480 105.059 115.549 1.00 46.82  ? 20   DOC C C4    1 
HETATM 5164 C  C5    . DOC B 2 20  ? 110.235 103.889 115.113 1.00 47.58  ? 20   DOC C C5    1 
HETATM 5165 C  C6    . DOC B 2 20  ? 110.700 103.815 113.852 1.00 45.64  ? 20   DOC C C6    1 
HETATM 5166 O  O2    . DOC B 2 20  ? 109.543 106.872 112.599 1.00 37.32  ? 20   DOC C O2    1 
HETATM 5167 N  N4    . DOC B 2 20  ? 109.005 105.172 116.782 1.00 57.30  ? 20   DOC C N4    1 
HETATM 5168 C  "C1'" . DOC B 2 20  ? 110.924 104.876 111.569 1.00 31.59  ? 20   DOC C "C1'" 1 
HETATM 5169 C  "C2'" . DOC B 2 20  ? 112.269 105.519 111.419 1.00 31.77  ? 20   DOC C "C2'" 1 
HETATM 5170 C  "C3'" . DOC B 2 20  ? 113.212 104.333 111.428 1.00 26.44  ? 20   DOC C "C3'" 1 
HETATM 5171 C  "C4'" . DOC B 2 20  ? 112.438 103.249 110.731 1.00 28.45  ? 20   DOC C "C4'" 1 
HETATM 5172 O  "O4'" . DOC B 2 20  ? 111.081 103.521 111.157 1.00 34.42  ? 20   DOC C "O4'" 1 
HETATM 5173 C  "C5'" . DOC B 2 20  ? 112.872 101.917 111.246 1.00 32.11  ? 20   DOC C "C5'" 1 
HETATM 5174 O  "O5'" . DOC B 2 20  ? 112.630 101.756 112.649 1.00 32.06  ? 20   DOC C "O5'" 1 
HETATM 5175 P  P     . DOC B 2 20  ? 112.735 100.261 113.628 1.00 44.49  ? 20   DOC C P     1 
HETATM 5176 O  OP1   . DOC B 2 20  ? 114.131 99.751  113.502 1.00 42.54  ? 20   DOC C OP1   1 
HETATM 5177 O  OP2   . DOC B 2 20  ? 112.208 100.496 115.005 1.00 52.26  ? 20   DOC C OP2   1 
ATOM   5178 P  P     . DA  C 3 7   ? 88.114  111.612 124.892 1.00 146.28 ? 7    DA  D P     1 
ATOM   5179 O  OP1   . DA  C 3 7   ? 87.642  110.517 125.768 1.00 143.31 ? 7    DA  D OP1   1 
ATOM   5180 O  OP2   . DA  C 3 7   ? 87.265  112.805 124.676 1.00 141.88 ? 7    DA  D OP2   1 
ATOM   5181 O  "O5'" . DA  C 3 7   ? 89.546  112.112 125.403 1.00 145.42 ? 7    DA  D "O5'" 1 
ATOM   5182 C  "C5'" . DA  C 3 7   ? 90.680  111.256 125.295 1.00 141.41 ? 7    DA  D "C5'" 1 
ATOM   5183 C  "C4'" . DA  C 3 7   ? 91.446  111.529 124.012 1.00 143.22 ? 7    DA  D "C4'" 1 
ATOM   5184 O  "O4'" . DA  C 3 7   ? 90.629  112.313 123.122 1.00 145.77 ? 7    DA  D "O4'" 1 
ATOM   5185 C  "C3'" . DA  C 3 7   ? 92.712  112.346 124.185 1.00 140.56 ? 7    DA  D "C3'" 1 
ATOM   5186 O  "O3'" . DA  C 3 7   ? 93.797  111.491 124.517 1.00 143.48 ? 7    DA  D "O3'" 1 
ATOM   5187 C  "C2'" . DA  C 3 7   ? 92.896  112.976 122.802 1.00 135.09 ? 7    DA  D "C2'" 1 
ATOM   5188 C  "C1'" . DA  C 3 7   ? 91.461  113.066 122.261 1.00 138.76 ? 7    DA  D "C1'" 1 
ATOM   5189 N  N9    . DA  C 3 7   ? 90.942  114.431 122.184 1.00 138.59 ? 7    DA  D N9    1 
ATOM   5190 C  C8    . DA  C 3 7   ? 90.529  115.088 121.059 1.00 131.31 ? 7    DA  D C8    1 
ATOM   5191 N  N7    . DA  C 3 7   ? 90.108  116.310 121.283 1.00 131.40 ? 7    DA  D N7    1 
