data_8VWC
# 
_entry.id   8VWC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8VWC         pdb_00008vwc 10.2210/pdb8vwc/pdb 
WWPDB D_1000281094 ?            ?                   
EMDB  EMD-43581    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-15 ? 
2 'Structure model' 1 1 2025-01-29 ? 
3 'Structure model' 1 2 2025-06-11 ? 
# 
_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' 
3 3 'Structure model' 'Data collection'     
4 3 '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        
4 3 'Structure model' citation        
5 3 'Structure model' citation_author 
6 3 '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'             
11 3 'Structure model' '_citation.journal_volume'          
12 3 'Structure model' '_citation.page_first'              
13 3 'Structure model' '_citation.page_last'               
14 3 'Structure model' '_citation_author.identifier_ORCID' 
15 3 '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                        8VWC 
_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 Aged State' 
_pdbx_database_related.db_id          EMD-43581 
_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            21 
_citation.language                  ? 
_citation.page_first                883 
_citation.page_last                 893 
_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 ? 
primary 'Zhu, J.'         2 ? 
primary 'Zhang, Z.'       3 ? 
primary 'Wei, J.'         4 ? 
primary 'Wang, F.'        5 ? 
primary 'Meisl, G.'       6 ? 
primary 'Knowles, T.P.J.' 7 ? 
primary 'Egelman, E.H.'   8 ? 
primary 'Tezcan, F.A.'    9 ? 
# 
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 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 318 GLU 318 461 ?   ?   ?   A . n 
A 1 319 GLU 319 462 ?   ?   ?   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 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 452 ASP 452 595 ?   ?   ?   A . n 
A 1 453 GLU 453 596 ?   ?   ?   A . n 
A 1 454 LEU 454 597 ?   ?   ?   A . n 
A 1 455 ARG 455 598 ?   ?   ?   A . n 
A 1 456 ARG 456 599 ?   ?   ?   A . n 
A 1 457 ILE 457 600 ?   ?   ?   A . n 
A 1 458 LEU 458 601 ?   ?   ?   A . n 
A 1 459 SER 459 602 ?   ?   ?   A . n 
A 1 460 GLU 460 603 ?   ?   ?   A . n 
A 1 461 GLU 461 604 ?   ?   ?   A . n 
A 1 462 PHE 462 605 ?   ?   ?   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                     8VWC 
_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                         8VWC 
_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                   8VWC 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8VWC 
_struct.title                        'CryoEM Structure of a FtsH Helical Assembly in the Aged State' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8VWC 
_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              8VWC 
_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 8VWC SER A 1   ? UNP Q9WZ49 ?   ?   'expression tag'      144 1 
1 8VWC GLY A 2   ? UNP Q9WZ49 ?   ?   'expression tag'      145 2 
1 8VWC GLY A 3   ? UNP Q9WZ49 ?   ?   'expression tag'      146 3 
1 8VWC SER A 112 ? UNP Q9WZ49 CYS 255 'engineered mutation' 255 4 
1 8VWC LEU A 267 ? UNP Q9WZ49 LYS 410 'engineered mutation' 410 5 
1 8VWC ALA A 272 ? UNP Q9WZ49 LYS 415 'engineered mutation' 415 6 
1 8VWC SER A 370 ? UNP Q9WZ49 CYS 513 'engineered mutation' 513 7 
1 8VWC 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' ? eicosameric 20 
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 '(1-20)' 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' ?     ?     0.75241500  0.65868900  0.00000000 -79.19510 -0.65868900 0.75241500  0.00000000 
174.58500 0.00000000  -0.00000000 1.00000000 16.10000  
3  'helical symmetry operation' ?     ?     0.13225600  0.99121600  0.00000000 -23.78560 -0.99121600 0.13225600  0.00000000 
358.11000 0.00000000  -0.00000000 1.00000000 32.20000  
4  'helical symmetry operation' ?     ?     -0.55339200 0.83292100  0.00000000 138.79100 -0.83292100 -0.55339200 0.00000000 
459.69900 0.00000000  0.00000000  1.00000000 48.30000  
5  'helical symmetry operation' ?     ?     -0.96501600 0.26218900  0.00000000 328.03300 -0.26218900 -0.96501600 0.00000000 
429.04900 0.00000000  0.00000000  1.00000000 64.40000  
6  'helical symmetry operation' ?     ?     -0.89879400 -0.43837100 0.00000000 450.23200 0.43837100  -0.89879400 0.00000000 
281.33600 0.00000000  0.00000000  1.00000000 80.50000  
7  'helical symmetry operation' ?     ?     -0.38751600 -0.92186300 0.00000000 444.87900 0.92186300  -0.38751600 0.00000000 
89.70330  0.00000000  0.00000000  1.00000000 96.60000  
8  'helical symmetry operation' ?     ?     0.31564900  -0.94887600 0.00000000 314.62500 0.94887600  0.31564900  0.00000000 
-50.95810 -0.00000000 0.00000000  1.00000000 112.70000 
9  'helical symmetry operation' ?     ?     0.86251400  -0.50603400 0.00000000 123.96800 0.50603400  0.86251400  0.00000000 
-70.99700 -0.00000000 0.00000000  1.00000000 128.80000 
10 'helical symmetry operation' ?     ?     0.98228700  0.18738100  0.00000000 -32.68500 -0.18738100 0.98228700  0.00000000 
39.50930  0.00000000  -0.00000000 1.00000000 144.90000 
11 'helical symmetry operation' ?     ?     -1.00000000 -0.00000000 0.00000000 385.28000 0.00000000  -1.00000000 0.00000000 
385.28000 0.00000000  0.00000000  1.00000000 0.00000   
12 'helical symmetry operation' ?     ?     -0.75241500 -0.65868900 0.00000000 464.47500 0.65868900  -0.75241500 0.00000000 
210.69500 0.00000000  0.00000000  1.00000000 16.10000  
13 'helical symmetry operation' ?     ?     -0.13225600 -0.99121600 0.00000000 409.06600 0.99121600  -0.13225600 0.00000000 
27.17010  0.00000000  0.00000000  1.00000000 32.20000  
14 'helical symmetry operation' ?     ?     0.55339200  -0.83292100 0.00000000 246.48900 0.83292100  0.55339200  0.00000000 
-74.41930 -0.00000000 0.00000000  1.00000000 48.30000  
15 'helical symmetry operation' ?     ?     0.96501600  -0.26218900 0.00000000 57.24730  0.26218900  0.96501600  0.00000000 
-43.76890 -0.00000000 0.00000000  1.00000000 64.40000  
16 'helical symmetry operation' ?     ?     0.89879400  0.43837100  0.00000000 -64.95150 -0.43837100 0.89879400  0.00000000 
103.94400 0.00000000  -0.00000000 1.00000000 80.50000  
17 'helical symmetry operation' ?     ?     0.38751600  0.92186300  0.00000000 -59.59870 -0.92186300 0.38751600  0.00000000 
295.57700 0.00000000  -0.00000000 1.00000000 96.60000  
18 'helical symmetry operation' ?     ?     -0.31564900 0.94887600  0.00000000 70.65520  -0.94887600 -0.31564900 0.00000000 
436.23800 0.00000000  0.00000000  1.00000000 112.70000 
19 'helical symmetry operation' ?     ?     -0.86251400 0.50603400  0.00000000 261.31200 -0.50603400 -0.86251400 0.00000000 
456.27700 0.00000000  0.00000000  1.00000000 128.80000 
20 'helical symmetry operation' ?     ?     -0.98228700 -0.18738100 0.00000000 417.96500 0.18738100  -0.98228700 0.00000000 
345.77100 0.00000000  0.00000000  1.00000000 144.90000 
# 
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 GLU A 118 ? GLY A 123 ? GLU A 261 GLY A 266 1 ? 6  
HELX_P HELX_P8  AA8 GLU A 138 ? GLY A 150 ? GLU A 281 GLY A 293 1 ? 13 
HELX_P HELX_P9  AA9 PHE A 151 ? GLU A 155 ? PHE A 294 GLU A 298 5 ? 5  
HELX_P HELX_P10 AB1 ARG A 165 ? LEU A 169 ? ARG A 308 LEU A 312 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 170 ? ARG A 175 ? ASP A 313 ARG A 318 5 ? 6  
HELX_P HELX_P12 AB3 ASP A 189 ? HIS A 200 ? ASP A 332 HIS A 343 1 ? 12 
HELX_P HELX_P13 AB4 ASN A 211 ? ARG A 218 ? ASN A 354 ARG A 361 1 ? 8  
HELX_P HELX_P14 AB5 VAL A 223 ? ARG A 240 ? VAL A 366 ARG A 383 1 ? 18 
HELX_P HELX_P15 AB6 THR A 247 ? ILE A 259 ? THR A 390 ILE A 402 1 ? 13 
HELX_P HELX_P16 AB7 SER A 270 ? VAL A 291 ? SER A 413 VAL A 434 1 ? 22 
HELX_P HELX_P17 AB8 SER A 325 ? LEU A 337 ? SER A 468 LEU A 480 1 ? 13 
HELX_P HELX_P18 AB9 LEU A 337 ? PHE A 347 ? LEU A 480 PHE A 490 1 ? 11 
HELX_P HELX_P19 AC1 THR A 351 ? LEU A 372 ? THR A 494 LEU A 515 1 ? 22 
HELX_P HELX_P20 AC2 ASP A 411 ? TYR A 432 ? ASP A 554 TYR A 575 1 ? 22 
HELX_P HELX_P21 AC3 TYR A 432 ? GLU A 447 ? TYR A 575 GLU A 590 1 ? 16 
# 
_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 HIS 280 NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 423 A ZN  801 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc2 metalc ? ? A HIS 284 NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 427 A ZN  801 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc3 metalc ? ? A ASP 357 OD2 ? ? ? 1_555 C ZN  . ZN  ? ? A ASP 500 A ZN  801 1_555 ? ? ? ? ? ? ? 2.233 ? ? 
metalc4 metalc ? ? B MG  .   MG  ? ? ? 1_555 D ATP . O3G ? ? A MG  800 A ATP 802 1_555 ? ? ? ? ? ? ? 2.585 ? ? 
metalc5 metalc ? ? B MG  .   MG  ? ? ? 1_555 D ATP . O2A ? ? A MG  800 A ATP 802 1_555 ? ? ? ? ? ? ? 2.618 ? ? 
# 
_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 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_555 110.4 ? 
2 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_555 119.3 ? 
3 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_555 113.4 ? 
4 O3G ? D ATP .   ? A ATP 802 ? 1_555 MG ? B MG . ? A MG 800 ? 1_555 O2A ? D ATP .   ? A ATP 802 ? 1_555 104.8 ? 
# 
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 79  ? SER A 83  ? PHE A 222 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 PHE A 80  ? N PHE A 223 O PHE A 115 ? O PHE A 258 
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 LEU A 55  ? N LEU A 198 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                   8VWC 
_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 ? ? -157.04 89.12  
2 1 GLU A 590 ? ? 78.14   -12.81 
# 
_pdbx_helical_symmetry.entry_id                  8VWC 
_pdbx_helical_symmetry.number_of_operations      10 
_pdbx_helical_symmetry.rotation_per_n_subunits   -41.2 
_pdbx_helical_symmetry.rise_per_n_subunits       16.1 
_pdbx_helical_symmetry.n_subunits_divisor        1 
_pdbx_helical_symmetry.dyad_axis                 no 
_pdbx_helical_symmetry.circular_symmetry         2 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8VWC 
_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                    8VWC 
_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               579201 
_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 in the Aged State' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8VWC 
_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              8VWC 
_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                8VWC 
_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 LYS 156 ? A LYS 13  
14 1 Y 1 A VAL 231 ? A VAL 88  
15 1 Y 1 A GLU 232 ? A GLU 89  
16 1 Y 1 A LEU 233 ? A LEU 90  
17 1 Y 1 A PHE 234 ? A PHE 91  
18 1 Y 1 A VAL 235 ? A VAL 92  
19 1 Y 1 A GLY 236 ? A GLY 93  
20 1 Y 1 A ARG 267 ? A ARG 124 
21 1 Y 1 A HIS 268 ? A HIS 125 
22 1 Y 1 A ARG 269 ? A ARG 126 
23 1 Y 1 A GLY 270 ? A GLY 127 
24 1 Y 1 A ALA 271 ? A ALA 128 
25 1 Y 1 A GLY 272 ? A GLY 129 
26 1 Y 1 A LEU 273 ? A LEU 130 
27 1 Y 1 A GLY 274 ? A GLY 131 
28 1 Y 1 A GLY 275 ? A GLY 132 
29 1 Y 1 A GLY 276 ? A GLY 133 
30 1 Y 1 A HIS 277 ? A HIS 134 
31 1 Y 1 A ASP 278 ? A ASP 135 
32 1 Y 1 A GLU 279 ? A GLU 136 
33 1 Y 1 A PRO 460 ? A PRO 317 
34 1 Y 1 A GLU 461 ? A GLU 318 
35 1 Y 1 A GLU 462 ? A GLU 319 
36 1 Y 1 A MET 517 ? A MET 374 
37 1 Y 1 A SER 518 ? A SER 375 
38 1 Y 1 A GLU 519 ? A GLU 376 
39 1 Y 1 A GLU 520 ? A GLU 377 
40 1 Y 1 A LEU 521 ? A LEU 378 
41 1 Y 1 A GLY 522 ? A GLY 379 
42 1 Y 1 A PRO 523 ? A PRO 380 
43 1 Y 1 A LEU 524 ? A LEU 381 
44 1 Y 1 A ALA 525 ? A ALA 382 
45 1 Y 1 A TRP 526 ? A TRP 383 
46 1 Y 1 A GLY 527 ? A GLY 384 
47 1 Y 1 A LYS 528 ? A LYS 385 
48 1 Y 1 A GLU 529 ? A GLU 386 
49 1 Y 1 A GLU 530 ? A GLU 387 
50 1 Y 1 A GLN 531 ? A GLN 388 
51 1 Y 1 A GLU 532 ? A GLU 389 
52 1 Y 1 A VAL 533 ? A VAL 390 
53 1 Y 1 A PHE 534 ? A PHE 391 
54 1 Y 1 A LEU 535 ? A LEU 392 
55 1 Y 1 A GLY 536 ? A GLY 393 
56 1 Y 1 A LYS 537 ? A LYS 394 
57 1 Y 1 A GLU 538 ? A GLU 395 
58 1 Y 1 A ILE 539 ? A ILE 396 
59 1 Y 1 A THR 540 ? A THR 397 
60 1 Y 1 A ARG 541 ? A ARG 398 
61 1 Y 1 A LEU 542 ? A LEU 399 
62 1 Y 1 A ARG 543 ? A ARG 400 
63 1 Y 1 A ASN 544 ? A ASN 401 
64 1 Y 1 A TYR 545 ? A TYR 402 
65 1 Y 1 A SER 546 ? A SER 403 
66 1 Y 1 A GLU 547 ? A GLU 404 
67 1 Y 1 A GLU 548 ? A GLU 405 
68 1 Y 1 A VAL 549 ? A VAL 406 
69 1 Y 1 A ALA 550 ? A ALA 407 
70 1 Y 1 A SER 551 ? A SER 408 
71 1 Y 1 A LYS 552 ? A LYS 409 
72 1 Y 1 A GLY 594 ? A GLY 451 
73 1 Y 1 A ASP 595 ? A ASP 452 
74 1 Y 1 A GLU 596 ? A GLU 453 
75 1 Y 1 A LEU 597 ? A LEU 454 
76 1 Y 1 A ARG 598 ? A ARG 455 
77 1 Y 1 A ARG 599 ? A ARG 456 
78 1 Y 1 A ILE 600 ? A ILE 457 
79 1 Y 1 A LEU 601 ? A LEU 458 
80 1 Y 1 A SER 602 ? A SER 459 
81 1 Y 1 A GLU 603 ? A GLU 460 
82 1 Y 1 A GLU 604 ? A GLU 461 
83 1 Y 1 A PHE 605 ? A PHE 462 
84 1 Y 1 A GLU 606 ? A GLU 463 
85 1 Y 1 A LYS 607 ? A LYS 464 
86 1 Y 1 A VAL 608 ? A VAL 465 
87 1 Y 1 A VAL 609 ? A VAL 466 
88 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           8VWC 
_em_admin.last_update        2025-06-11 
_em_admin.map_release_date   2025-01-15 
_em_admin.title              'CryoEM Structure of a FtsH Helical Assembly in the Aged State' 
# 
_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                 C2 
_em_helical_entity.angular_rotation_per_subunit   -41.2 
_em_helical_entity.axial_rise_per_subunit         16.1 
# 
_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                    8VWC 
_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      . ARG A 1 14  ? 154.560 141.013 157.166 1.00 42.60 ? 157 ARG A N      1 
ATOM   2    C  CA     . ARG A 1 14  ? 153.450 141.211 158.087 1.00 45.98 ? 157 ARG A CA     1 
ATOM   3    C  C      . ARG A 1 14  ? 153.705 140.511 159.415 1.00 44.32 ? 157 ARG A C      1 
ATOM   4    O  O      . ARG A 1 14  ? 154.113 139.353 159.447 1.00 45.30 ? 157 ARG A O      1 
ATOM   5    C  CB     . ARG A 1 14  ? 152.144 140.706 157.472 1.00 48.91 ? 157 ARG A CB     1 
ATOM   6    C  CG     . ARG A 1 14  ? 150.916 140.933 158.342 1.00 52.54 ? 157 ARG A CG     1 
ATOM   7    C  CD     . ARG A 1 14  ? 149.671 140.363 157.696 1.00 58.18 ? 157 ARG A CD     1 
ATOM   8    N  NE     . ARG A 1 14  ? 148.457 140.737 158.413 1.00 64.02 ? 157 ARG A NE     1 
ATOM   9    C  CZ     . ARG A 1 14  ? 147.728 139.899 159.136 1.00 66.31 ? 157 ARG A CZ     1 
ATOM   10   N  NH1    . ARG A 1 14  ? 148.068 138.628 159.274 1.00 65.30 ? 157 ARG A NH1    1 
ATOM   11   N  NH2    . ARG A 1 14  ? 146.628 140.346 159.734 1.00 61.37 ? 157 ARG A NH2    1 
ATOM   12   N  N      . VAL A 1 15  ? 153.462 141.228 160.513 1.00 40.50 ? 158 VAL A N      1 
ATOM   13   C  CA     . VAL A 1 15  ? 153.611 140.691 161.857 1.00 40.43 ? 158 VAL A CA     1 
ATOM   14   C  C      . VAL A 1 15  ? 152.371 141.042 162.666 1.00 35.89 ? 158 VAL A C      1 
ATOM   15   O  O      . VAL A 1 15  ? 151.632 141.972 162.344 1.00 37.71 ? 158 VAL A O      1 
ATOM   16   C  CB     . VAL A 1 15  ? 154.886 141.211 162.559 1.00 39.86 ? 158 VAL A CB     1 
ATOM   17   C  CG1    . VAL A 1 15  ? 156.125 140.765 161.806 1.00 41.02 ? 158 VAL A CG1    1 
ATOM   18   C  CG2    . VAL A 1 15  ? 154.862 142.718 162.672 1.00 32.33 ? 158 VAL A CG2    1 
ATOM   19   N  N      . THR A 1 16  ? 152.143 140.267 163.722 1.00 34.49 ? 159 THR A N      1 
ATOM   20   C  CA     . THR A 1 16  ? 151.039 140.504 164.642 1.00 35.56 ? 159 THR A CA     1 
ATOM   21   C  C      . THR A 1 16  ? 151.566 140.323 166.061 1.00 34.27 ? 159 THR A C      1 
ATOM   22   O  O      . THR A 1 16  ? 152.774 140.218 166.285 1.00 35.75 ? 159 THR A O      1 
ATOM   23   C  CB     . THR A 1 16  ? 149.854 139.578 164.337 1.00 39.70 ? 159 THR A CB     1 
ATOM   24   O  OG1    . THR A 1 16  ? 150.258 138.212 164.474 1.00 45.32 ? 159 THR A OG1    1 
ATOM   25   C  CG2    . THR A 1 16  ? 149.345 139.812 162.924 1.00 37.13 ? 159 THR A CG2    1 
ATOM   26   N  N      . PHE A 1 17  ? 150.653 140.289 167.032 1.00 33.79 ? 160 PHE A N      1 
ATOM   27   C  CA     . PHE A 1 17  ? 151.047 140.169 168.430 1.00 33.72 ? 160 PHE A CA     1 
ATOM   28   C  C      . PHE A 1 17  ? 151.578 138.787 168.780 1.00 36.60 ? 160 PHE A C      1 
ATOM   29   O  O      . PHE A 1 17  ? 152.086 138.606 169.890 1.00 36.60 ? 160 PHE A O      1 
ATOM   30   C  CB     . PHE A 1 17  ? 149.873 140.519 169.345 1.00 31.44 ? 160 PHE A CB     1 
ATOM   31   C  CG     . PHE A 1 17  ? 149.625 141.994 169.478 1.00 36.94 ? 160 PHE A CG     1 
ATOM   32   C  CD1    . PHE A 1 17  ? 150.666 142.897 169.382 1.00 35.92 ? 160 PHE A CD1    1 
ATOM   33   C  CD2    . PHE A 1 17  ? 148.347 142.479 169.684 1.00 39.98 ? 160 PHE A CD2    1 
ATOM   34   C  CE1    . PHE A 1 17  ? 150.438 144.254 169.497 1.00 31.12 ? 160 PHE A CE1    1 
ATOM   35   C  CE2    . PHE A 1 17  ? 148.117 143.833 169.800 1.00 34.91 ? 160 PHE A CE2    1 
ATOM   36   C  CZ     . PHE A 1 17  ? 149.164 144.721 169.705 1.00 30.54 ? 160 PHE A CZ     1 
ATOM   37   N  N      . LYS A 1 18  ? 151.465 137.813 167.878 1.00 37.99 ? 161 LYS A N      1 
ATOM   38   C  CA     . LYS A 1 18  ? 152.025 136.487 168.105 1.00 37.63 ? 161 LYS A CA     1 
ATOM   39   C  C      . LYS A 1 18  ? 153.524 136.421 167.857 1.00 35.61 ? 161 LYS A C      1 
ATOM   40   O  O      . LYS A 1 18  ? 154.136 135.388 168.144 1.00 36.30 ? 161 LYS A O      1 
ATOM   41   C  CB     . LYS A 1 18  ? 151.324 135.457 167.222 1.00 41.41 ? 161 LYS A CB     1 
ATOM   42   C  CG     . LYS A 1 18  ? 149.899 135.167 167.622 1.00 51.92 ? 161 LYS A CG     1 
ATOM   43   C  CD     . LYS A 1 18  ? 149.276 134.134 166.702 1.00 61.36 ? 161 LYS A CD     1 
ATOM   44   C  CE     . LYS A 1 18  ? 147.779 134.027 166.927 1.00 67.08 ? 161 LYS A CE     1 
ATOM   45   N  NZ     . LYS A 1 18  ? 147.460 133.638 168.328 1.00 67.49 ? 161 LYS A NZ     1 
ATOM   46   N  N      . ASP A 1 19  ? 154.125 137.485 167.333 1.00 31.70 ? 162 ASP A N      1 
ATOM   47   C  CA     . ASP A 1 19  ? 155.554 137.545 167.074 1.00 27.68 ? 162 ASP A CA     1 
ATOM   48   C  C      . ASP A 1 19  ? 156.310 138.317 168.144 1.00 26.24 ? 162 ASP A C      1 
ATOM   49   O  O      . ASP A 1 19  ? 157.473 138.667 167.933 1.00 25.66 ? 162 ASP A O      1 
ATOM   50   C  CB     . ASP A 1 19  ? 155.809 138.176 165.707 1.00 29.85 ? 162 ASP A CB     1 
ATOM   51   C  CG     . ASP A 1 19  ? 155.144 137.418 164.588 1.00 37.22 ? 162 ASP A CG     1 
ATOM   52   O  OD1    . ASP A 1 19  ? 154.913 136.205 164.751 1.00 43.70 ? 162 ASP A OD1    1 
ATOM   53   O  OD2    . ASP A 1 19  ? 154.847 138.028 163.545 1.00 40.17 ? 162 ASP A OD2    1 
ATOM   54   N  N      . VAL A 1 20  ? 155.679 138.594 169.280 1.00 26.05 ? 163 VAL A N      1 
ATOM   55   C  CA     . VAL A 1 20  ? 156.257 139.418 170.334 1.00 25.30 ? 163 VAL A CA     1 
ATOM   56   C  C      . VAL A 1 20  ? 156.285 138.604 171.620 1.00 26.20 ? 163 VAL A C      1 
ATOM   57   O  O      . VAL A 1 20  ? 155.308 137.925 171.950 1.00 28.20 ? 163 VAL A O      1 
ATOM   58   C  CB     . VAL A 1 20  ? 155.464 140.724 170.530 1.00 24.22 ? 163 VAL A CB     1 
ATOM   59   C  CG1    . VAL A 1 20  ? 156.199 141.654 171.472 1.00 21.24 ? 163 VAL A CG1    1 
ATOM   60   C  CG2    . VAL A 1 20  ? 155.202 141.400 169.194 1.00 24.98 ? 163 VAL A CG2    1 
ATOM   61   N  N      . GLY A 1 21  ? 157.398 138.670 172.337 1.00 25.34 ? 164 GLY A N      1 
ATOM   62   C  CA     . GLY A 1 21  ? 157.567 137.935 173.582 1.00 24.78 ? 164 GLY A CA     1 
ATOM   63   C  C      . GLY A 1 21  ? 157.960 138.846 174.727 1.00 29.21 ? 164 GLY A C      1 
ATOM   64   O  O      . GLY A 1 21  ? 158.731 139.788 174.542 1.00 27.75 ? 164 GLY A O      1 
ATOM   65   N  N      . GLY A 1 22  ? 157.417 138.563 175.906 1.00 35.66 ? 165 GLY A N      1 
ATOM   66   C  CA     . GLY A 1 22  ? 157.792 139.273 177.120 1.00 38.85 ? 165 GLY A CA     1 
ATOM   67   C  C      . GLY A 1 22  ? 157.410 140.737 177.174 1.00 47.60 ? 165 GLY A C      1 
ATOM   68   O  O      . GLY A 1 22  ? 158.171 141.552 177.709 1.00 52.72 ? 165 GLY A O      1 
ATOM   69   N  N      . ALA A 1 23  ? 156.244 141.095 176.643 1.00 41.78 ? 166 ALA A N      1 
ATOM   70   C  CA     . ALA A 1 23  ? 155.774 142.478 176.662 1.00 38.55 ? 166 ALA A CA     1 
ATOM   71   C  C      . ALA A 1 23  ? 154.287 142.520 176.997 1.00 40.66 ? 166 ALA A C      1 
ATOM   72   O  O      . ALA A 1 23  ? 153.501 143.221 176.360 1.00 39.04 ? 166 ALA A O      1 
ATOM   73   C  CB     . ALA A 1 23  ? 156.060 143.168 175.332 1.00 32.49 ? 166 ALA A CB     1 
ATOM   74   N  N      . GLU A 1 24  ? 153.885 141.758 178.016 1.00 42.46 ? 167 GLU A N      1 
ATOM   75   C  CA     . GLU A 1 24  ? 152.465 141.622 178.327 1.00 41.71 ? 167 GLU A CA     1 
ATOM   76   C  C      . GLU A 1 24  ? 151.842 142.950 178.737 1.00 41.28 ? 167 GLU A C      1 
ATOM   77   O  O      . GLU A 1 24  ? 150.740 143.288 178.293 1.00 42.54 ? 167 GLU A O      1 
ATOM   78   C  CB     . GLU A 1 24  ? 152.267 140.582 179.427 1.00 47.71 ? 167 GLU A CB     1 
ATOM   79   C  CG     . GLU A 1 24  ? 152.454 139.148 178.975 1.00 51.77 ? 167 GLU A CG     1 
ATOM   80   C  CD     . GLU A 1 24  ? 153.881 138.666 179.126 1.00 60.01 ? 167 GLU A CD     1 
ATOM   81   O  OE1    . GLU A 1 24  ? 154.614 139.219 179.973 1.00 58.52 ? 167 GLU A OE1    1 
ATOM   82   O  OE2    . GLU A 1 24  ? 154.268 137.727 178.401 1.00 63.31 ? 167 GLU A OE2    1 
ATOM   83   N  N      . GLU A 1 25  ? 152.520 143.710 179.597 1.00 41.64 ? 168 GLU A N      1 
ATOM   84   C  CA     . GLU A 1 25  ? 151.954 144.969 180.071 1.00 40.70 ? 168 GLU A CA     1 
ATOM   85   C  C      . GLU A 1 25  ? 151.825 145.987 178.944 1.00 38.91 ? 168 GLU A C      1 
ATOM   86   O  O      . GLU A 1 25  ? 150.820 146.700 178.860 1.00 41.26 ? 168 GLU A O      1 
ATOM   87   C  CB     . GLU A 1 25  ? 152.803 145.526 181.212 1.00 47.55 ? 168 GLU A CB     1 
ATOM   88   C  CG     . GLU A 1 25  ? 152.750 144.687 182.473 1.00 59.28 ? 168 GLU A CG     1 
ATOM   89   C  CD     . GLU A 1 25  ? 153.641 145.224 183.575 1.00 69.05 ? 168 GLU A CD     1 
ATOM   90   O  OE1    . GLU A 1 25  ? 154.365 146.214 183.332 1.00 68.15 ? 168 GLU A OE1    1 
ATOM   91   O  OE2    . GLU A 1 25  ? 153.616 144.657 184.687 1.00 70.48 ? 168 GLU A OE2    1 
ATOM   92   N  N      . ALA A 1 26  ? 152.834 146.082 178.077 1.00 37.16 ? 169 ALA A N      1 
ATOM   93   C  CA     . ALA A 1 26  ? 152.767 147.020 176.962 1.00 32.83 ? 169 ALA A CA     1 
ATOM   94   C  C      . ALA A 1 26  ? 151.665 146.646 175.980 1.00 33.07 ? 169 ALA A C      1 
ATOM   95   O  O      . ALA A 1 26  ? 150.968 147.521 175.460 1.00 32.35 ? 169 ALA A O      1 
ATOM   96   C  CB     . ALA A 1 26  ? 154.117 147.090 176.253 1.00 26.75 ? 169 ALA A CB     1 
ATOM   97   N  N      . ILE A 1 27  ? 151.503 145.350 175.704 1.00 32.84 ? 170 ILE A N      1 
ATOM   98   C  CA     . ILE A 1 27  ? 150.452 144.898 174.796 1.00 32.31 ? 170 ILE A CA     1 
ATOM   99   C  C      . ILE A 1 27  ? 149.075 145.169 175.382 1.00 37.43 ? 170 ILE A C      1 
ATOM   100  O  O      . ILE A 1 27  ? 148.105 145.371 174.644 1.00 39.11 ? 170 ILE A O      1 
ATOM   101  C  CB     . ILE A 1 27  ? 150.648 143.405 174.467 1.00 35.06 ? 170 ILE A CB     1 
ATOM   102  C  CG1    . ILE A 1 27  ? 151.826 143.225 173.511 1.00 34.46 ? 170 ILE A CG1    1 
ATOM   103  C  CG2    . ILE A 1 27  ? 149.382 142.811 173.878 1.00 34.79 ? 170 ILE A CG2    1 
ATOM   104  C  CD1    . ILE A 1 27  ? 152.163 141.790 173.219 1.00 29.69 ? 170 ILE A CD1    1 
ATOM   105  N  N      . GLU A 1 28  ? 148.959 145.161 176.709 1.00 38.40 ? 171 GLU A N      1 
ATOM   106  C  CA     . GLU A 1 28  ? 147.682 145.457 177.349 1.00 39.22 ? 171 GLU A CA     1 
ATOM   107  C  C      . GLU A 1 28  ? 147.241 146.890 177.072 1.00 38.70 ? 171 GLU A C      1 
ATOM   108  O  O      . GLU A 1 28  ? 146.055 147.147 176.841 1.00 41.02 ? 171 GLU A O      1 
ATOM   109  C  CB     . GLU A 1 28  ? 147.789 145.205 178.851 1.00 43.78 ? 171 GLU A CB     1 
ATOM   110  C  CG     . GLU A 1 28  ? 146.469 144.962 179.538 1.00 55.35 ? 171 GLU A CG     1 
ATOM   111  C  CD     . GLU A 1 28  ? 145.647 143.896 178.849 1.00 64.46 ? 171 GLU A CD     1 
ATOM   112  O  OE1    . GLU A 1 28  ? 146.247 143.002 178.218 1.00 61.44 ? 171 GLU A OE1    1 
ATOM   113  O  OE2    . GLU A 1 28  ? 144.402 143.953 178.938 1.00 66.81 ? 171 GLU A OE2    1 
ATOM   114  N  N      . GLU A 1 29  ? 148.182 147.836 177.095 1.00 37.94 ? 172 GLU A N      1 
ATOM   115  C  CA     . GLU A 1 29  ? 147.847 149.237 176.871 1.00 34.46 ? 172 GLU A CA     1 
ATOM   116  C  C      . GLU A 1 29  ? 147.516 149.527 175.412 1.00 33.74 ? 172 GLU A C      1 
ATOM   117  O  O      . GLU A 1 29  ? 146.801 150.492 175.125 1.00 34.64 ? 172 GLU A O      1 
ATOM   118  C  CB     . GLU A 1 29  ? 148.999 150.128 177.328 1.00 36.97 ? 172 GLU A CB     1 
ATOM   119  C  CG     . GLU A 1 29  ? 149.243 150.120 178.821 1.00 42.37 ? 172 GLU A CG     1 
ATOM   120  C  CD     . GLU A 1 29  ? 148.205 150.922 179.584 1.00 58.88 ? 172 GLU A CD     1 
ATOM   121  O  OE1    . GLU A 1 29  ? 147.577 151.816 178.979 1.00 58.02 ? 172 GLU A OE1    1 
ATOM   122  O  OE2    . GLU A 1 29  ? 148.017 150.663 180.790 1.00 68.44 ? 172 GLU A OE2    1 
ATOM   123  N  N      . LEU A 1 30  ? 148.028 148.728 174.483 1.00 33.94 ? 173 LEU A N      1 
ATOM   124  C  CA     . LEU A 1 30  ? 147.830 148.968 173.061 1.00 28.66 ? 173 LEU A CA     1 
ATOM   125  C  C      . LEU A 1 30  ? 146.559 148.336 172.513 1.00 31.30 ? 173 LEU A C      1 
ATOM   126  O  O      . LEU A 1 30  ? 146.238 148.548 171.341 1.00 31.17 ? 173 LEU A O      1 
ATOM   127  C  CB     . LEU A 1 30  ? 149.037 148.467 172.264 1.00 26.10 ? 173 LEU A CB     1 
ATOM   128  C  CG     . LEU A 1 30  ? 150.331 149.267 172.400 1.00 25.91 ? 173 LEU A CG     1 
ATOM   129  C  CD1    . LEU A 1 30  ? 151.505 148.485 171.847 1.00 23.38 ? 173 LEU A CD1    1 
ATOM   130  C  CD2    . LEU A 1 30  ? 150.208 150.610 171.706 1.00 22.07 ? 173 LEU A CD2    1 
ATOM   131  N  N      . LYS A 1 31  ? 145.829 147.569 173.324 1.00 34.53 ? 174 LYS A N      1 
ATOM   132  C  CA     . LYS A 1 31  ? 144.575 146.985 172.861 1.00 35.42 ? 174 LYS A CA     1 
ATOM   133  C  C      . LYS A 1 31  ? 143.540 148.055 172.548 1.00 34.27 ? 174 LYS A C      1 
ATOM   134  O  O      . LYS A 1 31  ? 142.710 147.870 171.653 1.00 33.90 ? 174 LYS A O      1 
ATOM   135  C  CB     . LYS A 1 31  ? 144.027 146.019 173.909 1.00 38.42 ? 174 LYS A CB     1 
ATOM   136  C  CG     . LYS A 1 31  ? 144.834 144.749 174.067 1.00 42.82 ? 174 LYS A CG     1 
ATOM   137  C  CD     . LYS A 1 31  ? 144.809 143.909 172.809 1.00 42.74 ? 174 LYS A CD     1 
ATOM   138  C  CE     . LYS A 1 31  ? 145.489 142.572 173.039 1.00 48.29 ? 174 LYS A CE     1 
ATOM   139  N  NZ     . LYS A 1 31  ? 145.191 142.023 174.388 1.00 49.49 ? 174 LYS A NZ     1 
ATOM   140  N  N      . GLU A 1 32  ? 143.571 149.169 173.281 1.00 34.97 ? 175 GLU A N      1 
ATOM   141  C  CA     . GLU A 1 32  ? 142.645 150.268 173.036 1.00 31.66 ? 175 GLU A CA     1 
ATOM   142  C  C      . GLU A 1 32  ? 142.847 150.875 171.655 1.00 29.47 ? 175 GLU A C      1 
ATOM   143  O  O      . GLU A 1 32  ? 141.881 151.256 170.989 1.00 30.49 ? 175 GLU A O      1 
ATOM   144  C  CB     . GLU A 1 32  ? 142.827 151.329 174.115 1.00 34.70 ? 175 GLU A CB     1 
ATOM   145  C  CG     . GLU A 1 32  ? 141.749 152.377 174.165 1.00 41.75 ? 175 GLU A CG     1 
ATOM   146  C  CD     . GLU A 1 32  ? 141.914 153.291 175.355 1.00 53.02 ? 175 GLU A CD     1 
ATOM   147  O  OE1    . GLU A 1 32  ? 142.649 154.292 175.235 1.00 51.87 ? 175 GLU A OE1    1 
ATOM   148  O  OE2    . GLU A 1 32  ? 141.315 153.005 176.413 1.00 61.20 ? 175 GLU A OE2    1 
ATOM   149  N  N      . VAL A 1 33  ? 144.102 150.999 171.221 1.00 27.02 ? 176 VAL A N      1 
ATOM   150  C  CA     . VAL A 1 33  ? 144.393 151.583 169.917 1.00 25.99 ? 176 VAL A CA     1 
ATOM   151  C  C      . VAL A 1 33  ? 143.866 150.702 168.791 1.00 25.79 ? 176 VAL A C      1 
ATOM   152  O  O      . VAL A 1 33  ? 143.362 151.210 167.786 1.00 27.42 ? 176 VAL A O      1 
ATOM   153  C  CB     . VAL A 1 33  ? 145.906 151.839 169.781 1.00 26.60 ? 176 VAL A CB     1 
ATOM   154  C  CG1    . VAL A 1 33  ? 146.202 152.667 168.547 1.00 21.54 ? 176 VAL A CG1    1 
ATOM   155  C  CG2    . VAL A 1 33  ? 146.432 152.531 171.019 1.00 24.74 ? 176 VAL A CG2    1 
ATOM   156  N  N      . VAL A 1 34  ? 143.985 149.381 168.922 1.00 27.07 ? 177 VAL A N      1 
ATOM   157  C  CA     . VAL A 1 34  ? 143.523 148.489 167.863 1.00 29.34 ? 177 VAL A CA     1 
ATOM   158  C  C      . VAL A 1 34  ? 142.013 148.597 167.690 1.00 29.20 ? 177 VAL A C      1 
ATOM   159  O  O      . VAL A 1 34  ? 141.509 148.663 166.564 1.00 28.14 ? 177 VAL A O      1 
ATOM   160  C  CB     . VAL A 1 34  ? 143.968 147.042 168.149 1.00 31.53 ? 177 VAL A CB     1 
ATOM   161  C  CG1    . VAL A 1 34  ? 143.300 146.074 167.188 1.00 29.54 ? 177 VAL A CG1    1 
ATOM   162  C  CG2    . VAL A 1 34  ? 145.478 146.923 168.049 1.00 28.72 ? 177 VAL A CG2    1 
ATOM   163  N  N      . GLU A 1 35  ? 141.267 148.628 168.797 1.00 28.02 ? 178 GLU A N      1 
ATOM   164  C  CA     . GLU A 1 35  ? 139.814 148.743 168.715 1.00 25.90 ? 178 GLU A CA     1 
ATOM   165  C  C      . GLU A 1 35  ? 139.391 150.054 168.066 1.00 27.70 ? 178 GLU A C      1 
ATOM   166  O  O      . GLU A 1 35  ? 138.454 150.084 167.262 1.00 30.89 ? 178 GLU A O      1 
ATOM   167  C  CB     . GLU A 1 35  ? 139.200 148.618 170.107 1.00 27.90 ? 178 GLU A CB     1 
ATOM   168  C  CG     . GLU A 1 35  ? 139.265 147.229 170.703 1.00 34.27 ? 178 GLU A CG     1 
ATOM   169  C  CD     . GLU A 1 35  ? 138.937 146.142 169.700 1.00 43.11 ? 178 GLU A CD     1 
ATOM   170  O  OE1    . GLU A 1 35  ? 137.895 146.247 169.024 1.00 46.16 ? 178 GLU A OE1    1 
ATOM   171  O  OE2    . GLU A 1 35  ? 139.716 145.175 169.592 1.00 44.12 ? 178 GLU A OE2    1 
ATOM   172  N  N      . PHE A 1 36  ? 140.063 151.152 168.410 1.00 25.49 ? 179 PHE A N      1 
ATOM   173  C  CA     . PHE A 1 36  ? 139.709 152.448 167.843 1.00 23.35 ? 179 PHE A CA     1 
ATOM   174  C  C      . PHE A 1 36  ? 139.910 152.467 166.333 1.00 25.93 ? 179 PHE A C      1 
ATOM   175  O  O      . PHE A 1 36  ? 139.095 153.031 165.599 1.00 27.14 ? 179 PHE A O      1 
ATOM   176  C  CB     . PHE A 1 36  ? 140.530 153.547 168.521 1.00 22.28 ? 179 PHE A CB     1 
ATOM   177  C  CG     . PHE A 1 36  ? 140.352 154.908 167.917 1.00 22.20 ? 179 PHE A CG     1 
ATOM   178  C  CD1    . PHE A 1 36  ? 139.151 155.581 168.032 1.00 24.14 ? 179 PHE A CD1    1 
ATOM   179  C  CD2    . PHE A 1 36  ? 141.391 155.522 167.244 1.00 21.72 ? 179 PHE A CD2    1 
ATOM   180  C  CE1    . PHE A 1 36  ? 138.988 156.834 167.484 1.00 25.49 ? 179 PHE A CE1    1 
ATOM   181  C  CE2    . PHE A 1 36  ? 141.234 156.775 166.694 1.00 24.21 ? 179 PHE A CE2    1 
ATOM   182  C  CZ     . PHE A 1 36  ? 140.031 157.432 166.815 1.00 25.64 ? 179 PHE A CZ     1 
ATOM   183  N  N      . LEU A 1 37  ? 140.997 151.865 165.849 1.00 25.99 ? 180 LEU A N      1 
ATOM   184  C  CA     . LEU A 1 37  ? 141.281 151.881 164.420 1.00 25.39 ? 180 LEU A CA     1 
ATOM   185  C  C      . LEU A 1 37  ? 140.331 150.995 163.625 1.00 28.73 ? 180 LEU A C      1 
ATOM   186  O  O      . LEU A 1 37  ? 140.143 151.229 162.428 1.00 29.68 ? 180 LEU A O      1 
ATOM   187  C  CB     . LEU A 1 37  ? 142.723 151.449 164.166 1.00 24.53 ? 180 LEU A CB     1 
ATOM   188  C  CG     . LEU A 1 37  ? 143.801 152.497 164.437 1.00 23.86 ? 180 LEU A CG     1 
ATOM   189  C  CD1    . LEU A 1 37  ? 145.120 151.826 164.741 1.00 23.34 ? 180 LEU A CD1    1 
ATOM   190  C  CD2    . LEU A 1 37  ? 143.938 153.449 163.270 1.00 22.17 ? 180 LEU A CD2    1 
ATOM   191  N  N      . LYS A 1 38  ? 139.737 149.984 164.254 1.00 29.82 ? 181 LYS A N      1 
ATOM   192  C  CA     . LYS A 1 38  ? 138.818 149.103 163.547 1.00 29.24 ? 181 LYS A CA     1 
ATOM   193  C  C      . LYS A 1 38  ? 137.444 149.733 163.342 1.00 35.58 ? 181 LYS A C      1 
ATOM   194  O  O      . LYS A 1 38  ? 136.787 149.453 162.334 1.00 39.34 ? 181 LYS A O      1 
ATOM   195  C  CB     . LYS A 1 38  ? 138.692 147.778 164.295 1.00 30.09 ? 181 LYS A CB     1 
ATOM   196  C  CG     . LYS A 1 38  ? 139.814 146.807 163.983 1.00 32.86 ? 181 LYS A CG     1 
ATOM   197  C  CD     . LYS A 1 38  ? 139.466 145.395 164.393 1.00 33.13 ? 181 LYS A CD     1 
ATOM   198  C  CE     . LYS A 1 38  ? 139.778 145.148 165.852 1.00 38.11 ? 181 LYS A CE     1 
ATOM   199  N  NZ     . LYS A 1 38  ? 139.861 143.694 166.153 1.00 44.65 ? 181 LYS A NZ     1 
ATOM   200  N  N      . ASP A 1 39  ? 136.987 150.570 164.271 1.00 36.53 ? 182 ASP A N      1 
ATOM   201  C  CA     . ASP A 1 39  ? 135.691 151.226 164.138 1.00 34.56 ? 182 ASP A CA     1 
ATOM   202  C  C      . ASP A 1 39  ? 135.635 152.500 164.971 1.00 32.70 ? 182 ASP A C      1 
ATOM   203  O  O      . ASP A 1 39  ? 135.229 152.463 166.138 1.00 33.26 ? 182 ASP A O      1 
ATOM   204  C  CB     . ASP A 1 39  ? 134.570 150.271 164.545 1.00 37.86 ? 182 ASP A CB     1 
ATOM   205  C  CG     . ASP A 1 39  ? 133.205 150.748 164.095 1.00 44.98 ? 182 ASP A CG     1 
ATOM   206  O  OD1    . ASP A 1 39  ? 133.126 151.456 163.071 1.00 46.11 ? 182 ASP A OD1    1 
ATOM   207  O  OD2    . ASP A 1 39  ? 132.209 150.408 164.762 1.00 46.48 ? 182 ASP A OD2    1 
ATOM   208  N  N      . PRO A 1 40  ? 136.033 153.643 164.412 1.00 32.91 ? 183 PRO A N      1 
ATOM   209  C  CA     . PRO A 1 40  ? 136.019 154.889 165.199 1.00 31.44 ? 183 PRO A CA     1 
ATOM   210  C  C      . PRO A 1 40  ? 134.643 155.296 165.694 1.00 33.53 ? 183 PRO A C      1 
ATOM   211  O  O      . PRO A 1 40  ? 134.544 155.952 166.736 1.00 32.69 ? 183 PRO A O      1 
ATOM   212  C  CB     . PRO A 1 40  ? 136.592 155.926 164.223 1.00 28.39 ? 183 PRO A CB     1 
ATOM   213  C  CG     . PRO A 1 40  ? 137.305 155.138 163.191 1.00 30.27 ? 183 PRO A CG     1 
ATOM   214  C  CD     . PRO A 1 40  ? 136.576 153.847 163.062 1.00 30.50 ? 183 PRO A CD     1 
ATOM   215  N  N      . SER A 1 41  ? 133.575 154.932 164.982 1.00 35.08 ? 184 SER A N      1 
ATOM   216  C  CA     . SER A 1 41  ? 132.246 155.415 165.338 1.00 34.09 ? 184 SER A CA     1 
ATOM   217  C  C      . SER A 1 41  ? 131.816 154.949 166.723 1.00 33.76 ? 184 SER A C      1 
ATOM   218  O  O      . SER A 1 41  ? 131.007 155.617 167.373 1.00 36.12 ? 184 SER A O      1 
ATOM   219  C  CB     . SER A 1 41  ? 131.229 154.970 164.288 1.00 36.14 ? 184 SER A CB     1 
ATOM   220  O  OG     . SER A 1 41  ? 130.815 153.637 164.509 1.00 41.67 ? 184 SER A OG     1 
ATOM   221  N  N      . LYS A 1 42  ? 132.329 153.810 167.188 1.00 33.12 ? 185 LYS A N      1 
ATOM   222  C  CA     . LYS A 1 42  ? 131.976 153.334 168.520 1.00 35.07 ? 185 LYS A CA     1 
ATOM   223  C  C      . LYS A 1 42  ? 132.529 154.226 169.623 1.00 35.35 ? 185 LYS A C      1 
ATOM   224  O  O      . LYS A 1 42  ? 131.957 154.266 170.715 1.00 37.53 ? 185 LYS A O      1 
ATOM   225  C  CB     . LYS A 1 42  ? 132.463 151.902 168.715 1.00 38.24 ? 185 LYS A CB     1 
ATOM   226  C  CG     . LYS A 1 42  ? 131.648 150.873 167.965 1.00 44.79 ? 185 LYS A CG     1 
ATOM   227  C  CD     . LYS A 1 42  ? 131.848 149.487 168.538 1.00 49.41 ? 185 LYS A CD     1 
ATOM   228  C  CE     . LYS A 1 42  ? 130.968 148.469 167.836 1.00 53.28 ? 185 LYS A CE     1 
ATOM   229  N  NZ     . LYS A 1 42  ? 129.525 148.754 168.032 1.00 55.17 ? 185 LYS A NZ     1 
ATOM   230  N  N      . PHE A 1 43  ? 133.631 154.927 169.370 1.00 34.60 ? 186 PHE A N      1 
ATOM   231  C  CA     . PHE A 1 43  ? 134.165 155.896 170.318 1.00 30.78 ? 186 PHE A CA     1 
ATOM   232  C  C      . PHE A 1 43  ? 133.452 157.240 170.226 1.00 33.01 ? 186 PHE A C      1 
ATOM   233  O  O      . PHE A 1 43  ? 133.267 157.912 171.244 1.00 33.04 ? 186 PHE A O      1 
ATOM   234  C  CB     . PHE A 1 43  ? 135.668 156.087 170.083 1.00 28.66 ? 186 PHE A CB     1 
ATOM   235  C  CG     . PHE A 1 43  ? 136.511 154.953 170.590 1.00 29.24 ? 186 PHE A CG     1 
ATOM   236  C  CD1    . PHE A 1 43  ? 136.432 153.697 170.016 1.00 28.21 ? 186 PHE A CD1    1 
ATOM   237  C  CD2    . PHE A 1 43  ? 137.397 155.147 171.632 1.00 27.37 ? 186 PHE A CD2    1 
ATOM   238  C  CE1    . PHE A 1 43  ? 137.206 152.658 170.483 1.00 24.47 ? 186 PHE A CE1    1 
ATOM   239  C  CE2    . PHE A 1 43  ? 138.175 154.109 172.102 1.00 25.65 ? 186 PHE A CE2    1 
ATOM   240  C  CZ     . PHE A 1 43  ? 138.079 152.865 171.525 1.00 23.31 ? 186 PHE A CZ     1 
ATOM   241  N  N      . ASN A 1 44  ? 133.046 157.639 169.020 1.00 33.87 ? 187 ASN A N      1 
ATOM   242  C  CA     . ASN A 1 44  ? 132.446 158.953 168.822 1.00 32.49 ? 187 ASN A CA     1 
ATOM   243  C  C      . ASN A 1 44  ? 131.054 159.049 169.434 1.00 35.74 ? 187 ASN A C      1 
ATOM   244  O  O      . ASN A 1 44  ? 130.676 160.110 169.943 1.00 40.37 ? 187 ASN A O      1 
ATOM   245  C  CB     . ASN A 1 44  ? 132.381 159.279 167.330 1.00 31.10 ? 187 ASN A CB     1 
ATOM   246  C  CG     . ASN A 1 44  ? 133.750 159.372 166.690 1.00 35.28 ? 187 ASN A CG     1 
ATOM   247  O  OD1    . ASN A 1 44  ? 134.768 159.401 167.374 1.00 37.05 ? 187 ASN A OD1    1 
ATOM   248  N  ND2    . ASN A 1 44  ? 133.779 159.401 165.367 1.00 33.69 ? 187 ASN A ND2    1 
