data_8VW9
# 
_entry.id   8VW9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8VW9         pdb_00008vw9 10.2210/pdb8vw9/pdb 
WWPDB D_1000281028 ?            ?                   
EMDB  EMD-43577    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.pdbx_database_id_DOI'    
6  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7  2 'Structure model' '_citation.title'                   
8  2 'Structure model' '_citation.year'                    
9  2 'Structure model' '_citation_author.identifier_ORCID' 
10 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VW9 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-31 
_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        'CryoEM Structure of a FtsH Helical Assembly in the Presence of ATP' 
_pdbx_database_related.db_id          EMD-43577 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tezcan@ucsd.edu 
_pdbx_contact_author.name_first         F. 
_pdbx_contact_author.name_last          Tezcan 
_pdbx_contact_author.name_mi            Akif 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4733-6500 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Y.'        1 ? 
'Zhu, J.'       2 ? 
'Zhang, Z.'     3 ? 
'Wang, F.'      4 ? 
'Egelman, E.H.' 5 ? 
'Tezcan, F.A.'  6 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Chem.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1552-4469 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41589-024-01811-1 
_citation.pdbx_database_id_PubMed   39806067 
_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, Y.'          1 0000-0003-3566-6008 
primary 'Zhu, J.'         2 ?                   
primary 'Zhang, Z.'       3 ?                   
primary 'Wei, J.'         4 ?                   
primary 'Wang, F.'        5 ?                   
primary 'Meisl, G.'       6 0000-0002-6562-7715 
primary 'Knowles, T.P.J.' 7 0000-0002-7879-0140 
primary 'Egelman, E.H.'   8 ?                   
primary 'Tezcan, F.A.'    9 0000-0002-4733-6500 
# 
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 'ATP-dependent zinc metalloprotease FtsH' 51493.832 1 3.4.24.- 'C255S, C513S, C564S, K410L, K415A' ? ? 
2 non-polymer syn 'MAGNESIUM ION'                           24.305    1 ?        ?                                   ? ? 
3 non-polymer syn 'ZINC ION'                                65.409    1 ?        ?                                   ? ? 
4 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"               507.181   1 ?        ?                                   ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGGATMYKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILLVGPPGTGKTLLARAVAGEANVPFF
HISGSDFVELFVGVGAARVRDLFAQAKAHAPSIVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFDSKEGIIVM
AATNRPDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEIIAKRTPGFVGADLENLVNEAALLAAR
EGRDKITMKDFEEAIDRVIAGPARKSLLISPAEKRIIAYHEAGHAVVSTVVPNGEPVHRISIIPRGYKALGYTLHLPEED
KYLVSRNELLDKLTALLGGRAAEEVVFGDVTSGAANDIERATEIARNMVSQLGMSEELGPLAWGKEEQEVFLGKEITRLR
NYSEEVASKIDEEVKKIVTNSYERAKEIIRKYRKQLDNIVEILLEKETIEGDELRRILSEEFEKVVE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGGATMYKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILLVGPPGTGKTLLARAVAGEANVPFF
HISGSDFVELFVGVGAARVRDLFAQAKAHAPSIVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFDSKEGIIVM
AATNRPDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEIIAKRTPGFVGADLENLVNEAALLAAR
EGRDKITMKDFEEAIDRVIAGPARKSLLISPAEKRIIAYHEAGHAVVSTVVPNGEPVHRISIIPRGYKALGYTLHLPEED
KYLVSRNELLDKLTALLGGRAAEEVVFGDVTSGAANDIERATEIARNMVSQLGMSEELGPLAWGKEEQEVFLGKEITRLR
NYSEEVASKIDEEVKKIVTNSYERAKEIIRKYRKQLDNIVEILLEKETIEGDELRRILSEEFEKVVE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION'             MG  
3 'ZINC ION'                  ZN  
4 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   GLY n 
1 4   ALA n 
1 5   THR n 
1 6   MET n 
1 7   TYR n 
1 8   LYS n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  ASN n 
1 13  LYS n 
1 14  ARG n 
1 15  VAL n 
1 16  THR n 
1 17  PHE n 
1 18  LYS n 
1 19  ASP n 
1 20  VAL n 
1 21  GLY n 
1 22  GLY n 
1 23  ALA n 
1 24  GLU n 
1 25  GLU n 
1 26  ALA n 
1 27  ILE n 
1 28  GLU n 
1 29  GLU n 
1 30  LEU n 
1 31  LYS n 
1 32  GLU n 
1 33  VAL n 
1 34  VAL n 
1 35  GLU n 
1 36  PHE n 
1 37  LEU n 
1 38  LYS n 
1 39  ASP n 
1 40  PRO n 
1 41  SER n 
1 42  LYS n 
1 43  PHE n 
1 44  ASN n 
1 45  ARG n 
1 46  ILE n 
1 47  GLY n 
1 48  ALA n 
1 49  ARG n 
1 50  MET n 
1 51  PRO n 
1 52  LYS n 
1 53  GLY n 
1 54  ILE n 
1 55  LEU n 
1 56  LEU n 
1 57  VAL n 
1 58  GLY n 
1 59  PRO n 
1 60  PRO n 
1 61  GLY n 
1 62  THR n 
1 63  GLY n 
1 64  LYS n 
1 65  THR n 
1 66  LEU n 
1 67  LEU n 
1 68  ALA n 
1 69  ARG n 
1 70  ALA n 
1 71  VAL n 
1 72  ALA n 
1 73  GLY n 
1 74  GLU n 
1 75  ALA n 
1 76  ASN n 
1 77  VAL n 
1 78  PRO n 
1 79  PHE n 
1 80  PHE n 
1 81  HIS n 
1 82  ILE n 
1 83  SER n 
1 84  GLY n 
1 85  SER n 
1 86  ASP n 
1 87  PHE n 
1 88  VAL n 
1 89  GLU n 
1 90  LEU n 
1 91  PHE n 
1 92  VAL n 
1 93  GLY n 
1 94  VAL n 
1 95  GLY n 
1 96  ALA n 
1 97  ALA n 
1 98  ARG n 
1 99  VAL n 
1 100 ARG n 
1 101 ASP n 
1 102 LEU n 
1 103 PHE n 
1 104 ALA n 
1 105 GLN n 
1 106 ALA n 
1 107 LYS n 
1 108 ALA n 
1 109 HIS n 
1 110 ALA n 
1 111 PRO n 
1 112 SER n 
1 113 ILE n 
1 114 VAL n 
1 115 PHE n 
1 116 ILE n 
1 117 ASP n 
1 118 GLU n 
1 119 ILE n 
1 120 ASP n 
1 121 ALA n 
1 122 VAL n 
1 123 GLY n 
1 124 ARG n 
1 125 HIS n 
1 126 ARG n 
1 127 GLY n 
1 128 ALA n 
1 129 GLY n 
1 130 LEU n 
1 131 GLY n 
1 132 GLY n 
1 133 GLY n 
1 134 HIS n 
1 135 ASP n 
1 136 GLU n 
1 137 ARG n 
1 138 GLU n 
1 139 GLN n 
1 140 THR n 
1 141 LEU n 
1 142 ASN n 
1 143 GLN n 
1 144 LEU n 
1 145 LEU n 
1 146 VAL n 
1 147 GLU n 
1 148 MET n 
1 149 ASP n 
1 150 GLY n 
1 151 PHE n 
1 152 ASP n 
1 153 SER n 
1 154 LYS n 
1 155 GLU n 
1 156 GLY n 
1 157 ILE n 
1 158 ILE n 
1 159 VAL n 
1 160 MET n 
1 161 ALA n 
1 162 ALA n 
1 163 THR n 
1 164 ASN n 
1 165 ARG n 
1 166 PRO n 
1 167 ASP n 
1 168 ILE n 
1 169 LEU n 
1 170 ASP n 
1 171 PRO n 
1 172 ALA n 
1 173 LEU n 
1 174 LEU n 
1 175 ARG n 
1 176 PRO n 
1 177 GLY n 
1 178 ARG n 
1 179 PHE n 
1 180 ASP n 
1 181 LYS n 
1 182 LYS n 
1 183 ILE n 
1 184 VAL n 
1 185 VAL n 
1 186 ASP n 
1 187 PRO n 
1 188 PRO n 
1 189 ASP n 
1 190 MET n 
1 191 LEU n 
1 192 GLY n 
1 193 ARG n 
1 194 LYS n 
1 195 LYS n 
1 196 ILE n 
1 197 LEU n 
1 198 GLU n 
1 199 ILE n 
1 200 HIS n 
1 201 THR n 
1 202 ARG n 
1 203 ASN n 
1 204 LYS n 
1 205 PRO n 
1 206 LEU n 
1 207 ALA n 
1 208 GLU n 
1 209 ASP n 
1 210 VAL n 
1 211 ASN n 
1 212 LEU n 
1 213 GLU n 
1 214 ILE n 
1 215 ILE n 
1 216 ALA n 
1 217 LYS n 
1 218 ARG n 
1 219 THR n 
1 220 PRO n 
1 221 GLY n 
1 222 PHE n 
1 223 VAL n 
1 224 GLY n 
1 225 ALA n 
1 226 ASP n 
1 227 LEU n 
1 228 GLU n 
1 229 ASN n 
1 230 LEU n 
1 231 VAL n 
1 232 ASN n 
1 233 GLU n 
1 234 ALA n 
1 235 ALA n 
1 236 LEU n 
1 237 LEU n 
1 238 ALA n 
1 239 ALA n 
1 240 ARG n 
1 241 GLU n 
1 242 GLY n 
1 243 ARG n 
1 244 ASP n 
1 245 LYS n 
1 246 ILE n 
1 247 THR n 
1 248 MET n 
1 249 LYS n 
1 250 ASP n 
1 251 PHE n 
1 252 GLU n 
1 253 GLU n 
1 254 ALA n 
1 255 ILE n 
1 256 ASP n 
1 257 ARG n 
1 258 VAL n 
1 259 ILE n 
1 260 ALA n 
1 261 GLY n 
1 262 PRO n 
1 263 ALA n 
1 264 ARG n 
1 265 LYS n 
1 266 SER n 
1 267 LEU n 
1 268 LEU n 
1 269 ILE n 
1 270 SER n 
1 271 PRO n 
1 272 ALA n 
1 273 GLU n 
1 274 LYS n 
1 275 ARG n 
1 276 ILE n 
1 277 ILE n 
1 278 ALA n 
1 279 TYR n 
1 280 HIS n 
1 281 GLU n 
1 282 ALA n 
1 283 GLY n 
1 284 HIS n 
1 285 ALA n 
1 286 VAL n 
1 287 VAL n 
1 288 SER n 
1 289 THR n 
1 290 VAL n 
1 291 VAL n 
1 292 PRO n 
1 293 ASN n 
1 294 GLY n 
1 295 GLU n 
1 296 PRO n 
1 297 VAL n 
1 298 HIS n 
1 299 ARG n 
1 300 ILE n 
1 301 SER n 
1 302 ILE n 
1 303 ILE n 
1 304 PRO n 
1 305 ARG n 
1 306 GLY n 
1 307 TYR n 
1 308 LYS n 
1 309 ALA n 
1 310 LEU n 
1 311 GLY n 
1 312 TYR n 
1 313 THR n 
1 314 LEU n 
1 315 HIS n 
1 316 LEU n 
1 317 PRO n 
1 318 GLU n 
1 319 GLU n 
1 320 ASP n 
1 321 LYS n 
1 322 TYR n 
1 323 LEU n 
1 324 VAL n 
1 325 SER n 
1 326 ARG n 
1 327 ASN n 
1 328 GLU n 
1 329 LEU n 
1 330 LEU n 
1 331 ASP n 
1 332 LYS n 
1 333 LEU n 
1 334 THR n 
1 335 ALA n 
1 336 LEU n 
1 337 LEU n 
1 338 GLY n 
1 339 GLY n 
1 340 ARG n 
1 341 ALA n 
1 342 ALA n 
1 343 GLU n 
1 344 GLU n 
1 345 VAL n 
1 346 VAL n 
1 347 PHE n 
1 348 GLY n 
1 349 ASP n 
1 350 VAL n 
1 351 THR n 
1 352 SER n 
1 353 GLY n 
1 354 ALA n 
1 355 ALA n 
1 356 ASN n 
1 357 ASP n 
1 358 ILE n 
1 359 GLU n 
1 360 ARG n 
1 361 ALA n 
1 362 THR n 
1 363 GLU n 
1 364 ILE n 
1 365 ALA n 
1 366 ARG n 
1 367 ASN n 
1 368 MET n 
1 369 VAL n 
1 370 SER n 
1 371 GLN n 
1 372 LEU n 
1 373 GLY n 
1 374 MET n 
1 375 SER n 
1 376 GLU n 
1 377 GLU n 
1 378 LEU n 
1 379 GLY n 
1 380 PRO n 
1 381 LEU n 
1 382 ALA n 
1 383 TRP n 
1 384 GLY n 
1 385 LYS n 
1 386 GLU n 
1 387 GLU n 
1 388 GLN n 
1 389 GLU n 
1 390 VAL n 
1 391 PHE n 
1 392 LEU n 
1 393 GLY n 
1 394 LYS n 
1 395 GLU n 
1 396 ILE n 
1 397 THR n 
1 398 ARG n 
1 399 LEU n 
1 400 ARG n 
1 401 ASN n 
1 402 TYR n 
1 403 SER n 
1 404 GLU n 
1 405 GLU n 
1 406 VAL n 
1 407 ALA n 
1 408 SER n 
1 409 LYS n 
1 410 ILE n 
1 411 ASP n 
1 412 GLU n 
1 413 GLU n 
1 414 VAL n 
1 415 LYS n 
1 416 LYS n 
1 417 ILE n 
1 418 VAL n 
1 419 THR n 
1 420 ASN n 
1 421 SER n 
1 422 TYR n 
1 423 GLU n 
1 424 ARG n 
1 425 ALA n 
1 426 LYS n 
1 427 GLU n 
1 428 ILE n 
1 429 ILE n 
1 430 ARG n 
1 431 LYS n 
1 432 TYR n 
1 433 ARG n 
1 434 LYS n 
1 435 GLN n 
1 436 LEU n 
1 437 ASP n 
1 438 ASN n 
1 439 ILE n 
1 440 VAL n 
1 441 GLU n 
1 442 ILE n 
1 443 LEU n 
1 444 LEU n 
1 445 GLU n 
1 446 LYS n 
1 447 GLU n 
1 448 THR n 
1 449 ILE n 
1 450 GLU n 
1 451 GLY n 
1 452 ASP n 
1 453 GLU n 
1 454 LEU n 
1 455 ARG n 
1 456 ARG n 
1 457 ILE n 
1 458 LEU n 
1 459 SER n 
1 460 GLU n 
1 461 GLU n 
1 462 PHE n 
1 463 GLU n 
1 464 LYS n 
1 465 VAL n 
1 466 VAL n 
1 467 GLU 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                   467 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ftsH, TM_0580' 
_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      'Thermotoga maritima' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2336 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
ZN  non-polymer         . 'ZINC ION'                  ? 'Zn 2'              65.409  
# 
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   SER 1   144 ?   ?   ?   A . n 
A 1 2   GLY 2   145 ?   ?   ?   A . n 
A 1 3   GLY 3   146 ?   ?   ?   A . n 
A 1 4   ALA 4   147 ?   ?   ?   A . n 
A 1 5   THR 5   148 ?   ?   ?   A . n 
A 1 6   MET 6   149 ?   ?   ?   A . n 
A 1 7   TYR 7   150 ?   ?   ?   A . n 
A 1 8   LYS 8   151 ?   ?   ?   A . n 
A 1 9   PRO 9   152 ?   ?   ?   A . n 
A 1 10  SER 10  153 ?   ?   ?   A . n 
A 1 11  GLY 11  154 ?   ?   ?   A . n 
A 1 12  ASN 12  155 ?   ?   ?   A . n 
A 1 13  LYS 13  156 156 LYS LYS A . n 
A 1 14  ARG 14  157 157 ARG ARG A . n 
A 1 15  VAL 15  158 158 VAL VAL A . n 
A 1 16  THR 16  159 159 THR THR A . n 
A 1 17  PHE 17  160 160 PHE PHE A . n 
A 1 18  LYS 18  161 161 LYS LYS A . n 
A 1 19  ASP 19  162 162 ASP ASP A . n 
A 1 20  VAL 20  163 163 VAL VAL A . n 
A 1 21  GLY 21  164 164 GLY GLY A . n 
A 1 22  GLY 22  165 165 GLY GLY A . n 
A 1 23  ALA 23  166 166 ALA ALA A . n 
A 1 24  GLU 24  167 167 GLU GLU A . n 
A 1 25  GLU 25  168 168 GLU GLU A . n 
A 1 26  ALA 26  169 169 ALA ALA A . n 
A 1 27  ILE 27  170 170 ILE ILE A . n 
A 1 28  GLU 28  171 171 GLU GLU A . n 
A 1 29  GLU 29  172 172 GLU GLU A . n 
A 1 30  LEU 30  173 173 LEU LEU A . n 
A 1 31  LYS 31  174 174 LYS LYS A . n 
A 1 32  GLU 32  175 175 GLU GLU A . n 
A 1 33  VAL 33  176 176 VAL VAL A . n 
A 1 34  VAL 34  177 177 VAL VAL A . n 
A 1 35  GLU 35  178 178 GLU GLU A . n 
A 1 36  PHE 36  179 179 PHE PHE A . n 
A 1 37  LEU 37  180 180 LEU LEU A . n 
A 1 38  LYS 38  181 181 LYS LYS A . n 
A 1 39  ASP 39  182 182 ASP ASP A . n 
A 1 40  PRO 40  183 183 PRO PRO A . n 
A 1 41  SER 41  184 184 SER SER A . n 
A 1 42  LYS 42  185 185 LYS LYS A . n 
A 1 43  PHE 43  186 186 PHE PHE A . n 
A 1 44  ASN 44  187 187 ASN ASN A . n 
A 1 45  ARG 45  188 188 ARG ARG A . n 
A 1 46  ILE 46  189 189 ILE ILE A . n 
A 1 47  GLY 47  190 190 GLY GLY A . n 
A 1 48  ALA 48  191 191 ALA ALA A . n 
A 1 49  ARG 49  192 192 ARG ARG A . n 
A 1 50  MET 50  193 193 MET MET A . n 
A 1 51  PRO 51  194 194 PRO PRO A . n 
A 1 52  LYS 52  195 195 LYS LYS A . n 
A 1 53  GLY 53  196 196 GLY GLY A . n 
A 1 54  ILE 54  197 197 ILE ILE A . n 
A 1 55  LEU 55  198 198 LEU LEU A . n 
A 1 56  LEU 56  199 199 LEU LEU A . n 
A 1 57  VAL 57  200 200 VAL VAL A . n 
A 1 58  GLY 58  201 201 GLY GLY A . n 
A 1 59  PRO 59  202 202 PRO PRO A . n 
A 1 60  PRO 60  203 203 PRO PRO A . n 
A 1 61  GLY 61  204 204 GLY GLY A . n 
A 1 62  THR 62  205 205 THR THR A . n 
A 1 63  GLY 63  206 206 GLY GLY A . n 
A 1 64  LYS 64  207 207 LYS LYS A . n 
A 1 65  THR 65  208 208 THR THR A . n 
A 1 66  LEU 66  209 209 LEU LEU A . n 
A 1 67  LEU 67  210 210 LEU LEU A . n 
A 1 68  ALA 68  211 211 ALA ALA A . n 
A 1 69  ARG 69  212 212 ARG ARG A . n 
A 1 70  ALA 70  213 213 ALA ALA A . n 
A 1 71  VAL 71  214 214 VAL VAL A . n 
A 1 72  ALA 72  215 215 ALA ALA A . n 
A 1 73  GLY 73  216 216 GLY GLY A . n 
A 1 74  GLU 74  217 217 GLU GLU A . n 
A 1 75  ALA 75  218 218 ALA ALA A . n 
A 1 76  ASN 76  219 219 ASN ASN A . n 
A 1 77  VAL 77  220 220 VAL VAL A . n 
A 1 78  PRO 78  221 221 PRO PRO A . n 
A 1 79  PHE 79  222 222 PHE PHE A . n 
A 1 80  PHE 80  223 223 PHE PHE A . n 
A 1 81  HIS 81  224 224 HIS HIS A . n 
A 1 82  ILE 82  225 225 ILE ILE A . n 
A 1 83  SER 83  226 226 SER SER A . n 
A 1 84  GLY 84  227 227 GLY GLY A . n 
A 1 85  SER 85  228 228 SER SER A . n 
A 1 86  ASP 86  229 229 ASP ASP A . n 
A 1 87  PHE 87  230 230 PHE PHE A . n 
A 1 88  VAL 88  231 ?   ?   ?   A . n 
A 1 89  GLU 89  232 ?   ?   ?   A . n 
A 1 90  LEU 90  233 ?   ?   ?   A . n 
A 1 91  PHE 91  234 ?   ?   ?   A . n 
A 1 92  VAL 92  235 ?   ?   ?   A . n 
A 1 93  GLY 93  236 ?   ?   ?   A . n 
A 1 94  VAL 94  237 237 VAL VAL A . n 
A 1 95  GLY 95  238 238 GLY GLY A . n 
A 1 96  ALA 96  239 239 ALA ALA A . n 
A 1 97  ALA 97  240 240 ALA ALA A . n 
A 1 98  ARG 98  241 241 ARG ARG A . n 
A 1 99  VAL 99  242 242 VAL VAL A . n 
A 1 100 ARG 100 243 243 ARG ARG A . n 
A 1 101 ASP 101 244 244 ASP ASP A . n 
A 1 102 LEU 102 245 245 LEU LEU A . n 
A 1 103 PHE 103 246 246 PHE PHE A . n 
A 1 104 ALA 104 247 247 ALA ALA A . n 
A 1 105 GLN 105 248 248 GLN GLN A . n 
A 1 106 ALA 106 249 249 ALA ALA A . n 
A 1 107 LYS 107 250 250 LYS LYS A . n 
A 1 108 ALA 108 251 251 ALA ALA A . n 
A 1 109 HIS 109 252 252 HIS HIS A . n 
A 1 110 ALA 110 253 253 ALA ALA A . n 
A 1 111 PRO 111 254 254 PRO PRO A . n 
A 1 112 SER 112 255 255 SER SER A . n 
A 1 113 ILE 113 256 256 ILE ILE A . n 
A 1 114 VAL 114 257 257 VAL VAL A . n 
A 1 115 PHE 115 258 258 PHE PHE A . n 
A 1 116 ILE 116 259 259 ILE ILE A . n 
A 1 117 ASP 117 260 260 ASP ASP A . n 
A 1 118 GLU 118 261 261 GLU GLU A . n 
A 1 119 ILE 119 262 262 ILE ILE A . n 
A 1 120 ASP 120 263 263 ASP ASP A . n 
A 1 121 ALA 121 264 264 ALA ALA A . n 
A 1 122 VAL 122 265 265 VAL VAL A . n 
A 1 123 GLY 123 266 266 GLY GLY A . n 
A 1 124 ARG 124 267 ?   ?   ?   A . n 
A 1 125 HIS 125 268 ?   ?   ?   A . n 
A 1 126 ARG 126 269 ?   ?   ?   A . n 
A 1 127 GLY 127 270 ?   ?   ?   A . n 
A 1 128 ALA 128 271 ?   ?   ?   A . n 
A 1 129 GLY 129 272 ?   ?   ?   A . n 
A 1 130 LEU 130 273 ?   ?   ?   A . n 
A 1 131 GLY 131 274 ?   ?   ?   A . n 
A 1 132 GLY 132 275 ?   ?   ?   A . n 
A 1 133 GLY 133 276 ?   ?   ?   A . n 
A 1 134 HIS 134 277 ?   ?   ?   A . n 
A 1 135 ASP 135 278 ?   ?   ?   A . n 
A 1 136 GLU 136 279 ?   ?   ?   A . n 
A 1 137 ARG 137 280 280 ARG ARG A . n 
A 1 138 GLU 138 281 281 GLU GLU A . n 
A 1 139 GLN 139 282 282 GLN GLN A . n 
A 1 140 THR 140 283 283 THR THR A . n 
A 1 141 LEU 141 284 284 LEU LEU A . n 
A 1 142 ASN 142 285 285 ASN ASN A . n 
A 1 143 GLN 143 286 286 GLN GLN A . n 
A 1 144 LEU 144 287 287 LEU LEU A . n 
A 1 145 LEU 145 288 288 LEU LEU A . n 
A 1 146 VAL 146 289 289 VAL VAL A . n 
A 1 147 GLU 147 290 290 GLU GLU A . n 
A 1 148 MET 148 291 291 MET MET A . n 
A 1 149 ASP 149 292 292 ASP ASP A . n 
A 1 150 GLY 150 293 293 GLY GLY A . n 
A 1 151 PHE 151 294 294 PHE PHE A . n 
A 1 152 ASP 152 295 295 ASP ASP A . n 
A 1 153 SER 153 296 296 SER SER A . n 
A 1 154 LYS 154 297 297 LYS LYS A . n 
A 1 155 GLU 155 298 298 GLU GLU A . n 
A 1 156 GLY 156 299 299 GLY GLY A . n 
A 1 157 ILE 157 300 300 ILE ILE A . n 
A 1 158 ILE 158 301 301 ILE ILE A . n 
A 1 159 VAL 159 302 302 VAL VAL A . n 
A 1 160 MET 160 303 303 MET MET A . n 
A 1 161 ALA 161 304 304 ALA ALA A . n 
A 1 162 ALA 162 305 305 ALA ALA A . n 
A 1 163 THR 163 306 306 THR THR A . n 
A 1 164 ASN 164 307 307 ASN ASN A . n 
A 1 165 ARG 165 308 308 ARG ARG A . n 
A 1 166 PRO 166 309 309 PRO PRO A . n 
A 1 167 ASP 167 310 310 ASP ASP A . n 
A 1 168 ILE 168 311 311 ILE ILE A . n 
A 1 169 LEU 169 312 312 LEU LEU A . n 
A 1 170 ASP 170 313 313 ASP ASP A . n 
A 1 171 PRO 171 314 314 PRO PRO A . n 
A 1 172 ALA 172 315 315 ALA ALA A . n 
A 1 173 LEU 173 316 316 LEU LEU A . n 
A 1 174 LEU 174 317 317 LEU LEU A . n 
A 1 175 ARG 175 318 318 ARG ARG A . n 
A 1 176 PRO 176 319 319 PRO PRO A . n 
A 1 177 GLY 177 320 320 GLY GLY A . n 
A 1 178 ARG 178 321 321 ARG ARG A . n 
A 1 179 PHE 179 322 322 PHE PHE A . n 
A 1 180 ASP 180 323 323 ASP ASP A . n 
A 1 181 LYS 181 324 324 LYS LYS A . n 
A 1 182 LYS 182 325 325 LYS LYS A . n 
A 1 183 ILE 183 326 326 ILE ILE A . n 
A 1 184 VAL 184 327 327 VAL VAL A . n 
A 1 185 VAL 185 328 328 VAL VAL A . n 
A 1 186 ASP 186 329 329 ASP ASP A . n 
A 1 187 PRO 187 330 330 PRO PRO A . n 
A 1 188 PRO 188 331 331 PRO PRO A . n 
A 1 189 ASP 189 332 332 ASP ASP A . n 
A 1 190 MET 190 333 333 MET MET A . n 
A 1 191 LEU 191 334 334 LEU LEU A . n 
A 1 192 GLY 192 335 335 GLY GLY A . n 
A 1 193 ARG 193 336 336 ARG ARG A . n 
A 1 194 LYS 194 337 337 LYS LYS A . n 
A 1 195 LYS 195 338 338 LYS LYS A . n 
A 1 196 ILE 196 339 339 ILE ILE A . n 
A 1 197 LEU 197 340 340 LEU LEU A . n 
A 1 198 GLU 198 341 341 GLU GLU A . n 
A 1 199 ILE 199 342 342 ILE ILE A . n 
A 1 200 HIS 200 343 343 HIS HIS A . n 
A 1 201 THR 201 344 344 THR THR A . n 
A 1 202 ARG 202 345 345 ARG ARG A . n 
A 1 203 ASN 203 346 346 ASN ASN A . n 
A 1 204 LYS 204 347 347 LYS LYS A . n 
A 1 205 PRO 205 348 348 PRO PRO A . n 
A 1 206 LEU 206 349 349 LEU LEU A . n 
A 1 207 ALA 207 350 350 ALA ALA A . n 
A 1 208 GLU 208 351 351 GLU GLU A . n 
A 1 209 ASP 209 352 352 ASP ASP A . n 
A 1 210 VAL 210 353 353 VAL VAL A . n 
A 1 211 ASN 211 354 354 ASN ASN A . n 
A 1 212 LEU 212 355 355 LEU LEU A . n 
A 1 213 GLU 213 356 356 GLU GLU A . n 
A 1 214 ILE 214 357 357 ILE ILE A . n 
A 1 215 ILE 215 358 358 ILE ILE A . n 
A 1 216 ALA 216 359 359 ALA ALA A . n 
A 1 217 LYS 217 360 360 LYS LYS A . n 
A 1 218 ARG 218 361 361 ARG ARG A . n 
A 1 219 THR 219 362 362 THR THR A . n 
A 1 220 PRO 220 363 363 PRO PRO A . n 
A 1 221 GLY 221 364 364 GLY GLY A . n 
A 1 222 PHE 222 365 365 PHE PHE A . n 
A 1 223 VAL 223 366 366 VAL VAL A . n 
A 1 224 GLY 224 367 367 GLY GLY A . n 
A 1 225 ALA 225 368 368 ALA ALA A . n 
A 1 226 ASP 226 369 369 ASP ASP A . n 
A 1 227 LEU 227 370 370 LEU LEU A . n 
A 1 228 GLU 228 371 371 GLU GLU A . n 
A 1 229 ASN 229 372 372 ASN ASN A . n 
A 1 230 LEU 230 373 373 LEU LEU A . n 
A 1 231 VAL 231 374 374 VAL VAL A . n 
A 1 232 ASN 232 375 375 ASN ASN A . n 
A 1 233 GLU 233 376 376 GLU GLU A . n 
A 1 234 ALA 234 377 377 ALA ALA A . n 
A 1 235 ALA 235 378 378 ALA ALA A . n 
A 1 236 LEU 236 379 379 LEU LEU A . n 
A 1 237 LEU 237 380 380 LEU LEU A . n 
A 1 238 ALA 238 381 381 ALA ALA A . n 
A 1 239 ALA 239 382 382 ALA ALA A . n 
A 1 240 ARG 240 383 383 ARG ARG A . n 
A 1 241 GLU 241 384 384 GLU GLU A . n 
A 1 242 GLY 242 385 385 GLY GLY A . n 
A 1 243 ARG 243 386 386 ARG ARG A . n 
A 1 244 ASP 244 387 387 ASP ASP A . n 
A 1 245 LYS 245 388 388 LYS LYS A . n 
A 1 246 ILE 246 389 389 ILE ILE A . n 
A 1 247 THR 247 390 390 THR THR A . n 
A 1 248 MET 248 391 391 MET MET A . n 
A 1 249 LYS 249 392 392 LYS LYS A . n 
A 1 250 ASP 250 393 393 ASP ASP A . n 
A 1 251 PHE 251 394 394 PHE PHE A . n 
A 1 252 GLU 252 395 395 GLU GLU A . n 
A 1 253 GLU 253 396 396 GLU GLU A . n 
A 1 254 ALA 254 397 397 ALA ALA A . n 
A 1 255 ILE 255 398 398 ILE ILE A . n 
A 1 256 ASP 256 399 399 ASP ASP A . n 
A 1 257 ARG 257 400 400 ARG ARG A . n 
A 1 258 VAL 258 401 401 VAL VAL A . n 
A 1 259 ILE 259 402 402 ILE ILE A . n 
A 1 260 ALA 260 403 403 ALA ALA A . n 
A 1 261 GLY 261 404 404 GLY GLY A . n 
A 1 262 PRO 262 405 405 PRO PRO A . n 
A 1 263 ALA 263 406 406 ALA ALA A . n 
A 1 264 ARG 264 407 407 ARG ARG A . n 
A 1 265 LYS 265 408 408 LYS LYS A . n 
A 1 266 SER 266 409 409 SER SER A . n 
A 1 267 LEU 267 410 410 LEU LEU A . n 
A 1 268 LEU 268 411 411 LEU LEU A . n 
A 1 269 ILE 269 412 412 ILE ILE A . n 
A 1 270 SER 270 413 413 SER SER A . n 
A 1 271 PRO 271 414 414 PRO PRO A . n 
A 1 272 ALA 272 415 415 ALA ALA A . n 
A 1 273 GLU 273 416 416 GLU GLU A . n 
A 1 274 LYS 274 417 417 LYS LYS A . n 
A 1 275 ARG 275 418 418 ARG ARG A . n 
A 1 276 ILE 276 419 419 ILE ILE A . n 
A 1 277 ILE 277 420 420 ILE ILE A . n 
A 1 278 ALA 278 421 421 ALA ALA A . n 
A 1 279 TYR 279 422 422 TYR TYR A . n 
A 1 280 HIS 280 423 423 HIS HIS A . n 
A 1 281 GLU 281 424 424 GLU GLU A . n 
A 1 282 ALA 282 425 425 ALA ALA A . n 
A 1 283 GLY 283 426 426 GLY GLY A . n 
A 1 284 HIS 284 427 427 HIS HIS A . n 
A 1 285 ALA 285 428 428 ALA ALA A . n 
A 1 286 VAL 286 429 429 VAL VAL A . n 
A 1 287 VAL 287 430 430 VAL VAL A . n 
A 1 288 SER 288 431 431 SER SER A . n 
A 1 289 THR 289 432 432 THR THR A . n 
A 1 290 VAL 290 433 433 VAL VAL A . n 
A 1 291 VAL 291 434 434 VAL VAL A . n 
A 1 292 PRO 292 435 435 PRO PRO A . n 
A 1 293 ASN 293 436 436 ASN ASN A . n 
A 1 294 GLY 294 437 437 GLY GLY A . n 
A 1 295 GLU 295 438 438 GLU GLU A . n 
A 1 296 PRO 296 439 439 PRO PRO A . n 
A 1 297 VAL 297 440 440 VAL VAL A . n 
A 1 298 HIS 298 441 441 HIS HIS A . n 
A 1 299 ARG 299 442 442 ARG ARG A . n 
A 1 300 ILE 300 443 443 ILE ILE A . n 
A 1 301 SER 301 444 444 SER SER A . n 
A 1 302 ILE 302 445 445 ILE ILE A . n 
A 1 303 ILE 303 446 446 ILE ILE A . n 
A 1 304 PRO 304 447 447 PRO PRO A . n 
A 1 305 ARG 305 448 448 ARG ARG A . n 
A 1 306 GLY 306 449 449 GLY GLY A . n 
A 1 307 TYR 307 450 450 TYR TYR A . n 
A 1 308 LYS 308 451 451 LYS LYS A . n 
A 1 309 ALA 309 452 452 ALA ALA A . n 
A 1 310 LEU 310 453 453 LEU LEU A . n 
A 1 311 GLY 311 454 454 GLY GLY A . n 
A 1 312 TYR 312 455 455 TYR TYR A . n 
A 1 313 THR 313 456 456 THR THR A . n 
A 1 314 LEU 314 457 457 LEU LEU A . n 
A 1 315 HIS 315 458 458 HIS HIS A . n 
A 1 316 LEU 316 459 459 LEU LEU A . n 
A 1 317 PRO 317 460 460 PRO PRO A . n 
A 1 318 GLU 318 461 461 GLU GLU A . n 
A 1 319 GLU 319 462 462 GLU GLU A . n 
A 1 320 ASP 320 463 463 ASP ASP A . n 
A 1 321 LYS 321 464 464 LYS LYS A . n 
A 1 322 TYR 322 465 465 TYR TYR A . n 
A 1 323 LEU 323 466 466 LEU LEU A . n 
A 1 324 VAL 324 467 467 VAL VAL A . n 
A 1 325 SER 325 468 468 SER SER A . n 
A 1 326 ARG 326 469 469 ARG ARG A . n 
A 1 327 ASN 327 470 470 ASN ASN A . n 
A 1 328 GLU 328 471 471 GLU GLU A . n 
A 1 329 LEU 329 472 472 LEU LEU A . n 
A 1 330 LEU 330 473 473 LEU LEU A . n 
A 1 331 ASP 331 474 474 ASP ASP A . n 
A 1 332 LYS 332 475 475 LYS LYS A . n 
A 1 333 LEU 333 476 476 LEU LEU A . n 
A 1 334 THR 334 477 477 THR THR A . n 
A 1 335 ALA 335 478 478 ALA ALA A . n 
A 1 336 LEU 336 479 479 LEU LEU A . n 
A 1 337 LEU 337 480 480 LEU LEU A . n 
A 1 338 GLY 338 481 481 GLY GLY A . n 
A 1 339 GLY 339 482 482 GLY GLY A . n 
A 1 340 ARG 340 483 483 ARG ARG A . n 
A 1 341 ALA 341 484 484 ALA ALA A . n 
A 1 342 ALA 342 485 485 ALA ALA A . n 
A 1 343 GLU 343 486 486 GLU GLU A . n 
A 1 344 GLU 344 487 487 GLU GLU A . n 
A 1 345 VAL 345 488 488 VAL VAL A . n 
A 1 346 VAL 346 489 489 VAL VAL A . n 
A 1 347 PHE 347 490 490 PHE PHE A . n 
A 1 348 GLY 348 491 491 GLY GLY A . n 
A 1 349 ASP 349 492 492 ASP ASP A . n 
A 1 350 VAL 350 493 493 VAL VAL A . n 
A 1 351 THR 351 494 494 THR THR A . n 
A 1 352 SER 352 495 495 SER SER A . n 
A 1 353 GLY 353 496 496 GLY GLY A . n 
A 1 354 ALA 354 497 497 ALA ALA A . n 
A 1 355 ALA 355 498 498 ALA ALA A . n 
A 1 356 ASN 356 499 499 ASN ASN A . n 
A 1 357 ASP 357 500 500 ASP ASP A . n 
A 1 358 ILE 358 501 501 ILE ILE A . n 
A 1 359 GLU 359 502 502 GLU GLU A . n 
A 1 360 ARG 360 503 503 ARG ARG A . n 
A 1 361 ALA 361 504 504 ALA ALA A . n 
A 1 362 THR 362 505 505 THR THR A . n 
A 1 363 GLU 363 506 506 GLU GLU A . n 
A 1 364 ILE 364 507 507 ILE ILE A . n 
A 1 365 ALA 365 508 508 ALA ALA A . n 
A 1 366 ARG 366 509 509 ARG ARG A . n 
A 1 367 ASN 367 510 510 ASN ASN A . n 
A 1 368 MET 368 511 511 MET MET A . n 
A 1 369 VAL 369 512 512 VAL VAL A . n 
A 1 370 SER 370 513 513 SER SER A . n 
A 1 371 GLN 371 514 514 GLN GLN A . n 
A 1 372 LEU 372 515 515 LEU LEU A . n 
A 1 373 GLY 373 516 516 GLY GLY A . n 
A 1 374 MET 374 517 ?   ?   ?   A . n 
A 1 375 SER 375 518 ?   ?   ?   A . n 
A 1 376 GLU 376 519 ?   ?   ?   A . n 
A 1 377 GLU 377 520 ?   ?   ?   A . n 
A 1 378 LEU 378 521 ?   ?   ?   A . n 
A 1 379 GLY 379 522 ?   ?   ?   A . n 
A 1 380 PRO 380 523 ?   ?   ?   A . n 
A 1 381 LEU 381 524 ?   ?   ?   A . n 
A 1 382 ALA 382 525 ?   ?   ?   A . n 
A 1 383 TRP 383 526 ?   ?   ?   A . n 
A 1 384 GLY 384 527 ?   ?   ?   A . n 
A 1 385 LYS 385 528 ?   ?   ?   A . n 
A 1 386 GLU 386 529 ?   ?   ?   A . n 
A 1 387 GLU 387 530 ?   ?   ?   A . n 
A 1 388 GLN 388 531 ?   ?   ?   A . n 
A 1 389 GLU 389 532 ?   ?   ?   A . n 
A 1 390 VAL 390 533 ?   ?   ?   A . n 
A 1 391 PHE 391 534 ?   ?   ?   A . n 
A 1 392 LEU 392 535 ?   ?   ?   A . n 
A 1 393 GLY 393 536 ?   ?   ?   A . n 
A 1 394 LYS 394 537 ?   ?   ?   A . n 
A 1 395 GLU 395 538 ?   ?   ?   A . n 
A 1 396 ILE 396 539 ?   ?   ?   A . n 
A 1 397 THR 397 540 ?   ?   ?   A . n 
A 1 398 ARG 398 541 ?   ?   ?   A . n 
A 1 399 LEU 399 542 ?   ?   ?   A . n 
A 1 400 ARG 400 543 ?   ?   ?   A . n 
A 1 401 ASN 401 544 ?   ?   ?   A . n 
A 1 402 TYR 402 545 ?   ?   ?   A . n 
A 1 403 SER 403 546 ?   ?   ?   A . n 
A 1 404 GLU 404 547 ?   ?   ?   A . n 
A 1 405 GLU 405 548 ?   ?   ?   A . n 
A 1 406 VAL 406 549 ?   ?   ?   A . n 
A 1 407 ALA 407 550 ?   ?   ?   A . n 
A 1 408 SER 408 551 ?   ?   ?   A . n 
A 1 409 LYS 409 552 552 LYS LYS A . n 
A 1 410 ILE 410 553 553 ILE ILE A . n 
A 1 411 ASP 411 554 554 ASP ASP A . n 
A 1 412 GLU 412 555 555 GLU GLU A . n 
A 1 413 GLU 413 556 556 GLU GLU A . n 
A 1 414 VAL 414 557 557 VAL VAL A . n 
A 1 415 LYS 415 558 558 LYS LYS A . n 
A 1 416 LYS 416 559 559 LYS LYS A . n 
A 1 417 ILE 417 560 560 ILE ILE A . n 
A 1 418 VAL 418 561 561 VAL VAL A . n 
A 1 419 THR 419 562 562 THR THR A . n 
A 1 420 ASN 420 563 563 ASN ASN A . n 
A 1 421 SER 421 564 564 SER SER A . n 
A 1 422 TYR 422 565 565 TYR TYR A . n 
A 1 423 GLU 423 566 566 GLU GLU A . n 
A 1 424 ARG 424 567 567 ARG ARG A . n 
A 1 425 ALA 425 568 568 ALA ALA A . n 
A 1 426 LYS 426 569 569 LYS LYS A . n 
A 1 427 GLU 427 570 570 GLU GLU A . n 
A 1 428 ILE 428 571 571 ILE ILE A . n 
A 1 429 ILE 429 572 572 ILE ILE A . n 
A 1 430 ARG 430 573 573 ARG ARG A . n 
A 1 431 LYS 431 574 574 LYS LYS A . n 
A 1 432 TYR 432 575 575 TYR TYR A . n 
A 1 433 ARG 433 576 576 ARG ARG A . n 
A 1 434 LYS 434 577 577 LYS LYS A . n 
A 1 435 GLN 435 578 578 GLN GLN A . n 
A 1 436 LEU 436 579 579 LEU LEU A . n 
A 1 437 ASP 437 580 580 ASP ASP A . n 
A 1 438 ASN 438 581 581 ASN ASN A . n 
A 1 439 ILE 439 582 582 ILE ILE A . n 
A 1 440 VAL 440 583 583 VAL VAL A . n 
A 1 441 GLU 441 584 584 GLU GLU A . n 
A 1 442 ILE 442 585 585 ILE ILE A . n 
A 1 443 LEU 443 586 586 LEU LEU A . n 
A 1 444 LEU 444 587 587 LEU LEU A . n 
A 1 445 GLU 445 588 588 GLU GLU A . n 
A 1 446 LYS 446 589 589 LYS LYS A . n 
A 1 447 GLU 447 590 590 GLU GLU A . n 
A 1 448 THR 448 591 591 THR THR A . n 
A 1 449 ILE 449 592 592 ILE ILE A . n 
A 1 450 GLU 450 593 593 GLU GLU A . n 
A 1 451 GLY 451 594 594 GLY GLY A . n 
A 1 452 ASP 452 595 595 ASP ASP A . n 
A 1 453 GLU 453 596 596 GLU GLU A . n 
A 1 454 LEU 454 597 597 LEU LEU A . n 
A 1 455 ARG 455 598 598 ARG ARG A . n 
A 1 456 ARG 456 599 599 ARG ARG A . n 
A 1 457 ILE 457 600 600 ILE ILE A . n 
A 1 458 LEU 458 601 601 LEU LEU A . n 
A 1 459 SER 459 602 602 SER SER A . n 
A 1 460 GLU 460 603 603 GLU GLU A . n 
A 1 461 GLU 461 604 604 GLU GLU A . n 
A 1 462 PHE 462 605 605 PHE PHE A . n 
A 1 463 GLU 463 606 ?   ?   ?   A . n 
A 1 464 LYS 464 607 ?   ?   ?   A . n 
A 1 465 VAL 465 608 ?   ?   ?   A . n 
A 1 466 VAL 466 609 ?   ?   ?   A . n 
A 1 467 GLU 467 610 ?   ?   ?   A . 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 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 ZN  ? ? ZN  ? ? '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 
B 2 MG  1 800 800 MG  MG  A . 
C 3 ZN  1 801 801 ZN  ZN  A . 
D 4 ATP 1 802 802 ATP ATP A . 
# 
_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                     8VW9 
_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                         8VW9 
_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                   8VW9 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8VW9 
_struct.title                        'CryoEM Structure of a FtsH Helical Assembly in the Presence of ATP' 
_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        8VW9 
_struct_keywords.text            'nucleotide binding, protease, cytoplasmic domain, helical assembly, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FTSH_THEMA 
_struct_ref.pdbx_db_accession          Q9WZ49 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATMYKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILLVGPPGTGKTLLARAVAGEANVPFFHIS
GSDFVELFVGVGAARVRDLFAQAKAHAPCIVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFDSKEGIIVMAAT
NRPDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEIIAKRTPGFVGADLENLVNEAALLAAREGR
DKITMKDFEEAIDRVIAGPARKSKLISPKEKRIIAYHEAGHAVVSTVVPNGEPVHRISIIPRGYKALGYTLHLPEEDKYL
VSRNELLDKLTALLGGRAAEEVVFGDVTSGAANDIERATEIARNMVCQLGMSEELGPLAWGKEEQEVFLGKEITRLRNYS
EEVASKIDEEVKKIVTNCYERAKEIIRKYRKQLDNIVEILLEKETIEGDELRRILSEEFEKVVE
;
_struct_ref.pdbx_align_begin           147 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VW9 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 467 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9WZ49 
_struct_ref_seq.db_align_beg                  147 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  610 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       147 
_struct_ref_seq.pdbx_auth_seq_align_end       610 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8VW9 SER A 1   ? UNP Q9WZ49 ?   ?   'expression tag'      144 1 
1 8VW9 GLY A 2   ? UNP Q9WZ49 ?   ?   'expression tag'      145 2 
1 8VW9 GLY A 3   ? UNP Q9WZ49 ?   ?   'expression tag'      146 3 
1 8VW9 SER A 112 ? UNP Q9WZ49 CYS 255 'engineered mutation' 255 4 
1 8VW9 LEU A 267 ? UNP Q9WZ49 LYS 410 'engineered mutation' 410 5 
1 8VW9 ALA A 272 ? UNP Q9WZ49 LYS 415 'engineered mutation' 415 6 
1 8VW9 SER A 370 ? UNP Q9WZ49 CYS 513 'engineered mutation' 513 7 
1 8VW9 SER A 421 ? UNP Q9WZ49 CYS 564 'engineered mutation' 564 8 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 'representative helical assembly' ? 30-meric  30 
2 'helical asymmetric unit'         ? monomeric 1  
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 '(1-30)' A,B,C,D 
2 1        A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1  'identity operation'         1_555 x,y,z 1.00000000  0.00000000  0.00000000 0.00000   0.00000000  1.00000000  0.00000000 
0.00000   0.00000000  0.00000000  1.00000000 0.00000    
2  'helical symmetry operation' ?     ?     0.00000000  1.00000000  0.00000000 0.00860   -1.00000000 0.00000000  0.00000000 
385.27100 0.00000000  -0.00000000 1.00000000 -109.20000 
3  'helical symmetry operation' ?     ?     0.38268300  -0.92388000 0.00000000 296.88800 0.92388000  0.38268300  0.00000000 
-59.06160 -0.00000000 0.00000000  1.00000000 -100.10000 
4  'helical symmetry operation' ?     ?     -0.70710700 0.70710700  0.00000000 192.64600 -0.70710700 -0.70710700 0.00000000 
465.05900 0.00000000  0.00000000  1.00000000 -91.00000  
5  'helical symmetry operation' ?     ?     0.92388000  -0.38268300 0.00000000 88.38070  0.38268300  0.92388000  0.00000000 
-59.05690 -0.00000000 0.00000000  1.00000000 -81.90000  
6  'helical symmetry operation' ?     ?     -1.00000000 0.00000000  0.00000000 385.28000 -0.00000000 -1.00000000 0.00000000 
385.26300 0.00000000  0.00000000  1.00000000 -72.80000  
7  'helical symmetry operation' ?     ?     0.92388000  0.38268300  0.00000000 -59.05300 -0.38268300 0.92388000  0.00000000 
88.38330  0.00000000  -0.00000000 1.00000000 -63.70000  
8  'helical symmetry operation' ?     ?     -0.70710700 -0.70710700 0.00000000 465.06800 0.70710700  -0.70710700 0.00000000 
192.62500 0.00000000  0.00000000  1.00000000 -54.60000  
9  'helical symmetry operation' ?     ?     0.38268300  0.92388000  0.00000000 -59.04830 -0.92388000 0.38268300  0.00000000 
296.89100 0.00000000  -0.00000000 1.00000000 -45.50000  
10 'helical symmetry operation' ?     ?     -0.00000000 -1.00000000 0.00000000 385.27100 1.00000000  -0.00000000 0.00000000 
-0.00860  0.00000000  0.00000000  1.00000000 -36.40000  
11 'helical symmetry operation' ?     ?     -0.38268300 0.92388000  0.00000000 88.39190  -0.92388000 -0.38268300 0.00000000 
444.32400 0.00000000  0.00000000  1.00000000 -27.30000  
12 'helical symmetry operation' ?     ?     0.70710700  -0.70710700 0.00000000 192.63400 0.70710700  0.70710700  0.00000000 
-79.79660 -0.00000000 0.00000000  1.00000000 -18.20000  
13 'helical symmetry operation' ?     ?     -0.92388000 0.38268300  0.00000000 296.89900 -0.38268300 -0.92388000 0.00000000 
444.32000 0.00000000  0.00000000  1.00000000 -9.10000   
14 'helical symmetry operation' ?     ?     -0.92388000 -0.38268300 0.00000000 444.33300 0.38268300  -0.92388000 0.00000000 
296.87900 0.00000000  0.00000000  1.00000000 9.10000    
15 'helical symmetry operation' ?     ?     0.70710700  0.70710700  0.00000000 -79.78800 -0.70710700 0.70710700  0.00000000 
192.63700 0.00000000  -0.00000000 1.00000000 18.20000   
16 'helical symmetry operation' ?     ?     -0.38268300 -0.92388000 0.00000000 444.32800 0.92388000  -0.38268300 0.00000000 
88.37210  0.00000000  0.00000000  1.00000000 27.30000   
17 'helical symmetry operation' ?     ?     -0.00000000 1.00000000  0.00000000 0.00860   -1.00000000 -0.00000000 0.00000000 
385.27100 0.00000000  0.00000000  1.00000000 36.40000   
18 'helical symmetry operation' ?     ?     0.38268300  -0.92388000 0.00000000 296.88800 0.92388000  0.38268300  0.00000000 
-59.06160 -0.00000000 0.00000000  1.00000000 45.50000   
19 'helical symmetry operation' ?     ?     -0.70710700 0.70710700  0.00000000 192.64600 -0.70710700 -0.70710700 0.00000000 
465.05900 0.00000000  0.00000000  1.00000000 54.60000   
20 'helical symmetry operation' ?     ?     0.92388000  -0.38268300 0.00000000 88.38070  0.38268300  0.92388000  0.00000000 
-59.05690 -0.00000000 0.00000000  1.00000000 63.70000   
21 'helical symmetry operation' ?     ?     -1.00000000 -0.00000000 0.00000000 385.28000 0.00000000  -1.00000000 0.00000000 
385.26300 0.00000000  0.00000000  1.00000000 72.80000   
22 'helical symmetry operation' ?     ?     0.92388000  0.38268300  0.00000000 -59.05300 -0.38268300 0.92388000  0.00000000 
88.38330  0.00000000  -0.00000000 1.00000000 81.90000   
23 'helical symmetry operation' ?     ?     -0.70710700 -0.70710700 0.00000000 465.06800 0.70710700  -0.70710700 0.00000000 
192.62500 0.00000000  0.00000000  1.00000000 91.00000   
24 'helical symmetry operation' ?     ?     0.38268300  0.92388000  0.00000000 -59.04830 -0.92388000 0.38268300  0.00000000 
296.89100 0.00000000  -0.00000000 1.00000000 100.10000  
25 'helical symmetry operation' ?     ?     0.00000000  -1.00000000 0.00000000 385.27100 1.00000000  0.00000000  0.00000000 
-0.00860  -0.00000000 0.00000000  1.00000000 109.20000  
26 'helical symmetry operation' ?     ?     -0.38268300 0.92388000  0.00000000 88.39190  -0.92388000 -0.38268300 0.00000000 
444.32400 0.00000000  0.00000000  1.00000000 118.30000  
27 'helical symmetry operation' ?     ?     0.70710700  -0.70710700 0.00000000 192.63400 0.70710700  0.70710700  0.00000000 
-79.79660 -0.00000000 0.00000000  1.00000000 127.40000  
28 'helical symmetry operation' ?     ?     -0.92388000 0.38268300  0.00000000 296.89900 -0.38268300 -0.92388000 0.00000000 
444.32000 0.00000000  0.00000000  1.00000000 136.50000  
29 'helical symmetry operation' ?     ?     1.00000000  0.00000000  0.00000000 -0.00000  -0.00000000 1.00000000  0.00000000 
0.00000   0.00000000  -0.00000000 1.00000000 145.60000  
30 'helical symmetry operation' ?     ?     -0.92388000 -0.38268300 0.00000000 444.33300 0.38268300  -0.92388000 0.00000000 
296.87900 0.00000000  0.00000000  1.00000000 154.70000  
# 
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 THR A 16  ? VAL A 20  ? THR A 159 VAL A 163 5 ? 5  
HELX_P HELX_P2  AA2 ALA A 23  ? ASP A 39  ? ALA A 166 ASP A 182 1 ? 17 
HELX_P HELX_P3  AA3 PRO A 40  ? ARG A 45  ? PRO A 183 ARG A 188 1 ? 6  
HELX_P HELX_P4  AA4 GLY A 63  ? ALA A 75  ? GLY A 206 ALA A 218 1 ? 13 
HELX_P HELX_P5  AA5 SER A 85  ? PHE A 87  ? SER A 228 PHE A 230 5 ? 3  
HELX_P HELX_P6  AA6 GLY A 95  ? HIS A 109 ? GLY A 238 HIS A 252 1 ? 15 
HELX_P HELX_P7  AA7 ILE A 119 ? VAL A 122 ? ILE A 262 VAL A 265 5 ? 4  
HELX_P HELX_P8  AA8 GLU A 138 ? ASP A 149 ? GLU A 281 ASP A 292 1 ? 12 
HELX_P HELX_P9  AA9 GLY A 150 ? PHE A 151 ? GLY A 293 PHE A 294 5 ? 2  
HELX_P HELX_P10 AB1 ASP A 152 ? GLU A 155 ? ASP A 295 GLU A 298 5 ? 4  
HELX_P HELX_P11 AB2 ARG A 165 ? LEU A 169 ? ARG A 308 LEU A 312 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 170 ? ARG A 175 ? ASP A 313 ARG A 318 5 ? 6  
HELX_P HELX_P13 AB4 ASP A 189 ? HIS A 200 ? ASP A 332 HIS A 343 1 ? 12 
HELX_P HELX_P14 AB5 ASN A 211 ? ARG A 218 ? ASN A 354 ARG A 361 1 ? 8  
HELX_P HELX_P15 AB6 VAL A 223 ? ARG A 240 ? VAL A 366 ARG A 383 1 ? 18 
HELX_P HELX_P16 AB7 THR A 247 ? ILE A 259 ? THR A 390 ILE A 402 1 ? 13 
HELX_P HELX_P17 AB8 SER A 270 ? VAL A 291 ? SER A 413 VAL A 434 1 ? 22 
HELX_P HELX_P18 AB9 SER A 325 ? LEU A 337 ? SER A 468 LEU A 480 1 ? 13 
HELX_P HELX_P19 AC1 LEU A 337 ? PHE A 347 ? LEU A 480 PHE A 490 1 ? 11 
HELX_P HELX_P20 AC2 THR A 351 ? GLY A 373 ? THR A 494 GLY A 516 1 ? 23 
HELX_P HELX_P21 AC3 ILE A 410 ? LYS A 431 ? ILE A 553 LYS A 574 1 ? 22 
HELX_P HELX_P22 AC4 TYR A 432 ? GLU A 447 ? TYR A 575 GLU A 590 1 ? 16 
HELX_P HELX_P23 AC5 GLU A 450 ? GLU A 461 ? GLU A 593 GLU A 604 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A THR 65  OG1 ? ? ? 1_555 B MG  . MG  ? ? A THR 208 A MG  800 1_555 ? ? ? ? ? ? ? 2.871 ? ? 
metalc2 metalc ? ? A HIS 280 NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 423 A ZN  801 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc3 metalc ? ? A HIS 284 NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 427 A ZN  801 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc4 metalc ? ? A ASP 357 OD2 ? ? ? 1_555 C ZN  . ZN  ? ? A ASP 500 A ZN  801 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc5 metalc ? ? B MG  .   MG  ? ? ? 1_555 D ATP . O3G ? ? A MG  800 A ATP 802 1_555 ? ? ? ? ? ? ? 2.385 ? ? 
metalc6 metalc ? ? B MG  .   MG  ? ? ? 1_555 D ATP . O2B ? ? A MG  800 A ATP 802 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG1 ? A THR 65  ? A THR 208 ? 1_555 MG ? B MG . ? A MG 800 ? 1_555 O3G ? D ATP .   ? A ATP 802 ? 1_555 156.4 ? 