ATOM   5192 C  C5    . DA  C 3 7   ? 90.256  116.468 122.650 1.00 135.90 ? 7    DA  D C5    1 
ATOM   5193 C  C6    . DA  C 3 7   ? 89.986  117.547 123.515 1.00 129.97 ? 7    DA  D C6    1 
ATOM   5194 N  N6    . DA  C 3 7   ? 89.489  118.716 123.100 1.00 121.29 ? 7    DA  D N6    1 
ATOM   5195 N  N1    . DA  C 3 7   ? 90.247  117.377 124.828 1.00 134.51 ? 7    DA  D N1    1 
ATOM   5196 C  C2    . DA  C 3 7   ? 90.745  116.206 125.240 1.00 134.85 ? 7    DA  D C2    1 
ATOM   5197 N  N3    . DA  C 3 7   ? 91.039  115.122 124.523 1.00 139.61 ? 7    DA  D N3    1 
ATOM   5198 C  C4    . DA  C 3 7   ? 90.768  115.320 123.224 1.00 139.75 ? 7    DA  D C4    1 
ATOM   5199 P  P     . DG  C 3 8   ? 94.847  111.920 125.655 1.00 143.22 ? 8    DG  D P     1 
ATOM   5200 O  OP1   . DG  C 3 8   ? 95.550  110.698 126.103 1.00 136.75 ? 8    DG  D OP1   1 
ATOM   5201 O  OP2   . DG  C 3 8   ? 94.124  112.758 126.638 1.00 139.29 ? 8    DG  D OP2   1 
ATOM   5202 O  "O5'" . DG  C 3 8   ? 95.904  112.836 124.880 1.00 128.62 ? 8    DG  D "O5'" 1 
ATOM   5203 C  "C5'" . DG  C 3 8   ? 97.094  113.256 125.536 1.00 120.64 ? 8    DG  D "C5'" 1 
ATOM   5204 C  "C4'" . DG  C 3 8   ? 98.092  113.811 124.537 1.00 106.09 ? 8    DG  D "C4'" 1 
ATOM   5205 O  "O4'" . DG  C 3 8   ? 97.616  115.087 124.037 1.00 105.47 ? 8    DG  D "O4'" 1 
ATOM   5206 C  "C3'" . DG  C 3 8   ? 99.474  114.094 125.104 1.00 89.12  ? 8    DG  D "C3'" 1 
ATOM   5207 O  "O3'" . DG  C 3 8   ? 100.439 114.003 124.074 1.00 79.30  ? 8    DG  D "O3'" 1 
ATOM   5208 C  "C2'" . DG  C 3 8   ? 99.326  115.526 125.594 1.00 89.91  ? 8    DG  D "C2'" 1 
ATOM   5209 C  "C1'" . DG  C 3 8   ? 98.466  116.125 124.490 1.00 96.38  ? 8    DG  D "C1'" 1 
ATOM   5210 N  N9    . DG  C 3 8   ? 97.637  117.237 124.938 1.00 105.87 ? 8    DG  D N9    1 
ATOM   5211 C  C8    . DG  C 3 8   ? 96.280  117.224 125.149 1.00 105.89 ? 8    DG  D C8    1 
ATOM   5212 N  N7    . DG  C 3 8   ? 95.806  118.371 125.550 1.00 102.58 ? 8    DG  D N7    1 
ATOM   5213 C  C5    . DG  C 3 8   ? 96.921  119.197 125.610 1.00 106.19 ? 8    DG  D C5    1 
ATOM   5214 C  C6    . DG  C 3 8   ? 97.027  120.557 125.981 1.00 103.91 ? 8    DG  D C6    1 
ATOM   5215 O  O6    . DG  C 3 8   ? 96.127  121.327 126.343 1.00 99.21  ? 8    DG  D O6    1 
ATOM   5216 N  N1    . DG  C 3 8   ? 98.341  121.011 125.903 1.00 104.79 ? 8    DG  D N1    1 
ATOM   5217 C  C2    . DG  C 3 8   ? 99.415  120.246 125.515 1.00 103.35 ? 8    DG  D C2    1 
ATOM   5218 N  N2    . DG  C 3 8   ? 100.607 120.859 125.502 1.00 104.01 ? 8    DG  D N2    1 
ATOM   5219 N  N3    . DG  C 3 8   ? 99.329  118.970 125.165 1.00 102.89 ? 8    DG  D N3    1 
ATOM   5220 C  C4    . DG  C 3 8   ? 98.056  118.513 125.236 1.00 106.98 ? 8    DG  D C4    1 