ATOM   249  N  N      . ARG A 1 45  ? 130.283 157.966 169.398 1.00 35.55 ? 188 ARG A N      1 
ATOM   250  C  CA     . ARG A 1 45  ? 128.889 158.020 169.817 1.00 35.19 ? 188 ARG A CA     1 
ATOM   251  C  C      . ARG A 1 45  ? 128.715 158.214 171.318 1.00 37.84 ? 188 ARG A C      1 
ATOM   252  O  O      . ARG A 1 45  ? 127.593 158.473 171.759 1.00 41.04 ? 188 ARG A O      1 
ATOM   253  C  CB     . ARG A 1 45  ? 128.165 156.754 169.366 1.00 36.85 ? 188 ARG A CB     1 
ATOM   254  C  CG     . ARG A 1 45  ? 128.322 155.585 170.304 1.00 42.92 ? 188 ARG A CG     1 
ATOM   255  C  CD     . ARG A 1 45  ? 127.747 154.322 169.697 1.00 45.58 ? 188 ARG A CD     1 
ATOM   256  N  NE     . ARG A 1 45  ? 128.059 153.149 170.503 1.00 53.13 ? 188 ARG A NE     1 
ATOM   257  C  CZ     . ARG A 1 45  ? 127.906 151.897 170.095 1.00 55.71 ? 188 ARG A CZ     1 
ATOM   258  N  NH1    . ARG A 1 45  ? 127.456 151.615 168.885 1.00 54.58 ? 188 ARG A NH1    1 
ATOM   259  N  NH2    . ARG A 1 45  ? 128.218 150.903 170.921 1.00 55.66 ? 188 ARG A NH2    1 
ATOM   260  N  N      . ILE A 1 46  ? 129.779 158.095 172.112 1.00 35.26 ? 189 ILE A N      1 
ATOM   261  C  CA     . ILE A 1 46  ? 129.704 158.361 173.541 1.00 33.91 ? 189 ILE A CA     1 
ATOM   262  C  C      . ILE A 1 46  ? 130.695 159.430 173.979 1.00 35.25 ? 189 ILE A C      1 
ATOM   263  O  O      . ILE A 1 46  ? 130.913 159.614 175.173 1.00 37.51 ? 189 ILE A O      1 
ATOM   264  C  CB     . ILE A 1 46  ? 129.884 157.071 174.366 1.00 32.87 ? 189 ILE A CB     1 
ATOM   265  C  CG1    . ILE A 1 46  ? 131.279 156.479 174.163 1.00 33.26 ? 189 ILE A CG1    1 
ATOM   266  C  CG2    . ILE A 1 46  ? 128.810 156.063 174.013 1.00 33.80 ? 189 ILE A CG2    1 
ATOM   267  C  CD1    . ILE A 1 46  ? 131.664 155.482 175.223 1.00 26.56 ? 189 ILE A CD1    1 
ATOM   268  N  N      . GLY A 1 47  ? 131.296 160.145 173.033 1.00 33.25 ? 190 GLY A N      1 
ATOM   269  C  CA     . GLY A 1 47  ? 132.143 161.271 173.369 1.00 31.37 ? 190 GLY A CA     1 
ATOM   270  C  C      . GLY A 1 47  ? 133.492 160.939 173.964 1.00 32.57 ? 190 GLY A C      1 
ATOM   271  O  O      . GLY A 1 47  ? 134.059 161.769 174.679 1.00 35.61 ? 190 GLY A O      1 
ATOM   272  N  N      . ALA A 1 48  ? 134.029 159.752 173.693 1.00 31.95 ? 191 ALA A N      1 
ATOM   273  C  CA     . ALA A 1 48  ? 135.350 159.385 174.186 1.00 26.51 ? 191 ALA A CA     1 
ATOM   274  C  C      . ALA A 1 48  ? 136.425 159.929 173.255 1.00 26.84 ? 191 ALA A C      1 
ATOM   275  O  O      . ALA A 1 48  ? 136.432 159.630 172.058 1.00 29.63 ? 191 ALA A O      1 
ATOM   276  C  CB     . ALA A 1 48  ? 135.472 157.868 174.311 1.00 24.84 ? 191 ALA A CB     1 
ATOM   277  N  N      . ARG A 1 49  ? 137.339 160.718 173.808 1.00 26.08 ? 192 ARG A N      1 
ATOM   278  C  CA     . ARG A 1 49  ? 138.338 161.443 173.032 1.00 24.56 ? 192 ARG A CA     1 
ATOM   279  C  C      . ARG A 1 49  ? 139.689 160.750 173.176 1.00 24.38 ? 192 ARG A C      1 
ATOM   280  O  O      . ARG A 1 49  ? 140.164 160.536 174.294 1.00 28.41 ? 192 ARG A O      1 
ATOM   281  C  CB     . ARG A 1 49  ? 138.408 162.899 173.491 1.00 23.95 ? 192 ARG A CB     1 
ATOM   282  C  CG     . ARG A 1 49  ? 139.702 163.613 173.176 1.00 30.09 ? 192 ARG A CG     1 
ATOM   283  C  CD     . ARG A 1 49  ? 139.682 165.040 173.703 1.00 30.36 ? 192 ARG A CD     1 
ATOM   284  N  NE     . ARG A 1 49  ? 139.980 165.104 175.129 1.00 35.05 ? 192 ARG A NE     1 
ATOM   285  C  CZ     . ARG A 1 49  ? 139.115 165.474 176.065 1.00 37.44 ? 192 ARG A CZ     1 
ATOM   286  N  NH1    . ARG A 1 49  ? 137.875 165.821 175.765 1.00 32.73 ? 192 ARG A NH1    1 
ATOM   287  N  NH2    . ARG A 1 49  ? 139.506 165.495 177.336 1.00 32.78 ? 192 ARG A NH2    1 
ATOM   288  N  N      . MET A 1 50  ? 140.305 160.402 172.042 1.00 24.81 ? 193 MET A N      1 
ATOM   289  C  CA     . MET A 1 50  ? 141.573 159.689 171.975 1.00 24.83 ? 193 MET A CA     1 
ATOM   290  C  C      . MET A 1 50  ? 142.743 160.666 171.913 1.00 25.75 ? 193 MET A C      1 
ATOM   291  O  O      . MET A 1 50  ? 142.611 161.772 171.383 1.00 27.65 ? 193 MET A O      1 
ATOM   292  C  CB     . MET A 1 50  ? 141.613 158.785 170.746 1.00 23.38 ? 193 MET A CB     1 
ATOM   293  C  CG     . MET A 1 50  ? 140.980 157.418 170.936 1.00 24.69 ? 193 MET A CG     1 
ATOM   294  S  SD     . MET A 1 50  ? 141.785 156.394 172.181 1.00 45.59 ? 193 MET A SD     1 
ATOM   295  C  CE     . MET A 1 50  ? 142.837 155.371 171.165 1.00 26.83 ? 193 MET A CE     1 
ATOM   296  N  N      . PRO A 1 51  ? 143.897 160.282 172.449 1.00 26.23 ? 194 PRO A N      1 
ATOM   297  C  CA     . PRO A 1 51  ? 145.093 161.115 172.300 1.00 24.63 ? 194 PRO A CA     1 
ATOM   298  C  C      . PRO A 1 51  ? 145.558 161.166 170.854 1.00 21.50 ? 194 PRO A C      1 
ATOM   299  O  O      . PRO A 1 51  ? 145.322 160.256 170.060 1.00 25.00 ? 194 PRO A O      1 
ATOM   300  C  CB     . PRO A 1 51  ? 146.128 160.419 173.190 1.00 25.09 ? 194 PRO A CB     1 
ATOM   301  C  CG     . PRO A 1 51  ? 145.650 159.019 173.302 1.00 24.48 ? 194 PRO A CG     1 
ATOM   302  C  CD     . PRO A 1 51  ? 144.155 159.077 173.253 1.00 24.19 ? 194 PRO A CD     1 
ATOM   303  N  N      . LYS A 1 52  ? 146.231 162.259 170.514 1.00 22.01 ? 195 LYS A N      1 
ATOM   304  C  CA     . LYS A 1 52  ? 146.719 162.432 169.154 1.00 21.59 ? 195 LYS A CA     1 
ATOM   305  C  C      . LYS A 1 52  ? 148.066 161.761 168.914 1.00 23.95 ? 195 LYS A C      1 
ATOM   306  O  O      . LYS A 1 52  ? 148.347 161.359 167.782 1.00 24.80 ? 195 LYS A O      1 
ATOM   307  C  CB     . LYS A 1 52  ? 146.814 163.921 168.815 1.00 22.16 ? 195 LYS A CB     1 
ATOM   308  C  CG     . LYS A 1 52  ? 145.493 164.526 168.381 1.00 25.32 ? 195 LYS A CG     1 
ATOM   309  C  CD     . LYS A 1 52  ? 145.655 165.964 167.940 1.00 26.46 ? 195 LYS A CD     1 
ATOM   310  C  CE     . LYS A 1 52  ? 144.655 166.313 166.859 1.00 26.68 ? 195 LYS A CE     1 
ATOM   311  N  NZ     . LYS A 1 52  ? 145.186 167.321 165.912 1.00 26.72 ? 195 LYS A NZ     1 
ATOM   312  N  N      . GLY A 1 53  ? 148.890 161.618 169.943 1.00 21.73 ? 196 GLY A N      1 
ATOM   313  C  CA     . GLY A 1 53  ? 150.194 161.001 169.790 1.00 18.27 ? 196 GLY A CA     1 
ATOM   314  C  C      . GLY A 1 53  ? 150.526 160.111 170.968 1.00 20.65 ? 196 GLY A C      1 
ATOM   315  O  O      . GLY A 1 53  ? 150.064 160.329 172.087 1.00 25.03 ? 196 GLY A O      1 
ATOM   316  N  N      . ILE A 1 54  ? 151.343 159.095 170.696 1.00 20.95 ? 197 ILE A N      1 
ATOM   317  C  CA     . ILE A 1 54  ? 151.785 158.127 171.693 1.00 18.94 ? 197 ILE A CA     1 
ATOM   318  C  C      . ILE A 1 54  ? 153.291 157.942 171.572 1.00 16.94 ? 197 ILE A C      1 
ATOM   319  O  O      . ILE A 1 54  ? 153.827 157.871 170.463 1.00 18.07 ? 197 ILE A O      1 
ATOM   320  C  CB     . ILE A 1 54  ? 151.057 156.777 171.535 1.00 21.20 ? 197 ILE A CB     1 
ATOM   321  C  CG1    . ILE A 1 54  ? 149.553 156.963 171.700 1.00 19.44 ? 197 ILE A CG1    1 
ATOM   322  C  CG2    . ILE A 1 54  ? 151.582 155.770 172.541 1.00 18.84 ? 197 ILE A CG2    1 
ATOM   323  C  CD1    . ILE A 1 54  ? 148.760 155.716 171.454 1.00 18.81 ? 197 ILE A CD1    1 
ATOM   324  N  N      . LEU A 1 55  ? 153.970 157.848 172.712 1.00 17.32 ? 198 LEU A N      1 
ATOM   325  C  CA     . LEU A 1 55  ? 155.422 157.728 172.772 1.00 16.34 ? 198 LEU A CA     1 
ATOM   326  C  C      . LEU A 1 55  ? 155.818 156.395 173.396 1.00 15.72 ? 198 LEU A C      1 
ATOM   327  O  O      . LEU A 1 55  ? 155.308 156.028 174.456 1.00 17.74 ? 198 LEU A O      1 
ATOM   328  C  CB     . LEU A 1 55  ? 156.019 158.889 173.572 1.00 18.22 ? 198 LEU A CB     1 
ATOM   329  C  CG     . LEU A 1 55  ? 157.479 159.272 173.346 1.00 20.52 ? 198 LEU A CG     1 
ATOM   330  C  CD1    . LEU A 1 55  ? 157.742 159.581 171.891 1.00 19.11 ? 198 LEU A CD1    1 
ATOM   331  C  CD2    . LEU A 1 55  ? 157.847 160.456 174.216 1.00 17.79 ? 198 LEU A CD2    1 
ATOM   332  N  N      . LEU A 1 56  ? 156.734 155.683 172.741 1.00 15.17 ? 199 LEU A N      1 
ATOM   333  C  CA     . LEU A 1 56  ? 157.327 154.453 173.260 1.00 14.83 ? 199 LEU A CA     1 
ATOM   334  C  C      . LEU A 1 56  ? 158.761 154.742 173.682 1.00 15.51 ? 199 LEU A C      1 
ATOM   335  O  O      . LEU A 1 56  ? 159.530 155.318 172.908 1.00 16.14 ? 199 LEU A O      1 
ATOM   336  C  CB     . LEU A 1 56  ? 157.303 153.337 172.217 1.00 14.41 ? 199 LEU A CB     1 
ATOM   337  C  CG     . LEU A 1 56  ? 155.982 152.897 171.592 1.00 15.96 ? 199 LEU A CG     1 
ATOM   338  C  CD1    . LEU A 1 56  ? 156.249 151.953 170.437 1.00 14.40 ? 199 LEU A CD1    1 
ATOM   339  C  CD2    . LEU A 1 56  ? 155.074 152.244 172.613 1.00 17.41 ? 199 LEU A CD2    1 
ATOM   340  N  N      . VAL A 1 57  ? 159.121 154.343 174.899 1.00 15.23 ? 200 VAL A N      1 
ATOM   341  C  CA     . VAL A 1 57  ? 160.445 154.605 175.452 1.00 16.59 ? 200 VAL A CA     1 
ATOM   342  C  C      . VAL A 1 57  ? 161.023 153.307 175.998 1.00 16.70 ? 200 VAL A C      1 
ATOM   343  O  O      . VAL A 1 57  ? 160.325 152.551 176.680 1.00 16.30 ? 200 VAL A O      1 
ATOM   344  C  CB     . VAL A 1 57  ? 160.410 155.693 176.545 1.00 18.02 ? 200 VAL A CB     1 
ATOM   345  C  CG1    . VAL A 1 57  ? 159.697 156.929 176.040 1.00 16.59 ? 200 VAL A CG1    1 
ATOM   346  C  CG2    . VAL A 1 57  ? 159.735 155.176 177.793 1.00 19.89 ? 200 VAL A CG2    1 
ATOM   347  N  N      . GLY A 1 58  ? 162.294 153.049 175.692 1.00 17.78 ? 201 GLY A N      1 
ATOM   348  C  CA     . GLY A 1 58  ? 162.977 151.872 176.171 1.00 16.11 ? 201 GLY A CA     1 
ATOM   349  C  C      . GLY A 1 58  ? 164.402 151.760 175.666 1.00 18.37 ? 201 GLY A C      1 
ATOM   350  O  O      . GLY A 1 58  ? 164.835 152.510 174.791 1.00 21.84 ? 201 GLY A O      1 
ATOM   351  N  N      . PRO A 1 59  ? 165.161 150.817 176.218 1.00 20.48 ? 202 PRO A N      1 
ATOM   352  C  CA     . PRO A 1 59  ? 166.545 150.600 175.764 1.00 16.96 ? 202 PRO A CA     1 
ATOM   353  C  C      . PRO A 1 59  ? 166.584 150.003 174.369 1.00 16.26 ? 202 PRO A C      1 
ATOM   354  O  O      . PRO A 1 59  ? 165.607 149.392 173.916 1.00 18.01 ? 202 PRO A O      1 
ATOM   355  C  CB     . PRO A 1 59  ? 167.109 149.620 176.804 1.00 14.32 ? 202 PRO A CB     1 
ATOM   356  C  CG     . PRO A 1 59  ? 166.172 149.679 177.952 1.00 14.74 ? 202 PRO A CG     1 
ATOM   357  C  CD     . PRO A 1 59  ? 164.834 149.996 177.392 1.00 18.08 ? 202 PRO A CD     1 
ATOM   358  N  N      . PRO A 1 60  ? 167.694 150.169 173.650 1.00 18.27 ? 203 PRO A N      1 
ATOM   359  C  CA     . PRO A 1 60  ? 167.783 149.626 172.288 1.00 19.66 ? 203 PRO A CA     1 
ATOM   360  C  C      . PRO A 1 60  ? 167.713 148.105 172.247 1.00 18.19 ? 203 PRO A C      1 
ATOM   361  O  O      . PRO A 1 60  ? 168.228 147.410 173.125 1.00 20.15 ? 203 PRO A O      1 
ATOM   362  C  CB     . PRO A 1 60  ? 169.140 150.138 171.788 1.00 15.86 ? 203 PRO A CB     1 
ATOM   363  C  CG     . PRO A 1 60  ? 169.895 150.509 173.003 1.00 15.25 ? 203 PRO A CG     1 
ATOM   364  C  CD     . PRO A 1 60  ? 168.895 150.930 174.025 1.00 17.35 ? 203 PRO A CD     1 
ATOM   365  N  N      . GLY A 1 61  ? 167.082 147.595 171.192 1.00 16.36 ? 204 GLY A N      1 
ATOM   366  C  CA     . GLY A 1 61  ? 166.950 146.175 170.955 1.00 14.90 ? 204 GLY A CA     1 
ATOM   367  C  C      . GLY A 1 61  ? 165.772 145.498 171.620 1.00 17.19 ? 204 GLY A C      1 
ATOM   368  O  O      . GLY A 1 61  ? 165.637 144.278 171.490 1.00 18.79 ? 204 GLY A O      1 
ATOM   369  N  N      . THR A 1 62  ? 164.914 146.238 172.322 1.00 16.11 ? 205 THR A N      1 
ATOM   370  C  CA     . THR A 1 62  ? 163.796 145.655 173.054 1.00 15.20 ? 205 THR A CA     1 
ATOM   371  C  C      . THR A 1 62  ? 162.525 145.506 172.224 1.00 16.65 ? 205 THR A C      1 
ATOM   372  O  O      . THR A 1 62  ? 161.576 144.872 172.692 1.00 17.80 ? 205 THR A O      1 
ATOM   373  C  CB     . THR A 1 62  ? 163.489 146.484 174.311 1.00 16.17 ? 205 THR A CB     1 
ATOM   374  O  OG1    . THR A 1 62  ? 163.270 147.852 173.952 1.00 20.13 ? 205 THR A OG1    1 
ATOM   375  C  CG2    . THR A 1 62  ? 164.624 146.396 175.313 1.00 14.79 ? 205 THR A CG2    1 
ATOM   376  N  N      . GLY A 1 63  ? 162.478 146.057 171.017 1.00 16.37 ? 206 GLY A N      1 
ATOM   377  C  CA     . GLY A 1 63  ? 161.354 145.819 170.132 1.00 16.43 ? 206 GLY A CA     1 
ATOM   378  C  C      . GLY A 1 63  ? 160.320 146.923 170.040 1.00 17.71 ? 206 GLY A C      1 
ATOM   379  O  O      . GLY A 1 63  ? 159.123 146.642 169.972 1.00 17.63 ? 206 GLY A O      1 
ATOM   380  N  N      . LYS A 1 64  ? 160.763 148.180 170.030 1.00 17.96 ? 207 LYS A N      1 
ATOM   381  C  CA     . LYS A 1 64  ? 159.838 149.299 169.883 1.00 15.49 ? 207 LYS A CA     1 
ATOM   382  C  C      . LYS A 1 64  ? 159.326 149.427 168.452 1.00 15.75 ? 207 LYS A C      1 
ATOM   383  O  O      . LYS A 1 64  ? 158.148 149.729 168.239 1.00 17.16 ? 207 LYS A O      1 
ATOM   384  C  CB     . LYS A 1 64  ? 160.512 150.595 170.335 1.00 15.68 ? 207 LYS A CB     1 
ATOM   385  C  CG     . LYS A 1 64  ? 160.997 150.553 171.773 1.00 15.58 ? 207 LYS A CG     1 
ATOM   386  C  CD     . LYS A 1 64  ? 161.547 151.883 172.240 1.00 14.28 ? 207 LYS A CD     1 
ATOM   387  C  CE     . LYS A 1 64  ? 162.720 152.327 171.389 1.00 15.85 ? 207 LYS A CE     1 
ATOM   388  N  NZ     . LYS A 1 64  ? 163.967 151.604 171.731 1.00 17.07 ? 207 LYS A NZ     1 
ATOM   389  N  N      . THR A 1 65  ? 160.190 149.206 167.460 1.00 16.25 ? 208 THR A N      1 
ATOM   390  C  CA     . THR A 1 65  ? 159.746 149.255 166.071 1.00 16.81 ? 208 THR A CA     1 
ATOM   391  C  C      . THR A 1 65  ? 158.842 148.080 165.723 1.00 18.40 ? 208 THR A C      1 
ATOM   392  O  O      . THR A 1 65  ? 157.920 148.227 164.917 1.00 20.26 ? 208 THR A O      1 
ATOM   393  C  CB     . THR A 1 65  ? 160.950 149.285 165.133 1.00 19.84 ? 208 THR A CB     1 
ATOM   394  O  OG1    . THR A 1 65  ? 161.761 150.422 165.435 1.00 27.40 ? 208 THR A OG1    1 
ATOM   395  C  CG2    . THR A 1 65  ? 160.497 149.379 163.695 1.00 16.54 ? 208 THR A CG2    1 
ATOM   396  N  N      . LEU A 1 66  ? 159.101 146.910 166.308 1.00 17.79 ? 209 LEU A N      1 
ATOM   397  C  CA     . LEU A 1 66  ? 158.278 145.735 166.053 1.00 15.80 ? 209 LEU A CA     1 
ATOM   398  C  C      . LEU A 1 66  ? 156.877 145.879 166.637 1.00 17.09 ? 209 LEU A C      1 
ATOM   399  O  O      . LEU A 1 66  ? 155.907 145.424 166.026 1.00 19.49 ? 209 LEU A O      1 
ATOM   400  C  CB     . LEU A 1 66  ? 158.982 144.496 166.611 1.00 17.92 ? 209 LEU A CB     1 
ATOM   401  C  CG     . LEU A 1 66  ? 158.267 143.146 166.658 1.00 18.27 ? 209 LEU A CG     1 
ATOM   402  C  CD1    . LEU A 1 66  ? 158.313 142.456 165.313 1.00 17.06 ? 209 LEU A CD1    1 
ATOM   403  C  CD2    . LEU A 1 66  ? 158.881 142.272 167.728 1.00 16.67 ? 209 LEU A CD2    1 
ATOM   404  N  N      . LEU A 1 67  ? 156.750 146.500 167.810 1.00 17.23 ? 210 LEU A N      1 
ATOM   405  C  CA     . LEU A 1 67  ? 155.436 146.679 168.421 1.00 16.93 ? 210 LEU A CA     1 
ATOM   406  C  C      . LEU A 1 67  ? 154.540 147.565 167.567 1.00 19.42 ? 210 LEU A C      1 
ATOM   407  O  O      . LEU A 1 67  ? 153.340 147.308 167.442 1.00 21.49 ? 210 LEU A O      1 
ATOM   408  C  CB     . LEU A 1 67  ? 155.585 147.269 169.821 1.00 17.99 ? 210 LEU A CB     1 
ATOM   409  C  CG     . LEU A 1 67  ? 155.646 146.281 170.982 1.00 20.81 ? 210 LEU A CG     1 
ATOM   410  C  CD1    . LEU A 1 67  ? 155.905 147.018 172.277 1.00 19.46 ? 210 LEU A CD1    1 
ATOM   411  C  CD2    . LEU A 1 67  ? 154.382 145.455 171.075 1.00 22.99 ? 210 LEU A CD2    1 
ATOM   412  N  N      . ALA A 1 68  ? 155.102 148.627 166.991 1.00 18.88 ? 211 ALA A N      1 
ATOM   413  C  CA     . ALA A 1 68  ? 154.318 149.515 166.143 1.00 19.26 ? 211 ALA A CA     1 
ATOM   414  C  C      . ALA A 1 68  ? 153.808 148.796 164.900 1.00 22.76 ? 211 ALA A C      1 
ATOM   415  O  O      . ALA A 1 68  ? 152.664 149.001 164.484 1.00 24.19 ? 211 ALA A O      1 
ATOM   416  C  CB     . ALA A 1 68  ? 155.150 150.736 165.757 1.00 16.96 ? 211 ALA A CB     1 
ATOM   417  N  N      . ARG A 1 69  ? 154.647 147.959 164.287 1.00 21.45 ? 212 ARG A N      1 
ATOM   418  C  CA     . ARG A 1 69  ? 154.233 147.226 163.095 1.00 21.51 ? 212 ARG A CA     1 
ATOM   419  C  C      . ARG A 1 69  ? 153.177 146.176 163.409 1.00 23.57 ? 212 ARG A C      1 
ATOM   420  O  O      . ARG A 1 69  ? 152.356 145.852 162.546 1.00 27.21 ? 212 ARG A O      1 
ATOM   421  C  CB     . ARG A 1 69  ? 155.446 146.576 162.434 1.00 21.95 ? 212 ARG A CB     1 
ATOM   422  C  CG     . ARG A 1 69  ? 156.433 147.562 161.852 1.00 24.37 ? 212 ARG A CG     1 
ATOM   423  C  CD     . ARG A 1 69  ? 157.362 146.896 160.858 1.00 28.42 ? 212 ARG A CD     1 
ATOM   424  N  NE     . ARG A 1 69  ? 158.244 145.926 161.494 1.00 36.13 ? 212 ARG A NE     1 
ATOM   425  C  CZ     . ARG A 1 69  ? 158.664 144.805 160.924 1.00 39.88 ? 212 ARG A CZ     1 
ATOM   426  N  NH1    . ARG A 1 69  ? 158.272 144.457 159.710 1.00 36.55 ? 212 ARG A NH1    1 
ATOM   427  N  NH2    . ARG A 1 69  ? 159.489 144.007 161.593 1.00 34.40 ? 212 ARG A NH2    1 
ATOM   428  N  N      . ALA A 1 70  ? 153.185 145.626 164.622 1.00 21.26 ? 213 ALA A N      1 
ATOM   429  C  CA     . ALA A 1 70  ? 152.176 144.644 164.998 1.00 22.94 ? 213 ALA A CA     1 
ATOM   430  C  C      . ALA A 1 70  ? 150.807 145.283 165.196 1.00 27.68 ? 213 ALA A C      1 
ATOM   431  O  O      . ALA A 1 70  ? 149.785 144.611 165.032 1.00 30.84 ? 213 ALA A O      1 
ATOM   432  C  CB     . ALA A 1 70  ? 152.608 143.908 166.264 1.00 23.72 ? 213 ALA A CB     1 
ATOM   433  N  N      . VAL A 1 71  ? 150.765 146.563 165.572 1.00 27.70 ? 214 VAL A N      1 
ATOM   434  C  CA     . VAL A 1 71  ? 149.491 147.264 165.711 1.00 26.15 ? 214 VAL A CA     1 
ATOM   435  C  C      . VAL A 1 71  ? 148.812 147.411 164.354 1.00 26.84 ? 214 VAL A C      1 
ATOM   436  O  O      . VAL A 1 71  ? 147.597 147.229 164.229 1.00 29.61 ? 214 VAL A O      1 
ATOM   437  C  CB     . VAL A 1 71  ? 149.702 148.629 166.392 1.00 28.08 ? 214 VAL A CB     1 
ATOM   438  C  CG1    . VAL A 1 71  ? 148.480 149.508 166.220 1.00 26.28 ? 214 VAL A CG1    1 
ATOM   439  C  CG2    . VAL A 1 71  ? 150.018 148.452 167.865 1.00 24.00 ? 214 VAL A CG2    1 
ATOM   440  N  N      . ALA A 1 72  ? 149.582 147.750 163.321 1.00 27.16 ? 215 ALA A N      1 
ATOM   441  C  CA     . ALA A 1 72  ? 149.047 147.883 161.973 1.00 28.45 ? 215 ALA A CA     1 
ATOM   442  C  C      . ALA A 1 72  ? 148.701 146.547 161.332 1.00 33.63 ? 215 ALA A C      1 
ATOM   443  O  O      . ALA A 1 72  ? 148.081 146.538 160.267 1.00 40.48 ? 215 ALA A O      1 
ATOM   444  C  CB     . ALA A 1 72  ? 150.041 148.629 161.085 1.00 25.40 ? 215 ALA A CB     1 
ATOM   445  N  N      . GLY A 1 73  ? 149.096 145.430 161.935 1.00 34.01 ? 216 GLY A N      1 
ATOM   446  C  CA     . GLY A 1 73  ? 148.749 144.124 161.416 1.00 31.15 ? 216 GLY A CA     1 
ATOM   447  C  C      . GLY A 1 73  ? 147.484 143.581 162.041 1.00 34.62 ? 216 GLY A C      1 
ATOM   448  O  O      . GLY A 1 73  ? 146.668 142.954 161.363 1.00 41.47 ? 216 GLY A O      1 
ATOM   449  N  N      . GLU A 1 74  ? 147.312 143.815 163.343 1.00 31.82 ? 217 GLU A N      1 
ATOM   450  C  CA     . GLU A 1 74  ? 146.089 143.396 164.018 1.00 32.03 ? 217 GLU A CA     1 
ATOM   451  C  C      . GLU A 1 74  ? 144.870 144.117 163.460 1.00 35.21 ? 217 GLU A C      1 
ATOM   452  O  O      . GLU A 1 74  ? 143.766 143.564 163.459 1.00 37.26 ? 217 GLU A O      1 
ATOM   453  C  CB     . GLU A 1 74  ? 146.211 143.640 165.519 1.00 32.03 ? 217 GLU A CB     1 
ATOM   454  C  CG     . GLU A 1 74  ? 147.200 142.727 166.203 1.00 34.35 ? 217 GLU A CG     1 
ATOM   455  C  CD     . GLU A 1 74  ? 146.540 141.508 166.798 1.00 40.70 ? 217 GLU A CD     1 
ATOM   456  O  OE1    . GLU A 1 74  ? 145.428 141.645 167.344 1.00 43.27 ? 217 GLU A OE1    1 
ATOM   457  O  OE2    . GLU A 1 74  ? 147.126 140.410 166.718 1.00 41.32 ? 217 GLU A OE2    1 
ATOM   458  N  N      . ALA A 1 75  ? 145.044 145.355 163.014 1.00 36.79 ? 218 ALA A N      1 
ATOM   459  C  CA     . ALA A 1 75  ? 144.037 146.087 162.262 1.00 35.12 ? 218 ALA A CA     1 
ATOM   460  C  C      . ALA A 1 75  ? 144.584 146.356 160.869 1.00 39.07 ? 218 ALA A C      1 
ATOM   461  O  O      . ALA A 1 75  ? 145.665 146.932 160.726 1.00 43.82 ? 218 ALA A O      1 
ATOM   462  C  CB     . ALA A 1 75  ? 143.677 147.398 162.960 1.00 28.38 ? 218 ALA A CB     1 
ATOM   463  N  N      . ASN A 1 76  ? 143.844 145.944 159.844 1.00 36.10 ? 219 ASN A N      1 
ATOM   464  C  CA     . ASN A 1 76  ? 144.320 146.057 158.467 1.00 37.63 ? 219 ASN A CA     1 
ATOM   465  C  C      . ASN A 1 76  ? 144.211 147.509 158.018 1.00 38.82 ? 219 ASN A C      1 
ATOM   466  O  O      . ASN A 1 76  ? 143.246 147.927 157.376 1.00 46.14 ? 219 ASN A O      1 
ATOM   467  C  CB     . ASN A 1 76  ? 143.533 145.134 157.549 1.00 42.80 ? 219 ASN A CB     1 
ATOM   468  C  CG     . ASN A 1 76  ? 143.534 143.708 158.025 1.00 48.42 ? 219 ASN A CG     1 
ATOM   469  O  OD1    . ASN A 1 76  ? 143.087 143.412 159.132 1.00 48.29 ? 219 ASN A OD1    1 
ATOM   470  N  ND2    . ASN A 1 76  ? 144.034 142.809 157.192 1.00 54.45 ? 219 ASN A ND2    1 
ATOM   471  N  N      . VAL A 1 77  ? 145.233 148.291 158.349 1.00 33.60 ? 220 VAL A N      1 
ATOM   472  C  CA     . VAL A 1 77  ? 145.267 149.698 157.955 1.00 31.45 ? 220 VAL A CA     1 
ATOM   473  C  C      . VAL A 1 77  ? 146.637 150.009 157.370 1.00 30.56 ? 220 VAL A C      1 
ATOM   474  O  O      . VAL A 1 77  ? 147.627 149.320 157.657 1.00 30.52 ? 220 VAL A O      1 
ATOM   475  C  CB     . VAL A 1 77  ? 144.938 150.635 159.141 1.00 30.98 ? 220 VAL A CB     1 
ATOM   476  C  CG1    . VAL A 1 77  ? 143.511 150.413 159.619 1.00 26.94 ? 220 VAL A CG1    1 
ATOM   477  C  CG2    . VAL A 1 77  ? 145.922 150.440 160.278 1.00 29.35 ? 220 VAL A CG2    1 
ATOM   478  N  N      . PRO A 1 78  ? 146.723 151.036 156.529 1.00 29.58 ? 221 PRO A N      1 
ATOM   479  C  CA     . PRO A 1 78  ? 148.017 151.433 155.965 1.00 27.57 ? 221 PRO A CA     1 
ATOM   480  C  C      . PRO A 1 78  ? 148.974 151.956 157.027 1.00 27.41 ? 221 PRO A C      1 
ATOM   481  O  O      . PRO A 1 78  ? 148.581 152.404 158.104 1.00 29.36 ? 221 PRO A O      1 
ATOM   482  C  CB     . PRO A 1 78  ? 147.648 152.534 154.967 1.00 26.08 ? 221 PRO A CB     1 
ATOM   483  C  CG     . PRO A 1 78  ? 146.214 152.320 154.675 1.00 25.88 ? 221 PRO A CG     1 
ATOM   484  C  CD     . PRO A 1 78  ? 145.607 151.773 155.918 1.00 27.09 ? 221 PRO A CD     1 
ATOM   485  N  N      . PHE A 1 79  ? 150.262 151.895 156.693 1.00 25.39 ? 222 PHE A N      1 
ATOM   486  C  CA     . PHE A 1 79  ? 151.343 152.180 157.636 1.00 23.29 ? 222 PHE A CA     1 
ATOM   487  C  C      . PHE A 1 79  ? 152.360 153.086 156.944 1.00 24.73 ? 222 PHE A C      1 
ATOM   488  O  O      . PHE A 1 79  ? 153.138 152.627 156.106 1.00 30.70 ? 222 PHE A O      1 
ATOM   489  C  CB     . PHE A 1 79  ? 151.974 150.875 158.110 1.00 22.88 ? 222 PHE A CB     1 
ATOM   490  C  CG     . PHE A 1 79  ? 152.990 151.037 159.199 1.00 26.65 ? 222 PHE A CG     1 
ATOM   491  C  CD1    . PHE A 1 79  ? 152.597 151.163 160.519 1.00 26.67 ? 222 PHE A CD1    1 
ATOM   492  C  CD2    . PHE A 1 79  ? 154.341 151.022 158.910 1.00 26.83 ? 222 PHE A CD2    1 
ATOM   493  C  CE1    . PHE A 1 79  ? 153.531 151.299 161.524 1.00 23.35 ? 222 PHE A CE1    1 
ATOM   494  C  CE2    . PHE A 1 79  ? 155.278 151.156 159.912 1.00 24.92 ? 222 PHE A CE2    1 
ATOM   495  C  CZ     . PHE A 1 79  ? 154.872 151.294 161.220 1.00 21.51 ? 222 PHE A CZ     1 
ATOM   496  N  N      . PHE A 1 80  ? 152.352 154.368 157.293 1.00 23.55 ? 223 PHE A N      1 
ATOM   497  C  CA     . PHE A 1 80  ? 153.287 155.342 156.743 1.00 24.24 ? 223 PHE A CA     1 
ATOM   498  C  C      . PHE A 1 80  ? 154.339 155.670 157.792 1.00 25.06 ? 223 PHE A C      1 
ATOM   499  O  O      . PHE A 1 80  ? 153.997 156.003 158.929 1.00 27.19 ? 223 PHE A O      1 
ATOM   500  C  CB     . PHE A 1 80  ? 152.560 156.615 156.304 1.00 22.81 ? 223 PHE A CB     1 
ATOM   501  C  CG     . PHE A 1 80  ? 151.396 156.366 155.390 1.00 24.73 ? 223 PHE A CG     1 
ATOM   502  C  CD1    . PHE A 1 80  ? 151.581 156.267 154.025 1.00 24.86 ? 223 PHE A CD1    1 
ATOM   503  C  CD2    . PHE A 1 80  ? 150.117 156.231 155.895 1.00 26.25 ? 223 PHE A CD2    1 
ATOM   504  C  CE1    . PHE A 1 80  ? 150.518 156.034 153.185 1.00 24.32 ? 223 PHE A CE1    1 
ATOM   505  C  CE2    . PHE A 1 80  ? 149.052 155.999 155.058 1.00 27.62 ? 223 PHE A CE2    1 
ATOM   506  C  CZ     . PHE A 1 80  ? 149.254 155.901 153.701 1.00 26.84 ? 223 PHE A CZ     1 
ATOM   507  N  N      . HIS A 1 81  ? 155.612 155.578 157.415 1.00 25.22 ? 224 HIS A N      1 
ATOM   508  C  CA     . HIS A 1 81  ? 156.691 155.703 158.382 1.00 24.35 ? 224 HIS A CA     1 
ATOM   509  C  C      . HIS A 1 81  ? 157.840 156.516 157.804 1.00 24.91 ? 224 HIS A C      1 
ATOM   510  O  O      . HIS A 1 81  ? 158.017 156.614 156.589 1.00 25.46 ? 224 HIS A O      1 
ATOM   511  C  CB     . HIS A 1 81  ? 157.198 154.328 158.839 1.00 23.88 ? 224 HIS A CB     1 
ATOM   512  C  CG     . HIS A 1 81  ? 157.813 153.513 157.745 1.00 30.73 ? 224 HIS A CG     1 
ATOM   513  N  ND1    . HIS A 1 81  ? 157.064 152.768 156.861 1.00 33.46 ? 224 HIS A ND1    1 
ATOM   514  C  CD2    . HIS A 1 81  ? 159.107 153.320 157.398 1.00 31.18 ? 224 HIS A CD2    1 
ATOM   515  C  CE1    . HIS A 1 81  ? 157.869 152.157 156.012 1.00 33.91 ? 224 HIS A CE1    1 
ATOM   516  N  NE2    . HIS A 1 81  ? 159.114 152.476 156.316 1.00 35.84 ? 224 HIS A NE2    1 
ATOM   517  N  N      . ILE A 1 82  ? 158.617 157.107 158.710 1.00 26.78 ? 225 ILE A N      1 
ATOM   518  C  CA     . ILE A 1 82  ? 159.806 157.872 158.358 1.00 28.00 ? 225 ILE A CA     1 
ATOM   519  C  C      . ILE A 1 82  ? 160.801 157.707 159.495 1.00 29.66 ? 225 ILE A C      1 
ATOM   520  O  O      . ILE A 1 82  ? 160.419 157.443 160.636 1.00 30.94 ? 225 ILE A O      1 
ATOM   521  C  CB     . ILE A 1 82  ? 159.461 159.362 158.102 1.00 28.72 ? 225 ILE A CB     1 
ATOM   522  C  CG1    . ILE A 1 82  ? 160.668 160.106 157.547 1.00 34.27 ? 225 ILE A CG1    1 
ATOM   523  C  CG2    . ILE A 1 82  ? 159.004 160.038 159.379 1.00 26.15 ? 225 ILE A CG2    1 
ATOM   524  C  CD1    . ILE A 1 82  ? 160.298 161.303 156.713 1.00 39.91 ? 225 ILE A CD1    1 
ATOM   525  N  N      . SER A 1 83  ? 162.083 157.854 159.182 1.00 33.03 ? 226 SER A N      1 
ATOM   526  C  CA     . SER A 1 83  ? 163.157 157.667 160.149 1.00 36.97 ? 226 SER A CA     1 
ATOM   527  C  C      . SER A 1 83  ? 163.835 158.997 160.439 1.00 40.03 ? 226 SER A C      1 
ATOM   528  O  O      . SER A 1 83  ? 164.195 159.730 159.513 1.00 43.70 ? 226 SER A O      1 
ATOM   529  C  CB     . SER A 1 83  ? 164.183 156.656 159.640 1.00 41.82 ? 226 SER A CB     1 
ATOM   530  O  OG     . SER A 1 83  ? 165.066 156.276 160.675 1.00 44.51 ? 226 SER A OG     1 
ATOM   531  N  N      . GLY A 1 84  ? 164.019 159.300 161.722 1.00 40.05 ? 227 GLY A N      1 
ATOM   532  C  CA     . GLY A 1 84  ? 164.584 160.574 162.122 1.00 41.57 ? 227 GLY A CA     1 
ATOM   533  C  C      . GLY A 1 84  ? 166.082 160.689 161.942 1.00 45.01 ? 227 GLY A C      1 
ATOM   534  O  O      . GLY A 1 84  ? 166.612 161.799 162.041 1.00 46.98 ? 227 GLY A O      1 
ATOM   535  N  N      . SER A 1 85  ? 166.771 159.584 161.681 1.00 46.45 ? 228 SER A N      1 
ATOM   536  C  CA     . SER A 1 85  ? 168.211 159.604 161.479 1.00 47.45 ? 228 SER A CA     1 
ATOM   537  C  C      . SER A 1 85  ? 168.606 159.941 160.047 1.00 52.46 ? 228 SER A C      1 
ATOM   538  O  O      . SER A 1 85  ? 169.796 160.121 159.775 1.00 55.09 ? 228 SER A O      1 
ATOM   539  C  CB     . SER A 1 85  ? 168.816 158.256 161.878 1.00 49.28 ? 228 SER A CB     1 
ATOM   540  O  OG     . SER A 1 85  ? 168.512 157.259 160.922 1.00 49.44 ? 228 SER A OG     1 
ATOM   541  N  N      . ASP A 1 86  ? 167.644 160.035 159.132 1.00 53.11 ? 229 ASP A N      1 
ATOM   542  C  CA     . ASP A 1 86  ? 167.905 160.397 157.746 1.00 51.53 ? 229 ASP A CA     1 
ATOM   543  C  C      . ASP A 1 86  ? 167.925 161.901 157.519 1.00 50.20 ? 229 ASP A C      1 
ATOM   544  O  O      . ASP A 1 86  ? 168.293 162.342 156.428 1.00 52.91 ? 229 ASP A O      1 
ATOM   545  C  CB     . ASP A 1 86  ? 166.853 159.765 156.834 1.00 52.16 ? 229 ASP A CB     1 
ATOM   546  C  CG     . ASP A 1 86  ? 166.964 158.262 156.778 1.00 61.10 ? 229 ASP A CG     1 
ATOM   547  O  OD1    . ASP A 1 86  ? 167.899 157.713 157.394 1.00 61.30 ? 229 ASP A OD1    1 
ATOM   548  O  OD2    . ASP A 1 86  ? 166.109 157.625 156.128 1.00 63.88 ? 229 ASP A OD2    1 
ATOM   549  N  N      . PHE A 1 87  ? 167.539 162.693 158.510 1.00 48.65 ? 230 PHE A N      1 
ATOM   550  C  CA     . PHE A 1 87  ? 167.501 164.140 158.372 1.00 49.23 ? 230 PHE A CA     1 
ATOM   551  C  C      . PHE A 1 87  ? 168.879 164.760 158.551 1.00 53.78 ? 230 PHE A C      1 
ATOM   552  O  O      . PHE A 1 87  ? 169.870 164.055 158.726 1.00 58.67 ? 230 PHE A O      1 
ATOM   553  C  CB     . PHE A 1 87  ? 166.521 164.740 159.378 1.00 47.83 ? 230 PHE A CB     1 
ATOM   554  C  CG     . PHE A 1 87  ? 165.082 164.573 158.993 1.00 48.93 ? 230 PHE A CG     1 
ATOM   555  C  CD1    . PHE A 1 87  ? 164.428 163.376 159.202 1.00 49.00 ? 230 PHE A CD1    1 
ATOM   556  C  CD2    . PHE A 1 87  ? 164.381 165.622 158.430 1.00 46.55 ? 230 PHE A CD2    1 
ATOM   557  C  CE1    . PHE A 1 87  ? 163.106 163.226 158.847 1.00 47.82 ? 230 PHE A CE1    1 
ATOM   558  C  CE2    . PHE A 1 87  ? 163.060 165.476 158.075 1.00 44.12 ? 230 PHE A CE2    1 
ATOM   559  C  CZ     . PHE A 1 87  ? 162.421 164.278 158.284 1.00 46.23 ? 230 PHE A CZ     1 
ATOM   560  N  N      . VAL A 1 94  ? 164.175 171.069 152.564 1.00 41.31 ? 237 VAL A N      1 
ATOM   561  C  CA     . VAL A 1 94  ? 163.830 169.722 152.134 1.00 44.54 ? 237 VAL A CA     1 
ATOM   562  C  C      . VAL A 1 94  ? 163.246 168.928 153.293 1.00 46.42 ? 237 VAL A C      1 
ATOM   563  O  O      . VAL A 1 94  ? 162.420 168.043 153.092 1.00 46.57 ? 237 VAL A O      1 
ATOM   564  C  CB     . VAL A 1 94  ? 165.048 169.001 151.541 1.00 46.85 ? 237 VAL A CB     1 
ATOM   565  C  CG1    . VAL A 1 94  ? 164.659 167.625 151.030 1.00 42.90 ? 237 VAL A CG1    1 
ATOM   566  C  CG2    . VAL A 1 94  ? 165.656 169.832 150.432 1.00 45.73 ? 237 VAL A CG2    1 
ATOM   567  N  N      . GLY A 1 95  ? 163.688 169.242 154.511 1.00 44.91 ? 238 GLY A N      1 
ATOM   568  C  CA     . GLY A 1 95  ? 163.144 168.564 155.676 1.00 38.36 ? 238 GLY A CA     1 
ATOM   569  C  C      . GLY A 1 95  ? 161.680 168.882 155.907 1.00 37.85 ? 238 GLY A C      1 
ATOM   570  O  O      . GLY A 1 95  ? 160.879 167.989 156.188 1.00 37.75 ? 238 GLY A O      1 
ATOM   571  N  N      . ALA A 1 96  ? 161.311 170.158 155.792 1.00 36.98 ? 239 ALA A N      1 
ATOM   572  C  CA     . ALA A 1 96  ? 159.922 170.553 156.000 1.00 34.36 ? 239 ALA A CA     1 
ATOM   573  C  C      . ALA A 1 96  ? 159.010 169.975 154.926 1.00 36.88 ? 239 ALA A C      1 
ATOM   574  O  O      . ALA A 1 96  ? 157.853 169.641 155.199 1.00 36.81 ? 239 ALA A O      1 
ATOM   575  C  CB     . ALA A 1 96  ? 159.815 172.075 156.040 1.00 35.67 ? 239 ALA A CB     1 
ATOM   576  N  N      . ALA A 1 97  ? 159.507 169.865 153.692 1.00 38.44 ? 240 ALA A N      1 
ATOM   577  C  CA     . ALA A 1 97  ? 158.694 169.327 152.606 1.00 37.28 ? 240 ALA A CA     1 
ATOM   578  C  C      . ALA A 1 97  ? 158.391 167.847 152.810 1.00 37.83 ? 240 ALA A C      1 
ATOM   579  O  O      . ALA A 1 97  ? 157.304 167.377 152.460 1.00 36.94 ? 240 ALA A O      1 
ATOM   580  C  CB     . ALA A 1 97  ? 159.394 169.556 151.268 1.00 37.09 ? 240 ALA A CB     1 
ATOM   581  N  N      . ARG A 1 98  ? 159.344 167.095 153.360 1.00 34.54 ? 241 ARG A N      1 
ATOM   582  C  CA     . ARG A 1 98  ? 159.128 165.671 153.596 1.00 36.90 ? 241 ARG A CA     1 
ATOM   583  C  C      . ARG A 1 98  ? 158.045 165.433 154.643 1.00 36.24 ? 241 ARG A C      1 
ATOM   584  O  O      . ARG A 1 98  ? 157.253 164.493 154.520 1.00 34.40 ? 241 ARG A O      1 
ATOM   585  C  CB     . ARG A 1 98  ? 160.440 165.014 154.021 1.00 42.09 ? 241 ARG A CB     1 
ATOM   586  C  CG     . ARG A 1 98  ? 161.419 164.814 152.885 1.00 44.72 ? 241 ARG A CG     1 
ATOM   587  C  CD     . ARG A 1 98  ? 162.226 163.545 153.057 1.00 59.22 ? 241 ARG A CD     1 
ATOM   588  N  NE     . ARG A 1 98  ? 163.475 163.606 152.308 1.00 73.83 ? 241 ARG A NE     1 
ATOM   589  C  CZ     . ARG A 1 98  ? 164.663 163.277 152.797 1.00 73.59 ? 241 ARG A CZ     1 
ATOM   590  N  NH1    . ARG A 1 98  ? 164.802 162.839 154.038 1.00 66.95 ? 241 ARG A NH1    1 
ATOM   591  N  NH2    . ARG A 1 98  ? 165.738 163.395 152.024 1.00 71.55 ? 241 ARG A NH2    1 
ATOM   592  N  N      . VAL A 1 99  ? 158.009 166.258 155.691 1.00 34.69 ? 242 VAL A N      1 
ATOM   593  C  CA     . VAL A 1 99  ? 156.982 166.118 156.721 1.00 31.64 ? 242 VAL A CA     1 
ATOM   594  C  C      . VAL A 1 99  ? 155.602 166.412 156.147 1.00 31.03 ? 242 VAL A C      1 
ATOM   595  O  O      . VAL A 1 99  ? 154.621 165.739 156.481 1.00 30.14 ? 242 VAL A O      1 
ATOM   596  C  CB     . VAL A 1 99  ? 157.308 167.024 157.926 1.00 34.95 ? 242 VAL A CB     1 
ATOM   597  C  CG1    . VAL A 1 99  ? 156.262 166.873 159.013 1.00 30.01 ? 242 VAL A CG1    1 
ATOM   598  C  CG2    . VAL A 1 99  ? 158.685 166.700 158.474 1.00 33.00 ? 242 VAL A CG2    1 
ATOM   599  N  N      . ARG A 1 100 ? 155.501 167.425 155.282 1.00 31.63 ? 243 ARG A N      1 
ATOM   600  C  CA     . ARG A 1 100 ? 154.218 167.750 154.665 1.00 31.49 ? 243 ARG A CA     1 
ATOM   601  C  C      . ARG A 1 100 ? 153.687 166.588 153.836 1.00 31.89 ? 243 ARG A C      1 
ATOM   602  O  O      . ARG A 1 100 ? 152.494 166.275 153.889 1.00 30.86 ? 243 ARG A O      1 
ATOM   603  C  CB     . ARG A 1 100 ? 154.347 168.996 153.790 1.00 34.42 ? 243 ARG A CB     1 
ATOM   604  C  CG     . ARG A 1 100 ? 153.918 170.288 154.448 1.00 38.54 ? 243 ARG A CG     1 
ATOM   605  C  CD     . ARG A 1 100 ? 153.793 171.425 153.435 1.00 42.68 ? 243 ARG A CD     1 
ATOM   606  N  NE     . ARG A 1 100 ? 154.992 172.253 153.374 1.00 47.04 ? 243 ARG A NE     1 
ATOM   607  C  CZ     . ARG A 1 100 ? 155.733 172.423 152.287 1.00 47.60 ? 243 ARG A CZ     1 
ATOM   608  N  NH1    . ARG A 1 100 ? 155.407 171.863 151.134 1.00 47.81 ? 243 ARG A NH1    1 
ATOM   609  N  NH2    . ARG A 1 100 ? 156.827 173.174 152.360 1.00 42.70 ? 243 ARG A NH2    1 
ATOM   610  N  N      . ASP A 1 101 ? 154.555 165.944 153.056 1.00 29.18 ? 244 ASP A N      1 
ATOM   611  C  CA     . ASP A 1 101 ? 154.109 164.863 152.185 1.00 29.00 ? 244 ASP A CA     1 
ATOM   612  C  C      . ASP A 1 101 ? 153.556 163.693 152.987 1.00 30.75 ? 244 ASP A C      1 
ATOM   613  O  O      . ASP A 1 101 ? 152.555 163.082 152.599 1.00 31.70 ? 244 ASP A O      1 
ATOM   614  C  CB     . ASP A 1 101 ? 155.260 164.393 151.300 1.00 34.80 ? 244 ASP A CB     1 
ATOM   615  C  CG     . ASP A 1 101 ? 155.562 165.352 150.172 1.00 43.68 ? 244 ASP A CG     1 
ATOM   616  O  OD1    . ASP A 1 101 ? 154.621 165.990 149.657 1.00 44.05 ? 244 ASP A OD1    1 
ATOM   617  O  OD2    . ASP A 1 101 ? 156.747 165.460 149.794 1.00 46.98 ? 244 ASP A OD2    1 
ATOM   618  N  N      . LEU A 1 102 ? 154.209 163.357 154.100 1.00 30.45 ? 245 LEU A N      1 
ATOM   619  C  CA     . LEU A 1 102 ? 153.833 162.175 154.869 1.00 26.03 ? 245 LEU A CA     1 
ATOM   620  C  C      . LEU A 1 102 ? 152.428 162.299 155.448 1.00 26.75 ? 245 LEU A C      1 
ATOM   621  O  O      . LEU A 1 102 ? 151.657 161.334 155.435 1.00 27.61 ? 245 LEU A O      1 
ATOM   622  C  CB     . LEU A 1 102 ? 154.855 161.941 155.979 1.00 27.11 ? 245 LEU A CB     1 
ATOM   623  C  CG     . LEU A 1 102 ? 154.727 160.667 156.811 1.00 27.53 ? 245 LEU A CG     1 
ATOM   624  C  CD1    . LEU A 1 102 ? 155.223 159.472 156.030 1.00 26.59 ? 245 LEU A CD1    1 
ATOM   625  C  CD2    . LEU A 1 102 ? 155.498 160.818 158.102 1.00 25.89 ? 245 LEU A CD2    1 
ATOM   626  N  N      . PHE A 1 103 ? 152.082 163.474 155.972 1.00 25.28 ? 246 PHE A N      1 
ATOM   627  C  CA     . PHE A 1 103 ? 150.781 163.654 156.606 1.00 25.25 ? 246 PHE A CA     1 
ATOM   628  C  C      . PHE A 1 103 ? 149.652 163.739 155.588 1.00 27.55 ? 246 PHE A C      1 
ATOM   629  O  O      . PHE A 1 103 ? 148.520 163.352 155.896 1.00 27.82 ? 246 PHE A O      1 
ATOM   630  C  CB     . PHE A 1 103 ? 150.798 164.901 157.488 1.00 24.67 ? 246 PHE A CB     1 
ATOM   631  C  CG     . PHE A 1 103 ? 151.212 164.634 158.906 1.00 24.95 ? 246 PHE A CG     1 
ATOM   632  C  CD1    . PHE A 1 103 ? 152.550 164.584 159.252 1.00 26.76 ? 246 PHE A CD1    1 
ATOM   633  C  CD2    . PHE A 1 103 ? 150.267 164.436 159.895 1.00 22.48 ? 246 PHE A CD2    1 
ATOM   634  C  CE1    . PHE A 1 103 ? 152.935 164.339 160.551 1.00 24.01 ? 246 PHE A CE1    1 
ATOM   635  C  CE2    . PHE A 1 103 ? 150.649 164.191 161.195 1.00 22.32 ? 246 PHE A CE2    1 
ATOM   636  C  CZ     . PHE A 1 103 ? 151.983 164.144 161.524 1.00 22.43 ? 246 PHE A CZ     1 
ATOM   637  N  N      . ALA A 1 104 ? 149.935 164.239 154.384 1.00 27.64 ? 247 ALA A N      1 
ATOM   638  C  CA     . ALA A 1 104 ? 148.923 164.282 153.334 1.00 25.03 ? 247 ALA A CA     1 