2 OG1 ? A THR 65  ? A THR 208 ? 1_555 MG ? B MG . ? A MG 800 ? 1_555 O2B ? D ATP .   ? A ATP 802 ? 1_555 80.0  ? 
3 O3G ? D ATP .   ? A ATP 802 ? 1_555 MG ? B MG . ? A MG 800 ? 1_555 O2B ? D ATP .   ? A ATP 802 ? 1_555 80.8  ? 
4 NE2 ? A HIS 280 ? A HIS 423 ? 1_555 ZN ? C ZN . ? A ZN 801 ? 1_555 NE2 ? A HIS 284 ? A HIS 427 ? 1_555 107.7 ? 
5 NE2 ? A HIS 280 ? A HIS 423 ? 1_555 ZN ? C ZN . ? A ZN 801 ? 1_555 OD2 ? A ASP 357 ? A ASP 500 ? 1_555 115.2 ? 
6 NE2 ? A HIS 284 ? A HIS 427 ? 1_555 ZN ? C ZN . ? A ZN 801 ? 1_555 OD2 ? A ASP 357 ? A ASP 500 ? 1_555 111.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 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 PHE A 80  ? SER A 83  ? PHE A 223 SER A 226 
AA1 2 SER A 112 ? ASP A 117 ? SER A 255 ASP A 260 
AA1 3 ILE A 157 ? THR A 163 ? ILE A 300 THR A 306 
AA1 4 GLY A 53  ? VAL A 57  ? GLY A 196 VAL A 200 
AA1 5 LYS A 182 ? VAL A 184 ? LYS A 325 VAL A 327 
AA2 1 ILE A 300 ? SER A 301 ? ILE A 443 SER A 444 
AA2 2 THR A 448 ? ILE A 449 ? THR A 591 ILE A 592 
# 
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 82  ? N ILE A 225 O ASP A 117 ? O ASP A 260 
AA1 2 3 N VAL A 114 ? N VAL A 257 O MET A 160 ? O MET A 303 
AA1 3 4 O ALA A 161 ? O ALA A 304 N LEU A 56  ? N LEU A 199 
AA1 4 5 N VAL A 57  ? N VAL A 200 O ILE A 183 ? O ILE A 326 
AA2 1 2 N ILE A 300 ? N ILE A 443 O ILE A 449 ? O ILE A 592 
# 
_pdbx_entry_details.entry_id                   8VW9 
_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 ASP A 182 ? ? -154.86 88.58 
2 1 GLU A 590 ? ? 75.13   -7.08 
# 
_pdbx_helical_symmetry.entry_id                  8VW9 
_pdbx_helical_symmetry.number_of_operations      30 
_pdbx_helical_symmetry.rotation_per_n_subunits   157.5 
_pdbx_helical_symmetry.rise_per_n_subunits       9.1 
_pdbx_helical_symmetry.n_subunits_divisor        1 
_pdbx_helical_symmetry.dyad_axis                 no 
_pdbx_helical_symmetry.circular_symmetry         1 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8VW9 
_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                    8VW9 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.6 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               840601 
_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               HELICAL 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            6.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Cryo-EM Structure of FtsH Helical Assembly' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8VW9 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_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                      2.7 
_em_imaging.nominal_defocus_min             1500 
_em_imaging.nominal_defocus_max             2100 
_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            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R2/1' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8VW9 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              95 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8VW9 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   HELICAL 
_em_experiment.aggregation_state       'HELICAL ARRAY' 
_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 SER 144 ? A SER 1   
2  1 Y 1 A GLY 145 ? A GLY 2   
3  1 Y 1 A GLY 146 ? A GLY 3   
4  1 Y 1 A ALA 147 ? A ALA 4   
5  1 Y 1 A THR 148 ? A THR 5   
6  1 Y 1 A MET 149 ? A MET 6   
7  1 Y 1 A TYR 150 ? A TYR 7   
8  1 Y 1 A LYS 151 ? A LYS 8   
9  1 Y 1 A PRO 152 ? A PRO 9   
10 1 Y 1 A SER 153 ? A SER 10  
11 1 Y 1 A GLY 154 ? A GLY 11  
12 1 Y 1 A ASN 155 ? A ASN 12  
13 1 Y 1 A VAL 231 ? A VAL 88  
14 1 Y 1 A GLU 232 ? A GLU 89  
15 1 Y 1 A LEU 233 ? A LEU 90  
16 1 Y 1 A PHE 234 ? A PHE 91  
17 1 Y 1 A VAL 235 ? A VAL 92  
18 1 Y 1 A GLY 236 ? A GLY 93  
19 1 Y 1 A ARG 267 ? A ARG 124 
20 1 Y 1 A HIS 268 ? A HIS 125 
21 1 Y 1 A ARG 269 ? A ARG 126 
22 1 Y 1 A GLY 270 ? A GLY 127 
23 1 Y 1 A ALA 271 ? A ALA 128 
24 1 Y 1 A GLY 272 ? A GLY 129 
25 1 Y 1 A LEU 273 ? A LEU 130 
26 1 Y 1 A GLY 274 ? A GLY 131 
27 1 Y 1 A GLY 275 ? A GLY 132 
28 1 Y 1 A GLY 276 ? A GLY 133 
29 1 Y 1 A HIS 277 ? A HIS 134 
30 1 Y 1 A ASP 278 ? A ASP 135 
31 1 Y 1 A GLU 279 ? A GLU 136 
32 1 Y 1 A MET 517 ? A MET 374 
33 1 Y 1 A SER 518 ? A SER 375 
34 1 Y 1 A GLU 519 ? A GLU 376 
35 1 Y 1 A GLU 520 ? A GLU 377 
36 1 Y 1 A LEU 521 ? A LEU 378 
37 1 Y 1 A GLY 522 ? A GLY 379 
38 1 Y 1 A PRO 523 ? A PRO 380 
39 1 Y 1 A LEU 524 ? A LEU 381 
40 1 Y 1 A ALA 525 ? A ALA 382 
41 1 Y 1 A TRP 526 ? A TRP 383 
42 1 Y 1 A GLY 527 ? A GLY 384 
43 1 Y 1 A LYS 528 ? A LYS 385 
44 1 Y 1 A GLU 529 ? A GLU 386 
45 1 Y 1 A GLU 530 ? A GLU 387 
46 1 Y 1 A GLN 531 ? A GLN 388 
47 1 Y 1 A GLU 532 ? A GLU 389 
48 1 Y 1 A VAL 533 ? A VAL 390 
49 1 Y 1 A PHE 534 ? A PHE 391 
50 1 Y 1 A LEU 535 ? A LEU 392 
51 1 Y 1 A GLY 536 ? A GLY 393 
52 1 Y 1 A LYS 537 ? A LYS 394 
53 1 Y 1 A GLU 538 ? A GLU 395 
54 1 Y 1 A ILE 539 ? A ILE 396 
55 1 Y 1 A THR 540 ? A THR 397 
56 1 Y 1 A ARG 541 ? A ARG 398 
57 1 Y 1 A LEU 542 ? A LEU 399 
58 1 Y 1 A ARG 543 ? A ARG 400 
59 1 Y 1 A ASN 544 ? A ASN 401 
60 1 Y 1 A TYR 545 ? A TYR 402 
61 1 Y 1 A SER 546 ? A SER 403 
62 1 Y 1 A GLU 547 ? A GLU 404 
63 1 Y 1 A GLU 548 ? A GLU 405 
64 1 Y 1 A VAL 549 ? A VAL 406 
65 1 Y 1 A ALA 550 ? A ALA 407 
66 1 Y 1 A SER 551 ? A SER 408 
67 1 Y 1 A GLU 606 ? A GLU 463 
68 1 Y 1 A LYS 607 ? A LYS 464 
69 1 Y 1 A VAL 608 ? A VAL 465 
70 1 Y 1 A VAL 609 ? A VAL 466 
71 1 Y 1 A GLU 610 ? A GLU 467 
# 
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  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GLN N      N  N N 135 
GLN CA     C  N S 136 
GLN C      C  N N 137 
GLN O      O  N N 138 
GLN CB     C  N N 139 
GLN CG     C  N N 140 
GLN CD     C  N N 141 
GLN OE1    O  N N 142 
GLN NE2    N  N N 143 
GLN OXT    O  N N 144 
GLN H      H  N N 145 
GLN H2     H  N N 146 
GLN HA     H  N N 147 
GLN HB2    H  N N 148 
GLN HB3    H  N N 149 
GLN HG2    H  N N 150 
GLN HG3    H  N N 151 
GLN HE21   H  N N 152 
GLN HE22   H  N N 153 
GLN HXT    H  N N 154 
GLU N      N  N N 155 
GLU CA     C  N S 156 
GLU C      C  N N 157 
GLU O      O  N N 158 
GLU CB     C  N N 159 
GLU CG     C  N N 160 
GLU CD     C  N N 161 
GLU OE1    O  N N 162 
GLU OE2    O  N N 163 
GLU OXT    O  N N 164 
GLU H      H  N N 165 
GLU H2     H  N N 166 
GLU HA     H  N N 167 
GLU HB2    H  N N 168 
GLU HB3    H  N N 169 
GLU HG2    H  N N 170 
GLU HG3    H  N N 171 
GLU HE2    H  N N 172 
GLU HXT    H  N N 173 
GLY N      N  N N 174 
GLY CA     C  N N 175 
GLY C      C  N N 176 
GLY O      O  N N 177 
GLY OXT    O  N N 178 
GLY H      H  N N 179 
GLY H2     H  N N 180 
GLY HA2    H  N N 181 
GLY HA3    H  N N 182 
GLY HXT    H  N N 183 
HIS N      N  N N 184 
HIS CA     C  N S 185 
HIS C      C  N N 186 
HIS O      O  N N 187 
HIS CB     C  N N 188 
HIS CG     C  Y N 189 
HIS ND1    N  Y N 190 
HIS CD2    C  Y N 191 
HIS CE1    C  Y N 192 
HIS NE2    N  Y N 193 
HIS OXT    O  N N 194 
HIS H      H  N N 195 
HIS H2     H  N N 196 
HIS HA     H  N N 197 
HIS HB2    H  N N 198 
HIS HB3    H  N N 199 
HIS HD1    H  N N 200 
HIS HD2    H  N N 201 
HIS HE1    H  N N 202 
HIS HE2    H  N N 203 
HIS HXT    H  N N 204 
ILE N      N  N N 205 
ILE CA     C  N S 206 
ILE C      C  N N 207 
ILE O      O  N N 208 
ILE CB     C  N S 209 
ILE CG1    C  N N 210 
ILE CG2    C  N N 211 
ILE CD1    C  N N 212 
ILE OXT    O  N N 213 
ILE H      H  N N 214 
ILE H2     H  N N 215 
ILE HA     H  N N 216 
ILE HB     H  N N 217 
ILE HG12   H  N N 218 
ILE HG13   H  N N 219 
ILE HG21   H  N N 220 
ILE HG22   H  N N 221 
ILE HG23   H  N N 222 
ILE HD11   H  N N 223 
ILE HD12   H  N N 224 
ILE HD13   H  N N 225 
ILE HXT    H  N N 226 
LEU N      N  N N 227 
LEU CA     C  N S 228 
LEU C      C  N N 229 
LEU O      O  N N 230 
LEU CB     C  N N 231 
LEU CG     C  N N 232 
LEU CD1    C  N N 233 
LEU CD2    C  N N 234 
LEU OXT    O  N N 235 
LEU H      H  N N 236 
LEU H2     H  N N 237 
LEU HA     H  N N 238 
LEU HB2    H  N N 239 
LEU HB3    H  N N 240 
LEU HG     H  N N 241 
LEU HD11   H  N N 242 
LEU HD12   H  N N 243 
LEU HD13   H  N N 244 
LEU HD21   H  N N 245 
LEU HD22   H  N N 246 
LEU HD23   H  N N 247 
LEU HXT    H  N N 248 
LYS N      N  N N 249 
LYS CA     C  N S 250 
LYS C      C  N N 251 
LYS O      O  N N 252 
LYS CB     C  N N 253 
LYS CG     C  N N 254 
LYS CD     C  N N 255 
LYS CE     C  N N 256 
LYS NZ     N  N N 257 
LYS OXT    O  N N 258 
LYS H      H  N N 259 
LYS H2     H  N N 260 
LYS HA     H  N N 261 
LYS HB2    H  N N 262 
LYS HB3    H  N N 263 
LYS HG2    H  N N 264 
LYS HG3    H  N N 265 
LYS HD2    H  N N 266 
LYS HD3    H  N N 267 
LYS HE2    H  N N 268 
LYS HE3    H  N N 269 
LYS HZ1    H  N N 270 
LYS HZ2    H  N N 271 
LYS HZ3    H  N N 272 
LYS HXT    H  N N 273 
MET N      N  N N 274 
MET CA     C  N S 275 
MET C      C  N N 276 
MET O      O  N N 277 
MET CB     C  N N 278 
MET CG     C  N N 279 
MET SD     S  N N 280 
MET CE     C  N N 281 
MET OXT    O  N N 282 
MET H      H  N N 283 
MET H2     H  N N 284 
MET HA     H  N N 285 
MET HB2    H  N N 286 
MET HB3    H  N N 287 
MET HG2    H  N N 288 
MET HG3    H  N N 289 
MET HE1    H  N N 290 
MET HE2    H  N N 291 
MET HE3    H  N N 292 
MET HXT    H  N N 293 
MG  MG     MG N N 294 
PHE N      N  N N 295 
PHE CA     C  N S 296 
PHE C      C  N N 297 
PHE O      O  N N 298 
PHE CB     C  N N 299 
PHE CG     C  Y N 300 
PHE CD1    C  Y N 301 
PHE CD2    C  Y N 302 
PHE CE1    C  Y N 303 
PHE CE2    C  Y N 304 
PHE CZ     C  Y N 305 
PHE OXT    O  N N 306 
PHE H      H  N N 307 
PHE H2     H  N N 308 
PHE HA     H  N N 309 
PHE HB2    H  N N 310 
PHE HB3    H  N N 311 
PHE HD1    H  N N 312 
PHE HD2    H  N N 313 
PHE HE1    H  N N 314 
PHE HE2    H  N N 315 
PHE HZ     H  N N 316 
PHE HXT    H  N N 317 
PRO N      N  N N 318 
PRO CA     C  N S 319 
PRO C      C  N N 320 
PRO O      O  N N 321 
PRO CB     C  N N 322 
PRO CG     C  N N 323 
PRO CD     C  N N 324 
PRO OXT    O  N N 325 
PRO H      H  N N 326 
PRO HA     H  N N 327 
PRO HB2    H  N N 328 
PRO HB3    H  N N 329 
PRO HG2    H  N N 330 
PRO HG3    H  N N 331 
PRO HD2    H  N N 332 
PRO HD3    H  N N 333 
PRO HXT    H  N N 334 
SER N      N  N N 335 
SER CA     C  N S 336 
SER C      C  N N 337 
SER O      O  N N 338 
SER CB     C  N N 339 
SER OG     O  N N 340 
SER OXT    O  N N 341 
SER H      H  N N 342 
SER H2     H  N N 343 
SER HA     H  N N 344 
SER HB2    H  N N 345 
SER HB3    H  N N 346 
SER HG     H  N N 347 
SER HXT    H  N N 348 
THR N      N  N N 349 
THR CA     C  N S 350 
THR C      C  N N 351 
THR O      O  N N 352 
THR CB     C  N R 353 
THR OG1    O  N N 354 
THR CG2    C  N N 355 
THR OXT    O  N N 356 
THR H      H  N N 357 
THR H2     H  N N 358 
THR HA     H  N N 359 
THR HB     H  N N 360 
THR HG1    H  N N 361 
THR HG21   H  N N 362 
THR HG22   H  N N 363 
THR HG23   H  N N 364 
THR HXT    H  N N 365 
TRP N      N  N N 366 
TRP CA     C  N S 367 
TRP C      C  N N 368 
TRP O      O  N N 369 
TRP CB     C  N N 370 
TRP CG     C  Y N 371 
TRP CD1    C  Y N 372 
TRP CD2    C  Y N 373 
TRP NE1    N  Y N 374 
TRP CE2    C  Y N 375 
TRP CE3    C  Y N 376 
TRP CZ2    C  Y N 377 
TRP CZ3    C  Y N 378 
TRP CH2    C  Y N 379 
TRP OXT    O  N N 380 
TRP H      H  N N 381 
TRP H2     H  N N 382 
TRP HA     H  N N 383 
TRP HB2    H  N N 384 
TRP HB3    H  N N 385 
TRP HD1    H  N N 386 
TRP HE1    H  N N 387 
TRP HE3    H  N N 388 
TRP HZ2    H  N N 389 
TRP HZ3    H  N N 390 
TRP HH2    H  N N 391 
TRP HXT    H  N N 392 
TYR N      N  N N 393 
TYR CA     C  N S 394 
TYR C      C  N N 395 
TYR O      O  N N 396 
TYR CB     C  N N 397 
TYR CG     C  Y N 398 
TYR CD1    C  Y N 399 
TYR CD2    C  Y N 400 
TYR CE1    C  Y N 401 
TYR CE2    C  Y N 402 
TYR CZ     C  Y N 403 
TYR OH     O  N N 404 
TYR OXT    O  N N 405 
TYR H      H  N N 406 
TYR H2     H  N N 407 
TYR HA     H  N N 408 
TYR HB2    H  N N 409 
TYR HB3    H  N N 410 
TYR HD1    H  N N 411 
TYR HD2    H  N N 412 
TYR HE1    H  N N 413 
TYR HE2    H  N N 414 
TYR HH     H  N N 415 
TYR HXT    H  N N 416 
VAL N      N  N N 417 
VAL CA     C  N S 418 
VAL C      C  N N 419 
VAL O      O  N N 420 
VAL CB     C  N N 421 
VAL CG1    C  N N 422 
VAL CG2    C  N N 423 
VAL OXT    O  N N 424 
VAL H      H  N N 425 
VAL H2     H  N N 426 
VAL HA     H  N N 427 
VAL HB     H  N N 428 
VAL HG11   H  N N 429 
VAL HG12   H  N N 430 
VAL HG13   H  N N 431 
VAL HG21   H  N N 432 
VAL HG22   H  N N 433 
VAL HG23   H  N N 434 
VAL HXT    H  N N 435 
ZN  ZN     ZN N N 436 
# 
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  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GLN N     CA     sing N N 132 
GLN N     H      sing N N 133 
GLN N     H2     sing N N 134 
GLN CA    C      sing N N 135 
GLN CA    CB     sing N N 136 
GLN CA    HA     sing N N 137 
GLN C     O      doub N N 138 
GLN C     OXT    sing N N 139 
GLN CB    CG     sing N N 140 
GLN CB    HB2    sing N N 141 
GLN CB    HB3    sing N N 142 
GLN CG    CD     sing N N 143 
GLN CG    HG2    sing N N 144 
GLN CG    HG3    sing N N 145 
GLN CD    OE1    doub N N 146 
GLN CD    NE2    sing N N 147 
GLN NE2   HE21   sing N N 148 
GLN NE2   HE22   sing N N 149 
GLN OXT   HXT    sing N N 150 
GLU N     CA     sing N N 151 
GLU N     H      sing N N 152 
GLU N     H2     sing N N 153 
GLU CA    C      sing N N 154 
GLU CA    CB     sing N N 155 
GLU CA    HA     sing N N 156 
GLU C     O      doub N N 157 
GLU C     OXT    sing N N 158 
GLU CB    CG     sing N N 159 
GLU CB    HB2    sing N N 160 
GLU CB    HB3    sing N N 161 
GLU CG    CD     sing N N 162 
GLU CG    HG2    sing N N 163 
GLU CG    HG3    sing N N 164 
GLU CD    OE1    doub N N 165 
GLU CD    OE2    sing N N 166 
GLU OE2   HE2    sing N N 167 
GLU OXT   HXT    sing N N 168 
GLY N     CA     sing N N 169 
GLY N     H      sing N N 170 
GLY N     H2     sing N N 171 
GLY CA    C      sing N N 172 
GLY CA    HA2    sing N N 173 
GLY CA    HA3    sing N N 174 
GLY C     O      doub N N 175 
GLY C     OXT    sing N N 176 
GLY OXT   HXT    sing N N 177 
HIS N     CA     sing N N 178 
HIS N     H      sing N N 179 
HIS N     H2     sing N N 180 
HIS CA    C      sing N N 181 
HIS CA    CB     sing N N 182 
HIS CA    HA     sing N N 183 
HIS C     O      doub N N 184 
HIS C     OXT    sing N N 185 
HIS CB    CG     sing N N 186 
HIS CB    HB2    sing N N 187 
HIS CB    HB3    sing N N 188 
HIS CG    ND1    sing Y N 189 
HIS CG    CD2    doub Y N 190 
HIS ND1   CE1    doub Y N 191 
HIS ND1   HD1    sing N N 192 
HIS CD2   NE2    sing Y N 193 
HIS CD2   HD2    sing N N 194 
HIS CE1   NE2    sing Y N 195 
HIS CE1   HE1    sing N N 196 
HIS NE2   HE2    sing N N 197 
HIS OXT   HXT    sing N N 198 
ILE N     CA     sing N N 199 
ILE N     H      sing N N 200 
ILE N     H2     sing N N 201 
ILE CA    C      sing N N 202 
ILE CA    CB     sing N N 203 
ILE CA    HA     sing N N 204 
ILE C     O      doub N N 205 
ILE C     OXT    sing N N 206 
ILE CB    CG1    sing N N 207 
ILE CB    CG2    sing N N 208 
ILE CB    HB     sing N N 209 
ILE CG1   CD1    sing N N 210 
ILE CG1   HG12   sing N N 211 
ILE CG1   HG13   sing N N 212 
ILE CG2   HG21   sing N N 213 
ILE CG2   HG22   sing N N 214 
ILE CG2   HG23   sing N N 215 
ILE CD1   HD11   sing N N 216 
ILE CD1   HD12   sing N N 217 
ILE CD1   HD13   sing N N 218 
ILE OXT   HXT    sing N N 219 
LEU N     CA     sing N N 220 
LEU N     H      sing N N 221 
LEU N     H2     sing N N 222 
LEU CA    C      sing N N 223 
LEU CA    CB     sing N N 224 
LEU CA    HA     sing N N 225 
LEU C     O      doub N N 226 
LEU C     OXT    sing N N 227 
LEU CB    CG     sing N N 228 
LEU CB    HB2    sing N N 229 
LEU CB    HB3    sing N N 230 
LEU CG    CD1    sing N N 231 
LEU CG    CD2    sing N N 232 
LEU CG    HG     sing N N 233 
LEU CD1   HD11   sing N N 234 
LEU CD1   HD12   sing N N 235 
LEU CD1   HD13   sing N N 236 
LEU CD2   HD21   sing N N 237 
LEU CD2   HD22   sing N N 238 
LEU CD2   HD23   sing N N 239 
LEU OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
THR N     CA     sing N N 337 
THR N     H      sing N N 338 
THR N     H2     sing N N 339 
THR CA    C      sing N N 340 
THR CA    CB     sing N N 341 
THR CA    HA     sing N N 342 
THR C     O      doub N N 343 
THR C     OXT    sing N N 344 
THR CB    OG1    sing N N 345 
THR CB    CG2    sing N N 346 
THR CB    HB     sing N N 347 
THR OG1   HG1    sing N N 348 
THR CG2   HG21   sing N N 349 
THR CG2   HG22   sing N N 350 
THR CG2   HG23   sing N N 351 
THR OXT   HXT    sing N N 352 
TRP N     CA     sing N N 353 
TRP N     H      sing N N 354 
TRP N     H2     sing N N 355 
TRP CA    C      sing N N 356 
TRP CA    CB     sing N N 357 
TRP CA    HA     sing N N 358 
TRP C     O      doub N N 359 
TRP C     OXT    sing N N 360 
TRP CB    CG     sing N N 361 
TRP CB    HB2    sing N N 362 
TRP CB    HB3    sing N N 363 
TRP CG    CD1    doub Y N 364 
TRP CG    CD2    sing Y N 365 
TRP CD1   NE1    sing Y N 366 
TRP CD1   HD1    sing N N 367 
TRP CD2   CE2    doub Y N 368 
TRP CD2   CE3    sing Y N 369 
TRP NE1   CE2    sing Y N 370 
TRP NE1   HE1    sing N N 371 
TRP CE2   CZ2    sing Y N 372 
TRP CE3   CZ3    doub Y N 373 
TRP CE3   HE3    sing N N 374 
TRP CZ2   CH2    doub Y N 375 
TRP CZ2   HZ2    sing N N 376 
TRP CZ3   CH2    sing Y N 377 
TRP CZ3   HZ3    sing N N 378 
TRP CH2   HH2    sing N N 379 
TRP OXT   HXT    sing N N 380 
TYR N     CA     sing N N 381 
TYR N     H      sing N N 382 
TYR N     H2     sing N N 383 
TYR CA    C      sing N N 384 
TYR CA    CB     sing N N 385 
TYR CA    HA     sing N N 386 
TYR C     O      doub N N 387 
TYR C     OXT    sing N N 388 
TYR CB    CG     sing N N 389 
TYR CB    HB2    sing N N 390 
TYR CB    HB3    sing N N 391 
TYR CG    CD1    doub Y N 392 
TYR CG    CD2    sing Y N 393 
TYR CD1   CE1    sing Y N 394 
TYR CD1   HD1    sing N N 395 
TYR CD2   CE2    doub Y N 396 
TYR CD2   HD2    sing N N 397 
TYR CE1   CZ     doub Y N 398 
TYR CE1   HE1    sing N N 399 
TYR CE2   CZ     sing Y N 400 
TYR CE2   HE2    sing N N 401 
TYR CZ    OH     sing N N 402 
TYR OH    HH     sing N N 403 
TYR OXT   HXT    sing N N 404 
VAL N     CA     sing N N 405 
VAL N     H      sing N N 406 
VAL N     H2     sing N N 407 
VAL CA    C      sing N N 408 
VAL CA    CB     sing N N 409 
VAL CA    HA     sing N N 410 
VAL C     O      doub N N 411 
VAL C     OXT    sing N N 412 
VAL CB    CG1    sing N N 413 
VAL CB    CG2    sing N N 414 
VAL CB    HB     sing N N 415 
VAL CG1   HG11   sing N N 416 
VAL CG1   HG12   sing N N 417 
VAL CG1   HG13   sing N N 418 
VAL CG2   HG21   sing N N 419 
VAL CG2   HG22   sing N N 420 
VAL CG2   HG23   sing N N 421 
VAL OXT   HXT    sing N N 422 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-01-31 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           8VW9 
_em_admin.last_update        2025-01-29 
_em_admin.map_release_date   2025-01-15 
_em_admin.title              'CryoEM Structure of a FtsH Helical Assembly in the Presence of ATP' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
_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          2336 
_em_entity_assembly_naturalsource.organism             'Thermotoga maritima' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_helical_entity.id                             1 
_em_helical_entity.image_processing_id            1 
_em_helical_entity.details                        ? 
_em_helical_entity.axial_symmetry                 C1 
_em_helical_entity.angular_rotation_per_subunit   157.5 
_em_helical_entity.axial_rise_per_subunit         9.1 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ?         ?          
'MODEL REFINEMENT'              ? 2  ? ? ? PHENIX    1.14_3260: 
'IMAGE ACQUISITION'             ? 3  ? ? 1 ?         ?          
MASKING                         ? 4  ? ? ? ?         ?          
'CTF CORRECTION'                ? 5  1 ? ? ?         ?          
'LAYERLINE INDEXING'            ? 6  ? ? ? ?         ?          
'DIFFRACTION INDEXING'          ? 7  ? ? ? ?         ?          
'MODEL FITTING'                 ? 8  ? ? ? ?         ?          
OTHER                           ? 9  ? ? ? ?         ?          
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?         ?          
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ?         ?          
CLASSIFICATION                  ? 12 1 ? ? ?         ?          
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC ?          
'VOLUME SELECTION'              ? 14 1 1 1 ?         ?          
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ?          
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ?          
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ?          
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ?          
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?         ?          
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' DMR-2004558  1 
'Department of Energy (DOE, United States)'        'United States' DE-SC0003844 2 
'Department of Energy (DOE, United States)'        'United States' DE-SC0019288 3 
# 
_atom_sites.entry_id                    8VW9 
_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  
H  
MG 
N  
O  
P  
S  
ZN 
# 
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      . LYS A 1 13  ? 222.403 146.733 203.991 1.00 68.58  ? 156 LYS A N      1 
ATOM   2    C  CA     . LYS A 1 13  ? 223.096 145.559 203.474 1.00 71.25  ? 156 LYS A CA     1 
ATOM   3    C  C      . LYS A 1 13  ? 224.096 145.947 202.389 1.00 66.30  ? 156 LYS A C      1 
ATOM   4    O  O      . LYS A 1 13  ? 223.858 146.874 201.616 1.00 66.12  ? 156 LYS A O      1 
ATOM   5    C  CB     . LYS A 1 13  ? 222.094 144.542 202.928 1.00 73.32  ? 156 LYS A CB     1 
ATOM   6    C  CG     . LYS A 1 13  ? 222.726 143.248 202.442 1.00 76.68  ? 156 LYS A CG     1 
ATOM   7    C  CD     . LYS A 1 13  ? 221.688 142.319 201.835 1.00 86.13  ? 156 LYS A CD     1 
ATOM   8    C  CE     . LYS A 1 13  ? 221.238 142.811 200.469 1.00 84.61  ? 156 LYS A CE     1 
ATOM   9    N  NZ     . LYS A 1 13  ? 220.311 141.850 199.810 1.00 87.40  ? 156 LYS A NZ     1 
ATOM   10   N  N      . ARG A 1 14  ? 225.213 145.228 202.337 1.00 62.58  ? 157 ARG A N      1 
ATOM   11   C  CA     . ARG A 1 14  ? 226.261 145.494 201.363 1.00 59.16  ? 157 ARG A CA     1 
ATOM   12   C  C      . ARG A 1 14  ? 226.025 144.681 200.097 1.00 57.19  ? 157 ARG A C      1 
ATOM   13   O  O      . ARG A 1 14  ? 225.701 143.492 200.158 1.00 61.43  ? 157 ARG A O      1 
ATOM   14   C  CB     . ARG A 1 14  ? 227.635 145.166 201.949 1.00 58.00  ? 157 ARG A CB     1 
ATOM   15   C  CG     . ARG A 1 14  ? 228.783 145.313 200.966 1.00 60.39  ? 157 ARG A CG     1 
ATOM   16   C  CD     . ARG A 1 14  ? 229.977 144.472 201.383 1.00 66.55  ? 157 ARG A CD     1 
ATOM   17   N  NE     . ARG A 1 14  ? 231.024 144.469 200.369 1.00 71.21  ? 157 ARG A NE     1 
ATOM   18   C  CZ     . ARG A 1 14  ? 232.060 143.640 200.365 1.00 77.21  ? 157 ARG A CZ     1 
ATOM   19   N  NH1    . ARG A 1 14  ? 232.220 142.730 201.311 1.00 80.59  ? 157 ARG A NH1    1 
ATOM   20   N  NH2    . ARG A 1 14  ? 232.957 143.727 199.387 1.00 69.17  ? 157 ARG A NH2    1 
ATOM   21   N  N      . VAL A 1 15  ? 226.192 145.333 198.947 1.00 49.49  ? 158 VAL A N      1 
ATOM   22   C  CA     . VAL A 1 15  ? 225.978 144.704 197.651 1.00 47.42  ? 158 VAL A CA     1 
ATOM   23   C  C      . VAL A 1 15  ? 227.183 144.967 196.761 1.00 40.77  ? 158 VAL A C      1 
ATOM   24   O  O      . VAL A 1 15  ? 227.919 145.941 196.947 1.00 43.90  ? 158 VAL A O      1 
ATOM   25   C  CB     . VAL A 1 15  ? 224.684 145.207 196.973 1.00 45.81  ? 158 VAL A CB     1 
ATOM   26   C  CG1    . VAL A 1 15  ? 223.462 144.675 197.702 1.00 52.28  ? 158 VAL A CG1    1 
ATOM   27   C  CG2    . VAL A 1 15  ? 224.665 146.726 196.927 1.00 37.14  ? 158 VAL A CG2    1 
ATOM   28   N  N      . THR A 1 16  ? 227.380 144.084 195.783 1.00 40.92  ? 159 THR A N      1 
ATOM   29   C  CA     . THR A 1 16  ? 228.459 144.231 194.815 1.00 38.83  ? 159 THR A CA     1 
ATOM   30   C  C      . THR A 1 16  ? 227.928 144.040 193.400 1.00 39.12  ? 159 THR A C      1 
ATOM   31   O  O      . THR A 1 16  ? 226.713 143.971 193.193 1.00 43.43  ? 159 THR A O      1 
ATOM   32   C  CB     . THR A 1 16  ? 229.585 143.235 195.100 1.00 46.28  ? 159 THR A CB     1 
ATOM   33   O  OG1    . THR A 1 16  ? 229.043 141.912 195.196 1.00 53.44  ? 159 THR A OG1    1 
ATOM   34   C  CG2    . THR A 1 16  ? 230.288 143.585 196.403 1.00 42.51  ? 159 THR A CG2    1 
ATOM   35   N  N      . PHE A 1 17  ? 228.828 143.954 192.420 1.00 38.30  ? 160 PHE A N      1 
ATOM   36   C  CA     . PHE A 1 17  ? 228.412 143.772 191.035 1.00 37.16  ? 160 PHE A CA     1 
ATOM   37   C  C      . PHE A 1 17  ? 227.817 142.396 190.771 1.00 40.85  ? 160 PHE A C      1 
ATOM   38   O  O      . PHE A 1 17  ? 227.228 142.191 189.705 1.00 42.58  ? 160 PHE A O      1 
ATOM   39   C  CB     . PHE A 1 17  ? 229.594 144.013 190.094 1.00 36.63  ? 160 PHE A CB     1 
ATOM   40   C  CG     . PHE A 1 17  ? 229.861 145.465 189.817 1.00 40.24  ? 160 PHE A CG     1 
ATOM   41   C  CD1    . PHE A 1 17  ? 228.846 146.400 189.916 1.00 37.93  ? 160 PHE A CD1    1 
ATOM   42   C  CD2    . PHE A 1 17  ? 231.127 145.893 189.456 1.00 41.43  ? 160 PHE A CD2    1 
ATOM   43   C  CE1    . PHE A 1 17  ? 229.088 147.736 189.662 1.00 34.13  ? 160 PHE A CE1    1 
ATOM   44   C  CE2    . PHE A 1 17  ? 231.375 147.227 189.202 1.00 37.14  ? 160 PHE A CE2    1 
ATOM   45   C  CZ     . PHE A 1 17  ? 230.355 148.149 189.304 1.00 34.05  ? 160 PHE A CZ     1 
ATOM   46   N  N      . LYS A 1 18  ? 227.953 141.453 191.706 1.00 42.05  ? 161 LYS A N      1 
ATOM   47   C  CA     . LYS A 1 18  ? 227.363 140.132 191.537 1.00 43.69  ? 161 LYS A CA     1 
ATOM   48   C  C      . LYS A 1 18  ? 225.855 140.128 191.747 1.00 40.00  ? 161 LYS A C      1 
ATOM   49   O  O      . LYS A 1 18  ? 225.211 139.114 191.460 1.00 40.70  ? 161 LYS A O      1 
ATOM   50   C  CB     . LYS A 1 18  ? 228.017 139.137 192.497 1.00 47.36  ? 161 LYS A CB     1 
ATOM   51   C  CG     . LYS A 1 18  ? 229.429 138.733 192.107 1.00 56.74  ? 161 LYS A CG     1 
ATOM   52   C  CD     . LYS A 1 18  ? 230.002 137.719 193.082 1.00 68.39  ? 161 LYS A CD     1 
ATOM   53   C  CE     . LYS A 1 18  ? 230.399 138.377 194.393 1.00 74.85  ? 161 LYS A CE     1 
ATOM   54   N  NZ     . LYS A 1 18  ? 231.067 137.417 195.314 1.00 83.19  ? 161 LYS A NZ     1 
ATOM   55   N  N      . ASP A 1 19  ? 225.281 141.227 192.236 1.00 36.86  ? 162 ASP A N      1 
ATOM   56   C  CA     . ASP A 1 19  ? 223.851 141.328 192.492 1.00 32.85  ? 162 ASP A CA     1 
ATOM   57   C  C      . ASP A 1 19  ? 223.115 142.104 191.404 1.00 29.56  ? 162 ASP A C      1 
ATOM   58   O  O      . ASP A 1 19  ? 221.962 142.496 191.606 1.00 30.83  ? 162 ASP A O      1 
ATOM   59   C  CB     . ASP A 1 19  ? 223.608 141.974 193.857 1.00 36.46  ? 162 ASP A CB     1 
ATOM   60   C  CG     . ASP A 1 19  ? 224.308 141.241 194.983 1.00 45.83  ? 162 ASP A CG     1 
ATOM   61   O  OD1    . ASP A 1 19  ? 224.180 140.002 195.059 1.00 53.08  ? 162 ASP A OD1    1 
ATOM   62   O  OD2    . ASP A 1 19  ? 224.987 141.905 195.794 1.00 48.30  ? 162 ASP A OD2    1 
ATOM   63   N  N      . VAL A 1 20  ? 223.756 142.333 190.260 1.00 28.54  ? 163 VAL A N      1 
ATOM   64   C  CA     . VAL A 1 20  ? 223.181 143.102 189.165 1.00 27.70  ? 163 VAL A CA     1 
ATOM   65   C  C      . VAL A 1 20  ? 223.156 142.234 187.916 1.00 30.71  ? 163 VAL A C      1 
ATOM   66   O  O      . VAL A 1 20  ? 224.124 141.525 187.621 1.00 35.05  ? 163 VAL A O      1 
ATOM   67   C  CB     . VAL A 1 20  ? 223.968 144.404 188.906 1.00 28.58  ? 163 VAL A CB     1 
ATOM   68   C  CG1    . VAL A 1 20  ? 223.207 145.302 187.942 1.00 22.38  ? 163 VAL A CG1    1 
ATOM   69   C  CG2    . VAL A 1 20  ? 224.245 145.128 190.213 1.00 26.69  ? 163 VAL A CG2    1 
ATOM   70   N  N      . GLY A 1 21  ? 222.053 142.292 187.187 1.00 27.67  ? 164 GLY A N      1 
ATOM   71   C  CA     . GLY A 1 21  ? 221.899 141.508 185.972 1.00 24.79  ? 164 GLY A CA     1 
ATOM   72   C  C      . GLY A 1 21  ? 221.448 142.358 184.805 1.00 30.63  ? 164 GLY A C      1 
ATOM   73   O  O      . GLY A 1 21  ? 220.642 143.274 184.964 1.00 30.77  ? 164 GLY A O      1 
ATOM   74   N  N      . GLY A 1 22  ? 221.979 142.043 183.629 1.00 36.35  ? 165 GLY A N      1 
ATOM   75   C  CA     . GLY A 1 22  ? 221.596 142.727 182.404 1.00 40.81  ? 165 GLY A CA     1 
ATOM   76   C  C      . GLY A 1 22  ? 221.989 144.186 182.322 1.00 47.86  ? 165 GLY A C      1 
ATOM   77   O  O      . GLY A 1 22  ? 221.234 144.995 181.769 1.00 50.66  ? 165 GLY A O      1 
ATOM   78   N  N      . ALA A 1 23  ? 223.154 144.545 182.855 1.00 42.72  ? 166 ALA A N      1 
ATOM   79   C  CA     . ALA A 1 23  ? 223.660 145.914 182.789 1.00 41.48  ? 166 ALA A CA     1 
ATOM   80   C  C      . ALA A 1 23  ? 225.142 145.903 182.427 1.00 46.02  ? 166 ALA A C      1 
ATOM   81   O  O      . ALA A 1 23  ? 225.963 146.592 183.034 1.00 47.53  ? 166 ALA A O      1 
ATOM   82   C  CB     . ALA A 1 23  ? 223.416 146.651 184.104 1.00 36.08  ? 166 ALA A CB     1 
ATOM   83   N  N      . GLU A 1 24  ? 225.499 145.105 181.419 1.00 47.34  ? 167 GLU A N      1 
ATOM   84   C  CA     . GLU A 1 24  ? 226.907 144.933 181.075 1.00 47.04  ? 167 GLU A CA     1 
ATOM   85   C  C      . GLU A 1 24  ? 227.533 146.238 180.594 1.00 45.84  ? 167 GLU A C      1 
ATOM   86   O  O      . GLU A 1 24  ? 228.623 146.612 181.045 1.00 46.85  ? 167 GLU A O      1 
ATOM   87   C  CB     . GLU A 1 24  ? 227.053 143.844 180.013 1.00 50.08  ? 167 GLU A CB     1 
ATOM   88   C  CG     . GLU A 1 24  ? 227.010 142.428 180.565 1.00 56.45  ? 167 GLU A CG     1 
ATOM   89   C  CD     . GLU A 1 24  ? 225.662 141.764 180.361 1.00 65.26  ? 167 GLU A CD     1 
ATOM   90   O  OE1    . GLU A 1 24  ? 224.710 142.460 179.950 1.00 58.58  ? 167 GLU A OE1    1 
ATOM   91   O  OE2    . GLU A 1 24  ? 225.555 140.545 180.610 1.00 71.25  ? 167 GLU A OE2    1 
ATOM   92   N  N      . GLU A 1 25  ? 226.864 146.944 179.680 1.00 45.49  ? 168 GLU A N      1 
ATOM   93   C  CA     . GLU A 1 25  ? 227.430 148.173 179.136 1.00 44.55  ? 168 GLU A CA     1 
ATOM   94   C  C      . GLU A 1 25  ? 227.571 149.258 180.196 1.00 44.73  ? 168 GLU A C      1 
ATOM   95   O  O      . GLU A 1 25  ? 228.581 149.970 180.215 1.00 46.45  ? 168 GLU A O      1 
ATOM   96   C  CB     . GLU A 1 25  ? 226.578 148.677 177.970 1.00 49.64  ? 168 GLU A CB     1 
ATOM   97   C  CG     . GLU A 1 25  ? 225.283 149.357 178.380 1.00 58.64  ? 168 GLU A CG     1 
ATOM   98   C  CD     . GLU A 1 25  ? 225.365 150.868 178.280 1.00 66.83  ? 168 GLU A CD     1 
ATOM   99   O  OE1    . GLU A 1 25  ? 226.236 151.368 177.539 1.00 68.65  ? 168 GLU A OE1    1 
ATOM   100  O  OE2    . GLU A 1 25  ? 224.560 151.555 178.943 1.00 59.86  ? 168 GLU A OE2    1 
ATOM   101  N  N      . ALA A 1 26  ? 226.578 149.404 181.076 1.00 44.83  ? 169 ALA A N      1 
ATOM   102  C  CA     . ALA A 1 26  ? 226.691 150.375 182.159 1.00 39.65  ? 169 ALA A CA     1 
ATOM   103  C  C      . ALA A 1 26  ? 227.804 149.995 183.126 1.00 36.39  ? 169 ALA A C      1 
ATOM   104  O  O      . ALA A 1 26  ? 228.557 150.860 183.587 1.00 38.67  ? 169 ALA A O      1 
ATOM   105  C  CB     . ALA A 1 26  ? 225.357 150.500 182.894 1.00 36.19  ? 169 ALA A CB     1 
ATOM   106  N  N      . ILE A 1 27  ? 227.924 148.704 183.445 1.00 37.44  ? 170 ILE A N      1 
ATOM   107  C  CA     . ILE A 1 27  ? 228.969 148.260 184.362 1.00 36.62  ? 170 ILE A CA     1 
ATOM   108  C  C      . ILE A 1 27  ? 230.348 148.493 183.764 1.00 40.21  ? 170 ILE A C      1 
ATOM   109  O  O      . ILE A 1 27  ? 231.308 148.776 184.491 1.00 42.08  ? 170 ILE A O      1 
ATOM   110  C  CB     . ILE A 1 27  ? 228.760 146.781 184.735 1.00 39.26  ? 170 ILE A CB     1 
ATOM   111  C  CG1    . ILE A 1 27  ? 227.586 146.637 185.706 1.00 38.38  ? 170 ILE A CG1    1 
ATOM   112  C  CG2    . ILE A 1 27  ? 230.029 146.200 185.338 1.00 36.38  ? 170 ILE A CG2    1 
ATOM   113  C  CD1    . ILE A 1 27  ? 227.188 145.204 185.975 1.00 34.78  ? 170 ILE A CD1    1 
ATOM   114  N  N      . GLU A 1 28  ? 230.479 148.375 182.440 1.00 42.32  ? 171 GLU A N      1 
ATOM   115  C  CA     . GLU A 1 28  ? 231.775 148.597 181.806 1.00 40.50  ? 171 GLU A CA     1 
ATOM   116  C  C      . GLU A 1 28  ? 232.279 150.013 182.054 1.00 42.06  ? 171 GLU A C      1 
ATOM   117  O  O      . GLU A 1 28  ? 233.466 150.214 182.338 1.00 44.39  ? 171 GLU A O      1 
ATOM   118  C  CB     . GLU A 1 28  ? 231.680 148.318 180.307 1.00 45.82  ? 171 GLU A CB     1 
ATOM   119  C  CG     . GLU A 1 28  ? 232.270 146.985 179.883 1.00 54.55  ? 171 GLU A CG     1 
ATOM   120  C  CD     . GLU A 1 28  ? 233.711 146.821 180.321 1.00 66.19  ? 171 GLU A CD     1 
ATOM   121  O  OE1    . GLU A 1 28  ? 234.559 147.636 179.901 1.00 62.01  ? 171 GLU A OE1    1 
ATOM   122  O  OE2    . GLU A 1 28  ? 233.997 145.877 181.087 1.00 68.35  ? 171 GLU A OE2    1 
ATOM   123  N  N      . GLU A 1 29  ? 231.396 151.008 181.948 1.00 40.06  ? 172 GLU A N      1 
ATOM   124  C  CA     . GLU A 1 29  ? 231.810 152.390 182.165 1.00 36.27  ? 172 GLU A CA     1 
ATOM   125  C  C      . GLU A 1 29  ? 232.191 152.650 183.617 1.00 36.95  ? 172 GLU A C      1 
ATOM   126  O  O      . GLU A 1 29  ? 233.080 153.466 183.885 1.00 39.06  ? 172 GLU A O      1 
ATOM   127  C  CB     . GLU A 1 29  ? 230.697 153.345 181.733 1.00 38.85  ? 172 GLU A CB     1 
ATOM   128  C  CG     . GLU A 1 29  ? 230.185 153.109 180.323 1.00 45.28  ? 172 GLU A CG     1 
ATOM   129  C  CD     . GLU A 1 29  ? 231.126 153.646 179.263 1.00 63.48  ? 172 GLU A CD     1 
ATOM   130  O  OE1    . GLU A 1 29  ? 231.850 154.622 179.548 1.00 60.61  ? 172 GLU A OE1    1 
ATOM   131  O  OE2    . GLU A 1 29  ? 231.142 153.092 178.143 1.00 70.93  ? 172 GLU A OE2    1 
ATOM   132  N  N      . LEU A 1 30  ? 231.539 151.974 184.563 1.00 35.47  ? 173 LEU A N      1 
ATOM   133  C  CA     . LEU A 1 30  ? 231.754 152.244 185.978 1.00 30.42  ? 173 LEU A CA     1 
ATOM   134  C  C      . LEU A 1 30  ? 233.010 151.586 186.535 1.00 34.19  ? 173 LEU A C      1 
ATOM   135  O  O      . LEU A 1 30  ? 233.352 151.833 187.696 1.00 34.99  ? 173 LEU A O      1 
ATOM   136  C  CB     . LEU A 1 30  ? 230.537 151.788 186.788 1.00 29.20  ? 173 LEU A CB     1 
ATOM   137  C  CG     . LEU A 1 30  ? 229.276 152.641 186.642 1.00 30.00  ? 173 LEU A CG     1 
ATOM   138  C  CD1    . LEU A 1 30  ? 228.101 151.989 187.350 1.00 25.40  ? 173 LEU A CD1    1 
ATOM   139  C  CD2    . LEU A 1 30  ? 229.514 154.045 187.173 1.00 24.72  ? 173 LEU A CD2    1 
ATOM   140  N  N      . LYS A 1 31  ? 233.702 150.761 185.747 1.00 37.07  ? 174 LYS A N      1 
ATOM   141  C  CA     . LYS A 1 31  ? 234.914 150.115 186.242 1.00 36.24  ? 174 LYS A CA     1 
ATOM   142  C  C      . LYS A 1 31  ? 236.022 151.130 186.495 1.00 36.75  ? 174 LYS A C      1 
ATOM   143  O  O      . LYS A 1 31  ? 236.808 150.977 187.437 1.00 37.51  ? 174 LYS A O      1 
ATOM   144  C  CB     . LYS A 1 31  ? 235.379 149.045 185.255 1.00 39.84  ? 174 LYS A CB     1 
ATOM   145  C  CG     . LYS A 1 31  ? 234.486 147.817 185.208 1.00 42.65  ? 174 LYS A CG     1 
ATOM   146  C  CD     . LYS A 1 31  ? 234.593 147.010 186.491 1.00 46.78  ? 174 LYS A CD     1 
ATOM   147  C  CE     . LYS A 1 31  ? 233.929 145.651 186.346 1.00 48.54  ? 174 LYS A CE     1 
ATOM   148  N  NZ     . LYS A 1 31  ? 234.122 145.085 184.983 1.00 49.07  ? 174 LYS A NZ     1 
ATOM   149  N  N      . GLU A 1 32  ? 236.104 152.170 185.662 1.00 36.66  ? 175 GLU A N      1 
ATOM   150  C  CA     . GLU A 1 32  ? 237.135 153.187 185.841 1.00 35.54  ? 175 GLU A CA     1 
ATOM   151  C  C      . GLU A 1 32  ? 236.960 153.946 187.151 1.00 35.15  ? 175 GLU A C      1 
ATOM   152  O  O      . GLU A 1 32  ? 237.953 154.307 187.795 1.00 37.25  ? 175 GLU A O      1 
ATOM   153  C  CB     . GLU A 1 32  ? 237.121 154.151 184.656 1.00 34.66  ? 175 GLU A CB     1 
ATOM   154  C  CG     . GLU A 1 32  ? 238.135 155.275 184.747 1.00 44.62  ? 175 GLU A CG     1 
ATOM   155  C  CD     . GLU A 1 32  ? 237.703 156.504 183.974 1.00 53.28  ? 175 GLU A CD     1 
ATOM   156  O  OE1    . GLU A 1 32  ? 236.482 156.692 183.787 1.00 50.41  ? 175 GLU A OE1    1 
ATOM   157  O  OE2    . GLU A 1 32  ? 238.583 157.282 183.549 1.00 65.16  ? 175 GLU A OE2    1 
ATOM   158  N  N      . VAL A 1 33  ? 235.715 154.199 187.559 1.00 32.65  ? 176 VAL A N      1 
ATOM   159  C  CA     . VAL A 1 33  ? 235.471 154.891 188.819 1.00 29.36  ? 176 VAL A CA     1 
ATOM   160  C  C      . VAL A 1 33  ? 235.996 154.077 189.994 1.00 29.93  ? 176 VAL A C      1 
ATOM   161  O  O      . VAL A 1 33  ? 236.578 154.633 190.933 1.00 30.71  ? 176 VAL A O      1 
ATOM   162  C  CB     . VAL A 1 33  ? 233.972 155.201 188.976 1.00 30.67  ? 176 VAL A CB     1 
ATOM   163  C  CG1    . VAL A 1 33  ? 233.715 155.943 190.277 1.00 26.85  ? 176 VAL A CG1    1 
ATOM   164  C  CG2    . VAL A 1 33  ? 233.472 156.006 187.789 1.00 27.98  ? 176 VAL A CG2    1 
ATOM   165  N  N      . VAL A 1 34  ? 235.793 152.759 189.974 1.00 30.00  ? 177 VAL A N      1 
ATOM   166  C  CA     . VAL A 1 34  ? 236.295 151.912 191.051 1.00 34.53  ? 177 VAL A CA     1 
ATOM   167  C  C      . VAL A 1 34  ? 237.815 151.973 191.114 1.00 35.33  ? 177 VAL A C      1 
ATOM   168  O  O      . VAL A 1 34  ? 238.403 152.084 192.197 1.00 35.26  ? 177 VAL A O      1 
ATOM   169  C  CB     . VAL A 1 34  ? 235.789 150.469 190.871 1.00 35.08  ? 177 VAL A CB     1 
ATOM   170  C  CG1    . VAL A 1 34  ? 236.437 149.547 191.889 1.00 34.53  ? 177 VAL A CG1    1 
ATOM   171  C  CG2    . VAL A 1 34  ? 234.274 150.420 190.986 1.00 31.11  ? 177 VAL A CG2    1 
ATOM   172  N  N      . GLU A 1 35  ? 238.478 151.901 189.957 1.00 32.49  ? 178 GLU A N      1 
ATOM   173  C  CA     . GLU A 1 35  ? 239.934 151.988 189.936 1.00 31.36  ? 178 GLU A CA     1 
ATOM   174  C  C      . GLU A 1 35  ? 240.420 153.329 190.465 1.00 31.31  ? 178 GLU A C      1 
ATOM   175  O  O      . GLU A 1 35  ? 241.399 153.381 191.218 1.00 33.01  ? 178 GLU A O      1 
ATOM   176  C  CB     . GLU A 1 35  ? 240.455 151.753 188.519 1.00 33.44  ? 178 GLU A CB     1 
ATOM   177  C  CG     . GLU A 1 35  ? 240.185 150.358 187.981 1.00 41.23  ? 178 GLU A CG     1 
ATOM   178  C  CD     . GLU A 1 35  ? 240.998 149.291 188.688 1.00 53.90  ? 178 GLU A CD     1 
ATOM   179  O  OE1    . GLU A 1 35  ? 241.570 149.585 189.758 1.00 53.35  ? 178 GLU A OE1    1 
ATOM   180  O  OE2    . GLU A 1 35  ? 241.066 148.155 188.173 1.00 64.82  ? 178 GLU A OE2    1 
ATOM   181  N  N      . PHE A 1 36  ? 239.754 154.423 190.087 1.00 29.01  ? 179 PHE A N      1 
ATOM   182  C  CA     . PHE A 1 36  ? 240.132 155.729 190.615 1.00 27.10  ? 179 PHE A CA     1 
ATOM   183  C  C      . PHE A 1 36  ? 239.957 155.785 192.127 1.00 30.53  ? 179 PHE A C      1 
ATOM   184  O  O      . PHE A 1 36  ? 240.821 156.309 192.838 1.00 30.31  ? 179 PHE A O      1 
ATOM   185  C  CB     . PHE A 1 36  ? 239.311 156.828 189.941 1.00 24.92  ? 179 PHE A CB     1 
ATOM   186  C  CG     . PHE A 1 36  ? 239.543 158.196 190.519 1.00 25.74  ? 179 PHE A CG     1 
ATOM   187  C  CD1    . PHE A 1 36  ? 240.763 158.831 190.361 1.00 26.62  ? 179 PHE A CD1    1 
ATOM   188  C  CD2    . PHE A 1 36  ? 238.543 158.844 191.223 1.00 25.34  ? 179 PHE A CD2    1 
ATOM   189  C  CE1    . PHE A 1 36  ? 240.979 160.087 190.892 1.00 25.04  ? 179 PHE A CE1    1 
ATOM   190  C  CE2    . PHE A 1 36  ? 238.754 160.100 191.758 1.00 25.54  ? 179 PHE A CE2    1 
ATOM   191  C  CZ     . PHE A 1 36  ? 239.973 160.722 191.591 1.00 26.83  ? 179 PHE A CZ     1 
ATOM   192  N  N      . LEU A 1 37  ? 238.845 155.249 192.636 1.00 33.21  ? 180 LEU A N      1 
ATOM   193  C  CA     . LEU A 1 37  ? 238.585 155.313 194.070 1.00 30.37  ? 180 LEU A CA     1 
ATOM   194  C  C      . LEU A 1 37  ? 239.550 154.442 194.863 1.00 33.65  ? 180 LEU A C      1 
ATOM   195  O  O      . LEU A 1 37  ? 239.873 154.767 196.011 1.00 36.19  ? 180 LEU A O      1 
ATOM   196  C  CB     . LEU A 1 37  ? 237.142 154.903 194.361 1.00 29.56  ? 180 LEU A CB     1 
ATOM   197  C  CG     . LEU A 1 37  ? 236.063 155.952 194.089 1.00 30.02  ? 180 LEU A CG     1 
ATOM   198  C  CD1    . LEU A 1 37  ? 234.684 155.317 194.124 1.00 28.49  ? 180 LEU A CD1    1 
ATOM   199  C  CD2    . LEU A 1 37  ? 236.157 157.092 195.089 1.00 27.27  ? 180 LEU A CD2    1 
ATOM   200  N  N      . LYS A 1 38  ? 240.016 153.336 194.280 1.00 35.06  ? 181 LYS A N      1 
ATOM   201  C  CA     . LYS A 1 38  ? 240.910 152.443 195.010 1.00 34.07  ? 181 LYS A CA     1 
ATOM   202  C  C      . LYS A 1 38  ? 242.313 153.020 195.160 1.00 39.69  ? 181 LYS A C      1 
ATOM   203  O  O      . LYS A 1 38  ? 242.968 152.775 196.179 1.00 45.66  ? 181 LYS A O      1 
ATOM   204  C  CB     . LYS A 1 38  ? 240.972 151.080 194.320 1.00 34.05  ? 181 LYS A CB     1 
ATOM   205  C  CG     . LYS A 1 38  ? 239.765 150.198 194.598 1.00 37.48  ? 181 LYS A CG     1 
ATOM   206  C  CD     . LYS A 1 38  ? 240.038 148.747 194.242 1.00 39.72  ? 181 LYS A CD     1 
ATOM   207  C  CE     . LYS A 1 38  ? 240.462 148.602 192.791 1.00 48.60  ? 181 LYS A CE     1 
ATOM   208  N  NZ     . LYS A 1 38  ? 240.159 147.244 192.264 1.00 53.35  ? 181 LYS A NZ     1 
ATOM   209  N  N      . ASP A 1 39  ? 242.791 153.779 194.175 1.00 41.97  ? 182 ASP A N      1 
ATOM   210  C  CA     . ASP A 1 39  ? 244.127 154.359 194.255 1.00 39.53  ? 182 ASP A CA     1 
ATOM   211  C  C      . ASP A 1 39  ? 244.221 155.615 193.397 1.00 36.80  ? 182 ASP A C      1 
ATOM   212  O  O      . ASP A 1 39  ? 244.593 155.538 192.219 1.00 35.29  ? 182 ASP A O      1 
ATOM   213  C  CB     . ASP A 1 39  ? 245.180 153.339 193.820 1.00 42.74  ? 182 ASP A CB     1 
ATOM   214  C  CG     . ASP A 1 39  ? 246.580 153.723 194.260 1.00 52.48  ? 182 ASP A CG     1 
ATOM   215  O  OD1    . ASP A 1 39  ? 246.730 154.758 194.942 1.00 49.71  ? 182 ASP A OD1    1 
ATOM   216  O  OD2    . ASP A 1 39  ? 247.531 152.987 193.924 1.00 57.31  ? 182 ASP A OD2    1 
ATOM   217  N  N      . PRO A 1 40  ? 243.895 156.787 193.947 1.00 34.21  ? 183 PRO A N      1 
ATOM   218  C  CA     . PRO A 1 40  ? 243.977 158.020 193.147 1.00 34.59  ? 183 PRO A CA     1 
ATOM   219  C  C      . PRO A 1 40  ? 245.384 158.358 192.685 1.00 36.82  ? 183 PRO A C      1 
ATOM   220  O  O      . PRO A 1 40  ? 245.531 159.111 191.714 1.00 35.53  ? 183 PRO A O      1 
ATOM   221  C  CB     . PRO A 1 40  ? 243.432 159.098 194.095 1.00 30.53  ? 183 PRO A CB     1 
ATOM   222  C  CG     . PRO A 1 40  ? 242.702 158.354 195.168 1.00 32.21  ? 183 PRO A CG     1 
ATOM   223  C  CD     . PRO A 1 40  ? 243.394 157.039 195.307 1.00 31.42  ? 183 PRO A CD     1 
ATOM   224  N  N      . SER A 1 41  ? 246.419 157.833 193.343 1.00 40.53  ? 184 SER A N      1 
ATOM   225  C  CA     . SER A 1 41  ? 247.786 158.212 193.004 1.00 36.90  ? 184 SER A CA     1 
ATOM   226  C  C      . SER A 1 41  ? 248.156 157.812 191.581 1.00 36.77  ? 184 SER A C      1 
ATOM   227  O  O      . SER A 1 41  ? 248.937 158.512 190.927 1.00 37.96  ? 184 SER A O      1 
ATOM   228  C  CB     . SER A 1 41  ? 248.764 157.588 193.999 1.00 40.96  ? 184 SER A CB     1 
ATOM   229  O  OG     . SER A 1 41  ? 250.105 157.871 193.645 1.00 48.32  ? 184 SER A OG     1 
ATOM   230  N  N      . LYS A 1 42  ? 247.614 156.698 191.084 1.00 38.66  ? 185 LYS A N      1 
ATOM   231  C  CA     . LYS A 1 42  ? 247.966 156.240 189.746 1.00 38.89  ? 185 LYS A CA     1 
ATOM   232  C  C      . LYS A 1 42  ? 247.423 157.153 188.655 1.00 38.93  ? 185 LYS A C      1 
ATOM   233  O  O      . LYS A 1 42  ? 247.968 157.163 187.547 1.00 38.99  ? 185 LYS A O      1 
ATOM   234  C  CB     . LYS A 1 42  ? 247.463 154.813 189.530 1.00 41.47  ? 185 LYS A CB     1 
ATOM   235  C  CG     . LYS A 1 42  ? 248.285 153.758 190.247 1.00 48.87  ? 185 LYS A CG     1 
ATOM   236  C  CD     . LYS A 1 42  ? 247.803 152.360 189.910 1.00 55.80  ? 185 LYS A CD     1 
ATOM   237  C  CE     . LYS A 1 42  ? 248.642 151.306 190.613 1.00 61.58  ? 185 LYS A CE     1 
ATOM   238  N  NZ     . LYS A 1 42  ? 250.090 151.446 190.296 1.00 61.16  ? 185 LYS A NZ     1 
ATOM   239  N  N      . PHE A 1 43  ? 246.365 157.910 188.937 1.00 36.03  ? 186 PHE A N      1 
ATOM   240  C  CA     . PHE A 1 43  ? 245.831 158.860 187.970 1.00 31.49  ? 186 PHE A CA     1 
ATOM   241  C  C      . PHE A 1 43  ? 246.554 160.199 188.004 1.00 35.20  ? 186 PHE A C      1 
ATOM   242  O  O      . PHE A 1 43  ? 246.685 160.851 186.962 1.00 36.91  ? 186 PHE A O      1 
ATOM   243  C  CB     . PHE A 1 43  ? 244.336 159.085 188.217 1.00 30.43  ? 186 PHE A CB     1 
ATOM   244  C  CG     . PHE A 1 43  ? 243.464 157.952 187.754 1.00 31.08  ? 186 PHE A CG     1 
ATOM   245  C  CD1    . PHE A 1 43  ? 243.551 156.703 188.347 1.00 28.16  ? 186 PHE A CD1    1 
ATOM   246  C  CD2    . PHE A 1 43  ? 242.551 158.138 186.729 1.00 29.16  ? 186 PHE A CD2    1 
ATOM   247  C  CE1    . PHE A 1 43  ? 242.749 155.662 187.924 1.00 24.08  ? 186 PHE A CE1    1 
ATOM   248  C  CE2    . PHE A 1 43  ? 241.746 157.100 186.302 1.00 30.07  ? 186 PHE A CE2    1 
ATOM   249  C  CZ     . PHE A 1 43  ? 241.845 155.861 186.900 1.00 27.54  ? 186 PHE A CZ     1 
ATOM   250  N  N      . ASN A 1 44  ? 247.029 160.619 189.178 1.00 35.82  ? 187 ASN A N      1 
ATOM   251  C  CA     . ASN A 1 44  ? 247.637 161.939 189.307 1.00 34.32  ? 187 ASN A CA     1 
ATOM   252  C  C      . ASN A 1 44  ? 249.037 161.988 188.708 1.00 37.89  ? 187 ASN A C      1 
ATOM   253  O  O      . ASN A 1 44  ? 249.471 163.049 188.244 1.00 40.77  ? 187 ASN A O      1 
ATOM   254  C  CB     . ASN A 1 44  ? 247.680 162.352 190.778 1.00 32.60  ? 187 ASN A CB     1 
ATOM   255  C  CG     . ASN A 1 44  ? 246.299 162.545 191.370 1.00 36.27  ? 187 ASN A CG     1 
ATOM   256  O  OD1    . ASN A 1 44  ? 245.315 162.687 190.646 1.00 39.19  ? 187 ASN A OD1    1 