ATOM   5221 P  P     . DT  C 3 9   ? 101.949 113.582 124.415 1.00 73.29  ? 9    DT  D P     1 
ATOM   5222 O  OP1   . DT  C 3 9   ? 101.986 112.113 124.582 1.00 73.14  ? 9    DT  D OP1   1 
ATOM   5223 O  OP2   . DT  C 3 9   ? 102.430 114.460 125.502 1.00 66.34  ? 9    DT  D OP2   1 
ATOM   5224 O  "O5'" . DT  C 3 9   ? 102.753 113.963 123.091 1.00 65.35  ? 9    DT  D "O5'" 1 
ATOM   5225 C  "C5'" . DT  C 3 9   ? 104.115 113.614 122.971 1.00 61.31  ? 9    DT  D "C5'" 1 
ATOM   5226 C  "C4'" . DT  C 3 9   ? 104.636 113.951 121.589 1.00 55.54  ? 9    DT  D "C4'" 1 
ATOM   5227 O  "O4'" . DT  C 3 9   ? 106.008 113.518 121.482 1.00 59.30  ? 9    DT  D "O4'" 1 
ATOM   5228 C  "C3'" . DT  C 3 9   ? 103.899 113.269 120.452 1.00 47.35  ? 9    DT  D "C3'" 1 
ATOM   5229 O  "O3'" . DT  C 3 9   ? 102.840 114.108 120.009 1.00 50.51  ? 9    DT  D "O3'" 1 
ATOM   5230 C  "C2'" . DT  C 3 9   ? 104.975 113.127 119.382 1.00 47.27  ? 9    DT  D "C2'" 1 
ATOM   5231 C  "C1'" . DT  C 3 9   ? 106.265 113.016 120.188 1.00 49.93  ? 9    DT  D "C1'" 1 
ATOM   5232 N  N1    . DT  C 3 9   ? 106.790 111.629 120.320 1.00 44.90  ? 9    DT  D N1    1 
ATOM   5233 C  C2    . DT  C 3 9   ? 107.554 111.098 119.309 1.00 40.54  ? 9    DT  D C2    1 
ATOM   5234 O  O2    . DT  C 3 9   ? 107.816 111.697 118.284 1.00 42.58  ? 9    DT  D O2    1 
ATOM   5235 N  N3    . DT  C 3 9   ? 108.000 109.826 119.538 1.00 39.57  ? 9    DT  D N3    1 
ATOM   5236 C  C4    . DT  C 3 9   ? 107.767 109.051 120.656 1.00 57.99  ? 9    DT  D C4    1 
ATOM   5237 O  O4    . DT  C 3 9   ? 108.212 107.914 120.771 1.00 64.28  ? 9    DT  D O4    1 
ATOM   5238 C  C5    . DT  C 3 9   ? 106.965 109.671 121.681 1.00 68.41  ? 9    DT  D C5    1 
ATOM   5239 C  C7    . DT  C 3 9   ? 106.645 108.926 122.941 1.00 77.69  ? 9    DT  D C7    1 
ATOM   5240 C  C6    . DT  C 3 9   ? 106.523 110.916 121.466 1.00 57.16  ? 9    DT  D C6    1 
ATOM   5241 P  P     . DG  C 3 10  ? 101.721 113.562 118.994 1.00 64.50  ? 10   DG  D P     1 
ATOM   5242 O  OP1   . DG  C 3 10  ? 100.589 114.512 119.027 1.00 60.84  ? 10   DG  D OP1   1 
ATOM   5243 O  OP2   . DG  C 3 10  ? 101.496 112.129 119.286 1.00 68.31  ? 10   DG  D OP2   1 
ATOM   5244 O  "O5'" . DG  C 3 10  ? 102.416 113.663 117.560 1.00 46.41  ? 10   DG  D "O5'" 1 
ATOM   5245 C  "C5'" . DG  C 3 10  ? 102.974 114.894 117.120 1.00 47.08  ? 10   DG  D "C5'" 1 
ATOM   5246 C  "C4'" . DG  C 3 10  ? 103.835 114.672 115.893 1.00 42.29  ? 10   DG  D "C4'" 1 
ATOM   5247 O  "O4'" . DG  C 3 10  ? 104.858 113.684 116.199 1.00 38.74  ? 10   DG  D "O4'" 1 
ATOM   5248 C  "C3'" . DG  C 3 10  ? 103.078 114.133 114.677 1.00 48.05  ? 10   DG  D "C3'" 1 
ATOM   5249 O  "O3'" . DG  C 3 10  ? 103.535 114.758 113.488 1.00 47.45  ? 10   DG  D "O3'" 1 