ATOM   639  C  C      . ALA A 1 104 ? 148.523 162.882 152.882 1.00 28.47 ? 247 ALA A C      1 
ATOM   640  O  O      . ALA A 1 104 ? 147.355 162.638 152.567 1.00 29.99 ? 247 ALA A O      1 
ATOM   641  C  CB     . ALA A 1 104 ? 149.433 165.103 152.153 1.00 23.28 ? 247 ALA A CB     1 
ATOM   642  N  N      . GLN A 1 105 ? 149.480 161.955 152.826 1.00 27.53 ? 248 GLN A N      1 
ATOM   643  C  CA     . GLN A 1 105 ? 149.154 160.580 152.458 1.00 27.75 ? 248 GLN A CA     1 
ATOM   644  C  C      . GLN A 1 105 ? 148.209 159.944 153.468 1.00 30.11 ? 248 GLN A C      1 
ATOM   645  O  O      . GLN A 1 105 ? 147.277 159.228 153.090 1.00 31.76 ? 248 GLN A O      1 
ATOM   646  C  CB     . GLN A 1 105 ? 150.429 159.750 152.337 1.00 29.07 ? 248 GLN A CB     1 
ATOM   647  C  CG     . GLN A 1 105 ? 151.367 160.192 151.235 1.00 35.31 ? 248 GLN A CG     1 
ATOM   648  C  CD     . GLN A 1 105 ? 151.073 159.516 149.915 1.00 44.44 ? 248 GLN A CD     1 
ATOM   649  O  OE1    . GLN A 1 105 ? 150.892 158.302 149.853 1.00 42.00 ? 248 GLN A OE1    1 
ATOM   650  N  NE2    . GLN A 1 105 ? 151.027 160.302 148.847 1.00 46.14 ? 248 GLN A NE2    1 
ATOM   651  N  N      . ALA A 1 106 ? 148.444 160.178 154.760 1.00 28.80 ? 249 ALA A N      1 
ATOM   652  C  CA     . ALA A 1 106 ? 147.607 159.580 155.793 1.00 29.12 ? 249 ALA A CA     1 
ATOM   653  C  C      . ALA A 1 106 ? 146.186 160.129 155.772 1.00 29.84 ? 249 ALA A C      1 
ATOM   654  O  O      . ALA A 1 106 ? 145.234 159.379 156.002 1.00 31.09 ? 249 ALA A O      1 
ATOM   655  C  CB     . ALA A 1 106 ? 148.242 159.791 157.165 1.00 25.81 ? 249 ALA A CB     1 
ATOM   656  N  N      . LYS A 1 107 ? 146.019 161.425 155.507 1.00 29.93 ? 250 LYS A N      1 
ATOM   657  C  CA     . LYS A 1 107 ? 144.678 161.999 155.451 1.00 28.91 ? 250 LYS A CA     1 
ATOM   658  C  C      . LYS A 1 107 ? 143.862 161.405 154.311 1.00 32.57 ? 250 LYS A C      1 
ATOM   659  O  O      . LYS A 1 107 ? 142.668 161.132 154.474 1.00 35.52 ? 250 LYS A O      1 
ATOM   660  C  CB     . LYS A 1 107 ? 144.757 163.515 155.303 1.00 29.43 ? 250 LYS A CB     1 
ATOM   661  C  CG     . LYS A 1 107 ? 145.046 164.271 156.579 1.00 29.84 ? 250 LYS A CG     1 
ATOM   662  C  CD     . LYS A 1 107 ? 145.504 165.675 156.256 1.00 29.94 ? 250 LYS A CD     1 
ATOM   663  C  CE     . LYS A 1 107 ? 145.497 166.564 157.475 1.00 33.92 ? 250 LYS A CE     1 
ATOM   664  N  NZ     . LYS A 1 107 ? 145.883 167.954 157.129 1.00 30.06 ? 250 LYS A NZ     1 
ATOM   665  N  N      . ALA A 1 108 ? 144.481 161.212 153.144 1.00 31.46 ? 251 ALA A N      1 
ATOM   666  C  CA     . ALA A 1 108 ? 143.749 160.698 151.992 1.00 30.01 ? 251 ALA A CA     1 
ATOM   667  C  C      . ALA A 1 108 ? 143.232 159.285 152.227 1.00 35.81 ? 251 ALA A C      1 
ATOM   668  O  O      . ALA A 1 108 ? 142.261 158.868 151.587 1.00 41.25 ? 251 ALA A O      1 
ATOM   669  C  CB     . ALA A 1 108 ? 144.633 160.745 150.749 1.00 30.07 ? 251 ALA A CB     1 
ATOM   670  N  N      . HIS A 1 109 ? 143.864 158.531 153.120 1.00 33.95 ? 252 HIS A N      1 
ATOM   671  C  CA     . HIS A 1 109 ? 143.396 157.208 153.524 1.00 32.70 ? 252 HIS A CA     1 
ATOM   672  C  C      . HIS A 1 109 ? 143.064 157.277 155.009 1.00 35.29 ? 252 HIS A C      1 
ATOM   673  O  O      . HIS A 1 109 ? 143.952 157.148 155.855 1.00 39.77 ? 252 HIS A O      1 
ATOM   674  C  CB     . HIS A 1 109 ? 144.448 156.145 153.219 1.00 32.50 ? 252 HIS A CB     1 
ATOM   675  C  CG     . HIS A 1 109 ? 145.043 156.268 151.850 1.00 39.30 ? 252 HIS A CG     1 
ATOM   676  N  ND1    . HIS A 1 109 ? 145.911 157.278 151.500 1.00 39.33 ? 252 HIS A ND1    1 
ATOM   677  C  CD2    . HIS A 1 109 ? 144.876 155.517 150.736 1.00 42.33 ? 252 HIS A CD2    1 
ATOM   678  C  CE1    . HIS A 1 109 ? 146.259 157.142 150.234 1.00 37.50 ? 252 HIS A CE1    1 
ATOM   679  N  NE2    . HIS A 1 109 ? 145.644 156.080 149.747 1.00 40.40 ? 252 HIS A NE2    1 
ATOM   680  N  N      . ALA A 1 110 ? 141.783 157.467 155.320 1.00 36.84 ? 253 ALA A N      1 
ATOM   681  C  CA     . ALA A 1 110 ? 141.338 158.016 156.597 1.00 35.55 ? 253 ALA A CA     1 
ATOM   682  C  C      . ALA A 1 110 ? 141.879 157.252 157.797 1.00 38.86 ? 253 ALA A C      1 
ATOM   683  O  O      . ALA A 1 110 ? 142.674 157.812 158.560 1.00 42.09 ? 253 ALA A O      1 
ATOM   684  C  CB     . ALA A 1 110 ? 139.810 158.065 156.650 1.00 44.80 ? 253 ALA A CB     1 
ATOM   685  N  N      . PRO A 1 111 ? 141.475 155.992 158.026 1.00 40.02 ? 254 PRO A N      1 
ATOM   686  C  CA     . PRO A 1 111 ? 142.026 155.235 159.161 1.00 33.50 ? 254 PRO A CA     1 
ATOM   687  C  C      . PRO A 1 111 ? 143.400 154.684 158.822 1.00 31.18 ? 254 PRO A C      1 
ATOM   688  O  O      . PRO A 1 111 ? 143.533 153.747 158.027 1.00 34.78 ? 254 PRO A O      1 
ATOM   689  C  CB     . PRO A 1 111 ? 140.990 154.117 159.369 1.00 28.02 ? 254 PRO A CB     1 
ATOM   690  C  CG     . PRO A 1 111 ? 139.837 154.444 158.459 1.00 29.69 ? 254 PRO A CG     1 
ATOM   691  C  CD     . PRO A 1 111 ? 140.424 155.228 157.340 1.00 32.61 ? 254 PRO A CD     1 
ATOM   692  N  N      . SER A 1 112 ? 144.435 155.265 159.423 1.00 28.98 ? 255 SER A N      1 
ATOM   693  C  CA     . SER A 1 112 ? 145.806 154.884 159.125 1.00 28.18 ? 255 SER A CA     1 
ATOM   694  C  C      . SER A 1 112 ? 146.692 155.235 160.313 1.00 26.25 ? 255 SER A C      1 
ATOM   695  O  O      . SER A 1 112 ? 146.217 155.688 161.356 1.00 26.04 ? 255 SER A O      1 
ATOM   696  C  CB     . SER A 1 112 ? 146.294 155.561 157.841 1.00 28.87 ? 255 SER A CB     1 
ATOM   697  O  OG     . SER A 1 112 ? 145.896 156.917 157.792 1.00 29.92 ? 255 SER A OG     1 
ATOM   698  N  N      . ILE A 1 113 ? 147.995 155.019 160.145 1.00 24.07 ? 256 ILE A N      1 
ATOM   699  C  CA     . ILE A 1 113 ? 148.986 155.254 161.187 1.00 20.52 ? 256 ILE A CA     1 
ATOM   700  C  C      . ILE A 1 113 ? 150.143 156.053 160.609 1.00 21.72 ? 256 ILE A C      1 
ATOM   701  O  O      . ILE A 1 113 ? 150.567 155.817 159.474 1.00 23.91 ? 256 ILE A O      1 
ATOM   702  C  CB     . ILE A 1 113 ? 149.504 153.933 161.792 1.00 22.03 ? 256 ILE A CB     1 
ATOM   703  C  CG1    . ILE A 1 113 ? 148.475 153.331 162.743 1.00 23.43 ? 256 ILE A CG1    1 
ATOM   704  C  CG2    . ILE A 1 113 ? 150.813 154.157 162.523 1.00 20.60 ? 256 ILE A CG2    1 
ATOM   705  C  CD1    . ILE A 1 113 ? 148.818 151.936 163.183 1.00 23.56 ? 256 ILE A CD1    1 
ATOM   706  N  N      . VAL A 1 114 ? 150.653 156.997 161.394 1.00 20.38 ? 257 VAL A N      1 
ATOM   707  C  CA     . VAL A 1 114 ? 151.898 157.700 161.107 1.00 19.54 ? 257 VAL A CA     1 
ATOM   708  C  C      . VAL A 1 114 ? 152.900 157.320 162.188 1.00 19.53 ? 257 VAL A C      1 
ATOM   709  O  O      . VAL A 1 114 ? 152.599 157.428 163.380 1.00 22.53 ? 257 VAL A O      1 
ATOM   710  C  CB     . VAL A 1 114 ? 151.696 159.226 161.058 1.00 19.67 ? 257 VAL A CB     1 
ATOM   711  C  CG1    . VAL A 1 114 ? 153.034 159.940 161.019 1.00 21.00 ? 257 VAL A CG1    1 
ATOM   712  C  CG2    . VAL A 1 114 ? 150.851 159.615 159.865 1.00 16.68 ? 257 VAL A CG2    1 
ATOM   713  N  N      . PHE A 1 115 ? 154.079 156.862 161.776 1.00 17.72 ? 258 PHE A N      1 
ATOM   714  C  CA     . PHE A 1 115 ? 155.122 156.423 162.694 1.00 17.90 ? 258 PHE A CA     1 
ATOM   715  C  C      . PHE A 1 115 ? 156.400 157.210 162.447 1.00 18.62 ? 258 PHE A C      1 
ATOM   716  O  O      . PHE A 1 115 ? 156.813 157.383 161.299 1.00 21.19 ? 258 PHE A O      1 
ATOM   717  C  CB     . PHE A 1 115 ? 155.383 154.921 162.548 1.00 17.28 ? 258 PHE A CB     1 
ATOM   718  C  CG     . PHE A 1 115 ? 156.437 154.395 163.475 1.00 18.35 ? 258 PHE A CG     1 
ATOM   719  C  CD1    . PHE A 1 115 ? 156.299 154.514 164.845 1.00 17.89 ? 258 PHE A CD1    1 
ATOM   720  C  CD2    . PHE A 1 115 ? 157.569 153.778 162.976 1.00 17.02 ? 258 PHE A CD2    1 
ATOM   721  C  CE1    . PHE A 1 115 ? 157.270 154.036 165.698 1.00 17.71 ? 258 PHE A CE1    1 
ATOM   722  C  CE2    . PHE A 1 115 ? 158.540 153.291 163.826 1.00 19.85 ? 258 PHE A CE2    1 
ATOM   723  C  CZ     . PHE A 1 115 ? 158.391 153.420 165.187 1.00 19.34 ? 258 PHE A CZ     1 
ATOM   724  N  N      . ILE A 1 116 ? 157.020 157.685 163.524 1.00 18.36 ? 259 ILE A N      1 
ATOM   725  C  CA     . ILE A 1 116 ? 158.272 158.429 163.456 1.00 19.98 ? 259 ILE A CA     1 
ATOM   726  C  C      . ILE A 1 116 ? 159.291 157.750 164.361 1.00 22.47 ? 259 ILE A C      1 
ATOM   727  O  O      . ILE A 1 116 ? 159.026 157.529 165.546 1.00 21.58 ? 259 ILE A O      1 
ATOM   728  C  CB     . ILE A 1 116 ? 158.087 159.903 163.858 1.00 19.58 ? 259 ILE A CB     1 
ATOM   729  C  CG1    . ILE A 1 116 ? 156.937 160.527 163.068 1.00 18.47 ? 259 ILE A CG1    1 
ATOM   730  C  CG2    . ILE A 1 116 ? 159.369 160.676 163.643 1.00 21.00 ? 259 ILE A CG2    1 
ATOM   731  C  CD1    . ILE A 1 116 ? 156.617 161.934 163.473 1.00 18.36 ? 259 ILE A CD1    1 
ATOM   732  N  N      . ASP A 1 117 ? 160.457 157.441 163.807 1.00 27.18 ? 260 ASP A N      1 
ATOM   733  C  CA     . ASP A 1 117 ? 161.504 156.718 164.514 1.00 30.27 ? 260 ASP A CA     1 
ATOM   734  C  C      . ASP A 1 117 ? 162.692 157.638 164.766 1.00 35.80 ? 260 ASP A C      1 
ATOM   735  O  O      . ASP A 1 117 ? 163.012 158.493 163.936 1.00 39.75 ? 260 ASP A O      1 
ATOM   736  C  CB     . ASP A 1 117 ? 161.937 155.492 163.712 1.00 33.88 ? 260 ASP A CB     1 
ATOM   737  C  CG     . ASP A 1 117 ? 162.463 154.383 164.587 1.00 41.55 ? 260 ASP A CG     1 
ATOM   738  O  OD1    . ASP A 1 117 ? 162.488 154.561 165.821 1.00 40.87 ? 260 ASP A OD1    1 
ATOM   739  O  OD2    . ASP A 1 117 ? 162.848 153.330 164.041 1.00 44.70 ? 260 ASP A OD2    1 
ATOM   740  N  N      . GLU A 1 118 ? 163.345 157.455 165.915 1.00 32.01 ? 261 GLU A N      1 
ATOM   741  C  CA     . GLU A 1 118 ? 164.407 158.352 166.383 1.00 33.89 ? 261 GLU A CA     1 
ATOM   742  C  C      . GLU A 1 118 ? 163.937 159.805 166.407 1.00 37.25 ? 261 GLU A C      1 
ATOM   743  O  O      . GLU A 1 118 ? 164.562 160.691 165.825 1.00 41.92 ? 261 GLU A O      1 
ATOM   744  C  CB     . GLU A 1 118 ? 165.684 158.223 165.546 1.00 36.91 ? 261 GLU A CB     1 
ATOM   745  C  CG     . GLU A 1 118 ? 166.456 156.927 165.697 1.00 44.70 ? 261 GLU A CG     1 
ATOM   746  C  CD     . GLU A 1 118 ? 165.986 155.838 164.762 1.00 51.37 ? 261 GLU A CD     1 
ATOM   747  O  OE1    . GLU A 1 118 ? 165.113 156.111 163.916 1.00 48.89 ? 261 GLU A OE1    1 
ATOM   748  O  OE2    . GLU A 1 118 ? 166.495 154.703 164.869 1.00 52.97 ? 261 GLU A OE2    1 
ATOM   749  N  N      . ILE A 1 119 ? 162.828 160.053 167.103 1.00 32.69 ? 262 ILE A N      1 
ATOM   750  C  CA     . ILE A 1 119 ? 162.276 161.403 167.112 1.00 32.77 ? 262 ILE A CA     1 
ATOM   751  C  C      . ILE A 1 119 ? 163.199 162.370 167.846 1.00 34.56 ? 262 ILE A C      1 
ATOM   752  O  O      . ILE A 1 119 ? 163.093 163.588 167.668 1.00 37.12 ? 262 ILE A O      1 
ATOM   753  C  CB     . ILE A 1 119 ? 160.856 161.408 167.708 1.00 29.00 ? 262 ILE A CB     1 
ATOM   754  C  CG1    . ILE A 1 119 ? 160.239 162.803 167.568 1.00 25.03 ? 262 ILE A CG1    1 
ATOM   755  C  CG2    . ILE A 1 119 ? 160.875 160.962 169.162 1.00 24.41 ? 262 ILE A CG2    1 
ATOM   756  C  CD1    . ILE A 1 119 ? 158.737 162.817 167.563 1.00 20.95 ? 262 ILE A CD1    1 
ATOM   757  N  N      . ASP A 1 120 ? 164.109 161.864 168.679 1.00 34.74 ? 263 ASP A N      1 
ATOM   758  C  CA     . ASP A 1 120 ? 165.020 162.758 169.387 1.00 38.43 ? 263 ASP A CA     1 
ATOM   759  C  C      . ASP A 1 120 ? 166.042 163.386 168.447 1.00 41.97 ? 263 ASP A C      1 
ATOM   760  O  O      . ASP A 1 120 ? 166.558 164.472 168.733 1.00 43.99 ? 263 ASP A O      1 
ATOM   761  C  CB     . ASP A 1 120 ? 165.726 162.015 170.521 1.00 39.53 ? 263 ASP A CB     1 
ATOM   762  C  CG     . ASP A 1 120 ? 166.441 160.765 170.051 1.00 45.43 ? 263 ASP A CG     1 
ATOM   763  O  OD1    . ASP A 1 120 ? 166.463 160.504 168.833 1.00 46.78 ? 263 ASP A OD1    1 
ATOM   764  O  OD2    . ASP A 1 120 ? 166.984 160.039 170.904 1.00 48.58 ? 263 ASP A OD2    1 
ATOM   765  N  N      . ALA A 1 121 ? 166.358 162.720 167.337 1.00 39.62 ? 264 ALA A N      1 
ATOM   766  C  CA     . ALA A 1 121 ? 167.284 163.294 166.368 1.00 39.21 ? 264 ALA A CA     1 
ATOM   767  C  C      . ALA A 1 121 ? 166.692 164.524 165.692 1.00 45.66 ? 264 ALA A C      1 
ATOM   768  O  O      . ALA A 1 121 ? 167.398 165.511 165.459 1.00 50.14 ? 264 ALA A O      1 
ATOM   769  C  CB     . ALA A 1 121 ? 167.673 162.246 165.327 1.00 35.61 ? 264 ALA A CB     1 
ATOM   770  N  N      . VAL A 1 122 ? 165.400 164.483 165.363 1.00 44.73 ? 265 VAL A N      1 
ATOM   771  C  CA     . VAL A 1 122 ? 164.754 165.591 164.666 1.00 45.64 ? 265 VAL A CA     1 
ATOM   772  C  C      . VAL A 1 122 ? 164.026 166.542 165.603 1.00 46.81 ? 265 VAL A C      1 
ATOM   773  O  O      . VAL A 1 122 ? 163.682 167.659 165.189 1.00 50.94 ? 265 VAL A O      1 
ATOM   774  C  CB     . VAL A 1 122 ? 163.768 165.059 163.607 1.00 48.91 ? 265 VAL A CB     1 
ATOM   775  C  CG1    . VAL A 1 122 ? 162.604 164.349 164.273 1.00 41.48 ? 265 VAL A CG1    1 
ATOM   776  C  CG2    . VAL A 1 122 ? 163.273 166.187 162.730 1.00 49.35 ? 265 VAL A CG2    1 
ATOM   777  N  N      . GLY A 1 123 ? 163.779 166.144 166.846 1.00 44.54 ? 266 GLY A N      1 
ATOM   778  C  CA     . GLY A 1 123 ? 163.054 166.977 167.782 1.00 44.00 ? 266 GLY A CA     1 
ATOM   779  C  C      . GLY A 1 123 ? 163.872 167.383 168.989 1.00 46.87 ? 266 GLY A C      1 
ATOM   780  O  O      . GLY A 1 123 ? 163.334 167.905 169.963 1.00 50.02 ? 266 GLY A O      1 
ATOM   781  N  N      . ARG A 1 137 ? 167.269 172.936 160.947 1.00 55.11 ? 280 ARG A N      1 
ATOM   782  C  CA     . ARG A 1 137 ? 166.879 172.031 162.021 1.00 61.23 ? 280 ARG A CA     1 
ATOM   783  C  C      . ARG A 1 137 ? 165.675 172.576 162.778 1.00 57.94 ? 280 ARG A C      1 
ATOM   784  O  O      . ARG A 1 137 ? 164.858 171.817 163.290 1.00 57.34 ? 280 ARG A O      1 
ATOM   785  C  CB     . ARG A 1 137 ? 168.047 171.795 162.980 1.00 64.19 ? 280 ARG A CB     1 
ATOM   786  C  CG     . ARG A 1 137 ? 167.771 170.754 164.054 1.00 66.46 ? 280 ARG A CG     1 
ATOM   787  C  CD     . ARG A 1 137 ? 167.500 171.405 165.404 1.00 70.52 ? 280 ARG A CD     1 
ATOM   788  N  NE     . ARG A 1 137 ? 166.882 170.487 166.354 1.00 69.17 ? 280 ARG A NE     1 
ATOM   789  C  CZ     . ARG A 1 137 ? 166.419 170.843 167.545 1.00 67.33 ? 280 ARG A CZ     1 
ATOM   790  N  NH1    . ARG A 1 137 ? 166.507 172.090 167.976 1.00 65.47 ? 280 ARG A NH1    1 
ATOM   791  N  NH2    . ARG A 1 137 ? 165.854 169.924 168.323 1.00 59.96 ? 280 ARG A NH2    1 
ATOM   792  N  N      . GLU A 1 138 ? 165.576 173.900 162.853 1.00 58.97 ? 281 GLU A N      1 
ATOM   793  C  CA     . GLU A 1 138 ? 164.429 174.543 163.475 1.00 55.58 ? 281 GLU A CA     1 
ATOM   794  C  C      . GLU A 1 138 ? 163.217 174.623 162.559 1.00 55.81 ? 281 GLU A C      1 
ATOM   795  O  O      . GLU A 1 138 ? 162.093 174.751 163.053 1.00 53.78 ? 281 GLU A O      1 
ATOM   796  C  CB     . GLU A 1 138 ? 164.799 175.951 163.940 1.00 57.83 ? 281 GLU A CB     1 
ATOM   797  C  CG     . GLU A 1 138 ? 163.666 176.666 164.639 1.00 64.18 ? 281 GLU A CG     1 
ATOM   798  C  CD     . GLU A 1 138 ? 164.091 177.982 165.240 1.00 73.36 ? 281 GLU A CD     1 
ATOM   799  O  OE1    . GLU A 1 138 ? 165.290 178.320 165.147 1.00 73.38 ? 281 GLU A OE1    1 
ATOM   800  O  OE2    . GLU A 1 138 ? 163.226 178.681 165.805 1.00 75.34 ? 281 GLU A OE2    1 
ATOM   801  N  N      . GLN A 1 139 ? 163.418 174.571 161.241 1.00 55.68 ? 282 GLN A N      1 
ATOM   802  C  CA     . GLN A 1 139 ? 162.291 174.589 160.315 1.00 52.93 ? 282 GLN A CA     1 
ATOM   803  C  C      . GLN A 1 139 ? 161.541 173.264 160.327 1.00 47.19 ? 282 GLN A C      1 
ATOM   804  O  O      . GLN A 1 139 ? 160.313 173.240 160.206 1.00 47.18 ? 282 GLN A O      1 
ATOM   805  C  CB     . GLN A 1 139 ? 162.776 174.912 158.904 1.00 58.58 ? 282 GLN A CB     1 
ATOM   806  C  CG     . GLN A 1 139 ? 163.523 176.225 158.787 1.00 63.87 ? 282 GLN A CG     1 
ATOM   807  C  CD     . GLN A 1 139 ? 162.743 177.385 159.361 1.00 68.24 ? 282 GLN A CD     1 
ATOM   808  O  OE1    . GLN A 1 139 ? 161.525 177.463 159.215 1.00 67.58 ? 282 GLN A OE1    1 
ATOM   809  N  NE2    . GLN A 1 139 ? 163.445 178.299 160.022 1.00 66.57 ? 282 GLN A NE2    1 
ATOM   810  N  N      . THR A 1 140 ? 162.266 172.152 160.451 1.00 43.89 ? 283 THR A N      1 
ATOM   811  C  CA     . THR A 1 140 ? 161.625 170.842 160.493 1.00 40.49 ? 283 THR A CA     1 
ATOM   812  C  C      . THR A 1 140 ? 160.765 170.679 161.741 1.00 40.64 ? 283 THR A C      1 
ATOM   813  O  O      . THR A 1 140 ? 159.668 170.115 161.674 1.00 37.80 ? 283 THR A O      1 
ATOM   814  C  CB     . THR A 1 140 ? 162.685 169.743 160.414 1.00 39.84 ? 283 THR A CB     1 
ATOM   815  O  OG1    . THR A 1 140 ? 163.595 170.034 159.350 1.00 41.04 ? 283 THR A OG1    1 
ATOM   816  C  CG2    . THR A 1 140 ? 162.048 168.392 160.164 1.00 36.19 ? 283 THR A CG2    1 
ATOM   817  N  N      . LEU A 1 141 ? 161.243 171.157 162.891 1.00 40.36 ? 284 LEU A N      1 
ATOM   818  C  CA     . LEU A 1 141 ? 160.456 171.059 164.117 1.00 38.66 ? 284 LEU A CA     1 
ATOM   819  C  C      . LEU A 1 141 ? 159.183 171.892 164.034 1.00 37.05 ? 284 LEU A C      1 
ATOM   820  O  O      . LEU A 1 141 ? 158.121 171.462 164.497 1.00 36.79 ? 284 LEU A O      1 
ATOM   821  C  CB     . LEU A 1 141 ? 161.297 171.485 165.320 1.00 41.32 ? 284 LEU A CB     1 
ATOM   822  C  CG     . LEU A 1 141 ? 160.631 171.393 166.698 1.00 38.14 ? 284 LEU A CG     1 
ATOM   823  C  CD1    . LEU A 1 141 ? 160.160 169.981 166.996 1.00 35.07 ? 284 LEU A CD1    1 
ATOM   824  C  CD2    . LEU A 1 141 ? 161.571 171.878 167.779 1.00 39.32 ? 284 LEU A CD2    1 
ATOM   825  N  N      . ASN A 1 142 ? 159.273 173.094 163.464 1.00 38.89 ? 285 ASN A N      1 
ATOM   826  C  CA     . ASN A 1 142 ? 158.098 173.953 163.357 1.00 37.76 ? 285 ASN A CA     1 
ATOM   827  C  C      . ASN A 1 142 ? 157.029 173.327 162.472 1.00 34.21 ? 285 ASN A C      1 
ATOM   828  O  O      . ASN A 1 142 ? 155.834 173.419 162.769 1.00 31.98 ? 285 ASN A O      1 
ATOM   829  C  CB     . ASN A 1 142 ? 158.504 175.323 162.820 1.00 43.69 ? 285 ASN A CB     1 
ATOM   830  C  CG     . ASN A 1 142 ? 159.096 176.215 163.888 1.00 51.86 ? 285 ASN A CG     1 
ATOM   831  O  OD1    . ASN A 1 142 ? 158.693 176.165 165.049 1.00 52.17 ? 285 ASN A OD1    1 
ATOM   832  N  ND2    . ASN A 1 142 ? 160.062 177.037 163.503 1.00 57.38 ? 285 ASN A ND2    1 
ATOM   833  N  N      . GLN A 1 143 ? 157.439 172.696 161.371 1.00 32.18 ? 286 GLN A N      1 
ATOM   834  C  CA     . GLN A 1 143 ? 156.476 172.060 160.479 1.00 31.88 ? 286 GLN A CA     1 
ATOM   835  C  C      . GLN A 1 143 ? 155.739 170.921 161.172 1.00 30.91 ? 286 GLN A C      1 
ATOM   836  O  O      . GLN A 1 143 ? 154.535 170.737 160.967 1.00 30.54 ? 286 GLN A O      1 
ATOM   837  C  CB     . GLN A 1 143 ? 157.184 171.561 159.220 1.00 32.62 ? 286 GLN A CB     1 
ATOM   838  C  CG     . GLN A 1 143 ? 156.247 171.068 158.137 1.00 32.72 ? 286 GLN A CG     1 
ATOM   839  C  CD     . GLN A 1 143 ? 155.392 172.174 157.561 1.00 34.58 ? 286 GLN A CD     1 
ATOM   840  O  OE1    . GLN A 1 143 ? 155.900 173.213 157.150 1.00 35.83 ? 286 GLN A OE1    1 
ATOM   841  N  NE2    . GLN A 1 143 ? 154.088 171.957 157.528 1.00 32.15 ? 286 GLN A NE2    1 
ATOM   842  N  N      . LEU A 1 144 ? 156.443 170.145 161.997 1.00 30.30 ? 287 LEU A N      1 
ATOM   843  C  CA     . LEU A 1 144 ? 155.802 169.033 162.693 1.00 27.80 ? 287 LEU A CA     1 
ATOM   844  C  C      . LEU A 1 144 ? 154.714 169.518 163.645 1.00 27.56 ? 287 LEU A C      1 
ATOM   845  O  O      . LEU A 1 144 ? 153.663 168.884 163.766 1.00 27.12 ? 287 LEU A O      1 
ATOM   846  C  CB     . LEU A 1 144 ? 156.853 168.212 163.440 1.00 29.18 ? 287 LEU A CB     1 
ATOM   847  C  CG     . LEU A 1 144 ? 156.361 167.000 164.233 1.00 25.71 ? 287 LEU A CG     1 
ATOM   848  C  CD1    . LEU A 1 144 ? 155.701 165.986 163.324 1.00 26.96 ? 287 LEU A CD1    1 
ATOM   849  C  CD2    . LEU A 1 144 ? 157.505 166.367 164.993 1.00 21.73 ? 287 LEU A CD2    1 
ATOM   850  N  N      . LEU A 1 145 ? 154.955 170.630 164.344 1.00 28.70 ? 288 LEU A N      1 
ATOM   851  C  CA     . LEU A 1 145 ? 153.946 171.167 165.253 1.00 27.95 ? 288 LEU A CA     1 
ATOM   852  C  C      . LEU A 1 145 ? 152.715 171.658 164.498 1.00 29.89 ? 288 LEU A C      1 
ATOM   853  O  O      . LEU A 1 145 ? 151.591 171.558 164.999 1.00 32.92 ? 288 LEU A O      1 
ATOM   854  C  CB     . LEU A 1 145 ? 154.544 172.293 166.097 1.00 29.19 ? 288 LEU A CB     1 
ATOM   855  C  CG     . LEU A 1 145 ? 155.758 171.932 166.956 1.00 33.28 ? 288 LEU A CG     1 
ATOM   856  C  CD1    . LEU A 1 145 ? 156.407 173.179 167.520 1.00 31.65 ? 288 LEU A CD1    1 
ATOM   857  C  CD2    . LEU A 1 145 ? 155.367 170.981 168.071 1.00 31.62 ? 288 LEU A CD2    1 
ATOM   858  N  N      . VAL A 1 146 ? 152.912 172.207 163.299 1.00 29.36 ? 289 VAL A N      1 
ATOM   859  C  CA     . VAL A 1 146 ? 151.788 172.644 162.472 1.00 28.70 ? 289 VAL A CA     1 
ATOM   860  C  C      . VAL A 1 146 ? 150.939 171.453 162.038 1.00 28.21 ? 289 VAL A C      1 
ATOM   861  O  O      . VAL A 1 146 ? 149.707 171.532 162.003 1.00 29.24 ? 289 VAL A O      1 
ATOM   862  C  CB     . VAL A 1 146 ? 152.304 173.448 161.263 1.00 29.26 ? 289 VAL A CB     1 
ATOM   863  C  CG1    . VAL A 1 146 ? 151.220 173.599 160.213 1.00 24.15 ? 289 VAL A CG1    1 
ATOM   864  C  CG2    . VAL A 1 146 ? 152.785 174.810 161.709 1.00 28.42 ? 289 VAL A CG2    1 
ATOM   865  N  N      . GLU A 1 147 ? 151.582 170.343 161.675 1.00 26.77 ? 290 GLU A N      1 
ATOM   866  C  CA     . GLU A 1 147 ? 150.844 169.168 161.218 1.00 27.78 ? 290 GLU A CA     1 
ATOM   867  C  C      . GLU A 1 147 ? 150.036 168.521 162.336 1.00 30.16 ? 290 GLU A C      1 
ATOM   868  O  O      . GLU A 1 147 ? 148.922 168.047 162.094 1.00 30.03 ? 290 GLU A O      1 
ATOM   869  C  CB     . GLU A 1 147 ? 151.805 168.150 160.613 1.00 27.00 ? 290 GLU A CB     1 
ATOM   870  C  CG     . GLU A 1 147 ? 152.630 168.697 159.478 1.00 30.94 ? 290 GLU A CG     1 
ATOM   871  C  CD     . GLU A 1 147 ? 151.854 168.785 158.191 1.00 36.69 ? 290 GLU A CD     1 
ATOM   872  O  OE1    . GLU A 1 147 ? 150.660 168.432 158.193 1.00 39.26 ? 290 GLU A OE1    1 
ATOM   873  O  OE2    . GLU A 1 147 ? 152.433 169.218 157.178 1.00 41.82 ? 290 GLU A OE2    1 
ATOM   874  N  N      . MET A 1 148 ? 150.579 168.471 163.554 1.00 28.24 ? 291 MET A N      1 
ATOM   875  C  CA     . MET A 1 148 ? 149.865 167.834 164.656 1.00 27.14 ? 291 MET A CA     1 
ATOM   876  C  C      . MET A 1 148 ? 148.571 168.568 164.978 1.00 31.60 ? 291 MET A C      1 
ATOM   877  O  O      . MET A 1 148 ? 147.572 167.945 165.352 1.00 34.27 ? 291 MET A O      1 
ATOM   878  C  CB     . MET A 1 148 ? 150.757 167.761 165.896 1.00 30.85 ? 291 MET A CB     1 
ATOM   879  C  CG     . MET A 1 148 ? 151.967 166.847 165.759 1.00 34.00 ? 291 MET A CG     1 
ATOM   880  S  SD     . MET A 1 148 ? 151.557 165.095 165.698 1.00 42.56 ? 291 MET A SD     1 
ATOM   881  C  CE     . MET A 1 148 ? 151.140 164.765 167.409 1.00 23.61 ? 291 MET A CE     1 
ATOM   882  N  N      . ASP A 1 149 ? 148.570 169.894 164.852 1.00 31.67 ? 292 ASP A N      1 
ATOM   883  C  CA     . ASP A 1 149 ? 147.386 170.681 165.170 1.00 31.00 ? 292 ASP A CA     1 
ATOM   884  C  C      . ASP A 1 149 ? 146.352 170.694 164.052 1.00 33.73 ? 292 ASP A C      1 
ATOM   885  O  O      . ASP A 1 149 ? 145.210 171.090 164.295 1.00 34.94 ? 292 ASP A O      1 
ATOM   886  C  CB     . ASP A 1 149 ? 147.781 172.122 165.500 1.00 34.32 ? 292 ASP A CB     1 
ATOM   887  C  CG     . ASP A 1 149 ? 148.689 172.219 166.709 1.00 44.69 ? 292 ASP A CG     1 
ATOM   888  O  OD1    . ASP A 1 149 ? 148.669 171.302 167.554 1.00 48.28 ? 292 ASP A OD1    1 
ATOM   889  O  OD2    . ASP A 1 149 ? 149.425 173.221 166.818 1.00 46.19 ? 292 ASP A OD2    1 
ATOM   890  N  N      . GLY A 1 150 ? 146.712 170.266 162.847 1.00 31.73 ? 293 GLY A N      1 
ATOM   891  C  CA     . GLY A 1 150 ? 145.872 170.446 161.684 1.00 27.95 ? 293 GLY A CA     1 
ATOM   892  C  C      . GLY A 1 150 ? 145.100 169.250 161.172 1.00 32.08 ? 293 GLY A C      1 
ATOM   893  O  O      . GLY A 1 150 ? 144.502 169.348 160.095 1.00 34.08 ? 293 GLY A O      1 
ATOM   894  N  N      . PHE A 1 151 ? 145.075 168.129 161.888 1.00 32.63 ? 294 PHE A N      1 
ATOM   895  C  CA     . PHE A 1 151 ? 144.332 166.959 161.438 1.00 30.56 ? 294 PHE A CA     1 
ATOM   896  C  C      . PHE A 1 151 ? 143.282 166.578 162.472 1.00 31.63 ? 294 PHE A C      1 
ATOM   897  O  O      . PHE A 1 151 ? 143.400 166.906 163.654 1.00 31.41 ? 294 PHE A O      1 
ATOM   898  C  CB     . PHE A 1 151 ? 145.269 165.763 161.124 1.00 29.35 ? 294 PHE A CB     1 
ATOM   899  C  CG     . PHE A 1 151 ? 145.703 164.968 162.328 1.00 28.94 ? 294 PHE A CG     1 
ATOM   900  C  CD1    . PHE A 1 151 ? 144.910 163.951 162.831 1.00 28.65 ? 294 PHE A CD1    1 
ATOM   901  C  CD2    . PHE A 1 151 ? 146.929 165.203 162.921 1.00 28.49 ? 294 PHE A CD2    1 
ATOM   902  C  CE1    . PHE A 1 151 ? 145.310 163.220 163.923 1.00 27.14 ? 294 PHE A CE1    1 
ATOM   903  C  CE2    . PHE A 1 151 ? 147.336 164.469 164.011 1.00 27.43 ? 294 PHE A CE2    1 
ATOM   904  C  CZ     . PHE A 1 151 ? 146.525 163.477 164.512 1.00 26.29 ? 294 PHE A CZ     1 
ATOM   905  N  N      . ASP A 1 152 ? 142.239 165.896 162.004 1.00 34.28 ? 295 ASP A N      1 
ATOM   906  C  CA     . ASP A 1 152 ? 141.074 165.587 162.821 1.00 38.21 ? 295 ASP A CA     1 
ATOM   907  C  C      . ASP A 1 152 ? 141.170 164.156 163.342 1.00 39.97 ? 295 ASP A C      1 
ATOM   908  O  O      . ASP A 1 152 ? 141.236 163.205 162.557 1.00 38.54 ? 295 ASP A O      1 
ATOM   909  C  CB     . ASP A 1 152 ? 139.796 165.791 162.008 1.00 41.57 ? 295 ASP A CB     1 
ATOM   910  C  CG     . ASP A 1 152 ? 138.540 165.492 162.800 1.00 46.28 ? 295 ASP A CG     1 
ATOM   911  O  OD1    . ASP A 1 152 ? 138.513 165.768 164.016 1.00 45.55 ? 295 ASP A OD1    1 
ATOM   912  O  OD2    . ASP A 1 152 ? 137.566 164.998 162.199 1.00 46.88 ? 295 ASP A OD2    1 
ATOM   913  N  N      . SER A 1 153 ? 141.157 164.008 164.669 1.00 40.53 ? 296 SER A N      1 
ATOM   914  C  CA     . SER A 1 153 ? 141.349 162.699 165.285 1.00 37.70 ? 296 SER A CA     1 
ATOM   915  C  C      . SER A 1 153 ? 140.147 161.786 165.081 1.00 38.29 ? 296 SER A C      1 
ATOM   916  O  O      . SER A 1 153 ? 140.306 160.563 165.037 1.00 39.00 ? 296 SER A O      1 
ATOM   917  C  CB     . SER A 1 153 ? 141.641 162.866 166.775 1.00 37.12 ? 296 SER A CB     1 
ATOM   918  O  OG     . SER A 1 153 ? 141.508 161.643 167.471 1.00 42.38 ? 296 SER A OG     1 
ATOM   919  N  N      . LYS A 1 154 ? 138.947 162.352 164.951 1.00 37.35 ? 297 LYS A N      1 
ATOM   920  C  CA     . LYS A 1 154 ? 137.735 161.553 164.808 1.00 35.13 ? 297 LYS A CA     1 
ATOM   921  C  C      . LYS A 1 154 ? 137.702 160.742 163.521 1.00 38.53 ? 297 LYS A C      1 
ATOM   922  O  O      . LYS A 1 154 ? 136.879 159.829 163.408 1.00 37.19 ? 297 LYS A O      1 
ATOM   923  C  CB     . LYS A 1 154 ? 136.507 162.455 164.870 1.00 38.74 ? 297 LYS A CB     1 
ATOM   924  C  CG     . LYS A 1 154 ? 136.290 163.113 166.215 1.00 41.51 ? 297 LYS A CG     1 
ATOM   925  C  CD     . LYS A 1 154 ? 134.984 163.880 166.238 1.00 44.58 ? 297 LYS A CD     1 
ATOM   926  C  CE     . LYS A 1 154 ? 134.379 163.879 167.625 1.00 54.44 ? 297 LYS A CE     1 
ATOM   927  N  NZ     . LYS A 1 154 ? 132.908 163.665 167.584 1.00 55.39 ? 297 LYS A NZ     1 
ATOM   928  N  N      . GLU A 1 155 ? 138.562 161.054 162.552 1.00 41.99 ? 298 GLU A N      1 
ATOM   929  C  CA     . GLU A 1 155 ? 138.623 160.281 161.319 1.00 40.53 ? 298 GLU A CA     1 
ATOM   930  C  C      . GLU A 1 155 ? 139.218 158.896 161.528 1.00 40.61 ? 298 GLU A C      1 
ATOM   931  O  O      . GLU A 1 155 ? 138.959 157.997 160.723 1.00 39.93 ? 298 GLU A O      1 
ATOM   932  C  CB     . GLU A 1 155 ? 139.448 161.030 160.275 1.00 42.06 ? 298 GLU A CB     1 
ATOM   933  C  CG     . GLU A 1 155 ? 138.902 162.388 159.904 1.00 50.70 ? 298 GLU A CG     1 
ATOM   934  C  CD     . GLU A 1 155 ? 137.825 162.314 158.851 1.00 60.94 ? 298 GLU A CD     1 
ATOM   935  O  OE1    . GLU A 1 155 ? 137.444 161.188 158.470 1.00 62.53 ? 298 GLU A OE1    1 
ATOM   936  O  OE2    . GLU A 1 155 ? 137.362 163.381 158.401 1.00 60.16 ? 298 GLU A OE2    1 
ATOM   937  N  N      . GLY A 1 156 ? 140.008 158.705 162.582 1.00 36.50 ? 299 GLY A N      1 
ATOM   938  C  CA     . GLY A 1 156 ? 140.707 157.455 162.792 1.00 30.73 ? 299 GLY A CA     1 
ATOM   939  C  C      . GLY A 1 156 ? 142.176 157.530 162.432 1.00 31.40 ? 299 GLY A C      1 
ATOM   940  O  O      . GLY A 1 156 ? 142.708 156.624 161.791 1.00 32.81 ? 299 GLY A O      1 
ATOM   941  N  N      . ILE A 1 157 ? 142.842 158.608 162.834 1.00 31.15 ? 300 ILE A N      1 
ATOM   942  C  CA     . ILE A 1 157 ? 144.258 158.821 162.562 1.00 27.29 ? 300 ILE A CA     1 
ATOM   943  C  C      . ILE A 1 157 ? 144.989 158.945 163.890 1.00 27.17 ? 300 ILE A C      1 
ATOM   944  O  O      . ILE A 1 157 ? 144.483 159.573 164.825 1.00 30.09 ? 300 ILE A O      1 
ATOM   945  C  CB     . ILE A 1 157 ? 144.482 160.072 161.689 1.00 28.73 ? 300 ILE A CB     1 
ATOM   946  C  CG1    . ILE A 1 157 ? 143.732 159.932 160.365 1.00 32.80 ? 300 ILE A CG1    1 
ATOM   947  C  CG2    . ILE A 1 157 ? 145.962 160.299 161.441 1.00 24.66 ? 300 ILE A CG2    1 
ATOM   948  C  CD1    . ILE A 1 157 ? 143.628 161.213 159.576 1.00 30.24 ? 300 ILE A CD1    1 
ATOM   949  N  N      . ILE A 1 158 ? 146.168 158.331 163.980 1.00 24.61 ? 301 ILE A N      1 
ATOM   950  C  CA     . ILE A 1 158 ? 146.970 158.390 165.196 1.00 22.69 ? 301 ILE A CA     1 
ATOM   951  C  C      . ILE A 1 158 ? 148.446 158.382 164.822 1.00 21.69 ? 301 ILE A C      1 
ATOM   952  O  O      . ILE A 1 158 ? 148.846 157.800 163.813 1.00 22.13 ? 301 ILE A O      1 
ATOM   953  C  CB     . ILE A 1 158 ? 146.614 157.231 166.157 1.00 24.97 ? 301 ILE A CB     1 
ATOM   954  C  CG1    . ILE A 1 158 ? 147.122 157.536 167.564 1.00 25.38 ? 301 ILE A CG1    1 
ATOM   955  C  CG2    . ILE A 1 158 ? 147.175 155.921 165.653 1.00 22.03 ? 301 ILE A CG2    1 
ATOM   956  C  CD1    . ILE A 1 158 ? 146.452 156.724 168.628 1.00 27.09 ? 301 ILE A CD1    1 
ATOM   957  N  N      . VAL A 1 159 ? 149.257 159.042 165.650 1.00 20.40 ? 302 VAL A N      1 
ATOM   958  C  CA     . VAL A 1 159 ? 150.688 159.212 165.425 1.00 18.40 ? 302 VAL A CA     1 
ATOM   959  C  C      . VAL A 1 159 ? 151.456 158.509 166.539 1.00 18.68 ? 302 VAL A C      1 
ATOM   960  O  O      . VAL A 1 159 ? 151.076 158.587 167.710 1.00 19.82 ? 302 VAL A O      1 
ATOM   961  C  CB     . VAL A 1 159 ? 151.075 160.705 165.360 1.00 18.57 ? 302 VAL A CB     1 
ATOM   962  C  CG1    . VAL A 1 159 ? 152.550 160.870 165.056 1.00 17.53 ? 302 VAL A CG1    1 
ATOM   963  C  CG2    . VAL A 1 159 ? 150.240 161.428 164.330 1.00 18.44 ? 302 VAL A CG2    1 
ATOM   964  N  N      . MET A 1 160 ? 152.540 157.826 166.173 1.00 19.30 ? 303 MET A N      1 
ATOM   965  C  CA     . MET A 1 160 ? 153.379 157.105 167.121 1.00 17.72 ? 303 MET A CA     1 
ATOM   966  C  C      . MET A 1 160 ? 154.845 157.459 166.906 1.00 16.24 ? 303 MET A C      1 
ATOM   967  O  O      . MET A 1 160 ? 155.257 157.805 165.799 1.00 17.62 ? 303 MET A O      1 
ATOM   968  C  CB     . MET A 1 160 ? 153.186 155.593 166.994 1.00 17.34 ? 303 MET A CB     1 
ATOM   969  C  CG     . MET A 1 160 ? 151.894 155.089 167.594 1.00 21.36 ? 303 MET A CG     1 
ATOM   970  S  SD     . MET A 1 160 ? 151.965 153.372 168.121 1.00 48.65 ? 303 MET A SD     1 
ATOM   971  C  CE     . MET A 1 160 ? 151.074 152.593 166.788 1.00 25.72 ? 303 MET A CE     1 
ATOM   972  N  N      . ALA A 1 161 ? 155.628 157.372 167.978 1.00 14.88 ? 304 ALA A N      1 
ATOM   973  C  CA     . ALA A 1 161 ? 157.049 157.684 167.923 1.00 15.38 ? 304 ALA A CA     1 
ATOM   974  C  C      . ALA A 1 161 ? 157.793 156.827 168.939 1.00 15.18 ? 304 ALA A C      1 
ATOM   975  O  O      . ALA A 1 161 ? 157.197 156.268 169.859 1.00 15.88 ? 304 ALA A O      1 
ATOM   976  C  CB     . ALA A 1 161 ? 157.302 159.175 168.171 1.00 13.82 ? 304 ALA A CB     1 
ATOM   977  N  N      . ALA A 1 162 ? 159.111 156.720 168.754 1.00 17.30 ? 305 ALA A N      1 
ATOM   978  C  CA     . ALA A 1 162 ? 159.964 155.911 169.616 1.00 17.77 ? 305 ALA A CA     1 
ATOM   979  C  C      . ALA A 1 162 ? 161.284 156.626 169.868 1.00 21.01 ? 305 ALA A C      1 
ATOM   980  O  O      . ALA A 1 162 ? 161.730 157.439 169.058 1.00 21.89 ? 305 ALA A O      1 
ATOM   981  C  CB     . ALA A 1 162 ? 160.226 154.528 169.007 1.00 13.04 ? 305 ALA A CB     1 
ATOM   982  N  N      . THR A 1 163 ? 161.906 156.314 171.005 1.00 21.01 ? 306 THR A N      1 
ATOM   983  C  CA     . THR A 1 163 ? 163.187 156.900 171.381 1.00 21.83 ? 306 THR A CA     1 
ATOM   984  C  C      . THR A 1 163 ? 163.763 156.131 172.563 1.00 22.82 ? 306 THR A C      1 
ATOM   985  O  O      . THR A 1 163 ? 163.044 155.435 173.280 1.00 22.86 ? 306 THR A O      1 
ATOM   986  C  CB     . THR A 1 163 ? 163.045 158.394 171.720 1.00 27.12 ? 306 THR A CB     1 
ATOM   987  O  OG1    . THR A 1 163 ? 164.332 159.020 171.708 1.00 33.37 ? 306 THR A OG1    1 
ATOM   988  C  CG2    . THR A 1 163 ? 162.404 158.597 173.083 1.00 23.62 ? 306 THR A CG2    1 
ATOM   989  N  N      . ASN A 1 164 ? 165.078 156.259 172.756 1.00 25.50 ? 307 ASN A N      1 
ATOM   990  C  CA     . ASN A 1 164 ? 165.714 155.787 173.981 1.00 27.77 ? 307 ASN A CA     1 
ATOM   991  C  C      . ASN A 1 164 ? 166.421 156.908 174.736 1.00 31.23 ? 307 ASN A C      1 
ATOM   992  O  O      . ASN A 1 164 ? 167.172 156.628 175.674 1.00 36.03 ? 307 ASN A O      1 
ATOM   993  C  CB     . ASN A 1 164 ? 166.688 154.629 173.707 1.00 25.07 ? 307 ASN A CB     1 
ATOM   994  C  CG     . ASN A 1 164 ? 167.643 154.903 172.563 1.00 32.90 ? 307 ASN A CG     1 
ATOM   995  O  OD1    . ASN A 1 164 ? 168.334 155.917 172.542 1.00 42.23 ? 307 ASN A OD1    1 
ATOM   996  N  ND2    . ASN A 1 164 ? 167.699 153.983 171.611 1.00 31.14 ? 307 ASN A ND2    1 
ATOM   997  N  N      . ARG A 1 165 ? 166.186 158.164 174.363 1.00 30.92 ? 308 ARG A N      1 
ATOM   998  C  CA     . ARG A 1 165 ? 166.719 159.331 175.066 1.00 32.58 ? 308 ARG A CA     1 
ATOM   999  C  C      . ARG A 1 165 ? 165.590 160.326 175.307 1.00 35.00 ? 308 ARG A C      1 
ATOM   1000 O  O      . ARG A 1 165 ? 165.598 161.437 174.769 1.00 37.86 ? 308 ARG A O      1 
ATOM   1001 C  CB     . ARG A 1 165 ? 167.853 159.977 174.272 1.00 37.94 ? 308 ARG A CB     1 
ATOM   1002 C  CG     . ARG A 1 165 ? 169.204 159.326 174.469 1.00 43.25 ? 308 ARG A CG     1 
ATOM   1003 C  CD     . ARG A 1 165 ? 170.000 159.299 173.180 1.00 50.32 ? 308 ARG A CD     1 
ATOM   1004 N  NE     . ARG A 1 165 ? 170.583 160.595 172.858 1.00 62.57 ? 308 ARG A NE     1 
ATOM   1005 C  CZ     . ARG A 1 165 ? 171.516 161.201 173.579 1.00 66.77 ? 308 ARG A CZ     1 
ATOM   1006 N  NH1    . ARG A 1 165 ? 171.994 160.662 174.689 1.00 63.18 ? 308 ARG A NH1    1 
ATOM   1007 N  NH2    . ARG A 1 165 ? 171.986 162.378 173.175 1.00 64.94 ? 308 ARG A NH2    1 
ATOM   1008 N  N      . PRO A 1 166 ? 164.600 159.959 176.125 1.00 35.88 ? 309 PRO A N      1 
ATOM   1009 C  CA     . PRO A 1 166 ? 163.417 160.823 176.276 1.00 33.31 ? 309 PRO A CA     1 
ATOM   1010 C  C      . PRO A 1 166 ? 163.676 162.137 176.993 1.00 35.88 ? 309 PRO A C      1 
ATOM   1011 O  O      . PRO A 1 166 ? 162.838 163.039 176.897 1.00 42.94 ? 309 PRO A O      1 
ATOM   1012 C  CB     . PRO A 1 166 ? 162.444 159.946 177.072 1.00 29.99 ? 309 PRO A CB     1 
ATOM   1013 C  CG     . PRO A 1 166 ? 163.312 158.983 177.792 1.00 31.09 ? 309 PRO A CG     1 
ATOM   1014 C  CD     . PRO A 1 166 ? 164.473 158.712 176.895 1.00 29.66 ? 309 PRO A CD     1 
ATOM   1015 N  N      . ASP A 1 167 ? 164.787 162.285 177.702 1.00 38.50 ? 310 ASP A N      1 
ATOM   1016 C  CA     . ASP A 1 167 ? 164.993 163.449 178.554 1.00 40.39 ? 310 ASP A CA     1 
ATOM   1017 C  C      . ASP A 1 167 ? 165.601 164.639 177.823 1.00 41.49 ? 310 ASP A C      1 
ATOM   1018 O  O      . ASP A 1 167 ? 165.800 165.688 178.441 1.00 45.01 ? 310 ASP A O      1 
ATOM   1019 C  CB     . ASP A 1 167 ? 165.868 163.075 179.753 1.00 40.66 ? 310 ASP A CB     1 
ATOM   1020 C  CG     . ASP A 1 167 ? 165.114 162.267 180.795 1.00 46.07 ? 310 ASP A CG     1 
ATOM   1021 O  OD1    . ASP A 1 167 ? 163.872 162.189 180.708 1.00 44.94 ? 310 ASP A OD1    1 
ATOM   1022 O  OD2    . ASP A 1 167 ? 165.762 161.711 181.703 1.00 43.67 ? 310 ASP A OD2    1 
ATOM   1023 N  N      . ILE A 1 168 ? 165.893 164.514 176.531 1.00 40.61 ? 311 ILE A N      1 
ATOM   1024 C  CA     . ILE A 1 168 ? 166.429 165.617 175.745 1.00 41.17 ? 311 ILE A CA     1 
ATOM   1025 C  C      . ILE A 1 168 ? 165.407 166.153 174.752 1.00 41.89 ? 311 ILE A C      1 
ATOM   1026 O  O      . ILE A 1 168 ? 165.752 166.974 173.899 1.00 43.56 ? 311 ILE A O      1 
ATOM   1027 C  CB     . ILE A 1 168 ? 167.727 165.214 175.027 1.00 39.97 ? 311 ILE A CB     1 
ATOM   1028 C  CG1    . ILE A 1 168 ? 167.437 164.206 173.919 1.00 40.86 ? 311 ILE A CG1    1 