ATOM   257  N  ND2    . ASN A 1 44  ? 246.219 162.549 192.695 1.00 35.53  ? 187 ASN A ND2    1 
ATOM   258  N  N      . ARG A 1 45  ? 249.757 160.866 188.707 1.00 38.04  ? 188 ARG A N      1 
ATOM   259  C  CA     . ARG A 1 45  ? 251.149 160.867 188.273 1.00 37.17  ? 188 ARG A CA     1 
ATOM   260  C  C      . ARG A 1 45  ? 251.312 161.002 186.765 1.00 39.81  ? 188 ARG A C      1 
ATOM   261  O  O      . ARG A 1 45  ? 252.436 161.218 186.301 1.00 44.08  ? 188 ARG A O      1 
ATOM   262  C  CB     . ARG A 1 45  ? 251.853 159.595 188.754 1.00 37.79  ? 188 ARG A CB     1 
ATOM   263  C  CG     . ARG A 1 45  ? 251.518 158.346 187.957 1.00 45.72  ? 188 ARG A CG     1 
ATOM   264  C  CD     . ARG A 1 45  ? 252.198 157.127 188.558 1.00 50.96  ? 188 ARG A CD     1 
ATOM   265  N  NE     . ARG A 1 45  ? 251.924 155.912 187.800 1.00 57.94  ? 188 ARG A NE     1 
ATOM   266  C  CZ     . ARG A 1 45  ? 252.206 154.687 188.223 1.00 59.58  ? 188 ARG A CZ     1 
ATOM   267  N  NH1    . ARG A 1 45  ? 252.777 154.476 189.397 1.00 62.89  ? 188 ARG A NH1    1 
ATOM   268  N  NH2    . ARG A 1 45  ? 251.906 153.648 187.449 1.00 60.21  ? 188 ARG A NH2    1 
ATOM   269  N  N      . ILE A 1 46  ? 250.234 160.880 185.990 1.00 37.05  ? 189 ILE A N      1 
ATOM   270  C  CA     . ILE A 1 46  ? 250.286 161.063 184.547 1.00 34.66  ? 189 ILE A CA     1 
ATOM   271  C  C      . ILE A 1 46  ? 249.349 162.168 184.076 1.00 33.56  ? 189 ILE A C      1 
ATOM   272  O  O      . ILE A 1 46  ? 249.115 162.307 182.876 1.00 32.18  ? 189 ILE A O      1 
ATOM   273  C  CB     . ILE A 1 46  ? 249.995 159.745 183.803 1.00 36.47  ? 189 ILE A CB     1 
ATOM   274  C  CG1    . ILE A 1 46  ? 248.568 159.271 184.083 1.00 34.59  ? 189 ILE A CG1    1 
ATOM   275  C  CG2    . ILE A 1 46  ? 251.006 158.680 184.195 1.00 36.86  ? 189 ILE A CG2    1 
ATOM   276  C  CD1    . ILE A 1 46  ? 248.128 158.121 183.209 1.00 29.77  ? 189 ILE A CD1    1 
ATOM   277  N  N      . GLY A 1 47  ? 248.809 162.958 184.997 1.00 32.88  ? 190 GLY A N      1 
ATOM   278  C  CA     . GLY A 1 47  ? 247.951 164.073 184.634 1.00 28.06  ? 190 GLY A CA     1 
ATOM   279  C  C      . GLY A 1 47  ? 246.618 163.691 184.029 1.00 31.97  ? 190 GLY A C      1 
ATOM   280  O  O      . GLY A 1 47  ? 246.159 164.351 183.088 1.00 34.59  ? 190 GLY A O      1 
ATOM   281  N  N      . ALA A 1 48  ? 245.980 162.644 184.545 1.00 34.05  ? 191 ALA A N      1 
ATOM   282  C  CA     . ALA A 1 48  ? 244.650 162.253 184.098 1.00 27.61  ? 191 ALA A CA     1 
ATOM   283  C  C      . ALA A 1 48  ? 243.603 162.926 184.976 1.00 32.65  ? 191 ALA A C      1 
ATOM   284  O  O      . ALA A 1 48  ? 243.668 162.839 186.206 1.00 36.06  ? 191 ALA A O      1 
ATOM   285  C  CB     . ALA A 1 48  ? 244.487 160.733 184.140 1.00 24.00  ? 191 ALA A CB     1 
ATOM   286  N  N      . ARG A 1 49  ? 242.642 163.591 184.343 1.00 33.26  ? 192 ARG A N      1 
ATOM   287  C  CA     . ARG A 1 49  ? 241.633 164.382 185.037 1.00 30.17  ? 192 ARG A CA     1 
ATOM   288  C  C      . ARG A 1 49  ? 240.299 163.648 184.996 1.00 30.99  ? 192 ARG A C      1 
ATOM   289  O  O      . ARG A 1 49  ? 239.778 163.361 183.913 1.00 36.47  ? 192 ARG A O      1 
ATOM   290  C  CB     . ARG A 1 49  ? 241.508 165.769 184.407 1.00 30.98  ? 192 ARG A CB     1 
ATOM   291  C  CG     . ARG A 1 49  ? 240.831 166.801 185.288 1.00 37.49  ? 192 ARG A CG     1 
ATOM   292  C  CD     . ARG A 1 49  ? 240.562 168.083 184.519 1.00 42.14  ? 192 ARG A CD     1 
ATOM   293  N  NE     . ARG A 1 49  ? 239.663 167.864 183.392 1.00 47.12  ? 192 ARG A NE     1 
ATOM   294  C  CZ     . ARG A 1 49  ? 239.979 168.099 182.125 1.00 48.92  ? 192 ARG A CZ     1 
ATOM   295  N  NH1    . ARG A 1 49  ? 241.170 168.563 181.785 1.00 40.31  ? 192 ARG A NH1    1 
ATOM   296  N  NH2    . ARG A 1 49  ? 239.078 167.859 181.177 1.00 45.12  ? 192 ARG A NH2    1 
ATOM   297  N  N      . MET A 1 50  ? 239.752 163.348 186.173 1.00 30.34  ? 193 MET A N      1 
ATOM   298  C  CA     . MET A 1 50  ? 238.474 162.663 186.270 1.00 30.43  ? 193 MET A CA     1 
ATOM   299  C  C      . MET A 1 50  ? 237.322 163.667 186.303 1.00 28.43  ? 193 MET A C      1 
ATOM   300  O  O      . MET A 1 50  ? 237.492 164.804 186.750 1.00 30.38  ? 193 MET A O      1 
ATOM   301  C  CB     . MET A 1 50  ? 238.429 161.793 187.521 1.00 26.53  ? 193 MET A CB     1 
ATOM   302  C  CG     . MET A 1 50  ? 239.131 160.454 187.377 1.00 25.57  ? 193 MET A CG     1 
ATOM   303  S  SD     . MET A 1 50  ? 238.243 159.312 186.301 1.00 48.32  ? 193 MET A SD     1 
ATOM   304  C  CE     . MET A 1 50  ? 237.078 158.594 187.456 1.00 31.63  ? 193 MET A CE     1 
ATOM   305  N  N      . PRO A 1 51  ? 236.143 163.269 185.834 1.00 28.07  ? 194 PRO A N      1 
ATOM   306  C  CA     . PRO A 1 51  ? 234.974 164.149 185.936 1.00 27.37  ? 194 PRO A CA     1 
ATOM   307  C  C      . PRO A 1 51  ? 234.554 164.348 187.384 1.00 26.23  ? 194 PRO A C      1 
ATOM   308  O  O      . PRO A 1 51  ? 234.784 163.507 188.255 1.00 30.94  ? 194 PRO A O      1 
ATOM   309  C  CB     . PRO A 1 51  ? 233.895 163.406 185.141 1.00 26.32  ? 194 PRO A CB     1 
ATOM   310  C  CG     . PRO A 1 51  ? 234.339 161.983 185.129 1.00 25.64  ? 194 PRO A CG     1 
ATOM   311  C  CD     . PRO A 1 51  ? 235.836 162.013 185.131 1.00 27.89  ? 194 PRO A CD     1 
ATOM   312  N  N      . LYS A 1 52  ? 233.923 165.497 187.635 1.00 25.00  ? 195 LYS A N      1 
ATOM   313  C  CA     . LYS A 1 52  ? 233.485 165.821 188.988 1.00 26.22  ? 195 LYS A CA     1 
ATOM   314  C  C      . LYS A 1 52  ? 232.169 165.138 189.338 1.00 27.69  ? 195 LYS A C      1 
ATOM   315  O  O      . LYS A 1 52  ? 231.967 164.729 190.487 1.00 26.99  ? 195 LYS A O      1 
ATOM   316  C  CB     . LYS A 1 52  ? 233.358 167.336 189.151 1.00 30.01  ? 195 LYS A CB     1 
ATOM   317  C  CG     . LYS A 1 52  ? 234.674 168.041 189.426 1.00 30.33  ? 195 LYS A CG     1 
ATOM   318  C  CD     . LYS A 1 52  ? 234.517 169.096 190.506 1.00 34.02  ? 195 LYS A CD     1 
ATOM   319  C  CE     . LYS A 1 52  ? 235.862 169.667 190.921 1.00 32.93  ? 195 LYS A CE     1 
ATOM   320  N  NZ     . LYS A 1 52  ? 235.730 170.649 192.031 1.00 35.86  ? 195 LYS A NZ     1 
ATOM   321  N  N      . GLY A 1 53  ? 231.263 165.005 188.368 1.00 27.06  ? 196 GLY A N      1 
ATOM   322  C  CA     . GLY A 1 53  ? 229.969 164.414 188.619 1.00 23.39  ? 196 GLY A CA     1 
ATOM   323  C  C      . GLY A 1 53  ? 229.560 163.469 187.506 1.00 26.33  ? 196 GLY A C      1 
ATOM   324  O  O      . GLY A 1 53  ? 229.978 163.600 186.356 1.00 29.17  ? 196 GLY A O      1 
ATOM   325  N  N      . ILE A 1 54  ? 228.723 162.503 187.877 1.00 26.47  ? 197 ILE A N      1 
ATOM   326  C  CA     . ILE A 1 54  ? 228.193 161.509 186.951 1.00 22.91  ? 197 ILE A CA     1 
ATOM   327  C  C      . ILE A 1 54  ? 226.690 161.407 187.168 1.00 22.00  ? 197 ILE A C      1 
ATOM   328  O  O      . ILE A 1 54  ? 226.213 161.438 188.307 1.00 24.20  ? 197 ILE A O      1 
ATOM   329  C  CB     . ILE A 1 54  ? 228.871 160.137 187.138 1.00 24.62  ? 197 ILE A CB     1 
ATOM   330  C  CG1    . ILE A 1 54  ? 230.360 160.230 186.802 1.00 25.83  ? 197 ILE A CG1    1 
ATOM   331  C  CG2    . ILE A 1 54  ? 228.193 159.087 186.274 1.00 24.05  ? 197 ILE A CG2    1 
ATOM   332  C  CD1    . ILE A 1 54  ? 231.154 159.003 187.188 1.00 25.09  ? 197 ILE A CD1    1 
ATOM   333  N  N      . LEU A 1 55  ? 225.943 161.285 186.073 1.00 21.68  ? 198 LEU A N      1 
ATOM   334  C  CA     . LEU A 1 55  ? 224.487 161.252 186.109 1.00 19.33  ? 198 LEU A CA     1 
ATOM   335  C  C      . LEU A 1 55  ? 223.985 159.941 185.520 1.00 19.84  ? 198 LEU A C      1 
ATOM   336  O  O      . LEU A 1 55  ? 224.439 159.524 184.450 1.00 21.69  ? 198 LEU A O      1 
ATOM   337  C  CB     . LEU A 1 55  ? 223.897 162.438 185.341 1.00 18.88  ? 198 LEU A CB     1 
ATOM   338  C  CG     . LEU A 1 55  ? 222.372 162.558 185.324 1.00 21.87  ? 198 LEU A CG     1 
ATOM   339  C  CD1    . LEU A 1 55  ? 221.827 162.713 186.734 1.00 20.56  ? 198 LEU A CD1    1 
ATOM   340  C  CD2    . LEU A 1 55  ? 221.936 163.719 184.445 1.00 20.02  ? 198 LEU A CD2    1 
ATOM   341  N  N      . LEU A 1 56  ? 223.054 159.297 186.220 1.00 19.14  ? 199 LEU A N      1 
ATOM   342  C  CA     . LEU A 1 56  ? 222.414 158.075 185.751 1.00 17.79  ? 199 LEU A CA     1 
ATOM   343  C  C      . LEU A 1 56  ? 220.973 158.373 185.360 1.00 19.75  ? 199 LEU A C      1 
ATOM   344  O  O      . LEU A 1 56  ? 220.232 158.992 186.130 1.00 21.71  ? 199 LEU A O      1 
ATOM   345  C  CB     . LEU A 1 56  ? 222.453 156.986 186.826 1.00 17.32  ? 199 LEU A CB     1 
ATOM   346  C  CG     . LEU A 1 56  ? 223.823 156.581 187.372 1.00 20.63  ? 199 LEU A CG     1 
ATOM   347  C  CD1    . LEU A 1 56  ? 223.666 155.779 188.651 1.00 16.70  ? 199 LEU A CD1    1 
ATOM   348  C  CD2    . LEU A 1 56  ? 224.603 155.791 186.337 1.00 21.37  ? 199 LEU A CD2    1 
ATOM   349  N  N      . VAL A 1 57  ? 220.580 157.930 184.168 1.00 20.71  ? 200 VAL A N      1 
ATOM   350  C  CA     . VAL A 1 57  ? 219.249 158.182 183.628 1.00 20.77  ? 200 VAL A CA     1 
ATOM   351  C  C      . VAL A 1 57  ? 218.646 156.863 183.165 1.00 20.91  ? 200 VAL A C      1 
ATOM   352  O  O      . VAL A 1 57  ? 219.334 156.031 182.564 1.00 22.79  ? 200 VAL A O      1 
ATOM   353  C  CB     . VAL A 1 57  ? 219.287 159.200 182.469 1.00 24.01  ? 200 VAL A CB     1 
ATOM   354  C  CG1    . VAL A 1 57  ? 219.932 160.499 182.924 1.00 19.76  ? 200 VAL A CG1    1 
ATOM   355  C  CG2    . VAL A 1 57  ? 220.029 158.622 181.276 1.00 24.08  ? 200 VAL A CG2    1 
ATOM   356  N  N      . GLY A 1 58  ? 217.359 156.673 183.447 1.00 22.34  ? 201 GLY A N      1 
ATOM   357  C  CA     . GLY A 1 58  ? 216.658 155.478 183.044 1.00 19.49  ? 201 GLY A CA     1 
ATOM   358  C  C      . GLY A 1 58  ? 215.245 155.415 183.588 1.00 22.17  ? 201 GLY A C      1 
ATOM   359  O  O      . GLY A 1 58  ? 214.850 156.206 184.449 1.00 24.99  ? 201 GLY A O      1 
ATOM   360  N  N      . PRO A 1 59  ? 214.455 154.469 183.090 1.00 23.60  ? 202 PRO A N      1 
ATOM   361  C  CA     . PRO A 1 59  ? 213.069 154.331 183.554 1.00 17.94  ? 202 PRO A CA     1 
ATOM   362  C  C      . PRO A 1 59  ? 213.019 153.827 184.984 1.00 20.05  ? 202 PRO A C      1 
ATOM   363  O  O      . PRO A 1 59  ? 213.965 153.181 185.460 1.00 22.07  ? 202 PRO A O      1 
ATOM   364  C  CB     . PRO A 1 59  ? 212.462 153.308 182.579 1.00 15.52  ? 202 PRO A CB     1 
ATOM   365  C  CG     . PRO A 1 59  ? 213.442 153.186 181.452 1.00 16.43  ? 202 PRO A CG     1 
ATOM   366  C  CD     . PRO A 1 59  ? 214.781 153.516 182.018 1.00 22.50  ? 202 PRO A CD     1 
ATOM   367  N  N      . PRO A 1 60  ? 211.933 154.103 185.703 1.00 22.27  ? 203 PRO A N      1 
ATOM   368  C  CA     . PRO A 1 60  ? 211.845 153.671 187.102 1.00 23.74  ? 203 PRO A CA     1 
ATOM   369  C  C      . PRO A 1 60  ? 211.932 152.159 187.239 1.00 22.82  ? 203 PRO A C      1 
ATOM   370  O  O      . PRO A 1 60  ? 211.433 151.402 186.403 1.00 23.66  ? 203 PRO A O      1 
ATOM   371  C  CB     . PRO A 1 60  ? 210.472 154.186 187.557 1.00 19.20  ? 203 PRO A CB     1 
ATOM   372  C  CG     . PRO A 1 60  ? 209.754 154.606 186.323 1.00 17.15  ? 203 PRO A CG     1 
ATOM   373  C  CD     . PRO A 1 60  ? 210.769 154.894 185.275 1.00 19.75  ? 203 PRO A CD     1 
ATOM   374  N  N      . GLY A 1 61  ? 212.577 151.724 188.319 1.00 21.43  ? 204 GLY A N      1 
ATOM   375  C  CA     . GLY A 1 61  ? 212.699 150.312 188.619 1.00 16.74  ? 204 GLY A CA     1 
ATOM   376  C  C      . GLY A 1 61  ? 213.793 149.578 187.879 1.00 19.56  ? 204 GLY A C      1 
ATOM   377  O  O      . GLY A 1 61  ? 213.855 148.347 187.967 1.00 22.01  ? 204 GLY A O      1 
ATOM   378  N  N      . THR A 1 62  ? 214.659 150.285 187.157 1.00 19.00  ? 205 THR A N      1 
ATOM   379  C  CA     . THR A 1 62  ? 215.713 149.646 186.381 1.00 17.31  ? 205 THR A CA     1 
ATOM   380  C  C      . THR A 1 62  ? 216.983 149.389 187.183 1.00 19.17  ? 205 THR A C      1 
ATOM   381  O  O      . THR A 1 62  ? 217.870 148.683 186.692 1.00 22.29  ? 205 THR A O      1 
ATOM   382  C  CB     . THR A 1 62  ? 216.051 150.495 185.151 1.00 20.14  ? 205 THR A CB     1 
ATOM   383  O  OG1    . THR A 1 62  ? 215.948 151.885 185.483 1.00 24.86  ? 205 THR A OG1    1 
ATOM   384  C  CG2    . THR A 1 62  ? 215.095 150.182 184.013 1.00 19.21  ? 205 THR A CG2    1 
ATOM   385  N  N      . GLY A 1 63  ? 217.095 149.936 188.391 1.00 18.77  ? 206 GLY A N      1 
ATOM   386  C  CA     . GLY A 1 63  ? 218.224 149.638 189.251 1.00 18.73  ? 206 GLY A CA     1 
ATOM   387  C  C      . GLY A 1 63  ? 219.304 150.700 189.285 1.00 22.77  ? 206 GLY A C      1 
ATOM   388  O  O      . GLY A 1 63  ? 220.494 150.376 189.285 1.00 24.49  ? 206 GLY A O      1 
ATOM   389  N  N      . LYS A 1 64  ? 218.909 151.974 189.313 1.00 22.88  ? 207 LYS A N      1 
ATOM   390  C  CA     . LYS A 1 64  ? 219.892 153.050 189.368 1.00 19.88  ? 207 LYS A CA     1 
ATOM   391  C  C      . LYS A 1 64  ? 220.527 153.184 190.747 1.00 22.62  ? 207 LYS A C      1 
ATOM   392  O  O      . LYS A 1 64  ? 221.741 153.389 190.845 1.00 23.77  ? 207 LYS A O      1 
ATOM   393  C  CB     . LYS A 1 64  ? 219.246 154.372 188.950 1.00 18.19  ? 207 LYS A CB     1 
ATOM   394  C  CG     . LYS A 1 64  ? 218.668 154.353 187.544 1.00 19.28  ? 207 LYS A CG     1 
ATOM   395  C  CD     . LYS A 1 64  ? 218.258 155.742 187.085 1.00 17.16  ? 207 LYS A CD     1 
ATOM   396  C  CE     . LYS A 1 64  ? 216.982 156.201 187.769 1.00 19.26  ? 207 LYS A CE     1 
ATOM   397  N  NZ     . LYS A 1 64  ? 215.843 155.289 187.481 1.00 19.03  ? 207 LYS A NZ     1 
ATOM   398  N  N      . THR A 1 65  ? 219.735 153.069 191.815 1.00 20.34  ? 208 THR A N      1 
ATOM   399  C  CA     . THR A 1 65  ? 220.287 153.112 193.166 1.00 22.83  ? 208 THR A CA     1 
ATOM   400  C  C      . THR A 1 65  ? 221.120 151.876 193.480 1.00 25.30  ? 208 THR A C      1 
ATOM   401  O  O      . THR A 1 65  ? 222.114 151.968 194.213 1.00 26.97  ? 208 THR A O      1 
ATOM   402  C  CB     . THR A 1 65  ? 219.160 153.256 194.191 1.00 25.90  ? 208 THR A CB     1 
ATOM   403  O  OG1    . THR A 1 65  ? 218.460 154.484 193.963 1.00 31.11  ? 208 THR A OG1    1 
ATOM   404  C  CG2    . THR A 1 65  ? 219.719 153.253 195.604 1.00 23.23  ? 208 THR A CG2    1 
ATOM   405  N  N      . LEU A 1 66  ? 220.728 150.718 192.943 1.00 24.22  ? 209 LEU A N      1 
ATOM   406  C  CA     . LEU A 1 66  ? 221.493 149.500 193.171 1.00 22.70  ? 209 LEU A CA     1 
ATOM   407  C  C      . LEU A 1 66  ? 222.898 149.615 192.595 1.00 23.49  ? 209 LEU A C      1 
ATOM   408  O  O      . LEU A 1 66  ? 223.866 149.173 193.220 1.00 25.25  ? 209 LEU A O      1 
ATOM   409  C  CB     . LEU A 1 66  ? 220.759 148.301 192.572 1.00 24.62  ? 209 LEU A CB     1 
ATOM   410  C  CG     . LEU A 1 66  ? 221.416 146.930 192.745 1.00 25.37  ? 209 LEU A CG     1 
ATOM   411  C  CD1    . LEU A 1 66  ? 221.297 146.452 194.183 1.00 20.68  ? 209 LEU A CD1    1 
ATOM   412  C  CD2    . LEU A 1 66  ? 220.801 145.923 191.788 1.00 23.47  ? 209 LEU A CD2    1 
ATOM   413  N  N      . LEU A 1 67  ? 223.032 150.199 191.401 1.00 22.17  ? 210 LEU A N      1 
ATOM   414  C  CA     . LEU A 1 67  ? 224.358 150.391 190.822 1.00 22.20  ? 210 LEU A CA     1 
ATOM   415  C  C      . LEU A 1 67  ? 225.202 151.348 191.654 1.00 24.03  ? 210 LEU A C      1 
ATOM   416  O  O      . LEU A 1 67  ? 226.404 151.116 191.835 1.00 27.23  ? 210 LEU A O      1 
ATOM   417  C  CB     . LEU A 1 67  ? 224.238 150.900 189.387 1.00 22.53  ? 210 LEU A CB     1 
ATOM   418  C  CG     . LEU A 1 67  ? 223.976 149.837 188.319 1.00 24.06  ? 210 LEU A CG     1 
ATOM   419  C  CD1    . LEU A 1 67  ? 223.598 150.486 187.000 1.00 22.11  ? 210 LEU A CD1    1 
ATOM   420  C  CD2    . LEU A 1 67  ? 225.188 148.936 188.151 1.00 25.12  ? 210 LEU A CD2    1 
ATOM   421  N  N      . ALA A 1 68  ? 224.599 152.425 192.163 1.00 25.48  ? 211 ALA A N      1 
ATOM   422  C  CA     . ALA A 1 68  ? 225.341 153.352 193.009 1.00 22.32  ? 211 ALA A CA     1 
ATOM   423  C  C      . ALA A 1 68  ? 225.829 152.669 194.280 1.00 26.95  ? 211 ALA A C      1 
ATOM   424  O  O      . ALA A 1 68  ? 226.970 152.882 194.706 1.00 28.20  ? 211 ALA A O      1 
ATOM   425  C  CB     . ALA A 1 68  ? 224.474 154.564 193.348 1.00 19.60  ? 211 ALA A CB     1 
ATOM   426  N  N      . ARG A 1 69  ? 224.981 151.847 194.902 1.00 26.10  ? 212 ARG A N      1 
ATOM   427  C  CA     . ARG A 1 69  ? 225.414 151.106 196.082 1.00 26.52  ? 212 ARG A CA     1 
ATOM   428  C  C      . ARG A 1 69  ? 226.479 150.064 195.755 1.00 28.12  ? 212 ARG A C      1 
ATOM   429  O  O      . ARG A 1 69  ? 227.414 149.880 196.541 1.00 31.00  ? 212 ARG A O      1 
ATOM   430  C  CB     . ARG A 1 69  ? 224.216 150.441 196.761 1.00 29.15  ? 212 ARG A CB     1 
ATOM   431  C  CG     . ARG A 1 69  ? 223.126 151.414 197.176 1.00 29.66  ? 212 ARG A CG     1 
ATOM   432  C  CD     . ARG A 1 69  ? 222.301 150.868 198.329 1.00 32.00  ? 212 ARG A CD     1 
ATOM   433  N  NE     . ARG A 1 69  ? 221.306 149.901 197.882 1.00 44.32  ? 212 ARG A NE     1 
ATOM   434  C  CZ     . ARG A 1 69  ? 221.089 148.728 198.461 1.00 48.54  ? 212 ARG A CZ     1 
ATOM   435  N  NH1    . ARG A 1 69  ? 221.783 148.339 199.518 1.00 44.98  ? 212 ARG A NH1    1 
ATOM   436  N  NH2    . ARG A 1 69  ? 220.153 147.923 197.965 1.00 47.04  ? 212 ARG A NH2    1 
ATOM   437  N  N      . ALA A 1 70  ? 226.364 149.383 194.614 1.00 28.03  ? 213 ALA A N      1 
ATOM   438  C  CA     . ALA A 1 70  ? 227.362 148.395 194.225 1.00 26.65  ? 213 ALA A CA     1 
ATOM   439  C  C      . ALA A 1 70  ? 228.711 149.032 193.926 1.00 30.30  ? 213 ALA A C      1 
ATOM   440  O  O      . ALA A 1 70  ? 229.750 148.408 194.165 1.00 32.21  ? 213 ALA A O      1 
ATOM   441  C  CB     . ALA A 1 70  ? 226.877 147.604 193.010 1.00 24.56  ? 213 ALA A CB     1 
ATOM   442  N  N      . VAL A 1 71  ? 228.719 150.257 193.395 1.00 30.11  ? 214 VAL A N      1 
ATOM   443  C  CA     . VAL A 1 71  ? 229.988 150.938 193.161 1.00 30.21  ? 214 VAL A CA     1 
ATOM   444  C  C      . VAL A 1 71  ? 230.727 151.155 194.475 1.00 31.47  ? 214 VAL A C      1 
ATOM   445  O  O      . VAL A 1 71  ? 231.941 150.933 194.556 1.00 35.18  ? 214 VAL A O      1 
ATOM   446  C  CB     . VAL A 1 71  ? 229.761 152.266 192.417 1.00 30.54  ? 214 VAL A CB     1 
ATOM   447  C  CG1    . VAL A 1 71  ? 230.946 153.196 192.619 1.00 26.52  ? 214 VAL A CG1    1 
ATOM   448  C  CG2    . VAL A 1 71  ? 229.532 152.011 190.938 1.00 29.11  ? 214 VAL A CG2    1 
ATOM   449  N  N      . ALA A 1 72  ? 230.020 151.592 195.518 1.00 29.75  ? 215 ALA A N      1 
ATOM   450  C  CA     . ALA A 1 72  ? 230.622 151.736 196.837 1.00 30.62  ? 215 ALA A CA     1 
ATOM   451  C  C      . ALA A 1 72  ? 230.970 150.397 197.470 1.00 35.94  ? 215 ALA A C      1 
ATOM   452  O  O      . ALA A 1 72  ? 231.922 150.326 198.253 1.00 39.83  ? 215 ALA A O      1 
ATOM   453  C  CB     . ALA A 1 72  ? 229.686 152.514 197.763 1.00 30.48  ? 215 ALA A CB     1 
ATOM   454  N  N      . GLY A 1 73  ? 230.210 149.348 197.173 1.00 39.55  ? 216 GLY A N      1 
ATOM   455  C  CA     . GLY A 1 73  ? 230.536 148.026 197.668 1.00 35.80  ? 216 GLY A CA     1 
ATOM   456  C  C      . GLY A 1 73  ? 231.823 147.470 197.092 1.00 36.25  ? 216 GLY A C      1 
ATOM   457  O  O      . GLY A 1 73  ? 232.633 146.884 197.815 1.00 40.54  ? 216 GLY A O      1 
ATOM   458  N  N      . GLU A 1 74  ? 232.021 147.649 195.783 1.00 36.37  ? 217 GLU A N      1 
ATOM   459  C  CA     . GLU A 1 74  ? 233.210 147.108 195.131 1.00 36.27  ? 217 GLU A CA     1 
ATOM   460  C  C      . GLU A 1 74  ? 234.482 147.756 195.663 1.00 40.16  ? 217 GLU A C      1 
ATOM   461  O  O      . GLU A 1 74  ? 235.474 147.066 195.925 1.00 42.42  ? 217 GLU A O      1 
ATOM   462  C  CB     . GLU A 1 74  ? 233.107 147.291 193.617 1.00 37.12  ? 217 GLU A CB     1 
ATOM   463  C  CG     . GLU A 1 74  ? 232.154 146.323 192.936 1.00 41.09  ? 217 GLU A CG     1 
ATOM   464  C  CD     . GLU A 1 74  ? 232.758 144.947 192.749 1.00 48.87  ? 217 GLU A CD     1 
ATOM   465  O  OE1    . GLU A 1 74  ? 233.788 144.656 193.391 1.00 55.08  ? 217 GLU A OE1    1 
ATOM   466  O  OE2    . GLU A 1 74  ? 232.203 144.154 191.960 1.00 49.40  ? 217 GLU A OE2    1 
ATOM   467  N  N      . ALA A 1 75  ? 234.476 149.076 195.826 1.00 42.37  ? 218 ALA A N      1 
ATOM   468  C  CA     . ALA A 1 75  ? 235.595 149.808 196.409 1.00 39.64  ? 218 ALA A CA     1 
ATOM   469  C  C      . ALA A 1 75  ? 235.222 150.165 197.842 1.00 45.30  ? 218 ALA A C      1 
ATOM   470  O  O      . ALA A 1 75  ? 234.293 150.945 198.071 1.00 50.82  ? 218 ALA A O      1 
ATOM   471  C  CB     . ALA A 1 75  ? 235.920 151.056 195.592 1.00 33.76  ? 218 ALA A CB     1 
ATOM   472  N  N      . ASN A 1 76  ? 235.961 149.616 198.805 1.00 40.20  ? 219 ASN A N      1 
ATOM   473  C  CA     . ASN A 1 76  ? 235.588 149.714 200.216 1.00 40.60  ? 219 ASN A CA     1 
ATOM   474  C  C      . ASN A 1 76  ? 235.827 151.143 200.695 1.00 43.67  ? 219 ASN A C      1 
ATOM   475  O  O      . ASN A 1 76  ? 236.851 151.476 201.297 1.00 50.90  ? 219 ASN A O      1 
ATOM   476  C  CB     . ASN A 1 76  ? 236.374 148.706 201.044 1.00 48.05  ? 219 ASN A CB     1 
ATOM   477  C  CG     . ASN A 1 76  ? 235.664 148.325 202.327 1.00 61.36  ? 219 ASN A CG     1 
ATOM   478  O  OD1    . ASN A 1 76  ? 236.233 148.412 203.415 1.00 66.22  ? 219 ASN A OD1    1 
ATOM   479  N  ND2    . ASN A 1 76  ? 234.414 147.895 202.206 1.00 64.41  ? 219 ASN A ND2    1 
ATOM   480  N  N      . VAL A 1 77  ? 234.850 152.003 200.423 1.00 38.98  ? 220 VAL A N      1 
ATOM   481  C  CA     . VAL A 1 77  ? 234.920 153.413 200.805 1.00 34.96  ? 220 VAL A CA     1 
ATOM   482  C  C      . VAL A 1 77  ? 233.591 153.832 201.412 1.00 32.90  ? 220 VAL A C      1 
ATOM   483  O  O      . VAL A 1 77  ? 232.554 153.196 201.184 1.00 36.26  ? 220 VAL A O      1 
ATOM   484  C  CB     . VAL A 1 77  ? 235.262 154.321 199.607 1.00 37.65  ? 220 VAL A CB     1 
ATOM   485  C  CG1    . VAL A 1 77  ? 236.640 153.983 199.060 1.00 33.44  ? 220 VAL A CG1    1 
ATOM   486  C  CG2    . VAL A 1 77  ? 234.204 154.192 198.522 1.00 34.93  ? 220 VAL A CG2    1 
ATOM   487  N  N      . PRO A 1 78  ? 233.596 154.905 202.201 1.00 34.39  ? 221 PRO A N      1 
ATOM   488  C  CA     . PRO A 1 78  ? 232.348 155.393 202.801 1.00 33.20  ? 221 PRO A CA     1 
ATOM   489  C  C      . PRO A 1 78  ? 231.326 155.765 201.737 1.00 32.05  ? 221 PRO A C      1 
ATOM   490  O  O      . PRO A 1 78  ? 231.617 155.840 200.542 1.00 35.94  ? 221 PRO A O      1 
ATOM   491  C  CB     . PRO A 1 78  ? 232.793 156.618 203.607 1.00 29.95  ? 221 PRO A CB     1 
ATOM   492  C  CG     . PRO A 1 78  ? 234.248 156.407 203.852 1.00 30.31  ? 221 PRO A CG     1 
ATOM   493  C  CD     . PRO A 1 78  ? 234.769 155.669 202.657 1.00 31.45  ? 221 PRO A CD     1 
ATOM   494  N  N      . PHE A 1 79  ? 230.096 156.008 202.196 1.00 30.06  ? 222 PHE A N      1 
ATOM   495  C  CA     . PHE A 1 79  ? 228.978 156.273 201.291 1.00 27.96  ? 222 PHE A CA     1 
ATOM   496  C  C      . PHE A 1 79  ? 228.031 157.249 201.985 1.00 28.48  ? 222 PHE A C      1 
ATOM   497  O  O      . PHE A 1 79  ? 227.271 156.853 202.873 1.00 32.07  ? 222 PHE A O      1 
ATOM   498  C  CB     . PHE A 1 79  ? 228.271 154.980 200.909 1.00 25.82  ? 222 PHE A CB     1 
ATOM   499  C  CG     . PHE A 1 79  ? 227.210 155.151 199.859 1.00 29.45  ? 222 PHE A CG     1 
ATOM   500  C  CD1    . PHE A 1 79  ? 227.549 155.500 198.563 1.00 31.21  ? 222 PHE A CD1    1 
ATOM   501  C  CD2    . PHE A 1 79  ? 225.874 154.954 200.166 1.00 28.58  ? 222 PHE A CD2    1 
ATOM   502  C  CE1    . PHE A 1 79  ? 226.577 155.655 197.595 1.00 28.85  ? 222 PHE A CE1    1 
ATOM   503  C  CE2    . PHE A 1 79  ? 224.897 155.108 199.201 1.00 26.77  ? 222 PHE A CE2    1 
ATOM   504  C  CZ     . PHE A 1 79  ? 225.249 155.458 197.914 1.00 28.00  ? 222 PHE A CZ     1 
ATOM   505  N  N      . PHE A 1 80  ? 228.086 158.514 201.578 1.00 25.64  ? 223 PHE A N      1 
ATOM   506  C  CA     . PHE A 1 80  ? 227.200 159.555 202.086 1.00 27.57  ? 223 PHE A CA     1 
ATOM   507  C  C      . PHE A 1 80  ? 226.156 159.855 201.020 1.00 29.98  ? 223 PHE A C      1 
ATOM   508  O  O      . PHE A 1 80  ? 226.505 160.145 199.871 1.00 34.20  ? 223 PHE A O      1 
ATOM   509  C  CB     . PHE A 1 80  ? 227.984 160.816 202.450 1.00 25.18  ? 223 PHE A CB     1 
ATOM   510  C  CG     . PHE A 1 80  ? 229.166 160.560 203.342 1.00 30.35  ? 223 PHE A CG     1 
ATOM   511  C  CD1    . PHE A 1 80  ? 229.036 160.609 204.720 1.00 27.69  ? 223 PHE A CD1    1 
ATOM   512  C  CD2    . PHE A 1 80  ? 230.408 160.271 202.802 1.00 29.63  ? 223 PHE A CD2    1 
ATOM   513  C  CE1    . PHE A 1 80  ? 230.122 160.373 205.541 1.00 26.71  ? 223 PHE A CE1    1 
ATOM   514  C  CE2    . PHE A 1 80  ? 231.496 160.034 203.618 1.00 30.78  ? 223 PHE A CE2    1 
ATOM   515  C  CZ     . PHE A 1 80  ? 231.353 160.086 204.989 1.00 30.58  ? 223 PHE A CZ     1 
ATOM   516  N  N      . HIS A 1 81  ? 224.881 159.783 201.397 1.00 29.05  ? 224 HIS A N      1 
ATOM   517  C  CA     . HIS A 1 81  ? 223.792 159.902 200.440 1.00 28.65  ? 224 HIS A CA     1 
ATOM   518  C  C      . HIS A 1 81  ? 222.673 160.757 201.014 1.00 30.53  ? 224 HIS A C      1 
ATOM   519  O  O      . HIS A 1 81  ? 222.514 160.870 202.232 1.00 32.36  ? 224 HIS A O      1 
ATOM   520  C  CB     . HIS A 1 81  ? 223.241 158.526 200.049 1.00 26.85  ? 224 HIS A CB     1 
ATOM   521  C  CG     . HIS A 1 81  ? 222.593 157.793 201.181 1.00 34.11  ? 224 HIS A CG     1 
ATOM   522  N  ND1    . HIS A 1 81  ? 223.307 157.021 202.073 1.00 38.52  ? 224 HIS A ND1    1 
ATOM   523  C  CD2    . HIS A 1 81  ? 221.298 157.714 201.569 1.00 36.00  ? 224 HIS A CD2    1 
ATOM   524  C  CE1    . HIS A 1 81  ? 222.480 156.499 202.960 1.00 36.87  ? 224 HIS A CE1    1 
ATOM   525  N  NE2    . HIS A 1 81  ? 221.255 156.904 202.677 1.00 41.74  ? 224 HIS A NE2    1 
ATOM   526  N  N      . ILE A 1 82  ? 221.896 161.359 200.112 1.00 33.42  ? 225 ILE A N      1 
ATOM   527  C  CA     . ILE A 1 82  ? 220.703 162.115 200.471 1.00 34.41  ? 225 ILE A CA     1 
ATOM   528  C  C      . ILE A 1 82  ? 219.682 161.932 199.357 1.00 35.87  ? 225 ILE A C      1 
ATOM   529  O  O      . ILE A 1 82  ? 220.023 161.585 198.225 1.00 39.78  ? 225 ILE A O      1 
ATOM   530  C  CB     . ILE A 1 82  ? 221.001 163.616 200.700 1.00 34.83  ? 225 ILE A CB     1 
ATOM   531  C  CG1    . ILE A 1 82  ? 219.904 164.252 201.556 1.00 41.62  ? 225 ILE A CG1    1 
ATOM   532  C  CG2    . ILE A 1 82  ? 221.138 164.344 199.373 1.00 33.85  ? 225 ILE A CG2    1 
ATOM   533  C  CD1    . ILE A 1 82  ? 220.306 165.564 202.191 1.00 48.51  ? 225 ILE A CD1    1 
ATOM   534  N  N      . SER A 1 83  ? 218.416 162.167 199.685 1.00 40.63  ? 226 SER A N      1 
ATOM   535  C  CA     . SER A 1 83  ? 217.317 161.994 198.746 1.00 44.77  ? 226 SER A CA     1 
ATOM   536  C  C      . SER A 1 83  ? 216.660 163.336 198.464 1.00 47.98  ? 226 SER A C      1 
ATOM   537  O  O      . SER A 1 83  ? 216.412 164.122 199.383 1.00 51.51  ? 226 SER A O      1 
ATOM   538  C  CB     . SER A 1 83  ? 216.278 161.006 199.284 1.00 48.49  ? 226 SER A CB     1 
ATOM   539  O  OG     . SER A 1 83  ? 215.248 160.789 198.336 1.00 52.93  ? 226 SER A OG     1 
ATOM   540  N  N      . GLY A 1 84  ? 216.378 163.592 197.187 1.00 45.71  ? 227 GLY A N      1 
ATOM   541  C  CA     . GLY A 1 84  ? 215.763 164.845 196.787 1.00 49.79  ? 227 GLY A CA     1 
ATOM   542  C  C      . GLY A 1 84  ? 214.286 164.951 197.097 1.00 54.22  ? 227 GLY A C      1 
ATOM   543  O  O      . GLY A 1 84  ? 213.740 166.058 197.039 1.00 57.03  ? 227 GLY A O      1 
ATOM   544  N  N      . SER A 1 85  ? 213.629 163.837 197.422 1.00 55.65  ? 228 SER A N      1 
ATOM   545  C  CA     . SER A 1 85  ? 212.217 163.875 197.778 1.00 56.43  ? 228 SER A CA     1 
ATOM   546  C  C      . SER A 1 85  ? 211.985 164.369 199.199 1.00 61.33  ? 228 SER A C      1 
ATOM   547  O  O      . SER A 1 85  ? 210.865 164.779 199.523 1.00 64.90  ? 228 SER A O      1 
ATOM   548  C  CB     . SER A 1 85  ? 211.591 162.489 197.606 1.00 55.37  ? 228 SER A CB     1 
ATOM   549  O  OG     . SER A 1 85  ? 212.196 161.544 198.471 1.00 55.50  ? 228 SER A OG     1 
ATOM   550  N  N      . ASP A 1 86  ? 213.012 164.338 200.050 1.00 61.51  ? 229 ASP A N      1 
ATOM   551  C  CA     . ASP A 1 86  ? 212.876 164.809 201.422 1.00 61.52  ? 229 ASP A CA     1 
ATOM   552  C  C      . ASP A 1 86  ? 212.842 166.327 201.525 1.00 61.77  ? 229 ASP A C      1 
ATOM   553  O  O      . ASP A 1 86  ? 212.414 166.850 202.559 1.00 62.96  ? 229 ASP A O      1 
ATOM   554  C  CB     . ASP A 1 86  ? 214.019 164.259 202.277 1.00 62.83  ? 229 ASP A CB     1 
ATOM   555  C  CG     . ASP A 1 86  ? 213.991 162.747 202.384 1.00 70.45  ? 229 ASP A CG     1 
ATOM   556  O  OD1    . ASP A 1 86  ? 213.044 162.130 201.854 1.00 69.01  ? 229 ASP A OD1    1 
ATOM   557  O  OD2    . ASP A 1 86  ? 214.917 162.176 202.997 1.00 72.57  ? 229 ASP A OD2    1 
ATOM   558  N  N      . PHE A 1 87  ? 213.277 167.041 200.492 1.00 60.89  ? 230 PHE A N      1 
ATOM   559  C  CA     . PHE A 1 87  ? 213.285 168.498 200.518 1.00 61.03  ? 230 PHE A CA     1 
ATOM   560  C  C      . PHE A 1 87  ? 211.890 169.056 200.259 1.00 66.19  ? 230 PHE A C      1 
ATOM   561  O  O      . PHE A 1 87  ? 211.510 170.087 200.814 1.00 67.36  ? 230 PHE A O      1 
ATOM   562  C  CB     . PHE A 1 87  ? 214.273 169.049 199.486 1.00 57.27  ? 230 PHE A CB     1 
ATOM   563  C  CG     . PHE A 1 87  ? 215.714 168.905 199.887 1.00 57.04  ? 230 PHE A CG     1 
ATOM   564  C  CD1    . PHE A 1 87  ? 216.309 167.657 199.949 1.00 55.78  ? 230 PHE A CD1    1 
ATOM   565  C  CD2    . PHE A 1 87  ? 216.473 170.020 200.202 1.00 57.72  ? 230 PHE A CD2    1 
ATOM   566  C  CE1    . PHE A 1 87  ? 217.634 167.522 200.317 1.00 54.71  ? 230 PHE A CE1    1 
ATOM   567  C  CE2    . PHE A 1 87  ? 217.798 169.891 200.571 1.00 54.94  ? 230 PHE A CE2    1 
ATOM   568  C  CZ     . PHE A 1 87  ? 218.379 168.641 200.629 1.00 53.07  ? 230 PHE A CZ     1 
ATOM   569  N  N      . VAL A 1 94  ? 216.757 175.256 205.777 1.00 50.88  ? 237 VAL A N      1 
ATOM   570  C  CA     . VAL A 1 94  ? 217.243 173.989 206.308 1.00 53.05  ? 237 VAL A CA     1 
ATOM   571  C  C      . VAL A 1 94  ? 217.900 173.172 205.203 1.00 51.05  ? 237 VAL A C      1 
ATOM   572  O  O      . VAL A 1 94  ? 218.829 172.406 205.454 1.00 50.55  ? 237 VAL A O      1 
ATOM   573  C  CB     . VAL A 1 94  ? 216.109 173.191 206.974 1.00 55.02  ? 237 VAL A CB     1 
ATOM   574  C  CG1    . VAL A 1 94  ? 216.672 171.997 207.728 1.00 49.95  ? 237 VAL A CG1    1 
ATOM   575  C  CG2    . VAL A 1 94  ? 215.307 174.086 207.904 1.00 53.13  ? 237 VAL A CG2    1 
ATOM   576  N  N      . GLY A 1 95  ? 217.408 173.340 203.974 1.00 49.36  ? 238 GLY A N      1 
ATOM   577  C  CA     . GLY A 1 95  ? 217.975 172.603 202.857 1.00 43.66  ? 238 GLY A CA     1 
ATOM   578  C  C      . GLY A 1 95  ? 219.412 172.989 202.568 1.00 42.63  ? 238 GLY A C      1 
ATOM   579  O  O      . GLY A 1 95  ? 220.249 172.129 202.279 1.00 44.87  ? 238 GLY A O      1 
ATOM   580  N  N      . ALA A 1 96  ? 219.721 174.286 202.638 1.00 41.42  ? 239 ALA A N      1 
ATOM   581  C  CA     . ALA A 1 96  ? 221.084 174.736 202.379 1.00 39.03  ? 239 ALA A CA     1 
ATOM   582  C  C      . ALA A 1 96  ? 222.059 174.216 203.427 1.00 39.57  ? 239 ALA A C      1 
ATOM   583  O  O      . ALA A 1 96  ? 223.193 173.856 203.091 1.00 38.03  ? 239 ALA A O      1 
ATOM   584  C  CB     . ALA A 1 96  ? 221.131 176.261 202.317 1.00 42.22  ? 239 ALA A CB     1 
ATOM   585  N  N      . ALA A 1 97  ? 221.643 174.172 204.694 1.00 41.79  ? 240 ALA A N      1 
ATOM   586  C  CA     . ALA A 1 97  ? 222.515 173.662 205.746 1.00 39.08  ? 240 ALA A CA     1 
ATOM   587  C  C      . ALA A 1 97  ? 222.756 172.165 205.613 1.00 40.56  ? 240 ALA A C      1 
ATOM   588  O  O      . ALA A 1 97  ? 223.846 171.686 205.944 1.00 40.07  ? 240 ALA A O      1 
ATOM   589  C  CB     . ALA A 1 97  ? 221.924 173.979 207.120 1.00 37.07  ? 240 ALA A CB     1 
ATOM   590  N  N      . ARG A 1 98  ? 221.760 171.414 205.139 1.00 37.87  ? 241 ARG A N      1 
ATOM   591  C  CA     . ARG A 1 98  ? 221.939 169.979 204.949 1.00 39.97  ? 241 ARG A CA     1 
ATOM   592  C  C      . ARG A 1 98  ? 222.976 169.679 203.874 1.00 40.01  ? 241 ARG A C      1 
ATOM   593  O  O      . ARG A 1 98  ? 223.752 168.727 204.013 1.00 39.26  ? 241 ARG A O      1 
ATOM   594  C  CB     . ARG A 1 98  ? 220.604 169.326 204.592 1.00 46.13  ? 241 ARG A CB     1 
ATOM   595  C  CG     . ARG A 1 98  ? 219.581 169.359 205.713 1.00 49.19  ? 241 ARG A CG     1 
ATOM   596  C  CD     . ARG A 1 98  ? 219.598 168.068 206.512 1.00 56.45  ? 241 ARG A CD     1 
ATOM   597  N  NE     . ARG A 1 98  ? 218.758 168.151 207.701 1.00 71.21  ? 241 ARG A NE     1 
ATOM   598  C  CZ     . ARG A 1 98  ? 219.212 168.390 208.923 1.00 67.60  ? 241 ARG A CZ     1 
ATOM   599  N  NH1    . ARG A 1 98  ? 220.501 168.578 209.156 1.00 64.44  ? 241 ARG A NH1    1 
ATOM   600  N  NH2    . ARG A 1 98  ? 218.353 168.442 209.936 1.00 56.78  ? 241 ARG A NH2    1 
ATOM   601  N  N      . VAL A 1 99  ? 223.001 170.470 202.800 1.00 38.09  ? 242 VAL A N      1 
ATOM   602  C  CA     . VAL A 1 99  ? 223.985 170.255 201.744 1.00 34.35  ? 242 VAL A CA     1 
ATOM   603  C  C      . VAL A 1 99  ? 225.391 170.550 202.247 1.00 35.90  ? 242 VAL A C      1 
ATOM   604  O  O      . VAL A 1 99  ? 226.346 169.850 201.887 1.00 37.46  ? 242 VAL A O      1 
ATOM   605  C  CB     . VAL A 1 99  ? 223.636 171.109 200.511 1.00 38.51  ? 242 VAL A CB     1 
ATOM   606  C  CG1    . VAL A 1 99  ? 224.704 170.958 199.441 1.00 36.16  ? 242 VAL A CG1    1 
ATOM   607  C  CG2    . VAL A 1 99  ? 222.272 170.719 199.967 1.00 33.72  ? 242 VAL A CG2    1 
ATOM   608  N  N      . ARG A 1 100 ? 225.549 171.580 203.082 1.00 36.53  ? 243 ARG A N      1 
ATOM   609  C  CA     . ARG A 1 100 ? 226.866 171.903 203.620 1.00 37.35  ? 243 ARG A CA     1 
ATOM   610  C  C      . ARG A 1 100 ? 227.410 170.764 204.474 1.00 37.24  ? 243 ARG A C      1 
ATOM   611  O  O      . ARG A 1 100 ? 228.599 170.435 204.396 1.00 39.36  ? 243 ARG A O      1 
ATOM   612  C  CB     . ARG A 1 100 ? 226.796 173.194 204.434 1.00 41.28  ? 243 ARG A CB     1 
ATOM   613  C  CG     . ARG A 1 100 ? 227.157 174.446 203.657 1.00 41.83  ? 243 ARG A CG     1 
ATOM   614  C  CD     . ARG A 1 100 ? 227.306 175.642 204.583 1.00 44.38  ? 243 ARG A CD     1 
ATOM   615  N  NE     . ARG A 1 100 ? 226.043 176.346 204.775 1.00 48.21  ? 243 ARG A NE     1 
ATOM   616  C  CZ     . ARG A 1 100 ? 225.447 176.509 205.948 1.00 48.17  ? 243 ARG A CZ     1 
ATOM   617  N  NH1    . ARG A 1 100 ? 225.972 176.028 207.062 1.00 48.01  ? 243 ARG A NH1    1 
ATOM   618  N  NH2    . ARG A 1 100 ? 224.295 177.170 206.004 1.00 42.40  ? 243 ARG A NH2    1 
ATOM   619  N  N      . ASP A 1 101 ? 226.556 170.154 205.298 1.00 33.44  ? 244 ASP A N      1 
ATOM   620  C  CA     . ASP A 1 101 ? 227.009 169.072 206.166 1.00 34.15  ? 244 ASP A CA     1 
ATOM   621  C  C      . ASP A 1 101 ? 227.498 167.878 205.356 1.00 37.07  ? 244 ASP A C      1 
ATOM   622  O  O      . ASP A 1 101 ? 228.510 167.257 205.701 1.00 37.47  ? 244 ASP A O      1 
ATOM   623  C  CB     . ASP A 1 101 ? 225.882 168.652 207.109 1.00 39.05  ? 244 ASP A CB     1 
ATOM   624  C  CG     . ASP A 1 101 ? 225.670 169.637 208.240 1.00 51.27  ? 244 ASP A CG     1 
ATOM   625  O  OD1    . ASP A 1 101 ? 226.537 170.514 208.439 1.00 53.81  ? 244 ASP A OD1    1 
ATOM   626  O  OD2    . ASP A 1 101 ? 224.635 169.536 208.932 1.00 59.34  ? 244 ASP A OD2    1 
ATOM   627  N  N      . LEU A 1 102 ? 226.791 167.540 204.275 1.00 37.58  ? 245 LEU A N      1 
ATOM   628  C  CA     . LEU A 1 102 ? 227.141 166.351 203.504 1.00 32.75  ? 245 LEU A CA     1 
ATOM   629  C  C      . LEU A 1 102 ? 228.539 166.462 202.909 1.00 33.75  ? 245 LEU A C      1 
ATOM   630  O  O      . LEU A 1 102 ? 229.320 165.505 202.959 1.00 33.85  ? 245 LEU A O      1 
ATOM   631  C  CB     . LEU A 1 102 ? 226.107 166.120 202.403 1.00 33.95  ? 245 LEU A CB     1 
ATOM   632  C  CG     . LEU A 1 102 ? 225.921 164.679 201.925 1.00 34.25  ? 245 LEU A CG     1 
ATOM   633  C  CD1    . LEU A 1 102 ? 225.204 163.851 202.977 1.00 28.51  ? 245 LEU A CD1    1 
ATOM   634  C  CD2    . LEU A 1 102 ? 225.167 164.644 200.607 1.00 34.99  ? 245 LEU A CD2    1 
ATOM   635  N  N      . PHE A 1 103 ? 228.876 167.622 202.342 1.00 33.44  ? 246 PHE A N      1 
ATOM   636  C  CA     . PHE A 1 103 ? 230.180 167.783 201.708 1.00 32.56  ? 246 PHE A CA     1 
ATOM   637  C  C      . PHE A 1 103 ? 231.303 167.910 202.729 1.00 33.94  ? 246 PHE A C      1 
ATOM   638  O  O      . PHE A 1 103 ? 232.421 167.452 202.470 1.00 36.45  ? 246 PHE A O      1 
ATOM   639  C  CB     . PHE A 1 103 ? 230.167 168.996 200.777 1.00 32.78  ? 246 PHE A CB     1 
ATOM   640  C  CG     . PHE A 1 103 ? 229.642 168.696 199.402 1.00 33.69  ? 246 PHE A CG     1 
ATOM   641  C  CD1    . PHE A 1 103 ? 228.280 168.636 199.165 1.00 34.49  ? 246 PHE A CD1    1 
ATOM   642  C  CD2    . PHE A 1 103 ? 230.511 168.468 198.348 1.00 34.12  ? 246 PHE A CD2    1 
ATOM   643  C  CE1    . PHE A 1 103 ? 227.794 168.359 197.903 1.00 31.24  ? 246 PHE A CE1    1 
ATOM   644  C  CE2    . PHE A 1 103 ? 230.030 168.189 197.084 1.00 31.85  ? 246 PHE A CE2    1 
ATOM   645  C  CZ     . PHE A 1 103 ? 228.670 168.135 196.861 1.00 30.22  ? 246 PHE A CZ     1 
ATOM   646  N  N      . ALA A 1 104 ? 231.034 168.525 203.882 1.00 34.09  ? 247 ALA A N      1 
ATOM   647  C  CA     . ALA A 1 104 ? 232.044 168.590 204.932 1.00 34.14  ? 247 ALA A CA     1 
ATOM   648  C  C      . ALA A 1 104 ? 232.391 167.205 205.459 1.00 35.34  ? 247 ALA A C      1 
ATOM   649  O  O      . ALA A 1 104 ? 233.563 166.921 205.732 1.00 36.58  ? 247 ALA A O      1 
ATOM   650  C  CB     . ALA A 1 104 ? 231.563 169.489 206.071 1.00 31.74  ? 247 ALA A CB     1 
ATOM   651  N  N      . GLN A 1 105 ? 231.392 166.332 205.607 1.00 35.68  ? 248 GLN A N      1 
ATOM   652  C  CA     . GLN A 1 105 ? 231.654 164.972 206.066 1.00 33.69  ? 248 GLN A CA     1 
ATOM   653  C  C      . GLN A 1 105 ? 232.516 164.200 205.075 1.00 36.53  ? 248 GLN A C      1 
ATOM   654  O  O      . GLN A 1 105 ? 233.401 163.442 205.486 1.00 38.05  ? 248 GLN A O      1 
ATOM   655  C  CB     . GLN A 1 105 ? 230.335 164.237 206.304 1.00 35.36  ? 248 GLN A CB     1 
ATOM   656  C  CG     . GLN A 1 105 ? 230.389 163.202 207.414 1.00 44.89  ? 248 GLN A CG     1 
ATOM   657  C  CD     . GLN A 1 105 ? 230.366 163.827 208.794 1.00 55.01  ? 248 GLN A CD     1 
ATOM   658  O  OE1    . GLN A 1 105 ? 229.591 164.746 209.058 1.00 57.58  ? 248 GLN A OE1    1 
ATOM   659  N  NE2    . GLN A 1 105 ? 231.216 163.329 209.685 1.00 57.61  ? 248 GLN A NE2    1 
ATOM   660  N  N      . ALA A 1 106 ? 232.275 164.376 203.775 1.00 36.79  ? 249 ALA A N      1 
ATOM   661  C  CA     . ALA A 1 106 ? 233.021 163.646 202.759 1.00 35.42  ? 249 ALA A CA     1 
ATOM   662  C  C      . ALA A 1 106 ? 234.481 164.071 202.672 1.00 37.36  ? 249 ALA A C      1 
ATOM   663  O  O      . ALA A 1 106 ? 235.321 163.262 202.264 1.00 41.00  ? 249 ALA A O      1 
ATOM   664  C  CB     . ALA A 1 106 ? 232.356 163.818 201.392 1.00 31.33  ? 249 ALA A CB     1 
ATOM   665  N  N      . LYS A 1 107 ? 234.802 165.314 203.034 1.00 37.12  ? 250 LYS A N      1 
ATOM   666  C  CA     . LYS A 1 107 ? 236.187 165.769 202.979 1.00 37.20  ? 250 LYS A CA     1 
ATOM   667  C  C      . LYS A 1 107 ? 237.026 165.202 204.117 1.00 42.64  ? 250 LYS A C      1 
ATOM   668  O  O      . LYS A 1 107 ? 238.223 164.954 203.931 1.00 43.28  ? 250 LYS A O      1 
ATOM   669  C  CB     . LYS A 1 107 ? 236.242 167.298 202.998 1.00 35.27  ? 250 LYS A CB     1 
ATOM   670  C  CG     . LYS A 1 107 ? 235.638 167.955 201.768 1.00 37.54  ? 250 LYS A CG     1 
ATOM   671  C  CD     . LYS A 1 107 ? 235.876 169.455 201.770 1.00 34.70  ? 250 LYS A CD     1 
ATOM   672  C  CE     . LYS A 1 107 ? 234.837 170.181 200.932 1.00 37.42  ? 250 LYS A CE     1 
ATOM   673  N  NZ     . LYS A 1 107 ? 235.087 171.648 200.887 1.00 40.17  ? 250 LYS A NZ     1 
ATOM   674  N  N      . ALA A 1 108 ? 236.429 164.990 205.293 1.00 40.77  ? 251 ALA A N      1 
ATOM   675  C  CA     . ALA A 1 108 ? 237.176 164.434 206.414 1.00 38.27  ? 251 ALA A CA     1 
ATOM   676  C  C      . ALA A 1 108 ? 237.681 163.026 206.130 1.00 42.85  ? 251 ALA A C      1 
ATOM   677  O  O      . ALA A 1 108 ? 238.651 162.590 206.759 1.00 48.30  ? 251 ALA A O      1 
ATOM   678  C  CB     . ALA A 1 108 ? 236.313 164.436 207.676 1.00 39.17  ? 251 ALA A CB     1 
ATOM   679  N  N      . HIS A 1 109 ? 237.049 162.311 205.204 1.00 43.10  ? 252 HIS A N      1 
ATOM   680  C  CA     . HIS A 1 109 ? 237.500 161.001 204.758 1.00 42.72  ? 252 HIS A CA     1 
ATOM   681  C  C      . HIS A 1 109 ? 237.990 161.128 203.323 1.00 45.69  ? 252 HIS A C      1 
ATOM   682  O  O      . HIS A 1 109 ? 237.253 161.606 202.455 1.00 45.33  ? 252 HIS A O      1 
ATOM   683  C  CB     . HIS A 1 109 ? 236.373 159.972 204.860 1.00 39.88  ? 252 HIS A CB     1 
ATOM   684  C  CG     . HIS A 1 109 ? 235.750 159.896 206.220 1.00 49.26  ? 252 HIS A CG     1 
ATOM   685  N  ND1    . HIS A 1 109 ? 235.034 160.938 206.769 1.00 50.60  ? 252 HIS A ND1    1 
ATOM   686  C  CD2    . HIS A 1 109 ? 235.739 158.906 207.143 1.00 55.87  ? 252 HIS A CD2    1 
ATOM   687  C  CE1    . HIS A 1 109 ? 234.608 160.593 207.970 1.00 51.50  ? 252 HIS A CE1    1 
ATOM   688  N  NE2    . HIS A 1 109 ? 235.022 159.365 208.222 1.00 55.48  ? 252 HIS A NE2    1 
ATOM   689  N  N      . ALA A 1 110 ? 239.227 160.702 203.074 1.00 50.56  ? 253 ALA A N      1 
ATOM   690  C  CA     . ALA A 1 110 ? 239.888 161.070 201.828 1.00 47.26  ? 253 ALA A CA     1 
ATOM   691  C  C      . ALA A 1 110 ? 239.125 160.537 200.618 1.00 45.73  ? 253 ALA A C      1 
ATOM   692  O  O      . ALA A 1 110 ? 238.577 161.334 199.846 1.00 48.25  ? 253 ALA A O      1 
ATOM   693  C  CB     . ALA A 1 110 ? 241.337 160.578 201.823 1.00 53.89  ? 253 ALA A CB     1 
ATOM   694  N  N      . PRO A 1 111 ? 239.057 159.217 200.405 1.00 45.62  ? 254 PRO A N      1 
ATOM   695  C  CA     . PRO A 1 111 ? 238.216 158.707 199.314 1.00 40.38  ? 254 PRO A CA     1 
ATOM   696  C  C      . PRO A 1 111 ? 236.786 158.478 199.774 1.00 37.02  ? 254 PRO A C      1 
ATOM   697  O  O      . PRO A 1 111 ? 236.554 157.768 200.757 1.00 40.57  ? 254 PRO A O      1 
ATOM   698  C  CB     . PRO A 1 111 ? 238.903 157.390 198.921 1.00 38.83  ? 254 PRO A CB     1 
ATOM   699  C  CG     . PRO A 1 111 ? 240.206 157.357 199.709 1.00 37.26  ? 254 PRO A CG     1 
ATOM   700  C  CD     . PRO A 1 111 ? 239.926 158.157 200.934 1.00 42.38  ? 254 PRO A CD     1 
ATOM   701  N  N      . SER A 1 112 ? 235.818 159.064 199.074 1.00 34.72  ? 255 SER A N      1 
ATOM   702  C  CA     . SER A 1 112 ? 234.421 158.958 199.469 1.00 33.97  ? 255 SER A CA     1 
ATOM   703  C  C      . SER A 1 112 ? 233.539 159.160 198.244 1.00 31.67  ? 255 SER A C      1 
ATOM   704  O  O      . SER A 1 112 ? 234.012 159.515 197.161 1.00 31.45  ? 255 SER A O      1 
ATOM   705  C  CB     . SER A 1 112 ? 234.083 159.968 200.569 1.00 34.31  ? 255 SER A CB     1 
ATOM   706  O  OG     . SER A 1 112 ? 234.818 159.700 201.749 1.00 40.49  ? 255 SER A OG     1 
ATOM   707  N  N      . ILE A 1 113 ? 232.241 158.932 198.430 1.00 29.65  ? 256 ILE A N      1 
ATOM   708  C  CA     . ILE A 1 113 ? 231.242 159.101 197.383 1.00 26.60  ? 256 ILE A CA     1 
ATOM   709  C  C      . ILE A 1 113 ? 230.084 159.913 197.941 1.00 26.59  ? 256 ILE A C      1 
ATOM   710  O  O      . ILE A 1 113 ? 229.627 159.671 199.063 1.00 29.47  ? 256 ILE A O      1 
ATOM   711  C  CB     . ILE A 1 113 ? 230.738 157.744 196.848 1.00 25.89  ? 256 ILE A CB     1 
ATOM   712  C  CG1    . ILE A 1 113 ? 231.835 157.037 196.053 1.00 29.48  ? 256 ILE A CG1    1 
ATOM   713  C  CG2    . ILE A 1 113 ? 229.494 157.938 195.998 1.00 26.82  ? 256 ILE A CG2    1 
ATOM   714  C  CD1    . ILE A 1 113 ? 231.503 155.605 195.701 1.00 27.55  ? 256 ILE A CD1    1 
ATOM   715  N  N      . VAL A 1 114 ? 229.607 160.876 197.157 1.00 24.87  ? 257 VAL A N      1 
ATOM   716  C  CA     . VAL A 1 114 ? 228.434 161.672 197.500 1.00 24.74  ? 257 VAL A CA     1 
ATOM   717  C  C      . VAL A 1 114 ? 227.346 161.346 196.488 1.00 26.52  ? 257 VAL A C      1 
ATOM   718  O  O      . VAL A 1 114 ? 227.542 161.517 195.279 1.00 28.80  ? 257 VAL A O      1 
ATOM   719  C  CB     . VAL A 1 114 ? 228.747 163.175 197.512 1.00 26.92  ? 257 VAL A CB     1 
ATOM   720  C  CG1    . VAL A 1 114 ? 227.482 163.978 197.774 1.00 24.30  ? 257 VAL A CG1    1 
ATOM   721  C  CG2    . VAL A 1 114 ? 229.805 163.489 198.554 1.00 25.13  ? 257 VAL A CG2    1 
ATOM   722  N  N      . PHE A 1 115 ? 226.201 160.878 196.978 1.00 22.71  ? 258 PHE A N      1 
ATOM   723  C  CA     . PHE A 1 115 ? 225.094 160.459 196.132 1.00 21.74  ? 258 PHE A CA     1 
ATOM   724  C  C      . PHE A 1 115 ? 223.878 161.334 196.398 1.00 23.71  ? 258 PHE A C      1 
ATOM   725  O  O      . PHE A 1 115 ? 223.530 161.596 197.554 1.00 29.13  ? 258 PHE A O      1 
ATOM   726  C  CB     . PHE A 1 115 ? 224.745 158.987 196.372 1.00 22.13  ? 258 PHE A CB     1 
ATOM   727  C  CG     . PHE A 1 115 ? 223.667 158.463 195.467 1.00 20.96  ? 258 PHE A CG     1 
ATOM   728  C  CD1    . PHE A 1 115 ? 223.728 158.674 194.100 1.00 22.11  ? 258 PHE A CD1    1 
ATOM   729  C  CD2    . PHE A 1 115 ? 222.596 157.755 195.983 1.00 22.33  ? 258 PHE A CD2    1 
ATOM   730  C  CE1    . PHE A 1 115 ? 222.739 158.192 193.266 1.00 21.99  ? 258 PHE A CE1    1 
ATOM   731  C  CE2    . PHE A 1 115 ? 221.605 157.269 195.154 1.00 25.28  ? 258 PHE A CE2    1 
ATOM   732  C  CZ     . PHE A 1 115 ? 221.676 157.488 193.794 1.00 22.77  ? 258 PHE A CZ     1 
ATOM   733  N  N      . ILE A 1 116 ? 223.235 161.783 195.323 1.00 23.82  ? 259 ILE A N      1 
ATOM   734  C  CA     . ILE A 1 116 ? 222.045 162.625 195.397 1.00 25.83  ? 259 ILE A CA     1 