ATOM   5250 C  "C2'" . DG  C 3 10  ? 103.418 112.650 114.689 1.00 46.29  ? 10   DG  D "C2'" 1 
ATOM   5251 C  "C1'" . DG  C 3 10  ? 104.840 112.680 115.213 1.00 37.95  ? 10   DG  D "C1'" 1 
ATOM   5252 N  N9    . DG  C 3 10  ? 105.271 111.417 115.797 1.00 35.50  ? 10   DG  D N9    1 
ATOM   5253 C  C8    . DG  C 3 10  ? 104.932 110.912 117.025 1.00 42.84  ? 10   DG  D C8    1 
ATOM   5254 N  N7    . DG  C 3 10  ? 105.459 109.749 117.273 1.00 49.17  ? 10   DG  D N7    1 
ATOM   5255 C  C5    . DG  C 3 10  ? 106.187 109.457 116.130 1.00 45.25  ? 10   DG  D C5    1 
ATOM   5256 C  C6    . DG  C 3 10  ? 106.970 108.326 115.816 1.00 49.95  ? 10   DG  D C6    1 
ATOM   5257 O  O6    . DG  C 3 10  ? 107.182 107.324 116.511 1.00 56.87  ? 10   DG  D O6    1 
ATOM   5258 N  N1    . DG  C 3 10  ? 107.540 108.428 114.551 1.00 46.58  ? 10   DG  D N1    1 
ATOM   5259 C  C2    . DG  C 3 10  ? 107.372 109.491 113.699 1.00 44.47  ? 10   DG  D C2    1 
ATOM   5260 N  N2    . DG  C 3 10  ? 108.001 109.411 112.519 1.00 45.82  ? 10   DG  D N2    1 
ATOM   5261 N  N3    . DG  C 3 10  ? 106.640 110.559 113.983 1.00 37.96  ? 10   DG  D N3    1 
ATOM   5262 C  C4    . DG  C 3 10  ? 106.083 110.475 115.213 1.00 37.12  ? 10   DG  D C4    1 
ATOM   5263 P  P     . DC  C 3 11  ? 102.657 114.660 112.146 1.00 51.00  ? 11   DC  D P     1 
ATOM   5264 O  OP1   . DC  C 3 11  ? 103.042 115.779 111.261 1.00 50.73  ? 11   DC  D OP1   1 
ATOM   5265 O  OP2   . DC  C 3 11  ? 101.246 114.476 112.544 1.00 34.90  ? 11   DC  D OP2   1 
ATOM   5266 O  "O5'" . DC  C 3 11  ? 103.138 113.301 111.463 1.00 40.58  ? 11   DC  D "O5'" 1 
ATOM   5267 C  "C5'" . DC  C 3 11  ? 102.441 112.801 110.335 1.00 37.39  ? 11   DC  D "C5'" 1 
ATOM   5268 C  "C4'" . DC  C 3 11  ? 103.367 112.008 109.434 1.00 35.65  ? 11   DC  D "C4'" 1 
ATOM   5269 O  "O4'" . DC  C 3 11  ? 104.539 111.613 110.183 1.00 33.71  ? 11   DC  D "O4'" 1 
ATOM   5270 C  "C3'" . DC  C 3 11  ? 102.764 110.724 108.888 1.00 36.37  ? 11   DC  D "C3'" 1 
ATOM   5271 O  "O3'" . DC  C 3 11  ? 102.207 110.965 107.612 1.00 36.74  ? 11   DC  D "O3'" 1 
ATOM   5272 C  "C2'" . DC  C 3 11  ? 103.962 109.787 108.799 1.00 39.21  ? 11   DC  D "C2'" 1 
ATOM   5273 C  "C1'" . DC  C 3 11  ? 104.826 110.248 109.961 1.00 35.89  ? 11   DC  D "C1'" 1 
ATOM   5274 N  N1    . DC  C 3 11  ? 104.609 109.508 111.240 1.00 43.47  ? 11   DC  D N1    1 
ATOM   5275 C  C2    . DC  C 3 11  ? 105.159 108.234 111.411 1.00 45.94  ? 11   DC  D C2    1 
ATOM   5276 O  O2    . DC  C 3 11  ? 105.794 107.723 110.482 1.00 46.67  ? 11   DC  D O2    1 
ATOM   5277 N  N3    . DC  C 3 11  ? 104.971 107.593 112.593 1.00 43.98  ? 11   DC  D N3    1 
ATOM   5278 C  C4    . DC  C 3 11  ? 104.280 108.184 113.569 1.00 42.72  ? 11   DC  D C4    1 