ATOM   1029 C  CG2    . ILE A 1 168 ? 168.726 164.646 176.013 1.00 39.97 ? 311 ILE A CG2    1 
ATOM   1030 C  CD1    . ILE A 1 168 ? 168.534 164.102 172.899 1.00 44.32 ? 311 ILE A CD1    1 
ATOM   1031 N  N      . LEU A 1 169 ? 164.157 165.712 174.842 1.00 40.95 ? 312 LEU A N      1 
ATOM   1032 C  CA     . LEU A 1 169 ? 163.131 166.156 173.912 1.00 40.22 ? 312 LEU A CA     1 
ATOM   1033 C  C      . LEU A 1 169 ? 162.701 167.585 174.223 1.00 43.13 ? 312 LEU A C      1 
ATOM   1034 O  O      . LEU A 1 169 ? 162.750 168.038 175.368 1.00 46.21 ? 312 LEU A O      1 
ATOM   1035 C  CB     . LEU A 1 169 ? 161.924 165.222 173.975 1.00 38.21 ? 312 LEU A CB     1 
ATOM   1036 C  CG     . LEU A 1 169 ? 162.040 163.882 173.248 1.00 35.69 ? 312 LEU A CG     1 
ATOM   1037 C  CD1    . LEU A 1 169 ? 160.792 163.050 173.473 1.00 28.18 ? 312 LEU A CD1    1 
ATOM   1038 C  CD2    . LEU A 1 169 ? 162.299 164.079 171.768 1.00 34.79 ? 312 LEU A CD2    1 
ATOM   1039 N  N      . ASP A 1 170 ? 162.273 168.295 173.188 1.00 42.73 ? 313 ASP A N      1 
ATOM   1040 C  CA     . ASP A 1 170 ? 161.797 169.662 173.360 1.00 40.15 ? 313 ASP A CA     1 
ATOM   1041 C  C      . ASP A 1 170 ? 160.493 169.673 174.151 1.00 43.49 ? 313 ASP A C      1 
ATOM   1042 O  O      . ASP A 1 170 ? 159.576 168.910 173.835 1.00 44.45 ? 313 ASP A O      1 
ATOM   1043 C  CB     . ASP A 1 170 ? 161.593 170.326 172.002 1.00 44.01 ? 313 ASP A CB     1 
ATOM   1044 C  CG     . ASP A 1 170 ? 161.706 171.835 172.065 1.00 49.32 ? 313 ASP A CG     1 
ATOM   1045 O  OD1    . ASP A 1 170 ? 160.833 172.481 172.677 1.00 47.23 ? 313 ASP A OD1    1 
ATOM   1046 O  OD2    . ASP A 1 170 ? 162.675 172.378 171.498 1.00 54.77 ? 313 ASP A OD2    1 
ATOM   1047 N  N      . PRO A 1 171 ? 160.362 170.530 175.165 1.00 45.67 ? 314 PRO A N      1 
ATOM   1048 C  CA     . PRO A 1 171 ? 159.127 170.535 175.967 1.00 42.43 ? 314 PRO A CA     1 
ATOM   1049 C  C      . PRO A 1 171 ? 157.881 170.895 175.180 1.00 43.04 ? 314 PRO A C      1 
ATOM   1050 O  O      . PRO A 1 171 ? 156.773 170.614 175.651 1.00 43.92 ? 314 PRO A O      1 
ATOM   1051 C  CB     . PRO A 1 171 ? 159.420 171.577 177.055 1.00 41.62 ? 314 PRO A CB     1 
ATOM   1052 C  CG     . PRO A 1 171 ? 160.903 171.694 177.089 1.00 42.86 ? 314 PRO A CG     1 
ATOM   1053 C  CD     . PRO A 1 171 ? 161.366 171.467 175.691 1.00 44.61 ? 314 PRO A CD     1 
ATOM   1054 N  N      . ALA A 1 172 ? 158.019 171.520 174.010 1.00 44.19 ? 315 ALA A N      1 
ATOM   1055 C  CA     . ALA A 1 172 ? 156.847 171.888 173.220 1.00 42.97 ? 315 ALA A CA     1 
ATOM   1056 C  C      . ALA A 1 172 ? 156.132 170.670 172.646 1.00 41.48 ? 315 ALA A C      1 
ATOM   1057 O  O      . ALA A 1 172 ? 154.935 170.741 172.350 1.00 36.36 ? 315 ALA A O      1 
ATOM   1058 C  CB     . ALA A 1 172 ? 157.254 172.838 172.095 1.00 40.85 ? 315 ALA A CB     1 
ATOM   1059 N  N      . LEU A 1 173 ? 156.843 169.553 172.473 1.00 42.12 ? 316 LEU A N      1 
ATOM   1060 C  CA     . LEU A 1 173 ? 156.217 168.357 171.921 1.00 36.01 ? 316 LEU A CA     1 
ATOM   1061 C  C      . LEU A 1 173 ? 155.293 167.679 172.922 1.00 36.66 ? 316 LEU A C      1 
ATOM   1062 O  O      . LEU A 1 173 ? 154.366 166.969 172.521 1.00 35.39 ? 316 LEU A O      1 
ATOM   1063 C  CB     . LEU A 1 173 ? 157.284 167.369 171.455 1.00 34.37 ? 316 LEU A CB     1 
ATOM   1064 C  CG     . LEU A 1 173 ? 157.952 167.601 170.100 1.00 37.97 ? 316 LEU A CG     1 
ATOM   1065 C  CD1    . LEU A 1 173 ? 159.267 166.851 170.036 1.00 35.41 ? 316 LEU A CD1    1 
ATOM   1066 C  CD2    . LEU A 1 173 ? 157.041 167.177 168.967 1.00 33.21 ? 316 LEU A CD2    1 
ATOM   1067 N  N      . LEU A 1 174 ? 155.522 167.881 174.217 1.00 36.77 ? 317 LEU A N      1 
ATOM   1068 C  CA     . LEU A 1 174 ? 154.808 167.156 175.259 1.00 35.60 ? 317 LEU A CA     1 
ATOM   1069 C  C      . LEU A 1 174 ? 153.616 167.914 175.824 1.00 38.08 ? 317 LEU A C      1 
ATOM   1070 O  O      . LEU A 1 174 ? 153.001 167.437 176.780 1.00 41.39 ? 317 LEU A O      1 
ATOM   1071 C  CB     . LEU A 1 174 ? 155.773 166.792 176.391 1.00 37.31 ? 317 LEU A CB     1 
ATOM   1072 C  CG     . LEU A 1 174 ? 157.080 166.142 175.939 1.00 37.14 ? 317 LEU A CG     1 
ATOM   1073 C  CD1    . LEU A 1 174 ? 158.136 166.238 177.017 1.00 33.30 ? 317 LEU A CD1    1 
ATOM   1074 C  CD2    . LEU A 1 174 ? 156.841 164.696 175.552 1.00 30.21 ? 317 LEU A CD2    1 
ATOM   1075 N  N      . ARG A 1 175 ? 153.271 169.070 175.267 1.00 40.41 ? 318 ARG A N      1 
ATOM   1076 C  CA     . ARG A 1 175 ? 152.141 169.831 175.769 1.00 41.58 ? 318 ARG A CA     1 
ATOM   1077 C  C      . ARG A 1 175 ? 150.827 169.135 175.430 1.00 41.98 ? 318 ARG A C      1 
ATOM   1078 O  O      . ARG A 1 175 ? 150.767 168.306 174.521 1.00 40.63 ? 318 ARG A O      1 
ATOM   1079 C  CB     . ARG A 1 175 ? 152.155 171.244 175.197 1.00 44.42 ? 318 ARG A CB     1 
ATOM   1080 C  CG     . ARG A 1 175 ? 153.324 172.064 175.686 1.00 50.69 ? 318 ARG A CG     1 
ATOM   1081 C  CD     . ARG A 1 175 ? 153.425 173.401 174.992 1.00 53.22 ? 318 ARG A CD     1 
ATOM   1082 N  NE     . ARG A 1 175 ? 154.657 174.083 175.367 1.00 61.44 ? 318 ARG A NE     1 
ATOM   1083 C  CZ     . ARG A 1 175 ? 155.121 175.180 174.784 1.00 65.58 ? 318 ARG A CZ     1 
ATOM   1084 N  NH1    . ARG A 1 175 ? 154.461 175.770 173.801 1.00 65.61 ? 318 ARG A NH1    1 
ATOM   1085 N  NH2    . ARG A 1 175 ? 156.276 175.694 175.194 1.00 59.62 ? 318 ARG A NH2    1 
ATOM   1086 N  N      . PRO A 1 176 ? 149.760 169.447 176.163 1.00 47.27 ? 319 PRO A N      1 
ATOM   1087 C  CA     . PRO A 1 176 ? 148.470 168.804 175.892 1.00 46.49 ? 319 PRO A CA     1 
ATOM   1088 C  C      . PRO A 1 176 ? 148.030 169.028 174.454 1.00 44.52 ? 319 PRO A C      1 
ATOM   1089 O  O      . PRO A 1 176 ? 148.151 170.126 173.909 1.00 42.67 ? 319 PRO A O      1 
ATOM   1090 C  CB     . PRO A 1 176 ? 147.521 169.482 176.885 1.00 42.35 ? 319 PRO A CB     1 
ATOM   1091 C  CG     . PRO A 1 176 ? 148.404 169.963 177.979 1.00 43.70 ? 319 PRO A CG     1 
ATOM   1092 C  CD     . PRO A 1 176 ? 149.698 170.345 177.327 1.00 47.39 ? 319 PRO A CD     1 
ATOM   1093 N  N      . GLY A 1 177 ? 147.501 167.968 173.846 1.00 42.97 ? 320 GLY A N      1 
ATOM   1094 C  CA     . GLY A 1 177 ? 147.128 167.987 172.452 1.00 34.31 ? 320 GLY A CA     1 
ATOM   1095 C  C      . GLY A 1 177 ? 148.197 167.527 171.483 1.00 37.30 ? 320 GLY A C      1 
ATOM   1096 O  O      . GLY A 1 177 ? 147.925 167.467 170.279 1.00 36.61 ? 320 GLY A O      1 
ATOM   1097 N  N      . ARG A 1 178 ? 149.405 167.212 171.954 1.00 36.29 ? 321 ARG A N      1 
ATOM   1098 C  CA     . ARG A 1 178 ? 150.476 166.785 171.061 1.00 33.49 ? 321 ARG A CA     1 
ATOM   1099 C  C      . ARG A 1 178 ? 150.972 165.374 171.355 1.00 31.35 ? 321 ARG A C      1 
ATOM   1100 O  O      . ARG A 1 178 ? 150.765 164.478 170.535 1.00 34.32 ? 321 ARG A O      1 
ATOM   1101 C  CB     . ARG A 1 178 ? 151.624 167.799 171.129 1.00 32.71 ? 321 ARG A CB     1 
ATOM   1102 C  CG     . ARG A 1 178 ? 151.456 168.946 170.159 1.00 34.63 ? 321 ARG A CG     1 
ATOM   1103 C  CD     . ARG A 1 178 ? 151.905 170.258 170.748 1.00 37.72 ? 321 ARG A CD     1 
ATOM   1104 N  NE     . ARG A 1 178 ? 151.580 171.370 169.865 1.00 40.64 ? 321 ARG A NE     1 
ATOM   1105 C  CZ     . ARG A 1 178 ? 152.173 172.555 169.898 1.00 38.93 ? 321 ARG A CZ     1 
ATOM   1106 N  NH1    . ARG A 1 178 ? 153.134 172.823 170.762 1.00 37.97 ? 321 ARG A NH1    1 
ATOM   1107 N  NH2    . ARG A 1 178 ? 151.787 173.495 169.041 1.00 37.79 ? 321 ARG A NH2    1 
ATOM   1108 N  N      . PHE A 1 179 ? 151.593 165.136 172.508 1.00 32.83 ? 322 PHE A N      1 
ATOM   1109 C  CA     . PHE A 1 179 ? 152.120 163.818 172.883 1.00 29.38 ? 322 PHE A CA     1 
ATOM   1110 C  C      . PHE A 1 179 ? 151.890 163.695 174.386 1.00 33.07 ? 322 PHE A C      1 
ATOM   1111 O  O      . PHE A 1 179 ? 152.725 164.121 175.184 1.00 36.14 ? 322 PHE A O      1 
ATOM   1112 C  CB     . PHE A 1 179 ? 153.598 163.662 172.535 1.00 24.91 ? 322 PHE A CB     1 
ATOM   1113 C  CG     . PHE A 1 179 ? 153.862 163.167 171.140 1.00 23.47 ? 322 PHE A CG     1 
ATOM   1114 C  CD1    . PHE A 1 179 ? 153.582 161.860 170.789 1.00 24.22 ? 322 PHE A CD1    1 
ATOM   1115 C  CD2    . PHE A 1 179 ? 154.415 164.003 170.187 1.00 25.88 ? 322 PHE A CD2    1 
ATOM   1116 C  CE1    . PHE A 1 179 ? 153.829 161.402 169.509 1.00 20.12 ? 322 PHE A CE1    1 
ATOM   1117 C  CE2    . PHE A 1 179 ? 154.660 163.551 168.908 1.00 26.15 ? 322 PHE A CE2    1 
ATOM   1118 C  CZ     . PHE A 1 179 ? 154.366 162.249 168.569 1.00 21.96 ? 322 PHE A CZ     1 
ATOM   1119 N  N      . ASP A 1 180 ? 150.764 163.101 174.767 1.00 31.84 ? 323 ASP A N      1 
ATOM   1120 C  CA     . ASP A 1 180 ? 150.380 163.045 176.168 1.00 34.48 ? 323 ASP A CA     1 
ATOM   1121 C  C      . ASP A 1 180 ? 150.181 161.633 176.695 1.00 34.31 ? 323 ASP A C      1 
ATOM   1122 O  O      . ASP A 1 180 ? 149.570 161.469 177.756 1.00 40.25 ? 323 ASP A O      1 
ATOM   1123 C  CB     . ASP A 1 180 ? 149.108 163.871 176.408 1.00 40.52 ? 323 ASP A CB     1 
ATOM   1124 C  CG     . ASP A 1 180 ? 147.998 163.534 175.442 1.00 48.30 ? 323 ASP A CG     1 
ATOM   1125 O  OD1    . ASP A 1 180 ? 148.147 163.822 174.238 1.00 46.10 ? 323 ASP A OD1    1 
ATOM   1126 O  OD2    . ASP A 1 180 ? 146.975 162.973 175.885 1.00 54.63 ? 323 ASP A OD2    1 
ATOM   1127 N  N      . LYS A 1 181 ? 150.670 160.615 175.999 1.00 27.73 ? 324 LYS A N      1 
ATOM   1128 C  CA     . LYS A 1 181 ? 150.651 159.252 176.500 1.00 24.25 ? 324 LYS A CA     1 
ATOM   1129 C  C      . LYS A 1 181 ? 152.024 158.625 176.314 1.00 24.28 ? 324 LYS A C      1 
ATOM   1130 O  O      . LYS A 1 181 ? 152.643 158.775 175.259 1.00 24.64 ? 324 LYS A O      1 
ATOM   1131 C  CB     . LYS A 1 181 ? 149.588 158.414 175.794 1.00 23.22 ? 324 LYS A CB     1 
ATOM   1132 C  CG     . LYS A 1 181 ? 149.269 157.135 176.522 1.00 27.66 ? 324 LYS A CG     1 
ATOM   1133 C  CD     . LYS A 1 181 ? 148.094 156.424 175.909 1.00 31.27 ? 324 LYS A CD     1 
ATOM   1134 C  CE     . LYS A 1 181 ? 147.858 155.104 176.611 1.00 39.65 ? 324 LYS A CE     1 
ATOM   1135 N  NZ     . LYS A 1 181 ? 147.752 155.292 178.081 1.00 42.18 ? 324 LYS A NZ     1 
ATOM   1136 N  N      . LYS A 1 182 ? 152.494 157.925 177.344 1.00 23.16 ? 325 LYS A N      1 
ATOM   1137 C  CA     . LYS A 1 182 ? 153.791 157.267 177.324 1.00 22.02 ? 325 LYS A CA     1 
ATOM   1138 C  C      . LYS A 1 182 ? 153.644 155.816 177.748 1.00 19.78 ? 325 LYS A C      1 
ATOM   1139 O  O      . LYS A 1 182 ? 152.887 155.502 178.668 1.00 23.19 ? 325 LYS A O      1 
ATOM   1140 C  CB     . LYS A 1 182 ? 154.794 157.974 178.236 1.00 22.30 ? 325 LYS A CB     1 
ATOM   1141 C  CG     . LYS A 1 182 ? 154.945 159.453 177.968 1.00 26.93 ? 325 LYS A CG     1 
ATOM   1142 C  CD     . LYS A 1 182 ? 155.977 160.070 178.890 1.00 33.92 ? 325 LYS A CD     1 
ATOM   1143 C  CE     . LYS A 1 182 ? 155.766 161.564 179.048 1.00 37.56 ? 325 LYS A CE     1 
ATOM   1144 N  NZ     . LYS A 1 182 ? 155.127 161.897 180.347 1.00 40.97 ? 325 LYS A NZ     1 
ATOM   1145 N  N      . ILE A 1 183 ? 154.374 154.934 177.068 1.00 17.84 ? 326 ILE A N      1 
ATOM   1146 C  CA     . ILE A 1 183 ? 154.371 153.503 177.346 1.00 18.90 ? 326 ILE A CA     1 
ATOM   1147 C  C      . ILE A 1 183 ? 155.816 153.034 177.448 1.00 17.46 ? 326 ILE A C      1 
ATOM   1148 O  O      . ILE A 1 183 ? 156.634 153.339 176.575 1.00 17.55 ? 326 ILE A O      1 
ATOM   1149 C  CB     . ILE A 1 183 ? 153.613 152.717 176.260 1.00 19.36 ? 326 ILE A CB     1 
ATOM   1150 C  CG1    . ILE A 1 183 ? 152.188 153.255 176.118 1.00 18.87 ? 326 ILE A CG1    1 
ATOM   1151 C  CG2    . ILE A 1 183 ? 153.592 151.235 176.581 1.00 18.04 ? 326 ILE A CG2    1 
ATOM   1152 C  CD1    . ILE A 1 183 ? 151.308 152.440 175.215 1.00 21.21 ? 326 ILE A CD1    1 
ATOM   1153 N  N      . VAL A 1 184 ? 156.125 152.286 178.504 1.00 17.51 ? 327 VAL A N      1 
ATOM   1154 C  CA     . VAL A 1 184 ? 157.486 151.845 178.806 1.00 18.55 ? 327 VAL A CA     1 
ATOM   1155 C  C      . VAL A 1 184 ? 157.659 150.406 178.338 1.00 18.74 ? 327 VAL A C      1 
ATOM   1156 O  O      . VAL A 1 184 ? 156.789 149.560 178.570 1.00 22.04 ? 327 VAL A O      1 
ATOM   1157 C  CB     . VAL A 1 184 ? 157.788 151.974 180.309 1.00 19.21 ? 327 VAL A CB     1 
ATOM   1158 C  CG1    . VAL A 1 184 ? 159.153 151.404 180.632 1.00 20.48 ? 327 VAL A CG1    1 
ATOM   1159 C  CG2    . VAL A 1 184 ? 157.708 153.422 180.742 1.00 16.89 ? 327 VAL A CG2    1 
ATOM   1160 N  N      . VAL A 1 185 ? 158.783 150.129 177.679 1.00 18.53 ? 328 VAL A N      1 
ATOM   1161 C  CA     . VAL A 1 185 ? 159.111 148.801 177.164 1.00 19.65 ? 328 VAL A CA     1 
ATOM   1162 C  C      . VAL A 1 185 ? 160.370 148.320 177.881 1.00 21.11 ? 328 VAL A C      1 
ATOM   1163 O  O      . VAL A 1 185 ? 161.400 149.001 177.855 1.00 23.22 ? 328 VAL A O      1 
ATOM   1164 C  CB     . VAL A 1 185 ? 159.315 148.823 175.639 1.00 18.54 ? 328 VAL A CB     1 
ATOM   1165 C  CG1    . VAL A 1 185 ? 159.590 147.431 175.108 1.00 17.75 ? 328 VAL A CG1    1 
ATOM   1166 C  CG2    . VAL A 1 185 ? 158.116 149.449 174.943 1.00 16.18 ? 328 VAL A CG2    1 
ATOM   1167 N  N      . ASP A 1 186 ? 160.296 147.139 178.492 1.00 22.00 ? 329 ASP A N      1 
ATOM   1168 C  CA     . ASP A 1 186 ? 161.292 146.651 179.441 1.00 23.02 ? 329 ASP A CA     1 
ATOM   1169 C  C      . ASP A 1 186 ? 162.101 145.474 178.903 1.00 23.82 ? 329 ASP A C      1 
ATOM   1170 O  O      . ASP A 1 186 ? 161.675 144.773 177.979 1.00 26.34 ? 329 ASP A O      1 
ATOM   1171 C  CB     . ASP A 1 186 ? 160.616 146.220 180.749 1.00 26.08 ? 329 ASP A CB     1 
ATOM   1172 C  CG     . ASP A 1 186 ? 160.225 147.390 181.620 1.00 35.03 ? 329 ASP A CG     1 
ATOM   1173 O  OD1    . ASP A 1 186 ? 161.120 148.155 182.032 1.00 36.44 ? 329 ASP A OD1    1 
ATOM   1174 O  OD2    . ASP A 1 186 ? 159.018 147.544 181.896 1.00 36.32 ? 329 ASP A OD2    1 
ATOM   1175 N  N      . PRO A 1 187 ? 163.291 145.237 179.463 1.00 23.61 ? 330 PRO A N      1 
ATOM   1176 C  CA     . PRO A 1 187 ? 164.039 144.028 179.118 1.00 20.39 ? 330 PRO A CA     1 
ATOM   1177 C  C      . PRO A 1 187 ? 163.350 142.783 179.646 1.00 20.25 ? 330 PRO A C      1 
ATOM   1178 O  O      . PRO A 1 187 ? 162.633 142.835 180.660 1.00 22.56 ? 330 PRO A O      1 
ATOM   1179 C  CB     . PRO A 1 187 ? 165.400 144.247 179.801 1.00 19.13 ? 330 PRO A CB     1 
ATOM   1180 C  CG     . PRO A 1 187 ? 165.474 145.695 180.063 1.00 18.48 ? 330 PRO A CG     1 
ATOM   1181 C  CD     . PRO A 1 187 ? 164.075 146.144 180.314 1.00 24.22 ? 330 PRO A CD     1 
ATOM   1182 N  N      . PRO A 1 188 ? 163.553 141.636 179.006 1.00 21.34 ? 331 PRO A N      1 
ATOM   1183 C  CA     . PRO A 1 188 ? 162.835 140.420 179.397 1.00 20.97 ? 331 PRO A CA     1 
ATOM   1184 C  C      . PRO A 1 188 ? 163.461 139.698 180.584 1.00 24.10 ? 331 PRO A C      1 
ATOM   1185 O  O      . PRO A 1 188 ? 164.657 139.793 180.859 1.00 28.24 ? 331 PRO A O      1 
ATOM   1186 C  CB     . PRO A 1 188 ? 162.911 139.552 178.138 1.00 19.54 ? 331 PRO A CB     1 
ATOM   1187 C  CG     . PRO A 1 188 ? 164.147 139.997 177.451 1.00 17.77 ? 331 PRO A CG     1 
ATOM   1188 C  CD     . PRO A 1 188 ? 164.361 141.442 177.789 1.00 19.81 ? 331 PRO A CD     1 
ATOM   1189 N  N      . ASP A 1 189 ? 162.611 138.954 181.286 1.00 26.81 ? 332 ASP A N      1 
ATOM   1190 C  CA     . ASP A 1 189 ? 163.011 138.075 182.370 1.00 27.23 ? 332 ASP A CA     1 
ATOM   1191 C  C      . ASP A 1 189 ? 163.150 136.645 181.844 1.00 28.40 ? 332 ASP A C      1 
ATOM   1192 O  O      . ASP A 1 189 ? 163.072 136.393 180.640 1.00 26.91 ? 332 ASP A O      1 
ATOM   1193 C  CB     . ASP A 1 189 ? 162.011 138.170 183.524 1.00 29.62 ? 332 ASP A CB     1 
ATOM   1194 C  CG     . ASP A 1 189 ? 160.610 137.770 183.118 1.00 39.55 ? 332 ASP A CG     1 
ATOM   1195 O  OD1    . ASP A 1 189 ? 160.202 138.086 181.984 1.00 40.19 ? 332 ASP A OD1    1 
ATOM   1196 O  OD2    . ASP A 1 189 ? 159.913 137.138 183.934 1.00 43.62 ? 332 ASP A OD2    1 
ATOM   1197 N  N      . MET A 1 190 ? 163.345 135.691 182.756 1.00 31.25 ? 333 MET A N      1 
ATOM   1198 C  CA     . MET A 1 190 ? 163.661 134.323 182.349 1.00 29.35 ? 333 MET A CA     1 
ATOM   1199 C  C      . MET A 1 190 ? 162.544 133.718 181.505 1.00 30.65 ? 333 MET A C      1 
ATOM   1200 O  O      . MET A 1 190 ? 162.805 133.080 180.481 1.00 29.70 ? 333 MET A O      1 
ATOM   1201 C  CB     . MET A 1 190 ? 163.933 133.460 183.580 1.00 30.92 ? 333 MET A CB     1 
ATOM   1202 C  CG     . MET A 1 190 ? 164.716 132.183 183.297 1.00 36.49 ? 333 MET A CG     1 
ATOM   1203 S  SD     . MET A 1 190 ? 163.725 130.831 182.627 1.00 53.83 ? 333 MET A SD     1 
ATOM   1204 C  CE     . MET A 1 190 ? 162.761 130.362 184.059 1.00 42.88 ? 333 MET A CE     1 
ATOM   1205 N  N      . LEU A 1 191 ? 161.290 133.898 181.923 1.00 32.47 ? 334 LEU A N      1 
ATOM   1206 C  CA     . LEU A 1 191 ? 160.177 133.359 181.144 1.00 31.63 ? 334 LEU A CA     1 
ATOM   1207 C  C      . LEU A 1 191 ? 159.961 134.140 179.855 1.00 31.65 ? 334 LEU A C      1 
ATOM   1208 O  O      . LEU A 1 191 ? 159.483 133.575 178.867 1.00 31.39 ? 334 LEU A O      1 
ATOM   1209 C  CB     . LEU A 1 191 ? 158.900 133.349 181.978 1.00 37.20 ? 334 LEU A CB     1 
ATOM   1210 C  CG     . LEU A 1 191 ? 158.688 132.117 182.859 1.00 41.43 ? 334 LEU A CG     1 
ATOM   1211 C  CD1    . LEU A 1 191 ? 157.433 132.267 183.699 1.00 39.48 ? 334 LEU A CD1    1 
ATOM   1212 C  CD2    . LEU A 1 191 ? 158.627 130.856 182.022 1.00 38.43 ? 334 LEU A CD2    1 
ATOM   1213 N  N      . GLY A 1 192 ? 160.280 135.433 179.851 1.00 29.94 ? 335 GLY A N      1 
ATOM   1214 C  CA     . GLY A 1 192 ? 160.208 136.197 178.618 1.00 24.03 ? 335 GLY A CA     1 
ATOM   1215 C  C      . GLY A 1 192 ? 161.251 135.774 177.603 1.00 24.73 ? 335 GLY A C      1 
ATOM   1216 O  O      . GLY A 1 192 ? 160.979 135.742 176.401 1.00 25.99 ? 335 GLY A O      1 
ATOM   1217 N  N      . ARG A 1 193 ? 162.461 135.460 178.067 1.00 24.96 ? 336 ARG A N      1 
ATOM   1218 C  CA     . ARG A 1 193 ? 163.510 135.003 177.162 1.00 22.65 ? 336 ARG A CA     1 
ATOM   1219 C  C      . ARG A 1 193 ? 163.166 133.663 176.527 1.00 23.74 ? 336 ARG A C      1 
ATOM   1220 O  O      . ARG A 1 193 ? 163.482 133.437 175.355 1.00 21.60 ? 336 ARG A O      1 
ATOM   1221 C  CB     . ARG A 1 193 ? 164.848 134.916 177.897 1.00 20.92 ? 336 ARG A CB     1 
ATOM   1222 C  CG     . ARG A 1 193 ? 165.358 136.251 178.399 1.00 22.89 ? 336 ARG A CG     1 
ATOM   1223 C  CD     . ARG A 1 193 ? 166.814 136.187 178.818 1.00 20.22 ? 336 ARG A CD     1 
ATOM   1224 N  NE     . ARG A 1 193 ? 167.039 135.254 179.914 1.00 23.86 ? 336 ARG A NE     1 
ATOM   1225 C  CZ     . ARG A 1 193 ? 167.138 135.598 181.190 1.00 24.23 ? 336 ARG A CZ     1 
ATOM   1226 N  NH1    . ARG A 1 193 ? 167.021 136.855 181.579 1.00 24.49 ? 336 ARG A NH1    1 
ATOM   1227 N  NH2    . ARG A 1 193 ? 167.356 134.655 182.099 1.00 23.92 ? 336 ARG A NH2    1 
ATOM   1228 N  N      . LYS A 1 194 ? 162.534 132.763 177.278 1.00 25.11 ? 337 LYS A N      1 
ATOM   1229 C  CA     . LYS A 1 194 ? 162.193 131.456 176.728 1.00 24.82 ? 337 LYS A CA     1 
ATOM   1230 C  C      . LYS A 1 194 ? 161.165 131.570 175.611 1.00 27.67 ? 337 LYS A C      1 
ATOM   1231 O  O      . LYS A 1 194 ? 161.205 130.804 174.643 1.00 27.26 ? 337 LYS A O      1 
ATOM   1232 C  CB     . LYS A 1 194 ? 161.680 130.540 177.834 1.00 27.44 ? 337 LYS A CB     1 
ATOM   1233 C  CG     . LYS A 1 194 ? 161.378 129.138 177.360 1.00 31.85 ? 337 LYS A CG     1 
ATOM   1234 C  CD     . LYS A 1 194 ? 161.110 128.210 178.515 1.00 37.52 ? 337 LYS A CD     1 
ATOM   1235 C  CE     . LYS A 1 194 ? 160.009 127.228 178.178 1.00 43.48 ? 337 LYS A CE     1 
ATOM   1236 N  NZ     . LYS A 1 194 ? 159.246 126.818 179.384 1.00 50.95 ? 337 LYS A NZ     1 
ATOM   1237 N  N      . LYS A 1 195 ? 160.226 132.506 175.736 1.00 28.11 ? 338 LYS A N      1 
ATOM   1238 C  CA     . LYS A 1 195 ? 159.214 132.685 174.702 1.00 25.38 ? 338 LYS A CA     1 
ATOM   1239 C  C      . LYS A 1 195 ? 159.831 133.172 173.396 1.00 25.05 ? 338 LYS A C      1 
ATOM   1240 O  O      . LYS A 1 195 ? 159.436 132.727 172.314 1.00 26.15 ? 338 LYS A O      1 
ATOM   1241 C  CB     . LYS A 1 195 ? 158.146 133.661 175.193 1.00 28.23 ? 338 LYS A CB     1 
ATOM   1242 C  CG     . LYS A 1 195 ? 157.018 133.907 174.211 1.00 34.24 ? 338 LYS A CG     1 
ATOM   1243 C  CD     . LYS A 1 195 ? 155.998 132.784 174.264 1.00 37.35 ? 338 LYS A CD     1 
ATOM   1244 C  CE     . LYS A 1 195 ? 155.317 132.584 172.924 1.00 41.97 ? 338 LYS A CE     1 
ATOM   1245 N  NZ     . LYS A 1 195 ? 156.010 131.565 172.091 1.00 42.05 ? 338 LYS A NZ     1 
ATOM   1246 N  N      . ILE A 1 196 ? 160.795 134.090 173.475 1.00 22.80 ? 339 ILE A N      1 
ATOM   1247 C  CA     . ILE A 1 196 ? 161.402 134.638 172.267 1.00 21.59 ? 339 ILE A CA     1 
ATOM   1248 C  C      . ILE A 1 196 ? 162.187 133.564 171.525 1.00 23.87 ? 339 ILE A C      1 
ATOM   1249 O  O      . ILE A 1 196 ? 162.202 133.532 170.290 1.00 24.08 ? 339 ILE A O      1 
ATOM   1250 C  CB     . ILE A 1 196 ? 162.274 135.858 172.623 1.00 20.55 ? 339 ILE A CB     1 
ATOM   1251 C  CG1    . ILE A 1 196 ? 161.420 136.930 173.302 1.00 20.68 ? 339 ILE A CG1    1 
ATOM   1252 C  CG2    . ILE A 1 196 ? 162.944 136.425 171.386 1.00 16.85 ? 339 ILE A CG2    1 
ATOM   1253 C  CD1    . ILE A 1 196 ? 162.174 138.167 173.720 1.00 16.27 ? 339 ILE A CD1    1 
ATOM   1254 N  N      . LEU A 1 197 ? 162.846 132.667 172.260 1.00 23.40 ? 340 LEU A N      1 
ATOM   1255 C  CA     . LEU A 1 197 ? 163.571 131.571 171.624 1.00 21.41 ? 340 LEU A CA     1 
ATOM   1256 C  C      . LEU A 1 197 ? 162.629 130.652 170.859 1.00 23.47 ? 340 LEU A C      1 
ATOM   1257 O  O      . LEU A 1 197 ? 162.989 130.125 169.801 1.00 24.92 ? 340 LEU A O      1 
ATOM   1258 C  CB     . LEU A 1 197 ? 164.361 130.782 172.670 1.00 22.50 ? 340 LEU A CB     1 
ATOM   1259 C  CG     . LEU A 1 197 ? 165.632 131.417 173.244 1.00 21.58 ? 340 LEU A CG     1 
ATOM   1260 C  CD1    . LEU A 1 197 ? 166.136 130.630 174.438 1.00 18.61 ? 340 LEU A CD1    1 
ATOM   1261 C  CD2    . LEU A 1 197 ? 166.720 131.558 172.193 1.00 16.69 ? 340 LEU A CD2    1 
ATOM   1262 N  N      . GLU A 1 198 ? 161.423 130.428 171.387 1.00 26.28 ? 341 GLU A N      1 
ATOM   1263 C  CA     . GLU A 1 198 ? 160.451 129.584 170.700 1.00 26.71 ? 341 GLU A CA     1 
ATOM   1264 C  C      . GLU A 1 198 ? 159.925 130.239 169.428 1.00 26.56 ? 341 GLU A C      1 
ATOM   1265 O  O      . GLU A 1 198 ? 159.646 129.550 168.443 1.00 28.67 ? 341 GLU A O      1 
ATOM   1266 C  CB     . GLU A 1 198 ? 159.295 129.243 171.635 1.00 27.41 ? 341 GLU A CB     1 
ATOM   1267 C  CG     . GLU A 1 198 ? 159.591 128.131 172.615 1.00 32.19 ? 341 GLU A CG     1 
ATOM   1268 C  CD     . GLU A 1 198 ? 158.742 128.219 173.864 1.00 43.62 ? 341 GLU A CD     1 
ATOM   1269 O  OE1    . GLU A 1 198 ? 157.812 129.049 173.896 1.00 43.79 ? 341 GLU A OE1    1 
ATOM   1270 O  OE2    . GLU A 1 198 ? 158.997 127.451 174.813 1.00 52.04 ? 341 GLU A OE2    1 
ATOM   1271 N  N      . ILE A 1 199 ? 159.763 131.563 169.434 1.00 26.53 ? 342 ILE A N      1 
ATOM   1272 C  CA     . ILE A 1 199 ? 159.245 132.252 168.255 1.00 24.85 ? 342 ILE A CA     1 
ATOM   1273 C  C      . ILE A 1 199 ? 160.197 132.094 167.079 1.00 25.00 ? 342 ILE A C      1 
ATOM   1274 O  O      . ILE A 1 199 ? 159.768 131.935 165.931 1.00 27.54 ? 342 ILE A O      1 
ATOM   1275 C  CB     . ILE A 1 199 ? 158.982 133.738 168.571 1.00 26.02 ? 342 ILE A CB     1 
ATOM   1276 C  CG1    . ILE A 1 199 ? 157.687 133.904 169.362 1.00 26.57 ? 342 ILE A CG1    1 
ATOM   1277 C  CG2    . ILE A 1 199 ? 158.932 134.559 167.296 1.00 22.17 ? 342 ILE A CG2    1 
ATOM   1278 C  CD1    . ILE A 1 199 ? 157.587 135.214 170.091 1.00 24.00 ? 342 ILE A CD1    1 
ATOM   1279 N  N      . HIS A 1 200 ? 161.501 132.137 167.338 1.00 25.57 ? 343 HIS A N      1 
ATOM   1280 C  CA     . HIS A 1 200 ? 162.499 132.163 166.280 1.00 23.90 ? 343 HIS A CA     1 
ATOM   1281 C  C      . HIS A 1 200 ? 163.053 130.791 165.919 1.00 25.75 ? 343 HIS A C      1 
ATOM   1282 O  O      . HIS A 1 200 ? 163.957 130.711 165.085 1.00 25.55 ? 343 HIS A O      1 
ATOM   1283 C  CB     . HIS A 1 200 ? 163.644 133.106 166.661 1.00 20.85 ? 343 HIS A CB     1 
ATOM   1284 C  CG     . HIS A 1 200 ? 163.325 134.553 166.445 1.00 23.06 ? 343 HIS A CG     1 
ATOM   1285 N  ND1    . HIS A 1 200 ? 163.069 135.424 167.481 1.00 24.15 ? 343 HIS A ND1    1 
ATOM   1286 C  CD2    . HIS A 1 200 ? 163.197 135.275 165.309 1.00 21.48 ? 343 HIS A CD2    1 
ATOM   1287 C  CE1    . HIS A 1 200 ? 162.811 136.623 166.993 1.00 22.10 ? 343 HIS A CE1    1 
ATOM   1288 N  NE2    . HIS A 1 200 ? 162.882 136.559 165.677 1.00 21.37 ? 343 HIS A NE2    1 
ATOM   1289 N  N      . THR A 1 201 ? 162.537 129.711 166.506 1.00 27.94 ? 344 THR A N      1 
ATOM   1290 C  CA     . THR A 1 201 ? 162.915 128.361 166.103 1.00 28.67 ? 344 THR A CA     1 
ATOM   1291 C  C      . THR A 1 201 ? 161.740 127.556 165.565 1.00 33.10 ? 344 THR A C      1 
ATOM   1292 O  O      . THR A 1 201 ? 161.881 126.347 165.358 1.00 40.55 ? 344 THR A O      1 
ATOM   1293 C  CB     . THR A 1 201 ? 163.556 127.589 167.262 1.00 27.92 ? 344 THR A CB     1 
ATOM   1294 O  OG1    . THR A 1 201 ? 162.758 127.732 168.440 1.00 30.34 ? 344 THR A OG1    1 
ATOM   1295 C  CG2    . THR A 1 201 ? 164.955 128.099 167.542 1.00 25.71 ? 344 THR A CG2    1 
ATOM   1296 N  N      . ARG A 1 202 ? 160.589 128.178 165.331 1.00 33.80 ? 345 ARG A N      1 
ATOM   1297 C  CA     . ARG A 1 202 ? 159.420 127.426 164.890 1.00 39.10 ? 345 ARG A CA     1 
ATOM   1298 C  C      . ARG A 1 202 ? 159.473 127.051 163.416 1.00 43.61 ? 345 ARG A C      1 
ATOM   1299 O  O      . ARG A 1 202 ? 158.621 126.284 162.961 1.00 46.65 ? 345 ARG A O      1 
ATOM   1300 C  CB     . ARG A 1 202 ? 158.136 128.205 165.187 1.00 36.76 ? 345 ARG A CB     1 
ATOM   1301 C  CG     . ARG A 1 202 ? 158.034 129.546 164.500 1.00 39.66 ? 345 ARG A CG     1 
ATOM   1302 C  CD     . ARG A 1 202 ? 156.750 130.270 164.876 1.00 41.55 ? 345 ARG A CD     1 
ATOM   1303 N  NE     . ARG A 1 202 ? 156.592 130.383 166.321 1.00 42.06 ? 345 ARG A NE     1 
ATOM   1304 C  CZ     . ARG A 1 202 ? 155.654 131.102 166.922 1.00 43.87 ? 345 ARG A CZ     1 
ATOM   1305 N  NH1    . ARG A 1 202 ? 154.816 131.859 166.235 1.00 42.68 ? 345 ARG A NH1    1 
ATOM   1306 N  NH2    . ARG A 1 202 ? 155.565 131.072 168.248 1.00 39.29 ? 345 ARG A NH2    1 
ATOM   1307 N  N      . ASN A 1 203 ? 160.446 127.561 162.663 1.00 42.03 ? 346 ASN A N      1 
ATOM   1308 C  CA     . ASN A 1 203 ? 160.650 127.153 161.278 1.00 41.66 ? 346 ASN A CA     1 
ATOM   1309 C  C      . ASN A 1 203 ? 161.980 126.437 161.086 1.00 44.27 ? 346 ASN A C      1 
ATOM   1310 O  O      . ASN A 1 203 ? 162.455 126.313 159.955 1.00 47.83 ? 346 ASN A O      1 
ATOM   1311 C  CB     . ASN A 1 203 ? 160.556 128.357 160.343 1.00 44.14 ? 346 ASN A CB     1 
ATOM   1312 C  CG     . ASN A 1 203 ? 159.127 128.728 160.021 1.00 59.10 ? 346 ASN A CG     1 
ATOM   1313 O  OD1    . ASN A 1 203 ? 158.423 127.988 159.335 1.00 63.24 ? 346 ASN A OD1    1 
ATOM   1314 N  ND2    . ASN A 1 203 ? 158.686 129.879 160.514 1.00 57.85 ? 346 ASN A ND2    1 
ATOM   1315 N  N      . LYS A 1 204 ? 162.590 125.961 162.168 1.00 41.37 ? 347 LYS A N      1 
ATOM   1316 C  CA     . LYS A 1 204 ? 163.879 125.305 162.109 1.00 39.92 ? 347 LYS A CA     1 
ATOM   1317 C  C      . LYS A 1 204 ? 163.792 123.912 162.716 1.00 42.41 ? 347 LYS A C      1 
ATOM   1318 O  O      . LYS A 1 204 ? 163.082 123.713 163.706 1.00 43.53 ? 347 LYS A O      1 
ATOM   1319 C  CB     . LYS A 1 204 ? 164.942 126.120 162.860 1.00 37.38 ? 347 LYS A CB     1 
ATOM   1320 C  CG     . LYS A 1 204 ? 165.233 127.482 162.258 1.00 33.64 ? 347 LYS A CG     1 
ATOM   1321 C  CD     . LYS A 1 204 ? 166.447 128.106 162.910 1.00 31.83 ? 347 LYS A CD     1 
ATOM   1322 C  CE     . LYS A 1 204 ? 166.836 129.417 162.254 1.00 26.81 ? 347 LYS A CE     1 
ATOM   1323 N  NZ     . LYS A 1 204 ? 166.417 129.489 160.839 1.00 28.36 ? 347 LYS A NZ     1 
ATOM   1324 N  N      . PRO A 1 205 ? 164.496 122.929 162.149 1.00 46.35 ? 348 PRO A N      1 
ATOM   1325 C  CA     . PRO A 1 205 ? 164.476 121.570 162.712 1.00 43.97 ? 348 PRO A CA     1 
ATOM   1326 C  C      . PRO A 1 205 ? 165.430 121.458 163.892 1.00 44.07 ? 348 PRO A C      1 
ATOM   1327 O  O      . PRO A 1 205 ? 166.610 121.797 163.784 1.00 46.56 ? 348 PRO A O      1 
ATOM   1328 C  CB     . PRO A 1 205 ? 164.929 120.699 161.537 1.00 42.85 ? 348 PRO A CB     1 
ATOM   1329 C  CG     . PRO A 1 205 ? 165.789 121.602 160.727 1.00 41.03 ? 348 PRO A CG     1 
ATOM   1330 C  CD     . PRO A 1 205 ? 165.258 122.998 160.891 1.00 40.64 ? 348 PRO A CD     1 
ATOM   1331 N  N      . LEU A 1 206 ? 164.920 120.971 165.017 1.00 42.38 ? 349 LEU A N      1 
ATOM   1332 C  CA     . LEU A 1 206 ? 165.698 120.808 166.235 1.00 43.88 ? 349 LEU A CA     1 
ATOM   1333 C  C      . LEU A 1 206 ? 165.822 119.333 166.591 1.00 48.49 ? 349 LEU A C      1 
ATOM   1334 O  O      . LEU A 1 206 ? 164.942 118.525 166.285 1.00 53.24 ? 349 LEU A O      1 
ATOM   1335 C  CB     . LEU A 1 206 ? 165.062 121.561 167.409 1.00 43.69 ? 349 LEU A CB     1 
ATOM   1336 C  CG     . LEU A 1 206 ? 164.814 123.065 167.301 1.00 42.21 ? 349 LEU A CG     1 
ATOM   1337 C  CD1    . LEU A 1 206 ? 164.206 123.579 168.587 1.00 37.02 ? 349 LEU A CD1    1 
ATOM   1338 C  CD2    . LEU A 1 206 ? 166.100 123.808 166.990 1.00 39.26 ? 349 LEU A CD2    1 
ATOM   1339 N  N      . ALA A 1 207 ? 166.931 118.989 167.237 1.00 50.34 ? 350 ALA A N      1 
ATOM   1340 C  CA     . ALA A 1 207 ? 167.122 117.641 167.745 1.00 51.93 ? 350 ALA A CA     1 
ATOM   1341 C  C      . ALA A 1 207 ? 166.298 117.432 169.015 1.00 59.06 ? 350 ALA A C      1 
ATOM   1342 O  O      . ALA A 1 207 ? 165.716 118.364 169.576 1.00 60.31 ? 350 ALA A O      1 
ATOM   1343 C  CB     . ALA A 1 207 ? 168.601 117.376 168.015 1.00 45.80 ? 350 ALA A CB     1 
ATOM   1344 N  N      . GLU A 1 208 ? 166.253 116.182 169.471 1.00 60.92 ? 351 GLU A N      1 
ATOM   1345 C  CA     . GLU A 1 208 ? 165.446 115.826 170.630 1.00 65.25 ? 351 GLU A CA     1 
ATOM   1346 C  C      . GLU A 1 208 ? 166.098 116.183 171.958 1.00 62.20 ? 351 GLU A C      1 
ATOM   1347 O  O      . GLU A 1 208 ? 165.423 116.127 172.991 1.00 62.62 ? 351 GLU A O      1 
ATOM   1348 C  CB     . GLU A 1 208 ? 165.129 114.329 170.609 1.00 69.77 ? 351 GLU A CB     1 
ATOM   1349 C  CG     . GLU A 1 208 ? 164.095 113.930 169.572 1.00 78.67 ? 351 GLU A CG     1 
ATOM   1350 C  CD     . GLU A 1 208 ? 162.813 114.731 169.689 1.00 86.90 ? 351 GLU A CD     1 
ATOM   1351 O  OE1    . GLU A 1 208 ? 162.613 115.392 170.730 1.00 83.04 ? 351 GLU A OE1    1 
ATOM   1352 O  OE2    . GLU A 1 208 ? 162.005 114.701 168.738 1.00 92.61 ? 351 GLU A OE2    1 
ATOM   1353 N  N      . ASP A 1 209 ? 167.377 116.542 171.967 1.00 57.27 ? 352 ASP A N      1 
ATOM   1354 C  CA     . ASP A 1 209 ? 168.072 116.869 173.205 1.00 55.05 ? 352 ASP A CA     1 
ATOM   1355 C  C      . ASP A 1 209 ? 168.089 118.361 173.509 1.00 53.30 ? 352 ASP A C      1 
ATOM   1356 O  O      . ASP A 1 209 ? 168.658 118.762 174.528 1.00 51.02 ? 352 ASP A O      1 
ATOM   1357 C  CB     . ASP A 1 209 ? 169.509 116.336 173.159 1.00 52.19 ? 352 ASP A CB     1 
ATOM   1358 C  CG     . ASP A 1 209 ? 170.331 116.963 172.052 1.00 54.29 ? 352 ASP A CG     1 
ATOM   1359 O  OD1    . ASP A 1 209 ? 169.757 117.314 171.002 1.00 54.86 ? 352 ASP A OD1    1 
ATOM   1360 O  OD2    . ASP A 1 209 ? 171.558 117.098 172.230 1.00 54.69 ? 352 ASP A OD2    1 
ATOM   1361 N  N      . VAL A 1 210 ? 167.481 119.187 172.664 1.00 51.89 ? 353 VAL A N      1 
ATOM   1362 C  CA     . VAL A 1 210 ? 167.484 120.630 172.870 1.00 48.98 ? 353 VAL A CA     1 
ATOM   1363 C  C      . VAL A 1 210 ? 166.492 120.983 173.970 1.00 48.36 ? 353 VAL A C      1 
ATOM   1364 O  O      . VAL A 1 210 ? 165.328 120.568 173.934 1.00 48.20 ? 353 VAL A O      1 
ATOM   1365 C  CB     . VAL A 1 210 ? 167.150 121.368 171.565 1.00 48.98 ? 353 VAL A CB     1 
ATOM   1366 C  CG1    . VAL A 1 210 ? 167.008 122.856 171.824 1.00 44.81 ? 353 VAL A CG1    1 
ATOM   1367 C  CG2    . VAL A 1 210 ? 168.218 121.109 170.520 1.00 45.02 ? 353 VAL A CG2    1 
ATOM   1368 N  N      . ASN A 1 211 ? 166.953 121.754 174.951 1.00 46.26 ? 354 ASN A N      1 
ATOM   1369 C  CA     . ASN A 1 211 ? 166.128 122.209 176.068 1.00 42.11 ? 354 ASN A CA     1 
ATOM   1370 C  C      . ASN A 1 211 ? 166.219 123.732 176.118 1.00 40.67 ? 354 ASN A C      1 
ATOM   1371 O  O      . ASN A 1 211 ? 167.176 124.283 176.664 1.00 39.97 ? 354 ASN A O      1 
ATOM   1372 C  CB     . ASN A 1 211 ? 166.584 121.579 177.379 1.00 41.35 ? 354 ASN A CB     1 
ATOM   1373 C  CG     . ASN A 1 211 ? 165.622 121.839 178.517 1.00 45.64 ? 354 ASN A CG     1 
ATOM   1374 O  OD1    . ASN A 1 211 ? 164.609 122.511 178.346 1.00 47.19 ? 354 ASN A OD1    1 
ATOM   1375 N  ND2    . ASN A 1 211 ? 165.933 121.305 179.688 1.00 44.74 ? 354 ASN A ND2    1 
ATOM   1376 N  N      . LEU A 1 212 ? 165.224 124.411 175.543 1.00 37.93 ? 355 LEU A N      1 
ATOM   1377 C  CA     . LEU A 1 212 ? 165.261 125.865 175.483 1.00 33.77 ? 355 LEU A CA     1 
ATOM   1378 C  C      . LEU A 1 212 ? 165.121 126.505 176.855 1.00 35.38 ? 355 LEU A C      1 
ATOM   1379 O  O      . LEU A 1 212 ? 165.445 127.685 177.010 1.00 36.16 ? 355 LEU A O      1 
ATOM   1380 C  CB     . LEU A 1 212 ? 164.170 126.385 174.549 1.00 31.59 ? 355 LEU A CB     1 
ATOM   1381 C  CG     . LEU A 1 212 ? 164.391 126.116 173.060 1.00 30.92 ? 355 LEU A CG     1 
ATOM   1382 C  CD1    . LEU A 1 212 ? 163.218 126.611 172.241 1.00 27.58 ? 355 LEU A CD1    1 
ATOM   1383 C  CD2    . LEU A 1 212 ? 165.682 126.742 172.578 1.00 28.01 ? 355 LEU A CD2    1 
ATOM   1384 N  N      . GLU A 1 213 ? 164.644 125.757 177.849 1.00 38.19 ? 356 GLU A N      1 
ATOM   1385 C  CA     . GLU A 1 213 ? 164.529 126.296 179.198 1.00 37.25 ? 356 GLU A CA     1 
ATOM   1386 C  C      . GLU A 1 213 ? 165.892 126.429 179.868 1.00 37.38 ? 356 GLU A C      1 
ATOM   1387 O  O      . GLU A 1 213 ? 166.116 127.371 180.634 1.00 37.58 ? 356 GLU A O      1 
ATOM   1388 C  CB     . GLU A 1 213 ? 163.596 125.410 180.021 1.00 38.78 ? 356 GLU A CB     1 
ATOM   1389 C  CG     . GLU A 1 213 ? 162.917 126.103 181.183 1.00 44.68 ? 356 GLU A CG     1 
ATOM   1390 C  CD     . GLU A 1 213 ? 163.680 125.964 182.475 1.00 52.25 ? 356 GLU A CD     1 
ATOM   1391 O  OE1    . GLU A 1 213 ? 164.392 124.954 182.637 1.00 52.36 ? 356 GLU A OE1    1 
ATOM   1392 O  OE2    . GLU A 1 213 ? 163.555 126.857 183.337 1.00 56.09 ? 356 GLU A OE2    1 
ATOM   1393 N  N      . ILE A 1 214 ? 166.808 125.496 179.604 1.00 38.42 ? 357 ILE A N      1 
ATOM   1394 C  CA     . ILE A 1 214 ? 168.161 125.600 180.141 1.00 38.62 ? 357 ILE A CA     1 
ATOM   1395 C  C      . ILE A 1 214 ? 168.929 126.723 179.456 1.00 36.31 ? 357 ILE A C      1 
ATOM   1396 O  O      . ILE A 1 214 ? 169.740 127.410 180.086 1.00 36.55 ? 357 ILE A O      1 
ATOM   1397 C  CB     . ILE A 1 214 ? 168.889 124.249 180.020 1.00 43.60 ? 357 ILE A CB     1 
ATOM   1398 C  CG1    . ILE A 1 214 ? 168.474 123.326 181.163 1.00 43.41 ? 357 ILE A CG1    1 
ATOM   1399 C  CG2    . ILE A 1 214 ? 170.393 124.442 180.022 1.00 40.34 ? 357 ILE A CG2    1 
ATOM   1400 C  CD1    . ILE A 1 214 ? 168.759 121.874 180.904 1.00 42.82 ? 357 ILE A CD1    1 
ATOM   1401 N  N      . ILE A 1 215 ? 168.702 126.919 178.157 1.00 33.82 ? 358 ILE A N      1 
ATOM   1402 C  CA     . ILE A 1 215 ? 169.359 128.013 177.451 1.00 32.05 ? 358 ILE A CA     1 
ATOM   1403 C  C      . ILE A 1 215 ? 168.914 129.361 178.004 1.00 32.98 ? 358 ILE A C      1 
ATOM   1404 O  O      . ILE A 1 215 ? 169.716 130.294 178.098 1.00 33.69 ? 358 ILE A O      1 
ATOM   1405 C  CB     . ILE A 1 215 ? 169.095 127.908 175.938 1.00 31.22 ? 358 ILE A CB     1 
ATOM   1406 C  CG1    . ILE A 1 215 ? 169.669 126.605 175.385 1.00 30.44 ? 358 ILE A CG1    1 
ATOM   1407 C  CG2    . ILE A 1 215 ? 169.685 129.101 175.205 1.00 28.02 ? 358 ILE A CG2    1 
ATOM   1408 C  CD1    . ILE A 1 215 ? 171.178 126.543 175.417 1.00 33.03 ? 358 ILE A CD1    1 
ATOM   1409 N  N      . ALA A 1 216 ? 167.638 129.490 178.373 1.00 32.43 ? 359 ALA A N      1 
ATOM   1410 C  CA     . ALA A 1 216 ? 167.138 130.752 178.912 1.00 29.07 ? 359 ALA A CA     1 
ATOM   1411 C  C      . ALA A 1 216 ? 167.795 131.098 180.243 1.00 31.13 ? 359 ALA A C      1 
ATOM   1412 O  O      . ALA A 1 216 ? 168.073 132.270 180.514 1.00 29.17 ? 359 ALA A O      1 
ATOM   1413 C  CB     . ALA A 1 216 ? 165.620 130.692 179.062 1.00 27.21 ? 359 ALA A CB     1 
ATOM   1414 N  N      . LYS A 1 217 ? 168.035 130.099 181.093 1.00 32.90 ? 360 LYS A N      1 
ATOM   1415 C  CA     . LYS A 1 217 ? 168.651 130.337 182.393 1.00 33.84 ? 360 LYS A CA     1 
ATOM   1416 C  C      . LYS A 1 217 ? 170.103 130.779 182.297 1.00 33.09 ? 360 LYS A C      1 
ATOM   1417 O  O      . LYS A 1 217 ? 170.652 131.252 183.296 1.00 34.52 ? 360 LYS A O      1 
ATOM   1418 C  CB     . LYS A 1 217 ? 168.571 129.078 183.250 1.00 34.89 ? 360 LYS A CB     1 
ATOM   1419 C  CG     . LYS A 1 217 ? 167.170 128.685 183.653 1.00 40.59 ? 360 LYS A CG     1 