ATOM   735  C  C      . ILE A 1 116 ? 220.969 161.944 194.561 1.00 26.72  ? 259 ILE A C      1 
ATOM   736  O  O      . ILE A 1 116 ? 221.020 161.971 193.327 1.00 27.32  ? 259 ILE A O      1 
ATOM   737  C  CB     . ILE A 1 116 ? 222.304 164.053 194.908 1.00 27.58  ? 259 ILE A CB     1 
ATOM   738  C  CG1    . ILE A 1 116 ? 223.466 164.677 195.683 1.00 25.50  ? 259 ILE A CG1    1 
ATOM   739  C  CG2    . ILE A 1 116 ? 221.051 164.902 195.055 1.00 26.78  ? 259 ILE A CG2    1 
ATOM   740  C  CD1    . ILE A 1 116 ? 223.935 165.999 195.120 1.00 27.54  ? 259 ILE A CD1    1 
ATOM   741  N  N      . ASP A 1 117 ? 219.993 161.333 195.226 1.00 29.83  ? 260 ASP A N      1 
ATOM   742  C  CA     . ASP A 1 117 ? 218.909 160.636 194.550 1.00 31.06  ? 260 ASP A CA     1 
ATOM   743  C  C      . ASP A 1 117 ? 217.776 161.602 194.229 1.00 38.69  ? 260 ASP A C      1 
ATOM   744  O  O      . ASP A 1 117 ? 217.492 162.524 194.999 1.00 43.19  ? 260 ASP A O      1 
ATOM   745  C  CB     . ASP A 1 117 ? 218.388 159.488 195.415 1.00 34.63  ? 260 ASP A CB     1 
ATOM   746  C  CG     . ASP A 1 117 ? 217.983 158.279 194.598 1.00 43.87  ? 260 ASP A CG     1 
ATOM   747  O  OD1    . ASP A 1 117 ? 217.924 158.390 193.356 1.00 45.72  ? 260 ASP A OD1    1 
ATOM   748  O  OD2    . ASP A 1 117 ? 217.723 157.217 195.200 1.00 44.70  ? 260 ASP A OD2    1 
ATOM   749  N  N      . GLU A 1 118 ? 217.129 161.381 193.085 1.00 35.57  ? 261 GLU A N      1 
ATOM   750  C  CA     . GLU A 1 118 ? 216.003 162.207 192.649 1.00 38.05  ? 261 GLU A CA     1 
ATOM   751  C  C      . GLU A 1 118 ? 216.402 163.680 192.567 1.00 40.58  ? 261 GLU A C      1 
ATOM   752  O  O      . GLU A 1 118 ? 215.756 164.558 193.141 1.00 45.90  ? 261 GLU A O      1 
ATOM   753  C  CB     . GLU A 1 118 ? 214.797 162.016 193.571 1.00 41.29  ? 261 GLU A CB     1 
ATOM   754  C  CG     . GLU A 1 118 ? 214.042 160.719 193.344 1.00 48.18  ? 261 GLU A CG     1 
ATOM   755  C  CD     . GLU A 1 118 ? 214.107 159.791 194.539 1.00 56.41  ? 261 GLU A CD     1 
ATOM   756  O  OE1    . GLU A 1 118 ? 214.117 160.293 195.683 1.00 57.58  ? 261 GLU A OE1    1 
ATOM   757  O  OE2    . GLU A 1 118 ? 214.148 158.560 194.336 1.00 58.54  ? 261 GLU A OE2    1 
ATOM   758  N  N      . ILE A 1 119 ? 217.485 163.948 191.833 1.00 37.54  ? 262 ILE A N      1 
ATOM   759  C  CA     . ILE A 1 119 ? 217.991 165.310 191.730 1.00 38.64  ? 262 ILE A CA     1 
ATOM   760  C  C      . ILE A 1 119 ? 217.030 166.221 190.980 1.00 40.59  ? 262 ILE A C      1 
ATOM   761  O  O      . ILE A 1 119 ? 217.129 167.447 191.096 1.00 42.81  ? 262 ILE A O      1 
ATOM   762  C  CB     . ILE A 1 119 ? 219.378 165.317 191.061 1.00 36.61  ? 262 ILE A CB     1 
ATOM   763  C  CG1    . ILE A 1 119 ? 220.002 166.711 191.146 1.00 33.00  ? 262 ILE A CG1    1 
ATOM   764  C  CG2    . ILE A 1 119 ? 219.277 164.856 189.614 1.00 29.95  ? 262 ILE A CG2    1 
ATOM   765  C  CD1    . ILE A 1 119 ? 221.490 166.732 190.889 1.00 26.99  ? 262 ILE A CD1    1 
ATOM   766  N  N      . ASP A 1 120 ? 216.096 165.658 190.210 1.00 44.46  ? 263 ASP A N      1 
ATOM   767  C  CA     . ASP A 1 120 ? 215.138 166.484 189.486 1.00 47.34  ? 263 ASP A CA     1 
ATOM   768  C  C      . ASP A 1 120 ? 214.170 167.201 190.418 1.00 49.92  ? 263 ASP A C      1 
ATOM   769  O  O      . ASP A 1 120 ? 213.652 168.262 190.055 1.00 54.53  ? 263 ASP A O      1 
ATOM   770  C  CB     . ASP A 1 120 ? 214.358 165.635 188.481 1.00 45.54  ? 263 ASP A CB     1 
ATOM   771  C  CG     . ASP A 1 120 ? 213.728 164.411 189.116 1.00 50.01  ? 263 ASP A CG     1 
ATOM   772  O  OD1    . ASP A 1 120 ? 214.424 163.382 189.248 1.00 47.54  ? 263 ASP A OD1    1 
ATOM   773  O  OD2    . ASP A 1 120 ? 212.536 164.477 189.482 1.00 53.96  ? 263 ASP A OD2    1 
ATOM   774  N  N      . ALA A 1 121 ? 213.914 166.650 191.605 1.00 47.81  ? 264 ALA A N      1 
ATOM   775  C  CA     . ALA A 1 121 ? 213.022 167.288 192.563 1.00 47.05  ? 264 ALA A CA     1 
ATOM   776  C  C      . ALA A 1 121 ? 213.649 168.496 193.245 1.00 53.50  ? 264 ALA A C      1 
ATOM   777  O  O      . ALA A 1 121 ? 212.932 169.256 193.904 1.00 59.97  ? 264 ALA A O      1 
ATOM   778  C  CB     . ALA A 1 121 ? 212.575 166.277 193.621 1.00 47.62  ? 264 ALA A CB     1 
ATOM   779  N  N      . VAL A 1 122 ? 214.960 168.689 193.107 1.00 55.33  ? 265 VAL A N      1 
ATOM   780  C  CA     . VAL A 1 122 ? 215.631 169.843 193.700 1.00 57.57  ? 265 VAL A CA     1 
ATOM   781  C  C      . VAL A 1 122 ? 216.304 170.739 192.674 1.00 59.57  ? 265 VAL A C      1 
ATOM   782  O  O      . VAL A 1 122 ? 216.707 171.865 193.018 1.00 62.44  ? 265 VAL A O      1 
ATOM   783  C  CB     . VAL A 1 122 ? 216.656 169.385 194.761 1.00 57.82  ? 265 VAL A CB     1 
ATOM   784  C  CG1    . VAL A 1 122 ? 217.869 168.758 194.093 1.00 49.64  ? 265 VAL A CG1    1 
ATOM   785  C  CG2    . VAL A 1 122 ? 217.067 170.553 195.641 1.00 60.64  ? 265 VAL A CG2    1 
ATOM   786  N  N      . GLY A 1 123 ? 216.457 170.313 191.424 1.00 58.68  ? 266 GLY A N      1 
ATOM   787  C  CA     . GLY A 1 123 ? 217.078 171.138 190.405 1.00 56.16  ? 266 GLY A CA     1 
ATOM   788  C  C      . GLY A 1 123 ? 216.266 171.211 189.127 1.00 56.16  ? 266 GLY A C      1 
ATOM   789  O  O      . GLY A 1 123 ? 216.812 171.141 188.027 1.00 56.38  ? 266 GLY A O      1 
ATOM   790  N  N      . ARG A 1 137 ? 213.681 176.969 197.511 1.00 66.99  ? 280 ARG A N      1 
ATOM   791  C  CA     . ARG A 1 137 ? 214.132 176.025 196.496 1.00 72.41  ? 280 ARG A CA     1 
ATOM   792  C  C      . ARG A 1 137 ? 215.352 176.563 195.756 1.00 70.22  ? 280 ARG A C      1 
ATOM   793  O  O      . ARG A 1 137 ? 216.263 175.811 195.412 1.00 66.55  ? 280 ARG A O      1 
ATOM   794  C  CB     . ARG A 1 137 ? 213.007 175.723 195.504 1.00 74.44  ? 280 ARG A CB     1 
ATOM   795  C  CG     . ARG A 1 137 ? 212.781 174.240 195.252 1.00 76.46  ? 280 ARG A CG     1 
ATOM   796  C  CD     . ARG A 1 137 ? 212.464 173.966 193.791 1.00 79.44  ? 280 ARG A CD     1 
ATOM   797  N  NE     . ARG A 1 137 ? 213.649 174.052 192.946 1.00 82.99  ? 280 ARG A NE     1 
ATOM   798  C  CZ     . ARG A 1 137 ? 213.672 174.599 191.738 1.00 83.65  ? 280 ARG A CZ     1 
ATOM   799  N  NH1    . ARG A 1 137 ? 212.585 175.124 191.197 1.00 83.61  ? 280 ARG A NH1    1 
ATOM   800  N  NH2    . ARG A 1 137 ? 214.813 174.618 191.056 1.00 75.24  ? 280 ARG A NH2    1 
ATOM   801  N  N      . GLU A 1 138 ? 215.362 177.876 195.514 1.00 71.59  ? 281 GLU A N      1 
ATOM   802  C  CA     . GLU A 1 138 ? 216.479 178.495 194.812 1.00 68.00  ? 281 GLU A CA     1 
ATOM   803  C  C      . GLU A 1 138 ? 217.736 178.550 195.670 1.00 63.66  ? 281 GLU A C      1 
ATOM   804  O  O      . GLU A 1 138 ? 218.848 178.483 195.135 1.00 60.71  ? 281 GLU A O      1 
ATOM   805  C  CB     . GLU A 1 138 ? 216.097 179.903 194.353 1.00 71.15  ? 281 GLU A CB     1 
ATOM   806  C  CG     . GLU A 1 138 ? 217.179 180.611 193.556 1.00 77.28  ? 281 GLU A CG     1 
ATOM   807  C  CD     . GLU A 1 138 ? 216.766 182.004 193.125 1.00 87.97  ? 281 GLU A CD     1 
ATOM   808  O  OE1    . GLU A 1 138 ? 215.645 182.427 193.473 1.00 88.56  ? 281 GLU A OE1    1 
ATOM   809  O  OE2    . GLU A 1 138 ? 217.564 182.676 192.438 1.00 92.54  ? 281 GLU A OE2    1 
ATOM   810  N  N      . GLN A 1 139 ? 217.586 178.674 196.990 1.00 61.54  ? 282 GLN A N      1 
ATOM   811  C  CA     . GLN A 1 139 ? 218.748 178.703 197.870 1.00 60.00  ? 282 GLN A CA     1 
ATOM   812  C  C      . GLN A 1 139 ? 219.425 177.342 197.967 1.00 53.06  ? 282 GLN A C      1 
ATOM   813  O  O      . GLN A 1 139 ? 220.657 177.273 198.047 1.00 51.47  ? 282 GLN A O      1 
ATOM   814  C  CB     . GLN A 1 139 ? 218.343 179.189 199.262 1.00 64.21  ? 282 GLN A CB     1 
ATOM   815  C  CG     . GLN A 1 139 ? 217.329 180.322 199.253 1.00 71.08  ? 282 GLN A CG     1 
ATOM   816  C  CD     . GLN A 1 139 ? 217.805 181.525 198.462 1.00 79.59  ? 282 GLN A CD     1 
ATOM   817  O  OE1    . GLN A 1 139 ? 219.006 181.727 198.278 1.00 78.03  ? 282 GLN A OE1    1 
ATOM   818  N  NE2    . GLN A 1 139 ? 216.863 182.333 197.990 1.00 79.96  ? 282 GLN A NE2    1 
ATOM   819  N  N      . THR A 1 140 ? 218.647 176.257 197.965 1.00 48.67  ? 283 THR A N      1 
ATOM   820  C  CA     . THR A 1 140 ? 219.239 174.925 198.018 1.00 47.60  ? 283 THR A CA     1 
ATOM   821  C  C      . THR A 1 140 ? 220.078 174.632 196.781 1.00 48.13  ? 283 THR A C      1 
ATOM   822  O  O      . THR A 1 140 ? 221.162 174.049 196.893 1.00 44.89  ? 283 THR A O      1 
ATOM   823  C  CB     . THR A 1 140 ? 218.147 173.867 198.178 1.00 48.70  ? 283 THR A CB     1 
ATOM   824  O  OG1    . THR A 1 140 ? 217.294 174.220 199.274 1.00 55.12  ? 283 THR A OG1    1 
ATOM   825  C  CG2    . THR A 1 140 ? 218.763 172.501 198.442 1.00 41.77  ? 283 THR A CG2    1 
ATOM   826  N  N      . LEU A 1 141 ? 219.596 175.022 195.599 1.00 47.16  ? 284 LEU A N      1 
ATOM   827  C  CA     . LEU A 1 141 ? 220.351 174.791 194.373 1.00 43.72  ? 284 LEU A CA     1 
ATOM   828  C  C      . LEU A 1 141 ? 221.633 175.615 194.339 1.00 42.40  ? 284 LEU A C      1 
ATOM   829  O  O      . LEU A 1 141 ? 222.667 175.139 193.859 1.00 41.76  ? 284 LEU A O      1 
ATOM   830  C  CB     . LEU A 1 141 ? 219.483 175.106 193.155 1.00 48.82  ? 284 LEU A CB     1 
ATOM   831  C  CG     . LEU A 1 141 ? 220.144 174.928 191.787 1.00 47.98  ? 284 LEU A CG     1 
ATOM   832  C  CD1    . LEU A 1 141 ? 220.279 173.455 191.440 1.00 46.12  ? 284 LEU A CD1    1 
ATOM   833  C  CD2    . LEU A 1 141 ? 219.360 175.665 190.715 1.00 48.93  ? 284 LEU A CD2    1 
ATOM   834  N  N      . ASN A 1 142 ? 221.584 176.853 194.838 1.00 43.83  ? 285 ASN A N      1 
ATOM   835  C  CA     . ASN A 1 142 ? 222.776 177.693 194.845 1.00 39.88  ? 285 ASN A CA     1 
ATOM   836  C  C      . ASN A 1 142 ? 223.874 177.104 195.720 1.00 37.91  ? 285 ASN A C      1 
ATOM   837  O  O      . ASN A 1 142 ? 225.054 177.162 195.358 1.00 38.12  ? 285 ASN A O      1 
ATOM   838  C  CB     . ASN A 1 142 ? 222.422 179.105 195.312 1.00 48.34  ? 285 ASN A CB     1 
ATOM   839  C  CG     . ASN A 1 142 ? 222.022 180.014 194.167 1.00 53.79  ? 285 ASN A CG     1 
ATOM   840  O  OD1    . ASN A 1 142 ? 222.869 180.481 193.406 1.00 55.92  ? 285 ASN A OD1    1 
ATOM   841  N  ND2    . ASN A 1 142 ? 220.726 180.270 194.040 1.00 59.73  ? 285 ASN A ND2    1 
ATOM   842  N  N      . GLN A 1 143 ? 223.510 176.539 196.874 1.00 36.24  ? 286 GLN A N      1 
ATOM   843  C  CA     . GLN A 1 143 ? 224.509 175.930 197.746 1.00 34.09  ? 286 GLN A CA     1 
ATOM   844  C  C      . GLN A 1 143 ? 225.192 174.751 197.065 1.00 35.65  ? 286 GLN A C      1 
ATOM   845  O  O      . GLN A 1 143 ? 226.406 174.561 197.210 1.00 34.35  ? 286 GLN A O      1 
ATOM   846  C  CB     . GLN A 1 143 ? 223.862 175.493 199.059 1.00 33.84  ? 286 GLN A CB     1 
ATOM   847  C  CG     . GLN A 1 143 ? 224.854 175.133 200.154 1.00 37.12  ? 286 GLN A CG     1 
ATOM   848  C  CD     . GLN A 1 143 ? 225.709 176.311 200.579 1.00 37.88  ? 286 GLN A CD     1 
ATOM   849  O  OE1    . GLN A 1 143 ? 225.202 177.305 201.097 1.00 41.84  ? 286 GLN A OE1    1 
ATOM   850  N  NE2    . GLN A 1 143 ? 227.014 176.204 200.363 1.00 34.52  ? 286 GLN A NE2    1 
ATOM   851  N  N      . LEU A 1 144 ? 224.431 173.944 196.322 1.00 35.37  ? 287 LEU A N      1 
ATOM   852  C  CA     . LEU A 1 144 ? 225.019 172.797 195.638 1.00 34.41  ? 287 LEU A CA     1 
ATOM   853  C  C      . LEU A 1 144 ? 226.039 173.236 194.596 1.00 32.85  ? 287 LEU A C      1 
ATOM   854  O  O      . LEU A 1 144 ? 227.090 172.603 194.444 1.00 32.01  ? 287 LEU A O      1 
ATOM   855  C  CB     . LEU A 1 144 ? 223.921 171.951 194.994 1.00 35.40  ? 287 LEU A CB     1 
ATOM   856  C  CG     . LEU A 1 144 ? 224.379 170.701 194.240 1.00 35.08  ? 287 LEU A CG     1 
ATOM   857  C  CD1    . LEU A 1 144 ? 224.981 169.684 195.196 1.00 32.42  ? 287 LEU A CD1    1 
ATOM   858  C  CD2    . LEU A 1 144 ? 223.224 170.093 193.464 1.00 31.30  ? 287 LEU A CD2    1 
ATOM   859  N  N      . LEU A 1 145 ? 225.747 174.313 193.864 1.00 33.20  ? 288 LEU A N      1 
ATOM   860  C  CA     . LEU A 1 145 ? 226.700 174.816 192.880 1.00 33.64  ? 288 LEU A CA     1 
ATOM   861  C  C      . LEU A 1 145 ? 227.986 175.298 193.538 1.00 35.16  ? 288 LEU A C      1 
ATOM   862  O  O      . LEU A 1 145 ? 229.074 175.096 192.989 1.00 38.78  ? 288 LEU A O      1 
ATOM   863  C  CB     . LEU A 1 145 ? 226.069 175.941 192.062 1.00 36.07  ? 288 LEU A CB     1 
ATOM   864  C  CG     . LEU A 1 145 ? 224.887 175.558 191.169 1.00 39.66  ? 288 LEU A CG     1 
ATOM   865  C  CD1    . LEU A 1 145 ? 224.315 176.787 190.483 1.00 39.56  ? 288 LEU A CD1    1 
ATOM   866  C  CD2    . LEU A 1 145 ? 225.301 174.513 190.146 1.00 39.66  ? 288 LEU A CD2    1 
ATOM   867  N  N      . VAL A 1 146 ? 227.883 175.936 194.706 1.00 34.23  ? 289 VAL A N      1 
ATOM   868  C  CA     . VAL A 1 146 ? 229.076 176.400 195.406 1.00 33.96  ? 289 VAL A CA     1 
ATOM   869  C  C      . VAL A 1 146 ? 229.908 175.223 195.900 1.00 33.49  ? 289 VAL A C      1 
ATOM   870  O  O      . VAL A 1 146 ? 231.144 175.274 195.874 1.00 35.78  ? 289 VAL A O      1 
ATOM   871  C  CB     . VAL A 1 146 ? 228.684 177.335 196.564 1.00 36.00  ? 289 VAL A CB     1 
ATOM   872  C  CG1    . VAL A 1 146 ? 229.868 177.559 197.491 1.00 34.29  ? 289 VAL A CG1    1 
ATOM   873  C  CG2    . VAL A 1 146 ? 228.167 178.658 196.026 1.00 34.60  ? 289 VAL A CG2    1 
ATOM   874  N  N      . GLU A 1 147 ? 229.257 174.152 196.359 1.00 35.61  ? 290 GLU A N      1 
ATOM   875  C  CA     . GLU A 1 147 ? 229.983 172.996 196.873 1.00 35.22  ? 290 GLU A CA     1 
ATOM   876  C  C      . GLU A 1 147 ? 230.733 172.249 195.778 1.00 37.46  ? 290 GLU A C      1 
ATOM   877  O  O      . GLU A 1 147 ? 231.841 171.758 196.019 1.00 38.17  ? 290 GLU A O      1 
ATOM   878  C  CB     . GLU A 1 147 ? 229.020 172.045 197.586 1.00 35.37  ? 290 GLU A CB     1 
ATOM   879  C  CG     . GLU A 1 147 ? 228.315 172.655 198.785 1.00 37.43  ? 290 GLU A CG     1 
ATOM   880  C  CD     . GLU A 1 147 ? 229.268 172.974 199.919 1.00 48.09  ? 290 GLU A CD     1 
ATOM   881  O  OE1    . GLU A 1 147 ? 230.412 172.475 199.893 1.00 50.24  ? 290 GLU A OE1    1 
ATOM   882  O  OE2    . GLU A 1 147 ? 228.872 173.721 200.837 1.00 53.01  ? 290 GLU A OE2    1 
ATOM   883  N  N      . MET A 1 148 ? 230.154 172.151 194.580 1.00 35.82  ? 291 MET A N      1 
ATOM   884  C  CA     . MET A 1 148 ? 230.809 171.417 193.502 1.00 34.80  ? 291 MET A CA     1 
ATOM   885  C  C      . MET A 1 148 ? 232.131 172.065 193.113 1.00 39.37  ? 291 MET A C      1 
ATOM   886  O  O      . MET A 1 148 ? 233.104 171.366 192.804 1.00 41.94  ? 291 MET A O      1 
ATOM   887  C  CB     . MET A 1 148 ? 229.880 171.322 192.291 1.00 39.55  ? 291 MET A CB     1 
ATOM   888  C  CG     . MET A 1 148 ? 228.569 170.606 192.567 1.00 40.54  ? 291 MET A CG     1 
ATOM   889  S  SD     . MET A 1 148 ? 228.753 168.813 192.618 1.00 50.03  ? 291 MET A SD     1 
ATOM   890  C  CE     . MET A 1 148 ? 229.193 168.467 190.917 1.00 31.40  ? 291 MET A CE     1 
ATOM   891  N  N      . ASP A 1 149 ? 232.187 173.396 193.115 1.00 39.63  ? 292 ASP A N      1 
ATOM   892  C  CA     . ASP A 1 149 ? 233.397 174.114 192.740 1.00 38.85  ? 292 ASP A CA     1 
ATOM   893  C  C      . ASP A 1 149 ? 234.405 174.228 193.877 1.00 39.63  ? 292 ASP A C      1 
ATOM   894  O  O      . ASP A 1 149 ? 235.514 174.721 193.648 1.00 40.61  ? 292 ASP A O      1 
ATOM   895  C  CB     . ASP A 1 149 ? 233.039 175.517 192.241 1.00 42.17  ? 292 ASP A CB     1 
ATOM   896  C  CG     . ASP A 1 149 ? 232.133 175.491 191.026 1.00 54.41  ? 292 ASP A CG     1 
ATOM   897  O  OD1    . ASP A 1 149 ? 232.221 174.530 190.234 1.00 58.68  ? 292 ASP A OD1    1 
ATOM   898  O  OD2    . ASP A 1 149 ? 231.329 176.433 190.865 1.00 55.01  ? 292 ASP A OD2    1 
ATOM   899  N  N      . GLY A 1 150 ? 234.057 173.786 195.084 1.00 37.41  ? 293 GLY A N      1 
ATOM   900  C  CA     . GLY A 1 150 ? 234.890 174.042 196.242 1.00 34.50  ? 293 GLY A CA     1 
ATOM   901  C  C      . GLY A 1 150 ? 235.726 172.886 196.754 1.00 39.81  ? 293 GLY A C      1 
ATOM   902  O  O      . GLY A 1 150 ? 236.500 173.063 197.699 1.00 41.69  ? 293 GLY A O      1 
ATOM   903  N  N      . PHE A 1 151 ? 235.593 171.704 196.160 1.00 38.60  ? 294 PHE A N      1 
ATOM   904  C  CA     . PHE A 1 151 ? 236.338 170.540 196.612 1.00 35.47  ? 294 PHE A CA     1 
ATOM   905  C  C      . PHE A 1 151 ? 237.370 170.128 195.569 1.00 37.02  ? 294 PHE A C      1 
ATOM   906  O  O      . PHE A 1 151 ? 237.240 170.423 194.378 1.00 37.50  ? 294 PHE A O      1 
ATOM   907  C  CB     . PHE A 1 151 ? 235.397 169.370 196.939 1.00 34.14  ? 294 PHE A CB     1 
ATOM   908  C  CG     . PHE A 1 151 ? 234.893 168.623 195.734 1.00 35.03  ? 294 PHE A CG     1 
ATOM   909  C  CD1    . PHE A 1 151 ? 235.594 167.539 195.230 1.00 33.48  ? 294 PHE A CD1    1 
ATOM   910  C  CD2    . PHE A 1 151 ? 233.708 168.990 195.121 1.00 34.05  ? 294 PHE A CD2    1 
ATOM   911  C  CE1    . PHE A 1 151 ? 235.129 166.846 194.128 1.00 31.90  ? 294 PHE A CE1    1 
ATOM   912  C  CE2    . PHE A 1 151 ? 233.238 168.301 194.019 1.00 34.27  ? 294 PHE A CE2    1 
ATOM   913  C  CZ     . PHE A 1 151 ? 233.950 167.227 193.523 1.00 31.41  ? 294 PHE A CZ     1 
ATOM   914  N  N      . ASP A 1 152 ? 238.411 169.445 196.041 1.00 37.81  ? 295 ASP A N      1 
ATOM   915  C  CA     . ASP A 1 152 ? 239.535 169.036 195.208 1.00 42.09  ? 295 ASP A CA     1 
ATOM   916  C  C      . ASP A 1 152 ? 239.308 167.612 194.717 1.00 45.54  ? 295 ASP A C      1 
ATOM   917  O  O      . ASP A 1 152 ? 239.145 166.691 195.524 1.00 46.10  ? 295 ASP A O      1 
ATOM   918  C  CB     . ASP A 1 152 ? 240.849 169.136 195.983 1.00 48.02  ? 295 ASP A CB     1 
ATOM   919  C  CG     . ASP A 1 152 ? 242.064 168.895 195.107 1.00 55.20  ? 295 ASP A CG     1 
ATOM   920  O  OD1    . ASP A 1 152 ? 241.950 169.054 193.873 1.00 55.70  ? 295 ASP A OD1    1 
ATOM   921  O  OD2    . ASP A 1 152 ? 243.132 168.548 195.652 1.00 55.93  ? 295 ASP A OD2    1 
ATOM   922  N  N      . SER A 1 153 ? 239.300 167.436 193.393 1.00 42.55  ? 296 SER A N      1 
ATOM   923  C  CA     . SER A 1 153 ? 239.051 166.118 192.820 1.00 39.40  ? 296 SER A CA     1 
ATOM   924  C  C      . SER A 1 153 ? 240.217 165.165 193.050 1.00 43.04  ? 296 SER A C      1 
ATOM   925  O  O      . SER A 1 153 ? 240.018 163.946 193.093 1.00 41.21  ? 296 SER A O      1 
ATOM   926  C  CB     . SER A 1 153 ? 238.759 166.246 191.325 1.00 38.85  ? 296 SER A CB     1 
ATOM   927  O  OG     . SER A 1 153 ? 238.574 164.974 190.731 1.00 43.89  ? 296 SER A OG     1 
ATOM   928  N  N      . LYS A 1 154 ? 241.432 165.693 193.203 1.00 46.66  ? 297 LYS A N      1 
ATOM   929  C  CA     . LYS A 1 154 ? 242.610 164.846 193.346 1.00 43.48  ? 297 LYS A CA     1 
ATOM   930  C  C      . LYS A 1 154 ? 242.655 164.106 194.676 1.00 44.48  ? 297 LYS A C      1 
ATOM   931  O  O      . LYS A 1 154 ? 243.500 163.221 194.841 1.00 42.63  ? 297 LYS A O      1 
ATOM   932  C  CB     . LYS A 1 154 ? 243.880 165.680 193.174 1.00 45.00  ? 297 LYS A CB     1 
ATOM   933  C  CG     . LYS A 1 154 ? 244.183 166.046 191.730 1.00 46.60  ? 297 LYS A CG     1 
ATOM   934  C  CD     . LYS A 1 154 ? 245.562 166.668 191.591 1.00 47.82  ? 297 LYS A CD     1 
ATOM   935  C  CE     . LYS A 1 154 ? 245.468 168.155 191.299 1.00 53.89  ? 297 LYS A CE     1 
ATOM   936  N  NZ     . LYS A 1 154 ? 246.782 168.724 190.893 1.00 61.59  ? 297 LYS A NZ     1 
ATOM   937  N  N      . GLU A 1 155 ? 241.780 164.444 195.624 1.00 47.19  ? 298 GLU A N      1 
ATOM   938  C  CA     . GLU A 1 155 ? 241.721 163.727 196.891 1.00 44.83  ? 298 GLU A CA     1 
ATOM   939  C  C      . GLU A 1 155 ? 240.985 162.398 196.788 1.00 45.08  ? 298 GLU A C      1 
ATOM   940  O  O      . GLU A 1 155 ? 241.079 161.585 197.713 1.00 42.96  ? 298 GLU A O      1 
ATOM   941  C  CB     . GLU A 1 155 ? 241.053 164.597 197.959 1.00 48.27  ? 298 GLU A CB     1 
ATOM   942  C  CG     . GLU A 1 155 ? 241.618 166.003 198.057 1.00 54.65  ? 298 GLU A CG     1 
ATOM   943  C  CD     . GLU A 1 155 ? 242.923 166.051 198.827 1.00 67.03  ? 298 GLU A CD     1 
ATOM   944  O  OE1    . GLU A 1 155 ? 243.692 165.069 198.760 1.00 69.75  ? 298 GLU A OE1    1 
ATOM   945  O  OE2    . GLU A 1 155 ? 243.179 167.071 199.501 1.00 70.95  ? 298 GLU A OE2    1 
ATOM   946  N  N      . GLY A 1 156 ? 240.261 162.158 195.697 1.00 40.70  ? 299 GLY A N      1 
ATOM   947  C  CA     . GLY A 1 156 ? 239.516 160.925 195.539 1.00 33.02  ? 299 GLY A CA     1 
ATOM   948  C  C      . GLY A 1 156 ? 238.065 161.054 195.953 1.00 36.16  ? 299 GLY A C      1 
ATOM   949  O  O      . GLY A 1 156 ? 237.546 160.211 196.690 1.00 41.94  ? 299 GLY A O      1 
ATOM   950  N  N      . ILE A 1 157 ? 237.401 162.108 195.486 1.00 34.33  ? 300 ILE A N      1 
ATOM   951  C  CA     . ILE A 1 157 ? 236.005 162.374 195.803 1.00 30.73  ? 300 ILE A CA     1 
ATOM   952  C  C      . ILE A 1 157 ? 235.220 162.470 194.503 1.00 31.01  ? 300 ILE A C      1 
ATOM   953  O  O      . ILE A 1 157 ? 235.632 163.165 193.568 1.00 36.23  ? 300 ILE A O      1 
ATOM   954  C  CB     . ILE A 1 157 ? 235.844 163.664 196.634 1.00 34.61  ? 300 ILE A CB     1 
ATOM   955  C  CG1    . ILE A 1 157 ? 236.587 163.536 197.965 1.00 37.14  ? 300 ILE A CG1    1 
ATOM   956  C  CG2    . ILE A 1 157 ? 234.373 163.968 196.868 1.00 29.16  ? 300 ILE A CG2    1 
ATOM   957  C  CD1    . ILE A 1 157 ? 236.886 164.863 198.628 1.00 35.48  ? 300 ILE A CD1    1 
ATOM   958  N  N      . ILE A 1 158 ? 234.089 161.768 194.446 1.00 30.31  ? 301 ILE A N      1 
ATOM   959  C  CA     . ILE A 1 158 ? 233.226 161.761 193.273 1.00 27.21  ? 301 ILE A CA     1 
ATOM   960  C  C      . ILE A 1 158 ? 231.787 161.982 193.719 1.00 26.08  ? 301 ILE A C      1 
ATOM   961  O  O      . ILE A 1 158 ? 231.396 161.607 194.827 1.00 28.62  ? 301 ILE A O      1 
ATOM   962  C  CB     . ILE A 1 158 ? 233.355 160.445 192.473 1.00 28.92  ? 301 ILE A CB     1 
ATOM   963  C  CG1    . ILE A 1 158 ? 232.566 160.531 191.165 1.00 31.11  ? 301 ILE A CG1    1 
ATOM   964  C  CG2    . ILE A 1 158 ? 232.885 159.267 193.308 1.00 29.34  ? 301 ILE A CG2    1 
ATOM   965  C  CD1    . ILE A 1 158 ? 233.173 161.468 190.145 1.00 29.33  ? 301 ILE A CD1    1 
ATOM   966  N  N      . VAL A 1 159 ? 230.998 162.597 192.842 1.00 25.57  ? 302 VAL A N      1 
ATOM   967  C  CA     . VAL A 1 159 ? 229.596 162.901 193.105 1.00 22.88  ? 302 VAL A CA     1 
ATOM   968  C  C      . VAL A 1 159 ? 228.748 162.199 192.054 1.00 23.36  ? 302 VAL A C      1 
ATOM   969  O  O      . VAL A 1 159 ? 229.067 162.245 190.860 1.00 24.23  ? 302 VAL A O      1 
ATOM   970  C  CB     . VAL A 1 159 ? 229.331 164.418 193.099 1.00 23.46  ? 302 VAL A CB     1 
ATOM   971  C  CG1    . VAL A 1 159 ? 227.893 164.707 193.498 1.00 21.10  ? 302 VAL A CG1    1 
ATOM   972  C  CG2    . VAL A 1 159 ? 230.298 165.126 194.030 1.00 23.25  ? 302 VAL A CG2    1 
ATOM   973  N  N      . MET A 1 160 ? 227.673 161.551 192.498 1.00 24.01  ? 303 MET A N      1 
ATOM   974  C  CA     . MET A 1 160 ? 226.778 160.818 191.615 1.00 21.36  ? 303 MET A CA     1 
ATOM   975  C  C      . MET A 1 160 ? 225.339 161.249 191.860 1.00 20.82  ? 303 MET A C      1 
ATOM   976  O  O      . MET A 1 160 ? 224.983 161.685 192.957 1.00 22.87  ? 303 MET A O      1 
ATOM   977  C  CB     . MET A 1 160 ? 226.909 159.302 191.816 1.00 22.48  ? 303 MET A CB     1 
ATOM   978  C  CG     . MET A 1 160 ? 228.046 158.667 191.035 1.00 26.77  ? 303 MET A CG     1 
ATOM   979  S  SD     . MET A 1 160 ? 228.650 157.144 191.787 1.00 51.46  ? 303 MET A SD     1 
ATOM   980  C  CE     . MET A 1 160 ? 227.755 155.917 190.838 1.00 34.31  ? 303 MET A CE     1 
ATOM   981  N  N      . ALA A 1 161 ? 224.515 161.122 190.822 1.00 20.14  ? 304 ALA A N      1 
ATOM   982  C  CA     . ALA A 1 161 ? 223.108 161.485 190.900 1.00 19.82  ? 304 ALA A CA     1 
ATOM   983  C  C      . ALA A 1 161 ? 222.315 160.591 189.957 1.00 19.62  ? 304 ALA A C      1 
ATOM   984  O  O      . ALA A 1 161 ? 222.868 159.963 189.051 1.00 20.65  ? 304 ALA A O      1 
ATOM   985  C  CB     . ALA A 1 161 ? 222.892 162.965 190.566 1.00 18.63  ? 304 ALA A CB     1 
ATOM   986  N  N      . ALA A 1 162 ? 221.003 160.538 190.182 1.00 20.71  ? 305 ALA A N      1 
ATOM   987  C  CA     . ALA A 1 162 ? 220.124 159.708 189.372 1.00 20.67  ? 305 ALA A CA     1 
ATOM   988  C  C      . ALA A 1 162 ? 218.789 160.413 189.185 1.00 24.91  ? 305 ALA A C      1 
ATOM   989  O  O      . ALA A 1 162 ? 218.368 161.212 190.026 1.00 29.69  ? 305 ALA A O      1 
ATOM   990  C  CB     . ALA A 1 162 ? 219.909 158.329 190.006 1.00 16.55  ? 305 ALA A CB     1 
ATOM   991  N  N      . THR A 1 163 ? 218.129 160.109 188.069 1.00 25.97  ? 306 THR A N      1 
ATOM   992  C  CA     . THR A 1 163 ? 216.826 160.685 187.765 1.00 29.58  ? 306 THR A CA     1 
ATOM   993  C  C      . THR A 1 163 ? 216.199 159.909 186.617 1.00 27.18  ? 306 THR A C      1 
ATOM   994  O  O      . THR A 1 163 ? 216.882 159.197 185.877 1.00 26.94  ? 306 THR A O      1 
ATOM   995  C  CB     . THR A 1 163 ? 216.933 162.172 187.406 1.00 33.01  ? 306 THR A CB     1 
ATOM   996  O  OG1    . THR A 1 163 ? 215.622 162.746 187.347 1.00 40.54  ? 306 THR A OG1    1 
ATOM   997  C  CG2    . THR A 1 163 ? 217.615 162.346 186.058 1.00 27.47  ? 306 THR A CG2    1 
ATOM   998  N  N      . ASN A 1 164 ? 214.879 160.057 186.480 1.00 28.61  ? 307 ASN A N      1 
ATOM   999  C  CA     . ASN A 1 164 ? 214.142 159.489 185.356 1.00 29.70  ? 307 ASN A CA     1 
ATOM   1000 C  C      . ASN A 1 164 ? 213.422 160.564 184.547 1.00 33.60  ? 307 ASN A C      1 
ATOM   1001 O  O      . ASN A 1 164 ? 212.584 160.241 183.700 1.00 38.25  ? 307 ASN A O      1 
ATOM   1002 C  CB     . ASN A 1 164 ? 213.151 158.426 185.839 1.00 25.69  ? 307 ASN A CB     1 
ATOM   1003 C  CG     . ASN A 1 164 ? 212.219 158.940 186.919 1.00 35.62  ? 307 ASN A CG     1 
ATOM   1004 O  OD1    . ASN A 1 164 ? 211.706 160.055 186.836 1.00 46.07  ? 307 ASN A OD1    1 
ATOM   1005 N  ND2    . ASN A 1 164 ? 211.991 158.122 187.940 1.00 32.02  ? 307 ASN A ND2    1 
ATOM   1006 N  N      . ARG A 1 165 ? 213.733 161.836 184.793 1.00 35.92  ? 308 ARG A N      1 
ATOM   1007 C  CA     . ARG A 1 165 ? 213.185 162.955 184.024 1.00 37.07  ? 308 ARG A CA     1 
ATOM   1008 C  C      . ARG A 1 165 ? 214.328 163.895 183.665 1.00 38.43  ? 308 ARG A C      1 
ATOM   1009 O  O      . ARG A 1 165 ? 214.389 165.039 184.129 1.00 42.03  ? 308 ARG A O      1 
ATOM   1010 C  CB     . ARG A 1 165 ? 212.095 163.681 184.814 1.00 41.06  ? 308 ARG A CB     1 
ATOM   1011 C  CG     . ARG A 1 165 ? 211.102 162.756 185.500 1.00 43.07  ? 308 ARG A CG     1 
ATOM   1012 C  CD     . ARG A 1 165 ? 210.027 163.541 186.233 1.00 56.95  ? 308 ARG A CD     1 
ATOM   1013 N  NE     . ARG A 1 165 ? 209.083 164.167 185.314 1.00 74.75  ? 308 ARG A NE     1 
ATOM   1014 C  CZ     . ARG A 1 165 ? 208.194 165.087 185.663 1.00 78.65  ? 308 ARG A CZ     1 
ATOM   1015 N  NH1    . ARG A 1 165 ? 208.096 165.515 186.910 1.00 73.49  ? 308 ARG A NH1    1 
ATOM   1016 N  NH2    . ARG A 1 165 ? 207.384 165.590 184.736 1.00 74.62  ? 308 ARG A NH2    1 
ATOM   1017 N  N      . PRO A 1 166 ? 215.260 163.437 182.824 1.00 38.94  ? 309 PRO A N      1 
ATOM   1018 C  CA     . PRO A 1 166 ? 216.464 164.240 182.555 1.00 38.31  ? 309 PRO A CA     1 
ATOM   1019 C  C      . PRO A 1 166 ? 216.203 165.522 181.783 1.00 41.88  ? 309 PRO A C      1 
ATOM   1020 O  O      . PRO A 1 166 ? 217.067 166.407 181.789 1.00 49.47  ? 309 PRO A O      1 
ATOM   1021 C  CB     . PRO A 1 166 ? 217.351 163.281 181.750 1.00 35.64  ? 309 PRO A CB     1 
ATOM   1022 C  CG     . PRO A 1 166 ? 216.394 162.329 181.118 1.00 35.95  ? 309 PRO A CG     1 
ATOM   1023 C  CD     . PRO A 1 166 ? 215.270 162.156 182.098 1.00 33.68  ? 309 PRO A CD     1 
ATOM   1024 N  N      . ASP A 1 167 ? 215.056 165.659 181.123 1.00 43.61  ? 310 ASP A N      1 
ATOM   1025 C  CA     . ASP A 1 167 ? 214.812 166.781 180.228 1.00 45.24  ? 310 ASP A CA     1 
ATOM   1026 C  C      . ASP A 1 167 ? 214.216 167.995 180.931 1.00 49.65  ? 310 ASP A C      1 
ATOM   1027 O  O      . ASP A 1 167 ? 213.892 168.982 180.264 1.00 54.93  ? 310 ASP A O      1 
ATOM   1028 C  CB     . ASP A 1 167 ? 213.900 166.347 179.078 1.00 47.74  ? 310 ASP A CB     1 
ATOM   1029 C  CG     . ASP A 1 167 ? 214.619 165.486 178.058 1.00 55.44  ? 310 ASP A CG     1 
ATOM   1030 O  OD1    . ASP A 1 167 ? 215.867 165.524 178.020 1.00 49.68  ? 310 ASP A OD1    1 
ATOM   1031 O  OD2    . ASP A 1 167 ? 213.938 164.771 177.294 1.00 54.31  ? 310 ASP A OD2    1 
ATOM   1032 N  N      . ILE A 1 168 ? 214.067 167.951 182.255 1.00 48.31  ? 311 ILE A N      1 
ATOM   1033 C  CA     . ILE A 1 168 ? 213.557 169.079 183.020 1.00 45.54  ? 311 ILE A CA     1 
ATOM   1034 C  C      . ILE A 1 168 ? 214.586 169.612 184.009 1.00 47.36  ? 311 ILE A C      1 
ATOM   1035 O  O      . ILE A 1 168 ? 214.239 170.387 184.900 1.00 49.72  ? 311 ILE A O      1 
ATOM   1036 C  CB     . ILE A 1 168 ? 212.244 168.718 183.743 1.00 42.77  ? 311 ILE A CB     1 
ATOM   1037 C  CG1    . ILE A 1 168 ? 212.535 167.892 184.997 1.00 43.22  ? 311 ILE A CG1    1 
ATOM   1038 C  CG2    . ILE A 1 168 ? 211.312 167.966 182.809 1.00 45.84  ? 311 ILE A CG2    1 
ATOM   1039 C  CD1    . ILE A 1 168 ? 211.346 167.741 185.918 1.00 46.14  ? 311 ILE A CD1    1 
ATOM   1040 N  N      . LEU A 1 169 ? 215.846 169.212 183.871 1.00 46.53  ? 312 LEU A N      1 
ATOM   1041 C  CA     . LEU A 1 169 ? 216.896 169.685 184.760 1.00 45.84  ? 312 LEU A CA     1 
ATOM   1042 C  C      . LEU A 1 169 ? 217.325 171.099 184.387 1.00 47.77  ? 312 LEU A C      1 
ATOM   1043 O  O      . LEU A 1 169 ? 217.256 171.508 183.225 1.00 48.38  ? 312 LEU A O      1 
ATOM   1044 C  CB     . LEU A 1 169 ? 218.102 168.747 184.714 1.00 46.25  ? 312 LEU A CB     1 
ATOM   1045 C  CG     . LEU A 1 169 ? 217.941 167.392 185.406 1.00 42.92  ? 312 LEU A CG     1 
ATOM   1046 C  CD1    . LEU A 1 169 ? 219.097 166.469 185.057 1.00 34.79  ? 312 LEU A CD1    1 
ATOM   1047 C  CD2    . LEU A 1 169 ? 217.828 167.570 186.911 1.00 41.17  ? 312 LEU A CD2    1 
ATOM   1048 N  N      . ASP A 1 170 ? 217.770 171.845 185.390 1.00 47.16  ? 313 ASP A N      1 
ATOM   1049 C  CA     . ASP A 1 170 ? 218.246 173.203 185.157 1.00 48.00  ? 313 ASP A CA     1 
ATOM   1050 C  C      . ASP A 1 170 ? 219.528 173.167 184.331 1.00 50.75  ? 313 ASP A C      1 
ATOM   1051 O  O      . ASP A 1 170 ? 220.430 172.376 184.630 1.00 49.86  ? 313 ASP A O      1 
ATOM   1052 C  CB     . ASP A 1 170 ? 218.486 173.918 186.484 1.00 52.23  ? 313 ASP A CB     1 
ATOM   1053 C  CG     . ASP A 1 170 ? 219.107 175.289 186.303 1.00 59.54  ? 313 ASP A CG     1 
ATOM   1054 O  OD1    . ASP A 1 170 ? 218.428 176.186 185.760 1.00 60.89  ? 313 ASP A OD1    1 
ATOM   1055 O  OD2    . ASP A 1 170 ? 220.274 175.470 186.707 1.00 60.80  ? 313 ASP A OD2    1 
ATOM   1056 N  N      . PRO A 1 171 ? 219.651 174.002 183.295 1.00 50.33  ? 314 PRO A N      1 
ATOM   1057 C  CA     . PRO A 1 171 ? 220.847 173.945 182.438 1.00 50.23  ? 314 PRO A CA     1 
ATOM   1058 C  C      . PRO A 1 171 ? 222.145 174.267 183.161 1.00 51.98  ? 314 PRO A C      1 
ATOM   1059 O  O      . PRO A 1 171 ? 223.212 173.876 182.671 1.00 49.96  ? 314 PRO A O      1 
ATOM   1060 C  CB     . PRO A 1 171 ? 220.551 174.986 181.348 1.00 48.75  ? 314 PRO A CB     1 
ATOM   1061 C  CG     . PRO A 1 171 ? 219.071 175.206 181.404 1.00 50.79  ? 314 PRO A CG     1 
ATOM   1062 C  CD     . PRO A 1 171 ? 218.684 175.009 182.833 1.00 49.82  ? 314 PRO A CD     1 
ATOM   1063 N  N      . ALA A 1 172 ? 222.096 174.964 184.297 1.00 52.32  ? 315 ALA A N      1 
ATOM   1064 C  CA     . ALA A 1 172 ? 223.319 175.298 185.016 1.00 50.16  ? 315 ALA A CA     1 
ATOM   1065 C  C      . ALA A 1 172 ? 224.018 174.068 185.579 1.00 50.02  ? 315 ALA A C      1 
ATOM   1066 O  O      . ALA A 1 172 ? 225.232 174.109 185.803 1.00 46.79  ? 315 ALA A O      1 
ATOM   1067 C  CB     . ALA A 1 172 ? 223.015 176.285 186.144 1.00 48.15  ? 315 ALA A CB     1 
ATOM   1068 N  N      . LEU A 1 173 ? 223.283 172.980 185.814 1.00 48.93  ? 316 LEU A N      1 
ATOM   1069 C  CA     . LEU A 1 173 ? 223.875 171.771 186.372 1.00 42.53  ? 316 LEU A CA     1 
ATOM   1070 C  C      . LEU A 1 173 ? 224.702 170.990 185.360 1.00 43.58  ? 316 LEU A C      1 
ATOM   1071 O  O      . LEU A 1 173 ? 225.544 170.182 185.764 1.00 40.53  ? 316 LEU A O      1 
ATOM   1072 C  CB     . LEU A 1 173 ? 222.781 170.863 186.938 1.00 42.93  ? 316 LEU A CB     1 
ATOM   1073 C  CG     . LEU A 1 173 ? 222.243 171.196 188.330 1.00 45.62  ? 316 LEU A CG     1 
ATOM   1074 C  CD1    . LEU A 1 173 ? 220.913 170.499 188.565 1.00 40.21  ? 316 LEU A CD1    1 
ATOM   1075 C  CD2    . LEU A 1 173 ? 223.248 170.811 189.401 1.00 38.08  ? 316 LEU A CD2    1 
ATOM   1076 N  N      . LEU A 1 174 ? 224.486 171.207 184.063 1.00 46.65  ? 317 LEU A N      1 
ATOM   1077 C  CA     . LEU A 1 174 ? 225.136 170.422 183.022 1.00 43.50  ? 317 LEU A CA     1 
ATOM   1078 C  C      . LEU A 1 174 ? 226.323 171.136 182.388 1.00 46.19  ? 317 LEU A C      1 
ATOM   1079 O  O      . LEU A 1 174 ? 226.861 170.650 181.387 1.00 49.01  ? 317 LEU A O      1 
ATOM   1080 C  CB     . LEU A 1 174 ? 224.119 170.037 181.945 1.00 44.31  ? 317 LEU A CB     1 
ATOM   1081 C  CG     . LEU A 1 174 ? 222.818 169.412 182.451 1.00 44.84  ? 317 LEU A CG     1 
ATOM   1082 C  CD1    . LEU A 1 174 ? 221.758 169.423 181.364 1.00 45.71  ? 317 LEU A CD1    1 
ATOM   1083 C  CD2    . LEU A 1 174 ? 223.059 167.999 182.955 1.00 40.81  ? 317 LEU A CD2    1 
ATOM   1084 N  N      . ARG A 1 175 ? 226.748 172.270 182.941 1.00 49.83  ? 318 ARG A N      1 
ATOM   1085 C  CA     . ARG A 1 175 ? 227.874 173.004 182.391 1.00 50.16  ? 318 ARG A CA     1 
ATOM   1086 C  C      . ARG A 1 175 ? 229.176 172.263 182.676 1.00 53.30  ? 318 ARG A C      1 
ATOM   1087 O  O      . ARG A 1 175 ? 229.242 171.414 183.567 1.00 51.55  ? 318 ARG A O      1 
ATOM   1088 C  CB     . ARG A 1 175 ? 227.918 174.417 182.967 1.00 50.59  ? 318 ARG A CB     1 
ATOM   1089 C  CG     . ARG A 1 175 ? 226.571 175.117 182.987 1.00 56.48  ? 318 ARG A CG     1 
ATOM   1090 C  CD     . ARG A 1 175 ? 226.685 176.550 182.495 1.00 58.98  ? 318 ARG A CD     1 
ATOM   1091 N  NE     . ARG A 1 175 ? 225.408 177.064 182.018 1.00 68.14  ? 318 ARG A NE     1 
ATOM   1092 C  CZ     . ARG A 1 175 ? 224.679 177.971 182.654 1.00 69.20  ? 318 ARG A CZ     1 
ATOM   1093 N  NH1    . ARG A 1 175 ? 225.077 178.496 183.802 1.00 68.71  ? 318 ARG A NH1    1 
ATOM   1094 N  NH2    . ARG A 1 175 ? 223.523 178.361 182.126 1.00 66.02  ? 318 ARG A NH2    1 
ATOM   1095 N  N      . PRO A 1 176 ? 230.233 172.561 181.922 1.00 57.35  ? 319 PRO A N      1 
ATOM   1096 C  CA     . PRO A 1 176 ? 231.514 171.884 182.155 1.00 55.95  ? 319 PRO A CA     1 
ATOM   1097 C  C      . PRO A 1 176 ? 232.009 172.115 183.575 1.00 54.05  ? 319 PRO A C      1 
ATOM   1098 O  O      . PRO A 1 176 ? 231.839 173.193 184.146 1.00 54.51  ? 319 PRO A O      1 
ATOM   1099 C  CB     . PRO A 1 176 ? 232.446 172.524 181.120 1.00 51.88  ? 319 PRO A CB     1 
ATOM   1100 C  CG     . PRO A 1 176 ? 231.533 173.036 180.055 1.00 53.90  ? 319 PRO A CG     1 
ATOM   1101 C  CD     . PRO A 1 176 ? 230.290 173.476 180.770 1.00 57.78  ? 319 PRO A CD     1 
ATOM   1102 N  N      . GLY A 1 177 ? 232.632 171.083 184.140 1.00 52.11  ? 320 GLY A N      1 
ATOM   1103 C  CA     . GLY A 1 177 ? 233.080 171.115 185.515 1.00 45.54  ? 320 GLY A CA     1 
ATOM   1104 C  C      . GLY A 1 177 ? 232.035 170.728 186.537 1.00 48.12  ? 320 GLY A C      1 
ATOM   1105 O  O      . GLY A 1 177 ? 232.327 170.765 187.740 1.00 48.75  ? 320 GLY A O      1 
ATOM   1106 N  N      . ARG A 1 178 ? 230.830 170.361 186.105 1.00 46.37  ? 321 ARG A N      1 
ATOM   1107 C  CA     . ARG A 1 178 ? 229.778 169.954 187.031 1.00 43.43  ? 321 ARG A CA     1 
ATOM   1108 C  C      . ARG A 1 178 ? 228.783 169.091 186.267 1.00 43.35  ? 321 ARG A C      1 
ATOM   1109 O  O      . ARG A 1 178 ? 228.026 169.610 185.441 1.00 50.96  ? 321 ARG A O      1 
ATOM   1110 C  CB     . ARG A 1 178 ? 229.096 171.172 187.644 1.00 45.11  ? 321 ARG A CB     1 
ATOM   1111 C  CG     . ARG A 1 178 ? 228.783 172.272 186.643 1.00 46.63  ? 321 ARG A CG     1 
ATOM   1112 C  CD     . ARG A 1 178 ? 227.908 173.351 187.256 1.00 47.39  ? 321 ARG A CD     1 
ATOM   1113 N  NE     . ARG A 1 178 ? 228.675 174.282 188.075 1.00 49.29  ? 321 ARG A NE     1 
ATOM   1114 C  CZ     . ARG A 1 178 ? 228.398 175.573 188.199 1.00 49.08  ? 321 ARG A CZ     1 
ATOM   1115 N  NH1    . ARG A 1 178 ? 227.379 176.125 187.560 1.00 43.00  ? 321 ARG A NH1    1 
ATOM   1116 N  NH2    . ARG A 1 178 ? 229.162 176.329 188.982 1.00 48.89  ? 321 ARG A NH2    1 
ATOM   1117 N  N      . PHE A 1 179 ? 228.784 167.786 186.541 1.00 36.32  ? 322 PHE A N      1 
ATOM   1118 C  CA     . PHE A 1 179 ? 227.825 166.848 185.956 1.00 35.53  ? 322 PHE A CA     1 
ATOM   1119 C  C      . PHE A 1 179 ? 227.894 166.881 184.425 1.00 39.11  ? 322 PHE A C      1 
ATOM   1120 O  O      . PHE A 1 179 ? 226.945 167.249 183.731 1.00 43.00  ? 322 PHE A O      1 
ATOM   1121 C  CB     . PHE A 1 179 ? 226.405 167.146 186.451 1.00 32.33  ? 322 PHE A CB     1 
ATOM   1122 C  CG     . PHE A 1 179 ? 226.136 166.673 187.851 1.00 31.51  ? 322 PHE A CG     1 
ATOM   1123 C  CD1    . PHE A 1 179 ? 226.426 165.372 188.225 1.00 28.19  ? 322 PHE A CD1    1 
ATOM   1124 C  CD2    . PHE A 1 179 ? 225.592 167.530 188.793 1.00 28.46  ? 322 PHE A CD2    1 
ATOM   1125 C  CE1    . PHE A 1 179 ? 226.180 164.935 189.511 1.00 25.03  ? 322 PHE A CE1    1 
ATOM   1126 C  CE2    . PHE A 1 179 ? 225.344 167.098 190.081 1.00 27.06  ? 322 PHE A CE2    1 
ATOM   1127 C  CZ     . PHE A 1 179 ? 225.639 165.800 190.440 1.00 26.00  ? 322 PHE A CZ     1 
ATOM   1128 N  N      . ASP A 1 180 ? 229.058 166.479 183.915 1.00 39.08  ? 323 ASP A N      1 
ATOM   1129 C  CA     . ASP A 1 180 ? 229.319 166.465 182.480 1.00 39.01  ? 323 ASP A CA     1 
ATOM   1130 C  C      . ASP A 1 180 ? 229.578 165.053 181.963 1.00 39.34  ? 323 ASP A C      1 
ATOM   1131 O  O      . ASP A 1 180 ? 230.375 164.858 181.043 1.00 44.46  ? 323 ASP A O      1 
ATOM   1132 C  CB     . ASP A 1 180 ? 230.489 167.387 182.137 1.00 46.66  ? 323 ASP A CB     1 
ATOM   1133 C  CG     . ASP A 1 180 ? 231.781 166.962 182.803 1.00 53.85  ? 323 ASP A CG     1 
ATOM   1134 O  OD1    . ASP A 1 180 ? 231.733 166.103 183.707 1.00 52.96  ? 323 ASP A OD1    1 
ATOM   1135 O  OD2    . ASP A 1 180 ? 232.847 167.489 182.421 1.00 54.36  ? 323 ASP A OD2    1 
ATOM   1136 N  N      . LYS A 1 181 ? 228.912 164.058 182.545 1.00 36.12  ? 324 LYS A N      1 
ATOM   1137 C  CA     . LYS A 1 181 ? 229.012 162.682 182.074 1.00 31.18  ? 324 LYS A CA     1 
ATOM   1138 C  C      . LYS A 1 181 ? 227.702 161.968 182.369 1.00 29.18  ? 324 LYS A C      1 
ATOM   1139 O  O      . LYS A 1 181 ? 227.172 162.080 183.478 1.00 32.32  ? 324 LYS A O      1 
ATOM   1140 C  CB     . LYS A 1 181 ? 230.183 161.949 182.735 1.00 27.81  ? 324 LYS A CB     1 
ATOM   1141 C  CG     . LYS A 1 181 ? 230.459 160.581 182.137 1.00 29.61  ? 324 LYS A CG     1 
ATOM   1142 C  CD     . LYS A 1 181 ? 231.545 159.848 182.899 1.00 31.37  ? 324 LYS A CD     1 
ATOM   1143 C  CE     . LYS A 1 181 ? 231.708 158.428 182.385 1.00 38.35  ? 324 LYS A CE     1 
ATOM   1144 N  NZ     . LYS A 1 181 ? 231.485 158.346 180.916 1.00 37.42  ? 324 LYS A NZ     1 
ATOM   1145 N  N      . LYS A 1 182 ? 227.186 161.238 181.382 1.00 27.50  ? 325 LYS A N      1 
ATOM   1146 C  CA     . LYS A 1 182 ? 225.893 160.578 181.489 1.00 26.64  ? 325 LYS A CA     1 
ATOM   1147 C  C      . LYS A 1 182 ? 226.020 159.105 181.134 1.00 23.45  ? 325 LYS A C      1 
ATOM   1148 O  O      . LYS A 1 182 ? 226.782 158.735 180.237 1.00 24.82  ? 325 LYS A O      1 
ATOM   1149 C  CB     . LYS A 1 182 ? 224.855 161.243 180.576 1.00 27.22  ? 325 LYS A CB     1 
ATOM   1150 C  CG     . LYS A 1 182 ? 224.653 162.725 180.839 1.00 32.67  ? 325 LYS A CG     1 
ATOM   1151 C  CD     . LYS A 1 182 ? 224.495 163.496 179.538 1.00 45.58  ? 325 LYS A CD     1 
ATOM   1152 C  CE     . LYS A 1 182 ? 223.798 164.828 179.763 1.00 49.46  ? 325 LYS A CE     1 
ATOM   1153 N  NZ     . LYS A 1 182 ? 224.741 165.868 180.257 1.00 49.67  ? 325 LYS A NZ     1 
ATOM   1154 N  N      . ILE A 1 183 ? 225.263 158.270 181.843 1.00 21.36  ? 326 ILE A N      1 
ATOM   1155 C  CA     . ILE A 1 183 ? 225.199 156.835 181.591 1.00 22.68  ? 326 ILE A CA     1 
ATOM   1156 C  C      . ILE A 1 183 ? 223.735 156.421 181.541 1.00 22.40  ? 326 ILE A C      1 
ATOM   1157 O  O      . ILE A 1 183 ? 222.920 156.893 182.342 1.00 23.33  ? 326 ILE A O      1 
ATOM   1158 C  CB     . ILE A 1 183 ? 225.960 156.029 182.665 1.00 22.91  ? 326 ILE A CB     1 
ATOM   1159 C  CG1    . ILE A 1 183 ? 227.411 156.504 182.757 1.00 25.63  ? 326 ILE A CG1    1 
ATOM   1160 C  CG2    . ILE A 1 183 ? 225.903 154.543 182.355 1.00 24.85  ? 326 ILE A CG2    1 
ATOM   1161 C  CD1    . ILE A 1 183 ? 228.214 155.810 183.834 1.00 26.58  ? 326 ILE A CD1    1 
ATOM   1162 N  N      . VAL A 1 184 ? 223.403 155.539 180.602 1.00 23.03  ? 327 VAL A N      1 
ATOM   1163 C  CA     . VAL A 1 184 ? 222.028 155.121 180.352 1.00 24.96  ? 327 VAL A CA     1 
ATOM   1164 C  C      . VAL A 1 184 ? 221.832 153.704 180.871 1.00 23.96  ? 327 VAL A C      1 
ATOM   1165 O  O      . VAL A 1 184 ? 222.668 152.823 180.637 1.00 27.92  ? 327 VAL A O      1 
ATOM   1166 C  CB     . VAL A 1 184 ? 221.679 155.206 178.854 1.00 25.52  ? 327 VAL A CB     1 
ATOM   1167 C  CG1    . VAL A 1 184 ? 220.251 154.744 178.615 1.00 26.27  ? 327 VAL A CG1    1 
ATOM   1168 C  CG2    . VAL A 1 184 ? 221.879 156.622 178.342 1.00 21.53  ? 327 VAL A CG2    1 
ATOM   1169 N  N      . VAL A 1 185 ? 220.724 153.488 181.576 1.00 21.62  ? 328 VAL A N      1 
ATOM   1170 C  CA     . VAL A 1 185 ? 220.345 152.179 182.098 1.00 24.63  ? 328 VAL A CA     1 
ATOM   1171 C  C      . VAL A 1 185 ? 219.079 151.736 181.379 1.00 27.20  ? 328 VAL A C      1 
ATOM   1172 O  O      . VAL A 1 185 ? 218.091 152.479 181.339 1.00 30.55  ? 328 VAL A O      1 
ATOM   1173 C  CB     . VAL A 1 185 ? 220.131 152.213 183.622 1.00 26.58  ? 328 VAL A CB     1 
ATOM   1174 C  CG1    . VAL A 1 185 ? 220.129 150.804 184.190 1.00 22.14  ? 328 VAL A CG1    1 
ATOM   1175 C  CG2    . VAL A 1 185 ? 221.204 153.059 184.287 1.00 21.32  ? 328 VAL A CG2    1 
ATOM   1176 N  N      . ASP A 1 186 ? 219.107 150.534 180.818 1.00 29.28  ? 329 ASP A N      1 
ATOM   1177 C  CA     . ASP A 1 186 ? 218.070 150.058 179.918 1.00 29.60  ? 329 ASP A CA     1 
ATOM   1178 C  C      . ASP A 1 186 ? 217.269 148.914 180.527 1.00 29.49  ? 329 ASP A C      1 
ATOM   1179 O  O      . ASP A 1 186 ? 217.748 148.206 181.419 1.00 34.35  ? 329 ASP A O      1 
ATOM   1180 C  CB     . ASP A 1 186 ? 218.689 149.590 178.596 1.00 33.20  ? 329 ASP A CB     1 
ATOM   1181 C  CG     . ASP A 1 186 ? 219.103 150.743 177.711 1.00 42.99  ? 329 ASP A CG     1 
ATOM   1182 O  OD1    . ASP A 1 186 ? 218.306 151.692 177.560 1.00 45.76  ? 329 ASP A OD1    1 
ATOM   1183 O  OD2    . ASP A 1 186 ? 220.227 150.705 177.168 1.00 48.13  ? 329 ASP A OD2    1 
ATOM   1184 N  N      . PRO A 1 187 ? 216.032 148.709 180.068 1.00 29.82  ? 330 PRO A N      1 
ATOM   1185 C  CA     . PRO A 1 187 ? 215.265 147.556 180.532 1.00 27.41  ? 330 PRO A CA     1 
ATOM   1186 C  C      . PRO A 1 187 ? 215.894 146.262 180.050 1.00 26.30  ? 330 PRO A C      1 
ATOM   1187 O  O      . PRO A 1 187 ? 216.559 146.230 179.000 1.00 29.51  ? 330 PRO A O      1 
ATOM   1188 C  CB     . PRO A 1 187 ? 213.877 147.775 179.902 1.00 23.39  ? 330 PRO A CB     1 
ATOM   1189 C  CG     . PRO A 1 187 ? 213.838 149.220 179.527 1.00 22.97  ? 330 PRO A CG     1 
ATOM   1190 C  CD     . PRO A 1 187 ? 215.244 149.586 179.187 1.00 29.89  ? 330 PRO A CD     1 
ATOM   1191 N  N      . PRO A 1 188 ? 215.711 145.167 180.781 1.00 26.44  ? 331 PRO A N      1 
ATOM   1192 C  CA     . PRO A 1 188 ? 216.353 143.906 180.402 1.00 26.08  ? 331 PRO A CA     1 
ATOM   1193 C  C      . PRO A 1 188 ? 215.653 143.219 179.240 1.00 27.43  ? 331 PRO A C      1 
ATOM   1194 O  O      . PRO A 1 188 ? 214.475 143.451 178.958 1.00 29.18  ? 331 PRO A O      1 
ATOM   1195 C  CB     . PRO A 1 188 ? 216.247 143.063 181.678 1.00 22.71  ? 331 PRO A CB     1 
ATOM   1196 C  CG     . PRO A 1 188 ? 215.032 143.582 182.365 1.00 20.87  ? 331 PRO A CG     1 
ATOM   1197 C  CD     . PRO A 1 188 ? 214.907 145.040 182.009 1.00 22.17  ? 331 PRO A CD     1 
ATOM   1198 N  N      . ASP A 1 189 ? 216.408 142.361 178.563 1.00 31.56  ? 332 ASP A N      1 
ATOM   1199 C  CA     . ASP A 1 189 ? 215.896 141.520 177.496 1.00 31.77  ? 332 ASP A CA     1 
ATOM   1200 C  C      . ASP A 1 189 ? 215.685 140.102 178.026 1.00 31.21  ? 332 ASP A C      1 
ATOM   1201 O  O      . ASP A 1 189 ? 215.784 139.844 179.229 1.00 31.80  ? 332 ASP A O      1 
ATOM   1202 C  CB     . ASP A 1 189 ? 216.843 141.556 176.294 1.00 34.08  ? 332 ASP A CB     1 
ATOM   1203 C  CG     . ASP A 1 189 ? 218.137 140.809 176.547 1.00 41.32  ? 332 ASP A CG     1 
ATOM   1204 O  OD1    . ASP A 1 189 ? 218.720 140.978 177.638 1.00 42.20  ? 332 ASP A OD1    1 
ATOM   1205 O  OD2    . ASP A 1 189 ? 218.571 140.053 175.654 1.00 46.82  ? 332 ASP A OD2    1 
ATOM   1206 N  N      . MET A 1 190 ? 215.390 139.166 177.120 1.00 32.03  ? 333 MET A N      1 
ATOM   1207 C  CA     . MET A 1 190 ? 215.077 137.802 177.538 1.00 33.28  ? 333 MET A CA     1 
ATOM   1208 C  C      . MET A 1 190 ? 216.206 137.204 178.369 1.00 32.43  ? 333 MET A C      1 
ATOM   1209 O  O      . MET A 1 190 ? 215.973 136.658 179.453 1.00 30.33  ? 333 MET A O      1 
ATOM   1210 C  CB     . MET A 1 190 ? 214.791 136.931 176.315 1.00 38.47  ? 333 MET A CB     1 
ATOM   1211 C  CG     . MET A 1 190 ? 213.817 135.792 176.577 1.00 42.24  ? 333 MET A CG     1 
ATOM   1212 S  SD     . MET A 1 190 ? 214.559 134.423 177.486 1.00 58.87  ? 333 MET A SD     1 