ATOM   5279 N  N4    . DC  C 3 11  ? 104.117 107.521 114.717 1.00 45.43  ? 11   DC  D N4    1 
ATOM   5280 C  C5    . DC  C 3 11  ? 103.720 109.480 113.410 1.00 47.33  ? 11   DC  D C5    1 
ATOM   5281 C  C6    . DC  C 3 11  ? 103.916 110.103 112.248 1.00 48.82  ? 11   DC  D C6    1 
ATOM   5282 P  P     . DT  C 3 12  ? 100.615 110.967 107.423 1.00 48.95  ? 12   DT  D P     1 
ATOM   5283 O  OP1   . DT  C 3 12  ? 100.337 110.962 105.972 1.00 44.71  ? 12   DT  D OP1   1 
ATOM   5284 O  OP2   . DT  C 3 12  ? 100.057 112.038 108.276 1.00 49.99  ? 12   DT  D OP2   1 
ATOM   5285 O  "O5'" . DT  C 3 12  ? 100.163 109.566 108.039 1.00 53.28  ? 12   DT  D "O5'" 1 
ATOM   5286 C  "C5'" . DT  C 3 12  ? 99.901  108.470 107.181 1.00 51.12  ? 12   DT  D "C5'" 1 
ATOM   5287 C  "C4'" . DT  C 3 12  ? 101.063 107.495 107.169 1.00 47.25  ? 12   DT  D "C4'" 1 
ATOM   5288 O  "O4'" . DT  C 3 12  ? 101.850 107.668 108.359 1.00 52.88  ? 12   DT  D "O4'" 1 
ATOM   5289 C  "C3'" . DT  C 3 12  ? 100.653 106.041 107.184 1.00 50.70  ? 12   DT  D "C3'" 1 
ATOM   5290 O  "O3'" . DT  C 3 12  ? 100.445 105.603 105.862 1.00 53.12  ? 12   DT  D "O3'" 1 
ATOM   5291 C  "C2'" . DT  C 3 12  ? 101.857 105.351 107.823 1.00 52.58  ? 12   DT  D "C2'" 1 
ATOM   5292 C  "C1'" . DT  C 3 12  ? 102.440 106.438 108.733 1.00 52.93  ? 12   DT  D "C1'" 1 
ATOM   5293 N  N1    . DT  C 3 12  ? 102.189 106.236 110.199 1.00 56.39  ? 12   DT  D N1    1 
ATOM   5294 C  C2    . DT  C 3 12  ? 102.649 105.101 110.834 1.00 54.54  ? 12   DT  D C2    1 
ATOM   5295 O  O2    . DT  C 3 12  ? 103.249 104.206 110.266 1.00 55.39  ? 12   DT  D O2    1 
ATOM   5296 N  N3    . DT  C 3 12  ? 102.372 105.050 112.176 1.00 54.94  ? 12   DT  D N3    1 
ATOM   5297 C  C4    . DT  C 3 12  ? 101.705 105.996 112.930 1.00 58.43  ? 12   DT  D C4    1 
ATOM   5298 O  O4    . DT  C 3 12  ? 101.506 105.859 114.132 1.00 64.18  ? 12   DT  D O4    1 
ATOM   5299 C  C5    . DT  C 3 12  ? 101.261 107.159 112.206 1.00 55.80  ? 12   DT  D C5    1 
ATOM   5300 C  C7    . DT  C 3 12  ? 100.524 108.254 112.918 1.00 57.28  ? 12   DT  D C7    1 
ATOM   5301 C  C6    . DT  C 3 12  ? 101.525 107.222 110.895 1.00 54.92  ? 12   DT  D C6    1 
ATOM   5302 P  P     . DA  C 3 13  ? 98.960  105.273 105.356 1.00 70.27  ? 13   DA  D P     1 
ATOM   5303 O  OP1   . DA  C 3 13  ? 98.848  105.727 103.954 1.00 61.89  ? 13   DA  D OP1   1 
ATOM   5304 O  OP2   . DA  C 3 13  ? 98.020  105.785 106.376 1.00 65.00  ? 13   DA  D OP2   1 
ATOM   5305 O  "O5'" . DA  C 3 13  ? 98.904  103.682 105.394 1.00 68.51  ? 13   DA  D "O5'" 1 
ATOM   5306 C  "C5'" . DA  C 3 13  ? 99.972  102.932 104.845 1.00 65.08  ? 13   DA  D "C5'" 1 
ATOM   5307 C  "C4'" . DA  C 3 13  ? 100.187 101.660 105.634 1.00 62.08  ? 13   DA  D "C4'" 1 