ATOM   1420 C  CD     . LYS A 1 217 ? 167.195 127.711 184.810 1.00 44.17 ? 360 LYS A CD     1 
ATOM   1421 C  CE     . LYS A 1 217 ? 165.810 127.174 185.107 1.00 48.02 ? 360 LYS A CE     1 
ATOM   1422 N  NZ     . LYS A 1 217 ? 165.703 126.642 186.490 1.00 52.66 ? 360 LYS A NZ     1 
ATOM   1423 N  N      . ARG A 1 218 ? 170.740 130.634 181.139 1.00 31.78 ? 361 ARG A N      1 
ATOM   1424 C  CA     . ARG A 1 218 ? 172.154 130.940 180.981 1.00 30.29 ? 361 ARG A CA     1 
ATOM   1425 C  C      . ARG A 1 218 ? 172.407 132.253 180.252 1.00 30.08 ? 361 ARG A C      1 
ATOM   1426 O  O      . ARG A 1 218 ? 173.559 132.551 179.931 1.00 31.85 ? 361 ARG A O      1 
ATOM   1427 C  CB     . ARG A 1 218 ? 172.855 129.794 180.251 1.00 32.30 ? 361 ARG A CB     1 
ATOM   1428 C  CG     . ARG A 1 218 ? 173.051 128.565 181.111 1.00 39.84 ? 361 ARG A CG     1 
ATOM   1429 C  CD     . ARG A 1 218 ? 173.885 127.509 180.415 1.00 43.95 ? 361 ARG A CD     1 
ATOM   1430 N  NE     . ARG A 1 218 ? 175.150 128.030 179.914 1.00 51.03 ? 361 ARG A NE     1 
ATOM   1431 C  CZ     . ARG A 1 218 ? 176.086 127.291 179.335 1.00 54.59 ? 361 ARG A CZ     1 
ATOM   1432 N  NH1    . ARG A 1 218 ? 175.928 125.990 179.161 1.00 50.04 ? 361 ARG A NH1    1 
ATOM   1433 N  NH2    . ARG A 1 218 ? 177.204 127.874 178.913 1.00 48.75 ? 361 ARG A NH2    1 
ATOM   1434 N  N      . THR A 1 219 ? 171.372 133.051 179.996 1.00 27.58 ? 362 THR A N      1 
ATOM   1435 C  CA     . THR A 1 219 ? 171.564 134.279 179.234 1.00 23.93 ? 362 THR A CA     1 
ATOM   1436 C  C      . THR A 1 219 ? 170.931 135.495 179.904 1.00 24.22 ? 362 THR A C      1 
ATOM   1437 O  O      . THR A 1 219 ? 170.266 136.285 179.224 1.00 24.18 ? 362 THR A O      1 
ATOM   1438 C  CB     . THR A 1 219 ? 170.986 134.119 177.825 1.00 23.53 ? 362 THR A CB     1 
ATOM   1439 O  OG1    . THR A 1 219 ? 169.717 133.464 177.897 1.00 27.75 ? 362 THR A OG1    1 
ATOM   1440 C  CG2    . THR A 1 219 ? 171.912 133.299 176.951 1.00 23.04 ? 362 THR A CG2    1 
ATOM   1441 N  N      . PRO A 1 220 ? 171.119 135.707 181.206 1.00 24.18 ? 363 PRO A N      1 
ATOM   1442 C  CA     . PRO A 1 220 ? 170.559 136.911 181.834 1.00 22.04 ? 363 PRO A CA     1 
ATOM   1443 C  C      . PRO A 1 220 ? 171.259 138.170 181.344 1.00 23.23 ? 363 PRO A C      1 
ATOM   1444 O  O      . PRO A 1 220 ? 172.488 138.234 181.279 1.00 26.00 ? 363 PRO A O      1 
ATOM   1445 C  CB     . PRO A 1 220 ? 170.794 136.671 183.329 1.00 22.01 ? 363 PRO A CB     1 
ATOM   1446 C  CG     . PRO A 1 220 ? 171.929 135.724 183.383 1.00 23.26 ? 363 PRO A CG     1 
ATOM   1447 C  CD     . PRO A 1 220 ? 171.784 134.839 182.191 1.00 23.16 ? 363 PRO A CD     1 
ATOM   1448 N  N      . GLY A 1 221 ? 170.465 139.185 181.018 1.00 22.69 ? 364 GLY A N      1 
ATOM   1449 C  CA     . GLY A 1 221 ? 170.968 140.415 180.449 1.00 18.95 ? 364 GLY A CA     1 
ATOM   1450 C  C      . GLY A 1 221 ? 170.809 140.538 178.949 1.00 22.85 ? 364 GLY A C      1 
ATOM   1451 O  O      . GLY A 1 221 ? 171.024 141.629 178.412 1.00 26.24 ? 364 GLY A O      1 
ATOM   1452 N  N      . PHE A 1 222 ? 170.440 139.463 178.261 1.00 21.82 ? 365 PHE A N      1 
ATOM   1453 C  CA     . PHE A 1 222 ? 170.180 139.507 176.830 1.00 20.46 ? 365 PHE A CA     1 
ATOM   1454 C  C      . PHE A 1 222 ? 168.846 140.189 176.542 1.00 18.97 ? 365 PHE A C      1 
ATOM   1455 O  O      . PHE A 1 222 ? 167.910 140.130 177.342 1.00 20.14 ? 365 PHE A O      1 
ATOM   1456 C  CB     . PHE A 1 222 ? 170.156 138.091 176.252 1.00 19.39 ? 365 PHE A CB     1 
ATOM   1457 C  CG     . PHE A 1 222 ? 171.491 137.596 175.781 1.00 20.52 ? 365 PHE A CG     1 
ATOM   1458 C  CD1    . PHE A 1 222 ? 172.658 138.002 176.399 1.00 22.84 ? 365 PHE A CD1    1 
ATOM   1459 C  CD2    . PHE A 1 222 ? 171.574 136.705 174.729 1.00 20.58 ? 365 PHE A CD2    1 
ATOM   1460 C  CE1    . PHE A 1 222 ? 173.883 137.537 175.965 1.00 22.81 ? 365 PHE A CE1    1 
ATOM   1461 C  CE2    . PHE A 1 222 ? 172.792 136.238 174.292 1.00 18.79 ? 365 PHE A CE2    1 
ATOM   1462 C  CZ     . PHE A 1 222 ? 173.947 136.653 174.913 1.00 20.25 ? 365 PHE A CZ     1 
ATOM   1463 N  N      . VAL A 1 223 ? 168.762 140.834 175.379 1.00 18.37 ? 366 VAL A N      1 
ATOM   1464 C  CA     . VAL A 1 223 ? 167.501 141.390 174.898 1.00 17.37 ? 366 VAL A CA     1 
ATOM   1465 C  C      . VAL A 1 223 ? 167.074 140.617 173.659 1.00 18.10 ? 366 VAL A C      1 
ATOM   1466 O  O      . VAL A 1 223 ? 167.803 139.745 173.179 1.00 19.51 ? 366 VAL A O      1 
ATOM   1467 C  CB     . VAL A 1 223 ? 167.601 142.900 174.602 1.00 16.34 ? 366 VAL A CB     1 
ATOM   1468 C  CG1    . VAL A 1 223 ? 167.876 143.676 175.873 1.00 16.88 ? 366 VAL A CG1    1 
ATOM   1469 C  CG2    . VAL A 1 223 ? 168.658 143.182 173.548 1.00 16.66 ? 366 VAL A CG2    1 
ATOM   1470 N  N      . GLY A 1 224 ? 165.894 140.939 173.128 1.00 15.46 ? 367 GLY A N      1 
ATOM   1471 C  CA     . GLY A 1 224 ? 165.352 140.179 172.014 1.00 15.01 ? 367 GLY A CA     1 
ATOM   1472 C  C      . GLY A 1 224 ? 166.234 140.180 170.783 1.00 16.78 ? 367 GLY A C      1 
ATOM   1473 O  O      . GLY A 1 224 ? 166.278 139.193 170.050 1.00 18.44 ? 367 GLY A O      1 
ATOM   1474 N  N      . ALA A 1 225 ? 166.923 141.290 170.519 1.00 17.29 ? 368 ALA A N      1 
ATOM   1475 C  CA     . ALA A 1 225 ? 167.835 141.333 169.381 1.00 16.50 ? 368 ALA A CA     1 
ATOM   1476 C  C      . ALA A 1 225 ? 169.022 140.394 169.580 1.00 18.60 ? 368 ALA A C      1 
ATOM   1477 O  O      . ALA A 1 225 ? 169.481 139.758 168.627 1.00 19.10 ? 368 ALA A O      1 
ATOM   1478 C  CB     . ALA A 1 225 ? 168.308 142.764 169.140 1.00 15.67 ? 368 ALA A CB     1 
ATOM   1479 N  N      . ASP A 1 226 ? 169.541 140.306 170.808 1.00 17.65 ? 369 ASP A N      1 
ATOM   1480 C  CA     . ASP A 1 226 ? 170.636 139.383 171.098 1.00 16.13 ? 369 ASP A CA     1 
ATOM   1481 C  C      . ASP A 1 226 ? 170.205 137.932 170.926 1.00 16.75 ? 369 ASP A C      1 
ATOM   1482 O  O      . ASP A 1 226 ? 170.967 137.107 170.417 1.00 18.56 ? 369 ASP A O      1 
ATOM   1483 C  CB     . ASP A 1 226 ? 171.149 139.602 172.519 1.00 18.24 ? 369 ASP A CB     1 
ATOM   1484 C  CG     . ASP A 1 226 ? 171.703 140.988 172.735 1.00 24.63 ? 369 ASP A CG     1 
ATOM   1485 O  OD1    . ASP A 1 226 ? 172.188 141.598 171.763 1.00 28.61 ? 369 ASP A OD1    1 
ATOM   1486 O  OD2    . ASP A 1 226 ? 171.656 141.470 173.884 1.00 28.12 ? 369 ASP A OD2    1 
ATOM   1487 N  N      . LEU A 1 227 ? 168.997 137.597 171.379 1.00 16.86 ? 370 LEU A N      1 
ATOM   1488 C  CA     . LEU A 1 227 ? 168.518 136.222 171.302 1.00 15.05 ? 370 LEU A CA     1 
ATOM   1489 C  C      . LEU A 1 227 ? 168.254 135.789 169.867 1.00 16.34 ? 370 LEU A C      1 
ATOM   1490 O  O      . LEU A 1 227 ? 168.422 134.612 169.537 1.00 17.92 ? 370 LEU A O      1 
ATOM   1491 C  CB     . LEU A 1 227 ? 167.256 136.066 172.149 1.00 14.87 ? 370 LEU A CB     1 
ATOM   1492 C  CG     . LEU A 1 227 ? 167.440 136.293 173.649 1.00 17.08 ? 370 LEU A CG     1 
ATOM   1493 C  CD1    . LEU A 1 227 ? 166.135 136.703 174.295 1.00 17.37 ? 370 LEU A CD1    1 
ATOM   1494 C  CD2    . LEU A 1 227 ? 167.989 135.045 174.310 1.00 15.95 ? 370 LEU A CD2    1 
ATOM   1495 N  N      . GLU A 1 228 ? 167.827 136.715 169.011 1.00 17.19 ? 371 GLU A N      1 
ATOM   1496 C  CA     . GLU A 1 228 ? 167.588 136.391 167.610 1.00 17.40 ? 371 GLU A CA     1 
ATOM   1497 C  C      . GLU A 1 228 ? 168.895 136.140 166.865 1.00 17.90 ? 371 GLU A C      1 
ATOM   1498 O  O      . GLU A 1 228 ? 168.938 135.304 165.957 1.00 19.76 ? 371 GLU A O      1 
ATOM   1499 C  CB     . GLU A 1 228 ? 166.786 137.523 166.963 1.00 19.72 ? 371 GLU A CB     1 
ATOM   1500 C  CG     . GLU A 1 228 ? 166.144 137.201 165.630 1.00 22.10 ? 371 GLU A CG     1 
ATOM   1501 C  CD     . GLU A 1 228 ? 167.035 137.494 164.447 1.00 30.81 ? 371 GLU A CD     1 
ATOM   1502 O  OE1    . GLU A 1 228 ? 167.885 138.400 164.541 1.00 31.12 ? 371 GLU A OE1    1 
ATOM   1503 O  OE2    . GLU A 1 228 ? 166.878 136.821 163.409 1.00 36.41 ? 371 GLU A OE2    1 
ATOM   1504 N  N      . ASN A 1 229 ? 169.965 136.848 167.236 1.00 18.09 ? 372 ASN A N      1 
ATOM   1505 C  CA     . ASN A 1 229 ? 171.272 136.628 166.629 1.00 17.05 ? 372 ASN A CA     1 
ATOM   1506 C  C      . ASN A 1 229 ? 171.916 135.332 167.113 1.00 17.53 ? 372 ASN A C      1 
ATOM   1507 O  O      . ASN A 1 229 ? 172.711 134.729 166.387 1.00 19.38 ? 372 ASN A O      1 
ATOM   1508 C  CB     . ASN A 1 229 ? 172.178 137.823 166.926 1.00 17.53 ? 372 ASN A CB     1 
ATOM   1509 C  CG     . ASN A 1 229 ? 173.513 137.738 166.219 1.00 21.82 ? 372 ASN A CG     1 
ATOM   1510 O  OD1    . ASN A 1 229 ? 174.554 137.587 166.852 1.00 20.80 ? 372 ASN A OD1    1 
ATOM   1511 N  ND2    . ASN A 1 229 ? 173.487 137.840 164.900 1.00 22.84 ? 372 ASN A ND2    1 
ATOM   1512 N  N      . LEU A 1 230 ? 171.587 134.890 168.327 1.00 15.54 ? 373 LEU A N      1 
ATOM   1513 C  CA     . LEU A 1 230 ? 172.147 133.652 168.857 1.00 15.30 ? 373 LEU A CA     1 
ATOM   1514 C  C      . LEU A 1 230 ? 171.635 132.430 168.103 1.00 16.91 ? 373 LEU A C      1 
ATOM   1515 O  O      . LEU A 1 230 ? 172.364 131.449 167.937 1.00 20.04 ? 373 LEU A O      1 
ATOM   1516 C  CB     . LEU A 1 230 ? 171.823 133.537 170.345 1.00 15.20 ? 373 LEU A CB     1 
ATOM   1517 C  CG     . LEU A 1 230 ? 172.354 132.312 171.087 1.00 17.86 ? 373 LEU A CG     1 
ATOM   1518 C  CD1    . LEU A 1 230 ? 173.769 132.560 171.555 1.00 22.32 ? 373 LEU A CD1    1 
ATOM   1519 C  CD2    . LEU A 1 230 ? 171.459 131.969 172.251 1.00 16.16 ? 373 LEU A CD2    1 
ATOM   1520 N  N      . VAL A 1 231 ? 170.377 132.458 167.662 1.00 16.26 ? 374 VAL A N      1 
ATOM   1521 C  CA     . VAL A 1 231 ? 169.821 131.328 166.926 1.00 16.34 ? 374 VAL A CA     1 
ATOM   1522 C  C      . VAL A 1 231 ? 170.497 131.175 165.568 1.00 18.58 ? 374 VAL A C      1 
ATOM   1523 O  O      . VAL A 1 231 ? 170.693 130.054 165.091 1.00 20.64 ? 374 VAL A O      1 
ATOM   1524 C  CB     . VAL A 1 231 ? 168.293 131.485 166.799 1.00 15.53 ? 374 VAL A CB     1 
ATOM   1525 C  CG1    . VAL A 1 231 ? 167.726 130.505 165.801 1.00 14.62 ? 374 VAL A CG1    1 
ATOM   1526 C  CG2    . VAL A 1 231 ? 167.632 131.293 168.146 1.00 16.09 ? 374 VAL A CG2    1 
ATOM   1527 N  N      . ASN A 1 232 ? 170.856 132.286 164.921 1.00 17.31 ? 375 ASN A N      1 
ATOM   1528 C  CA     . ASN A 1 232 ? 171.531 132.212 163.628 1.00 16.87 ? 375 ASN A CA     1 
ATOM   1529 C  C      . ASN A 1 232 ? 172.924 131.602 163.751 1.00 20.45 ? 375 ASN A C      1 
ATOM   1530 O  O      . ASN A 1 232 ? 173.358 130.860 162.865 1.00 21.23 ? 375 ASN A O      1 
ATOM   1531 C  CB     . ASN A 1 232 ? 171.605 133.601 162.997 1.00 16.00 ? 375 ASN A CB     1 
ATOM   1532 C  CG     . ASN A 1 232 ? 171.949 133.556 161.520 1.00 16.72 ? 375 ASN A CG     1 
ATOM   1533 O  OD1    . ASN A 1 232 ? 172.889 134.202 161.068 1.00 17.17 ? 375 ASN A OD1    1 
ATOM   1534 N  ND2    . ASN A 1 232 ? 171.185 132.790 160.764 1.00 19.33 ? 375 ASN A ND2    1 
ATOM   1535 N  N      . GLU A 1 233 ? 173.648 131.917 164.826 1.00 19.87 ? 376 GLU A N      1 
ATOM   1536 C  CA     . GLU A 1 233 ? 174.987 131.364 165.008 1.00 19.94 ? 376 GLU A CA     1 
ATOM   1537 C  C      . GLU A 1 233 ? 174.950 129.855 165.204 1.00 22.51 ? 376 GLU A C      1 
ATOM   1538 O  O      . GLU A 1 233 ? 175.826 129.140 164.707 1.00 26.49 ? 376 GLU A O      1 
ATOM   1539 C  CB     . GLU A 1 233 ? 175.682 132.032 166.192 1.00 21.67 ? 376 GLU A CB     1 
ATOM   1540 C  CG     . GLU A 1 233 ? 176.103 133.461 165.942 1.00 30.89 ? 376 GLU A CG     1 
ATOM   1541 C  CD     . GLU A 1 233 ? 177.216 133.575 164.921 1.00 37.97 ? 376 GLU A CD     1 
ATOM   1542 O  OE1    . GLU A 1 233 ? 178.067 132.663 164.863 1.00 43.21 ? 376 GLU A OE1    1 
ATOM   1543 O  OE2    . GLU A 1 233 ? 177.244 134.578 164.179 1.00 38.20 ? 376 GLU A OE2    1 
ATOM   1544 N  N      . ALA A 1 234 ? 173.961 129.354 165.945 1.00 21.55 ? 377 ALA A N      1 
ATOM   1545 C  CA     . ALA A 1 234 ? 173.855 127.917 166.157 1.00 21.60 ? 377 ALA A CA     1 
ATOM   1546 C  C      . ALA A 1 234 ? 173.526 127.177 164.866 1.00 23.38 ? 377 ALA A C      1 
ATOM   1547 O  O      . ALA A 1 234 ? 173.931 126.024 164.696 1.00 28.76 ? 377 ALA A O      1 
ATOM   1548 C  CB     . ALA A 1 234 ? 172.805 127.621 167.224 1.00 22.31 ? 377 ALA A CB     1 
ATOM   1549 N  N      . ALA A 1 235 ? 172.789 127.815 163.956 1.00 22.69 ? 378 ALA A N      1 
ATOM   1550 C  CA     . ALA A 1 235 ? 172.496 127.193 162.671 1.00 22.12 ? 378 ALA A CA     1 
ATOM   1551 C  C      . ALA A 1 235 ? 173.725 127.147 161.770 1.00 25.41 ? 378 ALA A C      1 
ATOM   1552 O  O      . ALA A 1 235 ? 173.873 126.212 160.979 1.00 29.06 ? 378 ALA A O      1 
ATOM   1553 C  CB     . ALA A 1 235 ? 171.353 127.932 161.977 1.00 20.50 ? 378 ALA A CB     1 
ATOM   1554 N  N      . LEU A 1 236 ? 174.605 128.146 161.862 1.00 25.00 ? 379 LEU A N      1 
ATOM   1555 C  CA     . LEU A 1 236 ? 175.824 128.137 161.060 1.00 22.49 ? 379 LEU A CA     1 
ATOM   1556 C  C      . LEU A 1 236 ? 176.768 127.025 161.496 1.00 26.27 ? 379 LEU A C      1 
ATOM   1557 O  O      . LEU A 1 236 ? 177.456 126.427 160.664 1.00 28.16 ? 379 LEU A O      1 
ATOM   1558 C  CB     . LEU A 1 236 ? 176.521 129.494 161.142 1.00 21.56 ? 379 LEU A CB     1 
ATOM   1559 C  CG     . LEU A 1 236 ? 175.907 130.652 160.354 1.00 20.32 ? 379 LEU A CG     1 
ATOM   1560 C  CD1    . LEU A 1 236 ? 176.440 131.982 160.853 1.00 17.77 ? 379 LEU A CD1    1 
ATOM   1561 C  CD2    . LEU A 1 236 ? 176.159 130.500 158.869 1.00 14.08 ? 379 LEU A CD2    1 
ATOM   1562 N  N      . LEU A 1 237 ? 176.823 126.742 162.799 1.00 26.04 ? 380 LEU A N      1 
ATOM   1563 C  CA     . LEU A 1 237 ? 177.658 125.651 163.290 1.00 26.54 ? 380 LEU A CA     1 
ATOM   1564 C  C      . LEU A 1 237 ? 177.186 124.305 162.758 1.00 33.39 ? 380 LEU A C      1 
ATOM   1565 O  O      . LEU A 1 237 ? 178.004 123.444 162.417 1.00 40.64 ? 380 LEU A O      1 
ATOM   1566 C  CB     . LEU A 1 237 ? 177.675 125.652 164.817 1.00 28.88 ? 380 LEU A CB     1 
ATOM   1567 C  CG     . LEU A 1 237 ? 178.460 126.778 165.489 1.00 31.01 ? 380 LEU A CG     1 
ATOM   1568 C  CD1    . LEU A 1 237 ? 178.477 126.602 166.989 1.00 32.99 ? 380 LEU A CD1    1 
ATOM   1569 C  CD2    . LEU A 1 237 ? 179.873 126.826 164.950 1.00 32.21 ? 380 LEU A CD2    1 
ATOM   1570 N  N      . ALA A 1 238 ? 175.872 124.094 162.697 1.00 31.83 ? 381 ALA A N      1 
ATOM   1571 C  CA     . ALA A 1 238 ? 175.354 122.832 162.181 1.00 35.30 ? 381 ALA A CA     1 
ATOM   1572 C  C      . ALA A 1 238 ? 175.544 122.720 160.672 1.00 37.03 ? 381 ALA A C      1 
ATOM   1573 O  O      . ALA A 1 238 ? 175.915 121.655 160.168 1.00 40.52 ? 381 ALA A O      1 
ATOM   1574 C  CB     . ALA A 1 238 ? 173.880 122.682 162.551 1.00 33.76 ? 381 ALA A CB     1 
ATOM   1575 N  N      . ALA A 1 239 ? 175.294 123.802 159.934 1.00 33.49 ? 382 ALA A N      1 
ATOM   1576 C  CA     . ALA A 1 239 ? 175.414 123.757 158.480 1.00 33.36 ? 382 ALA A CA     1 
ATOM   1577 C  C      . ALA A 1 239 ? 176.857 123.538 158.042 1.00 38.97 ? 382 ALA A C      1 
ATOM   1578 O  O      . ALA A 1 239 ? 177.107 122.896 157.017 1.00 41.61 ? 382 ALA A O      1 
ATOM   1579 C  CB     . ALA A 1 239 ? 174.860 125.040 157.863 1.00 27.27 ? 382 ALA A CB     1 
ATOM   1580 N  N      . ARG A 1 240 ? 177.818 124.080 158.789 1.00 39.54 ? 383 ARG A N      1 
ATOM   1581 C  CA     . ARG A 1 240 ? 179.218 123.935 158.415 1.00 41.55 ? 383 ARG A CA     1 
ATOM   1582 C  C      . ARG A 1 240 ? 179.689 122.489 158.484 1.00 45.61 ? 383 ARG A C      1 
ATOM   1583 O  O      . ARG A 1 240 ? 180.714 122.155 157.881 1.00 46.89 ? 383 ARG A O      1 
ATOM   1584 C  CB     . ARG A 1 240 ? 180.093 124.826 159.299 1.00 39.77 ? 383 ARG A CB     1 
ATOM   1585 C  CG     . ARG A 1 240 ? 181.558 124.815 158.918 1.00 50.66 ? 383 ARG A CG     1 
ATOM   1586 C  CD     . ARG A 1 240 ? 181.744 125.285 157.477 1.00 65.50 ? 383 ARG A CD     1 
ATOM   1587 N  NE     . ARG A 1 240 ? 181.671 126.734 157.311 1.00 63.19 ? 383 ARG A NE     1 
ATOM   1588 C  CZ     . ARG A 1 240 ? 182.716 127.521 157.098 1.00 55.51 ? 383 ARG A CZ     1 
ATOM   1589 N  NH1    . ARG A 1 240 ? 183.942 127.032 156.995 1.00 56.08 ? 383 ARG A NH1    1 
ATOM   1590 N  NH2    . ARG A 1 240 ? 182.526 128.828 156.966 1.00 42.96 ? 383 ARG A NH2    1 
ATOM   1591 N  N      . GLU A 1 241 ? 178.975 121.629 159.201 1.00 46.19 ? 384 GLU A N      1 
ATOM   1592 C  CA     . GLU A 1 241 ? 179.300 120.213 159.277 1.00 45.54 ? 384 GLU A CA     1 
ATOM   1593 C  C      . GLU A 1 241 ? 178.393 119.344 158.417 1.00 47.67 ? 384 GLU A C      1 
ATOM   1594 O  O      . GLU A 1 241 ? 178.511 118.118 158.465 1.00 50.24 ? 384 GLU A O      1 
ATOM   1595 C  CB     . GLU A 1 241 ? 179.239 119.740 160.728 1.00 47.39 ? 384 GLU A CB     1 
ATOM   1596 C  CG     . GLU A 1 241 ? 180.453 120.125 161.538 1.00 50.53 ? 384 GLU A CG     1 
ATOM   1597 C  CD     . GLU A 1 241 ? 180.523 119.394 162.855 1.00 60.16 ? 384 GLU A CD     1 
ATOM   1598 O  OE1    . GLU A 1 241 ? 179.698 118.487 163.075 1.00 64.66 ? 384 GLU A OE1    1 
ATOM   1599 O  OE2    . GLU A 1 241 ? 181.405 119.726 163.673 1.00 65.15 ? 384 GLU A OE2    1 
ATOM   1600 N  N      . GLY A 1 242 ? 177.492 119.939 157.643 1.00 47.75 ? 385 GLY A N      1 
ATOM   1601 C  CA     . GLY A 1 242 ? 176.624 119.184 156.765 1.00 46.82 ? 385 GLY A CA     1 
ATOM   1602 C  C      . GLY A 1 242 ? 175.407 118.565 157.413 1.00 52.40 ? 385 GLY A C      1 
ATOM   1603 O  O      . GLY A 1 242 ? 174.673 117.840 156.735 1.00 56.07 ? 385 GLY A O      1 
ATOM   1604 N  N      . ARG A 1 243 ? 175.161 118.823 158.694 1.00 50.68 ? 386 ARG A N      1 
ATOM   1605 C  CA     . ARG A 1 243 ? 174.033 118.212 159.381 1.00 50.29 ? 386 ARG A CA     1 
ATOM   1606 C  C      . ARG A 1 243 ? 172.727 118.927 159.049 1.00 52.59 ? 386 ARG A C      1 
ATOM   1607 O  O      . ARG A 1 243 ? 172.709 120.066 158.579 1.00 54.83 ? 386 ARG A O      1 
ATOM   1608 C  CB     . ARG A 1 243 ? 174.256 118.211 160.890 1.00 47.76 ? 386 ARG A CB     1 
ATOM   1609 C  CG     . ARG A 1 243 ? 175.401 117.337 161.337 1.00 51.14 ? 386 ARG A CG     1 
ATOM   1610 C  CD     . ARG A 1 243 ? 175.464 117.265 162.843 1.00 54.28 ? 386 ARG A CD     1 
ATOM   1611 N  NE     . ARG A 1 243 ? 176.359 118.278 163.387 1.00 57.62 ? 386 ARG A NE     1 
ATOM   1612 C  CZ     . ARG A 1 243 ? 175.967 119.280 164.159 1.00 55.41 ? 386 ARG A CZ     1 
ATOM   1613 N  NH1    . ARG A 1 243 ? 174.700 119.433 164.501 1.00 51.00 ? 386 ARG A NH1    1 
ATOM   1614 N  NH2    . ARG A 1 243 ? 176.871 120.153 164.595 1.00 51.77 ? 386 ARG A NH2    1 
ATOM   1615 N  N      . ASP A 1 244 ? 171.621 118.230 159.303 1.00 56.19 ? 387 ASP A N      1 
ATOM   1616 C  CA     . ASP A 1 244 ? 170.283 118.734 159.021 1.00 57.74 ? 387 ASP A CA     1 
ATOM   1617 C  C      . ASP A 1 244 ? 169.453 118.956 160.281 1.00 56.01 ? 387 ASP A C      1 
ATOM   1618 O  O      . ASP A 1 244 ? 168.230 119.088 160.188 1.00 56.25 ? 387 ASP A O      1 
ATOM   1619 C  CB     . ASP A 1 244 ? 169.556 117.780 158.071 1.00 57.56 ? 387 ASP A CB     1 
ATOM   1620 C  CG     . ASP A 1 244 ? 169.480 116.368 158.611 1.00 68.69 ? 387 ASP A CG     1 
ATOM   1621 O  OD1    . ASP A 1 244 ? 170.413 115.957 159.333 1.00 68.47 ? 387 ASP A OD1    1 
ATOM   1622 O  OD2    . ASP A 1 244 ? 168.491 115.667 158.314 1.00 69.80 ? 387 ASP A OD2    1 
ATOM   1623 N  N      . LYS A 1 245 ? 170.084 118.998 161.451 1.00 53.69 ? 388 LYS A N      1 
ATOM   1624 C  CA     . LYS A 1 245 ? 169.392 119.312 162.692 1.00 50.85 ? 388 LYS A CA     1 
ATOM   1625 C  C      . LYS A 1 245 ? 170.342 120.073 163.603 1.00 49.85 ? 388 LYS A C      1 
ATOM   1626 O  O      . LYS A 1 245 ? 171.561 119.926 163.510 1.00 52.80 ? 388 LYS A O      1 
ATOM   1627 C  CB     . LYS A 1 245 ? 168.884 118.053 163.397 1.00 51.30 ? 388 LYS A CB     1 
ATOM   1628 C  CG     . LYS A 1 245 ? 167.711 117.387 162.711 1.00 56.03 ? 388 LYS A CG     1 
ATOM   1629 C  CD     . LYS A 1 245 ? 166.978 116.462 163.662 1.00 56.95 ? 388 LYS A CD     1 
ATOM   1630 C  CE     . LYS A 1 245 ? 165.946 115.628 162.930 1.00 56.97 ? 388 LYS A CE     1 
ATOM   1631 N  NZ     . LYS A 1 245 ? 165.106 116.463 162.034 1.00 52.98 ? 388 LYS A NZ     1 
ATOM   1632 N  N      . ILE A 1 246 ? 169.770 120.882 164.488 1.00 41.97 ? 389 ILE A N      1 
ATOM   1633 C  CA     . ILE A 1 246 ? 170.535 121.673 165.444 1.00 40.03 ? 389 ILE A CA     1 
ATOM   1634 C  C      . ILE A 1 246 ? 170.479 120.964 166.788 1.00 41.70 ? 389 ILE A C      1 
ATOM   1635 O  O      . ILE A 1 246 ? 169.393 120.666 167.295 1.00 46.24 ? 389 ILE A O      1 
ATOM   1636 C  CB     . ILE A 1 246 ? 169.995 123.110 165.543 1.00 38.17 ? 389 ILE A CB     1 
ATOM   1637 C  CG1    . ILE A 1 246 ? 169.839 123.715 164.151 1.00 38.34 ? 389 ILE A CG1    1 
ATOM   1638 C  CG2    . ILE A 1 246 ? 170.916 123.973 166.384 1.00 36.17 ? 389 ILE A CG2    1 
ATOM   1639 C  CD1    . ILE A 1 246 ? 169.396 125.153 164.161 1.00 30.65 ? 389 ILE A CD1    1 
ATOM   1640 N  N      . THR A 1 247 ? 171.643 120.693 167.364 1.00 41.83 ? 390 THR A N      1 
ATOM   1641 C  CA     . THR A 1 247 ? 171.748 119.936 168.602 1.00 43.63 ? 390 THR A CA     1 
ATOM   1642 C  C      . THR A 1 247 ? 172.010 120.863 169.784 1.00 42.48 ? 390 THR A C      1 
ATOM   1643 O  O      . THR A 1 247 ? 172.254 122.060 169.632 1.00 44.08 ? 390 THR A O      1 
ATOM   1644 C  CB     . THR A 1 247 ? 172.855 118.882 168.500 1.00 44.95 ? 390 THR A CB     1 
ATOM   1645 O  OG1    . THR A 1 247 ? 174.109 119.524 168.248 1.00 45.63 ? 390 THR A OG1    1 
ATOM   1646 C  CG2    . THR A 1 247 ? 172.563 117.916 167.369 1.00 43.46 ? 390 THR A CG2    1 
ATOM   1647 N  N      . MET A 1 248 ? 171.947 120.285 170.983 1.00 43.63 ? 391 MET A N      1 
ATOM   1648 C  CA     . MET A 1 248 ? 172.175 121.063 172.194 1.00 42.91 ? 391 MET A CA     1 
ATOM   1649 C  C      . MET A 1 248 ? 173.606 121.576 172.278 1.00 43.37 ? 391 MET A C      1 
ATOM   1650 O  O      . MET A 1 248 ? 173.849 122.635 172.864 1.00 42.62 ? 391 MET A O      1 
ATOM   1651 C  CB     . MET A 1 248 ? 171.838 120.223 173.424 1.00 44.08 ? 391 MET A CB     1 
ATOM   1652 C  CG     . MET A 1 248 ? 171.846 120.997 174.727 1.00 48.38 ? 391 MET A CG     1 
ATOM   1653 S  SD     . MET A 1 248 ? 170.480 122.169 174.846 1.00 51.60 ? 391 MET A SD     1 
ATOM   1654 C  CE     . MET A 1 248 ? 170.833 122.939 176.416 1.00 41.29 ? 391 MET A CE     1 
ATOM   1655 N  N      . LYS A 1 249 ? 174.563 120.840 171.712 1.00 44.18 ? 392 LYS A N      1 
ATOM   1656 C  CA     . LYS A 1 249 ? 175.953 121.282 171.738 1.00 44.52 ? 392 LYS A CA     1 
ATOM   1657 C  C      . LYS A 1 249 ? 176.178 122.493 170.842 1.00 44.39 ? 392 LYS A C      1 
ATOM   1658 O  O      . LYS A 1 249 ? 177.059 123.312 171.122 1.00 44.79 ? 392 LYS A O      1 
ATOM   1659 C  CB     . LYS A 1 249 ? 176.869 120.131 171.330 1.00 46.10 ? 392 LYS A CB     1 
ATOM   1660 C  CG     . LYS A 1 249 ? 178.343 120.416 171.503 1.00 50.49 ? 392 LYS A CG     1 
ATOM   1661 C  CD     . LYS A 1 249 ? 179.187 119.223 171.095 1.00 55.69 ? 392 LYS A CD     1 
ATOM   1662 C  CE     . LYS A 1 249 ? 178.942 118.832 169.646 1.00 60.66 ? 392 LYS A CE     1 
ATOM   1663 N  NZ     . LYS A 1 249 ? 179.237 119.944 168.702 1.00 59.14 ? 392 LYS A NZ     1 
ATOM   1664 N  N      . ASP A 1 250 ? 175.404 122.621 169.762 1.00 41.70 ? 393 ASP A N      1 
ATOM   1665 C  CA     . ASP A 1 250 ? 175.504 123.804 168.912 1.00 39.05 ? 393 ASP A CA     1 
ATOM   1666 C  C      . ASP A 1 250 ? 175.099 125.065 169.664 1.00 38.74 ? 393 ASP A C      1 
ATOM   1667 O  O      . ASP A 1 250 ? 175.723 126.119 169.504 1.00 38.80 ? 393 ASP A O      1 
ATOM   1668 C  CB     . ASP A 1 250 ? 174.641 123.629 167.665 1.00 38.41 ? 393 ASP A CB     1 
ATOM   1669 C  CG     . ASP A 1 250 ? 175.222 122.633 166.690 1.00 46.16 ? 393 ASP A CG     1 
ATOM   1670 O  OD1    . ASP A 1 250 ? 176.455 122.445 166.696 1.00 48.94 ? 393 ASP A OD1    1 
ATOM   1671 O  OD2    . ASP A 1 250 ? 174.450 122.033 165.918 1.00 45.89 ? 393 ASP A OD2    1 
ATOM   1672 N  N      . PHE A 1 251 ? 174.045 124.982 170.478 1.00 36.98 ? 394 PHE A N      1 
ATOM   1673 C  CA     . PHE A 1 251 ? 173.586 126.150 171.219 1.00 34.28 ? 394 PHE A CA     1 
ATOM   1674 C  C      . PHE A 1 251 ? 174.602 126.587 172.266 1.00 35.44 ? 394 PHE A C      1 
ATOM   1675 O  O      . PHE A 1 251 ? 174.820 127.785 172.462 1.00 36.25 ? 394 PHE A O      1 
ATOM   1676 C  CB     . PHE A 1 251 ? 172.234 125.863 171.872 1.00 32.59 ? 394 PHE A CB     1 
ATOM   1677 C  CG     . PHE A 1 251 ? 171.061 126.219 171.012 1.00 31.06 ? 394 PHE A CG     1 
ATOM   1678 C  CD1    . PHE A 1 251 ? 170.674 127.537 170.857 1.00 28.62 ? 394 PHE A CD1    1 
ATOM   1679 C  CD2    . PHE A 1 251 ? 170.346 125.239 170.356 1.00 31.10 ? 394 PHE A CD2    1 
ATOM   1680 C  CE1    . PHE A 1 251 ? 169.600 127.867 170.062 1.00 27.82 ? 394 PHE A CE1    1 
ATOM   1681 C  CE2    . PHE A 1 251 ? 169.269 125.562 169.562 1.00 31.04 ? 394 PHE A CE2    1 
ATOM   1682 C  CZ     . PHE A 1 251 ? 168.896 126.878 169.414 1.00 28.47 ? 394 PHE A CZ     1 
ATOM   1683 N  N      . GLU A 1 252 ? 175.222 125.630 172.959 1.00 38.08 ? 395 GLU A N      1 
ATOM   1684 C  CA     . GLU A 1 252 ? 176.179 125.981 174.001 1.00 37.87 ? 395 GLU A CA     1 
ATOM   1685 C  C      . GLU A 1 252 ? 177.447 126.602 173.430 1.00 37.65 ? 395 GLU A C      1 
ATOM   1686 O  O      . GLU A 1 252 ? 178.024 127.502 174.049 1.00 37.63 ? 395 GLU A O      1 
ATOM   1687 C  CB     . GLU A 1 252 ? 176.520 124.752 174.839 1.00 41.38 ? 395 GLU A CB     1 
ATOM   1688 C  CG     . GLU A 1 252 ? 175.564 124.521 175.992 1.00 47.37 ? 395 GLU A CG     1 
ATOM   1689 C  CD     . GLU A 1 252 ? 175.369 123.055 176.310 1.00 57.83 ? 395 GLU A CD     1 
ATOM   1690 O  OE1    . GLU A 1 252 ? 176.085 122.216 175.725 1.00 60.15 ? 395 GLU A OE1    1 
ATOM   1691 O  OE2    . GLU A 1 252 ? 174.501 122.738 177.147 1.00 58.12 ? 395 GLU A OE2    1 
ATOM   1692 N  N      . GLU A 1 253 ? 177.905 126.135 172.269 1.00 37.57 ? 396 GLU A N      1 
ATOM   1693 C  CA     . GLU A 1 253 ? 179.084 126.730 171.652 1.00 35.90 ? 396 GLU A CA     1 
ATOM   1694 C  C      . GLU A 1 253 ? 178.803 128.107 171.075 1.00 36.44 ? 396 GLU A C      1 
ATOM   1695 O  O      . GLU A 1 253 ? 179.722 128.925 170.987 1.00 38.53 ? 396 GLU A O      1 
ATOM   1696 C  CB     . GLU A 1 253 ? 179.627 125.818 170.555 1.00 39.08 ? 396 GLU A CB     1 
ATOM   1697 C  CG     . GLU A 1 253 ? 180.533 124.720 171.058 1.00 46.71 ? 396 GLU A CG     1 
ATOM   1698 C  CD     . GLU A 1 253 ? 180.940 123.763 169.961 1.00 59.57 ? 396 GLU A CD     1 
ATOM   1699 O  OE1    . GLU A 1 253 ? 180.384 123.863 168.848 1.00 58.84 ? 396 GLU A OE1    1 
ATOM   1700 O  OE2    . GLU A 1 253 ? 181.812 122.907 170.212 1.00 62.36 ? 396 GLU A OE2    1 
ATOM   1701 N  N      . ALA A 1 254 ? 177.559 128.379 170.677 1.00 35.94 ? 397 ALA A N      1 
ATOM   1702 C  CA     . ALA A 1 254 ? 177.229 129.680 170.108 1.00 29.57 ? 397 ALA A CA     1 
ATOM   1703 C  C      . ALA A 1 254 ? 177.254 130.781 171.158 1.00 30.27 ? 397 ALA A C      1 
ATOM   1704 O  O      . ALA A 1 254 ? 177.495 131.945 170.823 1.00 31.19 ? 397 ALA A O      1 
ATOM   1705 C  CB     . ALA A 1 254 ? 175.862 129.622 169.430 1.00 27.52 ? 397 ALA A CB     1 
ATOM   1706 N  N      . ILE A 1 255 ? 177.009 130.442 172.423 1.00 30.86 ? 398 ILE A N      1 
ATOM   1707 C  CA     . ILE A 1 255 ? 177.022 131.450 173.479 1.00 30.75 ? 398 ILE A CA     1 
ATOM   1708 C  C      . ILE A 1 255 ? 178.412 132.053 173.626 1.00 33.55 ? 398 ILE A C      1 
ATOM   1709 O  O      . ILE A 1 255 ? 178.565 133.268 173.788 1.00 35.03 ? 398 ILE A O      1 
ATOM   1710 C  CB     . ILE A 1 255 ? 176.527 130.844 174.804 1.00 31.58 ? 398 ILE A CB     1 
ATOM   1711 C  CG1    . ILE A 1 255 ? 175.057 130.448 174.693 1.00 29.42 ? 398 ILE A CG1    1 
ATOM   1712 C  CG2    . ILE A 1 255 ? 176.707 131.830 175.933 1.00 25.30 ? 398 ILE A CG2    1 
ATOM   1713 C  CD1    . ILE A 1 255 ? 174.455 129.977 175.988 1.00 26.00 ? 398 ILE A CD1    1 
ATOM   1714 N  N      . ASP A 1 256 ? 179.450 131.214 173.576 1.00 36.35 ? 399 ASP A N      1 
ATOM   1715 C  CA     . ASP A 1 256 ? 180.812 131.702 173.764 1.00 36.32 ? 399 ASP A CA     1 
ATOM   1716 C  C      . ASP A 1 256 ? 181.300 132.520 172.577 1.00 36.81 ? 399 ASP A C      1 
ATOM   1717 O  O      . ASP A 1 256 ? 182.187 133.364 172.735 1.00 40.18 ? 399 ASP A O      1 
ATOM   1718 C  CB     . ASP A 1 256 ? 181.760 130.532 174.011 1.00 39.57 ? 399 ASP A CB     1 
ATOM   1719 C  CG     . ASP A 1 256 ? 181.474 129.819 175.311 1.00 51.84 ? 399 ASP A CG     1 
ATOM   1720 O  OD1    . ASP A 1 256 ? 181.178 130.502 176.314 1.00 52.12 ? 399 ASP A OD1    1 
ATOM   1721 O  OD2    . ASP A 1 256 ? 181.548 128.573 175.334 1.00 56.13 ? 399 ASP A OD2    1 
ATOM   1722 N  N      . ARG A 1 257 ? 180.751 132.282 171.388 1.00 33.80 ? 400 ARG A N      1 
ATOM   1723 C  CA     . ARG A 1 257 ? 181.211 132.997 170.205 1.00 34.44 ? 400 ARG A CA     1 
ATOM   1724 C  C      . ARG A 1 257 ? 180.692 134.427 170.137 1.00 34.39 ? 400 ARG A C      1 
ATOM   1725 O  O      . ARG A 1 257 ? 181.336 135.281 169.521 1.00 40.51 ? 400 ARG A O      1 
ATOM   1726 C  CB     . ARG A 1 257 ? 180.803 132.239 168.944 1.00 36.66 ? 400 ARG A CB     1 
ATOM   1727 C  CG     . ARG A 1 257 ? 181.425 130.867 168.839 1.00 39.12 ? 400 ARG A CG     1 
ATOM   1728 C  CD     . ARG A 1 257 ? 181.005 130.168 167.569 1.00 44.71 ? 400 ARG A CD     1 
ATOM   1729 N  NE     . ARG A 1 257 ? 181.199 131.004 166.393 1.00 53.37 ? 400 ARG A NE     1 
ATOM   1730 C  CZ     . ARG A 1 257 ? 182.078 130.749 165.435 1.00 56.88 ? 400 ARG A CZ     1 
ATOM   1731 N  NH1    . ARG A 1 257 ? 182.862 129.685 165.482 1.00 53.30 ? 400 ARG A NH1    1 
ATOM   1732 N  NH2    . ARG A 1 257 ? 182.172 131.580 164.402 1.00 61.06 ? 400 ARG A NH2    1 
ATOM   1733 N  N      . VAL A 1 258 ? 179.540 134.717 170.747 1.00 32.94 ? 401 VAL A N      1 
ATOM   1734 C  CA     . VAL A 1 258 ? 178.940 136.042 170.603 1.00 32.82 ? 401 VAL A CA     1 
ATOM   1735 C  C      . VAL A 1 258 ? 179.327 137.010 171.713 1.00 31.97 ? 401 VAL A C      1 
ATOM   1736 O  O      . VAL A 1 258 ? 179.029 138.208 171.600 1.00 32.28 ? 401 VAL A O      1 
ATOM   1737 C  CB     . VAL A 1 258 ? 177.401 135.960 170.520 1.00 28.50 ? 401 VAL A CB     1 
ATOM   1738 C  CG1    . VAL A 1 258 ? 176.974 135.138 169.321 1.00 25.89 ? 401 VAL A CG1    1 
ATOM   1739 C  CG2    . VAL A 1 258 ? 176.814 135.386 171.798 1.00 24.17 ? 401 VAL A CG2    1 
ATOM   1740 N  N      . ILE A 1 259 ? 179.989 136.546 172.772 1.00 30.53 ? 402 ILE A N      1 
ATOM   1741 C  CA     . ILE A 1 259 ? 180.326 137.398 173.908 1.00 32.44 ? 402 ILE A CA     1 
ATOM   1742 C  C      . ILE A 1 259 ? 181.810 137.694 174.007 1.00 37.80 ? 402 ILE A C      1 
ATOM   1743 O  O      . ILE A 1 259 ? 182.224 138.391 174.942 1.00 39.27 ? 402 ILE A O      1 
ATOM   1744 C  CB     . ILE A 1 259 ? 179.820 136.800 175.235 1.00 31.24 ? 402 ILE A CB     1 
ATOM   1745 C  CG1    . ILE A 1 259 ? 180.438 135.426 175.483 1.00 31.63 ? 402 ILE A CG1    1 
ATOM   1746 C  CG2    . ILE A 1 259 ? 178.305 136.732 175.253 1.00 26.78 ? 402 ILE A CG2    1 
ATOM   1747 C  CD1    . ILE A 1 259 ? 180.281 134.945 176.897 1.00 29.27 ? 402 ILE A CD1    1 
ATOM   1748 N  N      . ALA A 1 260 ? 182.628 137.198 173.082 1.00 38.85 ? 403 ALA A N      1 
ATOM   1749 C  CA     . ALA A 1 260 ? 184.065 137.420 173.157 1.00 38.71 ? 403 ALA A CA     1 
ATOM   1750 C  C      . ALA A 1 260 ? 184.657 137.407 171.757 1.00 44.31 ? 403 ALA A C      1 
ATOM   1751 O  O      . ALA A 1 260 ? 184.070 136.861 170.820 1.00 46.17 ? 403 ALA A O      1 
ATOM   1752 C  CB     . ALA A 1 260 ? 184.748 136.368 174.035 1.00 36.81 ? 403 ALA A CB     1 
ATOM   1753 N  N      . GLY A 1 261 ? 185.834 138.017 171.628 1.00 43.99 ? 404 GLY A N      1 
ATOM   1754 C  CA     . GLY A 1 261 ? 186.570 138.003 170.387 1.00 45.00 ? 404 GLY A CA     1 
ATOM   1755 C  C      . GLY A 1 261 ? 186.555 139.327 169.651 1.00 44.37 ? 404 GLY A C      1 
ATOM   1756 O  O      . GLY A 1 261 ? 185.956 140.308 170.097 1.00 44.67 ? 404 GLY A O      1 
ATOM   1757 N  N      . PRO A 1 262 ? 187.234 139.381 168.504 1.00 45.81 ? 405 PRO A N      1 
ATOM   1758 C  CA     . PRO A 1 262 ? 187.205 140.605 167.689 1.00 45.32 ? 405 PRO A CA     1 
ATOM   1759 C  C      . PRO A 1 262 ? 185.825 140.958 167.166 1.00 47.39 ? 405 PRO A C      1 
ATOM   1760 O  O      . PRO A 1 262 ? 185.596 142.117 166.802 1.00 46.38 ? 405 PRO A O      1 
ATOM   1761 C  CB     . PRO A 1 262 ? 188.169 140.286 166.537 1.00 39.33 ? 405 PRO A CB     1 
ATOM   1762 C  CG     . PRO A 1 262 ? 188.983 139.146 167.010 1.00 39.15 ? 405 PRO A CG     1 
ATOM   1763 C  CD     . PRO A 1 262 ? 188.121 138.358 167.931 1.00 41.93 ? 405 PRO A CD     1 
ATOM   1764 N  N      . ALA A 1 263 ? 184.899 140.000 167.102 1.00 48.88 ? 406 ALA A N      1 
ATOM   1765 C  CA     . ALA A 1 263 ? 183.537 140.244 166.625 1.00 51.34 ? 406 ALA A CA     1 
ATOM   1766 C  C      . ALA A 1 263 ? 182.560 139.778 167.705 1.00 51.77 ? 406 ALA A C      1 
ATOM   1767 O  O      . ALA A 1 263 ? 181.995 138.686 167.627 1.00 56.05 ? 406 ALA A O      1 
ATOM   1768 C  CB     . ALA A 1 263 ? 183.298 139.539 165.287 1.00 49.47 ? 406 ALA A CB     1 
ATOM   1769 N  N      . ARG A 1 264 ? 182.351 140.623 168.709 1.00 47.35 ? 407 ARG A N      1 
ATOM   1770 C  CA     . ARG A 1 264 ? 181.429 140.342 169.798 1.00 42.44 ? 407 ARG A CA     1 
ATOM   1771 C  C      . ARG A 1 264 ? 180.258 141.310 169.721 1.00 41.40 ? 407 ARG A C      1 
ATOM   1772 O  O      . ARG A 1 264 ? 180.400 142.447 169.264 1.00 39.75 ? 407 ARG A O      1 
ATOM   1773 C  CB     . ARG A 1 264 ? 182.114 140.461 171.166 1.00 37.57 ? 407 ARG A CB     1 
ATOM   1774 C  CG     . ARG A 1 264 ? 182.677 141.835 171.453 1.00 38.29 ? 407 ARG A CG     1 
ATOM   1775 C  CD     . ARG A 1 264 ? 183.021 142.022 172.920 1.00 42.32 ? 407 ARG A CD     1 
ATOM   1776 N  NE     . ARG A 1 264 ? 183.963 143.118 173.115 1.00 46.72 ? 407 ARG A NE     1 
ATOM   1777 C  CZ     . ARG A 1 264 ? 183.652 144.290 173.651 1.00 47.80 ? 407 ARG A CZ     1 
ATOM   1778 N  NH1    . ARG A 1 264 ? 182.425 144.560 174.062 1.00 47.65 ? 407 ARG A NH1    1 
ATOM   1779 N  NH2    . ARG A 1 264 ? 184.596 145.220 173.771 1.00 42.80 ? 407 ARG A NH2    1 
ATOM   1780 N  N      . LYS A 1 265 ? 179.095 140.852 170.177 1.00 39.09 ? 408 LYS A N      1 
ATOM   1781 C  CA     . LYS A 1 265 ? 177.871 141.630 170.050 1.00 32.58 ? 408 LYS A CA     1 
ATOM   1782 C  C      . LYS A 1 265 ? 177.086 141.803 171.339 1.00 33.84 ? 408 LYS A C      1 
ATOM   1783 O  O      . LYS A 1 265 ? 176.271 142.728 171.407 1.00 38.96 ? 408 LYS A O      1 
ATOM   1784 C  CB     . LYS A 1 265 ? 176.946 140.996 169.002 1.00 33.89 ? 408 LYS A CB     1 
ATOM   1785 C  CG     . LYS A 1 265 ? 177.655 140.559 167.738 1.00 36.26 ? 408 LYS A CG     1 
ATOM   1786 C  CD     . LYS A 1 265 ? 177.702 141.685 166.724 1.00 37.85 ? 408 LYS A CD     1 
ATOM   1787 C  CE     . LYS A 1 265 ? 177.899 141.155 165.318 1.00 37.91 ? 408 LYS A CE     1 
ATOM   1788 N  NZ     . LYS A 1 265 ? 179.328 141.171 164.913 1.00 42.69 ? 408 LYS A NZ     1 
ATOM   1789 N  N      . SER A 1 266 ? 177.302 140.977 172.360 1.00 32.00 ? 409 SER A N      1 
ATOM   1790 C  CA     . SER A 1 266 ? 176.405 140.916 173.503 1.00 28.73 ? 409 SER A CA     1 
ATOM   1791 C  C      . SER A 1 266 ? 177.179 140.915 174.814 1.00 28.68 ? 409 SER A C      1 
ATOM   1792 O  O      . SER A 1 266 ? 178.372 140.613 174.850 1.00 32.68 ? 409 SER A O      1 
ATOM   1793 C  CB     . SER A 1 266 ? 175.523 139.672 173.431 1.00 29.53 ? 409 SER A CB     1 
ATOM   1794 O  OG     . SER A 1 266 ? 174.969 139.522 172.141 1.00 31.49 ? 409 SER A OG     1 
ATOM   1795 N  N      . LEU A 1 267 ? 176.475 141.263 175.890 1.00 27.73 ? 410 LEU A N      1 
ATOM   1796 C  CA     . LEU A 1 267 ? 176.981 141.213 177.254 1.00 26.52 ? 410 LEU A CA     1 
ATOM   1797 C  C      . LEU A 1 267 ? 176.011 140.429 178.126 1.00 26.60 ? 410 LEU A C      1 
ATOM   1798 O  O      . LEU A 1 267 ? 174.794 140.565 177.984 1.00 29.42 ? 410 LEU A O      1 
ATOM   1799 C  CB     . LEU A 1 267 ? 177.153 142.620 177.835 1.00 26.74 ? 410 LEU A CB     1 
ATOM   1800 C  CG     . LEU A 1 267 ? 178.393 143.438 177.489 1.00 28.51 ? 410 LEU A CG     1 
ATOM   1801 C  CD1    . LEU A 1 267 ? 178.227 144.855 177.990 1.00 26.14 ? 410 LEU A CD1    1 
ATOM   1802 C  CD2    . LEU A 1 267 ? 179.629 142.806 178.084 1.00 28.68 ? 410 LEU A CD2    1 
ATOM   1803 N  N      . LEU A 1 268 ? 176.543 139.621 179.039 1.00 25.84 ? 411 LEU A N      1 
ATOM   1804 C  CA     . LEU A 1 268 ? 175.721 138.907 180.005 1.00 25.10 ? 411 LEU A CA     1 
ATOM   1805 C  C      . LEU A 1 268 ? 176.293 139.082 181.406 1.00 26.49 ? 411 LEU A C      1 
ATOM   1806 O  O      . LEU A 1 268 ? 177.446 139.475 181.585 1.00 32.49 ? 411 LEU A O      1 
ATOM   1807 C  CB     . LEU A 1 268 ? 175.589 137.414 179.663 1.00 26.11 ? 411 LEU A CB     1 
ATOM   1808 C  CG     . LEU A 1 268 ? 176.811 136.497 179.633 1.00 23.62 ? 411 LEU A CG     1 
ATOM   1809 C  CD1    . LEU A 1 268 ? 177.087 135.917 180.994 1.00 24.65 ? 411 LEU A CD1    1 