ATOM   1213 C  CE     . MET A 1 190 ? 215.762 133.836 176.297 1.00 46.63  ? 333 MET A CE     1 
ATOM   1214 N  N      . LEU A 1 191 ? 217.443 137.298 177.876 1.00 36.14  ? 334 LEU A N      1 
ATOM   1215 C  CA     . LEU A 1 191 ? 218.571 136.748 178.620 1.00 34.92  ? 334 LEU A CA     1 
ATOM   1216 C  C      . LEU A 1 191 ? 218.815 137.507 179.918 1.00 34.28  ? 334 LEU A C      1 
ATOM   1217 O  O      . LEU A 1 191 ? 219.226 136.905 180.916 1.00 32.12  ? 334 LEU A O      1 
ATOM   1218 C  CB     . LEU A 1 191 ? 219.829 136.759 177.753 1.00 42.32  ? 334 LEU A CB     1 
ATOM   1219 C  CG     . LEU A 1 191 ? 220.167 135.457 177.021 1.00 47.72  ? 334 LEU A CG     1 
ATOM   1220 C  CD1    . LEU A 1 191 ? 220.411 134.329 178.010 1.00 51.65  ? 334 LEU A CD1    1 
ATOM   1221 C  CD2    . LEU A 1 191 ? 219.064 135.085 176.044 1.00 45.57  ? 334 LEU A CD2    1 
ATOM   1222 N  N      . GLY A 1 192 ? 218.575 138.820 179.926 1.00 32.47  ? 335 GLY A N      1 
ATOM   1223 C  CA     . GLY A 1 192 ? 218.727 139.582 181.152 1.00 25.27  ? 335 GLY A CA     1 
ATOM   1224 C  C      . GLY A 1 192 ? 217.695 139.247 182.205 1.00 24.92  ? 335 GLY A C      1 
ATOM   1225 O  O      . GLY A 1 192 ? 218.013 139.224 183.398 1.00 27.76  ? 335 GLY A O      1 
ATOM   1226 N  N      . ARG A 1 193 ? 216.455 138.978 181.790 1.00 25.03  ? 336 ARG A N      1 
ATOM   1227 C  CA     . ARG A 1 193 ? 215.410 138.631 182.747 1.00 23.68  ? 336 ARG A CA     1 
ATOM   1228 C  C      . ARG A 1 193 ? 215.708 137.305 183.437 1.00 24.55  ? 336 ARG A C      1 
ATOM   1229 O  O      . ARG A 1 193 ? 215.466 137.158 184.641 1.00 22.96  ? 336 ARG A O      1 
ATOM   1230 C  CB     . ARG A 1 193 ? 214.053 138.578 182.046 1.00 21.75  ? 336 ARG A CB     1 
ATOM   1231 C  CG     . ARG A 1 193 ? 213.583 139.917 181.504 1.00 24.66  ? 336 ARG A CG     1 
ATOM   1232 C  CD     . ARG A 1 193 ? 212.105 139.884 181.156 1.00 21.55  ? 336 ARG A CD     1 
ATOM   1233 N  NE     . ARG A 1 193 ? 211.803 138.873 180.149 1.00 27.85  ? 336 ARG A NE     1 
ATOM   1234 C  CZ     . ARG A 1 193 ? 211.660 139.123 178.855 1.00 28.84  ? 336 ARG A CZ     1 
ATOM   1235 N  NH1    . ARG A 1 193 ? 211.786 140.347 178.370 1.00 27.43  ? 336 ARG A NH1    1 
ATOM   1236 N  NH2    . ARG A 1 193 ? 211.385 138.120 178.027 1.00 29.65  ? 336 ARG A NH2    1 
ATOM   1237 N  N      . LYS A 1 194 ? 216.228 136.328 182.692 1.00 25.14  ? 337 LYS A N      1 
ATOM   1238 C  CA     . LYS A 1 194 ? 216.537 135.033 183.287 1.00 27.22  ? 337 LYS A CA     1 
ATOM   1239 C  C      . LYS A 1 194 ? 217.646 135.141 184.325 1.00 30.95  ? 337 LYS A C      1 
ATOM   1240 O  O      . LYS A 1 194 ? 217.621 134.424 185.331 1.00 33.29  ? 337 LYS A O      1 
ATOM   1241 C  CB     . LYS A 1 194 ? 216.922 134.034 182.197 1.00 31.42  ? 337 LYS A CB     1 
ATOM   1242 C  CG     . LYS A 1 194 ? 217.566 132.760 182.716 1.00 37.27  ? 337 LYS A CG     1 
ATOM   1243 C  CD     . LYS A 1 194 ? 217.621 131.696 181.634 1.00 44.78  ? 337 LYS A CD     1 
ATOM   1244 C  CE     . LYS A 1 194 ? 218.505 130.531 182.044 1.00 53.85  ? 337 LYS A CE     1 
ATOM   1245 N  NZ     . LYS A 1 194 ? 219.764 130.489 181.253 1.00 58.51  ? 337 LYS A NZ     1 
ATOM   1246 N  N      . LYS A 1 195 ? 218.621 136.024 184.103 1.00 28.44  ? 338 LYS A N      1 
ATOM   1247 C  CA     . LYS A 1 195 ? 219.696 136.197 185.073 1.00 28.16  ? 338 LYS A CA     1 
ATOM   1248 C  C      . LYS A 1 195 ? 219.194 136.826 186.366 1.00 27.99  ? 338 LYS A C      1 
ATOM   1249 O  O      . LYS A 1 195 ? 219.653 136.455 187.452 1.00 29.32  ? 338 LYS A O      1 
ATOM   1250 C  CB     . LYS A 1 195 ? 220.815 137.046 184.469 1.00 31.23  ? 338 LYS A CB     1 
ATOM   1251 C  CG     . LYS A 1 195 ? 221.892 137.448 185.460 1.00 34.22  ? 338 LYS A CG     1 
ATOM   1252 C  CD     . LYS A 1 195 ? 222.856 136.303 185.721 1.00 38.11  ? 338 LYS A CD     1 
ATOM   1253 C  CE     . LYS A 1 195 ? 223.863 136.667 186.799 1.00 46.80  ? 338 LYS A CE     1 
ATOM   1254 N  NZ     . LYS A 1 195 ? 224.561 137.945 186.491 1.00 49.30  ? 338 LYS A NZ     1 
ATOM   1255 N  N      . ILE A 1 196 ? 218.261 137.775 186.274 1.00 26.95  ? 339 ILE A N      1 
ATOM   1256 C  CA     . ILE A 1 196 ? 217.725 138.404 187.476 1.00 24.90  ? 339 ILE A CA     1 
ATOM   1257 C  C      . ILE A 1 196 ? 216.920 137.410 188.306 1.00 26.32  ? 339 ILE A C      1 
ATOM   1258 O  O      . ILE A 1 196 ? 216.950 137.462 189.540 1.00 28.04  ? 339 ILE A O      1 
ATOM   1259 C  CB     . ILE A 1 196 ? 216.882 139.635 187.103 1.00 25.27  ? 339 ILE A CB     1 
ATOM   1260 C  CG1    . ILE A 1 196 ? 217.777 140.745 186.548 1.00 22.58  ? 339 ILE A CG1    1 
ATOM   1261 C  CG2    . ILE A 1 196 ? 216.101 140.132 188.310 1.00 22.09  ? 339 ILE A CG2    1 
ATOM   1262 C  CD1    . ILE A 1 196 ? 217.032 141.798 185.759 1.00 18.21  ? 339 ILE A CD1    1 
ATOM   1263 N  N      . LEU A 1 197 ? 216.191 136.499 187.657 1.00 25.88  ? 340 LEU A N      1 
ATOM   1264 C  CA     . LEU A 1 197 ? 215.419 135.505 188.396 1.00 25.62  ? 340 LEU A CA     1 
ATOM   1265 C  C      . LEU A 1 197 ? 216.319 134.568 189.191 1.00 28.86  ? 340 LEU A C      1 
ATOM   1266 O  O      . LEU A 1 197 ? 215.970 134.178 190.311 1.00 30.47  ? 340 LEU A O      1 
ATOM   1267 C  CB     . LEU A 1 197 ? 214.535 134.705 187.440 1.00 23.46  ? 340 LEU A CB     1 
ATOM   1268 C  CG     . LEU A 1 197 ? 213.306 135.422 186.877 1.00 21.66  ? 340 LEU A CG     1 
ATOM   1269 C  CD1    . LEU A 1 197 ? 212.744 134.666 185.684 1.00 20.18  ? 340 LEU A CD1    1 
ATOM   1270 C  CD2    . LEU A 1 197 ? 212.245 135.600 187.951 1.00 19.87  ? 340 LEU A CD2    1 
ATOM   1271 N  N      . GLU A 1 198 ? 217.469 134.189 188.632 1.00 30.44  ? 341 GLU A N      1 
ATOM   1272 C  CA     . GLU A 1 198 ? 218.392 133.308 189.337 1.00 31.56  ? 341 GLU A CA     1 
ATOM   1273 C  C      . GLU A 1 198 ? 219.013 133.982 190.554 1.00 32.20  ? 341 GLU A C      1 
ATOM   1274 O  O      . GLU A 1 198 ? 219.326 133.304 191.539 1.00 36.85  ? 341 GLU A O      1 
ATOM   1275 C  CB     . GLU A 1 198 ? 219.493 132.834 188.388 1.00 31.33  ? 341 GLU A CB     1 
ATOM   1276 C  CG     . GLU A 1 198 ? 219.076 131.700 187.470 1.00 38.69  ? 341 GLU A CG     1 
ATOM   1277 C  CD     . GLU A 1 198 ? 219.870 131.675 186.180 1.00 54.01  ? 341 GLU A CD     1 
ATOM   1278 O  OE1    . GLU A 1 198 ? 220.770 132.525 186.017 1.00 54.53  ? 341 GLU A OE1    1 
ATOM   1279 O  OE2    . GLU A 1 198 ? 219.593 130.806 185.326 1.00 62.78  ? 341 GLU A OE2    1 
ATOM   1280 N  N      . ILE A 1 199 ? 219.202 135.301 190.505 1.00 31.27  ? 342 ILE A N      1 
ATOM   1281 C  CA     . ILE A 1 199 ? 219.810 136.007 191.628 1.00 29.39  ? 342 ILE A CA     1 
ATOM   1282 C  C      . ILE A 1 199 ? 218.898 135.988 192.847 1.00 30.82  ? 342 ILE A C      1 
ATOM   1283 O  O      . ILE A 1 199 ? 219.374 135.878 193.984 1.00 34.74  ? 342 ILE A O      1 
ATOM   1284 C  CB     . ILE A 1 199 ? 220.170 137.447 191.221 1.00 32.08  ? 342 ILE A CB     1 
ATOM   1285 C  CG1    . ILE A 1 199 ? 221.519 137.479 190.500 1.00 33.30  ? 342 ILE A CG1    1 
ATOM   1286 C  CG2    . ILE A 1 199 ? 220.187 138.359 192.439 1.00 27.29  ? 342 ILE A CG2    1 
ATOM   1287 C  CD1    . ILE A 1 199 ? 221.730 138.715 189.654 1.00 24.80  ? 342 ILE A CD1    1 
ATOM   1288 N  N      . HIS A 1 200 ? 217.587 136.096 192.645 1.00 30.36  ? 343 HIS A N      1 
ATOM   1289 C  CA     . HIS A 1 200 ? 216.637 136.205 193.743 1.00 30.60  ? 343 HIS A CA     1 
ATOM   1290 C  C      . HIS A 1 200 ? 216.066 134.863 194.182 1.00 32.67  ? 343 HIS A C      1 
ATOM   1291 O  O      . HIS A 1 200 ? 215.222 134.831 195.082 1.00 32.65  ? 343 HIS A O      1 
ATOM   1292 C  CB     . HIS A 1 200 ? 215.495 137.152 193.359 1.00 26.10  ? 343 HIS A CB     1 
ATOM   1293 C  CG     . HIS A 1 200 ? 215.902 138.592 193.297 1.00 28.75  ? 343 HIS A CG     1 
ATOM   1294 N  ND1    . HIS A 1 200 ? 216.145 139.346 194.424 1.00 26.94  ? 343 HIS A ND1    1 
ATOM   1295 C  CD2    . HIS A 1 200 ? 216.113 139.413 192.242 1.00 28.21  ? 343 HIS A CD2    1 
ATOM   1296 C  CE1    . HIS A 1 200 ? 216.488 140.571 194.066 1.00 26.83  ? 343 HIS A CE1    1 
ATOM   1297 N  NE2    . HIS A 1 200 ? 216.476 140.638 192.747 1.00 27.83  ? 343 HIS A NE2    1 
ATOM   1298 N  N      . THR A 1 201 ? 216.500 133.758 193.575 1.00 33.74  ? 344 THR A N      1 
ATOM   1299 C  CA     . THR A 1 201 ? 216.069 132.426 193.985 1.00 34.82  ? 344 THR A CA     1 
ATOM   1300 C  C      . THR A 1 201 ? 217.231 131.554 194.443 1.00 39.40  ? 344 THR A C      1 
ATOM   1301 O  O      . THR A 1 201 ? 217.069 130.333 194.550 1.00 44.95  ? 344 THR A O      1 
ATOM   1302 C  CB     . THR A 1 201 ? 215.316 131.725 192.850 1.00 32.52  ? 344 THR A CB     1 
ATOM   1303 O  OG1    . THR A 1 201 ? 216.126 131.712 191.669 1.00 39.43  ? 344 THR A OG1    1 
ATOM   1304 C  CG2    . THR A 1 201 ? 214.008 132.439 192.553 1.00 29.83  ? 344 THR A CG2    1 
ATOM   1305 N  N      . ARG A 1 202 ? 218.397 132.142 194.716 1.00 40.80  ? 345 ARG A N      1 
ATOM   1306 C  CA     . ARG A 1 202 ? 219.561 131.356 195.104 1.00 46.15  ? 345 ARG A CA     1 
ATOM   1307 C  C      . ARG A 1 202 ? 219.502 130.884 196.551 1.00 50.00  ? 345 ARG A C      1 
ATOM   1308 O  O      . ARG A 1 202 ? 220.266 129.988 196.925 1.00 51.37  ? 345 ARG A O      1 
ATOM   1309 C  CB     . ARG A 1 202 ? 220.841 132.162 194.874 1.00 40.29  ? 345 ARG A CB     1 
ATOM   1310 C  CG     . ARG A 1 202 ? 220.916 133.460 195.656 1.00 45.42  ? 345 ARG A CG     1 
ATOM   1311 C  CD     . ARG A 1 202 ? 222.212 134.199 195.364 1.00 49.01  ? 345 ARG A CD     1 
ATOM   1312 N  NE     . ARG A 1 202 ? 222.563 134.144 193.950 1.00 48.16  ? 345 ARG A NE     1 
ATOM   1313 C  CZ     . ARG A 1 202 ? 223.377 134.998 193.345 1.00 49.57  ? 345 ARG A CZ     1 
ATOM   1314 N  NH1    . ARG A 1 202 ? 223.940 136.000 194.002 1.00 44.79  ? 345 ARG A NH1    1 
ATOM   1315 N  NH2    . ARG A 1 202 ? 223.631 134.846 192.049 1.00 44.01  ? 345 ARG A NH2    1 
ATOM   1316 N  N      . ASN A 1 203 ? 218.622 131.459 197.369 1.00 49.73  ? 346 ASN A N      1 
ATOM   1317 C  CA     . ASN A 1 203 ? 218.450 131.042 198.755 1.00 49.77  ? 346 ASN A CA     1 
ATOM   1318 C  C      . ASN A 1 203 ? 217.033 130.540 199.013 1.00 50.55  ? 346 ASN A C      1 
ATOM   1319 O  O      . ASN A 1 203 ? 216.533 130.619 200.137 1.00 52.94  ? 346 ASN A O      1 
ATOM   1320 C  CB     . ASN A 1 203 ? 218.801 132.179 199.714 1.00 54.44  ? 346 ASN A CB     1 
ATOM   1321 C  CG     . ASN A 1 203 ? 218.194 133.503 199.295 1.00 63.16  ? 346 ASN A CG     1 
ATOM   1322 O  OD1    . ASN A 1 203 ? 217.248 133.546 198.508 1.00 55.33  ? 346 ASN A OD1    1 
ATOM   1323 N  ND2    . ASN A 1 203 ? 218.736 134.595 199.824 1.00 64.62  ? 346 ASN A ND2    1 
ATOM   1324 N  N      . LYS A 1 204 ? 216.376 130.020 197.979 1.00 48.16  ? 347 LYS A N      1 
ATOM   1325 C  CA     . LYS A 1 204 ? 215.028 129.492 198.097 1.00 46.96  ? 347 LYS A CA     1 
ATOM   1326 C  C      . LYS A 1 204 ? 214.983 128.067 197.566 1.00 50.05  ? 347 LYS A C      1 
ATOM   1327 O  O      . LYS A 1 204 ? 215.628 127.758 196.556 1.00 52.06  ? 347 LYS A O      1 
ATOM   1328 C  CB     . LYS A 1 204 ? 214.023 130.362 197.328 1.00 42.39  ? 347 LYS A CB     1 
ATOM   1329 C  CG     . LYS A 1 204 ? 213.935 131.798 197.816 1.00 41.43  ? 347 LYS A CG     1 
ATOM   1330 C  CD     . LYS A 1 204 ? 212.498 132.291 197.813 1.00 37.24  ? 347 LYS A CD     1 
ATOM   1331 C  CE     . LYS A 1 204 ? 212.424 133.786 198.072 1.00 35.40  ? 347 LYS A CE     1 
ATOM   1332 N  NZ     . LYS A 1 204 ? 212.937 134.140 199.423 1.00 37.19  ? 347 LYS A NZ     1 
ATOM   1333 N  N      . PRO A 1 205 ? 214.234 127.177 198.219 1.00 52.59  ? 348 PRO A N      1 
ATOM   1334 C  CA     . PRO A 1 205 ? 214.131 125.794 197.734 1.00 49.70  ? 348 PRO A CA     1 
ATOM   1335 C  C      . PRO A 1 205 ? 213.155 125.695 196.570 1.00 49.58  ? 348 PRO A C      1 
ATOM   1336 O  O      . PRO A 1 205 ? 212.001 126.117 196.672 1.00 51.05  ? 348 PRO A O      1 
ATOM   1337 C  CB     . PRO A 1 205 ? 213.620 125.027 198.959 1.00 48.62  ? 348 PRO A CB     1 
ATOM   1338 C  CG     . PRO A 1 205 ? 212.842 126.045 199.723 1.00 43.96  ? 348 PRO A CG     1 
ATOM   1339 C  CD     . PRO A 1 205 ? 213.523 127.373 199.495 1.00 46.31  ? 348 PRO A CD     1 
ATOM   1340 N  N      . LEU A 1 206 ? 213.625 125.133 195.460 1.00 49.88  ? 349 LEU A N      1 
ATOM   1341 C  CA     . LEU A 1 206 ? 212.816 124.953 194.266 1.00 49.97  ? 349 LEU A CA     1 
ATOM   1342 C  C      . LEU A 1 206 ? 212.696 123.471 193.937 1.00 57.11  ? 349 LEU A C      1 
ATOM   1343 O  O      . LEU A 1 206 ? 213.556 122.661 194.292 1.00 59.67  ? 349 LEU A O      1 
ATOM   1344 C  CB     . LEU A 1 206 ? 213.412 125.707 193.069 1.00 49.29  ? 349 LEU A CB     1 
ATOM   1345 C  CG     . LEU A 1 206 ? 213.697 127.197 193.261 1.00 48.49  ? 349 LEU A CG     1 
ATOM   1346 C  CD1    . LEU A 1 206 ? 214.418 127.764 192.050 1.00 37.85  ? 349 LEU A CD1    1 
ATOM   1347 C  CD2    . LEU A 1 206 ? 212.410 127.960 193.526 1.00 43.33  ? 349 LEU A CD2    1 
ATOM   1348 N  N      . ALA A 1 207 ? 211.610 123.125 193.251 1.00 57.51  ? 350 ALA A N      1 
ATOM   1349 C  CA     . ALA A 1 207 ? 211.371 121.750 192.837 1.00 57.20  ? 350 ALA A CA     1 
ATOM   1350 C  C      . ALA A 1 207 ? 212.181 121.453 191.576 1.00 65.10  ? 350 ALA A C      1 
ATOM   1351 O  O      . ALA A 1 207 ? 212.917 122.301 191.065 1.00 67.95  ? 350 ALA A O      1 
ATOM   1352 C  CB     . ALA A 1 207 ? 209.877 121.511 192.633 1.00 51.08  ? 350 ALA A CB     1 
ATOM   1353 N  N      . GLU A 1 208 ? 212.052 120.232 191.055 1.00 67.77  ? 351 GLU A N      1 
ATOM   1354 C  CA     . GLU A 1 208 ? 212.794 119.825 189.870 1.00 68.76  ? 351 GLU A CA     1 
ATOM   1355 C  C      . GLU A 1 208 ? 212.069 120.127 188.567 1.00 66.07  ? 351 GLU A C      1 
ATOM   1356 O  O      . GLU A 1 208 ? 212.672 119.988 187.497 1.00 67.59  ? 351 GLU A O      1 
ATOM   1357 C  CB     . GLU A 1 208 ? 213.109 118.325 189.930 1.00 70.76  ? 351 GLU A CB     1 
ATOM   1358 C  CG     . GLU A 1 208 ? 213.576 117.843 191.293 1.00 76.50  ? 351 GLU A CG     1 
ATOM   1359 C  CD     . GLU A 1 208 ? 214.856 118.520 191.745 1.00 84.57  ? 351 GLU A CD     1 
ATOM   1360 O  OE1    . GLU A 1 208 ? 215.873 118.413 191.028 1.00 87.07  ? 351 GLU A OE1    1 
ATOM   1361 O  OE2    . GLU A 1 208 ? 214.844 119.159 192.818 1.00 82.85  ? 351 GLU A OE2    1 
ATOM   1362 N  N      . ASP A 1 209 ? 210.801 120.530 188.625 1.00 61.18  ? 352 ASP A N      1 
ATOM   1363 C  CA     . ASP A 1 209 ? 210.048 120.858 187.421 1.00 62.60  ? 352 ASP A CA     1 
ATOM   1364 C  C      . ASP A 1 209 ? 210.073 122.344 187.089 1.00 60.76  ? 352 ASP A C      1 
ATOM   1365 O  O      . ASP A 1 209 ? 209.432 122.753 186.115 1.00 57.58  ? 352 ASP A O      1 
ATOM   1366 C  CB     . ASP A 1 209 ? 208.598 120.386 187.563 1.00 61.10  ? 352 ASP A CB     1 
ATOM   1367 C  CG     . ASP A 1 209 ? 207.886 121.029 188.736 1.00 64.25  ? 352 ASP A CG     1 
ATOM   1368 O  OD1    . ASP A 1 209 ? 208.547 121.296 189.761 1.00 65.83  ? 352 ASP A OD1    1 
ATOM   1369 O  OD2    . ASP A 1 209 ? 206.665 121.268 188.633 1.00 62.57  ? 352 ASP A OD2    1 
ATOM   1370 N  N      . VAL A 1 210 ? 210.790 123.154 187.861 1.00 59.72  ? 353 VAL A N      1 
ATOM   1371 C  CA     . VAL A 1 210 ? 210.842 124.592 187.624 1.00 57.61  ? 353 VAL A CA     1 
ATOM   1372 C  C      . VAL A 1 210 ? 211.846 124.881 186.517 1.00 57.31  ? 353 VAL A C      1 
ATOM   1373 O  O      . VAL A 1 210 ? 213.005 124.456 186.584 1.00 58.17  ? 353 VAL A O      1 
ATOM   1374 C  CB     . VAL A 1 210 ? 211.207 125.343 188.914 1.00 55.49  ? 353 VAL A CB     1 
ATOM   1375 C  CG1    . VAL A 1 210 ? 211.549 126.792 188.604 1.00 49.70  ? 353 VAL A CG1    1 
ATOM   1376 C  CG2    . VAL A 1 210 ? 210.068 125.259 189.917 1.00 51.91  ? 353 VAL A CG2    1 
ATOM   1377 N  N      . ASN A 1 211 ? 211.401 125.606 185.493 1.00 53.94  ? 354 ASN A N      1 
ATOM   1378 C  CA     . ASN A 1 211 ? 212.245 126.005 184.371 1.00 48.92  ? 354 ASN A CA     1 
ATOM   1379 C  C      . ASN A 1 211 ? 212.265 127.527 184.313 1.00 46.58  ? 354 ASN A C      1 
ATOM   1380 O  O      . ASN A 1 211 ? 211.282 128.149 183.896 1.00 46.41  ? 354 ASN A O      1 
ATOM   1381 C  CB     . ASN A 1 211 ? 211.733 125.410 183.060 1.00 49.68  ? 354 ASN A CB     1 
ATOM   1382 C  CG     . ASN A 1 211 ? 212.790 125.396 181.974 1.00 55.09  ? 354 ASN A CG     1 
ATOM   1383 O  OD1    . ASN A 1 211 ? 213.985 125.493 182.252 1.00 59.95  ? 354 ASN A OD1    1 
ATOM   1384 N  ND2    . ASN A 1 211 ? 212.354 125.272 180.726 1.00 51.78  ? 354 ASN A ND2    1 
ATOM   1385 N  N      . LEU A 1 212 ? 213.382 128.125 184.733 1.00 42.91  ? 355 LEU A N      1 
ATOM   1386 C  CA     . LEU A 1 212 ? 213.473 129.579 184.784 1.00 39.52  ? 355 LEU A CA     1 
ATOM   1387 C  C      . LEU A 1 212 ? 213.514 130.212 183.400 1.00 42.31  ? 355 LEU A C      1 
ATOM   1388 O  O      . LEU A 1 212 ? 213.175 131.392 183.265 1.00 42.47  ? 355 LEU A O      1 
ATOM   1389 C  CB     . LEU A 1 212 ? 214.705 130.000 185.586 1.00 39.67  ? 355 LEU A CB     1 
ATOM   1390 C  CG     . LEU A 1 212 ? 214.602 129.861 187.106 1.00 40.17  ? 355 LEU A CG     1 
ATOM   1391 C  CD1    . LEU A 1 212 ? 215.732 130.610 187.790 1.00 37.95  ? 355 LEU A CD1    1 
ATOM   1392 C  CD2    . LEU A 1 212 ? 213.252 130.355 187.599 1.00 37.53  ? 355 LEU A CD2    1 
ATOM   1393 N  N      . GLU A 1 213 ? 213.918 129.463 182.373 1.00 45.71  ? 356 GLU A N      1 
ATOM   1394 C  CA     . GLU A 1 213 ? 213.938 130.013 181.022 1.00 44.05  ? 356 GLU A CA     1 
ATOM   1395 C  C      . GLU A 1 213 ? 212.537 130.155 180.442 1.00 42.35  ? 356 GLU A C      1 
ATOM   1396 O  O      . GLU A 1 213 ? 212.279 131.095 179.683 1.00 44.57  ? 356 GLU A O      1 
ATOM   1397 C  CB     . GLU A 1 213 ? 214.798 129.141 180.107 1.00 51.55  ? 356 GLU A CB     1 
ATOM   1398 C  CG     . GLU A 1 213 ? 215.016 129.729 178.723 1.00 60.96  ? 356 GLU A CG     1 
ATOM   1399 C  CD     . GLU A 1 213 ? 216.117 129.025 177.955 1.00 72.43  ? 356 GLU A CD     1 
ATOM   1400 O  OE1    . GLU A 1 213 ? 217.163 128.715 178.563 1.00 73.57  ? 356 GLU A OE1    1 
ATOM   1401 O  OE2    . GLU A 1 213 ? 215.938 128.784 176.743 1.00 75.90  ? 356 GLU A OE2    1 
ATOM   1402 N  N      . ILE A 1 214 ? 211.628 129.238 180.778 1.00 42.68  ? 357 ILE A N      1 
ATOM   1403 C  CA     . ILE A 1 214 ? 210.251 129.361 180.313 1.00 40.73  ? 357 ILE A CA     1 
ATOM   1404 C  C      . ILE A 1 214 ? 209.562 130.545 180.977 1.00 40.01  ? 357 ILE A C      1 
ATOM   1405 O  O      . ILE A 1 214 ? 208.766 131.245 180.341 1.00 41.59  ? 357 ILE A O      1 
ATOM   1406 C  CB     . ILE A 1 214 ? 209.483 128.050 180.560 1.00 47.94  ? 357 ILE A CB     1 
ATOM   1407 C  CG1    . ILE A 1 214 ? 209.977 126.958 179.609 1.00 46.91  ? 357 ILE A CG1    1 
ATOM   1408 C  CG2    . ILE A 1 214 ? 207.988 128.269 180.397 1.00 45.84  ? 357 ILE A CG2    1 
ATOM   1409 C  CD1    . ILE A 1 214 ? 209.240 125.646 179.747 1.00 47.19  ? 357 ILE A CD1    1 
ATOM   1410 N  N      . ILE A 1 215 ? 209.848 130.790 182.257 1.00 38.35  ? 358 ILE A N      1 
ATOM   1411 C  CA     . ILE A 1 215 ? 209.257 131.933 182.944 1.00 37.96  ? 358 ILE A CA     1 
ATOM   1412 C  C      . ILE A 1 215 ? 209.742 133.238 182.327 1.00 37.70  ? 358 ILE A C      1 
ATOM   1413 O  O      . ILE A 1 215 ? 208.979 134.203 182.202 1.00 37.61  ? 358 ILE A O      1 
ATOM   1414 C  CB     . ILE A 1 215 ? 209.567 131.869 184.451 1.00 37.00  ? 358 ILE A CB     1 
ATOM   1415 C  CG1    . ILE A 1 215 ? 208.944 130.619 185.072 1.00 38.32  ? 358 ILE A CG1    1 
ATOM   1416 C  CG2    . ILE A 1 215 ? 209.067 133.123 185.152 1.00 29.33  ? 358 ILE A CG2    1 
ATOM   1417 C  CD1    . ILE A 1 215 ? 207.445 130.534 184.896 1.00 39.68  ? 358 ILE A CD1    1 
ATOM   1418 N  N      . ALA A 1 216 ? 211.017 133.293 181.936 1.00 37.66  ? 359 ALA A N      1 
ATOM   1419 C  CA     . ALA A 1 216 ? 211.555 134.508 181.333 1.00 33.33  ? 359 ALA A CA     1 
ATOM   1420 C  C      . ALA A 1 216 ? 210.875 134.817 180.005 1.00 35.71  ? 359 ALA A C      1 
ATOM   1421 O  O      . ALA A 1 216 ? 210.622 135.985 179.688 1.00 35.78  ? 359 ALA A O      1 
ATOM   1422 C  CB     . ALA A 1 216 ? 213.066 134.378 181.147 1.00 29.14  ? 359 ALA A CB     1 
ATOM   1423 N  N      . LYS A 1 217 ? 210.575 133.785 179.214 1.00 37.16  ? 360 LYS A N      1 
ATOM   1424 C  CA     . LYS A 1 217 ? 209.942 133.996 177.917 1.00 38.42  ? 360 LYS A CA     1 
ATOM   1425 C  C      . LYS A 1 217 ? 208.517 134.516 178.038 1.00 36.50  ? 360 LYS A C      1 
ATOM   1426 O  O      . LYS A 1 217 ? 207.977 135.036 177.056 1.00 38.44  ? 360 LYS A O      1 
ATOM   1427 C  CB     . LYS A 1 217 ? 209.942 132.695 177.114 1.00 38.91  ? 360 LYS A CB     1 
ATOM   1428 C  CG     . LYS A 1 217 ? 211.230 132.417 176.362 1.00 45.05  ? 360 LYS A CG     1 
ATOM   1429 C  CD     . LYS A 1 217 ? 211.058 131.253 175.399 1.00 48.88  ? 360 LYS A CD     1 
ATOM   1430 C  CE     . LYS A 1 217 ? 212.392 130.799 174.832 1.00 52.69  ? 360 LYS A CE     1 
ATOM   1431 N  NZ     . LYS A 1 217 ? 213.418 130.638 175.898 1.00 60.89  ? 360 LYS A NZ     1 
ATOM   1432 N  N      . ARG A 1 218 ? 207.896 134.389 179.209 1.00 35.36  ? 361 ARG A N      1 
ATOM   1433 C  CA     . ARG A 1 218 ? 206.498 134.750 179.396 1.00 34.70  ? 361 ARG A CA     1 
ATOM   1434 C  C      . ARG A 1 218 ? 206.313 136.072 180.131 1.00 36.33  ? 361 ARG A C      1 
ATOM   1435 O  O      . ARG A 1 218 ? 205.190 136.389 180.534 1.00 38.96  ? 361 ARG A O      1 
ATOM   1436 C  CB     . ARG A 1 218 ? 205.764 133.635 180.143 1.00 38.46  ? 361 ARG A CB     1 
ATOM   1437 C  CG     . ARG A 1 218 ? 205.525 132.386 179.312 1.00 43.86  ? 361 ARG A CG     1 
ATOM   1438 C  CD     . ARG A 1 218 ? 204.795 131.323 180.113 1.00 50.21  ? 361 ARG A CD     1 
ATOM   1439 N  NE     . ARG A 1 218 ? 203.553 131.829 180.685 1.00 62.56  ? 361 ARG A NE     1 
ATOM   1440 C  CZ     . ARG A 1 218 ? 202.626 131.071 181.254 1.00 65.89  ? 361 ARG A CZ     1 
ATOM   1441 N  NH1    . ARG A 1 218 ? 202.766 129.759 181.345 1.00 60.63  ? 361 ARG A NH1    1 
ATOM   1442 N  NH2    . ARG A 1 218 ? 201.530 131.644 181.744 1.00 61.04  ? 361 ARG A NH2    1 
ATOM   1443 N  N      . THR A 1 219 ? 207.381 136.853 180.315 1.00 33.52  ? 362 THR A N      1 
ATOM   1444 C  CA     . THR A 1 219 ? 207.292 138.133 181.022 1.00 29.07  ? 362 THR A CA     1 
ATOM   1445 C  C      . THR A 1 219 ? 207.970 139.256 180.237 1.00 29.18  ? 362 THR A C      1 
ATOM   1446 O  O      . THR A 1 219 ? 208.807 139.984 180.769 1.00 31.43  ? 362 THR A O      1 
ATOM   1447 C  CB     . THR A 1 219 ? 207.897 138.012 182.417 1.00 30.15  ? 362 THR A CB     1 
ATOM   1448 O  OG1    . THR A 1 219 ? 209.122 137.273 182.347 1.00 29.69  ? 362 THR A OG1    1 
ATOM   1449 C  CG2    . THR A 1 219 ? 206.935 137.302 183.355 1.00 28.84  ? 362 THR A CG2    1 
ATOM   1450 N  N      . PRO A 1 220 ? 207.626 139.427 178.960 1.00 31.86  ? 363 PRO A N      1 
ATOM   1451 C  CA     . PRO A 1 220 ? 208.179 140.556 178.201 1.00 28.01  ? 363 PRO A CA     1 
ATOM   1452 C  C      . PRO A 1 220 ? 207.621 141.875 178.717 1.00 27.71  ? 363 PRO A C      1 
ATOM   1453 O  O      . PRO A 1 220 ? 206.416 142.012 178.933 1.00 32.82  ? 363 PRO A O      1 
ATOM   1454 C  CB     . PRO A 1 220 ? 207.732 140.275 176.763 1.00 28.62  ? 363 PRO A CB     1 
ATOM   1455 C  CG     . PRO A 1 220 ? 206.506 139.447 176.912 1.00 28.49  ? 363 PRO A CG     1 
ATOM   1456 C  CD     . PRO A 1 220 ? 206.718 138.606 178.139 1.00 32.73  ? 363 PRO A CD     1 
ATOM   1457 N  N      . GLY A 1 221 ? 208.508 142.848 178.911 1.00 25.67  ? 364 GLY A N      1 
ATOM   1458 C  CA     . GLY A 1 221 ? 208.134 144.151 179.422 1.00 24.30  ? 364 GLY A CA     1 
ATOM   1459 C  C      . GLY A 1 221 ? 208.367 144.339 180.905 1.00 29.26  ? 364 GLY A C      1 
ATOM   1460 O  O      . GLY A 1 221 ? 208.153 145.448 181.410 1.00 32.07  ? 364 GLY A O      1 
ATOM   1461 N  N      . PHE A 1 222 ? 208.789 143.299 181.618 1.00 28.24  ? 365 PHE A N      1 
ATOM   1462 C  CA     . PHE A 1 222 ? 209.054 143.410 183.044 1.00 25.93  ? 365 PHE A CA     1 
ATOM   1463 C  C      . PHE A 1 222 ? 210.425 144.027 183.295 1.00 25.13  ? 365 PHE A C      1 
ATOM   1464 O  O      . PHE A 1 222 ? 211.340 143.921 182.474 1.00 27.79  ? 365 PHE A O      1 
ATOM   1465 C  CB     . PHE A 1 222 ? 208.978 142.037 183.713 1.00 25.41  ? 365 PHE A CB     1 
ATOM   1466 C  CG     . PHE A 1 222 ? 207.604 141.670 184.197 1.00 28.44  ? 365 PHE A CG     1 
ATOM   1467 C  CD1    . PHE A 1 222 ? 206.476 142.184 183.581 1.00 31.77  ? 365 PHE A CD1    1 
ATOM   1468 C  CD2    . PHE A 1 222 ? 207.442 140.808 185.268 1.00 29.14  ? 365 PHE A CD2    1 
ATOM   1469 C  CE1    . PHE A 1 222 ? 205.212 141.846 184.026 1.00 32.79  ? 365 PHE A CE1    1 
ATOM   1470 C  CE2    . PHE A 1 222 ? 206.181 140.466 185.717 1.00 27.62  ? 365 PHE A CE2    1 
ATOM   1471 C  CZ     . PHE A 1 222 ? 205.065 140.986 185.095 1.00 30.94  ? 365 PHE A CZ     1 
ATOM   1472 N  N      . VAL A 1 223 ? 210.561 144.674 184.451 1.00 23.54  ? 366 VAL A N      1 
ATOM   1473 C  CA     . VAL A 1 223 ? 211.835 145.242 184.879 1.00 22.84  ? 366 VAL A CA     1 
ATOM   1474 C  C      . VAL A 1 223 ? 212.320 144.490 186.111 1.00 21.75  ? 366 VAL A C      1 
ATOM   1475 O  O      . VAL A 1 223 ? 211.638 143.589 186.609 1.00 25.13  ? 366 VAL A O      1 
ATOM   1476 C  CB     . VAL A 1 223 ? 211.719 146.752 185.162 1.00 21.79  ? 366 VAL A CB     1 
ATOM   1477 C  CG1    . VAL A 1 223 ? 211.459 147.516 183.874 1.00 16.92  ? 366 VAL A CG1    1 
ATOM   1478 C  CG2    . VAL A 1 223 ? 210.626 147.023 186.183 1.00 21.80  ? 366 VAL A CG2    1 
ATOM   1479 N  N      . GLY A 1 224 ? 213.502 144.855 186.609 1.00 18.68  ? 367 GLY A N      1 
ATOM   1480 C  CA     . GLY A 1 224 ? 214.068 144.148 187.744 1.00 17.80  ? 367 GLY A CA     1 
ATOM   1481 C  C      . GLY A 1 224 ? 213.215 144.231 188.994 1.00 20.20  ? 367 GLY A C      1 
ATOM   1482 O  O      . GLY A 1 224 ? 213.233 143.318 189.822 1.00 22.65  ? 367 GLY A O      1 
ATOM   1483 N  N      . ALA A 1 225 ? 212.463 145.322 189.153 1.00 20.82  ? 368 ALA A N      1 
ATOM   1484 C  CA     . ALA A 1 225 ? 211.592 145.457 190.315 1.00 20.23  ? 368 ALA A CA     1 
ATOM   1485 C  C      . ALA A 1 225 ? 210.373 144.548 190.227 1.00 25.31  ? 368 ALA A C      1 
ATOM   1486 O  O      . ALA A 1 225 ? 209.920 144.029 191.252 1.00 26.84  ? 368 ALA A O      1 
ATOM   1487 C  CB     . ALA A 1 225 ? 211.152 146.912 190.477 1.00 19.30  ? 368 ALA A CB     1 
ATOM   1488 N  N      . ASP A 1 226 ? 209.830 144.347 189.025 1.00 23.75  ? 369 ASP A N      1 
ATOM   1489 C  CA     . ASP A 1 226 ? 208.690 143.453 188.864 1.00 21.54  ? 369 ASP A CA     1 
ATOM   1490 C  C      . ASP A 1 226 ? 209.072 141.994 189.072 1.00 22.77  ? 369 ASP A C      1 
ATOM   1491 O  O      . ASP A 1 226 ? 208.294 141.233 189.656 1.00 24.69  ? 369 ASP A O      1 
ATOM   1492 C  CB     . ASP A 1 226 ? 208.068 143.636 187.479 1.00 26.41  ? 369 ASP A CB     1 
ATOM   1493 C  CG     . ASP A 1 226 ? 207.655 145.068 187.209 1.00 34.61  ? 369 ASP A CG     1 
ATOM   1494 O  OD1    . ASP A 1 226 ? 207.171 145.735 188.147 1.00 38.71  ? 369 ASP A OD1    1 
ATOM   1495 O  OD2    . ASP A 1 226 ? 207.814 145.526 186.059 1.00 35.90  ? 369 ASP A OD2    1 
ATOM   1496 N  N      . LEU A 1 227 ? 210.253 141.586 188.602 1.00 21.13  ? 370 LEU A N      1 
ATOM   1497 C  CA     . LEU A 1 227 ? 210.673 140.199 188.761 1.00 19.60  ? 370 LEU A CA     1 
ATOM   1498 C  C      . LEU A 1 227 ? 210.929 139.851 190.222 1.00 22.31  ? 370 LEU A C      1 
ATOM   1499 O  O      . LEU A 1 227 ? 210.647 138.726 190.647 1.00 24.39  ? 370 LEU A O      1 
ATOM   1500 C  CB     . LEU A 1 227 ? 211.922 139.929 187.923 1.00 20.07  ? 370 LEU A CB     1 
ATOM   1501 C  CG     . LEU A 1 227 ? 211.772 140.126 186.413 1.00 23.83  ? 370 LEU A CG     1 
ATOM   1502 C  CD1    . LEU A 1 227 ? 213.119 140.415 185.771 1.00 19.09  ? 370 LEU A CD1    1 
ATOM   1503 C  CD2    . LEU A 1 227 ? 211.118 138.912 185.775 1.00 18.66  ? 370 LEU A CD2    1 
ATOM   1504 N  N      . GLU A 1 228 ? 211.468 140.793 190.998 1.00 23.10  ? 371 GLU A N      1 
ATOM   1505 C  CA     . GLU A 1 228 ? 211.680 140.547 192.420 1.00 22.68  ? 371 GLU A CA     1 
ATOM   1506 C  C      . GLU A 1 228 ? 210.357 140.342 193.148 1.00 25.85  ? 371 GLU A C      1 
ATOM   1507 O  O      . GLU A 1 228 ? 210.248 139.471 194.019 1.00 27.93  ? 371 GLU A O      1 
ATOM   1508 C  CB     . GLU A 1 228 ? 212.463 141.704 193.037 1.00 25.69  ? 371 GLU A CB     1 
ATOM   1509 C  CG     . GLU A 1 228 ? 213.234 141.336 194.290 1.00 30.00  ? 371 GLU A CG     1 
ATOM   1510 C  CD     . GLU A 1 228 ? 212.553 141.820 195.551 1.00 42.78  ? 371 GLU A CD     1 
ATOM   1511 O  OE1    . GLU A 1 228 ? 211.674 142.702 195.453 1.00 41.17  ? 371 GLU A OE1    1 
ATOM   1512 O  OE2    . GLU A 1 228 ? 212.894 141.319 196.642 1.00 55.29  ? 371 GLU A OE2    1 
ATOM   1513 N  N      . ASN A 1 229 ? 209.340 141.137 192.807 1.00 23.28  ? 372 ASN A N      1 
ATOM   1514 C  CA     . ASN A 1 229 ? 208.035 140.992 193.441 1.00 21.50  ? 372 ASN A CA     1 
ATOM   1515 C  C      . ASN A 1 229 ? 207.342 139.702 193.017 1.00 23.31  ? 372 ASN A C      1 
ATOM   1516 O  O      . ASN A 1 229 ? 206.562 139.137 193.791 1.00 25.30  ? 372 ASN A O      1 
ATOM   1517 C  CB     . ASN A 1 229 ? 207.160 142.202 193.110 1.00 23.30  ? 372 ASN A CB     1 
ATOM   1518 C  CG     . ASN A 1 229 ? 205.830 142.179 193.836 1.00 27.17  ? 372 ASN A CG     1 
ATOM   1519 O  OD1    . ASN A 1 229 ? 204.803 141.819 193.263 1.00 27.47  ? 372 ASN A OD1    1 
ATOM   1520 N  ND2    . ASN A 1 229 ? 205.842 142.568 195.105 1.00 31.82  ? 372 ASN A ND2    1 
ATOM   1521 N  N      . LEU A 1 230 ? 207.609 139.227 191.799 1.00 20.69  ? 373 LEU A N      1 
ATOM   1522 C  CA     . LEU A 1 230 ? 206.998 137.985 191.336 1.00 20.50  ? 373 LEU A CA     1 
ATOM   1523 C  C      . LEU A 1 230 ? 207.480 136.791 192.150 1.00 24.22  ? 373 LEU A C      1 
ATOM   1524 O  O      . LEU A 1 230 ? 206.698 135.885 192.457 1.00 25.33  ? 373 LEU A O      1 
ATOM   1525 C  CB     . LEU A 1 230 ? 207.293 137.776 189.852 1.00 18.43  ? 373 LEU A CB     1 
ATOM   1526 C  CG     . LEU A 1 230 ? 206.674 136.536 189.203 1.00 22.87  ? 373 LEU A CG     1 
ATOM   1527 C  CD1    . LEU A 1 230 ? 205.185 136.738 188.976 1.00 29.74  ? 373 LEU A CD1    1 
ATOM   1528 C  CD2    . LEU A 1 230 ? 207.379 136.201 187.901 1.00 21.80  ? 373 LEU A CD2    1 
ATOM   1529 N  N      . VAL A 1 231 ? 208.768 136.767 192.502 1.00 24.06  ? 374 VAL A N      1 
ATOM   1530 C  CA     . VAL A 1 231 ? 209.306 135.650 193.271 1.00 22.25  ? 374 VAL A CA     1 
ATOM   1531 C  C      . VAL A 1 231 ? 208.668 135.584 194.652 1.00 22.93  ? 374 VAL A C      1 
ATOM   1532 O  O      . VAL A 1 231 ? 208.419 134.492 195.176 1.00 24.90  ? 374 VAL A O      1 
ATOM   1533 C  CB     . VAL A 1 231 ? 210.839 135.758 193.362 1.00 22.70  ? 374 VAL A CB     1 
ATOM   1534 C  CG1    . VAL A 1 231 ? 211.382 134.767 194.378 1.00 20.28  ? 374 VAL A CG1    1 
ATOM   1535 C  CG2    . VAL A 1 231 ? 211.467 135.527 191.999 1.00 18.84  ? 374 VAL A CG2    1 
ATOM   1536 N  N      . ASN A 1 232 ? 208.396 136.738 195.266 1.00 23.33  ? 375 ASN A N      1 
ATOM   1537 C  CA     . ASN A 1 232 ? 207.772 136.743 196.584 1.00 21.81  ? 375 ASN A CA     1 
ATOM   1538 C  C      . ASN A 1 232 ? 206.347 136.207 196.535 1.00 26.20  ? 375 ASN A C      1 
ATOM   1539 O  O      . ASN A 1 232 ? 205.915 135.516 197.464 1.00 26.57  ? 375 ASN A O      1 
ATOM   1540 C  CB     . ASN A 1 232 ? 207.789 138.156 197.167 1.00 21.04  ? 375 ASN A CB     1 
ATOM   1541 C  CG     . ASN A 1 232 ? 207.332 138.196 198.612 1.00 22.59  ? 375 ASN A CG     1 
ATOM   1542 O  OD1    . ASN A 1 232 ? 206.286 138.760 198.929 1.00 21.49  ? 375 ASN A OD1    1 
ATOM   1543 N  ND2    . ASN A 1 232 ? 208.118 137.597 199.498 1.00 22.44  ? 375 ASN A ND2    1 
ATOM   1544 N  N      . GLU A 1 233 ? 205.603 136.515 195.470 1.00 25.14  ? 376 GLU A N      1 
ATOM   1545 C  CA     . GLU A 1 233 ? 204.234 136.024 195.360 1.00 23.56  ? 376 GLU A CA     1 
ATOM   1546 C  C      . GLU A 1 233 ? 204.189 134.510 195.198 1.00 27.10  ? 376 GLU A C      1 
ATOM   1547 O  O      . GLU A 1 233 ? 203.291 133.858 195.742 1.00 31.21  ? 376 GLU A O      1 
ATOM   1548 C  CB     . GLU A 1 233 ? 203.523 136.705 194.190 1.00 28.56  ? 376 GLU A CB     1 
ATOM   1549 C  CG     . GLU A 1 233 ? 203.218 138.175 194.420 1.00 39.50  ? 376 GLU A CG     1 
ATOM   1550 C  CD     . GLU A 1 233 ? 202.114 138.390 195.437 1.00 48.13  ? 376 GLU A CD     1 
ATOM   1551 O  OE1    . GLU A 1 233 ? 201.394 137.420 195.750 1.00 53.05  ? 376 GLU A OE1    1 
ATOM   1552 O  OE2    . GLU A 1 233 ? 201.966 139.531 195.924 1.00 50.66  ? 376 GLU A OE2    1 
ATOM   1553 N  N      . ALA A 1 234 ? 205.140 133.935 194.459 1.00 27.58  ? 377 ALA A N      1 
ATOM   1554 C  CA     . ALA A 1 234 ? 205.170 132.486 194.295 1.00 25.55  ? 377 ALA A CA     1 
ATOM   1555 C  C      . ALA A 1 234 ? 205.452 131.777 195.612 1.00 27.37  ? 377 ALA A C      1 
ATOM   1556 O  O      . ALA A 1 234 ? 204.912 130.694 195.860 1.00 32.07  ? 377 ALA A O      1 
ATOM   1557 C  CB     . ALA A 1 234 ? 206.210 132.096 193.246 1.00 26.80  ? 377 ALA A CB     1 
ATOM   1558 N  N      . ALA A 1 235 ? 206.293 132.366 196.466 1.00 26.20  ? 378 ALA A N      1 
ATOM   1559 C  CA     . ALA A 1 235 ? 206.573 131.758 197.762 1.00 27.07  ? 378 ALA A CA     1 
ATOM   1560 C  C      . ALA A 1 235 ? 205.365 131.823 198.687 1.00 29.32  ? 378 ALA A C      1 
ATOM   1561 O  O      . ALA A 1 235 ? 205.172 130.926 199.514 1.00 32.11  ? 378 ALA A O      1 
ATOM   1562 C  CB     . ALA A 1 235 ? 207.779 132.435 198.412 1.00 23.34  ? 378 ALA A CB     1 
ATOM   1563 N  N      . LEU A 1 236 ? 204.547 132.872 198.567 1.00 29.63  ? 379 LEU A N      1 
ATOM   1564 C  CA     . LEU A 1 236 ? 203.357 132.979 199.404 1.00 26.25  ? 379 LEU A CA     1 
ATOM   1565 C  C      . LEU A 1 236 ? 202.315 131.931 199.037 1.00 30.25  ? 379 LEU A C      1 
ATOM   1566 O  O      . LEU A 1 236 ? 201.598 131.439 199.915 1.00 32.73  ? 379 LEU A O      1 
ATOM   1567 C  CB     . LEU A 1 236 ? 202.759 134.382 199.293 1.00 24.76  ? 379 LEU A CB     1 
ATOM   1568 C  CG     . LEU A 1 236 ? 203.422 135.483 200.121 1.00 24.09  ? 379 LEU A CG     1 
ATOM   1569 C  CD1    . LEU A 1 236 ? 202.968 136.853 199.647 1.00 21.86  ? 379 LEU A CD1    1 
ATOM   1570 C  CD2    . LEU A 1 236 ? 203.124 135.299 201.600 1.00 17.71  ? 379 LEU A CD2    1 
ATOM   1571 N  N      . LEU A 1 237 ? 202.211 131.580 197.753 1.00 29.89  ? 380 LEU A N      1 
ATOM   1572 C  CA     . LEU A 1 237 ? 201.258 130.560 197.336 1.00 30.78  ? 380 LEU A CA     1 
ATOM   1573 C  C      . LEU A 1 237 ? 201.624 129.179 197.861 1.00 37.55  ? 380 LEU A C      1 
ATOM   1574 O  O      . LEU A 1 237 ? 200.727 128.379 198.143 1.00 44.20  ? 380 LEU A O      1 
ATOM   1575 C  CB     . LEU A 1 237 ? 201.157 130.527 195.810 1.00 30.68  ? 380 LEU A CB     1 
ATOM   1576 C  CG     . LEU A 1 237 ? 200.344 131.646 195.157 1.00 34.47  ? 380 LEU A CG     1 
ATOM   1577 C  CD1    . LEU A 1 237 ? 200.395 131.536 193.642 1.00 33.32  ? 380 LEU A CD1    1 
ATOM   1578 C  CD2    . LEU A 1 237 ? 198.907 131.628 195.650 1.00 36.71  ? 380 LEU A CD2    1 
ATOM   1579 N  N      . ALA A 1 238 ? 202.916 128.882 197.999 1.00 36.76  ? 381 ALA A N      1 
ATOM   1580 C  CA     . ALA A 1 238 ? 203.349 127.600 198.538 1.00 37.45  ? 381 ALA A CA     1 
ATOM   1581 C  C      . ALA A 1 238 ? 203.220 127.527 200.052 1.00 38.75  ? 381 ALA A C      1 
ATOM   1582 O  O      . ALA A 1 238 ? 202.935 126.450 200.590 1.00 44.04  ? 381 ALA A O      1 
ATOM   1583 C  CB     . ALA A 1 238 ? 204.798 127.319 198.134 1.00 36.83  ? 381 ALA A CB     1 
ATOM   1584 N  N      . ALA A 1 239 ? 203.422 128.645 200.752 1.00 37.54  ? 382 ALA A N      1 
ATOM   1585 C  CA     . ALA A 1 239 ? 203.306 128.649 202.205 1.00 36.37  ? 382 ALA A CA     1 
ATOM   1586 C  C      . ALA A 1 239 ? 201.856 128.582 202.665 1.00 42.83  ? 382 ALA A C      1 
ATOM   1587 O  O      . ALA A 1 239 ? 201.581 128.077 203.759 1.00 46.00  ? 382 ALA A O      1 
ATOM   1588 C  CB     . ALA A 1 239 ? 203.982 129.892 202.785 1.00 25.95  ? 382 ALA A CB     1 
ATOM   1589 N  N      . ARG A 1 240 ? 200.920 129.082 201.855 1.00 43.96  ? 383 ARG A N      1 
ATOM   1590 C  CA     . ARG A 1 240 ? 199.511 129.010 202.217 1.00 43.99  ? 383 ARG A CA     1 
ATOM   1591 C  C      . ARG A 1 240 ? 198.999 127.575 202.248 1.00 47.69  ? 383 ARG A C      1 
ATOM   1592 O  O      . ARG A 1 240 ? 197.960 127.314 202.862 1.00 51.95  ? 383 ARG A O      1 
ATOM   1593 C  CB     . ARG A 1 240 ? 198.678 129.850 201.245 1.00 45.86  ? 383 ARG A CB     1 
ATOM   1594 C  CG     . ARG A 1 240 ? 197.177 129.792 201.482 1.00 55.96  ? 383 ARG A CG     1 
ATOM   1595 C  CD     . ARG A 1 240 ? 196.778 130.522 202.758 1.00 69.16  ? 383 ARG A CD     1 
ATOM   1596 N  NE     . ARG A 1 240 ? 197.023 131.958 202.678 1.00 78.24  ? 383 ARG A NE     1 
ATOM   1597 C  CZ     . ARG A 1 240 ? 196.341 132.873 203.354 1.00 66.37  ? 383 ARG A CZ     1 
ATOM   1598 N  NH1    . ARG A 1 240 ? 195.354 132.538 204.169 1.00 57.23  ? 383 ARG A NH1    1 
ATOM   1599 N  NH2    . ARG A 1 240 ? 196.656 134.157 203.209 1.00 51.50  ? 383 ARG A NH2    1 
ATOM   1600 N  N      . GLU A 1 241 ? 199.707 126.644 201.610 1.00 47.44  ? 384 GLU A N      1 
ATOM   1601 C  CA     . GLU A 1 241 ? 199.340 125.235 201.613 1.00 49.60  ? 384 GLU A CA     1 
ATOM   1602 C  C      . GLU A 1 241 ? 200.260 124.382 202.475 1.00 51.30  ? 384 GLU A C      1 
ATOM   1603 O  O      . GLU A 1 241 ? 200.089 123.160 202.517 1.00 55.73  ? 384 GLU A O      1 
ATOM   1604 C  CB     . GLU A 1 241 ? 199.326 124.689 200.180 1.00 49.98  ? 384 GLU A CB     1 
ATOM   1605 C  CG     . GLU A 1 241 ? 198.185 125.216 199.328 1.00 52.47  ? 384 GLU A CG     1 
ATOM   1606 C  CD     . GLU A 1 241 ? 198.098 124.528 197.980 1.00 64.12  ? 384 GLU A CD     1 
ATOM   1607 O  OE1    . GLU A 1 241 ? 199.087 123.882 197.577 1.00 66.09  ? 384 GLU A OE1    1 
ATOM   1608 O  OE2    . GLU A 1 241 ? 197.042 124.635 197.322 1.00 71.84  ? 384 GLU A OE2    1 
ATOM   1609 N  N      . GLY A 1 242 ? 201.230 124.987 203.157 1.00 48.51  ? 385 GLY A N      1 
ATOM   1610 C  CA     . GLY A 1 242 ? 202.110 124.252 204.041 1.00 47.51  ? 385 GLY A CA     1 
ATOM   1611 C  C      . GLY A 1 242 ? 203.231 123.495 203.366 1.00 55.31  ? 385 GLY A C      1 
ATOM   1612 O  O      . GLY A 1 242 ? 203.928 122.728 204.039 1.00 54.45  ? 385 GLY A O      1 
ATOM   1613 N  N      . ARG A 1 243 ? 203.431 123.682 202.065 1.00 55.60  ? 386 ARG A N      1 
ATOM   1614 C  CA     . ARG A 1 243 ? 204.495 122.982 201.364 1.00 52.60  ? 386 ARG A CA     1 
ATOM   1615 C  C      . ARG A 1 243 ? 205.846 123.635 201.647 1.00 55.09  ? 386 ARG A C      1 
ATOM   1616 O  O      . ARG A 1 243 ? 205.934 124.779 202.099 1.00 57.18  ? 386 ARG A O      1 
ATOM   1617 C  CB     . ARG A 1 243 ? 204.223 122.957 199.860 1.00 49.87  ? 386 ARG A CB     1 
ATOM   1618 C  CG     . ARG A 1 243 ? 202.987 122.163 199.474 1.00 52.81  ? 386 ARG A CG     1 
ATOM   1619 C  CD     . ARG A 1 243 ? 202.918 121.937 197.973 1.00 56.98  ? 386 ARG A CD     1 
ATOM   1620 N  NE     . ARG A 1 243 ? 202.008 122.872 197.322 1.00 58.98  ? 386 ARG A NE     1 
ATOM   1621 C  CZ     . ARG A 1 243 ? 202.395 123.948 196.651 1.00 56.26  ? 386 ARG A CZ     1 
ATOM   1622 N  NH1    . ARG A 1 243 ? 203.674 124.256 196.517 1.00 51.73  ? 386 ARG A NH1    1 
ATOM   1623 N  NH2    . ARG A 1 243 ? 201.474 124.734 196.101 1.00 53.24  ? 386 ARG A NH2    1 
ATOM   1624 N  N      . ASP A 1 244 ? 206.912 122.880 201.374 1.00 54.91  ? 387 ASP A N      1 
ATOM   1625 C  CA     . ASP A 1 244 ? 208.275 123.328 201.638 1.00 55.49  ? 387 ASP A CA     1 
ATOM   1626 C  C      . ASP A 1 244 ? 209.095 123.469 200.360 1.00 54.99  ? 387 ASP A C      1 
ATOM   1627 O  O      . ASP A 1 244 ? 210.329 123.468 200.417 1.00 55.05  ? 387 ASP A O      1 
ATOM   1628 C  CB     . ASP A 1 244 ? 208.970 122.372 202.609 1.00 56.66  ? 387 ASP A CB     1 
ATOM   1629 C  CG     . ASP A 1 244 ? 209.026 120.951 202.085 1.00 67.18  ? 387 ASP A CG     1 
ATOM   1630 O  OD1    . ASP A 1 244 ? 208.103 120.554 201.344 1.00 67.82  ? 387 ASP A OD1    1 
ATOM   1631 O  OD2    . ASP A 1 244 ? 209.994 120.233 202.412 1.00 66.09  ? 387 ASP A OD2    1 
ATOM   1632 N  N      . LYS A 1 245 ? 208.439 123.589 199.209 1.00 54.60  ? 388 LYS A N      1 
ATOM   1633 C  CA     . LYS A 1 245 ? 209.136 123.763 197.944 1.00 50.77  ? 388 LYS A CA     1 
ATOM   1634 C  C      . LYS A 1 245 ? 208.219 124.479 196.965 1.00 50.58  ? 388 LYS A C      1 
ATOM   1635 O  O      . LYS A 1 245 ? 207.009 124.238 196.947 1.00 56.66  ? 388 LYS A O      1 
ATOM   1636 C  CB     . LYS A 1 245 ? 209.587 122.420 197.360 1.00 52.89  ? 388 LYS A CB     1 
ATOM   1637 C  CG     . LYS A 1 245 ? 210.890 121.899 197.939 1.00 57.10  ? 388 LYS A CG     1 
ATOM   1638 C  CD     . LYS A 1 245 ? 211.600 120.984 196.957 1.00 60.57  ? 388 LYS A CD     1 
ATOM   1639 C  CE     . LYS A 1 245 ? 212.551 120.041 197.673 1.00 65.38  ? 388 LYS A CE     1 
ATOM   1640 N  NZ     . LYS A 1 245 ? 213.199 120.695 198.843 1.00 62.97  ? 388 LYS A NZ     1 
ATOM   1641 N  N      . ILE A 1 246 ? 208.803 125.353 196.155 1.00 45.04  ? 389 ILE A N      1 
ATOM   1642 C  CA     . ILE A 1 246 ? 208.066 126.095 195.141 1.00 43.83  ? 389 ILE A CA     1 
ATOM   1643 C  C      . ILE A 1 246 ? 208.080 125.302 193.844 1.00 45.60  ? 389 ILE A C      1 
ATOM   1644 O  O      . ILE A 1 246 ? 209.137 124.854 193.383 1.00 51.18  ? 389 ILE A O      1 
ATOM   1645 C  CB     . ILE A 1 246 ? 208.664 127.501 194.946 1.00 39.57  ? 389 ILE A CB     1 
ATOM   1646 C  CG1    . ILE A 1 246 ? 208.991 128.132 196.300 1.00 37.11  ? 389 ILE A CG1    1 
ATOM   1647 C  CG2    . ILE A 1 246 ? 207.705 128.383 194.161 1.00 36.94  ? 389 ILE A CG2    1 
ATOM   1648 C  CD1    . ILE A 1 246 ? 209.583 129.519 196.202 1.00 31.73  ? 389 ILE A CD1    1 
ATOM   1649 N  N      . THR A 1 247 ? 206.905 125.124 193.253 1.00 44.78  ? 390 THR A N      1 
ATOM   1650 C  CA     . THR A 1 247 ? 206.741 124.346 192.034 1.00 50.15  ? 390 THR A CA     1 
ATOM   1651 C  C      . THR A 1 247 ? 206.505 125.267 190.844 1.00 47.73  ? 390 THR A C      1 
ATOM   1652 O  O      . THR A 1 247 ? 206.343 126.482 190.984 1.00 47.22  ? 390 THR A O      1 
ATOM   1653 C  CB     . THR A 1 247 ? 205.582 123.352 192.174 1.00 50.35  ? 390 THR A CB     1 
ATOM   1654 O  OG1    . THR A 1 247 ? 204.350 124.069 192.320 1.00 49.27  ? 390 THR A OG1    1 
ATOM   1655 C  CG2    . THR A 1 247 ? 205.788 122.461 193.388 1.00 48.78  ? 390 THR A CG2    1 
ATOM   1656 N  N      . MET A 1 248 ? 206.489 124.663 189.654 1.00 48.69  ? 391 MET A N      1 
ATOM   1657 C  CA     . MET A 1 248 ? 206.251 125.433 188.438 1.00 48.24  ? 391 MET A CA     1 
ATOM   1658 C  C      . MET A 1 248 ? 204.842 126.010 188.406 1.00 49.06  ? 391 MET A C      1 
ATOM   1659 O  O      . MET A 1 248 ? 204.635 127.108 187.878 1.00 47.06  ? 391 MET A O      1 
ATOM   1660 C  CB     . MET A 1 248 ? 206.496 124.560 187.208 1.00 49.30  ? 391 MET A CB     1 
ATOM   1661 C  CG     . MET A 1 248 ? 206.479 125.321 185.892 1.00 50.97  ? 391 MET A CG     1 
ATOM   1662 S  SD     . MET A 1 248 ? 207.915 126.390 185.681 1.00 64.03  ? 391 MET A SD     1 
ATOM   1663 C  CE     . MET A 1 248 ? 207.464 127.270 184.189 1.00 48.44  ? 391 MET A CE     1 
ATOM   1664 N  N      . LYS A 1 249 ? 203.865 125.291 188.961 1.00 49.97  ? 392 LYS A N      1 
ATOM   1665 C  CA     . LYS A 1 249 ? 202.495 125.788 188.996 1.00 50.72  ? 392 LYS A CA     1 
ATOM   1666 C  C      . LYS A 1 249 ? 202.359 127.051 189.836 1.00 50.91  ? 392 LYS A C      1 
ATOM   1667 O  O      . LYS A 1 249 ? 201.526 127.905 189.517 1.00 50.67  ? 392 LYS A O      1 
ATOM   1668 C  CB     . LYS A 1 249 ? 201.560 124.702 189.528 1.00 55.70  ? 392 LYS A CB     1 
ATOM   1669 C  CG     . LYS A 1 249 ? 200.087 124.955 189.257 1.00 59.16  ? 392 LYS A CG     1 
ATOM   1670 C  CD     . LYS A 1 249 ? 199.255 123.724 189.581 1.00 65.10  ? 392 LYS A CD     1 
ATOM   1671 C  CE     . LYS A 1 249 ? 197.891 124.104 190.133 1.00 73.34  ? 392 LYS A CE     1 
ATOM   1672 N  NZ     . LYS A 1 249 ? 197.981 124.611 191.530 1.00 75.35  ? 392 LYS A NZ     1 
ATOM   1673 N  N      . ASP A 1 250 ? 203.153 127.186 190.900 1.00 47.47  ? 393 ASP A N      1 
ATOM   1674 C  CA     . ASP A 1 250 ? 203.101 128.398 191.711 1.00 42.85  ? 393 ASP A CA     1 
ATOM   1675 C  C      . ASP A 1 250 ? 203.540 129.618 190.910 1.00 42.83  ? 393 ASP A C      1 
ATOM   1676 O  O      . ASP A 1 250 ? 202.933 130.690 191.019 1.00 43.74  ? 393 ASP A O      1 
ATOM   1677 C  CB     . ASP A 1 250 ? 203.972 128.233 192.956 1.00 42.12  ? 393 ASP A CB     1 
ATOM   1678 C  CG     . ASP A 1 250 ? 203.343 127.322 193.991 1.00 51.24  ? 393 ASP A CG     1 
ATOM   1679 O  OD1    . ASP A 1 250 ? 202.121 127.434 194.221 1.00 52.91  ? 393 ASP A OD1    1 
ATOM   1680 O  OD2    . ASP A 1 250 ? 204.072 126.494 194.577 1.00 51.43  ? 393 ASP A OD2    1 
ATOM   1681 N  N      . PHE A 1 251 ? 204.595 129.476 190.104 1.00 41.58  ? 394 PHE A N      1 
ATOM   1682 C  CA     . PHE A 1 251 ? 205.082 130.602 189.315 1.00 38.35  ? 394 PHE A CA     1 
ATOM   1683 C  C      . PHE A 1 251 ? 204.056 131.063 188.288 1.00 40.28  ? 394 PHE A C      1 
ATOM   1684 O  O      . PHE A 1 251 ? 203.867 132.270 188.102 1.00 40.02  ? 394 PHE A O      1 
ATOM   1685 C  CB     . PHE A 1 251 ? 206.392 130.230 188.619 1.00 36.08  ? 394 PHE A CB     1 
ATOM   1686 C  CG     . PHE A 1 251 ? 207.617 130.497 189.446 1.00 35.84  ? 394 PHE A CG     1 
ATOM   1687 C  CD1    . PHE A 1 251 ? 208.119 131.782 189.569 1.00 34.63  ? 394 PHE A CD1    1 
ATOM   1688 C  CD2    . PHE A 1 251 ? 208.268 129.464 190.098 1.00 34.87  ? 394 PHE A CD2    1 
ATOM   1689 C  CE1    . PHE A 1 251 ? 209.245 132.030 190.328 1.00 32.08  ? 394 PHE A CE1    1 
ATOM   1690 C  CE2    . PHE A 1 251 ? 209.394 129.707 190.858 1.00 34.65  ? 394 PHE A CE2    1 