ATOM   5308 O  "O4'" . DA  C 3 13  ? 100.761 101.997 106.911 1.00 63.32  ? 13   DA  D "O4'" 1 
ATOM   5309 C  "C3'" . DA  C 3 13  ? 98.917  100.883 105.933 1.00 61.29  ? 13   DA  D "C3'" 1 
ATOM   5310 O  "O3'" . DA  C 3 13  ? 98.725  99.889  104.936 1.00 61.22  ? 13   DA  D "O3'" 1 
ATOM   5311 C  "C2'" . DA  C 3 13  ? 99.192  100.251 107.294 1.00 67.14  ? 13   DA  D "C2'" 1 
ATOM   5312 C  "C1'" . DA  C 3 13  ? 100.218 101.186 107.928 1.00 64.80  ? 13   DA  D "C1'" 1 
ATOM   5313 N  N9    . DA  C 3 13  ? 99.679  102.056 108.966 1.00 70.97  ? 13   DA  D N9    1 
ATOM   5314 C  C8    . DA  C 3 13  ? 99.128  103.294 108.802 1.00 66.05  ? 13   DA  D C8    1 
ATOM   5315 N  N7    . DA  C 3 13  ? 98.744  103.854 109.924 1.00 65.33  ? 13   DA  D N7    1 
ATOM   5316 C  C5    . DA  C 3 13  ? 99.074  102.920 110.889 1.00 67.28  ? 13   DA  D C5    1 
ATOM   5317 C  C6    . DA  C 3 13  ? 98.926  102.907 112.289 1.00 76.12  ? 13   DA  D C6    1 
ATOM   5318 N  N6    . DA  C 3 13  ? 98.382  103.913 112.981 1.00 79.16  ? 13   DA  D N6    1 
ATOM   5319 N  N1    . DA  C 3 13  ? 99.361  101.816 112.952 1.00 82.56  ? 13   DA  D N1    1 
ATOM   5320 C  C2    . DA  C 3 13  ? 99.904  100.812 112.256 1.00 75.11  ? 13   DA  D C2    1 
ATOM   5321 N  N3    . DA  C 3 13  ? 100.096 100.712 110.945 1.00 70.92  ? 13   DA  D N3    1 
ATOM   5322 C  C4    . DA  C 3 13  ? 99.654  101.808 110.314 1.00 71.13  ? 13   DA  D C4    1 
ATOM   5323 P  P     . DC  C 3 14  ? 97.257  99.314  104.634 1.00 82.84  ? 14   DC  D P     1 
ATOM   5324 O  OP1   . DC  C 3 14  ? 97.332  98.553  103.367 1.00 80.04  ? 14   DC  D OP1   1 
ATOM   5325 O  OP2   . DC  C 3 14  ? 96.301  100.435 104.770 1.00 80.83  ? 14   DC  D OP2   1 
ATOM   5326 O  "O5'" . DC  C 3 14  ? 96.990  98.289  105.831 1.00 89.23  ? 14   DC  D "O5'" 1 
ATOM   5327 C  "C5'" . DC  C 3 14  ? 97.800  97.127  105.970 1.00 86.53  ? 14   DC  D "C5'" 1 
ATOM   5328 C  "C4'" . DC  C 3 14  ? 97.666  96.549  107.366 1.00 83.15  ? 14   DC  D "C4'" 1 
ATOM   5329 O  "O4'" . DC  C 3 14  ? 97.952  97.582  108.326 1.00 86.64  ? 14   DC  D "O4'" 1 
ATOM   5330 C  "C3'" . DC  C 3 14  ? 96.273  96.057  107.717 1.00 91.44  ? 14   DC  D "C3'" 1 
ATOM   5331 O  "O3'" . DC  C 3 14  ? 96.152  94.674  107.393 1.00 99.28  ? 14   DC  D "O3'" 1 
ATOM   5332 C  "C2'" . DC  C 3 14  ? 96.185  96.275  109.228 1.00 97.35  ? 14   DC  D "C2'" 1 
ATOM   5333 C  "C1'" . DC  C 3 14  ? 97.245  97.337  109.520 1.00 95.39  ? 14   DC  D "C1'" 1 
ATOM   5334 N  N1    . DC  C 3 14  ? 96.685  98.632  110.017 1.00 100.74 ? 14   DC  D N1    1 
ATOM   5335 C  C2    . DC  C 3 14  ? 96.534  98.838  111.393 1.00 102.85 ? 14   DC  D C2    1 