ATOM   1810 C  CD2    . LEU A 1 268 ? 176.553 135.384 178.652 1.00 26.05 ? 411 LEU A CD2    1 
ATOM   1811 N  N      . ILE A 1 269 ? 175.456 138.802 182.399 1.00 24.75 ? 412 ILE A N      1 
ATOM   1812 C  CA     . ILE A 1 269 ? 175.840 138.940 183.800 1.00 25.67 ? 412 ILE A CA     1 
ATOM   1813 C  C      . ILE A 1 269 ? 176.510 137.655 184.270 1.00 27.27 ? 412 ILE A C      1 
ATOM   1814 O  O      . ILE A 1 269 ? 175.918 136.573 184.208 1.00 29.30 ? 412 ILE A O      1 
ATOM   1815 C  CB     . ILE A 1 269 ? 174.616 139.276 184.666 1.00 24.12 ? 412 ILE A CB     1 
ATOM   1816 C  CG1    . ILE A 1 269 ? 173.873 140.483 184.092 1.00 21.03 ? 412 ILE A CG1    1 
ATOM   1817 C  CG2    . ILE A 1 269 ? 175.031 139.533 186.100 1.00 23.80 ? 412 ILE A CG2    1 
ATOM   1818 C  CD1    . ILE A 1 269 ? 172.470 140.633 184.594 1.00 16.70 ? 412 ILE A CD1    1 
ATOM   1819 N  N      . SER A 1 270 ? 177.746 137.774 184.744 1.00 28.59 ? 413 SER A N      1 
ATOM   1820 C  CA     . SER A 1 270 ? 178.489 136.624 185.234 1.00 27.91 ? 413 SER A CA     1 
ATOM   1821 C  C      . SER A 1 270 ? 178.087 136.280 186.665 1.00 28.76 ? 413 SER A C      1 
ATOM   1822 O  O      . SER A 1 270 ? 177.505 137.101 187.374 1.00 29.58 ? 413 SER A O      1 
ATOM   1823 C  CB     . SER A 1 270 ? 179.987 136.891 185.165 1.00 26.67 ? 413 SER A CB     1 
ATOM   1824 O  OG     . SER A 1 270 ? 180.354 137.991 185.973 1.00 26.20 ? 413 SER A OG     1 
ATOM   1825 N  N      . PRO A 1 271 ? 178.390 135.060 187.113 1.00 30.76 ? 414 PRO A N      1 
ATOM   1826 C  CA     . PRO A 1 271 ? 178.020 134.669 188.483 1.00 29.01 ? 414 PRO A CA     1 
ATOM   1827 C  C      . PRO A 1 271 ? 178.596 135.568 189.564 1.00 27.94 ? 414 PRO A C      1 
ATOM   1828 O  O      . PRO A 1 271 ? 177.965 135.733 190.613 1.00 26.21 ? 414 PRO A O      1 
ATOM   1829 C  CB     . PRO A 1 271 ? 178.561 133.237 188.589 1.00 30.43 ? 414 PRO A CB     1 
ATOM   1830 C  CG     . PRO A 1 271 ? 178.611 132.752 187.182 1.00 32.04 ? 414 PRO A CG     1 
ATOM   1831 C  CD     . PRO A 1 271 ? 178.974 133.941 186.355 1.00 29.62 ? 414 PRO A CD     1 
ATOM   1832 N  N      . ALA A 1 272 ? 179.786 136.133 189.362 1.00 28.17 ? 415 ALA A N      1 
ATOM   1833 C  CA     . ALA A 1 272 ? 180.343 137.042 190.358 1.00 24.56 ? 415 ALA A CA     1 
ATOM   1834 C  C      . ALA A 1 272 ? 179.577 138.358 190.407 1.00 28.18 ? 415 ALA A C      1 
ATOM   1835 O  O      . ALA A 1 272 ? 179.294 138.875 191.493 1.00 29.43 ? 415 ALA A O      1 
ATOM   1836 C  CB     . ALA A 1 272 ? 181.822 137.292 190.074 1.00 25.58 ? 415 ALA A CB     1 
ATOM   1837 N  N      . GLU A 1 273 ? 179.241 138.922 189.244 1.00 26.96 ? 416 GLU A N      1 
ATOM   1838 C  CA     . GLU A 1 273 ? 178.455 140.151 189.221 1.00 25.43 ? 416 GLU A CA     1 
ATOM   1839 C  C      . GLU A 1 273 ? 177.049 139.926 189.755 1.00 23.03 ? 416 GLU A C      1 
ATOM   1840 O  O      . GLU A 1 273 ? 176.441 140.850 190.300 1.00 22.66 ? 416 GLU A O      1 
ATOM   1841 C  CB     . GLU A 1 273 ? 178.391 140.717 187.803 1.00 25.96 ? 416 GLU A CB     1 
ATOM   1842 C  CG     . GLU A 1 273 ? 179.732 141.077 187.205 1.00 30.08 ? 416 GLU A CG     1 
ATOM   1843 C  CD     . GLU A 1 273 ? 179.627 141.531 185.761 1.00 34.43 ? 416 GLU A CD     1 
ATOM   1844 O  OE1    . GLU A 1 273 ? 179.084 140.772 184.937 1.00 32.14 ? 416 GLU A OE1    1 
ATOM   1845 O  OE2    . GLU A 1 273 ? 180.088 142.644 185.448 1.00 35.08 ? 416 GLU A OE2    1 
ATOM   1846 N  N      . LYS A 1 274 ? 176.523 138.712 189.610 1.00 21.66 ? 417 LYS A N      1 
ATOM   1847 C  CA     . LYS A 1 274 ? 175.173 138.426 190.076 1.00 19.86 ? 417 LYS A CA     1 
ATOM   1848 C  C      . LYS A 1 274 ? 175.058 138.586 191.586 1.00 22.02 ? 417 LYS A C      1 
ATOM   1849 O  O      . LYS A 1 274 ? 174.048 139.088 192.088 1.00 22.86 ? 417 LYS A O      1 
ATOM   1850 C  CB     . LYS A 1 274 ? 174.770 137.017 189.649 1.00 20.94 ? 417 LYS A CB     1 
ATOM   1851 C  CG     . LYS A 1 274 ? 173.331 136.895 189.218 1.00 23.36 ? 417 LYS A CG     1 
ATOM   1852 C  CD     . LYS A 1 274 ? 172.915 135.448 189.091 1.00 25.37 ? 417 LYS A CD     1 
ATOM   1853 C  CE     . LYS A 1 274 ? 173.170 134.923 187.695 1.00 28.85 ? 417 LYS A CE     1 
ATOM   1854 N  NZ     . LYS A 1 274 ? 172.236 133.819 187.354 1.00 35.71 ? 417 LYS A NZ     1 
ATOM   1855 N  N      . ARG A 1 275 ? 176.081 138.159 192.326 1.00 22.38 ? 418 ARG A N      1 
ATOM   1856 C  CA     . ARG A 1 275 ? 176.021 138.197 193.784 1.00 20.45 ? 418 ARG A CA     1 
ATOM   1857 C  C      . ARG A 1 275 ? 175.984 139.627 194.313 1.00 19.97 ? 418 ARG A C      1 
ATOM   1858 O  O      . ARG A 1 275 ? 175.297 139.910 195.298 1.00 21.76 ? 418 ARG A O      1 
ATOM   1859 C  CB     . ARG A 1 275 ? 177.207 137.435 194.369 1.00 26.82 ? 418 ARG A CB     1 
ATOM   1860 C  CG     . ARG A 1 275 ? 177.052 137.077 195.829 1.00 33.45 ? 418 ARG A CG     1 
ATOM   1861 C  CD     . ARG A 1 275 ? 178.092 136.064 196.262 1.00 40.31 ? 418 ARG A CD     1 
ATOM   1862 N  NE     . ARG A 1 275 ? 178.133 135.923 197.712 1.00 44.27 ? 418 ARG A NE     1 
ATOM   1863 C  CZ     . ARG A 1 275 ? 177.351 135.108 198.405 1.00 48.28 ? 418 ARG A CZ     1 
ATOM   1864 N  NH1    . ARG A 1 275 ? 176.471 134.323 197.809 1.00 45.78 ? 418 ARG A NH1    1 
ATOM   1865 N  NH2    . ARG A 1 275 ? 177.457 135.079 199.730 1.00 48.68 ? 418 ARG A NH2    1 
ATOM   1866 N  N      . ILE A 1 276 ? 176.738 140.536 193.693 1.00 19.92 ? 419 ILE A N      1 
ATOM   1867 C  CA     . ILE A 1 276 ? 176.757 141.925 194.140 1.00 18.18 ? 419 ILE A CA     1 
ATOM   1868 C  C      . ILE A 1 276 ? 175.430 142.615 193.843 1.00 19.09 ? 419 ILE A C      1 
ATOM   1869 O  O      . ILE A 1 276 ? 174.966 143.451 194.624 1.00 19.54 ? 419 ILE A O      1 
ATOM   1870 C  CB     . ILE A 1 276 ? 177.937 142.676 193.500 1.00 20.41 ? 419 ILE A CB     1 
ATOM   1871 C  CG1    . ILE A 1 276 ? 179.252 141.969 193.806 1.00 25.41 ? 419 ILE A CG1    1 
ATOM   1872 C  CG2    . ILE A 1 276 ? 177.986 144.105 193.986 1.00 17.67 ? 419 ILE A CG2    1 
ATOM   1873 C  CD1    . ILE A 1 276 ? 180.446 142.604 193.141 1.00 28.84 ? 419 ILE A CD1    1 
ATOM   1874 N  N      . ILE A 1 277 ? 174.818 142.306 192.701 1.00 18.19 ? 420 ILE A N      1 
ATOM   1875 C  CA     . ILE A 1 277 ? 173.546 142.928 192.347 1.00 15.66 ? 420 ILE A CA     1 
ATOM   1876 C  C      . ILE A 1 277 ? 172.440 142.469 193.290 1.00 16.69 ? 420 ILE A C      1 
ATOM   1877 O  O      . ILE A 1 277 ? 171.570 143.255 193.675 1.00 18.00 ? 420 ILE A O      1 
ATOM   1878 C  CB     . ILE A 1 277 ? 173.202 142.639 190.875 1.00 16.40 ? 420 ILE A CB     1 
ATOM   1879 C  CG1    . ILE A 1 277 ? 174.127 143.421 189.946 1.00 16.35 ? 420 ILE A CG1    1 
ATOM   1880 C  CG2    . ILE A 1 277 ? 171.755 142.983 190.575 1.00 15.94 ? 420 ILE A CG2    1 
ATOM   1881 C  CD1    . ILE A 1 277 ? 174.204 142.862 188.553 1.00 15.08 ? 420 ILE A CD1    1 
ATOM   1882 N  N      . ALA A 1 278 ? 172.455 141.193 193.678 1.00 15.62 ? 421 ALA A N      1 
ATOM   1883 C  CA     . ALA A 1 278 ? 171.418 140.673 194.562 1.00 13.97 ? 421 ALA A CA     1 
ATOM   1884 C  C      . ALA A 1 278 ? 171.448 141.356 195.925 1.00 15.53 ? 421 ALA A C      1 
ATOM   1885 O  O      . ALA A 1 278 ? 170.397 141.632 196.509 1.00 16.17 ? 421 ALA A O      1 
ATOM   1886 C  CB     . ALA A 1 278 ? 171.567 139.161 194.713 1.00 14.94 ? 421 ALA A CB     1 
ATOM   1887 N  N      . TYR A 1 279 ? 172.642 141.622 196.454 1.00 14.29 ? 422 TYR A N      1 
ATOM   1888 C  CA     . TYR A 1 279 ? 172.747 142.300 197.740 1.00 14.28 ? 422 TYR A CA     1 
ATOM   1889 C  C      . TYR A 1 279 ? 172.272 143.746 197.658 1.00 14.52 ? 422 TYR A C      1 
ATOM   1890 O  O      . TYR A 1 279 ? 171.731 144.273 198.632 1.00 15.62 ? 422 TYR A O      1 
ATOM   1891 C  CB     . TYR A 1 279 ? 174.189 142.234 198.253 1.00 15.35 ? 422 TYR A CB     1 
ATOM   1892 C  CG     . TYR A 1 279 ? 174.454 141.058 199.163 1.00 17.87 ? 422 TYR A CG     1 
ATOM   1893 C  CD1    . TYR A 1 279 ? 174.079 141.089 200.494 1.00 19.81 ? 422 TYR A CD1    1 
ATOM   1894 C  CD2    . TYR A 1 279 ? 175.061 139.906 198.682 1.00 17.82 ? 422 TYR A CD2    1 
ATOM   1895 C  CE1    . TYR A 1 279 ? 174.307 140.013 201.324 1.00 19.29 ? 422 TYR A CE1    1 
ATOM   1896 C  CE2    . TYR A 1 279 ? 175.294 138.827 199.502 1.00 18.31 ? 422 TYR A CE2    1 
ATOM   1897 C  CZ     . TYR A 1 279 ? 174.913 138.886 200.822 1.00 20.97 ? 422 TYR A CZ     1 
ATOM   1898 O  OH     . TYR A 1 279 ? 175.141 137.814 201.646 1.00 23.81 ? 422 TYR A OH     1 
ATOM   1899 N  N      . HIS A 1 280 ? 172.483 144.403 196.517 1.00 15.27 ? 423 HIS A N      1 
ATOM   1900 C  CA     . HIS A 1 280 ? 172.012 145.773 196.335 1.00 13.23 ? 423 HIS A CA     1 
ATOM   1901 C  C      . HIS A 1 280 ? 170.489 145.847 196.343 1.00 15.58 ? 423 HIS A C      1 
ATOM   1902 O  O      . HIS A 1 280 ? 169.910 146.729 196.984 1.00 15.19 ? 423 HIS A O      1 
ATOM   1903 C  CB     . HIS A 1 280 ? 172.575 146.338 195.031 1.00 13.94 ? 423 HIS A CB     1 
ATOM   1904 C  CG     . HIS A 1 280 ? 172.257 147.782 194.800 1.00 15.08 ? 423 HIS A CG     1 
ATOM   1905 N  ND1    . HIS A 1 280 ? 173.151 148.793 195.073 1.00 15.63 ? 423 HIS A ND1    1 
ATOM   1906 C  CD2    . HIS A 1 280 ? 171.145 148.384 194.323 1.00 15.88 ? 423 HIS A CD2    1 
ATOM   1907 C  CE1    . HIS A 1 280 ? 172.605 149.955 194.769 1.00 14.97 ? 423 HIS A CE1    1 
ATOM   1908 N  NE2    . HIS A 1 280 ? 171.385 149.735 194.317 1.00 17.21 ? 423 HIS A NE2    1 
ATOM   1909 N  N      . GLU A 1 281 ? 169.822 144.935 195.631 1.00 15.00 ? 424 GLU A N      1 
ATOM   1910 C  CA     . GLU A 1 281 ? 168.365 144.957 195.560 1.00 14.07 ? 424 GLU A CA     1 
ATOM   1911 C  C      . GLU A 1 281 ? 167.729 144.586 196.892 1.00 16.36 ? 424 GLU A C      1 
ATOM   1912 O  O      . GLU A 1 281 ? 166.737 145.197 197.302 1.00 18.03 ? 424 GLU A O      1 
ATOM   1913 C  CB     . GLU A 1 281 ? 167.879 144.015 194.459 1.00 14.03 ? 424 GLU A CB     1 
ATOM   1914 C  CG     . GLU A 1 281 ? 168.165 144.498 193.052 1.00 18.56 ? 424 GLU A CG     1 
ATOM   1915 C  CD     . GLU A 1 281 ? 167.904 145.979 192.875 1.00 26.55 ? 424 GLU A CD     1 
ATOM   1916 O  OE1    . GLU A 1 281 ? 166.795 146.436 193.212 1.00 24.29 ? 424 GLU A OE1    1 
ATOM   1917 O  OE2    . GLU A 1 281 ? 168.806 146.691 192.391 1.00 29.14 ? 424 GLU A OE2    1 
ATOM   1918 N  N      . ALA A 1 282 ? 168.266 143.574 197.572 1.00 14.75 ? 425 ALA A N      1 
ATOM   1919 C  CA     . ALA A 1 282 ? 167.738 143.178 198.869 1.00 13.05 ? 425 ALA A CA     1 
ATOM   1920 C  C      . ALA A 1 282 ? 167.964 144.237 199.937 1.00 14.04 ? 425 ALA A C      1 
ATOM   1921 O  O      . ALA A 1 282 ? 167.224 144.269 200.922 1.00 15.33 ? 425 ALA A O      1 
ATOM   1922 C  CB     . ALA A 1 282 ? 168.358 141.853 199.305 1.00 13.52 ? 425 ALA A CB     1 
ATOM   1923 N  N      . GLY A 1 283 ? 168.974 145.091 199.774 1.00 13.98 ? 426 GLY A N      1 
ATOM   1924 C  CA     . GLY A 1 283 ? 169.193 146.158 200.735 1.00 12.80 ? 426 GLY A CA     1 
ATOM   1925 C  C      . GLY A 1 283 ? 168.086 147.196 200.729 1.00 13.01 ? 426 GLY A C      1 
ATOM   1926 O  O      . GLY A 1 283 ? 167.729 147.738 201.777 1.00 13.66 ? 426 GLY A O      1 
ATOM   1927 N  N      . HIS A 1 284 ? 167.544 147.503 199.549 1.00 13.43 ? 427 HIS A N      1 
ATOM   1928 C  CA     . HIS A 1 284 ? 166.407 148.413 199.462 1.00 13.36 ? 427 HIS A CA     1 
ATOM   1929 C  C      . HIS A 1 284 ? 165.176 147.832 200.148 1.00 14.51 ? 427 HIS A C      1 
ATOM   1930 O  O      . HIS A 1 284 ? 164.444 148.547 200.837 1.00 16.27 ? 427 HIS A O      1 
ATOM   1931 C  CB     . HIS A 1 284 ? 166.088 148.722 198.000 1.00 12.55 ? 427 HIS A CB     1 
ATOM   1932 C  CG     . HIS A 1 284 ? 166.970 149.762 197.386 1.00 14.75 ? 427 HIS A CG     1 
ATOM   1933 N  ND1    . HIS A 1 284 ? 167.154 151.007 197.941 1.00 14.46 ? 427 HIS A ND1    1 
ATOM   1934 C  CD2    . HIS A 1 284 ? 167.710 149.744 196.254 1.00 14.72 ? 427 HIS A CD2    1 
ATOM   1935 C  CE1    . HIS A 1 284 ? 167.971 151.710 197.181 1.00 13.43 ? 427 HIS A CE1    1 
ATOM   1936 N  NE2    . HIS A 1 284 ? 168.326 150.965 196.152 1.00 16.18 ? 427 HIS A NE2    1 
ATOM   1937 N  N      . ALA A 1 285 ? 164.931 146.534 199.961 1.00 15.00 ? 428 ALA A N      1 
ATOM   1938 C  CA     . ALA A 1 285 ? 163.707 145.917 200.459 1.00 14.35 ? 428 ALA A CA     1 
ATOM   1939 C  C      . ALA A 1 285 ? 163.684 145.830 201.982 1.00 15.85 ? 428 ALA A C      1 
ATOM   1940 O  O      . ALA A 1 285 ? 162.635 146.027 202.599 1.00 18.08 ? 428 ALA A O      1 
ATOM   1941 C  CB     . ALA A 1 285 ? 163.538 144.532 199.837 1.00 14.43 ? 428 ALA A CB     1 
ATOM   1942 N  N      . VAL A 1 286 ? 164.821 145.514 202.605 1.00 15.45 ? 429 VAL A N      1 
ATOM   1943 C  CA     . VAL A 1 286 ? 164.856 145.358 204.057 1.00 14.24 ? 429 VAL A CA     1 
ATOM   1944 C  C      . VAL A 1 286 ? 164.659 146.699 204.756 1.00 15.26 ? 429 VAL A C      1 
ATOM   1945 O  O      . VAL A 1 286 ? 163.925 146.795 205.744 1.00 18.30 ? 429 VAL A O      1 
ATOM   1946 C  CB     . VAL A 1 286 ? 166.168 144.676 204.491 1.00 15.67 ? 429 VAL A CB     1 
ATOM   1947 C  CG1    . VAL A 1 286 ? 166.349 144.766 205.992 1.00 16.96 ? 429 VAL A CG1    1 
ATOM   1948 C  CG2    . VAL A 1 286 ? 166.177 143.224 204.060 1.00 14.10 ? 429 VAL A CG2    1 
ATOM   1949 N  N      . VAL A 1 287 ? 165.312 147.753 204.265 1.00 14.84 ? 430 VAL A N      1 
ATOM   1950 C  CA     . VAL A 1 287 ? 165.217 149.053 204.921 1.00 14.66 ? 430 VAL A CA     1 
ATOM   1951 C  C      . VAL A 1 287 ? 163.804 149.620 204.807 1.00 16.03 ? 430 VAL A C      1 
ATOM   1952 O  O      . VAL A 1 287 ? 163.321 150.297 205.721 1.00 17.70 ? 430 VAL A O      1 
ATOM   1953 C  CB     . VAL A 1 287 ? 166.272 150.018 204.355 1.00 13.88 ? 430 VAL A CB     1 
ATOM   1954 C  CG1    . VAL A 1 287 ? 166.090 151.403 204.932 1.00 11.11 ? 430 VAL A CG1    1 
ATOM   1955 C  CG2    . VAL A 1 287 ? 167.663 149.512 204.674 1.00 10.68 ? 430 VAL A CG2    1 
ATOM   1956 N  N      . SER A 1 288 ? 163.124 149.371 203.685 1.00 15.76 ? 431 SER A N      1 
ATOM   1957 C  CA     . SER A 1 288 ? 161.756 149.858 203.526 1.00 17.20 ? 431 SER A CA     1 
ATOM   1958 C  C      . SER A 1 288 ? 160.797 149.160 204.481 1.00 19.86 ? 431 SER A C      1 
ATOM   1959 O  O      . SER A 1 288 ? 159.832 149.768 204.953 1.00 26.51 ? 431 SER A O      1 
ATOM   1960 C  CB     . SER A 1 288 ? 161.288 149.677 202.084 1.00 15.78 ? 431 SER A CB     1 
ATOM   1961 O  OG     . SER A 1 288 ? 162.034 150.484 201.198 1.00 18.59 ? 431 SER A OG     1 
ATOM   1962 N  N      . THR A 1 289 ? 161.028 147.878 204.756 1.00 17.74 ? 432 THR A N      1 
ATOM   1963 C  CA     . THR A 1 289 ? 160.155 147.122 205.643 1.00 19.03 ? 432 THR A CA     1 
ATOM   1964 C  C      . THR A 1 289 ? 160.295 147.520 207.107 1.00 21.20 ? 432 THR A C      1 
ATOM   1965 O  O      . THR A 1 289 ? 159.389 147.230 207.893 1.00 23.89 ? 432 THR A O      1 
ATOM   1966 C  CB     . THR A 1 289 ? 160.433 145.625 205.486 1.00 19.31 ? 432 THR A CB     1 
ATOM   1967 O  OG1    . THR A 1 289 ? 160.227 145.242 204.123 1.00 24.38 ? 432 THR A OG1    1 
ATOM   1968 C  CG2    . THR A 1 289 ? 159.526 144.809 206.377 1.00 15.44 ? 432 THR A CG2    1 
ATOM   1969 N  N      . VAL A 1 290 ? 161.379 148.184 207.491 1.00 20.72 ? 433 VAL A N      1 
ATOM   1970 C  CA     . VAL A 1 290 ? 161.659 148.460 208.891 1.00 20.29 ? 433 VAL A CA     1 
ATOM   1971 C  C      . VAL A 1 290 ? 161.263 149.880 209.285 1.00 22.60 ? 433 VAL A C      1 
ATOM   1972 O  O      . VAL A 1 290 ? 160.782 150.098 210.395 1.00 27.21 ? 433 VAL A O      1 
ATOM   1973 C  CB     . VAL A 1 290 ? 163.147 148.182 209.202 1.00 21.22 ? 433 VAL A CB     1 
ATOM   1974 C  CG1    . VAL A 1 290 ? 163.563 148.861 210.492 1.00 17.82 ? 433 VAL A CG1    1 
ATOM   1975 C  CG2    . VAL A 1 290 ? 163.401 146.688 209.275 1.00 18.65 ? 433 VAL A CG2    1 
ATOM   1976 N  N      . VAL A 1 291 ? 161.463 150.859 208.410 1.00 22.06 ? 434 VAL A N      1 
ATOM   1977 C  CA     . VAL A 1 291 ? 161.072 152.233 208.754 1.00 26.36 ? 434 VAL A CA     1 
ATOM   1978 C  C      . VAL A 1 291 ? 159.550 152.343 208.756 1.00 28.88 ? 434 VAL A C      1 
ATOM   1979 O  O      . VAL A 1 291 ? 158.888 151.743 207.892 1.00 29.82 ? 434 VAL A O      1 
ATOM   1980 C  CB     . VAL A 1 291 ? 161.700 153.235 207.784 1.00 25.55 ? 434 VAL A CB     1 
ATOM   1981 C  CG1    . VAL A 1 291 ? 163.194 153.337 208.029 1.00 21.38 ? 434 VAL A CG1    1 
ATOM   1982 C  CG2    . VAL A 1 291 ? 161.404 152.857 206.349 1.00 26.35 ? 434 VAL A CG2    1 
ATOM   1983 N  N      . PRO A 1 292 ? 158.956 153.080 209.701 1.00 31.95 ? 435 PRO A N      1 
ATOM   1984 C  CA     . PRO A 1 292 ? 157.485 153.127 209.791 1.00 32.83 ? 435 PRO A CA     1 
ATOM   1985 C  C      . PRO A 1 292 ? 156.786 153.742 208.589 1.00 34.42 ? 435 PRO A C      1 
ATOM   1986 O  O      . PRO A 1 292 ? 155.678 153.311 208.252 1.00 37.16 ? 435 PRO A O      1 
ATOM   1987 C  CB     . PRO A 1 292 ? 157.242 153.952 211.062 1.00 27.45 ? 435 PRO A CB     1 
ATOM   1988 C  CG     . PRO A 1 292 ? 158.488 154.727 211.261 1.00 32.16 ? 435 PRO A CG     1 
ATOM   1989 C  CD     . PRO A 1 292 ? 159.602 153.871 210.760 1.00 29.13 ? 435 PRO A CD     1 
ATOM   1990 N  N      . ASN A 1 293 ? 157.376 154.741 207.942 1.00 32.40 ? 436 ASN A N      1 
ATOM   1991 C  CA     . ASN A 1 293 ? 156.734 155.404 206.815 1.00 33.56 ? 436 ASN A CA     1 
ATOM   1992 C  C      . ASN A 1 293 ? 157.146 154.833 205.466 1.00 38.12 ? 436 ASN A C      1 
ATOM   1993 O  O      . ASN A 1 293 ? 156.754 155.384 204.435 1.00 43.31 ? 436 ASN A O      1 
ATOM   1994 C  CB     . ASN A 1 293 ? 157.027 156.908 206.842 1.00 33.70 ? 436 ASN A CB     1 
ATOM   1995 C  CG     . ASN A 1 293 ? 156.120 157.662 207.791 1.00 35.87 ? 436 ASN A CG     1 
ATOM   1996 O  OD1    . ASN A 1 293 ? 154.907 157.693 207.609 1.00 39.27 ? 436 ASN A OD1    1 
ATOM   1997 N  ND2    . ASN A 1 293 ? 156.705 158.276 208.809 1.00 33.26 ? 436 ASN A ND2    1 
ATOM   1998 N  N      . GLY A 1 294 ? 157.924 153.755 205.443 1.00 39.44 ? 437 GLY A N      1 
ATOM   1999 C  CA     . GLY A 1 294 ? 158.330 153.171 204.181 1.00 41.84 ? 437 GLY A CA     1 
ATOM   2000 C  C      . GLY A 1 294 ? 157.170 152.527 203.447 1.00 48.31 ? 437 GLY A C      1 
ATOM   2001 O  O      . GLY A 1 294 ? 156.141 152.191 204.030 1.00 49.07 ? 437 GLY A O      1 
ATOM   2002 N  N      . GLU A 1 295 ? 157.347 152.355 202.142 1.00 49.20 ? 438 GLU A N      1 
ATOM   2003 C  CA     . GLU A 1 295 ? 156.306 151.801 201.293 1.00 53.92 ? 438 GLU A CA     1 
ATOM   2004 C  C      . GLU A 1 295 ? 156.380 150.279 201.239 1.00 54.85 ? 438 GLU A C      1 
ATOM   2005 O  O      . GLU A 1 295 ? 157.448 149.690 201.411 1.00 51.81 ? 438 GLU A O      1 
ATOM   2006 C  CB     . GLU A 1 295 ? 156.425 152.373 199.888 1.00 57.03 ? 438 GLU A CB     1 
ATOM   2007 C  CG     . GLU A 1 295 ? 156.174 153.858 199.823 1.00 65.15 ? 438 GLU A CG     1 
ATOM   2008 C  CD     . GLU A 1 295 ? 156.282 154.396 198.420 1.00 80.20 ? 438 GLU A CD     1 
ATOM   2009 O  OE1    . GLU A 1 295 ? 156.703 153.632 197.527 1.00 80.26 ? 438 GLU A OE1    1 
ATOM   2010 O  OE2    . GLU A 1 295 ? 155.942 155.579 198.209 1.00 85.84 ? 438 GLU A OE2    1 
ATOM   2011 N  N      . PRO A 1 296 ? 155.248 149.619 201.007 1.00 56.52 ? 439 PRO A N      1 
ATOM   2012 C  CA     . PRO A 1 296 ? 155.254 148.156 200.906 1.00 57.18 ? 439 PRO A CA     1 
ATOM   2013 C  C      . PRO A 1 296 ? 155.977 147.680 199.657 1.00 52.55 ? 439 PRO A C      1 
ATOM   2014 O  O      . PRO A 1 296 ? 156.021 148.365 198.633 1.00 50.18 ? 439 PRO A O      1 
ATOM   2015 C  CB     . PRO A 1 296 ? 153.763 147.794 200.858 1.00 59.40 ? 439 PRO A CB     1 
ATOM   2016 C  CG     . PRO A 1 296 ? 153.041 149.020 201.323 1.00 56.94 ? 439 PRO A CG     1 
ATOM   2017 C  CD     . PRO A 1 296 ? 153.890 150.175 200.916 1.00 56.70 ? 439 PRO A CD     1 
ATOM   2018 N  N      . VAL A 1 297 ? 156.535 146.477 199.749 1.00 50.46 ? 440 VAL A N      1 
ATOM   2019 C  CA     . VAL A 1 297 ? 157.328 145.881 198.681 1.00 49.43 ? 440 VAL A CA     1 
ATOM   2020 C  C      . VAL A 1 297 ? 156.508 144.779 198.031 1.00 48.93 ? 440 VAL A C      1 
ATOM   2021 O  O      . VAL A 1 297 ? 155.981 143.901 198.722 1.00 50.69 ? 440 VAL A O      1 
ATOM   2022 C  CB     . VAL A 1 297 ? 158.665 145.331 199.212 1.00 45.25 ? 440 VAL A CB     1 
ATOM   2023 C  CG1    . VAL A 1 297 ? 159.530 144.841 198.066 1.00 40.96 ? 440 VAL A CG1    1 
ATOM   2024 C  CG2    . VAL A 1 297 ? 159.395 146.391 200.017 1.00 39.84 ? 440 VAL A CG2    1 
ATOM   2025 N  N      . HIS A 1 298 ? 156.408 144.817 196.702 1.00 46.71 ? 441 HIS A N      1 
ATOM   2026 C  CA     . HIS A 1 298 ? 155.647 143.820 195.966 1.00 50.29 ? 441 HIS A CA     1 
ATOM   2027 C  C      . HIS A 1 298 ? 156.491 142.905 195.091 1.00 51.43 ? 441 HIS A C      1 
ATOM   2028 O  O      . HIS A 1 298 ? 156.004 141.843 194.699 1.00 50.93 ? 441 HIS A O      1 
ATOM   2029 C  CB     . HIS A 1 298 ? 154.588 144.500 195.085 1.00 52.33 ? 441 HIS A CB     1 
ATOM   2030 C  CG     . HIS A 1 298 ? 153.536 145.228 195.861 1.00 65.41 ? 441 HIS A CG     1 
ATOM   2031 N  ND1    . HIS A 1 298 ? 152.727 144.604 196.786 1.00 70.37 ? 441 HIS A ND1    1 
ATOM   2032 C  CD2    . HIS A 1 298 ? 153.160 146.529 195.851 1.00 67.39 ? 441 HIS A CD2    1 
ATOM   2033 C  CE1    . HIS A 1 298 ? 151.901 145.488 197.314 1.00 67.52 ? 441 HIS A CE1    1 
ATOM   2034 N  NE2    . HIS A 1 298 ? 152.142 146.664 196.763 1.00 66.91 ? 441 HIS A NE2    1 
ATOM   2035 N  N      . ARG A 1 299 ? 157.727 143.281 194.770 1.00 49.39 ? 442 ARG A N      1 
ATOM   2036 C  CA     . ARG A 1 299 ? 158.533 142.484 193.856 1.00 42.95 ? 442 ARG A CA     1 
ATOM   2037 C  C      . ARG A 1 299 ? 160.009 142.832 194.003 1.00 40.35 ? 442 ARG A C      1 
ATOM   2038 O  O      . ARG A 1 299 ? 160.361 143.993 194.210 1.00 43.22 ? 442 ARG A O      1 
ATOM   2039 C  CB     . ARG A 1 299 ? 158.075 142.696 192.410 1.00 41.99 ? 442 ARG A CB     1 
ATOM   2040 C  CG     . ARG A 1 299 ? 159.021 142.119 191.393 1.00 46.38 ? 442 ARG A CG     1 
ATOM   2041 C  CD     . ARG A 1 299 ? 158.445 142.132 189.999 1.00 46.63 ? 442 ARG A CD     1 
ATOM   2042 N  NE     . ARG A 1 299 ? 159.483 141.848 189.018 1.00 51.56 ? 442 ARG A NE     1 
ATOM   2043 C  CZ     . ARG A 1 299 ? 159.255 141.543 187.750 1.00 53.43 ? 442 ARG A CZ     1 
ATOM   2044 N  NH1    . ARG A 1 299 ? 158.026 141.414 187.283 1.00 58.68 ? 442 ARG A NH1    1 
ATOM   2045 N  NH2    . ARG A 1 299 ? 160.286 141.349 186.935 1.00 47.73 ? 442 ARG A NH2    1 
ATOM   2046 N  N      . ILE A 1 300 ? 160.859 141.811 193.890 1.00 36.23 ? 443 ILE A N      1 
ATOM   2047 C  CA     . ILE A 1 300 ? 162.312 141.957 193.871 1.00 33.54 ? 443 ILE A CA     1 
ATOM   2048 C  C      . ILE A 1 300 ? 162.852 141.132 192.711 1.00 33.77 ? 443 ILE A C      1 
ATOM   2049 O  O      . ILE A 1 300 ? 162.425 139.992 192.503 1.00 36.32 ? 443 ILE A O      1 
ATOM   2050 C  CB     . ILE A 1 300 ? 162.954 141.505 195.200 1.00 31.96 ? 443 ILE A CB     1 
ATOM   2051 C  CG1    . ILE A 1 300 ? 162.093 141.924 196.387 1.00 37.45 ? 443 ILE A CG1    1 
ATOM   2052 C  CG2    . ILE A 1 300 ? 164.348 142.081 195.349 1.00 29.07 ? 443 ILE A CG2    1 
ATOM   2053 C  CD1    . ILE A 1 300 ? 162.528 141.312 197.690 1.00 35.31 ? 443 ILE A CD1    1 
ATOM   2054 N  N      . SER A 1 301 ? 163.789 141.700 191.953 1.00 31.74 ? 444 SER A N      1 
ATOM   2055 C  CA     . SER A 1 301 ? 164.303 141.009 190.778 1.00 28.31 ? 444 SER A CA     1 
ATOM   2056 C  C      . SER A 1 301 ? 165.720 141.461 190.458 1.00 25.81 ? 444 SER A C      1 
ATOM   2057 O  O      . SER A 1 301 ? 166.186 142.504 190.920 1.00 28.75 ? 444 SER A O      1 
ATOM   2058 C  CB     . SER A 1 301 ? 163.401 141.230 189.561 1.00 28.06 ? 444 SER A CB     1 
ATOM   2059 O  OG     . SER A 1 301 ? 163.723 140.325 188.524 1.00 30.77 ? 444 SER A OG     1 
ATOM   2060 N  N      . ILE A 1 302 ? 166.397 140.651 189.646 1.00 27.24 ? 445 ILE A N      1 
ATOM   2061 C  CA     . ILE A 1 302 ? 167.734 140.975 189.159 1.00 23.69 ? 445 ILE A CA     1 
ATOM   2062 C  C      . ILE A 1 302 ? 167.693 141.860 187.915 1.00 23.11 ? 445 ILE A C      1 
ATOM   2063 O  O      . ILE A 1 302 ? 168.666 142.561 187.626 1.00 21.40 ? 445 ILE A O      1 
ATOM   2064 C  CB     . ILE A 1 302 ? 168.518 139.676 188.884 1.00 25.07 ? 445 ILE A CB     1 
ATOM   2065 C  CG1    . ILE A 1 302 ? 168.718 138.875 190.170 1.00 26.30 ? 445 ILE A CG1    1 
ATOM   2066 C  CG2    . ILE A 1 302 ? 169.862 139.969 188.246 1.00 21.47 ? 445 ILE A CG2    1 
ATOM   2067 C  CD1    . ILE A 1 302 ? 169.700 139.488 191.125 1.00 22.68 ? 445 ILE A CD1    1 
ATOM   2068 N  N      . ILE A 1 303 ? 166.590 141.841 187.170 1.00 22.59 ? 446 ILE A N      1 
ATOM   2069 C  CA     . ILE A 1 303 ? 166.421 142.652 185.964 1.00 22.27 ? 446 ILE A CA     1 
ATOM   2070 C  C      . ILE A 1 303 ? 165.600 143.897 186.288 1.00 22.83 ? 446 ILE A C      1 
ATOM   2071 O  O      . ILE A 1 303 ? 164.584 143.799 186.987 1.00 24.71 ? 446 ILE A O      1 
ATOM   2072 C  CB     . ILE A 1 303 ? 165.760 141.834 184.839 1.00 25.85 ? 446 ILE A CB     1 
ATOM   2073 C  CG1    . ILE A 1 303 ? 166.336 140.414 184.780 1.00 26.74 ? 446 ILE A CG1    1 
ATOM   2074 C  CG2    . ILE A 1 303 ? 165.899 142.536 183.496 1.00 21.65 ? 446 ILE A CG2    1 
ATOM   2075 C  CD1    . ILE A 1 303 ? 167.776 140.339 184.322 1.00 21.42 ? 446 ILE A CD1    1 
ATOM   2076 N  N      . PRO A 1 304 ? 165.993 145.075 185.807 1.00 24.89 ? 447 PRO A N      1 
ATOM   2077 C  CA     . PRO A 1 304 ? 165.195 146.287 186.051 1.00 25.68 ? 447 PRO A CA     1 
ATOM   2078 C  C      . PRO A 1 304 ? 163.836 146.241 185.363 1.00 30.51 ? 447 PRO A C      1 
ATOM   2079 O  O      . PRO A 1 304 ? 163.669 145.629 184.306 1.00 30.23 ? 447 PRO A O      1 
ATOM   2080 C  CB     . PRO A 1 304 ? 166.066 147.411 185.476 1.00 23.04 ? 447 PRO A CB     1 
ATOM   2081 C  CG     . PRO A 1 304 ? 167.411 146.806 185.245 1.00 21.94 ? 447 PRO A CG     1 
ATOM   2082 C  CD     . PRO A 1 304 ? 167.202 145.355 185.019 1.00 21.26 ? 447 PRO A CD     1 
ATOM   2083 N  N      . ARG A 1 305 ? 162.855 146.917 185.973 1.00 32.03 ? 448 ARG A N      1 
ATOM   2084 C  CA     . ARG A 1 305 ? 161.477 146.773 185.510 1.00 32.62 ? 448 ARG A CA     1 
ATOM   2085 C  C      . ARG A 1 305 ? 160.742 148.087 185.263 1.00 35.71 ? 448 ARG A C      1 
ATOM   2086 O  O      . ARG A 1 305 ? 159.939 148.160 184.332 1.00 39.59 ? 448 ARG A O      1 
ATOM   2087 C  CB     . ARG A 1 305 ? 160.695 145.918 186.514 1.00 37.62 ? 448 ARG A CB     1 
ATOM   2088 C  CG     . ARG A 1 305 ? 159.203 145.848 186.264 1.00 37.05 ? 448 ARG A CG     1 
ATOM   2089 C  CD     . ARG A 1 305 ? 158.888 145.481 184.834 1.00 39.57 ? 448 ARG A CD     1 
ATOM   2090 N  NE     . ARG A 1 305 ? 159.181 144.089 184.522 1.00 45.82 ? 448 ARG A NE     1 
ATOM   2091 C  CZ     . ARG A 1 305 ? 158.330 143.086 184.685 1.00 49.71 ? 448 ARG A CZ     1 
ATOM   2092 N  NH1    . ARG A 1 305 ? 157.137 143.275 185.222 1.00 50.45 ? 448 ARG A NH1    1 
ATOM   2093 N  NH2    . ARG A 1 305 ? 158.683 141.866 184.295 1.00 48.70 ? 448 ARG A NH2    1 
ATOM   2094 N  N      . GLY A 1 306 ? 160.975 149.122 186.071 1.00 35.22 ? 449 GLY A N      1 
ATOM   2095 C  CA     . GLY A 1 306 ? 160.221 150.355 185.953 1.00 32.76 ? 449 GLY A CA     1 
ATOM   2096 C  C      . GLY A 1 306 ? 160.956 151.450 185.194 1.00 31.53 ? 449 GLY A C      1 
ATOM   2097 O  O      . GLY A 1 306 ? 162.091 151.293 184.753 1.00 36.22 ? 449 GLY A O      1 
ATOM   2098 N  N      . TYR A 1 307 ? 160.278 152.595 185.051 1.00 28.73 ? 450 TYR A N      1 
ATOM   2099 C  CA     . TYR A 1 307 ? 160.910 153.740 184.402 1.00 29.98 ? 450 TYR A CA     1 
ATOM   2100 C  C      . TYR A 1 307 ? 161.910 154.437 185.317 1.00 31.77 ? 450 TYR A C      1 
ATOM   2101 O  O      . TYR A 1 307 ? 162.861 155.055 184.829 1.00 30.99 ? 450 TYR A O      1 
ATOM   2102 C  CB     . TYR A 1 307 ? 159.857 154.738 183.899 1.00 28.66 ? 450 TYR A CB     1 
ATOM   2103 C  CG     . TYR A 1 307 ? 159.188 155.597 184.956 1.00 32.15 ? 450 TYR A CG     1 
ATOM   2104 C  CD1    . TYR A 1 307 ? 159.753 156.799 185.366 1.00 32.65 ? 450 TYR A CD1    1 
ATOM   2105 C  CD2    . TYR A 1 307 ? 157.974 155.225 185.517 1.00 33.52 ? 450 TYR A CD2    1 
ATOM   2106 C  CE1    . TYR A 1 307 ? 159.146 157.583 186.324 1.00 33.17 ? 450 TYR A CE1    1 
ATOM   2107 C  CE2    . TYR A 1 307 ? 157.359 156.005 186.473 1.00 31.84 ? 450 TYR A CE2    1 
ATOM   2108 C  CZ     . TYR A 1 307 ? 157.948 157.181 186.873 1.00 33.90 ? 450 TYR A CZ     1 
ATOM   2109 O  OH     . TYR A 1 307 ? 157.335 157.958 187.824 1.00 32.96 ? 450 TYR A OH     1 
ATOM   2110 N  N      . LYS A 1 308 ? 161.709 154.369 186.635 1.00 31.63 ? 451 LYS A N      1 
ATOM   2111 C  CA     . LYS A 1 308 ? 162.716 154.878 187.561 1.00 33.31 ? 451 LYS A CA     1 
ATOM   2112 C  C      . LYS A 1 308 ? 163.959 153.997 187.573 1.00 34.17 ? 451 LYS A C      1 
ATOM   2113 O  O      . LYS A 1 308 ? 165.085 154.504 187.609 1.00 33.23 ? 451 LYS A O      1 
ATOM   2114 C  CB     . LYS A 1 308 ? 162.133 154.987 188.968 1.00 37.66 ? 451 LYS A CB     1 
ATOM   2115 C  CG     . LYS A 1 308 ? 161.266 156.203 189.190 1.00 38.77 ? 451 LYS A CG     1 
ATOM   2116 C  CD     . LYS A 1 308 ? 160.702 156.208 190.593 1.00 40.82 ? 451 LYS A CD     1 
ATOM   2117 C  CE     . LYS A 1 308 ? 160.441 157.621 191.072 1.00 45.64 ? 451 LYS A CE     1 
ATOM   2118 N  NZ     . LYS A 1 308 ? 159.868 157.633 192.442 1.00 53.97 ? 451 LYS A NZ     1 
ATOM   2119 N  N      . ALA A 1 309 ? 163.773 152.675 187.550 1.00 33.25 ? 452 ALA A N      1 
ATOM   2120 C  CA     . ALA A 1 309 ? 164.903 151.755 187.524 1.00 28.48 ? 452 ALA A CA     1 
ATOM   2121 C  C      . ALA A 1 309 ? 165.695 151.839 186.228 1.00 30.17 ? 452 ALA A C      1 
ATOM   2122 O  O      . ALA A 1 309 ? 166.866 151.447 186.208 1.00 28.90 ? 452 ALA A O      1 
ATOM   2123 C  CB     . ALA A 1 309 ? 164.418 150.325 187.742 1.00 28.36 ? 452 ALA A CB     1 
ATOM   2124 N  N      . LEU A 1 310 ? 165.091 152.329 185.150 1.00 30.65 ? 453 LEU A N      1 
ATOM   2125 C  CA     . LEU A 1 310 ? 165.778 152.473 183.875 1.00 29.28 ? 453 LEU A CA     1 
ATOM   2126 C  C      . LEU A 1 310 ? 166.475 153.819 183.725 1.00 32.22 ? 453 LEU A C      1 
ATOM   2127 O  O      . LEU A 1 310 ? 167.147 154.039 182.714 1.00 30.69 ? 453 LEU A O      1 
ATOM   2128 C  CB     . LEU A 1 310 ? 164.793 152.268 182.720 1.00 28.32 ? 453 LEU A CB     1 
ATOM   2129 C  CG     . LEU A 1 310 ? 164.159 150.879 182.600 1.00 26.89 ? 453 LEU A CG     1 
ATOM   2130 C  CD1    . LEU A 1 310 ? 163.179 150.835 181.447 1.00 25.16 ? 453 LEU A CD1    1 
ATOM   2131 C  CD2    . LEU A 1 310 ? 165.218 149.803 182.442 1.00 25.30 ? 453 LEU A CD2    1 
ATOM   2132 N  N      . GLY A 1 311 ? 166.330 154.716 184.696 1.00 32.85 ? 454 GLY A N      1 
ATOM   2133 C  CA     . GLY A 1 311 ? 167.037 155.980 184.670 1.00 30.76 ? 454 GLY A CA     1 
ATOM   2134 C  C      . GLY A 1 311 ? 166.349 157.121 183.959 1.00 33.41 ? 454 GLY A C      1 
ATOM   2135 O  O      . GLY A 1 311 ? 167.033 158.012 183.445 1.00 38.40 ? 454 GLY A O      1 
ATOM   2136 N  N      . TYR A 1 312 ? 165.019 157.134 183.911 1.00 31.72 ? 455 TYR A N      1 
ATOM   2137 C  CA     . TYR A 1 312 ? 164.260 158.190 183.254 1.00 32.87 ? 455 TYR A CA     1 
ATOM   2138 C  C      . TYR A 1 312 ? 163.527 159.037 184.285 1.00 34.55 ? 455 TYR A C      1 
ATOM   2139 O  O      . TYR A 1 312 ? 163.058 158.523 185.304 1.00 36.99 ? 455 TYR A O      1 
ATOM   2140 C  CB     . TYR A 1 312 ? 163.242 157.617 182.263 1.00 30.85 ? 455 TYR A CB     1 
ATOM   2141 C  CG     . TYR A 1 312 ? 163.813 156.706 181.202 1.00 28.58 ? 455 TYR A CG     1 
ATOM   2142 C  CD1    . TYR A 1 312 ? 165.051 156.956 180.638 1.00 27.97 ? 455 TYR A CD1    1 
ATOM   2143 C  CD2    . TYR A 1 312 ? 163.103 155.603 180.757 1.00 28.29 ? 455 TYR A CD2    1 
ATOM   2144 C  CE1    . TYR A 1 312 ? 165.570 156.131 179.668 1.00 27.12 ? 455 TYR A CE1    1 
ATOM   2145 C  CE2    . TYR A 1 312 ? 163.614 154.771 179.787 1.00 26.31 ? 455 TYR A CE2    1 
ATOM   2146 C  CZ     . TYR A 1 312 ? 164.848 155.040 179.245 1.00 28.10 ? 455 TYR A CZ     1 
ATOM   2147 O  OH     . TYR A 1 312 ? 165.360 154.213 178.277 1.00 27.39 ? 455 TYR A OH     1 
ATOM   2148 N  N      . THR A 1 313 ? 163.429 160.337 184.019 1.00 37.67 ? 456 THR A N      1 
ATOM   2149 C  CA     . THR A 1 313 ? 162.565 161.213 184.801 1.00 37.89 ? 456 THR A CA     1 
ATOM   2150 C  C      . THR A 1 313 ? 161.239 161.501 184.113 1.00 36.45 ? 456 THR A C      1 
ATOM   2151 O  O      . THR A 1 313 ? 160.242 161.751 184.795 1.00 35.60 ? 456 THR A O      1 
ATOM   2152 C  CB     . THR A 1 313 ? 163.272 162.539 185.108 1.00 39.55 ? 456 THR A CB     1 
ATOM   2153 O  OG1    . THR A 1 313 ? 163.933 163.017 183.934 1.00 45.89 ? 456 THR A OG1    1 
ATOM   2154 C  CG2    . THR A 1 313 ? 164.297 162.346 186.207 1.00 36.30 ? 456 THR A CG2    1 
ATOM   2155 N  N      . LEU A 1 314 ? 161.210 161.465 182.781 1.00 36.08 ? 457 LEU A N      1 
ATOM   2156 C  CA     . LEU A 1 314 ? 159.998 161.588 181.976 1.00 37.35 ? 457 LEU A CA     1 
ATOM   2157 C  C      . LEU A 1 314 ? 159.326 162.949 182.113 1.00 39.50 ? 457 LEU A C      1 
ATOM   2158 O  O      . LEU A 1 314 ? 158.121 163.066 181.884 1.00 40.88 ? 457 LEU A O      1 
ATOM   2159 C  CB     . LEU A 1 314 ? 158.996 160.477 182.307 1.00 36.53 ? 457 LEU A CB     1 
ATOM   2160 C  CG     . LEU A 1 314 ? 159.359 159.048 181.891 1.00 33.44 ? 457 LEU A CG     1 
ATOM   2161 C  CD1    . LEU A 1 314 ? 158.134 158.151 181.926 1.00 29.24 ? 457 LEU A CD1    1 
ATOM   2162 C  CD2    . LEU A 1 314 ? 160.001 159.023 180.520 1.00 28.05 ? 457 LEU A CD2    1 
ATOM   2163 N  N      . HIS A 1 315 ? 160.083 163.985 182.472 1.00 41.65 ? 458 HIS A N      1 
ATOM   2164 C  CA     . HIS A 1 315 ? 159.557 165.348 182.573 1.00 40.56 ? 458 HIS A CA     1 
ATOM   2165 C  C      . HIS A 1 315 ? 158.399 165.429 183.565 1.00 42.19 ? 458 HIS A C      1 
ATOM   2166 O  O      . HIS A 1 315 ? 157.440 166.175 183.366 1.00 44.00 ? 458 HIS A O      1 
ATOM   2167 C  CB     . HIS A 1 315 ? 159.132 165.873 181.200 1.00 40.93 ? 458 HIS A CB     1 
ATOM   2168 C  CG     . HIS A 1 315 ? 160.277 166.214 180.297 1.00 47.76 ? 458 HIS A CG     1 
ATOM   2169 N  ND1    . HIS A 1 315 ? 160.694 165.383 179.279 1.00 48.82 ? 458 HIS A ND1    1 
ATOM   2170 C  CD2    . HIS A 1 315 ? 161.082 167.301 180.249 1.00 45.88 ? 458 HIS A CD2    1 
ATOM   2171 C  CE1    . HIS A 1 315 ? 161.716 165.939 178.652 1.00 45.65 ? 458 HIS A CE1    1 
ATOM   2172 N  NE2    . HIS A 1 315 ? 161.969 167.104 179.219 1.00 48.08 ? 458 HIS A NE2    1 
ATOM   2173 N  N      . LEU A 1 316 ? 158.490 164.663 184.646 1.00 43.18 ? 459 LEU A N      1 
ATOM   2174 C  CA     . LEU A 1 316 ? 157.437 164.648 185.656 1.00 42.92 ? 459 LEU A CA     1 
ATOM   2175 C  C      . LEU A 1 316 ? 157.810 165.513 186.854 1.00 44.92 ? 459 LEU A C      1 
ATOM   2176 O  O      . LEU A 1 316 ? 158.975 165.581 187.245 1.00 48.62 ? 459 LEU A O      1 
ATOM   2177 C  CB     . LEU A 1 316 ? 157.148 163.218 186.115 1.00 41.55 ? 459 LEU A CB     1 
ATOM   2178 C  CG     . LEU A 1 316 ? 156.309 162.346 185.179 1.00 41.47 ? 459 LEU A CG     1 
ATOM   2179 C  CD1    . LEU A 1 316 ? 156.581 160.873 185.428 1.00 35.69 ? 459 LEU A CD1    1 
ATOM   2180 C  CD2    . LEU A 1 316 ? 154.833 162.656 185.330 1.00 40.38 ? 459 LEU A CD2    1 
ATOM   2181 N  N      . ASP A 1 320 ? 155.856 163.949 194.996 1.00 52.71 ? 463 ASP A N      1 
ATOM   2182 C  CA     . ASP A 1 320 ? 154.573 163.566 194.425 1.00 52.00 ? 463 ASP A CA     1 
ATOM   2183 C  C      . ASP A 1 320 ? 153.555 163.219 195.505 1.00 51.03 ? 463 ASP A C      1 
ATOM   2184 O  O      . ASP A 1 320 ? 152.811 162.250 195.381 1.00 48.39 ? 463 ASP A O      1 
ATOM   2185 C  CB     . ASP A 1 320 ? 154.743 162.382 193.481 1.00 56.79 ? 463 ASP A CB     1 
ATOM   2186 C  CG     . ASP A 1 320 ? 155.598 161.287 194.072 1.00 62.43 ? 463 ASP A CG     1 
ATOM   2187 O  OD1    . ASP A 1 320 ? 156.070 161.451 195.216 1.00 59.33 ? 463 ASP A OD1    1 
ATOM   2188 O  OD2    . ASP A 1 320 ? 155.799 160.260 193.392 1.00 65.56 ? 463 ASP A OD2    1 
ATOM   2189 N  N      . LYS A 1 321 ? 153.529 164.018 196.566 1.00 48.00 ? 464 LYS A N      1 
ATOM   2190 C  CA     . LYS A 1 321 ? 152.564 163.861 197.640 1.00 39.52 ? 464 LYS A CA     1 
ATOM   2191 C  C      . LYS A 1 321 ? 151.853 165.185 197.865 1.00 34.19 ? 464 LYS A C      1 
ATOM   2192 O  O      . LYS A 1 321 ? 152.418 166.256 197.639 1.00 35.47 ? 464 LYS A O      1 
ATOM   2193 C  CB     . LYS A 1 321 ? 153.229 163.405 198.942 1.00 39.24 ? 464 LYS A CB     1 
ATOM   2194 C  CG     . LYS A 1 321 ? 153.802 162.009 198.902 1.00 42.90 ? 464 LYS A CG     1 
ATOM   2195 C  CD     . LYS A 1 321 ? 152.705 160.963 198.911 1.00 48.35 ? 464 LYS A CD     1 
ATOM   2196 C  CE     . LYS A 1 321 ? 152.217 160.680 200.318 1.00 55.32 ? 464 LYS A CE     1 
ATOM   2197 N  NZ     . LYS A 1 321 ? 153.342 160.451 201.259 1.00 56.95 ? 464 LYS A NZ     1 
ATOM   2198 N  N      . TYR A 1 322 ? 150.599 165.099 198.305 1.00 30.74 ? 465 TYR A N      1 
ATOM   2199 C  CA     . TYR A 1 322 ? 149.842 166.306 198.616 1.00 25.32 ? 465 TYR A CA     1 