ATOM   1691 C  CZ     . PHE A 1 251 ? 209.883 130.992 190.973 1.00 30.40  ? 394 PHE A CZ     1 
ATOM   1692 N  N      . GLU A 1 252 ? 203.385 130.125 187.615 1.00 42.71  ? 395 GLU A N      1 
ATOM   1693 C  CA     . GLU A 1 252 ? 202.437 130.495 186.570 1.00 42.63  ? 395 GLU A CA     1 
ATOM   1694 C  C      . GLU A 1 252 ? 201.197 131.180 187.130 1.00 41.91  ? 395 GLU A C      1 
ATOM   1695 O  O      . GLU A 1 252 ? 200.653 132.083 186.487 1.00 43.27  ? 395 GLU A O      1 
ATOM   1696 C  CB     . GLU A 1 252 ? 202.041 129.259 185.761 1.00 50.30  ? 395 GLU A CB     1 
ATOM   1697 C  CG     . GLU A 1 252 ? 203.155 128.726 184.873 1.00 53.93  ? 395 GLU A CG     1 
ATOM   1698 C  CD     . GLU A 1 252 ? 202.884 127.323 184.369 1.00 63.73  ? 395 GLU A CD     1 
ATOM   1699 O  OE1    . GLU A 1 252 ? 202.002 126.645 184.937 1.00 64.13  ? 395 GLU A OE1    1 
ATOM   1700 O  OE2    . GLU A 1 252 ? 203.554 126.897 183.405 1.00 64.67  ? 395 GLU A OE2    1 
ATOM   1701 N  N      . GLU A 1 253 ? 200.736 130.771 188.313 1.00 40.95  ? 396 GLU A N      1 
ATOM   1702 C  CA     . GLU A 1 253 ? 199.600 131.442 188.935 1.00 39.71  ? 396 GLU A CA     1 
ATOM   1703 C  C      . GLU A 1 253 ? 199.975 132.815 189.476 1.00 39.88  ? 396 GLU A C      1 
ATOM   1704 O  O      . GLU A 1 253 ? 199.118 133.702 189.548 1.00 44.09  ? 396 GLU A O      1 
ATOM   1705 C  CB     . GLU A 1 253 ? 199.024 130.579 190.058 1.00 43.99  ? 396 GLU A CB     1 
ATOM   1706 C  CG     . GLU A 1 253 ? 198.576 129.197 189.617 1.00 54.94  ? 396 GLU A CG     1 
ATOM   1707 C  CD     . GLU A 1 253 ? 197.799 128.466 190.695 1.00 68.99  ? 396 GLU A CD     1 
ATOM   1708 O  OE1    . GLU A 1 253 ? 197.909 128.857 191.877 1.00 69.43  ? 396 GLU A OE1    1 
ATOM   1709 O  OE2    . GLU A 1 253 ? 197.078 127.502 190.363 1.00 71.08  ? 396 GLU A OE2    1 
ATOM   1710 N  N      . ALA A 1 254 ? 201.239 133.008 189.860 1.00 37.64  ? 397 ALA A N      1 
ATOM   1711 C  CA     . ALA A 1 254 ? 201.670 134.306 190.366 1.00 32.54  ? 397 ALA A CA     1 
ATOM   1712 C  C      . ALA A 1 254 ? 201.609 135.381 189.289 1.00 33.58  ? 397 ALA A C      1 
ATOM   1713 O  O      . ALA A 1 254 ? 201.299 136.539 189.590 1.00 35.03  ? 397 ALA A O      1 
ATOM   1714 C  CB     . ALA A 1 254 ? 203.084 134.204 190.936 1.00 32.65  ? 397 ALA A CB     1 
ATOM   1715 N  N      . ILE A 1 255 ? 201.902 135.023 188.037 1.00 32.79  ? 398 ILE A N      1 
ATOM   1716 C  CA     . ILE A 1 255 ? 201.895 136.008 186.960 1.00 35.92  ? 398 ILE A CA     1 
ATOM   1717 C  C      . ILE A 1 255 ? 200.509 136.619 186.802 1.00 39.83  ? 398 ILE A C      1 
ATOM   1718 O  O      . ILE A 1 255 ? 200.365 137.835 186.632 1.00 42.43  ? 398 ILE A O      1 
ATOM   1719 C  CB     . ILE A 1 255 ? 202.385 135.369 185.647 1.00 33.95  ? 398 ILE A CB     1 
ATOM   1720 C  CG1    . ILE A 1 255 ? 203.809 134.834 185.811 1.00 32.28  ? 398 ILE A CG1    1 
ATOM   1721 C  CG2    . ILE A 1 255 ? 202.318 136.373 184.508 1.00 25.84  ? 398 ILE A CG2    1 
ATOM   1722 C  CD1    . ILE A 1 255 ? 204.362 134.176 184.566 1.00 30.07  ? 398 ILE A CD1    1 
ATOM   1723 N  N      . ASP A 1 256 ? 199.467 135.786 186.852 1.00 40.19  ? 399 ASP A N      1 
ATOM   1724 C  CA     . ASP A 1 256 ? 198.106 136.282 186.688 1.00 42.59  ? 399 ASP A CA     1 
ATOM   1725 C  C      . ASP A 1 256 ? 197.672 137.193 187.829 1.00 41.27  ? 399 ASP A C      1 
ATOM   1726 O  O      . ASP A 1 256 ? 196.811 138.054 187.623 1.00 44.81  ? 399 ASP A O      1 
ATOM   1727 C  CB     . ASP A 1 256 ? 197.132 135.109 186.567 1.00 46.35  ? 399 ASP A CB     1 
ATOM   1728 C  CG     . ASP A 1 256 ? 197.347 134.300 185.305 1.00 55.22  ? 399 ASP A CG     1 
ATOM   1729 O  OD1    . ASP A 1 256 ? 197.741 134.891 184.278 1.00 54.80  ? 399 ASP A OD1    1 
ATOM   1730 O  OD2    . ASP A 1 256 ? 197.125 133.072 185.340 1.00 57.13  ? 399 ASP A OD2    1 
ATOM   1731 N  N      . ARG A 1 257 ? 198.244 137.027 189.021 1.00 38.43  ? 400 ARG A N      1 
ATOM   1732 C  CA     . ARG A 1 257 ? 197.820 137.795 190.185 1.00 42.07  ? 400 ARG A CA     1 
ATOM   1733 C  C      . ARG A 1 257 ? 198.426 139.190 190.241 1.00 44.26  ? 400 ARG A C      1 
ATOM   1734 O  O      . ARG A 1 257 ? 197.838 140.085 190.860 1.00 49.83  ? 400 ARG A O      1 
ATOM   1735 C  CB     . ARG A 1 257 ? 198.176 137.041 191.470 1.00 40.33  ? 400 ARG A CB     1 
ATOM   1736 C  CG     . ARG A 1 257 ? 197.381 135.766 191.684 1.00 44.95  ? 400 ARG A CG     1 
ATOM   1737 C  CD     . ARG A 1 257 ? 197.877 135.008 192.903 1.00 49.25  ? 400 ARG A CD     1 
ATOM   1738 N  NE     . ARG A 1 257 ? 197.854 135.836 194.103 1.00 55.11  ? 400 ARG A NE     1 
ATOM   1739 C  CZ     . ARG A 1 257 ? 196.853 135.869 194.971 1.00 54.53  ? 400 ARG A CZ     1 
ATOM   1740 N  NH1    . ARG A 1 257 ? 195.770 135.126 194.806 1.00 50.73  ? 400 ARG A NH1    1 
ATOM   1741 N  NH2    . ARG A 1 257 ? 196.939 136.667 196.031 1.00 49.97  ? 400 ARG A NH2    1 
ATOM   1742 N  N      . VAL A 1 258 ? 199.586 139.404 189.613 1.00 41.06  ? 401 VAL A N      1 
ATOM   1743 C  CA     . VAL A 1 258 ? 200.276 140.688 189.717 1.00 41.41  ? 401 VAL A CA     1 
ATOM   1744 C  C      . VAL A 1 258 ? 199.931 141.651 188.591 1.00 42.80  ? 401 VAL A C      1 
ATOM   1745 O  O      . VAL A 1 258 ? 200.381 142.807 188.622 1.00 42.13  ? 401 VAL A O      1 
ATOM   1746 C  CB     . VAL A 1 258 ? 201.805 140.493 189.754 1.00 38.34  ? 401 VAL A CB     1 
ATOM   1747 C  CG1    . VAL A 1 258 ? 202.197 139.591 190.912 1.00 35.09  ? 401 VAL A CG1    1 
ATOM   1748 C  CG2    . VAL A 1 258 ? 202.300 139.923 188.435 1.00 34.39  ? 401 VAL A CG2    1 
ATOM   1749 N  N      . ILE A 1 259 ? 199.147 141.222 187.599 1.00 42.68  ? 402 ILE A N      1 
ATOM   1750 C  CA     . ILE A 1 259 ? 198.820 142.080 186.464 1.00 44.49  ? 402 ILE A CA     1 
ATOM   1751 C  C      . ILE A 1 259 ? 197.377 142.569 186.479 1.00 50.79  ? 402 ILE A C      1 
ATOM   1752 O  O      . ILE A 1 259 ? 196.991 143.341 185.587 1.00 55.62  ? 402 ILE A O      1 
ATOM   1753 C  CB     . ILE A 1 259 ? 199.107 141.369 185.124 1.00 40.12  ? 402 ILE A CB     1 
ATOM   1754 C  CG1    . ILE A 1 259 ? 198.260 140.101 184.997 1.00 41.32  ? 402 ILE A CG1    1 
ATOM   1755 C  CG2    . ILE A 1 259 ? 200.589 141.047 184.996 1.00 37.27  ? 402 ILE A CG2    1 
ATOM   1756 C  CD1    . ILE A 1 259 ? 198.408 139.401 183.665 1.00 39.66  ? 402 ILE A CD1    1 
ATOM   1757 N  N      . ALA A 1 260 ? 196.570 142.153 187.453 1.00 50.44  ? 403 ALA A N      1 
ATOM   1758 C  CA     . ALA A 1 260 ? 195.177 142.571 187.506 1.00 57.12  ? 403 ALA A CA     1 
ATOM   1759 C  C      . ALA A 1 260 ? 194.696 142.557 188.949 1.00 64.15  ? 403 ALA A C      1 
ATOM   1760 O  O      . ALA A 1 260 ? 195.282 141.903 189.815 1.00 65.11  ? 403 ALA A O      1 
ATOM   1761 C  CB     . ALA A 1 260 ? 194.287 141.674 186.637 1.00 56.49  ? 403 ALA A CB     1 
ATOM   1762 N  N      . GLY A 1 261 ? 193.616 143.295 189.195 1.00 62.92  ? 404 GLY A N      1 
ATOM   1763 C  CA     . GLY A 1 261 ? 193.001 143.336 190.500 1.00 63.62  ? 404 GLY A CA     1 
ATOM   1764 C  C      . GLY A 1 261 ? 193.065 144.709 191.135 1.00 64.54  ? 404 GLY A C      1 
ATOM   1765 O  O      . GLY A 1 261 ? 193.654 145.648 190.590 1.00 64.88  ? 404 GLY A O      1 
ATOM   1766 N  N      . PRO A 1 262 ? 192.448 144.854 192.311 1.00 66.74  ? 405 PRO A N      1 
ATOM   1767 C  CA     . PRO A 1 262 ? 192.515 146.143 193.017 1.00 66.25  ? 405 PRO A CA     1 
ATOM   1768 C  C      . PRO A 1 262 ? 193.925 146.545 193.407 1.00 67.51  ? 405 PRO A C      1 
ATOM   1769 O  O      . PRO A 1 262 ? 194.171 147.736 193.629 1.00 67.77  ? 405 PRO A O      1 
ATOM   1770 C  CB     . PRO A 1 262 ? 191.638 145.917 194.258 1.00 59.73  ? 405 PRO A CB     1 
ATOM   1771 C  CG     . PRO A 1 262 ? 190.789 144.731 193.927 1.00 60.05  ? 405 PRO A CG     1 
ATOM   1772 C  CD     . PRO A 1 262 ? 191.613 143.873 193.022 1.00 65.51  ? 405 PRO A CD     1 
ATOM   1773 N  N      . ALA A 1 263 ? 194.857 145.592 193.501 1.00 69.03  ? 406 ALA A N      1 
ATOM   1774 C  CA     . ALA A 1 263 ? 196.256 145.867 193.833 1.00 71.08  ? 406 ALA A CA     1 
ATOM   1775 C  C      . ALA A 1 263 ? 197.126 145.186 192.777 1.00 72.31  ? 406 ALA A C      1 
ATOM   1776 O  O      . ALA A 1 263 ? 197.565 144.047 192.952 1.00 72.40  ? 406 ALA A O      1 
ATOM   1777 C  CB     . ALA A 1 263 ? 196.590 145.391 195.247 1.00 70.57  ? 406 ALA A CB     1 
ATOM   1778 N  N      . ARG A 1 264 ? 197.372 145.893 191.678 1.00 70.40  ? 407 ARG A N      1 
ATOM   1779 C  CA     . ARG A 1 264 ? 198.209 145.406 190.593 1.00 63.79  ? 407 ARG A CA     1 
ATOM   1780 C  C      . ARG A 1 264 ? 199.518 146.183 190.566 1.00 63.36  ? 407 ARG A C      1 
ATOM   1781 O  O      . ARG A 1 264 ? 199.564 147.367 190.910 1.00 64.28  ? 407 ARG A O      1 
ATOM   1782 C  CB     . ARG A 1 264 ? 197.494 145.530 189.245 1.00 60.38  ? 407 ARG A CB     1 
ATOM   1783 C  CG     . ARG A 1 264 ? 197.053 146.942 188.904 1.00 62.84  ? 407 ARG A CG     1 
ATOM   1784 C  CD     . ARG A 1 264 ? 196.546 147.029 187.475 1.00 61.95  ? 407 ARG A CD     1 
ATOM   1785 N  NE     . ARG A 1 264 ? 195.569 148.099 187.308 1.00 65.72  ? 407 ARG A NE     1 
ATOM   1786 C  CZ     . ARG A 1 264 ? 195.864 149.324 186.896 1.00 65.57  ? 407 ARG A CZ     1 
ATOM   1787 N  NH1    . ARG A 1 264 ? 197.105 149.672 186.596 1.00 61.88  ? 407 ARG A NH1    1 
ATOM   1788 N  NH2    . ARG A 1 264 ? 194.891 150.222 186.783 1.00 63.67  ? 407 ARG A NH2    1 
ATOM   1789 N  N      . LYS A 1 265 ? 200.590 145.502 190.154 1.00 57.02  ? 408 LYS A N      1 
ATOM   1790 C  CA     . LYS A 1 265 ? 201.927 146.073 190.207 1.00 50.61  ? 408 LYS A CA     1 
ATOM   1791 C  C      . LYS A 1 265 ? 202.643 146.151 188.867 1.00 49.91  ? 408 LYS A C      1 
ATOM   1792 O  O      . LYS A 1 265 ? 203.517 147.010 188.713 1.00 52.85  ? 408 LYS A O      1 
ATOM   1793 C  CB     . LYS A 1 265 ? 202.812 145.271 191.176 1.00 50.21  ? 408 LYS A CB     1 
ATOM   1794 C  CG     . LYS A 1 265 ? 202.297 145.217 192.605 1.00 53.39  ? 408 LYS A CG     1 
ATOM   1795 C  CD     . LYS A 1 265 ? 202.314 146.590 193.253 1.00 59.10  ? 408 LYS A CD     1 
ATOM   1796 C  CE     . LYS A 1 265 ? 201.980 146.503 194.734 1.00 63.77  ? 408 LYS A CE     1 
ATOM   1797 N  NZ     . LYS A 1 265 ? 200.521 146.326 194.969 1.00 63.17  ? 408 LYS A NZ     1 
ATOM   1798 N  N      . SER A 1 266 ? 202.308 145.299 187.900 1.00 46.14  ? 409 SER A N      1 
ATOM   1799 C  CA     . SER A 1 266 ? 203.129 145.151 186.708 1.00 39.43  ? 409 SER A CA     1 
ATOM   1800 C  C      . SER A 1 266 ? 202.267 145.198 185.455 1.00 39.85  ? 409 SER A C      1 
ATOM   1801 O  O      . SER A 1 266 ? 201.053 144.982 185.497 1.00 43.46  ? 409 SER A O      1 
ATOM   1802 C  CB     . SER A 1 266 ? 203.928 143.842 186.744 1.00 39.51  ? 409 SER A CB     1 
ATOM   1803 O  OG     . SER A 1 266 ? 204.683 143.740 187.937 1.00 42.25  ? 409 SER A OG     1 
ATOM   1804 N  N      . LEU A 1 267 ? 202.923 145.488 184.333 1.00 38.55  ? 410 LEU A N      1 
ATOM   1805 C  CA     . LEU A 1 267 ? 202.307 145.488 183.014 1.00 36.79  ? 410 LEU A CA     1 
ATOM   1806 C  C      . LEU A 1 267 ? 203.181 144.676 182.070 1.00 35.73  ? 410 LEU A C      1 
ATOM   1807 O  O      . LEU A 1 267 ? 204.407 144.820 182.081 1.00 39.86  ? 410 LEU A O      1 
ATOM   1808 C  CB     . LEU A 1 267 ? 202.133 146.913 182.478 1.00 37.89  ? 410 LEU A CB     1 
ATOM   1809 C  CG     . LEU A 1 267 ? 200.727 147.515 182.477 1.00 41.87  ? 410 LEU A CG     1 
ATOM   1810 C  CD1    . LEU A 1 267 ? 200.090 147.406 183.850 1.00 45.14  ? 410 LEU A CD1    1 
ATOM   1811 C  CD2    . LEU A 1 267 ? 200.772 148.962 182.020 1.00 30.40  ? 410 LEU A CD2    1 
ATOM   1812 N  N      . LEU A 1 268 ? 202.556 143.830 181.257 1.00 34.15  ? 411 LEU A N      1 
ATOM   1813 C  CA     . LEU A 1 268 ? 203.271 143.008 180.294 1.00 34.09  ? 411 LEU A CA     1 
ATOM   1814 C  C      . LEU A 1 268 ? 202.665 143.182 178.908 1.00 34.83  ? 411 LEU A C      1 
ATOM   1815 O  O      . LEU A 1 268 ? 201.547 143.680 178.751 1.00 40.23  ? 411 LEU A O      1 
ATOM   1816 C  CB     . LEU A 1 268 ? 203.257 141.527 180.700 1.00 34.36  ? 411 LEU A CB     1 
ATOM   1817 C  CG     . LEU A 1 268 ? 201.907 140.814 180.789 1.00 32.23  ? 411 LEU A CG     1 
ATOM   1818 C  CD1    . LEU A 1 268 ? 201.501 140.249 179.438 1.00 30.86  ? 411 LEU A CD1    1 
ATOM   1819 C  CD2    . LEU A 1 268 ? 201.957 139.714 181.835 1.00 36.61  ? 411 LEU A CD2    1 
ATOM   1820 N  N      . ILE A 1 269 ? 203.422 142.764 177.899 1.00 30.94  ? 412 ILE A N      1 
ATOM   1821 C  CA     . ILE A 1 269 ? 203.011 142.895 176.506 1.00 33.16  ? 412 ILE A CA     1 
ATOM   1822 C  C      . ILE A 1 269 ? 202.219 141.655 176.113 1.00 33.20  ? 412 ILE A C      1 
ATOM   1823 O  O      . ILE A 1 269 ? 202.715 140.529 176.222 1.00 34.66  ? 412 ILE A O      1 
ATOM   1824 C  CB     . ILE A 1 269 ? 204.225 143.089 175.585 1.00 31.06  ? 412 ILE A CB     1 
ATOM   1825 C  CG1    . ILE A 1 269 ? 205.098 144.239 176.093 1.00 26.34  ? 412 ILE A CG1    1 
ATOM   1826 C  CG2    . ILE A 1 269 ? 203.774 143.351 174.159 1.00 28.33  ? 412 ILE A CG2    1 
ATOM   1827 C  CD1    . ILE A 1 269 ? 206.414 144.378 175.362 1.00 21.05  ? 412 ILE A CD1    1 
ATOM   1828 N  N      . SER A 1 270 ? 200.988 141.862 175.657 1.00 35.01  ? 413 SER A N      1 
ATOM   1829 C  CA     . SER A 1 270 ? 200.128 140.765 175.250 1.00 36.22  ? 413 SER A CA     1 
ATOM   1830 C  C      . SER A 1 270 ? 200.458 140.315 173.830 1.00 37.35  ? 413 SER A C      1 
ATOM   1831 O  O      . SER A 1 270 ? 201.105 141.039 173.070 1.00 37.37  ? 413 SER A O      1 
ATOM   1832 C  CB     . SER A 1 270 ? 198.664 141.181 175.341 1.00 37.24  ? 413 SER A CB     1 
ATOM   1833 O  OG     . SER A 1 270 ? 198.335 142.112 174.325 1.00 38.74  ? 413 SER A OG     1 
ATOM   1834 N  N      . PRO A 1 271 ? 200.024 139.112 173.449 1.00 42.83  ? 414 PRO A N      1 
ATOM   1835 C  CA     . PRO A 1 271 ? 200.313 138.631 172.088 1.00 39.88  ? 414 PRO A CA     1 
ATOM   1836 C  C      . PRO A 1 271 ? 199.780 139.542 170.999 1.00 37.29  ? 414 PRO A C      1 
ATOM   1837 O  O      . PRO A 1 271 ? 200.409 139.660 169.940 1.00 35.13  ? 414 PRO A O      1 
ATOM   1838 C  CB     . PRO A 1 271 ? 199.635 137.254 172.055 1.00 38.07  ? 414 PRO A CB     1 
ATOM   1839 C  CG     . PRO A 1 271 ? 199.544 136.840 173.488 1.00 39.60  ? 414 PRO A CG     1 
ATOM   1840 C  CD     . PRO A 1 271 ? 199.317 138.105 174.257 1.00 41.94  ? 414 PRO A CD     1 
ATOM   1841 N  N      . ALA A 1 272 ? 198.635 140.190 171.219 1.00 37.52  ? 415 ALA A N      1 
ATOM   1842 C  CA     . ALA A 1 272 ? 198.085 141.087 170.211 1.00 35.23  ? 415 ALA A CA     1 
ATOM   1843 C  C      . ALA A 1 272 ? 198.917 142.352 170.054 1.00 36.99  ? 415 ALA A C      1 
ATOM   1844 O  O      . ALA A 1 272 ? 199.131 142.811 168.926 1.00 36.85  ? 415 ALA A O      1 
ATOM   1845 C  CB     . ALA A 1 272 ? 196.641 141.450 170.560 1.00 34.70  ? 415 ALA A CB     1 
ATOM   1846 N  N      . GLU A 1 273 ? 199.389 142.930 171.161 1.00 35.98  ? 416 GLU A N      1 
ATOM   1847 C  CA     . GLU A 1 273 ? 200.226 144.121 171.081 1.00 32.37  ? 416 GLU A CA     1 
ATOM   1848 C  C      . GLU A 1 273 ? 201.597 143.825 170.490 1.00 30.53  ? 416 GLU A C      1 
ATOM   1849 O  O      . GLU A 1 273 ? 202.225 144.730 169.931 1.00 30.96  ? 416 GLU A O      1 
ATOM   1850 C  CB     . GLU A 1 273 ? 200.383 144.749 172.467 1.00 33.80  ? 416 GLU A CB     1 
ATOM   1851 C  CG     . GLU A 1 273 ? 199.100 145.321 173.044 1.00 42.06  ? 416 GLU A CG     1 
ATOM   1852 C  CD     . GLU A 1 273 ? 199.256 145.769 174.484 1.00 46.88  ? 416 GLU A CD     1 
ATOM   1853 O  OE1    . GLU A 1 273 ? 199.849 145.014 175.283 1.00 42.09  ? 416 GLU A OE1    1 
ATOM   1854 O  OE2    . GLU A 1 273 ? 198.785 146.876 174.819 1.00 47.11  ? 416 GLU A OE2    1 
ATOM   1855 N  N      . LYS A 1 274 ? 202.072 142.584 170.599 1.00 30.29  ? 417 LYS A N      1 
ATOM   1856 C  CA     . LYS A 1 274 ? 203.383 142.223 170.077 1.00 27.91  ? 417 LYS A CA     1 
ATOM   1857 C  C      . LYS A 1 274 ? 203.446 142.268 168.556 1.00 29.66  ? 417 LYS A C      1 
ATOM   1858 O  O      . LYS A 1 274 ? 204.500 142.602 168.004 1.00 31.64  ? 417 LYS A O      1 
ATOM   1859 C  CB     . LYS A 1 274 ? 203.775 140.828 170.567 1.00 29.11  ? 417 LYS A CB     1 
ATOM   1860 C  CG     . LYS A 1 274 ? 205.273 140.587 170.629 1.00 34.32  ? 417 LYS A CG     1 
ATOM   1861 C  CD     . LYS A 1 274 ? 205.585 139.154 171.026 1.00 35.08  ? 417 LYS A CD     1 
ATOM   1862 C  CE     . LYS A 1 274 ? 205.327 138.925 172.505 1.00 33.54  ? 417 LYS A CE     1 
ATOM   1863 N  NZ     . LYS A 1 274 ? 205.954 137.664 172.987 1.00 36.63  ? 417 LYS A NZ     1 
ATOM   1864 N  N      . ARG A 1 275 ? 202.350 141.941 167.868 1.00 29.51  ? 418 ARG A N      1 
ATOM   1865 C  CA     . ARG A 1 275 ? 202.360 141.974 166.409 1.00 27.06  ? 418 ARG A CA     1 
ATOM   1866 C  C      . ARG A 1 275 ? 202.494 143.399 165.887 1.00 26.03  ? 418 ARG A C      1 
ATOM   1867 O  O      . ARG A 1 275 ? 203.210 143.643 164.909 1.00 26.76  ? 418 ARG A O      1 
ATOM   1868 C  CB     . ARG A 1 275 ? 201.094 141.317 165.861 1.00 35.06  ? 418 ARG A CB     1 
ATOM   1869 C  CG     . ARG A 1 275 ? 201.319 139.934 165.276 1.00 44.45  ? 418 ARG A CG     1 
ATOM   1870 C  CD     . ARG A 1 275 ? 200.027 139.349 164.729 1.00 48.25  ? 418 ARG A CD     1 
ATOM   1871 N  NE     . ARG A 1 275 ? 199.882 139.588 163.298 1.00 51.10  ? 418 ARG A NE     1 
ATOM   1872 C  CZ     . ARG A 1 275 ? 200.443 138.845 162.354 1.00 55.82  ? 418 ARG A CZ     1 
ATOM   1873 N  NH1    . ARG A 1 275 ? 201.198 137.800 162.654 1.00 54.32  ? 418 ARG A NH1    1 
ATOM   1874 N  NH2    . ARG A 1 275 ? 200.241 139.157 161.077 1.00 52.49  ? 418 ARG A NH2    1 
ATOM   1875 N  N      . ILE A 1 276 ? 201.810 144.352 166.522 1.00 25.19  ? 419 ILE A N      1 
ATOM   1876 C  CA     . ILE A 1 276 ? 201.897 145.742 166.086 1.00 24.31  ? 419 ILE A CA     1 
ATOM   1877 C  C      . ILE A 1 276 ? 203.312 146.275 166.274 1.00 25.36  ? 419 ILE A C      1 
ATOM   1878 O  O      . ILE A 1 276 ? 203.844 146.980 165.408 1.00 27.73  ? 419 ILE A O      1 
ATOM   1879 C  CB     . ILE A 1 276 ? 200.863 146.602 166.834 1.00 26.70  ? 419 ILE A CB     1 
ATOM   1880 C  CG1    . ILE A 1 276 ? 199.594 145.795 167.108 1.00 32.47  ? 419 ILE A CG1    1 
ATOM   1881 C  CG2    . ILE A 1 276 ? 200.537 147.854 166.036 1.00 25.17  ? 419 ILE A CG2    1 
ATOM   1882 C  CD1    . ILE A 1 276 ? 198.724 145.593 165.890 1.00 33.44  ? 419 ILE A CD1    1 
ATOM   1883 N  N      . ILE A 1 277 ? 203.942 145.954 167.406 1.00 21.99  ? 420 ILE A N      1 
ATOM   1884 C  CA     . ILE A 1 277 ? 205.293 146.438 167.666 1.00 20.36  ? 420 ILE A CA     1 
ATOM   1885 C  C      . ILE A 1 277 ? 206.291 145.809 166.703 1.00 21.85  ? 420 ILE A C      1 
ATOM   1886 O  O      . ILE A 1 277 ? 207.239 146.471 166.262 1.00 23.20  ? 420 ILE A O      1 
ATOM   1887 C  CB     . ILE A 1 277 ? 205.680 146.174 169.132 1.00 24.55  ? 420 ILE A CB     1 
ATOM   1888 C  CG1    . ILE A 1 277 ? 204.858 147.060 170.069 1.00 22.31  ? 420 ILE A CG1    1 
ATOM   1889 C  CG2    . ILE A 1 277 ? 207.169 146.404 169.342 1.00 23.46  ? 420 ILE A CG2    1 
ATOM   1890 C  CD1    . ILE A 1 277 ? 204.807 146.563 171.496 1.00 17.37  ? 420 ILE A CD1    1 
ATOM   1891 N  N      . ALA A 1 278 ? 206.106 144.532 166.362 1.00 22.55  ? 421 ALA A N      1 
ATOM   1892 C  CA     . ALA A 1 278 ? 207.030 143.871 165.447 1.00 19.37  ? 421 ALA A CA     1 
ATOM   1893 C  C      . ALA A 1 278 ? 207.000 144.513 164.066 1.00 20.01  ? 421 ALA A C      1 
ATOM   1894 O  O      . ALA A 1 278 ? 208.046 144.674 163.428 1.00 22.47  ? 421 ALA A O      1 
ATOM   1895 C  CB     . ALA A 1 278 ? 206.702 142.381 165.356 1.00 20.48  ? 421 ALA A CB     1 
ATOM   1896 N  N      . TYR A 1 279 ? 205.811 144.880 163.583 1.00 19.67  ? 422 TYR A N      1 
ATOM   1897 C  CA     . TYR A 1 279 ? 205.715 145.528 162.280 1.00 19.82  ? 422 TYR A CA     1 
ATOM   1898 C  C      . TYR A 1 279 ? 206.343 146.916 162.293 1.00 19.56  ? 422 TYR A C      1 
ATOM   1899 O  O      . TYR A 1 279 ? 206.957 147.325 161.303 1.00 22.61  ? 422 TYR A O      1 
ATOM   1900 C  CB     . TYR A 1 279 ? 204.254 145.611 161.838 1.00 22.19  ? 422 TYR A CB     1 
ATOM   1901 C  CG     . TYR A 1 279 ? 203.804 144.435 161.003 1.00 23.14  ? 422 TYR A CG     1 
ATOM   1902 C  CD1    . TYR A 1 279 ? 204.103 144.366 159.649 1.00 23.51  ? 422 TYR A CD1    1 
ATOM   1903 C  CD2    . TYR A 1 279 ? 203.082 143.393 161.568 1.00 24.59  ? 422 TYR A CD2    1 
ATOM   1904 C  CE1    . TYR A 1 279 ? 203.695 143.292 158.882 1.00 26.68  ? 422 TYR A CE1    1 
ATOM   1905 C  CE2    . TYR A 1 279 ? 202.670 142.316 160.809 1.00 24.83  ? 422 TYR A CE2    1 
ATOM   1906 C  CZ     . TYR A 1 279 ? 202.979 142.270 159.467 1.00 30.08  ? 422 TYR A CZ     1 
ATOM   1907 O  OH     . TYR A 1 279 ? 202.570 141.199 158.708 1.00 32.68  ? 422 TYR A OH     1 
ATOM   1908 N  N      . HIS A 1 280 ? 206.197 147.651 163.398 1.00 21.21  ? 423 HIS A N      1 
ATOM   1909 C  CA     . HIS A 1 280 ? 206.780 148.985 163.486 1.00 19.34  ? 423 HIS A CA     1 
ATOM   1910 C  C      . HIS A 1 280 ? 208.301 148.933 163.409 1.00 22.30  ? 423 HIS A C      1 
ATOM   1911 O  O      . HIS A 1 280 ? 208.919 149.725 162.688 1.00 22.01  ? 423 HIS A O      1 
ATOM   1912 C  CB     . HIS A 1 280 ? 206.328 149.662 164.779 1.00 19.91  ? 423 HIS A CB     1 
ATOM   1913 C  CG     . HIS A 1 280 ? 206.763 151.089 164.904 1.00 23.51  ? 423 HIS A CG     1 
ATOM   1914 N  ND1    . HIS A 1 280 ? 205.883 152.146 164.815 1.00 25.99  ? 423 HIS A ND1    1 
ATOM   1915 C  CD2    . HIS A 1 280 ? 207.983 151.634 165.120 1.00 24.85  ? 423 HIS A CD2    1 
ATOM   1916 C  CE1    . HIS A 1 280 ? 206.543 153.280 164.965 1.00 23.21  ? 423 HIS A CE1    1 
ATOM   1917 N  NE2    . HIS A 1 280 ? 207.819 152.997 165.151 1.00 24.89  ? 423 HIS A NE2    1 
ATOM   1918 N  N      . GLU A 1 281 ? 208.923 148.008 164.144 1.00 20.28  ? 424 GLU A N      1 
ATOM   1919 C  CA     . GLU A 1 281 ? 210.379 147.916 164.137 1.00 19.49  ? 424 GLU A CA     1 
ATOM   1920 C  C      . GLU A 1 281 ? 210.899 147.437 162.788 1.00 21.20  ? 424 GLU A C      1 
ATOM   1921 O  O      . GLU A 1 281 ? 211.928 147.922 162.306 1.00 25.15  ? 424 GLU A O      1 
ATOM   1922 C  CB     . GLU A 1 281 ? 210.852 146.990 165.257 1.00 18.78  ? 424 GLU A CB     1 
ATOM   1923 C  CG     . GLU A 1 281 ? 210.614 147.534 166.656 1.00 25.79  ? 424 GLU A CG     1 
ATOM   1924 C  CD     . GLU A 1 281 ? 210.969 149.004 166.781 1.00 35.83  ? 424 GLU A CD     1 
ATOM   1925 O  OE1    . GLU A 1 281 ? 212.122 149.367 166.468 1.00 37.80  ? 424 GLU A OE1    1 
ATOM   1926 O  OE2    . GLU A 1 281 ? 210.096 149.796 167.193 1.00 38.20  ? 424 GLU A OE2    1 
ATOM   1927 N  N      . ALA A 1 282 ? 210.204 146.482 162.165 1.00 19.91  ? 425 ALA A N      1 
ATOM   1928 C  CA     . ALA A 1 282 ? 210.632 145.976 160.867 1.00 18.45  ? 425 ALA A CA     1 
ATOM   1929 C  C      . ALA A 1 282 ? 210.496 147.016 159.764 1.00 21.10  ? 425 ALA A C      1 
ATOM   1930 O  O      . ALA A 1 282 ? 211.218 146.939 158.765 1.00 24.33  ? 425 ALA A O      1 
ATOM   1931 C  CB     . ALA A 1 282 ? 209.837 144.722 160.502 1.00 20.29  ? 425 ALA A CB     1 
ATOM   1932 N  N      . GLY A 1 283 ? 209.588 147.980 159.918 1.00 19.37  ? 426 GLY A N      1 
ATOM   1933 C  CA     . GLY A 1 283 ? 209.444 149.013 158.906 1.00 17.44  ? 426 GLY A CA     1 
ATOM   1934 C  C      . GLY A 1 283 ? 210.660 149.914 158.809 1.00 19.46  ? 426 GLY A C      1 
ATOM   1935 O  O      . GLY A 1 283 ? 211.041 150.341 157.716 1.00 21.20  ? 426 GLY A O      1 
ATOM   1936 N  N      . HIS A 1 284 ? 211.281 150.225 159.949 1.00 19.77  ? 427 HIS A N      1 
ATOM   1937 C  CA     . HIS A 1 284 ? 212.481 151.054 159.933 1.00 19.38  ? 427 HIS A CA     1 
ATOM   1938 C  C      . HIS A 1 284 ? 213.614 150.370 159.177 1.00 21.76  ? 427 HIS A C      1 
ATOM   1939 O  O      . HIS A 1 284 ? 214.325 151.011 158.395 1.00 25.52  ? 427 HIS A O      1 
ATOM   1940 C  CB     . HIS A 1 284 ? 212.915 151.379 161.363 1.00 19.39  ? 427 HIS A CB     1 
ATOM   1941 C  CG     . HIS A 1 284 ? 212.135 152.489 161.996 1.00 21.48  ? 427 HIS A CG     1 
ATOM   1942 N  ND1    . HIS A 1 284 ? 212.026 153.740 161.429 1.00 22.64  ? 427 HIS A ND1    1 
ATOM   1943 C  CD2    . HIS A 1 284 ? 211.431 152.537 163.151 1.00 20.68  ? 427 HIS A CD2    1 
ATOM   1944 C  CE1    . HIS A 1 284 ? 211.287 154.510 162.207 1.00 20.38  ? 427 HIS A CE1    1 
ATOM   1945 N  NE2    . HIS A 1 284 ? 210.913 153.804 163.258 1.00 21.08  ? 427 HIS A NE2    1 
ATOM   1946 N  N      . ALA A 1 285 ? 213.798 149.067 159.399 1.00 21.19  ? 428 ALA A N      1 
ATOM   1947 C  CA     . ALA A 1 285 ? 214.908 148.350 158.783 1.00 23.01  ? 428 ALA A CA     1 
ATOM   1948 C  C      . ALA A 1 285 ? 214.720 148.163 157.283 1.00 25.01  ? 428 ALA A C      1 
ATOM   1949 O  O      . ALA A 1 285 ? 215.700 148.219 156.532 1.00 28.14  ? 428 ALA A O      1 
ATOM   1950 C  CB     . ALA A 1 285 ? 215.093 146.991 159.458 1.00 21.27  ? 428 ALA A CB     1 
ATOM   1951 N  N      . VAL A 1 286 ? 213.486 147.938 156.829 1.00 23.41  ? 429 VAL A N      1 
ATOM   1952 C  CA     . VAL A 1 286 ? 213.256 147.701 155.407 1.00 23.09  ? 429 VAL A CA     1 
ATOM   1953 C  C      . VAL A 1 286 ? 213.498 148.972 154.602 1.00 22.57  ? 429 VAL A C      1 
ATOM   1954 O  O      . VAL A 1 286 ? 214.139 148.941 153.545 1.00 25.36  ? 429 VAL A O      1 
ATOM   1955 C  CB     . VAL A 1 286 ? 211.837 147.149 155.180 1.00 24.06  ? 429 VAL A CB     1 
ATOM   1956 C  CG1    . VAL A 1 286 ? 211.444 147.279 153.718 1.00 22.20  ? 429 VAL A CG1    1 
ATOM   1957 C  CG2    . VAL A 1 286 ? 211.753 145.702 155.631 1.00 22.43  ? 429 VAL A CG2    1 
ATOM   1958 N  N      . VAL A 1 287 ? 212.995 150.109 155.086 1.00 21.77  ? 430 VAL A N      1 
ATOM   1959 C  CA     . VAL A 1 287 ? 213.136 151.357 154.341 1.00 21.79  ? 430 VAL A CA     1 
ATOM   1960 C  C      . VAL A 1 287 ? 214.593 151.800 154.299 1.00 23.37  ? 430 VAL A C      1 
ATOM   1961 O  O      . VAL A 1 287 ? 215.095 152.224 153.251 1.00 27.24  ? 430 VAL A O      1 
ATOM   1962 C  CB     . VAL A 1 287 ? 212.228 152.444 154.943 1.00 19.21  ? 430 VAL A CB     1 
ATOM   1963 C  CG1    . VAL A 1 287 ? 212.472 153.778 154.259 1.00 15.41  ? 430 VAL A CG1    1 
ATOM   1964 C  CG2    . VAL A 1 287 ? 210.769 152.043 154.818 1.00 19.55  ? 430 VAL A CG2    1 
ATOM   1965 N  N      . SER A 1 288 ? 215.296 151.709 155.430 1.00 22.96  ? 431 SER A N      1 
ATOM   1966 C  CA     . SER A 1 288 ? 216.686 152.146 155.473 1.00 25.52  ? 431 SER A CA     1 
ATOM   1967 C  C      . SER A 1 288 ? 217.598 151.261 154.634 1.00 27.23  ? 431 SER A C      1 
ATOM   1968 O  O      . SER A 1 288 ? 218.688 151.701 154.256 1.00 32.74  ? 431 SER A O      1 
ATOM   1969 C  CB     . SER A 1 288 ? 217.184 152.184 156.918 1.00 23.91  ? 431 SER A CB     1 
ATOM   1970 O  OG     . SER A 1 288 ? 217.743 150.940 157.299 1.00 34.21  ? 431 SER A OG     1 
ATOM   1971 N  N      . THR A 1 289 ? 217.181 150.030 154.337 1.00 26.55  ? 432 THR A N      1 
ATOM   1972 C  CA     . THR A 1 289 ? 217.984 149.140 153.509 1.00 26.82  ? 432 THR A CA     1 
ATOM   1973 C  C      . THR A 1 289 ? 217.794 149.390 152.019 1.00 29.28  ? 432 THR A C      1 
ATOM   1974 O  O      . THR A 1 289 ? 218.575 148.873 151.214 1.00 34.03  ? 432 THR A O      1 
ATOM   1975 C  CB     . THR A 1 289 ? 217.651 147.680 153.830 1.00 28.64  ? 432 THR A CB     1 
ATOM   1976 O  OG1    . THR A 1 289 ? 217.796 147.453 155.237 1.00 35.87  ? 432 THR A OG1    1 
ATOM   1977 C  CG2    . THR A 1 289 ? 218.580 146.740 153.077 1.00 25.99  ? 432 THR A CG2    1 
ATOM   1978 N  N      . VAL A 1 290 ? 216.788 150.173 151.633 1.00 29.03  ? 433 VAL A N      1 
ATOM   1979 C  CA     . VAL A 1 290 ? 216.473 150.381 150.224 1.00 27.50  ? 433 VAL A CA     1 
ATOM   1980 C  C      . VAL A 1 290 ? 217.049 151.707 149.746 1.00 32.74  ? 433 VAL A C      1 
ATOM   1981 O  O      . VAL A 1 290 ? 217.576 151.799 148.632 1.00 39.10  ? 433 VAL A O      1 
ATOM   1982 C  CB     . VAL A 1 290 ? 214.954 150.322 149.982 1.00 28.51  ? 433 VAL A CB     1 
ATOM   1983 C  CG1    . VAL A 1 290 ? 214.604 150.960 148.648 1.00 24.31  ? 433 VAL A CG1    1 
ATOM   1984 C  CG2    . VAL A 1 290 ? 214.464 148.884 150.034 1.00 24.86  ? 433 VAL A CG2    1 
ATOM   1985 N  N      . VAL A 1 291 ? 216.957 152.740 150.577 1.00 32.02  ? 434 VAL A N      1 
ATOM   1986 C  CA     . VAL A 1 291 ? 217.438 154.068 150.201 1.00 37.51  ? 434 VAL A CA     1 
ATOM   1987 C  C      . VAL A 1 291 ? 218.951 154.018 150.025 1.00 41.49  ? 434 VAL A C      1 
ATOM   1988 O  O      . VAL A 1 291 ? 219.651 153.395 150.837 1.00 42.34  ? 434 VAL A O      1 
ATOM   1989 C  CB     . VAL A 1 291 ? 217.032 155.128 151.237 1.00 37.17  ? 434 VAL A CB     1 
ATOM   1990 C  CG1    . VAL A 1 291 ? 215.532 155.374 151.181 1.00 28.48  ? 434 VAL A CG1    1 
ATOM   1991 C  CG2    . VAL A 1 291 ? 217.458 154.701 152.632 1.00 37.76  ? 434 VAL A CG2    1 
ATOM   1992 N  N      . PRO A 1 292 ? 219.497 154.650 148.982 1.00 42.69  ? 435 PRO A N      1 
ATOM   1993 C  CA     . PRO A 1 292 ? 220.951 154.562 148.762 1.00 43.87  ? 435 PRO A CA     1 
ATOM   1994 C  C      . PRO A 1 292 ? 221.776 155.145 149.896 1.00 44.31  ? 435 PRO A C      1 
ATOM   1995 O  O      . PRO A 1 292 ? 222.869 154.640 150.179 1.00 46.31  ? 435 PRO A O      1 
ATOM   1996 C  CB     . PRO A 1 292 ? 221.154 155.335 147.451 1.00 39.68  ? 435 PRO A CB     1 
ATOM   1997 C  CG     . PRO A 1 292 ? 219.964 156.227 147.339 1.00 45.95  ? 435 PRO A CG     1 
ATOM   1998 C  CD     . PRO A 1 292 ? 218.827 155.494 147.979 1.00 43.20  ? 435 PRO A CD     1 
ATOM   1999 N  N      . ASN A 1 293 ? 221.290 156.195 150.552 1.00 45.78  ? 436 ASN A N      1 
ATOM   2000 C  CA     . ASN A 1 293 ? 222.043 156.880 151.594 1.00 45.56  ? 436 ASN A CA     1 
ATOM   2001 C  C      . ASN A 1 293 ? 221.696 156.395 152.997 1.00 48.93  ? 436 ASN A C      1 
ATOM   2002 O  O      . ASN A 1 293 ? 222.140 157.003 153.975 1.00 53.50  ? 436 ASN A O      1 
ATOM   2003 C  CB     . ASN A 1 293 ? 221.818 158.392 151.498 1.00 45.22  ? 436 ASN A CB     1 
ATOM   2004 C  CG     . ASN A 1 293 ? 222.792 159.066 150.551 1.00 48.12  ? 436 ASN A CG     1 
ATOM   2005 O  OD1    . ASN A 1 293 ? 224.007 158.973 150.722 1.00 50.40  ? 436 ASN A OD1    1 
ATOM   2006 N  ND2    . ASN A 1 293 ? 222.261 159.749 149.543 1.00 44.00  ? 436 ASN A ND2    1 
ATOM   2007 N  N      . GLY A 1 294 ? 220.918 155.323 153.117 1.00 52.06  ? 437 GLY A N      1 
ATOM   2008 C  CA     . GLY A 1 294 ? 220.544 154.831 154.425 1.00 52.36  ? 437 GLY A CA     1 
ATOM   2009 C  C      . GLY A 1 294 ? 221.724 154.273 155.196 1.00 59.35  ? 437 GLY A C      1 
ATOM   2010 O  O      . GLY A 1 294 ? 222.748 153.877 154.638 1.00 59.60  ? 437 GLY A O      1 
ATOM   2011 N  N      . GLU A 1 295 ? 221.568 154.244 156.515 1.00 65.05  ? 438 GLU A N      1 
ATOM   2012 C  CA     . GLU A 1 295 ? 222.602 153.747 157.406 1.00 69.74  ? 438 GLU A CA     1 
ATOM   2013 C  C      . GLU A 1 295 ? 222.454 152.248 157.621 1.00 69.80  ? 438 GLU A C      1 
ATOM   2014 O  O      . GLU A 1 295 ? 221.356 151.695 157.510 1.00 64.86  ? 438 GLU A O      1 
ATOM   2015 C  CB     . GLU A 1 295 ? 222.535 154.476 158.746 1.00 73.10  ? 438 GLU A CB     1 
ATOM   2016 C  CG     . GLU A 1 295 ? 222.941 155.939 158.674 1.00 82.09  ? 438 GLU A CG     1 
ATOM   2017 C  CD     . GLU A 1 295 ? 222.360 156.761 159.806 1.00 93.39  ? 438 GLU A CD     1 
ATOM   2018 O  OE1    . GLU A 1 295 ? 222.798 156.579 160.962 1.00 95.33  ? 438 GLU A OE1    1 
ATOM   2019 O  OE2    . GLU A 1 295 ? 221.465 157.591 159.541 1.00 95.44  ? 438 GLU A OE2    1 
ATOM   2020 N  N      . PRO A 1 296 ? 223.551 151.559 157.925 1.00 75.16  ? 439 PRO A N      1 
ATOM   2021 C  CA     . PRO A 1 296 ? 223.469 150.114 158.163 1.00 71.31  ? 439 PRO A CA     1 
ATOM   2022 C  C      . PRO A 1 296 ? 222.664 149.794 159.412 1.00 65.73  ? 439 PRO A C      1 
ATOM   2023 O  O      . PRO A 1 296 ? 222.632 150.562 160.377 1.00 64.13  ? 439 PRO A O      1 
ATOM   2024 C  CB     . PRO A 1 296 ? 224.936 149.692 158.324 1.00 71.68  ? 439 PRO A CB     1 
ATOM   2025 C  CG     . PRO A 1 296 ? 225.746 150.842 157.795 1.00 69.20  ? 439 PRO A CG     1 
ATOM   2026 C  CD     . PRO A 1 296 ? 224.927 152.065 158.036 1.00 70.33  ? 439 PRO A CD     1 
ATOM   2027 N  N      . VAL A 1 297 ? 222.009 148.636 159.383 1.00 62.43  ? 440 VAL A N      1 
ATOM   2028 C  CA     . VAL A 1 297 ? 221.200 148.150 160.495 1.00 59.34  ? 440 VAL A CA     1 
ATOM   2029 C  C      . VAL A 1 297 ? 221.960 147.029 161.189 1.00 57.50  ? 440 VAL A C      1 
ATOM   2030 O  O      . VAL A 1 297 ? 222.400 146.072 160.539 1.00 58.23  ? 440 VAL A O      1 
ATOM   2031 C  CB     . VAL A 1 297 ? 219.822 147.666 160.014 1.00 53.28  ? 440 VAL A CB     1 
ATOM   2032 C  CG1    . VAL A 1 297 ? 218.961 147.257 161.199 1.00 50.24  ? 440 VAL A CG1    1 
ATOM   2033 C  CG2    . VAL A 1 297 ? 219.136 148.749 159.198 1.00 45.20  ? 440 VAL A CG2    1 
ATOM   2034 N  N      . HIS A 1 298 ? 222.114 147.143 162.510 1.00 56.17  ? 441 HIS A N      1 
ATOM   2035 C  CA     . HIS A 1 298 ? 222.895 146.183 163.275 1.00 56.24  ? 441 HIS A CA     1 
ATOM   2036 C  C      . HIS A 1 298 ? 222.079 145.336 164.241 1.00 56.11  ? 441 HIS A C      1 
ATOM   2037 O  O      . HIS A 1 298 ? 222.542 144.257 164.623 1.00 58.33  ? 441 HIS A O      1 
ATOM   2038 C  CB     . HIS A 1 298 ? 223.997 146.903 164.067 1.00 59.27  ? 441 HIS A CB     1 
ATOM   2039 C  CG     . HIS A 1 298 ? 225.057 147.516 163.207 1.00 73.30  ? 441 HIS A CG     1 
ATOM   2040 N  ND1    . HIS A 1 298 ? 225.651 146.841 162.163 1.00 76.06  ? 441 HIS A ND1    1 
ATOM   2041 C  CD2    . HIS A 1 298 ? 225.632 148.742 163.237 1.00 74.07  ? 441 HIS A CD2    1 
ATOM   2042 C  CE1    . HIS A 1 298 ? 226.544 147.624 161.586 1.00 74.76  ? 441 HIS A CE1    1 
ATOM   2043 N  NE2    . HIS A 1 298 ? 226.553 148.783 162.219 1.00 75.28  ? 441 HIS A NE2    1 
ATOM   2044 N  N      . ARG A 1 299 ? 220.891 145.783 164.643 1.00 52.15  ? 442 ARG A N      1 
ATOM   2045 C  CA     . ARG A 1 299 ? 220.116 145.043 165.629 1.00 46.56  ? 442 ARG A CA     1 
ATOM   2046 C  C      . ARG A 1 299 ? 218.645 145.416 165.516 1.00 45.31  ? 442 ARG A C      1 
ATOM   2047 O  O      . ARG A 1 299 ? 218.309 146.580 165.285 1.00 47.31  ? 442 ARG A O      1 
ATOM   2048 C  CB     . ARG A 1 299 ? 220.625 145.318 167.049 1.00 43.81  ? 442 ARG A CB     1 
ATOM   2049 C  CG     . ARG A 1 299 ? 219.556 145.208 168.122 1.00 46.86  ? 442 ARG A CG     1 
ATOM   2050 C  CD     . ARG A 1 299 ? 220.165 145.039 169.504 1.00 47.58  ? 442 ARG A CD     1 
ATOM   2051 N  NE     . ARG A 1 299 ? 219.230 145.417 170.558 1.00 52.41  ? 442 ARG A NE     1 
ATOM   2052 C  CZ     . ARG A 1 299 ? 219.058 144.741 171.686 1.00 54.34  ? 442 ARG A CZ     1 
ATOM   2053 N  NH1    . ARG A 1 299 ? 219.744 143.641 171.944 1.00 52.60  ? 442 ARG A NH1    1 
ATOM   2054 N  NH2    . ARG A 1 299 ? 218.172 145.180 172.575 1.00 50.49  ? 442 ARG A NH2    1 
ATOM   2055 N  N      . ILE A 1 300 ? 217.779 144.417 165.680 1.00 43.06  ? 443 ILE A N      1 
ATOM   2056 C  CA     . ILE A 1 300 ? 216.334 144.605 165.736 1.00 40.16  ? 443 ILE A CA     1 
ATOM   2057 C  C      . ILE A 1 300 ? 215.813 143.865 166.959 1.00 40.49  ? 443 ILE A C      1 
ATOM   2058 O  O      . ILE A 1 300 ? 216.156 142.697 167.173 1.00 43.73  ? 443 ILE A O      1 
ATOM   2059 C  CB     . ILE A 1 300 ? 215.635 144.101 164.459 1.00 37.86  ? 443 ILE A CB     1 
ATOM   2060 C  CG1    . ILE A 1 300 ? 216.436 144.497 163.217 1.00 46.58  ? 443 ILE A CG1    1 
ATOM   2061 C  CG2    . ILE A 1 300 ? 214.221 144.650 164.376 1.00 33.96  ? 443 ILE A CG2    1 
ATOM   2062 C  CD1    . ILE A 1 300 ? 215.877 143.938 161.926 1.00 40.00  ? 443 ILE A CD1    1 
ATOM   2063 N  N      . SER A 1 301 ? 214.984 144.536 167.756 1.00 38.88  ? 444 SER A N      1 
ATOM   2064 C  CA     . SER A 1 301 ? 214.495 143.953 168.996 1.00 36.88  ? 444 SER A CA     1 
ATOM   2065 C  C      . SER A 1 301 ? 213.126 144.527 169.331 1.00 33.01  ? 444 SER A C      1 
ATOM   2066 O  O      . SER A 1 301 ? 212.713 145.559 168.797 1.00 35.23  ? 444 SER A O      1 
ATOM   2067 C  CB     . SER A 1 301 ? 215.470 144.196 170.154 1.00 37.20  ? 444 SER A CB     1 
ATOM   2068 O  OG     . SER A 1 301 ? 215.039 143.534 171.329 1.00 38.32  ? 444 SER A OG     1 
ATOM   2069 N  N      . ILE A 1 302 ? 212.425 143.834 170.229 1.00 34.35  ? 445 ILE A N      1 
ATOM   2070 C  CA     . ILE A 1 302 ? 211.117 144.296 170.681 1.00 31.27  ? 445 ILE A CA     1 
ATOM   2071 C  C      . ILE A 1 302 ? 211.253 145.269 171.848 1.00 31.72  ? 445 ILE A C      1 
ATOM   2072 O  O      . ILE A 1 302 ? 210.364 146.097 172.075 1.00 30.18  ? 445 ILE A O      1 
ATOM   2073 C  CB     . ILE A 1 302 ? 210.230 143.096 171.055 1.00 33.81  ? 445 ILE A CB     1 
ATOM   2074 C  CG1    . ILE A 1 302 ? 209.869 142.285 169.809 1.00 31.98  ? 445 ILE A CG1    1 
ATOM   2075 C  CG2    . ILE A 1 302 ? 208.972 143.562 171.770 1.00 31.74  ? 445 ILE A CG2    1 
ATOM   2076 C  CD1    . ILE A 1 302 ? 209.011 143.036 168.819 1.00 29.79  ? 445 ILE A CD1    1 
ATOM   2077 N  N      . ILE A 1 303 ? 212.348 145.191 172.597 1.00 29.92  ? 446 ILE A N      1 
ATOM   2078 C  CA     . ILE A 1 303 ? 212.580 146.060 173.747 1.00 27.83  ? 446 ILE A CA     1 
ATOM   2079 C  C      . ILE A 1 303 ? 213.470 147.223 173.326 1.00 29.55  ? 446 ILE A C      1 
ATOM   2080 O  O      . ILE A 1 303 ? 214.466 147.013 172.619 1.00 32.31  ? 446 ILE A O      1 
ATOM   2081 C  CB     . ILE A 1 303 ? 213.205 145.279 174.914 1.00 35.40  ? 446 ILE A CB     1 
ATOM   2082 C  CG1    . ILE A 1 303 ? 212.538 143.910 175.059 1.00 35.44  ? 446 ILE A CG1    1 
ATOM   2083 C  CG2    . ILE A 1 303 ? 213.098 146.070 176.209 1.00 31.08  ? 446 ILE A CG2    1 
ATOM   2084 C  CD1    . ILE A 1 303 ? 211.109 143.973 175.549 1.00 26.81  ? 446 ILE A CD1    1 
ATOM   2085 N  N      . PRO A 1 304 ? 213.157 148.453 173.723 1.00 33.28  ? 447 PRO A N      1 
ATOM   2086 C  CA     . PRO A 1 304 ? 214.020 149.587 173.374 1.00 31.29  ? 447 PRO A CA     1 
ATOM   2087 C  C      . PRO A 1 304 ? 215.358 149.522 174.093 1.00 37.10  ? 447 PRO A C      1 
ATOM   2088 O  O      . PRO A 1 304 ? 215.461 149.061 175.232 1.00 37.24  ? 447 PRO A O      1 
ATOM   2089 C  CB     . PRO A 1 304 ? 213.211 150.810 173.830 1.00 27.50  ? 447 PRO A CB     1 
ATOM   2090 C  CG     . PRO A 1 304 ? 211.842 150.296 174.182 1.00 29.43  ? 447 PRO A CG     1 
ATOM   2091 C  CD     . PRO A 1 304 ? 212.003 148.860 174.537 1.00 28.57  ? 447 PRO A CD     1 
ATOM   2092 N  N      . ARG A 1 305 ? 216.396 149.995 173.404 1.00 38.79  ? 448 ARG A N      1 
ATOM   2093 C  CA     . ARG A 1 305 ? 217.751 149.976 173.945 1.00 36.76  ? 448 ARG A CA     1 
ATOM   2094 C  C      . ARG A 1 305 ? 218.386 151.354 174.035 1.00 40.45  ? 448 ARG A C      1 
ATOM   2095 O  O      . ARG A 1 305 ? 218.933 151.709 175.084 1.00 45.38  ? 448 ARG A O      1 
ATOM   2096 C  CB     . ARG A 1 305 ? 218.641 149.049 173.102 1.00 40.20  ? 448 ARG A CB     1 
ATOM   2097 C  CG     . ARG A 1 305 ? 220.050 148.891 173.649 1.00 42.16  ? 448 ARG A CG     1 
ATOM   2098 C  CD     . ARG A 1 305 ? 220.534 147.459 173.530 1.00 48.39  ? 448 ARG A CD     1 
ATOM   2099 N  NE     . ARG A 1 305 ? 220.174 146.667 174.700 1.00 50.97  ? 448 ARG A NE     1 
ATOM   2100 C  CZ     . ARG A 1 305 ? 220.819 145.578 175.095 1.00 56.89  ? 448 ARG A CZ     1 
ATOM   2101 N  NH1    . ARG A 1 305 ? 221.868 145.119 174.433 1.00 55.70  ? 448 ARG A NH1    1 
ATOM   2102 N  NH2    . ARG A 1 305 ? 220.402 144.935 176.181 1.00 55.93  ? 448 ARG A NH2    1 
ATOM   2103 N  N      . GLY A 1 306 ? 218.341 152.145 172.966 1.00 41.42  ? 449 GLY A N      1 
ATOM   2104 C  CA     . GLY A 1 306 ? 219.056 153.403 172.953 1.00 41.79  ? 449 GLY A CA     1 
ATOM   2105 C  C      . GLY A 1 306 ? 218.373 154.495 173.755 1.00 39.74  ? 449 GLY A C      1 
ATOM   2106 O  O      . GLY A 1 306 ? 217.219 154.385 174.165 1.00 42.47  ? 449 GLY A O      1 
ATOM   2107 N  N      . TYR A 1 307 ? 219.119 155.580 173.978 1.00 35.65  ? 450 TYR A N      1 
ATOM   2108 C  CA     . TYR A 1 307 ? 218.548 156.734 174.664 1.00 37.60  ? 450 TYR A CA     1 
ATOM   2109 C  C      . TYR A 1 307 ? 217.541 157.463 173.784 1.00 38.84  ? 450 TYR A C      1 
ATOM   2110 O  O      . TYR A 1 307 ? 216.575 158.040 174.296 1.00 35.96  ? 450 TYR A O      1 
ATOM   2111 C  CB     . TYR A 1 307 ? 219.659 157.683 175.121 1.00 34.46  ? 450 TYR A CB     1 
ATOM   2112 C  CG     . TYR A 1 307 ? 220.232 158.559 174.029 1.00 38.99  ? 450 TYR A CG     1 
ATOM   2113 C  CD1    . TYR A 1 307 ? 219.690 159.808 173.755 1.00 40.61  ? 450 TYR A CD1    1 
ATOM   2114 C  CD2    . TYR A 1 307 ? 221.320 158.140 173.277 1.00 39.50  ? 450 TYR A CD2    1 
ATOM   2115 C  CE1    . TYR A 1 307 ? 220.212 160.611 172.760 1.00 41.74  ? 450 TYR A CE1    1 
ATOM   2116 C  CE2    . TYR A 1 307 ? 221.850 158.936 172.282 1.00 37.75  ? 450 TYR A CE2    1 
ATOM   2117 C  CZ     . TYR A 1 307 ? 221.292 160.169 172.027 1.00 41.31  ? 450 TYR A CZ     1 
ATOM   2118 O  OH     . TYR A 1 307 ? 221.818 160.963 171.036 1.00 42.34  ? 450 TYR A OH     1 
ATOM   2119 N  N      . LYS A 1 308 ? 217.752 157.457 172.466 1.00 39.51  ? 451 LYS A N      1 
ATOM   2120 C  CA     . LYS A 1 308 ? 216.749 158.002 171.557 1.00 40.92  ? 451 LYS A CA     1 
ATOM   2121 C  C      . LYS A 1 308 ? 215.482 157.156 171.573 1.00 41.28  ? 451 LYS A C      1 
ATOM   2122 O  O      . LYS A 1 308 ? 214.369 157.693 171.528 1.00 40.73  ? 451 LYS A O      1 
ATOM   2123 C  CB     . LYS A 1 308 ? 217.317 158.093 170.141 1.00 45.75  ? 451 LYS A CB     1 
ATOM   2124 C  CG     . LYS A 1 308 ? 217.965 159.427 169.810 1.00 49.39  ? 451 LYS A CG     1 
ATOM   2125 C  CD     . LYS A 1 308 ? 218.593 159.401 168.426 1.00 47.70  ? 451 LYS A CD     1 
ATOM   2126 C  CE     . LYS A 1 308 ? 218.742 160.801 167.857 1.00 51.90  ? 451 LYS A CE     1 
ATOM   2127 N  NZ     . LYS A 1 308 ? 219.341 160.782 166.494 1.00 61.36  ? 451 LYS A NZ     1 
ATOM   2128 N  N      . ALA A 1 309 ? 215.633 155.831 171.636 1.00 41.60  ? 452 ALA A N      1 
ATOM   2129 C  CA     . ALA A 1 309 ? 214.478 154.946 171.706 1.00 35.59  ? 452 ALA A CA     1 
ATOM   2130 C  C      . ALA A 1 309 ? 213.709 155.099 173.011 1.00 36.52  ? 452 ALA A C      1 
ATOM   2131 O  O      . ALA A 1 309 ? 212.544 154.693 173.079 1.00 38.91  ? 452 ALA A O      1 
ATOM   2132 C  CB     . ALA A 1 309 ? 214.918 153.493 171.529 1.00 33.11  ? 452 ALA A CB     1 
ATOM   2133 N  N      . LEU A 1 310 ? 214.329 155.667 174.043 1.00 38.76  ? 453 LEU A N      1 
ATOM   2134 C  CA     . LEU A 1 310 ? 213.668 155.885 175.321 1.00 35.26  ? 453 LEU A CA     1 
ATOM   2135 C  C      . LEU A 1 310 ? 213.009 157.254 175.426 1.00 36.76  ? 453 LEU A C      1 
ATOM   2136 O  O      . LEU A 1 310 ? 212.387 157.546 176.453 1.00 36.09  ? 453 LEU A O      1 
ATOM   2137 C  CB     . LEU A 1 310 ? 214.667 155.712 176.471 1.00 34.48  ? 453 LEU A CB     1 
ATOM   2138 C  CG     . LEU A 1 310 ? 215.271 154.318 176.654 1.00 34.89  ? 453 LEU A CG     1 
ATOM   2139 C  CD1    . LEU A 1 310 ? 216.402 154.356 177.669 1.00 33.21  ? 453 LEU A CD1    1 
ATOM   2140 C  CD2    . LEU A 1 310 ? 214.206 153.316 177.072 1.00 31.22  ? 453 LEU A CD2    1 
ATOM   2141 N  N      . GLY A 1 311 ? 213.128 158.094 174.401 1.00 38.27  ? 454 GLY A N      1 
ATOM   2142 C  CA     . GLY A 1 311 ? 212.492 159.394 174.416 1.00 35.78  ? 454 GLY A CA     1 
ATOM   2143 C  C      . GLY A 1 311 ? 213.297 160.506 175.047 1.00 42.33  ? 454 GLY A C      1 
ATOM   2144 O  O      . GLY A 1 311 ? 212.711 161.496 175.501 1.00 45.60  ? 454 GLY A O      1 
ATOM   2145 N  N      . TYR A 1 312 ? 214.620 160.383 175.091 1.00 40.78  ? 455 TYR A N      1 
ATOM   2146 C  CA     . TYR A 1 312 ? 215.484 161.388 175.692 1.00 40.75  ? 455 TYR A CA     1 
ATOM   2147 C  C      . TYR A 1 312 ? 216.235 162.155 174.613 1.00 43.72  ? 455 TYR A C      1 
ATOM   2148 O  O      . TYR A 1 312 ? 216.734 161.564 173.650 1.00 46.11  ? 455 TYR A O      1 
ATOM   2149 C  CB     . TYR A 1 312 ? 216.489 160.751 176.656 1.00 37.98  ? 455 TYR A CB     1 
ATOM   2150 C  CG     . TYR A 1 312 ? 215.866 159.940 177.768 1.00 36.04  ? 455 TYR A CG     1 
ATOM   2151 C  CD1    . TYR A 1 312 ? 214.633 160.288 178.302 1.00 34.23  ? 455 TYR A CD1    1 
ATOM   2152 C  CD2    . TYR A 1 312 ? 216.517 158.832 178.291 1.00 32.91  ? 455 TYR A CD2    1 
ATOM   2153 C  CE1    . TYR A 1 312 ? 214.064 159.550 179.321 1.00 32.29  ? 455 TYR A CE1    1 
ATOM   2154 C  CE2    . TYR A 1 312 ? 215.956 158.089 179.310 1.00 30.60  ? 455 TYR A CE2    1 
ATOM   2155 C  CZ     . TYR A 1 312 ? 214.730 158.452 179.821 1.00 33.86  ? 455 TYR A CZ     1 
ATOM   2156 O  OH     . TYR A 1 312 ? 214.167 157.714 180.836 1.00 33.57  ? 455 TYR A OH     1 
ATOM   2157 N  N      . THR A 1 313 ? 216.313 163.475 174.781 1.00 44.06  ? 456 THR A N      1 
ATOM   2158 C  CA     . THR A 1 313 ? 217.136 164.310 173.915 1.00 45.72  ? 456 THR A CA     1 
ATOM   2159 C  C      . THR A 1 313 ? 218.511 164.568 174.518 1.00 49.23  ? 456 THR A C      1 
ATOM   2160 O  O      . THR A 1 313 ? 219.494 164.706 173.782 1.00 50.15  ? 456 THR A O      1 
ATOM   2161 C  CB     . THR A 1 313 ? 216.435 165.642 173.633 1.00 46.52  ? 456 THR A CB     1 
ATOM   2162 O  OG1    . THR A 1 313 ? 216.437 166.446 174.819 1.00 56.71  ? 456 THR A OG1    1 
ATOM   2163 C  CG2    . THR A 1 313 ? 215.000 165.405 173.190 1.00 44.11  ? 456 THR A CG2    1 
ATOM   2164 N  N      . LEU A 1 314 ? 218.596 164.637 175.846 1.00 48.03  ? 457 LEU A N      1 
ATOM   2165 C  CA     . LEU A 1 314 ? 219.847 164.826 176.573 1.00 45.98  ? 457 LEU A CA     1 
ATOM   2166 C  C      . LEU A 1 314 ? 220.514 166.159 176.263 1.00 49.66  ? 457 LEU A C      1 
ATOM   2167 O  O      . LEU A 1 314 ? 221.736 166.285 176.390 1.00 50.93  ? 457 LEU A O      1 
ATOM   2168 C  CB     . LEU A 1 314 ? 220.825 163.677 176.300 1.00 46.12  ? 457 LEU A CB     1 