ATOM   5336 O  O2    . DC  C 3 14  ? 96.860  97.934  112.172 1.00 104.83 ? 14   DC  D O2    1 
ATOM   5337 N  N3    . DC  C 3 14  ? 96.032  100.020 111.829 1.00 100.09 ? 14   DC  D N3    1 
ATOM   5338 C  C4    . DC  C 3 14  ? 95.695  100.965 110.949 1.00 93.91  ? 14   DC  D C4    1 
ATOM   5339 N  N4    . DC  C 3 14  ? 95.204  102.115 111.420 1.00 95.72  ? 14   DC  D N4    1 
ATOM   5340 C  C5    . DC  C 3 14  ? 95.844  100.773 109.545 1.00 86.60  ? 14   DC  D C5    1 
ATOM   5341 C  C6    . DC  C 3 14  ? 96.337  99.604  109.129 1.00 89.88  ? 14   DC  D C6    1 
ATOM   5342 P  P     . DG  C 3 15  ? 94.702  94.001  107.219 1.00 103.72 ? 15   DG  D P     1 
ATOM   5343 O  OP1   . DG  C 3 15  ? 94.903  92.642  106.671 1.00 94.57  ? 15   DG  D OP1   1 
ATOM   5344 O  OP2   . DG  C 3 15  ? 93.848  94.967  106.493 1.00 91.22  ? 15   DG  D OP2   1 
ATOM   5345 O  "O5'" . DG  C 3 15  ? 94.142  93.877  108.716 1.00 105.23 ? 15   DG  D "O5'" 1 
ATOM   5346 C  "C5'" . DG  C 3 15  ? 94.716  92.936  109.624 1.00 101.27 ? 15   DG  D "C5'" 1 
ATOM   5347 C  "C4'" . DG  C 3 15  ? 94.374  93.300  111.059 1.00 102.15 ? 15   DG  D "C4'" 1 
ATOM   5348 O  "O4'" . DG  C 3 15  ? 94.610  94.703  111.251 1.00 99.01  ? 15   DG  D "O4'" 1 
ATOM   5349 C  "C3'" . DG  C 3 15  ? 92.920  93.078  111.446 1.00 117.43 ? 15   DG  D "C3'" 1 
ATOM   5350 O  "O3'" . DG  C 3 15  ? 92.778  91.800  112.062 1.00 127.79 ? 15   DG  D "O3'" 1 
ATOM   5351 C  "C2'" . DG  C 3 15  ? 92.617  94.207  112.440 1.00 118.28 ? 15   DG  D "C2'" 1 
ATOM   5352 C  "C1'" . DG  C 3 15  ? 93.758  95.207  112.248 1.00 106.06 ? 15   DG  D "C1'" 1 
ATOM   5353 N  N9    . DG  C 3 15  ? 93.310  96.535  111.840 1.00 112.21 ? 15   DG  D N9    1 
ATOM   5354 C  C8    . DG  C 3 15  ? 93.202  97.013  110.558 1.00 109.95 ? 15   DG  D C8    1 
ATOM   5355 N  N7    . DG  C 3 15  ? 92.778  98.244  110.496 1.00 114.06 ? 15   DG  D N7    1 
ATOM   5356 C  C5    . DG  C 3 15  ? 92.591  98.605  111.824 1.00 119.67 ? 15   DG  D C5    1 
ATOM   5357 C  C6    . DG  C 3 15  ? 92.141  99.825  112.381 1.00 122.24 ? 15   DG  D C6    1 
ATOM   5358 O  O6    . DG  C 3 15  ? 91.808  100.861 111.791 1.00 121.09 ? 15   DG  D O6    1 
ATOM   5359 N  N1    . DG  C 3 15  ? 92.097  99.770  113.773 1.00 124.64 ? 15   DG  D N1    1 
ATOM   5360 C  C2    . DG  C 3 15  ? 92.442  98.672  114.525 1.00 121.42 ? 15   DG  D C2    1 
ATOM   5361 N  N2    . DG  C 3 15  ? 92.334  98.806  115.855 1.00 118.90 ? 15   DG  D N2    1 
ATOM   5362 N  N3    . DG  C 3 15  ? 92.865  97.525  114.014 1.00 118.63 ? 15   DG  D N3    1 
ATOM   5363 C  C4    . DG  C 3 15  ? 92.914  97.563  112.663 1.00 117.58 ? 15   DG  D C4    1 
HETATM 5364 P  PA    . TTP D 4 .   ? 116.364 105.521 113.160 0.00 39.40  ? 2601 TTP A PA    1 