ATOM   2200 C  C      . TYR A 1 322 ? 150.455 167.066 199.787 1.00 27.51 ? 465 TYR A C      1 
ATOM   2201 O  O      . TYR A 1 322 ? 150.535 168.297 199.760 1.00 30.04 ? 465 TYR A O      1 
ATOM   2202 C  CB     . TYR A 1 322 ? 148.387 165.944 198.904 1.00 24.83 ? 465 TYR A CB     1 
ATOM   2203 C  CG     . TYR A 1 322 ? 147.486 167.136 199.101 1.00 28.04 ? 465 TYR A CG     1 
ATOM   2204 C  CD1    . TYR A 1 322 ? 147.315 167.699 200.358 1.00 26.15 ? 465 TYR A CD1    1 
ATOM   2205 C  CD2    . TYR A 1 322 ? 146.805 167.701 198.033 1.00 23.85 ? 465 TYR A CD2    1 
ATOM   2206 C  CE1    . TYR A 1 322 ? 146.501 168.787 200.544 1.00 24.29 ? 465 TYR A CE1    1 
ATOM   2207 C  CE2    . TYR A 1 322 ? 145.985 168.793 198.211 1.00 24.82 ? 465 TYR A CE2    1 
ATOM   2208 C  CZ     . TYR A 1 322 ? 145.836 169.330 199.469 1.00 27.78 ? 465 TYR A CZ     1 
ATOM   2209 O  OH     . TYR A 1 322 ? 145.020 170.416 199.654 1.00 30.32 ? 465 TYR A OH     1 
ATOM   2210 N  N      . LEU A 1 323 ? 150.905 166.352 200.815 1.00 25.38 ? 466 LEU A N      1 
ATOM   2211 C  CA     . LEU A 1 323 ? 151.390 166.953 202.049 1.00 22.48 ? 466 LEU A CA     1 
ATOM   2212 C  C      . LEU A 1 323 ? 152.892 166.751 202.191 1.00 23.82 ? 466 LEU A C      1 
ATOM   2213 O  O      . LEU A 1 323 ? 153.417 165.685 201.859 1.00 30.18 ? 466 LEU A O      1 
ATOM   2214 C  CB     . LEU A 1 323 ? 150.659 166.356 203.255 1.00 21.97 ? 466 LEU A CB     1 
ATOM   2215 C  CG     . LEU A 1 323 ? 151.035 166.866 204.644 1.00 23.13 ? 466 LEU A CG     1 
ATOM   2216 C  CD1    . LEU A 1 323 ? 150.339 168.180 204.921 1.00 22.34 ? 466 LEU A CD1    1 
ATOM   2217 C  CD2    . LEU A 1 323 ? 150.670 165.839 205.694 1.00 18.43 ? 466 LEU A CD2    1 
ATOM   2218 N  N      . VAL A 1 324 ? 153.580 167.774 202.690 1.00 23.62 ? 467 VAL A N      1 
ATOM   2219 C  CA     . VAL A 1 324 ? 155.026 167.749 202.897 1.00 23.95 ? 467 VAL A CA     1 
ATOM   2220 C  C      . VAL A 1 324 ? 155.286 167.676 204.395 1.00 22.84 ? 467 VAL A C      1 
ATOM   2221 O  O      . VAL A 1 324 ? 154.934 168.597 205.139 1.00 26.49 ? 467 VAL A O      1 
ATOM   2222 C  CB     . VAL A 1 324 ? 155.708 168.982 202.282 1.00 24.71 ? 467 VAL A CB     1 
ATOM   2223 C  CG1    . VAL A 1 324 ? 157.212 168.906 202.458 1.00 24.17 ? 467 VAL A CG1    1 
ATOM   2224 C  CG2    . VAL A 1 324 ? 155.339 169.124 200.820 1.00 24.78 ? 467 VAL A CG2    1 
ATOM   2225 N  N      . SER A 1 325 ? 155.923 166.593 204.833 1.00 24.89 ? 468 SER A N      1 
ATOM   2226 C  CA     . SER A 1 325 ? 156.136 166.305 206.243 1.00 21.73 ? 468 SER A CA     1 
ATOM   2227 C  C      . SER A 1 325 ? 157.587 165.903 206.477 1.00 23.59 ? 468 SER A C      1 
ATOM   2228 O  O      . SER A 1 325 ? 158.229 165.317 205.605 1.00 26.33 ? 468 SER A O      1 
ATOM   2229 C  CB     . SER A 1 325 ? 155.192 165.193 206.712 1.00 23.96 ? 468 SER A CB     1 
ATOM   2230 O  OG     . SER A 1 325 ? 155.518 164.744 208.010 1.00 31.00 ? 468 SER A OG     1 
ATOM   2231 N  N      . ARG A 1 326 ? 158.101 166.225 207.666 1.00 21.82 ? 469 ARG A N      1 
ATOM   2232 C  CA     . ARG A 1 326 ? 159.504 165.947 207.969 1.00 21.97 ? 469 ARG A CA     1 
ATOM   2233 C  C      . ARG A 1 326 ? 159.758 164.464 208.221 1.00 21.78 ? 469 ARG A C      1 
ATOM   2234 O  O      . ARG A 1 326 ? 160.781 163.929 207.788 1.00 21.05 ? 469 ARG A O      1 
ATOM   2235 C  CB     . ARG A 1 326 ? 159.964 166.768 209.175 1.00 21.30 ? 469 ARG A CB     1 
ATOM   2236 C  CG     . ARG A 1 326 ? 161.382 166.440 209.634 1.00 21.43 ? 469 ARG A CG     1 
ATOM   2237 C  CD     . ARG A 1 326 ? 161.659 166.882 211.061 1.00 22.55 ? 469 ARG A CD     1 
ATOM   2238 N  NE     . ARG A 1 326 ? 160.978 166.068 212.060 1.00 28.17 ? 469 ARG A NE     1 
ATOM   2239 C  CZ     . ARG A 1 326 ? 160.877 166.389 213.343 1.00 31.12 ? 469 ARG A CZ     1 
ATOM   2240 N  NH1    . ARG A 1 326 ? 161.408 167.502 213.820 1.00 26.89 ? 469 ARG A NH1    1 
ATOM   2241 N  NH2    . ARG A 1 326 ? 160.223 165.577 214.167 1.00 30.02 ? 469 ARG A NH2    1 
ATOM   2242 N  N      . ASN A 1 327 ? 158.852 163.789 208.925 1.00 23.05 ? 470 ASN A N      1 
ATOM   2243 C  CA     . ASN A 1 327 ? 159.086 162.395 209.285 1.00 20.06 ? 470 ASN A CA     1 
ATOM   2244 C  C      . ASN A 1 327 ? 159.075 161.487 208.062 1.00 23.21 ? 470 ASN A C      1 
ATOM   2245 O  O      . ASN A 1 327 ? 159.903 160.579 207.955 1.00 25.38 ? 470 ASN A O      1 
ATOM   2246 C  CB     . ASN A 1 327 ? 158.050 161.937 210.308 1.00 20.32 ? 470 ASN A CB     1 
ATOM   2247 C  CG     . ASN A 1 327 ? 158.417 162.328 211.722 1.00 22.85 ? 470 ASN A CG     1 
ATOM   2248 O  OD1    . ASN A 1 327 ? 159.440 162.965 211.955 1.00 23.65 ? 470 ASN A OD1    1 
ATOM   2249 N  ND2    . ASN A 1 327 ? 157.581 161.950 212.673 1.00 20.10 ? 470 ASN A ND2    1 
ATOM   2250 N  N      . GLU A 1 328 ? 158.141 161.704 207.135 1.00 23.50 ? 471 GLU A N      1 
ATOM   2251 C  CA     . GLU A 1 328 ? 158.068 160.869 205.943 1.00 24.88 ? 471 GLU A CA     1 
ATOM   2252 C  C      . GLU A 1 328 ? 159.149 161.198 204.920 1.00 23.77 ? 471 GLU A C      1 
ATOM   2253 O  O      . GLU A 1 328 ? 159.507 160.330 204.120 1.00 25.13 ? 471 GLU A O      1 
ATOM   2254 C  CB     . GLU A 1 328 ? 156.683 160.980 205.300 1.00 26.51 ? 471 GLU A CB     1 
ATOM   2255 C  CG     . GLU A 1 328 ? 156.314 162.356 204.800 1.00 32.28 ? 471 GLU A CG     1 
ATOM   2256 C  CD     . GLU A 1 328 ? 156.522 162.518 203.306 1.00 39.98 ? 471 GLU A CD     1 
ATOM   2257 O  OE1    . GLU A 1 328 ? 156.631 161.490 202.603 1.00 42.16 ? 471 GLU A OE1    1 
ATOM   2258 O  OE2    . GLU A 1 328 ? 156.560 163.673 202.831 1.00 36.42 ? 471 GLU A OE2    1 
ATOM   2259 N  N      . LEU A 1 329 ? 159.668 162.425 204.920 1.00 23.78 ? 472 LEU A N      1 
ATOM   2260 C  CA     . LEU A 1 329 ? 160.773 162.758 204.031 1.00 22.35 ? 472 LEU A CA     1 
ATOM   2261 C  C      . LEU A 1 329 ? 162.079 162.126 204.493 1.00 21.29 ? 472 LEU A C      1 
ATOM   2262 O  O      . LEU A 1 329 ? 162.903 161.737 203.661 1.00 22.67 ? 472 LEU A O      1 
ATOM   2263 C  CB     . LEU A 1 329 ? 160.928 164.274 203.928 1.00 23.08 ? 472 LEU A CB     1 
ATOM   2264 C  CG     . LEU A 1 329 ? 160.179 164.975 202.795 1.00 29.36 ? 472 LEU A CG     1 
ATOM   2265 C  CD1    . LEU A 1 329 ? 160.627 166.415 202.674 1.00 31.66 ? 472 LEU A CD1    1 
ATOM   2266 C  CD2    . LEU A 1 329 ? 160.363 164.247 201.480 1.00 25.83 ? 472 LEU A CD2    1 
ATOM   2267 N  N      . LEU A 1 330 ? 162.290 162.026 205.805 1.00 19.73 ? 473 LEU A N      1 
ATOM   2268 C  CA     . LEU A 1 330 ? 163.496 161.395 206.328 1.00 18.67 ? 473 LEU A CA     1 
ATOM   2269 C  C      . LEU A 1 330 ? 163.471 159.887 206.123 1.00 18.84 ? 473 LEU A C      1 
ATOM   2270 O  O      . LEU A 1 330 ? 164.513 159.279 205.861 1.00 20.90 ? 473 LEU A O      1 
ATOM   2271 C  CB     . LEU A 1 330 ? 163.661 161.734 207.809 1.00 17.81 ? 473 LEU A CB     1 
ATOM   2272 C  CG     . LEU A 1 330 ? 164.170 163.144 208.111 1.00 17.65 ? 473 LEU A CG     1 
ATOM   2273 C  CD1    . LEU A 1 330 ? 164.450 163.313 209.584 1.00 14.89 ? 473 LEU A CD1    1 
ATOM   2274 C  CD2    . LEU A 1 330 ? 165.408 163.450 207.296 1.00 18.90 ? 473 LEU A CD2    1 
ATOM   2275 N  N      . ASP A 1 331 ? 162.297 159.268 206.247 1.00 19.51 ? 474 ASP A N      1 
ATOM   2276 C  CA     . ASP A 1 331 ? 162.173 157.839 205.996 1.00 17.46 ? 474 ASP A CA     1 
ATOM   2277 C  C      . ASP A 1 331 ? 162.415 157.503 204.534 1.00 18.61 ? 474 ASP A C      1 
ATOM   2278 O  O      . ASP A 1 331 ? 162.916 156.419 204.220 1.00 19.25 ? 474 ASP A O      1 
ATOM   2279 C  CB     . ASP A 1 331 ? 160.791 157.351 206.421 1.00 22.76 ? 474 ASP A CB     1 
ATOM   2280 C  CG     . ASP A 1 331 ? 160.704 157.069 207.899 1.00 31.72 ? 474 ASP A CG     1 
ATOM   2281 O  OD1    . ASP A 1 331 ? 161.710 157.273 208.604 1.00 35.41 ? 474 ASP A OD1    1 
ATOM   2282 O  OD2    . ASP A 1 331 ? 159.625 156.649 208.362 1.00 33.32 ? 474 ASP A OD2    1 
ATOM   2283 N  N      . LYS A 1 332 ? 162.033 158.402 203.630 1.00 18.97 ? 475 LYS A N      1 
ATOM   2284 C  CA     . LYS A 1 332 ? 162.263 158.188 202.208 1.00 16.56 ? 475 LYS A CA     1 
ATOM   2285 C  C      . LYS A 1 332 ? 163.747 158.267 201.872 1.00 16.43 ? 475 LYS A C      1 
ATOM   2286 O  O      . LYS A 1 332 ? 164.243 157.495 201.046 1.00 17.42 ? 475 LYS A O      1 
ATOM   2287 C  CB     . LYS A 1 332 ? 161.461 159.215 201.413 1.00 19.68 ? 475 LYS A CB     1 
ATOM   2288 C  CG     . LYS A 1 332 ? 161.438 159.011 199.924 1.00 22.74 ? 475 LYS A CG     1 
ATOM   2289 C  CD     . LYS A 1 332 ? 160.991 160.278 199.240 1.00 26.34 ? 475 LYS A CD     1 
ATOM   2290 C  CE     . LYS A 1 332 ? 160.912 160.104 197.740 1.00 38.56 ? 475 LYS A CE     1 
ATOM   2291 N  NZ     . LYS A 1 332 ? 160.575 161.386 197.072 1.00 39.46 ? 475 LYS A NZ     1 
ATOM   2292 N  N      . LEU A 1 333 ? 164.467 159.196 202.502 1.00 16.69 ? 476 LEU A N      1 
ATOM   2293 C  CA     . LEU A 1 333 ? 165.903 159.316 202.283 1.00 16.06 ? 476 LEU A CA     1 
ATOM   2294 C  C      . LEU A 1 333 ? 166.648 158.081 202.767 1.00 15.53 ? 476 LEU A C      1 
ATOM   2295 O  O      . LEU A 1 333 ? 167.571 157.606 202.100 1.00 17.10 ? 476 LEU A O      1 
ATOM   2296 C  CB     . LEU A 1 333 ? 166.440 160.557 202.991 1.00 18.92 ? 476 LEU A CB     1 
ATOM   2297 C  CG     . LEU A 1 333 ? 166.471 161.865 202.211 1.00 21.41 ? 476 LEU A CG     1 
ATOM   2298 C  CD1    . LEU A 1 333 ? 166.846 163.005 203.130 1.00 26.49 ? 476 LEU A CD1    1 
ATOM   2299 C  CD2    . LEU A 1 333 ? 167.430 161.773 201.055 1.00 21.87 ? 476 LEU A CD2    1 
ATOM   2300 N  N      . THR A 1 334 ? 166.270 157.556 203.933 1.00 13.92 ? 477 THR A N      1 
ATOM   2301 C  CA     . THR A 1 334 ? 166.976 156.415 204.504 1.00 13.51 ? 477 THR A CA     1 
ATOM   2302 C  C      . THR A 1 334 ? 166.819 155.174 203.634 1.00 11.67 ? 477 THR A C      1 
ATOM   2303 O  O      . THR A 1 334 ? 167.779 154.420 203.445 1.00 11.62 ? 477 THR A O      1 
ATOM   2304 C  CB     . THR A 1 334 ? 166.470 156.161 205.927 1.00 14.43 ? 477 THR A CB     1 
ATOM   2305 O  OG1    . THR A 1 334 ? 166.682 157.334 206.716 1.00 18.55 ? 477 THR A OG1    1 
ATOM   2306 C  CG2    . THR A 1 334 ? 167.208 155.012 206.578 1.00 11.62 ? 477 THR A CG2    1 
ATOM   2307 N  N      . ALA A 1 335 ? 165.622 154.946 203.098 1.00 13.06 ? 478 ALA A N      1 
ATOM   2308 C  CA     . ALA A 1 335 ? 165.394 153.779 202.253 1.00 12.65 ? 478 ALA A CA     1 
ATOM   2309 C  C      . ALA A 1 335 ? 166.094 153.904 200.906 1.00 13.29 ? 478 ALA A C      1 
ATOM   2310 O  O      . ALA A 1 335 ? 166.469 152.891 200.309 1.00 13.72 ? 478 ALA A O      1 
ATOM   2311 C  CB     . ALA A 1 335 ? 163.897 153.559 202.058 1.00 10.17 ? 478 ALA A CB     1 
ATOM   2312 N  N      . LEU A 1 336 ? 166.274 155.128 200.413 1.00 13.06 ? 479 LEU A N      1 
ATOM   2313 C  CA     . LEU A 1 336 ? 166.954 155.347 199.146 1.00 11.79 ? 479 LEU A CA     1 
ATOM   2314 C  C      . LEU A 1 336 ? 168.450 155.076 199.230 1.00 13.43 ? 479 LEU A C      1 
ATOM   2315 O  O      . LEU A 1 336 ? 169.089 154.878 198.192 1.00 16.12 ? 479 LEU A O      1 
ATOM   2316 C  CB     . LEU A 1 336 ? 166.700 156.775 198.668 1.00 13.33 ? 479 LEU A CB     1 
ATOM   2317 C  CG     . LEU A 1 336 ? 167.375 157.263 197.386 1.00 17.60 ? 479 LEU A CG     1 
ATOM   2318 C  CD1    . LEU A 1 336 ? 166.935 156.449 196.187 1.00 18.40 ? 479 LEU A CD1    1 
ATOM   2319 C  CD2    . LEU A 1 336 ? 167.088 158.732 197.172 1.00 18.67 ? 479 LEU A CD2    1 
ATOM   2320 N  N      . LEU A 1 337 ? 169.026 155.068 200.429 1.00 12.78 ? 480 LEU A N      1 
ATOM   2321 C  CA     . LEU A 1 337 ? 170.432 154.752 200.623 1.00 10.68 ? 480 LEU A CA     1 
ATOM   2322 C  C      . LEU A 1 337 ? 170.647 153.319 201.096 1.00 9.59  ? 480 LEU A C      1 
ATOM   2323 O  O      . LEU A 1 337 ? 171.760 152.966 201.481 1.00 11.57 ? 480 LEU A O      1 
ATOM   2324 C  CB     . LEU A 1 337 ? 171.057 155.738 201.610 1.00 10.89 ? 480 LEU A CB     1 
ATOM   2325 C  CG     . LEU A 1 337 ? 171.072 157.209 201.182 1.00 12.45 ? 480 LEU A CG     1 
ATOM   2326 C  CD1    . LEU A 1 337 ? 171.422 158.122 202.339 1.00 13.34 ? 480 LEU A CD1    1 
ATOM   2327 C  CD2    . LEU A 1 337 ? 172.016 157.441 200.019 1.00 12.98 ? 480 LEU A CD2    1 
ATOM   2328 N  N      . GLY A 1 338 ? 169.603 152.491 201.066 1.00 10.47 ? 481 GLY A N      1 
ATOM   2329 C  CA     . GLY A 1 338 ? 169.727 151.123 201.539 1.00 9.67  ? 481 GLY A CA     1 
ATOM   2330 C  C      . GLY A 1 338 ? 170.612 150.250 200.669 1.00 11.00 ? 481 GLY A C      1 
ATOM   2331 O  O      . GLY A 1 338 ? 171.314 149.372 201.173 1.00 11.80 ? 481 GLY A O      1 
ATOM   2332 N  N      . GLY A 1 339 ? 170.560 150.446 199.351 1.00 13.52 ? 482 GLY A N      1 
ATOM   2333 C  CA     . GLY A 1 339 ? 171.405 149.667 198.461 1.00 10.72 ? 482 GLY A CA     1 
ATOM   2334 C  C      . GLY A 1 339 ? 172.881 149.988 198.615 1.00 12.47 ? 482 GLY A C      1 
ATOM   2335 O  O      . GLY A 1 339 ? 173.727 149.094 198.577 1.00 13.48 ? 482 GLY A O      1 
ATOM   2336 N  N      . ARG A 1 340 ? 173.206 151.267 198.784 1.00 13.21 ? 483 ARG A N      1 
ATOM   2337 C  CA     . ARG A 1 340 ? 174.591 151.682 198.963 1.00 12.16 ? 483 ARG A CA     1 
ATOM   2338 C  C      . ARG A 1 340 ? 175.153 151.223 200.302 1.00 14.76 ? 483 ARG A C      1 
ATOM   2339 O  O      . ARG A 1 340 ? 176.361 150.994 200.418 1.00 17.43 ? 483 ARG A O      1 
ATOM   2340 C  CB     . ARG A 1 340 ? 174.689 153.200 198.835 1.00 14.09 ? 483 ARG A CB     1 
ATOM   2341 C  CG     . ARG A 1 340 ? 176.032 153.786 199.180 1.00 17.53 ? 483 ARG A CG     1 
ATOM   2342 C  CD     . ARG A 1 340 ? 176.035 155.276 198.954 1.00 20.65 ? 483 ARG A CD     1 
ATOM   2343 N  NE     . ARG A 1 340 ? 177.356 155.865 199.129 1.00 26.88 ? 483 ARG A NE     1 
ATOM   2344 C  CZ     . ARG A 1 340 ? 178.077 156.401 198.154 1.00 30.92 ? 483 ARG A CZ     1 
ATOM   2345 N  NH1    . ARG A 1 340 ? 177.639 156.431 196.907 1.00 27.58 ? 483 ARG A NH1    1 
ATOM   2346 N  NH2    . ARG A 1 340 ? 179.265 156.924 198.438 1.00 27.81 ? 483 ARG A NH2    1 
ATOM   2347 N  N      . ALA A 1 341 ? 174.304 151.098 201.324 1.00 14.22 ? 484 ALA A N      1 
ATOM   2348 C  CA     . ALA A 1 341 ? 174.775 150.677 202.638 1.00 13.09 ? 484 ALA A CA     1 
ATOM   2349 C  C      . ALA A 1 341 ? 175.120 149.195 202.674 1.00 14.69 ? 484 ALA A C      1 
ATOM   2350 O  O      . ALA A 1 341 ? 176.087 148.806 203.334 1.00 17.75 ? 484 ALA A O      1 
ATOM   2351 C  CB     . ALA A 1 341 ? 173.729 151.006 203.701 1.00 12.33 ? 484 ALA A CB     1 
ATOM   2352 N  N      . ALA A 1 342 ? 174.349 148.356 201.984 1.00 13.22 ? 485 ALA A N      1 
ATOM   2353 C  CA     . ALA A 1 342 ? 174.645 146.929 201.963 1.00 12.71 ? 485 ALA A CA     1 
ATOM   2354 C  C      . ALA A 1 342 ? 175.946 146.628 201.227 1.00 17.29 ? 485 ALA A C      1 
ATOM   2355 O  O      . ALA A 1 342 ? 176.635 145.662 201.564 1.00 22.01 ? 485 ALA A O      1 
ATOM   2356 C  CB     . ALA A 1 342 ? 173.489 146.160 201.330 1.00 10.56 ? 485 ALA A CB     1 
ATOM   2357 N  N      . GLU A 1 343 ? 176.288 147.425 200.213 1.00 17.32 ? 486 GLU A N      1 
ATOM   2358 C  CA     . GLU A 1 343 ? 177.542 147.216 199.496 1.00 18.10 ? 486 GLU A CA     1 
ATOM   2359 C  C      . GLU A 1 343 ? 178.746 147.479 200.389 1.00 18.16 ? 486 GLU A C      1 
ATOM   2360 O  O      . GLU A 1 343 ? 179.736 146.745 200.338 1.00 18.63 ? 486 GLU A O      1 
ATOM   2361 C  CB     . GLU A 1 343 ? 177.601 148.111 198.261 1.00 17.62 ? 486 GLU A CB     1 
ATOM   2362 C  CG     . GLU A 1 343 ? 176.826 147.597 197.074 1.00 18.62 ? 486 GLU A CG     1 
ATOM   2363 C  CD     . GLU A 1 343 ? 176.651 148.652 196.004 1.00 23.03 ? 486 GLU A CD     1 
ATOM   2364 O  OE1    . GLU A 1 343 ? 177.164 149.773 196.182 1.00 23.34 ? 486 GLU A OE1    1 
ATOM   2365 O  OE2    . GLU A 1 343 ? 176.001 148.360 194.984 1.00 23.02 ? 486 GLU A OE2    1 
ATOM   2366 N  N      . GLU A 1 344 ? 178.671 148.541 201.168 1.00 18.77 ? 487 GLU A N      1 
ATOM   2367 C  CA     . GLU A 1 344 ? 179.787 148.956 202.037 1.00 20.42 ? 487 GLU A CA     1 
ATOM   2368 C  C      . GLU A 1 344 ? 179.970 148.020 203.241 1.00 21.56 ? 487 GLU A C      1 
ATOM   2369 O  O      . GLU A 1 344 ? 181.106 147.774 203.579 1.00 22.53 ? 487 GLU A O      1 
ATOM   2370 C  CB     . GLU A 1 344 ? 179.617 150.433 202.368 1.00 19.96 ? 487 GLU A CB     1 
ATOM   2371 C  CG     . GLU A 1 344 ? 179.990 150.778 203.780 1.00 23.70 ? 487 GLU A CG     1 
ATOM   2372 C  CD     . GLU A 1 344 ? 181.084 151.812 203.913 1.00 36.38 ? 487 GLU A CD     1 
ATOM   2373 O  OE1    . GLU A 1 344 ? 180.770 152.986 204.124 1.00 39.30 ? 487 GLU A OE1    1 
ATOM   2374 O  OE2    . GLU A 1 344 ? 182.247 151.432 203.811 1.00 37.39 ? 487 GLU A OE2    1 
ATOM   2375 N  N      . VAL A 1 345 ? 178.903 147.480 203.827 1.00 17.59 ? 488 VAL A N      1 
ATOM   2376 C  CA     . VAL A 1 345 ? 178.996 146.616 204.999 1.00 16.43 ? 488 VAL A CA     1 
ATOM   2377 C  C      . VAL A 1 345 ? 179.437 145.205 204.626 1.00 17.07 ? 488 VAL A C      1 
ATOM   2378 O  O      . VAL A 1 345 ? 180.121 144.540 205.409 1.00 21.97 ? 488 VAL A O      1 
ATOM   2379 C  CB     . VAL A 1 345 ? 177.652 146.611 205.754 1.00 19.43 ? 488 VAL A CB     1 
ATOM   2380 C  CG1    . VAL A 1 345 ? 177.579 145.447 206.715 1.00 17.11 ? 488 VAL A CG1    1 
ATOM   2381 C  CG2    . VAL A 1 345 ? 177.459 147.915 206.503 1.00 18.09 ? 488 VAL A CG2    1 
ATOM   2382 N  N      . VAL A 1 346 ? 179.057 144.719 203.450 1.00 15.99 ? 489 VAL A N      1 
ATOM   2383 C  CA     . VAL A 1 346 ? 179.311 143.336 203.065 1.00 18.19 ? 489 VAL A CA     1 
ATOM   2384 C  C      . VAL A 1 346 ? 180.568 143.200 202.211 1.00 17.59 ? 489 VAL A C      1 
ATOM   2385 O  O      . VAL A 1 346 ? 181.318 142.237 202.366 1.00 18.64 ? 489 VAL A O      1 
ATOM   2386 C  CB     . VAL A 1 346 ? 178.079 142.743 202.347 1.00 19.53 ? 489 VAL A CB     1 
ATOM   2387 C  CG1    . VAL A 1 346 ? 178.350 141.322 201.887 1.00 15.89 ? 489 VAL A CG1    1 
ATOM   2388 C  CG2    . VAL A 1 346 ? 176.874 142.770 203.264 1.00 17.05 ? 489 VAL A CG2    1 
ATOM   2389 N  N      . PHE A 1 347 ? 180.818 144.140 201.297 1.00 18.69 ? 490 PHE A N      1 
ATOM   2390 C  CA     . PHE A 1 347 ? 181.946 144.038 200.381 1.00 19.13 ? 490 PHE A CA     1 
ATOM   2391 C  C      . PHE A 1 347 ? 182.963 145.161 200.495 1.00 20.34 ? 490 PHE A C      1 
ATOM   2392 O  O      . PHE A 1 347 ? 184.101 144.972 200.062 1.00 23.72 ? 490 PHE A O      1 
ATOM   2393 C  CB     . PHE A 1 347 ? 181.469 143.999 198.919 1.00 17.95 ? 490 PHE A CB     1 
ATOM   2394 C  CG     . PHE A 1 347 ? 180.578 142.840 198.592 1.00 18.71 ? 490 PHE A CG     1 
ATOM   2395 C  CD1    . PHE A 1 347 ? 181.105 141.580 198.393 1.00 17.50 ? 490 PHE A CD1    1 
ATOM   2396 C  CD2    . PHE A 1 347 ? 179.214 143.017 198.455 1.00 19.25 ? 490 PHE A CD2    1 
ATOM   2397 C  CE1    . PHE A 1 347 ? 180.286 140.517 198.080 1.00 18.93 ? 490 PHE A CE1    1 
ATOM   2398 C  CE2    . PHE A 1 347 ? 178.392 141.958 198.141 1.00 18.06 ? 490 PHE A CE2    1 
ATOM   2399 C  CZ     . PHE A 1 347 ? 178.928 140.707 197.957 1.00 19.66 ? 490 PHE A CZ     1 
ATOM   2400 N  N      . GLY A 1 348 ? 182.597 146.313 201.040 1.00 19.11 ? 491 GLY A N      1 
ATOM   2401 C  CA     . GLY A 1 348 ? 183.468 147.474 200.995 1.00 17.83 ? 491 GLY A CA     1 
ATOM   2402 C  C      . GLY A 1 348 ? 183.685 148.047 199.609 1.00 22.93 ? 491 GLY A C      1 
ATOM   2403 O  O      . GLY A 1 348 ? 184.803 148.462 199.287 1.00 26.08 ? 491 GLY A O      1 
ATOM   2404 N  N      . ASP A 1 349 ? 182.641 148.093 198.781 1.00 22.55 ? 492 ASP A N      1 
ATOM   2405 C  CA     . ASP A 1 349 ? 182.738 148.558 197.403 1.00 20.15 ? 492 ASP A CA     1 
ATOM   2406 C  C      . ASP A 1 349 ? 181.637 149.577 197.117 1.00 22.36 ? 492 ASP A C      1 
ATOM   2407 O  O      . ASP A 1 349 ? 180.862 149.951 197.998 1.00 25.28 ? 492 ASP A O      1 
ATOM   2408 C  CB     . ASP A 1 349 ? 182.665 147.379 196.423 1.00 20.98 ? 492 ASP A CB     1 
ATOM   2409 C  CG     . ASP A 1 349 ? 183.286 147.698 195.075 1.00 27.19 ? 492 ASP A CG     1 
ATOM   2410 O  OD1    . ASP A 1 349 ? 183.699 148.854 194.865 1.00 26.38 ? 492 ASP A OD1    1 
ATOM   2411 O  OD2    . ASP A 1 349 ? 183.361 146.793 194.225 1.00 29.15 ? 492 ASP A OD2    1 
ATOM   2412 N  N      . VAL A 1 350 ? 181.581 150.034 195.868 1.00 20.35 ? 493 VAL A N      1 
ATOM   2413 C  CA     . VAL A 1 350 ? 180.578 150.996 195.421 1.00 19.54 ? 493 VAL A CA     1 
ATOM   2414 C  C      . VAL A 1 350 ? 180.429 150.866 193.911 1.00 18.06 ? 493 VAL A C      1 
ATOM   2415 O  O      . VAL A 1 350 ? 181.419 150.813 193.181 1.00 19.62 ? 493 VAL A O      1 
ATOM   2416 C  CB     . VAL A 1 350 ? 180.957 152.437 195.842 1.00 17.95 ? 493 VAL A CB     1 
ATOM   2417 C  CG1    . VAL A 1 350 ? 182.255 152.854 195.199 1.00 20.49 ? 493 VAL A CG1    1 
ATOM   2418 C  CG2    . VAL A 1 350 ? 179.851 153.407 195.471 1.00 18.98 ? 493 VAL A CG2    1 
ATOM   2419 N  N      . THR A 1 351 ? 179.183 150.819 193.446 1.00 18.25 ? 494 THR A N      1 
ATOM   2420 C  CA     . THR A 1 351 ? 178.859 150.693 192.032 1.00 16.10 ? 494 THR A CA     1 
ATOM   2421 C  C      . THR A 1 351 ? 178.333 152.019 191.492 1.00 15.67 ? 494 THR A C      1 
ATOM   2422 O  O      . THR A 1 351 ? 178.192 153.003 192.218 1.00 17.33 ? 494 THR A O      1 
ATOM   2423 C  CB     . THR A 1 351 ? 177.841 149.574 191.800 1.00 17.74 ? 494 THR A CB     1 
ATOM   2424 O  OG1    . THR A 1 351 ? 176.683 149.800 192.610 1.00 20.70 ? 494 THR A OG1    1 
ATOM   2425 C  CG2    . THR A 1 351 ? 178.440 148.226 192.141 1.00 16.98 ? 494 THR A CG2    1 
ATOM   2426 N  N      . SER A 1 352 ? 178.052 152.040 190.188 1.00 16.17 ? 495 SER A N      1 
ATOM   2427 C  CA     . SER A 1 352 ? 177.530 153.250 189.561 1.00 15.87 ? 495 SER A CA     1 
ATOM   2428 C  C      . SER A 1 352 ? 176.068 153.491 189.913 1.00 17.01 ? 495 SER A C      1 
ATOM   2429 O  O      . SER A 1 352 ? 175.626 154.643 189.942 1.00 17.76 ? 495 SER A O      1 
ATOM   2430 C  CB     . SER A 1 352 ? 177.707 153.184 188.042 1.00 12.18 ? 495 SER A CB     1 
ATOM   2431 O  OG     . SER A 1 352 ? 177.215 151.968 187.514 1.00 16.07 ? 495 SER A OG     1 
ATOM   2432 N  N      . GLY A 1 353 ? 175.306 152.430 190.173 1.00 16.85 ? 496 GLY A N      1 
ATOM   2433 C  CA     . GLY A 1 353 ? 173.941 152.609 190.633 1.00 16.02 ? 496 GLY A CA     1 
ATOM   2434 C  C      . GLY A 1 353 ? 173.867 153.258 192.001 1.00 17.13 ? 496 GLY A C      1 
ATOM   2435 O  O      . GLY A 1 353 ? 172.976 154.066 192.266 1.00 19.39 ? 496 GLY A O      1 
ATOM   2436 N  N      . ALA A 1 354 ? 174.799 152.911 192.890 1.00 17.03 ? 497 ALA A N      1 
ATOM   2437 C  CA     . ALA A 1 354 ? 174.849 153.533 194.207 1.00 17.32 ? 497 ALA A CA     1 
ATOM   2438 C  C      . ALA A 1 354 ? 175.277 154.991 194.131 1.00 19.55 ? 497 ALA A C      1 
ATOM   2439 O  O      . ALA A 1 354 ? 174.900 155.788 194.994 1.00 20.46 ? 497 ALA A O      1 
ATOM   2440 C  CB     . ALA A 1 354 ? 175.788 152.753 195.124 1.00 16.49 ? 497 ALA A CB     1 
ATOM   2441 N  N      . ALA A 1 355 ? 176.078 155.356 193.128 1.00 19.93 ? 498 ALA A N      1 
ATOM   2442 C  CA     . ALA A 1 355 ? 176.464 156.753 192.956 1.00 18.52 ? 498 ALA A CA     1 
ATOM   2443 C  C      . ALA A 1 355 ? 175.306 157.600 192.443 1.00 20.24 ? 498 ALA A C      1 
ATOM   2444 O  O      . ALA A 1 355 ? 175.207 158.781 192.786 1.00 22.36 ? 498 ALA A O      1 
ATOM   2445 C  CB     . ALA A 1 355 ? 177.664 156.856 192.018 1.00 16.99 ? 498 ALA A CB     1 
ATOM   2446 N  N      . ASN A 1 356 ? 174.434 157.024 191.613 1.00 20.19 ? 499 ASN A N      1 
ATOM   2447 C  CA     . ASN A 1 356 ? 173.225 157.727 191.196 1.00 19.90 ? 499 ASN A CA     1 
ATOM   2448 C  C      . ASN A 1 356 ? 172.293 157.974 192.376 1.00 22.73 ? 499 ASN A C      1 
ATOM   2449 O  O      . ASN A 1 356 ? 171.661 159.031 192.466 1.00 26.25 ? 499 ASN A O      1 
ATOM   2450 C  CB     . ASN A 1 356 ? 172.501 156.937 190.107 1.00 22.00 ? 499 ASN A CB     1 
ATOM   2451 C  CG     . ASN A 1 356 ? 173.162 157.069 188.754 1.00 31.99 ? 499 ASN A CG     1 
ATOM   2452 O  OD1    . ASN A 1 356 ? 173.788 158.081 188.454 1.00 38.32 ? 499 ASN A OD1    1 
ATOM   2453 N  ND2    . ASN A 1 356 ? 173.029 156.040 187.929 1.00 30.62 ? 499 ASN A ND2    1 
ATOM   2454 N  N      . ASP A 1 357 ? 172.185 157.001 193.284 1.00 22.89 ? 500 ASP A N      1 
ATOM   2455 C  CA     . ASP A 1 357 ? 171.310 157.147 194.443 1.00 18.45 ? 500 ASP A CA     1 
ATOM   2456 C  C      . ASP A 1 357 ? 171.751 158.299 195.336 1.00 19.66 ? 500 ASP A C      1 
ATOM   2457 O  O      . ASP A 1 357 ? 170.915 159.044 195.856 1.00 22.99 ? 500 ASP A O      1 
ATOM   2458 C  CB     . ASP A 1 357 ? 171.272 155.842 195.240 1.00 17.76 ? 500 ASP A CB     1 
ATOM   2459 C  CG     . ASP A 1 357 ? 170.532 154.736 194.522 1.00 20.30 ? 500 ASP A CG     1 
ATOM   2460 O  OD1    . ASP A 1 357 ? 169.720 155.039 193.632 1.00 24.34 ? 500 ASP A OD1    1 
ATOM   2461 O  OD2    . ASP A 1 357 ? 170.761 153.556 194.844 1.00 23.37 ? 500 ASP A OD2    1 
ATOM   2462 N  N      . ILE A 1 358 ? 173.060 158.453 195.538 1.00 19.33 ? 501 ILE A N      1 
ATOM   2463 C  CA     . ILE A 1 358 ? 173.562 159.518 196.399 1.00 19.57 ? 501 ILE A CA     1 
ATOM   2464 C  C      . ILE A 1 358 ? 173.293 160.885 195.786 1.00 20.60 ? 501 ILE A C      1 
ATOM   2465 O  O      . ILE A 1 358 ? 173.124 161.873 196.508 1.00 22.04 ? 501 ILE A O      1 
ATOM   2466 C  CB     . ILE A 1 358 ? 175.060 159.308 196.691 1.00 22.60 ? 501 ILE A CB     1 
ATOM   2467 C  CG1    . ILE A 1 358 ? 175.520 160.202 197.838 1.00 23.48 ? 501 ILE A CG1    1 
ATOM   2468 C  CG2    . ILE A 1 358 ? 175.894 159.605 195.470 1.00 24.13 ? 501 ILE A CG2    1 
ATOM   2469 C  CD1    . ILE A 1 358 ? 174.983 159.800 199.172 1.00 22.97 ? 501 ILE A CD1    1 
ATOM   2470 N  N      . GLU A 1 359 ? 173.266 160.976 194.458 1.00 23.36 ? 502 GLU A N      1 
ATOM   2471 C  CA     . GLU A 1 359 ? 172.993 162.248 193.800 1.00 25.63 ? 502 GLU A CA     1 
ATOM   2472 C  C      . GLU A 1 359 ? 171.529 162.655 193.926 1.00 26.46 ? 502 GLU A C      1 
ATOM   2473 O  O      . GLU A 1 359 ? 171.226 163.841 194.083 1.00 28.32 ? 502 GLU A O      1 
ATOM   2474 C  CB     . GLU A 1 359 ? 173.403 162.170 192.331 1.00 29.84 ? 502 GLU A CB     1 
ATOM   2475 C  CG     . GLU A 1 359 ? 173.296 163.483 191.594 1.00 38.67 ? 502 GLU A CG     1 
ATOM   2476 C  CD     . GLU A 1 359 ? 173.712 163.369 190.150 1.00 57.33 ? 502 GLU A CD     1 
ATOM   2477 O  OE1    . GLU A 1 359 ? 174.046 162.248 189.717 1.00 62.16 ? 502 GLU A OE1    1 
ATOM   2478 O  OE2    . GLU A 1 359 ? 173.704 164.397 189.444 1.00 63.22 ? 502 GLU A OE2    1 
ATOM   2479 N  N      . ARG A 1 360 ? 170.607 161.693 193.841 1.00 24.08 ? 503 ARG A N      1 
ATOM   2480 C  CA     . ARG A 1 360 ? 169.193 161.997 194.038 1.00 23.87 ? 503 ARG A CA     1 
ATOM   2481 C  C      . ARG A 1 360 ? 168.904 162.432 195.468 1.00 23.47 ? 503 ARG A C      1 
ATOM   2482 O  O      . ARG A 1 360 ? 168.086 163.328 195.697 1.00 25.22 ? 503 ARG A O      1 
ATOM   2483 C  CB     . ARG A 1 360 ? 168.338 160.786 193.680 1.00 24.45 ? 503 ARG A CB     1 
ATOM   2484 C  CG     . ARG A 1 360 ? 168.011 160.668 192.219 1.00 36.51 ? 503 ARG A CG     1 
ATOM   2485 C  CD     . ARG A 1 360 ? 167.380 159.322 191.925 1.00 47.42 ? 503 ARG A CD     1 
ATOM   2486 N  NE     . ARG A 1 360 ? 166.061 159.201 192.534 1.00 51.35 ? 503 ARG A NE     1 
ATOM   2487 C  CZ     . ARG A 1 360 ? 165.401 158.059 192.673 1.00 51.45 ? 503 ARG A CZ     1 
ATOM   2488 N  NH1    . ARG A 1 360 ? 165.906 156.913 192.249 1.00 43.63 ? 503 ARG A NH1    1 
ATOM   2489 N  NH2    . ARG A 1 360 ? 164.207 158.069 193.256 1.00 48.19 ? 503 ARG A NH2    1 
ATOM   2490 N  N      . ALA A 1 361 ? 169.548 161.795 196.446 1.00 21.20 ? 504 ALA A N      1 
ATOM   2491 C  CA     . ALA A 1 361 ? 169.298 162.133 197.842 1.00 19.62 ? 504 ALA A CA     1 
ATOM   2492 C  C      . ALA A 1 361 ? 169.687 163.574 198.143 1.00 22.86 ? 504 ALA A C      1 
ATOM   2493 O  O      . ALA A 1 361 ? 169.010 164.256 198.918 1.00 25.83 ? 504 ALA A O      1 
ATOM   2494 C  CB     . ALA A 1 361 ? 170.048 161.168 198.758 1.00 16.96 ? 504 ALA A CB     1 
ATOM   2495 N  N      . THR A 1 362 ? 170.781 164.050 197.553 1.00 23.39 ? 505 THR A N      1 
ATOM   2496 C  CA     . THR A 1 362 ? 171.217 165.422 197.787 1.00 23.54 ? 505 THR A CA     1 
ATOM   2497 C  C      . THR A 1 362 ? 170.217 166.430 197.232 1.00 25.93 ? 505 THR A C      1 
ATOM   2498 O  O      . THR A 1 362 ? 170.044 167.514 197.797 1.00 29.24 ? 505 THR A O      1 
ATOM   2499 C  CB     . THR A 1 362 ? 172.603 165.640 197.179 1.00 24.04 ? 505 THR A CB     1 
ATOM   2500 O  OG1    . THR A 1 362 ? 173.538 164.752 197.800 1.00 25.48 ? 505 THR A OG1    1 
ATOM   2501 C  CG2    . THR A 1 362 ? 173.064 167.062 197.389 1.00 25.60 ? 505 THR A CG2    1 
ATOM   2502 N  N      . GLU A 1 363 ? 169.572 166.106 196.112 1.00 25.95 ? 506 GLU A N      1 
ATOM   2503 C  CA     . GLU A 1 363 ? 168.557 166.994 195.556 1.00 26.35 ? 506 GLU A CA     1 
ATOM   2504 C  C      . GLU A 1 363 ? 167.330 167.075 196.456 1.00 27.32 ? 506 GLU A C      1 
ATOM   2505 O  O      . GLU A 1 363 ? 166.751 168.152 196.626 1.00 30.51 ? 506 GLU A O      1 
ATOM   2506 C  CB     . GLU A 1 363 ? 168.170 166.528 194.155 1.00 28.70 ? 506 GLU A CB     1 
ATOM   2507 C  CG     . GLU A 1 363 ? 169.214 166.844 193.103 1.00 37.81 ? 506 GLU A CG     1 
ATOM   2508 C  CD     . GLU A 1 363 ? 169.030 166.039 191.832 1.00 48.18 ? 506 GLU A CD     1 
ATOM   2509 O  OE1    . GLU A 1 363 ? 167.928 165.490 191.625 1.00 52.87 ? 506 GLU A OE1    1 
ATOM   2510 O  OE2    . GLU A 1 363 ? 169.990 165.955 191.040 1.00 48.38 ? 506 GLU A OE2    1 
ATOM   2511 N  N      . ILE A 1 364 ? 166.909 165.946 197.029 1.00 25.53 ? 507 ILE A N      1 
ATOM   2512 C  CA     . ILE A 1 364 ? 165.755 165.947 197.920 1.00 24.78 ? 507 ILE A CA     1 
ATOM   2513 C  C      . ILE A 1 364 ? 166.052 166.744 199.186 1.00 27.13 ? 507 ILE A C      1 
ATOM   2514 O  O      . ILE A 1 364 ? 165.212 167.516 199.659 1.00 28.88 ? 507 ILE A O      1 
ATOM   2515 C  CB     . ILE A 1 364 ? 165.334 164.503 198.245 1.00 24.44 ? 507 ILE A CB     1 
ATOM   2516 C  CG1    . ILE A 1 364 ? 164.670 163.854 197.033 1.00 24.11 ? 507 ILE A CG1    1 
ATOM   2517 C  CG2    . ILE A 1 364 ? 164.391 164.480 199.433 1.00 22.11 ? 507 ILE A CG2    1 
ATOM   2518 C  CD1    . ILE A 1 364 ? 164.531 162.358 197.145 1.00 23.70 ? 507 ILE A CD1    1 
ATOM   2519 N  N      . ALA A 1 365 ? 167.241 166.564 199.759 1.00 24.93 ? 508 ALA A N      1 
ATOM   2520 C  CA     . ALA A 1 365 ? 167.589 167.273 200.985 1.00 24.33 ? 508 ALA A CA     1 
ATOM   2521 C  C      . ALA A 1 365 ? 167.642 168.777 200.763 1.00 29.15 ? 508 ALA A C      1 
ATOM   2522 O  O      . ALA A 1 365 ? 167.272 169.554 201.648 1.00 32.91 ? 508 ALA A O      1 
ATOM   2523 C  CB     . ALA A 1 365 ? 168.925 166.765 201.522 1.00 23.19 ? 508 ALA A CB     1 
ATOM   2524 N  N      . ARG A 1 366 ? 168.114 169.209 199.596 1.00 31.46 ? 509 ARG A N      1 
ATOM   2525 C  CA     . ARG A 1 366 ? 168.208 170.636 199.313 1.00 32.38 ? 509 ARG A CA     1 
ATOM   2526 C  C      . ARG A 1 366 ? 166.830 171.287 199.292 1.00 33.74 ? 509 ARG A C      1 
ATOM   2527 O  O      . ARG A 1 366 ? 166.662 172.417 199.760 1.00 36.96 ? 509 ARG A O      1 
ATOM   2528 C  CB     . ARG A 1 366 ? 168.933 170.848 197.987 1.00 34.69 ? 509 ARG A CB     1 
ATOM   2529 C  CG     . ARG A 1 366 ? 169.336 172.275 197.711 1.00 40.04 ? 509 ARG A CG     1 
ATOM   2530 C  CD     . ARG A 1 366 ? 170.222 172.355 196.483 1.00 45.05 ? 509 ARG A CD     1 
ATOM   2531 N  NE     . ARG A 1 366 ? 171.548 171.799 196.725 1.00 48.59 ? 509 ARG A NE     1 
ATOM   2532 C  CZ     . ARG A 1 366 ? 172.087 170.811 196.025 1.00 50.21 ? 509 ARG A CZ     1 
ATOM   2533 N  NH1    . ARG A 1 366 ? 171.435 170.229 195.032 1.00 47.58 ? 509 ARG A NH1    1 
ATOM   2534 N  NH2    . ARG A 1 366 ? 173.313 170.394 196.330 1.00 45.38 ? 509 ARG A NH2    1 
ATOM   2535 N  N      . ASN A 1 367 ? 165.837 170.593 198.740 1.00 33.02 ? 510 ASN A N      1 
ATOM   2536 C  CA     . ASN A 1 367 ? 164.475 171.111 198.735 1.00 34.23 ? 510 ASN A CA     1 
ATOM   2537 C  C      . ASN A 1 367 ? 163.858 171.090 200.130 1.00 36.95 ? 510 ASN A C      1 
ATOM   2538 O  O      . ASN A 1 367 ? 162.962 171.886 200.423 1.00 38.69 ? 510 ASN A O      1 
ATOM   2539 C  CB     . ASN A 1 367 ? 163.625 170.301 197.759 1.00 34.51 ? 510 ASN A CB     1 
ATOM   2540 C  CG     . ASN A 1 367 ? 162.336 170.996 197.393 1.00 46.94 ? 510 ASN A CG     1 
ATOM   2541 O  OD1    . ASN A 1 367 ? 162.062 172.104 197.849 1.00 51.55 ? 510 ASN A OD1    1 
ATOM   2542 N  ND2    . ASN A 1 367 ? 161.529 170.346 196.566 1.00 49.00 ? 510 ASN A ND2    1 
ATOM   2543 N  N      . MET A 1 368 ? 164.310 170.178 200.993 1.00 36.67 ? 511 MET A N      1 
ATOM   2544 C  CA     . MET A 1 368 ? 163.799 170.117 202.358 1.00 33.96 ? 511 MET A CA     1 
ATOM   2545 C  C      . MET A 1 368 ? 164.205 171.345 203.161 1.00 36.01 ? 511 MET A C      1 
ATOM   2546 O  O      . MET A 1 368 ? 163.426 171.851 203.974 1.00 38.09 ? 511 MET A O      1 
ATOM   2547 C  CB     . MET A 1 368 ? 164.298 168.845 203.040 1.00 32.42 ? 511 MET A CB     1 
ATOM   2548 C  CG     . MET A 1 368 ? 163.778 168.640 204.444 1.00 38.69 ? 511 MET A CG     1 
ATOM   2549 S  SD     . MET A 1 368 ? 164.574 167.257 205.279 1.00 54.30 ? 511 MET A SD     1 
ATOM   2550 C  CE     . MET A 1 368 ? 163.953 165.884 204.318 1.00 34.81 ? 511 MET A CE     1 
ATOM   2551 N  N      . VAL A 1 369 ? 165.430 171.829 202.960 1.00 35.25 ? 512 VAL A N      1 
ATOM   2552 C  CA     . VAL A 1 369 ? 165.927 172.952 203.747 1.00 33.76 ? 512 VAL A CA     1 
ATOM   2553 C  C      . VAL A 1 369 ? 165.141 174.219 203.436 1.00 36.54 ? 512 VAL A C      1 
ATOM   2554 O  O      . VAL A 1 369 ? 164.902 175.048 204.319 1.00 40.03 ? 512 VAL A O      1 
ATOM   2555 C  CB     . VAL A 1 369 ? 167.434 173.144 203.506 1.00 33.32 ? 512 VAL A CB     1 
ATOM   2556 C  CG1    . VAL A 1 369 ? 167.870 174.528 203.944 1.00 38.51 ? 512 VAL A CG1    1 
ATOM   2557 C  CG2    . VAL A 1 369 ? 168.222 172.085 204.242 1.00 33.58 ? 512 VAL A CG2    1 
ATOM   2558 N  N      . SER A 1 370 ? 164.728 174.392 202.185 1.00 35.07 ? 513 SER A N      1 
ATOM   2559 C  CA     . SER A 1 370 ? 164.040 175.608 201.773 1.00 37.74 ? 513 SER A CA     1 
ATOM   2560 C  C      . SER A 1 370 ? 162.539 175.577 202.035 1.00 39.43 ? 513 SER A C      1 
ATOM   2561 O  O      . SER A 1 370 ? 161.883 176.607 201.864 1.00 41.09 ? 513 SER A O      1 
ATOM   2562 C  CB     . SER A 1 370 ? 164.292 175.872 200.288 1.00 39.07 ? 513 SER A CB     1 
ATOM   2563 O  OG     . SER A 1 370 ? 163.418 175.107 199.481 1.00 36.79 ? 513 SER A OG     1 
ATOM   2564 N  N      . GLN A 1 371 ? 161.978 174.446 202.445 1.00 39.26 ? 514 GLN A N      1 
ATOM   2565 C  CA     . GLN A 1 371 ? 160.545 174.337 202.677 1.00 34.54 ? 514 GLN A CA     1 
ATOM   2566 C  C      . GLN A 1 371 ? 160.169 174.091 204.126 1.00 34.44 ? 514 GLN A C      1 
ATOM   2567 O  O      . GLN A 1 371 ? 159.093 174.517 204.544 1.00 36.31 ? 514 GLN A O      1 
ATOM   2568 C  CB     . GLN A 1 371 ? 159.945 173.209 201.828 1.00 33.96 ? 514 GLN A CB     1 
ATOM   2569 C  CG     . GLN A 1 371 ? 159.475 173.650 200.466 1.00 38.62 ? 514 GLN A CG     1 
ATOM   2570 C  CD     . GLN A 1 371 ? 158.614 172.610 199.791 1.00 46.22 ? 514 GLN A CD     1 
ATOM   2571 O  OE1    . GLN A 1 371 ? 157.387 172.675 199.843 1.00 44.59 ? 514 GLN A OE1    1 
ATOM   2572 N  NE2    . GLN A 1 371 ? 159.252 171.638 199.152 1.00 46.43 ? 514 GLN A NE2    1 
ATOM   2573 N  N      . LEU A 1 372 ? 161.009 173.412 204.898 1.00 34.06 ? 515 LEU A N      1 
ATOM   2574 C  CA     . LEU A 1 372 ? 160.714 173.100 206.286 1.00 31.75 ? 515 LEU A CA     1 
ATOM   2575 C  C      . LEU A 1 372 ? 161.492 173.973 207.258 1.00 33.83 ? 515 LEU A C      1 
ATOM   2576 O  O      . LEU A 1 372 ? 161.517 173.678 208.454 1.00 35.79 ? 515 LEU A O      1 
ATOM   2577 C  CB     . LEU A 1 372 ? 161.000 171.624 206.566 1.00 32.94 ? 515 LEU A CB     1 
ATOM   2578 C  CG     . LEU A 1 372 ? 160.004 170.626 205.974 1.00 30.62 ? 515 LEU A CG     1 
ATOM   2579 C  CD1    . LEU A 1 372 ? 160.567 169.222 206.036 1.00 31.64 ? 515 LEU A CD1    1 
ATOM   2580 C  CD2    . LEU A 1 372 ? 158.669 170.698 206.675 1.00 27.35 ? 515 LEU A CD2    1 
ATOM   2581 N  N      . GLY A 1 373 ? 162.128 175.033 206.775 1.00 32.66 ? 516 GLY A N      1 
ATOM   2582 C  CA     . GLY A 1 373 ? 162.914 175.900 207.631 1.00 33.29 ? 516 GLY A CA     1 
ATOM   2583 C  C      . GLY A 1 373 ? 164.398 175.595 207.612 1.00 39.51 ? 516 GLY A C      1 
ATOM   2584 O  O      . GLY A 1 373 ? 164.900 174.836 208.440 1.00 35.75 ? 516 GLY A O      1 
ATOM   2585 N  N      . ILE A 1 410 ? 173.775 176.945 204.252 1.00 56.86 ? 553 ILE A N      1 
ATOM   2586 C  CA     . ILE A 1 410 ? 172.793 176.125 203.553 1.00 58.45 ? 553 ILE A CA     1 
ATOM   2587 C  C      . ILE A 1 410 ? 173.433 174.833 203.070 1.00 58.31 ? 553 ILE A C      1 
ATOM   2588 O  O      . ILE A 1 410 ? 172.886 173.752 203.266 1.00 58.08 ? 553 ILE A O      1 
ATOM   2589 C  CB     . ILE A 1 410 ? 172.162 176.887 202.382 1.00 56.53 ? 553 ILE A CB     1 