ATOM   2169 C  CG     . LEU A 1 314 ? 220.400 162.297 176.806 1.00 45.07  ? 457 LEU A CG     1 
ATOM   2170 C  CD1    . LEU A 1 314 ? 221.573 161.330 176.776 1.00 40.31  ? 457 LEU A CD1    1 
ATOM   2171 C  CD2    . LEU A 1 314 ? 219.813 162.391 178.206 1.00 35.02  ? 457 LEU A CD2    1 
ATOM   2172 N  N      . HIS A 1 315 ? 219.737 167.165 175.859 1.00 53.27  ? 458 HIS A N      1 
ATOM   2173 C  CA     . HIS A 1 315 ? 220.266 168.493 175.553 1.00 54.58  ? 458 HIS A CA     1 
ATOM   2174 C  C      . HIS A 1 315 ? 221.339 168.441 174.469 1.00 56.76  ? 458 HIS A C      1 
ATOM   2175 O  O      . HIS A 1 315 ? 222.346 169.149 174.544 1.00 61.39  ? 458 HIS A O      1 
ATOM   2176 C  CB     . HIS A 1 315 ? 220.815 169.173 176.811 1.00 53.00  ? 458 HIS A CB     1 
ATOM   2177 C  CG     . HIS A 1 315 ? 219.769 169.485 177.836 1.00 59.38  ? 458 HIS A CG     1 
ATOM   2178 N  ND1    . HIS A 1 315 ? 219.406 168.595 178.824 1.00 61.76  ? 458 HIS A ND1    1 
ATOM   2179 C  CD2    . HIS A 1 315 ? 219.010 170.590 178.027 1.00 57.58  ? 458 HIS A CD2    1 
ATOM   2180 C  CE1    . HIS A 1 315 ? 218.467 169.138 179.578 1.00 56.91  ? 458 HIS A CE1    1 
ATOM   2181 N  NE2    . HIS A 1 315 ? 218.209 170.348 179.116 1.00 57.40  ? 458 HIS A NE2    1 
ATOM   2182 N  N      . LEU A 1 316 ? 221.135 167.603 173.452 1.00 55.53  ? 459 LEU A N      1 
ATOM   2183 C  CA     . LEU A 1 316 ? 222.098 167.473 172.372 1.00 57.35  ? 459 LEU A CA     1 
ATOM   2184 C  C      . LEU A 1 316 ? 221.475 167.880 171.040 1.00 64.04  ? 459 LEU A C      1 
ATOM   2185 O  O      . LEU A 1 316 ? 220.275 167.687 170.823 1.00 64.20  ? 459 LEU A O      1 
ATOM   2186 C  CB     . LEU A 1 316 ? 222.616 166.034 172.261 1.00 57.55  ? 459 LEU A CB     1 
ATOM   2187 C  CG     . LEU A 1 316 ? 223.597 165.564 173.336 1.00 57.09  ? 459 LEU A CG     1 
ATOM   2188 C  CD1    . LEU A 1 316 ? 223.683 164.047 173.349 1.00 49.00  ? 459 LEU A CD1    1 
ATOM   2189 C  CD2    . LEU A 1 316 ? 224.968 166.179 173.114 1.00 60.88  ? 459 LEU A CD2    1 
ATOM   2190 N  N      . PRO A 1 317 ? 222.263 168.447 170.129 1.00 69.22  ? 460 PRO A N      1 
ATOM   2191 C  CA     . PRO A 1 317 ? 221.726 168.797 168.810 1.00 68.06  ? 460 PRO A CA     1 
ATOM   2192 C  C      . PRO A 1 317 ? 221.332 167.557 168.024 1.00 69.95  ? 460 PRO A C      1 
ATOM   2193 O  O      . PRO A 1 317 ? 221.950 166.495 168.137 1.00 71.04  ? 460 PRO A O      1 
ATOM   2194 C  CB     . PRO A 1 317 ? 222.887 169.538 168.133 1.00 63.98  ? 460 PRO A CB     1 
ATOM   2195 C  CG     . PRO A 1 317 ? 223.819 169.915 169.245 1.00 62.87  ? 460 PRO A CG     1 
ATOM   2196 C  CD     . PRO A 1 317 ? 223.669 168.850 170.280 1.00 64.64  ? 460 PRO A CD     1 
ATOM   2197 N  N      . GLU A 1 318 ? 220.284 167.707 167.211 1.00 71.65  ? 461 GLU A N      1 
ATOM   2198 C  CA     . GLU A 1 318 ? 219.815 166.587 166.403 1.00 71.89  ? 461 GLU A CA     1 
ATOM   2199 C  C      . GLU A 1 318 ? 220.794 166.243 165.287 1.00 78.50  ? 461 GLU A C      1 
ATOM   2200 O  O      . GLU A 1 318 ? 221.010 165.061 164.997 1.00 79.43  ? 461 GLU A O      1 
ATOM   2201 C  CB     . GLU A 1 318 ? 218.437 166.898 165.820 1.00 69.09  ? 461 GLU A CB     1 
ATOM   2202 C  CG     . GLU A 1 318 ? 217.965 165.895 164.779 1.00 74.02  ? 461 GLU A CG     1 
ATOM   2203 C  CD     . GLU A 1 318 ? 217.196 164.739 165.389 1.00 76.67  ? 461 GLU A CD     1 
ATOM   2204 O  OE1    . GLU A 1 318 ? 216.305 164.991 166.227 1.00 74.18  ? 461 GLU A OE1    1 
ATOM   2205 O  OE2    . GLU A 1 318 ? 217.483 163.577 165.032 1.00 74.80  ? 461 GLU A OE2    1 
ATOM   2206 N  N      . GLU A 1 319 ? 221.392 167.250 164.654 1.00 78.24  ? 462 GLU A N      1 
ATOM   2207 C  CA     . GLU A 1 319 ? 222.312 167.017 163.550 1.00 77.93  ? 462 GLU A CA     1 
ATOM   2208 C  C      . GLU A 1 319 ? 223.653 166.521 164.076 1.00 73.04  ? 462 GLU A C      1 
ATOM   2209 O  O      . GLU A 1 319 ? 224.199 167.075 165.034 1.00 71.28  ? 462 GLU A O      1 
ATOM   2210 C  CB     . GLU A 1 319 ? 222.500 168.296 162.735 1.00 82.85  ? 462 GLU A CB     1 
ATOM   2211 C  CG     . GLU A 1 319 ? 221.212 168.853 162.152 1.00 88.90  ? 462 GLU A CG     1 
ATOM   2212 C  CD     . GLU A 1 319 ? 220.509 167.866 161.239 1.00 90.35  ? 462 GLU A CD     1 
ATOM   2213 O  OE1    . GLU A 1 319 ? 221.204 167.074 160.569 1.00 90.52  ? 462 GLU A OE1    1 
ATOM   2214 O  OE2    . GLU A 1 319 ? 219.261 167.883 161.192 1.00 81.77  ? 462 GLU A OE2    1 
ATOM   2215 N  N      . ASP A 1 320 ? 224.185 165.472 163.441 1.00 66.17  ? 463 ASP A N      1 
ATOM   2216 C  CA     . ASP A 1 320 ? 225.437 164.860 163.870 1.00 61.92  ? 463 ASP A CA     1 
ATOM   2217 C  C      . ASP A 1 320 ? 226.426 164.701 162.720 1.00 60.57  ? 463 ASP A C      1 
ATOM   2218 O  O      . ASP A 1 320 ? 227.351 163.888 162.815 1.00 58.89  ? 463 ASP A O      1 
ATOM   2219 C  CB     . ASP A 1 320 ? 225.174 163.502 164.526 1.00 70.43  ? 463 ASP A CB     1 
ATOM   2220 C  CG     . ASP A 1 320 ? 224.399 162.562 163.624 1.00 80.39  ? 463 ASP A CG     1 
ATOM   2221 O  OD1    . ASP A 1 320 ? 223.382 162.998 163.044 1.00 79.84  ? 463 ASP A OD1    1 
ATOM   2222 O  OD2    . ASP A 1 320 ? 224.806 161.389 163.493 1.00 81.64  ? 463 ASP A OD2    1 
ATOM   2223 N  N      . LYS A 1 321 ? 226.253 165.453 161.636 1.00 58.99  ? 464 LYS A N      1 
ATOM   2224 C  CA     . LYS A 1 321 ? 227.125 165.366 160.476 1.00 44.53  ? 464 LYS A CA     1 
ATOM   2225 C  C      . LYS A 1 321 ? 227.828 166.696 160.245 1.00 42.41  ? 464 LYS A C      1 
ATOM   2226 O  O      . LYS A 1 321 ? 227.261 167.768 160.479 1.00 43.24  ? 464 LYS A O      1 
ATOM   2227 C  CB     . LYS A 1 321 ? 226.344 164.965 159.219 1.00 47.73  ? 464 LYS A CB     1 
ATOM   2228 C  CG     . LYS A 1 321 ? 225.921 163.506 159.194 1.00 54.57  ? 464 LYS A CG     1 
ATOM   2229 C  CD     . LYS A 1 321 ? 227.112 162.594 158.952 1.00 55.89  ? 464 LYS A CD     1 
ATOM   2230 C  CE     . LYS A 1 321 ? 226.769 161.146 159.254 1.00 58.15  ? 464 LYS A CE     1 
ATOM   2231 N  NZ     . LYS A 1 321 ? 225.732 160.618 158.326 1.00 66.20  ? 464 LYS A NZ     1 
ATOM   2232 N  N      . TYR A 1 322 ? 229.076 166.614 159.783 1.00 40.50  ? 465 TYR A N      1 
ATOM   2233 C  CA     . TYR A 1 322 ? 229.849 167.816 159.491 1.00 35.58  ? 465 TYR A CA     1 
ATOM   2234 C  C      . TYR A 1 322 ? 229.319 168.542 158.260 1.00 37.92  ? 465 TYR A C      1 
ATOM   2235 O  O      . TYR A 1 322 ? 229.316 169.778 158.220 1.00 38.65  ? 465 TYR A O      1 
ATOM   2236 C  CB     . TYR A 1 322 ? 231.324 167.456 159.304 1.00 33.66  ? 465 TYR A CB     1 
ATOM   2237 C  CG     . TYR A 1 322 ? 232.215 168.635 158.981 1.00 36.48  ? 465 TYR A CG     1 
ATOM   2238 C  CD1    . TYR A 1 322 ? 232.867 169.334 159.987 1.00 33.48  ? 465 TYR A CD1    1 
ATOM   2239 C  CD2    . TYR A 1 322 ? 232.409 169.045 157.668 1.00 34.11  ? 465 TYR A CD2    1 
ATOM   2240 C  CE1    . TYR A 1 322 ? 233.683 170.409 159.697 1.00 33.38  ? 465 TYR A CE1    1 
ATOM   2241 C  CE2    . TYR A 1 322 ? 233.222 170.120 157.368 1.00 32.94  ? 465 TYR A CE2    1 
ATOM   2242 C  CZ     . TYR A 1 322 ? 233.857 170.798 158.386 1.00 38.23  ? 465 TYR A CZ     1 
ATOM   2243 O  OH     . TYR A 1 322 ? 234.669 171.868 158.090 1.00 42.71  ? 465 TYR A OH     1 
ATOM   2244 N  N      . LEU A 1 323 ? 228.868 167.799 157.254 1.00 34.60  ? 466 LEU A N      1 
ATOM   2245 C  CA     . LEU A 1 323 ? 228.409 168.368 155.996 1.00 31.06  ? 466 LEU A CA     1 
ATOM   2246 C  C      . LEU A 1 323 ? 226.901 168.202 155.865 1.00 34.13  ? 466 LEU A C      1 
ATOM   2247 O  O      . LEU A 1 323 ? 226.342 167.175 156.263 1.00 42.99  ? 466 LEU A O      1 
ATOM   2248 C  CB     . LEU A 1 323 ? 229.112 167.704 154.808 1.00 30.42  ? 466 LEU A CB     1 
ATOM   2249 C  CG     . LEU A 1 323 ? 228.754 168.232 153.418 1.00 33.51  ? 466 LEU A CG     1 
ATOM   2250 C  CD1    . LEU A 1 323 ? 229.586 169.458 153.076 1.00 35.22  ? 466 LEU A CD1    1 
ATOM   2251 C  CD2    . LEU A 1 323 ? 228.935 167.147 152.370 1.00 32.08  ? 466 LEU A CD2    1 
ATOM   2252 N  N      . VAL A 1 324 ? 226.249 169.215 155.305 1.00 32.51  ? 467 VAL A N      1 
ATOM   2253 C  CA     . VAL A 1 324 ? 224.803 169.229 155.117 1.00 32.67  ? 467 VAL A CA     1 
ATOM   2254 C  C      . VAL A 1 324 ? 224.544 169.183 153.617 1.00 31.00  ? 467 VAL A C      1 
ATOM   2255 O  O      . VAL A 1 324 ? 224.858 170.133 152.891 1.00 37.06  ? 467 VAL A O      1 
ATOM   2256 C  CB     . VAL A 1 324 ? 224.154 170.458 155.762 1.00 33.88  ? 467 VAL A CB     1 
ATOM   2257 C  CG1    . VAL A 1 324 ? 222.641 170.387 155.636 1.00 35.20  ? 467 VAL A CG1    1 
ATOM   2258 C  CG2    . VAL A 1 324 ? 224.569 170.575 157.219 1.00 32.39  ? 467 VAL A CG2    1 
ATOM   2259 N  N      . SER A 1 325 ? 223.966 168.082 153.145 1.00 30.43  ? 468 SER A N      1 
ATOM   2260 C  CA     . SER A 1 325 ? 223.611 167.918 151.744 1.00 29.76  ? 468 SER A CA     1 
ATOM   2261 C  C      . SER A 1 325 ? 222.156 167.485 151.624 1.00 29.82  ? 468 SER A C      1 
ATOM   2262 O  O      . SER A 1 325 ? 221.601 166.837 152.515 1.00 31.52  ? 468 SER A O      1 
ATOM   2263 C  CB     . SER A 1 325 ? 224.526 166.902 151.049 1.00 28.55  ? 468 SER A CB     1 
ATOM   2264 O  OG     . SER A 1 325 ? 224.472 165.640 151.686 1.00 38.67  ? 468 SER A OG     1 
ATOM   2265 N  N      . ARG A 1 326 ? 221.540 167.857 150.500 1.00 28.65  ? 469 ARG A N      1 
ATOM   2266 C  CA     . ARG A 1 326 ? 220.122 167.588 150.293 1.00 26.34  ? 469 ARG A CA     1 
ATOM   2267 C  C      . ARG A 1 326 ? 219.833 166.097 150.158 1.00 28.11  ? 469 ARG A C      1 
ATOM   2268 O  O      . ARG A 1 326 ? 218.839 165.605 150.703 1.00 30.04  ? 469 ARG A O      1 
ATOM   2269 C  CB     . ARG A 1 326 ? 219.624 168.335 149.055 1.00 25.86  ? 469 ARG A CB     1 
ATOM   2270 C  CG     . ARG A 1 326 ? 218.163 168.081 148.723 1.00 27.43  ? 469 ARG A CG     1 
ATOM   2271 C  CD     . ARG A 1 326 ? 217.847 168.450 147.283 1.00 27.58  ? 469 ARG A CD     1 
ATOM   2272 N  NE     . ARG A 1 326 ? 218.599 167.642 146.331 1.00 28.79  ? 469 ARG A NE     1 
ATOM   2273 C  CZ     . ARG A 1 326 ? 218.684 167.900 145.032 1.00 30.98  ? 469 ARG A CZ     1 
ATOM   2274 N  NH1    . ARG A 1 326 ? 218.070 168.939 144.492 1.00 29.10  ? 469 ARG A NH1    1 
ATOM   2275 N  NH2    . ARG A 1 326 ? 219.402 167.093 144.257 1.00 26.07  ? 469 ARG A NH2    1 
ATOM   2276 N  N      . ASN A 1 327 ? 220.682 165.363 149.435 1.00 29.20  ? 470 ASN A N      1 
ATOM   2277 C  CA     . ASN A 1 327 ? 220.389 163.960 149.161 1.00 25.86  ? 470 ASN A CA     1 
ATOM   2278 C  C      . ASN A 1 327 ? 220.390 163.116 150.429 1.00 30.26  ? 470 ASN A C      1 
ATOM   2279 O  O      . ASN A 1 327 ? 219.513 162.262 150.601 1.00 35.21  ? 470 ASN A O      1 
ATOM   2280 C  CB     . ASN A 1 327 ? 221.391 163.400 148.152 1.00 27.06  ? 470 ASN A CB     1 
ATOM   2281 C  CG     . ASN A 1 327 ? 221.012 163.716 146.719 1.00 28.16  ? 470 ASN A CG     1 
ATOM   2282 O  OD1    . ASN A 1 327 ? 219.940 164.259 146.454 1.00 26.56  ? 470 ASN A OD1    1 
ATOM   2283 N  ND2    . ASN A 1 327 ? 221.890 163.375 145.785 1.00 26.64  ? 470 ASN A ND2    1 
ATOM   2284 N  N      . GLU A 1 328 ? 221.354 163.332 151.323 1.00 30.76  ? 471 GLU A N      1 
ATOM   2285 C  CA     . GLU A 1 328 ? 221.434 162.550 152.549 1.00 31.49  ? 471 GLU A CA     1 
ATOM   2286 C  C      . GLU A 1 328 ? 220.407 162.968 153.591 1.00 29.88  ? 471 GLU A C      1 
ATOM   2287 O  O      . GLU A 1 328 ? 220.053 162.154 154.451 1.00 31.04  ? 471 GLU A O      1 
ATOM   2288 C  CB     . GLU A 1 328 ? 222.840 162.646 153.150 1.00 31.87  ? 471 GLU A CB     1 
ATOM   2289 C  CG     . GLU A 1 328 ? 223.203 164.023 153.674 1.00 37.86  ? 471 GLU A CG     1 
ATOM   2290 C  CD     . GLU A 1 328 ? 223.127 164.111 155.185 1.00 48.67  ? 471 GLU A CD     1 
ATOM   2291 O  OE1    . GLU A 1 328 ? 223.039 163.052 155.841 1.00 51.93  ? 471 GLU A OE1    1 
ATOM   2292 O  OE2    . GLU A 1 328 ? 223.161 165.241 155.717 1.00 45.16  ? 471 GLU A OE2    1 
ATOM   2293 N  N      . LEU A 1 329 ? 219.923 164.210 153.539 1.00 29.81  ? 472 LEU A N      1 
ATOM   2294 C  CA     . LEU A 1 329 ? 218.887 164.642 154.469 1.00 30.25  ? 472 LEU A CA     1 
ATOM   2295 C  C      . LEU A 1 329 ? 217.517 164.095 154.091 1.00 27.36  ? 472 LEU A C      1 
ATOM   2296 O  O      . LEU A 1 329 ? 216.720 163.770 154.977 1.00 27.74  ? 472 LEU A O      1 
ATOM   2297 C  CB     . LEU A 1 329 ? 218.842 166.169 154.535 1.00 30.99  ? 472 LEU A CB     1 
ATOM   2298 C  CG     . LEU A 1 329 ? 219.680 166.833 155.630 1.00 34.73  ? 472 LEU A CG     1 
ATOM   2299 C  CD1    . LEU A 1 329 ? 219.396 168.323 155.688 1.00 39.63  ? 472 LEU A CD1    1 
ATOM   2300 C  CD2    . LEU A 1 329 ? 219.421 166.182 156.978 1.00 35.80  ? 472 LEU A CD2    1 
ATOM   2301 N  N      . LEU A 1 330 ? 217.225 163.990 152.793 1.00 28.78  ? 473 LEU A N      1 
ATOM   2302 C  CA     . LEU A 1 330 ? 215.940 163.444 152.368 1.00 24.77  ? 473 LEU A CA     1 
ATOM   2303 C  C      . LEU A 1 330 ? 215.844 161.954 152.674 1.00 26.06  ? 473 LEU A C      1 
ATOM   2304 O  O      . LEU A 1 330 ? 214.781 161.465 153.073 1.00 29.83  ? 473 LEU A O      1 
ATOM   2305 C  CB     . LEU A 1 330 ? 215.727 163.703 150.877 1.00 23.88  ? 473 LEU A CB     1 
ATOM   2306 C  CG     . LEU A 1 330 ? 215.314 165.126 150.494 1.00 27.35  ? 473 LEU A CG     1 
ATOM   2307 C  CD1    . LEU A 1 330 ? 215.005 165.213 149.010 1.00 26.81  ? 473 LEU A CD1    1 
ATOM   2308 C  CD2    . LEU A 1 330 ? 214.123 165.580 151.321 1.00 29.52  ? 473 LEU A CD2    1 
ATOM   2309 N  N      . ASP A 1 331 ? 216.941 161.217 152.490 1.00 25.44  ? 474 ASP A N      1 
ATOM   2310 C  CA     . ASP A 1 331 ? 216.936 159.796 152.820 1.00 25.92  ? 474 ASP A CA     1 
ATOM   2311 C  C      . ASP A 1 331 ? 216.773 159.569 154.317 1.00 26.14  ? 474 ASP A C      1 
ATOM   2312 O  O      . ASP A 1 331 ? 216.117 158.605 154.728 1.00 25.36  ? 474 ASP A O      1 
ATOM   2313 C  CB     . ASP A 1 331 ? 218.219 159.135 152.318 1.00 32.35  ? 474 ASP A CB     1 
ATOM   2314 C  CG     . ASP A 1 331 ? 218.155 158.783 150.846 1.00 44.32  ? 474 ASP A CG     1 
ATOM   2315 O  OD1    . ASP A 1 331 ? 217.112 159.051 150.215 1.00 48.04  ? 474 ASP A OD1    1 
ATOM   2316 O  OD2    . ASP A 1 331 ? 219.146 158.237 150.320 1.00 49.07  ? 474 ASP A OD2    1 
ATOM   2317 N  N      . LYS A 1 332 ? 217.364 160.435 155.142 1.00 25.40  ? 475 LYS A N      1 
ATOM   2318 C  CA     . LYS A 1 332 ? 217.189 160.322 156.585 1.00 21.62  ? 475 LYS A CA     1 
ATOM   2319 C  C      . LYS A 1 332 ? 215.734 160.539 156.983 1.00 21.10  ? 475 LYS A C      1 
ATOM   2320 O  O      . LYS A 1 332 ? 215.217 159.848 157.868 1.00 20.96  ? 475 LYS A O      1 
ATOM   2321 C  CB     . LYS A 1 332 ? 218.099 161.321 157.298 1.00 25.59  ? 475 LYS A CB     1 
ATOM   2322 C  CG     . LYS A 1 332 ? 218.343 161.018 158.764 1.00 30.82  ? 475 LYS A CG     1 
ATOM   2323 C  CD     . LYS A 1 332 ? 218.479 162.301 159.565 1.00 32.46  ? 475 LYS A CD     1 
ATOM   2324 C  CE     . LYS A 1 332 ? 219.165 162.057 160.898 1.00 51.59  ? 475 LYS A CE     1 
ATOM   2325 N  NZ     . LYS A 1 332 ? 219.247 163.303 161.708 1.00 64.66  ? 475 LYS A NZ     1 
ATOM   2326 N  N      . LEU A 1 333 ? 215.062 161.502 156.348 1.00 23.14  ? 476 LEU A N      1 
ATOM   2327 C  CA     . LEU A 1 333 ? 213.657 161.750 156.654 1.00 21.51  ? 476 LEU A CA     1 
ATOM   2328 C  C      . LEU A 1 333 ? 212.784 160.563 156.267 1.00 20.07  ? 476 LEU A C      1 
ATOM   2329 O  O      . LEU A 1 333 ? 211.874 160.185 157.014 1.00 23.10  ? 476 LEU A O      1 
ATOM   2330 C  CB     . LEU A 1 333 ? 213.182 163.016 155.941 1.00 23.41  ? 476 LEU A CB     1 
ATOM   2331 C  CG     . LEU A 1 333 ? 213.284 164.329 156.718 1.00 25.62  ? 476 LEU A CG     1 
ATOM   2332 C  CD1    . LEU A 1 333 ? 212.982 165.512 155.815 1.00 31.61  ? 476 LEU A CD1    1 
ATOM   2333 C  CD2    . LEU A 1 333 ? 212.353 164.317 157.917 1.00 26.93  ? 476 LEU A CD2    1 
ATOM   2334 N  N      . THR A 1 334 ? 213.042 159.963 155.102 1.00 19.00  ? 477 THR A N      1 
ATOM   2335 C  CA     . THR A 1 334 ? 212.218 158.850 154.645 1.00 17.50  ? 477 THR A CA     1 
ATOM   2336 C  C      . THR A 1 334 ? 212.361 157.630 155.545 1.00 17.65  ? 477 THR A C      1 
ATOM   2337 O  O      . THR A 1 334 ? 211.370 156.942 155.814 1.00 17.00  ? 477 THR A O      1 
ATOM   2338 C  CB     . THR A 1 334 ? 212.575 158.487 153.203 1.00 18.27  ? 477 THR A CB     1 
ATOM   2339 O  OG1    . THR A 1 334 ? 212.440 159.645 152.371 1.00 24.47  ? 477 THR A OG1    1 
ATOM   2340 C  CG2    . THR A 1 334 ? 211.657 157.391 152.683 1.00 15.47  ? 477 THR A CG2    1 
ATOM   2341 N  N      . ALA A 1 335 ? 213.576 157.343 156.017 1.00 19.19  ? 478 ALA A N      1 
ATOM   2342 C  CA     . ALA A 1 335 ? 213.774 156.179 156.874 1.00 16.82  ? 478 ALA A CA     1 
ATOM   2343 C  C      . ALA A 1 335 ? 213.182 156.391 158.260 1.00 18.55  ? 478 ALA A C      1 
ATOM   2344 O  O      . ALA A 1 335 ? 212.817 155.420 158.932 1.00 21.54  ? 478 ALA A O      1 
ATOM   2345 C  CB     . ALA A 1 335 ? 215.262 155.848 156.977 1.00 14.37  ? 478 ALA A CB     1 
ATOM   2346 N  N      . LEU A 1 336 ? 213.076 157.644 158.705 1.00 18.15  ? 479 LEU A N      1 
ATOM   2347 C  CA     . LEU A 1 336 ? 212.491 157.933 160.006 1.00 16.79  ? 479 LEU A CA     1 
ATOM   2348 C  C      . LEU A 1 336 ? 210.976 157.778 160.016 1.00 21.67  ? 479 LEU A C      1 
ATOM   2349 O  O      . LEU A 1 336 ? 210.389 157.640 161.094 1.00 22.35  ? 479 LEU A O      1 
ATOM   2350 C  CB     . LEU A 1 336 ? 212.867 159.350 160.447 1.00 19.21  ? 479 LEU A CB     1 
ATOM   2351 C  CG     . LEU A 1 336 ? 212.329 159.820 161.799 1.00 25.69  ? 479 LEU A CG     1 
ATOM   2352 C  CD1    . LEU A 1 336 ? 213.032 159.102 162.940 1.00 26.57  ? 479 LEU A CD1    1 
ATOM   2353 C  CD2    . LEU A 1 336 ? 212.479 161.325 161.937 1.00 26.11  ? 479 LEU A CD2    1 
ATOM   2354 N  N      . LEU A 1 337 ? 210.334 157.796 158.850 1.00 19.22  ? 480 LEU A N      1 
ATOM   2355 C  CA     . LEU A 1 337 ? 208.891 157.645 158.745 1.00 15.68  ? 480 LEU A CA     1 
ATOM   2356 C  C      . LEU A 1 337 ? 208.473 156.233 158.355 1.00 15.08  ? 480 LEU A C      1 
ATOM   2357 O  O      . LEU A 1 337 ? 207.282 155.987 158.142 1.00 16.12  ? 480 LEU A O      1 
ATOM   2358 C  CB     . LEU A 1 337 ? 208.329 158.653 157.741 1.00 16.79  ? 480 LEU A CB     1 
ATOM   2359 C  CG     . LEU A 1 337 ? 208.440 160.129 158.130 1.00 18.93  ? 480 LEU A CG     1 
ATOM   2360 C  CD1    . LEU A 1 337 ? 208.115 161.018 156.944 1.00 19.37  ? 480 LEU A CD1    1 
ATOM   2361 C  CD2    . LEU A 1 337 ? 207.532 160.447 159.307 1.00 18.14  ? 480 LEU A CD2    1 
ATOM   2362 N  N      . GLY A 1 338 ? 209.423 155.300 158.261 1.00 15.19  ? 481 GLY A N      1 
ATOM   2363 C  CA     . GLY A 1 338 ? 209.105 153.940 157.863 1.00 14.01  ? 481 GLY A CA     1 
ATOM   2364 C  C      . GLY A 1 338 ? 208.248 153.180 158.855 1.00 17.10  ? 481 GLY A C      1 
ATOM   2365 O  O      . GLY A 1 338 ? 207.399 152.386 158.440 1.00 18.65  ? 481 GLY A O      1 
ATOM   2366 N  N      . GLY A 1 339 ? 208.460 153.394 160.155 1.00 19.28  ? 482 GLY A N      1 
ATOM   2367 C  CA     . GLY A 1 339 ? 207.641 152.718 161.146 1.00 16.23  ? 482 GLY A CA     1 
ATOM   2368 C  C      . GLY A 1 339 ? 206.192 153.165 161.110 1.00 18.52  ? 482 GLY A C      1 
ATOM   2369 O  O      . GLY A 1 339 ? 205.278 152.353 161.276 1.00 20.24  ? 482 GLY A O      1 
ATOM   2370 N  N      . ARG A 1 340 ? 205.962 154.461 160.897 1.00 20.44  ? 483 ARG A N      1 
ATOM   2371 C  CA     . ARG A 1 340 ? 204.603 154.979 160.806 1.00 19.45  ? 483 ARG A CA     1 
ATOM   2372 C  C      . ARG A 1 340 ? 203.913 154.550 159.518 1.00 22.16  ? 483 ARG A C      1 
ATOM   2373 O  O      . ARG A 1 340 ? 202.687 154.400 159.497 1.00 24.59  ? 483 ARG A O      1 
ATOM   2374 C  CB     . ARG A 1 340 ? 204.621 156.505 160.912 1.00 22.01  ? 483 ARG A CB     1 
ATOM   2375 C  CG     . ARG A 1 340 ? 203.256 157.158 160.802 1.00 26.74  ? 483 ARG A CG     1 
ATOM   2376 C  CD     . ARG A 1 340 ? 203.384 158.663 160.648 1.00 28.75  ? 483 ARG A CD     1 
ATOM   2377 N  NE     . ARG A 1 340 ? 202.084 159.321 160.606 1.00 41.97  ? 483 ARG A NE     1 
ATOM   2378 C  CZ     . ARG A 1 340 ? 201.514 159.920 161.643 1.00 45.59  ? 483 ARG A CZ     1 
ATOM   2379 N  NH1    . ARG A 1 340 ? 202.104 159.966 162.825 1.00 43.76  ? 483 ARG A NH1    1 
ATOM   2380 N  NH2    . ARG A 1 340 ? 200.320 160.487 161.489 1.00 41.78  ? 483 ARG A NH2    1 
ATOM   2381 N  N      . ALA A 1 341 ? 204.676 154.351 158.441 1.00 21.53  ? 484 ALA A N      1 
ATOM   2382 C  CA     . ALA A 1 341 ? 204.078 153.932 157.179 1.00 19.22  ? 484 ALA A CA     1 
ATOM   2383 C  C      . ALA A 1 341 ? 203.611 152.483 157.228 1.00 19.74  ? 484 ALA A C      1 
ATOM   2384 O  O      . ALA A 1 341 ? 202.624 152.131 156.572 1.00 22.68  ? 484 ALA A O      1 
ATOM   2385 C  CB     . ALA A 1 341 ? 205.071 154.132 156.035 1.00 17.25  ? 484 ALA A CB     1 
ATOM   2386 N  N      . ALA A 1 342 ? 204.301 151.630 157.989 1.00 18.55  ? 485 ALA A N      1 
ATOM   2387 C  CA     . ALA A 1 342 ? 203.908 150.228 158.068 1.00 18.30  ? 485 ALA A CA     1 
ATOM   2388 C  C      . ALA A 1 342 ? 202.610 150.047 158.847 1.00 24.62  ? 485 ALA A C      1 
ATOM   2389 O  O      . ALA A 1 342 ? 201.807 149.169 158.512 1.00 27.33  ? 485 ALA A O      1 
ATOM   2390 C  CB     . ALA A 1 342 ? 205.027 149.402 158.702 1.00 15.48  ? 485 ALA A CB     1 
ATOM   2391 N  N      . GLU A 1 343 ? 202.390 150.856 159.885 1.00 23.87  ? 486 GLU A N      1 
ATOM   2392 C  CA     . GLU A 1 343 ? 201.152 150.757 160.650 1.00 25.04  ? 486 GLU A CA     1 
ATOM   2393 C  C      . GLU A 1 343 ? 199.940 151.149 159.815 1.00 25.52  ? 486 GLU A C      1 
ATOM   2394 O  O      . GLU A 1 343 ? 198.884 150.516 159.924 1.00 28.23  ? 486 GLU A O      1 
ATOM   2395 C  CB     . GLU A 1 343 ? 201.234 151.635 161.899 1.00 25.47  ? 486 GLU A CB     1 
ATOM   2396 C  CG     . GLU A 1 343 ? 202.175 151.116 162.971 1.00 27.79  ? 486 GLU A CG     1 
ATOM   2397 C  CD     . GLU A 1 343 ? 202.509 152.173 164.005 1.00 33.17  ? 486 GLU A CD     1 
ATOM   2398 O  OE1    . GLU A 1 343 ? 202.098 153.337 163.820 1.00 31.25  ? 486 GLU A OE1    1 
ATOM   2399 O  OE2    . GLU A 1 343 ? 203.181 151.841 165.004 1.00 34.00  ? 486 GLU A OE2    1 
ATOM   2400 N  N      . GLU A 1 344 ? 200.069 152.187 158.987 1.00 25.72  ? 487 GLU A N      1 
ATOM   2401 C  CA     . GLU A 1 344 ? 198.935 152.654 158.198 1.00 27.26  ? 487 GLU A CA     1 
ATOM   2402 C  C      . GLU A 1 344 ? 198.582 151.686 157.076 1.00 30.50  ? 487 GLU A C      1 
ATOM   2403 O  O      . GLU A 1 344 ? 197.400 151.516 156.758 1.00 33.74  ? 487 GLU A O      1 
ATOM   2404 C  CB     . GLU A 1 344 ? 199.235 154.039 157.625 1.00 29.03  ? 487 GLU A CB     1 
ATOM   2405 C  CG     . GLU A 1 344 ? 198.288 154.475 156.521 1.00 36.83  ? 487 GLU A CG     1 
ATOM   2406 C  CD     . GLU A 1 344 ? 198.062 155.973 156.505 1.00 51.62  ? 487 GLU A CD     1 
ATOM   2407 O  OE1    . GLU A 1 344 ? 198.625 156.671 157.373 1.00 54.31  ? 487 GLU A OE1    1 
ATOM   2408 O  OE2    . GLU A 1 344 ? 197.320 156.455 155.623 1.00 56.60  ? 487 GLU A OE2    1 
ATOM   2409 N  N      . VAL A 1 345 ? 199.581 151.047 156.468 1.00 26.07  ? 488 VAL A N      1 
ATOM   2410 C  CA     . VAL A 1 345 ? 199.318 150.206 155.306 1.00 23.48  ? 488 VAL A CA     1 
ATOM   2411 C  C      . VAL A 1 345 ? 198.816 148.824 155.711 1.00 26.01  ? 488 VAL A C      1 
ATOM   2412 O  O      . VAL A 1 345 ? 198.072 148.188 154.957 1.00 32.36  ? 488 VAL A O      1 
ATOM   2413 C  CB     . VAL A 1 345 ? 200.579 150.106 154.430 1.00 25.97  ? 488 VAL A CB     1 
ATOM   2414 C  CG1    . VAL A 1 345 ? 200.489 148.909 153.500 1.00 26.35  ? 488 VAL A CG1    1 
ATOM   2415 C  CG2    . VAL A 1 345 ? 200.773 151.386 153.635 1.00 24.53  ? 488 VAL A CG2    1 
ATOM   2416 N  N      . VAL A 1 346 ? 199.197 148.336 156.891 1.00 25.78  ? 489 VAL A N      1 
ATOM   2417 C  CA     . VAL A 1 346 ? 198.866 146.973 157.291 1.00 25.20  ? 489 VAL A CA     1 
ATOM   2418 C  C      . VAL A 1 346 ? 197.678 146.965 158.244 1.00 27.59  ? 489 VAL A C      1 
ATOM   2419 O  O      . VAL A 1 346 ? 196.851 146.048 158.212 1.00 29.08  ? 489 VAL A O      1 
ATOM   2420 C  CB     . VAL A 1 346 ? 200.081 146.273 157.928 1.00 26.42  ? 489 VAL A CB     1 
ATOM   2421 C  CG1    . VAL A 1 346 ? 199.699 144.883 158.410 1.00 23.23  ? 489 VAL A CG1    1 
ATOM   2422 C  CG2    . VAL A 1 346 ? 201.232 146.201 156.938 1.00 24.26  ? 489 VAL A CG2    1 
ATOM   2423 N  N      . PHE A 1 347 ? 197.581 147.984 159.100 1.00 28.48  ? 490 PHE A N      1 
ATOM   2424 C  CA     . PHE A 1 347 ? 196.539 148.039 160.114 1.00 26.52  ? 490 PHE A CA     1 
ATOM   2425 C  C      . PHE A 1 347 ? 195.630 149.254 160.016 1.00 28.57  ? 490 PHE A C      1 
ATOM   2426 O  O      . PHE A 1 347 ? 194.518 149.209 160.552 1.00 31.51  ? 490 PHE A O      1 
ATOM   2427 C  CB     . PHE A 1 347 ? 197.155 148.013 161.523 1.00 25.05  ? 490 PHE A CB     1 
ATOM   2428 C  CG     . PHE A 1 347 ? 197.910 146.753 161.835 1.00 27.19  ? 490 PHE A CG     1 
ATOM   2429 C  CD1    . PHE A 1 347 ? 197.238 145.592 162.174 1.00 24.22  ? 490 PHE A CD1    1 
ATOM   2430 C  CD2    . PHE A 1 347 ? 199.295 146.733 161.797 1.00 28.52  ? 490 PHE A CD2    1 
ATOM   2431 C  CE1    . PHE A 1 347 ? 197.931 144.433 162.464 1.00 25.08  ? 490 PHE A CE1    1 
ATOM   2432 C  CE2    . PHE A 1 347 ? 199.992 145.577 162.087 1.00 26.51  ? 490 PHE A CE2    1 
ATOM   2433 C  CZ     . PHE A 1 347 ? 199.310 144.426 162.421 1.00 26.49  ? 490 PHE A CZ     1 
ATOM   2434 N  N      . GLY A 1 348 ? 196.057 150.326 159.356 1.00 29.42  ? 491 GLY A N      1 
ATOM   2435 C  CA     . GLY A 1 348 ? 195.281 151.551 159.361 1.00 26.43  ? 491 GLY A CA     1 
ATOM   2436 C  C      . GLY A 1 348 ? 195.183 152.203 160.721 1.00 31.66  ? 491 GLY A C      1 
ATOM   2437 O  O      . GLY A 1 348 ? 194.147 152.790 161.047 1.00 35.58  ? 491 GLY A O      1 
ATOM   2438 N  N      . ASP A 1 349 ? 196.243 152.120 161.525 1.00 31.03  ? 492 ASP A N      1 
ATOM   2439 C  CA     . ASP A 1 349 ? 196.233 152.662 162.878 1.00 28.27  ? 492 ASP A CA     1 
ATOM   2440 C  C      . ASP A 1 349 ? 197.429 153.578 163.107 1.00 31.42  ? 492 ASP A C      1 
ATOM   2441 O  O      . ASP A 1 349 ? 198.212 153.829 162.186 1.00 37.97  ? 492 ASP A O      1 
ATOM   2442 C  CB     . ASP A 1 349 ? 196.230 151.525 163.903 1.00 30.92  ? 492 ASP A CB     1 
ATOM   2443 C  CG     . ASP A 1 349 ? 195.643 151.941 165.238 1.00 38.84  ? 492 ASP A CG     1 
ATOM   2444 O  OD1    . ASP A 1 349 ? 195.319 153.135 165.403 1.00 37.85  ? 492 ASP A OD1    1 
ATOM   2445 O  OD2    . ASP A 1 349 ? 195.510 151.072 166.124 1.00 38.97  ? 492 ASP A OD2    1 
ATOM   2446 N  N      . VAL A 1 350 ? 197.575 154.080 164.330 1.00 30.09  ? 493 VAL A N      1 
ATOM   2447 C  CA     . VAL A 1 350 ? 198.708 154.921 164.696 1.00 30.25  ? 493 VAL A CA     1 
ATOM   2448 C  C      . VAL A 1 350 ? 198.912 154.800 166.199 1.00 28.45  ? 493 VAL A C      1 
ATOM   2449 O  O      . VAL A 1 350 ? 197.949 154.797 166.970 1.00 32.07  ? 493 VAL A O      1 
ATOM   2450 C  CB     . VAL A 1 350 ? 198.485 156.390 164.264 1.00 26.77  ? 493 VAL A CB     1 
ATOM   2451 C  CG1    . VAL A 1 350 ? 197.155 156.900 164.787 1.00 30.99  ? 493 VAL A CG1    1 
ATOM   2452 C  CG2    . VAL A 1 350 ? 199.625 157.267 164.752 1.00 29.96  ? 493 VAL A CG2    1 
ATOM   2453 N  N      . THR A 1 351 ? 200.170 154.702 166.610 1.00 29.25  ? 494 THR A N      1 
ATOM   2454 C  CA     . THR A 1 351 ? 200.525 154.499 168.008 1.00 26.48  ? 494 THR A CA     1 
ATOM   2455 C  C      . THR A 1 351 ? 201.249 155.733 168.546 1.00 26.31  ? 494 THR A C      1 
ATOM   2456 O  O      . THR A 1 351 ? 201.439 156.728 167.842 1.00 26.20  ? 494 THR A O      1 
ATOM   2457 C  CB     . THR A 1 351 ? 201.379 153.239 168.172 1.00 28.70  ? 494 THR A CB     1 
ATOM   2458 O  OG1    . THR A 1 351 ? 202.617 153.401 167.468 1.00 33.24  ? 494 THR A OG1    1 
ATOM   2459 C  CG2    . THR A 1 351 ? 200.648 152.022 167.628 1.00 27.75  ? 494 THR A CG2    1 
ATOM   2460 N  N      . SER A 1 352 ? 201.655 155.654 169.814 1.00 28.86  ? 495 SER A N      1 
ATOM   2461 C  CA     . SER A 1 352 ? 202.351 156.764 170.454 1.00 26.16  ? 495 SER A CA     1 
ATOM   2462 C  C      . SER A 1 352 ? 203.764 156.932 169.908 1.00 26.83  ? 495 SER A C      1 
ATOM   2463 O  O      . SER A 1 352 ? 204.256 158.060 169.789 1.00 25.94  ? 495 SER A O      1 
ATOM   2464 C  CB     . SER A 1 352 ? 202.387 156.555 171.968 1.00 20.15  ? 495 SER A CB     1 
ATOM   2465 O  OG     . SER A 1 352 ? 202.864 157.711 172.632 1.00 30.22  ? 495 SER A OG     1 
ATOM   2466 N  N      . GLY A 1 353 ? 204.431 155.826 169.575 1.00 28.15  ? 496 GLY A N      1 
ATOM   2467 C  CA     . GLY A 1 353 ? 205.774 155.923 169.029 1.00 24.57  ? 496 GLY A CA     1 
ATOM   2468 C  C      . GLY A 1 353 ? 205.807 156.609 167.676 1.00 25.98  ? 496 GLY A C      1 
ATOM   2469 O  O      . GLY A 1 353 ? 206.715 157.394 167.391 1.00 28.32  ? 496 GLY A O      1 
ATOM   2470 N  N      . ALA A 1 354 ? 204.819 156.324 166.825 1.00 26.33  ? 497 ALA A N      1 
ATOM   2471 C  CA     . ALA A 1 354 ? 204.754 156.965 165.518 1.00 24.96  ? 497 ALA A CA     1 
ATOM   2472 C  C      . ALA A 1 354 ? 204.454 158.454 165.616 1.00 27.56  ? 497 ALA A C      1 
ATOM   2473 O  O      . ALA A 1 354 ? 204.751 159.196 164.674 1.00 30.03  ? 497 ALA A O      1 
ATOM   2474 C  CB     . ALA A 1 354 ? 203.702 156.279 164.647 1.00 27.28  ? 497 ALA A CB     1 
ATOM   2475 N  N      . ALA A 1 355 ? 203.870 158.907 166.728 1.00 29.24  ? 498 ALA A N      1 
ATOM   2476 C  CA     . ALA A 1 355 ? 203.601 160.329 166.899 1.00 27.68  ? 498 ALA A CA     1 
ATOM   2477 C  C      . ALA A 1 355 ? 204.865 161.114 167.222 1.00 31.24  ? 498 ALA A C      1 
ATOM   2478 O  O      . ALA A 1 355 ? 204.987 162.275 166.818 1.00 31.72  ? 498 ALA A O      1 
ATOM   2479 C  CB     . ALA A 1 355 ? 202.555 160.540 167.995 1.00 23.58  ? 498 ALA A CB     1 
ATOM   2480 N  N      . ASN A 1 356 ? 205.805 160.507 167.950 1.00 29.84  ? 499 ASN A N      1 
ATOM   2481 C  CA     . ASN A 1 356 ? 207.081 161.162 168.211 1.00 30.71  ? 499 ASN A CA     1 
ATOM   2482 C  C      . ASN A 1 356 ? 207.948 161.237 166.962 1.00 32.11  ? 499 ASN A C      1 
ATOM   2483 O  O      . ASN A 1 356 ? 208.689 162.210 166.785 1.00 36.06  ? 499 ASN A O      1 
ATOM   2484 C  CB     . ASN A 1 356 ? 207.831 160.431 169.325 1.00 33.23  ? 499 ASN A CB     1 
ATOM   2485 C  CG     . ASN A 1 356 ? 207.142 160.553 170.668 1.00 48.31  ? 499 ASN A CG     1 
ATOM   2486 O  OD1    . ASN A 1 356 ? 206.639 161.618 171.026 1.00 55.12  ? 499 ASN A OD1    1 
ATOM   2487 N  ND2    . ASN A 1 356 ? 207.117 159.460 171.423 1.00 48.56  ? 499 ASN A ND2    1 
ATOM   2488 N  N      . ASP A 1 357 ? 207.871 160.227 166.092 1.00 30.89  ? 500 ASP A N      1 
ATOM   2489 C  CA     . ASP A 1 357 ? 208.665 160.242 164.869 1.00 25.97  ? 500 ASP A CA     1 
ATOM   2490 C  C      . ASP A 1 357 ? 208.270 161.404 163.966 1.00 27.81  ? 500 ASP A C      1 
ATOM   2491 O  O      . ASP A 1 357 ? 209.138 162.079 163.400 1.00 33.54  ? 500 ASP A O      1 
ATOM   2492 C  CB     . ASP A 1 357 ? 208.511 158.913 164.130 1.00 26.80  ? 500 ASP A CB     1 
ATOM   2493 C  CG     . ASP A 1 357 ? 209.188 157.767 164.850 1.00 27.81  ? 500 ASP A CG     1 
ATOM   2494 O  OD1    . ASP A 1 357 ? 210.059 158.031 165.702 1.00 32.78  ? 500 ASP A OD1    1 
ATOM   2495 O  OD2    . ASP A 1 357 ? 208.849 156.600 164.563 1.00 29.94  ? 500 ASP A OD2    1 
ATOM   2496 N  N      . ILE A 1 358 ? 206.967 161.654 163.818 1.00 28.15  ? 501 ILE A N      1 
ATOM   2497 C  CA     . ILE A 1 358 ? 206.515 162.763 162.990 1.00 29.41  ? 501 ILE A CA     1 
ATOM   2498 C  C      . ILE A 1 358 ? 206.906 164.105 163.590 1.00 30.41  ? 501 ILE A C      1 
ATOM   2499 O  O      . ILE A 1 358 ? 207.118 165.073 162.851 1.00 34.05  ? 501 ILE A O      1 
ATOM   2500 C  CB     . ILE A 1 358 ? 204.993 162.690 162.772 1.00 31.29  ? 501 ILE A CB     1 
ATOM   2501 C  CG1    . ILE A 1 358 ? 204.566 163.647 161.657 1.00 31.80  ? 501 ILE A CG1    1 
ATOM   2502 C  CG2    . ILE A 1 358 ? 204.255 163.008 164.061 1.00 34.67  ? 501 ILE A CG2    1 
ATOM   2503 C  CD1    . ILE A 1 358 ? 204.713 163.071 160.268 1.00 34.73  ? 501 ILE A CD1    1 
ATOM   2504 N  N      . GLU A 1 359 ? 207.004 164.192 164.917 1.00 32.46  ? 502 GLU A N      1 
ATOM   2505 C  CA     . GLU A 1 359 ? 207.410 165.438 165.555 1.00 34.70  ? 502 GLU A CA     1 
ATOM   2506 C  C      . GLU A 1 359 ? 208.891 165.723 165.330 1.00 37.39  ? 502 GLU A C      1 
ATOM   2507 O  O      . GLU A 1 359 ? 209.276 166.875 165.106 1.00 36.78  ? 502 GLU A O      1 
ATOM   2508 C  CB     . GLU A 1 359 ? 207.094 165.386 167.050 1.00 37.07  ? 502 GLU A CB     1 
ATOM   2509 C  CG     . GLU A 1 359 ? 206.993 166.747 167.715 1.00 43.23  ? 502 GLU A CG     1 
ATOM   2510 C  CD     . GLU A 1 359 ? 208.244 167.109 168.490 1.00 58.15  ? 502 GLU A CD     1 
ATOM   2511 O  OE1    . GLU A 1 359 ? 209.021 166.193 168.830 1.00 57.33  ? 502 GLU A OE1    1 
ATOM   2512 O  OE2    . GLU A 1 359 ? 208.449 168.311 168.761 1.00 68.48  ? 502 GLU A OE2    1 
ATOM   2513 N  N      . ARG A 1 360 ? 209.733 164.689 165.392 1.00 36.07  ? 503 ARG A N      1 
ATOM   2514 C  CA     . ARG A 1 360 ? 211.153 164.874 165.115 1.00 34.34  ? 503 ARG A CA     1 
ATOM   2515 C  C      . ARG A 1 360 ? 211.398 165.235 163.656 1.00 36.01  ? 503 ARG A C      1 
ATOM   2516 O  O      . ARG A 1 360 ? 212.270 166.061 163.361 1.00 38.87  ? 503 ARG A O      1 
ATOM   2517 C  CB     . ARG A 1 360 ? 211.931 163.612 165.484 1.00 34.30  ? 503 ARG A CB     1 
ATOM   2518 C  CG     . ARG A 1 360 ? 212.374 163.555 166.935 1.00 44.55  ? 503 ARG A CG     1 
ATOM   2519 C  CD     . ARG A 1 360 ? 212.956 162.195 167.279 1.00 49.53  ? 503 ARG A CD     1 
ATOM   2520 N  NE     . ARG A 1 360 ? 214.139 161.892 166.483 1.00 55.01  ? 503 ARG A NE     1 
ATOM   2521 C  CZ     . ARG A 1 360 ? 214.632 160.675 166.305 1.00 52.89  ? 503 ARG A CZ     1 
ATOM   2522 N  NH1    . ARG A 1 360 ? 214.069 159.613 166.857 1.00 47.22  ? 503 ARG A NH1    1 
ATOM   2523 N  NH2    . ARG A 1 360 ? 215.718 160.518 165.553 1.00 46.48  ? 503 ARG A NH2    1 
ATOM   2524 N  N      . ALA A 1 361 ? 210.647 164.630 162.734 1.00 33.26  ? 504 ALA A N      1 
ATOM   2525 C  CA     . ALA A 1 361 ? 210.831 164.926 161.318 1.00 31.05  ? 504 ALA A CA     1 
ATOM   2526 C  C      . ALA A 1 361 ? 210.451 166.363 160.987 1.00 32.98  ? 504 ALA A C      1 
ATOM   2527 O  O      . ALA A 1 361 ? 211.066 166.977 160.109 1.00 35.23  ? 504 ALA A O      1 
ATOM   2528 C  CB     . ALA A 1 361 ? 210.016 163.952 160.467 1.00 25.93  ? 504 ALA A CB     1 
ATOM   2529 N  N      . THR A 1 362 ? 209.447 166.913 161.672 1.00 34.96  ? 505 THR A N      1 
ATOM   2530 C  CA     . THR A 1 362 ? 209.015 168.276 161.382 1.00 33.86  ? 505 THR A CA     1 
ATOM   2531 C  C      . THR A 1 362 ? 210.087 169.297 161.737 1.00 38.52  ? 505 THR A C      1 
ATOM   2532 O  O      . THR A 1 362 ? 210.246 170.296 161.028 1.00 42.93  ? 505 THR A O      1 
ATOM   2533 C  CB     . THR A 1 362 ? 207.719 168.588 162.130 1.00 35.16  ? 505 THR A CB     1 
ATOM   2534 O  OG1    . THR A 1 362 ? 206.653 167.795 161.594 1.00 36.97  ? 505 THR A OG1    1 
ATOM   2535 C  CG2    . THR A 1 362 ? 207.365 170.061 161.994 1.00 36.21  ? 505 THR A CG2    1 
ATOM   2536 N  N      . GLU A 1 363 ? 210.828 169.070 162.821 1.00 40.11  ? 506 GLU A N      1 
ATOM   2537 C  CA     . GLU A 1 363 ? 211.895 169.980 163.214 1.00 38.19  ? 506 GLU A CA     1 
ATOM   2538 C  C      . GLU A 1 363 ? 213.143 169.837 162.356 1.00 40.28  ? 506 GLU A C      1 
ATOM   2539 O  O      . GLU A 1 363 ? 213.896 170.807 162.218 1.00 44.94  ? 506 GLU A O      1 
ATOM   2540 C  CB     . GLU A 1 363 ? 212.260 169.764 164.686 1.00 42.00  ? 506 GLU A CB     1 
ATOM   2541 C  CG     . GLU A 1 363 ? 212.872 168.409 164.985 1.00 46.68  ? 506 GLU A CG     1 
ATOM   2542 C  CD     . GLU A 1 363 ? 214.366 168.485 165.221 1.00 59.84  ? 506 GLU A CD     1 
ATOM   2543 O  OE1    . GLU A 1 363 ? 214.898 169.611 165.315 1.00 62.11  ? 506 GLU A OE1    1 
ATOM   2544 O  OE2    . GLU A 1 363 ? 215.010 167.418 165.312 1.00 61.76  ? 506 GLU A OE2    1 
ATOM   2545 N  N      . ILE A 1 364 ? 213.384 168.657 161.784 1.00 40.58  ? 507 ILE A N      1 
ATOM   2546 C  CA     . ILE A 1 364 ? 214.495 168.497 160.852 1.00 38.70  ? 507 ILE A CA     1 
ATOM   2547 C  C      . ILE A 1 364 ? 214.211 169.233 159.549 1.00 37.31  ? 507 ILE A C      1 
ATOM   2548 O  O      . ILE A 1 364 ? 215.096 169.885 158.985 1.00 38.43  ? 507 ILE A O      1 
ATOM   2549 C  CB     . ILE A 1 364 ? 214.778 167.004 160.609 1.00 37.35  ? 507 ILE A CB     1 
ATOM   2550 C  CG1    . ILE A 1 364 ? 215.449 166.382 161.834 1.00 48.44  ? 507 ILE A CG1    1 
ATOM   2551 C  CG2    . ILE A 1 364 ? 215.643 166.821 159.372 1.00 32.05  ? 507 ILE A CG2    1 
ATOM   2552 C  CD1    . ILE A 1 364 ? 215.690 164.894 161.709 1.00 45.18  ? 507 ILE A CD1    1 
ATOM   2553 N  N      . ALA A 1 365 ? 212.977 169.141 159.050 1.00 35.22  ? 508 ALA A N      1 
ATOM   2554 C  CA     . ALA A 1 365 ? 212.610 169.849 157.830 1.00 34.00  ? 508 ALA A CA     1 
ATOM   2555 C  C      . ALA A 1 365 ? 212.620 171.359 158.013 1.00 38.07  ? 508 ALA A C      1 
ATOM   2556 O  O      . ALA A 1 365 ? 212.776 172.089 157.028 1.00 39.08  ? 508 ALA A O      1 
ATOM   2557 C  CB     . ALA A 1 365 ? 211.231 169.392 157.351 1.00 31.42  ? 508 ALA A CB     1 
ATOM   2558 N  N      . ARG A 1 366 ? 212.459 171.844 159.245 1.00 40.07  ? 509 ARG A N      1 
ATOM   2559 C  CA     . ARG A 1 366 ? 212.496 173.281 159.491 1.00 41.83  ? 509 ARG A CA     1 
ATOM   2560 C  C      . ARG A 1 366 ? 213.903 173.847 159.351 1.00 43.13  ? 509 ARG A C      1 
ATOM   2561 O  O      . ARG A 1 366 ? 214.069 174.962 158.844 1.00 46.29  ? 509 ARG A O      1 
ATOM   2562 C  CB     . ARG A 1 366 ? 211.938 173.590 160.880 1.00 43.84  ? 509 ARG A CB     1 
ATOM   2563 C  CG     . ARG A 1 366 ? 211.542 175.042 161.081 1.00 50.06  ? 509 ARG A CG     1 
ATOM   2564 C  CD     . ARG A 1 366 ? 210.723 175.218 162.348 1.00 56.61  ? 509 ARG A CD     1 
ATOM   2565 N  NE     . ARG A 1 366 ? 209.330 174.835 162.155 1.00 69.80  ? 509 ARG A NE     1 
ATOM   2566 C  CZ     . ARG A 1 366 ? 208.703 173.904 162.862 1.00 70.30  ? 509 ARG A CZ     1 
ATOM   2567 N  NH1    . ARG A 1 366 ? 209.319 173.232 163.821 1.00 63.34  ? 509 ARG A NH1    1 
ATOM   2568 N  NH2    . ARG A 1 366 ? 207.426 173.640 162.599 1.00 63.48  ? 509 ARG A NH2    1 
ATOM   2569 N  N      . ASN A 1 367 ? 214.920 173.106 159.793 1.00 39.94  ? 510 ASN A N      1 
ATOM   2570 C  CA     . ASN A 1 367 ? 216.299 173.543 159.619 1.00 43.44  ? 510 ASN A CA     1 
ATOM   2571 C  C      . ASN A 1 367 ? 216.783 173.390 158.184 1.00 44.85  ? 510 ASN A C      1 
ATOM   2572 O  O      . ASN A 1 367 ? 217.709 174.100 157.779 1.00 49.04  ? 510 ASN A O      1 
ATOM   2573 C  CB     . ASN A 1 367 ? 217.221 172.765 160.560 1.00 45.78  ? 510 ASN A CB     1 
ATOM   2574 C  CG     . ASN A 1 367 ? 216.900 173.006 162.021 1.00 55.66  ? 510 ASN A CG     1 
ATOM   2575 O  OD1    . ASN A 1 367 ? 216.871 172.074 162.824 1.00 62.44  ? 510 ASN A OD1    1 
ATOM   2576 N  ND2    . ASN A 1 367 ? 216.655 174.262 162.373 1.00 56.72  ? 510 ASN A ND2    1 
ATOM   2577 N  N      . MET A 1 368 ? 216.180 172.486 157.412 1.00 43.15  ? 511 MET A N      1 
ATOM   2578 C  CA     . MET A 1 368 ? 216.571 172.311 156.019 1.00 40.86  ? 511 MET A CA     1 
ATOM   2579 C  C      . MET A 1 368 ? 216.139 173.485 155.153 1.00 43.31  ? 511 MET A C      1 
ATOM   2580 O  O      . MET A 1 368 ? 216.829 173.822 154.185 1.00 44.53  ? 511 MET A O      1 
ATOM   2581 C  CB     . MET A 1 368 ? 215.984 171.010 155.470 1.00 39.91  ? 511 MET A CB     1 
ATOM   2582 C  CG     . MET A 1 368 ? 216.298 170.754 154.007 1.00 46.34  ? 511 MET A CG     1 
ATOM   2583 S  SD     . MET A 1 368 ? 215.349 169.384 153.319 1.00 63.90  ? 511 MET A SD     1 
ATOM   2584 C  CE     . MET A 1 368 ? 215.733 168.086 154.490 1.00 41.65  ? 511 MET A CE     1 
ATOM   2585 N  N      . VAL A 1 369 ? 215.009 174.115 155.479 1.00 44.43  ? 512 VAL A N      1 
ATOM   2586 C  CA     . VAL A 1 369 ? 214.537 175.249 154.690 1.00 44.10  ? 512 VAL A CA     1 
ATOM   2587 C  C      . VAL A 1 369 ? 215.454 176.451 154.876 1.00 46.43  ? 512 VAL A C      1 
ATOM   2588 O  O      . VAL A 1 369 ? 215.766 177.165 153.916 1.00 50.67  ? 512 VAL A O      1 
ATOM   2589 C  CB     . VAL A 1 369 ? 213.081 175.584 155.057 1.00 44.83  ? 512 VAL A CB     1 
ATOM   2590 C  CG1    . VAL A 1 369 ? 212.734 176.997 154.617 1.00 49.88  ? 512 VAL A CG1    1 
ATOM   2591 C  CG2    . VAL A 1 369 ? 212.130 174.578 154.431 1.00 43.94  ? 512 VAL A CG2    1 
ATOM   2592 N  N      . SER A 1 370 ? 215.898 176.697 156.110 1.00 44.22  ? 513 SER A N      1 
ATOM   2593 C  CA     . SER A 1 370 ? 216.731 177.858 156.396 1.00 48.36  ? 513 SER A CA     1 
ATOM   2594 C  C      . SER A 1 370 ? 218.170 177.693 155.923 1.00 50.30  ? 513 SER A C      1 
ATOM   2595 O  O      . SER A 1 370 ? 218.838 178.699 155.660 1.00 53.01  ? 513 SER A O      1 
ATOM   2596 C  CB     . SER A 1 370 ? 216.718 178.158 157.897 1.00 49.16  ? 513 SER A CB     1 
ATOM   2597 O  OG     . SER A 1 370 ? 217.363 177.132 158.629 1.00 51.05  ? 513 SER A OG     1 
ATOM   2598 N  N      . GLN A 1 371 ? 218.663 176.459 155.811 1.00 48.54  ? 514 GLN A N      1 
ATOM   2599 C  CA     . GLN A 1 371 ? 220.045 176.217 155.417 1.00 46.36  ? 514 GLN A CA     1 
ATOM   2600 C  C      . GLN A 1 371 ? 220.209 175.877 153.943 1.00 46.42  ? 514 GLN A C      1 
ATOM   2601 O  O      . GLN A 1 371 ? 221.271 176.155 153.377 1.00 50.38  ? 514 GLN A O      1 
ATOM   2602 C  CB     . GLN A 1 371 ? 220.646 175.083 156.256 1.00 44.90  ? 514 GLN A CB     1 
ATOM   2603 C  CG     . GLN A 1 371 ? 221.126 175.512 157.631 1.00 48.87  ? 514 GLN A CG     1 
ATOM   2604 C  CD     . GLN A 1 371 ? 221.480 174.333 158.515 1.00 58.40  ? 514 GLN A CD     1 
ATOM   2605 O  OE1    . GLN A 1 371 ? 221.177 173.186 158.188 1.00 60.18  ? 514 GLN A OE1    1 
ATOM   2606 N  NE2    . GLN A 1 371 ? 222.126 174.609 159.641 1.00 62.69  ? 514 GLN A NE2    1 
ATOM   2607 N  N      . LEU A 1 372 ? 219.197 175.286 153.311 1.00 45.75  ? 515 LEU A N      1 
ATOM   2608 C  CA     . LEU A 1 372 ? 219.279 174.884 151.913 1.00 43.70  ? 515 LEU A CA     1 
ATOM   2609 C  C      . LEU A 1 372 ? 218.443 175.770 150.999 1.00 45.45  ? 515 LEU A C      1 
ATOM   2610 O  O      . LEU A 1 372 ? 218.307 175.463 149.810 1.00 47.30  ? 515 LEU A O      1 
ATOM   2611 C  CB     . LEU A 1 372 ? 218.855 173.422 151.758 1.00 40.50  ? 515 LEU A CB     1 
ATOM   2612 C  CG     . LEU A 1 372 ? 219.872 172.374 152.215 1.00 36.31  ? 515 LEU A CG     1 
ATOM   2613 C  CD1    . LEU A 1 372 ? 219.274 170.979 152.142 1.00 39.43  ? 515 LEU A CD1    1 
ATOM   2614 C  CD2    . LEU A 1 372 ? 221.142 172.459 151.386 1.00 35.02  ? 515 LEU A CD2    1 
ATOM   2615 N  N      . GLY A 1 373 ? 217.883 176.857 151.519 1.00 44.77  ? 516 GLY A N      1 
ATOM   2616 C  CA     . GLY A 1 373 ? 217.071 177.751 150.716 1.00 48.81  ? 516 GLY A CA     1 
ATOM   2617 C  C      . GLY A 1 373 ? 215.669 177.229 150.474 1.00 51.36  ? 516 GLY A C      1 
ATOM   2618 O  O      . GLY A 1 373 ? 215.352 176.755 149.383 1.00 54.25  ? 516 GLY A O      1 
ATOM   2619 N  N      . LYS A 1 409 ? 204.347 181.526 154.775 1.00 73.95  ? 552 LYS A N      1 
ATOM   2620 C  CA     . LYS A 1 409 ? 204.923 180.930 153.576 1.00 79.20  ? 552 LYS A CA     1 
ATOM   2621 C  C      . LYS A 1 409 ? 205.985 179.898 153.938 1.00 77.75  ? 552 LYS A C      1 
ATOM   2622 O  O      . LYS A 1 409 ? 206.131 178.882 153.260 1.00 75.62  ? 552 LYS A O      1 
ATOM   2623 C  CB     . LYS A 1 409 ? 205.521 182.008 152.667 1.00 80.06  ? 552 LYS A CB     1 
ATOM   2624 C  CG     . LYS A 1 409 ? 206.644 182.824 153.295 1.00 85.72  ? 552 LYS A CG     1 
ATOM   2625 C  CD     . LYS A 1 409 ? 206.118 183.818 154.321 1.00 92.43  ? 552 LYS A CD     1 
ATOM   2626 C  CE     . LYS A 1 409 ? 207.109 184.947 154.558 1.00 91.10  ? 552 LYS A CE     1 
ATOM   2627 N  NZ     . LYS A 1 409 ? 206.618 185.909 155.582 1.00 86.05  ? 552 LYS A NZ     1 
ATOM   2628 N  N      . ILE A 1 410 ? 206.729 180.167 155.011 1.00 77.44  ? 553 ILE A N      1 
ATOM   2629 C  CA     . ILE A 1 410 ? 207.736 179.216 155.468 1.00 71.93  ? 553 ILE A CA     1 
ATOM   2630 C  C      . ILE A 1 410 ? 207.079 177.956 156.016 1.00 69.03  ? 553 ILE A C      1 
ATOM   2631 O  O      . ILE A 1 410 ? 207.545 176.840 155.764 1.00 69.64  ? 553 ILE A O      1 
ATOM   2632 C  CB     . ILE A 1 410 ? 208.657 179.874 156.510 1.00 69.54  ? 553 ILE A CB     1 
ATOM   2633 C  CG1    . ILE A 1 410 ? 209.806 180.607 155.816 1.00 68.68  ? 553 ILE A CG1    1 
ATOM   2634 C  CG2    . ILE A 1 410 ? 209.191 178.831 157.478 1.00 67.43  ? 553 ILE A CG2    1 
ATOM   2635 C  CD1    . ILE A 1 410 ? 210.756 181.293 156.771 1.00 67.53  ? 553 ILE A CD1    1 
ATOM   2636 N  N      . ASP A 1 411 ? 205.991 178.111 156.774 1.00 68.04  ? 554 ASP A N      1 
ATOM   2637 C  CA     . ASP A 1 411 ? 205.289 176.945 157.299 1.00 67.88  ? 554 ASP A CA     1 
ATOM   2638 C  C      . ASP A 1 411 ? 204.694 176.099 156.182 1.00 65.66  ? 554 ASP A C      1 
ATOM   2639 O  O      . ASP A 1 411 ? 204.534 174.884 156.345 1.00 64.58  ? 554 ASP A O      1 
ATOM   2640 C  CB     . ASP A 1 411 ? 204.195 177.384 158.272 1.00 73.26  ? 554 ASP A CB     1 
ATOM   2641 C  CG     . ASP A 1 411 ? 204.755 178.000 159.536 1.00 81.99  ? 554 ASP A CG     1 
ATOM   2642 O  OD1    . ASP A 1 411 ? 205.872 178.557 159.484 1.00 85.26  ? 554 ASP A OD1    1 
ATOM   2643 O  OD2    . ASP A 1 411 ? 204.080 177.926 160.584 1.00 82.73  ? 554 ASP A OD2    1 
ATOM   2644 N  N      . GLU A 1 412 ? 204.360 176.715 155.047 1.00 65.46  ? 555 GLU A N      1 
ATOM   2645 C  CA     . GLU A 1 412 ? 203.822 175.960 153.923 1.00 67.68  ? 555 GLU A CA     1 
ATOM   2646 C  C      . GLU A 1 412 ? 204.894 175.127 153.233 1.00 62.98  ? 555 GLU A C      1 