HETATM 5365 O  O1A   . TTP D 4 .   ? 115.408 104.577 113.831 1.00 38.79  ? 2601 TTP A O1A   1 
HETATM 5366 O  O2A   . TTP D 4 .   ? 116.953 105.123 111.851 1.00 36.78  ? 2601 TTP A O2A   1 
HETATM 5367 O  O3A   . TTP D 4 .   ? 116.981 106.641 114.046 1.00 38.45  ? 2601 TTP A O3A   1 
HETATM 5368 P  PB    . TTP D 4 .   ? 118.558 107.269 114.002 0.00 44.10  ? 2601 TTP A PB    1 
HETATM 5369 O  O1B   . TTP D 4 .   ? 118.150 108.407 114.905 1.00 37.95  ? 2601 TTP A O1B   1 
HETATM 5370 O  O2B   . TTP D 4 .   ? 118.900 107.588 112.571 1.00 46.26  ? 2601 TTP A O2B   1 
HETATM 5371 O  O3B   . TTP D 4 .   ? 119.424 106.149 114.619 1.00 42.65  ? 2601 TTP A O3B   1 
HETATM 5372 P  PG    . TTP D 4 .   ? 120.023 104.452 114.834 1.00 78.21  ? 2601 TTP A PG    1 
HETATM 5373 O  O1G   . TTP D 4 .   ? 121.321 104.462 114.056 1.00 75.90  ? 2601 TTP A O1G   1 
HETATM 5374 O  O2G   . TTP D 4 .   ? 120.206 104.377 116.335 1.00 62.87  ? 2601 TTP A O2G   1 
HETATM 5375 O  O3G   . TTP D 4 .   ? 118.970 103.489 114.325 1.00 70.94  ? 2601 TTP A O3G   1 
HETATM 5376 O  "O5'" . TTP D 4 .   ? 115.122 106.687 112.444 1.00 29.62  ? 2601 TTP A "O5'" 1 
HETATM 5377 C  "C5'" . TTP D 4 .   ? 114.905 107.821 113.149 1.00 31.34  ? 2601 TTP A "C5'" 1 
HETATM 5378 C  "C4'" . TTP D 4 .   ? 113.619 108.506 112.618 1.00 31.90  ? 2601 TTP A "C4'" 1 
HETATM 5379 O  "O4'" . TTP D 4 .   ? 112.510 108.034 113.385 0.00 34.26  ? 2601 TTP A "O4'" 1 
HETATM 5380 C  "C3'" . TTP D 4 .   ? 113.646 110.028 112.831 0.00 34.41  ? 2601 TTP A "C3'" 1 
HETATM 5381 O  "O3'" . TTP D 4 .   ? 112.671 110.532 111.961 1.00 34.09  ? 2601 TTP A "O3'" 1 
HETATM 5382 C  "C2'" . TTP D 4 .   ? 113.107 110.142 114.248 0.00 33.81  ? 2601 TTP A "C2'" 1 
HETATM 5383 C  "C1'" . TTP D 4 .   ? 112.028 109.067 114.175 1.00 32.24  ? 2601 TTP A "C1'" 1 
HETATM 5384 N  N1    . TTP D 4 .   ? 111.658 108.517 115.505 1.00 29.70  ? 2601 TTP A N1    1 
HETATM 5385 C  C2    . TTP D 4 .   ? 110.793 109.310 116.274 1.00 33.29  ? 2601 TTP A C2    1 
HETATM 5386 O  O2    . TTP D 4 .   ? 110.345 110.407 115.919 0.00 36.80  ? 2601 TTP A O2    1 
HETATM 5387 N  N3    . TTP D 4 .   ? 110.405 108.836 117.535 1.00 35.61  ? 2601 TTP A N3    1 
HETATM 5388 C  C4    . TTP D 4 .   ? 110.847 107.599 118.054 1.00 39.20  ? 2601 TTP A C4    1 
HETATM 5389 O  O4    . TTP D 4 .   ? 110.438 107.296 119.167 0.00 45.53  ? 2601 TTP A O4    1 
HETATM 5390 C  C5    . TTP D 4 .   ? 111.734 106.846 117.194 0.00 40.44  ? 2601 TTP A C5    1 
HETATM 5391 C  C5M   . TTP D 4 .   ? 112.169 105.560 117.779 1.00 42.69  ? 2601 TTP A C5M   1 
HETATM 5392 C  C6    . TTP D 4 .   ? 112.122 107.290 115.964 0.00 37.17  ? 2601 TTP A C6    1 
HETATM 5393 MG MG    . MG  E 5 .   ? 117.260 103.525 110.622 1.00 38.11  ? 2602 MG  A MG    1 
# 