ATOM   2590 C  CG1    . ILE A 1 410 ? 171.154 177.913 202.897 1.00 54.21 ? 553 ILE A CG1    1 
ATOM   2591 C  CG2    . ILE A 1 410 ? 171.487 175.925 201.426 1.00 52.50 ? 553 ILE A CG2    1 
ATOM   2592 C  CD1    . ILE A 1 410 ? 170.337 178.556 201.804 1.00 54.23 ? 553 ILE A CD1    1 
ATOM   2593 N  N      . ASP A 1 411 ? 174.597 174.950 202.427 1.00 58.71 ? 554 ASP A N      1 
ATOM   2594 C  CA     . ASP A 1 411 ? 175.328 173.763 202.001 1.00 56.07 ? 554 ASP A CA     1 
ATOM   2595 C  C      . ASP A 1 411 ? 175.778 172.928 203.189 1.00 53.72 ? 554 ASP A C      1 
ATOM   2596 O  O      . ASP A 1 411 ? 175.753 171.695 203.129 1.00 51.46 ? 554 ASP A O      1 
ATOM   2597 C  CB     . ASP A 1 411 ? 176.531 174.163 201.150 1.00 62.37 ? 554 ASP A CB     1 
ATOM   2598 C  CG     . ASP A 1 411 ? 176.135 174.633 199.770 1.00 71.22 ? 554 ASP A CG     1 
ATOM   2599 O  OD1    . ASP A 1 411 ? 175.093 174.170 199.262 1.00 72.05 ? 554 ASP A OD1    1 
ATOM   2600 O  OD2    . ASP A 1 411 ? 176.861 175.468 199.193 1.00 75.93 ? 554 ASP A OD2    1 
ATOM   2601 N  N      . GLU A 1 412 ? 176.209 173.580 204.268 1.00 55.18 ? 555 GLU A N      1 
ATOM   2602 C  CA     . GLU A 1 412 ? 176.572 172.853 205.479 1.00 56.26 ? 555 GLU A CA     1 
ATOM   2603 C  C      . GLU A 1 412 ? 175.369 172.131 206.072 1.00 51.92 ? 555 GLU A C      1 
ATOM   2604 O  O      . GLU A 1 412 ? 175.509 171.045 206.642 1.00 49.34 ? 555 GLU A O      1 
ATOM   2605 C  CB     . GLU A 1 412 ? 177.185 173.820 206.491 1.00 60.11 ? 555 GLU A CB     1 
ATOM   2606 C  CG     . GLU A 1 412 ? 176.240 174.928 206.931 1.00 65.75 ? 555 GLU A CG     1 
ATOM   2607 C  CD     . GLU A 1 412 ? 176.298 176.146 206.019 1.00 72.72 ? 555 GLU A CD     1 
ATOM   2608 O  OE1    . GLU A 1 412 ? 176.890 176.045 204.923 1.00 71.56 ? 555 GLU A OE1    1 
ATOM   2609 O  OE2    . GLU A 1 412 ? 175.743 177.202 206.391 1.00 71.35 ? 555 GLU A OE2    1 
ATOM   2610 N  N      . GLU A 1 413 ? 174.182 172.728 205.966 1.00 50.96 ? 556 GLU A N      1 
ATOM   2611 C  CA     . GLU A 1 413 ? 172.975 172.087 206.477 1.00 48.86 ? 556 GLU A CA     1 
ATOM   2612 C  C      . GLU A 1 413 ? 172.573 170.890 205.622 1.00 45.63 ? 556 GLU A C      1 
ATOM   2613 O  O      . GLU A 1 413 ? 172.118 169.871 206.150 1.00 44.96 ? 556 GLU A O      1 
ATOM   2614 C  CB     . GLU A 1 413 ? 171.840 173.108 206.550 1.00 50.21 ? 556 GLU A CB     1 
ATOM   2615 C  CG     . GLU A 1 413 ? 170.559 172.579 207.166 1.00 52.24 ? 556 GLU A CG     1 
ATOM   2616 C  CD     . GLU A 1 413 ? 170.755 172.079 208.581 1.00 61.51 ? 556 GLU A CD     1 
ATOM   2617 O  OE1    . GLU A 1 413 ? 171.744 172.487 209.223 1.00 63.65 ? 556 GLU A OE1    1 
ATOM   2618 O  OE2    . GLU A 1 413 ? 169.924 171.276 209.051 1.00 59.85 ? 556 GLU A OE2    1 
ATOM   2619 N  N      . VAL A 1 414 ? 172.723 170.999 204.301 1.00 44.81 ? 557 VAL A N      1 
ATOM   2620 C  CA     . VAL A 1 414 ? 172.358 169.898 203.412 1.00 39.83 ? 557 VAL A CA     1 
ATOM   2621 C  C      . VAL A 1 414 ? 173.281 168.707 203.632 1.00 38.44 ? 557 VAL A C      1 
ATOM   2622 O  O      . VAL A 1 414 ? 172.859 167.549 203.555 1.00 37.17 ? 557 VAL A O      1 
ATOM   2623 C  CB     . VAL A 1 414 ? 172.382 170.366 201.946 1.00 41.31 ? 557 VAL A CB     1 
ATOM   2624 C  CG1    . VAL A 1 414 ? 172.376 169.177 201.002 1.00 34.89 ? 557 VAL A CG1    1 
ATOM   2625 C  CG2    . VAL A 1 414 ? 171.214 171.283 201.663 1.00 37.72 ? 557 VAL A CG2    1 
ATOM   2626 N  N      . LYS A 1 415 ? 174.556 168.976 203.906 1.00 41.68 ? 558 LYS A N      1 
ATOM   2627 C  CA     . LYS A 1 415 ? 175.538 167.906 204.033 1.00 40.14 ? 558 LYS A CA     1 
ATOM   2628 C  C      . LYS A 1 415 ? 175.266 167.033 205.251 1.00 36.81 ? 558 LYS A C      1 
ATOM   2629 O  O      . LYS A 1 415 ? 175.466 165.815 205.205 1.00 34.21 ? 558 LYS A O      1 
ATOM   2630 C  CB     . LYS A 1 415 ? 176.940 168.506 204.094 1.00 44.50 ? 558 LYS A CB     1 
ATOM   2631 C  CG     . LYS A 1 415 ? 178.055 167.519 203.857 1.00 46.37 ? 558 LYS A CG     1 
ATOM   2632 C  CD     . LYS A 1 415 ? 179.396 168.215 203.905 1.00 52.61 ? 558 LYS A CD     1 
ATOM   2633 C  CE     . LYS A 1 415 ? 179.385 169.472 203.048 1.00 54.17 ? 558 LYS A CE     1 
ATOM   2634 N  NZ     . LYS A 1 415 ? 179.376 169.165 201.592 1.00 56.36 ? 558 LYS A NZ     1 
ATOM   2635 N  N      . LYS A 1 416 ? 174.830 167.635 206.358 1.00 37.82 ? 559 LYS A N      1 
ATOM   2636 C  CA     . LYS A 1 416 ? 174.613 166.857 207.573 1.00 37.70 ? 559 LYS A CA     1 
ATOM   2637 C  C      . LYS A 1 416 ? 173.334 166.029 207.510 1.00 35.51 ? 559 LYS A C      1 
ATOM   2638 O  O      . LYS A 1 416 ? 173.248 164.986 208.163 1.00 34.60 ? 559 LYS A O      1 
ATOM   2639 C  CB     . LYS A 1 416 ? 174.588 167.774 208.792 1.00 40.51 ? 559 LYS A CB     1 
ATOM   2640 C  CG     . LYS A 1 416 ? 173.429 168.739 208.816 1.00 46.31 ? 559 LYS A CG     1 
ATOM   2641 C  CD     . LYS A 1 416 ? 173.402 169.517 210.114 1.00 50.01 ? 559 LYS A CD     1 
ATOM   2642 C  CE     . LYS A 1 416 ? 173.043 168.609 211.276 1.00 54.92 ? 559 LYS A CE     1 
ATOM   2643 N  NZ     . LYS A 1 416 ? 171.669 168.051 211.129 1.00 56.39 ? 559 LYS A NZ     1 
ATOM   2644 N  N      . ILE A 1 417 ? 172.329 166.473 206.752 1.00 33.01 ? 560 ILE A N      1 
ATOM   2645 C  CA     . ILE A 1 417 ? 171.110 165.681 206.613 1.00 29.15 ? 560 ILE A CA     1 
ATOM   2646 C  C      . ILE A 1 417 ? 171.412 164.360 205.919 1.00 27.85 ? 560 ILE A C      1 
ATOM   2647 O  O      . ILE A 1 417 ? 170.918 163.301 206.320 1.00 29.10 ? 560 ILE A O      1 
ATOM   2648 C  CB     . ILE A 1 417 ? 170.025 166.474 205.861 1.00 29.60 ? 560 ILE A CB     1 
ATOM   2649 C  CG1    . ILE A 1 417 ? 169.476 167.601 206.729 1.00 32.86 ? 560 ILE A CG1    1 
ATOM   2650 C  CG2    . ILE A 1 417 ? 168.894 165.559 205.435 1.00 25.55 ? 560 ILE A CG2    1 
ATOM   2651 C  CD1    . ILE A 1 417 ? 168.650 168.600 205.963 1.00 32.05 ? 560 ILE A CD1    1 
ATOM   2652 N  N      . VAL A 1 418 ? 172.221 164.403 204.859 1.00 25.93 ? 561 VAL A N      1 
ATOM   2653 C  CA     . VAL A 1 418 ? 172.532 163.191 204.108 1.00 24.83 ? 561 VAL A CA     1 
ATOM   2654 C  C      . VAL A 1 418 ? 173.420 162.261 204.926 1.00 24.34 ? 561 VAL A C      1 
ATOM   2655 O  O      . VAL A 1 418 ? 173.250 161.037 204.899 1.00 25.84 ? 561 VAL A O      1 
ATOM   2656 C  CB     . VAL A 1 418 ? 173.176 163.552 202.757 1.00 25.59 ? 561 VAL A CB     1 
ATOM   2657 C  CG1    . VAL A 1 418 ? 173.596 162.296 202.017 1.00 20.93 ? 561 VAL A CG1    1 
ATOM   2658 C  CG2    . VAL A 1 418 ? 172.213 164.363 201.912 1.00 21.43 ? 561 VAL A CG2    1 
ATOM   2659 N  N      . THR A 1 419 ? 174.378 162.818 205.666 1.00 25.36 ? 562 THR A N      1 
ATOM   2660 C  CA     . THR A 1 419 ? 175.277 161.990 206.464 1.00 26.23 ? 562 THR A CA     1 
ATOM   2661 C  C      . THR A 1 419 ? 174.533 161.249 207.570 1.00 25.58 ? 562 THR A C      1 
ATOM   2662 O  O      . THR A 1 419 ? 174.834 160.085 207.851 1.00 24.81 ? 562 THR A O      1 
ATOM   2663 C  CB     . THR A 1 419 ? 176.396 162.848 207.051 1.00 30.50 ? 562 THR A CB     1 
ATOM   2664 O  OG1    . THR A 1 419 ? 177.119 163.482 205.992 1.00 33.26 ? 562 THR A OG1    1 
ATOM   2665 C  CG2    . THR A 1 419 ? 177.351 162.000 207.866 1.00 30.02 ? 562 THR A CG2    1 
ATOM   2666 N  N      . ASN A 1 420 ? 173.575 161.911 208.221 1.00 25.11 ? 563 ASN A N      1 
ATOM   2667 C  CA     . ASN A 1 420 ? 172.817 161.260 209.286 1.00 24.00 ? 563 ASN A CA     1 
ATOM   2668 C  C      . ASN A 1 420 ? 171.958 160.122 208.749 1.00 22.69 ? 563 ASN A C      1 
ATOM   2669 O  O      . ASN A 1 420 ? 171.815 159.085 209.404 1.00 22.34 ? 563 ASN A O      1 
ATOM   2670 C  CB     . ASN A 1 420 ? 171.949 162.280 210.019 1.00 27.91 ? 563 ASN A CB     1 
ATOM   2671 C  CG     . ASN A 1 420 ? 172.757 163.241 210.862 1.00 32.49 ? 563 ASN A CG     1 
ATOM   2672 O  OD1    . ASN A 1 420 ? 173.773 162.871 211.446 1.00 32.02 ? 563 ASN A OD1    1 
ATOM   2673 N  ND2    . ASN A 1 420 ? 172.301 164.480 210.941 1.00 32.50 ? 563 ASN A ND2    1 
ATOM   2674 N  N      . SER A 1 421 ? 171.354 160.307 207.575 1.00 20.74 ? 564 SER A N      1 
ATOM   2675 C  CA     . SER A 1 421 ? 170.526 159.257 206.989 1.00 18.19 ? 564 SER A CA     1 
ATOM   2676 C  C      . SER A 1 421 ? 171.355 158.037 206.611 1.00 19.62 ? 564 SER A C      1 
ATOM   2677 O  O      . SER A 1 421 ? 170.884 156.901 206.729 1.00 18.15 ? 564 SER A O      1 
ATOM   2678 C  CB     . SER A 1 421 ? 169.784 159.794 205.767 1.00 18.16 ? 564 SER A CB     1 
ATOM   2679 O  OG     . SER A 1 421 ? 168.781 160.715 206.136 1.00 22.48 ? 564 SER A OG     1 
ATOM   2680 N  N      . TYR A 1 422 ? 172.576 158.253 206.117 1.00 18.91 ? 565 TYR A N      1 
ATOM   2681 C  CA     . TYR A 1 422 ? 173.432 157.140 205.728 1.00 18.10 ? 565 TYR A CA     1 
ATOM   2682 C  C      . TYR A 1 422 ? 173.850 156.304 206.932 1.00 19.06 ? 565 TYR A C      1 
ATOM   2683 O  O      . TYR A 1 422 ? 173.904 155.073 206.848 1.00 19.16 ? 565 TYR A O      1 
ATOM   2684 C  CB     . TYR A 1 422 ? 174.657 157.659 204.977 1.00 19.84 ? 565 TYR A CB     1 
ATOM   2685 C  CG     . TYR A 1 422 ? 175.486 156.569 204.344 1.00 19.61 ? 565 TYR A CG     1 
ATOM   2686 C  CD1    . TYR A 1 422 ? 174.899 155.607 203.536 1.00 18.73 ? 565 TYR A CD1    1 
ATOM   2687 C  CD2    . TYR A 1 422 ? 176.849 156.488 204.571 1.00 21.53 ? 565 TYR A CD2    1 
ATOM   2688 C  CE1    . TYR A 1 422 ? 175.644 154.607 202.968 1.00 19.04 ? 565 TYR A CE1    1 
ATOM   2689 C  CE2    . TYR A 1 422 ? 177.604 155.492 204.003 1.00 22.39 ? 565 TYR A CE2    1 
ATOM   2690 C  CZ     . TYR A 1 422 ? 176.998 154.554 203.202 1.00 21.55 ? 565 TYR A CZ     1 
ATOM   2691 O  OH     . TYR A 1 422 ? 177.748 153.558 202.635 1.00 26.17 ? 565 TYR A OH     1 
ATOM   2692 N  N      . GLU A 1 423 ? 174.165 156.951 208.055 1.00 19.99 ? 566 GLU A N      1 
ATOM   2693 C  CA     . GLU A 1 423 ? 174.521 156.207 209.260 1.00 21.46 ? 566 GLU A CA     1 
ATOM   2694 C  C      . GLU A 1 423 ? 173.348 155.381 209.768 1.00 20.79 ? 566 GLU A C      1 
ATOM   2695 O  O      . GLU A 1 423 ? 173.534 154.261 210.252 1.00 21.33 ? 566 GLU A O      1 
ATOM   2696 C  CB     . GLU A 1 423 ? 175.002 157.162 210.349 1.00 23.81 ? 566 GLU A CB     1 
ATOM   2697 C  CG     . GLU A 1 423 ? 176.256 157.934 210.007 1.00 27.58 ? 566 GLU A CG     1 
ATOM   2698 C  CD     . GLU A 1 423 ? 177.425 157.037 209.668 1.00 38.32 ? 566 GLU A CD     1 
ATOM   2699 O  OE1    . GLU A 1 423 ? 177.685 156.080 210.424 1.00 38.04 ? 566 GLU A OE1    1 
ATOM   2700 O  OE2    . GLU A 1 423 ? 178.090 157.292 208.643 1.00 41.52 ? 566 GLU A OE2    1 
ATOM   2701 N  N      . ARG A 1 424 ? 172.134 155.925 209.677 1.00 17.50 ? 567 ARG A N      1 
ATOM   2702 C  CA     . ARG A 1 424 ? 170.950 155.210 210.137 1.00 16.51 ? 567 ARG A CA     1 
ATOM   2703 C  C      . ARG A 1 424 ? 170.724 153.926 209.345 1.00 16.64 ? 567 ARG A C      1 
ATOM   2704 O  O      . ARG A 1 424 ? 170.383 152.887 209.920 1.00 17.31 ? 567 ARG A O      1 
ATOM   2705 C  CB     . ARG A 1 424 ? 169.732 156.128 210.041 1.00 15.85 ? 567 ARG A CB     1 
ATOM   2706 C  CG     . ARG A 1 424 ? 168.524 155.671 210.819 1.00 14.49 ? 567 ARG A CG     1 
ATOM   2707 C  CD     . ARG A 1 424 ? 167.398 156.669 210.689 1.00 14.26 ? 567 ARG A CD     1 
ATOM   2708 N  NE     . ARG A 1 424 ? 166.097 156.064 210.940 1.00 19.75 ? 567 ARG A NE     1 
ATOM   2709 C  CZ     . ARG A 1 424 ? 164.949 156.517 210.456 1.00 20.85 ? 567 ARG A CZ     1 
ATOM   2710 N  NH1    . ARG A 1 424 ? 164.903 157.574 209.665 1.00 17.09 ? 567 ARG A NH1    1 
ATOM   2711 N  NH2    . ARG A 1 424 ? 163.821 155.893 210.774 1.00 22.44 ? 567 ARG A NH2    1 
ATOM   2712 N  N      . ALA A 1 425 ? 170.907 153.977 208.024 1.00 16.76 ? 568 ALA A N      1 
ATOM   2713 C  CA     . ALA A 1 425 ? 170.721 152.791 207.194 1.00 15.72 ? 568 ALA A CA     1 
ATOM   2714 C  C      . ALA A 1 425 ? 171.749 151.708 207.500 1.00 17.85 ? 568 ALA A C      1 
ATOM   2715 O  O      . ALA A 1 425 ? 171.414 150.520 207.487 1.00 16.15 ? 568 ALA A O      1 
ATOM   2716 C  CB     . ALA A 1 425 ? 170.775 153.173 205.715 1.00 11.26 ? 568 ALA A CB     1 
ATOM   2717 N  N      . LYS A 1 426 ? 172.998 152.090 207.771 1.00 17.26 ? 569 LYS A N      1 
ATOM   2718 C  CA     . LYS A 1 426 ? 174.037 151.101 208.037 1.00 17.62 ? 569 LYS A CA     1 
ATOM   2719 C  C      . LYS A 1 426 ? 173.759 150.296 209.300 1.00 20.52 ? 569 LYS A C      1 
ATOM   2720 O  O      . LYS A 1 426 ? 174.079 149.104 209.351 1.00 21.41 ? 569 LYS A O      1 
ATOM   2721 C  CB     . LYS A 1 426 ? 175.397 151.783 208.131 1.00 19.82 ? 569 LYS A CB     1 
ATOM   2722 C  CG     . LYS A 1 426 ? 176.119 151.864 206.803 1.00 20.66 ? 569 LYS A CG     1 
ATOM   2723 C  CD     . LYS A 1 426 ? 177.535 152.359 206.967 1.00 22.29 ? 569 LYS A CD     1 
ATOM   2724 C  CE     . LYS A 1 426 ? 177.583 153.851 207.171 1.00 24.63 ? 569 LYS A CE     1 
ATOM   2725 N  NZ     . LYS A 1 426 ? 178.987 154.324 207.243 1.00 31.20 ? 569 LYS A NZ     1 
ATOM   2726 N  N      . GLU A 1 427 ? 173.189 150.924 210.330 1.00 20.85 ? 570 GLU A N      1 
ATOM   2727 C  CA     . GLU A 1 427 ? 172.851 150.199 211.550 1.00 21.24 ? 570 GLU A CA     1 
ATOM   2728 C  C      . GLU A 1 427 ? 171.735 149.187 211.315 1.00 19.46 ? 570 GLU A C      1 
ATOM   2729 O  O      . GLU A 1 427 ? 171.744 148.104 211.905 1.00 21.35 ? 570 GLU A O      1 
ATOM   2730 C  CB     . GLU A 1 427 ? 172.463 151.178 212.652 1.00 23.55 ? 570 GLU A CB     1 
ATOM   2731 C  CG     . GLU A 1 427 ? 173.469 152.285 212.870 1.00 32.01 ? 570 GLU A CG     1 
ATOM   2732 C  CD     . GLU A 1 427 ? 172.910 153.424 213.698 1.00 48.67 ? 570 GLU A CD     1 
ATOM   2733 O  OE1    . GLU A 1 427 ? 171.688 153.431 213.954 1.00 44.83 ? 570 GLU A OE1    1 
ATOM   2734 O  OE2    . GLU A 1 427 ? 173.693 154.315 214.092 1.00 52.87 ? 570 GLU A OE2    1 
ATOM   2735 N  N      . ILE A 1 428 ? 170.758 149.526 210.475 1.00 17.06 ? 571 ILE A N      1 
ATOM   2736 C  CA     . ILE A 1 428 ? 169.689 148.582 210.166 1.00 17.19 ? 571 ILE A CA     1 
ATOM   2737 C  C      . ILE A 1 428 ? 170.239 147.363 209.437 1.00 18.48 ? 571 ILE A C      1 
ATOM   2738 O  O      . ILE A 1 428 ? 169.797 146.234 209.672 1.00 18.26 ? 571 ILE A O      1 
ATOM   2739 C  CB     . ILE A 1 428 ? 168.574 149.279 209.361 1.00 17.12 ? 571 ILE A CB     1 
ATOM   2740 C  CG1    . ILE A 1 428 ? 167.892 150.351 210.211 1.00 15.33 ? 571 ILE A CG1    1 
ATOM   2741 C  CG2    . ILE A 1 428 ? 167.562 148.267 208.844 1.00 13.63 ? 571 ILE A CG2    1 
ATOM   2742 C  CD1    . ILE A 1 428 ? 167.078 151.331 209.419 1.00 12.26 ? 571 ILE A CD1    1 
ATOM   2743 N  N      . ILE A 1 429 ? 171.203 147.568 208.535 1.00 17.30 ? 572 ILE A N      1 
ATOM   2744 C  CA     . ILE A 1 429 ? 171.781 146.452 207.790 1.00 16.62 ? 572 ILE A CA     1 
ATOM   2745 C  C      . ILE A 1 429 ? 172.518 145.500 208.726 1.00 19.04 ? 572 ILE A C      1 
ATOM   2746 O  O      . ILE A 1 429 ? 172.442 144.276 208.572 1.00 21.73 ? 572 ILE A O      1 
ATOM   2747 C  CB     . ILE A 1 429 ? 172.702 146.974 206.669 1.00 18.06 ? 572 ILE A CB     1 
ATOM   2748 C  CG1    . ILE A 1 429 ? 171.900 147.766 205.633 1.00 14.32 ? 572 ILE A CG1    1 
ATOM   2749 C  CG2    . ILE A 1 429 ? 173.443 145.827 205.997 1.00 14.71 ? 572 ILE A CG2    1 
ATOM   2750 C  CD1    . ILE A 1 429 ? 171.082 146.914 204.704 1.00 11.30 ? 572 ILE A CD1    1 
ATOM   2751 N  N      . ARG A 1 430 ? 173.261 146.041 209.693 1.00 19.74 ? 573 ARG A N      1 
ATOM   2752 C  CA     . ARG A 1 430 ? 173.992 145.197 210.633 1.00 18.73 ? 573 ARG A CA     1 
ATOM   2753 C  C      . ARG A 1 430 ? 173.051 144.386 211.511 1.00 21.23 ? 573 ARG A C      1 
ATOM   2754 O  O      . ARG A 1 430 ? 173.313 143.214 211.799 1.00 24.64 ? 573 ARG A O      1 
ATOM   2755 C  CB     . ARG A 1 430 ? 174.913 146.049 211.503 1.00 17.73 ? 573 ARG A CB     1 
ATOM   2756 C  CG     . ARG A 1 430 ? 176.101 146.616 210.773 1.00 19.85 ? 573 ARG A CG     1 
ATOM   2757 C  CD     . ARG A 1 430 ? 176.962 147.444 211.693 1.00 24.45 ? 573 ARG A CD     1 
ATOM   2758 N  NE     . ARG A 1 430 ? 177.866 148.307 210.944 1.00 27.76 ? 573 ARG A NE     1 
ATOM   2759 C  CZ     . ARG A 1 430 ? 177.857 149.632 211.008 1.00 30.43 ? 573 ARG A CZ     1 
ATOM   2760 N  NH1    . ARG A 1 430 ? 177.019 150.280 211.800 1.00 28.68 ? 573 ARG A NH1    1 
ATOM   2761 N  NH2    . ARG A 1 430 ? 178.709 150.323 210.257 1.00 27.47 ? 573 ARG A NH2    1 
ATOM   2762 N  N      . LYS A 1 431 ? 171.954 144.996 211.958 1.00 21.44 ? 574 LYS A N      1 
ATOM   2763 C  CA     . LYS A 1 431 ? 171.049 144.332 212.885 1.00 20.72 ? 574 LYS A CA     1 
ATOM   2764 C  C      . LYS A 1 431 ? 170.202 143.252 212.226 1.00 23.50 ? 574 LYS A C      1 
ATOM   2765 O  O      . LYS A 1 431 ? 169.757 142.332 212.915 1.00 26.62 ? 574 LYS A O      1 
ATOM   2766 C  CB     . LYS A 1 431 ? 170.136 145.353 213.552 1.00 23.20 ? 574 LYS A CB     1 
ATOM   2767 C  CG     . LYS A 1 431 ? 169.139 144.721 214.494 1.00 28.85 ? 574 LYS A CG     1 
ATOM   2768 C  CD     . LYS A 1 431 ? 168.325 145.748 215.240 1.00 36.57 ? 574 LYS A CD     1 
ATOM   2769 C  CE     . LYS A 1 431 ? 167.319 145.059 216.142 1.00 43.86 ? 574 LYS A CE     1 
ATOM   2770 N  NZ     . LYS A 1 431 ? 167.006 143.691 215.646 1.00 39.37 ? 574 LYS A NZ     1 
ATOM   2771 N  N      . TYR A 1 432 ? 169.955 143.343 210.923 1.00 23.20 ? 575 TYR A N      1 
ATOM   2772 C  CA     . TYR A 1 432 ? 169.129 142.371 210.220 1.00 22.82 ? 575 TYR A CA     1 
ATOM   2773 C  C      . TYR A 1 432 ? 169.936 141.582 209.198 1.00 25.73 ? 575 TYR A C      1 
ATOM   2774 O  O      . TYR A 1 432 ? 169.402 141.150 208.179 1.00 29.23 ? 575 TYR A O      1 
ATOM   2775 C  CB     . TYR A 1 432 ? 167.938 143.057 209.553 1.00 22.63 ? 575 TYR A CB     1 
ATOM   2776 C  CG     . TYR A 1 432 ? 166.921 143.593 210.530 1.00 25.80 ? 575 TYR A CG     1 
ATOM   2777 C  CD1    . TYR A 1 432 ? 165.880 142.798 210.975 1.00 25.88 ? 575 TYR A CD1    1 
ATOM   2778 C  CD2    . TYR A 1 432 ? 167.008 144.888 211.014 1.00 23.18 ? 575 TYR A CD2    1 
ATOM   2779 C  CE1    . TYR A 1 432 ? 164.957 143.274 211.870 1.00 24.32 ? 575 TYR A CE1    1 
ATOM   2780 C  CE2    . TYR A 1 432 ? 166.090 145.372 211.911 1.00 23.36 ? 575 TYR A CE2    1 
ATOM   2781 C  CZ     . TYR A 1 432 ? 165.065 144.560 212.335 1.00 26.58 ? 575 TYR A CZ     1 
ATOM   2782 O  OH     . TYR A 1 432 ? 164.138 145.034 213.229 1.00 29.60 ? 575 TYR A OH     1 
ATOM   2783 N  N      . ARG A 1 433 ? 171.223 141.366 209.477 1.00 26.08 ? 576 ARG A N      1 
ATOM   2784 C  CA     . ARG A 1 433 ? 172.101 140.702 208.520 1.00 25.92 ? 576 ARG A CA     1 
ATOM   2785 C  C      . ARG A 1 433 ? 171.627 139.293 208.186 1.00 27.31 ? 576 ARG A C      1 
ATOM   2786 O  O      . ARG A 1 433 ? 171.782 138.847 207.047 1.00 28.62 ? 576 ARG A O      1 
ATOM   2787 C  CB     . ARG A 1 433 ? 173.530 140.672 209.065 1.00 26.14 ? 576 ARG A CB     1 
ATOM   2788 C  CG     . ARG A 1 433 ? 174.509 139.879 208.219 1.00 27.54 ? 576 ARG A CG     1 
ATOM   2789 C  CD     . ARG A 1 433 ? 175.037 140.680 207.046 1.00 24.38 ? 576 ARG A CD     1 
ATOM   2790 N  NE     . ARG A 1 433 ? 175.972 139.903 206.242 1.00 25.62 ? 576 ARG A NE     1 
ATOM   2791 C  CZ     . ARG A 1 433 ? 177.289 140.045 206.263 1.00 25.62 ? 576 ARG A CZ     1 
ATOM   2792 N  NH1    . ARG A 1 433 ? 177.876 140.957 207.018 1.00 23.53 ? 576 ARG A NH1    1 
ATOM   2793 N  NH2    . ARG A 1 433 ? 178.037 139.253 205.503 1.00 23.45 ? 576 ARG A NH2    1 
ATOM   2794 N  N      . LYS A 1 434 ? 171.052 138.581 209.154 1.00 28.89 ? 577 LYS A N      1 
ATOM   2795 C  CA     . LYS A 1 434 ? 170.624 137.206 208.913 1.00 30.39 ? 577 LYS A CA     1 
ATOM   2796 C  C      . LYS A 1 434 ? 169.498 137.143 207.891 1.00 30.42 ? 577 LYS A C      1 
ATOM   2797 O  O      . LYS A 1 434 ? 169.510 136.290 206.998 1.00 30.55 ? 577 LYS A O      1 
ATOM   2798 C  CB     . LYS A 1 434 ? 170.179 136.561 210.222 1.00 35.63 ? 577 LYS A CB     1 
ATOM   2799 C  CG     . LYS A 1 434 ? 171.308 136.211 211.162 1.00 41.17 ? 577 LYS A CG     1 
ATOM   2800 C  CD     . LYS A 1 434 ? 172.023 137.475 211.613 1.00 46.06 ? 577 LYS A CD     1 
ATOM   2801 C  CE     . LYS A 1 434 ? 171.052 138.447 212.282 1.00 41.33 ? 577 LYS A CE     1 
ATOM   2802 N  NZ     . LYS A 1 434 ? 171.713 139.714 212.692 1.00 38.93 ? 577 LYS A NZ     1 
ATOM   2803 N  N      . GLN A 1 435 ? 168.506 138.028 208.016 1.00 28.97 ? 578 GLN A N      1 
ATOM   2804 C  CA     . GLN A 1 435 ? 167.397 138.056 207.068 1.00 28.42 ? 578 GLN A CA     1 
ATOM   2805 C  C      . GLN A 1 435 ? 167.859 138.470 205.678 1.00 27.79 ? 578 GLN A C      1 
ATOM   2806 O  O      . GLN A 1 435 ? 167.319 137.989 204.678 1.00 27.66 ? 578 GLN A O      1 
ATOM   2807 C  CB     . GLN A 1 435 ? 166.309 139.009 207.562 1.00 31.81 ? 578 GLN A CB     1 
ATOM   2808 C  CG     . GLN A 1 435 ? 165.506 138.500 208.746 1.00 32.92 ? 578 GLN A CG     1 
ATOM   2809 C  CD     . GLN A 1 435 ? 166.132 138.864 210.077 1.00 31.65 ? 578 GLN A CD     1 
ATOM   2810 O  OE1    . GLN A 1 435 ? 167.349 138.952 210.204 1.00 33.17 ? 578 GLN A OE1    1 
ATOM   2811 N  NE2    . GLN A 1 435 ? 165.294 139.085 211.076 1.00 34.57 ? 578 GLN A NE2    1 
ATOM   2812 N  N      . LEU A 1 436 ? 168.840 139.369 205.600 1.00 25.22 ? 579 LEU A N      1 
ATOM   2813 C  CA     . LEU A 1 436 ? 169.385 139.785 204.314 1.00 23.13 ? 579 LEU A CA     1 
ATOM   2814 C  C      . LEU A 1 436 ? 170.051 138.619 203.588 1.00 25.16 ? 579 LEU A C      1 
ATOM   2815 O  O      . LEU A 1 436 ? 169.920 138.483 202.368 1.00 26.79 ? 579 LEU A O      1 
ATOM   2816 C  CB     . LEU A 1 436 ? 170.368 140.933 204.533 1.00 23.42 ? 579 LEU A CB     1 
ATOM   2817 C  CG     . LEU A 1 436 ? 171.038 141.632 203.353 1.00 25.29 ? 579 LEU A CG     1 
ATOM   2818 C  CD1    . LEU A 1 436 ? 170.028 142.372 202.511 1.00 18.78 ? 579 LEU A CD1    1 
ATOM   2819 C  CD2    . LEU A 1 436 ? 172.102 142.583 203.859 1.00 23.70 ? 579 LEU A CD2    1 
ATOM   2820 N  N      . ASP A 1 437 ? 170.774 137.769 204.322 1.00 24.93 ? 580 ASP A N      1 
ATOM   2821 C  CA     . ASP A 1 437 ? 171.414 136.606 203.711 1.00 23.97 ? 580 ASP A CA     1 
ATOM   2822 C  C      . ASP A 1 437 ? 170.390 135.606 203.187 1.00 28.06 ? 580 ASP A C      1 
ATOM   2823 O  O      . ASP A 1 437 ? 170.594 135.004 202.129 1.00 29.29 ? 580 ASP A O      1 
ATOM   2824 C  CB     . ASP A 1 437 ? 172.347 135.926 204.711 1.00 27.89 ? 580 ASP A CB     1 
ATOM   2825 C  CG     . ASP A 1 437 ? 173.537 136.781 205.080 1.00 33.76 ? 580 ASP A CG     1 
ATOM   2826 O  OD1    . ASP A 1 437 ? 173.796 137.785 204.390 1.00 36.07 ? 580 ASP A OD1    1 
ATOM   2827 O  OD2    . ASP A 1 437 ? 174.216 136.451 206.070 1.00 34.03 ? 580 ASP A OD2    1 
ATOM   2828 N  N      . ASN A 1 438 ? 169.298 135.394 203.923 1.00 28.26 ? 581 ASN A N      1 
ATOM   2829 C  CA     . ASN A 1 438 ? 168.299 134.415 203.504 1.00 28.66 ? 581 ASN A CA     1 
ATOM   2830 C  C      . ASN A 1 438 ? 167.616 134.822 202.204 1.00 30.27 ? 581 ASN A C      1 
ATOM   2831 O  O      . ASN A 1 438 ? 167.335 133.972 201.355 1.00 32.71 ? 581 ASN A O      1 
ATOM   2832 C  CB     . ASN A 1 438 ? 167.264 134.211 204.609 1.00 31.86 ? 581 ASN A CB     1 
ATOM   2833 C  CG     . ASN A 1 438 ? 167.836 133.503 205.819 1.00 41.20 ? 581 ASN A CG     1 
ATOM   2834 O  OD1    . ASN A 1 438 ? 168.623 132.570 205.690 1.00 46.52 ? 581 ASN A OD1    1 
ATOM   2835 N  ND2    . ASN A 1 438 ? 167.439 133.946 207.004 1.00 41.97 ? 581 ASN A ND2    1 
ATOM   2836 N  N      . ILE A 1 439 ? 167.319 136.112 202.039 1.00 27.57 ? 582 ILE A N      1 
ATOM   2837 C  CA     . ILE A 1 439 ? 166.658 136.573 200.822 1.00 25.58 ? 582 ILE A CA     1 
ATOM   2838 C  C      . ILE A 1 439 ? 167.571 136.404 199.612 1.00 27.52 ? 582 ILE A C      1 
ATOM   2839 O  O      . ILE A 1 439 ? 167.118 136.028 198.526 1.00 27.99 ? 582 ILE A O      1 
ATOM   2840 C  CB     . ILE A 1 439 ? 166.197 138.032 200.986 1.00 24.95 ? 582 ILE A CB     1 
ATOM   2841 C  CG1    . ILE A 1 439 ? 165.063 138.126 202.004 1.00 23.89 ? 582 ILE A CG1    1 
ATOM   2842 C  CG2    . ILE A 1 439 ? 165.752 138.607 199.657 1.00 20.89 ? 582 ILE A CG2    1 
ATOM   2843 C  CD1    . ILE A 1 439 ? 164.862 139.508 202.554 1.00 20.75 ? 582 ILE A CD1    1 
ATOM   2844 N  N      . VAL A 1 440 ? 168.867 136.680 199.776 1.00 24.99 ? 583 VAL A N      1 
ATOM   2845 C  CA     . VAL A 1 440 ? 169.793 136.619 198.647 1.00 25.12 ? 583 VAL A CA     1 
ATOM   2846 C  C      . VAL A 1 440 ? 169.891 135.198 198.106 1.00 30.90 ? 583 VAL A C      1 
ATOM   2847 O  O      . VAL A 1 440 ? 170.000 134.989 196.893 1.00 33.13 ? 583 VAL A O      1 
ATOM   2848 C  CB     . VAL A 1 440 ? 171.175 137.166 199.052 1.00 24.81 ? 583 VAL A CB     1 
ATOM   2849 C  CG1    . VAL A 1 440 ? 172.240 136.675 198.094 1.00 25.91 ? 583 VAL A CG1    1 
ATOM   2850 C  CG2    . VAL A 1 440 ? 171.161 138.679 199.090 1.00 18.32 ? 583 VAL A CG2    1 
ATOM   2851 N  N      . GLU A 1 441 ? 169.864 134.200 198.990 1.00 29.58 ? 584 GLU A N      1 
ATOM   2852 C  CA     . GLU A 1 441 ? 170.000 132.817 198.543 1.00 31.35 ? 584 GLU A CA     1 
ATOM   2853 C  C      . GLU A 1 441 ? 168.851 132.410 197.629 1.00 34.59 ? 584 GLU A C      1 
ATOM   2854 O  O      . GLU A 1 441 ? 169.066 131.745 196.610 1.00 38.76 ? 584 GLU A O      1 
ATOM   2855 C  CB     . GLU A 1 441 ? 170.085 131.883 199.748 1.00 34.27 ? 584 GLU A CB     1 
ATOM   2856 C  CG     . GLU A 1 441 ? 171.335 132.058 200.600 1.00 41.26 ? 584 GLU A CG     1 
ATOM   2857 C  CD     . GLU A 1 441 ? 172.559 132.465 199.796 1.00 52.77 ? 584 GLU A CD     1 
ATOM   2858 O  OE1    . GLU A 1 441 ? 172.813 131.852 198.737 1.00 51.12 ? 584 GLU A OE1    1 
ATOM   2859 O  OE2    . GLU A 1 441 ? 173.274 133.396 200.230 1.00 53.37 ? 584 GLU A OE2    1 
ATOM   2860 N  N      . ILE A 1 442 ? 167.621 132.792 197.979 1.00 31.83 ? 585 ILE A N      1 
ATOM   2861 C  CA     . ILE A 1 442 ? 166.471 132.466 197.140 1.00 33.12 ? 585 ILE A CA     1 
ATOM   2862 C  C      . ILE A 1 442 ? 166.540 133.216 195.816 1.00 34.25 ? 585 ILE A C      1 
ATOM   2863 O  O      . ILE A 1 442 ? 166.145 132.694 194.769 1.00 35.03 ? 585 ILE A O      1 
ATOM   2864 C  CB     . ILE A 1 442 ? 165.162 132.774 197.889 1.00 33.72 ? 585 ILE A CB     1 
ATOM   2865 C  CG1    . ILE A 1 442 ? 165.120 132.030 199.219 1.00 32.16 ? 585 ILE A CG1    1 
ATOM   2866 C  CG2    . ILE A 1 442 ? 163.963 132.418 197.036 1.00 34.94 ? 585 ILE A CG2    1 
ATOM   2867 C  CD1    . ILE A 1 442 ? 164.031 132.509 200.134 1.00 30.54 ? 585 ILE A CD1    1 
ATOM   2868 N  N      . LEU A 1 443 ? 167.023 134.456 195.845 1.00 32.47 ? 586 LEU A N      1 
ATOM   2869 C  CA     . LEU A 1 443 ? 167.092 135.260 194.633 1.00 32.03 ? 586 LEU A CA     1 
ATOM   2870 C  C      . LEU A 1 443 ? 168.106 134.691 193.648 1.00 34.03 ? 586 LEU A C      1 
ATOM   2871 O  O      . LEU A 1 443 ? 167.908 134.763 192.431 1.00 35.58 ? 586 LEU A O      1 
ATOM   2872 C  CB     . LEU A 1 443 ? 167.433 136.703 195.005 1.00 29.85 ? 586 LEU A CB     1 
ATOM   2873 C  CG     . LEU A 1 443 ? 166.944 137.871 194.155 1.00 29.42 ? 586 LEU A CG     1 
ATOM   2874 C  CD1    . LEU A 1 443 ? 165.483 137.710 193.798 1.00 31.36 ? 586 LEU A CD1    1 
ATOM   2875 C  CD2    . LEU A 1 443 ? 167.159 139.156 194.923 1.00 21.48 ? 586 LEU A CD2    1 
ATOM   2876 N  N      . LEU A 1 444 ? 169.199 134.118 194.156 1.00 34.69 ? 587 LEU A N      1 
ATOM   2877 C  CA     . LEU A 1 444 ? 170.247 133.590 193.291 1.00 34.62 ? 587 LEU A CA     1 
ATOM   2878 C  C      . LEU A 1 444 ? 169.817 132.339 192.538 1.00 37.90 ? 587 LEU A C      1 
ATOM   2879 O  O      . LEU A 1 444 ? 170.506 131.934 191.597 1.00 41.85 ? 587 LEU A O      1 
ATOM   2880 C  CB     . LEU A 1 444 ? 171.502 133.290 194.111 1.00 33.05 ? 587 LEU A CB     1 
ATOM   2881 C  CG     . LEU A 1 444 ? 172.428 134.472 194.394 1.00 31.36 ? 587 LEU A CG     1 
ATOM   2882 C  CD1    . LEU A 1 444 ? 173.635 134.026 195.189 1.00 31.25 ? 587 LEU A CD1    1 
ATOM   2883 C  CD2    . LEU A 1 444 ? 172.849 135.155 193.109 1.00 28.63 ? 587 LEU A CD2    1 
ATOM   2884 N  N      . GLU A 1 445 ? 168.709 131.713 192.925 1.00 38.50 ? 588 GLU A N      1 
ATOM   2885 C  CA     . GLU A 1 445 ? 168.218 130.522 192.248 1.00 40.01 ? 588 GLU A CA     1 
ATOM   2886 C  C      . GLU A 1 445 ? 166.970 130.760 191.414 1.00 41.84 ? 588 GLU A C      1 
ATOM   2887 O  O      . GLU A 1 445 ? 166.797 130.100 190.390 1.00 44.94 ? 588 GLU A O      1 
ATOM   2888 C  CB     . GLU A 1 445 ? 167.922 129.416 193.267 1.00 41.35 ? 588 GLU A CB     1 
ATOM   2889 C  CG     . GLU A 1 445 ? 166.743 129.722 194.169 1.00 47.37 ? 588 GLU A CG     1 
ATOM   2890 C  CD     . GLU A 1 445 ? 166.539 128.672 195.237 1.00 57.14 ? 588 GLU A CD     1 
ATOM   2891 O  OE1    . GLU A 1 445 ? 167.348 127.724 195.292 1.00 61.07 ? 588 GLU A OE1    1 
ATOM   2892 O  OE2    . GLU A 1 445 ? 165.572 128.792 196.019 1.00 56.27 ? 588 GLU A OE2    1 
ATOM   2893 N  N      . LYS A 1 446 ? 166.102 131.682 191.826 1.00 40.60 ? 589 LYS A N      1 
ATOM   2894 C  CA     . LYS A 1 446 ? 164.849 131.950 191.135 1.00 39.01 ? 589 LYS A CA     1 
ATOM   2895 C  C      . LYS A 1 446 ? 164.890 133.194 190.261 1.00 38.27 ? 589 LYS A C      1 
ATOM   2896 O  O      . LYS A 1 446 ? 164.138 133.273 189.286 1.00 37.78 ? 589 LYS A O      1 
ATOM   2897 C  CB     . LYS A 1 446 ? 163.714 132.097 192.152 1.00 40.37 ? 589 LYS A CB     1 
ATOM   2898 C  CG     . LYS A 1 446 ? 163.406 130.835 192.925 1.00 43.76 ? 589 LYS A CG     1 
ATOM   2899 C  CD     . LYS A 1 446 ? 161.996 130.869 193.475 1.00 46.05 ? 589 LYS A CD     1 
ATOM   2900 C  CE     . LYS A 1 446 ? 161.020 131.404 192.443 1.00 56.94 ? 589 LYS A CE     1 
ATOM   2901 N  NZ     . LYS A 1 446 ? 160.920 130.534 191.239 1.00 59.66 ? 589 LYS A NZ     1 
ATOM   2902 N  N      . GLU A 1 447 ? 165.734 134.169 190.588 1.00 38.48 ? 590 GLU A N      1 
ATOM   2903 C  CA     . GLU A 1 447 ? 165.949 135.412 189.862 1.00 34.66 ? 590 GLU A CA     1 
ATOM   2904 C  C      . GLU A 1 447 ? 164.850 136.443 190.116 1.00 35.50 ? 590 GLU A C      1 
ATOM   2905 O  O      . GLU A 1 447 ? 165.045 137.612 189.793 1.00 34.93 ? 590 GLU A O      1 
ATOM   2906 C  CB     . GLU A 1 447 ? 166.078 135.198 188.342 1.00 33.39 ? 590 GLU A CB     1 
ATOM   2907 C  CG     . GLU A 1 447 ? 166.457 136.432 187.553 1.00 35.78 ? 590 GLU A CG     1 
ATOM   2908 C  CD     . GLU A 1 447 ? 166.262 136.247 186.063 1.00 39.62 ? 590 GLU A CD     1 
ATOM   2909 O  OE1    . GLU A 1 447 ? 165.123 136.422 185.587 1.00 39.07 ? 590 GLU A OE1    1 
ATOM   2910 O  OE2    . GLU A 1 447 ? 167.243 135.919 185.367 1.00 38.73 ? 590 GLU A OE2    1 
ATOM   2911 N  N      . THR A 1 448 ? 163.722 136.068 190.716 1.00 35.37 ? 591 THR A N      1 
ATOM   2912 C  CA     . THR A 1 448 ? 162.605 136.982 190.907 1.00 35.59 ? 591 THR A CA     1 
ATOM   2913 C  C      . THR A 1 448 ? 161.681 136.418 191.973 1.00 39.80 ? 591 THR A C      1 
ATOM   2914 O  O      . THR A 1 448 ? 161.398 135.220 191.977 1.00 43.58 ? 591 THR A O      1 
ATOM   2915 C  CB     . THR A 1 448 ? 161.822 137.192 189.604 1.00 37.75 ? 591 THR A CB     1 
ATOM   2916 O  OG1    . THR A 1 448 ? 162.662 137.815 188.626 1.00 39.25 ? 591 THR A OG1    1 
ATOM   2917 C  CG2    . THR A 1 448 ? 160.609 138.068 189.848 1.00 40.45 ? 591 THR A CG2    1 
ATOM   2918 N  N      . ILE A 1 449 ? 161.212 137.284 192.865 1.00 40.94 ? 592 ILE A N      1 
ATOM   2919 C  CA     . ILE A 1 449 ? 160.242 136.917 193.890 1.00 42.72 ? 592 ILE A CA     1 
ATOM   2920 C  C      . ILE A 1 449 ? 159.028 137.822 193.745 1.00 49.82 ? 592 ILE A C      1 
ATOM   2921 O  O      . ILE A 1 449 ? 159.119 139.033 193.976 1.00 48.30 ? 592 ILE A O      1 
ATOM   2922 C  CB     . ILE A 1 449 ? 160.839 137.019 195.304 1.00 41.26 ? 592 ILE A CB     1 
ATOM   2923 C  CG1    . ILE A 1 449 ? 162.253 136.446 195.326 1.00 42.94 ? 592 ILE A CG1    1 
ATOM   2924 C  CG2    . ILE A 1 449 ? 159.972 136.275 196.293 1.00 41.64 ? 592 ILE A CG2    1 
ATOM   2925 C  CD1    . ILE A 1 449 ? 163.006 136.732 196.603 1.00 35.31 ? 592 ILE A CD1    1 
ATOM   2926 N  N      . GLU A 1 450 ? 157.896 137.233 193.378 1.00 55.49 ? 593 GLU A N      1 
ATOM   2927 C  CA     . GLU A 1 450 ? 156.664 137.981 193.152 1.00 53.18 ? 593 GLU A CA     1 
ATOM   2928 C  C      . GLU A 1 450 ? 155.877 138.139 194.444 1.00 52.26 ? 593 GLU A C      1 
ATOM   2929 O  O      . GLU A 1 450 ? 155.528 137.153 195.091 1.00 55.39 ? 593 GLU A O      1 
ATOM   2930 C  CB     . GLU A 1 450 ? 155.801 137.285 192.100 1.00 57.90 ? 593 GLU A CB     1 
ATOM   2931 C  CG     . GLU A 1 450 ? 156.209 137.559 190.663 1.00 58.50 ? 593 GLU A CG     1 
ATOM   2932 C  CD     . GLU A 1 450 ? 155.890 138.970 190.229 1.00 65.09 ? 593 GLU A CD     1 
ATOM   2933 O  OE1    . GLU A 1 450 ? 155.669 139.827 191.108 1.00 67.03 ? 593 GLU A OE1    1 
ATOM   2934 O  OE2    . GLU A 1 450 ? 155.859 139.222 189.008 1.00 67.09 ? 593 GLU A OE2    1 
HETATM 2935 MG MG     . MG  B 2 .   ? 165.002 149.388 164.787 1.00 39.90 ? 800 MG  A MG     1 
HETATM 2936 ZN ZN     . ZN  C 3 .   ? 169.938 151.495 194.599 1.00 65.17 ? 801 ZN  A ZN     1 
HETATM 2937 P  PG     . ATP D 4 .   ? 166.616 150.025 167.947 1.00 49.55 ? 802 ATP A PG     1 
HETATM 2938 O  O1G    . ATP D 4 .   ? 166.865 150.902 169.121 1.00 32.43 ? 802 ATP A O1G    1 
HETATM 2939 O  O2G    . ATP D 4 .   ? 167.858 149.327 167.420 1.00 39.99 ? 802 ATP A O2G    1 
HETATM 2940 O  O3G    . ATP D 4 .   ? 165.933 150.742 166.783 1.00 42.76 ? 802 ATP A O3G    1 
HETATM 2941 P  PB     . ATP D 4 .   ? 164.113 148.605 168.728 1.00 20.82 ? 802 ATP A PB     1 
HETATM 2942 O  O1B    . ATP D 4 .   ? 163.869 148.828 170.153 1.00 20.84 ? 802 ATP A O1B    1 
HETATM 2943 O  O2B    . ATP D 4 .   ? 163.278 149.455 167.791 1.00 24.86 ? 802 ATP A O2B    1 
HETATM 2944 O  O3B    . ATP D 4 .   ? 165.619 148.835 168.330 1.00 29.10 ? 802 ATP A O3B    1 
HETATM 2945 P  PA     . ATP D 4 .   ? 163.708 146.254 166.984 1.00 25.60 ? 802 ATP A PA     1 
HETATM 2946 O  O1A    . ATP D 4 .   ? 162.325 145.761 166.856 1.00 21.79 ? 802 ATP A O1A    1 
HETATM 2947 O  O2A    . ATP D 4 .   ? 164.168 147.140 165.837 1.00 27.58 ? 802 ATP A O2A    1 
HETATM 2948 O  O3A    . ATP D 4 .   ? 163.890 147.084 168.322 1.00 22.16 ? 802 ATP A O3A    1 
HETATM 2949 O  "O5'"  . ATP D 4 .   ? 164.725 145.059 167.177 1.00 25.58 ? 802 ATP A "O5'"  1 
HETATM 2950 C  "C5'"  . ATP D 4 .   ? 165.341 144.400 166.050 1.00 25.94 ? 802 ATP A "C5'"  1 
HETATM 2951 C  "C4'"  . ATP D 4 .   ? 165.102 142.914 166.141 1.00 26.28 ? 802 ATP A "C4'"  1 
HETATM 2952 O  "O4'"  . ATP D 4 .   ? 164.756 142.644 167.505 1.00 26.48 ? 802 ATP A "O4'"  1 
HETATM 2953 C  "C3'"  . ATP D 4 .   ? 163.841 142.526 165.376 1.00 28.00 ? 802 ATP A "C3'"  1 
HETATM 2954 O  "O3'"  . ATP D 4 .   ? 164.300 141.813 164.237 1.00 30.87 ? 802 ATP A "O3'"  1 
HETATM 2955 C  "C2'"  . ATP D 4 .   ? 163.173 141.462 166.263 1.00 24.70 ? 802 ATP A "C2'"  1 
HETATM 2956 O  "O2'"  . ATP D 4 .   ? 163.454 140.223 165.633 1.00 27.60 ? 802 ATP A "O2'"  1 
HETATM 2957 C  "C1'"  . ATP D 4 .   ? 164.032 141.441 167.529 1.00 22.44 ? 802 ATP A "C1'"  1 
HETATM 2958 N  N9     . ATP D 4 .   ? 163.202 141.506 168.722 1.00 19.34 ? 802 ATP A N9     1 
HETATM 2959 C  C8     . ATP D 4 .   ? 163.232 142.492 169.668 1.00 18.53 ? 802 ATP A C8     1 
HETATM 2960 N  N7     . ATP D 4 .   ? 162.378 142.323 170.645 1.00 18.13 ? 802 ATP A N7     1 
HETATM 2961 C  C5     . ATP D 4 .   ? 161.730 141.146 170.313 1.00 17.51 ? 802 ATP A C5     1 
HETATM 2962 C  C6     . ATP D 4 .   ? 160.702 140.421 170.943 1.00 18.04 ? 802 ATP A C6     1 
HETATM 2963 N  N6     . ATP D 4 .   ? 160.126 140.794 172.089 1.00 17.65 ? 802 ATP A N6     1 
HETATM 2964 N  N1     . ATP D 4 .   ? 160.282 139.282 170.350 1.00 17.93 ? 802 ATP A N1     1 
HETATM 2965 C  C2     . ATP D 4 .   ? 160.856 138.905 169.205 1.00 19.47 ? 802 ATP A C2     1 
HETATM 2966 N  N3     . ATP D 4 .   ? 161.831 139.506 168.520 1.00 21.03 ? 802 ATP A N3     1 
HETATM 2967 C  C4     . ATP D 4 .   ? 162.227 140.628 169.129 1.00 20.49 ? 802 ATP A C4     1 
HETATM 2968 H  "H5'1" . ATP D 4 .   ? 164.966 144.741 165.223 1.00 26.44 ? 802 ATP A "H5'1" 1 
HETATM 2969 H  "H5'2" . ATP D 4 .   ? 166.296 144.573 166.063 1.00 25.05 ? 802 ATP A "H5'2" 1 
HETATM 2970 H  "H4'"  . ATP D 4 .   ? 165.875 142.412 165.844 1.00 24.63 ? 802 ATP A "H4'"  1 
HETATM 2971 H  "H3'"  . ATP D 4 .   ? 163.263 143.276 165.163 1.00 25.95 ? 802 ATP A "H3'"  1 
HETATM 2972 H  "HO3'" . ATP D 4 .   ? 163.629 141.705 163.727 1.00 29.42 ? 802 ATP A "HO3'" 1 
HETATM 2973 H  "H2'"  . ATP D 4 .   ? 162.230 141.619 166.427 1.00 22.99 ? 802 ATP A "H2'"  1 
HETATM 2974 H  "HO2'" . ATP D 4 .   ? 163.058 140.235 164.881 1.00 26.38 ? 802 ATP A "HO2'" 1 
HETATM 2975 H  "H1'"  . ATP D 4 .   ? 164.616 140.668 167.546 1.00 21.90 ? 802 ATP A "H1'"  1 
HETATM 2976 H  H8     . ATP D 4 .   ? 163.815 143.215 169.627 1.00 19.33 ? 802 ATP A H8     1 
HETATM 2977 H  HN61   . ATP D 4 .   ? 159.544 140.286 172.464 1.00 20.38 ? 802 ATP A HN61   1 
HETATM 2978 H  HN62   . ATP D 4 .   ? 160.338 141.545 172.452 1.00 18.17 ? 802 ATP A HN62   1 
HETATM 2979 H  H2     . ATP D 4 .   ? 160.534 138.115 168.835 1.00 20.49 ? 802 ATP A H2     1 
# 