ATOM   2647 O  O      . GLU A 1 412 ? 204.598 174.036 152.734 1.00 61.19  ? 555 GLU A O      1 
ATOM   2648 C  CB     . GLU A 1 412 ? 203.165 176.908 152.919 1.00 72.11  ? 555 GLU A CB     1 
ATOM   2649 C  CG     . GLU A 1 412 ? 202.522 176.207 151.735 1.00 79.71  ? 555 GLU A CG     1 
ATOM   2650 C  CD     . GLU A 1 412 ? 201.508 175.163 152.158 1.00 83.54  ? 555 GLU A CD     1 
ATOM   2651 O  OE1    . GLU A 1 412 ? 200.930 175.307 153.256 1.00 81.63  ? 555 GLU A OE1    1 
ATOM   2652 O  OE2    . GLU A 1 412 ? 201.289 174.200 151.395 1.00 78.56  ? 555 GLU A OE2    1 
ATOM   2653 N  N      . GLU A 1 413 ? 206.134 175.619 153.194 1.00 61.33  ? 556 GLU A N      1 
ATOM   2654 C  CA     . GLU A 1 413 ? 207.218 174.845 152.600 1.00 60.17  ? 556 GLU A CA     1 
ATOM   2655 C  C      . GLU A 1 413 ? 207.610 173.663 153.477 1.00 56.53  ? 556 GLU A C      1 
ATOM   2656 O  O      . GLU A 1 413 ? 207.921 172.585 152.959 1.00 53.96  ? 556 GLU A O      1 
ATOM   2657 C  CB     . GLU A 1 413 ? 208.427 175.746 152.349 1.00 61.08  ? 556 GLU A CB     1 
ATOM   2658 C  CG     . GLU A 1 413 ? 209.676 175.005 151.907 1.00 60.19  ? 556 GLU A CG     1 
ATOM   2659 C  CD     . GLU A 1 413 ? 209.590 174.524 150.472 1.00 69.44  ? 556 GLU A CD     1 
ATOM   2660 O  OE1    . GLU A 1 413 ? 208.668 174.960 149.752 1.00 71.89  ? 556 GLU A OE1    1 
ATOM   2661 O  OE2    . GLU A 1 413 ? 210.445 173.710 150.065 1.00 68.77  ? 556 GLU A OE2    1 
ATOM   2662 N  N      . VAL A 1 414 ? 207.602 173.843 154.799 1.00 54.23  ? 557 VAL A N      1 
ATOM   2663 C  CA     . VAL A 1 414 ? 207.939 172.746 155.700 1.00 49.43  ? 557 VAL A CA     1 
ATOM   2664 C  C      . VAL A 1 414 ? 206.901 171.636 155.603 1.00 48.07  ? 557 VAL A C      1 
ATOM   2665 O  O      . VAL A 1 414 ? 207.237 170.447 155.660 1.00 46.44  ? 557 VAL A O      1 
ATOM   2666 C  CB     . VAL A 1 414 ? 208.080 173.265 157.143 1.00 47.91  ? 557 VAL A CB     1 
ATOM   2667 C  CG1    . VAL A 1 414 ? 208.126 172.104 158.122 1.00 43.37  ? 557 VAL A CG1    1 
ATOM   2668 C  CG2    . VAL A 1 414 ? 209.322 174.130 157.275 1.00 47.47  ? 557 VAL A CG2    1 
ATOM   2669 N  N      . LYS A 1 415 ? 205.627 172.003 155.453 1.00 50.90  ? 558 LYS A N      1 
ATOM   2670 C  CA     . LYS A 1 415 ? 204.572 170.999 155.371 1.00 49.69  ? 558 LYS A CA     1 
ATOM   2671 C  C      . LYS A 1 415 ? 204.698 170.145 154.116 1.00 47.61  ? 558 LYS A C      1 
ATOM   2672 O  O      . LYS A 1 415 ? 204.383 168.951 154.148 1.00 45.88  ? 558 LYS A O      1 
ATOM   2673 C  CB     . LYS A 1 415 ? 203.203 171.678 155.416 1.00 57.08  ? 558 LYS A CB     1 
ATOM   2674 C  CG     . LYS A 1 415 ? 202.037 170.724 155.608 1.00 58.72  ? 558 LYS A CG     1 
ATOM   2675 C  CD     . LYS A 1 415 ? 201.485 170.252 154.274 1.00 65.36  ? 558 LYS A CD     1 
ATOM   2676 C  CE     . LYS A 1 415 ? 200.884 171.404 153.488 1.00 69.89  ? 558 LYS A CE     1 
ATOM   2677 N  NZ     . LYS A 1 415 ? 200.394 170.964 152.154 1.00 72.21  ? 558 LYS A NZ     1 
ATOM   2678 N  N      . LYS A 1 416 ? 205.153 170.731 153.007 1.00 50.39  ? 559 LYS A N      1 
ATOM   2679 C  CA     . LYS A 1 416 ? 205.276 169.978 151.764 1.00 46.99  ? 559 LYS A CA     1 
ATOM   2680 C  C      . LYS A 1 416 ? 206.425 168.979 151.806 1.00 41.86  ? 559 LYS A C      1 
ATOM   2681 O  O      . LYS A 1 416 ? 206.308 167.886 151.241 1.00 41.36  ? 559 LYS A O      1 
ATOM   2682 C  CB     . LYS A 1 416 ? 205.459 170.935 150.585 1.00 52.88  ? 559 LYS A CB     1 
ATOM   2683 C  CG     . LYS A 1 416 ? 204.198 171.690 150.199 1.00 63.38  ? 559 LYS A CG     1 
ATOM   2684 C  CD     . LYS A 1 416 ? 204.387 172.456 148.900 1.00 68.54  ? 559 LYS A CD     1 
ATOM   2685 C  CE     . LYS A 1 416 ? 205.201 173.720 149.117 1.00 72.60  ? 559 LYS A CE     1 
ATOM   2686 N  NZ     . LYS A 1 416 ? 205.250 174.566 147.893 1.00 74.79  ? 559 LYS A NZ     1 
ATOM   2687 N  N      . ILE A 1 417 ? 207.534 169.327 152.461 1.00 40.91  ? 560 ILE A N      1 
ATOM   2688 C  CA     . ILE A 1 417 ? 208.673 168.417 152.524 1.00 36.96  ? 560 ILE A CA     1 
ATOM   2689 C  C      . ILE A 1 417 ? 208.305 167.149 153.285 1.00 35.81  ? 560 ILE A C      1 
ATOM   2690 O  O      . ILE A 1 417 ? 208.646 166.037 152.866 1.00 34.61  ? 560 ILE A O      1 
ATOM   2691 C  CB     . ILE A 1 417 ? 209.887 169.123 153.154 1.00 39.46  ? 560 ILE A CB     1 
ATOM   2692 C  CG1    . ILE A 1 417 ? 210.437 170.189 152.204 1.00 41.38  ? 560 ILE A CG1    1 
ATOM   2693 C  CG2    . ILE A 1 417 ? 210.965 168.113 153.512 1.00 32.83  ? 560 ILE A CG2    1 
ATOM   2694 C  CD1    . ILE A 1 417 ? 211.362 171.183 152.871 1.00 41.29  ? 560 ILE A CD1    1 
ATOM   2695 N  N      . VAL A 1 418 ? 207.608 167.293 154.414 1.00 35.44  ? 561 VAL A N      1 
ATOM   2696 C  CA     . VAL A 1 418 ? 207.248 166.128 155.216 1.00 33.35  ? 561 VAL A CA     1 
ATOM   2697 C  C      . VAL A 1 418 ? 206.257 165.245 154.469 1.00 30.57  ? 561 VAL A C      1 
ATOM   2698 O  O      . VAL A 1 418 ? 206.348 164.013 154.513 1.00 31.74  ? 561 VAL A O      1 
ATOM   2699 C  CB     . VAL A 1 418 ? 206.692 166.573 156.581 1.00 33.33  ? 561 VAL A CB     1 
ATOM   2700 C  CG1    . VAL A 1 418 ? 206.112 165.384 157.331 1.00 31.02  ? 561 VAL A CG1    1 
ATOM   2701 C  CG2    . VAL A 1 418 ? 207.779 167.246 157.402 1.00 28.51  ? 561 VAL A CG2    1 
ATOM   2702 N  N      . THR A 1 419 ? 205.295 165.856 153.774 1.00 32.36  ? 562 THR A N      1 
ATOM   2703 C  CA     . THR A 1 419 ? 204.291 165.077 153.057 1.00 31.94  ? 562 THR A CA     1 
ATOM   2704 C  C      . THR A 1 419 ? 204.905 164.260 151.927 1.00 31.23  ? 562 THR A C      1 
ATOM   2705 O  O      . THR A 1 419 ? 204.509 163.110 151.712 1.00 32.27  ? 562 THR A O      1 
ATOM   2706 C  CB     . THR A 1 419 ? 203.201 165.998 152.509 1.00 37.58  ? 562 THR A CB     1 
ATOM   2707 O  OG1    . THR A 1 419 ? 202.526 166.641 153.597 1.00 41.66  ? 562 THR A OG1    1 
ATOM   2708 C  CG2    . THR A 1 419 ? 202.193 165.204 151.694 1.00 34.42  ? 562 THR A CG2    1 
ATOM   2709 N  N      . ASN A 1 420 ? 205.863 164.833 151.194 1.00 32.35  ? 563 ASN A N      1 
ATOM   2710 C  CA     . ASN A 1 420 ? 206.483 164.103 150.093 1.00 29.56  ? 563 ASN A CA     1 
ATOM   2711 C  C      . ASN A 1 420 ? 207.248 162.884 150.593 1.00 29.51  ? 563 ASN A C      1 
ATOM   2712 O  O      . ASN A 1 420 ? 207.194 161.814 149.975 1.00 28.83  ? 563 ASN A O      1 
ATOM   2713 C  CB     . ASN A 1 420 ? 207.406 165.031 149.303 1.00 32.80  ? 563 ASN A CB     1 
ATOM   2714 C  CG     . ASN A 1 420 ? 206.645 166.086 148.526 1.00 39.93  ? 563 ASN A CG     1 
ATOM   2715 O  OD1    . ASN A 1 420 ? 205.608 165.805 147.926 1.00 40.75  ? 563 ASN A OD1    1 
ATOM   2716 N  ND2    . ASN A 1 420 ? 207.158 167.311 148.533 1.00 40.41  ? 563 ASN A ND2    1 
ATOM   2717 N  N      . SER A 1 421 ? 207.970 163.024 151.708 1.00 26.91  ? 564 SER A N      1 
ATOM   2718 C  CA     . SER A 1 421 ? 208.721 161.896 152.247 1.00 22.65  ? 564 SER A CA     1 
ATOM   2719 C  C      . SER A 1 421 ? 207.799 160.783 152.729 1.00 22.86  ? 564 SER A C      1 
ATOM   2720 O  O      . SER A 1 421 ? 208.127 159.601 152.579 1.00 21.24  ? 564 SER A O      1 
ATOM   2721 C  CB     . SER A 1 421 ? 209.628 162.364 153.385 1.00 24.23  ? 564 SER A CB     1 
ATOM   2722 O  OG     . SER A 1 421 ? 210.419 163.469 152.987 1.00 28.57  ? 564 SER A OG     1 
ATOM   2723 N  N      . TYR A 1 422 ? 206.651 161.137 153.312 1.00 23.78  ? 565 TYR A N      1 
ATOM   2724 C  CA     . TYR A 1 422 ? 205.721 160.119 153.788 1.00 23.00  ? 565 TYR A CA     1 
ATOM   2725 C  C      . TYR A 1 422 ? 205.176 159.282 152.637 1.00 24.18  ? 565 TYR A C      1 
ATOM   2726 O  O      . TYR A 1 422 ? 205.025 158.062 152.768 1.00 23.29  ? 565 TYR A O      1 
ATOM   2727 C  CB     . TYR A 1 422 ? 204.580 160.774 154.565 1.00 26.79  ? 565 TYR A CB     1 
ATOM   2728 C  CG     . TYR A 1 422 ? 203.683 159.790 155.279 1.00 29.33  ? 565 TYR A CG     1 
ATOM   2729 C  CD1    . TYR A 1 422 ? 204.216 158.796 156.088 1.00 29.51  ? 565 TYR A CD1    1 
ATOM   2730 C  CD2    . TYR A 1 422 ? 202.304 159.853 155.142 1.00 30.85  ? 565 TYR A CD2    1 
ATOM   2731 C  CE1    . TYR A 1 422 ? 203.402 157.894 156.741 1.00 30.09  ? 565 TYR A CE1    1 
ATOM   2732 C  CE2    . TYR A 1 422 ? 201.481 158.955 155.791 1.00 34.20  ? 565 TYR A CE2    1 
ATOM   2733 C  CZ     . TYR A 1 422 ? 202.035 157.978 156.590 1.00 32.81  ? 565 TYR A CZ     1 
ATOM   2734 O  OH     . TYR A 1 422 ? 201.221 157.080 157.240 1.00 35.32  ? 565 TYR A OH     1 
ATOM   2735 N  N      . GLU A 1 423 ? 204.866 159.919 151.506 1.00 24.98  ? 566 GLU A N      1 
ATOM   2736 C  CA     . GLU A 1 423 ? 204.394 159.172 150.345 1.00 26.11  ? 566 GLU A CA     1 
ATOM   2737 C  C      . GLU A 1 423 ? 205.475 158.237 149.816 1.00 24.20  ? 566 GLU A C      1 
ATOM   2738 O  O      . GLU A 1 423 ? 205.180 157.114 149.392 1.00 27.66  ? 566 GLU A O      1 
ATOM   2739 C  CB     . GLU A 1 423 ? 203.936 160.135 149.251 1.00 28.30  ? 566 GLU A CB     1 
ATOM   2740 C  CG     . GLU A 1 423 ? 202.900 161.148 149.705 1.00 34.54  ? 566 GLU A CG     1 
ATOM   2741 C  CD     . GLU A 1 423 ? 201.671 160.496 150.305 1.00 50.49  ? 566 GLU A CD     1 
ATOM   2742 O  OE1    . GLU A 1 423 ? 201.175 159.509 149.721 1.00 52.75  ? 566 GLU A OE1    1 
ATOM   2743 O  OE2    . GLU A 1 423 ? 201.199 160.970 151.360 1.00 53.56  ? 566 GLU A OE2    1 
ATOM   2744 N  N      . ARG A 1 424 ? 206.731 158.686 149.832 1.00 21.42  ? 567 ARG A N      1 
ATOM   2745 C  CA     . ARG A 1 424 ? 207.826 157.850 149.352 1.00 18.54  ? 567 ARG A CA     1 
ATOM   2746 C  C      . ARG A 1 424 ? 207.963 156.583 150.189 1.00 20.50  ? 567 ARG A C      1 
ATOM   2747 O  O      . ARG A 1 424 ? 208.163 155.491 149.646 1.00 22.71  ? 567 ARG A O      1 
ATOM   2748 C  CB     . ARG A 1 424 ? 209.128 158.650 149.364 1.00 19.91  ? 567 ARG A CB     1 
ATOM   2749 C  CG     . ARG A 1 424 ? 210.312 157.947 148.725 1.00 19.50  ? 567 ARG A CG     1 
ATOM   2750 C  CD     . ARG A 1 424 ? 211.519 158.868 148.676 1.00 21.59  ? 567 ARG A CD     1 
ATOM   2751 N  NE     . ARG A 1 424 ? 212.723 158.182 148.223 1.00 26.71  ? 567 ARG A NE     1 
ATOM   2752 C  CZ     . ARG A 1 424 ? 213.952 158.494 148.609 1.00 29.10  ? 567 ARG A CZ     1 
ATOM   2753 N  NH1    . ARG A 1 424 ? 214.179 159.482 149.459 1.00 25.93  ? 567 ARG A NH1    1 
ATOM   2754 N  NH2    . ARG A 1 424 ? 214.979 157.797 148.132 1.00 31.60  ? 567 ARG A NH2    1 
ATOM   2755 N  N      . ALA A 1 425 ? 207.859 156.709 151.514 1.00 20.92  ? 568 ALA A N      1 
ATOM   2756 C  CA     . ALA A 1 425 ? 207.989 155.542 152.379 1.00 19.53  ? 568 ALA A CA     1 
ATOM   2757 C  C      . ALA A 1 425 ? 206.845 154.556 152.180 1.00 22.61  ? 568 ALA A C      1 
ATOM   2758 O  O      . ALA A 1 425 ? 207.065 153.341 152.219 1.00 21.58  ? 568 ALA A O      1 
ATOM   2759 C  CB     . ALA A 1 425 ? 208.067 155.978 153.842 1.00 15.99  ? 568 ALA A CB     1 
ATOM   2760 N  N      . LYS A 1 426 ? 205.623 155.053 151.971 1.00 22.17  ? 569 LYS A N      1 
ATOM   2761 C  CA     . LYS A 1 426 ? 204.481 154.161 151.802 1.00 24.62  ? 569 LYS A CA     1 
ATOM   2762 C  C      . LYS A 1 426 ? 204.597 153.321 150.536 1.00 27.53  ? 569 LYS A C      1 
ATOM   2763 O  O      . LYS A 1 426 ? 204.230 152.141 150.544 1.00 27.70  ? 569 LYS A O      1 
ATOM   2764 C  CB     . LYS A 1 426 ? 203.181 154.966 151.788 1.00 27.03  ? 569 LYS A CB     1 
ATOM   2765 C  CG     . LYS A 1 426 ? 202.656 155.310 153.171 1.00 30.09  ? 569 LYS A CG     1 
ATOM   2766 C  CD     . LYS A 1 426 ? 201.184 155.672 153.129 1.00 31.26  ? 569 LYS A CD     1 
ATOM   2767 C  CE     . LYS A 1 426 ? 200.989 157.147 152.829 1.00 35.53  ? 569 LYS A CE     1 
ATOM   2768 N  NZ     . LYS A 1 426 ? 199.553 157.487 152.646 1.00 44.08  ? 569 LYS A NZ     1 
ATOM   2769 N  N      . GLU A 1 427 ? 205.096 153.903 149.443 1.00 27.74  ? 570 GLU A N      1 
ATOM   2770 C  CA     . GLU A 1 427 ? 205.272 153.128 148.220 1.00 28.17  ? 570 GLU A CA     1 
ATOM   2771 C  C      . GLU A 1 427 ? 206.328 152.045 148.391 1.00 26.12  ? 570 GLU A C      1 
ATOM   2772 O  O      . GLU A 1 427 ? 206.196 150.957 147.821 1.00 28.72  ? 570 GLU A O      1 
ATOM   2773 C  CB     . GLU A 1 427 ? 205.639 154.051 147.057 1.00 25.77  ? 570 GLU A CB     1 
ATOM   2774 C  CG     . GLU A 1 427 ? 204.469 154.837 146.490 1.00 41.58  ? 570 GLU A CG     1 
ATOM   2775 C  CD     . GLU A 1 427 ? 203.173 154.045 146.493 1.00 55.12  ? 570 GLU A CD     1 
ATOM   2776 O  OE1    . GLU A 1 427 ? 203.012 153.162 145.624 1.00 54.02  ? 570 GLU A OE1    1 
ATOM   2777 O  OE2    . GLU A 1 427 ? 202.315 154.308 147.362 1.00 49.11  ? 570 GLU A OE2    1 
ATOM   2778 N  N      . ILE A 1 428 ? 207.377 152.321 149.166 1.00 23.34  ? 571 ILE A N      1 
ATOM   2779 C  CA     . ILE A 1 428 ? 208.382 151.301 149.440 1.00 24.15  ? 571 ILE A CA     1 
ATOM   2780 C  C      . ILE A 1 428 ? 207.803 150.181 150.295 1.00 26.81  ? 571 ILE A C      1 
ATOM   2781 O  O      . ILE A 1 428 ? 208.214 149.024 150.163 1.00 27.15  ? 571 ILE A O      1 
ATOM   2782 C  CB     . ILE A 1 428 ? 209.620 151.925 150.105 1.00 22.52  ? 571 ILE A CB     1 
ATOM   2783 C  CG1    . ILE A 1 428 ? 210.383 152.796 149.104 1.00 18.01  ? 571 ILE A CG1    1 
ATOM   2784 C  CG2    . ILE A 1 428 ? 210.527 150.841 150.666 1.00 17.70  ? 571 ILE A CG2    1 
ATOM   2785 C  CD1    . ILE A 1 428 ? 211.283 153.825 149.751 1.00 18.46  ? 571 ILE A CD1    1 
ATOM   2786 N  N      . ILE A 1 429 ? 206.870 150.498 151.194 1.00 26.07  ? 572 ILE A N      1 
ATOM   2787 C  CA     . ILE A 1 429 ? 206.257 149.466 152.025 1.00 24.12  ? 572 ILE A CA     1 
ATOM   2788 C  C      . ILE A 1 429 ? 205.343 148.570 151.198 1.00 27.95  ? 572 ILE A C      1 
ATOM   2789 O  O      . ILE A 1 429 ? 205.343 147.346 151.364 1.00 28.81  ? 572 ILE A O      1 
ATOM   2790 C  CB     . ILE A 1 429 ? 205.505 150.109 153.205 1.00 24.74  ? 572 ILE A CB     1 
ATOM   2791 C  CG1    . ILE A 1 429 ? 206.490 150.769 154.173 1.00 22.14  ? 572 ILE A CG1    1 
ATOM   2792 C  CG2    . ILE A 1 429 ? 204.665 149.071 153.929 1.00 20.99  ? 572 ILE A CG2    1 
ATOM   2793 C  CD1    . ILE A 1 429 ? 207.256 149.788 155.030 1.00 17.02  ? 572 ILE A CD1    1 
ATOM   2794 N  N      . ARG A 1 430 ? 204.550 149.157 150.297 1.00 28.68  ? 573 ARG A N      1 
ATOM   2795 C  CA     . ARG A 1 430 ? 203.657 148.358 149.463 1.00 27.31  ? 573 ARG A CA     1 
ATOM   2796 C  C      . ARG A 1 430 ? 204.446 147.347 148.642 1.00 29.54  ? 573 ARG A C      1 
ATOM   2797 O  O      . ARG A 1 430 ? 204.136 146.151 148.635 1.00 34.83  ? 573 ARG A O      1 
ATOM   2798 C  CB     . ARG A 1 430 ? 202.828 149.270 148.559 1.00 27.03  ? 573 ARG A CB     1 
ATOM   2799 C  CG     . ARG A 1 430 ? 201.494 149.678 149.156 1.00 28.21  ? 573 ARG A CG     1 
ATOM   2800 C  CD     . ARG A 1 430 ? 200.955 150.934 148.499 1.00 35.57  ? 573 ARG A CD     1 
ATOM   2801 N  NE     . ARG A 1 430 ? 200.007 151.631 149.359 1.00 39.92  ? 573 ARG A NE     1 
ATOM   2802 C  CZ     . ARG A 1 430 ? 199.922 152.950 149.464 1.00 44.79  ? 573 ARG A CZ     1 
ATOM   2803 N  NH1    . ARG A 1 430 ? 200.715 153.751 148.771 1.00 40.94  ? 573 ARG A NH1    1 
ATOM   2804 N  NH2    . ARG A 1 430 ? 199.020 153.479 150.285 1.00 43.72  ? 573 ARG A NH2    1 
ATOM   2805 N  N      . LYS A 1 431 ? 205.471 147.816 147.937 1.00 31.18  ? 574 LYS A N      1 
ATOM   2806 C  CA     . LYS A 1 431 ? 206.464 146.912 147.386 1.00 28.20  ? 574 LYS A CA     1 
ATOM   2807 C  C      . LYS A 1 431 ? 207.278 146.303 148.523 1.00 33.74  ? 574 LYS A C      1 
ATOM   2808 O  O      . LYS A 1 431 ? 207.349 146.843 149.629 1.00 40.79  ? 574 LYS A O      1 
ATOM   2809 C  CB     . LYS A 1 431 ? 207.372 147.651 146.404 1.00 27.96  ? 574 LYS A CB     1 
ATOM   2810 C  CG     . LYS A 1 431 ? 208.334 146.762 145.638 1.00 35.17  ? 574 LYS A CG     1 
ATOM   2811 C  CD     . LYS A 1 431 ? 209.087 147.560 144.587 1.00 37.61  ? 574 LYS A CD     1 
ATOM   2812 C  CE     . LYS A 1 431 ? 209.971 146.667 143.733 1.00 41.76  ? 574 LYS A CE     1 
ATOM   2813 N  NZ     . LYS A 1 431 ? 210.588 147.419 142.606 1.00 37.48  ? 574 LYS A NZ     1 
ATOM   2814 N  N      . TYR A 1 432 ? 207.879 145.148 148.258 1.00 30.63  ? 575 TYR A N      1 
ATOM   2815 C  CA     . TYR A 1 432 ? 208.646 144.413 149.257 1.00 34.23  ? 575 TYR A CA     1 
ATOM   2816 C  C      . TYR A 1 432 ? 207.783 143.931 150.415 1.00 31.88  ? 575 TYR A C      1 
ATOM   2817 O  O      . TYR A 1 432 ? 208.322 143.530 151.453 1.00 33.28  ? 575 TYR A O      1 
ATOM   2818 C  CB     . TYR A 1 432 ? 209.803 145.251 149.817 1.00 31.34  ? 575 TYR A CB     1 
ATOM   2819 C  CG     . TYR A 1 432 ? 210.747 145.794 148.770 1.00 33.05  ? 575 TYR A CG     1 
ATOM   2820 C  CD1    . TYR A 1 432 ? 211.655 144.964 148.129 1.00 32.60  ? 575 TYR A CD1    1 
ATOM   2821 C  CD2    . TYR A 1 432 ? 210.731 147.139 148.426 1.00 30.67  ? 575 TYR A CD2    1 
ATOM   2822 C  CE1    . TYR A 1 432 ? 212.520 145.457 147.173 1.00 34.88  ? 575 TYR A CE1    1 
ATOM   2823 C  CE2    . TYR A 1 432 ? 211.591 147.640 147.470 1.00 32.15  ? 575 TYR A CE2    1 
ATOM   2824 C  CZ     . TYR A 1 432 ? 212.484 146.795 146.847 1.00 39.16  ? 575 TYR A CZ     1 
ATOM   2825 O  OH     . TYR A 1 432 ? 213.344 147.289 145.894 1.00 40.66  ? 575 TYR A OH     1 
ATOM   2826 N  N      . ARG A 1 433 ? 206.455 143.965 150.273 1.00 33.38  ? 576 ARG A N      1 
ATOM   2827 C  CA     . ARG A 1 433 ? 205.583 143.553 151.368 1.00 31.32  ? 576 ARG A CA     1 
ATOM   2828 C  C      . ARG A 1 433 ? 205.820 142.101 151.759 1.00 35.82  ? 576 ARG A C      1 
ATOM   2829 O  O      . ARG A 1 433 ? 205.568 141.718 152.906 1.00 36.44  ? 576 ARG A O      1 
ATOM   2830 C  CB     . ARG A 1 433 ? 204.120 143.768 150.981 1.00 30.64  ? 576 ARG A CB     1 
ATOM   2831 C  CG     . ARG A 1 433 ? 203.126 143.030 151.861 1.00 31.64  ? 576 ARG A CG     1 
ATOM   2832 C  CD     . ARG A 1 433 ? 202.719 143.868 153.061 1.00 33.16  ? 576 ARG A CD     1 
ATOM   2833 N  NE     . ARG A 1 433 ? 201.765 143.169 153.914 1.00 33.10  ? 576 ARG A NE     1 
ATOM   2834 C  CZ     . ARG A 1 433 ? 200.478 143.475 154.007 1.00 31.15  ? 576 ARG A CZ     1 
ATOM   2835 N  NH1    . ARG A 1 433 ? 199.952 144.471 153.314 1.00 28.87  ? 576 ARG A NH1    1 
ATOM   2836 N  NH2    . ARG A 1 433 ? 199.699 142.761 154.815 1.00 28.70  ? 576 ARG A NH2    1 
ATOM   2837 N  N      . LYS A 1 434 ? 206.302 141.281 150.825 1.00 36.28  ? 577 LYS A N      1 
ATOM   2838 C  CA     . LYS A 1 434 ? 206.617 139.894 151.141 1.00 36.62  ? 577 LYS A CA     1 
ATOM   2839 C  C      . LYS A 1 434 ? 207.831 139.780 152.054 1.00 36.46  ? 577 LYS A C      1 
ATOM   2840 O  O      . LYS A 1 434 ? 207.854 138.920 152.941 1.00 41.44  ? 577 LYS A O      1 
ATOM   2841 C  CB     . LYS A 1 434 ? 206.848 139.103 149.853 1.00 43.14  ? 577 LYS A CB     1 
ATOM   2842 C  CG     . LYS A 1 434 ? 206.987 137.604 150.056 1.00 46.77  ? 577 LYS A CG     1 
ATOM   2843 C  CD     . LYS A 1 434 ? 208.447 137.187 150.086 1.00 49.73  ? 577 LYS A CD     1 
ATOM   2844 C  CE     . LYS A 1 434 ? 209.090 137.338 148.717 1.00 56.77  ? 577 LYS A CE     1 
ATOM   2845 N  NZ     . LYS A 1 434 ? 210.514 136.906 148.719 1.00 64.90  ? 577 LYS A NZ     1 
ATOM   2846 N  N      . GLN A 1 435 ? 208.842 140.629 151.855 1.00 33.75  ? 578 GLN A N      1 
ATOM   2847 C  CA     . GLN A 1 435 ? 210.011 140.602 152.727 1.00 35.88  ? 578 GLN A CA     1 
ATOM   2848 C  C      . GLN A 1 435 ? 209.678 141.098 154.128 1.00 35.50  ? 578 GLN A C      1 
ATOM   2849 O  O      . GLN A 1 435 ? 210.226 140.588 155.111 1.00 37.23  ? 578 GLN A O      1 
ATOM   2850 C  CB     . GLN A 1 435 ? 211.138 141.438 152.123 1.00 40.29  ? 578 GLN A CB     1 
ATOM   2851 C  CG     . GLN A 1 435 ? 211.813 140.801 150.918 1.00 46.30  ? 578 GLN A CG     1 
ATOM   2852 C  CD     . GLN A 1 435 ? 211.043 141.023 149.631 1.00 41.60  ? 578 GLN A CD     1 
ATOM   2853 O  OE1    . GLN A 1 435 ? 210.214 141.927 149.538 1.00 40.66  ? 578 GLN A OE1    1 
ATOM   2854 N  NE2    . GLN A 1 435 ? 211.318 140.198 148.629 1.00 44.57  ? 578 GLN A NE2    1 
ATOM   2855 N  N      . LEU A 1 436 ? 208.789 142.088 154.240 1.00 33.14  ? 579 LEU A N      1 
ATOM   2856 C  CA     . LEU A 1 436 ? 208.408 142.597 155.553 1.00 29.98  ? 579 LEU A CA     1 
ATOM   2857 C  C      . LEU A 1 436 ? 207.711 141.525 156.382 1.00 33.04  ? 579 LEU A C      1 
ATOM   2858 O  O      . LEU A 1 436 ? 207.952 141.412 157.590 1.00 35.68  ? 579 LEU A O      1 
ATOM   2859 C  CB     . LEU A 1 436 ? 207.511 143.825 155.396 1.00 25.90  ? 579 LEU A CB     1 
ATOM   2860 C  CG     . LEU A 1 436 ? 206.944 144.447 156.674 1.00 29.94  ? 579 LEU A CG     1 
ATOM   2861 C  CD1    . LEU A 1 436 ? 207.990 145.297 157.375 1.00 25.21  ? 579 LEU A CD1    1 
ATOM   2862 C  CD2    . LEU A 1 436 ? 205.706 145.269 156.360 1.00 27.13  ? 579 LEU A CD2    1 
ATOM   2863 N  N      . ASP A 1 437 ? 206.842 140.729 155.754 1.00 32.61  ? 580 ASP A N      1 
ATOM   2864 C  CA     . ASP A 1 437 ? 206.147 139.672 156.481 1.00 31.36  ? 580 ASP A CA     1 
ATOM   2865 C  C      . ASP A 1 437 ? 207.108 138.600 156.978 1.00 35.97  ? 580 ASP A C      1 
ATOM   2866 O  O      . ASP A 1 437 ? 206.938 138.085 158.088 1.00 36.66  ? 580 ASP A O      1 
ATOM   2867 C  CB     . ASP A 1 437 ? 205.069 139.047 155.597 1.00 35.29  ? 580 ASP A CB     1 
ATOM   2868 C  CG     . ASP A 1 437 ? 203.927 140.000 155.308 1.00 41.92  ? 580 ASP A CG     1 
ATOM   2869 O  OD1    . ASP A 1 437 ? 203.962 141.142 155.810 1.00 45.02  ? 580 ASP A OD1    1 
ATOM   2870 O  OD2    . ASP A 1 437 ? 202.993 139.608 154.578 1.00 41.76  ? 580 ASP A OD2    1 
ATOM   2871 N  N      . ASN A 1 438 ? 208.118 138.251 156.178 1.00 38.61  ? 581 ASN A N      1 
ATOM   2872 C  CA     . ASN A 1 438 ? 209.056 137.210 156.584 1.00 38.00  ? 581 ASN A CA     1 
ATOM   2873 C  C      . ASN A 1 438 ? 209.854 137.615 157.817 1.00 37.72  ? 581 ASN A C      1 
ATOM   2874 O  O      . ASN A 1 438 ? 210.091 136.782 158.699 1.00 40.11  ? 581 ASN A O      1 
ATOM   2875 C  CB     . ASN A 1 438 ? 209.999 136.874 155.429 1.00 44.94  ? 581 ASN A CB     1 
ATOM   2876 C  CG     . ASN A 1 438 ? 209.387 135.902 154.442 1.00 53.33  ? 581 ASN A CG     1 
ATOM   2877 O  OD1    . ASN A 1 438 ? 208.637 135.004 154.821 1.00 56.51  ? 581 ASN A OD1    1 
ATOM   2878 N  ND2    . ASN A 1 438 ? 209.704 136.078 153.165 1.00 52.08  ? 581 ASN A ND2    1 
ATOM   2879 N  N      . ILE A 1 439 ? 210.278 138.876 157.896 1.00 35.41  ? 582 ILE A N      1 
ATOM   2880 C  CA     . ILE A 1 439 ? 211.054 139.322 159.048 1.00 31.75  ? 582 ILE A CA     1 
ATOM   2881 C  C      . ILE A 1 439 ? 210.209 139.321 160.316 1.00 33.57  ? 582 ILE A C      1 
ATOM   2882 O  O      . ILE A 1 439 ? 210.713 139.006 161.399 1.00 36.84  ? 582 ILE A O      1 
ATOM   2883 C  CB     . ILE A 1 439 ? 211.657 140.711 158.778 1.00 32.83  ? 582 ILE A CB     1 
ATOM   2884 C  CG1    . ILE A 1 439 ? 212.582 140.662 157.560 1.00 33.28  ? 582 ILE A CG1    1 
ATOM   2885 C  CG2    . ILE A 1 439 ? 212.406 141.216 160.002 1.00 25.58  ? 582 ILE A CG2    1 
ATOM   2886 C  CD1    . ILE A 1 439 ? 213.281 141.971 157.270 1.00 31.79  ? 582 ILE A CD1    1 
ATOM   2887 N  N      . VAL A 1 440 ? 208.926 139.674 160.212 1.00 33.27  ? 583 VAL A N      1 
ATOM   2888 C  CA     . VAL A 1 440 ? 208.067 139.709 161.391 1.00 33.59  ? 583 VAL A CA     1 
ATOM   2889 C  C      . VAL A 1 440 ? 207.923 138.321 162.002 1.00 37.15  ? 583 VAL A C      1 
ATOM   2890 O  O      . VAL A 1 440 ? 207.918 138.175 163.230 1.00 38.21  ? 583 VAL A O      1 
ATOM   2891 C  CB     . VAL A 1 440 ? 206.695 140.311 161.036 1.00 31.74  ? 583 VAL A CB     1 
ATOM   2892 C  CG1    . VAL A 1 440 ? 205.686 140.015 162.134 1.00 29.35  ? 583 VAL A CG1    1 
ATOM   2893 C  CG2    . VAL A 1 440 ? 206.818 141.808 160.810 1.00 25.00  ? 583 VAL A CG2    1 
ATOM   2894 N  N      . GLU A 1 441 ? 207.800 137.284 161.170 1.00 36.51  ? 584 GLU A N      1 
ATOM   2895 C  CA     . GLU A 1 441 ? 207.626 135.935 161.697 1.00 38.34  ? 584 GLU A CA     1 
ATOM   2896 C  C      . GLU A 1 441 ? 208.830 135.487 162.517 1.00 41.44  ? 584 GLU A C      1 
ATOM   2897 O  O      . GLU A 1 441 ? 208.661 134.867 163.572 1.00 47.31  ? 584 GLU A O      1 
ATOM   2898 C  CB     . GLU A 1 441 ? 207.366 134.953 160.555 1.00 40.87  ? 584 GLU A CB     1 
ATOM   2899 C  CG     . GLU A 1 441 ? 206.106 135.246 159.756 1.00 49.33  ? 584 GLU A CG     1 
ATOM   2900 C  CD     . GLU A 1 441 ? 204.934 135.644 160.634 1.00 61.46  ? 584 GLU A CD     1 
ATOM   2901 O  OE1    . GLU A 1 441 ? 204.715 134.986 161.673 1.00 58.66  ? 584 GLU A OE1    1 
ATOM   2902 O  OE2    . GLU A 1 441 ? 204.230 136.615 160.283 1.00 61.34  ? 584 GLU A OE2    1 
ATOM   2903 N  N      . ILE A 1 442 ? 210.044 135.782 162.051 1.00 38.81  ? 585 ILE A N      1 
ATOM   2904 C  CA     . ILE A 1 442 ? 211.232 135.421 162.816 1.00 39.96  ? 585 ILE A CA     1 
ATOM   2905 C  C      . ILE A 1 442 ? 211.330 136.242 164.097 1.00 41.78  ? 585 ILE A C      1 
ATOM   2906 O  O      . ILE A 1 442 ? 211.746 135.724 165.139 1.00 43.94  ? 585 ILE A O      1 
ATOM   2907 C  CB     . ILE A 1 442 ? 212.495 135.580 161.954 1.00 41.24  ? 585 ILE A CB     1 
ATOM   2908 C  CG1    . ILE A 1 442 ? 212.566 134.472 160.903 1.00 42.59  ? 585 ILE A CG1    1 
ATOM   2909 C  CG2    . ILE A 1 442 ? 213.741 135.568 162.827 1.00 40.23  ? 585 ILE A CG2    1 
ATOM   2910 C  CD1    . ILE A 1 442 ? 213.474 134.791 159.737 1.00 42.80  ? 585 ILE A CD1    1 
ATOM   2911 N  N      . LEU A 1 443 ? 210.956 137.521 164.046 1.00 41.11  ? 586 LEU A N      1 
ATOM   2912 C  CA     . LEU A 1 443 ? 211.024 138.378 165.222 1.00 38.80  ? 586 LEU A CA     1 
ATOM   2913 C  C      . LEU A 1 443 ? 210.023 137.985 166.300 1.00 39.62  ? 586 LEU A C      1 
ATOM   2914 O  O      . LEU A 1 443 ? 210.219 138.343 167.466 1.00 39.42  ? 586 LEU A O      1 
ATOM   2915 C  CB     . LEU A 1 443 ? 210.798 139.837 164.819 1.00 34.30  ? 586 LEU A CB     1 
ATOM   2916 C  CG     . LEU A 1 443 ? 211.352 140.913 165.755 1.00 33.70  ? 586 LEU A CG     1 
ATOM   2917 C  CD1    . LEU A 1 443 ? 212.839 140.710 165.991 1.00 37.93  ? 586 LEU A CD1    1 
ATOM   2918 C  CD2    . LEU A 1 443 ? 211.079 142.296 165.191 1.00 28.64  ? 586 LEU A CD2    1 
ATOM   2919 N  N      . LEU A 1 444 ? 208.963 137.262 165.943 1.00 39.38  ? 587 LEU A N      1 
ATOM   2920 C  CA     . LEU A 1 444 ? 207.950 136.856 166.909 1.00 40.38  ? 587 LEU A CA     1 
ATOM   2921 C  C      . LEU A 1 444 ? 208.306 135.571 167.644 1.00 44.72  ? 587 LEU A C      1 
ATOM   2922 O  O      . LEU A 1 444 ? 207.559 135.164 168.540 1.00 50.71  ? 587 LEU A O      1 
ATOM   2923 C  CB     . LEU A 1 444 ? 206.596 136.690 166.213 1.00 38.11  ? 587 LEU A CB     1 
ATOM   2924 C  CG     . LEU A 1 444 ? 205.837 137.978 165.886 1.00 36.59  ? 587 LEU A CG     1 
ATOM   2925 C  CD1    . LEU A 1 444 ? 204.562 137.669 165.121 1.00 37.22  ? 587 LEU A CD1    1 
ATOM   2926 C  CD2    . LEU A 1 444 ? 205.530 138.759 167.152 1.00 32.95  ? 587 LEU A CD2    1 
ATOM   2927 N  N      . GLU A 1 445 ? 209.420 134.925 167.294 1.00 45.59  ? 588 GLU A N      1 
ATOM   2928 C  CA     . GLU A 1 445 ? 209.835 133.697 167.955 1.00 47.59  ? 588 GLU A CA     1 
ATOM   2929 C  C      . GLU A 1 445 ? 211.200 133.784 168.622 1.00 48.67  ? 588 GLU A C      1 
ATOM   2930 O  O      . GLU A 1 445 ? 211.553 132.868 169.373 1.00 51.01  ? 588 GLU A O      1 
ATOM   2931 C  CB     . GLU A 1 445 ? 209.843 132.525 166.961 1.00 49.80  ? 588 GLU A CB     1 
ATOM   2932 C  CG     . GLU A 1 445 ? 210.832 132.678 165.818 1.00 55.36  ? 588 GLU A CG     1 
ATOM   2933 C  CD     . GLU A 1 445 ? 210.641 131.631 164.738 1.00 67.69  ? 588 GLU A CD     1 
ATOM   2934 O  OE1    . GLU A 1 445 ? 209.694 130.825 164.851 1.00 71.80  ? 588 GLU A OE1    1 
ATOM   2935 O  OE2    . GLU A 1 445 ? 211.438 131.614 163.776 1.00 67.78  ? 588 GLU A OE2    1 
ATOM   2936 N  N      . LYS A 1 446 ? 211.975 134.843 168.380 1.00 47.59  ? 589 LYS A N      1 
ATOM   2937 C  CA     . LYS A 1 446 ? 213.271 135.020 169.016 1.00 45.62  ? 589 LYS A CA     1 
ATOM   2938 C  C      . LYS A 1 446 ? 213.393 136.309 169.812 1.00 43.28  ? 589 LYS A C      1 
ATOM   2939 O  O      . LYS A 1 446 ? 214.220 136.368 170.728 1.00 43.43  ? 589 LYS A O      1 
ATOM   2940 C  CB     . LYS A 1 446 ? 214.395 134.979 167.968 1.00 46.12  ? 589 LYS A CB     1 
ATOM   2941 C  CG     . LYS A 1 446 ? 214.273 133.833 166.979 1.00 51.21  ? 589 LYS A CG     1 
ATOM   2942 C  CD     . LYS A 1 446 ? 215.263 133.977 165.838 1.00 57.21  ? 589 LYS A CD     1 
ATOM   2943 C  CE     . LYS A 1 446 ? 216.648 133.510 166.249 1.00 62.45  ? 589 LYS A CE     1 
ATOM   2944 N  NZ     . LYS A 1 446 ? 217.520 133.258 165.070 1.00 65.75  ? 589 LYS A NZ     1 
ATOM   2945 N  N      . GLU A 1 447 ? 212.606 137.333 169.495 1.00 43.32  ? 590 GLU A N      1 
ATOM   2946 C  CA     . GLU A 1 447 ? 212.498 138.606 170.195 1.00 40.58  ? 590 GLU A CA     1 
ATOM   2947 C  C      . GLU A 1 447 ? 213.693 139.522 169.928 1.00 41.29  ? 590 GLU A C      1 
ATOM   2948 O  O      . GLU A 1 447 ? 213.653 140.685 170.331 1.00 43.12  ? 590 GLU A O      1 
ATOM   2949 C  CB     . GLU A 1 447 ? 212.330 138.438 171.719 1.00 40.38  ? 590 GLU A CB     1 
ATOM   2950 C  CG     . GLU A 1 447 ? 212.169 139.736 172.493 1.00 45.41  ? 590 GLU A CG     1 
ATOM   2951 C  CD     . GLU A 1 447 ? 212.165 139.521 173.995 1.00 49.26  ? 590 GLU A CD     1 
ATOM   2952 O  OE1    . GLU A 1 447 ? 211.070 139.343 174.569 1.00 47.48  ? 590 GLU A OE1    1 
ATOM   2953 O  OE2    . GLU A 1 447 ? 213.256 139.528 174.600 1.00 49.64  ? 590 GLU A OE2    1 
ATOM   2954 N  N      . THR A 1 448 ? 214.738 139.060 169.246 1.00 41.65  ? 591 THR A N      1 
ATOM   2955 C  CA     . THR A 1 448 ? 215.899 139.902 168.993 1.00 41.02  ? 591 THR A CA     1 
ATOM   2956 C  C      . THR A 1 448 ? 216.793 139.237 167.957 1.00 45.85  ? 591 THR A C      1 
ATOM   2957 O  O      . THR A 1 448 ? 217.003 138.023 167.997 1.00 50.07  ? 591 THR A O      1 
ATOM   2958 C  CB     . THR A 1 448 ? 216.695 140.168 170.277 1.00 41.40  ? 591 THR A CB     1 
ATOM   2959 O  OG1    . THR A 1 448 ? 215.880 140.887 171.211 1.00 44.39  ? 591 THR A OG1    1 
ATOM   2960 C  CG2    . THR A 1 448 ? 217.942 140.982 169.971 1.00 42.93  ? 591 THR A CG2    1 
ATOM   2961 N  N      . ILE A 1 449 ? 217.313 140.046 167.036 1.00 48.84  ? 592 ILE A N      1 
ATOM   2962 C  CA     . ILE A 1 449 ? 218.286 139.613 166.040 1.00 50.40  ? 592 ILE A CA     1 
ATOM   2963 C  C      . ILE A 1 449 ? 219.405 140.643 166.007 1.00 54.17  ? 592 ILE A C      1 
ATOM   2964 O  O      . ILE A 1 449 ? 219.141 141.850 166.047 1.00 52.94  ? 592 ILE A O      1 
ATOM   2965 C  CB     . ILE A 1 449 ? 217.653 139.452 164.644 1.00 48.14  ? 592 ILE A CB     1 
ATOM   2966 C  CG1    . ILE A 1 449 ? 216.232 138.898 164.762 1.00 49.17  ? 592 ILE A CG1    1 
ATOM   2967 C  CG2    . ILE A 1 449 ? 218.506 138.544 163.776 1.00 53.42  ? 592 ILE A CG2    1 
ATOM   2968 C  CD1    . ILE A 1 449 ? 215.365 139.176 163.554 1.00 48.47  ? 592 ILE A CD1    1 
ATOM   2969 N  N      . GLU A 1 450 ? 220.649 140.175 165.932 1.00 60.13  ? 593 GLU A N      1 
ATOM   2970 C  CA     . GLU A 1 450 ? 221.803 141.060 166.032 1.00 62.10  ? 593 GLU A CA     1 
ATOM   2971 C  C      . GLU A 1 450 ? 222.785 140.726 164.913 1.00 67.60  ? 593 GLU A C      1 
ATOM   2972 O  O      . GLU A 1 450 ? 222.485 139.944 164.005 1.00 67.58  ? 593 GLU A O      1 
ATOM   2973 C  CB     . GLU A 1 450 ? 222.434 140.966 167.428 1.00 62.19  ? 593 GLU A CB     1 
ATOM   2974 C  CG     . GLU A 1 450 ? 222.869 139.572 167.831 1.00 73.21  ? 593 GLU A CG     1 
ATOM   2975 C  CD     . GLU A 1 450 ? 223.336 139.508 169.271 1.00 83.89  ? 593 GLU A CD     1 
ATOM   2976 O  OE1    . GLU A 1 450 ? 223.261 140.543 169.966 1.00 78.31  ? 593 GLU A OE1    1 
ATOM   2977 O  OE2    . GLU A 1 450 ? 223.777 138.424 169.708 1.00 90.58  ? 593 GLU A OE2    1 
ATOM   2978 N  N      . GLY A 1 451 ? 223.977 141.316 164.998 1.00 72.52  ? 594 GLY A N      1 
ATOM   2979 C  CA     . GLY A 1 451 ? 224.879 141.469 163.870 1.00 75.42  ? 594 GLY A CA     1 
ATOM   2980 C  C      . GLY A 1 451 ? 225.077 140.297 162.929 1.00 76.45  ? 594 GLY A C      1 
ATOM   2981 O  O      . GLY A 1 451 ? 224.665 140.365 161.768 1.00 74.43  ? 594 GLY A O      1 
ATOM   2982 N  N      . ASP A 1 452 ? 225.701 139.217 163.403 1.00 76.65  ? 595 ASP A N      1 
ATOM   2983 C  CA     . ASP A 1 452 ? 226.072 138.141 162.488 1.00 79.44  ? 595 ASP A CA     1 
ATOM   2984 C  C      . ASP A 1 452 ? 224.852 137.413 161.939 1.00 76.46  ? 595 ASP A C      1 
ATOM   2985 O  O      . ASP A 1 452 ? 224.767 137.166 160.731 1.00 73.74  ? 595 ASP A O      1 
ATOM   2986 C  CB     . ASP A 1 452 ? 227.014 137.157 163.182 1.00 86.36  ? 595 ASP A CB     1 
ATOM   2987 C  CG     . ASP A 1 452 ? 228.475 137.517 162.989 1.00 95.08  ? 595 ASP A CG     1 
ATOM   2988 O  OD1    . ASP A 1 452 ? 228.812 138.082 161.928 1.00 90.90  ? 595 ASP A OD1    1 
ATOM   2989 O  OD2    . ASP A 1 452 ? 229.285 137.236 163.897 1.00 101.69 ? 595 ASP A OD2    1 
ATOM   2990 N  N      . GLU A 1 453 ? 223.898 137.061 162.803 1.00 74.18  ? 596 GLU A N      1 
ATOM   2991 C  CA     . GLU A 1 453 ? 222.697 136.385 162.327 1.00 69.20  ? 596 GLU A CA     1 
ATOM   2992 C  C      . GLU A 1 453 ? 221.832 137.309 161.480 1.00 68.38  ? 596 GLU A C      1 
ATOM   2993 O  O      . GLU A 1 453 ? 221.149 136.846 160.560 1.00 68.53  ? 596 GLU A O      1 
ATOM   2994 C  CB     . GLU A 1 453 ? 221.896 135.839 163.509 1.00 69.53  ? 596 GLU A CB     1 
ATOM   2995 C  CG     . GLU A 1 453 ? 220.554 135.246 163.122 1.00 72.84  ? 596 GLU A CG     1 
ATOM   2996 C  CD     . GLU A 1 453 ? 220.239 133.976 163.883 1.00 82.42  ? 596 GLU A CD     1 
ATOM   2997 O  OE1    . GLU A 1 453 ? 220.872 133.737 164.934 1.00 87.59  ? 596 GLU A OE1    1 
ATOM   2998 O  OE2    . GLU A 1 453 ? 219.359 133.214 163.431 1.00 82.21  ? 596 GLU A OE2    1 
ATOM   2999 N  N      . LEU A 1 454 ? 221.846 138.611 161.773 1.00 65.65  ? 597 LEU A N      1 
ATOM   3000 C  CA     . LEU A 1 454 ? 221.044 139.558 161.008 1.00 63.50  ? 597 LEU A CA     1 
ATOM   3001 C  C      . LEU A 1 454 ? 221.609 139.795 159.613 1.00 64.61  ? 597 LEU A C      1 
ATOM   3002 O  O      . LEU A 1 454 ? 220.841 139.994 158.666 1.00 61.81  ? 597 LEU A O      1 
ATOM   3003 C  CB     . LEU A 1 454 ? 220.940 140.885 161.762 1.00 57.34  ? 597 LEU A CB     1 
ATOM   3004 C  CG     . LEU A 1 454 ? 220.107 141.988 161.107 1.00 55.84  ? 597 LEU A CG     1 
ATOM   3005 C  CD1    . LEU A 1 454 ? 218.701 141.494 160.811 1.00 52.42  ? 597 LEU A CD1    1 
ATOM   3006 C  CD2    . LEU A 1 454 ? 220.070 143.223 161.991 1.00 51.09  ? 597 LEU A CD2    1 
ATOM   3007 N  N      . ARG A 1 455 ? 222.936 139.781 159.467 1.00 67.89  ? 598 ARG A N      1 
ATOM   3008 C  CA     . ARG A 1 455 ? 223.534 140.013 158.156 1.00 66.77  ? 598 ARG A CA     1 
ATOM   3009 C  C      . ARG A 1 455 ? 223.113 138.940 157.160 1.00 65.85  ? 598 ARG A C      1 
ATOM   3010 O  O      . ARG A 1 455 ? 222.776 139.246 156.010 1.00 63.96  ? 598 ARG A O      1 
ATOM   3011 C  CB     . ARG A 1 455 ? 225.057 140.064 158.275 1.00 68.12  ? 598 ARG A CB     1 
ATOM   3012 C  CG     . ARG A 1 455 ? 225.634 141.468 158.331 1.00 73.94  ? 598 ARG A CG     1 
ATOM   3013 C  CD     . ARG A 1 455 ? 227.152 141.435 158.412 1.00 77.48  ? 598 ARG A CD     1 
ATOM   3014 N  NE     . ARG A 1 455 ? 227.623 141.168 159.766 1.00 85.66  ? 598 ARG A NE     1 
ATOM   3015 C  CZ     . ARG A 1 455 ? 227.948 142.107 160.644 1.00 87.71  ? 598 ARG A CZ     1 
ATOM   3016 N  NH1    . ARG A 1 455 ? 227.863 143.393 160.344 1.00 85.99  ? 598 ARG A NH1    1 
ATOM   3017 N  NH2    . ARG A 1 455 ? 228.369 141.747 161.853 1.00 84.73  ? 598 ARG A NH2    1 
ATOM   3018 N  N      . ARG A 1 456 ? 223.125 137.675 157.583 1.00 66.39  ? 599 ARG A N      1 
ATOM   3019 C  CA     . ARG A 1 456 ? 222.719 136.594 156.691 1.00 65.93  ? 599 ARG A CA     1 
ATOM   3020 C  C      . ARG A 1 456 ? 221.253 136.723 156.295 1.00 67.51  ? 599 ARG A C      1 
ATOM   3021 O  O      . ARG A 1 456 ? 220.901 136.531 155.126 1.00 68.11  ? 599 ARG A O      1 
ATOM   3022 C  CB     . ARG A 1 456 ? 222.979 135.242 157.355 1.00 69.10  ? 599 ARG A CB     1 
ATOM   3023 C  CG     . ARG A 1 456 ? 222.603 134.046 156.497 1.00 75.73  ? 599 ARG A CG     1 
ATOM   3024 C  CD     . ARG A 1 456 ? 222.875 132.740 157.224 1.00 79.28  ? 599 ARG A CD     1 
ATOM   3025 N  NE     . ARG A 1 456 ? 222.242 132.704 158.537 1.00 83.07  ? 599 ARG A NE     1 
ATOM   3026 C  CZ     . ARG A 1 456 ? 220.938 132.564 158.736 1.00 83.12  ? 599 ARG A CZ     1 
ATOM   3027 N  NH1    . ARG A 1 456 ? 220.094 132.444 157.724 1.00 80.62  ? 599 ARG A NH1    1 
ATOM   3028 N  NH2    . ARG A 1 456 ? 220.470 132.544 159.980 1.00 81.90  ? 599 ARG A NH2    1 
ATOM   3029 N  N      . ILE A 1 457 ? 220.385 137.049 157.255 1.00 68.21  ? 600 ILE A N      1 
ATOM   3030 C  CA     . ILE A 1 457 ? 218.960 137.159 156.960 1.00 66.83  ? 600 ILE A CA     1 
ATOM   3031 C  C      . ILE A 1 457 ? 218.703 138.272 155.953 1.00 64.64  ? 600 ILE A C      1 
ATOM   3032 O  O      . ILE A 1 457 ? 217.937 138.097 154.997 1.00 66.28  ? 600 ILE A O      1 
ATOM   3033 C  CB     . ILE A 1 457 ? 218.163 137.376 158.259 1.00 64.97  ? 600 ILE A CB     1 
ATOM   3034 C  CG1    . ILE A 1 457 ? 218.143 136.093 159.093 1.00 65.12  ? 600 ILE A CG1    1 
ATOM   3035 C  CG2    . ILE A 1 457 ? 216.749 137.836 157.946 1.00 61.98  ? 600 ILE A CG2    1 
ATOM   3036 C  CD1    . ILE A 1 457 ? 217.581 136.278 160.485 1.00 62.57  ? 600 ILE A CD1    1 
ATOM   3037 N  N      . LEU A 1 458 ? 219.334 139.431 156.146 1.00 61.33  ? 601 LEU A N      1 
ATOM   3038 C  CA     . LEU A 1 458 ? 219.139 140.552 155.236 1.00 62.24  ? 601 LEU A CA     1 
ATOM   3039 C  C      . LEU A 1 458 ? 219.697 140.289 153.844 1.00 66.33  ? 601 LEU A C      1 
ATOM   3040 O  O      . LEU A 1 458 ? 219.276 140.955 152.893 1.00 66.15  ? 601 LEU A O      1 
ATOM   3041 C  CB     . LEU A 1 458 ? 219.775 141.816 155.816 1.00 57.87  ? 601 LEU A CB     1 
ATOM   3042 C  CG     . LEU A 1 458 ? 219.005 142.506 156.944 1.00 56.69  ? 601 LEU A CG     1 
ATOM   3043 C  CD1    . LEU A 1 458 ? 219.730 143.761 157.400 1.00 50.92  ? 601 LEU A CD1    1 
ATOM   3044 C  CD2    . LEU A 1 458 ? 217.586 142.831 156.508 1.00 51.63  ? 601 LEU A CD2    1 
ATOM   3045 N  N      . SER A 1 459 ? 220.628 139.346 153.701 1.00 69.31  ? 602 SER A N      1 
ATOM   3046 C  CA     . SER A 1 459 ? 221.179 139.012 152.393 1.00 67.55  ? 602 SER A CA     1 
ATOM   3047 C  C      . SER A 1 459 ? 220.292 138.039 151.627 1.00 68.91  ? 602 SER A C      1 
ATOM   3048 O  O      . SER A 1 459 ? 220.162 138.154 150.404 1.00 70.97  ? 602 SER A O      1 
ATOM   3049 C  CB     . SER A 1 459 ? 222.585 138.427 152.547 1.00 67.48  ? 602 SER A CB     1 
ATOM   3050 O  OG     . SER A 1 459 ? 223.483 139.393 153.063 1.00 71.76  ? 602 SER A OG     1 
ATOM   3051 N  N      . GLU A 1 460 ? 219.679 137.078 152.323 1.00 69.14  ? 603 GLU A N      1 
ATOM   3052 C  CA     . GLU A 1 460 ? 218.749 136.172 151.658 1.00 70.89  ? 603 GLU A CA     1 
ATOM   3053 C  C      . GLU A 1 460 ? 217.567 136.937 151.078 1.00 70.56  ? 603 GLU A C      1 
ATOM   3054 O  O      . GLU A 1 460 ? 217.142 136.675 149.946 1.00 71.40  ? 603 GLU A O      1 
ATOM   3055 C  CB     . GLU A 1 460 ? 218.275 135.097 152.635 1.00 72.53  ? 603 GLU A CB     1 
ATOM   3056 C  CG     . GLU A 1 460 ? 219.399 134.430 153.412 1.00 75.09  ? 603 GLU A CG     1 
ATOM   3057 C  CD     . GLU A 1 460 ? 218.941 133.882 154.749 1.00 82.96  ? 603 GLU A CD     1 
ATOM   3058 O  OE1    . GLU A 1 460 ? 217.747 134.038 155.080 1.00 79.16  ? 603 GLU A OE1    1 
ATOM   3059 O  OE2    . GLU A 1 460 ? 219.777 133.296 155.470 1.00 83.56  ? 603 GLU A OE2    1 
ATOM   3060 N  N      . GLU A 1 461 ? 217.023 137.883 151.836 1.00 69.33  ? 604 GLU A N      1 
ATOM   3061 C  CA     . GLU A 1 461 ? 216.012 138.793 151.327 1.00 67.44  ? 604 GLU A CA     1 
ATOM   3062 C  C      . GLU A 1 461 ? 216.674 139.936 150.561 1.00 68.46  ? 604 GLU A C      1 
ATOM   3063 O  O      . GLU A 1 461 ? 217.880 140.169 150.658 1.00 70.61  ? 604 GLU A O      1 
ATOM   3064 C  CB     . GLU A 1 461 ? 215.152 139.337 152.468 1.00 63.78  ? 604 GLU A CB     1 
ATOM   3065 C  CG     . GLU A 1 461 ? 213.862 138.569 152.700 1.00 64.04  ? 604 GLU A CG     1 
ATOM   3066 C  CD     . GLU A 1 461 ? 214.078 137.285 153.475 1.00 74.67  ? 604 GLU A CD     1 
ATOM   3067 O  OE1    . GLU A 1 461 ? 214.919 137.281 154.398 1.00 77.23  ? 604 GLU A OE1    1 
ATOM   3068 O  OE2    . GLU A 1 461 ? 213.406 136.280 153.163 1.00 77.86  ? 604 GLU A OE2    1 
ATOM   3069 N  N      . PHE A 1 462 ? 215.867 140.653 149.788 1.00 64.14  ? 605 PHE A N      1 
ATOM   3070 C  CA     . PHE A 1 462 ? 216.365 141.783 149.013 1.00 69.11  ? 605 PHE A CA     1 
ATOM   3071 C  C      . PHE A 1 462 ? 217.380 141.330 147.969 1.00 73.13  ? 605 PHE A C      1 
ATOM   3072 O  O      . PHE A 1 462 ? 217.598 140.133 147.777 1.00 76.57  ? 605 PHE A O      1 
ATOM   3073 C  CB     . PHE A 1 462 ? 216.993 142.831 149.937 1.00 57.92  ? 605 PHE A CB     1 
ATOM   3074 C  CG     . PHE A 1 462 ? 216.033 143.411 150.936 1.00 54.69  ? 605 PHE A CG     1 
ATOM   3075 C  CD1    . PHE A 1 462 ? 214.995 144.229 150.524 1.00 50.77  ? 605 PHE A CD1    1 
ATOM   3076 C  CD2    . PHE A 1 462 ? 216.166 143.134 152.286 1.00 54.07  ? 605 PHE A CD2    1 
ATOM   3077 C  CE1    . PHE A 1 462 ? 214.111 144.763 151.440 1.00 46.21  ? 605 PHE A CE1    1 
ATOM   3078 C  CE2    . PHE A 1 462 ? 215.285 143.665 153.205 1.00 47.60  ? 605 PHE A CE2    1 
ATOM   3079 C  CZ     . PHE A 1 462 ? 214.256 144.480 152.782 1.00 43.75  ? 605 PHE A CZ     1 
HETATM 3080 MG MG     . MG  B 2 .   ? 215.668 154.912 193.449 1.00 36.95  ? 800 MG  A MG     1 
HETATM 3081 ZN ZN     . ZN  C 3 .   ? 209.508 154.542 164.923 1.00 70.96  ? 801 ZN  A ZN     1 
HETATM 3082 P  PG     . ATP D 4 .   ? 213.138 154.605 190.880 1.00 37.60  ? 802 ATP A PG     1 
HETATM 3083 O  O1G    . ATP D 4 .   ? 213.355 155.365 189.617 1.00 32.62  ? 802 ATP A O1G    1 
HETATM 3084 O  O2G    . ATP D 4 .   ? 211.672 154.264 191.146 1.00 39.18  ? 802 ATP A O2G    1 
HETATM 3085 O  O3G    . ATP D 4 .   ? 213.723 155.287 192.120 1.00 44.57  ? 802 ATP A O3G    1 
HETATM 3086 P  PB     . ATP D 4 .   ? 215.341 152.580 190.841 1.00 24.59  ? 802 ATP A PB     1 
HETATM 3087 O  O1B    . ATP D 4 .   ? 215.804 152.180 189.499 1.00 22.22  ? 802 ATP A O1B    1 
HETATM 3088 O  O2B    . ATP D 4 .   ? 216.236 153.587 191.562 1.00 32.00  ? 802 ATP A O2B    1 
HETATM 3089 O  O3B    . ATP D 4 .   ? 213.873 153.190 190.820 1.00 31.76  ? 802 ATP A O3B    1 
HETATM 3090 P  PA     . ATP D 4 .   ? 216.095 150.366 192.650 1.00 28.84  ? 802 ATP A PA     1 
HETATM 3091 O  O1A    . ATP D 4 .   ? 217.483 150.399 192.149 1.00 26.39  ? 802 ATP A O1A    1 
HETATM 3092 O  O2A    . ATP D 4 .   ? 215.944 150.746 194.121 1.00 35.64  ? 802 ATP A O2A    1 
HETATM 3093 O  O3A    . ATP D 4 .   ? 215.154 151.336 191.815 1.00 28.13  ? 802 ATP A O3A    1 
HETATM 3094 O  "O5'"  . ATP D 4 .   ? 215.447 148.945 192.418 1.00 27.82  ? 802 ATP A "O5'"  1 
HETATM 3095 C  "C5'"  . ATP D 4 .   ? 214.461 148.407 193.325 1.00 28.76  ? 802 ATP A "C5'"  1 
HETATM 3096 C  "C4'"  . ATP D 4 .   ? 214.680 146.920 193.398 1.00 26.84  ? 802 ATP A "C4'"  1 
HETATM 3097 O  "O4'"  . ATP D 4 .   ? 214.843 146.481 192.043 1.00 27.71  ? 802 ATP A "O4'"  1 
HETATM 3098 C  "C3'"  . ATP D 4 .   ? 216.041 146.627 194.010 1.00 29.98  ? 802 ATP A "C3'"  1 
HETATM 3099 O  "O3'"  . ATP D 4 .   ? 215.771 146.235 195.350 1.00 36.92  ? 802 ATP A "O3'"  1 
HETATM 3100 C  "C2'"  . ATP D 4 .   ? 216.491 145.348 193.289 1.00 26.92  ? 802 ATP A "C2'"  1 
HETATM 3101 O  "O2'"  . ATP D 4 .   ? 216.042 144.265 194.091 1.00 32.70  ? 802 ATP A "O2'"  1 
HETATM 3102 C  "C1'"  . ATP D 4 .   ? 215.600 145.294 192.041 1.00 25.65  ? 802 ATP A "C1'"  1 
HETATM 3103 N  N9     . ATP D 4 .   ? 216.399 145.334 190.823 1.00 21.72  ? 802 ATP A N9     1 
HETATM 3104 C  C8     . ATP D 4 .   ? 216.375 146.311 189.863 1.00 19.30  ? 802 ATP A C8     1 
HETATM 3105 N  N7     . ATP D 4 .   ? 217.200 146.104 188.867 1.00 20.17  ? 802 ATP A N7     1 
HETATM 3106 C  C5     . ATP D 4 .   ? 217.816 144.906 189.196 1.00 21.01  ? 802 ATP A C5     1 
HETATM 3107 C  C6     . ATP D 4 .   ? 218.801 144.136 188.549 1.00 21.54  ? 802 ATP A C6     1 
HETATM 3108 N  N6     . ATP D 4 .   ? 219.361 144.474 187.384 1.00 19.81  ? 802 ATP A N6     1 
HETATM 3109 N  N1     . ATP D 4 .   ? 219.197 142.990 189.147 1.00 21.87  ? 802 ATP A N1     1 
HETATM 3110 C  C2     . ATP D 4 .   ? 218.640 142.648 190.312 1.00 23.83  ? 802 ATP A C2     1 
HETATM 3111 N  N3     . ATP D 4 .   ? 217.706 143.292 191.014 1.00 25.22  ? 802 ATP A N3     1 
HETATM 3112 C  C4     . ATP D 4 .   ? 217.332 144.419 190.400 1.00 24.14  ? 802 ATP A C4     1 
HETATM 3113 H  "H5'1" . ATP D 4 .   ? 214.573 148.794 194.207 1.00 29.58  ? 802 ATP A "H5'1" 1 
HETATM 3114 H  "H5'2" . ATP D 4 .   ? 213.568 148.595 192.998 1.00 27.27  ? 802 ATP A "H5'2" 1 
HETATM 3115 H  "H4'"  . ATP D 4 .   ? 213.957 146.471 193.864 1.00 27.27  ? 802 ATP A "H4'"  1 
HETATM 3116 H  "H3'"  . ATP D 4 .   ? 216.672 147.360 193.940 1.00 28.39  ? 802 ATP A "H3'"  1 
HETATM 3117 H  "HO3'" . ATP D 4 .   ? 216.522 146.089 195.719 1.00 34.27  ? 802 ATP A "HO3'" 1 
HETATM 3118 H  "H2'"  . ATP D 4 .   ? 217.441 145.323 193.093 1.00 25.86  ? 802 ATP A "H2'"  1 
HETATM 3119 H  "HO2'" . ATP D 4 .   ? 216.458 144.316 194.830 1.00 31.42  ? 802 ATP A "HO2'" 1 
HETATM 3120 H  "H1'"  . ATP D 4 .   ? 215.032 144.509 192.059 1.00 25.06  ? 802 ATP A "H1'"  1 
HETATM 3121 H  H8     . ATP D 4 .   ? 215.818 147.054 189.912 1.00 21.41  ? 802 ATP A H8     1 
HETATM 3122 H  HN61   . ATP D 4 .   ? 219.973 143.977 187.040 1.00 23.27  ? 802 ATP A HN61   1 
HETATM 3123 H  HN62   . ATP D 4 .   ? 219.110 145.189 186.978 1.00 20.40  ? 802 ATP A HN62   1 
HETATM 3124 H  H2     . ATP D 4 .   ? 218.944 141.852 190.684 1.00 24.64  ? 802 ATP A H2     1 
# 
